data_9BE3
# 
_entry.id   9BE3 
# 
_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   9BE3         pdb_00009be3 10.2210/pdb9be3/pdb 
WWPDB D_1000283153 ?            ?                   
# 
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                        9BE3 
_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' 205906.109 2   ? ? ? 
'Complex built 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 
;(2~{R})-~{N}-[3-[2-[[(2~{S})-2-formamido-3-methyl-butanoyl]amino]ethylamino]-3-oxidanylidene-propyl]-3,3-dimethyl-2-oxidanyl-4-[oxidanyl-bis(oxidanylidene)-$l^{6}-phosphanyl]oxy-butanamide
;
467.431    2   ? ? ? ? 
4 non-polymer syn 'N-[2-(glycylamino)ethyl]-N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alaninamide' 398.349 
1   ? ? ? ? 
5 non-polymer syn 'MANGANESE (II) ION' 54.938     4   ? ? ? ? 
6 water       nat water 18.015     501 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGRILFLTTFMSKGNKVVRYLESLHHEVVICQEKVHAQSANLQEIDWIVSYAYGYILDKEIVSRFRGRIINLHPSLLPWN
KGRDPVFWSVWDETPKGVTIHLIDEHVDTGDILVQEEIAFADEDTLLDCYNKANQAIEELFIREWENIVHGRIAPYRQTA
GGTLHFKADRDFYKNLNMTTVRELLALKRLCAEPKRGEKPIDKTFHQLFEQQVEMTPDHVAVVDRGQSLTYKQLNERANQ
LAHHLRGKGVKPDDQVAIMLDKSLDMIVSILAVMKAGGAYVPIDPDYPGERIAYMLADSSAAILLTNALHEEKANGACDI
IDVHDPDSYSENTNNLPHVNRPDDLVYVMYTSGSTGLAKGVMIEHHNLVNFCEWYRPYFGVTPADKALVYSSFSFDGSAL
DIFTHLLAGAALHIVPSERKYDLDALNDYCNQEGITISYLPTGAAEQFMQMDNQSFRVVITGGDVLKKIERNGTYKLYNG
YGPTECTIMVTMFEVDKPYANIPIGKPIDRTRILILDEALALQPIGVAGELFIVGEGLGRGYLNRPELTAEKFIVHPQTG
ERMYRTGDRARFLPDGNIEFLGRLDNLVKIRGYRIEPGEIEPFLMNHPLIELTTVLAKEQADGRKYLVGYYVAPEEIPHG
ELREWLGNDLPDYMIPTYFVHMKAFPLTANGKVDRRALPDVQADAELLGEDYVAPTDELEQQLAQVWSHVLGIPQMGIDD
HFLERGGDSIKVMQLIHQLKNIGLSLRYDQLFTHPTIRQLKRLLTEQKQVNGLLEPLRELDEQAEYETSAVEKRMYIIQQ
QDVESIAYNVVYTINFPLTVDTEQIRVALEQLVLRHEGLRSTYHMRGDEIVKRIVPRAELSFVRQTGEEESVQSLLAEQI
KPFDLAKAPLLRAGVIETADKKVLWFDSHHILLDGLSKSILARELQALLGQQVLSPVEKTYKSFARWQNEWFASDEYEQQ
IAYWKTLLQGELPAVQLPTKKRPPQLTFDGAIQMYRVNPEITRKLKATAAKHDLTLYMLMLTIVSIWLSKMNSDSNQVIL
GTVTDGRQHPDTRELLGMFVNTLPLLLSIDHEESFLHNLQQVKAKLLPALQNQYVPFDKILEAARVKREGNRHPLFDVMF
MMQGAPETELESNMHHINAGISKFDLTLEVLERENGLNIVFEYNTHLFDEGMILRMVAQFEHLLLQAVHGLDQQVKRFEL
VTEDEKRDLFLRVNDTAKAYPNKLIMSMLEDWAAATPDKTALVFREQRVTYRELNERVNQLAHTLREKGVQPDDLVMLMA
ERSVEMMVAIFAVLKAGGAYLPIDPHSPAERIAYIFADSGAKLVLAQSPFVEKASMAEVVLDLNSASSYAADTSNPPLVN
QPGDLVYVMYTSGSTGKPKGVMIEHGALLNVLHGMQDEYPLLQDDAFLLKTTYIFDISVAEIFGWVPGRGKLVILEPEAE
KNPKAIWQAVVGAGITHINFVPSMLIPFVEYLEGRTEANRLRYILACGEAMPDELVPKVYEVLPEVKLENIYGPTEATIY
ASRYSLAKGSQESPVPIGKPLPNYRMYIINRHGQLQPIGVPGELCIAGASLARGYLNNPALTEEKFTPHPLEKGERIYRT
GDLARYREDGNIEYLGRMDHQVKIRGYRIELDEIRSKLIQEETIQDAVVVARNDQNGQAYLCAYLLSEQEWTVGQLRELL
RRELPEYMIPAHFVLLKQFPLTANGKLDRKALPEPDGSVKAEAEYAAPRTELEATLAHIWGEVLGIERIGIRDNFFELGG
DSIKGLQIASRLQRINWTMVINHLFLYPTIEQIAPFVTSEQVVIEAAAENLYFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGRILFLTTFMSKGNKVVRYLESLHHEVVICQEKVHAQSANLQEIDWIVSYAYGYILDKEIVSRFRGRIINLHPSLLPWN
KGRDPVFWSVWDETPKGVTIHLIDEHVDTGDILVQEEIAFADEDTLLDCYNKANQAIEELFIREWENIVHGRIAPYRQTA
GGTLHFKADRDFYKNLNMTTVRELLALKRLCAEPKRGEKPIDKTFHQLFEQQVEMTPDHVAVVDRGQSLTYKQLNERANQ
LAHHLRGKGVKPDDQVAIMLDKSLDMIVSILAVMKAGGAYVPIDPDYPGERIAYMLADSSAAILLTNALHEEKANGACDI
IDVHDPDSYSENTNNLPHVNRPDDLVYVMYTSGSTGLAKGVMIEHHNLVNFCEWYRPYFGVTPADKALVYSSFSFDGSAL
DIFTHLLAGAALHIVPSERKYDLDALNDYCNQEGITISYLPTGAAEQFMQMDNQSFRVVITGGDVLKKIERNGTYKLYNG
YGPTECTIMVTMFEVDKPYANIPIGKPIDRTRILILDEALALQPIGVAGELFIVGEGLGRGYLNRPELTAEKFIVHPQTG
ERMYRTGDRARFLPDGNIEFLGRLDNLVKIRGYRIEPGEIEPFLMNHPLIELTTVLAKEQADGRKYLVGYYVAPEEIPHG
ELREWLGNDLPDYMIPTYFVHMKAFPLTANGKVDRRALPDVQADAELLGEDYVAPTDELEQQLAQVWSHVLGIPQMGIDD
HFLERGGDSIKVMQLIHQLKNIGLSLRYDQLFTHPTIRQLKRLLTEQKQVNGLLEPLRELDEQAEYETSAVEKRMYIIQQ
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 
;(2~{R})-~{N}-[3-[2-[[(2~{S})-2-formamido-3-methyl-butanoyl]amino]ethylamino]-3-oxidanylidene-propyl]-3,3-dimethyl-2-oxidanyl-4-[oxidanyl-bis(oxidanylidene)-$l^{6}-phosphanyl]oxy-butanamide
;
JQG   
4 'N-[2-(glycylamino)ethyl]-N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alaninamide' A1AMO 
5 'MANGANESE (II) ION' MN    
6 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  SER 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 
A1AMO non-polymer         . 
'N-[2-(glycylamino)ethyl]-N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alaninamide' ? 'C13 H27 N4 O8 P' 
398.349 
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 
JQG   non-polymer         . 
;(2~{R})-~{N}-[3-[2-[[(2~{S})-2-formamido-3-methyl-butanoyl]amino]ethylamino]-3-oxidanylidene-propyl]-3,3-dimethyl-2-oxidanyl-4-[oxidanyl-bis(oxidanylidene)-$l^{6}-phosphanyl]oxy-butanamide
;
?                               'C17 H32 N4 O9 P' 467.431 
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  196  ARG ARG A . n 
A 1 197  GLY 197  197  197  GLY GLY 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  355  THR THR A . n 
A 1 356  GLY 356  356  356  GLY GLY 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  683  ALA ALA A . n 
A 1 684  ASP 684  684  684  ASP ASP A . n 
A 1 685  ALA 685  685  685  ALA ALA 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  SER 729  729  729  SER SER 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 1370 SER SER A . n 
A 1 1373 GLY 1373 1371 1371 GLY GLY A . n 
A 1 1374 SER 1374 1372 1372 SER SER A . n 
A 1 1375 THR 1375 1373 1373 THR THR 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 ASP A . n 
A 1 1655 GLN 1655 1653 1653 GLN GLN A . n 
A 1 1656 ASN 1656 1654 1654 ASN ASN A . n 
A 1 1657 GLY 1657 1655 1655 GLY GLY A . n 
A 1 1658 GLN 1658 1656 1656 GLN GLN 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 ?    ?   ?   A . n 
A 1 1670 GLU 1670 1668 ?    ?   ?   A . n 
A 1 1671 TRP 1671 1669 ?    ?   ?   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  ?    ?   ?   B . n 
B 1 195  LYS 195  195  ?    ?   ?   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  SER 729  729  729  SER SER 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 ?    ?   ?   B . n 
B 1 1649 VAL 1649 1647 ?    ?   ?   B . n 
B 1 1650 VAL 1650 1648 ?    ?   ?   B . n 
B 1 1651 ALA 1651 1649 ?    ?   ?   B . n 
B 1 1652 ARG 1652 1650 ?    ?   ?   B . n 
B 1 1653 ASN 1653 1651 ?    ?   ?   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 ?    ?   ?   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 ?    ?   ?   B . n 
B 1 1726 ALA 1726 1724 ?    ?   ?   B . n 
B 1 1727 ALA 1727 1725 ?    ?   ?   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 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 JQG   ? ? JQG   ? ? 'SUBJECT OF INVESTIGATION' ? 
2 A1AMO ? ? A1AMO ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 JQG   1   1903 1903 JQG   FPE A . 
F 4 A1AMO 1   1904 1904 A1AMO GPE A . 
G 5 MN    1   1905 3    MN    MN  A . 
H 2 GOL   1   1901 1901 GOL   LIG B . 
I 3 JQG   1   1902 1902 JQG   FPE B . 
J 5 MN    1   1903 2    MN    MN  B . 
K 5 MN    1   1904 5    MN    MN  B . 
L 5 MN    1   1905 6    MN    MN  B . 
M 6 HOH   1   2001 1001 HOH   HOH A . 
M 6 HOH   2   2002 205  HOH   HOH A . 
M 6 HOH   3   2003 1158 HOH   HOH A . 
M 6 HOH   4   2004 1160 HOH   HOH A . 
M 6 HOH   5   2005 304  HOH   HOH A . 
M 6 HOH   6   2006 491  HOH   HOH A . 
M 6 HOH   7   2007 257  HOH   HOH A . 
M 6 HOH   8   2008 237  HOH   HOH A . 
M 6 HOH   9   2009 967  HOH   HOH A . 
M 6 HOH   10  2010 461  HOH   HOH A . 
M 6 HOH   11  2011 604  HOH   HOH A . 
M 6 HOH   12  2012 575  HOH   HOH A . 
M 6 HOH   13  2013 92   HOH   HOH A . 
M 6 HOH   14  2014 23   HOH   HOH A . 
M 6 HOH   15  2015 934  HOH   HOH A . 
M 6 HOH   16  2016 587  HOH   HOH A . 
M 6 HOH   17  2017 163  HOH   HOH A . 
M 6 HOH   18  2018 263  HOH   HOH A . 
M 6 HOH   19  2019 990  HOH   HOH A . 
M 6 HOH   20  2020 517  HOH   HOH A . 
M 6 HOH   21  2021 233  HOH   HOH A . 
M 6 HOH   22  2022 490  HOH   HOH A . 
M 6 HOH   23  2023 109  HOH   HOH A . 
M 6 HOH   24  2024 157  HOH   HOH A . 
M 6 HOH   25  2025 1185 HOH   HOH A . 
M 6 HOH   26  2026 145  HOH   HOH A . 
M 6 HOH   27  2027 469  HOH   HOH A . 
M 6 HOH   28  2028 987  HOH   HOH A . 
M 6 HOH   29  2029 131  HOH   HOH A . 
M 6 HOH   30  2030 807  HOH   HOH A . 
M 6 HOH   31  2031 1179 HOH   HOH A . 
M 6 HOH   32  2032 113  HOH   HOH A . 
M 6 HOH   33  2033 367  HOH   HOH A . 
M 6 HOH   34  2034 675  HOH   HOH A . 
M 6 HOH   35  2035 260  HOH   HOH A . 
M 6 HOH   36  2036 1143 HOH   HOH A . 
M 6 HOH   37  2037 17   HOH   HOH A . 
M 6 HOH   38  2038 12   HOH   HOH A . 
M 6 HOH   39  2039 347  HOH   HOH A . 
M 6 HOH   40  2040 390  HOH   HOH A . 
M 6 HOH   41  2041 340  HOH   HOH A . 
M 6 HOH   42  2042 1018 HOH   HOH A . 
M 6 HOH   43  2043 969  HOH   HOH A . 
M 6 HOH   44  2044 1182 HOH   HOH A . 
M 6 HOH   45  2045 809  HOH   HOH A . 
M 6 HOH   46  2046 183  HOH   HOH A . 
M 6 HOH   47  2047 1198 HOH   HOH A . 
M 6 HOH   48  2048 242  HOH   HOH A . 
M 6 HOH   49  2049 986  HOH   HOH A . 
M 6 HOH   50  2050 582  HOH   HOH A . 
M 6 HOH   51  2051 346  HOH   HOH A . 
M 6 HOH   52  2052 154  HOH   HOH A . 
M 6 HOH   53  2053 36   HOH   HOH A . 
M 6 HOH   54  2054 87   HOH   HOH A . 
M 6 HOH   55  2055 988  HOH   HOH A . 
M 6 HOH   56  2056 115  HOH   HOH A . 
M 6 HOH   57  2057 886  HOH   HOH A . 
M 6 HOH   58  2058 792  HOH   HOH A . 
M 6 HOH   59  2059 1170 HOH   HOH A . 
M 6 HOH   60  2060 337  HOH   HOH A . 
M 6 HOH   61  2061 143  HOH   HOH A . 
M 6 HOH   62  2062 639  HOH   HOH A . 
M 6 HOH   63  2063 1033 HOH   HOH A . 
M 6 HOH   64  2064 357  HOH   HOH A . 
M 6 HOH   65  2065 266  HOH   HOH A . 
M 6 HOH   66  2066 441  HOH   HOH A . 
M 6 HOH   67  2067 1175 HOH   HOH A . 
M 6 HOH   68  2068 282  HOH   HOH A . 
M 6 HOH   69  2069 892  HOH   HOH A . 
M 6 HOH   70  2070 225  HOH   HOH A . 
M 6 HOH   71  2071 1030 HOH   HOH A . 
M 6 HOH   72  2072 970  HOH   HOH A . 
M 6 HOH   73  2073 144  HOH   HOH A . 
M 6 HOH   74  2074 483  HOH   HOH A . 
M 6 HOH   75  2075 1109 HOH   HOH A . 
M 6 HOH   76  2076 1197 HOH   HOH A . 
M 6 HOH   77  2077 182  HOH   HOH A . 
M 6 HOH   78  2078 408  HOH   HOH A . 
M 6 HOH   79  2079 380  HOH   HOH A . 
M 6 HOH   80  2080 684  HOH   HOH A . 
M 6 HOH   81  2081 1199 HOH   HOH A . 
M 6 HOH   82  2082 281  HOH   HOH A . 
M 6 HOH   83  2083 1047 HOH   HOH A . 
M 6 HOH   84  2084 302  HOH   HOH A . 
M 6 HOH   85  2085 691  HOH   HOH A . 
M 6 HOH   86  2086 898  HOH   HOH A . 
M 6 HOH   87  2087 619  HOH   HOH A . 
M 6 HOH   88  2088 106  HOH   HOH A . 
M 6 HOH   89  2089 791  HOH   HOH A . 
M 6 HOH   90  2090 1130 HOH   HOH A . 
M 6 HOH   91  2091 439  HOH   HOH A . 
M 6 HOH   92  2092 891  HOH   HOH A . 
M 6 HOH   93  2093 449  HOH   HOH A . 
M 6 HOH   94  2094 235  HOH   HOH A . 
M 6 HOH   95  2095 1017 HOH   HOH A . 
M 6 HOH   96  2096 1192 HOH   HOH A . 
M 6 HOH   97  2097 864  HOH   HOH A . 
M 6 HOH   98  2098 626  HOH   HOH A . 
M 6 HOH   99  2099 334  HOH   HOH A . 
M 6 HOH   100 2100 24   HOH   HOH A . 
M 6 HOH   101 2101 510  HOH   HOH A . 
M 6 HOH   102 2102 164  HOH   HOH A . 
M 6 HOH   103 2103 223  HOH   HOH A . 
M 6 HOH   104 2104 138  HOH   HOH A . 
M 6 HOH   105 2105 896  HOH   HOH A . 
M 6 HOH   106 2106 60   HOH   HOH A . 
M 6 HOH   107 2107 855  HOH   HOH A . 
M 6 HOH   108 2108 1090 HOH   HOH A . 
M 6 HOH   109 2109 230  HOH   HOH A . 
M 6 HOH   110 2110 127  HOH   HOH A . 
M 6 HOH   111 2111 58   HOH   HOH A . 
M 6 HOH   112 2112 536  HOH   HOH A . 
M 6 HOH   113 2113 848  HOH   HOH A . 
M 6 HOH   114 2114 1089 HOH   HOH A . 
M 6 HOH   115 2115 213  HOH   HOH A . 
M 6 HOH   116 2116 285  HOH   HOH A . 
M 6 HOH   117 2117 508  HOH   HOH A . 
M 6 HOH   118 2118 968  HOH   HOH A . 
M 6 HOH   119 2119 493  HOH   HOH A . 
M 6 HOH   120 2120 1111 HOH   HOH A . 
M 6 HOH   121 2121 1183 HOH   HOH A . 
M 6 HOH   122 2122 47   HOH   HOH A . 
M 6 HOH   123 2123 610  HOH   HOH A . 
M 6 HOH   124 2124 48   HOH   HOH A . 
M 6 HOH   125 2125 1044 HOH   HOH A . 
M 6 HOH   126 2126 178  HOH   HOH A . 
M 6 HOH   127 2127 1016 HOH   HOH A . 
M 6 HOH   128 2128 995  HOH   HOH A . 
M 6 HOH   129 2129 946  HOH   HOH A . 
M 6 HOH   130 2130 838  HOH   HOH A . 
M 6 HOH   131 2131 635  HOH   HOH A . 
M 6 HOH   132 2132 1146 HOH   HOH A . 
M 6 HOH   133 2133 580  HOH   HOH A . 
M 6 HOH   134 2134 1053 HOH   HOH A . 
M 6 HOH   135 2135 301  HOH   HOH A . 
M 6 HOH   136 2136 1066 HOH   HOH A . 
M 6 HOH   137 2137 101  HOH   HOH A . 
M 6 HOH   138 2138 298  HOH   HOH A . 
M 6 HOH   139 2139 234  HOH   HOH A . 
M 6 HOH   140 2140 1103 HOH   HOH A . 
M 6 HOH   141 2141 373  HOH   HOH A . 
M 6 HOH   142 2142 546  HOH   HOH A . 
M 6 HOH   143 2143 1173 HOH   HOH A . 
M 6 HOH   144 2144 152  HOH   HOH A . 
M 6 HOH   145 2145 962  HOH   HOH A . 
M 6 HOH   146 2146 1178 HOH   HOH A . 
M 6 HOH   147 2147 1086 HOH   HOH A . 
M 6 HOH   148 2148 1195 HOH   HOH A . 
M 6 HOH   149 2149 180  HOH   HOH A . 
M 6 HOH   150 2150 1163 HOH   HOH A . 
M 6 HOH   151 2151 238  HOH   HOH A . 
M 6 HOH   152 2152 1189 HOH   HOH A . 
M 6 HOH   153 2153 410  HOH   HOH A . 
M 6 HOH   154 2154 1067 HOH   HOH A . 
M 6 HOH   155 2155 1156 HOH   HOH A . 
M 6 HOH   156 2156 876  HOH   HOH A . 
M 6 HOH   157 2157 1139 HOH   HOH A . 
M 6 HOH   158 2158 555  HOH   HOH A . 
M 6 HOH   159 2159 953  HOH   HOH A . 
M 6 HOH   160 2160 509  HOH   HOH A . 
M 6 HOH   161 2161 365  HOH   HOH A . 
M 6 HOH   162 2162 387  HOH   HOH A . 
M 6 HOH   163 2163 1005 HOH   HOH A . 
M 6 HOH   164 2164 149  HOH   HOH A . 
M 6 HOH   165 2165 283  HOH   HOH A . 
M 6 HOH   166 2166 46   HOH   HOH A . 
M 6 HOH   167 2167 1085 HOH   HOH A . 
M 6 HOH   168 2168 630  HOH   HOH A . 
M 6 HOH   169 2169 771  HOH   HOH A . 
M 6 HOH   170 2170 227  HOH   HOH A . 
M 6 HOH   171 2171 53   HOH   HOH A . 
M 6 HOH   172 2172 1059 HOH   HOH A . 
M 6 HOH   173 2173 318  HOH   HOH A . 
M 6 HOH   174 2174 169  HOH   HOH A . 
M 6 HOH   175 2175 28   HOH   HOH A . 
M 6 HOH   176 2176 1167 HOH   HOH A . 
M 6 HOH   177 2177 498  HOH   HOH A . 
M 6 HOH   178 2178 166  HOH   HOH A . 
M 6 HOH   179 2179 95   HOH   HOH A . 
M 6 HOH   180 2180 88   HOH   HOH A . 
M 6 HOH   181 2181 111  HOH   HOH A . 
M 6 HOH   182 2182 1002 HOH   HOH A . 
M 6 HOH   183 2183 303  HOH   HOH A . 
M 6 HOH   184 2184 1022 HOH   HOH A . 
M 6 HOH   185 2185 194  HOH   HOH A . 
M 6 HOH   186 2186 960  HOH   HOH A . 
M 6 HOH   187 2187 470  HOH   HOH A . 
M 6 HOH   188 2188 255  HOH   HOH A . 
M 6 HOH   189 2189 421  HOH   HOH A . 
M 6 HOH   190 2190 1144 HOH   HOH A . 
M 6 HOH   191 2191 1037 HOH   HOH A . 
M 6 HOH   192 2192 526  HOH   HOH A . 
M 6 HOH   193 2193 1188 HOH   HOH A . 
M 6 HOH   194 2194 351  HOH   HOH A . 
M 6 HOH   195 2195 1190 HOH   HOH A . 
M 6 HOH   196 2196 1127 HOH   HOH A . 
M 6 HOH   197 2197 32   HOH   HOH A . 
M 6 HOH   198 2198 704  HOH   HOH A . 
M 6 HOH   199 2199 267  HOH   HOH A . 
M 6 HOH   200 2200 1159 HOH   HOH A . 
M 6 HOH   201 2201 241  HOH   HOH A . 
M 6 HOH   202 2202 893  HOH   HOH A . 
M 6 HOH   203 2203 349  HOH   HOH A . 
M 6 HOH   204 2204 247  HOH   HOH A . 
M 6 HOH   205 2205 264  HOH   HOH A . 
M 6 HOH   206 2206 1157 HOH   HOH A . 
M 6 HOH   207 2207 196  HOH   HOH A . 
M 6 HOH   208 2208 403  HOH   HOH A . 
M 6 HOH   209 2209 1180 HOH   HOH A . 
M 6 HOH   210 2210 472  HOH   HOH A . 
M 6 HOH   211 2211 360  HOH   HOH A . 
M 6 HOH   212 2212 428  HOH   HOH A . 
M 6 HOH   213 2213 798  HOH   HOH A . 
M 6 HOH   214 2214 1031 HOH   HOH A . 
M 6 HOH   215 2215 121  HOH   HOH A . 
M 6 HOH   216 2216 701  HOH   HOH A . 
M 6 HOH   217 2217 1129 HOH   HOH A . 
M 6 HOH   218 2218 1097 HOH   HOH A . 
M 6 HOH   219 2219 343  HOH   HOH A . 
M 6 HOH   220 2220 186  HOH   HOH A . 
M 6 HOH   221 2221 979  HOH   HOH A . 
M 6 HOH   222 2222 1061 HOH   HOH A . 
M 6 HOH   223 2223 1058 HOH   HOH A . 
M 6 HOH   224 2224 931  HOH   HOH A . 
M 6 HOH   225 2225 210  HOH   HOH A . 
M 6 HOH   226 2226 925  HOH   HOH A . 
M 6 HOH   227 2227 1087 HOH   HOH A . 
M 6 HOH   228 2228 1126 HOH   HOH A . 
M 6 HOH   229 2229 391  HOH   HOH A . 
M 6 HOH   230 2230 1101 HOH   HOH A . 
M 6 HOH   231 2231 1046 HOH   HOH A . 
M 6 HOH   232 2232 1079 HOH   HOH A . 
M 6 HOH   233 2233 1120 HOH   HOH A . 
M 6 HOH   234 2234 949  HOH   HOH A . 
M 6 HOH   235 2235 78   HOH   HOH A . 
M 6 HOH   236 2236 434  HOH   HOH A . 
M 6 HOH   237 2237 1064 HOH   HOH A . 
M 6 HOH   238 2238 1131 HOH   HOH A . 
M 6 HOH   239 2239 1020 HOH   HOH A . 
M 6 HOH   240 2240 1027 HOH   HOH A . 
M 6 HOH   241 2241 338  HOH   HOH A . 
M 6 HOH   242 2242 1117 HOH   HOH A . 
M 6 HOH   243 2243 1034 HOH   HOH A . 
M 6 HOH   244 2244 1070 HOH   HOH A . 
M 6 HOH   245 2245 571  HOH   HOH A . 
M 6 HOH   246 2246 658  HOH   HOH A . 
M 6 HOH   247 2247 860  HOH   HOH A . 
M 6 HOH   248 2248 1036 HOH   HOH A . 
M 6 HOH   249 2249 1088 HOH   HOH A . 
M 6 HOH   250 2250 621  HOH   HOH A . 
M 6 HOH   251 2251 1045 HOH   HOH A . 
M 6 HOH   252 2252 1096 HOH   HOH A . 
M 6 HOH   253 2253 1077 HOH   HOH A . 
M 6 HOH   254 2254 832  HOH   HOH A . 
M 6 HOH   255 2255 500  HOH   HOH A . 
M 6 HOH   256 2256 404  HOH   HOH A . 
M 6 HOH   257 2257 1102 HOH   HOH A . 
M 6 HOH   258 2258 1112 HOH   HOH A . 
M 6 HOH   259 2259 1098 HOH   HOH A . 
M 6 HOH   260 2260 1048 HOH   HOH A . 
M 6 HOH   261 2261 796  HOH   HOH A . 
M 6 HOH   262 2262 79   HOH   HOH A . 
M 6 HOH   263 2263 1072 HOH   HOH A . 
M 6 HOH   264 2264 1060 HOH   HOH A . 
M 6 HOH   265 2265 492  HOH   HOH A . 
M 6 HOH   266 2266 1110 HOH   HOH A . 
M 6 HOH   267 2267 1148 HOH   HOH A . 
M 6 HOH   268 2268 1128 HOH   HOH A . 
M 6 HOH   269 2269 1147 HOH   HOH A . 
M 6 HOH   270 2270 1099 HOH   HOH A . 
M 6 HOH   271 2271 1125 HOH   HOH A . 
M 6 HOH   272 2272 1121 HOH   HOH A . 
M 6 HOH   273 2273 1184 HOH   HOH A . 
M 6 HOH   274 2274 1091 HOH   HOH A . 
M 6 HOH   275 2275 1171 HOH   HOH A . 
M 6 HOH   276 2276 1095 HOH   HOH A . 
M 6 HOH   277 2277 1100 HOH   HOH A . 
N 6 HOH   1   2001 1063 HOH   HOH B . 
N 6 HOH   2   2002 603  HOH   HOH B . 
N 6 HOH   3   2003 286  HOH   HOH B . 
N 6 HOH   4   2004 1176 HOH   HOH B . 
N 6 HOH   5   2005 323  HOH   HOH B . 
N 6 HOH   6   2006 355  HOH   HOH B . 
N 6 HOH   7   2007 128  HOH   HOH B . 
N 6 HOH   8   2008 364  HOH   HOH B . 
N 6 HOH   9   2009 890  HOH   HOH B . 
N 6 HOH   10  2010 188  HOH   HOH B . 
N 6 HOH   11  2011 41   HOH   HOH B . 
N 6 HOH   12  2012 122  HOH   HOH B . 
N 6 HOH   13  2013 1073 HOH   HOH B . 
N 6 HOH   14  2014 738  HOH   HOH B . 
N 6 HOH   15  2015 481  HOH   HOH B . 
N 6 HOH   16  2016 1177 HOH   HOH B . 
N 6 HOH   17  2017 735  HOH   HOH B . 
N 6 HOH   18  2018 412  HOH   HOH B . 
N 6 HOH   19  2019 865  HOH   HOH B . 
N 6 HOH   20  2020 155  HOH   HOH B . 
N 6 HOH   21  2021 425  HOH   HOH B . 
N 6 HOH   22  2022 33   HOH   HOH B . 
N 6 HOH   23  2023 541  HOH   HOH B . 
N 6 HOH   24  2024 627  HOH   HOH B . 
N 6 HOH   25  2025 754  HOH   HOH B . 
N 6 HOH   26  2026 901  HOH   HOH B . 
N 6 HOH   27  2027 1078 HOH   HOH B . 
N 6 HOH   28  2028 102  HOH   HOH B . 
N 6 HOH   29  2029 715  HOH   HOH B . 
N 6 HOH   30  2030 396  HOH   HOH B . 
N 6 HOH   31  2031 972  HOH   HOH B . 
N 6 HOH   32  2032 174  HOH   HOH B . 
N 6 HOH   33  2033 19   HOH   HOH B . 
N 6 HOH   34  2034 981  HOH   HOH B . 
N 6 HOH   35  2035 1133 HOH   HOH B . 
N 6 HOH   36  2036 382  HOH   HOH B . 
N 6 HOH   37  2037 82   HOH   HOH B . 
N 6 HOH   38  2038 165  HOH   HOH B . 
N 6 HOH   39  2039 189  HOH   HOH B . 
N 6 HOH   40  2040 310  HOH   HOH B . 
N 6 HOH   41  2041 456  HOH   HOH B . 
N 6 HOH   42  2042 43   HOH   HOH B . 
N 6 HOH   43  2043 345  HOH   HOH B . 
N 6 HOH   44  2044 740  HOH   HOH B . 
N 6 HOH   45  2045 669  HOH   HOH B . 
N 6 HOH   46  2046 497  HOH   HOH B . 
N 6 HOH   47  2047 34   HOH   HOH B . 
N 6 HOH   48  2048 1043 HOH   HOH B . 
N 6 HOH   49  2049 661  HOH   HOH B . 
N 6 HOH   50  2050 6    HOH   HOH B . 
N 6 HOH   51  2051 350  HOH   HOH B . 
N 6 HOH   52  2052 177  HOH   HOH B . 
N 6 HOH   53  2053 161  HOH   HOH B . 
N 6 HOH   54  2054 316  HOH   HOH B . 
N 6 HOH   55  2055 540  HOH   HOH B . 
N 6 HOH   56  2056 978  HOH   HOH B . 
N 6 HOH   57  2057 306  HOH   HOH B . 
N 6 HOH   58  2058 1038 HOH   HOH B . 
N 6 HOH   59  2059 1083 HOH   HOH B . 
N 6 HOH   60  2060 268  HOH   HOH B . 
N 6 HOH   61  2061 730  HOH   HOH B . 
N 6 HOH   62  2062 1142 HOH   HOH B . 
N 6 HOH   63  2063 1153 HOH   HOH B . 
N 6 HOH   64  2064 195  HOH   HOH B . 
N 6 HOH   65  2065 159  HOH   HOH B . 
N 6 HOH   66  2066 885  HOH   HOH B . 
N 6 HOH   67  2067 86   HOH   HOH B . 
N 6 HOH   68  2068 965  HOH   HOH B . 
N 6 HOH   69  2069 495  HOH   HOH B . 
N 6 HOH   70  2070 729  HOH   HOH B . 
N 6 HOH   71  2071 381  HOH   HOH B . 
N 6 HOH   72  2072 271  HOH   HOH B . 
N 6 HOH   73  2073 527  HOH   HOH B . 
N 6 HOH   74  2074 293  HOH   HOH B . 
N 6 HOH   75  2075 1194 HOH   HOH B . 
N 6 HOH   76  2076 162  HOH   HOH B . 
N 6 HOH   77  2077 21   HOH   HOH B . 
N 6 HOH   78  2078 1168 HOH   HOH B . 
N 6 HOH   79  2079 1042 HOH   HOH B . 
N 6 HOH   80  2080 913  HOH   HOH B . 
N 6 HOH   81  2081 725  HOH   HOH B . 
N 6 HOH   82  2082 208  HOH   HOH B . 
N 6 HOH   83  2083 589  HOH   HOH B . 
N 6 HOH   84  2084 203  HOH   HOH B . 
N 6 HOH   85  2085 1050 HOH   HOH B . 
N 6 HOH   86  2086 602  HOH   HOH B . 
N 6 HOH   87  2087 1162 HOH   HOH B . 
N 6 HOH   88  2088 57   HOH   HOH B . 
N 6 HOH   89  2089 726  HOH   HOH B . 
N 6 HOH   90  2090 105  HOH   HOH B . 
N 6 HOH   91  2091 50   HOH   HOH B . 
N 6 HOH   92  2092 966  HOH   HOH B . 
N 6 HOH   93  2093 1134 HOH   HOH B . 
N 6 HOH   94  2094 871  HOH   HOH B . 
N 6 HOH   95  2095 820  HOH   HOH B . 
N 6 HOH   96  2096 168  HOH   HOH B . 
N 6 HOH   97  2097 97   HOH   HOH B . 
N 6 HOH   98  2098 1169 HOH   HOH B . 
N 6 HOH   99  2099 14   HOH   HOH B . 
N 6 HOH   100 2100 784  HOH   HOH B . 
N 6 HOH   101 2101 70   HOH   HOH B . 
N 6 HOH   102 2102 731  HOH   HOH B . 
N 6 HOH   103 2103 175  HOH   HOH B . 
N 6 HOH   104 2104 280  HOH   HOH B . 
N 6 HOH   105 2105 54   HOH   HOH B . 
N 6 HOH   106 2106 114  HOH   HOH B . 
N 6 HOH   107 2107 226  HOH   HOH B . 
N 6 HOH   108 2108 1123 HOH   HOH B . 
N 6 HOH   109 2109 192  HOH   HOH B . 
N 6 HOH   110 2110 190  HOH   HOH B . 
N 6 HOH   111 2111 542  HOH   HOH B . 
N 6 HOH   112 2112 655  HOH   HOH B . 
N 6 HOH   113 2113 107  HOH   HOH B . 
N 6 HOH   114 2114 936  HOH   HOH B . 
N 6 HOH   115 2115 1141 HOH   HOH B . 
N 6 HOH   116 2116 108  HOH   HOH B . 
N 6 HOH   117 2117 545  HOH   HOH B . 
N 6 HOH   118 2118 153  HOH   HOH B . 
N 6 HOH   119 2119 850  HOH   HOH B . 
N 6 HOH   120 2120 136  HOH   HOH B . 
N 6 HOH   121 2121 628  HOH   HOH B . 
N 6 HOH   122 2122 525  HOH   HOH B . 
N 6 HOH   123 2123 975  HOH   HOH B . 
N 6 HOH   124 2124 1161 HOH   HOH B . 
N 6 HOH   125 2125 209  HOH   HOH B . 
N 6 HOH   126 2126 833  HOH   HOH B . 
N 6 HOH   127 2127 427  HOH   HOH B . 
N 6 HOH   128 2128 780  HOH   HOH B . 
N 6 HOH   129 2129 974  HOH   HOH B . 
N 6 HOH   130 2130 259  HOH   HOH B . 
N 6 HOH   131 2131 1075 HOH   HOH B . 
N 6 HOH   132 2132 444  HOH   HOH B . 
N 6 HOH   133 2133 1052 HOH   HOH B . 
N 6 HOH   134 2134 590  HOH   HOH B . 
N 6 HOH   135 2135 197  HOH   HOH B . 
N 6 HOH   136 2136 66   HOH   HOH B . 
N 6 HOH   137 2137 1152 HOH   HOH B . 
N 6 HOH   138 2138 1172 HOH   HOH B . 
N 6 HOH   139 2139 770  HOH   HOH B . 
N 6 HOH   140 2140 438  HOH   HOH B . 
N 6 HOH   141 2141 1132 HOH   HOH B . 
N 6 HOH   142 2142 348  HOH   HOH B . 
N 6 HOH   143 2143 1055 HOH   HOH B . 
N 6 HOH   144 2144 405  HOH   HOH B . 
N 6 HOH   145 2145 134  HOH   HOH B . 
N 6 HOH   146 2146 836  HOH   HOH B . 
N 6 HOH   147 2147 431  HOH   HOH B . 
N 6 HOH   148 2148 1196 HOH   HOH B . 
N 6 HOH   149 2149 49   HOH   HOH B . 
N 6 HOH   150 2150 961  HOH   HOH B . 
N 6 HOH   151 2151 926  HOH   HOH B . 
N 6 HOH   152 2152 1145 HOH   HOH B . 
N 6 HOH   153 2153 1174 HOH   HOH B . 
N 6 HOH   154 2154 1122 HOH   HOH B . 
N 6 HOH   155 2155 1040 HOH   HOH B . 
N 6 HOH   156 2156 534  HOH   HOH B . 
N 6 HOH   157 2157 951  HOH   HOH B . 
N 6 HOH   158 2158 840  HOH   HOH B . 
N 6 HOH   159 2159 1164 HOH   HOH B . 
N 6 HOH   160 2160 1115 HOH   HOH B . 
N 6 HOH   161 2161 59   HOH   HOH B . 
N 6 HOH   162 2162 1181 HOH   HOH B . 
N 6 HOH   163 2163 680  HOH   HOH B . 
N 6 HOH   164 2164 668  HOH   HOH B . 
N 6 HOH   165 2165 501  HOH   HOH B . 
N 6 HOH   166 2166 184  HOH   HOH B . 
N 6 HOH   167 2167 1056 HOH   HOH B . 
N 6 HOH   168 2168 442  HOH   HOH B . 
N 6 HOH   169 2169 110  HOH   HOH B . 
N 6 HOH   170 2170 752  HOH   HOH B . 
N 6 HOH   171 2171 1057 HOH   HOH B . 
N 6 HOH   172 2172 531  HOH   HOH B . 
N 6 HOH   173 2173 825  HOH   HOH B . 
N 6 HOH   174 2174 187  HOH   HOH B . 
N 6 HOH   175 2175 950  HOH   HOH B . 
N 6 HOH   176 2176 1149 HOH   HOH B . 
N 6 HOH   177 2177 1071 HOH   HOH B . 
N 6 HOH   178 2178 1154 HOH   HOH B . 
N 6 HOH   179 2179 586  HOH   HOH B . 
N 6 HOH   180 2180 1151 HOH   HOH B . 
N 6 HOH   181 2181 623  HOH   HOH B . 
N 6 HOH   182 2182 827  HOH   HOH B . 
N 6 HOH   183 2183 245  HOH   HOH B . 
N 6 HOH   184 2184 732  HOH   HOH B . 
N 6 HOH   185 2185 1113 HOH   HOH B . 
N 6 HOH   186 2186 1166 HOH   HOH B . 
N 6 HOH   187 2187 948  HOH   HOH B . 
N 6 HOH   188 2188 1074 HOH   HOH B . 
N 6 HOH   189 2189 1187 HOH   HOH B . 
N 6 HOH   190 2190 1193 HOH   HOH B . 
N 6 HOH   191 2191 335  HOH   HOH B . 
N 6 HOH   192 2192 707  HOH   HOH B . 
N 6 HOH   193 2193 686  HOH   HOH B . 
N 6 HOH   194 2194 1137 HOH   HOH B . 
N 6 HOH   195 2195 728  HOH   HOH B . 
N 6 HOH   196 2196 1136 HOH   HOH B . 
N 6 HOH   197 2197 957  HOH   HOH B . 
N 6 HOH   198 2198 649  HOH   HOH B . 
N 6 HOH   199 2199 980  HOH   HOH B . 
N 6 HOH   200 2200 1104 HOH   HOH B . 
N 6 HOH   201 2201 1081 HOH   HOH B . 
N 6 HOH   202 2202 977  HOH   HOH B . 
N 6 HOH   203 2203 1138 HOH   HOH B . 
N 6 HOH   204 2204 795  HOH   HOH B . 
N 6 HOH   205 2205 1150 HOH   HOH B . 
N 6 HOH   206 2206 1186 HOH   HOH B . 
N 6 HOH   207 2207 1049 HOH   HOH B . 
N 6 HOH   208 2208 1108 HOH   HOH B . 
N 6 HOH   209 2209 1051 HOH   HOH B . 
N 6 HOH   210 2210 1082 HOH   HOH B . 
N 6 HOH   211 2211 1084 HOH   HOH B . 
N 6 HOH   212 2212 1039 HOH   HOH B . 
N 6 HOH   213 2213 1165 HOH   HOH B . 
N 6 HOH   214 2214 1191 HOH   HOH B . 
N 6 HOH   215 2215 1106 HOH   HOH B . 
N 6 HOH   216 2216 1107 HOH   HOH B . 
N 6 HOH   217 2217 1054 HOH   HOH B . 
N 6 HOH   218 2218 1076 HOH   HOH B . 
N 6 HOH   219 2219 1124 HOH   HOH B . 
N 6 HOH   220 2220 1155 HOH   HOH B . 
N 6 HOH   221 2221 923  HOH   HOH B . 
N 6 HOH   222 2222 868  HOH   HOH B . 
N 6 HOH   223 2223 1140 HOH   HOH B . 
N 6 HOH   224 2224 956  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 LYS 34   ? CG  ? A LYS 34   CG  
2   1 Y 1 A LYS 34   ? CD  ? A LYS 34   CD  
3   1 Y 1 A LYS 34   ? CE  ? A LYS 34   CE  
4   1 Y 1 A LYS 34   ? NZ  ? A LYS 34   NZ  
5   1 Y 1 A GLU 331  ? CG  ? A GLU 331  CG  
6   1 Y 1 A GLU 331  ? CD  ? A GLU 331  CD  
7   1 Y 1 A GLU 331  ? OE1 ? A GLU 331  OE1 
8   1 Y 1 A GLU 331  ? OE2 ? A GLU 331  OE2 
9   1 Y 1 A ARG 594  ? CG  ? A ARG 594  CG  
10  1 Y 1 A ARG 594  ? CD  ? A ARG 594  CD  
11  1 Y 1 A ARG 594  ? NE  ? A ARG 594  NE  
12  1 Y 1 A ARG 594  ? CZ  ? A ARG 594  CZ  
13  1 Y 1 A ARG 594  ? NH1 ? A ARG 594  NH1 
14  1 Y 1 A ARG 594  ? NH2 ? A ARG 594  NH2 
15  1 Y 1 A ARG 624  ? CG  ? A ARG 624  CG  
16  1 Y 1 A ARG 624  ? CD  ? A ARG 624  CD  
17  1 Y 1 A ARG 624  ? NE  ? A ARG 624  NE  
18  1 Y 1 A ARG 624  ? CZ  ? A ARG 624  CZ  
19  1 Y 1 A ARG 624  ? NH1 ? A ARG 624  NH1 
20  1 Y 1 A ARG 624  ? NH2 ? A ARG 624  NH2 
21  1 Y 1 A GLU 635  ? CG  ? A GLU 635  CG  
22  1 Y 1 A GLU 635  ? CD  ? A GLU 635  CD  
23  1 Y 1 A GLU 635  ? OE1 ? A GLU 635  OE1 
24  1 Y 1 A GLU 635  ? OE2 ? A GLU 635  OE2 
25  1 Y 1 A ARG 776  ? CG  ? A ARG 778  CG  
26  1 Y 1 A ARG 776  ? CD  ? A ARG 778  CD  
27  1 Y 1 A ARG 776  ? NE  ? A ARG 778  NE  
28  1 Y 1 A ARG 776  ? CZ  ? A ARG 778  CZ  
29  1 Y 1 A ARG 776  ? NH1 ? A ARG 778  NH1 
30  1 Y 1 A ARG 776  ? NH2 ? A ARG 778  NH2 
31  1 Y 1 A ARG 1103 ? CG  ? A ARG 1105 CG  
32  1 Y 1 A ARG 1103 ? CD  ? A ARG 1105 CD  
33  1 Y 1 A ARG 1103 ? NE  ? A ARG 1105 NE  
34  1 Y 1 A ARG 1103 ? CZ  ? A ARG 1105 CZ  
35  1 Y 1 A ARG 1103 ? NH1 ? A ARG 1105 NH1 
36  1 Y 1 A ARG 1103 ? NH2 ? A ARG 1105 NH2 
37  1 Y 1 A GLU 1308 ? CG  ? A GLU 1310 CG  
38  1 Y 1 A GLU 1308 ? CD  ? A GLU 1310 CD  
39  1 Y 1 A GLU 1308 ? OE1 ? A GLU 1310 OE1 
40  1 Y 1 A GLU 1308 ? OE2 ? A GLU 1310 OE2 
41  1 Y 1 A LYS 1320 ? CG  ? A LYS 1322 CG  
42  1 Y 1 A LYS 1320 ? CD  ? A LYS 1322 CD  
43  1 Y 1 A LYS 1320 ? CE  ? A LYS 1322 CE  
44  1 Y 1 A LYS 1320 ? NZ  ? A LYS 1322 NZ  
45  1 Y 1 A GLU 1330 ? CG  ? A GLU 1332 CG  
46  1 Y 1 A GLU 1330 ? CD  ? A GLU 1332 CD  
47  1 Y 1 A GLU 1330 ? OE1 ? A GLU 1332 OE1 
48  1 Y 1 A GLU 1330 ? OE2 ? A GLU 1332 OE2 
49  1 Y 1 A MET 1334 ? CG  ? A MET 1336 CG  
50  1 Y 1 A MET 1334 ? SD  ? A MET 1336 SD  
51  1 Y 1 A MET 1334 ? CE  ? A MET 1336 CE  
52  1 Y 1 A LYS 1377 ? CG  ? A LYS 1379 CG  
53  1 Y 1 A LYS 1377 ? CD  ? A LYS 1379 CD  
54  1 Y 1 A LYS 1377 ? CE  ? A LYS 1379 CE  
55  1 Y 1 A LYS 1377 ? NZ  ? A LYS 1379 NZ  
56  1 Y 1 A LYS 1635 ? CG  ? A LYS 1637 CG  
57  1 Y 1 A LYS 1635 ? CD  ? A LYS 1637 CD  
58  1 Y 1 A LYS 1635 ? CE  ? A LYS 1637 CE  
59  1 Y 1 A LYS 1635 ? NZ  ? A LYS 1637 NZ  
60  1 Y 1 A ILE 1637 ? CG1 ? A ILE 1639 CG1 
61  1 Y 1 A ILE 1637 ? CG2 ? A ILE 1639 CG2 
62  1 Y 1 A ILE 1637 ? CD1 ? A ILE 1639 CD1 
63  1 Y 1 A LEU 1674 ? CG  ? A LEU 1676 CG  
64  1 Y 1 A LEU 1674 ? CD1 ? A LEU 1676 CD1 
65  1 Y 1 A LEU 1674 ? CD2 ? A LEU 1676 CD2 
66  1 Y 1 B GLU 33   ? CG  ? B GLU 33   CG  
67  1 Y 1 B GLU 33   ? CD  ? B GLU 33   CD  
68  1 Y 1 B GLU 33   ? OE1 ? B GLU 33   OE1 
69  1 Y 1 B GLU 33   ? OE2 ? B GLU 33   OE2 
70  1 Y 1 B GLU 44   ? CG  ? B GLU 44   CG  
71  1 Y 1 B GLU 44   ? CD  ? B GLU 44   CD  
72  1 Y 1 B GLU 44   ? OE1 ? B GLU 44   OE1 
73  1 Y 1 B GLU 44   ? OE2 ? B GLU 44   OE2 
74  1 Y 1 B LYS 59   ? CG  ? B LYS 59   CG  
75  1 Y 1 B LYS 59   ? CD  ? B LYS 59   CD  
76  1 Y 1 B LYS 59   ? CE  ? B LYS 59   CE  
77  1 Y 1 B LYS 59   ? NZ  ? B LYS 59   NZ  
78  1 Y 1 B GLU 60   ? CG  ? B GLU 60   CG  
79  1 Y 1 B GLU 60   ? CD  ? B GLU 60   CD  
80  1 Y 1 B GLU 60   ? OE1 ? B GLU 60   OE1 
81  1 Y 1 B GLU 60   ? OE2 ? B GLU 60   OE2 
82  1 Y 1 B ARG 66   ? CG  ? B ARG 66   CG  
83  1 Y 1 B ARG 66   ? CD  ? B ARG 66   CD  
84  1 Y 1 B ARG 66   ? NE  ? B ARG 66   NE  
85  1 Y 1 B ARG 66   ? CZ  ? B ARG 66   CZ  
86  1 Y 1 B ARG 66   ? NH1 ? B ARG 66   NH1 
87  1 Y 1 B ARG 66   ? NH2 ? B ARG 66   NH2 
88  1 Y 1 B ARG 157  ? CG  ? B ARG 157  CG  
89  1 Y 1 B ARG 157  ? CD  ? B ARG 157  CD  
90  1 Y 1 B ARG 157  ? NE  ? B ARG 157  NE  
91  1 Y 1 B ARG 157  ? CZ  ? B ARG 157  CZ  
92  1 Y 1 B ARG 157  ? NH1 ? B ARG 157  NH1 
93  1 Y 1 B ARG 157  ? NH2 ? B ARG 157  NH2 
94  1 Y 1 B GLU 198  ? CG  ? B GLU 198  CG  
95  1 Y 1 B GLU 198  ? CD  ? B GLU 198  CD  
96  1 Y 1 B GLU 198  ? OE1 ? B GLU 198  OE1 
97  1 Y 1 B GLU 198  ? OE2 ? B GLU 198  OE2 
98  1 Y 1 B LYS 199  ? CG  ? B LYS 199  CG  
99  1 Y 1 B LYS 199  ? CD  ? B LYS 199  CD  
100 1 Y 1 B LYS 199  ? CE  ? B LYS 199  CE  
101 1 Y 1 B LYS 199  ? NZ  ? B LYS 199  NZ  
102 1 Y 1 B ASN 586  ? CG  ? B ASN 586  CG  
103 1 Y 1 B ASN 586  ? OD1 ? B ASN 586  OD1 
104 1 Y 1 B ASN 586  ? ND2 ? B ASN 586  ND2 
105 1 Y 1 B ARG 594  ? CG  ? B ARG 594  CG  
106 1 Y 1 B ARG 594  ? CD  ? B ARG 594  CD  
107 1 Y 1 B ARG 594  ? NE  ? B ARG 594  NE  
108 1 Y 1 B ARG 594  ? CZ  ? B ARG 594  CZ  
109 1 Y 1 B ARG 594  ? NH1 ? B ARG 594  NH1 
110 1 Y 1 B ARG 594  ? NH2 ? B ARG 594  NH2 
111 1 Y 1 B GLU 635  ? CG  ? B GLU 635  CG  
112 1 Y 1 B GLU 635  ? CD  ? B GLU 635  CD  
113 1 Y 1 B GLU 635  ? OE1 ? B GLU 635  OE1 
114 1 Y 1 B GLU 635  ? OE2 ? B GLU 635  OE2 
115 1 Y 1 B GLU 636  ? CG  ? B GLU 636  CG  
116 1 Y 1 B GLU 636  ? CD  ? B GLU 636  CD  
117 1 Y 1 B GLU 636  ? OE1 ? B GLU 636  OE1 
118 1 Y 1 B GLU 636  ? OE2 ? B GLU 636  OE2 
119 1 Y 1 B LYS 663  ? CG  ? B LYS 663  CG  
120 1 Y 1 B LYS 663  ? CD  ? B LYS 663  CD  
121 1 Y 1 B LYS 663  ? CE  ? B LYS 663  CE  
122 1 Y 1 B LYS 663  ? NZ  ? B LYS 663  NZ  
123 1 Y 1 B ARG 676  ? CG  ? B ARG 676  CG  
124 1 Y 1 B ARG 676  ? CD  ? B ARG 676  CD  
125 1 Y 1 B ARG 676  ? NE  ? B ARG 676  NE  
126 1 Y 1 B ARG 676  ? CZ  ? B ARG 676  CZ  
127 1 Y 1 B ARG 676  ? NH1 ? B ARG 676  NH1 
128 1 Y 1 B ARG 676  ? NH2 ? B ARG 676  NH2 
129 1 Y 1 B ASP 691  ? CG  ? B ASP 691  CG  
130 1 Y 1 B ASP 691  ? OD1 ? B ASP 691  OD1 
131 1 Y 1 B ASP 691  ? OD2 ? B ASP 691  OD2 
132 1 Y 1 B ARG 776  ? CG  ? B ARG 778  CG  
133 1 Y 1 B ARG 776  ? CD  ? B ARG 778  CD  
134 1 Y 1 B ARG 776  ? NE  ? B ARG 778  NE  
135 1 Y 1 B ARG 776  ? CZ  ? B ARG 778  CZ  
136 1 Y 1 B ARG 776  ? NH1 ? B ARG 778  NH1 
137 1 Y 1 B ARG 776  ? NH2 ? B ARG 778  NH2 
138 1 Y 1 B ARG 855  ? CG  ? B ARG 857  CG  
139 1 Y 1 B ARG 855  ? CD  ? B ARG 857  CD  
140 1 Y 1 B ARG 855  ? NE  ? B ARG 857  NE  
141 1 Y 1 B ARG 855  ? CZ  ? B ARG 857  CZ  
142 1 Y 1 B ARG 855  ? NH1 ? B ARG 857  NH1 
143 1 Y 1 B ARG 855  ? NH2 ? B ARG 857  NH2 
144 1 Y 1 B ARG 944  ? CG  ? B ARG 946  CG  
145 1 Y 1 B ARG 944  ? CD  ? B ARG 946  CD  
146 1 Y 1 B ARG 944  ? NE  ? B ARG 946  NE  
147 1 Y 1 B ARG 944  ? CZ  ? B ARG 946  CZ  
148 1 Y 1 B ARG 944  ? NH1 ? B ARG 946  NH1 
149 1 Y 1 B ARG 944  ? NH2 ? B ARG 946  NH2 
150 1 Y 1 B ASP 953  ? CG  ? B ASP 955  CG  
151 1 Y 1 B ASP 953  ? OD1 ? B ASP 955  OD1 
152 1 Y 1 B ASP 953  ? OD2 ? B ASP 955  OD2 
153 1 Y 1 B GLU 969  ? CG  ? B GLU 971  CG  
154 1 Y 1 B GLU 969  ? CD  ? B GLU 971  CD  
155 1 Y 1 B GLU 969  ? OE1 ? B GLU 971  OE1 
156 1 Y 1 B GLU 969  ? OE2 ? B GLU 971  OE2 
157 1 Y 1 B LYS 979  ? CG  ? B LYS 981  CG  
158 1 Y 1 B LYS 979  ? CD  ? B LYS 981  CD  
159 1 Y 1 B LYS 979  ? CE  ? B LYS 981  CE  
160 1 Y 1 B LYS 979  ? NZ  ? B LYS 981  NZ  
161 1 Y 1 B GLN 983  ? CG  ? B GLN 985  CG  
162 1 Y 1 B GLN 983  ? CD  ? B GLN 985  CD  
163 1 Y 1 B GLN 983  ? OE1 ? B GLN 985  OE1 
164 1 Y 1 B GLN 983  ? NE2 ? B GLN 985  NE2 
165 1 Y 1 B LYS 1002 ? CG  ? B LYS 1004 CG  
166 1 Y 1 B LYS 1002 ? CD  ? B LYS 1004 CD  
167 1 Y 1 B LYS 1002 ? CE  ? B LYS 1004 CE  
168 1 Y 1 B LYS 1002 ? NZ  ? B LYS 1004 NZ  
169 1 Y 1 B GLN 1078 ? CG  ? B GLN 1080 CG  
170 1 Y 1 B GLN 1078 ? CD  ? B GLN 1080 CD  
171 1 Y 1 B GLN 1078 ? OE1 ? B GLN 1080 OE1 
172 1 Y 1 B GLN 1078 ? NE2 ? B GLN 1080 NE2 
173 1 Y 1 B LYS 1083 ? CG  ? B LYS 1085 CG  
174 1 Y 1 B LYS 1083 ? CD  ? B LYS 1085 CD  
175 1 Y 1 B LYS 1083 ? CE  ? B LYS 1085 CE  
176 1 Y 1 B LYS 1083 ? NZ  ? B LYS 1085 NZ  
177 1 Y 1 B LYS 1097 ? CG  ? B LYS 1099 CG  
178 1 Y 1 B LYS 1097 ? CD  ? B LYS 1099 CD  
179 1 Y 1 B LYS 1097 ? CE  ? B LYS 1099 CE  
180 1 Y 1 B LYS 1097 ? NZ  ? B LYS 1099 NZ  
181 1 Y 1 B LYS 1105 ? CG  ? B LYS 1107 CG  
182 1 Y 1 B LYS 1105 ? CD  ? B LYS 1107 CD  
183 1 Y 1 B LYS 1105 ? CE  ? B LYS 1107 CE  
184 1 Y 1 B LYS 1105 ? NZ  ? B LYS 1107 NZ  
185 1 Y 1 B ARG 1106 ? CG  ? B ARG 1108 CG  
186 1 Y 1 B ARG 1106 ? CD  ? B ARG 1108 CD  
187 1 Y 1 B ARG 1106 ? NE  ? B ARG 1108 NE  
188 1 Y 1 B ARG 1106 ? CZ  ? B ARG 1108 CZ  
189 1 Y 1 B ARG 1106 ? NH1 ? B ARG 1108 NH1 
190 1 Y 1 B ARG 1106 ? NH2 ? B ARG 1108 NH2 
191 1 Y 1 B GLU 1168 ? CG  ? B GLU 1170 CG  
192 1 Y 1 B GLU 1168 ? CD  ? B GLU 1170 CD  
193 1 Y 1 B GLU 1168 ? OE1 ? B GLU 1170 OE1 
194 1 Y 1 B GLU 1168 ? OE2 ? B GLU 1170 OE2 
195 1 Y 1 B LYS 1221 ? CG  ? B LYS 1223 CG  
196 1 Y 1 B LYS 1221 ? CD  ? B LYS 1223 CD  
197 1 Y 1 B LYS 1221 ? CE  ? B LYS 1223 CE  
198 1 Y 1 B LYS 1221 ? NZ  ? B LYS 1223 NZ  
199 1 Y 1 B GLU 1254 ? CG  ? B GLU 1256 CG  
200 1 Y 1 B GLU 1254 ? CD  ? B GLU 1256 CD  
201 1 Y 1 B GLU 1254 ? OE1 ? B GLU 1256 OE1 
202 1 Y 1 B GLU 1254 ? OE2 ? B GLU 1256 OE2 
203 1 Y 1 B PHE 1314 ? CG  ? B PHE 1316 CG  
204 1 Y 1 B PHE 1314 ? CD1 ? B PHE 1316 CD1 
205 1 Y 1 B PHE 1314 ? CD2 ? B PHE 1316 CD2 
206 1 Y 1 B PHE 1314 ? CE1 ? B PHE 1316 CE1 
207 1 Y 1 B PHE 1314 ? CE2 ? B PHE 1316 CE2 
208 1 Y 1 B PHE 1314 ? CZ  ? B PHE 1316 CZ  
209 1 Y 1 B LYS 1320 ? CG  ? B LYS 1322 CG  
210 1 Y 1 B LYS 1320 ? CD  ? B LYS 1322 CD  
211 1 Y 1 B LYS 1320 ? CE  ? B LYS 1322 CE  
212 1 Y 1 B LYS 1320 ? NZ  ? B LYS 1322 NZ  
213 1 Y 1 B LYS 1375 ? CG  ? B LYS 1377 CG  
214 1 Y 1 B LYS 1375 ? CD  ? B LYS 1377 CD  
215 1 Y 1 B LYS 1375 ? CE  ? B LYS 1377 CE  
216 1 Y 1 B LYS 1375 ? NZ  ? B LYS 1377 NZ  
217 1 Y 1 B LYS 1377 ? CG  ? B LYS 1379 CG  
218 1 Y 1 B LYS 1377 ? CD  ? B LYS 1379 CD  
219 1 Y 1 B LYS 1377 ? CE  ? B LYS 1379 CE  
220 1 Y 1 B LYS 1377 ? NZ  ? B LYS 1379 NZ  
221 1 Y 1 B ARG 1427 ? CG  ? B ARG 1429 CG  
222 1 Y 1 B ARG 1427 ? CD  ? B ARG 1429 CD  
223 1 Y 1 B ARG 1427 ? NE  ? B ARG 1429 NE  
224 1 Y 1 B ARG 1427 ? CZ  ? B ARG 1429 CZ  
225 1 Y 1 B ARG 1427 ? NH1 ? B ARG 1429 NH1 
226 1 Y 1 B ARG 1427 ? NH2 ? B ARG 1429 NH2 
227 1 Y 1 B LYS 1429 ? CG  ? B LYS 1431 CG  
228 1 Y 1 B LYS 1429 ? CD  ? B LYS 1431 CD  
229 1 Y 1 B LYS 1429 ? CE  ? B LYS 1431 CE  
230 1 Y 1 B LYS 1429 ? NZ  ? B LYS 1431 NZ  
231 1 Y 1 B LYS 1442 ? CG  ? B LYS 1444 CG  
232 1 Y 1 B LYS 1442 ? CD  ? B LYS 1444 CD  
233 1 Y 1 B LYS 1442 ? CE  ? B LYS 1444 CE  
234 1 Y 1 B LYS 1442 ? NZ  ? B LYS 1444 NZ  
235 1 Y 1 B ARG 1473 ? CG  ? B ARG 1475 CG  
236 1 Y 1 B ARG 1473 ? CD  ? B ARG 1475 CD  
237 1 Y 1 B ARG 1473 ? NE  ? B ARG 1475 NE  
238 1 Y 1 B ARG 1473 ? CZ  ? B ARG 1475 CZ  
239 1 Y 1 B ARG 1473 ? NH1 ? B ARG 1475 NH1 
240 1 Y 1 B ARG 1473 ? NH2 ? B ARG 1475 NH2 
241 1 Y 1 B GLU 1487 ? CG  ? B GLU 1489 CG  
242 1 Y 1 B GLU 1487 ? CD  ? B GLU 1489 CD  
243 1 Y 1 B GLU 1487 ? OE1 ? B GLU 1489 OE1 
244 1 Y 1 B GLU 1487 ? OE2 ? B GLU 1489 OE2 
245 1 Y 1 B GLU 1492 ? CG  ? B GLU 1494 CG  
246 1 Y 1 B GLU 1492 ? CD  ? B GLU 1494 CD  
247 1 Y 1 B GLU 1492 ? OE1 ? B GLU 1494 OE1 
248 1 Y 1 B GLU 1492 ? OE2 ? B GLU 1494 OE2 
249 1 Y 1 B LEU 1493 ? CG  ? B LEU 1495 CG  
250 1 Y 1 B LEU 1493 ? CD1 ? B LEU 1495 CD1 
251 1 Y 1 B LEU 1493 ? CD2 ? B LEU 1495 CD2 
252 1 Y 1 B LYS 1496 ? CG  ? B LYS 1498 CG  
253 1 Y 1 B LYS 1496 ? CD  ? B LYS 1498 CD  
254 1 Y 1 B LYS 1496 ? CE  ? B LYS 1498 CE  
255 1 Y 1 B LYS 1496 ? NZ  ? B LYS 1498 NZ  
256 1 Y 1 B GLU 1499 ? CG  ? B GLU 1501 CG  
257 1 Y 1 B GLU 1499 ? CD  ? B GLU 1501 CD  
258 1 Y 1 B GLU 1499 ? OE1 ? B GLU 1501 OE1 
259 1 Y 1 B GLU 1499 ? OE2 ? B GLU 1501 OE2 
260 1 Y 1 B LYS 1505 ? CG  ? B LYS 1507 CG  
261 1 Y 1 B LYS 1505 ? CD  ? B LYS 1507 CD  
262 1 Y 1 B LYS 1505 ? CE  ? B LYS 1507 CE  
263 1 Y 1 B LYS 1505 ? NZ  ? B LYS 1507 NZ  
264 1 Y 1 B LYS 1526 ? CG  ? B LYS 1528 CG  
265 1 Y 1 B LYS 1526 ? CD  ? B LYS 1528 CD  
266 1 Y 1 B LYS 1526 ? CE  ? B LYS 1528 CE  
267 1 Y 1 B LYS 1526 ? NZ  ? B LYS 1528 NZ  
268 1 Y 1 B GLN 1529 ? CG  ? B GLN 1531 CG  
269 1 Y 1 B GLN 1529 ? CD  ? B GLN 1531 CD  
270 1 Y 1 B GLN 1529 ? OE1 ? B GLN 1531 OE1 
271 1 Y 1 B GLN 1529 ? NE2 ? B GLN 1531 NE2 
272 1 Y 1 B ASP 1617 ? CG  ? B ASP 1619 CG  
273 1 Y 1 B ASP 1617 ? OD1 ? B ASP 1619 OD1 
274 1 Y 1 B ASP 1617 ? OD2 ? B ASP 1619 OD2 
275 1 Y 1 B HIS 1618 ? CG  ? B HIS 1620 CG  
276 1 Y 1 B HIS 1618 ? ND1 ? B HIS 1620 ND1 
277 1 Y 1 B HIS 1618 ? CD2 ? B HIS 1620 CD2 
278 1 Y 1 B HIS 1618 ? CE1 ? B HIS 1620 CE1 
279 1 Y 1 B HIS 1618 ? NE2 ? B HIS 1620 NE2 
280 1 Y 1 B GLU 1628 ? CG  ? B GLU 1630 CG  
281 1 Y 1 B GLU 1628 ? CD  ? B GLU 1630 CD  
282 1 Y 1 B GLU 1628 ? OE1 ? B GLU 1630 OE1 
283 1 Y 1 B GLU 1628 ? OE2 ? B GLU 1630 OE2 
284 1 Y 1 B ASP 1630 ? CG  ? B ASP 1632 CG  
285 1 Y 1 B ASP 1630 ? OD1 ? B ASP 1632 OD1 
286 1 Y 1 B ASP 1630 ? OD2 ? B ASP 1632 OD2 
287 1 Y 1 B GLU 1631 ? CG  ? B GLU 1633 CG  
288 1 Y 1 B GLU 1631 ? CD  ? B GLU 1633 CD  
289 1 Y 1 B GLU 1631 ? OE1 ? B GLU 1633 OE1 
290 1 Y 1 B GLU 1631 ? OE2 ? B GLU 1633 OE2 
291 1 Y 1 B ARG 1633 ? CG  ? B ARG 1635 CG  
292 1 Y 1 B ARG 1633 ? CD  ? B ARG 1635 CD  
293 1 Y 1 B ARG 1633 ? NE  ? B ARG 1635 NE  
294 1 Y 1 B ARG 1633 ? CZ  ? B ARG 1635 CZ  
295 1 Y 1 B ARG 1633 ? NH1 ? B ARG 1635 NH1 
296 1 Y 1 B ARG 1633 ? NH2 ? B ARG 1635 NH2 
297 1 Y 1 B LYS 1635 ? CG  ? B LYS 1637 CG  
298 1 Y 1 B LYS 1635 ? CD  ? B LYS 1637 CD  
299 1 Y 1 B LYS 1635 ? CE  ? B LYS 1637 CE  
300 1 Y 1 B LYS 1635 ? NZ  ? B LYS 1637 NZ  
301 1 Y 1 B ILE 1637 ? CG1 ? B ILE 1639 CG1 
302 1 Y 1 B ILE 1637 ? CG2 ? B ILE 1639 CG2 
303 1 Y 1 B ILE 1637 ? CD1 ? B ILE 1639 CD1 
304 1 Y 1 B ASP 1652 ? CG  ? B ASP 1654 CG  
305 1 Y 1 B ASP 1652 ? OD1 ? B ASP 1654 OD1 
306 1 Y 1 B ASP 1652 ? OD2 ? B ASP 1654 OD2 
307 1 Y 1 B GLN 1653 ? CG  ? B GLN 1655 CG  
308 1 Y 1 B GLN 1653 ? CD  ? B GLN 1655 CD  
309 1 Y 1 B GLN 1653 ? OE1 ? B GLN 1655 OE1 
310 1 Y 1 B GLN 1653 ? NE2 ? B GLN 1655 NE2 
311 1 Y 1 B ASN 1654 ? CG  ? B ASN 1656 CG  
312 1 Y 1 B ASN 1654 ? OD1 ? B ASN 1656 OD1 
313 1 Y 1 B ASN 1654 ? ND2 ? B ASN 1656 ND2 
314 1 Y 1 B TYR 1658 ? CG  ? B TYR 1660 CG  
315 1 Y 1 B TYR 1658 ? CD1 ? B TYR 1660 CD1 
316 1 Y 1 B TYR 1658 ? CD2 ? B TYR 1660 CD2 
317 1 Y 1 B TYR 1658 ? CE1 ? B TYR 1660 CE1 
318 1 Y 1 B TYR 1658 ? CE2 ? B TYR 1660 CE2 
319 1 Y 1 B TYR 1658 ? CZ  ? B TYR 1660 CZ  
320 1 Y 1 B TYR 1658 ? OH  ? B TYR 1660 OH  
321 1 Y 1 B LEU 1659 ? CG  ? B LEU 1661 CG  
322 1 Y 1 B LEU 1659 ? CD1 ? B LEU 1661 CD1 
323 1 Y 1 B LEU 1659 ? CD2 ? B LEU 1661 CD2 
324 1 Y 1 B GLN 1673 ? CG  ? B GLN 1675 CG  
325 1 Y 1 B GLN 1673 ? CD  ? B GLN 1675 CD  
326 1 Y 1 B GLN 1673 ? OE1 ? B GLN 1675 OE1 
327 1 Y 1 B GLN 1673 ? NE2 ? B GLN 1675 NE2 
328 1 Y 1 B LEU 1674 ? CG  ? B LEU 1676 CG  
329 1 Y 1 B LEU 1674 ? CD1 ? B LEU 1676 CD1 
330 1 Y 1 B LEU 1674 ? CD2 ? B LEU 1676 CD2 
331 1 Y 1 B ARG 1675 ? CG  ? B ARG 1677 CG  
332 1 Y 1 B ARG 1675 ? CD  ? B ARG 1677 CD  
333 1 Y 1 B ARG 1675 ? NE  ? B ARG 1677 NE  
334 1 Y 1 B ARG 1675 ? CZ  ? B ARG 1677 CZ  
335 1 Y 1 B ARG 1675 ? NH1 ? B ARG 1677 NH1 
336 1 Y 1 B ARG 1675 ? NH2 ? B ARG 1677 NH2 
337 1 Y 1 B GLU 1676 ? CG  ? B GLU 1678 CG  
338 1 Y 1 B GLU 1676 ? CD  ? B GLU 1678 CD  
339 1 Y 1 B GLU 1676 ? OE1 ? B GLU 1678 OE1 
340 1 Y 1 B GLU 1676 ? OE2 ? B GLU 1678 OE2 
341 1 Y 1 B LEU 1678 ? CG  ? B LEU 1680 CG  
342 1 Y 1 B LEU 1678 ? CD1 ? B LEU 1680 CD1 
343 1 Y 1 B LEU 1678 ? CD2 ? B LEU 1680 CD2 
344 1 Y 1 B ARG 1679 ? CG  ? B ARG 1681 CG  
345 1 Y 1 B ARG 1679 ? CD  ? B ARG 1681 CD  
346 1 Y 1 B ARG 1679 ? NE  ? B ARG 1681 NE  
347 1 Y 1 B ARG 1679 ? CZ  ? B ARG 1681 CZ  
348 1 Y 1 B ARG 1679 ? NH1 ? B ARG 1681 NH1 
349 1 Y 1 B ARG 1679 ? NH2 ? B ARG 1681 NH2 
350 1 Y 1 B ARG 1680 ? CG  ? B ARG 1682 CG  
351 1 Y 1 B ARG 1680 ? CD  ? B ARG 1682 CD  
352 1 Y 1 B ARG 1680 ? NE  ? B ARG 1682 NE  
353 1 Y 1 B ARG 1680 ? CZ  ? B ARG 1682 CZ  
354 1 Y 1 B ARG 1680 ? NH1 ? B ARG 1682 NH1 
355 1 Y 1 B ARG 1680 ? NH2 ? B ARG 1682 NH2 
356 1 Y 1 B LEU 1682 ? CG  ? B LEU 1684 CG  
357 1 Y 1 B LEU 1682 ? CD1 ? B LEU 1684 CD1 
358 1 Y 1 B LEU 1682 ? CD2 ? B LEU 1684 CD2 
359 1 Y 1 B GLU 1684 ? CG  ? B GLU 1686 CG  
360 1 Y 1 B GLU 1684 ? CD  ? B GLU 1686 CD  
361 1 Y 1 B GLU 1684 ? OE1 ? B GLU 1686 OE1 
362 1 Y 1 B GLU 1684 ? OE2 ? B GLU 1686 OE2 
363 1 Y 1 B TYR 1685 ? CG  ? B TYR 1687 CG  
364 1 Y 1 B TYR 1685 ? CD1 ? B TYR 1687 CD1 
365 1 Y 1 B TYR 1685 ? CD2 ? B TYR 1687 CD2 
366 1 Y 1 B TYR 1685 ? CE1 ? B TYR 1687 CE1 
367 1 Y 1 B TYR 1685 ? CE2 ? B TYR 1687 CE2 
368 1 Y 1 B TYR 1685 ? CZ  ? B TYR 1687 CZ  
369 1 Y 1 B TYR 1685 ? OH  ? B TYR 1687 OH  
370 1 Y 1 B MET 1686 ? CG  ? B MET 1688 CG  
371 1 Y 1 B MET 1686 ? SD  ? B MET 1688 SD  
372 1 Y 1 B MET 1686 ? CE  ? B MET 1688 CE  
373 1 Y 1 B ILE 1687 ? CG1 ? B ILE 1689 CG1 
374 1 Y 1 B ILE 1687 ? CG2 ? B ILE 1689 CG2 
375 1 Y 1 B ILE 1687 ? CD1 ? B ILE 1689 CD1 
376 1 Y 1 B ARG 1727 ? CG  ? B ARG 1729 CG  
377 1 Y 1 B ARG 1727 ? CD  ? B ARG 1729 CD  
378 1 Y 1 B ARG 1727 ? NE  ? B ARG 1729 NE  
379 1 Y 1 B ARG 1727 ? CZ  ? B ARG 1729 CZ  
380 1 Y 1 B ARG 1727 ? NH1 ? B ARG 1729 NH1 
381 1 Y 1 B ARG 1727 ? NH2 ? B ARG 1729 NH2 
382 1 Y 1 B THR 1728 ? OG1 ? B THR 1730 OG1 
383 1 Y 1 B THR 1728 ? CG2 ? B THR 1730 CG2 
384 1 Y 1 B ARG 1746 ? CG  ? B ARG 1748 CG  
385 1 Y 1 B ARG 1746 ? CD  ? B ARG 1748 CD  
386 1 Y 1 B ARG 1746 ? NE  ? B ARG 1748 NE  
387 1 Y 1 B ARG 1746 ? CZ  ? B ARG 1748 CZ  
388 1 Y 1 B ARG 1746 ? NH1 ? B ARG 1748 NH1 
389 1 Y 1 B ARG 1746 ? NH2 ? B ARG 1748 NH2 
390 1 Y 1 B ARG 1750 ? CG  ? B ARG 1752 CG  
391 1 Y 1 B ARG 1750 ? CD  ? B ARG 1752 CD  
392 1 Y 1 B ARG 1750 ? NE  ? B ARG 1752 NE  
393 1 Y 1 B ARG 1750 ? CZ  ? B ARG 1752 CZ  
394 1 Y 1 B ARG 1750 ? NH1 ? B ARG 1752 NH1 
395 1 Y 1 B ARG 1750 ? NH2 ? B ARG 1752 NH2 
396 1 Y 1 B GLU 1755 ? CG  ? B GLU 1757 CG  
397 1 Y 1 B GLU 1755 ? CD  ? B GLU 1757 CD  
398 1 Y 1 B GLU 1755 ? OE1 ? B GLU 1757 OE1 
399 1 Y 1 B GLU 1755 ? OE2 ? B GLU 1757 OE2 
400 1 Y 1 B GLU 1789 ? CG  ? B GLU 1791 CG  
401 1 Y 1 B GLU 1789 ? CD  ? B GLU 1791 CD  
402 1 Y 1 B GLU 1789 ? OE1 ? B GLU 1791 OE1 
403 1 Y 1 B GLU 1789 ? OE2 ? B GLU 1791 OE2 
404 1 Y 1 B GLN 1790 ? CG  ? B GLN 1792 CG  
405 1 Y 1 B GLN 1790 ? CD  ? B GLN 1792 CD  
406 1 Y 1 B GLN 1790 ? OE1 ? B GLN 1792 OE1 
407 1 Y 1 B GLN 1790 ? NE2 ? B GLN 1792 NE2 
# 
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   ? ? ? 1.20.1_4487 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                     9BE3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     184.816 
_cell.length_a_esd                 ? 
_cell.length_b                     427.905 
_cell.length_b_esd                 ? 
_cell.length_c                     77.318 
_cell.length_c_esd                 ? 
_cell.volume                       6114592.781 
_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                         9BE3 
_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                   9BE3 
_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             3.76 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          67.25 
_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         2022-09-22 
_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                          58.31 
_reflns.entry_id                                       9BE3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.84 
_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                                     144224 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.877 
_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                                0.198 
_reflns.pdbx_Rpim_I_all                                0.073 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.990 
_reflns.pdbx_CC_star                                   0.997 
_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                                    2.84 
_reflns_shell.d_res_low                                     2.89 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.846 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7058 
_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                               5.2 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.666 
_reflns_shell.pdbx_Rpim_I_all                               0.694 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.336 
_reflns_shell.pdbx_CC_star                                  0.709 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.5 
_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                               61.07 
_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                                 9BE3 
_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                            2.90 
_refine.ls_d_res_low                             48.74 
_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                     135580 
_refine.ls_number_reflns_R_free                  2963 
_refine.ls_number_reflns_R_work                  132617 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.92 
_refine.ls_percent_reflns_R_free                 2.19 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2166 
_refine.ls_R_factor_R_free                       0.2583 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2157 
_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                 26.7275 
_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                            0.3684 
_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                       2.90 
_refine_hist.d_res_low                        48.74 
_refine_hist.number_atoms_solvent             501 
_refine_hist.number_atoms_total               28345 
_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        27737 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         107 
_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' ? 0.0032  ? 28454 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5948  ? 38670 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0442  ? 4352  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0060  ? 5034  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 17.9598 ? 10508 ? 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' 2.90 2.95  . . 135 6080 96.76 . . . . 0.3376 . . . . . . . . . . . 0.3390 
'X-RAY DIFFRACTION' 2.95 3.00  . . 135 6138 97.54 . . . . 0.3201 . . . . . . . . . . . 0.3570 
'X-RAY DIFFRACTION' 3.00 3.05  . . 138 6166 97.83 . . . . 0.3006 . . . . . . . . . . . 0.3412 
'X-RAY DIFFRACTION' 3.05 3.11  . . 141 6193 98.06 . . . . 0.3007 . . . . . . . . . . . 0.3923 
'X-RAY DIFFRACTION' 3.11 3.18  . . 137 6167 98.03 . . . . 0.2847 . . . . . . . . . . . 0.3068 
'X-RAY DIFFRACTION' 3.18 3.24  . . 142 6236 98.30 . . . . 0.2723 . . . . . . . . . . . 0.3440 
'X-RAY DIFFRACTION' 3.24 3.32  . . 140 6190 98.63 . . . . 0.2609 . . . . . . . . . . . 0.3526 
'X-RAY DIFFRACTION' 3.32 3.40  . . 140 6300 98.97 . . . . 0.2559 . . . . . . . . . . . 0.3073 
'X-RAY DIFFRACTION' 3.40 3.49  . . 139 6287 99.18 . . . . 0.2464 . . . . . . . . . . . 0.3135 
'X-RAY DIFFRACTION' 3.49 3.60  . . 138 6242 99.15 . . . . 0.2279 . . . . . . . . . . . 0.2406 
'X-RAY DIFFRACTION' 3.60 3.71  . . 144 6339 99.40 . . . . 0.2223 . . . . . . . . . . . 0.3078 
'X-RAY DIFFRACTION' 3.71 3.85  . . 141 6307 99.43 . . . . 0.2112 . . . . . . . . . . . 0.2835 
'X-RAY DIFFRACTION' 3.85 4.00  . . 141 6334 99.68 . . . . 0.2021 . . . . . . . . . . . 0.2524 
'X-RAY DIFFRACTION' 4.00 4.18  . . 142 6327 99.60 . . . . 0.1857 . . . . . . . . . . . 0.2549 
'X-RAY DIFFRACTION' 4.18 4.40  . . 141 6369 99.71 . . . . 0.1827 . . . . . . . . . . . 0.2213 
'X-RAY DIFFRACTION' 4.40 4.68  . . 143 6363 99.60 . . . . 0.1697 . . . . . . . . . . . 0.2014 
'X-RAY DIFFRACTION' 4.68 5.04  . . 141 6409 99.62 . . . . 0.1687 . . . . . . . . . . . 0.2050 
'X-RAY DIFFRACTION' 5.04 5.55  . . 145 6444 99.53 . . . . 0.1962 . . . . . . . . . . . 0.2004 
'X-RAY DIFFRACTION' 5.55 6.35  . . 142 6432 99.56 . . . . 0.2195 . . . . . . . . . . . 0.2706 
'X-RAY DIFFRACTION' 6.35 7.99  . . 146 6530 99.55 . . . . 0.2079 . . . . . . . . . . . 0.2394 
'X-RAY DIFFRACTION' 7.99 48.74 . . 152 6764 98.96 . . . . 0.1847 . . . . . . . . . . . 0.1979 
# 
_struct.entry_id                     9BE3 
_struct.title                        'The pre-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        9BE3 
_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 4 ? 
G N N 5 ? 
H N N 2 ? 
I N N 3 ? 
J N N 5 ? 
K N N 5 ? 
L N N 5 ? 
M N N 6 ? 
N N N 6 ? 
# 
_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   
;RILFLTTFMSKGNKVVRYLESLHHEVVICQEKVHAQSANLQEIDWIVSYAYGYILDKEIVSRFRGRIINLHPSLLPWNKG
RDPVFWSVWDETPKGVTIHLIDEHVDTGDILVQEEIAFADEDTLLDCYNKANQAIEELFIREWENIVHGRIAPYRQTAGG
TLHFKADRDFYKNLNMTTVRELLALKRLCAEPKRGEKPIDKTFHQLFEQQVEMTPDHVAVVDRGQSLTYKQLNERANQLA
HHLRGKGVKPDDQVAIMLDKSLDMIVSILAVMKAGGAYVPIDPDYPGERIAYMLADSSAAILLTNALHEEKANGACDIID
VHDPDSYSENTNNLPHVNRPDDLVYVMYTSGSTGLAKGVMIEHHNLVNFCEWYRPYFGVTPADKALVYSSFSFDGSALDI
FTHLLAGAALHIVPSERKYDLDALNDYCNQEGITISYLPTGAAEQFMQMDNQSFRVVITGGDVLKKIERNGTYKLYNGYG
PTECTIMVTMFEVDKPYANIPIGKPIDRTRILILDEALALQPIGVAGELFIVGEGLGRGYLNRPELTAEKFIVHPQTGER
MYRTGDRARFLPDGNIEFLGRLDNLVKIRGYRIEPGEIEPFLMNHPLIELTTVLAKEQADGRKYLVGYYVAPEEIPHGEL
REWLGNDLPDYMIPTYFVHMKAFPLTANGKVDRRALPDVQADAELLGEDYVAPTDELEQQLAQVWSHVLGIPQMGIDDHF
LERGGDSIKVMQLIHQLKNIGLSLRYDQLFTHPTIRQLKRLLTEQKQVSLEPLRELDEQAEYETSAVEKRMYIIQQQDVE
SIAYNVVYTINFPLTVDTEQIRVALEQLVLRHEGLRSTYHMRGDEIVKRIVPRAELSFVRQTGEEESVQSLLAEQIKPFD
LAKAPLLRAGVIETADKKVLWFDSHHILLDGLSKSILARELQALLGQQVLSPVEKTYKSFARWQNEWFASDEYEQQIAYW
KTLLQGELPAVQLPTKKRPPQLTFDGAIQMYRVNPEITRKLKATAAKHDLTLYMLMLTIVSIWLSKMNSDSNQVILGTVT
DGRQHPDTRELLGMFVNTLPLLLSIDHEESFLHNLQQVKAKLLPALQNQYVPFDKILEAARVKREGNRHPLFDVMFMMQG
APETELESNMHHINAGISKFDLTLEVLERENGLNIVFEYNTHLFDEGMILRMVAQFEHLLLQAVHGLDQQVKRFELVTED
EKRDLFLRVNDTAKAYPNKLIMSMLEDWAAATPDKTALVFREQRVTYRELNERVNQLAHTLREKGVQPDDLVMLMAERSV
EMMVAIFAVLKAGGAYLPIDPHSPAERIAYIFADSGAKLVLAQSPFVEKASMAEVVLDLNSASSYAADTSNPPLVNQPGD
LVYVMYTSGSTGKPKGVMIEHGALLNVLHGMQDEYPLLQDDAFLLKTTYIFDISVAEIFGWVPGRGKLVILEPEAEKNPK
AIWQAVVGAGITHINFVPSMLIPFVEYLEGRTEANRLRYILACGEAMPDELVPKVYEVLPEVKLENIYGPTEATIYASRY
SLAKGSQESPVPIGKPLPNYRMYIINRHGQLQPIGVPGELCIAGASLARGYLNNPALTEEKFTPHPLEKGERIYRTGDLA
RYREDGNIEYLGRMDHQVKIRGYRIELDEIRSKLIQEETIQDAVVVARNDQNGQAYLCAYLLSEQEWTVGQLRELLRREL
PEYMIPAHFVLLKQFPLTANGKLDRKALPEPDGSVKAEAEYAAPRTELEATLAHIWGEVLGIERIGIRDNFFELGGDSIK
GLQIASRLQRINWTMVINHLFLYPTIEQIAPFVTSEQVVIE
;
_struct_ref.pdbx_align_begin           2 
# 
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 9BE3 A 3 ? 1805 ? Q70LM7 2 ? 1802 ? 3 1803 
2 1 9BE3 B 3 ? 1805 ? Q70LM7 2 ? 1802 ? 3 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 9BE3 MET A 1    ? UNP Q70LM7 ?   ?   'initiating methionine' 1    1  
1 9BE3 GLY A 2    ? UNP Q70LM7 ?   ?   'expression tag'        2    2  
1 9BE3 ASN A 771  A UNP Q70LM7 SER 770 conflict                770  3  
1 9BE3 GLY A 772  B UNP Q70LM7 ?   ?   insertion               770  4  
1 9BE3 LEU A 773  ? UNP Q70LM7 ?   ?   insertion               771  5  
1 9BE3 ALA A 1806 ? UNP Q70LM7 ?   ?   'expression tag'        1804 6  
1 9BE3 ALA A 1807 ? UNP Q70LM7 ?   ?   'expression tag'        1805 7  
1 9BE3 ALA A 1808 ? UNP Q70LM7 ?   ?   'expression tag'        1806 8  
1 9BE3 GLU A 1809 ? UNP Q70LM7 ?   ?   'expression tag'        1807 9  
1 9BE3 ASN A 1810 ? UNP Q70LM7 ?   ?   'expression tag'        1808 10 
1 9BE3 LEU A 1811 ? UNP Q70LM7 ?   ?   'expression tag'        1809 11 
1 9BE3 TYR A 1812 ? UNP Q70LM7 ?   ?   'expression tag'        1810 12 
1 9BE3 PHE A 1813 ? UNP Q70LM7 ?   ?   'expression tag'        1811 13 
1 9BE3 GLN A 1814 ? UNP Q70LM7 ?   ?   'expression tag'        1812 14 
2 9BE3 MET B 1    ? UNP Q70LM7 ?   ?   'initiating methionine' 1    15 
2 9BE3 GLY B 2    ? UNP Q70LM7 ?   ?   'expression tag'        2    16 
2 9BE3 ASN B 771  A UNP Q70LM7 SER 770 conflict                770  17 
2 9BE3 GLY B 772  B UNP Q70LM7 ?   ?   insertion               770  18 
2 9BE3 LEU B 773  ? UNP Q70LM7 ?   ?   insertion               771  19 
2 9BE3 ALA B 1806 ? UNP Q70LM7 ?   ?   'expression tag'        1804 20 
2 9BE3 ALA B 1807 ? UNP Q70LM7 ?   ?   'expression tag'        1805 21 
2 9BE3 ALA B 1808 ? UNP Q70LM7 ?   ?   'expression tag'        1806 22 
2 9BE3 GLU B 1809 ? UNP Q70LM7 ?   ?   'expression tag'        1807 23 
2 9BE3 ASN B 1810 ? UNP Q70LM7 ?   ?   'expression tag'        1808 24 
2 9BE3 LEU B 1811 ? UNP Q70LM7 ?   ?   'expression tag'        1809 25 
2 9BE3 TYR B 1812 ? UNP Q70LM7 ?   ?   'expression tag'        1810 26 
2 9BE3 PHE B 1813 ? UNP Q70LM7 ?   ?   'expression tag'        1811 27 
2 9BE3 GLN B 1814 ? UNP Q70LM7 ?   ?   'expression tag'        1812 28 
# 
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,F,G,M 
2 1 B,H,I,J,K,L,N 
# 
_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 TYR A 173  ? ASN A 177  ? TYR A 173  ASN A 177  5 ? 5  
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  ? ASN A 315  ? HIS A 310  ASN A 315  5 ? 6  
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 PRO A 416  ? TYR A 421  ? PRO A 416  TYR A 421  1 ? 6  
HELX_P HELX_P17  AB8 ASP A 422  ? GLY A 434  ? ASP A 422  GLY A 434  1 ? 13 
HELX_P HELX_P18  AB9 PRO A 441  ? GLN A 447  ? PRO A 441  GLN A 447  1 ? 7  
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 ASP A 674  ? LEU A 678  ? ASP A 674  LEU A 678  5 ? 5  
HELX_P HELX_P24  AC6 VAL A 681  ? ALA A 685  ? VAL A 681  ALA A 685  5 ? 5  
HELX_P HELX_P25  AC7 ASP A 697  ? GLY A 712  ? ASP A 697  GLY A 712  1 ? 16 
HELX_P HELX_P26  AC8 PHE A 722  ? GLY A 726  ? PHE A 722  GLY A 726  5 ? 5  
HELX_P HELX_P27  AC9 ASP A 728  ? GLY A 743  ? ASP A 728  GLY A 743  1 ? 16 
HELX_P HELX_P28  AD1 ARG A 747  ? HIS A 754  ? ARG A 747  HIS A 754  1 ? 8  
HELX_P HELX_P29  AD2 THR A 756  ? THR A 765  ? THR A 756  THR A 765  1 ? 10 
HELX_P HELX_P30  AD3 SER A 789  ? ASP A 802  ? SER A 787  ASP A 800  1 ? 14 
HELX_P HELX_P31  AD4 ASP A 821  ? HIS A 836  ? ASP A 819  HIS A 834  1 ? 16 
HELX_P HELX_P32  AD5 GLU A 837  ? LEU A 839  ? GLU A 835  LEU A 837  5 ? 3  
HELX_P HELX_P33  AD6 SER A 871  ? GLU A 878  ? SER A 869  GLU A 876  1 ? 8  
HELX_P HELX_P34  AD7 ASP A 914  ? GLY A 930  ? ASP A 912  GLY A 928  1 ? 17 
HELX_P HELX_P35  AD8 THR A 940  ? PHE A 952  ? THR A 938  PHE A 950  1 ? 13 
HELX_P HELX_P36  AD9 SER A 954  ? LEU A 968  ? SER A 952  LEU A 966  1 ? 15 
HELX_P HELX_P37  AE1 ASN A 998  ? HIS A 1012 ? ASN A 996  HIS A 1010 1 ? 15 
HELX_P HELX_P38  AE2 THR A 1015 ? ASN A 1032 ? THR A 1013 ASN A 1030 1 ? 18 
HELX_P HELX_P39  AE3 HIS A 1049 ? ARG A 1053 ? HIS A 1047 ARG A 1051 5 ? 5  
HELX_P HELX_P40  AE4 SER A 1074 ? ASN A 1092 ? SER A 1072 ASN A 1090 1 ? 19 
HELX_P HELX_P41  AE5 PRO A 1096 ? ARG A 1105 ? PRO A 1094 ARG A 1103 1 ? 10 
HELX_P HELX_P42  AE6 THR A 1128 ? ASN A 1133 ? THR A 1126 ASN A 1131 1 ? 6  
HELX_P HELX_P43  AE7 ASP A 1169 ? GLY A 1190 ? ASP A 1167 GLY A 1188 1 ? 22 
HELX_P HELX_P44  AE8 GLN A 1194 ? PHE A 1198 ? GLN A 1192 PHE A 1196 5 ? 5  
HELX_P HELX_P45  AE9 THR A 1202 ? ASP A 1215 ? THR A 1200 ASP A 1213 1 ? 14 
HELX_P HELX_P46  AF1 LEU A 1224 ? THR A 1236 ? LEU A 1222 THR A 1234 1 ? 13 
HELX_P HELX_P47  AF2 TYR A 1251 ? LYS A 1268 ? TYR A 1249 LYS A 1266 1 ? 18 
HELX_P HELX_P48  AF3 SER A 1283 ? GLY A 1297 ? SER A 1281 GLY A 1295 1 ? 15 
HELX_P HELX_P49  AF4 PRO A 1308 ? GLY A 1320 ? PRO A 1306 GLY A 1318 1 ? 13 
HELX_P HELX_P50  AF5 SER A 1328 ? SER A 1335 ? SER A 1326 SER A 1333 5 ? 8  
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 ASP A 1416 ? GLY A 1424 ? ASP A 1414 GLY A 1422 1 ? 9  
HELX_P HELX_P54  AF9 ASN A 1442 ? ALA A 1453 ? ASN A 1440 ALA A 1451 1 ? 12 
HELX_P HELX_P55  AG1 MET A 1464 ? GLU A 1473 ? MET A 1462 GLU A 1471 1 ? 10 
HELX_P HELX_P56  AG2 GLU A 1494 ? LEU A 1503 ? GLU A 1492 LEU A 1501 1 ? 10 
HELX_P HELX_P57  AG3 PRO A 1514 ? THR A 1518 ? PRO A 1512 THR A 1516 5 ? 5  
HELX_P HELX_P58  AG4 ASN A 1578 ? LYS A 1585 ? ASN A 1576 LYS A 1583 1 ? 8  
HELX_P HELX_P59  AG5 PRO A 1590 ? LYS A 1593 ? PRO A 1588 LYS A 1591 5 ? 4  
HELX_P HELX_P60  AG6 GLU A 1630 ? LEU A 1638 ? GLU A 1628 LEU A 1636 1 ? 9  
HELX_P HELX_P61  AG7 VAL A 1673 ? ARG A 1682 ? VAL A 1671 ARG A 1680 1 ? 10 
HELX_P HELX_P62  AG8 THR A 1730 ? GLY A 1745 ? THR A 1728 GLY A 1743 1 ? 16 
HELX_P HELX_P63  AG9 ASN A 1754 ? GLY A 1759 ? ASN A 1752 GLY A 1757 5 ? 6  
HELX_P HELX_P64  AH1 ASP A 1761 ? ARG A 1774 ? ASP A 1759 ARG A 1772 1 ? 14 
HELX_P HELX_P65  AH2 ASN A 1782 ? TYR A 1787 ? ASN A 1780 TYR A 1785 1 ? 6  
HELX_P HELX_P66  AH3 THR A 1789 ? ALA A 1794 ? THR A 1787 ALA A 1792 1 ? 6  
HELX_P HELX_P67  AH4 PRO A 1795 ? VAL A 1797 ? PRO A 1793 VAL A 1795 5 ? 3  
HELX_P HELX_P68  AH5 ASN B 15   ? LEU B 24   ? ASN B 15   LEU B 24   1 ? 10 
HELX_P HELX_P69  AH6 SER B 39   ? GLN B 43   ? SER B 39   GLN B 43   5 ? 5  
HELX_P HELX_P70  AH7 ASP B 58   ? PHE B 65   ? ASP B 58   PHE B 65   1 ? 8  
HELX_P HELX_P71  AH8 ASP B 84   ? ASP B 92   ? ASP B 84   ASP B 92   1 ? 9  
HELX_P HELX_P72  AH9 THR B 125  ? HIS B 150  ? THR B 125  HIS B 150  1 ? 26 
HELX_P HELX_P73  AI1 THR B 180  ? CYS B 191  ? THR B 180  CYS B 191  1 ? 12 
HELX_P HELX_P74  AI2 THR B 204  ? THR B 216  ? THR B 204  THR B 216  1 ? 13 
HELX_P HELX_P75  AI3 TYR B 231  ? LYS B 248  ? TYR B 231  LYS B 248  1 ? 18 
HELX_P HELX_P76  AI4 SER B 263  ? GLY B 277  ? SER B 263  GLY B 277  1 ? 15 
HELX_P HELX_P77  AI5 PRO B 288  ? SER B 299  ? PRO B 288  SER B 299  1 ? 12 
HELX_P HELX_P78  AI6 HIS B 310  ? ASN B 315  ? HIS B 310  ASN B 315  5 ? 6  
HELX_P HELX_P79  AI7 ASP B 325  ? TYR B 329  ? ASP B 325  TYR B 329  5 ? 5  
HELX_P HELX_P80  AI8 HIS B 365  ? GLY B 380  ? HIS B 365  GLY B 380  1 ? 16 
HELX_P HELX_P81  AI9 PHE B 395  ? LEU B 407  ? PHE B 395  LEU B 407  1 ? 13 
HELX_P HELX_P82  AJ1 PRO B 416  ? LYS B 420  ? PRO B 416  LYS B 420  5 ? 5  
HELX_P HELX_P83  AJ2 ASP B 422  ? GLY B 434  ? ASP B 422  GLY B 434  1 ? 13 
HELX_P HELX_P84  AJ3 PRO B 441  ? MET B 449  ? PRO B 441  MET B 449  1 ? 9  
HELX_P HELX_P85  AJ4 PRO B 483  ? THR B 487  ? PRO B 483  THR B 487  5 ? 5  
HELX_P HELX_P86  AJ5 ARG B 545  ? LYS B 552  ? ARG B 545  LYS B 552  1 ? 8  
HELX_P HELX_P87  AJ6 GLU B 596  ? GLU B 599  ? GLU B 596  GLU B 599  5 ? 4  
HELX_P HELX_P88  AJ7 ILE B 600  ? ASN B 606  ? ILE B 600  ASN B 606  1 ? 7  
HELX_P HELX_P89  AJ8 PRO B 638  ? GLY B 647  ? PRO B 638  GLY B 647  1 ? 10 
HELX_P HELX_P90  AJ9 PRO B 651  ? ILE B 655  ? PRO B 651  ILE B 655  5 ? 5  
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 ASP B 728  ? ASN B 741  ? ASP B 728  ASN B 741  1 ? 14 
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  ? GLN B 801  ? SER B 787  GLN B 799  1 ? 13 
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 GLU B 868  ? GLU B 870  ? GLU B 866  GLU B 868  5 ? 3  
HELX_P HELX_P101 AL2 SER B 871  ? GLU B 878  ? SER B 869  GLU B 876  1 ? 8  
HELX_P HELX_P102 AL3 ASP B 914  ? GLY B 930  ? ASP B 912  GLY B 928  1 ? 17 
HELX_P HELX_P103 AL4 THR B 940  ? ALA B 953  ? THR B 938  ALA B 951  1 ? 14 
HELX_P HELX_P104 AL5 SER B 954  ? LEU B 968  ? SER B 952  LEU B 966  1 ? 15 
HELX_P HELX_P105 AL6 ASN B 998  ? HIS B 1012 ? ASN B 996  HIS B 1010 1 ? 15 
HELX_P HELX_P106 AL7 THR B 1015 ? ASN B 1032 ? THR B 1013 ASN B 1030 1 ? 18 
HELX_P HELX_P107 AL8 PRO B 1050 ? GLU B 1054 ? PRO B 1048 GLU B 1052 5 ? 5  
HELX_P HELX_P108 AL9 SER B 1074 ? ASN B 1092 ? SER B 1072 ASN B 1090 1 ? 19 
HELX_P HELX_P109 AM1 PRO B 1096 ? ARG B 1105 ? PRO B 1094 ARG B 1103 1 ? 10 
HELX_P HELX_P110 AM2 THR B 1128 ? ASN B 1133 ? THR B 1126 ASN B 1131 1 ? 6  
HELX_P HELX_P111 AM3 ASP B 1169 ? GLY B 1190 ? ASP B 1167 GLY B 1188 1 ? 22 
HELX_P HELX_P112 AM4 GLN B 1194 ? PHE B 1198 ? GLN B 1192 PHE B 1196 5 ? 5  
HELX_P HELX_P113 AM5 THR B 1202 ? VAL B 1213 ? THR B 1200 VAL B 1211 1 ? 12 
HELX_P HELX_P114 AM6 LEU B 1224 ? THR B 1236 ? LEU B 1222 THR B 1234 1 ? 13 
HELX_P HELX_P115 AM7 TYR B 1251 ? LYS B 1268 ? TYR B 1249 LYS B 1266 1 ? 18 
HELX_P HELX_P116 AM8 SER B 1283 ? GLY B 1297 ? SER B 1281 GLY B 1295 1 ? 15 
HELX_P HELX_P117 AM9 PRO B 1308 ? GLY B 1320 ? PRO B 1306 GLY B 1318 1 ? 13 
HELX_P HELX_P118 AN1 SER B 1328 ? VAL B 1331 ? SER B 1326 VAL B 1329 5 ? 4  
HELX_P HELX_P119 AN2 GLU B 1332 ? ALA B 1337 ? GLU B 1330 ALA B 1335 5 ? 6  
HELX_P HELX_P120 AN3 SER B 1345 ? TYR B 1349 ? SER B 1343 TYR B 1347 5 ? 5  
HELX_P HELX_P121 AN4 HIS B 1385 ? TYR B 1399 ? HIS B 1383 TYR B 1397 1 ? 15 
HELX_P HELX_P122 AN5 PHE B 1415 ? PHE B 1423 ? PHE B 1413 PHE B 1421 1 ? 9  
HELX_P HELX_P123 AN6 GLU B 1438 ? LYS B 1441 ? GLU B 1436 LYS B 1439 5 ? 4  
HELX_P HELX_P124 AN7 ASN B 1442 ? ALA B 1453 ? ASN B 1440 ALA B 1451 1 ? 12 
HELX_P HELX_P125 AN8 VAL B 1461 ? LEU B 1472 ? VAL B 1459 LEU B 1470 1 ? 12 
HELX_P HELX_P126 AN9 GLU B 1494 ? LEU B 1503 ? GLU B 1492 LEU B 1501 1 ? 10 
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 GLU B 1630 ? ILE B 1639 ? GLU B 1628 ILE B 1637 1 ? 10 
HELX_P HELX_P130 AO4 GLN B 1675 ? LEU B 1679 ? GLN B 1673 LEU B 1677 1 ? 5  
HELX_P HELX_P131 AO5 LEU B 1680 ? LEU B 1684 ? LEU B 1678 LEU B 1682 5 ? 5  
HELX_P HELX_P132 AO6 PRO B 1685 ? ILE B 1689 ? PRO B 1683 ILE B 1687 5 ? 5  
HELX_P HELX_P133 AO7 THR B 1730 ? GLY B 1745 ? THR B 1728 GLY B 1743 1 ? 16 
HELX_P HELX_P134 AO8 ASP B 1761 ? ILE B 1775 ? ASP B 1759 ILE B 1773 1 ? 15 
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 ? ALA B 1794 ? THR B 1787 ALA B 1792 1 ? 6  
HELX_P HELX_P137 AP2 PRO B 1795 ? VAL B 1797 ? PRO B 1793 VAL B 1795 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale one ? A SER 729  OG  ? ? ? 1_555 E JQG   . P18 ? ? A SER 729  A JQG   1903 1_555 ? ? ? ? ? ? ? 1.636 ? ? 
covale2 covale one ? A SER 1762 OG  ? ? ? 1_555 F A1AMO . P18 ? ? A SER 1760 A A1AMO 1904 1_555 ? ? ? ? ? ? ? 1.642 ? ? 
covale3 covale one ? B SER 729  OG  ? ? ? 1_555 I JQG   . P18 ? ? B SER 729  B JQG   1902 1_555 ? ? ? ? ? ? ? 1.639 ? ? 
metalc1 metalc ?   ? A ASP 128  OD2 ? ? ? 1_555 K MN    . MN  ? ? A ASP 128  B MN    1904 1_455 ? ? ? ? ? ? ? 2.605 ? ? 
metalc2 metalc ?   ? M HOH .    O   ? ? ? 1_655 K MN    . MN  ? ? A HOH 2240 B MN    1904 1_555 ? ? ? ? ? ? ? 2.138 ? ? 
metalc3 metalc ?   ? B GLU 364  OE1 ? ? ? 1_555 L MN    . MN  ? ? B GLU 364  B MN    1905 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
# 
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   OD2 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   ASP 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    128 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    ASP 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     128 
_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   K 
_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     1904 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_455 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   M 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   HOH 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    HOH 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     2240 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_655 
_pdbx_struct_conn_angle.value                 103.9 
_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 JQG   E . ? SER A 729  ? JQG   A 1903 ? 1_555 SER A 729  ? 1_555 P18 OG SER 1 JQG   None 'Covalent chemical modification' 
2 A1AMO F . ? SER A 1762 ? A1AMO A 1904 ? 1_555 SER A 1760 ? 1_555 P18 OG SER 1 A1AMO None 'Covalent chemical modification' 
3 JQG   I . ? SER B 729  ? JQG   B 1902 ? 1_555 SER B 729  ? 1_555 P18 OG SER 1 JQG   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 10.98 
2 ALA 888 A . ? ALA 886 A PRO 889 A ? PRO 887 A 1 0.97  
3 LEU 77  B . ? LEU 77  B PRO 78  B ? PRO 78  B 1 5.35  
4 ALA 888 B . ? ALA 886 B PRO 889 B ? PRO 887 B 1 -0.58 
# 
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 ? 6 ? 
AE1 ? 4 ? 
AE2 ? 3 ? 
AE3 ? 3 ? 
AE4 ? 5 ? 
AE5 ? 4 ? 
AE6 ? 4 ? 
AE7 ? 2 ? 
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      
AD9 4 5 ? parallel      
AD9 5 6 ? anti-parallel 
AE1 1 2 ? anti-parallel 
AE1 2 3 ? parallel      
AE1 3 4 ? parallel      
AE2 1 2 ? parallel      
AE2 2 3 ? parallel      
AE3 1 2 ? anti-parallel 
AE3 2 3 ? anti-parallel 
AE4 1 2 ? parallel      
AE4 2 3 ? parallel      
AE4 3 4 ? anti-parallel 
AE4 4 5 ? anti-parallel 
AE5 1 2 ? anti-parallel 
AE5 2 3 ? anti-parallel 
AE5 3 4 ? anti-parallel 
AE6 1 2 ? anti-parallel 
AE6 2 3 ? anti-parallel 
AE6 3 4 ? anti-parallel 
AE7 1 2 ? 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  ? ILE A 320  ? ASP A 319  ILE A 320  
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  ? TYR A 439  ? ILE A 437  TYR A 439  
AA6 2 VAL A 458  ? GLY A 462  ? VAL A 458  GLY A 462  
AA6 3 LYS A 476  ? TYR A 481  ? LYS A 476  TYR A 481  
AA6 4 THR A 491  ? VAL A 495  ? THR A 491  VAL A 495  
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 LEU A 1432 ? ILE A 1434 ? LEU A 1430 ILE A 1432 
AB6 4 PHE A 1407 ? LEU A 1409 ? PHE A 1405 LEU A 1407 
AB7 1 ALA A 1299 ? ILE A 1303 ? ALA A 1297 ILE A 1301 
AB7 2 LEU A 1275 ? MET A 1279 ? LEU A 1273 MET A 1277 
AB7 3 VAL A 1324 ? ALA A 1326 ? VAL A 1322 ALA A 1324 
AB7 4 VAL A 1340 ? ASP A 1342 ? VAL A 1338 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 ? TYR A 1575 ? GLY A 1572 TYR A 1573 
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 GLY A 1562 ? GLY A 1568 ? GLY A 1560 GLY A 1566 
AC1 3 ARG A 1596 ? ARG A 1605 ? ARG A 1594 ARG A 1603 
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 GLY A 1562 ? GLY A 1568 ? GLY A 1560 GLY A 1566 
AC2 3 ARG A 1596 ? ARG A 1605 ? ARG A 1594 ARG A 1603 
AC2 4 GLU A 1613 ? ARG A 1617 ? GLU A 1611 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 ? ASP A 1654 ? VAL A 1648 ASP A 1652 
AC4 2 GLN A 1658 ? CYS A 1662 ? GLN A 1656 CYS A 1660 
AC5 1 TRP A 1777 ? THR A 1778 ? TRP A 1775 THR A 1776 
AC5 2 THR A 1798 ? SER A 1799 ? THR A 1796 SER A 1797 
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  ? TYR B 439  ? ILE B 437  TYR B 439  
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 ALA B 528  ? GLY B 535  ? ALA B 528  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 ALA B 528  ? GLY B 535  ? ALA B 528  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  ? ILE B 590  ? VAL B 588  ILE B 590  
AD5 2 TYR B 593  ? ILE B 595  ? TYR B 593  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 
AD9 5 GLN B 1037 ? THR B 1044 ? GLN B 1035 THR B 1042 
AD9 6 ASN B 1061 ? SER B 1068 ? ASN B 1059 SER B 1066 
AE1 1 GLN B 1247 ? THR B 1250 ? GLN B 1245 THR B 1248 
AE1 2 THR B 1240 ? PHE B 1244 ? THR B 1238 PHE B 1242 
AE1 3 LYS B 1431 ? ILE B 1434 ? LYS B 1429 ILE B 1432 
AE1 4 ALA B 1406 ? LEU B 1409 ? ALA B 1404 LEU B 1407 
AE2 1 ALA B 1299 ? PRO B 1302 ? ALA B 1297 PRO B 1300 
AE2 2 LEU B 1275 ? MET B 1279 ? LEU B 1273 MET B 1277 
AE2 3 LEU B 1323 ? ALA B 1326 ? LEU B 1321 ALA B 1324 
AE3 1 LEU B 1365 ? TYR B 1370 ? LEU B 1363 TYR B 1368 
AE3 2 GLY B 1380 ? GLU B 1384 ? GLY B 1378 GLU B 1382 
AE3 3 GLY B 1574 ? TYR B 1575 ? GLY B 1572 TYR B 1573 
AE4 1 HIS B 1457 ? PHE B 1460 ? HIS B 1455 PHE B 1458 
AE4 2 TYR B 1483 ? ALA B 1486 ? TYR B 1481 ALA B 1484 
AE4 3 LYS B 1507 ? TYR B 1512 ? LYS B 1505 TYR B 1510 
AE4 4 SER B 1522 ? SER B 1525 ? SER B 1520 SER B 1523 
AE4 5 LYS B 1539 ? PRO B 1540 ? LYS B 1537 PRO B 1538 
AE5 1 TYR B 1544 ? ILE B 1549 ? TYR B 1542 ILE B 1547 
AE5 2 GLY B 1562 ? GLY B 1568 ? GLY B 1560 GLY B 1566 
AE5 3 ARG B 1596 ? TYR B 1606 ? ARG B 1594 TYR B 1604 
AE5 4 PHE B 1586 ? PRO B 1588 ? PHE B 1584 PRO B 1586 
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 ILE B 1612 ? ARG B 1617 ? ILE B 1610 ARG B 1615 
AE7 1 LYS B 1623 ? ILE B 1624 ? LYS B 1621 ILE B 1622 
AE7 2 TYR B 1627 ? ARG B 1628 ? TYR B 1625 ARG B 1626 
AE8 1 TRP B 1777 ? THR B 1778 ? TRP B 1775 THR B 1776 
AE8 2 THR B 1798 ? SER B 1799 ? THR B 1796 SER B 1797 
# 
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 ILE A 48   ? N ILE A 48   O ILE A 70   ? O ILE A 70   
AA1 4 5 N ASN A 71   ? N ASN A 71   O HIS A 101  ? O HIS A 101  
AA1 5 6 N ILE A 100  ? N ILE A 100  O VAL A 114  ? O VAL A 114  
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 ALA A 411  ? O ALA A 411  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 ASP A 319  ? O ASP A 319  
AA5 1 2 N VAL A 346  ? N VAL A 346  O ILE A 363  ? O ILE A 363  
AA5 2 3 N MET A 362  ? N MET A 362  O GLY A 541  ? O GLY A 541  
AA6 1 2 N SER A 438  ? N SER A 438  O ILE A 460  ? O ILE A 460  
AA6 2 3 N THR A 461  ? N THR A 461  O TYR A 478  ? O TYR A 478  
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 ILE A 590  ? N ILE A 590  O TYR A 593  ? O TYR A 593  
AB1 1 2 N LEU A 612  ? N LEU A 612  O VAL A 632  ? O VAL A 632  
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 GLU A 849  ? O GLU A 847  N ARG A 846  ? N ARG A 844  
AB3 1 2 N GLN A 865  ? N GLN A 863  O GLU A 897  ? O GLU A 895  
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 TYR A 995  ? N TYR A 993  O ILE A 1159 ? O ILE A 1157 
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 GLN A 1247 ? O GLN A 1245 N PHE A 1244 ? N PHE A 1242 
AB6 2 3 N ALA A 1241 ? N ALA A 1239 O LEU A 1432 ? O LEU A 1430 
AB6 3 4 O VAL A 1433 ? O VAL A 1431 N PHE A 1407 ? N PHE A 1405 
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 1279 ? N MET A 1277 O LEU A 1325 ? O LEU A 1323 
AB7 3 4 O ALA A 1326 ? O ALA A 1324 N LEU A 1341 ? N LEU A 1339 
AB8 1 2 N VAL A 1366 ? N VAL A 1364 O ILE A 1383 ? O ILE A 1381 
AB8 2 3 N MET A 1382 ? N MET A 1380 O GLY A 1574 ? O GLY A 1572 
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 TYR A 1547 ? N TYR A 1545 O CYS A 1565 ? O CYS A 1563 
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 TYR A 1547 ? N TYR A 1545 O CYS A 1565 ? O CYS A 1563 
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 ASP A 1654 ? N ASP A 1652 O GLN A 1658 ? O GLN A 1656 
AC5 1 2 N THR A 1778 ? N THR A 1776 O THR A 1798 ? O THR A 1796 
AC6 1 2 O VAL B 29   ? O VAL B 29   N PHE B 6    ? N PHE B 6    
AC6 2 3 N LEU B 5    ? N LEU B 5    O TRP B 47   ? O TRP B 47   
AC6 3 4 N SER B 50   ? N SER B 50   O ILE B 70   ? O ILE B 70   
AC6 4 5 N ASN B 71   ? N ASN B 71   O HIS B 101  ? O HIS B 101  
AC6 5 6 N ILE B 100  ? N ILE B 100  O VAL B 114  ? O VAL B 114  
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 VAL B 346  ? N VAL B 346  O ILE B 363  ? O ILE B 363  
AD1 2 3 N MET B 362  ? N MET B 362  O GLY B 541  ? O GLY B 541  
AD2 1 2 N SER B 438  ? N SER B 438  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 GLU B 897  ? O GLU B 895  
AD8 2 3 N ILE B 896  ? N ILE B 894  O VAL B 903  ? O VAL B 901  
AD8 3 4 O LYS B 902  ? O LYS B 900  N PHE B 816  ? N PHE B 814  
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 GLU B 1162 ? O GLU B 1160 N THR B 1147 ? N THR B 1145 
AD9 3 4 O LEU B 1148 ? O LEU B 1146 N MET B 1119 ? N MET B 1117 
AD9 4 5 O PHE B 1120 ? O PHE B 1118 N GLY B 1041 ? N GLY B 1039 
AD9 5 6 N THR B 1042 ? N THR B 1040 O LEU B 1063 ? O LEU B 1061 
AE1 1 2 O VAL B 1249 ? O VAL B 1247 N ALA B 1241 ? N ALA B 1239 
AE1 2 3 N ALA B 1241 ? N ALA B 1239 O LEU B 1432 ? O LEU B 1430 
AE1 3 4 O VAL B 1433 ? O VAL B 1431 N PHE B 1407 ? N PHE B 1405 
AE2 1 2 O LEU B 1301 ? O LEU B 1299 N LEU B 1278 ? N LEU B 1276 
AE2 2 3 N MET B 1277 ? N MET B 1275 O LEU B 1323 ? O LEU B 1321 
AE3 1 2 N MET B 1369 ? N MET B 1367 O VAL B 1381 ? O VAL B 1379 
AE3 2 3 N MET B 1382 ? N MET B 1380 O GLY B 1574 ? O GLY B 1572 
AE4 1 2 N ILE B 1458 ? N ILE B 1456 O LEU B 1485 ? O LEU B 1483 
AE4 2 3 N ALA B 1486 ? N ALA B 1484 O GLU B 1509 ? O GLU B 1507 
AE4 3 4 N TYR B 1512 ? N TYR B 1510 O SER B 1522 ? O SER B 1520 
AE4 4 5 N ARG B 1523 ? N ARG B 1521 O LYS B 1539 ? O LYS B 1537 
AE5 1 2 N TYR B 1547 ? N TYR B 1545 O CYS B 1565 ? O CYS B 1563 
AE5 2 3 N ILE B 1566 ? N ILE B 1564 O TYR B 1598 ? O TYR B 1596 
AE5 3 4 O ILE B 1597 ? O ILE B 1595 N THR B 1587 ? N THR B 1585 
AE6 1 2 N TYR B 1547 ? N TYR B 1545 O CYS B 1565 ? O CYS B 1563 
AE6 2 3 N ILE B 1566 ? N ILE B 1564 O TYR B 1598 ? O TYR B 1596 
AE6 3 4 N LEU B 1603 ? N LEU B 1601 O GLY B 1616 ? O GLY B 1614 
AE7 1 2 N ILE B 1624 ? N ILE B 1622 O TYR B 1627 ? O TYR B 1625 
AE8 1 2 N THR B 1778 ? N THR B 1776 O THR B 1798 ? O THR B 1796 
# 
_pdbx_entry_details.entry_id                   9BE3 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_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 NZ  A LYS 248  ? ? OD2 A ASP 319  ? ? 2.05 
2 1 OH  B TYR 130  ? ? NH2 B ARG 170  ? ? 2.08 
3 1 NH2 B ARG 1264 ? ? O   B PRO 1355 ? ? 2.11 
4 1 OD2 B ASP 104  ? ? OG1 B THR 109  ? ? 2.18 
5 1 NH2 A ARG 170  ? ? OD1 A ASN 177  ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 NE2 A GLN 38 ? ? 1_555 OE1 B GLN 43 ? ? 1_456 2.12 
2 1 NE2 A GLN 38 ? ? 1_555 NE2 B GLN 43 ? ? 1_456 2.17 
# 
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 LEU A 24   ? ? -66.01  4.76    
2   1 ASP A 104  ? ? -116.46 -153.38 
3   1 PRO A 194  ? ? -79.41  -125.32 
4   1 ARG A 196  ? ? 36.88   40.98   
5   1 GLU A 198  ? ? -75.17  -101.72 
6   1 ARG A 225  ? ? 54.36   -118.57 
7   1 MET A 259  ? ? -116.20 63.82   
8   1 LYS A 262  ? ? -50.37  108.21  
9   1 ASN A 307  ? ? -110.45 -162.69 
10  1 SER A 352  ? ? -160.59 -142.78 
11  1 SER A 354  ? ? -151.92 -136.43 
12  1 ALA A 358  ? ? -174.65 136.41  
13  1 ASP A 464  ? ? -108.75 -163.76 
14  1 ILE A 488  ? ? 61.06   -76.09  
15  1 VAL A 495  ? ? -69.66  99.39   
16  1 ASN A 586  ? ? -87.22  31.33   
17  1 ALA A 669  ? ? -69.63  7.87    
18  1 ALA A 683  ? ? -81.13  36.42   
19  1 ALA A 685  ? ? 7.31    -86.17  
20  1 GLU A 686  ? ? -161.76 4.88    
21  1 LEU A 687  ? ? -38.02  101.65  
22  1 LEU A 688  ? ? -65.74  13.75   
23  1 GLN A 715  ? ? 58.33   78.14   
24  1 LEU A 888  ? ? -82.46  42.25   
25  1 ASP A 912  ? ? -118.24 -169.21 
26  1 PRO A 976  ? ? -66.63  71.82   
27  1 ASN A 1030 ? ? -89.48  39.68   
28  1 PRO A 1112 ? ? -10.83  -99.65  
29  1 PRO A 1112 ? ? -17.00  -99.65  
30  1 ALA A 1137 ? ? -89.55  32.78   
31  1 ASN A 1153 ? ? 58.88   14.10   
32  1 VAL A 1211 ? ? -134.95 -56.02  
33  1 ARG A 1243 ? ? 53.21   -114.49 
34  1 LEU A 1252 ? ? -55.75  -71.29  
35  1 LYS A 1266 ? ? -69.42  0.64    
36  1 PRO A 1270 ? ? -39.89  140.22  
37  1 HIS A 1304 ? ? -88.77  31.66   
38  1 LEU A 1323 ? ? -66.59  92.66   
39  1 GLU A 1336 ? ? -133.92 -111.44 
40  1 PRO A 1360 ? ? -57.81  -8.19   
41  1 PRO A 1376 ? ? -35.25  127.41  
42  1 SER A 1461 ? ? 79.92   -17.26  
43  1 THR A 1474 ? ? -147.21 13.09   
44  1 GLU A 1503 ? ? 75.10   -4.66   
45  1 THR A 1516 ? ? 56.63   -101.96 
46  1 ILE A 1517 ? ? -108.76 -66.70  
47  1 ALA A 1519 ? ? -146.55 -40.44  
48  1 VAL A 1533 ? ? 63.06   101.73  
49  1 SER A 1568 ? ? -81.09  42.91   
50  1 ASN A 1576 ? ? -152.96 65.73   
51  1 GLN A 1653 ? ? 52.63   -118.38 
52  1 GLU A 1681 ? ? 69.25   -45.33  
53  1 THR B 9    ? ? -139.18 -47.08  
54  1 TYR B 51   ? ? -166.77 107.51  
55  1 LEU B 72   ? ? -110.63 71.51   
56  1 ASP B 104  ? ? -122.75 -150.86 
57  1 ALA B 168  ? ? 68.12   -5.93   
58  1 TYR B 173  ? ? -102.27 40.93   
59  1 CYS B 191  ? ? -143.44 44.88   
60  1 ARG B 225  ? ? 54.41   -107.88 
61  1 SER B 300  ? ? -78.54  30.93   
62  1 LEU B 357  ? ? 33.47   71.04   
63  1 CYS B 486  ? ? -118.89 60.24   
64  1 THR B 487  ? ? 58.43   -142.90 
65  1 ASP B 674  ? ? -69.75  81.40   
66  1 GLU B 686  ? ? 89.81   -20.81  
67  1 LEU B 687  ? ? 39.05   50.86   
68  1 GLN B 769  ? ? -89.69  33.63   
69  1 ASP B 800  ? ? 59.51   78.79   
70  1 LEU B 888  ? ? -77.67  43.40   
71  1 LEU B 910  ? ? -131.66 -33.95  
72  1 LEU B 966  ? ? -111.15 65.01   
73  1 LYS B 1009 ? ? -59.45  -9.86   
74  1 ASN B 1030 ? ? -104.36 73.24   
75  1 SER B 1031 ? ? 56.52   -128.33 
76  1 PHE B 1057 ? ? -132.31 -31.64  
77  1 LEU B 1113 ? ? 68.50   -67.98  
78  1 ASN B 1153 ? ? 58.41   13.70   
79  1 VAL B 1211 ? ? -135.49 -64.74  
80  1 THR B 1234 ? ? -115.59 79.56   
81  1 ARG B 1243 ? ? 54.23   -115.13 
82  1 HIS B 1304 ? ? -95.16  31.10   
83  1 VAL B 1357 ? ? -143.30 -5.14   
84  1 LEU B 1400 ? ? -98.76  -158.20 
85  1 ASP B 1402 ? ? 65.25   -6.27   
86  1 GLU B 1436 ? ? 70.38   -0.20   
87  1 ARG B 1473 ? ? 63.60   165.68  
88  1 GLU B 1475 ? ? 53.28   -135.38 
89  1 ALA B 1515 ? ? -91.11  -128.44 
90  1 ILE B 1517 ? ? 67.12   -65.90  
91  1 ALA B 1519 ? ? -149.06 -39.60  
92  1 SER B 1528 ? ? 52.97   -143.63 
93  1 GLN B 1529 ? ? 60.99   69.11   
94  1 SER B 1568 ? ? -84.32  33.39   
95  1 GLN B 1653 ? ? 179.01  -156.27 
96  1 ASN B 1654 ? ? 72.18   178.07  
97  1 ALA B 1657 ? ? -150.55 -21.14  
98  1 TYR B 1658 ? ? -123.09 -166.32 
99  1 LEU B 1678 ? ? 63.80   -62.31  
100 1 MET B 1686 ? ? -102.27 40.11   
101 1 ARG B 1727 ? ? -89.12  -71.10  
102 1 ARG B 1750 ? ? -100.34 74.10   
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     1746 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.078 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 2277 ? 5.92 . 
2 1 O ? B HOH 2224 ? 6.28 . 
# 
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 TYR 1662 ? A TYR 1664 
2   1 Y 1 A LEU 1663 ? A LEU 1665 
3   1 Y 1 A LEU 1664 ? A LEU 1666 
4   1 Y 1 A SER 1665 ? A SER 1667 
5   1 Y 1 A GLU 1666 ? A GLU 1668 
6   1 Y 1 A GLN 1667 ? A GLN 1669 
7   1 Y 1 A GLU 1668 ? A GLU 1670 
8   1 Y 1 A TRP 1669 ? A TRP 1671 
9   1 Y 1 A VAL 1692 ? A VAL 1694 
10  1 Y 1 A LEU 1693 ? A LEU 1695 
11  1 Y 1 A LEU 1694 ? A LEU 1696 
12  1 Y 1 A LYS 1695 ? A LYS 1697 
13  1 Y 1 A GLN 1696 ? A GLN 1698 
14  1 Y 1 A PHE 1697 ? A PHE 1699 
15  1 Y 1 A PRO 1698 ? A PRO 1700 
16  1 Y 1 A LEU 1699 ? A LEU 1701 
17  1 Y 1 A THR 1700 ? A THR 1702 
18  1 Y 1 A ALA 1701 ? A ALA 1703 
19  1 Y 1 A ASN 1702 ? A ASN 1704 
20  1 Y 1 A GLY 1703 ? A GLY 1705 
21  1 Y 1 A LYS 1704 ? A LYS 1706 
22  1 Y 1 A LEU 1705 ? A LEU 1707 
23  1 Y 1 A ASP 1706 ? A ASP 1708 
24  1 Y 1 A ARG 1707 ? A ARG 1709 
25  1 Y 1 A LYS 1708 ? A LYS 1710 
26  1 Y 1 A ALA 1709 ? A ALA 1711 
27  1 Y 1 A LEU 1710 ? A LEU 1712 
28  1 Y 1 A PRO 1711 ? A PRO 1713 
29  1 Y 1 A GLU 1712 ? A GLU 1714 
30  1 Y 1 A PRO 1713 ? A PRO 1715 
31  1 Y 1 A ASP 1714 ? A ASP 1716 
32  1 Y 1 A GLY 1715 ? A GLY 1717 
33  1 Y 1 A SER 1716 ? A SER 1718 
34  1 Y 1 A VAL 1717 ? A VAL 1719 
35  1 Y 1 A LYS 1718 ? A LYS 1720 
36  1 Y 1 A ALA 1719 ? A ALA 1721 
37  1 Y 1 A GLU 1720 ? A GLU 1722 
38  1 Y 1 A ALA 1721 ? A ALA 1723 
39  1 Y 1 A GLU 1722 ? A GLU 1724 
40  1 Y 1 A TYR 1723 ? A TYR 1725 
41  1 Y 1 B PRO 194  ? B PRO 194  
42  1 Y 1 B LYS 195  ? B LYS 195  
43  1 Y 1 B ARG 196  ? B ARG 196  
44  1 Y 1 B GLY 197  ? B GLY 197  
45  1 Y 1 B GLY 1371 ? B GLY 1373 
46  1 Y 1 B SER 1372 ? B SER 1374 
47  1 Y 1 B GLN 1638 ? B GLN 1640 
48  1 Y 1 B GLU 1639 ? B GLU 1641 
49  1 Y 1 B GLU 1640 ? B GLU 1642 
50  1 Y 1 B THR 1641 ? B THR 1643 
51  1 Y 1 B ILE 1642 ? B ILE 1644 
52  1 Y 1 B GLN 1643 ? B GLN 1645 
53  1 Y 1 B ASP 1644 ? B ASP 1646 
54  1 Y 1 B ALA 1645 ? B ALA 1647 
55  1 Y 1 B VAL 1646 ? B VAL 1648 
56  1 Y 1 B VAL 1647 ? B VAL 1649 
57  1 Y 1 B VAL 1648 ? B VAL 1650 
58  1 Y 1 B ALA 1649 ? B ALA 1651 
59  1 Y 1 B ARG 1650 ? B ARG 1652 
60  1 Y 1 B ASN 1651 ? B ASN 1653 
61  1 Y 1 B CYS 1660 ? B CYS 1662 
62  1 Y 1 B ALA 1661 ? B ALA 1663 
63  1 Y 1 B TYR 1662 ? B TYR 1664 
64  1 Y 1 B LEU 1663 ? B LEU 1665 
65  1 Y 1 B LEU 1664 ? B LEU 1666 
66  1 Y 1 B SER 1665 ? B SER 1667 
67  1 Y 1 B GLU 1666 ? B GLU 1668 
68  1 Y 1 B GLN 1667 ? B GLN 1669 
69  1 Y 1 B GLU 1668 ? B GLU 1670 
70  1 Y 1 B TRP 1669 ? B TRP 1671 
71  1 Y 1 B THR 1670 ? B THR 1672 
72  1 Y 1 B VAL 1671 ? B VAL 1673 
73  1 Y 1 B HIS 1690 ? B HIS 1692 
74  1 Y 1 B PHE 1691 ? B PHE 1693 
75  1 Y 1 B VAL 1692 ? B VAL 1694 
76  1 Y 1 B LEU 1693 ? B LEU 1695 
77  1 Y 1 B LEU 1694 ? B LEU 1696 
78  1 Y 1 B LYS 1695 ? B LYS 1697 
79  1 Y 1 B GLN 1696 ? B GLN 1698 
80  1 Y 1 B PHE 1697 ? B PHE 1699 
81  1 Y 1 B PRO 1698 ? B PRO 1700 
82  1 Y 1 B LEU 1699 ? B LEU 1701 
83  1 Y 1 B THR 1700 ? B THR 1702 
84  1 Y 1 B ALA 1701 ? B ALA 1703 
85  1 Y 1 B ASN 1702 ? B ASN 1704 
86  1 Y 1 B GLY 1703 ? B GLY 1705 
87  1 Y 1 B LYS 1704 ? B LYS 1706 
88  1 Y 1 B LEU 1705 ? B LEU 1707 
89  1 Y 1 B ASP 1706 ? B ASP 1708 
90  1 Y 1 B ARG 1707 ? B ARG 1709 
91  1 Y 1 B LYS 1708 ? B LYS 1710 
92  1 Y 1 B ALA 1709 ? B ALA 1711 
93  1 Y 1 B LEU 1710 ? B LEU 1712 
94  1 Y 1 B PRO 1711 ? B PRO 1713 
95  1 Y 1 B GLU 1712 ? B GLU 1714 
96  1 Y 1 B PRO 1713 ? B PRO 1715 
97  1 Y 1 B ASP 1714 ? B ASP 1716 
98  1 Y 1 B GLY 1715 ? B GLY 1717 
99  1 Y 1 B SER 1716 ? B SER 1718 
100 1 Y 1 B VAL 1717 ? B VAL 1719 
101 1 Y 1 B LYS 1718 ? B LYS 1720 
102 1 Y 1 B ALA 1719 ? B ALA 1721 
103 1 Y 1 B GLU 1720 ? B GLU 1722 
104 1 Y 1 B ALA 1721 ? B ALA 1723 
105 1 Y 1 B GLU 1722 ? B GLU 1724 
106 1 Y 1 B TYR 1723 ? B TYR 1725 
107 1 Y 1 B ALA 1724 ? B ALA 1726 
108 1 Y 1 B ALA 1725 ? B ALA 1727 
# 
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 
A1AMO O13  O  N N 1   
A1AMO O21  O  N N 2   
A1AMO C11  C  N N 3   
A1AMO C12  C  N S 4   
A1AMO C02  C  N N 5   
A1AMO C04  C  N N 6   
A1AMO C05  C  N N 7   
A1AMO C07  C  N N 8   
A1AMO C08  C  N N 9   
A1AMO C09  C  N N 10  
A1AMO C14  C  N N 11  
A1AMO C15  C  N N 12  
A1AMO C16  C  N N 13  
A1AMO C22  C  N N 14  
A1AMO C25  C  N N 15  
A1AMO N03  N  N N 16  
A1AMO N06  N  N N 17  
A1AMO N10  N  N N 18  
A1AMO N29  N  N N 19  
A1AMO O01  O  N N 20  
A1AMO O17  O  N N 21  
A1AMO O19  O  N N 22  
A1AMO O23  O  N N 23  
A1AMO O24  O  N N 24  
A1AMO P18  P  N N 25  
A1AMO H131 H  N N 26  
A1AMO H121 H  N N 27  
A1AMO H041 H  N N 28  
A1AMO H042 H  N N 29  
A1AMO H052 H  N N 30  
A1AMO H051 H  N N 31  
A1AMO H081 H  N N 32  
A1AMO H082 H  N N 33  
A1AMO H091 H  N N 34  
A1AMO H092 H  N N 35  
A1AMO H151 H  N N 36  
A1AMO H153 H  N N 37  
A1AMO H152 H  N N 38  
A1AMO H162 H  N N 39  
A1AMO H161 H  N N 40  
A1AMO H223 H  N N 41  
A1AMO H221 H  N N 42  
A1AMO H222 H  N N 43  
A1AMO H251 H  N N 44  
A1AMO H252 H  N N 45  
A1AMO H031 H  N N 46  
A1AMO H061 H  N N 47  
A1AMO H101 H  N N 48  
A1AMO H291 H  N N 49  
A1AMO H292 H  N N 50  
A1AMO H2   H  N N 51  
A1AMO O1   O  N N 52  
A1AMO H1   H  N N 53  
ALA   N    N  N N 54  
ALA   CA   C  N S 55  
ALA   C    C  N N 56  
ALA   O    O  N N 57  
ALA   CB   C  N N 58  
ALA   OXT  O  N N 59  
ALA   H    H  N N 60  
ALA   H2   H  N N 61  
ALA   HA   H  N N 62  
ALA   HB1  H  N N 63  
ALA   HB2  H  N N 64  
ALA   HB3  H  N N 65  
ALA   HXT  H  N N 66  
ARG   N    N  N N 67  
ARG   CA   C  N S 68  
ARG   C    C  N N 69  
ARG   O    O  N N 70  
ARG   CB   C  N N 71  
ARG   CG   C  N N 72  
ARG   CD   C  N N 73  
ARG   NE   N  N N 74  
ARG   CZ   C  N N 75  
ARG   NH1  N  N N 76  
ARG   NH2  N  N N 77  
ARG   OXT  O  N N 78  
ARG   H    H  N N 79  
ARG   H2   H  N N 80  
ARG   HA   H  N N 81  
ARG   HB2  H  N N 82  
ARG   HB3  H  N N 83  
ARG   HG2  H  N N 84  
ARG   HG3  H  N N 85  
ARG   HD2  H  N N 86  
ARG   HD3  H  N N 87  
ARG   HE   H  N N 88  
ARG   HH11 H  N N 89  
ARG   HH12 H  N N 90  
ARG   HH21 H  N N 91  
ARG   HH22 H  N N 92  
ARG   HXT  H  N N 93  
ASN   N    N  N N 94  
ASN   CA   C  N S 95  
ASN   C    C  N N 96  
ASN   O    O  N N 97  
ASN   CB   C  N N 98  
ASN   CG   C  N N 99  
ASN   OD1  O  N N 100 
ASN   ND2  N  N N 101 
ASN   OXT  O  N N 102 
ASN   H    H  N N 103 
ASN   H2   H  N N 104 
ASN   HA   H  N N 105 
ASN   HB2  H  N N 106 
ASN   HB3  H  N N 107 
ASN   HD21 H  N N 108 
ASN   HD22 H  N N 109 
ASN   HXT  H  N N 110 
ASP   N    N  N N 111 
ASP   CA   C  N S 112 
ASP   C    C  N N 113 
ASP   O    O  N N 114 
ASP   CB   C  N N 115 
ASP   CG   C  N N 116 
ASP   OD1  O  N N 117 
ASP   OD2  O  N N 118 
ASP   OXT  O  N N 119 
ASP   H    H  N N 120 
ASP   H2   H  N N 121 
ASP   HA   H  N N 122 
ASP   HB2  H  N N 123 
ASP   HB3  H  N N 124 
ASP   HD2  H  N N 125 
ASP   HXT  H  N N 126 
CYS   N    N  N N 127 
CYS   CA   C  N R 128 
CYS   C    C  N N 129 
CYS   O    O  N N 130 
CYS   CB   C  N N 131 
CYS   SG   S  N N 132 
CYS   OXT  O  N N 133 
CYS   H    H  N N 134 
CYS   H2   H  N N 135 
CYS   HA   H  N N 136 
CYS   HB2  H  N N 137 
CYS   HB3  H  N N 138 
CYS   HG   H  N N 139 
CYS   HXT  H  N N 140 
GLN   N    N  N N 141 
GLN   CA   C  N S 142 
GLN   C    C  N N 143 
GLN   O    O  N N 144 
GLN   CB   C  N N 145 
GLN   CG   C  N N 146 
GLN   CD   C  N N 147 
GLN   OE1  O  N N 148 
GLN   NE2  N  N N 149 
GLN   OXT  O  N N 150 
GLN   H    H  N N 151 
GLN   H2   H  N N 152 
GLN   HA   H  N N 153 
GLN   HB2  H  N N 154 
GLN   HB3  H  N N 155 
GLN   HG2  H  N N 156 
GLN   HG3  H  N N 157 
GLN   HE21 H  N N 158 
GLN   HE22 H  N N 159 
GLN   HXT  H  N N 160 
GLU   N    N  N N 161 
GLU   CA   C  N S 162 
GLU   C    C  N N 163 
GLU   O    O  N N 164 
GLU   CB   C  N N 165 
GLU   CG   C  N N 166 
GLU   CD   C  N N 167 
GLU   OE1  O  N N 168 
GLU   OE2  O  N N 169 
GLU   OXT  O  N N 170 
GLU   H    H  N N 171 
GLU   H2   H  N N 172 
GLU   HA   H  N N 173 
GLU   HB2  H  N N 174 
GLU   HB3  H  N N 175 
GLU   HG2  H  N N 176 
GLU   HG3  H  N N 177 
GLU   HE2  H  N N 178 
GLU   HXT  H  N N 179 
GLY   N    N  N N 180 
GLY   CA   C  N N 181 
GLY   C    C  N N 182 
GLY   O    O  N N 183 
GLY   OXT  O  N N 184 
GLY   H    H  N N 185 
GLY   H2   H  N N 186 
GLY   HA2  H  N N 187 
GLY   HA3  H  N N 188 
GLY   HXT  H  N N 189 
GOL   C1   C  N N 190 
GOL   O1   O  N N 191 
GOL   C2   C  N N 192 
GOL   O2   O  N N 193 
GOL   C3   C  N N 194 
GOL   O3   O  N N 195 
GOL   H11  H  N N 196 
GOL   H12  H  N N 197 
GOL   HO1  H  N N 198 
GOL   H2   H  N N 199 
GOL   HO2  H  N N 200 
GOL   H31  H  N N 201 
GOL   H32  H  N N 202 
GOL   HO3  H  N N 203 
HIS   N    N  N N 204 
HIS   CA   C  N S 205 
HIS   C    C  N N 206 
HIS   O    O  N N 207 
HIS   CB   C  N N 208 
HIS   CG   C  Y N 209 
HIS   ND1  N  Y N 210 
HIS   CD2  C  Y N 211 
HIS   CE1  C  Y N 212 
HIS   NE2  N  Y N 213 
HIS   OXT  O  N N 214 
HIS   H    H  N N 215 
HIS   H2   H  N N 216 
HIS   HA   H  N N 217 
HIS   HB2  H  N N 218 
HIS   HB3  H  N N 219 
HIS   HD1  H  N N 220 
HIS   HD2  H  N N 221 
HIS   HE1  H  N N 222 
HIS   HE2  H  N N 223 
HIS   HXT  H  N N 224 
HOH   O    O  N N 225 
HOH   H1   H  N N 226 
HOH   H2   H  N N 227 
ILE   N    N  N N 228 
ILE   CA   C  N S 229 
ILE   C    C  N N 230 
ILE   O    O  N N 231 
ILE   CB   C  N S 232 
ILE   CG1  C  N N 233 
ILE   CG2  C  N N 234 
ILE   CD1  C  N N 235 
ILE   OXT  O  N N 236 
ILE   H    H  N N 237 
ILE   H2   H  N N 238 
ILE   HA   H  N N 239 
ILE   HB   H  N N 240 
ILE   HG12 H  N N 241 
ILE   HG13 H  N N 242 
ILE   HG21 H  N N 243 
ILE   HG22 H  N N 244 
ILE   HG23 H  N N 245 
ILE   HD11 H  N N 246 
ILE   HD12 H  N N 247 
ILE   HD13 H  N N 248 
ILE   HXT  H  N N 249 
JQG   C02  C  N N 250 
JQG   C04  C  N N 251 
JQG   C05  C  N N 252 
JQG   C07  C  N N 253 
JQG   C08  C  N N 254 
JQG   C09  C  N N 255 
JQG   C11  C  N N 256 
JQG   C12  C  N R 257 
JQG   C14  C  N N 258 
JQG   C15  C  N N 259 
JQG   C16  C  N N 260 
JQG   C22  C  N N 261 
JQG   C25  C  N S 262 
JQG   C26  C  N N 263 
JQG   C27  C  N N 264 
JQG   C28  C  N N 265 
JQG   C30  C  N N 266 
JQG   N03  N  N N 267 
JQG   N06  N  N N 268 
JQG   N10  N  N N 269 
JQG   N29  N  N N 270 
JQG   O01  O  N N 271 
JQG   O13  O  N N 272 
JQG   O17  O  N N 273 
JQG   O19  O  N N 274 
JQG   O21  O  N N 275 
JQG   O23  O  N N 276 
JQG   O24  O  N N 277 
JQG   O31  O  N N 278 
JQG   P18  P  N N 279 
JQG   H041 H  N N 280 
JQG   H042 H  N N 281 
JQG   H052 H  N N 282 
JQG   H051 H  N N 283 
JQG   H081 H  N N 284 
JQG   H082 H  N N 285 
JQG   H092 H  N N 286 
JQG   H091 H  N N 287 
JQG   H121 H  N N 288 
JQG   H153 H  N N 289 
JQG   H152 H  N N 290 
JQG   H151 H  N N 291 
JQG   H162 H  N N 292 
JQG   H161 H  N N 293 
JQG   H223 H  N N 294 
JQG   H222 H  N N 295 
JQG   H221 H  N N 296 
JQG   H251 H  N N 297 
JQG   H261 H  N N 298 
JQG   H273 H  N N 299 
JQG   H272 H  N N 300 
JQG   H271 H  N N 301 
JQG   H283 H  N N 302 
JQG   H282 H  N N 303 
JQG   H281 H  N N 304 
JQG   H301 H  N N 305 
JQG   H031 H  N N 306 
JQG   H061 H  N N 307 
JQG   H101 H  N N 308 
JQG   H291 H  N N 309 
JQG   H131 H  N N 310 
JQG   O1   O  N N 311 
JQG   H1   H  N N 312 
LEU   N    N  N N 313 
LEU   CA   C  N S 314 
LEU   C    C  N N 315 
LEU   O    O  N N 316 
LEU   CB   C  N N 317 
LEU   CG   C  N N 318 
LEU   CD1  C  N N 319 
LEU   CD2  C  N N 320 
LEU   OXT  O  N N 321 
LEU   H    H  N N 322 
LEU   H2   H  N N 323 
LEU   HA   H  N N 324 
LEU   HB2  H  N N 325 
LEU   HB3  H  N N 326 
LEU   HG   H  N N 327 
LEU   HD11 H  N N 328 
LEU   HD12 H  N N 329 
LEU   HD13 H  N N 330 
LEU   HD21 H  N N 331 
LEU   HD22 H  N N 332 
LEU   HD23 H  N N 333 
LEU   HXT  H  N N 334 
LYS   N    N  N N 335 
LYS   CA   C  N S 336 
LYS   C    C  N N 337 
LYS   O    O  N N 338 
LYS   CB   C  N N 339 
LYS   CG   C  N N 340 
LYS   CD   C  N N 341 
LYS   CE   C  N N 342 
LYS   NZ   N  N N 343 
LYS   OXT  O  N N 344 
LYS   H    H  N N 345 
LYS   H2   H  N N 346 
LYS   HA   H  N N 347 
LYS   HB2  H  N N 348 
LYS   HB3  H  N N 349 
LYS   HG2  H  N N 350 
LYS   HG3  H  N N 351 
LYS   HD2  H  N N 352 
LYS   HD3  H  N N 353 
LYS   HE2  H  N N 354 
LYS   HE3  H  N N 355 
LYS   HZ1  H  N N 356 
LYS   HZ2  H  N N 357 
LYS   HZ3  H  N N 358 
LYS   HXT  H  N N 359 
MET   N    N  N N 360 
MET   CA   C  N S 361 
MET   C    C  N N 362 
MET   O    O  N N 363 
MET   CB   C  N N 364 
MET   CG   C  N N 365 
MET   SD   S  N N 366 
MET   CE   C  N N 367 
MET   OXT  O  N N 368 
MET   H    H  N N 369 
MET   H2   H  N N 370 
MET   HA   H  N N 371 
MET   HB2  H  N N 372 
MET   HB3  H  N N 373 
MET   HG2  H  N N 374 
MET   HG3  H  N N 375 
MET   HE1  H  N N 376 
MET   HE2  H  N N 377 
MET   HE3  H  N N 378 
MET   HXT  H  N N 379 
MN    MN   MN N N 380 
PHE   N    N  N N 381 
PHE   CA   C  N S 382 
PHE   C    C  N N 383 
PHE   O    O  N N 384 
PHE   CB   C  N N 385 
PHE   CG   C  Y N 386 
PHE   CD1  C  Y N 387 
PHE   CD2  C  Y N 388 
PHE   CE1  C  Y N 389 
PHE   CE2  C  Y N 390 
PHE   CZ   C  Y N 391 
PHE   OXT  O  N N 392 
PHE   H    H  N N 393 
PHE   H2   H  N N 394 
PHE   HA   H  N N 395 
PHE   HB2  H  N N 396 
PHE   HB3  H  N N 397 
PHE   HD1  H  N N 398 
PHE   HD2  H  N N 399 
PHE   HE1  H  N N 400 
PHE   HE2  H  N N 401 
PHE   HZ   H  N N 402 
PHE   HXT  H  N N 403 
PRO   N    N  N N 404 
PRO   CA   C  N S 405 
PRO   C    C  N N 406 
PRO   O    O  N N 407 
PRO   CB   C  N N 408 
PRO   CG   C  N N 409 
PRO   CD   C  N N 410 
PRO   OXT  O  N N 411 
PRO   H    H  N N 412 
PRO   HA   H  N N 413 
PRO   HB2  H  N N 414 
PRO   HB3  H  N N 415 
PRO   HG2  H  N N 416 
PRO   HG3  H  N N 417 
PRO   HD2  H  N N 418 
PRO   HD3  H  N N 419 
PRO   HXT  H  N N 420 
SER   N    N  N N 421 
SER   CA   C  N S 422 
SER   C    C  N N 423 
SER   O    O  N N 424 
SER   CB   C  N N 425 
SER   OG   O  N N 426 
SER   OXT  O  N N 427 
SER   H    H  N N 428 
SER   H2   H  N N 429 
SER   HA   H  N N 430 
SER   HB2  H  N N 431 
SER   HB3  H  N N 432 
SER   HG   H  N N 433 
SER   HXT  H  N N 434 
THR   N    N  N N 435 
THR   CA   C  N S 436 
THR   C    C  N N 437 
THR   O    O  N N 438 
THR   CB   C  N R 439 
THR   OG1  O  N N 440 
THR   CG2  C  N N 441 
THR   OXT  O  N N 442 
THR   H    H  N N 443 
THR   H2   H  N N 444 
THR   HA   H  N N 445 
THR   HB   H  N N 446 
THR   HG1  H  N N 447 
THR   HG21 H  N N 448 
THR   HG22 H  N N 449 
THR   HG23 H  N N 450 
THR   HXT  H  N N 451 
TRP   N    N  N N 452 
TRP   CA   C  N S 453 
TRP   C    C  N N 454 
TRP   O    O  N N 455 
TRP   CB   C  N N 456 
TRP   CG   C  Y N 457 
TRP   CD1  C  Y N 458 
TRP   CD2  C  Y N 459 
TRP   NE1  N  Y N 460 
TRP   CE2  C  Y N 461 
TRP   CE3  C  Y N 462 
TRP   CZ2  C  Y N 463 
TRP   CZ3  C  Y N 464 
TRP   CH2  C  Y N 465 
TRP   OXT  O  N N 466 
TRP   H    H  N N 467 
TRP   H2   H  N N 468 
TRP   HA   H  N N 469 
TRP   HB2  H  N N 470 
TRP   HB3  H  N N 471 
TRP   HD1  H  N N 472 
TRP   HE1  H  N N 473 
TRP   HE3  H  N N 474 
TRP   HZ2  H  N N 475 
TRP   HZ3  H  N N 476 
TRP   HH2  H  N N 477 
TRP   HXT  H  N N 478 
TYR   N    N  N N 479 
TYR   CA   C  N S 480 
TYR   C    C  N N 481 
TYR   O    O  N N 482 
TYR   CB   C  N N 483 
TYR   CG   C  Y N 484 
TYR   CD1  C  Y N 485 
TYR   CD2  C  Y N 486 
TYR   CE1  C  Y N 487 
TYR   CE2  C  Y N 488 
TYR   CZ   C  Y N 489 
TYR   OH   O  N N 490 
TYR   OXT  O  N N 491 
TYR   H    H  N N 492 
TYR   H2   H  N N 493 
TYR   HA   H  N N 494 
TYR   HB2  H  N N 495 
TYR   HB3  H  N N 496 
TYR   HD1  H  N N 497 
TYR   HD2  H  N N 498 
TYR   HE1  H  N N 499 
TYR   HE2  H  N N 500 
TYR   HH   H  N N 501 
TYR   HXT  H  N N 502 
VAL   N    N  N N 503 
VAL   CA   C  N S 504 
VAL   C    C  N N 505 
VAL   O    O  N N 506 
VAL   CB   C  N N 507 
VAL   CG1  C  N N 508 
VAL   CG2  C  N N 509 
VAL   OXT  O  N N 510 
VAL   H    H  N N 511 
VAL   H2   H  N N 512 
VAL   HA   H  N N 513 
VAL   HB   H  N N 514 
VAL   HG11 H  N N 515 
VAL   HG12 H  N N 516 
VAL   HG13 H  N N 517 
VAL   HG21 H  N N 518 
VAL   HG22 H  N N 519 
VAL   HG23 H  N N 520 
VAL   HXT  H  N N 521 
# 
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 
A1AMO C02 O01  doub N N 1   
A1AMO C04 N03  sing N N 2   
A1AMO C05 C04  sing N N 3   
A1AMO N06 C05  sing N N 4   
A1AMO C07 N06  sing N N 5   
A1AMO C09 C08  sing N N 6   
A1AMO N10 C09  sing N N 7   
A1AMO C11 N10  sing N N 8   
A1AMO O13 C12  sing N N 9   
A1AMO C14 C12  sing N N 10  
A1AMO C15 C14  sing N N 11  
A1AMO O17 C16  sing N N 12  
A1AMO P18 O17  sing N N 13  
A1AMO O19 P18  sing N N 14  
A1AMO O21 P18  doub N N 15  
A1AMO C16 C14  sing N N 16  
A1AMO C22 C14  sing N N 17  
A1AMO C12 C11  sing N N 18  
A1AMO O23 C11  doub N N 19  
A1AMO C08 C07  sing N N 20  
A1AMO O24 C07  doub N N 21  
A1AMO N03 C02  sing N N 22  
A1AMO C25 C02  sing N N 23  
A1AMO N29 C25  sing N N 24  
A1AMO O13 H131 sing N N 25  
A1AMO C12 H121 sing N N 26  
A1AMO C04 H041 sing N N 27  
A1AMO C04 H042 sing N N 28  
A1AMO C05 H052 sing N N 29  
A1AMO C05 H051 sing N N 30  
A1AMO C08 H081 sing N N 31  
A1AMO C08 H082 sing N N 32  
A1AMO C09 H091 sing N N 33  
A1AMO C09 H092 sing N N 34  
A1AMO C15 H151 sing N N 35  
A1AMO C15 H153 sing N N 36  
A1AMO C15 H152 sing N N 37  
A1AMO C16 H162 sing N N 38  
A1AMO C16 H161 sing N N 39  
A1AMO C22 H223 sing N N 40  
A1AMO C22 H221 sing N N 41  
A1AMO C22 H222 sing N N 42  
A1AMO C25 H251 sing N N 43  
A1AMO C25 H252 sing N N 44  
A1AMO N03 H031 sing N N 45  
A1AMO N06 H061 sing N N 46  
A1AMO N10 H101 sing N N 47  
A1AMO N29 H291 sing N N 48  
A1AMO N29 H292 sing N N 49  
A1AMO O19 H2   sing N N 50  
A1AMO P18 O1   sing N N 51  
A1AMO O1  H1   sing N N 52  
ALA   N   CA   sing N N 53  
ALA   N   H    sing N N 54  
ALA   N   H2   sing N N 55  
ALA   CA  C    sing N N 56  
ALA   CA  CB   sing N N 57  
ALA   CA  HA   sing N N 58  
ALA   C   O    doub N N 59  
ALA   C   OXT  sing N N 60  
ALA   CB  HB1  sing N N 61  
ALA   CB  HB2  sing N N 62  
ALA   CB  HB3  sing N N 63  
ALA   OXT HXT  sing N N 64  
ARG   N   CA   sing N N 65  
ARG   N   H    sing N N 66  
ARG   N   H2   sing N N 67  
ARG   CA  C    sing N N 68  
ARG   CA  CB   sing N N 69  
ARG   CA  HA   sing N N 70  
ARG   C   O    doub N N 71  
ARG   C   OXT  sing N N 72  
ARG   CB  CG   sing N N 73  
ARG   CB  HB2  sing N N 74  
ARG   CB  HB3  sing N N 75  
ARG   CG  CD   sing N N 76  
ARG   CG  HG2  sing N N 77  
ARG   CG  HG3  sing N N 78  
ARG   CD  NE   sing N N 79  
ARG   CD  HD2  sing N N 80  
ARG   CD  HD3  sing N N 81  
ARG   NE  CZ   sing N N 82  
ARG   NE  HE   sing N N 83  
ARG   CZ  NH1  sing N N 84  
ARG   CZ  NH2  doub N N 85  
ARG   NH1 HH11 sing N N 86  
ARG   NH1 HH12 sing N N 87  
ARG   NH2 HH21 sing N N 88  
ARG   NH2 HH22 sing N N 89  
ARG   OXT HXT  sing N N 90  
ASN   N   CA   sing N N 91  
ASN   N   H    sing N N 92  
ASN   N   H2   sing N N 93  
ASN   CA  C    sing N N 94  
ASN   CA  CB   sing N N 95  
ASN   CA  HA   sing N N 96  
ASN   C   O    doub N N 97  
ASN   C   OXT  sing N N 98  
ASN   CB  CG   sing N N 99  
ASN   CB  HB2  sing N N 100 
ASN   CB  HB3  sing N N 101 
ASN   CG  OD1  doub N N 102 
ASN   CG  ND2  sing N N 103 
ASN   ND2 HD21 sing N N 104 
ASN   ND2 HD22 sing N N 105 
ASN   OXT HXT  sing N N 106 
ASP   N   CA   sing N N 107 
ASP   N   H    sing N N 108 
ASP   N   H2   sing N N 109 
ASP   CA  C    sing N N 110 
ASP   CA  CB   sing N N 111 
ASP   CA  HA   sing N N 112 
ASP   C   O    doub N N 113 
ASP   C   OXT  sing N N 114 
ASP   CB  CG   sing N N 115 
ASP   CB  HB2  sing N N 116 
ASP   CB  HB3  sing N N 117 
ASP   CG  OD1  doub N N 118 
ASP   CG  OD2  sing N N 119 
ASP   OD2 HD2  sing N N 120 
ASP   OXT HXT  sing N N 121 
CYS   N   CA   sing N N 122 
CYS   N   H    sing N N 123 
CYS   N   H2   sing N N 124 
CYS   CA  C    sing N N 125 
CYS   CA  CB   sing N N 126 
CYS   CA  HA   sing N N 127 
CYS   C   O    doub N N 128 
CYS   C   OXT  sing N N 129 
CYS   CB  SG   sing N N 130 
CYS   CB  HB2  sing N N 131 
CYS   CB  HB3  sing N N 132 
CYS   SG  HG   sing N N 133 
CYS   OXT HXT  sing N N 134 
GLN   N   CA   sing N N 135 
GLN   N   H    sing N N 136 
GLN   N   H2   sing N N 137 
GLN   CA  C    sing N N 138 
GLN   CA  CB   sing N N 139 
GLN   CA  HA   sing N N 140 
GLN   C   O    doub N N 141 
GLN   C   OXT  sing N N 142 
GLN   CB  CG   sing N N 143 
GLN   CB  HB2  sing N N 144 
GLN   CB  HB3  sing N N 145 
GLN   CG  CD   sing N N 146 
GLN   CG  HG2  sing N N 147 
GLN   CG  HG3  sing N N 148 
GLN   CD  OE1  doub N N 149 
GLN   CD  NE2  sing N N 150 
GLN   NE2 HE21 sing N N 151 
GLN   NE2 HE22 sing N N 152 
GLN   OXT HXT  sing N N 153 
GLU   N   CA   sing N N 154 
GLU   N   H    sing N N 155 
GLU   N   H2   sing N N 156 
GLU   CA  C    sing N N 157 
GLU   CA  CB   sing N N 158 
GLU   CA  HA   sing N N 159 
GLU   C   O    doub N N 160 
GLU   C   OXT  sing N N 161 
GLU   CB  CG   sing N N 162 
GLU   CB  HB2  sing N N 163 
GLU   CB  HB3  sing N N 164 
GLU   CG  CD   sing N N 165 
GLU   CG  HG2  sing N N 166 
GLU   CG  HG3  sing N N 167 
GLU   CD  OE1  doub N N 168 
GLU   CD  OE2  sing N N 169 
GLU   OE2 HE2  sing N N 170 
GLU   OXT HXT  sing N N 171 
GLY   N   CA   sing N N 172 
GLY   N   H    sing N N 173 
GLY   N   H2   sing N N 174 
GLY   CA  C    sing N N 175 
GLY   CA  HA2  sing N N 176 
GLY   CA  HA3  sing N N 177 
GLY   C   O    doub N N 178 
GLY   C   OXT  sing N N 179 
GLY   OXT HXT  sing N N 180 
GOL   C1  O1   sing N N 181 
GOL   C1  C2   sing N N 182 
GOL   C1  H11  sing N N 183 
GOL   C1  H12  sing N N 184 
GOL   O1  HO1  sing N N 185 
GOL   C2  O2   sing N N 186 
GOL   C2  C3   sing N N 187 
GOL   C2  H2   sing N N 188 
GOL   O2  HO2  sing N N 189 
GOL   C3  O3   sing N N 190 
GOL   C3  H31  sing N N 191 
GOL   C3  H32  sing N N 192 
GOL   O3  HO3  sing N N 193 
HIS   N   CA   sing N N 194 
HIS   N   H    sing N N 195 
HIS   N   H2   sing N N 196 
HIS   CA  C    sing N N 197 
HIS   CA  CB   sing N N 198 
HIS   CA  HA   sing N N 199 
HIS   C   O    doub N N 200 
HIS   C   OXT  sing N N 201 
HIS   CB  CG   sing N N 202 
HIS   CB  HB2  sing N N 203 
HIS   CB  HB3  sing N N 204 
HIS   CG  ND1  sing Y N 205 
HIS   CG  CD2  doub Y N 206 
HIS   ND1 CE1  doub Y N 207 
HIS   ND1 HD1  sing N N 208 
HIS   CD2 NE2  sing Y N 209 
HIS   CD2 HD2  sing N N 210 
HIS   CE1 NE2  sing Y N 211 
HIS   CE1 HE1  sing N N 212 
HIS   NE2 HE2  sing N N 213 
HIS   OXT HXT  sing N N 214 
HOH   O   H1   sing N N 215 
HOH   O   H2   sing N N 216 
ILE   N   CA   sing N N 217 
ILE   N   H    sing N N 218 
ILE   N   H2   sing N N 219 
ILE   CA  C    sing N N 220 
ILE   CA  CB   sing N N 221 
ILE   CA  HA   sing N N 222 
ILE   C   O    doub N N 223 
ILE   C   OXT  sing N N 224 
ILE   CB  CG1  sing N N 225 
ILE   CB  CG2  sing N N 226 
ILE   CB  HB   sing N N 227 
ILE   CG1 CD1  sing N N 228 
ILE   CG1 HG12 sing N N 229 
ILE   CG1 HG13 sing N N 230 
ILE   CG2 HG21 sing N N 231 
ILE   CG2 HG22 sing N N 232 
ILE   CG2 HG23 sing N N 233 
ILE   CD1 HD11 sing N N 234 
ILE   CD1 HD12 sing N N 235 
ILE   CD1 HD13 sing N N 236 
ILE   OXT HXT  sing N N 237 
JQG   C27 C26  sing N N 238 
JQG   C28 C26  sing N N 239 
JQG   C26 C25  sing N N 240 
JQG   C25 N29  sing N N 241 
JQG   C25 C02  sing N N 242 
JQG   N29 C30  sing N N 243 
JQG   C30 O31  doub N N 244 
JQG   C02 O01  doub N N 245 
JQG   C02 N03  sing N N 246 
JQG   N03 C04  sing N N 247 
JQG   C04 C05  sing N N 248 
JQG   C05 N06  sing N N 249 
JQG   N06 C07  sing N N 250 
JQG   O24 C07  doub N N 251 
JQG   C07 C08  sing N N 252 
JQG   C08 C09  sing N N 253 
JQG   C09 N10  sing N N 254 
JQG   C15 C14  sing N N 255 
JQG   O23 C11  doub N N 256 
JQG   C22 C14  sing N N 257 
JQG   N10 C11  sing N N 258 
JQG   C11 C12  sing N N 259 
JQG   C14 C12  sing N N 260 
JQG   C14 C16  sing N N 261 
JQG   C12 O13  sing N N 262 
JQG   C16 O17  sing N N 263 
JQG   O17 P18  sing N N 264 
JQG   O21 P18  doub N N 265 
JQG   P18 O19  doub N N 266 
JQG   C04 H041 sing N N 267 
JQG   C04 H042 sing N N 268 
JQG   C05 H052 sing N N 269 
JQG   C05 H051 sing N N 270 
JQG   C08 H081 sing N N 271 
JQG   C08 H082 sing N N 272 
JQG   C09 H092 sing N N 273 
JQG   C09 H091 sing N N 274 
JQG   C12 H121 sing N N 275 
JQG   C15 H153 sing N N 276 
JQG   C15 H152 sing N N 277 
JQG   C15 H151 sing N N 278 
JQG   C16 H162 sing N N 279 
JQG   C16 H161 sing N N 280 
JQG   C22 H223 sing N N 281 
JQG   C22 H222 sing N N 282 
JQG   C22 H221 sing N N 283 
JQG   C25 H251 sing N N 284 
JQG   C26 H261 sing N N 285 
JQG   C27 H273 sing N N 286 
JQG   C27 H272 sing N N 287 
JQG   C27 H271 sing N N 288 
JQG   C28 H283 sing N N 289 
JQG   C28 H282 sing N N 290 
JQG   C28 H281 sing N N 291 
JQG   C30 H301 sing N N 292 
JQG   N03 H031 sing N N 293 
JQG   N06 H061 sing N N 294 
JQG   N10 H101 sing N N 295 
JQG   N29 H291 sing N N 296 
JQG   O13 H131 sing N N 297 
JQG   P18 O1   sing N N 298 
JQG   O1  H1   sing N N 299 
LEU   N   CA   sing N N 300 
LEU   N   H    sing N N 301 
LEU   N   H2   sing N N 302 
LEU   CA  C    sing N N 303 
LEU   CA  CB   sing N N 304 
LEU   CA  HA   sing N N 305 
LEU   C   O    doub N N 306 
LEU   C   OXT  sing N N 307 
LEU   CB  CG   sing N N 308 
LEU   CB  HB2  sing N N 309 
LEU   CB  HB3  sing N N 310 
LEU   CG  CD1  sing N N 311 
LEU   CG  CD2  sing N N 312 
LEU   CG  HG   sing N N 313 
LEU   CD1 HD11 sing N N 314 
LEU   CD1 HD12 sing N N 315 
LEU   CD1 HD13 sing N N 316 
LEU   CD2 HD21 sing N N 317 
LEU   CD2 HD22 sing N N 318 
LEU   CD2 HD23 sing N N 319 
LEU   OXT HXT  sing N N 320 
LYS   N   CA   sing N N 321 
LYS   N   H    sing N N 322 
LYS   N   H2   sing N N 323 
LYS   CA  C    sing N N 324 
LYS   CA  CB   sing N N 325 
LYS   CA  HA   sing N N 326 
LYS   C   O    doub N N 327 
LYS   C   OXT  sing N N 328 
LYS   CB  CG   sing N N 329 
LYS   CB  HB2  sing N N 330 
LYS   CB  HB3  sing N N 331 
LYS   CG  CD   sing N N 332 
LYS   CG  HG2  sing N N 333 
LYS   CG  HG3  sing N N 334 
LYS   CD  CE   sing N N 335 
LYS   CD  HD2  sing N N 336 
LYS   CD  HD3  sing N N 337 
LYS   CE  NZ   sing N N 338 
LYS   CE  HE2  sing N N 339 
LYS   CE  HE3  sing N N 340 
LYS   NZ  HZ1  sing N N 341 
LYS   NZ  HZ2  sing N N 342 
LYS   NZ  HZ3  sing N N 343 
LYS   OXT HXT  sing N N 344 
MET   N   CA   sing N N 345 
MET   N   H    sing N N 346 
MET   N   H2   sing N N 347 
MET   CA  C    sing N N 348 
MET   CA  CB   sing N N 349 
MET   CA  HA   sing N N 350 
MET   C   O    doub N N 351 
MET   C   OXT  sing N N 352 
MET   CB  CG   sing N N 353 
MET   CB  HB2  sing N N 354 
MET   CB  HB3  sing N N 355 
MET   CG  SD   sing N N 356 
MET   CG  HG2  sing N N 357 
MET   CG  HG3  sing N N 358 
MET   SD  CE   sing N N 359 
MET   CE  HE1  sing N N 360 
MET   CE  HE2  sing N N 361 
MET   CE  HE3  sing N N 362 
MET   OXT HXT  sing N N 363 
PHE   N   CA   sing N N 364 
PHE   N   H    sing N N 365 
PHE   N   H2   sing N N 366 
PHE   CA  C    sing N N 367 
PHE   CA  CB   sing N N 368 
PHE   CA  HA   sing N N 369 
PHE   C   O    doub N N 370 
PHE   C   OXT  sing N N 371 
PHE   CB  CG   sing N N 372 
PHE   CB  HB2  sing N N 373 
PHE   CB  HB3  sing N N 374 
PHE   CG  CD1  doub Y N 375 
PHE   CG  CD2  sing Y N 376 
PHE   CD1 CE1  sing Y N 377 
PHE   CD1 HD1  sing N N 378 
PHE   CD2 CE2  doub Y N 379 
PHE   CD2 HD2  sing N N 380 
PHE   CE1 CZ   doub Y N 381 
PHE   CE1 HE1  sing N N 382 
PHE   CE2 CZ   sing Y N 383 
PHE   CE2 HE2  sing N N 384 
PHE   CZ  HZ   sing N N 385 
PHE   OXT HXT  sing N N 386 
PRO   N   CA   sing N N 387 
PRO   N   CD   sing N N 388 
PRO   N   H    sing N N 389 
PRO   CA  C    sing N N 390 
PRO   CA  CB   sing N N 391 
PRO   CA  HA   sing N N 392 
PRO   C   O    doub N N 393 
PRO   C   OXT  sing N N 394 
PRO   CB  CG   sing N N 395 
PRO   CB  HB2  sing N N 396 
PRO   CB  HB3  sing N N 397 
PRO   CG  CD   sing N N 398 
PRO   CG  HG2  sing N N 399 
PRO   CG  HG3  sing N N 400 
PRO   CD  HD2  sing N N 401 
PRO   CD  HD3  sing N N 402 
PRO   OXT HXT  sing N N 403 
SER   N   CA   sing N N 404 
SER   N   H    sing N N 405 
SER   N   H2   sing N N 406 
SER   CA  C    sing N N 407 
SER   CA  CB   sing N N 408 
SER   CA  HA   sing N N 409 
SER   C   O    doub N N 410 
SER   C   OXT  sing N N 411 
SER   CB  OG   sing N N 412 
SER   CB  HB2  sing N N 413 
SER   CB  HB3  sing N N 414 
SER   OG  HG   sing N N 415 
SER   OXT HXT  sing N N 416 
THR   N   CA   sing N N 417 
THR   N   H    sing N N 418 
THR   N   H2   sing N N 419 
THR   CA  C    sing N N 420 
THR   CA  CB   sing N N 421 
THR   CA  HA   sing N N 422 
THR   C   O    doub N N 423 
THR   C   OXT  sing N N 424 
THR   CB  OG1  sing N N 425 
THR   CB  CG2  sing N N 426 
THR   CB  HB   sing N N 427 
THR   OG1 HG1  sing N N 428 
THR   CG2 HG21 sing N N 429 
THR   CG2 HG22 sing N N 430 
THR   CG2 HG23 sing N N 431 
THR   OXT HXT  sing N N 432 
TRP   N   CA   sing N N 433 
TRP   N   H    sing N N 434 
TRP   N   H2   sing N N 435 
TRP   CA  C    sing N N 436 
TRP   CA  CB   sing N N 437 
TRP   CA  HA   sing N N 438 
TRP   C   O    doub N N 439 
TRP   C   OXT  sing N N 440 
TRP   CB  CG   sing N N 441 
TRP   CB  HB2  sing N N 442 
TRP   CB  HB3  sing N N 443 
TRP   CG  CD1  doub Y N 444 
TRP   CG  CD2  sing Y N 445 
TRP   CD1 NE1  sing Y N 446 
TRP   CD1 HD1  sing N N 447 
TRP   CD2 CE2  doub Y N 448 
TRP   CD2 CE3  sing Y N 449 
TRP   NE1 CE2  sing Y N 450 
TRP   NE1 HE1  sing N N 451 
TRP   CE2 CZ2  sing Y N 452 
TRP   CE3 CZ3  doub Y N 453 
TRP   CE3 HE3  sing N N 454 
TRP   CZ2 CH2  doub Y N 455 
TRP   CZ2 HZ2  sing N N 456 
TRP   CZ3 CH2  sing Y N 457 
TRP   CZ3 HZ3  sing N N 458 
TRP   CH2 HH2  sing N N 459 
TRP   OXT HXT  sing N N 460 
TYR   N   CA   sing N N 461 
TYR   N   H    sing N N 462 
TYR   N   H2   sing N N 463 
TYR   CA  C    sing N N 464 
TYR   CA  CB   sing N N 465 
TYR   CA  HA   sing N N 466 
TYR   C   O    doub N N 467 
TYR   C   OXT  sing N N 468 
TYR   CB  CG   sing N N 469 
TYR   CB  HB2  sing N N 470 
TYR   CB  HB3  sing N N 471 
TYR   CG  CD1  doub Y N 472 
TYR   CG  CD2  sing Y N 473 
TYR   CD1 CE1  sing Y N 474 
TYR   CD1 HD1  sing N N 475 
TYR   CD2 CE2  doub Y N 476 
TYR   CD2 HD2  sing N N 477 
TYR   CE1 CZ   doub Y N 478 
TYR   CE1 HE1  sing N N 479 
TYR   CE2 CZ   sing Y N 480 
TYR   CE2 HE2  sing N N 481 
TYR   CZ  OH   sing N N 482 
TYR   OH  HH   sing N N 483 
TYR   OXT HXT  sing N N 484 
VAL   N   CA   sing N N 485 
VAL   N   H    sing N N 486 
VAL   N   H2   sing N N 487 
VAL   CA  C    sing N N 488 
VAL   CA  CB   sing N N 489 
VAL   CA  HA   sing N N 490 
VAL   C   O    doub N N 491 
VAL   C   OXT  sing N N 492 
VAL   CB  CG1  sing N N 493 
VAL   CB  CG2  sing N N 494 
VAL   CB  HB   sing N N 495 
VAL   CG1 HG11 sing N N 496 
VAL   CG1 HG12 sing N N 497 
VAL   CG1 HG13 sing N N 498 
VAL   CG2 HG21 sing N N 499 
VAL   CG2 HG22 sing N N 500 
VAL   CG2 HG23 sing N N 501 
VAL   OXT HXT  sing N N 502 
# 
_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                    9BE3 
_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]   0.005411 
_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]   0.002337 
_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]   0.012934 
_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   ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-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    ? -81.14900  49.68600  28.87200  1.000 101.07741 ?  1    MET   A N   1 
ATOM   2     C  CA  . MET   A 1 1    ? -80.77500  51.04500  28.49900  1.000 87.28528  ?  1    MET   A CA  1 
ATOM   3     C  C   . MET   A 1 1    ? -81.22700  52.04400  29.56300  1.000 91.35131  ?  1    MET   A C   1 
ATOM   4     O  O   . MET   A 1 1    ? -82.16000  51.77500  30.32100  1.000 100.26223 ?  1    MET   A O   1 
ATOM   5     C  CB  . MET   A 1 1    ? -81.37700  51.41000  27.14000  1.000 97.91821  ?  1    MET   A CB  1 
ATOM   6     C  CG  . MET   A 1 1    ? -82.81200  51.91200  27.21100  1.000 94.30894  ?  1    MET   A CG  1 
ATOM   7     S  SD  . MET   A 1 1    ? -83.63600  51.99000  25.60800  1.000 109.98761 ?  1    MET   A SD  1 
ATOM   8     C  CE  . MET   A 1 1    ? -83.02400  50.49800  24.82400  1.000 67.10079  ?  1    MET   A CE  1 
ATOM   9     N  N   . GLY   A 1 2    ? -80.56200  53.20000  29.61400  1.000 71.85702  ?  2    GLY   A N   1 
ATOM   10    C  CA  . GLY   A 1 2    ? -80.90600  54.22900  30.57500  1.000 64.14537  ?  2    GLY   A CA  1 
ATOM   11    C  C   . GLY   A 1 2    ? -80.53600  55.60400  30.06300  1.000 68.26748  ?  2    GLY   A C   1 
ATOM   12    O  O   . GLY   A 1 2    ? -79.90900  55.75500  29.01200  1.000 68.53769  ?  2    GLY   A O   1 
ATOM   13    N  N   . ARG   A 1 3    ? -80.93900  56.61600  30.82700  1.000 64.38273  ?  3    ARG   A N   1 
ATOM   14    C  CA  . ARG   A 1 3    ? -80.64100  57.99700  30.47900  1.000 59.32473  ?  3    ARG   A CA  1 
ATOM   15    C  C   . ARG   A 1 3    ? -79.24400  58.36900  30.95100  1.000 63.66764  ?  3    ARG   A C   1 
ATOM   16    O  O   . ARG   A 1 3    ? -78.83000  58.01100  32.05700  1.000 64.68092  ?  3    ARG   A O   1 
ATOM   17    C  CB  . ARG   A 1 3    ? -81.66900  58.94200  31.10000  1.000 62.02292  ?  3    ARG   A CB  1 
ATOM   18    C  CG  . ARG   A 1 3    ? -82.88800  59.20100  30.23000  1.000 70.66821  ?  3    ARG   A CG  1 
ATOM   19    C  CD  . ARG   A 1 3    ? -83.83600  60.17400  30.90600  1.000 65.29078  ?  3    ARG   A CD  1 
ATOM   20    N  NE  . ARG   A 1 3    ? -83.72000  61.52100  30.36500  1.000 73.19039  ?  3    ARG   A NE  1 
ATOM   21    C  CZ  . ARG   A 1 3    ? -83.86600  62.62700  31.08100  1.000 80.23276  ?  3    ARG   A CZ  1 
ATOM   22    N  NH1 . ARG   A 1 3    ? -84.11600  62.58100  32.38000  1.000 87.98029  ?  3    ARG   A NH1 1 
ATOM   23    N  NH2 . ARG   A 1 3    ? -83.75400  63.80900  30.48100  1.000 70.38288  ?  3    ARG   A NH2 1 
ATOM   24    N  N   . ILE   A 1 4    ? -78.51400  59.09100  30.10400  1.000 66.42846  ?  4    ILE   A N   1 
ATOM   25    C  CA  . ILE   A 1 4    ? -77.16300  59.53600  30.41700  1.000 56.97882  ?  4    ILE   A CA  1 
ATOM   26    C  C   . ILE   A 1 4    ? -77.09700  61.04900  30.27700  1.000 56.17034  ?  4    ILE   A C   1 
ATOM   27    O  O   . ILE   A 1 4    ? -77.60500  61.61000  29.30000  1.000 55.83255  ?  4    ILE   A O   1 
ATOM   28    C  CB  . ILE   A 1 4    ? -76.10700  58.87100  29.51400  1.000 43.53402  ?  4    ILE   A CB  1 
ATOM   29    C  CG1 . ILE   A 1 4    ? -76.34100  57.36400  29.41300  1.000 41.19639  ?  4    ILE   A CG1 1 
ATOM   30    C  CG2 . ILE   A 1 4    ? -74.71300  59.16300  30.02900  1.000 67.97690  ?  4    ILE   A CG2 1 
ATOM   31    C  CD1 . ILE   A 1 4    ? -75.75200  56.74700  28.17200  1.000 51.91382  ?  4    ILE   A CD1 1 
ATOM   32    N  N   . LEU   A 1 5    ? -76.46900  61.70600  31.25000  1.000 53.54396  ?  5    LEU   A N   1 
ATOM   33    C  CA  . LEU   A 1 5    ? -76.16300  63.12900  31.17100  1.000 51.12379  ?  5    LEU   A CA  1 
ATOM   34    C  C   . LEU   A 1 5    ? -74.71200  63.27900  30.72700  1.000 62.69814  ?  5    LEU   A C   1 
ATOM   35    O  O   . LEU   A 1 5    ? -73.78900  63.03600  31.51100  1.000 68.93255  ?  5    LEU   A O   1 
ATOM   36    C  CB  . LEU   A 1 5    ? -76.39700  63.82100  32.51000  1.000 39.35589  ?  5    LEU   A CB  1 
ATOM   37    C  CG  . LEU   A 1 5    ? -76.28100  65.34600  32.47900  1.000 59.75791  ?  5    LEU   A CG  1 
ATOM   38    C  CD1 . LEU   A 1 5    ? -77.25000  65.94300  31.46700  1.000 63.87360  ?  5    LEU   A CD1 1 
ATOM   39    C  CD2 . LEU   A 1 5    ? -76.51000  65.93200  33.86300  1.000 62.49173  ?  5    LEU   A CD2 1 
ATOM   40    N  N   . PHE   A 1 6    ? -74.51100  63.67800  29.47400  1.000 55.26144  ?  6    PHE   A N   1 
ATOM   41    C  CA  . PHE   A 1 6    ? -73.17200  63.88400  28.93600  1.000 46.27396  ?  6    PHE   A CA  1 
ATOM   42    C  C   . PHE   A 1 6    ? -72.73500  65.31800  29.20700  1.000 57.18179  ?  6    PHE   A C   1 
ATOM   43    O  O   . PHE   A 1 6    ? -73.38700  66.26600  28.75700  1.000 51.94994  ?  6    PHE   A O   1 
ATOM   44    C  CB  . PHE   A 1 6    ? -73.12700  63.58000  27.44100  1.000 40.81761  ?  6    PHE   A CB  1 
ATOM   45    C  CG  . PHE   A 1 6    ? -71.74500  63.29900  26.92600  1.000 44.66555  ?  6    PHE   A CG  1 
ATOM   46    C  CD1 . PHE   A 1 6    ? -70.92800  64.33100  26.49200  1.000 47.47418  ?  6    PHE   A CD1 1 
ATOM   47    C  CD2 . PHE   A 1 6    ? -71.25600  62.00400  26.89300  1.000 41.89567  ?  6    PHE   A CD2 1 
ATOM   48    C  CE1 . PHE   A 1 6    ? -69.65400  64.07500  26.02200  1.000 37.40228  ?  6    PHE   A CE1 1 
ATOM   49    C  CE2 . PHE   A 1 6    ? -69.98200  61.74100  26.42500  1.000 49.70405  ?  6    PHE   A CE2 1 
ATOM   50    C  CZ  . PHE   A 1 6    ? -69.18000  62.77800  25.98900  1.000 44.91609  ?  6    PHE   A CZ  1 
ATOM   51    N  N   . LEU   A 1 7    ? -71.63200  65.47300  29.93700  1.000 53.92618  ?  7    LEU   A N   1 
ATOM   52    C  CA  . LEU   A 1 7    ? -71.11200  66.78300  30.31500  1.000 46.65097  ?  7    LEU   A CA  1 
ATOM   53    C  C   . LEU   A 1 7    ? -69.84600  67.05300  29.51500  1.000 51.85145  ?  7    LEU   A C   1 
ATOM   54    O  O   . LEU   A 1 7    ? -68.83200  66.37100  29.69700  1.000 57.47724  ?  7    LEU   A O   1 
ATOM   55    C  CB  . LEU   A 1 7    ? -70.83100  66.85300  31.81300  1.000 58.72732  ?  7    LEU   A CB  1 
ATOM   56    C  CG  . LEU   A 1 7    ? -71.99500  66.56200  32.75700  1.000 62.44219  ?  7    LEU   A CG  1 
ATOM   57    C  CD1 . LEU   A 1 7    ? -71.47300  66.12600  34.11300  1.000 47.20672  ?  7    LEU   A CD1 1 
ATOM   58    C  CD2 . LEU   A 1 7    ? -72.88500  67.78400  32.89200  1.000 69.60427  ?  7    LEU   A CD2 1 
ATOM   59    N  N   . THR   A 1 8    ? -69.90500  68.04800  28.63500  1.000 46.49677  ?  8    THR   A N   1 
ATOM   60    C  CA  . THR   A 1 8    ? -68.74000  68.48700  27.88200  1.000 51.63133  ?  8    THR   A CA  1 
ATOM   61    C  C   . THR   A 1 8    ? -68.77700  69.99900  27.73400  1.000 45.57890  ?  8    THR   A C   1 
ATOM   62    O  O   . THR   A 1 8    ? -69.82800  70.57800  27.45200  1.000 46.65089  ?  8    THR   A O   1 
ATOM   63    C  CB  . THR   A 1 8    ? -68.66700  67.82700  26.49700  1.000 47.86041  ?  8    THR   A CB  1 
ATOM   64    O  OG1 . THR   A 1 8    ? -67.60200  68.42300  25.74700  1.000 60.35579  ?  8    THR   A OG1 1 
ATOM   65    C  CG2 . THR   A 1 8    ? -69.97600  67.99100  25.73900  1.000 45.56001  ?  8    THR   A CG2 1 
ATOM   66    N  N   . THR   A 1 9    ? -67.62900  70.63400  27.93700  1.000 50.85121  ?  9    THR   A N   1 
ATOM   67    C  CA  . THR   A 1 9    ? -67.49700  72.07500  27.76200  1.000 49.89936  ?  9    THR   A CA  1 
ATOM   68    C  C   . THR   A 1 9    ? -66.62900  72.45200  26.57700  1.000 57.21912  ?  9    THR   A C   1 
ATOM   69    O  O   . THR   A 1 9    ? -66.92200  73.43300  25.89000  1.000 62.14625  ?  9    THR   A O   1 
ATOM   70    C  CB  . THR   A 1 9    ? -66.91200  72.71600  29.02500  1.000 46.88153  ?  9    THR   A CB  1 
ATOM   71    O  OG1 . THR   A 1 9    ? -67.42300  72.04700  30.18200  1.000 67.59900  ?  9    THR   A OG1 1 
ATOM   72    C  CG2 . THR   A 1 9    ? -67.28100  74.19200  29.09400  1.000 59.70218  ?  9    THR   A CG2 1 
ATOM   73    N  N   . PHE   A 1 10   ? -65.56800  71.68800  26.32100  1.000 60.54549  ?  10   PHE   A N   1 
ATOM   74    C  CA  . PHE   A 1 10   ? -64.61400  72.00000  25.27100  1.000 50.22376  ?  10   PHE   A CA  1 
ATOM   75    C  C   . PHE   A 1 10   ? -64.65000  71.02000  24.10700  1.000 48.73926  ?  10   PHE   A C   1 
ATOM   76    O  O   . PHE   A 1 10   ? -64.02700  71.29000  23.07600  1.000 51.57376  ?  10   PHE   A O   1 
ATOM   77    C  CB  . PHE   A 1 10   ? -63.19500  72.05500  25.85600  1.000 42.43372  ?  10   PHE   A CB  1 
ATOM   78    C  CG  . PHE   A 1 10   ? -63.06200  72.99600  27.02000  1.000 47.83932  ?  10   PHE   A CG  1 
ATOM   79    C  CD1 . PHE   A 1 10   ? -63.13700  74.36700  26.83200  1.000 52.39326  ?  10   PHE   A CD1 1 
ATOM   80    C  CD2 . PHE   A 1 10   ? -62.87300  72.51000  28.30400  1.000 45.09443  ?  10   PHE   A CD2 1 
ATOM   81    C  CE1 . PHE   A 1 10   ? -63.02100  75.23800  27.90200  1.000 45.84059  ?  10   PHE   A CE1 1 
ATOM   82    C  CE2 . PHE   A 1 10   ? -62.75600  73.37600  29.37700  1.000 52.29971  ?  10   PHE   A CE2 1 
ATOM   83    C  CZ  . PHE   A 1 10   ? -62.83000  74.74000  29.17500  1.000 50.98598  ?  10   PHE   A CZ  1 
ATOM   84    N  N   . MET   A 1 11   ? -65.35200  69.90200  24.23600  1.000 45.72710  ?  11   MET   A N   1 
ATOM   85    C  CA  . MET   A 1 11   ? -65.54700  68.99700  23.11800  1.000 49.79576  ?  11   MET   A CA  1 
ATOM   86    C  C   . MET   A 1 11   ? -66.86700  69.31700  22.42300  1.000 56.57901  ?  11   MET   A C   1 
ATOM   87    O  O   . MET   A 1 11   ? -67.55400  70.29100  22.75000  1.000 51.43359  ?  11   MET   A O   1 
ATOM   88    C  CB  . MET   A 1 11   ? -65.49500  67.54200  23.58400  1.000 44.12149  ?  11   MET   A CB  1 
ATOM   89    C  CG  . MET   A 1 11   ? -64.15400  67.11500  24.13400  1.000 46.33078  ?  11   MET   A CG  1 
ATOM   90    S  SD  . MET   A 1 11   ? -62.87600  67.02400  22.86500  1.000 55.40539  ?  11   MET   A SD  1 
ATOM   91    C  CE  . MET   A 1 11   ? -63.78800  66.32000  21.49200  1.000 69.58320  ?  11   MET   A CE  1 
ATOM   92    N  N   . SER   A 1 12   ? -67.22700  68.49000  21.44900  1.000 51.12923  ?  12   SER   A N   1 
ATOM   93    C  CA  . SER   A 1 12   ? -68.40500  68.74500  20.64100  1.000 57.34163  ?  12   SER   A CA  1 
ATOM   94    C  C   . SER   A 1 12   ? -69.65900  68.21000  21.32800  1.000 59.30953  ?  12   SER   A C   1 
ATOM   95    O  O   . SER   A 1 12   ? -69.61400  67.58700  22.39200  1.000 65.84297  ?  12   SER   A O   1 
ATOM   96    C  CB  . SER   A 1 12   ? -68.24200  68.12700  19.25500  1.000 63.56993  ?  12   SER   A CB  1 
ATOM   97    O  OG  . SER   A 1 12   ? -69.50500  67.79400  18.70300  1.000 80.50362  ?  12   SER   A OG  1 
ATOM   98    N  N   . LYS   A 1 13   ? -70.79900  68.46600  20.69600  1.000 65.13697  ?  13   LYS   A N   1 
ATOM   99    C  CA  . LYS   A 1 13   ? -72.08900  67.99300  21.16700  1.000 52.49528  ?  13   LYS   A CA  1 
ATOM   100   C  C   . LYS   A 1 13   ? -72.49200  66.69400  20.49300  1.000 52.55941  ?  13   LYS   A C   1 
ATOM   101   O  O   . LYS   A 1 13   ? -73.31500  65.95200  21.03900  1.000 58.93724  ?  13   LYS   A O   1 
ATOM   102   C  CB  . LYS   A 1 13   ? -73.18200  69.05200  20.92200  1.000 50.88426  ?  13   LYS   A CB  1 
ATOM   103   C  CG  . LYS   A 1 13   ? -72.99400  70.44900  21.56800  1.000 77.83252  ?  13   LYS   A CG  1 
ATOM   104   C  CD  . LYS   A 1 13   ? -71.66800  71.14000  21.23700  1.000 81.09660  ?  13   LYS   A CD  1 
ATOM   105   C  CE  . LYS   A 1 13   ? -71.67400  71.82700  19.88800  1.000 62.80627  ?  13   LYS   A CE  1 
ATOM   106   N  NZ  . LYS   A 1 13   ? -70.29400  72.20400  19.47400  1.000 61.14376  ?  13   LYS   A NZ  1 
ATOM   107   N  N   . GLY   A 1 14   ? -71.93200  66.41700  19.31900  1.000 43.08563  ?  14   GLY   A N   1 
ATOM   108   C  CA  . GLY   A 1 14   ? -72.11300  65.15000  18.65000  1.000 52.19836  ?  14   GLY   A CA  1 
ATOM   109   C  C   . GLY   A 1 14   ? -70.78500  64.45600  18.44200  1.000 62.52139  ?  14   GLY   A C   1 
ATOM   110   O  O   . GLY   A 1 14   ? -70.39800  64.16400  17.30700  1.000 69.71869  ?  14   GLY   A O   1 
ATOM   111   N  N   . ASN   A 1 15   ? -70.06800  64.20500  19.53400  1.000 56.31126  ?  15   ASN   A N   1 
ATOM   112   C  CA  . ASN   A 1 15   ? -68.83500  63.44200  19.46000  1.000 57.27690  ?  15   ASN   A CA  1 
ATOM   113   C  C   . ASN   A 1 15   ? -69.12700  61.99200  19.08600  1.000 51.96987  ?  15   ASN   A C   1 
ATOM   114   O  O   . ASN   A 1 15   ? -70.27600  61.54300  19.03900  1.000 54.12299  ?  15   ASN   A O   1 
ATOM   115   C  CB  . ASN   A 1 15   ? -68.08700  63.48600  20.79000  1.000 66.97849  ?  15   ASN   A CB  1 
ATOM   116   C  CG  . ASN   A 1 15   ? -68.20100  64.82500  21.47300  1.000 87.13144  ?  15   ASN   A CG  1 
ATOM   117   O  OD1 . ASN   A 1 15   ? -67.39500  65.72300  21.23200  1.000 116.01618 ?  15   ASN   A OD1 1 
ATOM   118   N  ND2 . ASN   A 1 15   ? -69.20500  64.97300  22.32900  1.000 84.41255  ?  15   ASN   A ND2 1 
ATOM   119   N  N   . LYS   A 1 16   ? -68.05100  61.25000  18.82500  1.000 50.35236  ?  16   LYS   A N   1 
ATOM   120   C  CA  . LYS   A 1 16   ? -68.19200  59.83400  18.51700  1.000 40.95670  ?  16   LYS   A CA  1 
ATOM   121   C  C   . LYS   A 1 16   ? -68.71800  59.06100  19.71800  1.000 43.34485  ?  16   LYS   A C   1 
ATOM   122   O  O   . LYS   A 1 16   ? -69.41600  58.05400  19.55400  1.000 57.60229  ?  16   LYS   A O   1 
ATOM   123   C  CB  . LYS   A 1 16   ? -66.84800  59.28000  18.04000  1.000 40.22366  ?  16   LYS   A CB  1 
ATOM   124   C  CG  . LYS   A 1 16   ? -66.72600  57.76900  18.03000  1.000 54.73213  ?  16   LYS   A CG  1 
ATOM   125   C  CD  . LYS   A 1 16   ? -65.27400  57.35000  17.86300  1.000 52.28104  ?  16   LYS   A CD  1 
ATOM   126   C  CE  . LYS   A 1 16   ? -64.85100  57.35300  16.40400  1.000 51.65183  ?  16   LYS   A CE  1 
ATOM   127   N  NZ  . LYS   A 1 16   ? -64.94900  55.99100  15.81000  1.000 61.91500  ?  16   LYS   A NZ  1 
ATOM   128   N  N   . VAL   A 1 17   ? -68.42600  59.53500  20.93000  1.000 47.68967  ?  17   VAL   A N   1 
ATOM   129   C  CA  . VAL   A 1 17   ? -68.87800  58.83900  22.13000  1.000 51.65254  ?  17   VAL   A CA  1 
ATOM   130   C  C   . VAL   A 1 17   ? -70.39200  58.95500  22.27400  1.000 51.38370  ?  17   VAL   A C   1 
ATOM   131   O  O   . VAL   A 1 17   ? -71.08700  57.95500  22.49200  1.000 50.52022  ?  17   VAL   A O   1 
ATOM   132   C  CB  . VAL   A 1 17   ? -68.14600  59.38200  23.37000  1.000 45.66334  ?  17   VAL   A CB  1 
ATOM   133   C  CG1 . VAL   A 1 17   ? -66.84800  58.61700  23.59000  1.000 47.71126  ?  17   VAL   A CG1 1 
ATOM   134   C  CG2 . VAL   A 1 17   ? -67.86700  60.86400  23.21400  1.000 57.11226  ?  17   VAL   A CG2 1 
ATOM   135   N  N   . VAL   A 1 18   ? -70.92500  60.17500  22.14600  1.000 47.41960  ?  18   VAL   A N   1 
ATOM   136   C  CA  . VAL   A 1 18   ? -72.36800  60.38100  22.25200  1.000 47.88479  ?  18   VAL   A CA  1 
ATOM   137   C  C   . VAL   A 1 18   ? -73.10400  59.54300  21.21500  1.000 54.22128  ?  18   VAL   A C   1 
ATOM   138   O  O   . VAL   A 1 18   ? -74.16100  58.96300  21.49500  1.000 65.38144  ?  18   VAL   A O   1 
ATOM   139   C  CB  . VAL   A 1 18   ? -72.70200  61.88000  22.11800  1.000 39.29062  ?  18   VAL   A CB  1 
ATOM   140   C  CG1 . VAL   A 1 18   ? -74.16200  62.08400  21.74300  1.000 47.91370  ?  18   VAL   A CG1 1 
ATOM   141   C  CG2 . VAL   A 1 18   ? -72.38600  62.60700  23.41300  1.000 51.60110  ?  18   VAL   A CG2 1 
ATOM   142   N  N   . ARG   A 1 19   ? -72.54200  59.44000  20.01000  1.000 43.93307  ?  19   ARG   A N   1 
ATOM   143   C  CA  . ARG   A 1 19   ? -73.18800  58.66500  18.95800  1.000 44.51619  ?  19   ARG   A CA  1 
ATOM   144   C  C   . ARG   A 1 19   ? -73.14800  57.17200  19.26100  1.000 49.82053  ?  19   ARG   A C   1 
ATOM   145   O  O   . ARG   A 1 19   ? -74.12200  56.45600  19.00200  1.000 68.75646  ?  19   ARG   A O   1 
ATOM   146   C  CB  . ARG   A 1 19   ? -72.52700  58.96400  17.61600  1.000 49.90779  ?  19   ARG   A CB  1 
ATOM   147   C  CG  . ARG   A 1 19   ? -72.73600  60.39200  17.14900  1.000 46.61016  ?  19   ARG   A CG  1 
ATOM   148   C  CD  . ARG   A 1 19   ? -72.37500  60.54900  15.68500  1.000 45.31213  ?  19   ARG   A CD  1 
ATOM   149   N  NE  . ARG   A 1 19   ? -70.97800  60.21900  15.43800  1.000 53.06851  ?  19   ARG   A NE  1 
ATOM   150   C  CZ  . ARG   A 1 19   ? -70.04200  61.11300  15.15200  1.000 58.97051  ?  19   ARG   A CZ  1 
ATOM   151   N  NH1 . ARG   A 1 19   ? -70.32400  62.40200  15.05700  1.000 59.42862  ?  19   ARG   A NH1 1 
ATOM   152   N  NH2 . ARG   A 1 19   ? -68.79100  60.70500  14.96100  1.000 50.79581  ?  19   ARG   A NH2 1 
ATOM   153   N  N   . TYR   A 1 20   ? -72.03200  56.68100  19.80400  1.000 43.82840  ?  20   TYR   A N   1 
ATOM   154   C  CA  . TYR   A 1 20   ? -71.96800  55.27600  20.19100  1.000 50.64695  ?  20   TYR   A CA  1 
ATOM   155   C  C   . TYR   A 1 20   ? -72.97800  54.96900  21.28800  1.000 54.21804  ?  20   TYR   A C   1 
ATOM   156   O  O   . TYR   A 1 20   ? -73.59800  53.89900  21.29200  1.000 49.66075  ?  20   TYR   A O   1 
ATOM   157   C  CB  . TYR   A 1 20   ? -70.55400  54.91500  20.64500  1.000 37.34520  ?  20   TYR   A CB  1 
ATOM   158   C  CG  . TYR   A 1 20   ? -70.44800  53.57100  21.33000  1.000 43.23814  ?  20   TYR   A CG  1 
ATOM   159   C  CD1 . TYR   A 1 20   ? -70.55800  52.38800  20.60900  1.000 46.61028  ?  20   TYR   A CD1 1 
ATOM   160   C  CD2 . TYR   A 1 20   ? -70.23500  53.48400  22.70100  1.000 49.06999  ?  20   TYR   A CD2 1 
ATOM   161   C  CE1 . TYR   A 1 20   ? -70.45900  51.15400  21.23500  1.000 52.09857  ?  20   TYR   A CE1 1 
ATOM   162   C  CE2 . TYR   A 1 20   ? -70.13500  52.25500  23.33600  1.000 51.87074  ?  20   TYR   A CE2 1 
ATOM   163   C  CZ  . TYR   A 1 20   ? -70.24600  51.09400  22.59800  1.000 57.41436  ?  20   TYR   A CZ  1 
ATOM   164   O  OH  . TYR   A 1 20   ? -70.14800  49.87000  23.22400  1.000 62.21146  ?  20   TYR   A OH  1 
ATOM   165   N  N   . LEU   A 1 21   ? -73.16000  55.90200  22.22700  1.000 51.22869  ?  21   LEU   A N   1 
ATOM   166   C  CA  . LEU   A 1 21   ? -74.18100  55.72700  23.25400  1.000 48.24428  ?  21   LEU   A CA  1 
ATOM   167   C  C   . LEU   A 1 21   ? -75.57300  55.69400  22.64000  1.000 63.32123  ?  21   LEU   A C   1 
ATOM   168   O  O   . LEU   A 1 21   ? -76.42900  54.90800  23.06400  1.000 65.35587  ?  21   LEU   A O   1 
ATOM   169   C  CB  . LEU   A 1 21   ? -74.07900  56.84400  24.29300  1.000 37.73349  ?  21   LEU   A CB  1 
ATOM   170   C  CG  . LEU   A 1 21   ? -72.83700  56.82200  25.18700  1.000 45.85523  ?  21   LEU   A CG  1 
ATOM   171   C  CD1 . LEU   A 1 21   ? -72.78900  58.05500  26.07500  1.000 38.27869  ?  21   LEU   A CD1 1 
ATOM   172   C  CD2 . LEU   A 1 21   ? -72.80900  55.55300  26.02600  1.000 34.39673  ?  21   LEU   A CD2 1 
ATOM   173   N  N   . GLU   A 1 22   ? -75.81400  56.53500  21.63200  1.000 52.98763  ?  22   GLU   A N   1 
ATOM   174   C  CA  . GLU   A 1 22   ? -77.12600  56.57000  20.99700  1.000 49.34930  ?  22   GLU   A CA  1 
ATOM   175   C  C   . GLU   A 1 22   ? -77.37400  55.33000  20.14600  1.000 58.73929  ?  22   GLU   A C   1 
ATOM   176   O  O   . GLU   A 1 22   ? -78.53100  54.94800  19.93500  1.000 59.58471  ?  22   GLU   A O   1 
ATOM   177   C  CB  . GLU   A 1 22   ? -77.26400  57.84100  20.15900  1.000 41.13201  ?  22   GLU   A CB  1 
ATOM   178   C  CG  . GLU   A 1 22   ? -77.51300  59.09300  20.99200  1.000 52.09374  ?  22   GLU   A CG  1 
ATOM   179   C  CD  . GLU   A 1 22   ? -77.38800  60.37600  20.18900  1.000 65.10379  ?  22   GLU   A CD  1 
ATOM   180   O  OE1 . GLU   A 1 22   ? -77.04300  60.30200  18.99000  1.000 52.88128  ?  22   GLU   A OE1 1 
ATOM   181   O  OE2 . GLU   A 1 22   ? -77.63200  61.46000  20.76000  1.000 65.43844  -1 22   GLU   A OE2 1 
ATOM   182   N  N   . SER   A 1 23   ? -76.30800  54.68600  19.65600  1.000 43.08839  ?  23   SER   A N   1 
ATOM   183   C  CA  . SER   A 1 23   ? -76.48000  53.45200  18.89400  1.000 48.37249  ?  23   SER   A CA  1 
ATOM   184   C  C   . SER   A 1 23   ? -76.89100  52.30000  19.80100  1.000 46.12677  ?  23   SER   A C   1 
ATOM   185   O  O   . SER   A 1 23   ? -77.77700  51.51300  19.45000  1.000 57.82977  ?  23   SER   A O   1 
ATOM   186   C  CB  . SER   A 1 23   ? -75.19600  53.10700  18.14100  1.000 40.60315  ?  23   SER   A CB  1 
ATOM   187   O  OG  . SER   A 1 23   ? -74.19000  52.64000  19.02100  1.000 58.50554  ?  23   SER   A OG  1 
ATOM   188   N  N   . LEU   A 1 24   ? -76.26700  52.19000  20.97600  1.000 56.28543  ?  24   LEU   A N   1 
ATOM   189   C  CA  . LEU   A 1 24   ? -76.70600  51.24100  21.99300  1.000 57.60918  ?  24   LEU   A CA  1 
ATOM   190   C  C   . LEU   A 1 24   ? -78.08100  51.58000  22.55100  1.000 54.14690  ?  24   LEU   A C   1 
ATOM   191   O  O   . LEU   A 1 24   ? -78.52900  50.92200  23.49700  1.000 62.72389  ?  24   LEU   A O   1 
ATOM   192   C  CB  . LEU   A 1 24   ? -75.68300  51.17900  23.12900  1.000 48.93578  ?  24   LEU   A CB  1 
ATOM   193   C  CG  . LEU   A 1 24   ? -74.23900  50.89800  22.71300  1.000 49.55058  ?  24   LEU   A CG  1 
ATOM   194   C  CD1 . LEU   A 1 24   ? -73.37300  50.64400  23.93300  1.000 59.23040  ?  24   LEU   A CD1 1 
ATOM   195   C  CD2 . LEU   A 1 24   ? -74.17000  49.71900  21.75200  1.000 64.87671  ?  24   LEU   A CD2 1 
ATOM   196   N  N   . HIS   A 1 25   ? -78.73400  52.60300  21.99300  1.000 52.26684  ?  25   HIS   A N   1 
ATOM   197   C  CA  . HIS   A 1 25   ? -80.10300  52.98800  22.32900  1.000 56.48514  ?  25   HIS   A CA  1 
ATOM   198   C  C   . HIS   A 1 25   ? -80.18000  53.56200  23.74400  1.000 56.69092  ?  25   HIS   A C   1 
ATOM   199   O  O   . HIS   A 1 25   ? -81.05800  53.22200  24.53500  1.000 67.08349  ?  25   HIS   A O   1 
ATOM   200   C  CB  . HIS   A 1 25   ? -81.07100  51.81700  22.13100  1.000 52.75289  ?  25   HIS   A CB  1 
ATOM   201   C  CG  . HIS   A 1 25   ? -81.35400  51.51500  20.69000  1.000 49.13113  ?  25   HIS   A CG  1 
ATOM   202   N  ND1 . HIS   A 1 25   ? -81.72700  52.48700  19.78700  1.000 61.32476  ?  25   HIS   A ND1 1 
ATOM   203   C  CD2 . HIS   A 1 25   ? -81.30200  50.35500  19.99300  1.000 45.89608  ?  25   HIS   A CD2 1 
ATOM   204   C  CE1 . HIS   A 1 25   ? -81.90000  51.93800  18.59800  1.000 65.72419  ?  25   HIS   A CE1 1 
ATOM   205   N  NE2 . HIS   A 1 25   ? -81.65000  50.64500  18.69600  1.000 58.52136  ?  25   HIS   A NE2 1 
ATOM   206   N  N   . HIS   A 1 26   ? -79.24600  54.45000  24.05200  1.000 53.66818  ?  26   HIS   A N   1 
ATOM   207   C  CA  . HIS   A 1 26   ? -79.32700  55.28300  25.23800  1.000 58.07496  ?  26   HIS   A CA  1 
ATOM   208   C  C   . HIS   A 1 26   ? -79.88800  56.64300  24.84500  1.000 49.59402  ?  26   HIS   A C   1 
ATOM   209   O  O   . HIS   A 1 26   ? -79.72700  57.09500  23.70900  1.000 60.70986  ?  26   HIS   A O   1 
ATOM   210   C  CB  . HIS   A 1 26   ? -77.95200  55.45000  25.88800  1.000 61.28085  ?  26   HIS   A CB  1 
ATOM   211   C  CG  . HIS   A 1 26   ? -77.43000  54.20500  26.53900  1.000 59.53359  ?  26   HIS   A CG  1 
ATOM   212   N  ND1 . HIS   A 1 26   ? -77.80100  53.81600  27.80900  1.000 61.74961  ?  26   HIS   A ND1 1 
ATOM   213   C  CD2 . HIS   A 1 26   ? -76.56300  53.26400  26.09500  1.000 56.08419  ?  26   HIS   A CD2 1 
ATOM   214   C  CE1 . HIS   A 1 26   ? -77.18600  52.68800  28.11800  1.000 75.25293  ?  26   HIS   A CE1 1 
ATOM   215   N  NE2 . HIS   A 1 26   ? -76.42900  52.33100  27.09500  1.000 54.70130  ?  26   HIS   A NE2 1 
ATOM   216   N  N   . GLU   A 1 27   ? -80.56800  57.28700  25.78600  1.000 51.87036  ?  27   GLU   A N   1 
ATOM   217   C  CA  . GLU   A 1 27   ? -80.98600  58.67100  25.60700  1.000 55.31775  ?  27   GLU   A CA  1 
ATOM   218   C  C   . GLU   A 1 27   ? -79.92600  59.56800  26.23300  1.000 66.02136  ?  27   GLU   A C   1 
ATOM   219   O  O   . GLU   A 1 27   ? -79.78700  59.61500  27.46000  1.000 67.20044  ?  27   GLU   A O   1 
ATOM   220   C  CB  . GLU   A 1 27   ? -82.35300  58.92200  26.23100  1.000 61.27106  ?  27   GLU   A CB  1 
ATOM   221   C  CG  . GLU   A 1 27   ? -82.67400  60.39200  26.34600  1.000 78.52200  ?  27   GLU   A CG  1 
ATOM   222   C  CD  . GLU   A 1 27   ? -83.94900  60.64000  27.10000  1.000 77.29431  ?  27   GLU   A CD  1 
ATOM   223   O  OE1 . GLU   A 1 27   ? -84.64500  59.65700  27.42900  1.000 67.07255  ?  27   GLU   A OE1 1 
ATOM   224   O  OE2 . GLU   A 1 27   ? -84.26800  61.82000  27.35500  1.000 87.02013  -1 27   GLU   A OE2 1 
ATOM   225   N  N   . VAL   A 1 28   ? -79.17800  60.27500  25.39500  1.000 60.12536  ?  28   VAL   A N   1 
ATOM   226   C  CA  . VAL   A 1 28   ? -78.05900  61.09300  25.84300  1.000 56.29435  ?  28   VAL   A CA  1 
ATOM   227   C  C   . VAL   A 1 28   ? -78.53800  62.53400  25.95700  1.000 54.44915  ?  28   VAL   A C   1 
ATOM   228   O  O   . VAL   A 1 28   ? -78.79700  63.19700  24.94700  1.000 51.29910  ?  28   VAL   A O   1 
ATOM   229   C  CB  . VAL   A 1 28   ? -76.86100  60.97300  24.89400  1.000 46.92125  ?  28   VAL   A CB  1 
ATOM   230   C  CG1 . VAL   A 1 28   ? -75.64700  61.67800  25.48200  1.000 52.47881  ?  28   VAL   A CG1 1 
ATOM   231   C  CG2 . VAL   A 1 28   ? -76.56000  59.50700  24.62100  1.000 52.32666  ?  28   VAL   A CG2 1 
ATOM   232   N  N   . VAL   A 1 29   ? -78.66300  63.01600  27.18900  1.000 54.68785  ?  29   VAL   A N   1 
ATOM   233   C  CA  . VAL   A 1 29   ? -78.95200  64.42000  27.45500  1.000 57.21119  ?  29   VAL   A CA  1 
ATOM   234   C  C   . VAL   A 1 29   ? -77.62400  65.14100  27.63900  1.000 64.95587  ?  29   VAL   A C   1 
ATOM   235   O  O   . VAL   A 1 29   ? -76.81900  64.76600  28.49900  1.000 55.13167  ?  29   VAL   A O   1 
ATOM   236   C  CB  . VAL   A 1 29   ? -79.84600  64.58200  28.69300  1.000 51.10519  ?  29   VAL   A CB  1 
ATOM   237   C  CG1 . VAL   A 1 29   ? -80.42400  65.98500  28.74400  1.000 54.21420  ?  29   VAL   A CG1 1 
ATOM   238   C  CG2 . VAL   A 1 29   ? -80.95300  63.54200  28.68400  1.000 61.85115  ?  29   VAL   A CG2 1 
ATOM   239   N  N   . ILE   A 1 30   ? -77.38900  66.17100  26.83200  1.000 64.96882  ?  30   ILE   A N   1 
ATOM   240   C  CA  . ILE   A 1 30   ? -76.10300  66.85400  26.78000  1.000 54.12889  ?  30   ILE   A CA  1 
ATOM   241   C  C   . ILE   A 1 30   ? -76.24900  68.22900  27.41600  1.000 49.38651  ?  30   ILE   A C   1 
ATOM   242   O  O   . ILE   A 1 30   ? -77.13100  69.00800  27.03400  1.000 62.13101  ?  30   ILE   A O   1 
ATOM   243   C  CB  . ILE   A 1 30   ? -75.58300  66.96000  25.33600  1.000 52.09112  ?  30   ILE   A CB  1 
ATOM   244   C  CG1 . ILE   A 1 30   ? -75.56600  65.57300  24.68500  1.000 47.86214  ?  30   ILE   A CG1 1 
ATOM   245   C  CG2 . ILE   A 1 30   ? -74.19500  67.58700  25.31200  1.000 57.89032  ?  30   ILE   A CG2 1 
ATOM   246   C  CD1 . ILE   A 1 30   ? -75.73600  65.59200  23.18400  1.000 52.40290  ?  30   ILE   A CD1 1 
ATOM   247   N  N   . CYS   A 1 31   ? -75.38900  68.51900  28.38800  1.000 57.70597  ?  31   CYS   A N   1 
ATOM   248   C  CA  . CYS   A 1 31   ? -75.35200  69.81800  29.04700  1.000 62.19072  ?  31   CYS   A CA  1 
ATOM   249   C  C   . CYS   A 1 31   ? -73.92400  70.33600  28.98800  1.000 59.11331  ?  31   CYS   A C   1 
ATOM   250   O  O   . CYS   A 1 31   ? -72.99700  69.66300  29.45100  1.000 50.61343  ?  31   CYS   A O   1 
ATOM   251   C  CB  . CYS   A 1 31   ? -75.83900  69.72100  30.49600  1.000 59.39509  ?  31   CYS   A CB  1 
ATOM   252   S  SG  . CYS   A 1 31   ? -76.51900  71.26200  31.15400  1.000 100.32845 ?  31   CYS   A SG  1 
ATOM   253   N  N   . GLN   A 1 32   ? -73.74900  71.52300  28.41100  1.000 59.14068  ?  32   GLN   A N   1 
ATOM   254   C  CA  . GLN   A 1 32   ? -72.43700  72.13000  28.24500  1.000 63.75600  ?  32   GLN   A CA  1 
ATOM   255   C  C   . GLN   A 1 32   ? -72.14300  73.21300  29.27200  1.000 79.38602  ?  32   GLN   A C   1 
ATOM   256   O  O   . GLN   A 1 32   ? -71.05400  73.79600  29.24400  1.000 69.21698  ?  32   GLN   A O   1 
ATOM   257   C  CB  . GLN   A 1 32   ? -72.30600  72.71400  26.83700  1.000 52.02204  ?  32   GLN   A CB  1 
ATOM   258   C  CG  . GLN   A 1 32   ? -72.41000  71.68400  25.73300  1.000 55.72346  ?  32   GLN   A CG  1 
ATOM   259   C  CD  . GLN   A 1 32   ? -71.60600  72.07300  24.51500  1.000 59.38924  ?  32   GLN   A CD  1 
ATOM   260   O  OE1 . GLN   A 1 32   ? -71.98900  72.97600  23.77000  1.000 54.18101  ?  32   GLN   A OE1 1 
ATOM   261   N  NE2 . GLN   A 1 32   ? -70.47700  71.40200  24.30800  1.000 69.61240  ?  32   GLN   A NE2 1 
ATOM   262   N  N   . GLU   A 1 33   ? -73.07200  73.49100  30.17400  1.000 74.50387  ?  33   GLU   A N   1 
ATOM   263   C  CA  . GLU   A 1 33   ? -72.93600  74.57000  31.13800  1.000 75.60410  ?  33   GLU   A CA  1 
ATOM   264   C  C   . GLU   A 1 33   ? -72.87100  73.99500  32.54800  1.000 84.57868  ?  33   GLU   A C   1 
ATOM   265   O  O   . GLU   A 1 33   ? -72.94500  72.78100  32.75400  1.000 89.32468  ?  33   GLU   A O   1 
ATOM   266   C  CB  . GLU   A 1 33   ? -74.09200  75.56400  30.99800  1.000 89.90268  ?  33   GLU   A CB  1 
ATOM   267   C  CG  . GLU   A 1 33   ? -74.47300  75.86600  29.55400  1.000 87.63145  ?  33   GLU   A CG  1 
ATOM   268   C  CD  . GLU   A 1 33   ? -73.53600  76.86400  28.89400  1.000 101.86279 ?  33   GLU   A CD  1 
ATOM   269   O  OE1 . GLU   A 1 33   ? -72.35700  76.52000  28.66200  1.000 98.54223  ?  33   GLU   A OE1 1 
ATOM   270   O  OE2 . GLU   A 1 33   ? -73.98100  77.99500  28.60400  1.000 97.12633  -1 33   GLU   A OE2 1 
ATOM   271   N  N   . LYS   A 1 34   ? -72.73000  74.89700  33.51800  1.000 82.89649  ?  34   LYS   A N   1 
ATOM   272   C  CA  . LYS   A 1 34   ? -72.67500  74.46600  34.93100  1.000 72.95147  ?  34   LYS   A CA  1 
ATOM   273   C  C   . LYS   A 1 34   ? -74.03400  73.89000  35.32000  1.000 75.02283  ?  34   LYS   A C   1 
ATOM   274   O  O   . LYS   A 1 34   ? -75.05400  74.55100  35.06200  1.000 72.07549  ?  34   LYS   A O   1 
ATOM   275   C  CB  . LYS   A 1 34   ? -72.32500  75.67000  35.80600  1.000 75.84728  ?  34   LYS   A CB  1 
ATOM   276   N  N   . VAL   A 1 35   ? -74.03200  72.69600  35.90500  1.000 78.52517  ?  35   VAL   A N   1 
ATOM   277   C  CA  . VAL   A 1 35   ? -75.30100  72.05200  36.34200  1.000 94.64806  ?  35   VAL   A CA  1 
ATOM   278   C  C   . VAL   A 1 35   ? -75.48700  72.34900  37.83600  1.000 96.42255  ?  35   VAL   A C   1 
ATOM   279   O  O   . VAL   A 1 35   ? -74.47400  72.41600  38.55800  1.000 85.41255  ?  35   VAL   A O   1 
ATOM   280   C  CB  . VAL   A 1 35   ? -75.27300  70.54200  36.04700  1.000 78.51996  ?  35   VAL   A CB  1 
ATOM   281   C  CG1 . VAL   A 1 35   ? -76.57800  69.85400  36.42700  1.000 88.63481  ?  35   VAL   A CG1 1 
ATOM   282   C  CG2 . VAL   A 1 35   ? -74.93400  70.26700  34.59000  1.000 72.67481  ?  35   VAL   A CG2 1 
ATOM   283   N  N   . HIS   A 1 36   ? -76.73300  72.54900  38.26300  1.000 101.70255 ?  36   HIS   A N   1 
ATOM   284   C  CA  . HIS   A 1 36   ? -77.01900  72.84800  39.69000  1.000 111.74255 ?  36   HIS   A CA  1 
ATOM   285   C  C   . HIS   A 1 36   ? -77.44500  71.55200  40.38300  1.000 109.54136 ?  36   HIS   A C   1 
ATOM   286   O  O   . HIS   A 1 36   ? -77.96500  70.65100  39.69700  1.000 113.79395 ?  36   HIS   A O   1 
ATOM   287   C  CB  . HIS   A 1 36   ? -78.04700  73.98000  39.78800  1.000 111.65187 ?  36   HIS   A CB  1 
ATOM   288   C  CG  . HIS   A 1 36   ? -77.86200  75.00900  38.72700  1.000 118.29236 ?  36   HIS   A CG  1 
ATOM   289   N  ND1 . HIS   A 1 36   ? -76.80000  75.88700  38.73000  1.000 119.54077 ?  36   HIS   A ND1 1 
ATOM   290   C  CD2 . HIS   A 1 36   ? -78.57500  75.29500  37.63100  1.000 117.92992 ?  36   HIS   A CD2 1 
ATOM   291   C  CE1 . HIS   A 1 36   ? -76.88500  76.67900  37.67200  1.000 107.95780 ?  36   HIS   A CE1 1 
ATOM   292   N  NE2 . HIS   A 1 36   ? -77.95600  76.33600  36.99000  1.000 120.01844 ?  36   HIS   A NE2 1 
ATOM   293   N  N   . ALA   A 1 37   ? -77.26400  71.47400  41.70100  1.000 108.01190 ?  37   ALA   A N   1 
ATOM   294   C  CA  . ALA   A 1 37   ? -77.55400  70.22300  42.44400  1.000 109.65420 ?  37   ALA   A CA  1 
ATOM   295   C  C   . ALA   A 1 37   ? -78.99700  69.75800  42.25300  1.000 112.77255 ?  37   ALA   A C   1 
ATOM   296   O  O   . ALA   A 1 37   ? -79.24300  68.54200  42.36100  1.000 105.62255 ?  37   ALA   A O   1 
ATOM   297   C  CB  . ALA   A 1 37   ? -77.26100  70.44100  43.90500  1.000 111.79917 ?  37   ALA   A CB  1 
ATOM   298   N  N   . GLN   A 1 38   ? -79.92800  70.68000  42.02000  1.000 113.37255 ?  38   GLN   A N   1 
ATOM   299   C  CA  . GLN   A 1 38   ? -81.35400  70.27900  41.93600  1.000 111.18255 ?  38   GLN   A CA  1 
ATOM   300   C  C   . GLN   A 1 38   ? -81.94300  70.78400  40.61600  1.000 112.55255 ?  38   GLN   A C   1 
ATOM   301   O  O   . GLN   A 1 38   ? -83.02900  71.40000  40.64500  1.000 102.27255 ?  38   GLN   A O   1 
ATOM   302   C  CB  . GLN   A 1 38   ? -82.11000  70.81000  43.15200  1.000 111.65948 ?  38   GLN   A CB  1 
ATOM   303   C  CG  . GLN   A 1 38   ? -82.54300  69.72500  44.13000  1.000 108.18139 ?  38   GLN   A CG  1 
ATOM   304   C  CD  . GLN   A 1 38   ? -81.39600  69.15100  44.93300  1.000 120.76963 ?  38   GLN   A CD  1 
ATOM   305   O  OE1 . GLN   A 1 38   ? -80.49000  69.86900  45.36700  1.000 109.07131 ?  38   GLN   A OE1 1 
ATOM   306   N  NE2 . GLN   A 1 38   ? -81.42800  67.84300  45.13800  1.000 118.56203 ?  38   GLN   A NE2 1 
ATOM   307   N  N   . SER   A 1 39   ? -81.25000  70.52600  39.50800  1.000 110.93032 ?  39   SER   A N   1 
ATOM   308   C  CA  . SER   A 1 39   ? -81.76700  70.92200  38.20900  1.000 99.00139  ?  39   SER   A CA  1 
ATOM   309   C  C   . SER   A 1 39   ? -82.64700  69.82400  37.62000  1.000 100.59873 ?  39   SER   A C   1 
ATOM   310   O  O   . SER   A 1 39   ? -82.77400  68.72600  38.16700  1.000 100.70458 ?  39   SER   A O   1 
ATOM   311   C  CB  . SER   A 1 39   ? -80.62400  71.24500  37.24700  1.000 95.28816  ?  39   SER   A CB  1 
ATOM   312   O  OG  . SER   A 1 39   ? -79.71300  72.16100  37.82100  1.000 95.94255  ?  39   SER   A OG  1 
ATOM   313   N  N   . ALA   A 1 40   ? -83.26000  70.13700  36.47600  1.000 100.32049 ?  40   ALA   A N   1 
ATOM   314   C  CA  . ALA   A 1 40   ? -84.05500  69.15000  35.75800  1.000 88.92664  ?  40   ALA   A CA  1 
ATOM   315   C  C   . ALA   A 1 40   ? -83.18000  68.16100  35.00300  1.000 94.33043  ?  40   ALA   A C   1 
ATOM   316   O  O   . ALA   A 1 40   ? -83.56400  66.99700  34.83900  1.000 93.00907  ?  40   ALA   A O   1 
ATOM   317   C  CB  . ALA   A 1 40   ? -85.01400  69.84400  34.79100  1.000 80.14416  ?  40   ALA   A CB  1 
ATOM   318   N  N   . ASN   A 1 41   ? -82.00700  68.60200  34.54200  1.000 101.69071 ?  41   ASN   A N   1 
ATOM   319   C  CA  . ASN   A 1 41   ? -81.07200  67.71000  33.87000  1.000 99.99786  ?  41   ASN   A CA  1 
ATOM   320   C  C   . ASN   A 1 41   ? -80.56000  66.60500  34.78200  1.000 102.59293 ?  41   ASN   A C   1 
ATOM   321   O  O   . ASN   A 1 41   ? -79.93500  65.66000  34.29000  1.000 97.84112  ?  41   ASN   A O   1 
ATOM   322   C  CB  . ASN   A 1 41   ? -79.88300  68.50300  33.32100  1.000 97.59039  ?  41   ASN   A CB  1 
ATOM   323   C  CG  . ASN   A 1 41   ? -80.29400  69.83400  32.72200  1.000 104.29155 ?  41   ASN   A CG  1 
ATOM   324   O  OD1 . ASN   A 1 41   ? -80.93300  69.88600  31.67100  1.000 108.57652 ?  41   ASN   A OD1 1 
ATOM   325   N  ND2 . ASN   A 1 41   ? -79.92800  70.92000  33.39200  1.000 101.24755 ?  41   ASN   A ND2 1 
ATOM   326   N  N   . LEU   A 1 42   ? -80.80600  66.70000  36.08700  1.000 99.87411  ?  42   LEU   A N   1 
ATOM   327   C  CA  . LEU   A 1 42   ? -80.33500  65.71300  37.04200  1.000 86.75447  ?  42   LEU   A CA  1 
ATOM   328   C  C   . LEU   A 1 42   ? -81.39700  64.67400  37.37900  1.000 94.96550  ?  42   LEU   A C   1 
ATOM   329   O  O   . LEU   A 1 42   ? -81.06800  63.63400  37.96200  1.000 87.96158  ?  42   LEU   A O   1 
ATOM   330   C  CB  . LEU   A 1 42   ? -79.87500  66.41300  38.32600  1.000 91.53647  ?  42   LEU   A CB  1 
ATOM   331   C  CG  . LEU   A 1 42   ? -78.36200  66.41800  38.54500  1.000 74.81466  ?  42   LEU   A CG  1 
ATOM   332   C  CD1 . LEU   A 1 42   ? -77.96300  67.26400  39.73600  1.000 87.47591  ?  42   LEU   A CD1 1 
ATOM   333   C  CD2 . LEU   A 1 42   ? -77.83000  65.02500  38.66000  1.000 76.50892  ?  42   LEU   A CD2 1 
ATOM   334   N  N   . GLN   A 1 43   ? -82.65500  64.93000  37.02400  1.000 92.74406  ?  43   GLN   A N   1 
ATOM   335   C  CA  . GLN   A 1 43   ? -83.74100  64.01100  37.33200  1.000 90.64163  ?  43   GLN   A CA  1 
ATOM   336   C  C   . GLN   A 1 43   ? -83.79100  62.87500  36.32000  1.000 78.59983  ?  43   GLN   A C   1 
ATOM   337   O  O   . GLN   A 1 43   ? -83.55400  63.07700  35.12600  1.000 86.05224  ?  43   GLN   A O   1 
ATOM   338   C  CB  . GLN   A 1 43   ? -85.07900  64.75100  37.34200  1.000 97.03145  ?  43   GLN   A CB  1 
ATOM   339   C  CG  . GLN   A 1 43   ? -85.03800  66.11300  38.01800  1.000 104.68246 ?  43   GLN   A CG  1 
ATOM   340   C  CD  . GLN   A 1 43   ? -86.32900  66.89200  37.83700  1.000 116.46891 ?  43   GLN   A CD  1 
ATOM   341   O  OE1 . GLN   A 1 43   ? -87.34600  66.34100  37.41600  1.000 107.26386 ?  43   GLN   A OE1 1 
ATOM   342   N  NE2 . GLN   A 1 43   ? -86.29100  68.18400  38.15000  1.000 106.05557 ?  43   GLN   A NE2 1 
ATOM   343   N  N   . GLU   A 1 44   ? -84.11500  61.67500  36.81100  1.000 74.62638  ?  44   GLU   A N   1 
ATOM   344   C  CA  . GLU   A 1 44   ? -84.30600  60.48900  35.97100  1.000 79.83798  ?  44   GLU   A CA  1 
ATOM   345   C  C   . GLU   A 1 44   ? -83.06000  60.16800  35.15000  1.000 76.53987  ?  44   GLU   A C   1 
ATOM   346   O  O   . GLU   A 1 44   ? -83.14800  59.72800  34.00200  1.000 73.05899  ?  44   GLU   A O   1 
ATOM   347   C  CB  . GLU   A 1 44   ? -85.52400  60.64100  35.05400  1.000 104.27742 ?  44   GLU   A CB  1 
ATOM   348   C  CG  . GLU   A 1 44   ? -86.69400  61.40600  35.65600  1.000 105.33797 ?  44   GLU   A CG  1 
ATOM   349   C  CD  . GLU   A 1 44   ? -87.41300  60.64000  36.74900  1.000 106.42904 ?  44   GLU   A CD  1 
ATOM   350   O  OE1 . GLU   A 1 44   ? -87.02700  59.48900  37.04400  1.000 117.90591 ?  44   GLU   A OE1 1 
ATOM   351   O  OE2 . GLU   A 1 44   ? -88.37200  61.19700  37.31600  1.000 105.70459 ?  44   GLU   A OE2 1 
ATOM   352   N  N   . ILE   A 1 45   ? -81.88800  60.39100  35.73700  1.000 75.99601  ?  45   ILE   A N   1 
ATOM   353   C  CA  . ILE   A 1 45   ? -80.61100  60.11600  35.08900  1.000 62.61120  ?  45   ILE   A CA  1 
ATOM   354   C  C   . ILE   A 1 45   ? -79.98900  58.90000  35.75700  1.000 55.12540  ?  45   ILE   A C   1 
ATOM   355   O  O   . ILE   A 1 45   ? -79.92200  58.82800  36.99000  1.000 73.95142  ?  45   ILE   A O   1 
ATOM   356   C  CB  . ILE   A 1 45   ? -79.66900  61.32900  35.15800  1.000 64.83692  ?  45   ILE   A CB  1 
ATOM   357   C  CG1 . ILE   A 1 45   ? -80.30400  62.53000  34.45800  1.000 72.01715  ?  45   ILE   A CG1 1 
ATOM   358   C  CG2 . ILE   A 1 45   ? -78.33200  60.99800  34.52300  1.000 75.35385  ?  45   ILE   A CG2 1 
ATOM   359   C  CD1 . ILE   A 1 45   ? -80.73400  62.25000  33.03200  1.000 75.30605  ?  45   ILE   A CD1 1 
ATOM   360   N  N   . ASP   A 1 46   ? -79.53600  57.94600  34.94400  1.000 58.47552  ?  46   ASP   A N   1 
ATOM   361   C  CA  . ASP   A 1 46   ? -78.96400  56.71000  35.45900  1.000 66.83013  ?  46   ASP   A CA  1 
ATOM   362   C  C   . ASP   A 1 46   ? -77.44500  56.66700  35.38300  1.000 71.04358  ?  46   ASP   A C   1 
ATOM   363   O  O   . ASP   A 1 46   ? -76.82300  55.92800  36.15400  1.000 82.84303  ?  46   ASP   A O   1 
ATOM   364   C  CB  . ASP   A 1 46   ? -79.54200  55.50800  34.70300  1.000 72.80602  ?  46   ASP   A CB  1 
ATOM   365   C  CG  . ASP   A 1 46   ? -81.05600  55.53200  34.64700  1.000 79.89585  ?  46   ASP   A CG  1 
ATOM   366   O  OD1 . ASP   A 1 46   ? -81.69000  55.73400  35.70500  1.000 80.31555  ?  46   ASP   A OD1 1 
ATOM   367   O  OD2 . ASP   A 1 46   ? -81.61100  55.35400  33.54200  1.000 81.34409  -1 46   ASP   A OD2 1 
ATOM   368   N  N   . TRP   A 1 47   ? -76.83600  57.43300  34.48000  1.000 74.67848  ?  47   TRP   A N   1 
ATOM   369   C  CA  . TRP   A 1 47   ? -75.38600  57.49300  34.37100  1.000 57.36538  ?  47   TRP   A CA  1 
ATOM   370   C  C   . TRP   A 1 47   ? -74.98200  58.90500  33.97800  1.000 56.89413  ?  47   TRP   A C   1 
ATOM   371   O  O   . TRP   A 1 47   ? -75.73500  59.61800  33.31000  1.000 52.73389  ?  47   TRP   A O   1 
ATOM   372   C  CB  . TRP   A 1 47   ? -74.85100  56.48400  33.34600  1.000 54.69734  ?  47   TRP   A CB  1 
ATOM   373   C  CG  . TRP   A 1 47   ? -74.86200  55.06300  33.82400  1.000 60.67325  ?  47   TRP   A CG  1 
ATOM   374   C  CD1 . TRP   A 1 47   ? -75.83600  54.13300  33.60600  1.000 70.22922  ?  47   TRP   A CD1 1 
ATOM   375   C  CD2 . TRP   A 1 47   ? -73.84800  54.40600  34.59700  1.000 65.31336  ?  47   TRP   A CD2 1 
ATOM   376   N  NE1 . TRP   A 1 47   ? -75.49400  52.94000  34.19500  1.000 72.38466  ?  47   TRP   A NE1 1 
ATOM   377   C  CE2 . TRP   A 1 47   ? -74.27700  53.08100  34.81000  1.000 67.33038  ?  47   TRP   A CE2 1 
ATOM   378   C  CE3 . TRP   A 1 47   ? -72.61900  54.81100  35.12900  1.000 72.08654  ?  47   TRP   A CE3 1 
ATOM   379   C  CZ2 . TRP   A 1 47   ? -73.52300  52.15700  35.53200  1.000 65.26471  ?  47   TRP   A CZ2 1 
ATOM   380   C  CZ3 . TRP   A 1 47   ? -71.87000  53.89100  35.84700  1.000 75.79386  ?  47   TRP   A CZ3 1 
ATOM   381   C  CH2 . TRP   A 1 47   ? -72.32600  52.58000  36.04100  1.000 69.20273  ?  47   TRP   A CH2 1 
ATOM   382   N  N   . ILE   A 1 48   ? -73.78500  59.30300  34.40000  1.000 64.95447  ?  48   ILE   A N   1 
ATOM   383   C  CA  . ILE   A 1 48   ? -73.22000  60.60100  34.04900  1.000 54.71633  ?  48   ILE   A CA  1 
ATOM   384   C  C   . ILE   A 1 48   ? -71.85300  60.36700  33.42300  1.000 57.25045  ?  48   ILE   A C   1 
ATOM   385   O  O   . ILE   A 1 48   ? -70.95200  59.82500  34.07300  1.000 57.39914  ?  48   ILE   A O   1 
ATOM   386   C  CB  . ILE   A 1 48   ? -73.09800  61.53300  35.26300  1.000 50.93025  ?  48   ILE   A CB  1 
ATOM   387   C  CG1 . ILE   A 1 48   ? -74.47400  62.06500  35.67000  1.000 65.38377  ?  48   ILE   A CG1 1 
ATOM   388   C  CG2 . ILE   A 1 48   ? -72.16200  62.68200  34.93200  1.000 50.19387  ?  48   ILE   A CG2 1 
ATOM   389   C  CD1 . ILE   A 1 48   ? -74.42900  63.15300  36.73200  1.000 49.37297  ?  48   ILE   A CD1 1 
ATOM   390   N  N   . VAL   A 1 49   ? -71.69700  60.77800  32.16800  1.000 58.92654  ?  49   VAL   A N   1 
ATOM   391   C  CA  . VAL   A 1 49   ? -70.43800  60.66200  31.44400  1.000 48.52749  ?  49   VAL   A CA  1 
ATOM   392   C  C   . VAL   A 1 49   ? -69.91100  62.06300  31.17800  1.000 53.81490  ?  49   VAL   A C   1 
ATOM   393   O  O   . VAL   A 1 49   ? -70.63400  62.91500  30.64700  1.000 46.19684  ?  49   VAL   A O   1 
ATOM   394   C  CB  . VAL   A 1 49   ? -70.61100  59.87900  30.13200  1.000 42.91436  ?  49   VAL   A CB  1 
ATOM   395   C  CG1 . VAL   A 1 49   ? -69.29900  59.82800  29.37600  1.000 35.81723  ?  49   VAL   A CG1 1 
ATOM   396   C  CG2 . VAL   A 1 49   ? -71.11600  58.47500  30.42100  1.000 50.70664  ?  49   VAL   A CG2 1 
ATOM   397   N  N   . SER   A 1 50   ? -68.65700  62.30400  31.55000  1.000 60.38374  ?  50   SER   A N   1 
ATOM   398   C  CA  . SER   A 1 50   ? -68.03000  63.60400  31.37500  1.000 63.78444  ?  50   SER   A CA  1 
ATOM   399   C  C   . SER   A 1 50   ? -66.82500  63.48700  30.45000  1.000 60.12638  ?  50   SER   A C   1 
ATOM   400   O  O   . SER   A 1 50   ? -66.11200  62.47900  30.44900  1.000 58.61806  ?  50   SER   A O   1 
ATOM   401   C  CB  . SER   A 1 50   ? -67.60600  64.20600  32.72100  1.000 48.94155  ?  50   SER   A CB  1 
ATOM   402   O  OG  . SER   A 1 50   ? -67.08200  63.21300  33.58400  1.000 55.27303  ?  50   SER   A OG  1 
ATOM   403   N  N   . TYR   A 1 51   ? -66.61000  64.53700  29.66000  1.000 46.86236  ?  51   TYR   A N   1 
ATOM   404   C  CA  . TYR   A 1 51   ? -65.52700  64.55900  28.68100  1.000 42.35394  ?  51   TYR   A CA  1 
ATOM   405   C  C   . TYR   A 1 51   ? -65.18200  66.02100  28.42500  1.000 48.08570  ?  51   TYR   A C   1 
ATOM   406   O  O   . TYR   A 1 51   ? -65.94800  66.72900  27.76500  1.000 47.46225  ?  51   TYR   A O   1 
ATOM   407   C  CB  . TYR   A 1 51   ? -65.94500  63.84400  27.40000  1.000 38.78968  ?  51   TYR   A CB  1 
ATOM   408   C  CG  . TYR   A 1 51   ? -64.82700  63.58400  26.41100  1.000 49.74940  ?  51   TYR   A CG  1 
ATOM   409   C  CD1 . TYR   A 1 51   ? -63.50200  63.83700  26.73900  1.000 54.79977  ?  51   TYR   A CD1 1 
ATOM   410   C  CD2 . TYR   A 1 51   ? -65.10500  63.09400  25.14100  1.000 50.78768  ?  51   TYR   A CD2 1 
ATOM   411   C  CE1 . TYR   A 1 51   ? -62.48400  63.60500  25.82900  1.000 55.31344  ?  51   TYR   A CE1 1 
ATOM   412   C  CE2 . TYR   A 1 51   ? -64.09600  62.86000  24.22700  1.000 58.38502  ?  51   TYR   A CE2 1 
ATOM   413   C  CZ  . TYR   A 1 51   ? -62.78900  63.11700  24.57500  1.000 54.40594  ?  51   TYR   A CZ  1 
ATOM   414   O  OH  . TYR   A 1 51   ? -61.78500  62.88400  23.66300  1.000 63.83763  ?  51   TYR   A OH  1 
ATOM   415   N  N   . ALA   A 1 52   ? -64.04100  66.46400  28.95500  1.000 37.64909  ?  52   ALA   A N   1 
ATOM   416   C  CA  . ALA   A 1 52   ? -63.60700  67.85700  28.85700  1.000 39.11870  ?  52   ALA   A CA  1 
ATOM   417   C  C   . ALA   A 1 52   ? -64.66200  68.80300  29.42700  1.000 44.83207  ?  52   ALA   A C   1 
ATOM   418   O  O   . ALA   A 1 52   ? -65.05200  69.79000  28.80100  1.000 51.24169  ?  52   ALA   A O   1 
ATOM   419   C  CB  . ALA   A 1 52   ? -63.25500  68.23100  27.41600  1.000 53.65906  ?  52   ALA   A CB  1 
ATOM   420   N  N   . TYR   A 1 53   ? -65.13400  68.48500  30.63000  1.000 55.07107  ?  53   TYR   A N   1 
ATOM   421   C  CA  . TYR   A 1 53   ? -66.04300  69.36700  31.34800  1.000 54.82458  ?  53   TYR   A CA  1 
ATOM   422   C  C   . TYR   A 1 53   ? -65.23000  70.44400  32.05600  1.000 44.05897  ?  53   TYR   A C   1 
ATOM   423   O  O   . TYR   A 1 53   ? -64.32800  70.13200  32.84100  1.000 51.98552  ?  53   TYR   A O   1 
ATOM   424   C  CB  . TYR   A 1 53   ? -66.88800  68.57600  32.34500  1.000 53.15085  ?  53   TYR   A CB  1 
ATOM   425   C  CG  . TYR   A 1 53   ? -68.08100  69.34100  32.88100  1.000 61.41190  ?  53   TYR   A CG  1 
ATOM   426   C  CD1 . TYR   A 1 53   ? -68.97000  69.97400  32.02300  1.000 61.38566  ?  53   TYR   A CD1 1 
ATOM   427   C  CD2 . TYR   A 1 53   ? -68.31500  69.43100  34.24800  1.000 66.59064  ?  53   TYR   A CD2 1 
ATOM   428   C  CE1 . TYR   A 1 53   ? -70.06000  70.67500  32.51000  1.000 69.08190  ?  53   TYR   A CE1 1 
ATOM   429   C  CE2 . TYR   A 1 53   ? -69.40100  70.12800  34.74400  1.000 66.90862  ?  53   TYR   A CE2 1 
ATOM   430   C  CZ  . TYR   A 1 53   ? -70.27000  70.74800  33.87200  1.000 76.84002  ?  53   TYR   A CZ  1 
ATOM   431   O  OH  . TYR   A 1 53   ? -71.35200  71.44300  34.36300  1.000 81.84788  ?  53   TYR   A OH  1 
ATOM   432   N  N   . GLY   A 1 54   ? -65.54400  71.70600  31.77600  1.000 47.96576  ?  54   GLY   A N   1 
ATOM   433   C  CA  . GLY   A 1 54   ? -64.79300  72.82100  32.32300  1.000 59.48932  ?  54   GLY   A CA  1 
ATOM   434   C  C   . GLY   A 1 54   ? -65.42000  73.44300  33.55200  1.000 66.82133  ?  54   GLY   A C   1 
ATOM   435   O  O   . GLY   A 1 54   ? -65.23800  74.63500  33.81900  1.000 75.13421  ?  54   GLY   A O   1 
ATOM   436   N  N   . TYR   A 1 55   ? -66.16600  72.64300  34.30800  1.000 72.77307  ?  55   TYR   A N   1 
ATOM   437   C  CA  . TYR   A 1 55   ? -66.76900  73.08900  35.55200  1.000 55.44104  ?  55   TYR   A CA  1 
ATOM   438   C  C   . TYR   A 1 55   ? -66.62900  71.98100  36.58500  1.000 65.36456  ?  55   TYR   A C   1 
ATOM   439   O  O   . TYR   A 1 55   ? -66.32600  70.83100  36.25600  1.000 52.67333  ?  55   TYR   A O   1 
ATOM   440   C  CB  . TYR   A 1 55   ? -68.24400  73.46400  35.36500  1.000 62.29872  ?  55   TYR   A CB  1 
ATOM   441   C  CG  . TYR   A 1 55   ? -68.49700  74.50300  34.29400  1.000 73.44429  ?  55   TYR   A CG  1 
ATOM   442   C  CD1 . TYR   A 1 55   ? -68.21900  75.84500  34.52100  1.000 75.05372  ?  55   TYR   A CD1 1 
ATOM   443   C  CD2 . TYR   A 1 55   ? -69.02700  74.14400  33.06000  1.000 78.98388  ?  55   TYR   A CD2 1 
ATOM   444   C  CE1 . TYR   A 1 55   ? -68.45600  76.80100  33.54800  1.000 66.97377  ?  55   TYR   A CE1 1 
ATOM   445   C  CE2 . TYR   A 1 55   ? -69.26700  75.09300  32.08100  1.000 79.30276  ?  55   TYR   A CE2 1 
ATOM   446   C  CZ  . TYR   A 1 55   ? -68.98000  76.41900  32.33100  1.000 71.11350  ?  55   TYR   A CZ  1 
ATOM   447   O  OH  . TYR   A 1 55   ? -69.21600  77.36700  31.36300  1.000 78.80739  ?  55   TYR   A OH  1 
ATOM   448   N  N   . ILE   A 1 56   ? -66.84500  72.34000  37.84700  1.000 64.10668  ?  56   ILE   A N   1 
ATOM   449   C  CA  . ILE   A 1 56   ? -66.79300  71.39900  38.95900  1.000 62.90717  ?  56   ILE   A CA  1 
ATOM   450   C  C   . ILE   A 1 56   ? -68.21600  71.14100  39.43100  1.000 64.85670  ?  56   ILE   A C   1 
ATOM   451   O  O   . ILE   A 1 56   ? -68.96800  72.08600  39.70200  1.000 61.74396  ?  56   ILE   A O   1 
ATOM   452   C  CB  . ILE   A 1 56   ? -65.91800  71.92600  40.10900  1.000 63.85193  ?  56   ILE   A CB  1 
ATOM   453   C  CG1 . ILE   A 1 56   ? -64.46100  72.03600  39.65600  1.000 44.21695  ?  56   ILE   A CG1 1 
ATOM   454   C  CG2 . ILE   A 1 56   ? -66.03300  71.01800  41.32800  1.000 46.62617  ?  56   ILE   A CG2 1 
ATOM   455   C  CD1 . ILE   A 1 56   ? -63.68600  70.74300  39.77900  1.000 51.91225  ?  56   ILE   A CD1 1 
ATOM   456   N  N   . LEU   A 1 57   ? -68.58700  69.86600  39.52300  1.000 65.71406  ?  57   LEU   A N   1 
ATOM   457   C  CA  . LEU   A 1 57   ? -69.91900  69.49800  39.97700  1.000 69.38095  ?  57   LEU   A CA  1 
ATOM   458   C  C   . LEU   A 1 57   ? -70.02500  69.62200  41.49100  1.000 85.73804  ?  57   LEU   A C   1 
ATOM   459   O  O   . LEU   A 1 57   ? -69.07000  69.34000  42.22400  1.000 75.61964  ?  57   LEU   A O   1 
ATOM   460   C  CB  . LEU   A 1 57   ? -70.26300  68.07300  39.54600  1.000 59.46206  ?  57   LEU   A CB  1 
ATOM   461   C  CG  . LEU   A 1 57   ? -70.66900  67.90400  38.08300  1.000 63.91921  ?  57   LEU   A CG  1 
ATOM   462   C  CD1 . LEU   A 1 57   ? -70.75300  66.42600  37.73200  1.000 45.94562  ?  57   LEU   A CD1 1 
ATOM   463   C  CD2 . LEU   A 1 57   ? -71.98400  68.62000  37.79700  1.000 70.80122  ?  57   LEU   A CD2 1 
ATOM   464   N  N   . ASP   A 1 58   ? -71.19900  70.04800  41.95200  1.000 87.66325  ?  58   ASP   A N   1 
ATOM   465   C  CA  . ASP   A 1 58   ? -71.43900  70.20600  43.37900  1.000 89.86280  ?  58   ASP   A CA  1 
ATOM   466   C  C   . ASP   A 1 58   ? -71.25100  68.87700  44.10800  1.000 90.63932  ?  58   ASP   A C   1 
ATOM   467   O  O   . ASP   A 1 58   ? -71.46000  67.79700  43.54600  1.000 87.48693  ?  58   ASP   A O   1 
ATOM   468   C  CB  . ASP   A 1 58   ? -72.84600  70.75900  43.62000  1.000 97.52534  ?  58   ASP   A CB  1 
ATOM   469   C  CG  . ASP   A 1 58   ? -72.95300  71.53700  44.92000  1.000 113.88693 ?  58   ASP   A CG  1 
ATOM   470   O  OD1 . ASP   A 1 58   ? -72.11100  71.31700  45.81400  1.000 112.99543 ?  58   ASP   A OD1 1 
ATOM   471   O  OD2 . ASP   A 1 58   ? -73.87000  72.37900  45.03800  1.000 120.63853 -1 58   ASP   A OD2 1 
ATOM   472   N  N   . LYS   A 1 59   ? -70.84400  68.97400  45.37900  1.000 92.39000  ?  59   LYS   A N   1 
ATOM   473   C  CA  . LYS   A 1 59   ? -70.50100  67.78700  46.15900  1.000 96.36443  ?  59   LYS   A CA  1 
ATOM   474   C  C   . LYS   A 1 59   ? -71.70300  66.86900  46.34100  1.000 90.02475  ?  59   LYS   A C   1 
ATOM   475   O  O   . LYS   A 1 59   ? -71.53900  65.65000  46.47600  1.000 78.04532  ?  59   LYS   A O   1 
ATOM   476   C  CB  . LYS   A 1 59   ? -69.91900  68.17400  47.53100  1.000 88.09149  ?  59   LYS   A CB  1 
ATOM   477   C  CG  . LYS   A 1 59   ? -68.58000  68.96500  47.55100  1.000 88.26934  ?  59   LYS   A CG  1 
ATOM   478   C  CD  . LYS   A 1 59   ? -68.59500  70.28000  46.78600  1.000 97.14593  ?  59   LYS   A CD  1 
ATOM   479   C  CE  . LYS   A 1 59   ? -69.56100  71.25200  47.42500  1.000 99.67901  ?  59   LYS   A CE  1 
ATOM   480   N  NZ  . LYS   A 1 59   ? -69.71100  72.48600  46.61400  1.000 94.57316  ?  59   LYS   A NZ  1 
ATOM   481   N  N   . GLU   A 1 60   ? -72.91400  67.43100  46.34700  1.000 79.13720  ?  60   GLU   A N   1 
ATOM   482   C  CA  . GLU   A 1 60   ? -74.11500  66.60800  46.43000  1.000 84.42534  ?  60   GLU   A CA  1 
ATOM   483   C  C   . GLU   A 1 60   ? -74.26300  65.72700  45.19500  1.000 87.36928  ?  60   GLU   A C   1 
ATOM   484   O  O   . GLU   A 1 60   ? -74.60100  64.54200  45.30300  1.000 74.67542  ?  60   GLU   A O   1 
ATOM   485   C  CB  . GLU   A 1 60   ? -75.34300  67.50200  46.60400  1.000 89.13699  ?  60   GLU   A CB  1 
ATOM   486   C  CG  . GLU   A 1 60   ? -75.24000  68.48500  47.76400  1.000 106.37237 ?  60   GLU   A CG  1 
ATOM   487   C  CD  . GLU   A 1 60   ? -75.35100  67.81600  49.12300  1.000 115.59618 ?  60   GLU   A CD  1 
ATOM   488   O  OE1 . GLU   A 1 60   ? -75.72700  66.62500  49.18200  1.000 108.82694 ?  60   GLU   A OE1 1 
ATOM   489   O  OE2 . GLU   A 1 60   ? -75.06300  68.48700  50.13600  1.000 109.63713 -1 60   GLU   A OE2 1 
ATOM   490   N  N   . ILE   A 1 61   ? -74.00500  66.29100  44.01200  1.000 83.77393  ?  61   ILE   A N   1 
ATOM   491   C  CA  . ILE   A 1 61   ? -74.11000  65.52500  42.77300  1.000 66.18340  ?  61   ILE   A CA  1 
ATOM   492   C  C   . ILE   A 1 61   ? -73.11300  64.37500  42.76700  1.000 65.88807  ?  61   ILE   A C   1 
ATOM   493   O  O   . ILE   A 1 61   ? -73.44500  63.24900  42.37600  1.000 68.63827  ?  61   ILE   A O   1 
ATOM   494   C  CB  . ILE   A 1 61   ? -73.90700  66.44900  41.55900  1.000 68.74697  ?  61   ILE   A CB  1 
ATOM   495   C  CG1 . ILE   A 1 61   ? -74.43500  67.85400  41.86600  1.000 77.03145  ?  61   ILE   A CG1 1 
ATOM   496   C  CG2 . ILE   A 1 61   ? -74.57900  65.86100  40.32800  1.000 60.26565  ?  61   ILE   A CG2 1 
ATOM   497   C  CD1 . ILE   A 1 61   ? -74.36600  68.80900  40.69800  1.000 75.42481  ?  61   ILE   A CD1 1 
ATOM   498   N  N   . VAL   A 1 62   ? -71.87700  64.64100  43.19600  1.000 57.80570  ?  62   VAL   A N   1 
ATOM   499   C  CA  . VAL   A 1 62   ? -70.85100  63.60100  43.23700  1.000 59.74121  ?  62   VAL   A CA  1 
ATOM   500   C  C   . VAL   A 1 62   ? -71.28700  62.45200  44.13600  1.000 73.10143  ?  62   VAL   A C   1 
ATOM   501   O  O   . VAL   A 1 62   ? -71.06500  61.27700  43.82100  1.000 69.08740  ?  62   VAL   A O   1 
ATOM   502   C  CB  . VAL   A 1 62   ? -69.50900  64.20000  43.69700  1.000 59.86190  ?  62   VAL   A CB  1 
ATOM   503   C  CG1 . VAL   A 1 62   ? -68.41200  63.14100  43.67500  1.000 53.16095  ?  62   VAL   A CG1 1 
ATOM   504   C  CG2 . VAL   A 1 62   ? -69.13700  65.39500  42.83100  1.000 66.57181  ?  62   VAL   A CG2 1 
ATOM   505   N  N   . SER   A 1 63   ? -71.91800  62.77200  45.26800  1.000 78.12821  ?  63   SER   A N   1 
ATOM   506   C  CA  . SER   A 1 63   ? -72.35900  61.74000  46.20000  1.000 79.42496  ?  63   SER   A CA  1 
ATOM   507   C  C   . SER   A 1 63   ? -73.67600  61.11100  45.76300  1.000 77.02316  ?  63   SER   A C   1 
ATOM   508   O  O   . SER   A 1 63   ? -73.86200  59.89700  45.90200  1.000 81.66510  ?  63   SER   A O   1 
ATOM   509   C  CB  . SER   A 1 63   ? -72.49700  62.32900  47.60300  1.000 96.74409  ?  63   SER   A CB  1 
ATOM   510   O  OG  . SER   A 1 63   ? -73.21000  63.55400  47.56600  1.000 88.73707  ?  63   SER   A OG  1 
ATOM   511   N  N   . ARG   A 1 64   ? -74.60100  61.92300  45.24200  1.000 65.60851  ?  64   ARG   A N   1 
ATOM   512   C  CA  . ARG   A 1 64   ? -75.88500  61.39600  44.79000  1.000 61.33407  ?  64   ARG   A CA  1 
ATOM   513   C  C   . ARG   A 1 64   ? -75.69900  60.39200  43.65900  1.000 65.16642  ?  64   ARG   A C   1 
ATOM   514   O  O   . ARG   A 1 64   ? -76.41800  59.38900  43.58400  1.000 65.81263  ?  64   ARG   A O   1 
ATOM   515   C  CB  . ARG   A 1 64   ? -76.79000  62.55000  44.35500  1.000 60.23058  ?  64   ARG   A CB  1 
ATOM   516   C  CG  . ARG   A 1 64   ? -78.15500  62.16000  43.80900  1.000 62.69544  ?  64   ARG   A CG  1 
ATOM   517   C  CD  . ARG   A 1 64   ? -79.09500  63.35800  43.86700  1.000 76.84038  ?  64   ARG   A CD  1 
ATOM   518   N  NE  . ARG   A 1 64   ? -80.01100  63.42500  42.73400  1.000 76.89958  ?  64   ARG   A NE  1 
ATOM   519   C  CZ  . ARG   A 1 64   ? -80.50300  64.55400  42.24100  1.000 80.46408  ?  64   ARG   A CZ  1 
ATOM   520   N  NH1 . ARG   A 1 64   ? -80.18200  65.73100  42.75600  1.000 68.64375  ?  64   ARG   A NH1 1 
ATOM   521   N  NH2 . ARG   A 1 64   ? -81.33100  64.50400  41.20200  1.000 90.66029  ?  64   ARG   A NH2 1 
ATOM   522   N  N   . PHE   A 1 65   ? -74.72400  60.63600  42.78100  1.000 69.83523  ?  65   PHE   A N   1 
ATOM   523   C  CA  . PHE   A 1 65   ? -74.41900  59.75500  41.65900  1.000 74.54643  ?  65   PHE   A CA  1 
ATOM   524   C  C   . PHE   A 1 65   ? -73.06400  59.07700  41.82600  1.000 69.10492  ?  65   PHE   A C   1 
ATOM   525   O  O   . PHE   A 1 65   ? -72.36100  58.81600  40.84500  1.000 67.49992  ?  65   PHE   A O   1 
ATOM   526   C  CB  . PHE   A 1 65   ? -74.49500  60.52600  40.34300  1.000 57.22738  ?  65   PHE   A CB  1 
ATOM   527   C  CG  . PHE   A 1 65   ? -75.89100  60.91600  39.97000  1.000 65.58391  ?  65   PHE   A CG  1 
ATOM   528   C  CD1 . PHE   A 1 65   ? -76.56800  61.86700  40.70900  1.000 69.95322  ?  65   PHE   A CD1 1 
ATOM   529   C  CD2 . PHE   A 1 65   ? -76.53100  60.32900  38.89300  1.000 67.97613  ?  65   PHE   A CD2 1 
ATOM   530   C  CE1 . PHE   A 1 65   ? -77.85400  62.22500  40.39300  1.000 74.30105  ?  65   PHE   A CE1 1 
ATOM   531   C  CE2 . PHE   A 1 65   ? -77.82500  60.68800  38.56700  1.000 65.44779  ?  65   PHE   A CE2 1 
ATOM   532   C  CZ  . PHE   A 1 65   ? -78.48700  61.63900  39.32100  1.000 84.86439  ?  65   PHE   A CZ  1 
ATOM   533   N  N   . ARG   A 1 66   ? -72.70200  58.78100  43.07300  1.000 71.08392  ?  66   ARG   A N   1 
ATOM   534   C  CA  . ARG   A 1 66   ? -71.46700  58.06800  43.36000  1.000 69.58365  ?  66   ARG   A CA  1 
ATOM   535   C  C   . ARG   A 1 66   ? -71.48500  56.70000  42.69200  1.000 52.40283  ?  66   ARG   A C   1 
ATOM   536   O  O   . ARG   A 1 66   ? -72.48500  55.98000  42.73900  1.000 68.25141  ?  66   ARG   A O   1 
ATOM   537   C  CB  . ARG   A 1 66   ? -71.28300  57.92300  44.87100  1.000 75.67685  ?  66   ARG   A CB  1 
ATOM   538   C  CG  . ARG   A 1 66   ? -69.95300  57.31800  45.29300  1.000 82.94272  ?  66   ARG   A CG  1 
ATOM   539   C  CD  . ARG   A 1 66   ? -69.54800  57.82500  46.66800  1.000 84.94392  ?  66   ARG   A CD  1 
ATOM   540   N  NE  . ARG   A 1 66   ? -68.66500  58.98200  46.58200  1.000 101.00791 ?  66   ARG   A NE  1 
ATOM   541   C  CZ  . ARG   A 1 66   ? -68.58100  59.93100  47.50500  1.000 103.70751 ?  66   ARG   A CZ  1 
ATOM   542   N  NH1 . ARG   A 1 66   ? -69.32300  59.89800  48.60000  1.000 91.00607  ?  66   ARG   A NH1 1 
ATOM   543   N  NH2 . ARG   A 1 66   ? -67.73500  60.94200  47.32300  1.000 93.56467  ?  66   ARG   A NH2 1 
ATOM   544   N  N   . GLY   A 1 67   ? -70.36700  56.34800  42.06100  1.000 60.10796  ?  67   GLY   A N   1 
ATOM   545   C  CA  . GLY   A 1 67   ? -70.30300  55.16000  41.24100  1.000 53.19611  ?  67   GLY   A CA  1 
ATOM   546   C  C   . GLY   A 1 67   ? -71.02600  55.26600  39.91900  1.000 67.86459  ?  67   GLY   A C   1 
ATOM   547   O  O   . GLY   A 1 67   ? -71.04600  54.28700  39.16300  1.000 75.58436  ?  67   GLY   A O   1 
ATOM   548   N  N   . ARG   A 1 68   ? -71.61900  56.42100  39.61200  1.000 62.69628  ?  68   ARG   A N   1 
ATOM   549   C  CA  . ARG   A 1 68   ? -72.34600  56.61000  38.36900  1.000 67.64031  ?  68   ARG   A CA  1 
ATOM   550   C  C   . ARG   A 1 68   ? -71.88000  57.81900  37.56800  1.000 71.34038  ?  68   ARG   A C   1 
ATOM   551   O  O   . ARG   A 1 68   ? -72.49500  58.13100  36.54200  1.000 77.48050  ?  68   ARG   A O   1 
ATOM   552   C  CB  . ARG   A 1 68   ? -73.85400  56.73300  38.65000  1.000 68.52226  ?  68   ARG   A CB  1 
ATOM   553   C  CG  . ARG   A 1 68   ? -74.58800  55.40300  38.63800  1.000 64.74601  ?  68   ARG   A CG  1 
ATOM   554   C  CD  . ARG   A 1 68   ? -75.69100  55.35900  39.69000  1.000 80.27532  ?  68   ARG   A CD  1 
ATOM   555   N  NE  . ARG   A 1 68   ? -76.68100  56.41800  39.51900  1.000 90.88287  ?  68   ARG   A NE  1 
ATOM   556   C  CZ  . ARG   A 1 68   ? -77.83100  56.48200  40.17800  1.000 84.91037  ?  68   ARG   A CZ  1 
ATOM   557   N  NH1 . ARG   A 1 68   ? -78.17100  55.56200  41.06700  1.000 91.52585  ?  68   ARG   A NH1 1 
ATOM   558   N  NH2 . ARG   A 1 68   ? -78.66300  57.49200  39.93900  1.000 68.19289  ?  68   ARG   A NH2 1 
ATOM   559   N  N   . ILE   A 1 69   ? -70.82500  58.50700  38.00000  1.000 58.42997  ?  69   ILE   A N   1 
ATOM   560   C  CA  . ILE   A 1 69   ? -70.24000  59.61800  37.25600  1.000 56.35799  ?  69   ILE   A CA  1 
ATOM   561   C  C   . ILE   A 1 69   ? -68.92100  59.13000  36.67100  1.000 62.87832  ?  69   ILE   A C   1 
ATOM   562   O  O   . ILE   A 1 69   ? -67.96000  58.87200  37.40700  1.000 60.05870  ?  69   ILE   A O   1 
ATOM   563   C  CB  . ILE   A 1 69   ? -70.03000  60.86000  38.13300  1.000 55.93272  ?  69   ILE   A CB  1 
ATOM   564   C  CG1 . ILE   A 1 69   ? -71.34000  61.27000  38.80000  1.000 60.33091  ?  69   ILE   A CG1 1 
ATOM   565   C  CG2 . ILE   A 1 69   ? -69.50900  62.02100  37.29900  1.000 50.11760  ?  69   ILE   A CG2 1 
ATOM   566   C  CD1 . ILE   A 1 69   ? -71.31900  62.67500  39.35600  1.000 57.03911  ?  69   ILE   A CD1 1 
ATOM   567   N  N   . ILE   A 1 70   ? -68.87200  59.00700  35.34600  1.000 63.90685  ?  70   ILE   A N   1 
ATOM   568   C  CA  . ILE   A 1 70   ? -67.70800  58.49500  34.62900  1.000 49.67574  ?  70   ILE   A CA  1 
ATOM   569   C  C   . ILE   A 1 70   ? -67.06100  59.65600  33.88600  1.000 52.16607  ?  70   ILE   A C   1 
ATOM   570   O  O   . ILE   A 1 70   ? -67.74800  60.42200  33.19800  1.000 54.65370  ?  70   ILE   A O   1 
ATOM   571   C  CB  . ILE   A 1 70   ? -68.09900  57.35900  33.66300  1.000 41.24867  ?  70   ILE   A CB  1 
ATOM   572   C  CG1 . ILE   A 1 70   ? -67.95200  55.99200  34.33500  1.000 43.50418  ?  70   ILE   A CG1 1 
ATOM   573   C  CG2 . ILE   A 1 70   ? -67.26400  57.38900  32.39100  1.000 52.58204  ?  70   ILE   A CG2 1 
ATOM   574   C  CD1 . ILE   A 1 70   ? -68.73000  55.84700  35.61600  1.000 61.99199  ?  70   ILE   A CD1 1 
ATOM   575   N  N   . ASN   A 1 71   ? -65.74800  59.79900  34.03600  1.000 51.52983  ?  71   ASN   A N   1 
ATOM   576   C  CA  . ASN   A 1 71   ? -64.99100  60.81200  33.32000  1.000 53.41142  ?  71   ASN   A CA  1 
ATOM   577   C  C   . ASN   A 1 71   ? -64.04500  60.15300  32.32700  1.000 55.03392  ?  71   ASN   A C   1 
ATOM   578   O  O   . ASN   A 1 71   ? -63.60400  59.01600  32.51900  1.000 54.50197  ?  71   ASN   A O   1 
ATOM   579   C  CB  . ASN   A 1 71   ? -64.19600  61.70400  34.27600  1.000 38.25813  ?  71   ASN   A CB  1 
ATOM   580   C  CG  . ASN   A 1 71   ? -63.58700  62.90200  33.57400  1.000 45.90539  ?  71   ASN   A CG  1 
ATOM   581   O  OD1 . ASN   A 1 71   ? -64.29700  63.82400  33.17500  1.000 49.46097  ?  71   ASN   A OD1 1 
ATOM   582   N  ND2 . ASN   A 1 71   ? -62.26900  62.89100  33.41200  1.000 51.34233  ?  71   ASN   A ND2 1 
ATOM   583   N  N   . LEU   A 1 72   ? -63.74700  60.88300  31.25600  1.000 53.42675  ?  72   LEU   A N   1 
ATOM   584   C  CA  . LEU   A 1 72   ? -62.83200  60.43800  30.20900  1.000 45.26802  ?  72   LEU   A CA  1 
ATOM   585   C  C   . LEU   A 1 72   ? -61.65300  61.40300  30.21200  1.000 48.63209  ?  72   LEU   A C   1 
ATOM   586   O  O   . LEU   A 1 72   ? -61.75800  62.52300  29.70000  1.000 53.64046  ?  72   LEU   A O   1 
ATOM   587   C  CB  . LEU   A 1 72   ? -63.52500  60.39400  28.84700  1.000 47.62279  ?  72   LEU   A CB  1 
ATOM   588   C  CG  . LEU   A 1 72   ? -64.43400  59.20100  28.53000  1.000 49.78676  ?  72   LEU   A CG  1 
ATOM   589   C  CD1 . LEU   A 1 72   ? -65.68100  59.18300  29.40000  1.000 55.67440  ?  72   LEU   A CD1 1 
ATOM   590   C  CD2 . LEU   A 1 72   ? -64.81500  59.20000  27.05900  1.000 51.97381  ?  72   LEU   A CD2 1 
ATOM   591   N  N   . HIS   A 1 73   ? -60.53800  60.97500  30.80200  1.000 40.69011  ?  73   HIS   A N   1 
ATOM   592   C  CA  . HIS   A 1 73   ? -59.35800  61.82000  30.93000  1.000 39.73616  ?  73   HIS   A CA  1 
ATOM   593   C  C   . HIS   A 1 73   ? -58.24500  61.26700  30.05700  1.000 42.72583  ?  73   HIS   A C   1 
ATOM   594   O  O   . HIS   A 1 73   ? -57.81800  60.12000  30.26300  1.000 46.96921  ?  73   HIS   A O   1 
ATOM   595   C  CB  . HIS   A 1 73   ? -58.90400  61.90100  32.38800  1.000 42.81652  ?  73   HIS   A CB  1 
ATOM   596   C  CG  . HIS   A 1 73   ? -57.88600  62.96900  32.64600  1.000 42.38139  ?  73   HIS   A CG  1 
ATOM   597   N  ND1 . HIS   A 1 73   ? -58.16400  64.31200  32.51200  1.000 45.75285  ?  73   HIS   A ND1 1 
ATOM   598   C  CD2 . HIS   A 1 73   ? -56.58900  62.89000  33.02700  1.000 46.04201  ?  73   HIS   A CD2 1 
ATOM   599   C  CE1 . HIS   A 1 73   ? -57.08300  65.01500  32.80000  1.000 48.66535  ?  73   HIS   A CE1 1 
ATOM   600   N  NE2 . HIS   A 1 73   ? -56.11200  64.17600  33.11500  1.000 52.55094  ?  73   HIS   A NE2 1 
ATOM   601   N  N   . PRO   A 1 74   ? -57.74800  62.03000  29.08000  1.000 43.50322  ?  74   PRO   A N   1 
ATOM   602   C  CA  . PRO   A 1 74   ? -56.68900  61.53600  28.18000  1.000 46.19716  ?  74   PRO   A CA  1 
ATOM   603   C  C   . PRO   A 1 74   ? -55.30500  61.58300  28.82100  1.000 51.95378  ?  74   PRO   A C   1 
ATOM   604   O  O   . PRO   A 1 74   ? -54.38000  62.24100  28.33400  1.000 52.84846  ?  74   PRO   A O   1 
ATOM   605   C  CB  . PRO   A 1 74   ? -56.81800  62.48200  26.98000  1.000 38.36588  ?  74   PRO   A CB  1 
ATOM   606   C  CG  . PRO   A 1 74   ? -57.28400  63.76700  27.58300  1.000 41.42390  ?  74   PRO   A CG  1 
ATOM   607   C  CD  . PRO   A 1 74   ? -58.19800  63.38700  28.72000  1.000 30.01938  ?  74   PRO   A CD  1 
ATOM   608   N  N   . SER   A 1 75   ? -55.15600  60.86800  29.93300  1.000 55.94432  ?  75   SER   A N   1 
ATOM   609   C  CA  . SER   A 1 75   ? -53.89400  60.81200  30.65500  1.000 43.13129  ?  75   SER   A CA  1 
ATOM   610   C  C   . SER   A 1 75   ? -53.86000  59.52800  31.46300  1.000 47.81237  ?  75   SER   A C   1 
ATOM   611   O  O   . SER   A 1 75   ? -54.90200  59.01900  31.88200  1.000 64.66735  ?  75   SER   A O   1 
ATOM   612   C  CB  . SER   A 1 75   ? -53.71200  62.02300  31.57300  1.000 50.18365  ?  75   SER   A CB  1 
ATOM   613   O  OG  . SER   A 1 75   ? -52.85200  61.70700  32.65200  1.000 58.18374  ?  75   SER   A OG  1 
ATOM   614   N  N   . LEU   A 1 76   ? -52.65400  59.00600  31.67200  1.000 59.58351  ?  76   LEU   A N   1 
ATOM   615   C  CA  . LEU   A 1 76   ? -52.47000  57.82000  32.50700  1.000 52.63285  ?  76   LEU   A CA  1 
ATOM   616   C  C   . LEU   A 1 76   ? -52.42100  58.27500  33.95800  1.000 50.53041  ?  76   LEU   A C   1 
ATOM   617   O  O   . LEU   A 1 76   ? -51.35500  58.54200  34.51400  1.000 58.05465  ?  76   LEU   A O   1 
ATOM   618   C  CB  . LEU   A 1 76   ? -51.20600  57.06400  32.11700  1.000 50.12095  ?  76   LEU   A CB  1 
ATOM   619   C  CG  . LEU   A 1 76   ? -51.15600  55.59900  32.55000  1.000 51.15859  ?  76   LEU   A CG  1 
ATOM   620   C  CD1 . LEU   A 1 76   ? -51.72100  54.70200  31.46500  1.000 54.64789  ?  76   LEU   A CD1 1 
ATOM   621   C  CD2 . LEU   A 1 76   ? -49.73500  55.19300  32.89300  1.000 54.19281  ?  76   LEU   A CD2 1 
ATOM   622   N  N   . LEU   A 1 77   ? -53.59700  58.38300  34.57200  1.000 60.69383  ?  77   LEU   A N   1 
ATOM   623   C  CA  . LEU   A 1 77   ? -53.66700  58.74200  35.97700  1.000 51.74587  ?  77   LEU   A CA  1 
ATOM   624   C  C   . LEU   A 1 77   ? -52.95000  57.68300  36.81300  1.000 62.61550  ?  77   LEU   A C   1 
ATOM   625   O  O   . LEU   A 1 77   ? -52.98300  56.49200  36.48300  1.000 62.58054  ?  77   LEU   A O   1 
ATOM   626   C  CB  . LEU   A 1 77   ? -55.12100  58.88900  36.42200  1.000 51.04528  ?  77   LEU   A CB  1 
ATOM   627   C  CG  . LEU   A 1 77   ? -55.91100  59.99300  35.71200  1.000 51.67937  ?  77   LEU   A CG  1 
ATOM   628   C  CD1 . LEU   A 1 77   ? -57.34000  60.07700  36.22600  1.000 45.77588  ?  77   LEU   A CD1 1 
ATOM   629   C  CD2 . LEU   A 1 77   ? -55.21000  61.32700  35.87700  1.000 38.34454  ?  77   LEU   A CD2 1 
ATOM   630   N  N   . PRO   A 1 78   ? -52.29900  58.08300  37.91300  1.000 61.96333  ?  78   PRO   A N   1 
ATOM   631   C  CA  . PRO   A 1 78   ? -52.34300  59.39200  38.57800  1.000 58.82617  ?  78   PRO   A CA  1 
ATOM   632   C  C   . PRO   A 1 78   ? -51.53500  60.50100  37.90800  1.000 60.95988  ?  78   PRO   A C   1 
ATOM   633   O  O   . PRO   A 1 78   ? -51.53400  61.61800  38.40300  1.000 64.01302  ?  78   PRO   A O   1 
ATOM   634   C  CB  . PRO   A 1 78   ? -51.77700  59.06600  39.96300  1.000 72.71460  ?  78   PRO   A CB  1 
ATOM   635   C  CG  . PRO   A 1 78   ? -50.71800  58.03900  39.66300  1.000 65.11733  ?  78   PRO   A CG  1 
ATOM   636   C  CD  . PRO   A 1 78   ? -51.27300  57.21100  38.51800  1.000 61.92797  ?  78   PRO   A CD  1 
ATOM   637   N  N   . TRP   A 1 79   ? -50.84800  60.26300  36.79700  1.000 52.45887  ?  79   TRP   A N   1 
ATOM   638   C  CA  . TRP   A 1 79   ? -50.01300  61.30300  36.21700  1.000 52.41313  ?  79   TRP   A CA  1 
ATOM   639   C  C   . TRP   A 1 79   ? -50.84600  62.29800  35.41700  1.000 50.91605  ?  79   TRP   A C   1 
ATOM   640   O  O   . TRP   A 1 79   ? -51.90600  61.96500  34.88100  1.000 54.84200  ?  79   TRP   A O   1 
ATOM   641   C  CB  . TRP   A 1 79   ? -48.93500  60.69600  35.32100  1.000 50.21059  ?  79   TRP   A CB  1 
ATOM   642   C  CG  . TRP   A 1 79   ? -48.15100  59.61900  35.98200  1.000 53.00902  ?  79   TRP   A CG  1 
ATOM   643   C  CD1 . TRP   A 1 79   ? -48.44300  58.28600  36.00700  1.000 56.01568  ?  79   TRP   A CD1 1 
ATOM   644   C  CD2 . TRP   A 1 79   ? -46.94200  59.78100  36.72800  1.000 60.96020  ?  79   TRP   A CD2 1 
ATOM   645   N  NE1 . TRP   A 1 79   ? -47.48500  57.60600  36.71900  1.000 59.96249  ?  79   TRP   A NE1 1 
ATOM   646   C  CE2 . TRP   A 1 79   ? -46.55300  58.50200  37.17300  1.000 68.44637  ?  79   TRP   A CE2 1 
ATOM   647   C  CE3 . TRP   A 1 79   ? -46.15000  60.88300  37.06100  1.000 54.86469  ?  79   TRP   A CE3 1 
ATOM   648   C  CZ2 . TRP   A 1 79   ? -45.40500  58.29600  37.93300  1.000 83.40074  ?  79   TRP   A CZ2 1 
ATOM   649   C  CZ3 . TRP   A 1 79   ? -45.01200  60.67700  37.81400  1.000 67.01444  ?  79   TRP   A CZ3 1 
ATOM   650   C  CH2 . TRP   A 1 79   ? -44.64900  59.39300  38.24300  1.000 75.70552  ?  79   TRP   A CH2 1 
ATOM   651   N  N   . ASN   A 1 80   ? -50.34800  63.53300  35.35200  1.000 46.46498  ?  80   ASN   A N   1 
ATOM   652   C  CA  . ASN   A 1 80   ? -50.91800  64.59200  34.51700  1.000 44.93521  ?  80   ASN   A CA  1 
ATOM   653   C  C   . ASN   A 1 80   ? -52.41100  64.78100  34.77400  1.000 55.24726  ?  80   ASN   A C   1 
ATOM   654   O  O   . ASN   A 1 80   ? -53.23500  64.76500  33.85600  1.000 52.26188  ?  80   ASN   A O   1 
ATOM   655   C  CB  . ASN   A 1 80   ? -50.65100  64.32000  33.03700  1.000 43.36469  ?  80   ASN   A CB  1 
ATOM   656   C  CG  . ASN   A 1 80   ? -49.20200  64.00500  32.76000  1.000 41.78921  ?  80   ASN   A CG  1 
ATOM   657   O  OD1 . ASN   A 1 80   ? -48.32800  64.85800  32.92100  1.000 52.11808  ?  80   ASN   A OD1 1 
ATOM   658   N  ND2 . ASN   A 1 80   ? -48.93400  62.77400  32.34300  1.000 50.85544  ?  80   ASN   A ND2 1 
ATOM   659   N  N   . LYS   A 1 81   ? -52.76200  64.96200  36.04200  1.000 55.98977  ?  81   LYS   A N   1 
ATOM   660   C  CA  . LYS   A 1 81   ? -54.12600  65.33700  36.36900  1.000 45.23004  ?  81   LYS   A CA  1 
ATOM   661   C  C   . LYS   A 1 81   ? -54.34100  66.81500  36.07200  1.000 47.46203  ?  81   LYS   A C   1 
ATOM   662   O  O   . LYS   A 1 81   ? -53.39400  67.59200  35.92200  1.000 58.68725  ?  81   LYS   A O   1 
ATOM   663   C  CB  . LYS   A 1 81   ? -54.43800  65.05300  37.83800  1.000 59.03726  ?  81   LYS   A CB  1 
ATOM   664   C  CG  . LYS   A 1 81   ? -54.05900  63.66000  38.29700  1.000 68.24922  ?  81   LYS   A CG  1 
ATOM   665   C  CD  . LYS   A 1 81   ? -53.29200  63.70300  39.60800  1.000 69.36266  ?  81   LYS   A CD  1 
ATOM   666   C  CE  . LYS   A 1 81   ? -54.20300  63.47700  40.79200  1.000 58.17935  ?  81   LYS   A CE  1 
ATOM   667   N  NZ  . LYS   A 1 81   ? -53.42500  63.40700  42.06000  1.000 83.38069  ?  81   LYS   A NZ  1 
ATOM   668   N  N   . GLY   A 1 82   ? -55.60400  67.19900  35.98300  1.000 44.68008  ?  82   GLY   A N   1 
ATOM   669   C  CA  . GLY   A 1 82   ? -55.95300  68.59600  35.79500  1.000 39.09314  ?  82   GLY   A CA  1 
ATOM   670   C  C   . GLY   A 1 82   ? -56.02500  68.96500  34.32700  1.000 50.71708  ?  82   GLY   A C   1 
ATOM   671   O  O   . GLY   A 1 82   ? -56.60500  68.23300  33.52500  1.000 57.52192  ?  82   GLY   A O   1 
ATOM   672   N  N   . ARG   A 1 83   ? -55.41600  70.09400  33.97800  1.000 50.02287  ?  83   ARG   A N   1 
ATOM   673   C  CA  . ARG   A 1 83   ? -55.60500  70.73800  32.68900  1.000 46.05183  ?  83   ARG   A CA  1 
ATOM   674   C  C   . ARG   A 1 83   ? -54.40800  70.52200  31.77300  1.000 57.42878  ?  83   ARG   A C   1 
ATOM   675   O  O   . ARG   A 1 83   ? -53.28600  70.26600  32.22300  1.000 47.87320  ?  83   ARG   A O   1 
ATOM   676   C  CB  . ARG   A 1 83   ? -55.84800  72.23600  32.88000  1.000 41.61427  ?  83   ARG   A CB  1 
ATOM   677   C  CG  . ARG   A 1 83   ? -57.04300  72.52400  33.75400  1.000 60.37363  ?  83   ARG   A CG  1 
ATOM   678   C  CD  . ARG   A 1 83   ? -58.31000  72.05700  33.07800  1.000 63.87200  ?  83   ARG   A CD  1 
ATOM   679   N  NE  . ARG   A 1 83   ? -58.89700  73.12700  32.28500  1.000 63.59255  ?  83   ARG   A NE  1 
ATOM   680   C  CZ  . ARG   A 1 83   ? -59.97800  73.80700  32.63900  1.000 69.56131  ?  83   ARG   A CZ  1 
ATOM   681   N  NH1 . ARG   A 1 83   ? -60.64100  73.52100  33.74700  1.000 88.68330  ?  83   ARG   A NH1 1 
ATOM   682   N  NH2 . ARG   A 1 83   ? -60.40500  74.79500  31.86000  1.000 75.22737  ?  83   ARG   A NH2 1 
ATOM   683   N  N   . ASP   A 1 84   ? -54.67200  70.65400  30.47100  1.000 51.09649  ?  84   ASP   A N   1 
ATOM   684   C  CA  . ASP   A 1 84   ? -53.70600  70.45500  29.39300  1.000 36.01225  ?  84   ASP   A CA  1 
ATOM   685   C  C   . ASP   A 1 84   ? -52.86800  69.19500  29.65100  1.000 45.86641  ?  84   ASP   A C   1 
ATOM   686   O  O   . ASP   A 1 84   ? -51.64100  69.27500  29.77000  1.000 37.88449  ?  84   ASP   A O   1 
ATOM   687   C  CB  . ASP   A 1 84   ? -52.81800  71.68100  29.21600  1.000 24.27459  ?  84   ASP   A CB  1 
ATOM   688   C  CG  . ASP   A 1 84   ? -53.60100  72.90700  28.75800  1.000 41.70689  ?  84   ASP   A CG  1 
ATOM   689   O  OD1 . ASP   A 1 84   ? -54.06500  72.92300  27.59900  1.000 63.11872  ?  84   ASP   A OD1 1 
ATOM   690   O  OD2 . ASP   A 1 84   ? -53.76000  73.85500  29.55500  1.000 54.70298  -1 84   ASP   A OD2 1 
ATOM   691   N  N   . PRO   A 1 85   ? -53.50400  68.02200  29.74300  1.000 46.82946  ?  85   PRO   A N   1 
ATOM   692   C  CA  . PRO   A 1 85   ? -52.77400  66.84900  30.24500  1.000 40.73213  ?  85   PRO   A CA  1 
ATOM   693   C  C   . PRO   A 1 85   ? -51.78100  66.28300  29.25000  1.000 40.29057  ?  85   PRO   A C   1 
ATOM   694   O  O   . PRO   A 1 85   ? -50.71700  65.80300  29.65700  1.000 58.32628  ?  85   PRO   A O   1 
ATOM   695   C  CB  . PRO   A 1 85   ? -53.89900  65.85500  30.56100  1.000 38.96425  ?  85   PRO   A CB  1 
ATOM   696   C  CG  . PRO   A 1 85   ? -54.97200  66.20200  29.58500  1.000 41.67922  ?  85   PRO   A CG  1 
ATOM   697   C  CD  . PRO   A 1 85   ? -54.90100  67.69900  29.39700  1.000 50.73890  ?  85   PRO   A CD  1 
ATOM   698   N  N   . VAL   A 1 86   ? -52.08900  66.33200  27.95400  1.000 48.80918  ?  86   VAL   A N   1 
ATOM   699   C  CA  . VAL   A 1 86   ? -51.21800  65.68800  26.97600  1.000 49.35378  ?  86   VAL   A CA  1 
ATOM   700   C  C   . VAL   A 1 86   ? -49.89300  66.43100  26.86700  1.000 45.95068  ?  86   VAL   A C   1 
ATOM   701   O  O   . VAL   A 1 86   ? -48.82500  65.81000  26.79100  1.000 39.37561  ?  86   VAL   A O   1 
ATOM   702   C  CB  . VAL   A 1 86   ? -51.93100  65.57600  25.61700  1.000 38.88832  ?  86   VAL   A CB  1 
ATOM   703   C  CG1 . VAL   A 1 86   ? -51.04600  64.85800  24.61600  1.000 37.15672  ?  86   VAL   A CG1 1 
ATOM   704   C  CG2 . VAL   A 1 86   ? -53.24500  64.83500  25.78200  1.000 38.12194  ?  86   VAL   A CG2 1 
ATOM   705   N  N   . PHE   A 1 87   ? -49.93400  67.76500  26.87100  1.000 39.99181  ?  87   PHE   A N   1 
ATOM   706   C  CA  . PHE   A 1 87   ? -48.69800  68.53900  26.82100  1.000 44.54925  ?  87   PHE   A CA  1 
ATOM   707   C  C   . PHE   A 1 87   ? -47.81200  68.22600  28.01900  1.000 50.62959  ?  87   PHE   A C   1 
ATOM   708   O  O   . PHE   A 1 87   ? -46.62300  67.92300  27.86600  1.000 55.79914  ?  87   PHE   A O   1 
ATOM   709   C  CB  . PHE   A 1 87   ? -49.00800  70.03300  26.76900  1.000 34.47391  ?  87   PHE   A CB  1 
ATOM   710   C  CG  . PHE   A 1 87   ? -47.84200  70.90000  27.14300  1.000 47.02588  ?  87   PHE   A CG  1 
ATOM   711   C  CD1 . PHE   A 1 87   ? -46.76500  71.04200  26.28500  1.000 50.64660  ?  87   PHE   A CD1 1 
ATOM   712   C  CD2 . PHE   A 1 87   ? -47.81700  71.56400  28.35700  1.000 48.38581  ?  87   PHE   A CD2 1 
ATOM   713   C  CE1 . PHE   A 1 87   ? -45.68800  71.83700  26.62600  1.000 50.88913  ?  87   PHE   A CE1 1 
ATOM   714   C  CE2 . PHE   A 1 87   ? -46.74200  72.36100  28.70400  1.000 56.62065  ?  87   PHE   A CE2 1 
ATOM   715   C  CZ  . PHE   A 1 87   ? -45.67600  72.49700  27.83700  1.000 45.35034  ?  87   PHE   A CZ  1 
ATOM   716   N  N   . TRP   A 1 88   ? -48.38000  68.29300  29.22500  1.000 45.32266  ?  88   TRP   A N   1 
ATOM   717   C  CA  . TRP   A 1 88   ? -47.60400  68.00900  30.42300  1.000 40.35092  ?  88   TRP   A CA  1 
ATOM   718   C  C   . TRP   A 1 88   ? -47.13900  66.56400  30.47500  1.000 45.34419  ?  88   TRP   A C   1 
ATOM   719   O  O   . TRP   A 1 88   ? -46.13900  66.27200  31.13900  1.000 58.21317  ?  88   TRP   A O   1 
ATOM   720   C  CB  . TRP   A 1 88   ? -48.41900  68.35400  31.66800  1.000 35.45192  ?  88   TRP   A CB  1 
ATOM   721   C  CG  . TRP   A 1 88   ? -48.59200  69.82500  31.84100  1.000 30.49855  ?  88   TRP   A CG  1 
ATOM   722   C  CD1 . TRP   A 1 88   ? -49.76300  70.51800  31.83600  1.000 36.16264  ?  88   TRP   A CD1 1 
ATOM   723   C  CD2 . TRP   A 1 88   ? -47.55200  70.79300  32.02500  1.000 34.49275  ?  88   TRP   A CD2 1 
ATOM   724   N  NE1 . TRP   A 1 88   ? -49.52100  71.85900  32.01400  1.000 38.19456  ?  88   TRP   A NE1 1 
ATOM   725   C  CE2 . TRP   A 1 88   ? -48.17000  72.05200  32.13200  1.000 33.78088  ?  88   TRP   A CE2 1 
ATOM   726   C  CE3 . TRP   A 1 88   ? -46.15900  70.71500  32.11500  1.000 40.83545  ?  88   TRP   A CE3 1 
ATOM   727   C  CZ2 . TRP   A 1 88   ? -47.44500  73.22500  32.32300  1.000 40.55921  ?  88   TRP   A CZ2 1 
ATOM   728   C  CZ3 . TRP   A 1 88   ? -45.44000  71.88000  32.30500  1.000 39.47318  ?  88   TRP   A CZ3 1 
ATOM   729   C  CH2 . TRP   A 1 88   ? -46.08400  73.11900  32.40700  1.000 43.18351  ?  88   TRP   A CH2 1 
ATOM   730   N  N   . SER   A 1 89   ? -47.83300  65.65500  29.78700  1.000 41.55803  ?  89   SER   A N   1 
ATOM   731   C  CA  . SER   A 1 89   ? -47.33800  64.28700  29.68700  1.000 50.19026  ?  89   SER   A CA  1 
ATOM   732   C  C   . SER   A 1 89   ? -46.02100  64.23100  28.92400  1.000 52.54625  ?  89   SER   A C   1 
ATOM   733   O  O   . SER   A 1 89   ? -45.18600  63.35900  29.19000  1.000 47.83007  ?  89   SER   A O   1 
ATOM   734   C  CB  . SER   A 1 89   ? -48.38400  63.39400  29.01800  1.000 36.15617  ?  89   SER   A CB  1 
ATOM   735   O  OG  . SER   A 1 89   ? -48.24600  63.40700  27.60900  1.000 52.77270  ?  89   SER   A OG  1 
ATOM   736   N  N   . VAL   A 1 90   ? -45.81000  65.15800  27.99500  1.000 43.30954  ?  90   VAL   A N   1 
ATOM   737   C  CA  . VAL   A 1 90   ? -44.59400  65.17900  27.18600  1.000 50.91637  ?  90   VAL   A CA  1 
ATOM   738   C  C   . VAL   A 1 90   ? -43.49600  65.99200  27.85600  1.000 44.19400  ?  90   VAL   A C   1 
ATOM   739   O  O   . VAL   A 1 90   ? -42.35300  65.53800  27.96300  1.000 39.18294  ?  90   VAL   A O   1 
ATOM   740   C  CB  . VAL   A 1 90   ? -44.91400  65.72300  25.77700  1.000 57.58559  ?  90   VAL   A CB  1 
ATOM   741   C  CG1 . VAL   A 1 90   ? -43.65600  65.75500  24.91400  1.000 41.92203  ?  90   VAL   A CG1 1 
ATOM   742   C  CG2 . VAL   A 1 90   ? -46.00800  64.89100  25.12200  1.000 37.16306  ?  90   VAL   A CG2 1 
ATOM   743   N  N   . TRP   A 1 91   ? -43.83300  67.20000  28.31600  1.000 46.54921  ?  91   TRP   A N   1 
ATOM   744   C  CA  . TRP   A 1 91   ? -42.83300  68.09500  28.89200  1.000 39.87461  ?  91   TRP   A CA  1 
ATOM   745   C  C   . TRP   A 1 91   ? -42.21600  67.50000  30.15200  1.000 42.95584  ?  91   TRP   A C   1 
ATOM   746   O  O   . TRP   A 1 91   ? -40.99000  67.45600  30.29500  1.000 46.87448  ?  91   TRP   A O   1 
ATOM   747   C  CB  . TRP   A 1 91   ? -43.46700  69.45400  29.18800  1.000 34.86049  ?  91   TRP   A CB  1 
ATOM   748   C  CG  . TRP   A 1 91   ? -42.49200  70.49500  29.62600  1.000 43.43862  ?  91   TRP   A CG  1 
ATOM   749   C  CD1 . TRP   A 1 91   ? -42.11200  70.77600  30.90500  1.000 51.70800  ?  91   TRP   A CD1 1 
ATOM   750   C  CD2 . TRP   A 1 91   ? -41.77200  71.40400  28.78400  1.000 52.39427  ?  91   TRP   A CD2 1 
ATOM   751   N  NE1 . TRP   A 1 91   ? -41.19800  71.80300  30.91300  1.000 56.61840  ?  91   TRP   A NE1 1 
ATOM   752   C  CE2 . TRP   A 1 91   ? -40.97300  72.20600  29.62300  1.000 48.35777  ?  91   TRP   A CE2 1 
ATOM   753   C  CE3 . TRP   A 1 91   ? -41.72400  71.61600  27.40300  1.000 47.79096  ?  91   TRP   A CE3 1 
ATOM   754   C  CZ2 . TRP   A 1 91   ? -40.13700  73.20300  29.12700  1.000 52.39167  ?  91   TRP   A CZ2 1 
ATOM   755   C  CZ3 . TRP   A 1 91   ? -40.89500  72.60700  26.91300  1.000 57.86695  ?  91   TRP   A CZ3 1 
ATOM   756   C  CH2 . TRP   A 1 91   ? -40.11200  73.38800  27.77300  1.000 53.15766  ?  91   TRP   A CH2 1 
ATOM   757   N  N   . ASP   A 1 92   ? -43.05000  67.03100  31.07600  1.000 48.75499  ?  92   ASP   A N   1 
ATOM   758   C  CA  . ASP   A 1 92   ? -42.56000  66.43700  32.31300  1.000 39.61732  ?  92   ASP   A CA  1 
ATOM   759   C  C   . ASP   A 1 92   ? -42.14700  64.97900  32.15100  1.000 34.30691  ?  92   ASP   A C   1 
ATOM   760   O  O   . ASP   A 1 92   ? -41.84800  64.32600  33.15700  1.000 49.00034  ?  92   ASP   A O   1 
ATOM   761   C  CB  . ASP   A 1 92   ? -43.61700  66.56000  33.41200  1.000 26.58136  ?  92   ASP   A CB  1 
ATOM   762   C  CG  . ASP   A 1 92   ? -43.77700  67.98200  33.90500  1.000 52.81395  ?  92   ASP   A CG  1 
ATOM   763   O  OD1 . ASP   A 1 92   ? -42.82300  68.77700  33.75400  1.000 44.74543  ?  92   ASP   A OD1 1 
ATOM   764   O  OD2 . ASP   A 1 92   ? -44.85900  68.30400  34.44200  1.000 52.76251  -1 92   ASP   A OD2 1 
ATOM   765   N  N   . GLU   A 1 93   ? -42.13200  64.46100  30.92200  1.000 41.37663  ?  93   GLU   A N   1 
ATOM   766   C  CA  . GLU   A 1 93   ? -41.64500  63.10900  30.62800  1.000 42.37768  ?  93   GLU   A CA  1 
ATOM   767   C  C   . GLU   A 1 93   ? -42.34900  62.05100  31.47700  1.000 43.84389  ?  93   GLU   A C   1 
ATOM   768   O  O   . GLU   A 1 93   ? -41.74700  61.06400  31.90300  1.000 59.39139  ?  93   GLU   A O   1 
ATOM   769   C  CB  . GLU   A 1 93   ? -40.12800  63.03000  30.79900  1.000 50.57143  ?  93   GLU   A CB  1 
ATOM   770   C  CG  . GLU   A 1 93   ? -39.37800  64.19600  30.16800  1.000 63.76894  ?  93   GLU   A CG  1 
ATOM   771   C  CD  . GLU   A 1 93   ? -38.05900  63.78000  29.54600  1.000 65.89878  ?  93   GLU   A CD  1 
ATOM   772   O  OE1 . GLU   A 1 93   ? -37.94900  62.62000  29.09300  1.000 57.95308  ?  93   GLU   A OE1 1 
ATOM   773   O  OE2 . GLU   A 1 93   ? -37.13200  64.61600  29.51400  1.000 67.78631  -1 93   GLU   A OE2 1 
ATOM   774   N  N   . THR   A 1 94   ? -43.64300  62.25400  31.71800  1.000 49.94218  ?  94   THR   A N   1 
ATOM   775   C  CA  . THR   A 1 94   ? -44.43800  61.30900  32.48700  1.000 51.89204  ?  94   THR   A CA  1 
ATOM   776   C  C   . THR   A 1 94   ? -44.88900  60.14900  31.60400  1.000 51.79114  ?  94   THR   A C   1 
ATOM   777   O  O   . THR   A 1 94   ? -44.83200  60.23600  30.37500  1.000 54.89980  ?  94   THR   A O   1 
ATOM   778   C  CB  . THR   A 1 94   ? -45.66100  62.00300  33.08100  1.000 47.18579  ?  94   THR   A CB  1 
ATOM   779   O  OG1 . THR   A 1 94   ? -46.69800  62.06100  32.09500  1.000 52.23387  ?  94   THR   A OG1 1 
ATOM   780   C  CG2 . THR   A 1 94   ? -45.31600  63.41100  33.54100  1.000 44.22636  ?  94   THR   A CG2 1 
ATOM   781   N  N   . PRO   A 1 95   ? -45.33700  59.04300  32.20600  1.000 52.50843  ?  95   PRO   A N   1 
ATOM   782   C  CA  . PRO   A 1 95   ? -45.91100  57.95900  31.40000  1.000 53.39709  ?  95   PRO   A CA  1 
ATOM   783   C  C   . PRO   A 1 95   ? -47.13100  58.43900  30.62800  1.000 55.44063  ?  95   PRO   A C   1 
ATOM   784   O  O   . PRO   A 1 95   ? -47.81000  59.39100  31.02200  1.000 54.97150  ?  95   PRO   A O   1 
ATOM   785   C  CB  . PRO   A 1 95   ? -46.28400  56.89800  32.44200  1.000 52.54492  ?  95   PRO   A CB  1 
ATOM   786   C  CG  . PRO   A 1 95   ? -45.38600  57.17100  33.59400  1.000 44.00919  ?  95   PRO   A CG  1 
ATOM   787   C  CD  . PRO   A 1 95   ? -45.20000  58.65900  33.62300  1.000 55.50569  ?  95   PRO   A CD  1 
ATOM   788   N  N   . LYS   A 1 96   ? -47.40300  57.76700  29.51200  1.000 46.39650  ?  96   LYS   A N   1 
ATOM   789   C  CA  . LYS   A 1 96   ? -48.43700  58.17900  28.57300  1.000 61.89408  ?  96   LYS   A CA  1 
ATOM   790   C  C   . LYS   A 1 96   ? -49.57600  57.16700  28.55100  1.000 61.28952  ?  96   LYS   A C   1 
ATOM   791   O  O   . LYS   A 1 96   ? -49.34300  55.95400  28.52800  1.000 53.48606  ?  96   LYS   A O   1 
ATOM   792   C  CB  . LYS   A 1 96   ? -47.85900  58.33700  27.16300  1.000 53.60466  ?  96   LYS   A CB  1 
ATOM   793   C  CG  . LYS   A 1 96   ? -46.46700  58.95000  27.12700  1.000 49.01844  ?  96   LYS   A CG  1 
ATOM   794   C  CD  . LYS   A 1 96   ? -46.51400  60.47100  27.19100  1.000 40.57514  ?  96   LYS   A CD  1 
ATOM   795   C  CE  . LYS   A 1 96   ? -45.11500  61.06200  27.12000  1.000 49.95167  ?  96   LYS   A CE  1 
ATOM   796   N  NZ  . LYS   A 1 96   ? -44.28500  60.43400  26.05700  1.000 72.87106  ?  96   LYS   A NZ  1 
ATOM   797   N  N   . GLY   A 1 97   ? -50.80400  57.67000  28.54600  1.000 60.60637  ?  97   GLY   A N   1 
ATOM   798   C  CA  . GLY   A 1 97   ? -51.95200  56.78800  28.47300  1.000 59.36233  ?  97   GLY   A CA  1 
ATOM   799   C  C   . GLY   A 1 97   ? -53.25100  57.56500  28.51400  1.000 49.75881  ?  97   GLY   A C   1 
ATOM   800   O  O   . GLY   A 1 97   ? -53.27000  58.79100  28.39500  1.000 42.67748  ?  97   GLY   A O   1 
ATOM   801   N  N   . VAL   A 1 98   ? -54.34500  56.81700  28.67100  1.000 54.73488  ?  98   VAL   A N   1 
ATOM   802   C  CA  . VAL   A 1 98   ? -55.69100  57.37000  28.78300  1.000 43.22212  ?  98   VAL   A CA  1 
ATOM   803   C  C   . VAL   A 1 98   ? -56.42400  56.62400  29.89000  1.000 45.46487  ?  98   VAL   A C   1 
ATOM   804   O  O   . VAL   A 1 98   ? -56.14900  55.45200  30.16100  1.000 48.91410  ?  98   VAL   A O   1 
ATOM   805   C  CB  . VAL   A 1 98   ? -56.47600  57.27500  27.45400  1.000 37.05414  ?  98   VAL   A CB  1 
ATOM   806   C  CG1 . VAL   A 1 98   ? -55.91900  58.24500  26.43200  1.000 27.30248  ?  98   VAL   A CG1 1 
ATOM   807   C  CG2 . VAL   A 1 98   ? -56.44900  55.85400  26.91300  1.000 36.47589  ?  98   VAL   A CG2 1 
ATOM   808   N  N   . THR   A 1 99   ? -57.37500  57.30600  30.52500  1.000 50.97388  ?  99   THR   A N   1 
ATOM   809   C  CA  . THR   A 1 99   ? -58.02700  56.76400  31.71100  1.000 54.93808  ?  99   THR   A CA  1 
ATOM   810   C  C   . THR   A 1 99   ? -59.51100  57.09500  31.72200  1.000 49.76474  ?  99   THR   A C   1 
ATOM   811   O  O   . THR   A 1 99   ? -59.89300  58.25900  31.56800  1.000 45.29998  ?  99   THR   A O   1 
ATOM   812   C  CB  . THR   A 1 99   ? -57.37000  57.30700  32.98500  1.000 50.90623  ?  99   THR   A CB  1 
ATOM   813   O  OG1 . THR   A 1 99   ? -55.98400  56.94500  33.00000  1.000 57.02679  ?  99   THR   A OG1 1 
ATOM   814   C  CG2 . THR   A 1 99   ? -58.05100  56.75300  34.22400  1.000 46.94577  ?  99   THR   A CG2 1 
ATOM   815   N  N   . ILE   A 1 100  ? -60.33900  56.07100  31.91200  1.000 50.81217  ?  100  ILE   A N   1 
ATOM   816   C  CA  . ILE   A 1 100  ? -61.75000  56.24100  32.24100  1.000 56.42644  ?  100  ILE   A CA  1 
ATOM   817   C  C   . ILE   A 1 100  ? -61.89800  55.97800  33.73300  1.000 58.02271  ?  100  ILE   A C   1 
ATOM   818   O  O   . ILE   A 1 100  ? -61.66200  54.85600  34.19900  1.000 56.84722  ?  100  ILE   A O   1 
ATOM   819   C  CB  . ILE   A 1 100  ? -62.64300  55.29700  31.42100  1.000 52.23038  ?  100  ILE   A CB  1 
ATOM   820   C  CG1 . ILE   A 1 100  ? -62.66100  55.71700  29.95300  1.000 54.04807  ?  100  ILE   A CG1 1 
ATOM   821   C  CG2 . ILE   A 1 100  ? -64.05800  55.27700  31.98100  1.000 43.63447  ?  100  ILE   A CG2 1 
ATOM   822   C  CD1 . ILE   A 1 100  ? -63.03000  54.59700  29.01400  1.000 49.92410  ?  100  ILE   A CD1 1 
ATOM   823   N  N   . HIS   A 1 101  ? -62.27800  57.00700  34.48800  1.000 56.91023  ?  101  HIS   A N   1 
ATOM   824   C  CA  . HIS   A 1 101  ? -62.27700  56.94000  35.94200  1.000 55.10696  ?  101  HIS   A CA  1 
ATOM   825   C  C   . HIS   A 1 101  ? -63.58700  57.47500  36.50300  1.000 54.15680  ?  101  HIS   A C   1 
ATOM   826   O  O   . HIS   A 1 101  ? -64.44300  57.98800  35.77700  1.000 59.79263  ?  101  HIS   A O   1 
ATOM   827   C  CB  . HIS   A 1 101  ? -61.09400  57.72200  36.53300  1.000 48.82701  ?  101  HIS   A CB  1 
ATOM   828   C  CG  . HIS   A 1 101  ? -61.17000  59.20000  36.30600  1.000 37.33124  ?  101  HIS   A CG  1 
ATOM   829   N  ND1 . HIS   A 1 101  ? -61.67500  60.07300  37.24600  1.000 42.31413  ?  101  HIS   A ND1 1 
ATOM   830   C  CD2 . HIS   A 1 101  ? -60.80200  59.96000  35.24700  1.000 48.00888  ?  101  HIS   A CD2 1 
ATOM   831   C  CE1 . HIS   A 1 101  ? -61.61500  61.30600  36.77600  1.000 50.83674  ?  101  HIS   A CE1 1 
ATOM   832   N  NE2 . HIS   A 1 101  ? -61.08900  61.26500  35.56500  1.000 47.66364  ?  101  HIS   A NE2 1 
ATOM   833   N  N   . LEU   A 1 102  ? -63.72900  57.34500  37.81900  1.000 51.60661  ?  102  LEU   A N   1 
ATOM   834   C  CA  . LEU   A 1 102  ? -64.87600  57.85000  38.55600  1.000 50.71261  ?  102  LEU   A CA  1 
ATOM   835   C  C   . LEU   A 1 102  ? -64.55500  59.21700  39.14900  1.000 49.20679  ?  102  LEU   A C   1 
ATOM   836   O  O   . LEU   A 1 102  ? -63.41500  59.49900  39.52400  1.000 64.21111  ?  102  LEU   A O   1 
ATOM   837   C  CB  . LEU   A 1 102  ? -65.27700  56.87500  39.66500  1.000 49.74955  ?  102  LEU   A CB  1 
ATOM   838   C  CG  . LEU   A 1 102  ? -65.87100  55.54800  39.18900  1.000 62.53270  ?  102  LEU   A CG  1 
ATOM   839   C  CD1 . LEU   A 1 102  ? -65.58300  54.43000  40.18100  1.000 51.31152  ?  102  LEU   A CD1 1 
ATOM   840   C  CD2 . LEU   A 1 102  ? -67.36800  55.69700  38.96500  1.000 53.95851  ?  102  LEU   A CD2 1 
ATOM   841   N  N   . ILE   A 1 103  ? -65.57400  60.06500  39.23100  1.000 44.42639  ?  103  ILE   A N   1 
ATOM   842   C  CA  . ILE   A 1 103  ? -65.40100  61.44100  39.68000  1.000 60.41053  ?  103  ILE   A CA  1 
ATOM   843   C  C   . ILE   A 1 103  ? -65.59600  61.50600  41.18900  1.000 56.84538  ?  103  ILE   A C   1 
ATOM   844   O  O   . ILE   A 1 103  ? -66.55400  60.94000  41.72700  1.000 67.51649  ?  103  ILE   A O   1 
ATOM   845   C  CB  . ILE   A 1 103  ? -66.37800  62.38200  38.95500  1.000 46.01593  ?  103  ILE   A CB  1 
ATOM   846   C  CG1 . ILE   A 1 103  ? -65.95700  62.56000  37.49500  1.000 53.47065  ?  103  ILE   A CG1 1 
ATOM   847   C  CG2 . ILE   A 1 103  ? -66.46900  63.72600  39.66600  1.000 44.17312  ?  103  ILE   A CG2 1 
ATOM   848   C  CD1 . ILE   A 1 103  ? -64.88900  63.61200  37.28500  1.000 58.90846  ?  103  ILE   A CD1 1 
ATOM   849   N  N   . ASP   A 1 104  ? -64.68000  62.19000  41.87300  1.000 64.22532  ?  104  ASP   A N   1 
ATOM   850   C  CA  . ASP   A 1 104  ? -64.81700  62.44000  43.30100  1.000 45.58645  ?  104  ASP   A CA  1 
ATOM   851   C  C   . ASP   A 1 104  ? -64.93800  63.93900  43.54500  1.000 61.45377  ?  104  ASP   A C   1 
ATOM   852   O  O   . ASP   A 1 104  ? -65.39500  64.67800  42.66600  1.000 62.84017  ?  104  ASP   A O   1 
ATOM   853   C  CB  . ASP   A 1 104  ? -63.63600  61.84000  44.06800  1.000 46.21107  ?  104  ASP   A CB  1 
ATOM   854   C  CG  . ASP   A 1 104  ? -62.31300  62.47500  43.69400  1.000 77.05212  ?  104  ASP   A CG  1 
ATOM   855   O  OD1 . ASP   A 1 104  ? -62.05300  63.60800  44.14100  1.000 79.33794  ?  104  ASP   A OD1 1 
ATOM   856   O  OD2 . ASP   A 1 104  ? -61.53700  61.84400  42.94700  1.000 85.65006  -1 104  ASP   A OD2 1 
ATOM   857   N  N   . GLU   A 1 105  ? -64.53500  64.40200  44.72900  1.000 67.78977  ?  105  GLU   A N   1 
ATOM   858   C  CA  . GLU   A 1 105  ? -64.61300  65.81200  45.08400  1.000 66.80644  ?  105  GLU   A CA  1 
ATOM   859   C  C   . GLU   A 1 105  ? -63.30600  66.55100  44.82600  1.000 75.61579  ?  105  GLU   A C   1 
ATOM   860   O  O   . GLU   A 1 105  ? -63.12700  67.67500  45.30800  1.000 69.74547  ?  105  GLU   A O   1 
ATOM   861   C  CB  . GLU   A 1 105  ? -65.03500  65.96500  46.54400  1.000 73.03966  ?  105  GLU   A CB  1 
ATOM   862   C  CG  . GLU   A 1 105  ? -66.49300  66.35100  46.70300  1.000 93.27431  ?  105  GLU   A CG  1 
ATOM   863   C  CD  . GLU   A 1 105  ? -67.12100  65.79400  47.96300  1.000 110.32569 ?  105  GLU   A CD  1 
ATOM   864   O  OE1 . GLU   A 1 105  ? -66.38100  65.55100  48.93800  1.000 109.20658 ?  105  GLU   A OE1 1 
ATOM   865   O  OE2 . GLU   A 1 105  ? -68.35700  65.60500  47.98000  1.000 105.17826 -1 105  GLU   A OE2 1 
ATOM   866   N  N   . HIS   A 1 106  ? -62.39300  65.94100  44.07000  1.000 84.82874  ?  106  HIS   A N   1 
ATOM   867   C  CA  . HIS   A 1 106  ? -61.11100  66.54100  43.73300  1.000 89.70051  ?  106  HIS   A CA  1 
ATOM   868   C  C   . HIS   A 1 106  ? -60.84000  66.28800  42.25400  1.000 84.51886  ?  106  HIS   A C   1 
ATOM   869   O  O   . HIS   A 1 106  ? -61.68100  65.73900  41.53300  1.000 82.55201  ?  106  HIS   A O   1 
ATOM   870   C  CB  . HIS   A 1 106  ? -59.99500  65.98700  44.62700  1.000 87.64317  ?  106  HIS   A CB  1 
ATOM   871   C  CG  . HIS   A 1 106  ? -60.30400  66.05900  46.09100  1.000 87.15116  ?  106  HIS   A CG  1 
ATOM   872   N  ND1 . HIS   A 1 106  ? -60.72500  67.21800  46.70800  1.000 81.22313  ?  106  HIS   A ND1 1 
ATOM   873   C  CD2 . HIS   A 1 106  ? -60.26900  65.11100  47.05800  1.000 76.83561  ?  106  HIS   A CD2 1 
ATOM   874   C  CE1 . HIS   A 1 106  ? -60.92700  66.98300  47.99200  1.000 90.42694  ?  106  HIS   A CE1 1 
ATOM   875   N  NE2 . HIS   A 1 106  ? -60.65800  65.71200  48.23000  1.000 91.45454  ?  106  HIS   A NE2 1 
ATOM   876   N  N   . VAL   A 1 107  ? -59.65300  66.68000  41.80200  1.000 71.16400  ?  107  VAL   A N   1 
ATOM   877   C  CA  . VAL   A 1 107  ? -59.33700  66.72400  40.37800  1.000 49.09285  ?  107  VAL   A CA  1 
ATOM   878   C  C   . VAL   A 1 107  ? -58.66600  65.41500  39.97200  1.000 61.32902  ?  107  VAL   A C   1 
ATOM   879   O  O   . VAL   A 1 107  ? -57.49100  65.18900  40.27600  1.000 77.83237  ?  107  VAL   A O   1 
ATOM   880   C  CB  . VAL   A 1 107  ? -58.45000  67.92700  40.04300  1.000 49.40672  ?  107  VAL   A CB  1 
ATOM   881   C  CG1 . VAL   A 1 107  ? -58.48200  68.20100  38.55200  1.000 76.58824  ?  107  VAL   A CG1 1 
ATOM   882   C  CG2 . VAL   A 1 107  ? -58.90100  69.15100  40.82700  1.000 62.44388  ?  107  VAL   A CG2 1 
ATOM   883   N  N   . ASP   A 1 108  ? -59.41700  64.56200  39.27400  1.000 66.70559  ?  108  ASP   A N   1 
ATOM   884   C  CA  . ASP   A 1 108  ? -58.90000  63.33400  38.66500  1.000 60.31285  ?  108  ASP   A CA  1 
ATOM   885   C  C   . ASP   A 1 108  ? -58.18900  62.45300  39.69000  1.000 52.18742  ?  108  ASP   A C   1 
ATOM   886   O  O   . ASP   A 1 108  ? -57.09300  61.93900  39.45700  1.000 62.26283  ?  108  ASP   A O   1 
ATOM   887   C  CB  . ASP   A 1 108  ? -57.98300  63.65800  37.48400  1.000 65.90355  ?  108  ASP   A CB  1 
ATOM   888   C  CG  . ASP   A 1 108  ? -58.53600  64.76800  36.61300  1.000 67.97016  ?  108  ASP   A CG  1 
ATOM   889   O  OD1 . ASP   A 1 108  ? -59.77700  64.88400  36.52500  1.000 67.03255  ?  108  ASP   A OD1 1 
ATOM   890   O  OD2 . ASP   A 1 108  ? -57.73600  65.52400  36.02100  1.000 70.99416  -1 108  ASP   A OD2 1 
ATOM   891   N  N   . THR   A 1 109  ? -58.83800  62.27300  40.83600  1.000 67.78216  ?  109  THR   A N   1 
ATOM   892   C  CA  . THR   A 1 109  ? -58.33300  61.46000  41.93600  1.000 69.58062  ?  109  THR   A CA  1 
ATOM   893   C  C   . THR   A 1 109  ? -59.27500  60.29900  42.22600  1.000 69.30472  ?  109  THR   A C   1 
ATOM   894   O  O   . THR   A 1 109  ? -59.47200  59.90700  43.37800  1.000 82.93616  ?  109  THR   A O   1 
ATOM   895   C  CB  . THR   A 1 109  ? -58.13600  62.30300  43.19500  1.000 59.20695  ?  109  THR   A CB  1 
ATOM   896   O  OG1 . THR   A 1 109  ? -59.20700  63.24800  43.31400  1.000 70.57279  ?  109  THR   A OG1 1 
ATOM   897   C  CG2 . THR   A 1 109  ? -56.81700  63.04800  43.14000  1.000 67.74152  ?  109  THR   A CG2 1 
ATOM   898   N  N   . GLY   A 1 110  ? -59.87200  59.73700  41.17600  1.000 74.24436  ?  110  GLY   A N   1 
ATOM   899   C  CA  . GLY   A 1 110  ? -60.89500  58.72700  41.32600  1.000 63.93227  ?  110  GLY   A CA  1 
ATOM   900   C  C   . GLY   A 1 110  ? -60.39500  57.32200  41.03400  1.000 69.66634  ?  110  GLY   A C   1 
ATOM   901   O  O   . GLY   A 1 110  ? -59.32000  57.10800  40.48000  1.000 83.63612  ?  110  GLY   A O   1 
ATOM   902   N  N   . ASP   A 1 111  ? -61.21600  56.35400  41.42400  1.000 65.95495  ?  111  ASP   A N   1 
ATOM   903   C  CA  . ASP   A 1 111  ? -60.88800  54.95200  41.20900  1.000 77.06601  ?  111  ASP   A CA  1 
ATOM   904   C  C   . ASP   A 1 111  ? -60.91200  54.64000  39.71800  1.000 56.35644  ?  111  ASP   A C   1 
ATOM   905   O  O   . ASP   A 1 111  ? -61.95100  54.77200  39.06200  1.000 65.45751  ?  111  ASP   A O   1 
ATOM   906   C  CB  . ASP   A 1 111  ? -61.87000  54.06200  41.96700  1.000 88.11347  ?  111  ASP   A CB  1 
ATOM   907   C  CG  . ASP   A 1 111  ? -61.66600  54.11700  43.46800  1.000 87.36776  ?  111  ASP   A CG  1 
ATOM   908   O  OD1 . ASP   A 1 111  ? -62.28600  54.98000  44.12600  1.000 82.99197  ?  111  ASP   A OD1 1 
ATOM   909   O  OD2 . ASP   A 1 111  ? -60.89000  53.29000  43.98800  1.000 86.76360  -1 111  ASP   A OD2 1 
ATOM   910   N  N   . ILE   A 1 112  ? -59.76100  54.23300  39.18200  1.000 54.53080  ?  112  ILE   A N   1 
ATOM   911   C  CA  . ILE   A 1 112  ? -59.67600  53.90400  37.76600  1.000 63.26047  ?  112  ILE   A CA  1 
ATOM   912   C  C   . ILE   A 1 112  ? -60.53900  52.69200  37.45600  1.000 66.99881  ?  112  ILE   A C   1 
ATOM   913   O  O   . ILE   A 1 112  ? -60.53600  51.69300  38.18700  1.000 61.01032  ?  112  ILE   A O   1 
ATOM   914   C  CB  . ILE   A 1 112  ? -58.21500  53.65300  37.36000  1.000 58.00778  ?  112  ILE   A CB  1 
ATOM   915   C  CG1 . ILE   A 1 112  ? -57.29800  54.74000  37.92200  1.000 50.31433  ?  112  ILE   A CG1 1 
ATOM   916   C  CG2 . ILE   A 1 112  ? -58.08700  53.54600  35.85100  1.000 63.98968  ?  112  ILE   A CG2 1 
ATOM   917   C  CD1 . ILE   A 1 112  ? -55.84100  54.34700  37.91900  1.000 72.15950  ?  112  ILE   A CD1 1 
ATOM   918   N  N   . LEU   A 1 113  ? -61.28900  52.77900  36.35800  1.000 61.70297  ?  113  LEU   A N   1 
ATOM   919   C  CA  . LEU   A 1 113  ? -62.06000  51.65400  35.84700  1.000 48.21676  ?  113  LEU   A CA  1 
ATOM   920   C  C   . LEU   A 1 113  ? -61.32600  50.92300  34.73000  1.000 51.50172  ?  113  LEU   A C   1 
ATOM   921   O  O   . LEU   A 1 113  ? -61.22800  49.69200  34.75000  1.000 49.35660  ?  113  LEU   A O   1 
ATOM   922   C  CB  . LEU   A 1 113  ? -63.43000  52.13400  35.35300  1.000 57.89031  ?  113  LEU   A CB  1 
ATOM   923   C  CG  . LEU   A 1 113  ? -64.29700  52.85300  36.39000  1.000 58.80267  ?  113  LEU   A CG  1 
ATOM   924   C  CD1 . LEU   A 1 113  ? -65.33200  53.73700  35.71700  1.000 55.88649  ?  113  LEU   A CD1 1 
ATOM   925   C  CD2 . LEU   A 1 113  ? -64.97100  51.85200  37.30800  1.000 58.96574  ?  113  LEU   A CD2 1 
ATOM   926   N  N   . VAL   A 1 114  ? -60.79500  51.66100  33.75800  1.000 47.14752  ?  114  VAL   A N   1 
ATOM   927   C  CA  . VAL   A 1 114  ? -60.02500  51.07100  32.67300  1.000 57.08808  ?  114  VAL   A CA  1 
ATOM   928   C  C   . VAL   A 1 114  ? -58.98300  52.09100  32.23500  1.000 62.25527  ?  114  VAL   A C   1 
ATOM   929   O  O   . VAL   A 1 114  ? -59.20800  53.30300  32.30600  1.000 54.83120  ?  114  VAL   A O   1 
ATOM   930   C  CB  . VAL   A 1 114  ? -60.94100  50.62900  31.50500  1.000 56.57098  ?  114  VAL   A CB  1 
ATOM   931   C  CG1 . VAL   A 1 114  ? -61.69800  51.81600  30.93800  1.000 64.46189  ?  114  VAL   A CG1 1 
ATOM   932   C  CG2 . VAL   A 1 114  ? -60.14300  49.90900  30.42200  1.000 59.76473  ?  114  VAL   A CG2 1 
ATOM   933   N  N   . GLN   A 1 115  ? -57.83000  51.58900  31.79300  1.000 53.54620  ?  115  GLN   A N   1 
ATOM   934   C  CA  . GLN   A 1 115  ? -56.67200  52.42400  31.50200  1.000 47.08425  ?  115  GLN   A CA  1 
ATOM   935   C  C   . GLN   A 1 115  ? -55.83000  51.75500  30.42500  1.000 59.94435  ?  115  GLN   A C   1 
ATOM   936   O  O   . GLN   A 1 115  ? -55.49600  50.57200  30.54600  1.000 61.71612  ?  115  GLN   A O   1 
ATOM   937   C  CB  . GLN   A 1 115  ? -55.84300  52.64000  32.77200  1.000 53.70012  ?  115  GLN   A CB  1 
ATOM   938   C  CG  . GLN   A 1 115  ? -55.04300  53.92300  32.81800  1.000 63.73607  ?  115  GLN   A CG  1 
ATOM   939   C  CD  . GLN   A 1 115  ? -54.44300  54.17000  34.19100  1.000 71.39354  ?  115  GLN   A CD  1 
ATOM   940   O  OE1 . GLN   A 1 115  ? -53.89300  53.25900  34.81200  1.000 55.76817  ?  115  GLN   A OE1 1 
ATOM   941   N  NE2 . GLN   A 1 115  ? -54.54500  55.40400  34.67100  1.000 69.99830  ?  115  GLN   A NE2 1 
ATOM   942   N  N   . GLU   A 1 116  ? -55.48800  52.50700  29.38100  1.000 59.92909  ?  116  GLU   A N   1 
ATOM   943   C  CA  . GLU   A 1 116  ? -54.64600  52.01600  28.30000  1.000 63.41578  ?  116  GLU   A CA  1 
ATOM   944   C  C   . GLU   A 1 116  ? -53.41300  52.90300  28.16900  1.000 64.85480  ?  116  GLU   A C   1 
ATOM   945   O  O   . GLU   A 1 116  ? -53.42500  54.07300  28.55600  1.000 55.23404  ?  116  GLU   A O   1 
ATOM   946   C  CB  . GLU   A 1 116  ? -55.41600  51.96700  26.96900  1.000 59.34586  ?  116  GLU   A CB  1 
ATOM   947   C  CG  . GLU   A 1 116  ? -54.66300  51.29300  25.82900  1.000 65.04197  ?  116  GLU   A CG  1 
ATOM   948   C  CD  . GLU   A 1 116  ? -55.57300  50.85000  24.70200  1.000 98.00837  ?  116  GLU   A CD  1 
ATOM   949   O  OE1 . GLU   A 1 116  ? -56.33100  51.69500  24.18000  1.000 92.62879  ?  116  GLU   A OE1 1 
ATOM   950   O  OE2 . GLU   A 1 116  ? -55.52700  49.65500  24.33700  1.000 105.66903 -1 116  GLU   A OE2 1 
ATOM   951   N  N   . GLU   A 1 117  ? -52.34000  52.32900  27.62400  1.000 57.57318  ?  117  GLU   A N   1 
ATOM   952   C  CA  . GLU   A 1 117  ? -51.05800  53.01100  27.49000  1.000 51.62347  ?  117  GLU   A CA  1 
ATOM   953   C  C   . GLU   A 1 117  ? -50.88100  53.47000  26.04600  1.000 64.04809  ?  117  GLU   A C   1 
ATOM   954   O  O   . GLU   A 1 117  ? -50.75900  52.64400  25.13600  1.000 78.21705  ?  117  GLU   A O   1 
ATOM   955   C  CB  . GLU   A 1 117  ? -49.91700  52.08900  27.91400  1.000 61.37917  ?  117  GLU   A CB  1 
ATOM   956   C  CG  . GLU   A 1 117  ? -48.79100  52.78600  28.65500  1.000 78.18847  ?  117  GLU   A CG  1 
ATOM   957   C  CD  . GLU   A 1 117  ? -47.54900  51.92300  28.76300  1.000 98.90461  ?  117  GLU   A CD  1 
ATOM   958   O  OE1 . GLU   A 1 117  ? -47.47300  51.10600  29.70600  1.000 109.80615 ?  117  GLU   A OE1 1 
ATOM   959   O  OE2 . GLU   A 1 117  ? -46.65000  52.06100  27.90600  1.000 96.29945  -1 117  GLU   A OE2 1 
ATOM   960   N  N   . ILE   A 1 118  ? -50.85800  54.78500  25.84000  1.000 63.67986  ?  118  ILE   A N   1 
ATOM   961   C  CA  . ILE   A 1 118  ? -50.61000  55.35400  24.52200  1.000 65.70212  ?  118  ILE   A CA  1 
ATOM   962   C  C   . ILE   A 1 118  ? -49.10900  55.57700  24.35300  1.000 62.05846  ?  118  ILE   A C   1 
ATOM   963   O  O   . ILE   A 1 118  ? -48.35400  55.66400  25.32500  1.000 52.78915  ?  118  ILE   A O   1 
ATOM   964   C  CB  . ILE   A 1 118  ? -51.40900  56.66100  24.31700  1.000 52.32098  ?  118  ILE   A CB  1 
ATOM   965   C  CG1 . ILE   A 1 118  ? -51.51600  57.01300  22.83100  1.000 77.78387  ?  118  ILE   A CG1 1 
ATOM   966   C  CG2 . ILE   A 1 118  ? -50.77100  57.80900  25.08000  1.000 63.27898  ?  118  ILE   A CG2 1 
ATOM   967   C  CD1 . ILE   A 1 118  ? -51.98300  55.86800  21.95600  1.000 89.39078  ?  118  ILE   A CD1 1 
ATOM   968   N  N   . ALA   A 1 119  ? -48.66400  55.65200  23.09800  1.000 62.04902  ?  119  ALA   A N   1 
ATOM   969   C  CA  . ALA   A 1 119  ? -47.25000  55.82200  22.77200  1.000 47.96031  ?  119  ALA   A CA  1 
ATOM   970   C  C   . ALA   A 1 119  ? -47.09100  56.96700  21.78200  1.000 52.10624  ?  119  ALA   A C   1 
ATOM   971   O  O   . ALA   A 1 119  ? -47.60600  56.89700  20.66100  1.000 60.31191  ?  119  ALA   A O   1 
ATOM   972   C  CB  . ALA   A 1 119  ? -46.65800  54.53300  22.19500  1.000 42.39220  ?  119  ALA   A CB  1 
ATOM   973   N  N   . PHE   A 1 120  ? -46.37600  58.01100  22.19200  1.000 42.79663  ?  120  PHE   A N   1 
ATOM   974   C  CA  . PHE   A 1 120  ? -46.06100  59.13900  21.32700  1.000 47.82560  ?  120  PHE   A CA  1 
ATOM   975   C  C   . PHE   A 1 120  ? -44.66000  58.97300  20.74800  1.000 57.54428  ?  120  PHE   A C   1 
ATOM   976   O  O   . PHE   A 1 120  ? -43.76400  58.42000  21.39200  1.000 73.23593  ?  120  PHE   A O   1 
ATOM   977   C  CB  . PHE   A 1 120  ? -46.15400  60.46500  22.08800  1.000 40.75358  ?  120  PHE   A CB  1 
ATOM   978   C  CG  . PHE   A 1 120  ? -47.50900  60.73700  22.67800  1.000 41.72282  ?  120  PHE   A CG  1 
ATOM   979   C  CD1 . PHE   A 1 120  ? -48.66000  60.38000  21.99800  1.000 55.32999  ?  120  PHE   A CD1 1 
ATOM   980   C  CD2 . PHE   A 1 120  ? -47.63100  61.35200  23.91500  1.000 42.48769  ?  120  PHE   A CD2 1 
ATOM   981   C  CE1 . PHE   A 1 120  ? -49.90700  60.63000  22.53900  1.000 61.57272  ?  120  PHE   A CE1 1 
ATOM   982   C  CE2 . PHE   A 1 120  ? -48.87500  61.60300  24.46000  1.000 41.12761  ?  120  PHE   A CE2 1 
ATOM   983   C  CZ  . PHE   A 1 120  ? -50.01400  61.24200  23.77200  1.000 45.92375  ?  120  PHE   A CZ  1 
ATOM   984   N  N   . ALA   A 1 121  ? -44.47800  59.46100  19.52500  1.000 44.75550  ?  121  ALA   A N   1 
ATOM   985   C  CA  . ALA   A 1 121  ? -43.22100  59.32600  18.80600  1.000 46.28766  ?  121  ALA   A CA  1 
ATOM   986   C  C   . ALA   A 1 121  ? -42.37600  60.58600  18.94800  1.000 62.81878  ?  121  ALA   A C   1 
ATOM   987   O  O   . ALA   A 1 121  ? -42.86600  61.65600  19.31300  1.000 66.81974  ?  121  ALA   A O   1 
ATOM   988   C  CB  . ALA   A 1 121  ? -43.47000  59.02800  17.32600  1.000 49.69390  ?  121  ALA   A CB  1 
ATOM   989   N  N   . ASP   A 1 122  ? -41.08200  60.44200  18.64600  1.000 61.70511  ?  122  ASP   A N   1 
ATOM   990   C  CA  . ASP   A 1 122  ? -40.17000  61.57300  18.77500  1.000 54.63230  ?  122  ASP   A CA  1 
ATOM   991   C  C   . ASP   A 1 122  ? -40.35700  62.57500  17.64600  1.000 52.52917  ?  122  ASP   A C   1 
ATOM   992   O  O   . ASP   A 1 122  ? -40.10100  63.77000  17.83000  1.000 48.74412  ?  122  ASP   A O   1 
ATOM   993   C  CB  . ASP   A 1 122  ? -38.72400  61.08300  18.81600  1.000 51.60819  ?  122  ASP   A CB  1 
ATOM   994   C  CG  . ASP   A 1 122  ? -38.47500  60.09400  19.93700  1.000 73.32109  ?  122  ASP   A CG  1 
ATOM   995   O  OD1 . ASP   A 1 122  ? -38.95900  58.94400  19.84400  1.000 71.64347  ?  122  ASP   A OD1 1 
ATOM   996   O  OD2 . ASP   A 1 122  ? -37.78500  60.46400  20.91000  1.000 78.51143  -1 122  ASP   A OD2 1 
ATOM   997   N  N   . GLU   A 1 123  ? -40.80000  62.11500  16.48100  1.000 46.91168  ?  123  GLU   A N   1 
ATOM   998   C  CA  . GLU   A 1 123  ? -41.05800  62.99900  15.35700  1.000 56.02926  ?  123  GLU   A CA  1 
ATOM   999   C  C   . GLU   A 1 123  ? -42.50200  63.47500  15.30400  1.000 44.53442  ?  123  GLU   A C   1 
ATOM   1000  O  O   . GLU   A 1 123  ? -42.90400  64.08700  14.31000  1.000 48.63262  ?  123  GLU   A O   1 
ATOM   1001  C  CB  . GLU   A 1 123  ? -40.67900  62.30600  14.04700  1.000 54.62521  ?  123  GLU   A CB  1 
ATOM   1002  C  CG  . GLU   A 1 123  ? -39.18100  62.10100  13.88500  1.000 63.16023  ?  123  GLU   A CG  1 
ATOM   1003  C  CD  . GLU   A 1 123  ? -38.38500  63.38800  14.07700  1.000 77.91864  ?  123  GLU   A CD  1 
ATOM   1004  O  OE1 . GLU   A 1 123  ? -38.73700  64.41600  13.45900  1.000 63.80342  ?  123  GLU   A OE1 1 
ATOM   1005  O  OE2 . GLU   A 1 123  ? -37.40300  63.37000  14.84900  1.000 78.74526  -1 123  GLU   A OE2 1 
ATOM   1006  N  N   . ASP   A 1 124  ? -43.28500  63.21300  16.34600  1.000 50.03171  ?  124  ASP   A N   1 
ATOM   1007  C  CA  . ASP   A 1 124  ? -44.66600  63.66500  16.41700  1.000 47.82530  ?  124  ASP   A CA  1 
ATOM   1008  C  C   . ASP   A 1 124  ? -44.72700  65.08200  16.96900  1.000 52.94605  ?  124  ASP   A C   1 
ATOM   1009  O  O   . ASP   A 1 124  ? -44.02700  65.41600  17.92900  1.000 50.20515  ?  124  ASP   A O   1 
ATOM   1010  C  CB  . ASP   A 1 124  ? -45.49400  62.73700  17.30900  1.000 44.66184  ?  124  ASP   A CB  1 
ATOM   1011  C  CG  . ASP   A 1 124  ? -46.10200  61.57600  16.55000  1.000 65.09553  ?  124  ASP   A CG  1 
ATOM   1012  O  OD1 . ASP   A 1 124  ? -46.23600  61.66600  15.31000  1.000 79.33417  ?  124  ASP   A OD1 1 
ATOM   1013  O  OD2 . ASP   A 1 124  ? -46.44400  60.56700  17.20300  1.000 52.82837  -1 124  ASP   A OD2 1 
ATOM   1014  N  N   . THR   A 1 125  ? -45.57100  65.91100  16.36100  1.000 42.27908  ?  125  THR   A N   1 
ATOM   1015  C  CA  . THR   A 1 125  ? -45.84000  67.22200  16.92600  1.000 41.03474  ?  125  THR   A CA  1 
ATOM   1016  C  C   . THR   A 1 125  ? -46.78800  67.08800  18.11500  1.000 49.46257  ?  125  THR   A C   1 
ATOM   1017  O  O   . THR   A 1 125  ? -47.42300  66.04900  18.32600  1.000 43.93075  ?  125  THR   A O   1 
ATOM   1018  C  CB  . THR   A 1 125  ? -46.43000  68.16200  15.87500  1.000 50.83305  ?  125  THR   A CB  1 
ATOM   1019  O  OG1 . THR   A 1 125  ? -47.83800  67.92600  15.74600  1.000 50.41718  ?  125  THR   A OG1 1 
ATOM   1020  C  CG2 . THR   A 1 125  ? -45.76500  67.93900  14.53200  1.000 54.33897  ?  125  THR   A CG2 1 
ATOM   1021  N  N   . LEU   A 1 126  ? -46.87500  68.15700  18.90900  1.000 41.11760  ?  126  LEU   A N   1 
ATOM   1022  C  CA  . LEU   A 1 126  ? -47.78000  68.13700  20.05100  1.000 38.86305  ?  126  LEU   A CA  1 
ATOM   1023  C  C   . LEU   A 1 126  ? -49.22700  68.00200  19.59800  1.000 43.47566  ?  126  LEU   A C   1 
ATOM   1024  O  O   . LEU   A 1 126  ? -50.02100  67.30300  20.23800  1.000 49.84413  ?  126  LEU   A O   1 
ATOM   1025  C  CB  . LEU   A 1 126  ? -47.59100  69.39200  20.90100  1.000 51.90840  ?  126  LEU   A CB  1 
ATOM   1026  C  CG  . LEU   A 1 126  ? -46.55000  69.25400  22.01500  1.000 41.58131  ?  126  LEU   A CG  1 
ATOM   1027  C  CD1 . LEU   A 1 126  ? -46.41300  70.55700  22.77000  1.000 44.18007  ?  126  LEU   A CD1 1 
ATOM   1028  C  CD2 . LEU   A 1 126  ? -46.91000  68.11800  22.96300  1.000 39.31087  ?  126  LEU   A CD2 1 
ATOM   1029  N  N   . LEU   A 1 127  ? -49.58300  68.65000  18.48400  1.000 47.61095  ?  127  LEU   A N   1 
ATOM   1030  C  CA  . LEU   A 1 127  ? -50.93400  68.50800  17.94800  1.000 46.16185  ?  127  LEU   A CA  1 
ATOM   1031  C  C   . LEU   A 1 127  ? -51.22700  67.06200  17.56900  1.000 39.64827  ?  127  LEU   A C   1 
ATOM   1032  O  O   . LEU   A 1 127  ? -52.32700  66.55700  17.82200  1.000 43.56065  ?  127  LEU   A O   1 
ATOM   1033  C  CB  . LEU   A 1 127  ? -51.12100  69.42900  16.74200  1.000 33.04702  ?  127  LEU   A CB  1 
ATOM   1034  C  CG  . LEU   A 1 127  ? -51.07900  70.93000  17.03700  1.000 41.55155  ?  127  LEU   A CG  1 
ATOM   1035  C  CD1 . LEU   A 1 127  ? -51.34600  71.73800  15.77700  1.000 33.50014  ?  127  LEU   A CD1 1 
ATOM   1036  C  CD2 . LEU   A 1 127  ? -52.06800  71.29700  18.13200  1.000 43.61292  ?  127  LEU   A CD2 1 
ATOM   1037  N  N   . ASP   A 1 128  ? -50.25500  66.37800  16.96500  1.000 41.52351  ?  128  ASP   A N   1 
ATOM   1038  C  CA  . ASP   A 1 128  ? -50.43700  64.96400  16.65400  1.000 53.42619  ?  128  ASP   A CA  1 
ATOM   1039  C  C   . ASP   A 1 128  ? -50.66500  64.15200  17.92100  1.000 56.98540  ?  128  ASP   A C   1 
ATOM   1040  O  O   . ASP   A 1 128  ? -51.46500  63.20800  17.92900  1.000 62.49815  ?  128  ASP   A O   1 
ATOM   1041  C  CB  . ASP   A 1 128  ? -49.22500  64.43400  15.88900  1.000 50.76078  ?  128  ASP   A CB  1 
ATOM   1042  C  CG  . ASP   A 1 128  ? -48.91600  65.24800  14.64900  1.000 63.27565  ?  128  ASP   A CG  1 
ATOM   1043  O  OD1 . ASP   A 1 128  ? -49.74400  66.10300  14.26900  1.000 75.84860  ?  128  ASP   A OD1 1 
ATOM   1044  O  OD2 . ASP   A 1 128  ? -47.83500  65.03900  14.06100  1.000 74.48078  -1 128  ASP   A OD2 1 
ATOM   1045  N  N   . CYS   A 1 129  ? -49.97300  64.50900  19.00700  1.000 52.09318  ?  129  CYS   A N   1 
ATOM   1046  C  CA  . CYS   A 1 129  ? -50.16800  63.80700  20.27200  1.000 45.53142  ?  129  CYS   A CA  1 
ATOM   1047  C  C   . CYS   A 1 129  ? -51.55800  64.07000  20.83900  1.000 51.77739  ?  129  CYS   A C   1 
ATOM   1048  O  O   . CYS   A 1 129  ? -52.18200  63.16400  21.40400  1.000 46.66941  ?  129  CYS   A O   1 
ATOM   1049  C  CB  . CYS   A 1 129  ? -49.09100  64.21800  21.27600  1.000 42.73870  ?  129  CYS   A CB  1 
ATOM   1050  S  SG  . CYS   A 1 129  ? -47.40500  63.76800  20.80300  1.000 61.17231  ?  129  CYS   A SG  1 
ATOM   1051  N  N   . TYR   A 1 130  ? -52.05800  65.30300  20.70400  1.000 42.41993  ?  130  TYR   A N   1 
ATOM   1052  C  CA  . TYR   A 1 130  ? -53.42000  65.59700  21.14200  1.000 38.67065  ?  130  TYR   A CA  1 
ATOM   1053  C  C   . TYR   A 1 130  ? -54.42300  64.71600  20.40400  1.000 42.56728  ?  130  TYR   A C   1 
ATOM   1054  O  O   . TYR   A 1 130  ? -55.31400  64.11800  21.01700  1.000 41.54413  ?  130  TYR   A O   1 
ATOM   1055  C  CB  . TYR   A 1 130  ? -53.75500  67.07600  20.92200  1.000 33.05347  ?  130  TYR   A CB  1 
ATOM   1056  C  CG  . TYR   A 1 130  ? -52.81000  68.06600  21.57100  1.000 41.30752  ?  130  TYR   A CG  1 
ATOM   1057  C  CD1 . TYR   A 1 130  ? -51.98200  67.69300  22.62200  1.000 50.14125  ?  130  TYR   A CD1 1 
ATOM   1058  C  CD2 . TYR   A 1 130  ? -52.74700  69.38000  21.12500  1.000 37.66263  ?  130  TYR   A CD2 1 
ATOM   1059  C  CE1 . TYR   A 1 130  ? -51.11600  68.60100  23.20500  1.000 53.84794  ?  130  TYR   A CE1 1 
ATOM   1060  C  CE2 . TYR   A 1 130  ? -51.88700  70.29300  21.70200  1.000 39.40258  ?  130  TYR   A CE2 1 
ATOM   1061  C  CZ  . TYR   A 1 130  ? -51.07300  69.89800  22.74100  1.000 47.43930  ?  130  TYR   A CZ  1 
ATOM   1062  O  OH  . TYR   A 1 130  ? -50.21300  70.80400  23.31800  1.000 56.60526  ?  130  TYR   A OH  1 
ATOM   1063  N  N   . ASN   A 1 131  ? -54.28300  64.61700  19.07900  1.000 46.10460  ?  131  ASN   A N   1 
ATOM   1064  C  CA  . ASN   A 1 131  ? -55.21100  63.81000  18.29200  1.000 46.88182  ?  131  ASN   A CA  1 
ATOM   1065  C  C   . ASN   A 1 131  ? -55.13400  62.34200  18.69100  1.000 47.52576  ?  131  ASN   A C   1 
ATOM   1066  O  O   . ASN   A 1 131  ? -56.16300  61.68900  18.90200  1.000 59.40617  ?  131  ASN   A O   1 
ATOM   1067  C  CB  . ASN   A 1 131  ? -54.91600  63.97800  16.80100  1.000 48.67891  ?  131  ASN   A CB  1 
ATOM   1068  C  CG  . ASN   A 1 131  ? -55.37500  65.31800  16.26100  1.000 48.37286  ?  131  ASN   A CG  1 
ATOM   1069  O  OD1 . ASN   A 1 131  ? -56.40800  65.84600  16.66900  1.000 50.26661  ?  131  ASN   A OD1 1 
ATOM   1070  N  ND2 . ASN   A 1 131  ? -54.59900  65.87900  15.34000  1.000 64.42112  ?  131  ASN   A ND2 1 
ATOM   1071  N  N   . LYS   A 1 132  ? -53.91700  61.80500  18.80000  1.000 32.68488  ?  132  LYS   A N   1 
ATOM   1072  C  CA  . LYS   A 1 132  ? -53.75700  60.40200  19.16400  1.000 45.49079  ?  132  LYS   A CA  1 
ATOM   1073  C  C   . LYS   A 1 132  ? -54.36900  60.11100  20.52700  1.000 50.01201  ?  132  LYS   A C   1 
ATOM   1074  O  O   . LYS   A 1 132  ? -54.98900  59.05900  20.72700  1.000 54.05535  ?  132  LYS   A O   1 
ATOM   1075  C  CB  . LYS   A 1 132  ? -52.27700  60.02400  19.15300  1.000 48.13165  ?  132  LYS   A CB  1 
ATOM   1076  C  CG  . LYS   A 1 132  ? -52.00200  58.63200  18.62500  1.000 55.31029  ?  132  LYS   A CG  1 
ATOM   1077  C  CD  . LYS   A 1 132  ? -50.51900  58.42800  18.37600  1.000 70.92888  ?  132  LYS   A CD  1 
ATOM   1078  C  CE  . LYS   A 1 132  ? -50.03100  59.28000  17.21600  1.000 70.52398  ?  132  LYS   A CE  1 
ATOM   1079  N  NZ  . LYS   A 1 132  ? -48.56300  59.13700  17.00300  1.000 75.79825  ?  132  LYS   A NZ  1 
ATOM   1080  N  N   . ALA   A 1 133  ? -54.21200  61.03500  21.47600  1.000 49.87728  ?  133  ALA   A N   1 
ATOM   1081  C  CA  . ALA   A 1 133  ? -54.74600  60.82300  22.81600  1.000 48.04321  ?  133  ALA   A CA  1 
ATOM   1082  C  C   . ALA   A 1 133  ? -56.27000  60.82300  22.81000  1.000 46.91968  ?  133  ALA   A C   1 
ATOM   1083  O  O   . ALA   A 1 133  ? -56.90200  59.92500  23.38100  1.000 46.81648  ?  133  ALA   A O   1 
ATOM   1084  C  CB  . ALA   A 1 133  ? -54.20900  61.89200  23.76800  1.000 33.00553  ?  133  ALA   A CB  1 
ATOM   1085  N  N   . ASN   A 1 134  ? -56.88000  61.82400  22.16500  1.000 51.10123  ?  134  ASN   A N   1 
ATOM   1086  C  CA  . ASN   A 1 134  ? -58.33700  61.93200  22.16600  1.000 49.34682  ?  134  ASN   A CA  1 
ATOM   1087  C  C   . ASN   A 1 134  ? -58.98900  60.70000  21.55000  1.000 56.62530  ?  134  ASN   A C   1 
ATOM   1088  O  O   . ASN   A 1 134  ? -60.03300  60.24000  22.02600  1.000 69.92684  ?  134  ASN   A O   1 
ATOM   1089  C  CB  . ASN   A 1 134  ? -58.77700  63.19500  21.42500  1.000 42.86031  ?  134  ASN   A CB  1 
ATOM   1090  C  CG  . ASN   A 1 134  ? -58.45200  64.46600  22.18900  1.000 54.98148  ?  134  ASN   A CG  1 
ATOM   1091  O  OD1 . ASN   A 1 134  ? -58.78500  64.59800  23.36700  1.000 52.28544  ?  134  ASN   A OD1 1 
ATOM   1092  N  ND2 . ASN   A 1 134  ? -57.81200  65.41500  21.51500  1.000 63.53233  ?  134  ASN   A ND2 1 
ATOM   1093  N  N   . GLN   A 1 135  ? -58.39300  60.15200  20.48800  1.000 41.68644  ?  135  GLN   A N   1 
ATOM   1094  C  CA  . GLN   A 1 135  ? -58.91600  58.92400  19.89900  1.000 37.37978  ?  135  GLN   A CA  1 
ATOM   1095  C  C   . GLN   A 1 135  ? -58.90500  57.78200  20.90700  1.000 49.49168  ?  135  GLN   A C   1 
ATOM   1096  O  O   . GLN   A 1 135  ? -59.91500  57.09500  21.09500  1.000 71.02644  ?  135  GLN   A O   1 
ATOM   1097  C  CB  . GLN   A 1 135  ? -58.10400  58.54400  18.66300  1.000 52.51294  ?  135  GLN   A CB  1 
ATOM   1098  C  CG  . GLN   A 1 135  ? -58.25400  59.49000  17.49300  1.000 57.91354  ?  135  GLN   A CG  1 
ATOM   1099  C  CD  . GLN   A 1 135  ? -57.37000  59.09600  16.33000  1.000 73.79584  ?  135  GLN   A CD  1 
ATOM   1100  O  OE1 . GLN   A 1 135  ? -57.30800  57.92400  15.95600  1.000 70.96506  ?  135  GLN   A OE1 1 
ATOM   1101  N  NE2 . GLN   A 1 135  ? -56.67800  60.07100  15.75200  1.000 75.01692  ?  135  GLN   A NE2 1 
ATOM   1102  N  N   . ALA   A 1 136  ? -57.76800  57.57600  21.57700  1.000 47.34550  ?  136  ALA   A N   1 
ATOM   1103  C  CA  . ALA   A 1 136  ? -57.63000  56.45700  22.50600  1.000 44.54837  ?  136  ALA   A CA  1 
ATOM   1104  C  C   . ALA   A 1 136  ? -58.70000  56.48500  23.59600  1.000 49.69108  ?  136  ALA   A C   1 
ATOM   1105  O  O   . ALA   A 1 136  ? -59.27600  55.44300  23.93100  1.000 54.58841  ?  136  ALA   A O   1 
ATOM   1106  C  CB  . ALA   A 1 136  ? -56.23300  56.47000  23.12600  1.000 44.98213  ?  136  ALA   A CB  1 
ATOM   1107  N  N   . ILE   A 1 137  ? -58.97600  57.66200  24.16700  1.000 40.35002  ?  137  ILE   A N   1 
ATOM   1108  C  CA  . ILE   A 1 137  ? -59.98200  57.73400  25.22400  1.000 49.21609  ?  137  ILE   A CA  1 
ATOM   1109  C  C   . ILE   A 1 137  ? -61.37500  57.46900  24.66400  1.000 50.24064  ?  137  ILE   A C   1 
ATOM   1110  O  O   . ILE   A 1 137  ? -62.23700  56.92200  25.36400  1.000 57.08507  ?  137  ILE   A O   1 
ATOM   1111  C  CB  . ILE   A 1 137  ? -59.90300  59.08600  25.96600  1.000 45.63144  ?  137  ILE   A CB  1 
ATOM   1112  C  CG1 . ILE   A 1 137  ? -60.56600  58.98000  27.34100  1.000 40.84049  ?  137  ILE   A CG1 1 
ATOM   1113  C  CG2 . ILE   A 1 137  ? -60.54700  60.20500  25.16500  1.000 53.18188  ?  137  ILE   A CG2 1 
ATOM   1114  C  CD1 . ILE   A 1 137  ? -59.97500  57.90900  28.22000  1.000 42.91939  ?  137  ILE   A CD1 1 
ATOM   1115  N  N   . GLU   A 1 138  ? -61.61700  57.82300  23.39800  1.000 45.21594  ?  138  GLU   A N   1 
ATOM   1116  C  CA  . GLU   A 1 138  ? -62.91100  57.54700  22.78600  1.000 50.28129  ?  138  GLU   A CA  1 
ATOM   1117  C  C   . GLU   A 1 138  ? -63.05100  56.08600  22.38100  1.000 42.73543  ?  138  GLU   A C   1 
ATOM   1118  O  O   . GLU   A 1 138  ? -64.14800  55.52500  22.47500  1.000 58.53460  ?  138  GLU   A O   1 
ATOM   1119  C  CB  . GLU   A 1 138  ? -63.13200  58.46000  21.57700  1.000 37.82770  ?  138  GLU   A CB  1 
ATOM   1120  C  CG  . GLU   A 1 138  ? -63.18600  59.93900  21.93400  1.000 50.07858  ?  138  GLU   A CG  1 
ATOM   1121  C  CD  . GLU   A 1 138  ? -63.33800  60.83500  20.72000  1.000 56.69491  ?  138  GLU   A CD  1 
ATOM   1122  O  OE1 . GLU   A 1 138  ? -63.27600  60.31800  19.58600  1.000 66.37988  ?  138  GLU   A OE1 1 
ATOM   1123  O  OE2 . GLU   A 1 138  ? -63.51400  62.05900  20.90100  1.000 63.12308  -1 138  GLU   A OE2 1 
ATOM   1124  N  N   . GLU   A 1 139  ? -61.96300  55.45300  21.94100  1.000 43.58507  ?  139  GLU   A N   1 
ATOM   1125  C  CA  . GLU   A 1 139  ? -62.01700  54.02600  21.63900  1.000 42.71423  ?  139  GLU   A CA  1 
ATOM   1126  C  C   . GLU   A 1 139  ? -62.11100  53.19800  22.91400  1.000 57.81836  ?  139  GLU   A C   1 
ATOM   1127  O  O   . GLU   A 1 139  ? -62.83800  52.19700  22.95600  1.000 64.26396  ?  139  GLU   A O   1 
ATOM   1128  C  CB  . GLU   A 1 139  ? -60.79400  53.61300  20.82400  1.000 43.29481  ?  139  GLU   A CB  1 
ATOM   1129  C  CG  . GLU   A 1 139  ? -60.54000  54.47900  19.60300  1.000 66.64073  ?  139  GLU   A CG  1 
ATOM   1130  C  CD  . GLU   A 1 139  ? -61.45800  54.14900  18.44600  1.000 93.28607  ?  139  GLU   A CD  1 
ATOM   1131  O  OE1 . GLU   A 1 139  ? -61.47800  52.97500  18.02200  1.000 94.61159  ?  139  GLU   A OE1 1 
ATOM   1132  O  OE2 . GLU   A 1 139  ? -62.15600  55.06300  17.95600  1.000 92.59904  -1 139  GLU   A OE2 1 
ATOM   1133  N  N   . LEU   A 1 140  ? -61.37400  53.59200  23.95800  1.000 52.05165  ?  140  LEU   A N   1 
ATOM   1134  C  CA  . LEU   A 1 140  ? -61.46800  52.90200  25.24200  1.000 50.92891  ?  140  LEU   A CA  1 
ATOM   1135  C  C   . LEU   A 1 140  ? -62.89900  52.90200  25.75900  1.000 55.93599  ?  140  LEU   A C   1 
ATOM   1136  O  O   . LEU   A 1 140  ? -63.35300  51.92000  26.36000  1.000 56.22092  ?  140  LEU   A O   1 
ATOM   1137  C  CB  . LEU   A 1 140  ? -60.53700  53.55700  26.26200  1.000 57.40385  ?  140  LEU   A CB  1 
ATOM   1138  C  CG  . LEU   A 1 140  ? -60.12400  52.72500  27.47700  1.000 46.45033  ?  140  LEU   A CG  1 
ATOM   1139  C  CD1 . LEU   A 1 140  ? -59.40300  51.45800  27.04400  1.000 59.53080  ?  140  LEU   A CD1 1 
ATOM   1140  C  CD2 . LEU   A 1 140  ? -59.25500  53.55300  28.41000  1.000 43.55659  ?  140  LEU   A CD2 1 
ATOM   1141  N  N   . PHE   A 1 141  ? -63.62400  53.99900  25.53800  1.000 45.22505  ?  141  PHE   A N   1 
ATOM   1142  C  CA  . PHE   A 1 141  ? -65.03000  54.04900  25.91700  1.000 50.10663  ?  141  PHE   A CA  1 
ATOM   1143  C  C   . PHE   A 1 141  ? -65.84700  53.05400  25.10500  1.000 55.24554  ?  141  PHE   A C   1 
ATOM   1144  O  O   . PHE   A 1 141  ? -66.57000  52.22200  25.66400  1.000 62.06522  ?  141  PHE   A O   1 
ATOM   1145  C  CB  . PHE   A 1 141  ? -65.56700  55.46800  25.73300  1.000 43.03297  ?  141  PHE   A CB  1 
ATOM   1146  C  CG  . PHE   A 1 141  ? -66.92100  55.68500  26.33600  1.000 51.12638  ?  141  PHE   A CG  1 
ATOM   1147  C  CD1 . PHE   A 1 141  ? -67.05300  56.10800  27.64900  1.000 60.74803  ?  141  PHE   A CD1 1 
ATOM   1148  C  CD2 . PHE   A 1 141  ? -68.06600  55.46400  25.59100  1.000 44.34278  ?  141  PHE   A CD2 1 
ATOM   1149  C  CE1 . PHE   A 1 141  ? -68.30400  56.31000  28.20500  1.000 57.45598  ?  141  PHE   A CE1 1 
ATOM   1150  C  CE2 . PHE   A 1 141  ? -69.31500  55.66200  26.13900  1.000 57.47545  ?  141  PHE   A CE2 1 
ATOM   1151  C  CZ  . PHE   A 1 141  ? -69.43600  56.08500  27.44800  1.000 58.29488  ?  141  PHE   A CZ  1 
ATOM   1152  N  N   . ILE   A 1 142  ? -65.73700  53.12400  23.77600  1.000 46.72738  ?  142  ILE   A N   1 
ATOM   1153  C  CA  . ILE   A 1 142  ? -66.50100  52.23200  22.90900  1.000 50.48597  ?  142  ILE   A CA  1 
ATOM   1154  C  C   . ILE   A 1 142  ? -66.18900  50.77700  23.22000  1.000 44.76657  ?  142  ILE   A C   1 
ATOM   1155  O  O   . ILE   A 1 142  ? -67.04400  49.89600  23.06300  1.000 58.91485  ?  142  ILE   A O   1 
ATOM   1156  C  CB  . ILE   A 1 142  ? -66.21700  52.57400  21.43300  1.000 41.15985  ?  142  ILE   A CB  1 
ATOM   1157  C  CG1 . ILE   A 1 142  ? -66.70100  53.98800  21.11600  1.000 44.24260  ?  142  ILE   A CG1 1 
ATOM   1158  C  CG2 . ILE   A 1 142  ? -66.87700  51.57500  20.50800  1.000 38.19009  ?  142  ILE   A CG2 1 
ATOM   1159  C  CD1 . ILE   A 1 142  ? -66.23600  54.49000  19.77400  1.000 52.49532  ?  142  ILE   A CD1 1 
ATOM   1160  N  N   . ARG   A 1 143  ? -64.97900  50.50500  23.69600  1.000 45.15108  ?  143  ARG   A N   1 
ATOM   1161  C  CA  . ARG   A 1 143  ? -64.56700  49.13100  23.94800  1.000 55.93570  ?  143  ARG   A CA  1 
ATOM   1162  C  C   . ARG   A 1 143  ? -65.02700  48.62800  25.31000  1.000 55.26082  ?  143  ARG   A C   1 
ATOM   1163  O  O   . ARG   A 1 143  ? -65.20500  47.41800  25.48600  1.000 59.51073  ?  143  ARG   A O   1 
ATOM   1164  C  CB  . ARG   A 1 143  ? -63.04800  49.02800  23.83500  1.000 51.78934  ?  143  ARG   A CB  1 
ATOM   1165  C  CG  . ARG   A 1 143  ? -62.51400  47.64400  23.51900  1.000 66.94162  ?  143  ARG   A CG  1 
ATOM   1166  C  CD  . ARG   A 1 143  ? -60.99700  47.65000  23.61600  1.000 69.82198  ?  143  ARG   A CD  1 
ATOM   1167  N  NE  . ARG   A 1 143  ? -60.45000  48.89800  23.09500  1.000 77.98182  ?  143  ARG   A NE  1 
ATOM   1168  C  CZ  . ARG   A 1 143  ? -59.33600  49.47500  23.52400  1.000 78.64294  ?  143  ARG   A CZ  1 
ATOM   1169  N  NH1 . ARG   A 1 143  ? -58.61200  48.94500  24.49800  1.000 72.44382  ?  143  ARG   A NH1 1 
ATOM   1170  N  NH2 . ARG   A 1 143  ? -58.94400  50.61900  22.97100  1.000 72.44566  ?  143  ARG   A NH2 1 
ATOM   1171  N  N   . GLU   A 1 144  ? -65.23200  49.52500  26.27600  1.000 49.06405  ?  144  GLU   A N   1 
ATOM   1172  C  CA  . GLU   A 1 144  ? -65.47000  49.12100  27.65300  1.000 53.95403  ?  144  GLU   A CA  1 
ATOM   1173  C  C   . GLU   A 1 144  ? -66.79000  49.59700  28.23700  1.000 53.72538  ?  144  GLU   A C   1 
ATOM   1174  O  O   . GLU   A 1 144  ? -67.10600  49.21700  29.37100  1.000 57.06896  ?  144  GLU   A O   1 
ATOM   1175  C  CB  . GLU   A 1 144  ? -64.33000  49.61500  28.56100  1.000 49.14085  ?  144  GLU   A CB  1 
ATOM   1176  C  CG  . GLU   A 1 144  ? -62.93800  49.16600  28.13200  1.000 59.00491  ?  144  GLU   A CG  1 
ATOM   1177  C  CD  . GLU   A 1 144  ? -62.69900  47.68000  28.36100  1.000 67.39230  ?  144  GLU   A CD  1 
ATOM   1178  O  OE1 . GLU   A 1 144  ? -63.29100  47.11300  29.30400  1.000 65.46099  ?  144  GLU   A OE1 1 
ATOM   1179  O  OE2 . GLU   A 1 144  ? -61.91400  47.07700  27.59700  1.000 71.88766  -1 144  GLU   A OE2 1 
ATOM   1180  N  N   . TRP   A 1 145  ? -67.56900  50.40500  27.51400  1.000 52.09067  ?  145  TRP   A N   1 
ATOM   1181  C  CA  . TRP   A 1 145  ? -68.77500  50.98000  28.10500  1.000 45.66623  ?  145  TRP   A CA  1 
ATOM   1182  C  C   . TRP   A 1 145  ? -69.75800  49.89800  28.52800  1.000 52.69386  ?  145  TRP   A C   1 
ATOM   1183  O  O   . TRP   A 1 145  ? -70.37200  49.99300  29.59700  1.000 56.44673  ?  145  TRP   A O   1 
ATOM   1184  C  CB  . TRP   A 1 145  ? -69.44100  51.94800  27.12900  1.000 49.02354  ?  145  TRP   A CB  1 
ATOM   1185  C  CG  . TRP   A 1 145  ? -70.84400  52.29900  27.52600  1.000 55.37570  ?  145  TRP   A CG  1 
ATOM   1186  C  CD1 . TRP   A 1 145  ? -71.98500  51.99900  26.84200  1.000 58.17308  ?  145  TRP   A CD1 1 
ATOM   1187  C  CD2 . TRP   A 1 145  ? -71.25700  53.01200  28.70100  1.000 53.31640  ?  145  TRP   A CD2 1 
ATOM   1188  N  NE1 . TRP   A 1 145  ? -73.08200  52.47800  27.51500  1.000 43.82116  ?  145  TRP   A NE1 1 
ATOM   1189  C  CE2 . TRP   A 1 145  ? -72.66300  53.10500  28.65800  1.000 50.49604  ?  145  TRP   A CE2 1 
ATOM   1190  C  CE3 . TRP   A 1 145  ? -70.57600  53.58000  29.78200  1.000 55.64566  ?  145  TRP   A CE3 1 
ATOM   1191  C  CZ2 . TRP   A 1 145  ? -73.40100  53.74300  29.65500  1.000 62.59064  ?  145  TRP   A CZ2 1 
ATOM   1192  C  CZ3 . TRP   A 1 145  ? -71.31200  54.21500  30.77300  1.000 57.72604  ?  145  TRP   A CZ3 1 
ATOM   1193  C  CH2 . TRP   A 1 145  ? -72.70900  54.29100  30.70100  1.000 51.47459  ?  145  TRP   A CH2 1 
ATOM   1194  N  N   . GLU   A 1 146  ? -69.91900  48.85900  27.70400  1.000 57.90140  ?  146  GLU   A N   1 
ATOM   1195  C  CA  . GLU   A 1 146  ? -70.84200  47.78400  28.05200  1.000 57.96332  ?  146  GLU   A CA  1 
ATOM   1196  C  C   . GLU   A 1 146  ? -70.37900  47.04200  29.29900  1.000 61.00858  ?  146  GLU   A C   1 
ATOM   1197  O  O   . GLU   A 1 146  ? -71.19400  46.70600  30.16700  1.000 61.78652  ?  146  GLU   A O   1 
ATOM   1198  C  CB  . GLU   A 1 146  ? -70.99800  46.81900  26.87700  1.000 68.51740  ?  146  GLU   A CB  1 
ATOM   1199  C  CG  . GLU   A 1 146  ? -71.77200  47.39600  25.70400  1.000 77.33042  ?  146  GLU   A CG  1 
ATOM   1200  C  CD  . GLU   A 1 146  ? -72.44300  46.32600  24.86400  1.000 88.68734  ?  146  GLU   A CD  1 
ATOM   1201  O  OE1 . GLU   A 1 146  ? -72.28000  45.12900  25.18200  1.000 97.41679  ?  146  GLU   A OE1 1 
ATOM   1202  O  OE2 . GLU   A 1 146  ? -73.13500  46.68300  23.88600  1.000 75.68418  -1 146  GLU   A OE2 1 
ATOM   1203  N  N   . ASN   A 1 147  ? -69.07300  46.78200  29.40900  1.000 68.61891  ?  147  ASN   A N   1 
ATOM   1204  C  CA  . ASN   A 1 147  ? -68.55000  46.14900  30.61500  1.000 67.34547  ?  147  ASN   A CA  1 
ATOM   1205  C  C   . ASN   A 1 147  ? -68.67200  47.06600  31.82400  1.000 60.33479  ?  147  ASN   A C   1 
ATOM   1206  O  O   . ASN   A 1 147  ? -68.81800  46.58500  32.95400  1.000 67.42219  ?  147  ASN   A O   1 
ATOM   1207  C  CB  . ASN   A 1 147  ? -67.09300  45.73400  30.40600  1.000 51.42270  ?  147  ASN   A CB  1 
ATOM   1208  C  CG  . ASN   A 1 147  ? -66.94700  44.61700  29.39200  1.000 71.65460  ?  147  ASN   A CG  1 
ATOM   1209  O  OD1 . ASN   A 1 147  ? -67.70500  44.53900  28.42500  1.000 83.10095  ?  147  ASN   A OD1 1 
ATOM   1210  N  ND2 . ASN   A 1 147  ? -65.96900  43.74300  29.60700  1.000 71.94142  ?  147  ASN   A ND2 1 
ATOM   1211  N  N   . ILE   A 1 148  ? -68.62200  48.38000  31.61000  1.000 50.15912  ?  148  ILE   A N   1 
ATOM   1212  C  CA  . ILE   A 1 148  ? -68.77700  49.31600  32.71900  1.000 59.36260  ?  148  ILE   A CA  1 
ATOM   1213  C  C   . ILE   A 1 148  ? -70.22600  49.35000  33.18500  1.000 64.07722  ?  148  ILE   A C   1 
ATOM   1214  O  O   . ILE   A 1 148  ? -70.51600  49.20200  34.37800  1.000 73.87326  ?  148  ILE   A O   1 
ATOM   1215  C  CB  . ILE   A 1 148  ? -68.28700  50.71600  32.31300  1.000 50.90910  ?  148  ILE   A CB  1 
ATOM   1216  C  CG1 . ILE   A 1 148  ? -66.77000  50.72400  32.13200  1.000 45.11996  ?  148  ILE   A CG1 1 
ATOM   1217  C  CG2 . ILE   A 1 148  ? -68.70800  51.74500  33.34800  1.000 50.14529  ?  148  ILE   A CG2 1 
ATOM   1218  C  CD1 . ILE   A 1 148  ? -66.24500  52.01500  31.55500  1.000 41.39542  ?  148  ILE   A CD1 1 
ATOM   1219  N  N   . VAL   A 1 149  ? -71.15900  49.54000  32.24800  1.000 64.46853  ?  149  VAL   A N   1 
ATOM   1220  C  CA  . VAL   A 1 149  ? -72.56200  49.70300  32.60500  1.000 69.82313  ?  149  VAL   A CA  1 
ATOM   1221  C  C   . VAL   A 1 149  ? -73.15300  48.43200  33.20400  1.000 74.21990  ?  149  VAL   A C   1 
ATOM   1222  O  O   . VAL   A 1 149  ? -74.12900  48.50400  33.95900  1.000 71.09747  ?  149  VAL   A O   1 
ATOM   1223  C  CB  . VAL   A 1 149  ? -73.36500  50.16100  31.37100  1.000 56.11922  ?  149  VAL   A CB  1 
ATOM   1224  C  CG1 . VAL   A 1 149  ? -73.56900  49.00700  30.40400  1.000 57.88818  ?  149  VAL   A CG1 1 
ATOM   1225  C  CG2 . VAL   A 1 149  ? -74.69800  50.76200  31.78800  1.000 62.57469  ?  149  VAL   A CG2 1 
ATOM   1226  N  N   . HIS   A 1 150  ? -72.58000  47.26600  32.90500  1.000 71.15497  ?  150  HIS   A N   1 
ATOM   1227  C  CA  . HIS   A 1 150  ? -73.06700  46.00200  33.43800  1.000 57.35589  ?  150  HIS   A CA  1 
ATOM   1228  C  C   . HIS   A 1 150  ? -72.26100  45.52200  34.63900  1.000 62.47580  ?  150  HIS   A C   1 
ATOM   1229  O  O   . HIS   A 1 150  ? -72.38700  44.35700  35.03100  1.000 71.24533  ?  150  HIS   A O   1 
ATOM   1230  C  CB  . HIS   A 1 150  ? -73.07200  44.93600  32.34100  1.000 72.66899  ?  150  HIS   A CB  1 
ATOM   1231  C  CG  . HIS   A 1 150  ? -74.11000  45.16300  31.28700  1.000 74.60602  ?  150  HIS   A CG  1 
ATOM   1232  N  ND1 . HIS   A 1 150  ? -73.85500  44.99900  29.94200  1.000 72.13578  ?  150  HIS   A ND1 1 
ATOM   1233  C  CD2 . HIS   A 1 150  ? -75.40700  45.54200  31.37900  1.000 72.12426  ?  150  HIS   A CD2 1 
ATOM   1234  C  CE1 . HIS   A 1 150  ? -74.94800  45.26800  29.25200  1.000 77.96699  ?  150  HIS   A CE1 1 
ATOM   1235  N  NE2 . HIS   A 1 150  ? -75.90500  45.60000  30.10100  1.000 90.90406  ?  150  HIS   A NE2 1 
ATOM   1236  N  N   . GLY   A 1 151  ? -71.43700  46.38900  35.22400  1.000 68.09365  ?  151  GLY   A N   1 
ATOM   1237  C  CA  . GLY   A 1 151  ? -70.73800  46.06200  36.45600  1.000 67.84383  ?  151  GLY   A CA  1 
ATOM   1238  C  C   . GLY   A 1 151  ? -69.74600  44.92700  36.34800  1.000 75.18741  ?  151  GLY   A C   1 
ATOM   1239  O  O   . GLY   A 1 151  ? -69.46400  44.26400  37.35200  1.000 90.43671  ?  151  GLY   A O   1 
ATOM   1240  N  N   . ARG   A 1 152  ? -69.20400  44.68000  35.15900  1.000 67.60150  ?  152  ARG   A N   1 
ATOM   1241  C  CA  . ARG   A 1 152  ? -68.21100  43.63300  34.97100  1.000 61.20192  ?  152  ARG   A CA  1 
ATOM   1242  C  C   . ARG   A 1 152  ? -66.78700  44.13500  35.16900  1.000 70.48220  ?  152  ARG   A C   1 
ATOM   1243  O  O   . ARG   A 1 152  ? -65.83700  43.39900  34.88500  1.000 81.18568  ?  152  ARG   A O   1 
ATOM   1244  C  CB  . ARG   A 1 152  ? -68.35000  43.01100  33.57900  1.000 66.27367  ?  152  ARG   A CB  1 
ATOM   1245  C  CG  . ARG   A 1 152  ? -69.77200  42.63800  33.19500  1.000 69.14051  ?  152  ARG   A CG  1 
ATOM   1246  C  CD  . ARG   A 1 152  ? -69.82300  42.09200  31.77800  1.000 74.09810  ?  152  ARG   A CD  1 
ATOM   1247  N  NE  . ARG   A 1 152  ? -70.75600  42.82600  30.93200  1.000 77.10481  ?  152  ARG   A NE  1 
ATOM   1248  C  CZ  . ARG   A 1 152  ? -70.72900  42.81400  29.60600  1.000 92.03408  ?  152  ARG   A CZ  1 
ATOM   1249  N  NH1 . ARG   A 1 152  ? -69.82200  42.12000  28.93900  1.000 106.58222 ?  152  ARG   A NH1 1 
ATOM   1250  N  NH2 . ARG   A 1 152  ? -71.63500  43.51600  28.93100  1.000 96.82992  ?  152  ARG   A NH2 1 
ATOM   1251  N  N   . ILE   A 1 153  ? -66.62000  45.36500  35.64800  1.000 70.92782  ?  153  ILE   A N   1 
ATOM   1252  C  CA  . ILE   A 1 153  ? -65.31000  45.97700  35.83600  1.000 71.02982  ?  153  ILE   A CA  1 
ATOM   1253  C  C   . ILE   A 1 153  ? -65.19900  46.41300  37.28900  1.000 72.87263  ?  153  ILE   A C   1 
ATOM   1254  O  O   . ILE   A 1 153  ? -66.01000  47.21600  37.76700  1.000 64.70589  ?  153  ILE   A O   1 
ATOM   1255  C  CB  . ILE   A 1 153  ? -65.09400  47.16900  34.89100  1.000 71.61475  ?  153  ILE   A CB  1 
ATOM   1256  C  CG1 . ILE   A 1 153  ? -64.87400  46.68000  33.45700  1.000 62.51974  ?  153  ILE   A CG1 1 
ATOM   1257  C  CG2 . ILE   A 1 153  ? -63.92500  48.02100  35.36600  1.000 55.89566  ?  153  ILE   A CG2 1 
ATOM   1258  C  CD1 . ILE   A 1 153  ? -64.44900  47.77200  32.50000  1.000 56.06185  ?  153  ILE   A CD1 1 
ATOM   1259  N  N   . ALA   A 1 154  ? -64.19500  45.88600  37.98600  1.000 74.26864  ?  154  ALA   A N   1 
ATOM   1260  C  CA  . ALA   A 1 154  ? -63.97700  46.22200  39.38500  1.000 66.89419  ?  154  ALA   A CA  1 
ATOM   1261  C  C   . ALA   A 1 154  ? -63.09200  47.45500  39.48400  1.000 62.91017  ?  154  ALA   A C   1 
ATOM   1262  O  O   . ALA   A 1 154  ? -61.94600  47.41800  39.01600  1.000 69.12694  ?  154  ALA   A O   1 
ATOM   1263  C  CB  . ALA   A 1 154  ? -63.33300  45.06100  40.12200  1.000 58.68297  ?  154  ALA   A CB  1 
ATOM   1264  N  N   . PRO   A 1 155  ? -63.57000  48.55500  40.06500  1.000 57.55890  ?  155  PRO   A N   1 
ATOM   1265  C  CA  . PRO   A 1 155  ? -62.72200  49.74700  40.19200  1.000 60.94586  ?  155  PRO   A CA  1 
ATOM   1266  C  C   . PRO   A 1 155  ? -61.52900  49.47500  41.09500  1.000 71.40331  ?  155  PRO   A C   1 
ATOM   1267  O  O   . PRO   A 1 155  ? -61.67500  48.95300  42.20200  1.000 85.64132  ?  155  PRO   A O   1 
ATOM   1268  C  CB  . PRO   A 1 155  ? -63.66500  50.79300  40.80200  1.000 49.75203  ?  155  PRO   A CB  1 
ATOM   1269  C  CG  . PRO   A 1 155  ? -65.04500  50.27700  40.54600  1.000 58.82563  ?  155  PRO   A CG  1 
ATOM   1270  C  CD  . PRO   A 1 155  ? -64.93200  48.78500  40.57100  1.000 53.81580  ?  155  PRO   A CD  1 
ATOM   1271  N  N   . TYR   A 1 156  ? -60.34000  49.82300  40.61100  1.000 75.24045  ?  156  TYR   A N   1 
ATOM   1272  C  CA  . TYR   A 1 156  ? -59.12400  49.74300  41.40600  1.000 68.24097  ?  156  TYR   A CA  1 
ATOM   1273  C  C   . TYR   A 1 156  ? -58.61900  51.15100  41.69000  1.000 51.25658  ?  156  TYR   A C   1 
ATOM   1274  O  O   . TYR   A 1 156  ? -58.74800  52.04700  40.85000  1.000 67.62716  ?  156  TYR   A O   1 
ATOM   1275  C  CB  . TYR   A 1 156  ? -58.04400  48.90700  40.70400  1.000 61.85489  ?  156  TYR   A CB  1 
ATOM   1276  C  CG  . TYR   A 1 156  ? -57.62900  49.38600  39.33000  1.000 66.25930  ?  156  TYR   A CG  1 
ATOM   1277  C  CD1 . TYR   A 1 156  ? -56.70700  50.41400  39.17700  1.000 60.65295  ?  156  TYR   A CD1 1 
ATOM   1278  C  CD2 . TYR   A 1 156  ? -58.15000  48.79800  38.18400  1.000 67.29549  ?  156  TYR   A CD2 1 
ATOM   1279  C  CE1 . TYR   A 1 156  ? -56.31900  50.84600  37.92500  1.000 77.84903  ?  156  TYR   A CE1 1 
ATOM   1280  C  CE2 . TYR   A 1 156  ? -57.76900  49.22600  36.92600  1.000 77.98026  ?  156  TYR   A CE2 1 
ATOM   1281  C  CZ  . TYR   A 1 156  ? -56.85400  50.25200  36.80200  1.000 75.59331  ?  156  TYR   A CZ  1 
ATOM   1282  O  OH  . TYR   A 1 156  ? -56.46800  50.68500  35.55300  1.000 85.98958  ?  156  TYR   A OH  1 
ATOM   1283  N  N   . ARG   A 1 157  ? -58.05500  51.34500  42.87900  1.000 57.47843  ?  157  ARG   A N   1 
ATOM   1284  C  CA  . ARG   A 1 157  ? -57.63800  52.67600  43.29400  1.000 72.95664  ?  157  ARG   A CA  1 
ATOM   1285  C  C   . ARG   A 1 157  ? -56.40800  53.14700  42.53100  1.000 77.08635  ?  157  ARG   A C   1 
ATOM   1286  O  O   . ARG   A 1 157  ? -55.58400  52.35500  42.06400  1.000 71.07975  ?  157  ARG   A O   1 
ATOM   1287  C  CB  . ARG   A 1 157  ? -57.35000  52.71300  44.79300  1.000 78.75662  ?  157  ARG   A CB  1 
ATOM   1288  C  CG  . ARG   A 1 157  ? -58.55600  53.06500  45.62800  1.000 99.58900  ?  157  ARG   A CG  1 
ATOM   1289  C  CD  . ARG   A 1 157  ? -58.13100  53.75500  46.88700  1.000 94.24184  ?  157  ARG   A CD  1 
ATOM   1290  N  NE  . ARG   A 1 157  ? -58.65000  53.05800  48.04500  1.000 107.14096 ?  157  ARG   A NE  1 
ATOM   1291  C  CZ  . ARG   A 1 157  ? -57.91800  52.71100  49.09000  1.000 92.16129  ?  157  ARG   A CZ  1 
ATOM   1292  N  NH1 . ARG   A 1 157  ? -56.63100  53.01400  49.16500  1.000 90.22463  ?  157  ARG   A NH1 1 
ATOM   1293  N  NH2 . ARG   A 1 157  ? -58.48200  52.00800  50.07600  1.000 59.16221  ?  157  ARG   A NH2 1 
ATOM   1294  N  N   . GLN   A 1 158  ? -56.28900  54.46500  42.42500  1.000 72.86556  ?  158  GLN   A N   1 
ATOM   1295  C  CA  . GLN   A 1 158  ? -55.15500  55.06800  41.74700  1.000 83.46268  ?  158  GLN   A CA  1 
ATOM   1296  C  C   . GLN   A 1 158  ? -53.86800  54.77600  42.50700  1.000 87.41421  ?  158  GLN   A C   1 
ATOM   1297  O  O   . GLN   A 1 158  ? -53.81800  54.87700  43.73700  1.000 82.61975  ?  158  GLN   A O   1 
ATOM   1298  C  CB  . GLN   A 1 158  ? -55.37300  56.57500  41.62100  1.000 85.08241  ?  158  GLN   A CB  1 
ATOM   1299  C  CG  . GLN   A 1 158  ? -55.65800  57.04600  40.20800  1.000 70.46606  ?  158  GLN   A CG  1 
ATOM   1300  C  CD  . GLN   A 1 158  ? -56.05100  58.50600  40.15400  1.000 81.13493  ?  158  GLN   A CD  1 
ATOM   1301  O  OE1 . GLN   A 1 158  ? -55.41900  59.35600  40.78100  1.000 82.14661  ?  158  GLN   A OE1 1 
ATOM   1302  N  NE2 . GLN   A 1 158  ? -57.12000  58.80200  39.42300  1.000 67.88755  ?  158  GLN   A NE2 1 
ATOM   1303  N  N   . THR   A 1 159  ? -52.82400  54.40500  41.76800  1.000 82.04956  ?  159  THR   A N   1 
ATOM   1304  C  CA  . THR   A 1 159  ? -51.53200  54.13100  42.37900  1.000 73.86696  ?  159  THR   A CA  1 
ATOM   1305  C  C   . THR   A 1 159  ? -50.92300  55.41900  42.93800  1.000 71.51304  ?  159  THR   A C   1 
ATOM   1306  O  O   . THR   A 1 159  ? -51.36900  56.53300  42.64700  1.000 74.66338  ?  159  THR   A O   1 
ATOM   1307  C  CB  . THR   A 1 159  ? -50.58500  53.48100  41.36600  1.000 69.67678  ?  159  THR   A CB  1 
ATOM   1308  O  OG1 . THR   A 1 159  ? -49.55800  52.75900  42.05800  1.000 80.84249  ?  159  THR   A OG1 1 
ATOM   1309  C  CG2 . THR   A 1 159  ? -49.94300  54.53200  40.47200  1.000 68.84977  ?  159  THR   A CG2 1 
ATOM   1310  N  N   . ALA   A 1 160  ? -49.89100  55.25700  43.76000  1.000 61.60979  ?  160  ALA   A N   1 
ATOM   1311  C  CA  . ALA   A 1 160  ? -49.23400  56.40600  44.36800  1.000 73.74542  ?  160  ALA   A CA  1 
ATOM   1312  C  C   . ALA   A 1 160  ? -48.40700  57.16200  43.33300  1.000 81.02186  ?  160  ALA   A C   1 
ATOM   1313  O  O   . ALA   A 1 160  ? -47.69400  56.55400  42.52900  1.000 78.43020  ?  160  ALA   A O   1 
ATOM   1314  C  CB  . ALA   A 1 160  ? -48.34500  55.95700  45.52700  1.000 83.98876  ?  160  ALA   A CB  1 
ATOM   1315  N  N   . GLY   A 1 161  ? -48.50800  58.49700  43.35300  1.000 74.04506  ?  161  GLY   A N   1 
ATOM   1316  C  CA  . GLY   A 1 161  ? -47.71100  59.36800  42.51900  1.000 71.91027  ?  161  GLY   A CA  1 
ATOM   1317  C  C   . GLY   A 1 161  ? -48.57900  60.35300  41.76600  1.000 92.74969  ?  161  GLY   A C   1 
ATOM   1318  O  O   . GLY   A 1 161  ? -49.72000  60.63300  42.15600  1.000 83.68251  ?  161  GLY   A O   1 
ATOM   1319  N  N   . GLY   A 1 162  ? -48.02100  60.89900  40.69500  1.000 81.55321  ?  162  GLY   A N   1 
ATOM   1320  C  CA  . GLY   A 1 162  ? -48.76700  61.69600  39.74700  1.000 80.10156  ?  162  GLY   A CA  1 
ATOM   1321  C  C   . GLY   A 1 162  ? -48.42600  63.17700  39.83500  1.000 64.08002  ?  162  GLY   A C   1 
ATOM   1322  O  O   . GLY   A 1 162  ? -47.86500  63.66800  40.81800  1.000 72.60902  ?  162  GLY   A O   1 
ATOM   1323  N  N   . THR   A 1 163  ? -48.78100  63.88900  38.76900  1.000 55.32945  ?  163  THR   A N   1 
ATOM   1324  C  CA  . THR   A 1 163  ? -48.64600  65.33300  38.68800  1.000 44.90325  ?  163  THR   A CA  1 
ATOM   1325  C  C   . THR   A 1 163  ? -50.02800  65.95100  38.53700  1.000 57.65432  ?  163  THR   A C   1 
ATOM   1326  O  O   . THR   A 1 163  ? -50.93800  65.34700  37.96000  1.000 48.82196  ?  163  THR   A O   1 
ATOM   1327  C  CB  . THR   A 1 163  ? -47.75800  65.75400  37.50700  1.000 60.60864  ?  163  THR   A CB  1 
ATOM   1328  O  OG1 . THR   A 1 163  ? -48.55900  65.90800  36.32700  1.000 66.27324  ?  163  THR   A OG1 1 
ATOM   1329  C  CG2 . THR   A 1 163  ? -46.69300  64.70300  37.24500  1.000 79.86333  ?  163  THR   A CG2 1 
ATOM   1330  N  N   . LEU   A 1 164  ? -50.18000  67.15600  39.07200  1.000 55.99900  ?  164  LEU   A N   1 
ATOM   1331  C  CA  . LEU   A 1 164  ? -51.41300  67.91900  38.95800  1.000 46.05038  ?  164  LEU   A CA  1 
ATOM   1332  C  C   . LEU   A 1 164  ? -51.07800  69.28000  38.36900  1.000 45.39578  ?  164  LEU   A C   1 
ATOM   1333  O  O   . LEU   A 1 164  ? -50.16100  69.95700  38.84600  1.000 54.11779  ?  164  LEU   A O   1 
ATOM   1334  C  CB  . LEU   A 1 164  ? -52.10100  68.06500  40.31800  1.000 46.39291  ?  164  LEU   A CB  1 
ATOM   1335  C  CG  . LEU   A 1 164  ? -53.34700  68.94700  40.36000  1.000 53.30013  ?  164  LEU   A CG  1 
ATOM   1336  C  CD1 . LEU   A 1 164  ? -54.59400  68.12700  40.06000  1.000 62.28363  ?  164  LEU   A CD1 1 
ATOM   1337  C  CD2 . LEU   A 1 164  ? -53.45600  69.61800  41.71500  1.000 51.36201  ?  164  LEU   A CD2 1 
ATOM   1338  N  N   . HIS   A 1 165  ? -51.80300  69.66500  37.32300  1.000 52.83285  ?  165  HIS   A N   1 
ATOM   1339  C  CA  . HIS   A 1 165  ? -51.55900  70.91900  36.62900  1.000 48.21561  ?  165  HIS   A CA  1 
ATOM   1340  C  C   . HIS   A 1 165  ? -52.86900  71.66100  36.42400  1.000 40.37752  ?  165  HIS   A C   1 
ATOM   1341  O  O   . HIS   A 1 165  ? -53.92500  71.05300  36.23300  1.000 47.14940  ?  165  HIS   A O   1 
ATOM   1342  C  CB  . HIS   A 1 165  ? -50.87800  70.68800  35.28000  1.000 49.53231  ?  165  HIS   A CB  1 
ATOM   1343  C  CG  . HIS   A 1 165  ? -49.40300  70.47400  35.38700  1.000 42.51329  ?  165  HIS   A CG  1 
ATOM   1344  N  ND1 . HIS   A 1 165  ? -48.80400  69.27100  35.08100  1.000 45.23052  ?  165  HIS   A ND1 1 
ATOM   1345  C  CD2 . HIS   A 1 165  ? -48.40700  71.30500  35.77300  1.000 39.51162  ?  165  HIS   A CD2 1 
ATOM   1346  C  CE1 . HIS   A 1 165  ? -47.50100  69.37100  35.27200  1.000 69.30350  ?  165  HIS   A CE1 1 
ATOM   1347  N  NE2 . HIS   A 1 165  ? -47.23400  70.59600  35.69200  1.000 69.08302  ?  165  HIS   A NE2 1 
ATOM   1348  N  N   . PHE   A 1 166  ? -52.78800  72.98400  36.46100  1.000 42.48459  ?  166  PHE   A N   1 
ATOM   1349  C  CA  . PHE   A 1 166  ? -53.95200  73.83900  36.30700  1.000 46.62854  ?  166  PHE   A CA  1 
ATOM   1350  C  C   . PHE   A 1 166  ? -53.87100  74.63100  35.01000  1.000 51.03580  ?  166  PHE   A C   1 
ATOM   1351  O  O   . PHE   A 1 166  ? -52.83600  74.69400  34.34100  1.000 66.67259  ?  166  PHE   A O   1 
ATOM   1352  C  CB  . PHE   A 1 166  ? -54.09700  74.79700  37.49700  1.000 56.15830  ?  166  PHE   A CB  1 
ATOM   1353  C  CG  . PHE   A 1 166  ? -54.57200  74.13000  38.75200  1.000 63.69350  ?  166  PHE   A CG  1 
ATOM   1354  C  CD1 . PHE   A 1 166  ? -53.68100  73.47400  39.58300  1.000 60.02332  ?  166  PHE   A CD1 1 
ATOM   1355  C  CD2 . PHE   A 1 166  ? -55.91700  74.13500  39.08900  1.000 71.56122  ?  166  PHE   A CD2 1 
ATOM   1356  C  CE1 . PHE   A 1 166  ? -54.11500  72.85300  40.73600  1.000 63.92634  ?  166  PHE   A CE1 1 
ATOM   1357  C  CE2 . PHE   A 1 166  ? -56.35800  73.50900  40.23900  1.000 73.28924  ?  166  PHE   A CE2 1 
ATOM   1358  C  CZ  . PHE   A 1 166  ? -55.45600  72.86800  41.06500  1.000 74.76051  ?  166  PHE   A CZ  1 
ATOM   1359  N  N   . LYS   A 1 167  ? -55.00400  75.22700  34.66200  1.000 51.88235  ?  167  LYS   A N   1 
ATOM   1360  C  CA  . LYS   A 1 167  ? -55.07300  76.15900  33.54900  1.000 55.28138  ?  167  LYS   A CA  1 
ATOM   1361  C  C   . LYS   A 1 167  ? -54.07400  77.29300  33.75200  1.000 55.20639  ?  167  LYS   A C   1 
ATOM   1362  O  O   . LYS   A 1 167  ? -53.68200  77.61300  34.87800  1.000 60.90275  ?  167  LYS   A O   1 
ATOM   1363  C  CB  . LYS   A 1 167  ? -56.49500  76.71800  33.40700  1.000 37.20305  ?  167  LYS   A CB  1 
ATOM   1364  C  CG  . LYS   A 1 167  ? -57.14400  77.19100  34.72200  1.000 77.82123  ?  167  LYS   A CG  1 
ATOM   1365  C  CD  . LYS   A 1 167  ? -57.64100  76.04200  35.61200  1.000 73.92643  ?  167  LYS   A CD  1 
ATOM   1366  C  CE  . LYS   A 1 167  ? -58.43900  76.53900  36.80000  1.000 81.45968  ?  167  LYS   A CE  1 
ATOM   1367  N  NZ  . LYS   A 1 167  ? -58.82600  75.39200  37.66500  1.000 88.02860  ?  167  LYS   A NZ  1 
ATOM   1368  N  N   . ALA   A 1 168  ? -53.64700  77.88700  32.64100  1.000 49.11370  ?  168  ALA   A N   1 
ATOM   1369  C  CA  . ALA   A 1 168  ? -52.70800  79.00500  32.60700  1.000 61.88587  ?  168  ALA   A CA  1 
ATOM   1370  C  C   . ALA   A 1 168  ? -51.32300  78.63700  33.13100  1.000 54.87986  ?  168  ALA   A C   1 
ATOM   1371  O  O   . ALA   A 1 168  ? -50.46700  79.51900  33.27300  1.000 76.64873  ?  168  ALA   A O   1 
ATOM   1372  C  CB  . ALA   A 1 168  ? -53.25000  80.22300  33.36900  1.000 58.91306  ?  168  ALA   A CB  1 
ATOM   1373  N  N   . ASP   A 1 169  ? -51.07900  77.36300  33.43100  1.000 48.59376  ?  169  ASP   A N   1 
ATOM   1374  C  CA  . ASP   A 1 169  ? -49.72300  76.89200  33.68400  1.000 56.08650  ?  169  ASP   A CA  1 
ATOM   1375  C  C   . ASP   A 1 169  ? -48.95600  76.64100  32.39600  1.000 54.34047  ?  169  ASP   A C   1 
ATOM   1376  O  O   . ASP   A 1 169  ? -47.77300  76.28900  32.45000  1.000 67.87611  ?  169  ASP   A O   1 
ATOM   1377  C  CB  . ASP   A 1 169  ? -49.74700  75.60900  34.52000  1.000 50.62396  ?  169  ASP   A CB  1 
ATOM   1378  C  CG  . ASP   A 1 169  ? -50.22600  75.84400  35.93600  1.000 54.92626  ?  169  ASP   A CG  1 
ATOM   1379  O  OD1 . ASP   A 1 169  ? -50.64200  76.98000  36.24900  1.000 57.36618  ?  169  ASP   A OD1 1 
ATOM   1380  O  OD2 . ASP   A 1 169  ? -50.18500  74.88700  36.73700  1.000 58.59072  -1 169  ASP   A OD2 1 
ATOM   1381  N  N   . ARG   A 1 170  ? -49.60600  76.81800  31.25000  1.000 55.54595  ?  170  ARG   A N   1 
ATOM   1382  C  CA  . ARG   A 1 170  ? -49.02700  76.55000  29.94500  1.000 53.09443  ?  170  ARG   A CA  1 
ATOM   1383  C  C   . ARG   A 1 170  ? -48.78300  77.82500  29.15000  1.000 43.25025  ?  170  ARG   A C   1 
ATOM   1384  O  O   . ARG   A 1 170  ? -48.27400  77.75600  28.02600  1.000 51.32868  ?  170  ARG   A O   1 
ATOM   1385  C  CB  . ARG   A 1 170  ? -49.95200  75.60400  29.16900  1.000 61.04538  ?  170  ARG   A CB  1 
ATOM   1386  C  CG  . ARG   A 1 170  ? -49.33400  74.92400  27.96800  1.000 69.62809  ?  170  ARG   A CG  1 
ATOM   1387  C  CD  . ARG   A 1 170  ? -50.06500  75.31500  26.70200  1.000 64.55902  ?  170  ARG   A CD  1 
ATOM   1388  N  NE  . ARG   A 1 170  ? -49.42800  74.75700  25.51800  1.000 44.04996  ?  170  ARG   A NE  1 
ATOM   1389  C  CZ  . ARG   A 1 170  ? -49.83100  73.65000  24.91300  1.000 63.35859  ?  170  ARG   A CZ  1 
ATOM   1390  N  NH1 . ARG   A 1 170  ? -50.88300  72.97100  25.34400  1.000 62.31867  ?  170  ARG   A NH1 1 
ATOM   1391  N  NH2 . ARG   A 1 170  ? -49.16500  73.21500  23.84900  1.000 63.82225  ?  170  ARG   A NH2 1 
ATOM   1392  N  N   . ASP   A 1 171  ? -49.10900  78.98900  29.71700  1.000 42.22173  ?  171  ASP   A N   1 
ATOM   1393  C  CA  . ASP   A 1 171  ? -49.07500  80.23800  28.96400  1.000 49.31622  ?  171  ASP   A CA  1 
ATOM   1394  C  C   . ASP   A 1 171  ? -47.67600  80.60800  28.48900  1.000 57.51384  ?  171  ASP   A C   1 
ATOM   1395  O  O   . ASP   A 1 171  ? -47.54100  81.45900  27.60300  1.000 68.39200  ?  171  ASP   A O   1 
ATOM   1396  C  CB  . ASP   A 1 171  ? -49.65400  81.36600  29.81700  1.000 61.48958  ?  171  ASP   A CB  1 
ATOM   1397  C  CG  . ASP   A 1 171  ? -51.13300  81.18900  30.08600  1.000 63.66771  ?  171  ASP   A CG  1 
ATOM   1398  O  OD1 . ASP   A 1 171  ? -51.72400  80.22300  29.55600  1.000 62.92537  ?  171  ASP   A OD1 1 
ATOM   1399  O  OD2 . ASP   A 1 171  ? -51.70600  82.01700  30.82600  1.000 63.68811  -1 171  ASP   A OD2 1 
ATOM   1400  N  N   . PHE   A 1 172  ? -46.63800  79.99200  29.05000  1.000 53.84452  ?  172  PHE   A N   1 
ATOM   1401  C  CA  . PHE   A 1 172  ? -45.27200  80.25800  28.62200  1.000 44.93050  ?  172  PHE   A CA  1 
ATOM   1402  C  C   . PHE   A 1 172  ? -44.84700  79.39400  27.44200  1.000 49.57312  ?  172  PHE   A C   1 
ATOM   1403  O  O   . PHE   A 1 172  ? -43.93500  79.78300  26.70200  1.000 47.74478  ?  172  PHE   A O   1 
ATOM   1404  C  CB  . PHE   A 1 172  ? -44.31100  80.05100  29.79900  1.000 50.03011  ?  172  PHE   A CB  1 
ATOM   1405  C  CG  . PHE   A 1 172  ? -42.88700  80.42200  29.49900  1.000 50.13039  ?  172  PHE   A CG  1 
ATOM   1406  C  CD1 . PHE   A 1 172  ? -42.57200  81.68300  29.02000  1.000 54.83236  ?  172  PHE   A CD1 1 
ATOM   1407  C  CD2 . PHE   A 1 172  ? -41.86300  79.51400  29.71000  1.000 38.15303  ?  172  PHE   A CD2 1 
ATOM   1408  C  CE1 . PHE   A 1 172  ? -41.26200  82.03000  28.74600  1.000 50.58962  ?  172  PHE   A CE1 1 
ATOM   1409  C  CE2 . PHE   A 1 172  ? -40.55000  79.85400  29.43900  1.000 54.03491  ?  172  PHE   A CE2 1 
ATOM   1410  C  CZ  . PHE   A 1 172  ? -40.24900  81.11400  28.95600  1.000 59.27523  ?  172  PHE   A CZ  1 
ATOM   1411  N  N   . TYR   A 1 173  ? -45.49600  78.25000  27.23600  1.000 44.26353  ?  173  TYR   A N   1 
ATOM   1412  C  CA  . TYR   A 1 173  ? -45.17000  77.32600  26.15500  1.000 51.25704  ?  173  TYR   A CA  1 
ATOM   1413  C  C   . TYR   A 1 173  ? -46.26600  77.29700  25.09300  1.000 44.68257  ?  173  TYR   A C   1 
ATOM   1414  O  O   . TYR   A 1 173  ? -46.67600  76.23300  24.62900  1.000 54.15435  ?  173  TYR   A O   1 
ATOM   1415  C  CB  . TYR   A 1 173  ? -44.92800  75.92200  26.70300  1.000 53.56655  ?  173  TYR   A CB  1 
ATOM   1416  C  CG  . TYR   A 1 173  ? -44.28900  75.88800  28.07600  1.000 57.08892  ?  173  TYR   A CG  1 
ATOM   1417  C  CD1 . TYR   A 1 173  ? -42.90800  75.93100  28.22400  1.000 58.56793  ?  173  TYR   A CD1 1 
ATOM   1418  C  CD2 . TYR   A 1 173  ? -45.06700  75.80500  29.22300  1.000 56.64184  ?  173  TYR   A CD2 1 
ATOM   1419  C  CE1 . TYR   A 1 173  ? -42.32100  75.89500  29.47700  1.000 56.28523  ?  173  TYR   A CE1 1 
ATOM   1420  C  CE2 . TYR   A 1 173  ? -44.49100  75.76900  30.47900  1.000 52.50068  ?  173  TYR   A CE2 1 
ATOM   1421  C  CZ  . TYR   A 1 173  ? -43.11800  75.81400  30.60100  1.000 65.61691  ?  173  TYR   A CZ  1 
ATOM   1422  O  OH  . TYR   A 1 173  ? -42.54300  75.77800  31.85100  1.000 65.39152  ?  173  TYR   A OH  1 
ATOM   1423  N  N   . LYS   A 1 174  ? -46.75300  78.47000  24.69200  1.000 40.40091  ?  174  LYS   A N   1 
ATOM   1424  C  CA  . LYS   A 1 174  ? -47.86800  78.51700  23.75500  1.000 34.63385  ?  174  LYS   A CA  1 
ATOM   1425  C  C   . LYS   A 1 174  ? -47.41700  78.38500  22.30500  1.000 49.26472  ?  174  LYS   A C   1 
ATOM   1426  O  O   . LYS   A 1 174  ? -48.17600  77.87500  21.47300  1.000 65.02170  ?  174  LYS   A O   1 
ATOM   1427  C  CB  . LYS   A 1 174  ? -48.66000  79.81100  23.94600  1.000 36.32485  ?  174  LYS   A CB  1 
ATOM   1428  C  CG  . LYS   A 1 174  ? -47.80700  81.06300  23.99500  1.000 45.30228  ?  174  LYS   A CG  1 
ATOM   1429  C  CD  . LYS   A 1 174  ? -48.65000  82.29800  24.27000  1.000 49.34171  ?  174  LYS   A CD  1 
ATOM   1430  C  CE  . LYS   A 1 174  ? -47.96600  83.56000  23.76100  1.000 71.74939  ?  174  LYS   A CE  1 
ATOM   1431  N  NZ  . LYS   A 1 174  ? -47.63400  83.48400  22.30900  1.000 58.05930  ?  174  LYS   A NZ  1 
ATOM   1432  N  N   . ASN   A 1 175  ? -46.20100  78.82100  21.97800  1.000 42.22159  ?  175  ASN   A N   1 
ATOM   1433  C  CA  . ASN   A 1 175  ? -45.70900  78.77400  20.60800  1.000 38.69221  ?  175  ASN   A CA  1 
ATOM   1434  C  C   . ASN   A 1 175  ? -45.08700  77.43300  20.24700  1.000 41.76349  ?  175  ASN   A C   1 
ATOM   1435  O  O   . ASN   A 1 175  ? -44.37100  77.34500  19.24300  1.000 51.56084  ?  175  ASN   A O   1 
ATOM   1436  C  CB  . ASN   A 1 175  ? -44.69000  79.89000  20.36900  1.000 43.17516  ?  175  ASN   A CB  1 
ATOM   1437  C  CG  . ASN   A 1 175  ? -45.13400  81.21900  20.93500  1.000 54.65763  ?  175  ASN   A CG  1 
ATOM   1438  O  OD1 . ASN   A 1 175  ? -46.31600  81.56000  20.89700  1.000 62.59476  ?  175  ASN   A OD1 1 
ATOM   1439  N  ND2 . ASN   A 1 175  ? -44.18400  81.98300  21.46200  1.000 61.11839  ?  175  ASN   A ND2 1 
ATOM   1440  N  N   . LEU   A 1 176  ? -45.34400  76.38700  21.02700  1.000 42.01895  ?  176  LEU   A N   1 
ATOM   1441  C  CA  . LEU   A 1 176  ? -44.65400  75.11500  20.85400  1.000 47.58159  ?  176  LEU   A CA  1 
ATOM   1442  C  C   . LEU   A 1 176  ? -45.61100  73.98600  20.48800  1.000 53.25596  ?  176  LEU   A C   1 
ATOM   1443  O  O   . LEU   A 1 176  ? -45.34600  72.82000  20.78600  1.000 57.04573  ?  176  LEU   A O   1 
ATOM   1444  C  CB  . LEU   A 1 176  ? -43.87100  74.76000  22.11500  1.000 51.71112  ?  176  LEU   A CB  1 
ATOM   1445  C  CG  . LEU   A 1 176  ? -42.61000  75.59300  22.33200  1.000 55.14123  ?  176  LEU   A CG  1 
ATOM   1446  C  CD1 . LEU   A 1 176  ? -42.63700  76.26200  23.69500  1.000 62.96139  ?  176  LEU   A CD1 1 
ATOM   1447  C  CD2 . LEU   A 1 176  ? -41.37900  74.73200  22.16800  1.000 62.70619  ?  176  LEU   A CD2 1 
ATOM   1448  N  N   . ASN   A 1 177  ? -46.72100  74.31300  19.82700  1.000 55.73861  ?  177  ASN   A N   1 
ATOM   1449  C  CA  . ASN   A 1 177  ? -47.71400  73.29200  19.51600  1.000 57.53209  ?  177  ASN   A CA  1 
ATOM   1450  C  C   . ASN   A 1 177  ? -47.35900  72.49700  18.26800  1.000 55.09673  ?  177  ASN   A C   1 
ATOM   1451  O  O   . ASN   A 1 177  ? -47.70700  71.31400  18.17200  1.000 46.36901  ?  177  ASN   A O   1 
ATOM   1452  C  CB  . ASN   A 1 177  ? -49.09000  73.93300  19.35600  1.000 50.71816  ?  177  ASN   A CB  1 
ATOM   1453  C  CG  . ASN   A 1 177  ? -49.87800  73.92600  20.64200  1.000 68.56043  ?  177  ASN   A CG  1 
ATOM   1454  O  OD1 . ASN   A 1 177  ? -49.35300  73.58400  21.70000  1.000 73.41184  ?  177  ASN   A OD1 1 
ATOM   1455  N  ND2 . ASN   A 1 177  ? -51.14700  74.29400  20.56000  1.000 86.82542  ?  177  ASN   A ND2 1 
ATOM   1456  N  N   . MET   A 1 178  ? -46.67500  73.12000  17.30900  1.000 52.07423  ?  178  MET   A N   1 
ATOM   1457  C  CA  . MET   A 1 178  ? -46.26900  72.45600  16.07900  1.000 49.91339  ?  178  MET   A CA  1 
ATOM   1458  C  C   . MET   A 1 178  ? -44.83000  71.95800  16.13700  1.000 44.28708  ?  178  MET   A C   1 
ATOM   1459  O  O   . MET   A 1 178  ? -44.22900  71.68600  15.09300  1.000 50.61283  ?  178  MET   A O   1 
ATOM   1460  C  CB  . MET   A 1 178  ? -46.46400  73.39700  14.89200  1.000 43.25711  ?  178  MET   A CB  1 
ATOM   1461  C  CG  . MET   A 1 178  ? -47.80200  74.11600  14.90300  1.000 51.72384  ?  178  MET   A CG  1 
ATOM   1462  S  SD  . MET   A 1 178  ? -48.55500  74.16200  13.27100  1.000 79.79113  ?  178  MET   A SD  1 
ATOM   1463  C  CE  . MET   A 1 178  ? -48.52900  72.41700  12.86400  1.000 51.73108  ?  178  MET   A CE  1 
ATOM   1464  N  N   . THR   A 1 179  ? -44.27200  71.83100  17.33500  1.000 52.55798  ?  179  THR   A N   1 
ATOM   1465  C  CA  . THR   A 1 179  ? -42.90600  71.37500  17.53600  1.000 47.38156  ?  179  THR   A CA  1 
ATOM   1466  C  C   . THR   A 1 179  ? -42.91500  69.88900  17.87200  1.000 40.67253  ?  179  THR   A C   1 
ATOM   1467  O  O   . THR   A 1 179  ? -43.83600  69.40100  18.53200  1.000 51.84396  ?  179  THR   A O   1 
ATOM   1468  C  CB  . THR   A 1 179  ? -42.24100  72.18600  18.65400  1.000 44.26602  ?  179  THR   A CB  1 
ATOM   1469  O  OG1 . THR   A 1 179  ? -42.29300  73.58100  18.32500  1.000 51.54888  ?  179  THR   A OG1 1 
ATOM   1470  C  CG2 . THR   A 1 179  ? -40.79800  71.78300  18.84500  1.000 40.58455  ?  179  THR   A CG2 1 
ATOM   1471  N  N   . THR   A 1 180  ? -41.90300  69.16600  17.39600  1.000 46.61002  ?  180  THR   A N   1 
ATOM   1472  C  CA  . THR   A 1 180  ? -41.85600  67.72800  17.61800  1.000 43.27690  ?  180  THR   A CA  1 
ATOM   1473  C  C   . THR   A 1 180  ? -41.48000  67.41400  19.06600  1.000 37.80574  ?  180  THR   A C   1 
ATOM   1474  O  O   . THR   A 1 180  ? -41.01400  68.26800  19.82400  1.000 45.19130  ?  180  THR   A O   1 
ATOM   1475  C  CB  . THR   A 1 180  ? -40.86600  67.06400  16.66200  1.000 45.49489  ?  180  THR   A CB  1 
ATOM   1476  O  OG1 . THR   A 1 180  ? -39.53300  67.23500  17.15800  1.000 61.19669  ?  180  THR   A OG1 1 
ATOM   1477  C  CG2 . THR   A 1 180  ? -40.97700  67.67900  15.28000  1.000 46.64094  ?  180  THR   A CG2 1 
ATOM   1478  N  N   . VAL   A 1 181  ? -41.68500  66.15000  19.44200  1.000 45.60922  ?  181  VAL   A N   1 
ATOM   1479  C  CA  . VAL   A 1 181  ? -41.45800  65.73000  20.82200  1.000 40.27842  ?  181  VAL   A CA  1 
ATOM   1480  C  C   . VAL   A 1 181  ? -39.98600  65.86400  21.18800  1.000 47.49284  ?  181  VAL   A C   1 
ATOM   1481  O  O   . VAL   A 1 181  ? -39.63700  66.44400  22.22500  1.000 45.52773  ?  181  VAL   A O   1 
ATOM   1482  C  CB  . VAL   A 1 181  ? -41.96400  64.29200  21.02900  1.000 38.10230  ?  181  VAL   A CB  1 
ATOM   1483  C  CG1 . VAL   A 1 181  ? -41.37100  63.69100  22.28900  1.000 43.96835  ?  181  VAL   A CG1 1 
ATOM   1484  C  CG2 . VAL   A 1 181  ? -43.47700  64.28300  21.09000  1.000 39.41627  ?  181  VAL   A CG2 1 
ATOM   1485  N  N   . ARG   A 1 182  ? -39.09900  65.32700  20.34300  1.000 43.28331  ?  182  ARG   A N   1 
ATOM   1486  C  CA  . ARG   A 1 182  ? -37.66900  65.40800  20.62600  1.000 47.44819  ?  182  ARG   A CA  1 
ATOM   1487  C  C   . ARG   A 1 182  ? -37.19700  66.85600  20.67200  1.000 53.91615  ?  182  ARG   A C   1 
ATOM   1488  O  O   . ARG   A 1 182  ? -36.33000  67.21000  21.48000  1.000 67.25318  ?  182  ARG   A O   1 
ATOM   1489  C  CB  . ARG   A 1 182  ? -36.87400  64.61600  19.58600  1.000 53.15377  ?  182  ARG   A CB  1 
ATOM   1490  C  CG  . ARG   A 1 182  ? -37.09900  65.06500  18.15000  1.000 61.34705  ?  182  ARG   A CG  1 
ATOM   1491  C  CD  . ARG   A 1 182  ? -35.86300  64.83800  17.29000  1.000 67.68082  ?  182  ARG   A CD  1 
ATOM   1492  N  NE  . ARG   A 1 182  ? -35.88300  65.67300  16.09400  1.000 96.28430  ?  182  ARG   A NE  1 
ATOM   1493  C  CZ  . ARG   A 1 182  ? -35.32300  66.87300  16.00500  1.000 82.49441  ?  182  ARG   A CZ  1 
ATOM   1494  N  NH1 . ARG   A 1 182  ? -34.66800  67.40800  17.02200  1.000 83.41299  ?  182  ARG   A NH1 1 
ATOM   1495  N  NH2 . ARG   A 1 182  ? -35.42700  67.55500  14.86800  1.000 81.03764  ?  182  ARG   A NH2 1 
ATOM   1496  N  N   . GLU   A 1 183  ? -37.76200  67.71200  19.81700  1.000 46.05139  ?  183  GLU   A N   1 
ATOM   1497  C  CA  . GLU   A 1 183  ? -37.39700  69.12300  19.83800  1.000 46.50542  ?  183  GLU   A CA  1 
ATOM   1498  C  C   . GLU   A 1 183  ? -37.90800  69.80400  21.10100  1.000 51.68844  ?  183  GLU   A C   1 
ATOM   1499  O  O   . GLU   A 1 183  ? -37.22600  70.66500  21.66900  1.000 55.13542  ?  183  GLU   A O   1 
ATOM   1500  C  CB  . GLU   A 1 183  ? -37.94400  69.82300  18.59800  1.000 49.46568  ?  183  GLU   A CB  1 
ATOM   1501  C  CG  . GLU   A 1 183  ? -36.92100  70.10600  17.51800  1.000 53.44820  ?  183  GLU   A CG  1 
ATOM   1502  C  CD  . GLU   A 1 183  ? -37.55100  70.18800  16.14400  1.000 66.56367  ?  183  GLU   A CD  1 
ATOM   1503  O  OE1 . GLU   A 1 183  ? -38.73500  70.58000  16.05900  1.000 75.40988  ?  183  GLU   A OE1 1 
ATOM   1504  O  OE2 . GLU   A 1 183  ? -36.86500  69.86700  15.15000  1.000 71.62607  -1 183  GLU   A OE2 1 
ATOM   1505  N  N   . LEU   A 1 184  ? -39.11200  69.43700  21.54600  1.000 56.22293  ?  184  LEU   A N   1 
ATOM   1506  C  CA  . LEU   A 1 184  ? -39.65200  70.00000  22.77900  1.000 54.90777  ?  184  LEU   A CA  1 
ATOM   1507  C  C   . LEU   A 1 184  ? -38.75500  69.67000  23.96400  1.000 51.00634  ?  184  LEU   A C   1 
ATOM   1508  O  O   . LEU   A 1 184  ? -38.44500  70.53900  24.78800  1.000 54.04276  ?  184  LEU   A O   1 
ATOM   1509  C  CB  . LEU   A 1 184  ? -41.06700  69.47500  23.01600  1.000 41.79563  ?  184  LEU   A CB  1 
ATOM   1510  C  CG  . LEU   A 1 184  ? -42.00500  70.36100  23.83500  1.000 45.07944  ?  184  LEU   A CG  1 
ATOM   1511  C  CD1 . LEU   A 1 184  ? -42.56900  71.47100  22.97200  1.000 52.34949  ?  184  LEU   A CD1 1 
ATOM   1512  C  CD2 . LEU   A 1 184  ? -43.12200  69.53000  24.44700  1.000 52.61896  ?  184  LEU   A CD2 1 
ATOM   1513  N  N   . LEU   A 1 185  ? -38.32300  68.41200  24.06100  1.000 42.80501  ?  185  LEU   A N   1 
ATOM   1514  C  CA  . LEU   A 1 185  ? -37.45600  68.01300  25.16200  1.000 52.24476  ?  185  LEU   A CA  1 
ATOM   1515  C  C   . LEU   A 1 185  ? -36.09000  68.67800  25.05500  1.000 61.31431  ?  185  LEU   A C   1 
ATOM   1516  O  O   . LEU   A 1 185  ? -35.49900  69.06000  26.07200  1.000 57.28292  ?  185  LEU   A O   1 
ATOM   1517  C  CB  . LEU   A 1 185  ? -37.32400  66.49200  25.19200  1.000 47.58018  ?  185  LEU   A CB  1 
ATOM   1518  C  CG  . LEU   A 1 185  ? -38.62600  65.74300  25.48400  1.000 41.67691  ?  185  LEU   A CG  1 
ATOM   1519  C  CD1 . LEU   A 1 185  ? -38.36600  64.25700  25.66400  1.000 55.42046  ?  185  LEU   A CD1 1 
ATOM   1520  C  CD2 . LEU   A 1 185  ? -39.30200  66.32200  26.71600  1.000 41.50234  ?  185  LEU   A CD2 1 
ATOM   1521  N  N   . ALA   A 1 186  ? -35.58000  68.83800  23.83200  1.000 51.20050  ?  186  ALA   A N   1 
ATOM   1522  C  CA  . ALA   A 1 186  ? -34.29300  69.49900  23.64000  1.000 47.57173  ?  186  ALA   A CA  1 
ATOM   1523  C  C   . ALA   A 1 186  ? -34.33000  70.93300  24.15200  1.000 51.06975  ?  186  ALA   A C   1 
ATOM   1524  O  O   . ALA   A 1 186  ? -33.41200  71.38000  24.85000  1.000 63.57157  ?  186  ALA   A O   1 
ATOM   1525  C  CB  . ALA   A 1 186  ? -33.90200  69.46400  22.16300  1.000 49.13597  ?  186  ALA   A CB  1 
ATOM   1526  N  N   . LEU   A 1 187  ? -35.38800  71.67300  23.81000  1.000 51.61882  ?  187  LEU   A N   1 
ATOM   1527  C  CA  . LEU   A 1 187  ? -35.54800  73.02300  24.33900  1.000 48.73692  ?  187  LEU   A CA  1 
ATOM   1528  C  C   . LEU   A 1 187  ? -35.65800  73.00900  25.85700  1.000 51.11200  ?  187  LEU   A C   1 
ATOM   1529  O  O   . LEU   A 1 187  ? -35.15200  73.91200  26.53200  1.000 54.18613  ?  187  LEU   A O   1 
ATOM   1530  C  CB  . LEU   A 1 187  ? -36.77900  73.69000  23.72700  1.000 43.86095  ?  187  LEU   A CB  1 
ATOM   1531  C  CG  . LEU   A 1 187  ? -37.01800  75.13500  24.17700  1.000 46.85539  ?  187  LEU   A CG  1 
ATOM   1532  C  CD1 . LEU   A 1 187  ? -35.92500  76.04600  23.65900  1.000 42.85351  ?  187  LEU   A CD1 1 
ATOM   1533  C  CD2 . LEU   A 1 187  ? -38.37100  75.63900  23.73000  1.000 46.26582  ?  187  LEU   A CD2 1 
ATOM   1534  N  N   . LYS   A 1 188  ? -36.32300  71.99400  26.41200  1.000 46.88077  ?  188  LYS   A N   1 
ATOM   1535  C  CA  . LYS   A 1 188  ? -36.46500  71.90700  27.86100  1.000 57.26682  ?  188  LYS   A CA  1 
ATOM   1536  C  C   . LYS   A 1 188  ? -35.10200  71.78400  28.53300  1.000 62.32075  ?  188  LYS   A C   1 
ATOM   1537  O  O   . LYS   A 1 188  ? -34.75700  72.58100  29.41200  1.000 78.44377  ?  188  LYS   A O   1 
ATOM   1538  C  CB  . LYS   A 1 188  ? -37.36800  70.72900  28.23300  1.000 46.49325  ?  188  LYS   A CB  1 
ATOM   1539  C  CG  . LYS   A 1 188  ? -37.46100  70.48600  29.72800  1.000 48.58552  ?  188  LYS   A CG  1 
ATOM   1540  C  CD  . LYS   A 1 188  ? -38.31800  69.27500  30.04800  1.000 50.53110  ?  188  LYS   A CD  1 
ATOM   1541  C  CE  . LYS   A 1 188  ? -37.66100  68.40400  31.10800  1.000 49.66108  ?  188  LYS   A CE  1 
ATOM   1542  N  NZ  . LYS   A 1 188  ? -38.65600  67.80500  32.03800  1.000 59.06295  ?  188  LYS   A NZ  1 
ATOM   1543  N  N   . ARG   A 1 189  ? -34.30600  70.79300  28.11900  1.000 60.33876  ?  189  ARG   A N   1 
ATOM   1544  C  CA  . ARG   A 1 189  ? -32.94700  70.66700  28.64000  1.000 53.64920  ?  189  ARG   A CA  1 
ATOM   1545  C  C   . ARG   A 1 189  ? -32.16100  71.95900  28.45100  1.000 52.72998  ?  189  ARG   A C   1 
ATOM   1546  O  O   . ARG   A 1 189  ? -31.40300  72.37400  29.33500  1.000 75.55288  ?  189  ARG   A O   1 
ATOM   1547  C  CB  . ARG   A 1 189  ? -32.22100  69.50600  27.95400  1.000 44.07348  ?  189  ARG   A CB  1 
ATOM   1548  C  CG  . ARG   A 1 189  ? -33.06100  68.25400  27.75500  1.000 66.68198  ?  189  ARG   A CG  1 
ATOM   1549  C  CD  . ARG   A 1 189  ? -32.31600  67.22400  26.91300  1.000 74.85650  ?  189  ARG   A CD  1 
ATOM   1550  N  NE  . ARG   A 1 189  ? -33.21600  66.43600  26.07700  1.000 78.18024  ?  189  ARG   A NE  1 
ATOM   1551  C  CZ  . ARG   A 1 189  ? -33.11600  66.33300  24.75800  1.000 76.03433  ?  189  ARG   A CZ  1 
ATOM   1552  N  NH1 . ARG   A 1 189  ? -32.15900  66.95200  24.08500  1.000 76.89477  ?  189  ARG   A NH1 1 
ATOM   1553  N  NH2 . ARG   A 1 189  ? -34.00100  65.59200  24.09600  1.000 70.10534  ?  189  ARG   A NH2 1 
ATOM   1554  N  N   . LEU   A 1 190  ? -32.35300  72.62200  27.31100  1.000 48.93149  ?  190  LEU   A N   1 
ATOM   1555  C  CA  . LEU   A 1 190  ? -31.57400  73.80300  26.96700  1.000 41.08037  ?  190  LEU   A CA  1 
ATOM   1556  C  C   . LEU   A 1 190  ? -32.03400  75.06500  27.68900  1.000 55.63850  ?  190  LEU   A C   1 
ATOM   1557  O  O   . LEU   A 1 190  ? -31.25100  76.01500  27.79900  1.000 62.73429  ?  190  LEU   A O   1 
ATOM   1558  C  CB  . LEU   A 1 190  ? -31.63600  74.03300  25.45800  1.000 41.84964  ?  190  LEU   A CB  1 
ATOM   1559  C  CG  . LEU   A 1 190  ? -30.30200  74.21300  24.74200  1.000 51.72880  ?  190  LEU   A CG  1 
ATOM   1560  C  CD1 . LEU   A 1 190  ? -29.36300  73.05500  25.06300  1.000 67.54011  ?  190  LEU   A CD1 1 
ATOM   1561  C  CD2 . LEU   A 1 190  ? -30.53200  74.33600  23.24800  1.000 52.22692  ?  190  LEU   A CD2 1 
ATOM   1562  N  N   . CYS   A 1 191  ? -33.27700  75.10600  28.17800  1.000 73.92993  ?  191  CYS   A N   1 
ATOM   1563  C  CA  . CYS   A 1 191  ? -33.83000  76.33000  28.74500  1.000 85.72553  ?  191  CYS   A CA  1 
ATOM   1564  C  C   . CYS   A 1 191  ? -34.38800  76.19000  30.15500  1.000 92.03547  ?  191  CYS   A C   1 
ATOM   1565  O  O   . CYS   A 1 191  ? -34.69200  77.21700  30.77300  1.000 84.30451  ?  191  CYS   A O   1 
ATOM   1566  C  CB  . CYS   A 1 191  ? -34.93900  76.89000  27.83900  1.000 66.66963  ?  191  CYS   A CB  1 
ATOM   1567  S  SG  . CYS   A 1 191  ? -34.34200  77.87700  26.44700  1.000 97.97356  ?  191  CYS   A SG  1 
ATOM   1568  N  N   . ALA   A 1 192  ? -34.53300  74.97900  30.68600  1.000 95.17897  ?  192  ALA   A N   1 
ATOM   1569  C  CA  . ALA   A 1 192  ? -35.10000  74.82900  32.01500  1.000 104.95308 ?  192  ALA   A CA  1 
ATOM   1570  C  C   . ALA   A 1 192  ? -34.08800  75.23500  33.08300  1.000 115.49754 ?  192  ALA   A C   1 
ATOM   1571  O  O   . ALA   A 1 192  ? -32.89000  75.39100  32.83100  1.000 104.66095 ?  192  ALA   A O   1 
ATOM   1572  C  CB  . ALA   A 1 192  ? -35.55700  73.39200  32.25800  1.000 101.67868 ?  192  ALA   A CB  1 
ATOM   1573  N  N   . GLU   A 1 193  ? -34.59500  75.39900  34.29600  1.000 122.68080 ?  193  GLU   A N   1 
ATOM   1574  C  CA  . GLU   A 1 193  ? -33.78000  75.70700  35.45400  1.000 121.09399 ?  193  GLU   A CA  1 
ATOM   1575  C  C   . GLU   A 1 193  ? -33.04900  74.45200  35.92800  1.000 121.83290 ?  193  GLU   A C   1 
ATOM   1576  O  O   . GLU   A 1 193  ? -33.57400  73.34100  35.82000  1.000 117.38988 ?  193  GLU   A O   1 
ATOM   1577  C  CB  . GLU   A 1 193  ? -34.65000  76.26400  36.57700  1.000 124.64949 ?  193  GLU   A CB  1 
ATOM   1578  C  CG  . GLU   A 1 193  ? -35.09800  77.70600  36.35900  1.000 113.98414 ?  193  GLU   A CG  1 
ATOM   1579  C  CD  . GLU   A 1 193  ? -36.43200  77.81200  35.63900  1.000 106.26946 ?  193  GLU   A CD  1 
ATOM   1580  O  OE1 . GLU   A 1 193  ? -36.75400  76.91000  34.83900  1.000 98.60203  ?  193  GLU   A OE1 1 
ATOM   1581  O  OE2 . GLU   A 1 193  ? -37.16000  78.80200  35.87100  1.000 108.04603 -1 193  GLU   A OE2 1 
ATOM   1582  N  N   . PRO   A 1 194  ? -31.82900  74.60100  36.44900  1.000 121.59033 ?  194  PRO   A N   1 
ATOM   1583  C  CA  . PRO   A 1 194  ? -31.06000  73.41800  36.85600  1.000 129.24741 ?  194  PRO   A CA  1 
ATOM   1584  C  C   . PRO   A 1 194  ? -31.49700  72.87200  38.20700  1.000 139.42686 ?  194  PRO   A C   1 
ATOM   1585  O  O   . PRO   A 1 194  ? -32.67700  72.56900  38.41000  1.000 132.01615 ?  194  PRO   A O   1 
ATOM   1586  C  CB  . PRO   A 1 194  ? -29.62200  73.94400  36.88700  1.000 123.02753 ?  194  PRO   A CB  1 
ATOM   1587  C  CG  . PRO   A 1 194  ? -29.77100  75.37900  37.27800  1.000 130.39877 ?  194  PRO   A CG  1 
ATOM   1588  C  CD  . PRO   A 1 194  ? -31.10700  75.85400  36.73500  1.000 115.16411 ?  194  PRO   A CD  1 
ATOM   1589  N  N   . LYS   A 1 195  ? -30.55300  72.73100  39.13400  1.000 141.68924 ?  195  LYS   A N   1 
ATOM   1590  C  CA  . LYS   A 1 195  ? -30.82300  72.25500  40.48900  1.000 139.02302 ?  195  LYS   A CA  1 
ATOM   1591  C  C   . LYS   A 1 195  ? -30.46100  73.37700  41.45700  1.000 152.15351 ?  195  LYS   A C   1 
ATOM   1592  O  O   . LYS   A 1 195  ? -29.31700  73.46400  41.90500  1.000 162.44748 ?  195  LYS   A O   1 
ATOM   1593  C  CB  . LYS   A 1 195  ? -30.04200  70.97800  40.80000  1.000 120.87276 ?  195  LYS   A CB  1 
ATOM   1594  C  CG  . LYS   A 1 195  ? -30.59800  70.18900  41.97700  1.000 120.12727 ?  195  LYS   A CG  1 
ATOM   1595  C  CD  . LYS   A 1 195  ? -29.86600  68.87000  42.17200  1.000 113.17310 ?  195  LYS   A CD  1 
ATOM   1596  C  CE  . LYS   A 1 195  ? -30.19700  68.26300  43.52800  1.000 97.86108  ?  195  LYS   A CE  1 
ATOM   1597  N  NZ  . LYS   A 1 195  ? -29.01000  67.66400  44.19800  1.000 78.78328  ?  195  LYS   A NZ  1 
ATOM   1598  N  N   . ARG   A 1 196  ? -31.45100  74.21700  41.78600  1.000 151.61694 ?  196  ARG   A N   1 
ATOM   1599  C  CA  . ARG   A 1 196  ? -31.31000  75.38800  42.65600  1.000 149.58252 ?  196  ARG   A CA  1 
ATOM   1600  C  C   . ARG   A 1 196  ? -29.98500  76.12600  42.48600  1.000 159.79449 ?  196  ARG   A C   1 
ATOM   1601  O  O   . ARG   A 1 196  ? -29.39000  76.59500  43.46300  1.000 160.78285 ?  196  ARG   A O   1 
ATOM   1602  C  CB  . ARG   A 1 196  ? -31.53700  74.99400  44.12600  1.000 134.48856 ?  196  ARG   A CB  1 
ATOM   1603  C  CG  . ARG   A 1 196  ? -30.76800  73.77600  44.65100  1.000 141.94746 ?  196  ARG   A CG  1 
ATOM   1604  C  CD  . ARG   A 1 196  ? -29.38500  74.02600  45.25900  1.000 147.33633 ?  196  ARG   A CD  1 
ATOM   1605  N  NE  . ARG   A 1 196  ? -28.65100  72.76600  45.31600  1.000 146.61738 ?  196  ARG   A NE  1 
ATOM   1606  C  CZ  . ARG   A 1 196  ? -27.94000  72.24500  44.32400  1.000 135.54996 ?  196  ARG   A CZ  1 
ATOM   1607  N  NH1 . ARG   A 1 196  ? -27.64300  72.94600  43.24200  1.000 143.92925 ?  196  ARG   A NH1 1 
ATOM   1608  N  NH2 . ARG   A 1 196  ? -27.49400  70.99400  44.43100  1.000 112.00926 ?  196  ARG   A NH2 1 
ATOM   1609  N  N   . GLY   A 1 197  ? -29.54100  76.26900  41.24300  1.000 153.93071 ?  197  GLY   A N   1 
ATOM   1610  C  CA  . GLY   A 1 197  ? -28.28800  76.93400  40.95800  1.000 144.82917 ?  197  GLY   A CA  1 
ATOM   1611  C  C   . GLY   A 1 197  ? -27.09200  76.16300  41.49100  1.000 146.23376 ?  197  GLY   A C   1 
ATOM   1612  O  O   . GLY   A 1 197  ? -27.20300  75.12200  42.13700  1.000 143.67682 ?  197  GLY   A O   1 
ATOM   1613  N  N   . GLU   A 1 198  ? -25.91200  76.70300  41.19900  1.000 132.12745 ?  198  GLU   A N   1 
ATOM   1614  C  CA  . GLU   A 1 198  ? -24.68400  76.11000  41.70900  1.000 117.54536 ?  198  GLU   A CA  1 
ATOM   1615  C  C   . GLU   A 1 198  ? -24.53400  76.43900  43.18900  1.000 117.72661 ?  198  GLU   A C   1 
ATOM   1616  O  O   . GLU   A 1 198  ? -25.18500  75.81700  44.03500  1.000 119.90132 ?  198  GLU   A O   1 
ATOM   1617  C  CB  . GLU   A 1 198  ? -23.48600  76.60000  40.89600  1.000 97.34572  ?  198  GLU   A CB  1 
ATOM   1618  C  CG  . GLU   A 1 198  ? -23.84000  76.86500  39.44000  1.000 104.51357 ?  198  GLU   A CG  1 
ATOM   1619  C  CD  . GLU   A 1 198  ? -22.65200  77.28000  38.59700  1.000 106.34405 ?  198  GLU   A CD  1 
ATOM   1620  O  OE1 . GLU   A 1 198  ? -21.52500  77.35400  39.13500  1.000 96.08560  ?  198  GLU   A OE1 1 
ATOM   1621  O  OE2 . GLU   A 1 198  ? -22.85100  77.53400  37.38900  1.000 81.42189  ?  198  GLU   A OE2 1 
ATOM   1622  N  N   . LYS   A 1 199  ? -23.68800  77.41300  43.51300  1.000 107.15681 ?  199  LYS   A N   1 
ATOM   1623  C  CA  . LYS   A 1 199  ? -23.55100  77.88900  44.87800  1.000 94.77122  ?  199  LYS   A CA  1 
ATOM   1624  C  C   . LYS   A 1 199  ? -23.65100  79.40800  44.89500  1.000 88.55604  ?  199  LYS   A C   1 
ATOM   1625  O  O   . LYS   A 1 199  ? -23.19600  80.07100  43.95300  1.000 87.19436  ?  199  LYS   A O   1 
ATOM   1626  C  CB  . LYS   A 1 199  ? -22.21600  77.44700  45.50000  1.000 87.40898  ?  199  LYS   A CB  1 
ATOM   1627  C  CG  . LYS   A 1 199  ? -22.07200  75.93900  45.66600  1.000 88.69043  ?  199  LYS   A CG  1 
ATOM   1628  C  CD  . LYS   A 1 199  ? -21.33700  75.32000  44.48600  1.000 90.33604  ?  199  LYS   A CD  1 
ATOM   1629  C  CE  . LYS   A 1 199  ? -21.77200  73.88400  44.25100  1.000 93.70480  ?  199  LYS   A CE  1 
ATOM   1630  N  NZ  . LYS   A 1 199  ? -21.84100  73.55200  42.80000  1.000 91.67365  ?  199  LYS   A NZ  1 
ATOM   1631  N  N   . PRO   A 1 200  ? -24.24600  79.98600  45.93400  1.000 87.52881  ?  200  PRO   A N   1 
ATOM   1632  C  CA  . PRO   A 1 200  ? -24.32600  81.44700  46.00800  1.000 80.51110  ?  200  PRO   A CA  1 
ATOM   1633  C  C   . PRO   A 1 200  ? -22.95500  82.06200  46.23500  1.000 75.89427  ?  200  PRO   A C   1 
ATOM   1634  O  O   . PRO   A 1 200  ? -22.08100  81.47900  46.88100  1.000 75.38695  ?  200  PRO   A O   1 
ATOM   1635  C  CB  . PRO   A 1 200  ? -25.25400  81.69400  47.20300  1.000 62.09726  ?  200  PRO   A CB  1 
ATOM   1636  C  CG  . PRO   A 1 200  ? -25.09700  80.47700  48.05000  1.000 81.83343  ?  200  PRO   A CG  1 
ATOM   1637  C  CD  . PRO   A 1 200  ? -24.88100  79.33600  47.09300  1.000 87.76825  ?  200  PRO   A CD  1 
ATOM   1638  N  N   . ILE   A 1 201  ? -22.76900  83.25400  45.67800  1.000 60.44678  ?  201  ILE   A N   1 
ATOM   1639  C  CA  . ILE   A 1 201  ? -21.52300  83.99100  45.85400  1.000 61.16003  ?  201  ILE   A CA  1 
ATOM   1640  C  C   . ILE   A 1 201  ? -21.55400  84.67100  47.21700  1.000 67.59406  ?  201  ILE   A C   1 
ATOM   1641  O  O   . ILE   A 1 201  ? -22.43300  85.49400  47.49300  1.000 76.39313  ?  201  ILE   A O   1 
ATOM   1642  C  CB  . ILE   A 1 201  ? -21.31900  85.01100  44.72500  1.000 52.94902  ?  201  ILE   A CB  1 
ATOM   1643  C  CG1 . ILE   A 1 201  ? -20.95100  84.29500  43.42400  1.000 53.39330  ?  201  ILE   A CG1 1 
ATOM   1644  C  CG2 . ILE   A 1 201  ? -20.24500  86.02100  45.10200  1.000 45.56661  ?  201  ILE   A CG2 1 
ATOM   1645  C  CD1 . ILE   A 1 201  ? -22.12300  84.05900  42.50000  1.000 59.06984  ?  201  ILE   A CD1 1 
ATOM   1646  N  N   . ASP   A 1 202  ? -20.59600  84.32300  48.07400  1.000 65.77871  ?  202  ASP   A N   1 
ATOM   1647  C  CA  . ASP   A 1 202  ? -20.52600  84.85700  49.42800  1.000 69.63974  ?  202  ASP   A CA  1 
ATOM   1648  C  C   . ASP   A 1 202  ? -19.34200  85.79300  49.62700  1.000 68.00944  ?  202  ASP   A C   1 
ATOM   1649  O  O   . ASP   A 1 202  ? -19.05100  86.17600  50.76500  1.000 77.94380  ?  202  ASP   A O   1 
ATOM   1650  C  CB  . ASP   A 1 202  ? -20.46300  83.71100  50.44000  1.000 70.67038  ?  202  ASP   A CB  1 
ATOM   1651  C  CG  . ASP   A 1 202  ? -20.94100  84.12300  51.81800  1.000 102.95004 ?  202  ASP   A CG  1 
ATOM   1652  O  OD1 . ASP   A 1 202  ? -21.32200  85.30000  51.99200  1.000 110.62255 ?  202  ASP   A OD1 1 
ATOM   1653  O  OD2 . ASP   A 1 202  ? -20.93500  83.26600  52.72700  1.000 120.60057 -1 202  ASP   A OD2 1 
ATOM   1654  N  N   . LYS   A 1 203  ? -18.65900  86.17800  48.55500  1.000 69.49239  ?  203  LYS   A N   1 
ATOM   1655  C  CA  . LYS   A 1 203  ? -17.43300  86.95000  48.65100  1.000 52.34812  ?  203  LYS   A CA  1 
ATOM   1656  C  C   . LYS   A 1 203  ? -17.54400  88.23000  47.83500  1.000 41.78684  ?  203  LYS   A C   1 
ATOM   1657  O  O   . LYS   A 1 203  ? -18.32700  88.32200  46.88600  1.000 41.84918  ?  203  LYS   A O   1 
ATOM   1658  C  CB  . LYS   A 1 203  ? -16.23200  86.13500  48.15700  1.000 41.54257  ?  203  LYS   A CB  1 
ATOM   1659  C  CG  . LYS   A 1 203  ? -16.05300  84.79900  48.85500  1.000 61.78232  ?  203  LYS   A CG  1 
ATOM   1660  C  CD  . LYS   A 1 203  ? -15.28400  84.95300  50.15500  1.000 66.60863  ?  203  LYS   A CD  1 
ATOM   1661  C  CE  . LYS   A 1 203  ? -15.20500  83.63400  50.90800  1.000 73.87010  ?  203  LYS   A CE  1 
ATOM   1662  N  NZ  . LYS   A 1 203  ? -13.86800  82.98400  50.77800  1.000 84.26497  ?  203  LYS   A NZ  1 
ATOM   1663  N  N   . THR   A 1 204  ? -16.74600  89.22200  48.21900  1.000 33.76961  ?  204  THR   A N   1 
ATOM   1664  C  CA  . THR   A 1 204  ? -16.50900  90.39900  47.40200  1.000 40.75682  ?  204  THR   A CA  1 
ATOM   1665  C  C   . THR   A 1 204  ? -15.20700  90.20500  46.62600  1.000 48.20663  ?  204  THR   A C   1 
ATOM   1666  O  O   . THR   A 1 204  ? -14.51400  89.19500  46.77300  1.000 45.03710  ?  204  THR   A O   1 
ATOM   1667  C  CB  . THR   A 1 204  ? -16.46200  91.66000  48.26700  1.000 41.35433  ?  204  THR   A CB  1 
ATOM   1668  O  OG1 . THR   A 1 204  ? -15.20100  91.72900  48.94300  1.000 50.96221  ?  204  THR   A OG1 1 
ATOM   1669  C  CG2 . THR   A 1 204  ? -17.57700  91.63600  49.29800  1.000 42.19935  ?  204  THR   A CG2 1 
ATOM   1670  N  N   . PHE   A 1 205  ? -14.86700  91.18500  45.78400  1.000 48.36086  ?  205  PHE   A N   1 
ATOM   1671  C  CA  . PHE   A 1 205  ? -13.64300  91.06000  44.99800  1.000 41.06456  ?  205  PHE   A CA  1 
ATOM   1672  C  C   . PHE   A 1 205  ? -12.40800  91.25800  45.86700  1.000 47.05490  ?  205  PHE   A C   1 
ATOM   1673  O  O   . PHE   A 1 205  ? -11.47100  90.45100  45.81800  1.000 48.06302  ?  205  PHE   A O   1 
ATOM   1674  C  CB  . PHE   A 1 205  ? -13.63200  92.04800  43.83200  1.000 34.87294  ?  205  PHE   A CB  1 
ATOM   1675  C  CG  . PHE   A 1 205  ? -12.43000  91.89800  42.93700  1.000 46.49403  ?  205  PHE   A CG  1 
ATOM   1676  C  CD1 . PHE   A 1 205  ? -12.31500  90.81000  42.08700  1.000 43.55730  ?  205  PHE   A CD1 1 
ATOM   1677  C  CD2 . PHE   A 1 205  ? -11.39900  92.81900  42.97100  1.000 47.30555  ?  205  PHE   A CD2 1 
ATOM   1678  C  CE1 . PHE   A 1 205  ? -11.20800  90.66300  41.27400  1.000 28.14266  ?  205  PHE   A CE1 1 
ATOM   1679  C  CE2 . PHE   A 1 205  ? -10.29000  92.67700  42.16400  1.000 47.01647  ?  205  PHE   A CE2 1 
ATOM   1680  C  CZ  . PHE   A 1 205  ? -10.19400  91.59500  41.31400  1.000 35.75938  ?  205  PHE   A CZ  1 
ATOM   1681  N  N   . HIS   A 1 206  ? -12.38100  92.33000  46.66900  1.000 44.14293  ?  206  HIS   A N   1 
ATOM   1682  C  CA  . HIS   A 1 206  ? -11.19300  92.59200  47.47600  1.000 49.40330  ?  206  HIS   A CA  1 
ATOM   1683  C  C   . HIS   A 1 206  ? -10.91700  91.45400  48.44600  1.000 50.54122  ?  206  HIS   A C   1 
ATOM   1684  O  O   . HIS   A 1 206  ? -9.75200   91.15300  48.72800  1.000 61.85160  ?  206  HIS   A O   1 
ATOM   1685  C  CB  . HIS   A 1 206  ? -11.32300  93.91400  48.23800  1.000 44.13702  ?  206  HIS   A CB  1 
ATOM   1686  C  CG  . HIS   A 1 206  ? -12.70600  94.20500  48.72800  1.000 55.88404  ?  206  HIS   A CG  1 
ATOM   1687  N  ND1 . HIS   A 1 206  ? -13.60600  94.96100  48.00900  1.000 52.86710  ?  206  HIS   A ND1 1 
ATOM   1688  C  CD2 . HIS   A 1 206  ? -13.33800  93.85800  49.87400  1.000 66.83993  ?  206  HIS   A CD2 1 
ATOM   1689  C  CE1 . HIS   A 1 206  ? -14.73600  95.05900  48.68600  1.000 59.32058  ?  206  HIS   A CE1 1 
ATOM   1690  N  NE2 . HIS   A 1 206  ? -14.60000  94.39700  49.82100  1.000 62.58985  ?  206  HIS   A NE2 1 
ATOM   1691  N  N   . GLN   A 1 207  ? -11.96600  90.80900  48.95900  1.000 41.55192  ?  207  GLN   A N   1 
ATOM   1692  C  CA  . GLN   A 1 207  ? -11.77200  89.61500  49.77100  1.000 37.64542  ?  207  GLN   A CA  1 
ATOM   1693  C  C   . GLN   A 1 207  ? -10.93000  88.59100  49.02200  1.000 43.66682  ?  207  GLN   A C   1 
ATOM   1694  O  O   . GLN   A 1 207  ? -9.86600   88.17800  49.49000  1.000 63.34235  ?  207  GLN   A O   1 
ATOM   1695  C  CB  . GLN   A 1 207  ? -13.12500  89.01600  50.16300  1.000 50.44718  ?  207  GLN   A CB  1 
ATOM   1696  C  CG  . GLN   A 1 207  ? -13.90500  89.84100  51.17500  1.000 62.46879  ?  207  GLN   A CG  1 
ATOM   1697  C  CD  . GLN   A 1 207  ? -15.15000  89.13300  51.67800  1.000 66.34980  ?  207  GLN   A CD  1 
ATOM   1698  O  OE1 . GLN   A 1 207  ? -15.36200  87.95300  51.39700  1.000 60.64416  ?  207  GLN   A OE1 1 
ATOM   1699  N  NE2 . GLN   A 1 207  ? -15.98500  89.85500  52.41900  1.000 52.21368  ?  207  GLN   A NE2 1 
ATOM   1700  N  N   . LEU   A 1 208  ? -11.38200  88.19900  47.83000  1.000 47.78309  ?  208  LEU   A N   1 
ATOM   1701  C  CA  . LEU   A 1 208  ? -10.67500  87.16700  47.08000  1.000 51.95086  ?  208  LEU   A CA  1 
ATOM   1702  C  C   . LEU   A 1 208  ? -9.30000   87.64600  46.63800  1.000 44.62820  ?  208  LEU   A C   1 
ATOM   1703  O  O   . LEU   A 1 208  ? -8.34800   86.85800  46.59000  1.000 50.11617  ?  208  LEU   A O   1 
ATOM   1704  C  CB  . LEU   A 1 208  ? -11.50600  86.73000  45.87600  1.000 47.35981  ?  208  LEU   A CB  1 
ATOM   1705  C  CG  . LEU   A 1 208  ? -12.84200  86.07600  46.22300  1.000 43.36590  ?  208  LEU   A CG  1 
ATOM   1706  C  CD1 . LEU   A 1 208  ? -13.71700  85.93100  44.98800  1.000 36.07604  ?  208  LEU   A CD1 1 
ATOM   1707  C  CD2 . LEU   A 1 208  ? -12.59900  84.72800  46.87100  1.000 42.84130  ?  208  LEU   A CD2 1 
ATOM   1708  N  N   . PHE   A 1 209  ? -9.17000   88.93400  46.31000  1.000 48.08030  ?  209  PHE   A N   1 
ATOM   1709  C  CA  . PHE   A 1 209  ? -7.85600   89.45600  45.94900  1.000 50.46802  ?  209  PHE   A CA  1 
ATOM   1710  C  C   . PHE   A 1 209  ? -6.88900   89.33400  47.11400  1.000 47.68064  ?  209  PHE   A C   1 
ATOM   1711  O  O   . PHE   A 1 209  ? -5.72500   88.96300  46.92900  1.000 53.33126  ?  209  PHE   A O   1 
ATOM   1712  C  CB  . PHE   A 1 209  ? -7.96100   90.91000  45.49700  1.000 42.15479  ?  209  PHE   A CB  1 
ATOM   1713  C  CG  . PHE   A 1 209  ? -6.63100   91.55900  45.22600  1.000 38.26802  ?  209  PHE   A CG  1 
ATOM   1714  C  CD1 . PHE   A 1 209  ? -5.88700   91.21500  44.10800  1.000 32.76738  ?  209  PHE   A CD1 1 
ATOM   1715  C  CD2 . PHE   A 1 209  ? -6.13300   92.52600  46.08400  1.000 45.34622  ?  209  PHE   A CD2 1 
ATOM   1716  C  CE1 . PHE   A 1 209  ? -4.66400   91.82200  43.85600  1.000 38.61886  ?  209  PHE   A CE1 1 
ATOM   1717  C  CE2 . PHE   A 1 209  ? -4.91500   93.13600  45.83800  1.000 38.27241  ?  209  PHE   A CE2 1 
ATOM   1718  C  CZ  . PHE   A 1 209  ? -4.18000   92.78500  44.72300  1.000 39.59709  ?  209  PHE   A CZ  1 
ATOM   1719  N  N   . GLU   A 1 210  ? -7.36400   89.62000  48.32800  1.000 46.28994  ?  210  GLU   A N   1 
ATOM   1720  C  CA  . GLU   A 1 210  ? -6.51100   89.51000  49.50300  1.000 44.84836  ?  210  GLU   A CA  1 
ATOM   1721  C  C   . GLU   A 1 210  ? -6.14600   88.06200  49.80500  1.000 40.67692  ?  210  GLU   A C   1 
ATOM   1722  O  O   . GLU   A 1 210  ? -5.09600   87.80700  50.40300  1.000 48.06579  ?  210  GLU   A O   1 
ATOM   1723  C  CB  . GLU   A 1 210  ? -7.18900   90.16000  50.70700  1.000 35.89921  ?  210  GLU   A CB  1 
ATOM   1724  C  CG  . GLU   A 1 210  ? -7.29700   91.67400  50.59800  1.000 42.60417  ?  210  GLU   A CG  1 
ATOM   1725  C  CD  . GLU   A 1 210  ? -8.24800   92.26500  51.61500  1.000 52.70295  ?  210  GLU   A CD  1 
ATOM   1726  O  OE1 . GLU   A 1 210  ? -8.81300   91.48800  52.41500  1.000 43.72613  ?  210  GLU   A OE1 1 
ATOM   1727  O  OE2 . GLU   A 1 210  ? -8.43100   93.50200  51.61500  1.000 45.93182  -1 210  GLU   A OE2 1 
ATOM   1728  N  N   . GLN   A 1 211  ? -6.98300   87.10400  49.40200  1.000 35.00987  ?  211  GLN   A N   1 
ATOM   1729  C  CA  . GLN   A 1 211  ? -6.60300   85.70100  49.54400  1.000 44.45785  ?  211  GLN   A CA  1 
ATOM   1730  C  C   . GLN   A 1 211  ? -5.56600   85.29600  48.50300  1.000 48.53718  ?  211  GLN   A C   1 
ATOM   1731  O  O   . GLN   A 1 211  ? -4.71800   84.43900  48.77500  1.000 59.67675  ?  211  GLN   A O   1 
ATOM   1732  C  CB  . GLN   A 1 211  ? -7.83800   84.80500  49.44500  1.000 44.07082  ?  211  GLN   A CB  1 
ATOM   1733  C  CG  . GLN   A 1 211  ? -9.06100   85.37200  50.14700  1.000 65.80158  ?  211  GLN   A CG  1 
ATOM   1734  C  CD  . GLN   A 1 211  ? -10.14700  84.34200  50.39200  1.000 92.78184  ?  211  GLN   A CD  1 
ATOM   1735  O  OE1 . GLN   A 1 211  ? -9.98200   83.16200  50.08300  1.000 84.68653  ?  211  GLN   A OE1 1 
ATOM   1736  N  NE2 . GLN   A 1 211  ? -11.27500  84.79000  50.93700  1.000 79.27924  ?  211  GLN   A NE2 1 
ATOM   1737  N  N   . GLN   A 1 212  ? -5.61600   85.89300  47.31000  1.000 40.72188  ?  212  GLN   A N   1 
ATOM   1738  C  CA  . GLN   A 1 212  ? -4.60300   85.59300  46.30600  1.000 44.16006  ?  212  GLN   A CA  1 
ATOM   1739  C  C   . GLN   A 1 212  ? -3.27400   86.25000  46.64800  1.000 49.02606  ?  212  GLN   A C   1 
ATOM   1740  O  O   . GLN   A 1 212  ? -2.21200   85.69200  46.34500  1.000 43.66027  ?  212  GLN   A O   1 
ATOM   1741  C  CB  . GLN   A 1 212  ? -5.08400   86.03700  44.92600  1.000 38.06707  ?  212  GLN   A CB  1 
ATOM   1742  C  CG  . GLN   A 1 212  ? -4.17700   85.61700  43.78000  1.000 38.59735  ?  212  GLN   A CG  1 
ATOM   1743  C  CD  . GLN   A 1 212  ? -4.24500   84.13000  43.49200  1.000 38.32901  ?  212  GLN   A CD  1 
ATOM   1744  O  OE1 . GLN   A 1 212  ? -5.32500   83.53900  43.44200  1.000 48.34362  ?  212  GLN   A OE1 1 
ATOM   1745  N  NE2 . GLN   A 1 212  ? -3.08400   83.51400  43.30600  1.000 43.69492  ?  212  GLN   A NE2 1 
ATOM   1746  N  N   . VAL   A 1 213  ? -3.31200   87.42400  47.28300  1.000 35.85312  ?  213  VAL   A N   1 
ATOM   1747  C  CA  . VAL   A 1 213  ? -2.07900   88.08700  47.69400  1.000 41.59433  ?  213  VAL   A CA  1 
ATOM   1748  C  C   . VAL   A 1 213  ? -1.34500   87.24700  48.72900  1.000 44.89525  ?  213  VAL   A C   1 
ATOM   1749  O  O   . VAL   A 1 213  ? -0.11400   87.29800  48.82400  1.000 48.27236  ?  213  VAL   A O   1 
ATOM   1750  C  CB  . VAL   A 1 213  ? -2.38400   89.51100  48.20500  1.000 35.78654  ?  213  VAL   A CB  1 
ATOM   1751  C  CG1 . VAL   A 1 213  ? -1.13300   90.16900  48.75700  1.000 34.54222  ?  213  VAL   A CG1 1 
ATOM   1752  C  CG2 . VAL   A 1 213  ? -2.94100   90.35900  47.07500  1.000 39.40416  ?  213  VAL   A CG2 1 
ATOM   1753  N  N   . GLU   A 1 214  ? -2.07100   86.43700  49.49700  1.000 50.75423  ?  214  GLU   A N   1 
ATOM   1754  C  CA  . GLU   A 1 214  ? -1.40800   85.52900  50.42200  1.000 49.76926  ?  214  GLU   A CA  1 
ATOM   1755  C  C   . GLU   A 1 214  ? -0.90800   84.26400  49.73800  1.000 52.63495  ?  214  GLU   A C   1 
ATOM   1756  O  O   . GLU   A 1 214  ? 0.01200    83.62100  50.25600  1.000 61.84626  ?  214  GLU   A O   1 
ATOM   1757  C  CB  . GLU   A 1 214  ? -2.34700   85.15900  51.57200  1.000 46.46402  ?  214  GLU   A CB  1 
ATOM   1758  C  CG  . GLU   A 1 214  ? -3.07000   86.34600  52.19000  1.000 67.67738  ?  214  GLU   A CG  1 
ATOM   1759  C  CD  . GLU   A 1 214  ? -2.18200   87.17800  53.09800  1.000 83.94914  ?  214  GLU   A CD  1 
ATOM   1760  O  OE1 . GLU   A 1 214  ? -1.46300   86.59100  53.93400  1.000 90.71165  ?  214  GLU   A OE1 1 
ATOM   1761  O  OE2 . GLU   A 1 214  ? -2.20700   88.42200  52.97700  1.000 81.46558  -1 214  GLU   A OE2 1 
ATOM   1762  N  N   . MET   A 1 215  ? -1.48400   83.89700  48.59000  1.000 48.70253  ?  215  MET   A N   1 
ATOM   1763  C  CA  . MET   A 1 215  ? -1.04200   82.69700  47.88500  1.000 53.54352  ?  215  MET   A CA  1 
ATOM   1764  C  C   . MET   A 1 215  ? 0.17400    82.97300  47.00900  1.000 52.34686  ?  215  MET   A C   1 
ATOM   1765  O  O   . MET   A 1 215  ? 1.10500    82.16100  46.96500  1.000 54.74756  ?  215  MET   A O   1 
ATOM   1766  C  CB  . MET   A 1 215  ? -2.18500   82.13200  47.04000  1.000 51.99664  ?  215  MET   A CB  1 
ATOM   1767  C  CG  . MET   A 1 215  ? -3.34500   81.58100  47.84900  1.000 60.55557  ?  215  MET   A CG  1 
ATOM   1768  S  SD  . MET   A 1 215  ? -2.93100   80.03300  48.67600  1.000 102.12632 ?  215  MET   A SD  1 
ATOM   1769  C  CE  . MET   A 1 215  ? -2.88800   78.90500  47.28500  1.000 90.30941  ?  215  MET   A CE  1 
ATOM   1770  N  N   . THR   A 1 216  ? 0.18100    84.10300  46.30500  1.000 53.67224  ?  216  THR   A N   1 
ATOM   1771  C  CA  . THR   A 1 216  ? 1.28500    84.49700  45.42900  1.000 36.19403  ?  216  THR   A CA  1 
ATOM   1772  C  C   . THR   A 1 216  ? 1.72600    85.91100  45.78700  1.000 41.38032  ?  216  THR   A C   1 
ATOM   1773  O  O   . THR   A 1 216  ? 1.56400    86.84600  44.99300  1.000 44.95984  ?  216  THR   A O   1 
ATOM   1774  C  CB  . THR   A 1 216  ? 0.87400    84.41000  43.95900  1.000 34.36844  ?  216  THR   A CB  1 
ATOM   1775  O  OG1 . THR   A 1 216  ? -0.33600   85.15100  43.75900  1.000 50.18775  ?  216  THR   A OG1 1 
ATOM   1776  C  CG2 . THR   A 1 216  ? 0.64400    82.96400  43.55800  1.000 35.01636  ?  216  THR   A CG2 1 
ATOM   1777  N  N   . PRO   A 1 217  ? 2.30100    86.10100  46.97900  1.000 40.72465  ?  217  PRO   A N   1 
ATOM   1778  C  CA  . PRO   A 1 217  ? 2.65600    87.46900  47.39500  1.000 43.30368  ?  217  PRO   A CA  1 
ATOM   1779  C  C   . PRO   A 1 217  ? 3.78300    88.07500  46.58300  1.000 40.89369  ?  217  PRO   A C   1 
ATOM   1780  O  O   . PRO   A 1 217  ? 3.74000    89.27200  46.27000  1.000 43.23889  ?  217  PRO   A O   1 
ATOM   1781  C  CB  . PRO   A 1 217  ? 3.04400    87.29200  48.86900  1.000 38.21223  ?  217  PRO   A CB  1 
ATOM   1782  C  CG  . PRO   A 1 217  ? 3.51100    85.88000  48.96200  1.000 48.25056  ?  217  PRO   A CG  1 
ATOM   1783  C  CD  . PRO   A 1 217  ? 2.67200    85.09800  47.99300  1.000 40.97599  ?  217  PRO   A CD  1 
ATOM   1784  N  N   . ASP   A 1 218  ? 4.79300    87.28800  46.22800  1.000 36.85407  ?  218  ASP   A N   1 
ATOM   1785  C  CA  . ASP   A 1 218  ? 5.96800    87.81300  45.55200  1.000 57.81416  ?  218  ASP   A CA  1 
ATOM   1786  C  C   . ASP   A 1 218  ? 5.90000    87.67400  44.03500  1.000 51.20675  ?  218  ASP   A C   1 
ATOM   1787  O  O   . ASP   A 1 218  ? 6.84000    88.08500  43.34800  1.000 45.39004  ?  218  ASP   A O   1 
ATOM   1788  C  CB  . ASP   A 1 218  ? 7.22800    87.13000  46.09300  1.000 55.53996  ?  218  ASP   A CB  1 
ATOM   1789  C  CG  . ASP   A 1 218  ? 7.34000    87.23000  47.60800  1.000 46.92234  ?  218  ASP   A CG  1 
ATOM   1790  O  OD1 . ASP   A 1 218  ? 6.85600    88.22800  48.18600  1.000 35.68731  ?  218  ASP   A OD1 1 
ATOM   1791  O  OD2 . ASP   A 1 218  ? 7.91400    86.30600  48.22200  1.000 64.50541  -1 218  ASP   A OD2 1 
ATOM   1792  N  N   . HIS   A 1 219  ? 4.81900    87.11500  43.49800  1.000 42.36926  ?  219  HIS   A N   1 
ATOM   1793  C  CA  . HIS   A 1 219  ? 4.61900    87.12100  42.05600  1.000 31.77020  ?  219  HIS   A CA  1 
ATOM   1794  C  C   . HIS   A 1 219  ? 4.40300    88.54500  41.56000  1.000 39.89543  ?  219  HIS   A C   1 
ATOM   1795  O  O   . HIS   A 1 219  ? 3.83700    89.39200  42.25700  1.000 42.68888  ?  219  HIS   A O   1 
ATOM   1796  C  CB  . HIS   A 1 219  ? 3.41500    86.26400  41.66800  1.000 33.20779  ?  219  HIS   A CB  1 
ATOM   1797  C  CG  . HIS   A 1 219  ? 3.68000    84.79200  41.69700  1.000 31.37291  ?  219  HIS   A CG  1 
ATOM   1798  N  ND1 . HIS   A 1 219  ? 4.26900    84.16200  42.77300  1.000 38.12215  ?  219  HIS   A ND1 1 
ATOM   1799  C  CD2 . HIS   A 1 219  ? 3.43700    83.82500  40.78100  1.000 36.72979  ?  219  HIS   A CD2 1 
ATOM   1800  C  CE1 . HIS   A 1 219  ? 4.37500    82.87000  42.51900  1.000 40.65488  ?  219  HIS   A CE1 1 
ATOM   1801  N  NE2 . HIS   A 1 219  ? 3.87800    82.63900  41.31700  1.000 42.87061  ?  219  HIS   A NE2 1 
ATOM   1802  N  N   . VAL   A 1 220  ? 4.86100    88.80600  40.33800  1.000 37.47624  ?  220  VAL   A N   1 
ATOM   1803  C  CA  . VAL   A 1 220  ? 4.60900    90.09700  39.71300  1.000 35.78772  ?  220  VAL   A CA  1 
ATOM   1804  C  C   . VAL   A 1 220  ? 3.11700    90.24700  39.45400  1.000 38.63769  ?  220  VAL   A C   1 
ATOM   1805  O  O   . VAL   A 1 220  ? 2.47400    89.35000  38.89400  1.000 45.36884  ?  220  VAL   A O   1 
ATOM   1806  C  CB  . VAL   A 1 220  ? 5.41200    90.23100  38.41400  1.000 24.28108  ?  220  VAL   A CB  1 
ATOM   1807  C  CG1 . VAL   A 1 220  ? 5.34400    91.65500  37.90700  1.000 34.13485  ?  220  VAL   A CG1 1 
ATOM   1808  C  CG2 . VAL   A 1 220  ? 6.84500    89.81200  38.65200  1.000 32.41718  ?  220  VAL   A CG2 1 
ATOM   1809  N  N   . ALA   A 1 221  ? 2.55800    91.38600  39.86200  1.000 42.25117  ?  221  ALA   A N   1 
ATOM   1810  C  CA  . ALA   A 1 221  ? 1.13400    91.65200  39.70000  1.000 34.74700  ?  221  ALA   A CA  1 
ATOM   1811  C  C   . ALA   A 1 221  ? 0.84100    92.58300  38.53100  1.000 28.97221  ?  221  ALA   A C   1 
ATOM   1812  O  O   . ALA   A 1 221  ? 0.01800    92.25600  37.67100  1.000 40.87661  ?  221  ALA   A O   1 
ATOM   1813  C  CB  . ALA   A 1 221  ? 0.55500    92.23900  40.99200  1.000 40.27236  ?  221  ALA   A CB  1 
ATOM   1814  N  N   . VAL   A 1 222  ? 1.48900    93.74500  38.48200  1.000 30.05748  ?  222  VAL   A N   1 
ATOM   1815  C  CA  . VAL   A 1 222  ? 1.30600    94.68700  37.38600  1.000 49.66252  ?  222  VAL   A CA  1 
ATOM   1816  C  C   . VAL   A 1 222  ? 2.67100    95.13300  36.87900  1.000 42.34268  ?  222  VAL   A C   1 
ATOM   1817  O  O   . VAL   A 1 222  ? 3.64500    95.19800  37.63500  1.000 41.95120  ?  222  VAL   A O   1 
ATOM   1818  C  CB  . VAL   A 1 222  ? 0.46100    95.91000  37.80700  1.000 38.48573  ?  222  VAL   A CB  1 
ATOM   1819  C  CG1 . VAL   A 1 222  ? -0.08900   96.62000  36.58100  1.000 41.11661  ?  222  VAL   A CG1 1 
ATOM   1820  C  CG2 . VAL   A 1 222  ? -0.66400   95.49500  38.74200  1.000 55.84913  ?  222  VAL   A CG2 1 
ATOM   1821  N  N   . VAL   A 1 223  ? 2.73500    95.43600  35.58300  1.000 28.76248  ?  223  VAL   A N   1 
ATOM   1822  C  CA  . VAL   A 1 223  ? 3.94400    95.92800  34.92600  1.000 38.06970  ?  223  VAL   A CA  1 
ATOM   1823  C  C   . VAL   A 1 223  ? 3.55500    97.14500  34.09300  1.000 45.82133  ?  223  VAL   A C   1 
ATOM   1824  O  O   . VAL   A 1 223  ? 2.80200    97.01800  33.11900  1.000 49.84120  ?  223  VAL   A O   1 
ATOM   1825  C  CB  . VAL   A 1 223  ? 4.60600    94.85700  34.04400  1.000 46.36611  ?  223  VAL   A CB  1 
ATOM   1826  C  CG1 . VAL   A 1 223  ? 5.81300    95.43500  33.31900  1.000 32.62253  ?  223  VAL   A CG1 1 
ATOM   1827  C  CG2 . VAL   A 1 223  ? 5.00800    93.64600  34.87600  1.000 41.75939  ?  223  VAL   A CG2 1 
ATOM   1828  N  N   . ASP   A 1 224  ? 4.05900    98.31800  34.46900  1.000 36.53761  ?  224  ASP   A N   1 
ATOM   1829  C  CA  . ASP   A 1 224  ? 3.87500    99.53800  33.69300  1.000 43.62542  ?  224  ASP   A CA  1 
ATOM   1830  C  C   . ASP   A 1 224  ? 5.24200    100.11400 33.35900  1.000 55.23773  ?  224  ASP   A C   1 
ATOM   1831  O  O   . ASP   A 1 224  ? 6.10300    100.22400 34.24000  1.000 50.33254  ?  224  ASP   A O   1 
ATOM   1832  C  CB  . ASP   A 1 224  ? 3.02500    100.56600 34.44700  1.000 47.80021  ?  224  ASP   A CB  1 
ATOM   1833  C  CG  . ASP   A 1 224  ? 2.78600    101.83300 33.63900  1.000 64.44088  ?  224  ASP   A CG  1 
ATOM   1834  O  OD1 . ASP   A 1 224  ? 2.61100    101.73400 32.40500  1.000 53.01717  ?  224  ASP   A OD1 1 
ATOM   1835  O  OD2 . ASP   A 1 224  ? 2.76200    102.92800 34.24300  1.000 69.06591  -1 224  ASP   A OD2 1 
ATOM   1836  N  N   . ARG   A 1 225  ? 5.43300    100.48200 32.09000  1.000 68.99085  ?  225  ARG   A N   1 
ATOM   1837  C  CA  . ARG   A 1 225  ? 6.73900    100.88200 31.57800  1.000 68.74165  ?  225  ARG   A CA  1 
ATOM   1838  C  C   . ARG   A 1 225  ? 7.76600    99.79400  31.86200  1.000 67.27460  ?  225  ARG   A C   1 
ATOM   1839  O  O   . ARG   A 1 225  ? 7.62900    98.66100  31.38900  1.000 70.86820  ?  225  ARG   A O   1 
ATOM   1840  C  CB  . ARG   A 1 225  ? 7.17900    102.21500 32.18700  1.000 71.40035  ?  225  ARG   A CB  1 
ATOM   1841  C  CG  . ARG   A 1 225  ? 6.10900    103.29400 32.14900  1.000 74.36547  ?  225  ARG   A CG  1 
ATOM   1842  C  CD  . ARG   A 1 225  ? 5.76100    103.68200 30.71700  1.000 82.68550  ?  225  ARG   A CD  1 
ATOM   1843  N  NE  . ARG   A 1 225  ? 4.90400    104.86200 30.66000  1.000 101.04106 ?  225  ARG   A NE  1 
ATOM   1844  C  CZ  . ARG   A 1 225  ? 3.58800    104.84400 30.82200  1.000 91.70516  ?  225  ARG   A CZ  1 
ATOM   1845  N  NH1 . ARG   A 1 225  ? 2.93200    103.71600 31.04200  1.000 71.84441  ?  225  ARG   A NH1 1 
ATOM   1846  N  NH2 . ARG   A 1 225  ? 2.91100    105.98800 30.76000  1.000 72.86211  ?  225  ARG   A NH2 1 
ATOM   1847  N  N   . GLY   A 1 226  ? 8.79400    100.12000 32.63600  1.000 49.10575  ?  226  GLY   A N   1 
ATOM   1848  C  CA  . GLY   A 1 226  ? 9.76700    99.11800  33.01100  1.000 49.45862  ?  226  GLY   A CA  1 
ATOM   1849  C  C   . GLY   A 1 226  ? 9.65800    98.70800  34.46400  1.000 52.39144  ?  226  GLY   A C   1 
ATOM   1850  O  O   . GLY   A 1 226  ? 10.19400   97.67300  34.86100  1.000 55.04107  ?  226  GLY   A O   1 
ATOM   1851  N  N   . GLN   A 1 227  ? 8.97600    99.51900  35.26900  1.000 54.65012  ?  227  GLN   A N   1 
ATOM   1852  C  CA  . GLN   A 1 227  ? 8.78700    99.21400  36.67800  1.000 48.22664  ?  227  GLN   A CA  1 
ATOM   1853  C  C   . GLN   A 1 227  ? 7.67800    98.17800  36.85400  1.000 55.34621  ?  227  GLN   A C   1 
ATOM   1854  O  O   . GLN   A 1 227  ? 6.86700    97.93600  35.95500  1.000 52.16950  ?  227  GLN   A O   1 
ATOM   1855  C  CB  . GLN   A 1 227  ? 8.46000    100.48600 37.46100  1.000 55.64907  ?  227  GLN   A CB  1 
ATOM   1856  C  CG  . GLN   A 1 227  ? 9.37700    101.65700 37.13800  1.000 59.66336  ?  227  GLN   A CG  1 
ATOM   1857  C  CD  . GLN   A 1 227  ? 8.62000    102.86100 36.60800  1.000 84.79399  ?  227  GLN   A CD  1 
ATOM   1858  O  OE1 . GLN   A 1 227  ? 7.66400    102.71800 35.84500  1.000 80.41953  ?  227  GLN   A OE1 1 
ATOM   1859  N  NE2 . GLN   A 1 227  ? 9.05100    104.05400 37.00200  1.000 96.06613  ?  227  GLN   A NE2 1 
ATOM   1860  N  N   . SER   A 1 228  ? 7.64900    97.56400  38.03700  1.000 45.45972  ?  228  SER   A N   1 
ATOM   1861  C  CA  . SER   A 1 228  ? 6.71800    96.48100  38.31100  1.000 34.36502  ?  228  SER   A CA  1 
ATOM   1862  C  C   . SER   A 1 228  ? 6.20300    96.58100  39.73900  1.000 52.32704  ?  228  SER   A C   1 
ATOM   1863  O  O   . SER   A 1 228  ? 6.76100    97.28900  40.58100  1.000 45.39933  ?  228  SER   A O   1 
ATOM   1864  C  CB  . SER   A 1 228  ? 7.36800    95.11100  38.09300  1.000 33.55740  ?  228  SER   A CB  1 
ATOM   1865  O  OG  . SER   A 1 228  ? 7.95000    95.03800  36.80600  1.000 43.68353  ?  228  SER   A OG  1 
ATOM   1866  N  N   . LEU   A 1 229  ? 5.12100    95.84800  39.99400  1.000 47.13232  ?  229  LEU   A N   1 
ATOM   1867  C  CA  . LEU   A 1 229  ? 4.51200    95.76100  41.31300  1.000 29.42923  ?  229  LEU   A CA  1 
ATOM   1868  C  C   . LEU   A 1 229  ? 4.19000    94.30500  41.59900  1.000 35.72193  ?  229  LEU   A C   1 
ATOM   1869  O  O   . LEU   A 1 229  ? 3.57500    93.63200  40.76700  1.000 49.57953  ?  229  LEU   A O   1 
ATOM   1870  C  CB  . LEU   A 1 229  ? 3.23400    96.60100  41.39300  1.000 36.10019  ?  229  LEU   A CB  1 
ATOM   1871  C  CG  . LEU   A 1 229  ? 3.34100    98.05700  41.84300  1.000 39.82737  ?  229  LEU   A CG  1 
ATOM   1872  C  CD1 . LEU   A 1 229  ? 1.95900    98.68000  41.89800  1.000 35.70262  ?  229  LEU   A CD1 1 
ATOM   1873  C  CD2 . LEU   A 1 229  ? 4.01600    98.14900  43.19500  1.000 47.39958  ?  229  LEU   A CD2 1 
ATOM   1874  N  N   . THR   A 1 230  ? 4.61300    93.81800  42.76100  1.000 39.05726  ?  230  THR   A N   1 
ATOM   1875  C  CA  . THR   A 1 230  ? 4.21200    92.48700  43.18300  1.000 48.77557  ?  230  THR   A CA  1 
ATOM   1876  C  C   . THR   A 1 230  ? 2.81600    92.53700  43.79400  1.000 44.84393  ?  230  THR   A C   1 
ATOM   1877  O  O   . THR   A 1 230  ? 2.25800    93.60700  44.04800  1.000 42.86958  ?  230  THR   A O   1 
ATOM   1878  C  CB  . THR   A 1 230  ? 5.20800    91.90400  44.18400  1.000 43.92742  ?  230  THR   A CB  1 
ATOM   1879  O  OG1 . THR   A 1 230  ? 4.96700    92.46400  45.48200  1.000 42.90751  ?  230  THR   A OG1 1 
ATOM   1880  C  CG2 . THR   A 1 230  ? 6.63100    92.21000  43.75600  1.000 44.28308  ?  230  THR   A CG2 1 
ATOM   1881  N  N   . TYR   A 1 231  ? 2.24800    91.35300  44.03100  1.000 43.49863  ?  231  TYR   A N   1 
ATOM   1882  C  CA  . TYR   A 1 231  ? 0.90200    91.29100  44.58800  1.000 45.78583  ?  231  TYR   A CA  1 
ATOM   1883  C  C   . TYR   A 1 231  ? 0.84300    91.94600  45.95900  1.000 48.75252  ?  231  TYR   A C   1 
ATOM   1884  O  O   . TYR   A 1 231  ? -0.09500   92.69400  46.26000  1.000 39.99757  ?  231  TYR   A O   1 
ATOM   1885  C  CB  . TYR   A 1 231  ? 0.42600    89.84200  44.66000  1.000 37.39058  ?  231  TYR   A CB  1 
ATOM   1886  C  CG  . TYR   A 1 231  ? -0.28500   89.38900  43.40800  1.000 40.39404  ?  231  TYR   A CG  1 
ATOM   1887  C  CD1 . TYR   A 1 231  ? -1.64800   89.59900  43.24800  1.000 40.63144  ?  231  TYR   A CD1 1 
ATOM   1888  C  CD2 . TYR   A 1 231  ? 0.40700    88.77100  42.37900  1.000 42.68706  ?  231  TYR   A CD2 1 
ATOM   1889  C  CE1 . TYR   A 1 231  ? -2.30400   89.19300  42.10100  1.000 51.80518  ?  231  TYR   A CE1 1 
ATOM   1890  C  CE2 . TYR   A 1 231  ? -0.23900   88.36300  41.22800  1.000 43.12222  ?  231  TYR   A CE2 1 
ATOM   1891  C  CZ  . TYR   A 1 231  ? -1.59300   88.57600  41.09400  1.000 48.25916  ?  231  TYR   A CZ  1 
ATOM   1892  O  OH  . TYR   A 1 231  ? -2.23700   88.17100  39.94600  1.000 38.63870  ?  231  TYR   A OH  1 
ATOM   1893  N  N   . LYS   A 1 232  ? 1.84400    91.68700  46.80100  1.000 39.97371  ?  232  LYS   A N   1 
ATOM   1894  C  CA  . LYS   A 1 232  ? 1.85000    92.28700  48.12900  1.000 32.57759  ?  232  LYS   A CA  1 
ATOM   1895  C  C   . LYS   A 1 232  ? 2.11200    93.78500  48.05700  1.000 31.65979  ?  232  LYS   A C   1 
ATOM   1896  O  O   . LYS   A 1 232  ? 1.53000    94.55900  48.82600  1.000 41.98773  ?  232  LYS   A O   1 
ATOM   1897  C  CB  . LYS   A 1 232  ? 2.88200    91.58700  49.00700  1.000 29.65710  ?  232  LYS   A CB  1 
ATOM   1898  C  CG  . LYS   A 1 232  ? 3.55700    92.48700  50.01300  1.000 49.93202  ?  232  LYS   A CG  1 
ATOM   1899  C  CD  . LYS   A 1 232  ? 4.41600    91.67200  50.94000  1.000 45.84403  ?  232  LYS   A CD  1 
ATOM   1900  C  CE  . LYS   A 1 232  ? 5.45100    92.53000  51.62700  1.000 75.13245  ?  232  LYS   A CE  1 
ATOM   1901  N  NZ  . LYS   A 1 232  ? 6.75500    91.81300  51.62600  1.000 71.92878  ?  232  LYS   A NZ  1 
ATOM   1902  N  N   . GLN   A 1 233  ? 2.97000    94.21700  47.13100  1.000 31.25773  ?  233  GLN   A N   1 
ATOM   1903  C  CA  . GLN   A 1 233  ? 3.20600    95.64700  46.96700  1.000 37.29257  ?  233  GLN   A CA  1 
ATOM   1904  C  C   . GLN   A 1 233  ? 1.94500    96.36000  46.49800  1.000 36.26710  ?  233  GLN   A C   1 
ATOM   1905  O  O   . GLN   A 1 233  ? 1.63300    97.46100  46.96600  1.000 46.46511  ?  233  GLN   A O   1 
ATOM   1906  C  CB  . GLN   A 1 233  ? 4.35700    95.87900  45.99100  1.000 40.05812  ?  233  GLN   A CB  1 
ATOM   1907  C  CG  . GLN   A 1 233  ? 5.70100    95.41000  46.51300  1.000 42.31523  ?  233  GLN   A CG  1 
ATOM   1908  C  CD  . GLN   A 1 233  ? 6.76300    95.37200  45.43600  1.000 38.75604  ?  233  GLN   A CD  1 
ATOM   1909  O  OE1 . GLN   A 1 233  ? 6.47500    95.57100  44.25700  1.000 41.03908  ?  233  GLN   A OE1 1 
ATOM   1910  N  NE2 . GLN   A 1 233  ? 8.00500    95.12800  45.83700  1.000 55.46596  ?  233  GLN   A NE2 1 
ATOM   1911  N  N   . LEU   A 1 234  ? 1.20300    95.74200  45.57800  1.000 40.05287  ?  234  LEU   A N   1 
ATOM   1912  C  CA  . LEU   A 1 234  ? -0.05900   96.32000  45.12700  1.000 35.38918  ?  234  LEU   A CA  1 
ATOM   1913  C  C   . LEU   A 1 234  ? -1.08200   96.34000  46.25500  1.000 39.74390  ?  234  LEU   A C   1 
ATOM   1914  O  O   . LEU   A 1 234  ? -1.76800   97.34700  46.46900  1.000 33.10208  ?  234  LEU   A O   1 
ATOM   1915  C  CB  . LEU   A 1 234  ? -0.58800   95.53400  43.92700  1.000 36.79403  ?  234  LEU   A CB  1 
ATOM   1916  C  CG  . LEU   A 1 234  ? -1.93700   95.95300  43.34100  1.000 34.70209  ?  234  LEU   A CG  1 
ATOM   1917  C  CD1 . LEU   A 1 234  ? -1.83400   97.29700  42.63700  1.000 22.11780  ?  234  LEU   A CD1 1 
ATOM   1918  C  CD2 . LEU   A 1 234  ? -2.45900   94.88300  42.39100  1.000 31.98535  ?  234  LEU   A CD2 1 
ATOM   1919  N  N   . ASN   A 1 235  ? -1.18900   95.23400  46.99500  1.000 33.00054  ?  235  ASN   A N   1 
ATOM   1920  C  CA  . ASN   A 1 235  ? -2.15500   95.15400  48.08600  1.000 37.16741  ?  235  ASN   A CA  1 
ATOM   1921  C  C   . ASN   A 1 235  ? -1.88500   96.21100  49.15000  1.000 46.08250  ?  235  ASN   A C   1 
ATOM   1922  O  O   . ASN   A 1 235  ? -2.80900   96.88800  49.61700  1.000 53.65885  ?  235  ASN   A O   1 
ATOM   1923  C  CB  . ASN   A 1 235  ? -2.12600   93.75900  48.70100  1.000 37.45787  ?  235  ASN   A CB  1 
ATOM   1924  C  CG  . ASN   A 1 235  ? -3.38200   93.44600  49.47200  1.000 46.33190  ?  235  ASN   A CG  1 
ATOM   1925  O  OD1 . ASN   A 1 235  ? -4.48500   93.73500  49.01400  1.000 63.87698  ?  235  ASN   A OD1 1 
ATOM   1926  N  ND2 . ASN   A 1 235  ? -3.22600   92.85500  50.64900  1.000 40.19452  ?  235  ASN   A ND2 1 
ATOM   1927  N  N   . GLU   A 1 236  ? -0.61900   96.36800  49.54600  1.000 48.81229  ?  236  GLU   A N   1 
ATOM   1928  C  CA  . GLU   A 1 236  ? -0.29200   97.27100  50.64600  1.000 46.14810  ?  236  GLU   A CA  1 
ATOM   1929  C  C   . GLU   A 1 236  ? -0.45500   98.73100  50.24000  1.000 42.59537  ?  236  GLU   A C   1 
ATOM   1930  O  O   . GLU   A 1 236  ? -0.93800   99.55000  51.03200  1.000 52.34078  ?  236  GLU   A O   1 
ATOM   1931  C  CB  . GLU   A 1 236  ? 1.13000    97.00300  51.13800  1.000 46.78599  ?  236  GLU   A CB  1 
ATOM   1932  C  CG  . GLU   A 1 236  ? 1.27800    95.69200  51.89600  1.000 52.51962  ?  236  GLU   A CG  1 
ATOM   1933  C  CD  . GLU   A 1 236  ? 2.70200    95.42800  52.34800  1.000 69.12427  ?  236  GLU   A CD  1 
ATOM   1934  O  OE1 . GLU   A 1 236  ? 3.62500    96.11100  51.85400  1.000 60.76777  ?  236  GLU   A OE1 1 
ATOM   1935  O  OE2 . GLU   A 1 236  ? 2.89700    94.53000  53.19500  1.000 68.73970  -1 236  GLU   A OE2 1 
ATOM   1936  N  N   . ARG   A 1 237  ? -0.05100   99.08100  49.01800  1.000 37.25690  ?  237  ARG   A N   1 
ATOM   1937  C  CA  . ARG   A 1 237  ? -0.23900   100.45200 48.55900  1.000 45.11027  ?  237  ARG   A CA  1 
ATOM   1938  C  C   . ARG   A 1 237  ? -1.71600   100.78000 48.38600  1.000 55.60189  ?  237  ARG   A C   1 
ATOM   1939  O  O   . ARG   A 1 237  ? -2.13100   101.91600 48.64300  1.000 58.29627  ?  237  ARG   A O   1 
ATOM   1940  C  CB  . ARG   A 1 237  ? 0.52400    100.68000 47.25500  1.000 32.27892  ?  237  ARG   A CB  1 
ATOM   1941  C  CG  . ARG   A 1 237  ? 0.76400    102.14300 46.92300  1.000 40.45184  ?  237  ARG   A CG  1 
ATOM   1942  C  CD  . ARG   A 1 237  ? 2.13200    102.33200 46.30200  1.000 61.61059  ?  237  ARG   A CD  1 
ATOM   1943  N  NE  . ARG   A 1 237  ? 2.11300    103.27000 45.18700  1.000 78.26239  ?  237  ARG   A NE  1 
ATOM   1944  C  CZ  . ARG   A 1 237  ? 2.97800    103.24800 44.18300  1.000 75.08428  ?  237  ARG   A CZ  1 
ATOM   1945  N  NH1 . ARG   A 1 237  ? 3.94000    102.34200 44.12000  1.000 66.48681  ?  237  ARG   A NH1 1 
ATOM   1946  N  NH2 . ARG   A 1 237  ? 2.87300    104.15400 43.21400  1.000 67.55720  ?  237  ARG   A NH2 1 
ATOM   1947  N  N   . ALA   A 1 238  ? -2.52300   99.80200  47.96600  1.000 49.03980  ?  238  ALA   A N   1 
ATOM   1948  C  CA  . ALA   A 1 238  ? -3.96600   100.01300 47.91500  1.000 42.19756  ?  238  ALA   A CA  1 
ATOM   1949  C  C   . ALA   A 1 238  ? -4.55600   100.09700 49.31700  1.000 44.06257  ?  238  ALA   A C   1 
ATOM   1950  O  O   . ALA   A 1 238  ? -5.43500   100.92700 49.57600  1.000 49.59351  ?  238  ALA   A O   1 
ATOM   1951  C  CB  . ALA   A 1 238  ? -4.63500   98.89600  47.11500  1.000 45.31458  ?  238  ALA   A CB  1 
ATOM   1952  N  N   . ASN   A 1 239  ? -4.08300   99.24400  50.23200  1.000 44.20753  ?  239  ASN   A N   1 
ATOM   1953  C  CA  . ASN   A 1 239  ? -4.55100   99.29500  51.61400  1.000 42.80249  ?  239  ASN   A CA  1 
ATOM   1954  C  C   . ASN   A 1 239  ? -4.23700   100.64100 52.25500  1.000 51.58835  ?  239  ASN   A C   1 
ATOM   1955  O  O   . ASN   A 1 239  ? -5.01600   101.14500 53.07400  1.000 61.72819  ?  239  ASN   A O   1 
ATOM   1956  C  CB  . ASN   A 1 239  ? -3.92600   98.16000  52.42700  1.000 34.56949  ?  239  ASN   A CB  1 
ATOM   1957  C  CG  . ASN   A 1 239  ? -4.59500   96.82300  52.17300  1.000 49.68393  ?  239  ASN   A CG  1 
ATOM   1958  O  OD1 . ASN   A 1 239  ? -5.77200   96.76400  51.82300  1.000 59.68272  ?  239  ASN   A OD1 1 
ATOM   1959  N  ND2 . ASN   A 1 239  ? -3.84700   95.74000  52.35600  1.000 50.87307  ?  239  ASN   A ND2 1 
ATOM   1960  N  N   . GLN   A 1 240  ? -3.09800   101.23700 51.89800  1.000 53.54981  ?  240  GLN   A N   1 
ATOM   1961  C  CA  . GLN   A 1 240  ? -2.74400   102.54300 52.44300  1.000 62.61909  ?  240  GLN   A CA  1 
ATOM   1962  C  C   . GLN   A 1 240  ? -3.71500   103.61500 51.96700  1.000 57.21183  ?  240  GLN   A C   1 
ATOM   1963  O  O   . GLN   A 1 240  ? -4.23300   104.40100 52.76800  1.000 65.31461  ?  240  GLN   A O   1 
ATOM   1964  C  CB  . GLN   A 1 240  ? -1.31200   102.90700 52.04900  1.000 54.73700  ?  240  GLN   A CB  1 
ATOM   1965  C  CG  . GLN   A 1 240  ? -0.24300   102.28400 52.92900  1.000 62.31342  ?  240  GLN   A CG  1 
ATOM   1966  C  CD  . GLN   A 1 240  ? 1.15700    102.52900 52.39800  1.000 65.02487  ?  240  GLN   A CD  1 
ATOM   1967  O  OE1 . GLN   A 1 240  ? 1.58000    101.91100 51.42200  1.000 65.45491  ?  240  GLN   A OE1 1 
ATOM   1968  N  NE2 . GLN   A 1 240  ? 1.88000    103.44200 53.03600  1.000 58.09338  ?  240  GLN   A NE2 1 
ATOM   1969  N  N   . LEU   A 1 241  ? -3.97500   103.65700 50.66000  1.000 59.31494  ?  241  LEU   A N   1 
ATOM   1970  C  CA  . LEU   A 1 241  ? -4.89600   104.64800 50.11700  1.000 49.90207  ?  241  LEU   A CA  1 
ATOM   1971  C  C   . LEU   A 1 241  ? -6.32300   104.41200 50.59800  1.000 50.95194  ?  241  LEU   A C   1 
ATOM   1972  O  O   . LEU   A 1 241  ? -7.11600   105.35800 50.66700  1.000 44.74467  ?  241  LEU   A O   1 
ATOM   1973  C  CB  . LEU   A 1 241  ? -4.82400   104.63000 48.58900  1.000 38.90626  ?  241  LEU   A CB  1 
ATOM   1974  C  CG  . LEU   A 1 241  ? -5.62500   105.66200 47.79500  1.000 45.81917  ?  241  LEU   A CG  1 
ATOM   1975  C  CD1 . LEU   A 1 241  ? -5.37200   107.06700 48.30300  1.000 43.81863  ?  241  LEU   A CD1 1 
ATOM   1976  C  CD2 . LEU   A 1 241  ? -5.27900   105.55600 46.32100  1.000 32.44094  ?  241  LEU   A CD2 1 
ATOM   1977  N  N   . ALA   A 1 242  ? -6.66100   103.16700 50.95000  1.000 43.40172  ?  242  ALA   A N   1 
ATOM   1978  C  CA  . ALA   A 1 242  ? -8.01500   102.86200 51.40400  1.000 49.23433  ?  242  ALA   A CA  1 
ATOM   1979  C  C   . ALA   A 1 242  ? -8.25700   103.37200 52.81900  1.000 56.99065  ?  242  ALA   A C   1 
ATOM   1980  O  O   . ALA   A 1 242  ? -9.34400   103.87800 53.12300  1.000 58.69705  ?  242  ALA   A O   1 
ATOM   1981  C  CB  . ALA   A 1 242  ? -8.26900   101.35700 51.32500  1.000 42.37490  ?  242  ALA   A CB  1 
ATOM   1982  N  N   . HIS   A 1 243  ? -7.26500   103.23100 53.70400  1.000 53.48097  ?  243  HIS   A N   1 
ATOM   1983  C  CA  . HIS   A 1 243  ? -7.36700   103.84000 55.02600  1.000 46.69358  ?  243  HIS   A CA  1 
ATOM   1984  C  C   . HIS   A 1 243  ? -7.60200   105.34000 54.91600  1.000 46.53928  ?  243  HIS   A C   1 
ATOM   1985  O  O   . HIS   A 1 243  ? -8.40500   105.91000 55.66300  1.000 56.12521  ?  243  HIS   A O   1 
ATOM   1986  C  CB  . HIS   A 1 243  ? -6.10100   103.56900 55.83500  1.000 50.45421  ?  243  HIS   A CB  1 
ATOM   1987  C  CG  . HIS   A 1 243  ? -5.99300   102.16800 56.34700  1.000 56.06258  ?  243  HIS   A CG  1 
ATOM   1988  N  ND1 . HIS   A 1 243  ? -5.06700   101.27000 55.86200  1.000 53.97086  ?  243  HIS   A ND1 1 
ATOM   1989  C  CD2 . HIS   A 1 243  ? -6.68500   101.51400 57.30800  1.000 50.65099  ?  243  HIS   A CD2 1 
ATOM   1990  C  CE1 . HIS   A 1 243  ? -5.19500   100.12200 56.50200  1.000 52.62486  ?  243  HIS   A CE1 1 
ATOM   1991  N  NE2 . HIS   A 1 243  ? -6.17000   100.24200 57.38400  1.000 51.48331  ?  243  HIS   A NE2 1 
ATOM   1992  N  N   . HIS   A 1 244  ? -6.89800   105.99600 53.99100  1.000 46.00787  ?  244  HIS   A N   1 
ATOM   1993  C  CA  . HIS   A 1 244  ? -7.11200   107.41800 53.75200  1.000 51.27511  ?  244  HIS   A CA  1 
ATOM   1994  C  C   . HIS   A 1 244  ? -8.51900   107.68100 53.23400  1.000 68.15796  ?  244  HIS   A C   1 
ATOM   1995  O  O   . HIS   A 1 244  ? -9.19300   108.61200 53.68900  1.000 66.61277  ?  244  HIS   A O   1 
ATOM   1996  C  CB  . HIS   A 1 244  ? -6.06700   107.93300 52.76300  1.000 37.28046  ?  244  HIS   A CB  1 
ATOM   1997  C  CG  . HIS   A 1 244  ? -6.13300   109.40800 52.51000  1.000 44.50395  ?  244  HIS   A CG  1 
ATOM   1998  N  ND1 . HIS   A 1 244  ? -5.76500   110.34500 53.45100  1.000 67.54702  ?  244  HIS   A ND1 1 
ATOM   1999  C  CD2 . HIS   A 1 244  ? -6.50500   110.10700 51.41100  1.000 60.44889  ?  244  HIS   A CD2 1 
ATOM   2000  C  CE1 . HIS   A 1 244  ? -5.91500   111.55700 52.94600  1.000 67.20429  ?  244  HIS   A CE1 1 
ATOM   2001  N  NE2 . HIS   A 1 244  ? -6.36300   111.44100 51.70900  1.000 58.51546  ?  244  HIS   A NE2 1 
ATOM   2002  N  N   . LEU   A 1 245  ? -8.98300   106.86200 52.28600  1.000 70.73624  ?  245  LEU   A N   1 
ATOM   2003  C  CA  . LEU   A 1 245  ? -10.30700  107.06700 51.70600  1.000 60.91979  ?  245  LEU   A CA  1 
ATOM   2004  C  C   . LEU   A 1 245  ? -11.40600  106.81900 52.73300  1.000 58.14880  ?  245  LEU   A C   1 
ATOM   2005  O  O   . LEU   A 1 245  ? -12.33000  107.62900 52.87300  1.000 57.16663  ?  245  LEU   A O   1 
ATOM   2006  C  CB  . LEU   A 1 245  ? -10.49300  106.15900 50.48900  1.000 55.24606  ?  245  LEU   A CB  1 
ATOM   2007  C  CG  . LEU   A 1 245  ? -9.77000   106.57800 49.20900  1.000 51.80311  ?  245  LEU   A CG  1 
ATOM   2008  C  CD1 . LEU   A 1 245  ? -10.02200  105.57900 48.09200  1.000 38.68859  ?  245  LEU   A CD1 1 
ATOM   2009  C  CD2 . LEU   A 1 245  ? -10.21400  107.96400 48.79100  1.000 57.57117  ?  245  LEU   A CD2 1 
ATOM   2010  N  N   . ARG   A 1 246  ? -11.32100  105.70300 53.46200  1.000 48.37428  ?  246  ARG   A N   1 
ATOM   2011  C  CA  . ARG   A 1 246  ? -12.36800  105.36700 54.42400  1.000 46.18587  ?  246  ARG   A CA  1 
ATOM   2012  C  C   . ARG   A 1 246  ? -12.49400  106.43500 55.50400  1.000 61.85843  ?  246  ARG   A C   1 
ATOM   2013  O  O   . ARG   A 1 246  ? -13.60700  106.82600 55.87400  1.000 73.09962  ?  246  ARG   A O   1 
ATOM   2014  C  CB  . ARG   A 1 246  ? -12.09100  104.00200 55.05100  1.000 32.84380  ?  246  ARG   A CB  1 
ATOM   2015  C  CG  . ARG   A 1 246  ? -13.22600  103.49300 55.91900  1.000 30.27781  ?  246  ARG   A CG  1 
ATOM   2016  C  CD  . ARG   A 1 246  ? -12.95200  102.09200 56.43700  1.000 27.25332  ?  246  ARG   A CD  1 
ATOM   2017  N  NE  . ARG   A 1 246  ? -13.03400  101.08900 55.38300  1.000 26.06414  ?  246  ARG   A NE  1 
ATOM   2018  C  CZ  . ARG   A 1 246  ? -13.11600  99.78300  55.60100  1.000 39.45731  ?  246  ARG   A CZ  1 
ATOM   2019  N  NH1 . ARG   A 1 246  ? -13.13600  99.28700  56.82600  1.000 38.32675  ?  246  ARG   A NH1 1 
ATOM   2020  N  NH2 . ARG   A 1 246  ? -13.18000  98.95500  54.56200  1.000 57.71127  ?  246  ARG   A NH2 1 
ATOM   2021  N  N   . GLY   A 1 247  ? -11.36300  106.92400 56.01700  1.000 56.18469  ?  247  GLY   A N   1 
ATOM   2022  C  CA  . GLY   A 1 247  ? -11.39700  108.00000 56.99000  1.000 48.09787  ?  247  GLY   A CA  1 
ATOM   2023  C  C   . GLY   A 1 247  ? -11.90200  109.31600 56.43600  1.000 64.07001  ?  247  GLY   A C   1 
ATOM   2024  O  O   . GLY   A 1 247  ? -12.36400  110.16300 57.20900  1.000 72.37049  ?  247  GLY   A O   1 
ATOM   2025  N  N   . LYS   A 1 248  ? -11.82300  109.51100 55.11700  1.000 53.10871  ?  248  LYS   A N   1 
ATOM   2026  C  CA  . LYS   A 1 248  ? -12.32600  110.72900 54.49500  1.000 53.22821  ?  248  LYS   A CA  1 
ATOM   2027  C  C   . LYS   A 1 248  ? -13.83900  110.72200 54.31800  1.000 62.84112  ?  248  LYS   A C   1 
ATOM   2028  O  O   . LYS   A 1 248  ? -14.41600  111.77800 54.03200  1.000 55.61573  ?  248  LYS   A O   1 
ATOM   2029  C  CB  . LYS   A 1 248  ? -11.65300  110.95200 53.13800  1.000 50.31549  ?  248  LYS   A CB  1 
ATOM   2030  C  CG  . LYS   A 1 248  ? -10.24000  111.50100 53.23000  1.000 62.55559  ?  248  LYS   A CG  1 
ATOM   2031  C  CD  . LYS   A 1 248  ? -10.07600  112.76900 52.41400  1.000 57.93870  ?  248  LYS   A CD  1 
ATOM   2032  C  CE  . LYS   A 1 248  ? -10.96400  113.87500 52.94700  1.000 71.77853  ?  248  LYS   A CE  1 
ATOM   2033  N  NZ  . LYS   A 1 248  ? -10.69600  115.15900 52.25300  1.000 84.17133  ?  248  LYS   A NZ  1 
ATOM   2034  N  N   . GLY   A 1 249  ? -14.49100  109.56900 54.47200  1.000 51.34118  ?  249  GLY   A N   1 
ATOM   2035  C  CA  . GLY   A 1 249  ? -15.93900  109.51600 54.44700  1.000 58.35727  ?  249  GLY   A CA  1 
ATOM   2036  C  C   . GLY   A 1 249  ? -16.53400  108.49600 53.49700  1.000 60.60167  ?  249  GLY   A C   1 
ATOM   2037  O  O   . GLY   A 1 249  ? -17.73700  108.53600 53.22000  1.000 69.02133  ?  249  GLY   A O   1 
ATOM   2038  N  N   . VAL   A 1 250  ? -15.71500  107.57600 52.99400  1.000 61.15590  ?  250  VAL   A N   1 
ATOM   2039  C  CA  . VAL   A 1 250  ? -16.18900  106.56800 52.05000  1.000 51.99631  ?  250  VAL   A CA  1 
ATOM   2040  C  C   . VAL   A 1 250  ? -16.98100  105.50700 52.80500  1.000 48.23320  ?  250  VAL   A C   1 
ATOM   2041  O  O   . VAL   A 1 250  ? -16.48000  104.89900 53.75700  1.000 38.57871  ?  250  VAL   A O   1 
ATOM   2042  C  CB  . VAL   A 1 250  ? -15.02400  105.94200 51.27000  1.000 44.98767  ?  250  VAL   A CB  1 
ATOM   2043  C  CG1 . VAL   A 1 250  ? -15.53200  104.83200 50.36400  1.000 39.57346  ?  250  VAL   A CG1 1 
ATOM   2044  C  CG2 . VAL   A 1 250  ? -14.31500  107.00600 50.44300  1.000 50.63178  ?  250  VAL   A CG2 1 
ATOM   2045  N  N   . LYS   A 1 251  ? -18.22000  105.29100 52.38400  1.000 47.69525  ?  251  LYS   A N   1 
ATOM   2046  C  CA  . LYS   A 1 251  ? -19.11500  104.29500 52.94500  1.000 50.83237  ?  251  LYS   A CA  1 
ATOM   2047  C  C   . LYS   A 1 251  ? -19.51800  103.30800 51.85800  1.000 42.38729  ?  251  LYS   A C   1 
ATOM   2048  O  O   . LYS   A 1 251  ? -19.34400  103.58800 50.66500  1.000 32.45194  ?  251  LYS   A O   1 
ATOM   2049  C  CB  . LYS   A 1 251  ? -20.36000  104.96200 53.54900  1.000 49.73166  ?  251  LYS   A CB  1 
ATOM   2050  C  CG  . LYS   A 1 251  ? -20.08600  105.71000 54.84500  1.000 56.72856  ?  251  LYS   A CG  1 
ATOM   2051  C  CD  . LYS   A 1 251  ? -20.23600  104.79600 56.05400  1.000 77.44652  ?  251  LYS   A CD  1 
ATOM   2052  C  CE  . LYS   A 1 251  ? -19.38900  105.27900 57.22300  1.000 85.30434  ?  251  LYS   A CE  1 
ATOM   2053  N  NZ  . LYS   A 1 251  ? -20.20200  105.53200 58.44500  1.000 66.47173  ?  251  LYS   A NZ  1 
ATOM   2054  N  N   . PRO   A 1 252  ? -20.03100  102.13300 52.22700  1.000 30.81693  ?  252  PRO   A N   1 
ATOM   2055  C  CA  . PRO   A 1 252  ? -20.48700  101.18100 51.20900  1.000 27.11475  ?  252  PRO   A CA  1 
ATOM   2056  C  C   . PRO   A 1 252  ? -21.50200  101.81200 50.26300  1.000 54.08697  ?  252  PRO   A C   1 
ATOM   2057  O  O   . PRO   A 1 252  ? -22.31800  102.64800 50.66100  1.000 62.46155  ?  252  PRO   A O   1 
ATOM   2058  C  CB  . PRO   A 1 252  ? -21.11000  100.05400 52.03600  1.000 36.25757  ?  252  PRO   A CB  1 
ATOM   2059  C  CG  . PRO   A 1 252  ? -20.36300  100.08500 53.31400  1.000 36.54880  ?  252  PRO   A CG  1 
ATOM   2060  C  CD  . PRO   A 1 252  ? -20.06000  101.54000 53.57800  1.000 40.32258  ?  252  PRO   A CD  1 
ATOM   2061  N  N   . ASP   A 1 253  ? -21.42900  101.41000 48.99400  1.000 59.50826  ?  253  ASP   A N   1 
ATOM   2062  C  CA  . ASP   A 1 253  ? -22.25000  101.87800 47.87900  1.000 46.20705  ?  253  ASP   A CA  1 
ATOM   2063  C  C   . ASP   A 1 253  ? -21.97500  103.33100 47.50400  1.000 47.39859  ?  253  ASP   A C   1 
ATOM   2064  O  O   . ASP   A 1 253  ? -22.64100  103.85600 46.60300  1.000 40.21549  ?  253  ASP   A O   1 
ATOM   2065  C  CB  . ASP   A 1 253  ? -23.75500  101.70000 48.13600  1.000 41.42214  ?  253  ASP   A CB  1 
ATOM   2066  C  CG  . ASP   A 1 253  ? -24.26900  100.33500 47.69800  1.000 64.37971  ?  253  ASP   A CG  1 
ATOM   2067  O  OD1 . ASP   A 1 253  ? -23.44900  99.48200  47.29300  1.000 60.95349  ?  253  ASP   A OD1 1 
ATOM   2068  O  OD2 . ASP   A 1 253  ? -25.49700  100.11200 47.75700  1.000 74.61958  -1 253  ASP   A OD2 1 
ATOM   2069  N  N   . ASP   A 1 254  ? -21.02100  103.99800 48.15000  1.000 56.31740  ?  254  ASP   A N   1 
ATOM   2070  C  CA  . ASP   A 1 254  ? -20.62100  105.32100 47.70000  1.000 54.47019  ?  254  ASP   A CA  1 
ATOM   2071  C  C   . ASP   A 1 254  ? -19.90400  105.21800 46.35900  1.000 44.54979  ?  254  ASP   A C   1 
ATOM   2072  O  O   . ASP   A 1 254  ? -19.41300  104.15700 45.96500  1.000 59.30941  ?  254  ASP   A O   1 
ATOM   2073  C  CB  . ASP   A 1 254  ? -19.71400  105.99900 48.72600  1.000 53.26034  ?  254  ASP   A CB  1 
ATOM   2074  C  CG  . ASP   A 1 254  ? -20.49100  106.64100 49.85600  1.000 64.03720  ?  254  ASP   A CG  1 
ATOM   2075  O  OD1 . ASP   A 1 254  ? -21.73500  106.52600 49.86800  1.000 76.45329  ?  254  ASP   A OD1 1 
ATOM   2076  O  OD2 . ASP   A 1 254  ? -19.85400  107.25900 50.73500  1.000 63.99562  -1 254  ASP   A OD2 1 
ATOM   2077  N  N   . GLN   A 1 255  ? -19.85100  106.33800 45.65000  1.000 47.54182  ?  255  GLN   A N   1 
ATOM   2078  C  CA  . GLN   A 1 255  ? -19.25600  106.38200 44.32100  1.000 44.50963  ?  255  GLN   A CA  1 
ATOM   2079  C  C   . GLN   A 1 255  ? -18.08500  107.34900 44.34200  1.000 47.87841  ?  255  GLN   A C   1 
ATOM   2080  O  O   . GLN   A 1 255  ? -18.27500  108.56200 44.47900  1.000 48.31963  ?  255  GLN   A O   1 
ATOM   2081  C  CB  . GLN   A 1 255  ? -20.28600  106.77800 43.26700  1.000 52.85327  ?  255  GLN   A CB  1 
ATOM   2082  C  CG  . GLN   A 1 255  ? -21.11800  105.60600 42.79000  1.000 49.61334  ?  255  GLN   A CG  1 
ATOM   2083  C  CD  . GLN   A 1 255  ? -22.54700  105.98900 42.49400  1.000 57.30377  ?  255  GLN   A CD  1 
ATOM   2084  O  OE1 . GLN   A 1 255  ? -22.81000  106.91300 41.72400  1.000 55.00028  ?  255  GLN   A OE1 1 
ATOM   2085  N  NE2 . GLN   A 1 255  ? -23.48500  105.28100 43.11100  1.000 57.68126  ?  255  GLN   A NE2 1 
ATOM   2086  N  N   . VAL   A 1 256  ? -16.87900  106.80300 44.21500  1.000 54.51674  ?  256  VAL   A N   1 
ATOM   2087  C  CA  . VAL   A 1 256  ? -15.64900  107.57700 44.13100  1.000 46.43272  ?  256  VAL   A CA  1 
ATOM   2088  C  C   . VAL   A 1 256  ? -15.17900  107.55000 42.68500  1.000 36.59036  ?  256  VAL   A C   1 
ATOM   2089  O  O   . VAL   A 1 256  ? -15.02100  106.47400 42.09800  1.000 47.24402  ?  256  VAL   A O   1 
ATOM   2090  C  CB  . VAL   A 1 256  ? -14.56900  107.01900 45.07300  1.000 44.30000  ?  256  VAL   A CB  1 
ATOM   2091  C  CG1 . VAL   A 1 256  ? -13.36200  107.93600 45.09300  1.000 59.30546  ?  256  VAL   A CG1 1 
ATOM   2092  C  CG2 . VAL   A 1 256  ? -15.12900  106.82800 46.47600  1.000 42.94486  ?  256  VAL   A CG2 1 
ATOM   2093  N  N   . ALA   A 1 257  ? -14.96200  108.72800 42.11100  1.000 40.64307  ?  257  ALA   A N   1 
ATOM   2094  C  CA  . ALA   A 1 257  ? -14.52900  108.83300 40.72700  1.000 48.97155  ?  257  ALA   A CA  1 
ATOM   2095  C  C   . ALA   A 1 257  ? -13.01100  108.74600 40.62400  1.000 54.12346  ?  257  ALA   A C   1 
ATOM   2096  O  O   . ALA   A 1 257  ? -12.28100  109.10000 41.55400  1.000 46.41311  ?  257  ALA   A O   1 
ATOM   2097  C  CB  . ALA   A 1 257  ? -15.01500  110.14200 40.10500  1.000 46.28809  ?  257  ALA   A CB  1 
ATOM   2098  N  N   . ILE   A 1 258  ? -12.54300  108.26700 39.47400  1.000 53.04190  ?  258  ILE   A N   1 
ATOM   2099  C  CA  . ILE   A 1 258  ? -11.12100  108.15400 39.17900  1.000 34.15994  ?  258  ILE   A CA  1 
ATOM   2100  C  C   . ILE   A 1 258  ? -10.88100  108.73400 37.79500  1.000 39.34135  ?  258  ILE   A C   1 
ATOM   2101  O  O   . ILE   A 1 258  ? -11.41300  108.22300 36.80200  1.000 53.47182  ?  258  ILE   A O   1 
ATOM   2102  C  CB  . ILE   A 1 258  ? -10.62500  106.70100 39.24600  1.000 30.75875  ?  258  ILE   A CB  1 
ATOM   2103  C  CG1 . ILE   A 1 258  ? -10.60700  106.20900 40.69100  1.000 28.19204  ?  258  ILE   A CG1 1 
ATOM   2104  C  CG2 . ILE   A 1 258  ? -9.24400   106.57100 38.62300  1.000 47.03174  ?  258  ILE   A CG2 1 
ATOM   2105  C  CD1 . ILE   A 1 258  ? -10.79300  104.72600 40.81500  1.000 34.40676  ?  258  ILE   A CD1 1 
ATOM   2106  N  N   . MET   A 1 259  ? -10.09000  109.80000 37.72800  1.000 45.48955  ?  259  MET   A N   1 
ATOM   2107  C  CA  . MET   A 1 259  ? -9.71100   110.36600 36.44200  1.000 57.22929  ?  259  MET   A CA  1 
ATOM   2108  C  C   . MET   A 1 259  ? -8.20600   110.24400 36.24700  1.000 53.28705  ?  259  MET   A C   1 
ATOM   2109  O  O   . MET   A 1 259  ? -7.49000   111.24700 36.16300  1.000 61.19751  ?  259  MET   A O   1 
ATOM   2110  C  CB  . MET   A 1 259  ? -10.17000  111.82000 36.33600  1.000 50.77944  ?  259  MET   A CB  1 
ATOM   2111  C  CG  . MET   A 1 259  ? -10.10900  112.38800 34.92800  1.000 51.83626  ?  259  MET   A CG  1 
ATOM   2112  S  SD  . MET   A 1 259  ? -10.83600  114.02600 34.87100  1.000 70.17858  ?  259  MET   A SD  1 
ATOM   2113  C  CE  . MET   A 1 259  ? -10.19500  114.69600 36.39900  1.000 66.36333  ?  259  MET   A CE  1 
ATOM   2114  N  N   . LEU   A 1 260  ? -7.72400   109.01200 36.18100  1.000 47.10667  ?  260  LEU   A N   1 
ATOM   2115  C  CA  . LEU   A 1 260  ? -6.31900   108.72100 35.96100  1.000 44.02360  ?  260  LEU   A CA  1 
ATOM   2116  C  C   . LEU   A 1 260  ? -6.13200   108.12500 34.57400  1.000 53.72094  ?  260  LEU   A C   1 
ATOM   2117  O  O   . LEU   A 1 260  ? -7.08700   107.68900 33.92500  1.000 61.15885  ?  260  LEU   A O   1 
ATOM   2118  C  CB  . LEU   A 1 260  ? -5.79200   107.74800 37.02100  1.000 40.36901  ?  260  LEU   A CB  1 
ATOM   2119  C  CG  . LEU   A 1 260  ? -5.55700   108.33900 38.40900  1.000 41.37383  ?  260  LEU   A CG  1 
ATOM   2120  C  CD1 . LEU   A 1 260  ? -4.88500   107.32300 39.32500  1.000 46.29716  ?  260  LEU   A CD1 1 
ATOM   2121  C  CD2 . LEU   A 1 260  ? -4.72600   109.60600 38.29100  1.000 38.16652  ?  260  LEU   A CD2 1 
ATOM   2122  N  N   . ASP   A 1 261  ? -4.88500   108.11200 34.12500  1.000 54.62366  ?  261  ASP   A N   1 
ATOM   2123  C  CA  . ASP   A 1 261  ? -4.51600   107.44600 32.88800  1.000 45.98268  ?  261  ASP   A CA  1 
ATOM   2124  C  C   . ASP   A 1 261  ? -3.86500   106.10300 33.20300  1.000 43.16191  ?  261  ASP   A C   1 
ATOM   2125  O  O   . ASP   A 1 261  ? -3.39800   105.86300 34.31900  1.000 58.16889  ?  261  ASP   A O   1 
ATOM   2126  C  CB  . ASP   A 1 261  ? -3.57600   108.32600 32.06000  1.000 40.96209  ?  261  ASP   A CB  1 
ATOM   2127  C  CG  . ASP   A 1 261  ? -4.24400   108.87400 30.81000  1.000 87.33554  ?  261  ASP   A CG  1 
ATOM   2128  O  OD1 . ASP   A 1 261  ? -5.30400   108.33900 30.41800  1.000 91.39334  ?  261  ASP   A OD1 1 
ATOM   2129  O  OD2 . ASP   A 1 261  ? -3.71500   109.84400 30.22500  1.000 76.27088  -1 261  ASP   A OD2 1 
ATOM   2130  N  N   . LYS   A 1 262  ? -3.86700   105.21500 32.20500  1.000 38.75720  ?  262  LYS   A N   1 
ATOM   2131  C  CA  . LYS   A 1 262  ? -3.35300   103.85600 32.36100  1.000 43.16054  ?  262  LYS   A CA  1 
ATOM   2132  C  C   . LYS   A 1 262  ? -1.96000   103.85400 32.97900  1.000 48.72209  ?  262  LYS   A C   1 
ATOM   2133  O  O   . LYS   A 1 262  ? -0.98100   104.23300 32.32800  1.000 48.25258  ?  262  LYS   A O   1 
ATOM   2134  C  CB  . LYS   A 1 262  ? -3.33000   103.13300 31.01200  1.000 43.92641  ?  262  LYS   A CB  1 
ATOM   2135  C  CG  . LYS   A 1 262  ? -4.63100   102.43900 30.64200  1.000 39.98551  ?  262  LYS   A CG  1 
ATOM   2136  C  CD  . LYS   A 1 262  ? -4.41800   101.45700 29.50000  1.000 41.56910  ?  262  LYS   A CD  1 
ATOM   2137  C  CE  . LYS   A 1 262  ? -5.67700   101.28500 28.66700  1.000 40.07053  ?  262  LYS   A CE  1 
ATOM   2138  N  NZ  . LYS   A 1 262  ? -6.06400   102.55000 27.98000  1.000 64.25825  ?  262  LYS   A NZ  1 
ATOM   2139  N  N   . SER   A 1 263  ? -1.86500   103.42800 34.23400  1.000 43.27549  ?  263  SER   A N   1 
ATOM   2140  C  CA  . SER   A 1 263  ? -0.62000   103.51600 34.98400  1.000 40.80137  ?  263  SER   A CA  1 
ATOM   2141  C  C   . SER   A 1 263  ? -0.66800   102.51200 36.12900  1.000 45.93820  ?  263  SER   A C   1 
ATOM   2142  O  O   . SER   A 1 263  ? -1.63700   101.76500 36.28900  1.000 47.47477  ?  263  SER   A O   1 
ATOM   2143  C  CB  . SER   A 1 263  ? -0.39800   104.93700 35.50500  1.000 50.23983  ?  263  SER   A CB  1 
ATOM   2144  O  OG  . SER   A 1 263  ? -1.48100   105.34800 36.32300  1.000 47.71012  ?  263  SER   A OG  1 
ATOM   2145  N  N   . LEU   A 1 264  ? 0.39800    102.50200 36.93100  1.000 48.36430  ?  264  LEU   A N   1 
ATOM   2146  C  CA  . LEU   A 1 264  ? 0.40200    101.67700 38.13300  1.000 50.08323  ?  264  LEU   A CA  1 
ATOM   2147  C  C   . LEU   A 1 264  ? -0.52300   102.24700 39.19900  1.000 41.40209  ?  264  LEU   A C   1 
ATOM   2148  O  O   . LEU   A 1 264  ? -1.09800   101.49000 39.98900  1.000 37.83027  ?  264  LEU   A O   1 
ATOM   2149  C  CB  . LEU   A 1 264  ? 1.82300    101.55000 38.68000  1.000 45.05174  ?  264  LEU   A CB  1 
ATOM   2150  C  CG  . LEU   A 1 264  ? 2.70400    100.48300 38.03200  1.000 42.90059  ?  264  LEU   A CG  1 
ATOM   2151  C  CD1 . LEU   A 1 264  ? 4.03800    100.37900 38.74600  1.000 44.71739  ?  264  LEU   A CD1 1 
ATOM   2152  C  CD2 . LEU   A 1 264  ? 1.99600    99.14800  38.03800  1.000 44.20934  ?  264  LEU   A CD2 1 
ATOM   2153  N  N   . ASP   A 1 265  ? -0.67900   103.57100 39.23500  1.000 40.44063  ?  265  ASP   A N   1 
ATOM   2154  C  CA  . ASP   A 1 265  ? -1.54000   104.19100 40.23500  1.000 49.42301  ?  265  ASP   A CA  1 
ATOM   2155  C  C   . ASP   A 1 265  ? -3.01800   103.97800 39.93900  1.000 56.13387  ?  265  ASP   A C   1 
ATOM   2156  O  O   . ASP   A 1 265  ? -3.83700   104.05700 40.86200  1.000 48.92298  ?  265  ASP   A O   1 
ATOM   2157  C  CB  . ASP   A 1 265  ? -1.23500   105.68500 40.33300  1.000 52.60167  ?  265  ASP   A CB  1 
ATOM   2158  C  CG  . ASP   A 1 265  ? 0.05200    105.96700 41.08300  1.000 62.09400  ?  265  ASP   A CG  1 
ATOM   2159  O  OD1 . ASP   A 1 265  ? 0.24700    105.38700 42.17500  1.000 55.59408  ?  265  ASP   A OD1 1 
ATOM   2160  O  OD2 . ASP   A 1 265  ? 0.87000    106.76500 40.57800  1.000 58.32092  -1 265  ASP   A OD2 1 
ATOM   2161  N  N   . MET   A 1 266  ? -3.37600   103.71500 38.68000  1.000 60.43922  ?  266  MET   A N   1 
ATOM   2162  C  CA  . MET   A 1 266  ? -4.76800   103.42000 38.35500  1.000 45.56340  ?  266  MET   A CA  1 
ATOM   2163  C  C   . MET   A 1 266  ? -5.22000   102.12700 39.02000  1.000 46.54582  ?  266  MET   A C   1 
ATOM   2164  O  O   . MET   A 1 266  ? -6.30800   102.06300 39.60500  1.000 50.52514  ?  266  MET   A O   1 
ATOM   2165  C  CB  . MET   A 1 266  ? -4.94800   103.33700 36.84000  1.000 47.59467  ?  266  MET   A CB  1 
ATOM   2166  C  CG  . MET   A 1 266  ? -6.24800   102.67400 36.40600  1.000 44.27624  ?  266  MET   A CG  1 
ATOM   2167  S  SD  . MET   A 1 266  ? -6.47300   102.69700 34.61600  1.000 41.56398  ?  266  MET   A SD  1 
ATOM   2168  C  CE  . MET   A 1 266  ? -6.58700   104.45700 34.31700  1.000 49.18698  ?  266  MET   A CE  1 
ATOM   2169  N  N   . ILE   A 1 267  ? -4.39400   101.08200 38.93800  1.000 40.82385  ?  267  ILE   A N   1 
ATOM   2170  C  CA  . ILE   A 1 267  ? -4.74600   99.81400  39.56700  1.000 40.29747  ?  267  ILE   A CA  1 
ATOM   2171  C  C   . ILE   A 1 267  ? -4.79500   99.96700  41.08000  1.000 40.33636  ?  267  ILE   A C   1 
ATOM   2172  O  O   . ILE   A 1 267  ? -5.62700   99.34800  41.75500  1.000 41.62048  ?  267  ILE   A O   1 
ATOM   2173  C  CB  . ILE   A 1 267  ? -3.76200   98.71100  39.14200  1.000 35.94172  ?  267  ILE   A CB  1 
ATOM   2174  C  CG1 . ILE   A 1 267  ? -3.47500   98.79600  37.64200  1.000 33.37578  ?  267  ILE   A CG1 1 
ATOM   2175  C  CG2 . ILE   A 1 267  ? -4.31300   97.34200  39.51200  1.000 26.58682  ?  267  ILE   A CG2 1 
ATOM   2176  C  CD1 . ILE   A 1 267  ? -4.62100   98.33500  36.78000  1.000 27.40598  ?  267  ILE   A CD1 1 
ATOM   2177  N  N   . VAL   A 1 268  ? -3.90600   100.79100 41.63900  1.000 38.34992  ?  268  VAL   A N   1 
ATOM   2178  C  CA  . VAL   A 1 268  ? -3.92500   101.02900 43.07800  1.000 46.97739  ?  268  VAL   A CA  1 
ATOM   2179  C  C   . VAL   A 1 268  ? -5.18400   101.79000 43.46800  1.000 42.30610  ?  268  VAL   A C   1 
ATOM   2180  O  O   . VAL   A 1 268  ? -5.85400   101.44800 44.45000  1.000 41.11703  ?  268  VAL   A O   1 
ATOM   2181  C  CB  . VAL   A 1 268  ? -2.64600   101.77100 43.51300  1.000 52.87469  ?  268  VAL   A CB  1 
ATOM   2182  C  CG1 . VAL   A 1 268  ? -2.69900   102.12600 44.99800  1.000 42.33445  ?  268  VAL   A CG1 1 
ATOM   2183  C  CG2 . VAL   A 1 268  ? -1.41700   100.93300 43.20600  1.000 33.13070  ?  268  VAL   A CG2 1 
ATOM   2184  N  N   . SER   A 1 269  ? -5.53900   102.81700 42.69300  1.000 36.15942  ?  269  SER   A N   1 
ATOM   2185  C  CA  . SER   A 1 269  ? -6.72400   103.60700 43.00600  1.000 37.22138  ?  269  SER   A CA  1 
ATOM   2186  C  C   . SER   A 1 269  ? -7.99000   102.76400 42.92300  1.000 44.44440  ?  269  SER   A C   1 
ATOM   2187  O  O   . SER   A 1 269  ? -8.89500   102.90700 43.75400  1.000 51.99799  ?  269  SER   A O   1 
ATOM   2188  C  CB  . SER   A 1 269  ? -6.81500   104.80300 42.06100  1.000 37.43360  ?  269  SER   A CB  1 
ATOM   2189  O  OG  . SER   A 1 269  ? -5.67100   105.62800 42.18700  1.000 43.82515  ?  269  SER   A OG  1 
ATOM   2190  N  N   . ILE   A 1 270  ? -8.06800   101.87600 41.93100  1.000 43.17370  ?  270  ILE   A N   1 
ATOM   2191  C  CA  . ILE   A 1 270  ? -9.26000   101.04900 41.75700  1.000 39.99928  ?  270  ILE   A CA  1 
ATOM   2192  C  C   . ILE   A 1 270  ? -9.45000   100.13100 42.95800  1.000 46.53155  ?  270  ILE   A C   1 
ATOM   2193  O  O   . ILE   A 1 270  ? -10.53800  100.05600 43.54200  1.000 47.38219  ?  270  ILE   A O   1 
ATOM   2194  C  CB  . ILE   A 1 270  ? -9.16900   100.25500 40.44300  1.000 38.64162  ?  270  ILE   A CB  1 
ATOM   2195  C  CG1 . ILE   A 1 270  ? -9.51700   101.15600 39.25800  1.000 30.03870  ?  270  ILE   A CG1 1 
ATOM   2196  C  CG2 . ILE   A 1 270  ? -10.07200  99.03300  40.48500  1.000 27.08177  ?  270  ILE   A CG2 1 
ATOM   2197  C  CD1 . ILE   A 1 270  ? -9.13600   100.56600 37.92700  1.000 32.06206  ?  270  ILE   A CD1 1 
ATOM   2198  N  N   . LEU   A 1 271  ? -8.39000   99.42200  43.35100  1.000 41.63434  ?  271  LEU   A N   1 
ATOM   2199  C  CA  . LEU   A 1 271  ? -8.47700   98.55600  44.52000  1.000 37.11902  ?  271  LEU   A CA  1 
ATOM   2200  C  C   . LEU   A 1 271  ? -8.61100   99.34800  45.81200  1.000 34.93645  ?  271  LEU   A C   1 
ATOM   2201  O  O   . LEU   A 1 271  ? -9.11600   98.81100  46.80400  1.000 30.61594  ?  271  LEU   A O   1 
ATOM   2202  C  CB  . LEU   A 1 271  ? -7.25300   97.64200  44.58800  1.000 41.32858  ?  271  LEU   A CB  1 
ATOM   2203  C  CG  . LEU   A 1 271  ? -7.28300   96.41400  43.67700  1.000 48.67703  ?  271  LEU   A CG  1 
ATOM   2204  C  CD1 . LEU   A 1 271  ? -5.88700   96.09000  43.16600  1.000 41.51269  ?  271  LEU   A CD1 1 
ATOM   2205  C  CD2 . LEU   A 1 271  ? -7.88400   95.21600  44.40300  1.000 45.65108  ?  271  LEU   A CD2 1 
ATOM   2206  N  N   . ALA   A 1 272  ? -8.17300   100.60800 45.82300  1.000 42.73641  ?  272  ALA   A N   1 
ATOM   2207  C  CA  . ALA   A 1 272  ? -8.30500   101.42500 47.02400  1.000 44.81943  ?  272  ALA   A CA  1 
ATOM   2208  C  C   . ALA   A 1 272  ? -9.76600   101.73900 47.31200  1.000 47.56896  ?  272  ALA   A C   1 
ATOM   2209  O  O   . ALA   A 1 272  ? -10.24100  101.55200 48.43900  1.000 52.24092  ?  272  ALA   A O   1 
ATOM   2210  C  CB  . ALA   A 1 272  ? -7.49900   102.71300 46.87500  1.000 45.65377  ?  272  ALA   A CB  1 
ATOM   2211  N  N   . VAL   A 1 273  ? -10.49400  102.22200 46.30100  1.000 37.91573  ?  273  VAL   A N   1 
ATOM   2212  C  CA  . VAL   A 1 273  ? -11.91400  102.51000 46.47400  1.000 32.28945  ?  273  VAL   A CA  1 
ATOM   2213  C  C   . VAL   A 1 273  ? -12.66100  101.26000 46.91200  1.000 31.32648  ?  273  VAL   A C   1 
ATOM   2214  O  O   . VAL   A 1 273  ? -13.56800  101.32000 47.75000  1.000 41.16085  ?  273  VAL   A O   1 
ATOM   2215  C  CB  . VAL   A 1 273  ? -12.50200  103.09000 45.17700  1.000 32.53456  ?  273  VAL   A CB  1 
ATOM   2216  C  CG1 . VAL   A 1 273  ? -13.96900  103.42700 45.37600  1.000 47.60005  ?  273  VAL   A CG1 1 
ATOM   2217  C  CG2 . VAL   A 1 273  ? -11.72000  104.31600 44.75300  1.000 29.12706  ?  273  VAL   A CG2 1 
ATOM   2218  N  N   . MET   A 1 274  ? -12.28300  100.10700 46.36200  1.000 26.94263  ?  274  MET   A N   1 
ATOM   2219  C  CA  . MET   A 1 274  ? -12.94200  98.85800  46.71900  1.000 38.53698  ?  274  MET   A CA  1 
ATOM   2220  C  C   . MET   A 1 274  ? -12.68500  98.49800  48.17900  1.000 44.96093  ?  274  MET   A C   1 
ATOM   2221  O  O   . MET   A 1 274  ? -13.61300  98.13800  48.91500  1.000 41.89670  ?  274  MET   A O   1 
ATOM   2222  C  CB  . MET   A 1 274  ? -12.44900  97.73900  45.80700  1.000 47.95124  ?  274  MET   A CB  1 
ATOM   2223  C  CG  . MET   A 1 274  ? -12.87900  97.82500  44.35000  1.000 45.40481  ?  274  MET   A CG  1 
ATOM   2224  S  SD  . MET   A 1 274  ? -12.93300  96.17300  43.62600  1.000 53.05498  ?  274  MET   A SD  1 
ATOM   2225  C  CE  . MET   A 1 274  ? -12.27200  95.22500  44.99200  1.000 49.46412  ?  274  MET   A CE  1 
ATOM   2226  N  N   . LYS   A 1 275  ? -11.42200  98.57500  48.61000  1.000 53.52471  ?  275  LYS   A N   1 
ATOM   2227  C  CA  . LYS   A 1 275  ? -11.08000  98.19900  49.97800  1.000 50.08751  ?  275  LYS   A CA  1 
ATOM   2228  C  C   . LYS   A 1 275  ? -11.68100  99.16300  50.99200  1.000 47.64368  ?  275  LYS   A C   1 
ATOM   2229  O  O   . LYS   A 1 275  ? -12.05600  98.74500  52.09400  1.000 39.49284  ?  275  LYS   A O   1 
ATOM   2230  C  CB  . LYS   A 1 275  ? -9.56200   98.12800  50.14000  1.000 40.28761  ?  275  LYS   A CB  1 
ATOM   2231  C  CG  . LYS   A 1 275  ? -8.92400   96.94700  49.43300  1.000 34.81097  ?  275  LYS   A CG  1 
ATOM   2232  C  CD  . LYS   A 1 275  ? -7.46200   97.21100  49.12900  1.000 43.69595  ?  275  LYS   A CD  1 
ATOM   2233  C  CE  . LYS   A 1 275  ? -6.76500   95.93400  48.71000  1.000 37.82373  ?  275  LYS   A CE  1 
ATOM   2234  N  NZ  . LYS   A 1 275  ? -6.79900   94.91800  49.79900  1.000 31.34279  ?  275  LYS   A NZ  1 
ATOM   2235  N  N   . ALA   A 1 276  ? -11.78100  100.44900 50.63900  1.000 39.64723  ?  276  ALA   A N   1 
ATOM   2236  C  CA  . ALA   A 1 276  ? -12.46200  101.40500 51.50700  1.000 39.23652  ?  276  ALA   A CA  1 
ATOM   2237  C  C   . ALA   A 1 276  ? -13.92800  101.03700 51.68200  1.000 46.40846  ?  276  ALA   A C   1 
ATOM   2238  O  O   . ALA   A 1 276  ? -14.45800  101.07700 52.80000  1.000 54.11755  ?  276  ALA   A O   1 
ATOM   2239  C  CB  . ALA   A 1 276  ? -12.32700  102.81700 50.93600  1.000 44.05331  ?  276  ALA   A CB  1 
ATOM   2240  N  N   . GLY   A 1 277  ? -14.59900  100.67700 50.58700  1.000 60.87094  ?  277  GLY   A N   1 
ATOM   2241  C  CA  . GLY   A 1 277  ? -15.97800  100.22800 50.63200  1.000 51.39826  ?  277  GLY   A CA  1 
ATOM   2242  C  C   . GLY   A 1 277  ? -16.83300  100.74100 49.49000  1.000 42.18205  ?  277  GLY   A C   1 
ATOM   2243  O  O   . GLY   A 1 277  ? -17.99800  100.35600 49.35500  1.000 57.60779  ?  277  GLY   A O   1 
ATOM   2244  N  N   . GLY   A 1 278  ? -16.26200  101.60700 48.65200  1.000 37.21154  ?  278  GLY   A N   1 
ATOM   2245  C  CA  . GLY   A 1 278  ? -16.99900  102.26600 47.59800  1.000 39.95501  ?  278  GLY   A CA  1 
ATOM   2246  C  C   . GLY   A 1 278  ? -16.89800  101.55300 46.26000  1.000 41.49725  ?  278  GLY   A C   1 
ATOM   2247  O  O   . GLY   A 1 278  ? -16.38500  100.43900 46.14100  1.000 44.80274  ?  278  GLY   A O   1 
ATOM   2248  N  N   . ALA   A 1 279  ? -17.41800  102.22300 45.23400  1.000 34.83251  ?  279  ALA   A N   1 
ATOM   2249  C  CA  . ALA   A 1 279  ? -17.40100  101.73200 43.86400  1.000 38.48050  ?  279  ALA   A CA  1 
ATOM   2250  C  C   . ALA   A 1 279  ? -16.71200  102.76900 42.99400  1.000 39.35844  ?  279  ALA   A C   1 
ATOM   2251  O  O   . ALA   A 1 279  ? -17.00500  103.96400 43.10300  1.000 44.69935  ?  279  ALA   A O   1 
ATOM   2252  C  CB  . ALA   A 1 279  ? -18.81900  101.46000 43.35400  1.000 49.16967  ?  279  ALA   A CB  1 
ATOM   2253  N  N   . TYR   A 1 280  ? -15.79600  102.32300 42.14100  1.000 32.37779  ?  280  TYR   A N   1 
ATOM   2254  C  CA  . TYR   A 1 280  ? -15.00300  103.26900 41.37100  1.000 41.67434  ?  280  TYR   A CA  1 
ATOM   2255  C  C   . TYR   A 1 280  ? -15.75200  103.70400 40.11900  1.000 41.83471  ?  280  TYR   A C   1 
ATOM   2256  O  O   . TYR   A 1 280  ? -16.42800  102.90500 39.46600  1.000 43.12878  ?  280  TYR   A O   1 
ATOM   2257  C  CB  . TYR   A 1 280  ? -13.63300  102.67600 41.02500  1.000 37.28149  ?  280  TYR   A CB  1 
ATOM   2258  C  CG  . TYR   A 1 280  ? -13.59300  101.61900 39.93900  1.000 40.27788  ?  280  TYR   A CG  1 
ATOM   2259  C  CD1 . TYR   A 1 280  ? -13.72500  100.26900 40.25000  1.000 36.94336  ?  280  TYR   A CD1 1 
ATOM   2260  C  CD2 . TYR   A 1 280  ? -13.36400  101.96500 38.61300  1.000 31.23894  ?  280  TYR   A CD2 1 
ATOM   2261  C  CE1 . TYR   A 1 280  ? -13.66300  99.29800  39.26100  1.000 33.23315  ?  280  TYR   A CE1 1 
ATOM   2262  C  CE2 . TYR   A 1 280  ? -13.30300  101.00300 37.61900  1.000 31.89281  ?  280  TYR   A CE2 1 
ATOM   2263  C  CZ  . TYR   A 1 280  ? -13.45300  99.67200  37.94800  1.000 27.19572  ?  280  TYR   A CZ  1 
ATOM   2264  O  OH  . TYR   A 1 280  ? -13.39000  98.71900  36.95700  1.000 33.64223  ?  280  TYR   A OH  1 
ATOM   2265  N  N   . VAL   A 1 281  ? -15.65000  104.99200 39.81000  1.000 33.92221  ?  281  VAL   A N   1 
ATOM   2266  C  CA  . VAL   A 1 281  ? -16.33900  105.58800 38.67000  1.000 35.55815  ?  281  VAL   A CA  1 
ATOM   2267  C  C   . VAL   A 1 281  ? -15.29100  106.05000 37.66500  1.000 31.47193  ?  281  VAL   A C   1 
ATOM   2268  O  O   . VAL   A 1 281  ? -14.76000  107.16400 37.78900  1.000 41.86238  ?  281  VAL   A O   1 
ATOM   2269  C  CB  . VAL   A 1 281  ? -17.24700  106.74600 39.11200  1.000 50.90697  ?  281  VAL   A CB  1 
ATOM   2270  C  CG1 . VAL   A 1 281  ? -18.07500  107.25100 37.94000  1.000 25.25757  ?  281  VAL   A CG1 1 
ATOM   2271  C  CG2 . VAL   A 1 281  ? -18.14600  106.30400 40.26200  1.000 36.98187  ?  281  VAL   A CG2 1 
ATOM   2272  N  N   . PRO   A 1 282  ? -14.96200  105.23600 36.66400  1.000 29.88819  ?  282  PRO   A N   1 
ATOM   2273  C  CA  . PRO   A 1 282  ? -13.86900  105.59100 35.74900  1.000 33.07517  ?  282  PRO   A CA  1 
ATOM   2274  C  C   . PRO   A 1 282  ? -14.25900  106.72900 34.81700  1.000 38.63671  ?  282  PRO   A C   1 
ATOM   2275  O  O   . PRO   A 1 282  ? -15.27500  106.66600 34.12100  1.000 41.53464  ?  282  PRO   A O   1 
ATOM   2276  C  CB  . PRO   A 1 282  ? -13.61900  104.29100 34.97900  1.000 29.90903  ?  282  PRO   A CB  1 
ATOM   2277  C  CG  . PRO   A 1 282  ? -14.91800  103.56800 35.03500  1.000 37.67492  ?  282  PRO   A CG  1 
ATOM   2278  C  CD  . PRO   A 1 282  ? -15.53500  103.91400 36.36200  1.000 39.34517  ?  282  PRO   A CD  1 
ATOM   2279  N  N   . ILE   A 1 283  ? -13.43300  107.76900 34.80300  1.000 36.32490  ?  283  ILE   A N   1 
ATOM   2280  C  CA  . ILE   A 1 283  ? -13.63100  108.93200 33.94800  1.000 45.97848  ?  283  ILE   A CA  1 
ATOM   2281  C  C   . ILE   A 1 283  ? -12.37500  109.11500 33.10900  1.000 54.75559  ?  283  ILE   A C   1 
ATOM   2282  O  O   . ILE   A 1 283  ? -11.28900  109.35400 33.65400  1.000 54.09915  ?  283  ILE   A O   1 
ATOM   2283  C  CB  . ILE   A 1 283  ? -13.93700  110.19500 34.76800  1.000 43.61870  ?  283  ILE   A CB  1 
ATOM   2284  C  CG1 . ILE   A 1 283  ? -15.17100  109.97200 35.64600  1.000 30.74715  ?  283  ILE   A CG1 1 
ATOM   2285  C  CG2 . ILE   A 1 283  ? -14.12300  111.39100 33.85000  1.000 47.92213  ?  283  ILE   A CG2 1 
ATOM   2286  C  CD1 . ILE   A 1 283  ? -15.77900  111.24800 36.18000  1.000 44.87040  ?  283  ILE   A CD1 1 
ATOM   2287  N  N   . ASP   A 1 284  ? -12.51900  108.99800 31.79500  1.000 54.82583  ?  284  ASP   A N   1 
ATOM   2288  C  CA  . ASP   A 1 284  ? -11.37300  109.13500 30.90300  1.000 53.58420  ?  284  ASP   A CA  1 
ATOM   2289  C  C   . ASP   A 1 284  ? -10.88900  110.58200 30.90300  1.000 63.80904  ?  284  ASP   A C   1 
ATOM   2290  O  O   . ASP   A 1 284  ? -11.68500  111.49500 30.65000  1.000 60.50556  ?  284  ASP   A O   1 
ATOM   2291  C  CB  . ASP   A 1 284  ? -11.74700  108.69400 29.49000  1.000 58.13957  ?  284  ASP   A CB  1 
ATOM   2292  C  CG  . ASP   A 1 284  ? -10.64600  108.96000 28.48500  1.000 69.49414  ?  284  ASP   A CG  1 
ATOM   2293  O  OD1 . ASP   A 1 284  ? -9.69400   108.15400 28.41500  1.000 74.77051  ?  284  ASP   A OD1 1 
ATOM   2294  O  OD2 . ASP   A 1 284  ? -10.73100  109.97800 27.76700  1.000 68.42521  -1 284  ASP   A OD2 1 
ATOM   2295  N  N   . PRO   A 1 285  ? -9.60600   110.83400 31.17800  1.000 53.02140  ?  285  PRO   A N   1 
ATOM   2296  C  CA  . PRO   A 1 285  ? -9.13800   112.22500 31.31100  1.000 50.80478  ?  285  PRO   A CA  1 
ATOM   2297  C  C   . PRO   A 1 285  ? -9.24700   113.04600 30.03600  1.000 57.28855  ?  285  PRO   A C   1 
ATOM   2298  O  O   . PRO   A 1 285  ? -9.15800   114.27800 30.10500  1.000 54.47870  ?  285  PRO   A O   1 
ATOM   2299  C  CB  . PRO   A 1 285  ? -7.67300   112.06400 31.74300  1.000 53.98022  ?  285  PRO   A CB  1 
ATOM   2300  C  CG  . PRO   A 1 285  ? -7.58700   110.68800 32.32000  1.000 58.15217  ?  285  PRO   A CG  1 
ATOM   2301  C  CD  . PRO   A 1 285  ? -8.56500   109.85900 31.54400  1.000 59.29790  ?  285  PRO   A CD  1 
ATOM   2302  N  N   . ASP   A 1 286  ? -9.43100   112.41400 28.88000  1.000 60.72368  ?  286  ASP   A N   1 
ATOM   2303  C  CA  . ASP   A 1 286  ? -9.51800   113.13000 27.61300  1.000 60.26390  ?  286  ASP   A CA  1 
ATOM   2304  C  C   . ASP   A 1 286  ? -10.95000  113.45200 27.20500  1.000 69.64764  ?  286  ASP   A C   1 
ATOM   2305  O  O   . ASP   A 1 286  ? -11.15900  113.99600 26.11500  1.000 65.04202  ?  286  ASP   A O   1 
ATOM   2306  C  CB  . ASP   A 1 286  ? -8.83800   112.32200 26.50100  1.000 54.87248  ?  286  ASP   A CB  1 
ATOM   2307  C  CG  . ASP   A 1 286  ? -7.58600   111.61200 26.97800  1.000 74.28495  ?  286  ASP   A CG  1 
ATOM   2308  O  OD1 . ASP   A 1 286  ? -6.56100   112.29200 27.20300  1.000 83.29620  ?  286  ASP   A OD1 1 
ATOM   2309  O  OD2 . ASP   A 1 286  ? -7.62700   110.37200 27.13100  1.000 71.94087  -1 286  ASP   A OD2 1 
ATOM   2310  N  N   . TYR   A 1 287  ? -11.93400  113.12900 28.04400  1.000 75.80033  ?  287  TYR   A N   1 
ATOM   2311  C  CA  . TYR   A 1 287  ? -13.32500  113.41200 27.73200  1.000 61.55941  ?  287  TYR   A CA  1 
ATOM   2312  C  C   . TYR   A 1 287  ? -13.57100  114.91800 27.73300  1.000 63.27241  ?  287  TYR   A C   1 
ATOM   2313  O  O   . TYR   A 1 287  ? -12.83800  115.67600 28.37300  1.000 71.31192  ?  287  TYR   A O   1 
ATOM   2314  C  CB  . TYR   A 1 287  ? -14.24900  112.73800 28.74600  1.000 59.09362  ?  287  TYR   A CB  1 
ATOM   2315  C  CG  . TYR   A 1 287  ? -14.55200  111.28500 28.45300  1.000 64.37973  ?  287  TYR   A CG  1 
ATOM   2316  C  CD1 . TYR   A 1 287  ? -14.24300  110.72100 27.22200  1.000 69.23845  ?  287  TYR   A CD1 1 
ATOM   2317  C  CD2 . TYR   A 1 287  ? -15.13900  110.47300 29.41300  1.000 54.43016  ?  287  TYR   A CD2 1 
ATOM   2318  C  CE1 . TYR   A 1 287  ? -14.51800  109.38800 26.95500  1.000 69.11689  ?  287  TYR   A CE1 1 
ATOM   2319  C  CE2 . TYR   A 1 287  ? -15.41700  109.14200 29.15600  1.000 53.94166  ?  287  TYR   A CE2 1 
ATOM   2320  C  CZ  . TYR   A 1 287  ? -15.10600  108.60500 27.92900  1.000 61.80694  ?  287  TYR   A CZ  1 
ATOM   2321  O  OH  . TYR   A 1 287  ? -15.38500  107.28100 27.68300  1.000 69.49621  ?  287  TYR   A OH  1 
ATOM   2322  N  N   . PRO   A 1 288  ? -14.59100  115.37700 27.00700  1.000 74.02332  ?  288  PRO   A N   1 
ATOM   2323  C  CA  . PRO   A 1 288  ? -14.96900  116.79200 27.09200  1.000 66.78165  ?  288  PRO   A CA  1 
ATOM   2324  C  C   . PRO   A 1 288  ? -15.30200  117.17500 28.52600  1.000 73.19617  ?  288  PRO   A C   1 
ATOM   2325  O  O   . PRO   A 1 288  ? -15.89700  116.39400 29.27300  1.000 76.24993  ?  288  PRO   A O   1 
ATOM   2326  C  CB  . PRO   A 1 288  ? -16.19500  116.88700 26.17800  1.000 68.95811  ?  288  PRO   A CB  1 
ATOM   2327  C  CG  . PRO   A 1 288  ? -16.03000  115.75200 25.21400  1.000 74.14184  ?  288  PRO   A CG  1 
ATOM   2328  C  CD  . PRO   A 1 288  ? -15.37000  114.65100 25.98900  1.000 68.79094  ?  288  PRO   A CD  1 
ATOM   2329  N  N   . GLY   A 1 289  ? -14.89500  118.39000 28.91000  1.000 65.68754  ?  289  GLY   A N   1 
ATOM   2330  C  CA  . GLY   A 1 289  ? -15.10700  118.84500 30.27600  1.000 67.00862  ?  289  GLY   A CA  1 
ATOM   2331  C  C   . GLY   A 1 289  ? -16.55600  118.78700 30.71700  1.000 82.67971  ?  289  GLY   A C   1 
ATOM   2332  O  O   . GLY   A 1 289  ? -16.84000  118.62800 31.90800  1.000 75.02489  ?  289  GLY   A O   1 
ATOM   2333  N  N   . GLU   A 1 290  ? -17.49000  118.91600 29.77000  1.000 87.41441  ?  290  GLU   A N   1 
ATOM   2334  C  CA  . GLU   A 1 290  ? -18.90400  118.75100 30.09500  1.000 73.14952  ?  290  GLU   A CA  1 
ATOM   2335  C  C   . GLU   A 1 290  ? -19.22900  117.29900 30.42700  1.000 73.04297  ?  290  GLU   A C   1 
ATOM   2336  O  O   . GLU   A 1 290  ? -19.96500  117.02700 31.38400  1.000 68.77455  ?  290  GLU   A O   1 
ATOM   2337  C  CB  . GLU   A 1 290  ? -19.76900  119.24400 28.93500  1.000 85.69972  ?  290  GLU   A CB  1 
ATOM   2338  C  CG  . GLU   A 1 290  ? -19.26200  118.82800 27.55900  1.000 100.22925 ?  290  GLU   A CG  1 
ATOM   2339  C  CD  . GLU   A 1 290  ? -20.06500  117.68900 26.95700  1.000 102.48520 ?  290  GLU   A CD  1 
ATOM   2340  O  OE1 . GLU   A 1 290  ? -21.26700  117.57200 27.27600  1.000 108.70323 ?  290  GLU   A OE1 1 
ATOM   2341  O  OE2 . GLU   A 1 290  ? -19.49100  116.91100 26.16400  1.000 86.09840  ?  290  GLU   A OE2 1 
ATOM   2342  N  N   . ARG   A 1 291  ? -18.69600  116.35100 29.64700  1.000 72.00865  ?  291  ARG   A N   1 
ATOM   2343  C  CA  . ARG   A 1 291  ? -18.90100  114.94100 29.96500  1.000 66.81183  ?  291  ARG   A CA  1 
ATOM   2344  C  C   . ARG   A 1 291  ? -18.35900  114.61800 31.35000  1.000 63.88023  ?  291  ARG   A C   1 
ATOM   2345  O  O   . ARG   A 1 291  ? -19.01000  113.91300 32.12700  1.000 61.76115  ?  291  ARG   A O   1 
ATOM   2346  C  CB  . ARG   A 1 291  ? -18.23500  114.04900 28.91500  1.000 50.67733  ?  291  ARG   A CB  1 
ATOM   2347  C  CG  . ARG   A 1 291  ? -19.01200  112.77500 28.54100  1.000 50.78789  ?  291  ARG   A CG  1 
ATOM   2348  C  CD  . ARG   A 1 291  ? -18.06400  111.74400 27.91600  1.000 64.16057  ?  291  ARG   A CD  1 
ATOM   2349  N  NE  . ARG   A 1 291  ? -18.67700  110.61500 27.21300  1.000 76.63451  ?  291  ARG   A NE  1 
ATOM   2350  C  CZ  . ARG   A 1 291  ? -19.53900  109.74200 27.72400  1.000 92.48833  ?  291  ARG   A CZ  1 
ATOM   2351  N  NH1 . ARG   A 1 291  ? -20.05500  109.89200 28.93300  1.000 72.81025  ?  291  ARG   A NH1 1 
ATOM   2352  N  NH2 . ARG   A 1 291  ? -19.91000  108.69500 26.99200  1.000 83.19249  ?  291  ARG   A NH2 1 
ATOM   2353  N  N   . ILE   A 1 292  ? -17.17500  115.14300 31.68000  1.000 55.65610  ?  292  ILE   A N   1 
ATOM   2354  C  CA  . ILE   A 1 292  ? -16.58300  114.90700 32.99700  1.000 60.35665  ?  292  ILE   A CA  1 
ATOM   2355  C  C   . ILE   A 1 292  ? -17.50000  115.43300 34.09400  1.000 64.25720  ?  292  ILE   A C   1 
ATOM   2356  O  O   . ILE   A 1 292  ? -17.75900  114.75100 35.09400  1.000 63.83944  ?  292  ILE   A O   1 
ATOM   2357  C  CB  . ILE   A 1 292  ? -15.18600  115.54800 33.07900  1.000 70.06206  ?  292  ILE   A CB  1 
ATOM   2358  C  CG1 . ILE   A 1 292  ? -14.20800  114.81700 32.15800  1.000 59.40958  ?  292  ILE   A CG1 1 
ATOM   2359  C  CG2 . ILE   A 1 292  ? -14.68100  115.56000 34.52200  1.000 57.16632  ?  292  ILE   A CG2 1 
ATOM   2360  C  CD1 . ILE   A 1 292  ? -12.80400  115.37100 32.19900  1.000 68.52376  ?  292  ILE   A CD1 1 
ATOM   2361  N  N   . ALA   A 1 293  ? -18.00300  116.65800 33.92300  1.000 67.60617  ?  293  ALA   A N   1 
ATOM   2362  C  CA  . ALA   A 1 293  ? -18.88600  117.24200 34.92700  1.000 59.98173  ?  293  ALA   A CA  1 
ATOM   2363  C  C   . ALA   A 1 293  ? -20.18200  116.45100 35.04900  1.000 65.20577  ?  293  ALA   A C   1 
ATOM   2364  O  O   . ALA   A 1 293  ? -20.71400  116.28300 36.15300  1.000 58.41648  ?  293  ALA   A O   1 
ATOM   2365  C  CB  . ALA   A 1 293  ? -19.17800  118.70200 34.58500  1.000 42.74162  ?  293  ALA   A CB  1 
ATOM   2366  N  N   . TYR   A 1 294  ? -20.70100  115.95300 33.92200  1.000 62.75139  ?  294  TYR   A N   1 
ATOM   2367  C  CA  . TYR   A 1 294  ? -21.93500  115.17600 33.95400  1.000 53.82407  ?  294  TYR   A CA  1 
ATOM   2368  C  C   . TYR   A 1 294  ? -21.77700  113.93300 34.82200  1.000 63.14293  ?  294  TYR   A C   1 
ATOM   2369  O  O   . TYR   A 1 294  ? -22.58900  113.68800 35.72300  1.000 52.01294  ?  294  TYR   A O   1 
ATOM   2370  C  CB  . TYR   A 1 294  ? -22.36400  114.79500 32.53500  1.000 51.99759  ?  294  TYR   A CB  1 
ATOM   2371  C  CG  . TYR   A 1 294  ? -23.45300  113.74000 32.50400  1.000 64.26430  ?  294  TYR   A CG  1 
ATOM   2372  C  CD1 . TYR   A 1 294  ? -24.76800  114.05900 32.82700  1.000 60.87839  ?  294  TYR   A CD1 1 
ATOM   2373  C  CD2 . TYR   A 1 294  ? -23.16400  112.42500 32.16700  1.000 68.37432  ?  294  TYR   A CD2 1 
ATOM   2374  C  CE1 . TYR   A 1 294  ? -25.76200  113.09700 32.81000  1.000 64.43600  ?  294  TYR   A CE1 1 
ATOM   2375  C  CE2 . TYR   A 1 294  ? -24.15100  111.45900 32.14800  1.000 73.57376  ?  294  TYR   A CE2 1 
ATOM   2376  C  CZ  . TYR   A 1 294  ? -25.44700  111.80000 32.46900  1.000 75.22673  ?  294  TYR   A CZ  1 
ATOM   2377  O  OH  . TYR   A 1 294  ? -26.43300  110.84100 32.45000  1.000 84.90404  ?  294  TYR   A OH  1 
ATOM   2378  N  N   . MET   A 1 295  ? -20.73200  113.13700 34.57100  1.000 57.47322  ?  295  MET   A N   1 
ATOM   2379  C  CA  . MET   A 1 295  ? -20.52500  111.92700 35.36200  1.000 52.66393  ?  295  MET   A CA  1 
ATOM   2380  C  C   . MET   A 1 295  ? -20.39000  112.25600 36.84200  1.000 57.67518  ?  295  MET   A C   1 
ATOM   2381  O  O   . MET   A 1 295  ? -21.02300  111.61800 37.69100  1.000 58.27680  ?  295  MET   A O   1 
ATOM   2382  C  CB  . MET   A 1 295  ? -19.28200  111.17100 34.90100  1.000 45.39314  ?  295  MET   A CB  1 
ATOM   2383  C  CG  . MET   A 1 295  ? -18.91100  111.27300 33.45400  1.000 54.56219  ?  295  MET   A CG  1 
ATOM   2384  S  SD  . MET   A 1 295  ? -18.04600  109.77700 32.95800  1.000 74.05048  ?  295  MET   A SD  1 
ATOM   2385  C  CE  . MET   A 1 295  ? -18.03300  110.00300 31.20000  1.000 41.94665  ?  295  MET   A CE  1 
ATOM   2386  N  N   . LEU   A 1 296  ? -19.55200  113.24200 37.17000  1.000 47.82996  ?  296  LEU   A N   1 
ATOM   2387  C  CA  . LEU   A 1 296  ? -19.32300  113.58700 38.57000  1.000 60.87779  ?  296  LEU   A CA  1 
ATOM   2388  C  C   . LEU   A 1 296  ? -20.63000  113.95200 39.26400  1.000 59.03819  ?  296  LEU   A C   1 
ATOM   2389  O  O   . LEU   A 1 296  ? -20.92900  113.45600 40.35600  1.000 71.11666  ?  296  LEU   A O   1 
ATOM   2390  C  CB  . LEU   A 1 296  ? -18.31700  114.73600 38.66800  1.000 59.45604  ?  296  LEU   A CB  1 
ATOM   2391  C  CG  . LEU   A 1 296  ? -16.86800  114.42000 38.28800  1.000 59.46726  ?  296  LEU   A CG  1 
ATOM   2392  C  CD1 . LEU   A 1 296  ? -16.04400  115.69700 38.19400  1.000 50.11279  ?  296  LEU   A CD1 1 
ATOM   2393  C  CD2 . LEU   A 1 296  ? -16.25400  113.45600 39.28600  1.000 54.46795  ?  296  LEU   A CD2 1 
ATOM   2394  N  N   . ALA   A 1 297  ? -21.43500  114.80500 38.62700  1.000 66.05058  ?  297  ALA   A N   1 
ATOM   2395  C  CA  . ALA   A 1 297  ? -22.71300  115.19300 39.21300  1.000 53.65500  ?  297  ALA   A CA  1 
ATOM   2396  C  C   . ALA   A 1 297  ? -23.70000  114.03200 39.20900  1.000 61.33662  ?  297  ALA   A C   1 
ATOM   2397  O  O   . ALA   A 1 297  ? -24.41400  113.81500 40.19500  1.000 65.44830  ?  297  ALA   A O   1 
ATOM   2398  C  CB  . ALA   A 1 297  ? -23.28800  116.39400 38.46700  1.000 56.94147  ?  297  ALA   A CB  1 
ATOM   2399  N  N   . ASP   A 1 298  ? -23.75700  113.27500 38.10800  1.000 48.62361  ?  298  ASP   A N   1 
ATOM   2400  C  CA  . ASP   A 1 298  ? -24.65400  112.12400 38.05500  1.000 57.93323  ?  298  ASP   A CA  1 
ATOM   2401  C  C   . ASP   A 1 298  ? -24.26200  111.07400 39.08900  1.000 65.29950  ?  298  ASP   A C   1 
ATOM   2402  O  O   . ASP   A 1 298  ? -25.12700  110.51600 39.77400  1.000 78.94936  ?  298  ASP   A O   1 
ATOM   2403  C  CB  . ASP   A 1 298  ? -24.66200  111.52000 36.65000  1.000 64.48680  ?  298  ASP   A CB  1 
ATOM   2404  C  CG  . ASP   A 1 298  ? -25.91900  110.71100 36.36700  1.000 79.93905  ?  298  ASP   A CG  1 
ATOM   2405  O  OD1 . ASP   A 1 298  ? -26.78200  110.61100 37.26500  1.000 72.56299  ?  298  ASP   A OD1 1 
ATOM   2406  O  OD2 . ASP   A 1 298  ? -26.04600  110.17400 35.24500  1.000 78.69010  -1 298  ASP   A OD2 1 
ATOM   2407  N  N   . SER   A 1 299  ? -22.96400  110.79800 39.22300  1.000 66.50354  ?  299  SER   A N   1 
ATOM   2408  C  CA  . SER   A 1 299  ? -22.50400  109.83600 40.21800  1.000 64.12939  ?  299  SER   A CA  1 
ATOM   2409  C  C   . SER   A 1 299  ? -22.57500  110.37800 41.63700  1.000 57.96411  ?  299  SER   A C   1 
ATOM   2410  O  O   . SER   A 1 299  ? -22.48100  109.58900 42.58400  1.000 68.27818  ?  299  SER   A O   1 
ATOM   2411  C  CB  . SER   A 1 299  ? -21.07300  109.39900 39.90500  1.000 56.17846  ?  299  SER   A CB  1 
ATOM   2412  O  OG  . SER   A 1 299  ? -20.18300  110.49600 40.00200  1.000 58.93852  ?  299  SER   A OG  1 
ATOM   2413  N  N   . SER   A 1 300  ? -22.75400  111.69000 41.80200  1.000 55.73935  ?  300  SER   A N   1 
ATOM   2414  C  CA  . SER   A 1 300  ? -22.74900  112.33800 43.11400  1.000 71.50953  ?  300  SER   A CA  1 
ATOM   2415  C  C   . SER   A 1 300  ? -21.50000  111.94500 43.89600  1.000 74.30425  ?  300  SER   A C   1 
ATOM   2416  O  O   . SER   A 1 300  ? -21.55900  111.50500 45.04600  1.000 70.84616  ?  300  SER   A O   1 
ATOM   2417  C  CB  . SER   A 1 300  ? -24.02200  112.01400 43.89800  1.000 89.07053  ?  300  SER   A CB  1 
ATOM   2418  O  OG  . SER   A 1 300  ? -25.08200  112.88400 43.53500  1.000 84.66198  ?  300  SER   A OG  1 
ATOM   2419  N  N   . ALA   A 1 301  ? -20.35500  112.09100 43.24000  1.000 70.96461  ?  301  ALA   A N   1 
ATOM   2420  C  CA  . ALA   A 1 301  ? -19.07300  111.72100 43.81900  1.000 63.50957  ?  301  ALA   A CA  1 
ATOM   2421  C  C   . ALA   A 1 301  ? -18.49800  112.92000 44.56000  1.000 71.50513  ?  301  ALA   A C   1 
ATOM   2422  O  O   . ALA   A 1 301  ? -18.32800  113.99500 43.97400  1.000 73.62216  ?  301  ALA   A O   1 
ATOM   2423  C  CB  . ALA   A 1 301  ? -18.11100  111.24200 42.73300  1.000 58.79918  ?  301  ALA   A CB  1 
ATOM   2424  N  N   . ALA   A 1 302  ? -18.21500  112.74000 45.84700  1.000 63.94970  ?  302  ALA   A N   1 
ATOM   2425  C  CA  . ALA   A 1 302  ? -17.54900  113.77900 46.61800  1.000 55.64794  ?  302  ALA   A CA  1 
ATOM   2426  C  C   . ALA   A 1 302  ? -16.03700  113.72800 46.47300  1.000 64.95157  ?  302  ALA   A C   1 
ATOM   2427  O  O   . ALA   A 1 302  ? -15.37100  114.75600 46.63800  1.000 73.96673  ?  302  ALA   A O   1 
ATOM   2428  C  CB  . ALA   A 1 302  ? -17.92500  113.66400 48.09900  1.000 56.78967  ?  302  ALA   A CB  1 
ATOM   2429  N  N   . ILE   A 1 303  ? -15.48400  112.55700 46.16400  1.000 71.64566  ?  303  ILE   A N   1 
ATOM   2430  C  CA  . ILE   A 1 303  ? -14.04400  112.34300 46.10200  1.000 57.97512  ?  303  ILE   A CA  1 
ATOM   2431  C  C   . ILE   A 1 303  ? -13.67400  111.92300 44.68800  1.000 54.18035  ?  303  ILE   A C   1 
ATOM   2432  O  O   . ILE   A 1 303  ? -14.29500  111.01600 44.12200  1.000 51.84825  ?  303  ILE   A O   1 
ATOM   2433  C  CB  . ILE   A 1 303  ? -13.58700  111.28100 47.11900  1.000 56.30275  ?  303  ILE   A CB  1 
ATOM   2434  C  CG1 . ILE   A 1 303  ? -13.71900  111.81900 48.54300  1.000 53.07795  ?  303  ILE   A CG1 1 
ATOM   2435  C  CG2 . ILE   A 1 303  ? -12.14800  110.86000 46.84400  1.000 64.72096  ?  303  ILE   A CG2 1 
ATOM   2436  C  CD1 . ILE   A 1 303  ? -13.73100  110.74000 49.60100  1.000 49.12533  ?  303  ILE   A CD1 1 
ATOM   2437  N  N   . LEU   A 1 304  ? -12.66100  112.57600 44.12400  1.000 49.05017  ?  304  LEU   A N   1 
ATOM   2438  C  CA  . LEU   A 1 304  ? -12.12000  112.23300 42.81700  1.000 42.28471  ?  304  LEU   A CA  1 
ATOM   2439  C  C   . LEU   A 1 304  ? -10.64100  111.90600 42.96100  1.000 53.64661  ?  304  LEU   A C   1 
ATOM   2440  O  O   . LEU   A 1 304  ? -9.87500   112.71100 43.49900  1.000 67.78507  ?  304  LEU   A O   1 
ATOM   2441  C  CB  . LEU   A 1 304  ? -12.31100  113.37900 41.82000  1.000 39.29934  ?  304  LEU   A CB  1 
ATOM   2442  C  CG  . LEU   A 1 304  ? -11.50100  113.29900 40.52300  1.000 39.51098  ?  304  LEU   A CG  1 
ATOM   2443  C  CD1 . LEU   A 1 304  ? -11.96300  112.13900 39.65600  1.000 44.68133  ?  304  LEU   A CD1 1 
ATOM   2444  C  CD2 . LEU   A 1 304  ? -11.59600  114.60600 39.76100  1.000 42.43256  ?  304  LEU   A CD2 1 
ATOM   2445  N  N   . LEU   A 1 305  ? -10.24200  110.73000 42.48200  1.000 55.33470  ?  305  LEU   A N   1 
ATOM   2446  C  CA  . LEU   A 1 305  ? -8.84100   110.31300 42.49000  1.000 33.91834  ?  305  LEU   A CA  1 
ATOM   2447  C  C   . LEU   A 1 305  ? -8.23900   110.63600 41.12500  1.000 36.56642  ?  305  LEU   A C   1 
ATOM   2448  O  O   . LEU   A 1 305  ? -8.38700   109.86800 40.17100  1.000 49.10196  ?  305  LEU   A O   1 
ATOM   2449  C  CB  . LEU   A 1 305  ? -8.71400   108.83000 42.82000  1.000 40.93079  ?  305  LEU   A CB  1 
ATOM   2450  C  CG  . LEU   A 1 305  ? -9.15100   108.38200 44.21800  1.000 48.24460  ?  305  LEU   A CG  1 
ATOM   2451  C  CD1 . LEU   A 1 305  ? -9.22700   106.86800 44.29600  1.000 44.98487  ?  305  LEU   A CD1 1 
ATOM   2452  C  CD2 . LEU   A 1 305  ? -8.20400   108.91400 45.27400  1.000 48.24474  ?  305  LEU   A CD2 1 
ATOM   2453  N  N   . THR   A 1 306  ? -7.56300   111.77800 41.03300  1.000 34.57711  ?  306  THR   A N   1 
ATOM   2454  C  CA  . THR   A 1 306  ? -6.82400   112.17100 39.84200  1.000 49.62935  ?  306  THR   A CA  1 
ATOM   2455  C  C   . THR   A 1 306  ? -5.44400   112.66900 40.26600  1.000 53.33202  ?  306  THR   A C   1 
ATOM   2456  O  O   . THR   A 1 306  ? -5.06900   112.60200 41.44000  1.000 43.79754  ?  306  THR   A O   1 
ATOM   2457  C  CB  . THR   A 1 306  ? -7.58600   113.23700 39.04100  1.000 47.19909  ?  306  THR   A CB  1 
ATOM   2458  O  OG1 . THR   A 1 306  ? -6.88500   113.52600 37.82300  1.000 50.32584  ?  306  THR   A OG1 1 
ATOM   2459  C  CG2 . THR   A 1 306  ? -7.73200   114.50600 39.85400  1.000 49.33349  ?  306  THR   A CG2 1 
ATOM   2460  N  N   . ASN   A 1 307  ? -4.67100   113.15700 39.30000  1.000 48.55008  ?  307  ASN   A N   1 
ATOM   2461  C  CA  . ASN   A 1 307  ? -3.36300   113.71700 39.58200  1.000 44.12501  ?  307  ASN   A CA  1 
ATOM   2462  C  C   . ASN   A 1 307  ? -3.38800   115.23300 39.36200  1.000 62.71068  ?  307  ASN   A C   1 
ATOM   2463  O  O   . ASN   A 1 307  ? -4.46300   115.84700 39.30100  1.000 67.85592  ?  307  ASN   A O   1 
ATOM   2464  C  CB  . ASN   A 1 307  ? -2.31100   112.98700 38.73400  1.000 44.05163  ?  307  ASN   A CB  1 
ATOM   2465  C  CG  . ASN   A 1 307  ? -2.40600   113.30700 37.24500  1.000 67.31305  ?  307  ASN   A CG  1 
ATOM   2466  O  OD1 . ASN   A 1 307  ? -2.94700   114.33400 36.83400  1.000 76.01664  ?  307  ASN   A OD1 1 
ATOM   2467  N  ND2 . ASN   A 1 307  ? -1.86700   112.41400 36.42700  1.000 65.45461  ?  307  ASN   A ND2 1 
ATOM   2468  N  N   . ALA   A 1 308  ? -2.20400   115.83300 39.23200  1.000 61.25754  ?  308  ALA   A N   1 
ATOM   2469  C  CA  . ALA   A 1 308  ? -2.11800   117.26300 38.96500  1.000 62.04009  ?  308  ALA   A CA  1 
ATOM   2470  C  C   . ALA   A 1 308  ? -2.28900   117.59500 37.48900  1.000 66.64256  ?  308  ALA   A C   1 
ATOM   2471  O  O   . ALA   A 1 308  ? -2.68700   118.72000 37.16400  1.000 84.61430  ?  308  ALA   A O   1 
ATOM   2472  C  CB  . ALA   A 1 308  ? -0.78100   117.81400 39.46400  1.000 51.31687  ?  308  ALA   A CB  1 
ATOM   2473  N  N   . LEU   A 1 309  ? -1.99900   116.64800 36.59400  1.000 56.74019  ?  309  LEU   A N   1 
ATOM   2474  C  CA  . LEU   A 1 309  ? -2.12500   116.91300 35.16400  1.000 69.48658  ?  309  LEU   A CA  1 
ATOM   2475  C  C   . LEU   A 1 309  ? -3.58900   117.04500 34.75900  1.000 76.18453  ?  309  LEU   A C   1 
ATOM   2476  O  O   . LEU   A 1 309  ? -3.93700   117.90300 33.93900  1.000 80.57241  ?  309  LEU   A O   1 
ATOM   2477  C  CB  . LEU   A 1 309  ? -1.43400   115.80300 34.36900  1.000 58.61429  ?  309  LEU   A CB  1 
ATOM   2478  C  CG  . LEU   A 1 309  ? -1.42600   115.79700 32.83400  1.000 67.36949  ?  309  LEU   A CG  1 
ATOM   2479  C  CD1 . LEU   A 1 309  ? -1.40300   117.19900 32.22900  1.000 72.67526  ?  309  LEU   A CD1 1 
ATOM   2480  C  CD2 . LEU   A 1 309  ? -0.25100   114.98000 32.32200  1.000 84.12400  ?  309  LEU   A CD2 1 
ATOM   2481  N  N   . HIS   A 1 310  ? -4.46500   116.21700 35.32900  1.000 71.25956  ?  310  HIS   A N   1 
ATOM   2482  C  CA  . HIS   A 1 310  ? -5.88400   116.24900 35.00200  1.000 61.92081  ?  310  HIS   A CA  1 
ATOM   2483  C  C   . HIS   A 1 310  ? -6.72200   116.90200 36.09700  1.000 68.16997  ?  310  HIS   A C   1 
ATOM   2484  O  O   . HIS   A 1 310  ? -7.94200   116.72200 36.12700  1.000 79.46631  ?  310  HIS   A O   1 
ATOM   2485  C  CB  . HIS   A 1 310  ? -6.39300   114.83500 34.71700  1.000 69.16863  ?  310  HIS   A CB  1 
ATOM   2486  C  CG  . HIS   A 1 310  ? -5.48400   114.02800 33.84300  1.000 52.76046  ?  310  HIS   A CG  1 
ATOM   2487  N  ND1 . HIS   A 1 310  ? -5.18800   114.38700 32.54500  1.000 44.86188  ?  310  HIS   A ND1 1 
ATOM   2488  C  CD2 . HIS   A 1 310  ? -4.81500   112.87500 34.07700  1.000 39.22947  ?  310  HIS   A CD2 1 
ATOM   2489  C  CE1 . HIS   A 1 310  ? -4.37200   113.49100 32.01900  1.000 65.14967  ?  310  HIS   A CE1 1 
ATOM   2490  N  NE2 . HIS   A 1 310  ? -4.13000   112.56300 32.92700  1.000 61.40331  ?  310  HIS   A NE2 1 
ATOM   2491  N  N   . GLU   A 1 311  ? -6.09800   117.67600 36.98500  1.000 75.85773  ?  311  GLU   A N   1 
ATOM   2492  C  CA  . GLU   A 1 311  ? -6.82100   118.21200 38.13500  1.000 66.15802  ?  311  GLU   A CA  1 
ATOM   2493  C  C   . GLU   A 1 311  ? -7.85800   119.24700 37.71400  1.000 64.49115  ?  311  GLU   A C   1 
ATOM   2494  O  O   . GLU   A 1 311  ? -9.02400   119.16800 38.11600  1.000 73.66306  ?  311  GLU   A O   1 
ATOM   2495  C  CB  . GLU   A 1 311  ? -5.83500   118.81600 39.13300  1.000 78.65733  ?  311  GLU   A CB  1 
ATOM   2496  C  CG  . GLU   A 1 311  ? -6.28200   118.71300 40.57700  1.000 88.20233  ?  311  GLU   A CG  1 
ATOM   2497  C  CD  . GLU   A 1 311  ? -5.25900   119.28100 41.53800  1.000 92.03824  ?  311  GLU   A CD  1 
ATOM   2498  O  OE1 . GLU   A 1 311  ? -4.27400   119.88700 41.06600  1.000 77.66255  ?  311  GLU   A OE1 1 
ATOM   2499  O  OE2 . GLU   A 1 311  ? -5.43700   119.12000 42.76300  1.000 84.60385  -1 311  GLU   A OE2 1 
ATOM   2500  N  N   . GLU   A 1 312  ? -7.45100   120.22600 36.90200  1.000 77.26128  ?  312  GLU   A N   1 
ATOM   2501  C  CA  . GLU   A 1 312  ? -8.32500   121.33800 36.54500  1.000 62.06764  ?  312  GLU   A CA  1 
ATOM   2502  C  C   . GLU   A 1 312  ? -9.51400   120.92100 35.69200  1.000 62.88687  ?  312  GLU   A C   1 
ATOM   2503  O  O   . GLU   A 1 312  ? -10.39600  121.75000 35.44900  1.000 88.25754  ?  312  GLU   A O   1 
ATOM   2504  C  CB  . GLU   A 1 312  ? -7.53000   122.42000 35.81500  1.000 63.44625  ?  312  GLU   A CB  1 
ATOM   2505  C  CG  . GLU   A 1 312  ? -6.13200   122.63300 36.36000  1.000 71.05206  ?  312  GLU   A CG  1 
ATOM   2506  C  CD  . GLU   A 1 312  ? -5.72800   124.09300 36.35400  1.000 105.44846 ?  312  GLU   A CD  1 
ATOM   2507  O  OE1 . GLU   A 1 312  ? -6.49100   124.92400 36.89300  1.000 108.64947 ?  312  GLU   A OE1 1 
ATOM   2508  O  OE2 . GLU   A 1 312  ? -4.65100   124.41100 35.80800  1.000 116.45216 -1 312  GLU   A OE2 1 
ATOM   2509  N  N   . LYS   A 1 313  ? -9.56300   119.67500 35.23200  1.000 63.83908  ?  313  LYS   A N   1 
ATOM   2510  C  CA  . LYS   A 1 313  ? -10.71500  119.19200 34.48400  1.000 72.41307  ?  313  LYS   A CA  1 
ATOM   2511  C  C   . LYS   A 1 313  ? -11.91900  118.91700 35.37500  1.000 67.22493  ?  313  LYS   A C   1 
ATOM   2512  O  O   . LYS   A 1 313  ? -12.98800  118.57600 34.85600  1.000 64.59306  ?  313  LYS   A O   1 
ATOM   2513  C  CB  . LYS   A 1 313  ? -10.32600  117.93800 33.69900  1.000 61.94085  ?  313  LYS   A CB  1 
ATOM   2514  C  CG  . LYS   A 1 313  ? -8.95500   118.06500 33.06000  1.000 64.54694  ?  313  LYS   A CG  1 
ATOM   2515  C  CD  . LYS   A 1 313  ? -8.63500   116.91400 32.12900  1.000 62.95957  ?  313  LYS   A CD  1 
ATOM   2516  C  CE  . LYS   A 1 313  ? -7.24700   117.09400 31.53300  1.000 62.76431  ?  313  LYS   A CE  1 
ATOM   2517  N  NZ  . LYS   A 1 313  ? -6.88000   116.01600 30.57600  1.000 66.89404  ?  313  LYS   A NZ  1 
ATOM   2518  N  N   . ALA   A 1 314  ? -11.77100  119.05700 36.69400  1.000 64.34830  ?  314  ALA   A N   1 
ATOM   2519  C  CA  . ALA   A 1 314  ? -12.89700  118.99900 37.61400  1.000 69.73541  ?  314  ALA   A CA  1 
ATOM   2520  C  C   . ALA   A 1 314  ? -13.50200  120.36800 37.89100  1.000 78.03353  ?  314  ALA   A C   1 
ATOM   2521  O  O   . ALA   A 1 314  ? -14.66400  120.44200 38.30400  1.000 72.89848  ?  314  ALA   A O   1 
ATOM   2522  C  CB  . ALA   A 1 314  ? -12.47200  118.36000 38.94000  1.000 61.26678  ?  314  ALA   A CB  1 
ATOM   2523  N  N   . ASN   A 1 315  ? -12.74500  121.44500 37.66800  1.000 84.62402  ?  315  ASN   A N   1 
ATOM   2524  C  CA  . ASN   A 1 315  ? -13.20900  122.81400 37.91100  1.000 79.50793  ?  315  ASN   A CA  1 
ATOM   2525  C  C   . ASN   A 1 315  ? -13.64300  122.99900 39.36500  1.000 94.00001  ?  315  ASN   A C   1 
ATOM   2526  O  O   . ASN   A 1 315  ? -14.67900  123.60500 39.65100  1.000 84.13307  ?  315  ASN   A O   1 
ATOM   2527  C  CB  . ASN   A 1 315  ? -14.33900  123.20100 36.95200  1.000 78.87801  ?  315  ASN   A CB  1 
ATOM   2528  C  CG  . ASN   A 1 315  ? -13.89400  123.23200 35.49900  1.000 88.52292  ?  315  ASN   A CG  1 
ATOM   2529  O  OD1 . ASN   A 1 315  ? -13.03100  122.45900 35.08200  1.000 96.20510  ?  315  ASN   A OD1 1 
ATOM   2530  N  ND2 . ASN   A 1 315  ? -14.48500  124.13000 34.71900  1.000 90.66678  ?  315  ASN   A ND2 1 
ATOM   2531  N  N   . GLY   A 1 316  ? -12.84200  122.47000 40.29000  1.000 95.82960  ?  316  GLY   A N   1 
ATOM   2532  C  CA  . GLY   A 1 316  ? -13.13000  122.56400 41.70900  1.000 74.46466  ?  316  GLY   A CA  1 
ATOM   2533  C  C   . GLY   A 1 316  ? -14.45800  121.94500 42.09000  1.000 75.50360  ?  316  GLY   A C   1 
ATOM   2534  O  O   . GLY   A 1 316  ? -15.28500  122.58800 42.74300  1.000 75.93481  ?  316  GLY   A O   1 
ATOM   2535  N  N   . ALA   A 1 317  ? -14.67400  120.68900 41.69000  1.000 84.20454  ?  317  ALA   A N   1 
ATOM   2536  C  CA  . ALA   A 1 317  ? -15.96100  120.03500 41.87300  1.000 74.40192  ?  317  ALA   A CA  1 
ATOM   2537  C  C   . ALA   A 1 317  ? -15.94900  118.88800 42.86600  1.000 80.90780  ?  317  ALA   A C   1 
ATOM   2538  O  O   . ALA   A 1 317  ? -17.02400  118.45500 43.28800  1.000 92.84929  ?  317  ALA   A O   1 
ATOM   2539  C  CB  . ALA   A 1 317  ? -16.48600  119.49800 40.53600  1.000 67.65469  ?  317  ALA   A CB  1 
ATOM   2540  N  N   . CYS   A 1 318  ? -14.78200  118.36400 43.22800  1.000 68.90298  ?  318  CYS   A N   1 
ATOM   2541  C  CA  . CYS   A 1 318  ? -14.70300  117.27400 44.18600  1.000 62.89451  ?  318  CYS   A CA  1 
ATOM   2542  C  C   . CYS   A 1 318  ? -13.52500  117.51900 45.11200  1.000 66.07923  ?  318  CYS   A C   1 
ATOM   2543  O  O   . CYS   A 1 318  ? -12.73100  118.44300 44.91700  1.000 72.18087  ?  318  CYS   A O   1 
ATOM   2544  C  CB  . CYS   A 1 318  ? -14.55300  115.91100 43.49600  1.000 64.73366  ?  318  CYS   A CB  1 
ATOM   2545  S  SG  . CYS   A 1 318  ? -15.94900  115.39100 42.47600  1.000 73.07424  ?  318  CYS   A SG  1 
ATOM   2546  N  N   . ASP   A 1 319  ? -13.41900  116.67600 46.13300  1.000 58.20176  ?  319  ASP   A N   1 
ATOM   2547  C  CA  . ASP   A 1 319  ? -12.23300  116.65400 46.98200  1.000 59.78034  ?  319  ASP   A CA  1 
ATOM   2548  C  C   . ASP   A 1 319  ? -11.14500  115.89500 46.23400  1.000 62.65142  ?  319  ASP   A C   1 
ATOM   2549  O  O   . ASP   A 1 319  ? -11.13300  114.66300 46.20900  1.000 74.01096  ?  319  ASP   A O   1 
ATOM   2550  C  CB  . ASP   A 1 319  ? -12.54000  116.01200 48.32900  1.000 58.03376  ?  319  ASP   A CB  1 
ATOM   2551  C  CG  . ASP   A 1 319  ? -11.43600  116.23700 49.34500  1.000 87.70001  ?  319  ASP   A CG  1 
ATOM   2552  O  OD1 . ASP   A 1 319  ? -10.46500  116.95900 49.02900  1.000 92.53149  ?  319  ASP   A OD1 1 
ATOM   2553  O  OD2 . ASP   A 1 319  ? -11.53900  115.69100 50.46300  1.000 107.83285 -1 319  ASP   A OD2 1 
ATOM   2554  N  N   . ILE   A 1 320  ? -10.22900  116.63500 45.61300  1.000 53.70022  ?  320  ILE   A N   1 
ATOM   2555  C  CA  . ILE   A 1 320  ? -9.16300   116.01300 44.83700  1.000 59.20480  ?  320  ILE   A CA  1 
ATOM   2556  C  C   . ILE   A 1 320  ? -8.18200   115.34300 45.78900  1.000 68.97286  ?  320  ILE   A C   1 
ATOM   2557  O  O   . ILE   A 1 320  ? -7.63400   115.98200 46.69500  1.000 67.81961  ?  320  ILE   A O   1 
ATOM   2558  C  CB  . ILE   A 1 320  ? -8.45800   117.04200 43.94500  1.000 56.57148  ?  320  ILE   A CB  1 
ATOM   2559  C  CG1 . ILE   A 1 320  ? -9.48500   117.85800 43.15900  1.000 56.57889  ?  320  ILE   A CG1 1 
ATOM   2560  C  CG2 . ILE   A 1 320  ? -7.49800   116.34700 42.99600  1.000 75.46619  ?  320  ILE   A CG2 1 
ATOM   2561  C  CD1 . ILE   A 1 320  ? -10.36700  117.02100 42.25600  1.000 76.31888  ?  320  ILE   A CD1 1 
ATOM   2562  N  N   . ILE   A 1 321  ? -7.96400   114.04800 45.59000  1.000 59.53306  ?  321  ILE   A N   1 
ATOM   2563  C  CA  . ILE   A 1 321  ? -6.98500   113.27900 46.34400  1.000 54.43697  ?  321  ILE   A CA  1 
ATOM   2564  C  C   . ILE   A 1 321  ? -5.88700   112.89400 45.36300  1.000 60.61547  ?  321  ILE   A C   1 
ATOM   2565  O  O   . ILE   A 1 321  ? -6.05300   111.97200 44.55600  1.000 56.54081  ?  321  ILE   A O   1 
ATOM   2566  C  CB  . ILE   A 1 321  ? -7.61000   112.04900 47.00900  1.000 42.82907  ?  321  ILE   A CB  1 
ATOM   2567  C  CG1 . ILE   A 1 321  ? -8.71100   112.48200 47.97500  1.000 60.71005  ?  321  ILE   A CG1 1 
ATOM   2568  C  CG2 . ILE   A 1 321  ? -6.55500   111.23300 47.73200  1.000 51.70709  ?  321  ILE   A CG2 1 
ATOM   2569  C  CD1 . ILE   A 1 321  ? -9.17900   111.38100 48.88600  1.000 61.62340  ?  321  ILE   A CD1 1 
ATOM   2570  N  N   . ASP   A 1 322  ? -4.76600   113.61300 45.42000  1.000 65.18462  ?  322  ASP   A N   1 
ATOM   2571  C  CA  . ASP   A 1 322  ? -3.66100   113.35700 44.50600  1.000 66.91837  ?  322  ASP   A CA  1 
ATOM   2572  C  C   . ASP   A 1 322  ? -3.08300   111.97100 44.74700  1.000 64.60927  ?  322  ASP   A C   1 
ATOM   2573  O  O   . ASP   A 1 322  ? -2.69500   111.63300 45.86800  1.000 66.67163  ?  322  ASP   A O   1 
ATOM   2574  C  CB  . ASP   A 1 322  ? -2.57300   114.41600 44.68100  1.000 61.51940  ?  322  ASP   A CB  1 
ATOM   2575  C  CG  . ASP   A 1 322  ? -1.64500   114.50600 43.48300  1.000 68.86144  ?  322  ASP   A CG  1 
ATOM   2576  O  OD1 . ASP   A 1 322  ? -1.42800   113.47800 42.80400  1.000 80.30610  ?  322  ASP   A OD1 1 
ATOM   2577  O  OD2 . ASP   A 1 322  ? -1.13200   115.61200 43.21700  1.000 78.50013  -1 322  ASP   A OD2 1 
ATOM   2578  N  N   . VAL   A 1 323  ? -3.02100   111.16500 43.68100  1.000 52.59029  ?  323  VAL   A N   1 
ATOM   2579  C  CA  . VAL   A 1 323  ? -2.43900   109.82900 43.78400  1.000 60.29594  ?  323  VAL   A CA  1 
ATOM   2580  C  C   . VAL   A 1 323  ? -0.92100   109.85200 43.81100  1.000 59.33203  ?  323  VAL   A C   1 
ATOM   2581  O  O   . VAL   A 1 323  ? -0.29900   108.78400 43.86800  1.000 54.63524  ?  323  VAL   A O   1 
ATOM   2582  C  CB  . VAL   A 1 323  ? -2.92500   108.92800 42.63100  1.000 60.54372  ?  323  VAL   A CB  1 
ATOM   2583  C  CG1 . VAL   A 1 323  ? -4.42400   108.69200 42.74600  1.000 48.32858  ?  323  VAL   A CG1 1 
ATOM   2584  C  CG2 . VAL   A 1 323  ? -2.57600   109.55200 41.28700  1.000 57.28889  ?  323  VAL   A CG2 1 
ATOM   2585  N  N   . HIS   A 1 324  ? -0.30400   111.03700 43.77000  1.000 61.81754  ?  324  HIS   A N   1 
ATOM   2586  C  CA  . HIS   A 1 324  ? 1.13500    111.18300 43.92900  1.000 53.10412  ?  324  HIS   A CA  1 
ATOM   2587  C  C   . HIS   A 1 324  ? 1.53100    111.88500 45.22000  1.000 72.19456  ?  324  HIS   A C   1 
ATOM   2588  O  O   . HIS   A 1 324  ? 2.68500    111.75800 45.64400  1.000 79.33191  ?  324  HIS   A O   1 
ATOM   2589  C  CB  . HIS   A 1 324  ? 1.73100    111.95300 42.74100  1.000 57.58674  ?  324  HIS   A CB  1 
ATOM   2590  C  CG  . HIS   A 1 324  ? 1.56900    111.25400 41.42700  1.000 76.50026  ?  324  HIS   A CG  1 
ATOM   2591  N  ND1 . HIS   A 1 324  ? 2.23700    110.08900 41.11700  1.000 81.25163  ?  324  HIS   A ND1 1 
ATOM   2592  C  CD2 . HIS   A 1 324  ? 0.81600    111.55600 40.34200  1.000 80.32071  ?  324  HIS   A CD2 1 
ATOM   2593  C  CE1 . HIS   A 1 324  ? 1.90200    109.70200 39.89900  1.000 83.71172  ?  324  HIS   A CE1 1 
ATOM   2594  N  NE2 . HIS   A 1 324  ? 1.04100    110.57400 39.40700  1.000 88.60151  ?  324  HIS   A NE2 1 
ATOM   2595  N  N   . ASP   A 1 325  ? 0.61600    112.61700 45.84300  1.000 81.15813  ?  325  ASP   A N   1 
ATOM   2596  C  CA  . ASP   A 1 325  ? 0.86700    113.21700 47.14500  1.000 80.39204  ?  325  ASP   A CA  1 
ATOM   2597  C  C   . ASP   A 1 325  ? 1.04000    112.11800 48.18700  1.000 79.47106  ?  325  ASP   A C   1 
ATOM   2598  O  O   . ASP   A 1 325  ? 0.13500    111.28400 48.35100  1.000 73.38824  ?  325  ASP   A O   1 
ATOM   2599  C  CB  . ASP   A 1 325  ? -0.28600   114.14000 47.53200  1.000 87.35809  ?  325  ASP   A CB  1 
ATOM   2600  C  CG  . ASP   A 1 325  ? 0.06500    115.06700 48.67700  1.000 89.17242  ?  325  ASP   A CG  1 
ATOM   2601  O  OD1 . ASP   A 1 325  ? 1.05200    114.79100 49.39000  1.000 80.42255  ?  325  ASP   A OD1 1 
ATOM   2602  O  OD2 . ASP   A 1 325  ? -0.65400   116.07100 48.86700  1.000 112.12890 -1 325  ASP   A OD2 1 
ATOM   2603  N  N   . PRO   A 1 326  ? 2.17100    112.06500 48.89300  1.000 84.82862  ?  326  PRO   A N   1 
ATOM   2604  C  CA  . PRO   A 1 326  ? 2.35700    110.99400 49.88600  1.000 79.61604  ?  326  PRO   A CA  1 
ATOM   2605  C  C   . PRO   A 1 326  ? 1.34100    111.03100 51.01100  1.000 71.93301  ?  326  PRO   A C   1 
ATOM   2606  O  O   . PRO   A 1 326  ? 0.98100    109.97300 51.54200  1.000 79.00089  ?  326  PRO   A O   1 
ATOM   2607  C  CB  . PRO   A 1 326  ? 3.78300    111.23800 50.40100  1.000 78.26930  ?  326  PRO   A CB  1 
ATOM   2608  C  CG  . PRO   A 1 326  ? 4.44700    112.05800 49.33900  1.000 68.99142  ?  326  PRO   A CG  1 
ATOM   2609  C  CD  . PRO   A 1 326  ? 3.36900    112.90600 48.74500  1.000 81.47715  ?  326  PRO   A CD  1 
ATOM   2610  N  N   . ASP   A 1 327  ? 0.85700    112.21700 51.38600  1.000 72.52997  ?  327  ASP   A N   1 
ATOM   2611  C  CA  . ASP   A 1 327  ? -0.11600   112.31400 52.46800  1.000 80.66857  ?  327  ASP   A CA  1 
ATOM   2612  C  C   . ASP   A 1 327  ? -1.46100   111.70900 52.09400  1.000 79.02519  ?  327  ASP   A C   1 
ATOM   2613  O  O   . ASP   A 1 327  ? -2.28300   111.45800 52.98400  1.000 74.78697  ?  327  ASP   A O   1 
ATOM   2614  C  CB  . ASP   A 1 327  ? -0.29500   113.77300 52.88300  1.000 77.81153  ?  327  ASP   A CB  1 
ATOM   2615  C  CG  . ASP   A 1 327  ? 0.94800    114.34600 53.53000  1.000 98.32891  ?  327  ASP   A CG  1 
ATOM   2616  O  OD1 . ASP   A 1 327  ? 1.45200    113.73100 54.49300  1.000 98.47361  ?  327  ASP   A OD1 1 
ATOM   2617  O  OD2 . ASP   A 1 327  ? 1.42400    115.40600 53.07200  1.000 100.06515 -1 327  ASP   A OD2 1 
ATOM   2618  N  N   . SER   A 1 328  ? -1.70600   111.47500 50.80200  1.000 74.66480  ?  328  SER   A N   1 
ATOM   2619  C  CA  . SER   A 1 328  ? -2.91000   110.76800 50.38600  1.000 57.86614  ?  328  SER   A CA  1 
ATOM   2620  C  C   . SER   A 1 328  ? -2.82200   109.27800 50.67500  1.000 40.89553  ?  328  SER   A C   1 
ATOM   2621  O  O   . SER   A 1 328  ? -3.84800   108.59200 50.64100  1.000 55.77607  ?  328  SER   A O   1 
ATOM   2622  C  CB  . SER   A 1 328  ? -3.17400   110.99200 48.89700  1.000 57.66100  ?  328  SER   A CB  1 
ATOM   2623  O  OG  . SER   A 1 328  ? -3.00300   112.35300 48.53700  1.000 67.33133  ?  328  SER   A OG  1 
ATOM   2624  N  N   . TYR   A 1 329  ? -1.62800   108.76400 50.94700  1.000 44.79933  ?  329  TYR   A N   1 
ATOM   2625  C  CA  . TYR   A 1 329  ? -1.43700   107.38400 51.36800  1.000 60.17263  ?  329  TYR   A CA  1 
ATOM   2626  C  C   . TYR   A 1 329  ? -1.09700   107.36100 52.85200  1.000 59.85324  ?  329  TYR   A C   1 
ATOM   2627  O  O   . TYR   A 1 329  ? -0.31500   108.18800 53.33100  1.000 64.32613  ?  329  TYR   A O   1 
ATOM   2628  C  CB  . TYR   A 1 329  ? -0.32600   106.70300 50.55800  1.000 37.64340  ?  329  TYR   A CB  1 
ATOM   2629  C  CG  . TYR   A 1 329  ? -0.54800   106.70800 49.05700  1.000 41.69059  ?  329  TYR   A CG  1 
ATOM   2630  C  CD1 . TYR   A 1 329  ? -0.25900   107.83300 48.29500  1.000 47.99533  ?  329  TYR   A CD1 1 
ATOM   2631  C  CD2 . TYR   A 1 329  ? -1.04700   105.58600 48.40300  1.000 42.60310  ?  329  TYR   A CD2 1 
ATOM   2632  C  CE1 . TYR   A 1 329  ? -0.46000   107.84400 46.92600  1.000 48.41371  ?  329  TYR   A CE1 1 
ATOM   2633  C  CE2 . TYR   A 1 329  ? -1.25000   105.58800 47.03100  1.000 43.42014  ?  329  TYR   A CE2 1 
ATOM   2634  C  CZ  . TYR   A 1 329  ? -0.95500   106.72200 46.30000  1.000 39.29967  ?  329  TYR   A CZ  1 
ATOM   2635  O  OH  . TYR   A 1 329  ? -1.15000   106.74600 44.93800  1.000 52.38214  ?  329  TYR   A OH  1 
ATOM   2636  N  N   . SER   A 1 330  ? -1.69300   106.42200 53.58300  1.000 59.92437  ?  330  SER   A N   1 
ATOM   2637  C  CA  . SER   A 1 330  ? -1.45000   106.32100 55.01200  1.000 48.44282  ?  330  SER   A CA  1 
ATOM   2638  C  C   . SER   A 1 330  ? -0.20200   105.48300 55.27400  1.000 52.90453  ?  330  SER   A C   1 
ATOM   2639  O  O   . SER   A 1 330  ? 0.50100    105.05600 54.35600  1.000 73.73538  ?  330  SER   A O   1 
ATOM   2640  C  CB  . SER   A 1 330  ? -2.66200   105.72600 55.72900  1.000 46.15697  ?  330  SER   A CB  1 
ATOM   2641  O  OG  . SER   A 1 330  ? -2.63100   104.30800 55.69700  1.000 61.54951  ?  330  SER   A OG  1 
ATOM   2642  N  N   . GLU   A 1 331  ? 0.08400    105.25100 56.55300  1.000 56.42729  ?  331  GLU   A N   1 
ATOM   2643  C  CA  . GLU   A 1 331  ? 1.18200    104.38800 56.95500  1.000 56.60781  ?  331  GLU   A CA  1 
ATOM   2644  C  C   . GLU   A 1 331  ? 0.72600    102.97100 57.26400  1.000 58.27375  ?  331  GLU   A C   1 
ATOM   2645  O  O   . GLU   A 1 331  ? 1.56900    102.07700 57.39700  1.000 71.17737  ?  331  GLU   A O   1 
ATOM   2646  C  CB  . GLU   A 1 331  ? 1.90000    104.97400 58.17700  1.000 44.65862  ?  331  GLU   A CB  1 
ATOM   2647  N  N   . ASN   A 1 332  ? -0.58000   102.74700 57.37500  1.000 45.60989  ?  332  ASN   A N   1 
ATOM   2648  C  CA  . ASN   A 1 332  ? -1.11800   101.42200 57.65400  1.000 54.03586  ?  332  ASN   A CA  1 
ATOM   2649  C  C   . ASN   A 1 332  ? -1.13300   100.62200 56.35800  1.000 54.33141  ?  332  ASN   A C   1 
ATOM   2650  O  O   . ASN   A 1 332  ? -1.86800   100.95500 55.42300  1.000 60.47722  ?  332  ASN   A O   1 
ATOM   2651  C  CB  . ASN   A 1 332  ? -2.51500   101.53400 58.25600  1.000 43.25876  ?  332  ASN   A CB  1 
ATOM   2652  C  CG  . ASN   A 1 332  ? -2.91900   100.29400 59.02700  1.000 64.08646  ?  332  ASN   A CG  1 
ATOM   2653  O  OD1 . ASN   A 1 332  ? -2.51400   99.18000  58.69300  1.000 66.64968  ?  332  ASN   A OD1 1 
ATOM   2654  N  ND2 . ASN   A 1 332  ? -3.72600   100.48000 60.06500  1.000 59.51665  ?  332  ASN   A ND2 1 
ATOM   2655  N  N   . THR   A 1 333  ? -0.31600   99.57200  56.29400  1.000 56.74228  ?  333  THR   A N   1 
ATOM   2656  C  CA  . THR   A 1 333  ? -0.24300   98.71000  55.12300  1.000 57.53793  ?  333  THR   A CA  1 
ATOM   2657  C  C   . THR   A 1 333  ? -0.99400   97.40300  55.31900  1.000 49.28276  ?  333  THR   A C   1 
ATOM   2658  O  O   . THR   A 1 333  ? -0.67600   96.40900  54.65800  1.000 63.94480  ?  333  THR   A O   1 
ATOM   2659  C  CB  . THR   A 1 333  ? 1.21300    98.41300  54.76400  1.000 48.54873  ?  333  THR   A CB  1 
ATOM   2660  O  OG1 . THR   A 1 333  ? 1.85700    97.77500  55.87400  1.000 44.52250  ?  333  THR   A OG1 1 
ATOM   2661  C  CG2 . THR   A 1 333  ? 1.95100    99.69400  54.40400  1.000 35.79425  ?  333  THR   A CG2 1 
ATOM   2662  N  N   . ASN   A 1 334  ? -1.97300   97.37700  56.21500  1.000 46.21273  ?  334  ASN   A N   1 
ATOM   2663  C  CA  . ASN   A 1 334  ? -2.68400   96.15600  56.55100  1.000 50.75023  ?  334  ASN   A CA  1 
ATOM   2664  C  C   . ASN   A 1 334  ? -4.08300   96.17500  55.95100  1.000 58.81742  ?  334  ASN   A C   1 
ATOM   2665  O  O   . ASN   A 1 334  ? -4.65400   97.23500  55.67500  1.000 52.89299  ?  334  ASN   A O   1 
ATOM   2666  C  CB  . ASN   A 1 334  ? -2.75700   95.96900  58.06900  1.000 55.22938  ?  334  ASN   A CB  1 
ATOM   2667  C  CG  . ASN   A 1 334  ? -1.38500   95.88000  58.70800  1.000 74.23413  ?  334  ASN   A CG  1 
ATOM   2668  O  OD1 . ASN   A 1 334  ? -0.77300   94.81200  58.74800  1.000 75.66723  ?  334  ASN   A OD1 1 
ATOM   2669  N  ND2 . ASN   A 1 334  ? -0.88800   97.01000  59.20000  1.000 62.92424  ?  334  ASN   A ND2 1 
ATOM   2670  N  N   . ASN   A 1 335  ? -4.62700   94.97700  55.75000  1.000 52.17145  ?  335  ASN   A N   1 
ATOM   2671  C  CA  . ASN   A 1 335  ? -5.93700   94.84200  55.13000  1.000 45.86296  ?  335  ASN   A CA  1 
ATOM   2672  C  C   . ASN   A 1 335  ? -7.01200   95.47900  56.00200  1.000 59.64979  ?  335  ASN   A C   1 
ATOM   2673  O  O   . ASN   A 1 335  ? -7.13100   95.17000  57.19200  1.000 70.12720  ?  335  ASN   A O   1 
ATOM   2674  C  CB  . ASN   A 1 335  ? -6.25100   93.36500  54.88600  1.000 44.33368  ?  335  ASN   A CB  1 
ATOM   2675  C  CG  . ASN   A 1 335  ? -5.52900   92.80800  53.66800  1.000 41.43387  ?  335  ASN   A CG  1 
ATOM   2676  O  OD1 . ASN   A 1 335  ? -5.24800   93.53200  52.71200  1.000 32.95916  ?  335  ASN   A OD1 1 
ATOM   2677  N  ND2 . ASN   A 1 335  ? -5.23500   91.51300  53.69600  1.000 30.46703  ?  335  ASN   A ND2 1 
ATOM   2678  N  N   . LEU   A 1 336  ? -7.79300   96.37500  55.40300  1.000 57.54886  ?  336  LEU   A N   1 
ATOM   2679  C  CA  . LEU   A 1 336  ? -8.83300   97.07700  56.13700  1.000 49.68188  ?  336  LEU   A CA  1 
ATOM   2680  C  C   . LEU   A 1 336  ? -9.93300   96.10800  56.56800  1.000 54.59885  ?  336  LEU   A C   1 
ATOM   2681  O  O   . LEU   A 1 336  ? -10.14900  95.07500  55.92900  1.000 56.15809  ?  336  LEU   A O   1 
ATOM   2682  C  CB  . LEU   A 1 336  ? -9.43400   98.19200  55.28200  1.000 36.55060  ?  336  LEU   A CB  1 
ATOM   2683  C  CG  . LEU   A 1 336  ? -8.62200   99.48100  55.12900  1.000 54.01819  ?  336  LEU   A CG  1 
ATOM   2684  C  CD1 . LEU   A 1 336  ? -7.52100   99.31200  54.09700  1.000 54.05533  ?  336  LEU   A CD1 1 
ATOM   2685  C  CD2 . LEU   A 1 336  ? -9.52200   100.65300 54.76600  1.000 48.06214  ?  336  LEU   A CD2 1 
ATOM   2686  N  N   . PRO   A 1 337  ? -10.63600  96.41400  57.65800  1.000 60.38412  ?  337  PRO   A N   1 
ATOM   2687  C  CA  . PRO   A 1 337  ? -11.78600  95.58600  58.04400  1.000 56.35873  ?  337  PRO   A CA  1 
ATOM   2688  C  C   . PRO   A 1 337  ? -12.88700  95.65700  56.99300  1.000 58.80415  ?  337  PRO   A C   1 
ATOM   2689  O  O   . PRO   A 1 337  ? -13.19700  96.72600  56.46200  1.000 43.63064  ?  337  PRO   A O   1 
ATOM   2690  C  CB  . PRO   A 1 337  ? -12.23200  96.19700  59.37800  1.000 56.79361  ?  337  PRO   A CB  1 
ATOM   2691  C  CG  . PRO   A 1 337  ? -11.66800  97.58800  59.37500  1.000 38.86603  ?  337  PRO   A CG  1 
ATOM   2692  C  CD  . PRO   A 1 337  ? -10.37600  97.49200  58.62700  1.000 48.23011  ?  337  PRO   A CD  1 
ATOM   2693  N  N   . HIS   A 1 338  ? -13.48200  94.50200  56.70100  1.000 48.49830  ?  338  HIS   A N   1 
ATOM   2694  C  CA  . HIS   A 1 338  ? -14.44100  94.39200  55.60900  1.000 60.07672  ?  338  HIS   A CA  1 
ATOM   2695  C  C   . HIS   A 1 338  ? -15.79300  94.97200  56.00800  1.000 60.91576  ?  338  HIS   A C   1 
ATOM   2696  O  O   . HIS   A 1 338  ? -16.37500  94.57900  57.02400  1.000 50.62175  ?  338  HIS   A O   1 
ATOM   2697  C  CB  . HIS   A 1 338  ? -14.59400  92.93100  55.18900  1.000 44.44375  ?  338  HIS   A CB  1 
ATOM   2698  C  CG  . HIS   A 1 338  ? -13.40100  92.39300  54.46600  1.000 71.14814  ?  338  HIS   A CG  1 
ATOM   2699  N  ND1 . HIS   A 1 338  ? -13.04200  91.06300  54.50300  1.000 79.03384  ?  338  HIS   A ND1 1 
ATOM   2700  C  CD2 . HIS   A 1 338  ? -12.47600  93.01200  53.69400  1.000 75.05504  ?  338  HIS   A CD2 1 
ATOM   2701  C  CE1 . HIS   A 1 338  ? -11.94700  90.88500  53.78500  1.000 70.77045  ?  338  HIS   A CE1 1 
ATOM   2702  N  NE2 . HIS   A 1 338  ? -11.58400  92.05200  53.28200  1.000 72.13360  ?  338  HIS   A NE2 1 
ATOM   2703  N  N   . VAL   A 1 339  ? -16.29000  95.90600  55.19600  1.000 52.96371  ?  339  VAL   A N   1 
ATOM   2704  C  CA  . VAL   A 1 339  ? -17.57500  96.55700  55.40300  1.000 42.72334  ?  339  VAL   A CA  1 
ATOM   2705  C  C   . VAL   A 1 339  ? -18.51000  96.36000  54.21600  1.000 55.34205  ?  339  VAL   A C   1 
ATOM   2706  O  O   . VAL   A 1 339  ? -19.58700  96.95600  54.17300  1.000 52.45979  ?  339  VAL   A O   1 
ATOM   2707  C  CB  . VAL   A 1 339  ? -17.39700  98.05800  55.70700  1.000 46.35457  ?  339  VAL   A CB  1 
ATOM   2708  C  CG1 . VAL   A 1 339  ? -16.58200  98.24800  56.97200  1.000 49.33640  ?  339  VAL   A CG1 1 
ATOM   2709  C  CG2 . VAL   A 1 339  ? -16.74200  98.77300  54.53100  1.000 50.62988  ?  339  VAL   A CG2 1 
ATOM   2710  N  N   . ASN   A 1 340  ? -18.11500  95.53900  53.24800  1.000 57.35560  ?  340  ASN   A N   1 
ATOM   2711  C  CA  . ASN   A 1 340  ? -18.88300  95.32000  52.03400  1.000 37.64284  ?  340  ASN   A CA  1 
ATOM   2712  C  C   . ASN   A 1 340  ? -19.54900  93.95200  52.06500  1.000 50.54523  ?  340  ASN   A C   1 
ATOM   2713  O  O   . ASN   A 1 340  ? -19.14700  93.05100  52.80800  1.000 37.94321  ?  340  ASN   A O   1 
ATOM   2714  C  CB  . ASN   A 1 340  ? -17.99400  95.43800  50.79100  1.000 45.72237  ?  340  ASN   A CB  1 
ATOM   2715  C  CG  . ASN   A 1 340  ? -17.39000  96.81900  50.63500  1.000 58.19855  ?  340  ASN   A CG  1 
ATOM   2716  O  OD1 . ASN   A 1 340  ? -18.06200  97.75500  50.20600  1.000 56.98436  ?  340  ASN   A OD1 1 
ATOM   2717  N  ND2 . ASN   A 1 340  ? -16.11400  96.95200  50.98100  1.000 61.79339  ?  340  ASN   A ND2 1 
ATOM   2718  N  N   . ARG   A 1 341  ? -20.58100  93.81500  51.24000  1.000 52.50171  ?  341  ARG   A N   1 
ATOM   2719  C  CA  . ARG   A 1 341  ? -21.34000  92.59200  51.05400  1.000 40.66757  ?  341  ARG   A CA  1 
ATOM   2720  C  C   . ARG   A 1 341  ? -21.46300  92.31000  49.56500  1.000 40.00853  ?  341  ARG   A C   1 
ATOM   2721  O  O   . ARG   A 1 341  ? -21.38800  93.23700  48.75200  1.000 45.57279  ?  341  ARG   A O   1 
ATOM   2722  C  CB  . ARG   A 1 341  ? -22.73400  92.71400  51.68500  1.000 61.06075  ?  341  ARG   A CB  1 
ATOM   2723  C  CG  . ARG   A 1 341  ? -23.39200  94.06300  51.45600  1.000 65.61168  ?  341  ARG   A CG  1 
ATOM   2724  C  CD  . ARG   A 1 341  ? -24.58800  94.26000  52.37500  1.000 61.80852  ?  341  ARG   A CD  1 
ATOM   2725  N  NE  . ARG   A 1 341  ? -24.19800  94.77500  53.68200  1.000 66.20714  ?  341  ARG   A NE  1 
ATOM   2726  C  CZ  . ARG   A 1 341  ? -24.37600  94.13400  54.83000  1.000 74.11068  ?  341  ARG   A CZ  1 
ATOM   2727  N  NH1 . ARG   A 1 341  ? -24.94500  92.94100  54.87600  1.000 75.21990  ?  341  ARG   A NH1 1 
ATOM   2728  N  NH2 . ARG   A 1 341  ? -23.97800  94.70900  55.96300  1.000 70.81582  ?  341  ARG   A NH2 1 
ATOM   2729  N  N   . PRO   A 1 342  ? -21.64600  91.03600  49.17300  1.000 30.12567  ?  342  PRO   A N   1 
ATOM   2730  C  CA  . PRO   A 1 342  ? -21.66500  90.69400  47.74000  1.000 37.89196  ?  342  PRO   A CA  1 
ATOM   2731  C  C   . PRO   A 1 342  ? -22.65300  91.51000  46.91400  1.000 51.64312  ?  342  PRO   A C   1 
ATOM   2732  O  O   . PRO   A 1 342  ? -22.47700  91.65800  45.70000  1.000 50.41342  ?  342  PRO   A O   1 
ATOM   2733  C  CB  . PRO   A 1 342  ? -22.04600  89.20900  47.74700  1.000 42.32888  ?  342  PRO   A CB  1 
ATOM   2734  C  CG  . PRO   A 1 342  ? -21.52100  88.70100  49.04400  1.000 40.83389  ?  342  PRO   A CG  1 
ATOM   2735  C  CD  . PRO   A 1 342  ? -21.69900  89.83400  50.02600  1.000 38.63431  ?  342  PRO   A CD  1 
ATOM   2736  N  N   . ASP   A 1 343  ? -23.68700  92.04900  47.55800  1.000 61.53997  ?  343  ASP   A N   1 
ATOM   2737  C  CA  . ASP   A 1 343  ? -24.70100  92.84800  46.88400  1.000 49.77710  ?  343  ASP   A CA  1 
ATOM   2738  C  C   . ASP   A 1 343  ? -24.32500  94.32400  46.78100  1.000 53.20462  ?  343  ASP   A C   1 
ATOM   2739  O  O   . ASP   A 1 343  ? -25.13800  95.12700  46.31200  1.000 54.03463  ?  343  ASP   A O   1 
ATOM   2740  C  CB  . ASP   A 1 343  ? -26.04600  92.69700  47.60300  1.000 51.17220  ?  343  ASP   A CB  1 
ATOM   2741  C  CG  . ASP   A 1 343  ? -26.31100  91.26800  48.05000  1.000 79.75551  ?  343  ASP   A CG  1 
ATOM   2742  O  OD1 . ASP   A 1 343  ? -26.79900  90.46600  47.22500  1.000 79.00517  ?  343  ASP   A OD1 1 
ATOM   2743  O  OD2 . ASP   A 1 343  ? -26.03100  90.94600  49.22400  1.000 86.35394  -1 343  ASP   A OD2 1 
ATOM   2744  N  N   . ASP   A 1 344  ? -23.11800  94.69800  47.19300  1.000 52.82249  ?  344  ASP   A N   1 
ATOM   2745  C  CA  . ASP   A 1 344  ? -22.69800  96.09100  47.16800  1.000 51.75033  ?  344  ASP   A CA  1 
ATOM   2746  C  C   . ASP   A 1 344  ? -22.13900  96.45400  45.79600  1.000 43.30772  ?  344  ASP   A C   1 
ATOM   2747  O  O   . ASP   A 1 344  ? -21.54200  95.62300  45.10500  1.000 49.70559  ?  344  ASP   A O   1 
ATOM   2748  C  CB  . ASP   A 1 344  ? -21.64700  96.35700  48.25100  1.000 64.58470  ?  344  ASP   A CB  1 
ATOM   2749  C  CG  . ASP   A 1 344  ? -22.23600  96.98800  49.50500  1.000 76.78328  ?  344  ASP   A CG  1 
ATOM   2750  O  OD1 . ASP   A 1 344  ? -23.47700  96.98500  49.65500  1.000 84.37564  ?  344  ASP   A OD1 1 
ATOM   2751  O  OD2 . ASP   A 1 344  ? -21.45300  97.48400  50.34600  1.000 73.79619  -1 344  ASP   A OD2 1 
ATOM   2752  N  N   . LEU   A 1 345  ? -22.34600  97.71100  45.40700  1.000 32.55352  ?  345  LEU   A N   1 
ATOM   2753  C  CA  . LEU   A 1 345  ? -21.82500  98.20400  44.13900  1.000 40.61029  ?  345  LEU   A CA  1 
ATOM   2754  C  C   . LEU   A 1 345  ? -20.30600  98.11100  44.09800  1.000 58.58187  ?  345  LEU   A C   1 
ATOM   2755  O  O   . LEU   A 1 345  ? -19.62000  98.42400  45.07500  1.000 56.89869  ?  345  LEU   A O   1 
ATOM   2756  C  CB  . LEU   A 1 345  ? -22.25000  99.65300  43.91800  1.000 30.87764  ?  345  LEU   A CB  1 
ATOM   2757  C  CG  . LEU   A 1 345  ? -23.71400  99.87600  43.57200  1.000 42.45530  ?  345  LEU   A CG  1 
ATOM   2758  C  CD1 . LEU   A 1 345  ? -23.88100  101.26800 42.98100  1.000 30.94907  ?  345  LEU   A CD1 1 
ATOM   2759  C  CD2 . LEU   A 1 345  ? -24.18800  98.78900  42.61500  1.000 44.78410  ?  345  LEU   A CD2 1 
ATOM   2760  N  N   . VAL   A 1 346  ? -19.77800  97.69900  42.94900  1.000 57.59548  ?  346  VAL   A N   1 
ATOM   2761  C  CA  . VAL   A 1 346  ? -18.34400  97.58200  42.75000  1.000 42.20945  ?  346  VAL   A CA  1 
ATOM   2762  C  C   . VAL   A 1 346  ? -17.82600  98.60000  41.73900  1.000 38.54907  ?  346  VAL   A C   1 
ATOM   2763  O  O   . VAL   A 1 346  ? -16.72300  99.12700  41.90200  1.000 57.00766  ?  346  VAL   A O   1 
ATOM   2764  C  CB  . VAL   A 1 346  ? -17.95500  96.14000  42.34800  1.000 39.19927  ?  346  VAL   A CB  1 
ATOM   2765  C  CG1 . VAL   A 1 346  ? -18.43300  95.80400  40.94200  1.000 35.56391  ?  346  VAL   A CG1 1 
ATOM   2766  C  CG2 . VAL   A 1 346  ? -16.44900  95.93900  42.47800  1.000 24.39607  ?  346  VAL   A CG2 1 
ATOM   2767  N  N   . TYR   A 1 347  ? -18.60700  98.91100  40.70500  1.000 37.03591  ?  347  TYR   A N   1 
ATOM   2768  C  CA  . TYR   A 1 347  ? -18.22100  99.95900  39.77000  1.000 39.89636  ?  347  TYR   A CA  1 
ATOM   2769  C  C   . TYR   A 1 347  ? -19.45600  100.44500 39.02800  1.000 40.26349  ?  347  TYR   A C   1 
ATOM   2770  O  O   . TYR   A 1 347  ? -20.48500  99.76600  38.97400  1.000 38.96602  ?  347  TYR   A O   1 
ATOM   2771  C  CB  . TYR   A 1 347  ? -17.13400  99.49200  38.78400  1.000 36.78356  ?  347  TYR   A CB  1 
ATOM   2772  C  CG  . TYR   A 1 347  ? -17.54000  98.44000  37.76200  1.000 38.32487  ?  347  TYR   A CG  1 
ATOM   2773  C  CD1 . TYR   A 1 347  ? -18.29500  98.77600  36.64100  1.000 34.33860  ?  347  TYR   A CD1 1 
ATOM   2774  C  CD2 . TYR   A 1 347  ? -17.12300  97.12100  37.89400  1.000 34.06549  ?  347  TYR   A CD2 1 
ATOM   2775  C  CE1 . TYR   A 1 347  ? -18.65000  97.82400  35.70400  1.000 33.38483  ?  347  TYR   A CE1 1 
ATOM   2776  C  CE2 . TYR   A 1 347  ? -17.47100  96.16100  36.95900  1.000 30.52148  ?  347  TYR   A CE2 1 
ATOM   2777  C  CZ  . TYR   A 1 347  ? -18.23500  96.51800  35.86800  1.000 42.22019  ?  347  TYR   A CZ  1 
ATOM   2778  O  OH  . TYR   A 1 347  ? -18.58300  95.56600  34.93800  1.000 39.95115  ?  347  TYR   A OH  1 
ATOM   2779  N  N   . VAL   A 1 348  ? -19.33100  101.64200 38.45900  1.000 26.85878  ?  348  VAL   A N   1 
ATOM   2780  C  CA  . VAL   A 1 348  ? -20.37500  102.25900 37.65400  1.000 29.82301  ?  348  VAL   A CA  1 
ATOM   2781  C  C   . VAL   A 1 348  ? -19.72800  102.74600 36.36900  1.000 33.90181  ?  348  VAL   A C   1 
ATOM   2782  O  O   . VAL   A 1 348  ? -18.86800  103.63500 36.40300  1.000 33.85621  ?  348  VAL   A O   1 
ATOM   2783  C  CB  . VAL   A 1 348  ? -21.06500  103.42600 38.38000  1.000 40.24550  ?  348  VAL   A CB  1 
ATOM   2784  C  CG1 . VAL   A 1 348  ? -21.98200  104.17000 37.41700  1.000 27.93461  ?  348  VAL   A CG1 1 
ATOM   2785  C  CG2 . VAL   A 1 348  ? -21.83300  102.93000 39.59900  1.000 26.55667  ?  348  VAL   A CG2 1 
ATOM   2786  N  N   . MET   A 1 349  ? -20.13600  102.17100 35.24300  1.000 41.68017  ?  349  MET   A N   1 
ATOM   2787  C  CA  . MET   A 1 349  ? -19.61000  102.53200 33.93600  1.000 42.72435  ?  349  MET   A CA  1 
ATOM   2788  C  C   . MET   A 1 349  ? -20.71900  103.14000 33.09100  1.000 35.91712  ?  349  MET   A C   1 
ATOM   2789  O  O   . MET   A 1 349  ? -21.81300  102.57300 32.99400  1.000 39.33247  ?  349  MET   A O   1 
ATOM   2790  C  CB  . MET   A 1 349  ? -19.00700  101.31600 33.23700  1.000 38.18472  ?  349  MET   A CB  1 
ATOM   2791  C  CG  . MET   A 1 349  ? -17.49600  101.32700 33.22100  1.000 35.11889  ?  349  MET   A CG  1 
ATOM   2792  S  SD  . MET   A 1 349  ? -16.82400  99.68500  32.95700  1.000 53.62328  ?  349  MET   A SD  1 
ATOM   2793  C  CE  . MET   A 1 349  ? -15.71800  99.54900  34.35700  1.000 48.39985  ?  349  MET   A CE  1 
ATOM   2794  N  N   . TYR   A 1 350  ? -20.43100  104.28700 32.48300  1.000 45.63842  ?  350  TYR   A N   1 
ATOM   2795  C  CA  . TYR   A 1 350  ? -21.41400  105.01800 31.69800  1.000 43.73663  ?  350  TYR   A CA  1 
ATOM   2796  C  C   . TYR   A 1 350  ? -21.40600  104.53000 30.25700  1.000 47.80113  ?  350  TYR   A C   1 
ATOM   2797  O  O   . TYR   A 1 350  ? -20.34700  104.29000 29.67200  1.000 66.42115  ?  350  TYR   A O   1 
ATOM   2798  C  CB  . TYR   A 1 350  ? -21.14300  106.52400 31.75900  1.000 35.78220  ?  350  TYR   A CB  1 
ATOM   2799  C  CG  . TYR   A 1 350  ? -21.59100  107.14500 33.06500  1.000 56.19432  ?  350  TYR   A CG  1 
ATOM   2800  C  CD1 . TYR   A 1 350  ? -20.90800  106.88700 34.24700  1.000 56.95315  ?  350  TYR   A CD1 1 
ATOM   2801  C  CD2 . TYR   A 1 350  ? -22.71400  107.96400 33.12300  1.000 50.75258  ?  350  TYR   A CD2 1 
ATOM   2802  C  CE1 . TYR   A 1 350  ? -21.31800  107.43600 35.44700  1.000 53.90037  ?  350  TYR   A CE1 1 
ATOM   2803  C  CE2 . TYR   A 1 350  ? -23.13200  108.52000 34.32100  1.000 51.23397  ?  350  TYR   A CE2 1 
ATOM   2804  C  CZ  . TYR   A 1 350  ? -22.43000  108.25100 35.48000  1.000 61.94804  ?  350  TYR   A CZ  1 
ATOM   2805  O  OH  . TYR   A 1 350  ? -22.83800  108.79700 36.67600  1.000 64.78766  ?  350  TYR   A OH  1 
ATOM   2806  N  N   . THR   A 1 351  ? -22.60000  104.36500 29.69600  1.000 61.42378  ?  351  THR   A N   1 
ATOM   2807  C  CA  . THR   A 1 351  ? -22.76300  103.88600 28.33300  1.000 66.39483  ?  351  THR   A CA  1 
ATOM   2808  C  C   . THR   A 1 351  ? -23.65000  104.85700 27.56700  1.000 77.14230  ?  351  THR   A C   1 
ATOM   2809  O  O   . THR   A 1 351  ? -24.61900  105.39400 28.11400  1.000 89.17197  ?  351  THR   A O   1 
ATOM   2810  C  CB  . THR   A 1 351  ? -23.33000  102.44300 28.31500  1.000 78.58686  ?  351  THR   A CB  1 
ATOM   2811  O  OG1 . THR   A 1 351  ? -23.06700  101.82800 27.04700  1.000 93.01061  ?  351  THR   A OG1 1 
ATOM   2812  C  CG2 . THR   A 1 351  ? -24.81600  102.40600 28.60900  1.000 54.05608  ?  351  THR   A CG2 1 
ATOM   2813  N  N   . SER   A 1 352  ? -23.28700  105.11200 26.31100  1.000 80.07469  ?  352  SER   A N   1 
ATOM   2814  C  CA  . SER   A 1 352  ? -23.98800  106.11200 25.51500  1.000 111.22619 ?  352  SER   A CA  1 
ATOM   2815  C  C   . SER   A 1 352  ? -23.75100  105.92200 24.02300  1.000 119.37957 ?  352  SER   A C   1 
ATOM   2816  O  O   . SER   A 1 352  ? -23.66700  104.79100 23.53500  1.000 109.81072 ?  352  SER   A O   1 
ATOM   2817  C  CB  . SER   A 1 352  ? -23.56200  107.52000 25.93300  1.000 109.61598 ?  352  SER   A CB  1 
ATOM   2818  O  OG  . SER   A 1 352  ? -24.50300  108.48500 25.49500  1.000 120.80561 ?  352  SER   A OG  1 
ATOM   2819  N  N   . GLY   A 1 353  ? -23.63500  107.03000 23.29500  1.000 126.16217 ?  353  GLY   A N   1 
ATOM   2820  C  CA  . GLY   A 1 353  ? -23.53700  106.97900 21.85300  1.000 115.39833 ?  353  GLY   A CA  1 
ATOM   2821  C  C   . GLY   A 1 353  ? -24.86500  106.95200 21.13700  1.000 134.43209 ?  353  GLY   A C   1 
ATOM   2822  O  O   . GLY   A 1 353  ? -24.88700  106.82100 19.90800  1.000 138.32845 ?  353  GLY   A O   1 
ATOM   2823  N  N   . SER   A 1 354  ? -25.97400  107.08000 21.86600  1.000 130.37509 ?  354  SER   A N   1 
ATOM   2824  C  CA  . SER   A 1 354  ? -27.30000  106.99700 21.27000  1.000 133.10918 ?  354  SER   A CA  1 
ATOM   2825  C  C   . SER   A 1 354  ? -28.31100  107.81300 22.06700  1.000 130.51006 ?  354  SER   A C   1 
ATOM   2826  O  O   . SER   A 1 354  ? -28.02300  108.94400 22.47500  1.000 120.56594 ?  354  SER   A O   1 
ATOM   2827  C  CB  . SER   A 1 354  ? -27.75000  105.53700 21.17800  1.000 125.83084 ?  354  SER   A CB  1 
ATOM   2828  O  OG  . SER   A 1 354  ? -27.78400  104.92800 22.45800  1.000 124.13576 ?  354  SER   A OG  1 
ATOM   2829  N  N   . THR   A 1 355  ? -29.49400  107.24300 22.28800  1.000 136.76087 ?  355  THR   A N   1 
ATOM   2830  C  CA  . THR   A 1 355  ? -30.53800  107.93400 23.03200  1.000 139.01991 ?  355  THR   A CA  1 
ATOM   2831  C  C   . THR   A 1 355  ? -30.07900  108.22500 24.45500  1.000 138.54721 ?  355  THR   A C   1 
ATOM   2832  O  O   . THR   A 1 355  ? -29.42900  107.39700 25.10100  1.000 145.72916 ?  355  THR   A O   1 
ATOM   2833  C  CB  . THR   A 1 355  ? -31.82100  107.09900 23.05200  1.000 144.40078 ?  355  THR   A CB  1 
ATOM   2834  O  OG1 . THR   A 1 355  ? -31.50000  105.73300 23.34100  1.000 151.49745 ?  355  THR   A OG1 1 
ATOM   2835  C  CG2 . THR   A 1 355  ? -32.53000  107.17700 21.70700  1.000 119.86662 ?  355  THR   A CG2 1 
ATOM   2836  N  N   . GLY   A 1 356  ? -30.42300  109.41100 24.94100  1.000 134.07729 ?  356  GLY   A N   1 
ATOM   2837  C  CA  . GLY   A 1 356  ? -29.95700  109.87900 26.22700  1.000 123.20347 ?  356  GLY   A CA  1 
ATOM   2838  C  C   . GLY   A 1 356  ? -28.53800  110.41800 26.16000  1.000 123.73768 ?  356  GLY   A C   1 
ATOM   2839  O  O   . GLY   A 1 356  ? -27.79200  110.19000 25.20900  1.000 128.71819 ?  356  GLY   A O   1 
ATOM   2840  N  N   . LEU   A 1 357  ? -28.16300  111.16000 27.20300  1.000 114.49519 ?  357  LEU   A N   1 
ATOM   2841  C  CA  . LEU   A 1 357  ? -26.80200  111.68300 27.27200  1.000 106.04989 ?  357  LEU   A CA  1 
ATOM   2842  C  C   . LEU   A 1 357  ? -25.80900  110.57000 27.59000  1.000 109.70466 ?  357  LEU   A C   1 
ATOM   2843  O  O   . LEU   A 1 357  ? -24.87000  110.32200 26.82600  1.000 137.29404 ?  357  LEU   A O   1 
ATOM   2844  C  CB  . LEU   A 1 357  ? -26.71900  112.80700 28.30500  1.000 87.59213  ?  357  LEU   A CB  1 
ATOM   2845  C  CG  . LEU   A 1 357  ? -25.58500  113.81600 28.09100  1.000 110.70769 ?  357  LEU   A CG  1 
ATOM   2846  C  CD1 . LEU   A 1 357  ? -24.35300  113.44500 28.90700  1.000 96.94416  ?  357  LEU   A CD1 1 
ATOM   2847  C  CD2 . LEU   A 1 357  ? -25.23200  113.95400 26.60800  1.000 105.12829 ?  357  LEU   A CD2 1 
ATOM   2848  N  N   . ALA   A 1 358  ? -26.00700  109.88900 28.71700  1.000 89.21157  ?  358  ALA   A N   1 
ATOM   2849  C  CA  . ALA   A 1 358  ? -25.19900  108.75600 29.14700  1.000 69.65195  ?  358  ALA   A CA  1 
ATOM   2850  C  C   . ALA   A 1 358  ? -25.83100  108.18700 30.40300  1.000 70.11637  ?  358  ALA   A C   1 
ATOM   2851  O  O   . ALA   A 1 358  ? -26.23000  108.94100 31.29200  1.000 82.97370  ?  358  ALA   A O   1 
ATOM   2852  C  CB  . ALA   A 1 358  ? -23.74500  109.15700 29.43400  1.000 65.97234  ?  358  ALA   A CB  1 
ATOM   2853  N  N   . LYS   A 1 359  ? -25.91800  106.86600 30.46900  1.000 57.02826  ?  359  LYS   A N   1 
ATOM   2854  C  CA  . LYS   A 1 359  ? -26.53800  106.18500 31.59400  1.000 60.91809  ?  359  LYS   A CA  1 
ATOM   2855  C  C   . LYS   A 1 359  ? -25.47900  105.44600 32.39800  1.000 59.28306  ?  359  LYS   A C   1 
ATOM   2856  O  O   . LYS   A 1 359  ? -24.59800  104.79200 31.83200  1.000 59.42696  ?  359  LYS   A O   1 
ATOM   2857  C  CB  . LYS   A 1 359  ? -27.61700  105.20500 31.12700  1.000 60.03961  ?  359  LYS   A CB  1 
ATOM   2858  C  CG  . LYS   A 1 359  ? -27.26100  104.42300 29.87200  1.000 77.32737  ?  359  LYS   A CG  1 
ATOM   2859  C  CD  . LYS   A 1 359  ? -28.50000  103.96600 29.11200  1.000 81.08679  ?  359  LYS   A CD  1 
ATOM   2860  C  CE  . LYS   A 1 359  ? -28.14200  103.55900 27.69100  1.000 95.32067  ?  359  LYS   A CE  1 
ATOM   2861  N  NZ  . LYS   A 1 359  ? -28.91600  102.37600 27.20900  1.000 83.97871  ?  359  LYS   A NZ  1 
ATOM   2862  N  N   . GLY   A 1 360  ? -25.57900  105.54900 33.72000  1.000 57.01964  ?  360  GLY   A N   1 
ATOM   2863  C  CA  . GLY   A 1 360  ? -24.64700  104.88700 34.60700  1.000 40.42941  ?  360  GLY   A CA  1 
ATOM   2864  C  C   . GLY   A 1 360  ? -25.06500  103.47800 34.97400  1.000 41.30599  ?  360  GLY   A C   1 
ATOM   2865  O  O   . GLY   A 1 360  ? -25.89600  103.28300 35.86600  1.000 47.56343  ?  360  GLY   A O   1 
ATOM   2866  N  N   . VAL   A 1 361  ? -24.49100  102.48700 34.29300  1.000 40.02646  ?  361  VAL   A N   1 
ATOM   2867  C  CA  . VAL   A 1 361  ? -24.75200  101.09200 34.62300  1.000 34.84735  ?  361  VAL   A CA  1 
ATOM   2868  C  C   . VAL   A 1 361  ? -23.99200  100.72800 35.88700  1.000 36.96698  ?  361  VAL   A C   1 
ATOM   2869  O  O   . VAL   A 1 361  ? -22.78000  100.95700 35.98700  1.000 37.04212  ?  361  VAL   A O   1 
ATOM   2870  C  CB  . VAL   A 1 361  ? -24.34000  100.17600 33.46400  1.000 39.40347  ?  361  VAL   A CB  1 
ATOM   2871  C  CG1 . VAL   A 1 361  ? -24.63200  98.72300  33.81500  1.000 38.11510  ?  361  VAL   A CG1 1 
ATOM   2872  C  CG2 . VAL   A 1 361  ? -25.04800  100.58600 32.19600  1.000 47.12899  ?  361  VAL   A CG2 1 
ATOM   2873  N  N   . MET   A 1 362  ? -24.68800  100.14800 36.85500  1.000 34.93073  ?  362  MET   A N   1 
ATOM   2874  C  CA  . MET   A 1 362  ? -24.06700  99.82100  38.12700  1.000 38.81405  ?  362  MET   A CA  1 
ATOM   2875  C  C   . MET   A 1 362  ? -23.94200  98.31100  38.24500  1.000 42.94176  ?  362  MET   A C   1 
ATOM   2876  O  O   . MET   A 1 362  ? -24.92400  97.58500  38.05700  1.000 46.83052  ?  362  MET   A O   1 
ATOM   2877  C  CB  . MET   A 1 362  ? -24.87000  100.38300 39.29800  1.000 41.58164  ?  362  MET   A CB  1 
ATOM   2878  C  CG  . MET   A 1 362  ? -25.17300  101.87500 39.18500  1.000 53.07719  ?  362  MET   A CG  1 
ATOM   2879  S  SD  . MET   A 1 362  ? -26.76900  102.24200 39.93900  1.000 61.46347  ?  362  MET   A SD  1 
ATOM   2880  C  CE  . MET   A 1 362  ? -26.89100  100.86900 41.09600  1.000 40.73430  ?  362  MET   A CE  1 
ATOM   2881  N  N   . ILE   A 1 363  ? -22.73600  97.84600  38.55100  1.000 36.45743  ?  363  ILE   A N   1 
ATOM   2882  C  CA  . ILE   A 1 363  ? -22.44100  96.43000  38.71000  1.000 35.15713  ?  363  ILE   A CA  1 
ATOM   2883  C  C   . ILE   A 1 363  ? -22.07300  96.18700  40.16700  1.000 38.38208  ?  363  ILE   A C   1 
ATOM   2884  O  O   . ILE   A 1 363  ? -21.45400  97.04500  40.80700  1.000 31.21397  ?  363  ILE   A O   1 
ATOM   2885  C  CB  . ILE   A 1 363  ? -21.31100  96.00700  37.75100  1.000 27.15977  ?  363  ILE   A CB  1 
ATOM   2886  C  CG1 . ILE   A 1 363  ? -21.74600  96.25100  36.30200  1.000 30.03365  ?  363  ILE   A CG1 1 
ATOM   2887  C  CG2 . ILE   A 1 363  ? -20.91700  94.56100  37.96800  1.000 32.44935  ?  363  ILE   A CG2 1 
ATOM   2888  C  CD1 . ILE   A 1 363  ? -22.78900  95.27700  35.79300  1.000 29.73198  ?  363  ILE   A CD1 1 
ATOM   2889  N  N   . GLU   A 1 364  ? -22.47900  95.03600  40.70000  1.000 35.89920  ?  364  GLU   A N   1 
ATOM   2890  C  CA  . GLU   A 1 364  ? -22.20400  94.67400  42.08300  1.000 37.44548  ?  364  GLU   A CA  1 
ATOM   2891  C  C   . GLU   A 1 364  ? -21.08100  93.64500  42.16100  1.000 49.65370  ?  364  GLU   A C   1 
ATOM   2892  O  O   . GLU   A 1 364  ? -20.58900  93.13800  41.15000  1.000 60.59246  ?  364  GLU   A O   1 
ATOM   2893  C  CB  . GLU   A 1 364  ? -23.46400  94.13500  42.76400  1.000 41.90961  ?  364  GLU   A CB  1 
ATOM   2894  C  CG  . GLU   A 1 364  ? -24.73500  94.84900  42.35900  1.000 42.19947  ?  364  GLU   A CG  1 
ATOM   2895  C  CD  . GLU   A 1 364  ? -25.95900  94.27000  43.03500  1.000 64.17126  ?  364  GLU   A CD  1 
ATOM   2896  O  OE1 . GLU   A 1 364  ? -26.14900  93.03600  42.97400  1.000 55.43198  ?  364  GLU   A OE1 1 
ATOM   2897  O  OE2 . GLU   A 1 364  ? -26.73100  95.04800  43.63800  1.000 57.74663  -1 364  GLU   A OE2 1 
ATOM   2898  N  N   . HIS   A 1 365  ? -20.68700  93.32900  43.39800  1.000 48.43267  ?  365  HIS   A N   1 
ATOM   2899  C  CA  . HIS   A 1 365  ? -19.53700  92.45700  43.61900  1.000 39.75160  ?  365  HIS   A CA  1 
ATOM   2900  C  C   . HIS   A 1 365  ? -19.83200  91.02600  43.18600  1.000 45.61733  ?  365  HIS   A C   1 
ATOM   2901  O  O   . HIS   A 1 365  ? -19.00500  90.38700  42.52300  1.000 51.18492  ?  365  HIS   A O   1 
ATOM   2902  C  CB  . HIS   A 1 365  ? -19.12100  92.50300  45.08900  1.000 37.88169  ?  365  HIS   A CB  1 
ATOM   2903  C  CG  . HIS   A 1 365  ? -18.16900  93.61200  45.41200  1.000 44.34344  ?  365  HIS   A CG  1 
ATOM   2904  N  ND1 . HIS   A 1 365  ? -16.80000  93.45600  45.36500  1.000 38.22259  ?  365  HIS   A ND1 1 
ATOM   2905  C  CD2 . HIS   A 1 365  ? -18.38900  94.89700  45.77900  1.000 45.53743  ?  365  HIS   A CD2 1 
ATOM   2906  C  CE1 . HIS   A 1 365  ? -16.21800  94.59600  45.69400  1.000 46.26621  ?  365  HIS   A CE1 1 
ATOM   2907  N  NE2 . HIS   A 1 365  ? -17.16000  95.48600  45.94900  1.000 41.52343  ?  365  HIS   A NE2 1 
ATOM   2908  N  N   . HIS   A 1 366  ? -21.00400  90.49900  43.55800  1.000 37.51244  ?  366  HIS   A N   1 
ATOM   2909  C  CA  . HIS   A 1 366  ? -21.35700  89.13800  43.16500  1.000 42.03422  ?  366  HIS   A CA  1 
ATOM   2910  C  C   . HIS   A 1 366  ? -21.40400  88.99400  41.65100  1.000 39.27252  ?  366  HIS   A C   1 
ATOM   2911  O  O   . HIS   A 1 366  ? -21.18900  87.89700  41.12200  1.000 35.38905  ?  366  HIS   A O   1 
ATOM   2912  C  CB  . HIS   A 1 366  ? -22.70300  88.74400  43.77300  1.000 46.21117  ?  366  HIS   A CB  1 
ATOM   2913  C  CG  . HIS   A 1 366  ? -23.87300  89.38900  43.10000  1.000 50.96356  ?  366  HIS   A CG  1 
ATOM   2914  N  ND1 . HIS   A 1 366  ? -24.67700  88.72100  42.20200  1.000 41.52633  ?  366  HIS   A ND1 1 
ATOM   2915  C  CD2 . HIS   A 1 366  ? -24.35900  90.65100  43.17500  1.000 46.82593  ?  366  HIS   A CD2 1 
ATOM   2916  C  CE1 . HIS   A 1 366  ? -25.61500  89.54000  41.76100  1.000 48.54312  ?  366  HIS   A CE1 1 
ATOM   2917  N  NE2 . HIS   A 1 366  ? -25.44400  90.71700  42.33600  1.000 42.73333  ?  366  HIS   A NE2 1 
ATOM   2918  N  N   . ASN   A 1 367  ? -21.68100  90.09000  40.94100  1.000 30.48518  ?  367  ASN   A N   1 
ATOM   2919  C  CA  . ASN   A 1 367  ? -21.65400  90.06000  39.48500  1.000 35.51638  ?  367  ASN   A CA  1 
ATOM   2920  C  C   . ASN   A 1 367  ? -20.24300  89.80600  38.97200  1.000 38.90092  ?  367  ASN   A C   1 
ATOM   2921  O  O   . ASN   A 1 367  ? -20.01500  88.89000  38.17200  1.000 38.83014  ?  367  ASN   A O   1 
ATOM   2922  C  CB  . ASN   A 1 367  ? -22.19500  91.37500  38.92300  1.000 39.49345  ?  367  ASN   A CB  1 
ATOM   2923  C  CG  . ASN   A 1 367  ? -23.63200  91.63400  39.31200  1.000 35.74547  ?  367  ASN   A CG  1 
ATOM   2924  O  OD1 . ASN   A 1 367  ? -23.95900  92.69200  39.84500  1.000 41.64724  ?  367  ASN   A OD1 1 
ATOM   2925  N  ND2 . ASN   A 1 367  ? -24.49800  90.66000  39.06300  1.000 36.57990  ?  367  ASN   A ND2 1 
ATOM   2926  N  N   . LEU   A 1 368  ? -19.28200  90.61500  39.42500  1.000 40.93160  ?  368  LEU   A N   1 
ATOM   2927  C  CA  . LEU   A 1 368  ? -17.90100  90.48000  38.97200  1.000 31.69729  ?  368  LEU   A CA  1 
ATOM   2928  C  C   . LEU   A 1 368  ? -17.28800  89.16200  39.43000  1.000 37.94278  ?  368  LEU   A C   1 
ATOM   2929  O  O   . LEU   A 1 368  ? -16.58300  88.50000  38.65800  1.000 39.60139  ?  368  LEU   A O   1 
ATOM   2930  C  CB  . LEU   A 1 368  ? -17.07700  91.66100  39.48100  1.000 30.96207  ?  368  LEU   A CB  1 
ATOM   2931  C  CG  . LEU   A 1 368  ? -15.61600  91.73500  39.04200  1.000 42.43345  ?  368  LEU   A CG  1 
ATOM   2932  C  CD1 . LEU   A 1 368  ? -15.52300  92.09400  37.57000  1.000 33.45762  ?  368  LEU   A CD1 1 
ATOM   2933  C  CD2 . LEU   A 1 368  ? -14.85400  92.74000  39.89500  1.000 28.22857  ?  368  LEU   A CD2 1 
ATOM   2934  N  N   . VAL   A 1 369  ? -17.54000  88.77100  40.68200  1.000 33.18571  ?  369  VAL   A N   1 
ATOM   2935  C  CA  . VAL   A 1 369  ? -16.96700  87.53500  41.21400  1.000 38.20471  ?  369  VAL   A CA  1 
ATOM   2936  C  C   . VAL   A 1 369  ? -17.41300  86.33900  40.38200  1.000 37.72362  ?  369  VAL   A C   1 
ATOM   2937  O  O   . VAL   A 1 369  ? -16.60700  85.46900  40.02900  1.000 38.47726  ?  369  VAL   A O   1 
ATOM   2938  C  CB  . VAL   A 1 369  ? -17.34700  87.36400  42.69700  1.000 35.04378  ?  369  VAL   A CB  1 
ATOM   2939  C  CG1 . VAL   A 1 369  ? -17.05400  85.94600  43.16200  1.000 37.81249  ?  369  VAL   A CG1 1 
ATOM   2940  C  CG2 . VAL   A 1 369  ? -16.59800  88.37200  43.55800  1.000 33.71796  ?  369  VAL   A CG2 1 
ATOM   2941  N  N   . ASN   A 1 370  ? -18.70500  86.28200  40.05200  1.000 47.19583  ?  370  ASN   A N   1 
ATOM   2942  C  CA  . ASN   A 1 370  ? -19.21200  85.18300  39.23700  1.000 48.14463  ?  370  ASN   A CA  1 
ATOM   2943  C  C   . ASN   A 1 370  ? -18.50200  85.10700  37.89100  1.000 39.65385  ?  370  ASN   A C   1 
ATOM   2944  O  O   . ASN   A 1 370  ? -18.29500  84.01100  37.36000  1.000 47.60120  ?  370  ASN   A O   1 
ATOM   2945  C  CB  . ASN   A 1 370  ? -20.71800  85.33500  39.03800  1.000 38.25012  ?  370  ASN   A CB  1 
ATOM   2946  C  CG  . ASN   A 1 370  ? -21.28100  84.30800  38.08800  1.000 32.20779  ?  370  ASN   A CG  1 
ATOM   2947  O  OD1 . ASN   A 1 370  ? -21.36700  83.12500  38.41500  1.000 37.74529  ?  370  ASN   A OD1 1 
ATOM   2948  N  ND2 . ASN   A 1 370  ? -21.66100  84.75200  36.89700  1.000 33.31788  ?  370  ASN   A ND2 1 
ATOM   2949  N  N   . PHE   A 1 371  ? -18.11600  86.25400  37.33000  1.000 29.69928  ?  371  PHE   A N   1 
ATOM   2950  C  CA  . PHE   A 1 371  ? -17.38800  86.23900  36.06700  1.000 35.89667  ?  371  PHE   A CA  1 
ATOM   2951  C  C   . PHE   A 1 371  ? -15.94500  85.80400  36.27600  1.000 40.60207  ?  371  PHE   A C   1 
ATOM   2952  O  O   . PHE   A 1 371  ? -15.44000  84.92500  35.56700  1.000 38.94404  ?  371  PHE   A O   1 
ATOM   2953  C  CB  . PHE   A 1 371  ? -17.44600  87.61600  35.40700  1.000 33.81040  ?  371  PHE   A CB  1 
ATOM   2954  C  CG  . PHE   A 1 371  ? -16.99400  87.61800  33.97500  1.000 45.71529  ?  371  PHE   A CG  1 
ATOM   2955  C  CD1 . PHE   A 1 371  ? -17.88500  87.34300  32.95100  1.000 47.24067  ?  371  PHE   A CD1 1 
ATOM   2956  C  CD2 . PHE   A 1 371  ? -15.67600  87.89800  33.65100  1.000 43.85490  ?  371  PHE   A CD2 1 
ATOM   2957  C  CE1 . PHE   A 1 371  ? -17.46900  87.34500  31.63100  1.000 46.73180  ?  371  PHE   A CE1 1 
ATOM   2958  C  CE2 . PHE   A 1 371  ? -15.25400  87.90300  32.33300  1.000 36.60799  ?  371  PHE   A CE2 1 
ATOM   2959  C  CZ  . PHE   A 1 371  ? -16.15300  87.62600  31.32300  1.000 36.01780  ?  371  PHE   A CZ  1 
ATOM   2960  N  N   . CYS   A 1 372  ? -15.26700  86.40800  37.25500  1.000 32.16667  ?  372  CYS   A N   1 
ATOM   2961  C  CA  . CYS   A 1 372  ? -13.86700  86.08600  37.50000  1.000 28.15752  ?  372  CYS   A CA  1 
ATOM   2962  C  C   . CYS   A 1 372  ? -13.68500  84.63200  37.91700  1.000 38.57478  ?  372  CYS   A C   1 
ATOM   2963  O  O   . CYS   A 1 372  ? -12.67000  84.01300  37.57700  1.000 52.19941  ?  372  CYS   A O   1 
ATOM   2964  C  CB  . CYS   A 1 372  ? -13.29600  87.02100  38.56400  1.000 28.21907  ?  372  CYS   A CB  1 
ATOM   2965  S  SG  . CYS   A 1 372  ? -13.21200  88.75600  38.06100  1.000 38.96080  ?  372  CYS   A SG  1 
ATOM   2966  N  N   . GLU   A 1 373  ? -14.64700  84.07100  38.64900  1.000 38.54001  ?  373  GLU   A N   1 
ATOM   2967  C  CA  . GLU   A 1 373  ? -14.55700  82.67800  39.06400  1.000 32.86305  ?  373  GLU   A CA  1 
ATOM   2968  C  C   . GLU   A 1 373  ? -14.94600  81.70900  37.95900  1.000 34.62858  ?  373  GLU   A C   1 
ATOM   2969  O  O   . GLU   A 1 373  ? -14.68300  80.50800  38.09000  1.000 33.32994  ?  373  GLU   A O   1 
ATOM   2970  C  CB  . GLU   A 1 373  ? -15.42700  82.44100  40.29900  1.000 36.50483  ?  373  GLU   A CB  1 
ATOM   2971  C  CG  . GLU   A 1 373  ? -14.87300  83.09100  41.55000  1.000 41.06189  ?  373  GLU   A CG  1 
ATOM   2972  C  CD  . GLU   A 1 373  ? -13.62600  82.39400  42.05300  1.000 62.69469  ?  373  GLU   A CD  1 
ATOM   2973  O  OE1 . GLU   A 1 373  ? -13.64100  81.14800  42.15300  1.000 74.92407  ?  373  GLU   A OE1 1 
ATOM   2974  O  OE2 . GLU   A 1 373  ? -12.62700  83.08800  42.33900  1.000 67.03295  -1 373  GLU   A OE2 1 
ATOM   2975  N  N   . TRP   A 1 374  ? -15.57600  82.19600  36.89000  1.000 38.51625  ?  374  TRP   A N   1 
ATOM   2976  C  CA  . TRP   A 1 374  ? -15.77200  81.40100  35.68700  1.000 28.29846  ?  374  TRP   A CA  1 
ATOM   2977  C  C   . TRP   A 1 374  ? -14.61200  81.55800  34.71500  1.000 37.41321  ?  374  TRP   A C   1 
ATOM   2978  O  O   . TRP   A 1 374  ? -14.26200  80.60300  34.01400  1.000 29.11477  ?  374  TRP   A O   1 
ATOM   2979  C  CB  . TRP   A 1 374  ? -17.08600  81.79200  34.99300  1.000 28.68843  ?  374  TRP   A CB  1 
ATOM   2980  C  CG  . TRP   A 1 374  ? -17.14300  81.36100  33.55100  1.000 32.91506  ?  374  TRP   A CG  1 
ATOM   2981  C  CD1 . TRP   A 1 374  ? -17.56300  80.15100  33.07200  1.000 27.85524  ?  374  TRP   A CD1 1 
ATOM   2982  C  CD2 . TRP   A 1 374  ? -16.74200  82.12600  32.40800  1.000 32.97431  ?  374  TRP   A CD2 1 
ATOM   2983  N  NE1 . TRP   A 1 374  ? -17.45200  80.12100  31.70200  1.000 33.35877  ?  374  TRP   A NE1 1 
ATOM   2984  C  CE2 . TRP   A 1 374  ? -16.95000  81.32000  31.27000  1.000 31.43120  ?  374  TRP   A CE2 1 
ATOM   2985  C  CE3 . TRP   A 1 374  ? -16.22600  83.41400  32.23700  1.000 45.73155  ?  374  TRP   A CE3 1 
ATOM   2986  C  CZ2 . TRP   A 1 374  ? -16.66300  81.76200  29.97900  1.000 22.12704  ?  374  TRP   A CZ2 1 
ATOM   2987  C  CZ3 . TRP   A 1 374  ? -15.94400  83.85200  30.95500  1.000 37.17363  ?  374  TRP   A CZ3 1 
ATOM   2988  C  CH2 . TRP   A 1 374  ? -16.16400  83.02900  29.84400  1.000 33.32301  ?  374  TRP   A CH2 1 
ATOM   2989  N  N   . TYR   A 1 375  ? -13.99300  82.74100  34.68900  1.000 41.51820  ?  375  TYR   A N   1 
ATOM   2990  C  CA  . TYR   A 1 375  ? -12.93000  83.02300  33.73000  1.000 37.16114  ?  375  TYR   A CA  1 
ATOM   2991  C  C   . TYR   A 1 375  ? -11.70300  82.15200  33.98000  1.000 37.72922  ?  375  TYR   A C   1 
ATOM   2992  O  O   . TYR   A 1 375  ? -11.15000  81.56200  33.04300  1.000 39.19170  ?  375  TYR   A O   1 
ATOM   2993  C  CB  . TYR   A 1 375  ? -12.56600  84.50500  33.80300  1.000 38.93650  ?  375  TYR   A CB  1 
ATOM   2994  C  CG  . TYR   A 1 375  ? -11.63600  84.99700  32.72000  1.000 45.54942  ?  375  TYR   A CG  1 
ATOM   2995  C  CD1 . TYR   A 1 375  ? -10.26100  84.83300  32.82900  1.000 38.81305  ?  375  TYR   A CD1 1 
ATOM   2996  C  CD2 . TYR   A 1 375  ? -12.13100  85.65500  31.60400  1.000 43.33409  ?  375  TYR   A CD2 1 
ATOM   2997  C  CE1 . TYR   A 1 375  ? -9.41000   85.29500  31.85200  1.000 45.09035  ?  375  TYR   A CE1 1 
ATOM   2998  C  CE2 . TYR   A 1 375  ? -11.28700  86.12200  30.62000  1.000 40.96622  ?  375  TYR   A CE2 1 
ATOM   2999  C  CZ  . TYR   A 1 375  ? -9.92800   85.93900  30.74900  1.000 42.07196  ?  375  TYR   A CZ  1 
ATOM   3000  O  OH  . TYR   A 1 375  ? -9.08200   86.40300  29.77200  1.000 38.49490  ?  375  TYR   A OH  1 
ATOM   3001  N  N   . ARG   A 1 376  ? -11.25600  82.06600  35.23500  1.000 30.76809  ?  376  ARG   A N   1 
ATOM   3002  C  CA  . ARG   A 1 376  ? -10.01200  81.35600  35.53000  1.000 36.20136  ?  376  ARG   A CA  1 
ATOM   3003  C  C   . ARG   A 1 376  ? -10.06400  79.88000  35.15200  1.000 35.04462  ?  376  ARG   A C   1 
ATOM   3004  O  O   . ARG   A 1 376  ? -9.17600   79.42900  34.40600  1.000 36.55492  ?  376  ARG   A O   1 
ATOM   3005  C  CB  . ARG   A 1 376  ? -9.64200   81.54800  37.00600  1.000 35.90290  ?  376  ARG   A CB  1 
ATOM   3006  C  CG  . ARG   A 1 376  ? -8.40900   80.77300  37.45200  1.000 40.40462  ?  376  ARG   A CG  1 
ATOM   3007  C  CD  . ARG   A 1 376  ? -8.31600   80.70300  38.97200  1.000 43.47908  ?  376  ARG   A CD  1 
ATOM   3008  N  NE  . ARG   A 1 376  ? -8.93300   81.86100  39.61100  1.000 64.35303  ?  376  ARG   A NE  1 
ATOM   3009  C  CZ  . ARG   A 1 376  ? -9.96200   81.80200  40.44600  1.000 61.42896  ?  376  ARG   A CZ  1 
ATOM   3010  N  NH1 . ARG   A 1 376  ? -10.51100  80.64800  40.78800  1.000 49.89635  ?  376  ARG   A NH1 1 
ATOM   3011  N  NH2 . ARG   A 1 376  ? -10.45200  82.93100  40.95200  1.000 55.54804  ?  376  ARG   A NH2 1 
ATOM   3012  N  N   . PRO   A 1 377  ? -11.03800  79.07800  35.60100  1.000 36.29406  ?  377  PRO   A N   1 
ATOM   3013  C  CA  . PRO   A 1 377  ? -11.02200  77.65600  35.22400  1.000 30.62751  ?  377  PRO   A CA  1 
ATOM   3014  C  C   . PRO   A 1 377  ? -11.38300  77.41100  33.77100  1.000 26.15839  ?  377  PRO   A C   1 
ATOM   3015  O  O   . PRO   A 1 377  ? -10.98900  76.37500  33.22200  1.000 44.62250  ?  377  PRO   A O   1 
ATOM   3016  C  CB  . PRO   A 1 377  ? -12.05500  77.03000  36.16800  1.000 24.44164  ?  377  PRO   A CB  1 
ATOM   3017  C  CG  . PRO   A 1 377  ? -13.00600  78.13400  36.44300  1.000 37.89291  ?  377  PRO   A CG  1 
ATOM   3018  C  CD  . PRO   A 1 377  ? -12.18100  79.38900  36.48100  1.000 30.98161  ?  377  PRO   A CD  1 
ATOM   3019  N  N   . TYR   A 1 378  ? -12.11100  78.32400  33.12900  1.000 32.32420  ?  378  TYR   A N   1 
ATOM   3020  C  CA  . TYR   A 1 378  ? -12.50900  78.10700  31.74100  1.000 34.95045  ?  378  TYR   A CA  1 
ATOM   3021  C  C   . TYR   A 1 378  ? -11.31800  78.21400  30.80100  1.000 37.19048  ?  378  TYR   A C   1 
ATOM   3022  O  O   . TYR   A 1 378  ? -11.19500  77.42800  29.85500  1.000 39.38177  ?  378  TYR   A O   1 
ATOM   3023  C  CB  . TYR   A 1 378  ? -13.59500  79.10900  31.35200  1.000 35.96045  ?  378  TYR   A CB  1 
ATOM   3024  C  CG  . TYR   A 1 378  ? -14.18600  78.91800  29.97100  1.000 44.97555  ?  378  TYR   A CG  1 
ATOM   3025  C  CD1 . TYR   A 1 378  ? -15.29000  78.10000  29.77400  1.000 32.70566  ?  378  TYR   A CD1 1 
ATOM   3026  C  CD2 . TYR   A 1 378  ? -13.65700  79.58200  28.87100  1.000 49.31433  ?  378  TYR   A CD2 1 
ATOM   3027  C  CE1 . TYR   A 1 378  ? -15.84100  77.93600  28.51800  1.000 24.08275  ?  378  TYR   A CE1 1 
ATOM   3028  C  CE2 . TYR   A 1 378  ? -14.20200  79.42400  27.61100  1.000 36.15247  ?  378  TYR   A CE2 1 
ATOM   3029  C  CZ  . TYR   A 1 378  ? -15.29200  78.60000  27.44200  1.000 32.41263  ?  378  TYR   A CZ  1 
ATOM   3030  O  OH  . TYR   A 1 378  ? -15.83600  78.44100  26.19000  1.000 39.75879  ?  378  TYR   A OH  1 
ATOM   3031  N  N   . PHE   A 1 379  ? -10.43700  79.18400  31.04200  1.000 43.89133  ?  379  PHE   A N   1 
ATOM   3032  C  CA  . PHE   A 1 379  ? -9.26200   79.41100  30.21500  1.000 33.16524  ?  379  PHE   A CA  1 
ATOM   3033  C  C   . PHE   A 1 379  ? -7.98600   78.87000  30.84200  1.000 34.50795  ?  379  PHE   A C   1 
ATOM   3034  O  O   . PHE   A 1 379  ? -6.91400   79.00400  30.24400  1.000 41.62252  ?  379  PHE   A O   1 
ATOM   3035  C  CB  . PHE   A 1 379  ? -9.09900   80.90800  29.93300  1.000 33.55840  ?  379  PHE   A CB  1 
ATOM   3036  C  CG  . PHE   A 1 379  ? -10.13800  81.46800  29.00400  1.000 49.90481  ?  379  PHE   A CG  1 
ATOM   3037  C  CD1 . PHE   A 1 379  ? -10.39300  80.86500  27.78400  1.000 39.97199  ?  379  PHE   A CD1 1 
ATOM   3038  C  CD2 . PHE   A 1 379  ? -10.86800  82.59300  29.35600  1.000 56.41181  ?  379  PHE   A CD2 1 
ATOM   3039  C  CE1 . PHE   A 1 379  ? -11.34900  81.37900  26.92900  1.000 45.98106  ?  379  PHE   A CE1 1 
ATOM   3040  C  CE2 . PHE   A 1 379  ? -11.82800  83.11000  28.50600  1.000 36.64669  ?  379  PHE   A CE2 1 
ATOM   3041  C  CZ  . PHE   A 1 379  ? -12.06900  82.50300  27.29300  1.000 44.71374  ?  379  PHE   A CZ  1 
ATOM   3042  N  N   . GLY   A 1 380  ? -8.07400   78.27100  32.02500  1.000 34.02086  ?  380  GLY   A N   1 
ATOM   3043  C  CA  . GLY   A 1 380  ? -6.89200   77.73300  32.68000  1.000 31.31308  ?  380  GLY   A CA  1 
ATOM   3044  C  C   . GLY   A 1 380  ? -5.86900   78.78400  33.05000  1.000 33.18705  ?  380  GLY   A C   1 
ATOM   3045  O  O   . GLY   A 1 380  ? -4.66300   78.56000  32.88300  1.000 49.06557  ?  380  GLY   A O   1 
ATOM   3046  N  N   . VAL   A 1 381  ? -6.32200   79.93200  33.54800  1.000 28.10816  ?  381  VAL   A N   1 
ATOM   3047  C  CA  . VAL   A 1 381  ? -5.40000   80.99600  33.92000  1.000 36.85931  ?  381  VAL   A CA  1 
ATOM   3048  C  C   . VAL   A 1 381  ? -4.60700   80.57100  35.14800  1.000 43.53543  ?  381  VAL   A C   1 
ATOM   3049  O  O   . VAL   A 1 381  ? -5.17500   80.13400  36.15800  1.000 40.98729  ?  381  VAL   A O   1 
ATOM   3050  C  CB  . VAL   A 1 381  ? -6.16000   82.30500  34.16600  1.000 26.99928  ?  381  VAL   A CB  1 
ATOM   3051  C  CG1 . VAL   A 1 381  ? -5.20200   83.48300  34.14200  1.000 31.08416  ?  381  VAL   A CG1 1 
ATOM   3052  C  CG2 . VAL   A 1 381  ? -7.24500   82.47100  33.12000  1.000 26.40302  ?  381  VAL   A CG2 1 
ATOM   3053  N  N   . THR   A 1 382  ? -3.29200   80.68700  35.05900  1.000 44.02624  ?  382  THR   A N   1 
ATOM   3054  C  CA  . THR   A 1 382  ? -2.35700   80.30100  36.10500  1.000 36.01137  ?  382  THR   A CA  1 
ATOM   3055  C  C   . THR   A 1 382  ? -1.47700   81.49000  36.43200  1.000 36.69601  ?  382  THR   A C   1 
ATOM   3056  O  O   . THR   A 1 382  ? -1.45200   82.47700  35.69000  1.000 37.26138  ?  382  THR   A O   1 
ATOM   3057  C  CB  . THR   A 1 382  ? -1.49600   79.11500  35.64100  1.000 34.64640  ?  382  THR   A CB  1 
ATOM   3058  O  OG1 . THR   A 1 382  ? -0.91500   79.42100  34.36700  1.000 57.04358  ?  382  THR   A OG1 1 
ATOM   3059  C  CG2 . THR   A 1 382  ? -2.34000   77.86300  35.52500  1.000 31.21773  ?  382  THR   A CG2 1 
ATOM   3060  N  N   . PRO   A 1 383  ? -0.73200   81.43800  37.54200  1.000 41.25743  ?  383  PRO   A N   1 
ATOM   3061  C  CA  . PRO   A 1 383  ? 0.22300    82.52100  37.82300  1.000 32.99135  ?  383  PRO   A CA  1 
ATOM   3062  C  C   . PRO   A 1 383  ? 1.32700    82.64100  36.78400  1.000 37.73881  ?  383  PRO   A C   1 
ATOM   3063  O  O   . PRO   A 1 383  ? 2.12000    83.58900  36.85600  1.000 46.98748  ?  383  PRO   A O   1 
ATOM   3064  C  CB  . PRO   A 1 383  ? 0.78900    82.14600  39.20000  1.000 32.46028  ?  383  PRO   A CB  1 
ATOM   3065  C  CG  . PRO   A 1 383  ? -0.24400   81.28700  39.81200  1.000 35.77356  ?  383  PRO   A CG  1 
ATOM   3066  C  CD  . PRO   A 1 383  ? -0.84700   80.51000  38.68100  1.000 41.38767  ?  383  PRO   A CD  1 
ATOM   3067  N  N   . ALA   A 1 384  ? 1.40700    81.71300  35.82900  1.000 40.41743  ?  384  ALA   A N   1 
ATOM   3068  C  CA  . ALA   A 1 384  ? 2.39300    81.76700  34.75900  1.000 39.87973  ?  384  ALA   A CA  1 
ATOM   3069  C  C   . ALA   A 1 384  ? 1.94600    82.61300  33.57500  1.000 41.33692  ?  384  ALA   A C   1 
ATOM   3070  O  O   . ALA   A 1 384  ? 2.75700    82.88000  32.68200  1.000 40.52209  ?  384  ALA   A O   1 
ATOM   3071  C  CB  . ALA   A 1 384  ? 2.72400    80.35000  34.27400  1.000 40.04987  ?  384  ALA   A CB  1 
ATOM   3072  N  N   . ASP   A 1 385  ? 0.68800    83.04100  33.54600  1.000 39.97363  ?  385  ASP   A N   1 
ATOM   3073  C  CA  . ASP   A 1 385  ? 0.16800    83.80800  32.42800  1.000 37.57789  ?  385  ASP   A CA  1 
ATOM   3074  C  C   . ASP   A 1 385  ? 0.55300    85.28100  32.54900  1.000 38.20658  ?  385  ASP   A C   1 
ATOM   3075  O  O   . ASP   A 1 385  ? 0.93000    85.77200  33.61600  1.000 40.41134  ?  385  ASP   A O   1 
ATOM   3076  C  CB  . ASP   A 1 385  ? -1.35300   83.67000  32.34500  1.000 37.60838  ?  385  ASP   A CB  1 
ATOM   3077  C  CG  . ASP   A 1 385  ? -1.78900   82.36200  31.71200  1.000 44.41255  ?  385  ASP   A CG  1 
ATOM   3078  O  OD1 . ASP   A 1 385  ? -1.60700   82.20300  30.48500  1.000 40.47678  ?  385  ASP   A OD1 1 
ATOM   3079  O  OD2 . ASP   A 1 385  ? -2.31700   81.49300  32.43900  1.000 42.99148  -1 385  ASP   A OD2 1 
ATOM   3080  N  N   . LYS   A 1 386  ? 0.45700    85.98300  31.42200  1.000 37.63387  ?  386  LYS   A N   1 
ATOM   3081  C  CA  . LYS   A 1 386  ? 0.66300    87.42400  31.36500  1.000 35.24983  ?  386  LYS   A CA  1 
ATOM   3082  C  C   . LYS   A 1 386  ? -0.43700   88.01400  30.49800  1.000 37.52491  ?  386  LYS   A C   1 
ATOM   3083  O  O   . LYS   A 1 386  ? -0.71100   87.49700  29.41100  1.000 37.22750  ?  386  LYS   A O   1 
ATOM   3084  C  CB  . LYS   A 1 386  ? 2.04100    87.77700  30.79100  1.000 41.81050  ?  386  LYS   A CB  1 
ATOM   3085  C  CG  . LYS   A 1 386  ? 3.19600    87.56900  31.75900  1.000 38.50033  ?  386  LYS   A CG  1 
ATOM   3086  C  CD  . LYS   A 1 386  ? 4.38000    86.90200  31.07300  1.000 39.73146  ?  386  LYS   A CD  1 
ATOM   3087  C  CE  . LYS   A 1 386  ? 5.70000    87.31800  31.70500  1.000 42.96315  ?  386  LYS   A CE  1 
ATOM   3088  N  NZ  . LYS   A 1 386  ? 6.10900    88.69400  31.30800  1.000 59.11321  ?  386  LYS   A NZ  1 
ATOM   3089  N  N   . ALA   A 1 387  ? -1.06700   89.08400  30.97700  1.000 40.58000  ?  387  ALA   A N   1 
ATOM   3090  C  CA  . ALA   A 1 387  ? -2.22600   89.66000  30.31400  1.000 30.35067  ?  387  ALA   A CA  1 
ATOM   3091  C  C   . ALA   A 1 387  ? -1.99700   91.13400  30.01000  1.000 31.57984  ?  387  ALA   A C   1 
ATOM   3092  O  O   . ALA   A 1 387  ? -1.14100   91.79400  30.60600  1.000 56.01551  ?  387  ALA   A O   1 
ATOM   3093  C  CB  . ALA   A 1 387  ? -3.49400   89.49600  31.16300  1.000 30.52051  ?  387  ALA   A CB  1 
ATOM   3094  N  N   . LEU   A 1 388  ? -2.80100   91.64500  29.08300  1.000 29.13755  ?  388  LEU   A N   1 
ATOM   3095  C  CA  . LEU   A 1 388  ? -2.67400   92.99700  28.56000  1.000 23.81371  ?  388  LEU   A CA  1 
ATOM   3096  C  C   . LEU   A 1 388  ? -3.85400   93.83400  29.03900  1.000 37.19526  ?  388  LEU   A C   1 
ATOM   3097  O  O   . LEU   A 1 388  ? -5.01100   93.44500  28.84800  1.000 42.05350  ?  388  LEU   A O   1 
ATOM   3098  C  CB  . LEU   A 1 388  ? -2.63100   92.95900  27.03100  1.000 31.09489  ?  388  LEU   A CB  1 
ATOM   3099  C  CG  . LEU   A 1 388  ? -1.68000   93.84100  26.23300  1.000 45.19872  ?  388  LEU   A CG  1 
ATOM   3100  C  CD1 . LEU   A 1 388  ? -0.25300   93.32900  26.33000  1.000 46.99414  ?  388  LEU   A CD1 1 
ATOM   3101  C  CD2 . LEU   A 1 388  ? -2.13200   93.90000  24.78900  1.000 37.78862  ?  388  LEU   A CD2 1 
ATOM   3102  N  N   . VAL   A 1 389  ? -3.56600   94.97100  29.67200  1.000 37.47675  ?  389  VAL   A N   1 
ATOM   3103  C  CA  . VAL   A 1 389  ? -4.60400   95.93900  30.04700  1.000 24.30146  ?  389  VAL   A CA  1 
ATOM   3104  C  C   . VAL   A 1 389  ? -4.76000   96.86900  28.84700  1.000 38.29644  ?  389  VAL   A C   1 
ATOM   3105  O  O   . VAL   A 1 389  ? -4.14300   97.93300  28.76600  1.000 43.98103  ?  389  VAL   A O   1 
ATOM   3106  C  CB  . VAL   A 1 389  ? -4.25900   96.68500  31.33600  1.000 22.53676  ?  389  VAL   A CB  1 
ATOM   3107  C  CG1 . VAL   A 1 389  ? -5.34400   97.69100  31.69100  1.000 23.25407  ?  389  VAL   A CG1 1 
ATOM   3108  C  CG2 . VAL   A 1 389  ? -4.08700   95.69700  32.47700  1.000 32.83951  ?  389  VAL   A CG2 1 
ATOM   3109  N  N   . TYR   A 1 390  ? -5.60000   96.45400  27.89700  1.000 35.19482  ?  390  TYR   A N   1 
ATOM   3110  C  CA  . TYR   A 1 390  ? -5.74500   97.12200  26.60800  1.000 40.36145  ?  390  TYR   A CA  1 
ATOM   3111  C  C   . TYR   A 1 390  ? -6.90500   98.11300  26.57300  1.000 50.69212  ?  390  TYR   A C   1 
ATOM   3112  O  O   . TYR   A 1 390  ? -6.72400   99.26500  26.16600  1.000 50.88260  ?  390  TYR   A O   1 
ATOM   3113  C  CB  . TYR   A 1 390  ? -5.92000   96.07000  25.50600  1.000 42.14769  ?  390  TYR   A CB  1 
ATOM   3114  C  CG  . TYR   A 1 390  ? -6.05200   96.63700  24.11300  1.000 44.23938  ?  390  TYR   A CG  1 
ATOM   3115  C  CD1 . TYR   A 1 390  ? -4.93300   97.04500  23.40100  1.000 44.67498  ?  390  TYR   A CD1 1 
ATOM   3116  C  CD2 . TYR   A 1 390  ? -7.29400   96.75600  23.50700  1.000 42.09592  ?  390  TYR   A CD2 1 
ATOM   3117  C  CE1 . TYR   A 1 390  ? -5.04900   97.55900  22.12800  1.000 56.02243  ?  390  TYR   A CE1 1 
ATOM   3118  C  CE2 . TYR   A 1 390  ? -7.42000   97.27000  22.23600  1.000 52.35399  ?  390  TYR   A CE2 1 
ATOM   3119  C  CZ  . TYR   A 1 390  ? -6.29600   97.67000  21.55100  1.000 46.95678  ?  390  TYR   A CZ  1 
ATOM   3120  O  OH  . TYR   A 1 390  ? -6.42200   98.18300  20.28200  1.000 58.04903  ?  390  TYR   A OH  1 
ATOM   3121  N  N   . SER   A 1 391  ? -8.09400   97.68800  26.98900  1.000 50.49905  ?  391  SER   A N   1 
ATOM   3122  C  CA  . SER   A 1 391  ? -9.27200   98.53900  26.89900  1.000 50.04099  ?  391  SER   A CA  1 
ATOM   3123  C  C   . SER   A 1 391  ? -9.14900   99.74000  27.83000  1.000 46.37239  ?  391  SER   A C   1 
ATOM   3124  O  O   . SER   A 1 391  ? -8.45100   99.69700  28.84600  1.000 49.90964  ?  391  SER   A O   1 
ATOM   3125  C  CB  . SER   A 1 391  ? -10.53100  97.74400  27.24800  1.000 45.49181  ?  391  SER   A CB  1 
ATOM   3126  O  OG  . SER   A 1 391  ? -10.50500  96.46300  26.64300  1.000 54.66253  ?  391  SER   A OG  1 
ATOM   3127  N  N   . SER   A 1 392  ? -9.83300   100.82400 27.46300  1.000 39.65829  ?  392  SER   A N   1 
ATOM   3128  C  CA  . SER   A 1 392  ? -9.94700   101.97000 28.35400  1.000 46.08228  ?  392  SER   A CA  1 
ATOM   3129  C  C   . SER   A 1 392  ? -10.63000  101.55600 29.65000  1.000 47.22298  ?  392  SER   A C   1 
ATOM   3130  O  O   . SER   A 1 392  ? -11.57000  100.75700 29.64700  1.000 54.44836  ?  392  SER   A O   1 
ATOM   3131  C  CB  . SER   A 1 392  ? -10.73800  103.09200 27.68300  1.000 54.99851  ?  392  SER   A CB  1 
ATOM   3132  O  OG  . SER   A 1 392  ? -10.97100  104.15900 28.58800  1.000 62.16911  ?  392  SER   A OG  1 
ATOM   3133  N  N   . PHE   A 1 393  ? -10.15400  102.10600 30.76800  1.000 42.02108  ?  393  PHE   A N   1 
ATOM   3134  C  CA  . PHE   A 1 393  ? -10.72000  101.73100 32.05700  1.000 40.37214  ?  393  PHE   A CA  1 
ATOM   3135  C  C   . PHE   A 1 393  ? -12.15300  102.21900 32.23100  1.000 47.17205  ?  393  PHE   A C   1 
ATOM   3136  O  O   . PHE   A 1 393  ? -12.79400  101.85900 33.22300  1.000 47.90246  ?  393  PHE   A O   1 
ATOM   3137  C  CB  . PHE   A 1 393  ? -9.82600   102.23500 33.20200  1.000 32.98387  ?  393  PHE   A CB  1 
ATOM   3138  C  CG  . PHE   A 1 393  ? -9.99100   103.69800 33.52800  1.000 40.32403  ?  393  PHE   A CG  1 
ATOM   3139  C  CD1 . PHE   A 1 393  ? -10.02000  104.65700 32.52700  1.000 53.77290  ?  393  PHE   A CD1 1 
ATOM   3140  C  CD2 . PHE   A 1 393  ? -10.10000  104.11300 34.84700  1.000 41.27678  ?  393  PHE   A CD2 1 
ATOM   3141  C  CE1 . PHE   A 1 393  ? -10.16800  105.99700 32.83500  1.000 59.70639  ?  393  PHE   A CE1 1 
ATOM   3142  C  CE2 . PHE   A 1 393  ? -10.24600  105.45200 35.16000  1.000 41.24574  ?  393  PHE   A CE2 1 
ATOM   3143  C  CZ  . PHE   A 1 393  ? -10.28100  106.39400 34.15400  1.000 45.16857  ?  393  PHE   A CZ  1 
ATOM   3144  N  N   . SER   A 1 394  ? -12.67200  103.00200 31.28600  1.000 47.51715  ?  394  SER   A N   1 
ATOM   3145  C  CA  . SER   A 1 394  ? -14.06300  103.43400 31.29200  1.000 56.57805  ?  394  SER   A CA  1 
ATOM   3146  C  C   . SER   A 1 394  ? -15.00200  102.43800 30.61700  1.000 40.49147  ?  394  SER   A C   1 
ATOM   3147  O  O   . SER   A 1 394  ? -16.20100  102.71500 30.51400  1.000 49.34284  ?  394  SER   A O   1 
ATOM   3148  C  CB  . SER   A 1 394  ? -14.18700  104.80200 30.61200  1.000 50.65891  ?  394  SER   A CB  1 
ATOM   3149  O  OG  . SER   A 1 394  ? -13.36500  104.87000 29.45900  1.000 73.47318  ?  394  SER   A OG  1 
ATOM   3150  N  N   . PHE   A 1 395  ? -14.49200  101.29500 30.15900  1.000 46.43636  ?  395  PHE   A N   1 
ATOM   3151  C  CA  . PHE   A 1 395  ? -15.30200  100.26400 29.52500  1.000 48.92959  ?  395  PHE   A CA  1 
ATOM   3152  C  C   . PHE   A 1 395  ? -15.05000  98.92600  30.20400  1.000 45.45913  ?  395  PHE   A C   1 
ATOM   3153  O  O   . PHE   A 1 395  ? -13.94700  98.65200  30.68600  1.000 42.87637  ?  395  PHE   A O   1 
ATOM   3154  C  CB  . PHE   A 1 395  ? -15.00800  100.15600 28.02200  1.000 42.07067  ?  395  PHE   A CB  1 
ATOM   3155  C  CG  . PHE   A 1 395  ? -15.52900  101.31500 27.22500  1.000 61.49492  ?  395  PHE   A CG  1 
ATOM   3156  C  CD1 . PHE   A 1 395  ? -16.88300  101.60900 27.21300  1.000 82.93209  ?  395  PHE   A CD1 1 
ATOM   3157  C  CD2 . PHE   A 1 395  ? -14.66900  102.11800 26.49800  1.000 62.92527  ?  395  PHE   A CD2 1 
ATOM   3158  C  CE1 . PHE   A 1 395  ? -17.36900  102.67800 26.48500  1.000 88.98337  ?  395  PHE   A CE1 1 
ATOM   3159  C  CE2 . PHE   A 1 395  ? -15.15000  103.19000 25.77100  1.000 56.19194  ?  395  PHE   A CE2 1 
ATOM   3160  C  CZ  . PHE   A 1 395  ? -16.50000  103.46900 25.76300  1.000 76.99722  ?  395  PHE   A CZ  1 
ATOM   3161  N  N   . ASP   A 1 396  ? -16.08900  98.08800  30.23400  1.000 41.87488  ?  396  ASP   A N   1 
ATOM   3162  C  CA  . ASP   A 1 396  ? -16.01200  96.83700  30.97600  1.000 29.58752  ?  396  ASP   A CA  1 
ATOM   3163  C  C   . ASP   A 1 396  ? -15.01100  95.85800  30.38400  1.000 33.99460  ?  396  ASP   A C   1 
ATOM   3164  O  O   . ASP   A 1 396  ? -14.74400  94.82400  31.00600  1.000 36.18752  ?  396  ASP   A O   1 
ATOM   3165  C  CB  . ASP   A 1 396  ? -17.39700  96.18700  31.07100  1.000 43.37973  ?  396  ASP   A CB  1 
ATOM   3166  C  CG  . ASP   A 1 396  ? -18.01000  95.89200  29.71500  1.000 52.74646  ?  396  ASP   A CG  1 
ATOM   3167  O  OD1 . ASP   A 1 396  ? -17.45300  96.32300  28.68000  1.000 63.58733  ?  396  ASP   A OD1 1 
ATOM   3168  O  OD2 . ASP   A 1 396  ? -19.06100  95.21500  29.69100  1.000 48.16087  -1 396  ASP   A OD2 1 
ATOM   3169  N  N   . GLY   A 1 397  ? -14.46000  96.15100  29.20400  1.000 44.61139  ?  397  GLY   A N   1 
ATOM   3170  C  CA  . GLY   A 1 397  ? -13.35000  95.35700  28.70400  1.000 32.66459  ?  397  GLY   A CA  1 
ATOM   3171  C  C   . GLY   A 1 397  ? -12.16100  95.39000  29.64300  1.000 33.70265  ?  397  GLY   A C   1 
ATOM   3172  O  O   . GLY   A 1 397  ? -11.49600  94.37200  29.85200  1.000 38.05996  ?  397  GLY   A O   1 
ATOM   3173  N  N   . SER   A 1 398  ? -11.89300  96.55800  30.24100  1.000 39.31311  ?  398  SER   A N   1 
ATOM   3174  C  CA  . SER   A 1 398  ? -10.82100  96.67300  31.22700  1.000 46.69062  ?  398  SER   A CA  1 
ATOM   3175  C  C   . SER   A 1 398  ? -11.11000  95.86000  32.48400  1.000 32.68921  ?  398  SER   A C   1 
ATOM   3176  O  O   . SER   A 1 398  ? -10.17400  95.36000  33.11800  1.000 48.65111  ?  398  SER   A O   1 
ATOM   3177  C  CB  . SER   A 1 398  ? -10.59700  98.13900  31.59800  1.000 43.11056  ?  398  SER   A CB  1 
ATOM   3178  O  OG  . SER   A 1 398  ? -11.69100  98.64900  32.34000  1.000 53.77746  ?  398  SER   A OG  1 
ATOM   3179  N  N   . ALA   A 1 399  ? -12.38400  95.73000  32.87000  1.000 24.91929  ?  399  ALA   A N   1 
ATOM   3180  C  CA  . ALA   A 1 399  ? -12.72600  94.88400  34.01200  1.000 30.41418  ?  399  ALA   A CA  1 
ATOM   3181  C  C   . ALA   A 1 399  ? -12.28200  93.44500  33.78400  1.000 36.17964  ?  399  ALA   A C   1 
ATOM   3182  O  O   . ALA   A 1 399  ? -11.74600  92.80000  34.69400  1.000 40.02456  ?  399  ALA   A O   1 
ATOM   3183  C  CB  . ALA   A 1 399  ? -14.22800  94.94000  34.28400  1.000 32.54328  ?  399  ALA   A CB  1 
ATOM   3184  N  N   . LEU   A 1 400  ? -12.50800  92.91900  32.57800  1.000 33.17116  ?  400  LEU   A N   1 
ATOM   3185  C  CA  . LEU   A 1 400  ? -11.97000  91.60800  32.23400  1.000 41.34758  ?  400  LEU   A CA  1 
ATOM   3186  C  C   . LEU   A 1 400  ? -10.44800  91.63500  32.23500  1.000 41.32407  ?  400  LEU   A C   1 
ATOM   3187  O  O   . LEU   A 1 400  ? -9.80000   90.68800  32.69700  1.000 31.27730  ?  400  LEU   A O   1 
ATOM   3188  C  CB  . LEU   A 1 400  ? -12.50200  91.16500  30.86800  1.000 35.64710  ?  400  LEU   A CB  1 
ATOM   3189  C  CG  . LEU   A 1 400  ? -12.20800  89.74600  30.36100  1.000 40.16742  ?  400  LEU   A CG  1 
ATOM   3190  C  CD1 . LEU   A 1 400  ? -13.31100  89.28600  29.43000  1.000 40.51892  ?  400  LEU   A CD1 1 
ATOM   3191  C  CD2 . LEU   A 1 400  ? -10.87100  89.65200  29.64500  1.000 37.58771  ?  400  LEU   A CD2 1 
ATOM   3192  N  N   . ASP   A 1 401  ? -9.86200   92.72000  31.72400  1.000 30.81634  ?  401  ASP   A N   1 
ATOM   3193  C  CA  . ASP   A 1 401  ? -8.41300   92.78600  31.58900  1.000 32.34273  ?  401  ASP   A CA  1 
ATOM   3194  C  C   . ASP   A 1 401  ? -7.71900   92.82000  32.94500  1.000 35.73535  ?  401  ASP   A C   1 
ATOM   3195  O  O   . ASP   A 1 401  ? -6.59400   92.32500  33.07500  1.000 46.51884  ?  401  ASP   A O   1 
ATOM   3196  C  CB  . ASP   A 1 401  ? -8.02200   94.01000  30.75500  1.000 25.61124  ?  401  ASP   A CB  1 
ATOM   3197  C  CG  . ASP   A 1 401  ? -8.40900   93.87000  29.28700  1.000 42.38541  ?  401  ASP   A CG  1 
ATOM   3198  O  OD1 . ASP   A 1 401  ? -8.89900   92.78900  28.89500  1.000 47.45907  ?  401  ASP   A OD1 1 
ATOM   3199  O  OD2 . ASP   A 1 401  ? -8.22700   94.84300  28.52300  1.000 47.47818  -1 401  ASP   A OD2 1 
ATOM   3200  N  N   . ILE   A 1 402  ? -8.37300   93.36700  33.96300  1.000 32.79691  ?  402  ILE   A N   1 
ATOM   3201  C  CA  . ILE   A 1 402  ? -7.74300   93.61000  35.25700  1.000 33.76146  ?  402  ILE   A CA  1 
ATOM   3202  C  C   . ILE   A 1 402  ? -8.14300   92.56700  36.29200  1.000 36.16039  ?  402  ILE   A C   1 
ATOM   3203  O  O   . ILE   A 1 402  ? -7.28500   91.93800  36.91000  1.000 40.31279  ?  402  ILE   A O   1 
ATOM   3204  C  CB  . ILE   A 1 402  ? -8.07700   95.03600  35.74800  1.000 28.95675  ?  402  ILE   A CB  1 
ATOM   3205  C  CG1 . ILE   A 1 402  ? -7.43700   96.07500  34.82700  1.000 34.36703  ?  402  ILE   A CG1 1 
ATOM   3206  C  CG2 . ILE   A 1 402  ? -7.61700   95.21900  37.18100  1.000 23.38274  ?  402  ILE   A CG2 1 
ATOM   3207  C  CD1 . ILE   A 1 402  ? -8.05000   97.45000  34.94500  1.000 27.83255  ?  402  ILE   A CD1 1 
ATOM   3208  N  N   . PHE   A 1 403  ? -9.44700   92.37000  36.49500  1.000 31.02880  ?  403  PHE   A N   1 
ATOM   3209  C  CA  . PHE   A 1 403  ? -9.91300   91.60300  37.64600  1.000 32.49393  ?  403  PHE   A CA  1 
ATOM   3210  C  C   . PHE   A 1 403  ? -9.81100   90.09600  37.43900  1.000 27.58111  ?  403  PHE   A C   1 
ATOM   3211  O  O   . PHE   A 1 403  ? -9.53500   89.36700  38.39900  1.000 29.69407  ?  403  PHE   A O   1 
ATOM   3212  C  CB  . PHE   A 1 403  ? -11.35700  91.99100  37.98000  1.000 34.85907  ?  403  PHE   A CB  1 
ATOM   3213  C  CG  . PHE   A 1 403  ? -11.55000  93.46600  38.20000  1.000 23.31659  ?  403  PHE   A CG  1 
ATOM   3214  C  CD1 . PHE   A 1 403  ? -10.72000  94.16700  39.05500  1.000 28.98261  ?  403  PHE   A CD1 1 
ATOM   3215  C  CD2 . PHE   A 1 403  ? -12.55000  94.15500  37.53500  1.000 39.86936  ?  403  PHE   A CD2 1 
ATOM   3216  C  CE1 . PHE   A 1 403  ? -10.89100  95.52400  39.25600  1.000 35.06184  ?  403  PHE   A CE1 1 
ATOM   3217  C  CE2 . PHE   A 1 403  ? -12.72500  95.51500  37.73000  1.000 35.96119  ?  403  PHE   A CE2 1 
ATOM   3218  C  CZ  . PHE   A 1 403  ? -11.89300  96.19800  38.59200  1.000 31.44225  ?  403  PHE   A CZ  1 
ATOM   3219  N  N   . THR   A 1 404  ? -10.03600  89.60300  36.21900  1.000 32.39412  ?  404  THR   A N   1 
ATOM   3220  C  CA  . THR   A 1 404  ? -10.03200  88.15800  36.01000  1.000 38.32429  ?  404  THR   A CA  1 
ATOM   3221  C  C   . THR   A 1 404  ? -8.64200   87.57600  36.23600  1.000 39.22123  ?  404  THR   A C   1 
ATOM   3222  O  O   . THR   A 1 404  ? -8.48600   86.57400  36.94400  1.000 41.43387  ?  404  THR   A O   1 
ATOM   3223  C  CB  . THR   A 1 404  ? -10.53700  87.81500  34.60700  1.000 30.10341  ?  404  THR   A CB  1 
ATOM   3224  O  OG1 . THR   A 1 404  ? -9.59800   88.27500  33.62800  1.000 28.98497  ?  404  THR   A OG1 1 
ATOM   3225  C  CG2 . THR   A 1 404  ? -11.89100  88.46200  34.35100  1.000 43.55839  ?  404  THR   A CG2 1 
ATOM   3226  N  N   . HIS   A 1 405  ? -7.61600   88.20600  35.65800  1.000 33.70615  ?  405  HIS   A N   1 
ATOM   3227  C  CA  . HIS   A 1 405  ? -6.26100   87.67500  35.76000  1.000 42.89169  ?  405  HIS   A CA  1 
ATOM   3228  C  C   . HIS   A 1 405  ? -5.64300   87.91200  37.13400  1.000 37.46020  ?  405  HIS   A C   1 
ATOM   3229  O  O   . HIS   A 1 405  ? -4.79100   87.12700  37.56500  1.000 39.47392  ?  405  HIS   A O   1 
ATOM   3230  C  CB  . HIS   A 1 405  ? -5.37800   88.28300  34.66900  1.000 39.84977  ?  405  HIS   A CB  1 
ATOM   3231  C  CG  . HIS   A 1 405  ? -6.02100   88.30200  33.31600  1.000 39.14865  ?  405  HIS   A CG  1 
ATOM   3232  N  ND1 . HIS   A 1 405  ? -6.46900   89.46200  32.71900  1.000 36.99480  ?  405  HIS   A ND1 1 
ATOM   3233  C  CD2 . HIS   A 1 405  ? -6.30100   87.29900  32.44800  1.000 22.61151  ?  405  HIS   A CD2 1 
ATOM   3234  C  CE1 . HIS   A 1 405  ? -6.98900   89.17400  31.53900  1.000 39.96999  ?  405  HIS   A CE1 1 
ATOM   3235  N  NE2 . HIS   A 1 405  ? -6.90100   87.86900  31.35100  1.000 31.96307  ?  405  HIS   A NE2 1 
ATOM   3236  N  N   . LEU   A 1 406  ? -6.05200   88.97500  37.83100  1.000 27.37118  ?  406  LEU   A N   1 
ATOM   3237  C  CA  . LEU   A 1 406  ? -5.53800   89.21500  39.17700  1.000 25.15715  ?  406  LEU   A CA  1 
ATOM   3238  C  C   . LEU   A 1 406  ? -5.92100   88.08400  40.12400  1.000 41.92904  ?  406  LEU   A C   1 
ATOM   3239  O  O   . LEU   A 1 406  ? -5.13600   87.71000  41.00400  1.000 56.86146  ?  406  LEU   A O   1 
ATOM   3240  C  CB  . LEU   A 1 406  ? -6.05300   90.55200  39.70800  1.000 18.88979  ?  406  LEU   A CB  1 
ATOM   3241  C  CG  . LEU   A 1 406  ? -5.21400   91.78800  39.37700  1.000 33.66354  ?  406  LEU   A CG  1 
ATOM   3242  C  CD1 . LEU   A 1 406  ? -5.72200   93.00200  40.13700  1.000 31.07389  ?  406  LEU   A CD1 1 
ATOM   3243  C  CD2 . LEU   A 1 406  ? -3.74000   91.54700  39.67300  1.000 33.62935  ?  406  LEU   A CD2 1 
ATOM   3244  N  N   . LEU   A 1 407  ? -7.12000   87.52500  39.96100  1.000 29.69662  ?  407  LEU   A N   1 
ATOM   3245  C  CA  . LEU   A 1 407  ? -7.59000   86.44800  40.82400  1.000 35.51671  ?  407  LEU   A CA  1 
ATOM   3246  C  C   . LEU   A 1 407  ? -6.96100   85.10400  40.49100  1.000 43.43420  ?  407  LEU   A C   1 
ATOM   3247  O  O   . LEU   A 1 407  ? -7.34400   84.09300  41.09100  1.000 51.65689  ?  407  LEU   A O   1 
ATOM   3248  C  CB  . LEU   A 1 407  ? -9.11500   86.33200  40.74800  1.000 46.92140  ?  407  LEU   A CB  1 
ATOM   3249  C  CG  . LEU   A 1 407  ? -9.92200   87.42200  41.45300  1.000 40.44701  ?  407  LEU   A CG  1 
ATOM   3250  C  CD1 . LEU   A 1 407  ? -11.36500  86.99000  41.64700  1.000 46.47033  ?  407  LEU   A CD1 1 
ATOM   3251  C  CD2 . LEU   A 1 407  ? -9.29300   87.78300  42.78500  1.000 36.64023  ?  407  LEU   A CD2 1 
ATOM   3252  N  N   . ALA   A 1 408  ? -6.01400   85.06500  39.55500  1.000 29.01972  ?  408  ALA   A N   1 
ATOM   3253  C  CA  . ALA   A 1 408  ? -5.36200   83.82600  39.16800  1.000 29.75399  ?  408  ALA   A CA  1 
ATOM   3254  C  C   . ALA   A 1 408  ? -3.85400   83.85600  39.35900  1.000 34.00371  ?  408  ALA   A C   1 
ATOM   3255  O  O   . ALA   A 1 408  ? -3.19300   82.84200  39.10300  1.000 42.85071  ?  408  ALA   A O   1 
ATOM   3256  C  CB  . ALA   A 1 408  ? -5.68400   83.49000  37.70600  1.000 38.01758  ?  408  ALA   A CB  1 
ATOM   3257  N  N   . GLY   A 1 409  ? -3.29000   84.97700  39.80000  1.000 29.87357  ?  409  GLY   A N   1 
ATOM   3258  C  CA  . GLY   A 1 409  ? -1.86200   85.08400  39.99200  1.000 37.71862  ?  409  GLY   A CA  1 
ATOM   3259  C  C   . GLY   A 1 409  ? -1.08900   85.56800  38.78600  1.000 44.45118  ?  409  GLY   A C   1 
ATOM   3260  O  O   . GLY   A 1 409  ? 0.14700    85.62100  38.84600  1.000 36.74629  ?  409  GLY   A O   1 
ATOM   3261  N  N   . ALA   A 1 410  ? -1.77100   85.92900  37.70000  1.000 41.39090  ?  410  ALA   A N   1 
ATOM   3262  C  CA  . ALA   A 1 410  ? -1.11000   86.34700  36.47500  1.000 27.66303  ?  410  ALA   A CA  1 
ATOM   3263  C  C   . ALA   A 1 410  ? -0.60600   87.78300  36.60000  1.000 29.43277  ?  410  ALA   A C   1 
ATOM   3264  O  O   . ALA   A 1 410  ? -0.83500   88.47200  37.59800  1.000 37.43900  ?  410  ALA   A O   1 
ATOM   3265  C  CB  . ALA   A 1 410  ? -2.05300   86.20300  35.28500  1.000 36.17464  ?  410  ALA   A CB  1 
ATOM   3266  N  N   . ALA   A 1 411  ? 0.08500    88.24300  35.56300  1.000 32.41371  ?  411  ALA   A N   1 
ATOM   3267  C  CA  . ALA   A 1 411  ? 0.72600    89.54900  35.56100  1.000 34.99899  ?  411  ALA   A CA  1 
ATOM   3268  C  C   . ALA   A 1 411  ? 0.05400    90.44900  34.53500  1.000 39.10496  ?  411  ALA   A C   1 
ATOM   3269  O  O   . ALA   A 1 411  ? -0.09700   90.06700  33.36900  1.000 39.08419  ?  411  ALA   A O   1 
ATOM   3270  C  CB  . ALA   A 1 411  ? 2.22100    89.42000  35.25900  1.000 25.64759  ?  411  ALA   A CB  1 
ATOM   3271  N  N   . LEU   A 1 412  ? -0.34700   91.63900  34.97300  1.000 35.91380  ?  412  LEU   A N   1 
ATOM   3272  C  CA  . LEU   A 1 412  ? -0.94000   92.63200  34.09100  1.000 35.34390  ?  412  LEU   A CA  1 
ATOM   3273  C  C   . LEU   A 1 412  ? 0.14200    93.52500  33.50100  1.000 38.56865  ?  412  LEU   A C   1 
ATOM   3274  O  O   . LEU   A 1 412  ? 1.05700    93.95900  34.20600  1.000 41.48764  ?  412  LEU   A O   1 
ATOM   3275  C  CB  . LEU   A 1 412  ? -1.95800   93.48900  34.84600  1.000 38.75682  ?  412  LEU   A CB  1 
ATOM   3276  C  CG  . LEU   A 1 412  ? -3.03900   92.77000  35.64800  1.000 33.64012  ?  412  LEU   A CG  1 
ATOM   3277  C  CD1 . LEU   A 1 412  ? -3.97300   93.78600  36.28400  1.000 37.40580  ?  412  LEU   A CD1 1 
ATOM   3278  C  CD2 . LEU   A 1 412  ? -3.81200   91.80000  34.76800  1.000 32.11375  ?  412  LEU   A CD2 1 
ATOM   3279  N  N   . HIS   A 1 413  ? 0.02400    93.80900  32.20600  1.000 37.69998  ?  413  HIS   A N   1 
ATOM   3280  C  CA  . HIS   A 1 413  ? 0.94000    94.70300  31.50900  1.000 39.80505  ?  413  HIS   A CA  1 
ATOM   3281  C  C   . HIS   A 1 413  ? 0.15100    95.87300  30.94000  1.000 42.20410  ?  413  HIS   A C   1 
ATOM   3282  O  O   . HIS   A 1 413  ? -0.72400   95.67900  30.09000  1.000 45.56971  ?  413  HIS   A O   1 
ATOM   3283  C  CB  . HIS   A 1 413  ? 1.69500    93.96400  30.40500  1.000 35.81129  ?  413  HIS   A CB  1 
ATOM   3284  C  CG  . HIS   A 1 413  ? 2.69700    92.98300  30.92300  1.000 42.78189  ?  413  HIS   A CG  1 
ATOM   3285  N  ND1 . HIS   A 1 413  ? 4.05600    93.17900  30.81200  1.000 37.03452  ?  413  HIS   A ND1 1 
ATOM   3286  C  CD2 . HIS   A 1 413  ? 2.53800    91.80300  31.56800  1.000 43.29592  ?  413  HIS   A CD2 1 
ATOM   3287  C  CE1 . HIS   A 1 413  ? 4.69200    92.16100  31.36400  1.000 49.71688  ?  413  HIS   A CE1 1 
ATOM   3288  N  NE2 . HIS   A 1 413  ? 3.79400    91.31200  31.83000  1.000 40.97043  ?  413  HIS   A NE2 1 
ATOM   3289  N  N   . ILE   A 1 414  ? 0.46600    97.08400  31.40600  1.000 30.86323  ?  414  ILE   A N   1 
ATOM   3290  C  CA  . ILE   A 1 414  ? -0.26200   98.27100  30.97500  1.000 37.54227  ?  414  ILE   A CA  1 
ATOM   3291  C  C   . ILE   A 1 414  ? 0.15500    98.64700  29.55900  1.000 46.48156  ?  414  ILE   A C   1 
ATOM   3292  O  O   . ILE   A 1 414  ? 1.33700    98.57600  29.19600  1.000 62.95745  ?  414  ILE   A O   1 
ATOM   3293  C  CB  . ILE   A 1 414  ? -0.02200   99.43100  31.95700  1.000 41.59371  ?  414  ILE   A CB  1 
ATOM   3294  C  CG1 . ILE   A 1 414  ? -0.35400   98.99600  33.38700  1.000 35.37327  ?  414  ILE   A CG1 1 
ATOM   3295  C  CG2 . ILE   A 1 414  ? -0.83600   100.65100 31.56200  1.000 36.89882  ?  414  ILE   A CG2 1 
ATOM   3296  C  CD1 . ILE   A 1 414  ? -1.81800   98.66000  33.60200  1.000 41.24834  ?  414  ILE   A CD1 1 
ATOM   3297  N  N   . VAL   A 1 415  ? -0.81700   99.05700  28.75000  1.000 55.26935  ?  415  VAL   A N   1 
ATOM   3298  C  CA  . VAL   A 1 415  ? -0.61100   99.37200  27.34100  1.000 57.82813  ?  415  VAL   A CA  1 
ATOM   3299  C  C   . VAL   A 1 415  ? -0.69500   100.88800 27.17700  1.000 76.42989  ?  415  VAL   A C   1 
ATOM   3300  O  O   . VAL   A 1 415  ? -1.77100   101.47300 27.37400  1.000 68.70368  ?  415  VAL   A O   1 
ATOM   3301  C  CB  . VAL   A 1 415  ? -1.63900   98.67000  26.44600  1.000 53.66739  ?  415  VAL   A CB  1 
ATOM   3302  C  CG1 . VAL   A 1 415  ? -1.28300   98.85600  24.97700  1.000 64.02175  ?  415  VAL   A CG1 1 
ATOM   3303  C  CG2 . VAL   A 1 415  ? -1.72100   97.21400  26.80000  1.000 50.44336  ?  415  VAL   A CG2 1 
ATOM   3304  N  N   . PRO   A 1 416  ? 0.39100    101.55900 26.81000  1.000 91.15754  ?  416  PRO   A N   1 
ATOM   3305  C  CA  . PRO   A 1 416  ? 0.28800    102.96900 26.42800  1.000 91.10389  ?  416  PRO   A CA  1 
ATOM   3306  C  C   . PRO   A 1 416  ? -0.36400   103.09900 25.06100  1.000 103.30731 ?  416  PRO   A C   1 
ATOM   3307  O  O   . PRO   A 1 416  ? -0.33800   102.18100 24.23800  1.000 104.73556 ?  416  PRO   A O   1 
ATOM   3308  C  CB  . PRO   A 1 416  ? 1.74700    103.44700 26.39500  1.000 97.61224  ?  416  PRO   A CB  1 
ATOM   3309  C  CG  . PRO   A 1 416  ? 2.57700    102.28800 26.91800  1.000 100.35948 ?  416  PRO   A CG  1 
ATOM   3310  C  CD  . PRO   A 1 416  ? 1.76800    101.05700 26.69100  1.000 73.47262  ?  416  PRO   A CD  1 
ATOM   3311  N  N   . SER   A 1 417  ? -0.95500   104.27200 24.82200  1.000 111.99548 ?  417  SER   A N   1 
ATOM   3312  C  CA  . SER   A 1 417  ? -1.57600   104.54000 23.52900  1.000 100.04327 ?  417  SER   A CA  1 
ATOM   3313  C  C   . SER   A 1 417  ? -0.58200   104.47600 22.37600  1.000 87.02005  ?  417  SER   A C   1 
ATOM   3314  O  O   . SER   A 1 417  ? -1.00300   104.48500 21.21600  1.000 88.26467  ?  417  SER   A O   1 
ATOM   3315  C  CB  . SER   A 1 417  ? -2.26400   105.90600 23.55100  1.000 94.67427  ?  417  SER   A CB  1 
ATOM   3316  O  OG  . SER   A 1 417  ? -3.40000   105.88600 24.39700  1.000 89.94537  ?  417  SER   A OG  1 
ATOM   3317  N  N   . GLU   A 1 418  ? 0.71900    104.40900 22.66500  1.000 98.98271  ?  418  GLU   A N   1 
ATOM   3318  C  CA  . GLU   A 1 418  ? 1.71000    104.24400 21.60900  1.000 98.35512  ?  418  GLU   A CA  1 
ATOM   3319  C  C   . GLU   A 1 418  ? 1.52800    102.92500 20.86900  1.000 101.90351 ?  418  GLU   A C   1 
ATOM   3320  O  O   . GLU   A 1 418  ? 1.76900    102.85500 19.65800  1.000 113.91920 ?  418  GLU   A O   1 
ATOM   3321  C  CB  . GLU   A 1 418  ? 3.11500    104.33000 22.20300  1.000 94.68513  ?  418  GLU   A CB  1 
ATOM   3322  C  CG  . GLU   A 1 418  ? 3.23000    105.29700 23.37300  1.000 112.30499 ?  418  GLU   A CG  1 
ATOM   3323  C  CD  . GLU   A 1 418  ? 4.31300    104.89400 24.35800  1.000 122.13940 ?  418  GLU   A CD  1 
ATOM   3324  O  OE1 . GLU   A 1 418  ? 5.10900    103.98900 24.03100  1.000 126.07768 ?  418  GLU   A OE1 1 
ATOM   3325  O  OE2 . GLU   A 1 418  ? 4.36500    105.47700 25.46200  1.000 102.13152 -1 418  GLU   A OE2 1 
ATOM   3326  N  N   . ARG   A 1 419  ? 1.10200    101.87300 21.57000  1.000 89.58232  ?  419  ARG   A N   1 
ATOM   3327  C  CA  . ARG   A 1 419  ? 0.93700    100.55800 20.96900  1.000 85.10339  ?  419  ARG   A CA  1 
ATOM   3328  C  C   . ARG   A 1 419  ? -0.51100   100.09600 20.89500  1.000 84.96182  ?  419  ARG   A C   1 
ATOM   3329  O  O   . ARG   A 1 419  ? -0.79500   99.13100  20.17700  1.000 81.70674  ?  419  ARG   A O   1 
ATOM   3330  C  CB  . ARG   A 1 419  ? 1.75800    99.51200  21.73800  1.000 91.27435  ?  419  ARG   A CB  1 
ATOM   3331  C  CG  . ARG   A 1 419  ? 3.23400    99.85200  21.86500  1.000 90.77749  ?  419  ARG   A CG  1 
ATOM   3332  C  CD  . ARG   A 1 419  ? 4.01100    98.72700  22.53600  1.000 88.57585  ?  419  ARG   A CD  1 
ATOM   3333  N  NE  . ARG   A 1 419  ? 4.95200    98.09200  21.61900  1.000 105.85786 ?  419  ARG   A NE  1 
ATOM   3334  C  CZ  . ARG   A 1 419  ? 6.27100    98.21300  21.68800  1.000 98.40633  ?  419  ARG   A CZ  1 
ATOM   3335  N  NH1 . ARG   A 1 419  ? 6.85200    98.93900  22.63000  1.000 90.45637  ?  419  ARG   A NH1 1 
ATOM   3336  N  NH2 . ARG   A 1 419  ? 7.02800    97.58900  20.78900  1.000 77.83207  ?  419  ARG   A NH2 1 
ATOM   3337  N  N   . LYS   A 1 420  ? -1.42700   100.74600 21.62000  1.000 76.18679  ?  420  LYS   A N   1 
ATOM   3338  C  CA  . LYS   A 1 420  ? -2.84100   100.40300 21.52200  1.000 70.10485  ?  420  LYS   A CA  1 
ATOM   3339  C  C   . LYS   A 1 420  ? -3.37100   100.58100 20.10500  1.000 73.94076  ?  420  LYS   A C   1 
ATOM   3340  O  O   . LYS   A 1 420  ? -4.36100   99.94100  19.73600  1.000 71.95919  ?  420  LYS   A O   1 
ATOM   3341  C  CB  . LYS   A 1 420  ? -3.64900   101.25400 22.51000  1.000 77.39168  ?  420  LYS   A CB  1 
ATOM   3342  C  CG  . LYS   A 1 420  ? -5.16300   101.04400 22.47800  1.000 68.40442  ?  420  LYS   A CG  1 
ATOM   3343  C  CD  . LYS   A 1 420  ? -5.82500   101.57900 23.74200  1.000 64.27255  ?  420  LYS   A CD  1 
ATOM   3344  C  CE  . LYS   A 1 420  ? -7.31300   101.83200 23.53500  1.000 69.39407  ?  420  LYS   A CE  1 
ATOM   3345  N  NZ  . LYS   A 1 420  ? -8.09300   100.56900 23.42700  1.000 73.38987  ?  420  LYS   A NZ  1 
ATOM   3346  N  N   . TYR   A 1 421  ? -2.71600   101.41300 19.29500  1.000 75.54081  ?  421  TYR   A N   1 
ATOM   3347  C  CA  . TYR   A 1 421  ? -3.15300   101.67600 17.93500  1.000 77.29234  ?  421  TYR   A CA  1 
ATOM   3348  C  C   . TYR   A 1 421  ? -2.16700   101.21700 16.87100  1.000 67.30355  ?  421  TYR   A C   1 
ATOM   3349  O  O   . TYR   A 1 421  ? -2.58700   100.97700 15.73300  1.000 75.99045  ?  421  TYR   A O   1 
ATOM   3350  C  CB  . TYR   A 1 421  ? -3.44500   103.17400 17.76600  1.000 74.38090  ?  421  TYR   A CB  1 
ATOM   3351  C  CG  . TYR   A 1 421  ? -4.28800   103.69600 18.90600  1.000 83.33828  ?  421  TYR   A CG  1 
ATOM   3352  C  CD1 . TYR   A 1 421  ? -5.64400   103.40500 18.98200  1.000 95.83710  ?  421  TYR   A CD1 1 
ATOM   3353  C  CD2 . TYR   A 1 421  ? -3.72200   104.43800 19.93200  1.000 91.74375  ?  421  TYR   A CD2 1 
ATOM   3354  C  CE1 . TYR   A 1 421  ? -6.42000   103.86200 20.03600  1.000 87.45037  ?  421  TYR   A CE1 1 
ATOM   3355  C  CE2 . TYR   A 1 421  ? -4.48600   104.90000 20.99100  1.000 98.55139  ?  421  TYR   A CE2 1 
ATOM   3356  C  CZ  . TYR   A 1 421  ? -5.83600   104.60900 21.03800  1.000 99.52085  ?  421  TYR   A CZ  1 
ATOM   3357  O  OH  . TYR   A 1 421  ? -6.60700   105.06400 22.08700  1.000 89.90870  ?  421  TYR   A OH  1 
ATOM   3358  N  N   . ASP   A 1 422  ? -0.88600   101.07900 17.20100  1.000 63.24709  ?  422  ASP   A N   1 
ATOM   3359  C  CA  . ASP   A 1 422  ? 0.07500    100.41700 16.32100  1.000 64.08713  ?  422  ASP   A CA  1 
ATOM   3360  C  C   . ASP   A 1 422  ? 0.08600    98.94400  16.70700  1.000 64.69654  ?  422  ASP   A C   1 
ATOM   3361  O  O   . ASP   A 1 422  ? 0.81100    98.52000  17.60900  1.000 73.74385  ?  422  ASP   A O   1 
ATOM   3362  C  CB  . ASP   A 1 422  ? 1.45400    101.05500 16.44000  1.000 47.24553  ?  422  ASP   A CB  1 
ATOM   3363  C  CG  . ASP   A 1 422  ? 2.43700    100.51800 15.41600  1.000 66.79122  ?  422  ASP   A CG  1 
ATOM   3364  O  OD1 . ASP   A 1 422  ? 2.07700    99.58500  14.66800  1.000 75.54973  ?  422  ASP   A OD1 1 
ATOM   3365  O  OD2 . ASP   A 1 422  ? 3.57500    101.02900 15.36300  1.000 73.68654  -1 422  ASP   A OD2 1 
ATOM   3366  N  N   . LEU   A 1 423  ? -0.74100   98.15000  16.02100  1.000 50.76067  ?  423  LEU   A N   1 
ATOM   3367  C  CA  . LEU   A 1 423  ? -0.86900   96.73500  16.34400  1.000 51.95032  ?  423  LEU   A CA  1 
ATOM   3368  C  C   . LEU   A 1 423  ? 0.29400    95.90000  15.82600  1.000 67.11758  ?  423  LEU   A C   1 
ATOM   3369  O  O   . LEU   A 1 423  ? 0.38400    94.71500  16.16600  1.000 70.91447  ?  423  LEU   A O   1 
ATOM   3370  C  CB  . LEU   A 1 423  ? -2.19000   96.18300  15.80400  1.000 64.11379  ?  423  LEU   A CB  1 
ATOM   3371  C  CG  . LEU   A 1 423  ? -3.45200   96.82000  16.39400  1.000 59.81404  ?  423  LEU   A CG  1 
ATOM   3372  C  CD1 . LEU   A 1 423  ? -4.68600   96.08400  15.91800  1.000 53.04398  ?  423  LEU   A CD1 1 
ATOM   3373  C  CD2 . LEU   A 1 423  ? -3.40400   96.85500  17.91600  1.000 52.43848  ?  423  LEU   A CD2 1 
ATOM   3374  N  N   . ASP   A 1 424  ? 1.17600    96.48100  15.01100  1.000 71.78744  ?  424  ASP   A N   1 
ATOM   3375  C  CA  . ASP   A 1 424  ? 2.44700    95.82500  14.73000  1.000 74.76829  ?  424  ASP   A CA  1 
ATOM   3376  C  C   . ASP   A 1 424  ? 3.37500    95.91500  15.93500  1.000 67.73567  ?  424  ASP   A C   1 
ATOM   3377  O  O   . ASP   A 1 424  ? 4.02600    94.92900  16.30100  1.000 60.63849  ?  424  ASP   A O   1 
ATOM   3378  C  CB  . ASP   A 1 424  ? 3.09800    96.44700  13.49300  1.000 76.38079  ?  424  ASP   A CB  1 
ATOM   3379  C  CG  . ASP   A 1 424  ? 4.45900    95.84800  13.18500  1.000 94.12757  ?  424  ASP   A CG  1 
ATOM   3380  O  OD1 . ASP   A 1 424  ? 4.51400    94.70300  12.68700  1.000 85.28076  ?  424  ASP   A OD1 1 
ATOM   3381  O  OD2 . ASP   A 1 424  ? 5.47700    96.52500  13.44100  1.000 103.22002 -1 424  ASP   A OD2 1 
ATOM   3382  N  N   . ALA   A 1 425  ? 3.43100    97.08900  16.57300  1.000 63.98743  ?  425  ALA   A N   1 
ATOM   3383  C  CA  . ALA   A 1 425  ? 4.23400    97.25500  17.78000  1.000 58.68376  ?  425  ALA   A CA  1 
ATOM   3384  C  C   . ALA   A 1 425  ? 3.65100    96.48500  18.95500  1.000 65.43857  ?  425  ALA   A C   1 
ATOM   3385  O  O   . ALA   A 1 425  ? 4.39600    96.06300  19.84700  1.000 61.43393  ?  425  ALA   A O   1 
ATOM   3386  C  CB  . ALA   A 1 425  ? 4.35500    98.73600  18.13400  1.000 42.47140  ?  425  ALA   A CB  1 
ATOM   3387  N  N   . LEU   A 1 426  ? 2.32900    96.30700  18.98500  1.000 56.75894  ?  426  LEU   A N   1 
ATOM   3388  C  CA  . LEU   A 1 426  ? 1.72300    95.50500  20.04100  1.000 51.40392  ?  426  LEU   A CA  1 
ATOM   3389  C  C   . LEU   A 1 426  ? 2.17900    94.05700  19.94500  1.000 46.05080  ?  426  LEU   A C   1 
ATOM   3390  O  O   . LEU   A 1 426  ? 2.55400    93.44300  20.95000  1.000 50.69872  ?  426  LEU   A O   1 
ATOM   3391  C  CB  . LEU   A 1 426  ? 0.19900    95.59800  19.97100  1.000 52.16387  ?  426  LEU   A CB  1 
ATOM   3392  C  CG  . LEU   A 1 426  ? -0.52800   95.17300  21.25000  1.000 40.45935  ?  426  LEU   A CG  1 
ATOM   3393  C  CD1 . LEU   A 1 426  ? 0.01500    95.91800  22.45800  1.000 51.23375  ?  426  LEU   A CD1 1 
ATOM   3394  C  CD2 . LEU   A 1 426  ? -2.02000   95.39600  21.12300  1.000 31.15082  ?  426  LEU   A CD2 1 
ATOM   3395  N  N   . ASN   A 1 427  ? 2.15700    93.49600  18.73300  1.000 52.53338  ?  427  ASN   A N   1 
ATOM   3396  C  CA  . ASN   A 1 427  ? 2.65100    92.13800  18.53500  1.000 53.39625  ?  427  ASN   A CA  1 
ATOM   3397  C  C   . ASN   A 1 427  ? 4.11200    92.02700  18.94400  1.000 48.82600  ?  427  ASN   A C   1 
ATOM   3398  O  O   . ASN   A 1 427  ? 4.54400    90.99200  19.46500  1.000 46.54124  ?  427  ASN   A O   1 
ATOM   3399  C  CB  . ASN   A 1 427  ? 2.46900    91.72100  17.07700  1.000 48.84205  ?  427  ASN   A CB  1 
ATOM   3400  C  CG  . ASN   A 1 427  ? 2.85700    90.27800  16.83100  1.000 52.78748  ?  427  ASN   A CG  1 
ATOM   3401  O  OD1 . ASN   A 1 427  ? 2.21700    89.35800  17.34000  1.000 42.75725  ?  427  ASN   A OD1 1 
ATOM   3402  N  ND2 . ASN   A 1 427  ? 3.91000    90.07100  16.04800  1.000 53.64763  ?  427  ASN   A ND2 1 
ATOM   3403  N  N   . ASP   A 1 428  ? 4.88900    93.08600  18.71500  1.000 45.70819  ?  428  ASP   A N   1 
ATOM   3404  C  CA  . ASP   A 1 428  ? 6.26400    93.11200  19.19500  1.000 46.24160  ?  428  ASP   A CA  1 
ATOM   3405  C  C   . ASP   A 1 428  ? 6.30300    92.96000  20.71000  1.000 46.74223  ?  428  ASP   A C   1 
ATOM   3406  O  O   . ASP   A 1 428  ? 6.89700    92.01200  21.23600  1.000 48.00300  ?  428  ASP   A O   1 
ATOM   3407  C  CB  . ASP   A 1 428  ? 6.94900    94.40600  18.75200  1.000 59.95479  ?  428  ASP   A CB  1 
ATOM   3408  C  CG  . ASP   A 1 428  ? 7.21900    94.44200  17.25800  1.000 73.04309  ?  428  ASP   A CG  1 
ATOM   3409  O  OD1 . ASP   A 1 428  ? 7.09200    93.38600  16.60000  1.000 66.36210  ?  428  ASP   A OD1 1 
ATOM   3410  O  OD2 . ASP   A 1 428  ? 7.55900    95.52900  16.74200  1.000 73.00566  -1 428  ASP   A OD2 1 
ATOM   3411  N  N   . TYR   A 1 429  ? 5.63900    93.87400  21.42500  1.000 51.27735  ?  429  TYR   A N   1 
ATOM   3412  C  CA  . TYR   A 1 429  ? 5.59500    93.81400  22.88400  1.000 36.20864  ?  429  TYR   A CA  1 
ATOM   3413  C  C   . TYR   A 1 429  ? 5.12200    92.44900  23.36700  1.000 32.66172  ?  429  TYR   A C   1 
ATOM   3414  O  O   . TYR   A 1 429  ? 5.75200    91.83200  24.23200  1.000 39.89526  ?  429  TYR   A O   1 
ATOM   3415  C  CB  . TYR   A 1 429  ? 4.68800    94.92100  23.42500  1.000 41.52280  ?  429  TYR   A CB  1 
ATOM   3416  C  CG  . TYR   A 1 429  ? 4.67600    95.03300  24.93600  1.000 40.27685  ?  429  TYR   A CG  1 
ATOM   3417  C  CD1 . TYR   A 1 429  ? 3.84500    94.22700  25.70700  1.000 34.64610  ?  429  TYR   A CD1 1 
ATOM   3418  C  CD2 . TYR   A 1 429  ? 5.48500    95.95300  25.58900  1.000 33.51080  ?  429  TYR   A CD2 1 
ATOM   3419  C  CE1 . TYR   A 1 429  ? 3.82800    94.32700  27.08400  1.000 38.81207  ?  429  TYR   A CE1 1 
ATOM   3420  C  CE2 . TYR   A 1 429  ? 5.47400    96.06200  26.96900  1.000 27.33038  ?  429  TYR   A CE2 1 
ATOM   3421  C  CZ  . TYR   A 1 429  ? 4.64300    95.24600  27.71100  1.000 46.83616  ?  429  TYR   A CZ  1 
ATOM   3422  O  OH  . TYR   A 1 429  ? 4.62400    95.34600  29.08300  1.000 51.33410  ?  429  TYR   A OH  1 
ATOM   3423  N  N   . CYS   A 1 430  ? 4.01400    91.95600  22.81000  1.000 34.77639  ?  430  CYS   A N   1 
ATOM   3424  C  CA  . CYS   A 1 430  ? 3.50000    90.65400  23.22400  1.000 47.70055  ?  430  CYS   A CA  1 
ATOM   3425  C  C   . CYS   A 1 430  ? 4.53100    89.55700  22.99600  1.000 40.49307  ?  430  CYS   A C   1 
ATOM   3426  O  O   . CYS   A 1 430  ? 4.78000    88.73000  23.88000  1.000 41.20964  ?  430  CYS   A O   1 
ATOM   3427  C  CB  . CYS   A 1 430  ? 2.20500    90.33700  22.47800  1.000 45.71963  ?  430  CYS   A CB  1 
ATOM   3428  S  SG  . CYS   A 1 430  ? 0.89300    91.52800  22.78300  1.000 43.22735  ?  430  CYS   A SG  1 
ATOM   3429  N  N   . ASN   A 1 431  ? 5.15100    89.54100  21.81400  1.000 44.81849  ?  431  ASN   A N   1 
ATOM   3430  C  CA  . ASN   A 1 431  ? 6.11300    88.48800  21.50600  1.000 40.71115  ?  431  ASN   A CA  1 
ATOM   3431  C  C   . ASN   A 1 431  ? 7.36300    88.58500  22.37200  1.000 41.42550  ?  431  ASN   A C   1 
ATOM   3432  O  O   . ASN   A 1 431  ? 7.94700    87.55300  22.72100  1.000 43.86151  ?  431  ASN   A O   1 
ATOM   3433  C  CB  . ASN   A 1 431  ? 6.48800    88.53000  20.02500  1.000 35.81577  ?  431  ASN   A CB  1 
ATOM   3434  C  CG  . ASN   A 1 431  ? 5.58200    87.66700  19.16100  1.000 53.21001  ?  431  ASN   A CG  1 
ATOM   3435  O  OD1 . ASN   A 1 431  ? 4.89000    86.77200  19.65500  1.000 62.70508  ?  431  ASN   A OD1 1 
ATOM   3436  N  ND2 . ASN   A 1 431  ? 5.57900    87.93700  17.86200  1.000 40.13823  ?  431  ASN   A ND2 1 
ATOM   3437  N  N   . GLN   A 1 432  ? 7.78500    89.79800  22.73800  1.000 35.96637  ?  432  GLN   A N   1 
ATOM   3438  C  CA  . GLN   A 1 432  ? 8.99800    89.96600  23.53200  1.000 45.46824  ?  432  GLN   A CA  1 
ATOM   3439  C  C   . GLN   A 1 432  ? 8.74200    89.94300  25.03300  1.000 47.52896  ?  432  GLN   A C   1 
ATOM   3440  O  O   . GLN   A 1 432  ? 9.70500    89.88300  25.80500  1.000 55.37595  ?  432  GLN   A O   1 
ATOM   3441  C  CB  . GLN   A 1 432  ? 9.71000    91.27400  23.15500  1.000 34.96262  ?  432  GLN   A CB  1 
ATOM   3442  C  CG  . GLN   A 1 432  ? 8.91200    92.53600  23.44800  1.000 52.95642  ?  432  GLN   A CG  1 
ATOM   3443  C  CD  . GLN   A 1 432  ? 9.49800    93.77100  22.78000  1.000 66.96577  ?  432  GLN   A CD  1 
ATOM   3444  O  OE1 . GLN   A 1 432  ? 9.40900    94.88600  23.30300  1.000 63.30603  ?  432  GLN   A OE1 1 
ATOM   3445  N  NE2 . GLN   A 1 432  ? 10.10200   93.57500  21.61500  1.000 45.76189  ?  432  GLN   A NE2 1 
ATOM   3446  N  N   . GLU   A 1 433  ? 7.48100    89.98500  25.46700  1.000 45.42842  ?  433  GLU   A N   1 
ATOM   3447  C  CA  . GLU   A 1 433  ? 7.14900    89.88300  26.88100  1.000 37.36842  ?  433  GLU   A CA  1 
ATOM   3448  C  C   . GLU   A 1 433  ? 6.42400    88.59400  27.23800  1.000 40.77507  ?  433  GLU   A C   1 
ATOM   3449  O  O   . GLU   A 1 433  ? 6.22600    88.32600  28.42900  1.000 40.60983  ?  433  GLU   A O   1 
ATOM   3450  C  CB  . GLU   A 1 433  ? 6.29000    91.07500  27.32400  1.000 35.42568  ?  433  GLU   A CB  1 
ATOM   3451  C  CG  . GLU   A 1 433  ? 6.90800    92.42900  27.03800  1.000 51.46792  ?  433  GLU   A CG  1 
ATOM   3452  C  CD  . GLU   A 1 433  ? 8.16100    92.67900  27.84300  1.000 60.44152  ?  433  GLU   A CD  1 
ATOM   3453  O  OE1 . GLU   A 1 433  ? 8.27100    92.13600  28.96400  1.000 55.50253  ?  433  GLU   A OE1 1 
ATOM   3454  O  OE2 . GLU   A 1 433  ? 9.04100    93.42100  27.35700  1.000 69.40341  -1 433  GLU   A OE2 1 
ATOM   3455  N  N   . GLY   A 1 434  ? 6.02400    87.79900  26.25200  1.000 41.41013  ?  434  GLY   A N   1 
ATOM   3456  C  CA  . GLY   A 1 434  ? 5.34600    86.54600  26.53100  1.000 35.85994  ?  434  GLY   A CA  1 
ATOM   3457  C  C   . GLY   A 1 434  ? 3.92300    86.70000  27.02100  1.000 43.04194  ?  434  GLY   A C   1 
ATOM   3458  O  O   . GLY   A 1 434  ? 3.49700    85.95500  27.91200  1.000 55.41759  ?  434  GLY   A O   1 
ATOM   3459  N  N   . ILE   A 1 435  ? 3.17800    87.65400  26.46600  1.000 42.07960  ?  435  ILE   A N   1 
ATOM   3460  C  CA  . ILE   A 1 435  ? 1.76800    87.81200  26.80700  1.000 37.00482  ?  435  ILE   A CA  1 
ATOM   3461  C  C   . ILE   A 1 435  ? 1.00100    86.60400  26.28200  1.000 42.53373  ?  435  ILE   A C   1 
ATOM   3462  O  O   . ILE   A 1 435  ? 0.98400    86.33900  25.07400  1.000 35.24447  ?  435  ILE   A O   1 
ATOM   3463  C  CB  . ILE   A 1 435  ? 1.21000    89.12000  26.23200  1.000 43.41344  ?  435  ILE   A CB  1 
ATOM   3464  C  CG1 . ILE   A 1 435  ? 2.09900    90.30000  26.63200  1.000 32.66250  ?  435  ILE   A CG1 1 
ATOM   3465  C  CG2 . ILE   A 1 435  ? -0.22500   89.34400  26.69800  1.000 38.06328  ?  435  ILE   A CG2 1 
ATOM   3466  C  CD1 . ILE   A 1 435  ? 2.29800    90.43600  28.12200  1.000 35.55276  ?  435  ILE   A CD1 1 
ATOM   3467  N  N   . THR   A 1 436  ? 0.35700    85.86800  27.18900  1.000 36.36565  ?  436  THR   A N   1 
ATOM   3468  C  CA  . THR   A 1 436  ? -0.27800   84.60000  26.84600  1.000 40.45912  ?  436  THR   A CA  1 
ATOM   3469  C  C   . THR   A 1 436  ? -1.78200   84.69700  26.62100  1.000 42.34152  ?  436  THR   A C   1 
ATOM   3470  O  O   . THR   A 1 436  ? -2.32800   83.90100  25.85000  1.000 36.82122  ?  436  THR   A O   1 
ATOM   3471  C  CB  . THR   A 1 436  ? -0.00900   83.56400  27.94200  1.000 34.78861  ?  436  THR   A CB  1 
ATOM   3472  O  OG1 . THR   A 1 436  ? -0.41700   84.09000  29.21200  1.000 38.92424  ?  436  THR   A OG1 1 
ATOM   3473  C  CG2 . THR   A 1 436  ? 1.46200    83.24400  27.99300  1.000 31.58664  ?  436  THR   A CG2 1 
ATOM   3474  N  N   . ILE   A 1 437  ? -2.46400   85.63900  27.26700  1.000 31.25619  ?  437  ILE   A N   1 
ATOM   3475  C  CA  . ILE   A 1 437  ? -3.92100   85.71200  27.21200  1.000 32.58777  ?  437  ILE   A CA  1 
ATOM   3476  C  C   . ILE   A 1 437  ? -4.33300   87.17500  27.28300  1.000 35.63352  ?  437  ILE   A C   1 
ATOM   3477  O  O   . ILE   A 1 437  ? -3.72400   87.96900  28.00700  1.000 40.19291  ?  437  ILE   A O   1 
ATOM   3478  C  CB  . ILE   A 1 437  ? -4.56300   84.88300  28.34900  1.000 37.82857  ?  437  ILE   A CB  1 
ATOM   3479  C  CG1 . ILE   A 1 437  ? -6.08200   84.81300  28.19300  1.000 34.93357  ?  437  ILE   A CG1 1 
ATOM   3480  C  CG2 . ILE   A 1 437  ? -4.20000   85.44800  29.71700  1.000 34.44764  ?  437  ILE   A CG2 1 
ATOM   3481  C  CD1 . ILE   A 1 437  ? -6.70600   83.65000  28.93600  1.000 30.62296  ?  437  ILE   A CD1 1 
ATOM   3482  N  N   . SER   A 1 438  ? -5.36500   87.53400  26.52000  1.000 31.03686  ?  438  SER   A N   1 
ATOM   3483  C  CA  . SER   A 1 438  ? -5.88600   88.89600  26.54400  1.000 38.20182  ?  438  SER   A CA  1 
ATOM   3484  C  C   . SER   A 1 438  ? -7.20000   88.94700  25.78400  1.000 40.51239  ?  438  SER   A C   1 
ATOM   3485  O  O   . SER   A 1 438  ? -7.52300   88.04500  25.00600  1.000 39.66320  ?  438  SER   A O   1 
ATOM   3486  C  CB  . SER   A 1 438  ? -4.89500   89.89600  25.94500  1.000 23.93760  ?  438  SER   A CB  1 
ATOM   3487  O  OG  . SER   A 1 438  ? -3.88200   90.19700  26.88500  1.000 39.94007  ?  438  SER   A OG  1 
ATOM   3488  N  N   . TYR   A 1 439  ? -7.95100   90.02000  26.02200  1.000 39.75037  ?  439  TYR   A N   1 
ATOM   3489  C  CA  . TYR   A 1 439  ? -9.19200   90.29400  25.31000  1.000 37.49021  ?  439  TYR   A CA  1 
ATOM   3490  C  C   . TYR   A 1 439  ? -8.97000   91.48200  24.38500  1.000 29.40818  ?  439  TYR   A C   1 
ATOM   3491  O  O   . TYR   A 1 439  ? -8.61900   92.57500  24.84300  1.000 34.80815  ?  439  TYR   A O   1 
ATOM   3492  C  CB  . TYR   A 1 439  ? -10.34700  90.58200  26.26900  1.000 35.90623  ?  439  TYR   A CB  1 
ATOM   3493  C  CG  . TYR   A 1 439  ? -11.44400  91.40300  25.62300  1.000 38.59385  ?  439  TYR   A CG  1 
ATOM   3494  C  CD1 . TYR   A 1 439  ? -12.23300  90.86800  24.61000  1.000 38.72788  ?  439  TYR   A CD1 1 
ATOM   3495  C  CD2 . TYR   A 1 439  ? -11.67400  92.72000  26.00400  1.000 31.38131  ?  439  TYR   A CD2 1 
ATOM   3496  C  CE1 . TYR   A 1 439  ? -13.22600  91.61700  24.00300  1.000 38.88988  ?  439  TYR   A CE1 1 
ATOM   3497  C  CE2 . TYR   A 1 439  ? -12.66500  93.47700  25.40100  1.000 25.66786  ?  439  TYR   A CE2 1 
ATOM   3498  C  CZ  . TYR   A 1 439  ? -13.43900  92.91900  24.40100  1.000 44.36572  ?  439  TYR   A CZ  1 
ATOM   3499  O  OH  . TYR   A 1 439  ? -14.42900  93.65900  23.79500  1.000 50.08278  ?  439  TYR   A OH  1 
ATOM   3500  N  N   . LEU   A 1 440  ? -9.18300   91.26400  23.09100  1.000 35.93794  ?  440  LEU   A N   1 
ATOM   3501  C  CA  . LEU   A 1 440  ? -9.07500   92.29600  22.08200  1.000 34.06453  ?  440  LEU   A CA  1 
ATOM   3502  C  C   . LEU   A 1 440  ? -10.44200  92.52500  21.45200  1.000 53.10753  ?  440  LEU   A C   1 
ATOM   3503  O  O   . LEU   A 1 440  ? -11.09600  91.55500  21.04200  1.000 58.20555  ?  440  LEU   A O   1 
ATOM   3504  C  CB  . LEU   A 1 440  ? -8.06400   91.88700  21.00300  1.000 33.25515  ?  440  LEU   A CB  1 
ATOM   3505  C  CG  . LEU   A 1 440  ? -6.71600   92.60200  21.01500  1.000 36.39080  ?  440  LEU   A CG  1 
ATOM   3506  C  CD1 . LEU   A 1 440  ? -6.12400   92.61200  22.41300  1.000 38.16178  ?  440  LEU   A CD1 1 
ATOM   3507  C  CD2 . LEU   A 1 440  ? -5.77200   91.91400  20.04700  1.000 31.55013  ?  440  LEU   A CD2 1 
ATOM   3508  N  N   . PRO   A 1 441  ? -10.92200  93.76700  21.38100  1.000 54.73474  ?  441  PRO   A N   1 
ATOM   3509  C  CA  . PRO   A 1 441  ? -12.18700  94.03200  20.68300  1.000 41.91781  ?  441  PRO   A CA  1 
ATOM   3510  C  C   . PRO   A 1 441  ? -12.14100  93.56500  19.23300  1.000 45.69289  ?  441  PRO   A C   1 
ATOM   3511  O  O   . PRO   A 1 441  ? -11.07500  93.37000  18.64500  1.000 49.62550  ?  441  PRO   A O   1 
ATOM   3512  C  CB  . PRO   A 1 441  ? -12.34100  95.55700  20.77800  1.000 40.19159  ?  441  PRO   A CB  1 
ATOM   3513  C  CG  . PRO   A 1 441  ? -11.02800  96.07300  21.31000  1.000 57.04127  ?  441  PRO   A CG  1 
ATOM   3514  C  CD  . PRO   A 1 441  ? -10.41600  94.95700  22.08200  1.000 48.43282  ?  441  PRO   A CD  1 
ATOM   3515  N  N   . THR   A 1 442  ? -13.33600  93.40500  18.65500  1.000 41.34345  ?  442  THR   A N   1 
ATOM   3516  C  CA  . THR   A 1 442  ? -13.48200  92.70700  17.37900  1.000 44.83271  ?  442  THR   A CA  1 
ATOM   3517  C  C   . THR   A 1 442  ? -12.62600  93.33400  16.28100  1.000 50.15494  ?  442  THR   A C   1 
ATOM   3518  O  O   . THR   A 1 442  ? -11.85600  92.63800  15.60900  1.000 50.12825  ?  442  THR   A O   1 
ATOM   3519  C  CB  . THR   A 1 442  ? -14.95600  92.68100  16.96700  1.000 39.38539  ?  442  THR   A CB  1 
ATOM   3520  O  OG1 . THR   A 1 442  ? -15.68400  91.81300  17.84600  1.000 33.23741  ?  442  THR   A OG1 1 
ATOM   3521  C  CG2 . THR   A 1 442  ? -15.10200  92.17800  15.54300  1.000 37.85935  ?  442  THR   A CG2 1 
ATOM   3522  N  N   . GLY   A 1 443  ? -12.74700  94.64800  16.08100  1.000 37.00478  ?  443  GLY   A N   1 
ATOM   3523  C  CA  . GLY   A 1 443  ? -12.00200  95.28700  15.00700  1.000 48.83172  ?  443  GLY   A CA  1 
ATOM   3524  C  C   . GLY   A 1 443  ? -10.50100  95.19900  15.20500  1.000 50.05446  ?  443  GLY   A C   1 
ATOM   3525  O  O   . GLY   A 1 443  ? -9.75700   94.85800  14.28200  1.000 62.08930  ?  443  GLY   A O   1 
ATOM   3526  N  N   . ALA   A 1 444  ? -10.03600  95.50300  16.41800  1.000 55.58856  ?  444  ALA   A N   1 
ATOM   3527  C  CA  . ALA   A 1 444  ? -8.61200   95.38500  16.71300  1.000 46.42233  ?  444  ALA   A CA  1 
ATOM   3528  C  C   . ALA   A 1 444  ? -8.14200   93.94200  16.59000  1.000 45.42454  ?  444  ALA   A C   1 
ATOM   3529  O  O   . ALA   A 1 444  ? -7.01900   93.68400  16.14000  1.000 50.97250  ?  444  ALA   A O   1 
ATOM   3530  C  CB  . ALA   A 1 444  ? -8.32000   95.93300  18.11000  1.000 50.59182  ?  444  ALA   A CB  1 
ATOM   3531  N  N   . ALA   A 1 445  ? -8.99100   92.98500  16.97400  1.000 44.20353  ?  445  ALA   A N   1 
ATOM   3532  C  CA  . ALA   A 1 445  ? -8.61800   91.57800  16.86900  1.000 44.57223  ?  445  ALA   A CA  1 
ATOM   3533  C  C   . ALA   A 1 445  ? -8.44300   91.16500  15.41400  1.000 48.82896  ?  445  ALA   A C   1 
ATOM   3534  O  O   . ALA   A 1 445  ? -7.44300   90.53400  15.05300  1.000 51.83050  ?  445  ALA   A O   1 
ATOM   3535  C  CB  . ALA   A 1 445  ? -9.66700   90.70200  17.55500  1.000 38.18236  ?  445  ALA   A CB  1 
ATOM   3536  N  N   . GLU   A 1 446  ? -9.40800   91.51900  14.55900  1.000 46.92572  ?  446  GLU   A N   1 
ATOM   3537  C  CA  . GLU   A 1 446  ? -9.32000   91.16700  13.14700  1.000 42.65066  ?  446  GLU   A CA  1 
ATOM   3538  C  C   . GLU   A 1 446  ? -8.09400   91.77200  12.47500  1.000 49.76290  ?  446  GLU   A C   1 
ATOM   3539  O  O   . GLU   A 1 446  ? -7.61900   91.22600  11.47300  1.000 56.60121  ?  446  GLU   A O   1 
ATOM   3540  C  CB  . GLU   A 1 446  ? -10.59300  91.60500  12.41300  1.000 56.49886  ?  446  GLU   A CB  1 
ATOM   3541  C  CG  . GLU   A 1 446  ? -11.80300  90.72600  12.69500  1.000 50.36312  ?  446  GLU   A CG  1 
ATOM   3542  C  CD  . GLU   A 1 446  ? -13.04400  91.16200  11.93500  1.000 58.21791  ?  446  GLU   A CD  1 
ATOM   3543  O  OE1 . GLU   A 1 446  ? -13.15400  92.36100  11.60400  1.000 68.20491  ?  446  GLU   A OE1 1 
ATOM   3544  O  OE2 . GLU   A 1 446  ? -13.91800  90.30400  11.67800  1.000 55.47592  -1 446  GLU   A OE2 1 
ATOM   3545  N  N   . GLN   A 1 447  ? -7.57400   92.88200  13.00100  1.000 52.91108  ?  447  GLN   A N   1 
ATOM   3546  C  CA  . GLN   A 1 447  ? -6.34200   93.48000  12.50300  1.000 44.61129  ?  447  GLN   A CA  1 
ATOM   3547  C  C   . GLN   A 1 447  ? -5.10200   92.99600  13.24000  1.000 58.03569  ?  447  GLN   A C   1 
ATOM   3548  O  O   . GLN   A 1 447  ? -3.98800   93.36200  12.85400  1.000 70.95122  ?  447  GLN   A O   1 
ATOM   3549  C  CB  . GLN   A 1 447  ? -6.42500   95.00600  12.58800  1.000 40.95514  ?  447  GLN   A CB  1 
ATOM   3550  C  CG  . GLN   A 1 447  ? -7.52300   95.58600  11.72300  1.000 61.12121  ?  447  GLN   A CG  1 
ATOM   3551  C  CD  . GLN   A 1 447  ? -7.33900   97.06200  11.45600  1.000 78.06227  ?  447  GLN   A CD  1 
ATOM   3552  O  OE1 . GLN   A 1 447  ? -6.32000   97.64900  11.82200  1.000 64.91914  ?  447  GLN   A OE1 1 
ATOM   3553  N  NE2 . GLN   A 1 447  ? -8.31400   97.66600  10.78300  1.000 58.46768  ?  447  GLN   A NE2 1 
ATOM   3554  N  N   . PHE   A 1 448  ? -5.26700   92.19800  14.29100  1.000 55.10085  ?  448  PHE   A N   1 
ATOM   3555  C  CA  . PHE   A 1 448  ? -4.14300   91.54900  14.94800  1.000 43.11528  ?  448  PHE   A CA  1 
ATOM   3556  C  C   . PHE   A 1 448  ? -3.90900   90.14200  14.42400  1.000 50.66944  ?  448  PHE   A C   1 
ATOM   3557  O  O   . PHE   A 1 448  ? -2.81600   89.59500  14.61700  1.000 43.86424  ?  448  PHE   A O   1 
ATOM   3558  C  CB  . PHE   A 1 448  ? -4.37300   91.51300  16.46400  1.000 42.46860  ?  448  PHE   A CB  1 
ATOM   3559  C  CG  . PHE   A 1 448  ? -3.19000   91.01700  17.25800  1.000 44.67733  ?  448  PHE   A CG  1 
ATOM   3560  C  CD1 . PHE   A 1 448  ? -2.13100   91.86000  17.55500  1.000 35.47999  ?  448  PHE   A CD1 1 
ATOM   3561  C  CD2 . PHE   A 1 448  ? -3.15200   89.71100  17.72700  1.000 45.89452  ?  448  PHE   A CD2 1 
ATOM   3562  C  CE1 . PHE   A 1 448  ? -1.04800   91.40500  18.29200  1.000 43.69759  ?  448  PHE   A CE1 1 
ATOM   3563  C  CE2 . PHE   A 1 448  ? -2.07300   89.25100  18.46500  1.000 37.86264  ?  448  PHE   A CE2 1 
ATOM   3564  C  CZ  . PHE   A 1 448  ? -1.02000   90.09800  18.74800  1.000 36.21745  ?  448  PHE   A CZ  1 
ATOM   3565  N  N   . MET   A 1 449  ? -4.90600   89.55100  13.75700  1.000 46.14764  ?  449  MET   A N   1 
ATOM   3566  C  CA  . MET   A 1 449  ? -4.75000   88.21100  13.20400  1.000 55.79444  ?  449  MET   A CA  1 
ATOM   3567  C  C   . MET   A 1 449  ? -3.76200   88.17800  12.05000  1.000 54.36503  ?  449  MET   A C   1 
ATOM   3568  O  O   . MET   A 1 449  ? -3.27000   87.09900  11.70400  1.000 58.67037  ?  449  MET   A O   1 
ATOM   3569  C  CB  . MET   A 1 449  ? -6.10400   87.66300  12.74700  1.000 53.69899  ?  449  MET   A CB  1 
ATOM   3570  C  CG  . MET   A 1 449  ? -7.17900   87.71200  13.82100  1.000 63.85251  ?  449  MET   A CG  1 
ATOM   3571  S  SD  . MET   A 1 449  ? -8.66000   86.74700  13.45600  1.000 60.25296  ?  449  MET   A SD  1 
ATOM   3572  C  CE  . MET   A 1 449  ? -9.89400   87.68100  14.35900  1.000 42.21928  ?  449  MET   A CE  1 
ATOM   3573  N  N   . GLN   A 1 450  ? -3.46000   89.32900  11.44900  1.000 50.33799  ?  450  GLN   A N   1 
ATOM   3574  C  CA  . GLN   A 1 450  ? -2.46600   89.36700  10.38500  1.000 59.87892  ?  450  GLN   A CA  1 
ATOM   3575  C  C   . GLN   A 1 450  ? -1.04400   89.36700  10.93300  1.000 60.63478  ?  450  GLN   A C   1 
ATOM   3576  O  O   . GLN   A 1 450  ? -0.14100   88.81900  10.28900  1.000 68.78667  ?  450  GLN   A O   1 
ATOM   3577  C  CB  . GLN   A 1 450  ? -2.69100   90.59000  9.49600   1.000 64.73618  ?  450  GLN   A CB  1 
ATOM   3578  C  CG  . GLN   A 1 450  ? -3.25500   91.79200  10.23300  1.000 72.78371  ?  450  GLN   A CG  1 
ATOM   3579  C  CD  . GLN   A 1 450  ? -2.98500   93.10200  9.51500   1.000 89.09916  ?  450  GLN   A CD  1 
ATOM   3580  O  OE1 . GLN   A 1 450  ? -2.18000   93.16100  8.58400   1.000 94.84094  ?  450  GLN   A OE1 1 
ATOM   3581  N  NE2 . GLN   A 1 450  ? -3.65700   94.16300  9.95000   1.000 60.96633  ?  450  GLN   A NE2 1 
ATOM   3582  N  N   . MET   A 1 451  ? -0.82400   89.95900  12.10600  1.000 48.61373  ?  451  MET   A N   1 
ATOM   3583  C  CA  . MET   A 1 451  ? 0.50700    89.98100  12.70000  1.000 42.94789  ?  451  MET   A CA  1 
ATOM   3584  C  C   . MET   A 1 451  ? 0.96200    88.57200  13.06800  1.000 48.58514  ?  451  MET   A C   1 
ATOM   3585  O  O   . MET   A 1 451  ? 0.15300    87.68100  13.33400  1.000 53.12481  ?  451  MET   A O   1 
ATOM   3586  C  CB  . MET   A 1 451  ? 0.53300    90.87000  13.94300  1.000 42.72862  ?  451  MET   A CB  1 
ATOM   3587  C  CG  . MET   A 1 451  ? -0.21300   92.18900  13.80600  1.000 55.83763  ?  451  MET   A CG  1 
ATOM   3588  S  SD  . MET   A 1 451  ? -0.02500   92.95100  12.18500  1.000 65.77673  ?  451  MET   A SD  1 
ATOM   3589  C  CE  . MET   A 1 451  ? 1.72000    93.34400  12.17900  1.000 65.20661  ?  451  MET   A CE  1 
ATOM   3590  N  N   . ASP   A 1 452  ? 2.28000    88.38100  13.08500  1.000 60.09375  ?  452  ASP   A N   1 
ATOM   3591  C  CA  . ASP   A 1 452  ? 2.87800    87.08200  13.37700  1.000 58.61667  ?  452  ASP   A CA  1 
ATOM   3592  C  C   . ASP   A 1 452  ? 3.17300    87.00100  14.87100  1.000 53.33612  ?  452  ASP   A C   1 
ATOM   3593  O  O   . ASP   A 1 452  ? 4.11600    87.63200  15.36000  1.000 54.67709  ?  452  ASP   A O   1 
ATOM   3594  C  CB  . ASP   A 1 452  ? 4.14600    86.87400  12.55300  1.000 47.76838  ?  452  ASP   A CB  1 
ATOM   3595  C  CG  . ASP   A 1 452  ? 4.42400    85.41000  12.27500  1.000 80.80548  ?  452  ASP   A CG  1 
ATOM   3596  O  OD1 . ASP   A 1 452  ? 3.45400    84.63000  12.15400  1.000 89.75520  ?  452  ASP   A OD1 1 
ATOM   3597  O  OD2 . ASP   A 1 452  ? 5.61300    85.03800  12.18000  1.000 91.05976  -1 452  ASP   A OD2 1 
ATOM   3598  N  N   . ASN   A 1 453  ? 2.37700    86.21800  15.59000  1.000 44.55663  ?  453  ASN   A N   1 
ATOM   3599  C  CA  . ASN   A 1 453  ? 2.47500    86.11100  17.03600  1.000 47.10525  ?  453  ASN   A CA  1 
ATOM   3600  C  C   . ASN   A 1 453  ? 2.90900    84.71100  17.44600  1.000 60.70802  ?  453  ASN   A C   1 
ATOM   3601  O  O   . ASN   A 1 453  ? 2.54600    83.71600  16.81200  1.000 54.32408  ?  453  ASN   A O   1 
ATOM   3602  C  CB  . ASN   A 1 453  ? 1.13700    86.44800  17.70000  1.000 43.57735  ?  453  ASN   A CB  1 
ATOM   3603  C  CG  . ASN   A 1 453  ? 1.26400    86.64200  19.19400  1.000 47.29591  ?  453  ASN   A CG  1 
ATOM   3604  O  OD1 . ASN   A 1 453  ? 0.97700    85.73500  19.97600  1.000 45.67680  ?  453  ASN   A OD1 1 
ATOM   3605  N  ND2 . ASN   A 1 453  ? 1.70700    87.82600  19.60100  1.000 51.49422  ?  453  ASN   A ND2 1 
ATOM   3606  N  N   . GLN   A 1 454  ? 3.69800    84.64900  18.52100  1.000 50.83504  ?  454  GLN   A N   1 
ATOM   3607  C  CA  . GLN   A 1 454  ? 4.09200    83.38700  19.12800  1.000 50.58772  ?  454  GLN   A CA  1 
ATOM   3608  C  C   . GLN   A 1 454  ? 3.81000    83.34100  20.62200  1.000 48.95356  ?  454  GLN   A C   1 
ATOM   3609  O  O   . GLN   A 1 454  ? 4.01500    82.29100  21.24100  1.000 51.42511  ?  454  GLN   A O   1 
ATOM   3610  C  CB  . GLN   A 1 454  ? 5.58500    83.11400  18.89100  1.000 57.08509  ?  454  GLN   A CB  1 
ATOM   3611  C  CG  . GLN   A 1 454  ? 6.00300    83.17500  17.43600  1.000 65.69573  ?  454  GLN   A CG  1 
ATOM   3612  C  CD  . GLN   A 1 454  ? 6.75100    84.45000  17.10600  1.000 76.76910  ?  454  GLN   A CD  1 
ATOM   3613  O  OE1 . GLN   A 1 454  ? 7.56000    84.93100  17.90000  1.000 85.12912  ?  454  GLN   A OE1 1 
ATOM   3614  N  NE2 . GLN   A 1 454  ? 6.47900    85.01000  15.93300  1.000 63.74321  ?  454  GLN   A NE2 1 
ATOM   3615  N  N   . SER   A 1 455  ? 3.34300    84.44000  21.21400  1.000 38.99687  ?  455  SER   A N   1 
ATOM   3616  C  CA  . SER   A 1 455  ? 3.17600    84.53900  22.65900  1.000 41.70663  ?  455  SER   A CA  1 
ATOM   3617  C  C   . SER   A 1 455  ? 1.79700    84.09200  23.12900  1.000 37.24606  ?  455  SER   A C   1 
ATOM   3618  O  O   . SER   A 1 455  ? 1.68800    83.39200  24.14100  1.000 38.56664  ?  455  SER   A O   1 
ATOM   3619  C  CB  . SER   A 1 455  ? 3.43000    85.97800  23.11300  1.000 41.82321  ?  455  SER   A CB  1 
ATOM   3620  O  OG  . SER   A 1 455  ? 2.40600    86.84300  22.65000  1.000 33.70136  ?  455  SER   A OG  1 
ATOM   3621  N  N   . PHE   A 1 456  ? 0.74300    84.48300  22.41800  1.000 39.21904  ?  456  PHE   A N   1 
ATOM   3622  C  CA  . PHE   A 1 456  ? -0.61100   84.20100  22.87200  1.000 37.97206  ?  456  PHE   A CA  1 
ATOM   3623  C  C   . PHE   A 1 456  ? -0.94900   82.72200  22.73100  1.000 36.30399  ?  456  PHE   A C   1 
ATOM   3624  O  O   . PHE   A 1 456  ? -0.59500   82.07400  21.74100  1.000 45.93283  ?  456  PHE   A O   1 
ATOM   3625  C  CB  . PHE   A 1 456  ? -1.62300   85.03000  22.08000  1.000 32.13882  ?  456  PHE   A CB  1 
ATOM   3626  C  CG  . PHE   A 1 456  ? -1.72600   86.45800  22.52800  1.000 25.12683  ?  456  PHE   A CG  1 
ATOM   3627  C  CD1 . PHE   A 1 456  ? -2.34800   86.77800  23.72200  1.000 35.06926  ?  456  PHE   A CD1 1 
ATOM   3628  C  CD2 . PHE   A 1 456  ? -1.22500   87.48400  21.74300  1.000 32.79984  ?  456  PHE   A CD2 1 
ATOM   3629  C  CE1 . PHE   A 1 456  ? -2.45200   88.09200  24.13800  1.000 32.55126  ?  456  PHE   A CE1 1 
ATOM   3630  C  CE2 . PHE   A 1 456  ? -1.32800   88.80200  22.15200  1.000 35.32408  ?  456  PHE   A CE2 1 
ATOM   3631  C  CZ  . PHE   A 1 456  ? -1.94300   89.10600  23.35200  1.000 20.54006  ?  456  PHE   A CZ  1 
ATOM   3632  N  N   . ARG   A 1 457  ? -1.64100   82.18700  23.73900  1.000 34.22908  ?  457  ARG   A N   1 
ATOM   3633  C  CA  . ARG   A 1 457  ? -2.29800   80.89300  23.63200  1.000 42.01495  ?  457  ARG   A CA  1 
ATOM   3634  C  C   . ARG   A 1 457  ? -3.80900   81.00900  23.53900  1.000 39.57283  ?  457  ARG   A C   1 
ATOM   3635  O  O   . ARG   A 1 457  ? -4.45300   80.10200  23.00100  1.000 41.20515  ?  457  ARG   A O   1 
ATOM   3636  C  CB  . ARG   A 1 457  ? -1.94200   80.00200  24.83300  1.000 16.69226  ?  457  ARG   A CB  1 
ATOM   3637  C  CG  . ARG   A 1 457  ? -2.26400   80.62200  26.18100  1.000 30.91639  ?  457  ARG   A CG  1 
ATOM   3638  C  CD  . ARG   A 1 457  ? -2.03500   79.63900  27.31900  1.000 29.90010  ?  457  ARG   A CD  1 
ATOM   3639  N  NE  . ARG   A 1 457  ? -2.59900   80.12900  28.57100  1.000 39.87787  ?  457  ARG   A NE  1 
ATOM   3640  C  CZ  . ARG   A 1 457  ? -3.83300   79.87700  28.98600  1.000 35.64250  ?  457  ARG   A CZ  1 
ATOM   3641  N  NH1 . ARG   A 1 457  ? -4.66200   79.13100  28.27400  1.000 30.43217  ?  457  ARG   A NH1 1 
ATOM   3642  N  NH2 . ARG   A 1 457  ? -4.24500   80.38800  30.14300  1.000 23.54537  ?  457  ARG   A NH2 1 
ATOM   3643  N  N   . VAL   A 1 458  ? -4.38000   82.10000  24.04400  1.000 32.35201  ?  458  VAL   A N   1 
ATOM   3644  C  CA  . VAL   A 1 458  ? -5.81500   82.34600  24.02200  1.000 27.78331  ?  458  VAL   A CA  1 
ATOM   3645  C  C   . VAL   A 1 458  ? -6.02900   83.82400  23.74100  1.000 33.88681  ?  458  VAL   A C   1 
ATOM   3646  O  O   . VAL   A 1 458  ? -5.43500   84.67800  24.40800  1.000 31.90275  ?  458  VAL   A O   1 
ATOM   3647  C  CB  . VAL   A 1 458  ? -6.48600   81.95100  25.35200  1.000 30.87444  ?  458  VAL   A CB  1 
ATOM   3648  C  CG1 . VAL   A 1 458  ? -7.87300   82.57400  25.45700  1.000 26.86199  ?  458  VAL   A CG1 1 
ATOM   3649  C  CG2 . VAL   A 1 458  ? -6.55500   80.43800  25.48700  1.000 37.50752  ?  458  VAL   A CG2 1 
ATOM   3650  N  N   . VAL   A 1 459  ? -6.86500   84.12700  22.75100  1.000 41.09690  ?  459  VAL   A N   1 
ATOM   3651  C  CA  . VAL   A 1 459  ? -7.27300   85.49400  22.45200  1.000 35.02920  ?  459  VAL   A CA  1 
ATOM   3652  C  C   . VAL   A 1 459  ? -8.79200   85.52600  22.38300  1.000 37.08910  ?  459  VAL   A C   1 
ATOM   3653  O  O   . VAL   A 1 459  ? -9.39100   84.89000  21.50800  1.000 41.14113  ?  459  VAL   A O   1 
ATOM   3654  C  CB  . VAL   A 1 459  ? -6.66500   86.01500  21.14000  1.000 21.86331  ?  459  VAL   A CB  1 
ATOM   3655  C  CG1 . VAL   A 1 459  ? -7.32700   87.32100  20.74500  1.000 13.33448  ?  459  VAL   A CG1 1 
ATOM   3656  C  CG2 . VAL   A 1 459  ? -5.17200   86.20300  21.29300  1.000 26.91870  ?  459  VAL   A CG2 1 
ATOM   3657  N  N   . ILE   A 1 460  ? -9.41100   86.26700  23.29800  1.000 44.94564  ?  460  ILE   A N   1 
ATOM   3658  C  CA  . ILE   A 1 460  ? -10.85800  86.43900  23.34400  1.000 30.92813  ?  460  ILE   A CA  1 
ATOM   3659  C  C   . ILE   A 1 460  ? -11.22300  87.73100  22.63300  1.000 28.98567  ?  460  ILE   A C   1 
ATOM   3660  O  O   . ILE   A 1 460  ? -10.54300  88.75400  22.78900  1.000 38.24710  ?  460  ILE   A O   1 
ATOM   3661  C  CB  . ILE   A 1 460  ? -11.36600  86.45000  24.79900  1.000 34.45401  ?  460  ILE   A CB  1 
ATOM   3662  C  CG1 . ILE   A 1 460  ? -10.83700  85.23600  25.55600  1.000 35.82764  ?  460  ILE   A CG1 1 
ATOM   3663  C  CG2 . ILE   A 1 460  ? -12.88100  86.47800  24.84800  1.000 44.83177  ?  460  ILE   A CG2 1 
ATOM   3664  C  CD1 . ILE   A 1 460  ? -10.05500  85.59500  26.78300  1.000 40.66501  ?  460  ILE   A CD1 1 
ATOM   3665  N  N   . THR   A 1 461  ? -12.30000  87.69500  21.85400  1.000 29.42129  ?  461  THR   A N   1 
ATOM   3666  C  CA  . THR   A 1 461  ? -12.79600  88.87600  21.16500  1.000 35.48357  ?  461  THR   A CA  1 
ATOM   3667  C  C   . THR   A 1 461  ? -14.30500  88.98900  21.35100  1.000 35.95592  ?  461  THR   A C   1 
ATOM   3668  O  O   . THR   A 1 461  ? -14.96600  88.08100  21.86400  1.000 31.46047  ?  461  THR   A O   1 
ATOM   3669  C  CB  . THR   A 1 461  ? -12.43500  88.84500  19.67400  1.000 37.19477  ?  461  THR   A CB  1 
ATOM   3670  O  OG1 . THR   A 1 461  ? -12.72000  90.12100  19.08700  1.000 34.33945  ?  461  THR   A OG1 1 
ATOM   3671  C  CG2 . THR   A 1 461  ? -13.22400  87.75900  18.95500  1.000 38.39141  ?  461  THR   A CG2 1 
ATOM   3672  N  N   . GLY   A 1 462  ? -14.84500  90.12300  20.93000  1.000 36.12726  ?  462  GLY   A N   1 
ATOM   3673  C  CA  . GLY   A 1 462  ? -16.25600  90.40700  21.10300  1.000 35.23051  ?  462  GLY   A CA  1 
ATOM   3674  C  C   . GLY   A 1 462  ? -16.51000  91.89500  21.07300  1.000 41.27149  ?  462  GLY   A C   1 
ATOM   3675  O  O   . GLY   A 1 462  ? -15.59200  92.71200  21.12500  1.000 50.03178  ?  462  GLY   A O   1 
ATOM   3676  N  N   . GLY   A 1 463  ? -17.79100  92.23900  20.99100  1.000 52.37720  ?  463  GLY   A N   1 
ATOM   3677  C  CA  . GLY   A 1 463  ? -18.18500  93.63000  20.87600  1.000 50.75419  ?  463  GLY   A CA  1 
ATOM   3678  C  C   . GLY   A 1 463  ? -18.95400  93.89800  19.60000  1.000 42.70628  ?  463  GLY   A C   1 
ATOM   3679  O  O   . GLY   A 1 463  ? -20.09600  94.36400  19.63900  1.000 79.35698  ?  463  GLY   A O   1 
ATOM   3680  N  N   . ASP   A 1 464  ? -18.33100  93.61200  18.45900  1.000 40.12834  ?  464  ASP   A N   1 
ATOM   3681  C  CA  . ASP   A 1 464  ? -18.99000  93.64300  17.16900  1.000 42.39382  ?  464  ASP   A CA  1 
ATOM   3682  C  C   . ASP   A 1 464  ? -19.15900  92.20700  16.66800  1.000 55.98560  ?  464  ASP   A C   1 
ATOM   3683  O  O   . ASP   A 1 464  ? -19.04000  91.24700  17.44400  1.000 64.37120  ?  464  ASP   A O   1 
ATOM   3684  C  CB  . ASP   A 1 464  ? -18.19600  94.52300  16.20200  1.000 37.00457  ?  464  ASP   A CB  1 
ATOM   3685  C  CG  . ASP   A 1 464  ? -18.85200  95.86700  15.97100  1.000 52.11256  ?  464  ASP   A CG  1 
ATOM   3686  O  OD1 . ASP   A 1 464  ? -20.04200  96.01800  16.31900  1.000 78.59703  ?  464  ASP   A OD1 1 
ATOM   3687  O  OD2 . ASP   A 1 464  ? -18.18200  96.77100  15.42900  1.000 66.08078  -1 464  ASP   A OD2 1 
ATOM   3688  N  N   . VAL   A 1 465  ? -19.43400  92.05700  15.37800  1.000 52.37999  ?  465  VAL   A N   1 
ATOM   3689  C  CA  . VAL   A 1 465  ? -19.67500  90.74500  14.79100  1.000 39.72979  ?  465  VAL   A CA  1 
ATOM   3690  C  C   . VAL   A 1 465  ? -18.36500  90.21800  14.22300  1.000 33.05374  ?  465  VAL   A C   1 
ATOM   3691  O  O   . VAL   A 1 465  ? -17.78700  90.81800  13.31100  1.000 56.99922  ?  465  VAL   A O   1 
ATOM   3692  C  CB  . VAL   A 1 465  ? -20.76000  90.80800  13.70800  1.000 41.98536  ?  465  VAL   A CB  1 
ATOM   3693  C  CG1 . VAL   A 1 465  ? -20.97700  89.42900  13.11000  1.000 42.67352  ?  465  VAL   A CG1 1 
ATOM   3694  C  CG2 . VAL   A 1 465  ? -22.05600  91.35400  14.28800  1.000 33.47031  ?  465  VAL   A CG2 1 
ATOM   3695  N  N   . LEU   A 1 466  ? -17.89900  89.09500  14.76100  1.000 36.82755  ?  466  LEU   A N   1 
ATOM   3696  C  CA  . LEU   A 1 466  ? -16.67300  88.47700  14.27900  1.000 43.31304  ?  466  LEU   A CA  1 
ATOM   3697  C  C   . LEU   A 1 466  ? -16.92600  87.74900  12.96600  1.000 45.51042  ?  466  LEU   A C   1 
ATOM   3698  O  O   . LEU   A 1 466  ? -17.91600  87.02600  12.82100  1.000 53.95831  ?  466  LEU   A O   1 
ATOM   3699  C  CB  . LEU   A 1 466  ? -16.11700  87.50500  15.32000  1.000 41.07263  ?  466  LEU   A CB  1 
ATOM   3700  C  CG  . LEU   A 1 466  ? -14.75200  86.88400  15.00900  1.000 30.83452  ?  466  LEU   A CG  1 
ATOM   3701  C  CD1 . LEU   A 1 466  ? -13.65900  87.93800  15.01300  1.000 30.58786  ?  466  LEU   A CD1 1 
ATOM   3702  C  CD2 . LEU   A 1 466  ? -14.42700  85.78100  15.99700  1.000 33.40088  ?  466  LEU   A CD2 1 
ATOM   3703  N  N   . LYS   A 1 467  ? -16.02400  87.94700  12.00500  1.000 44.72422  ?  467  LYS   A N   1 
ATOM   3704  C  CA  . LYS   A 1 467  ? -16.14200  87.30300  10.70400  1.000 44.10022  ?  467  LYS   A CA  1 
ATOM   3705  C  C   . LYS   A 1 467  ? -14.85900  86.56500  10.34800  1.000 48.36704  ?  467  LYS   A C   1 
ATOM   3706  O  O   . LYS   A 1 467  ? -14.89400  85.52600  9.68100   1.000 56.31623  ?  467  LYS   A O   1 
ATOM   3707  C  CB  . LYS   A 1 467  ? -16.47500  88.33500  9.62300   1.000 32.80007  ?  467  LYS   A CB  1 
ATOM   3708  C  CG  . LYS   A 1 467  ? -17.83900  88.98300  9.77800   1.000 44.71391  ?  467  LYS   A CG  1 
ATOM   3709  C  CD  . LYS   A 1 467  ? -18.15300  89.89400  8.60200   1.000 43.40484  ?  467  LYS   A CD  1 
ATOM   3710  C  CE  . LYS   A 1 467  ? -17.19600  91.07500  8.53300   1.000 36.85260  ?  467  LYS   A CE  1 
ATOM   3711  N  NZ  . LYS   A 1 467  ? -17.65500  92.22700  9.36000   1.000 44.46414  ?  467  LYS   A NZ  1 
ATOM   3712  N  N   . LYS   A 1 468  ? -13.72400  87.09100  10.79900  1.000 52.28763  ?  468  LYS   A N   1 
ATOM   3713  C  CA  . LYS   A 1 468  ? -12.41700  86.57700  10.41300  1.000 53.43431  ?  468  LYS   A CA  1 
ATOM   3714  C  C   . LYS   A 1 468  ? -11.92400  85.55700  11.43200  1.000 47.74548  ?  468  LYS   A C   1 
ATOM   3715  O  O   . LYS   A 1 468  ? -11.88200  85.83900  12.63200  1.000 54.94060  ?  468  LYS   A O   1 
ATOM   3716  C  CB  . LYS   A 1 468  ? -11.41800  87.72800  10.29000  1.000 39.23946  ?  468  LYS   A CB  1 
ATOM   3717  C  CG  . LYS   A 1 468  ? -10.08400  87.35000  9.67800   1.000 48.17475  ?  468  LYS   A CG  1 
ATOM   3718  C  CD  . LYS   A 1 468  ? -9.34700   88.59300  9.20200   1.000 49.39413  ?  468  LYS   A CD  1 
ATOM   3719  C  CE  . LYS   A 1 468  ? -7.89700   88.29200  8.86400   1.000 64.44228  ?  468  LYS   A CE  1 
ATOM   3720  N  NZ  . LYS   A 1 468  ? -7.16000   89.52100  8.45400   1.000 70.84796  ?  468  LYS   A NZ  1 
ATOM   3721  N  N   . ILE   A 1 469  ? -11.55500  84.37400  10.95000  1.000 45.99314  ?  469  ILE   A N   1 
ATOM   3722  C  CA  . ILE   A 1 469  ? -10.97400  83.34900  11.80600  1.000 38.80894  ?  469  ILE   A CA  1 
ATOM   3723  C  C   . ILE   A 1 469  ? -9.53900   83.00900  11.42900  1.000 52.93034  ?  469  ILE   A C   1 
ATOM   3724  O  O   . ILE   A 1 469  ? -8.82000   82.42700  12.25900  1.000 53.32055  ?  469  ILE   A O   1 
ATOM   3725  C  CB  . ILE   A 1 469  ? -11.84200  82.07200  11.81300  1.000 39.40391  ?  469  ILE   A CB  1 
ATOM   3726  C  CG1 . ILE   A 1 469  ? -11.67900  81.28300  10.50900  1.000 56.11478  ?  469  ILE   A CG1 1 
ATOM   3727  C  CG2 . ILE   A 1 469  ? -13.30200  82.43400  12.01300  1.000 52.56577  ?  469  ILE   A CG2 1 
ATOM   3728  C  CD1 . ILE   A 1 469  ? -10.81500  80.03400  10.63100  1.000 60.26898  ?  469  ILE   A CD1 1 
ATOM   3729  N  N   . GLU   A 1 470  ? -9.09000   83.34600  10.22200  1.000 53.84591  ?  470  GLU   A N   1 
ATOM   3730  C  CA  . GLU   A 1 470  ? -7.73000   83.04600  9.79900   1.000 53.30814  ?  470  GLU   A CA  1 
ATOM   3731  C  C   . GLU   A 1 470  ? -6.75700   84.00800  10.46600  1.000 54.31040  ?  470  GLU   A C   1 
ATOM   3732  O  O   . GLU   A 1 470  ? -6.94700   85.22700  10.42000  1.000 63.44361  ?  470  GLU   A O   1 
ATOM   3733  C  CB  . GLU   A 1 470  ? -7.61400   83.14100  8.27800   1.000 63.76340  ?  470  GLU   A CB  1 
ATOM   3734  C  CG  . GLU   A 1 470  ? -8.63300   82.29600  7.53500   1.000 77.76714  ?  470  GLU   A CG  1 
ATOM   3735  C  CD  . GLU   A 1 470  ? -8.04200   81.59100  6.33200   1.000 101.55203 ?  470  GLU   A CD  1 
ATOM   3736  O  OE1 . GLU   A 1 470  ? -6.95500   80.99100  6.47100   1.000 120.80864 ?  470  GLU   A OE1 1 
ATOM   3737  O  OE2 . GLU   A 1 470  ? -8.66600   81.63400  5.25100   1.000 97.22450  -1 470  GLU   A OE2 1 
ATOM   3738  N  N   . ARG   A 1 471  ? -5.71300   83.46000  11.07900  1.000 57.55643  ?  471  ARG   A N   1 
ATOM   3739  C  CA  . ARG   A 1 471  ? -4.79300   84.25600  11.87400  1.000 57.54087  ?  471  ARG   A CA  1 
ATOM   3740  C  C   . ARG   A 1 471  ? -3.37800   83.71400  11.73100  1.000 64.49123  ?  471  ARG   A C   1 
ATOM   3741  O  O   . ARG   A 1 471  ? -3.17000   82.51900  11.50100  1.000 54.62419  ?  471  ARG   A O   1 
ATOM   3742  C  CB  . ARG   A 1 471  ? -5.20600   84.26700  13.35200  1.000 51.83363  ?  471  ARG   A CB  1 
ATOM   3743  C  CG  . ARG   A 1 471  ? -5.55000   82.89200  13.90700  1.000 49.06299  ?  471  ARG   A CG  1 
ATOM   3744  C  CD  . ARG   A 1 471  ? -6.69800   82.97500  14.89800  1.000 41.53979  ?  471  ARG   A CD  1 
ATOM   3745  N  NE  . ARG   A 1 471  ? -6.80000   81.78800  15.73800  1.000 40.08026  ?  471  ARG   A NE  1 
ATOM   3746  C  CZ  . ARG   A 1 471  ? -7.61100   80.76700  15.49500  1.000 50.66283  ?  471  ARG   A CZ  1 
ATOM   3747  N  NH1 . ARG   A 1 471  ? -8.39400   80.74500  14.42800  1.000 41.37929  ?  471  ARG   A NH1 1 
ATOM   3748  N  NH2 . ARG   A 1 471  ? -7.63500   79.74100  16.34200  1.000 48.27710  ?  471  ARG   A NH2 1 
ATOM   3749  N  N   . ASN   A 1 472  ? -2.40400   84.61600  11.87000  1.000 56.14759  ?  472  ASN   A N   1 
ATOM   3750  C  CA  . ASN   A 1 472  ? -0.98900   84.24800  11.86400  1.000 55.25278  ?  472  ASN   A CA  1 
ATOM   3751  C  C   . ASN   A 1 472  ? -0.54000   84.06300  13.31000  1.000 54.98451  ?  472  ASN   A C   1 
ATOM   3752  O  O   . ASN   A 1 472  ? 0.15000    84.89700  13.90000  1.000 66.55279  ?  472  ASN   A O   1 
ATOM   3753  C  CB  . ASN   A 1 472  ? -0.16000   85.30500  11.14500  1.000 52.72492  ?  472  ASN   A CB  1 
ATOM   3754  C  CG  . ASN   A 1 472  ? -0.13900   85.10800  9.64500   1.000 64.45330  ?  472  ASN   A CG  1 
ATOM   3755  O  OD1 . ASN   A 1 472  ? 0.08600    84.00100  9.15600   1.000 74.28389  ?  472  ASN   A OD1 1 
ATOM   3756  N  ND2 . ASN   A 1 472  ? -0.37300   86.18600  8.90400   1.000 55.46857  ?  472  ASN   A ND2 1 
ATOM   3757  N  N   . GLY   A 1 473  ? -0.95200   82.94400  13.89100  1.000 47.60546  ?  473  GLY   A N   1 
ATOM   3758  C  CA  . GLY   A 1 473  ? -0.58800   82.65200  15.26400  1.000 39.88031  ?  473  GLY   A CA  1 
ATOM   3759  C  C   . GLY   A 1 473  ? -1.02900   81.25800  15.64200  1.000 53.67309  ?  473  GLY   A C   1 
ATOM   3760  O  O   . GLY   A 1 473  ? -1.75000   80.58400  14.90100  1.000 69.52213  ?  473  GLY   A O   1 
ATOM   3761  N  N   . THR   A 1 474  ? -0.57900   80.83400  16.82300  1.000 51.11918  ?  474  THR   A N   1 
ATOM   3762  C  CA  . THR   A 1 474  ? -0.91100   79.52400  17.36700  1.000 56.43647  ?  474  THR   A CA  1 
ATOM   3763  C  C   . THR   A 1 474  ? -1.90200   79.61000  18.52200  1.000 56.52192  ?  474  THR   A C   1 
ATOM   3764  O  O   . THR   A 1 474  ? -1.95800   78.69900  19.35400  1.000 67.48913  ?  474  THR   A O   1 
ATOM   3765  C  CB  . THR   A 1 474  ? 0.35800    78.80200  17.82100  1.000 47.94283  ?  474  THR   A CB  1 
ATOM   3766  O  OG1 . THR   A 1 474  ? 1.27800    79.75100  18.37600  1.000 72.97267  ?  474  THR   A OG1 1 
ATOM   3767  C  CG2 . THR   A 1 474  ? 1.01200    78.09700  16.64700  1.000 54.27449  ?  474  THR   A CG2 1 
ATOM   3768  N  N   . TYR   A 1 475  ? -2.68800   80.68000  18.59100  1.000 45.92217  ?  475  TYR   A N   1 
ATOM   3769  C  CA  . TYR   A 1 475  ? -3.59100   80.90200  19.71000  1.000 40.89761  ?  475  TYR   A CA  1 
ATOM   3770  C  C   . TYR   A 1 475  ? -5.01800   80.49700  19.35800  1.000 54.27107  ?  475  TYR   A C   1 
ATOM   3771  O  O   . TYR   A 1 475  ? -5.43100   80.54700  18.19600  1.000 58.32024  ?  475  TYR   A O   1 
ATOM   3772  C  CB  . TYR   A 1 475  ? -3.56500   82.36700  20.14800  1.000 35.99529  ?  475  TYR   A CB  1 
ATOM   3773  C  CG  . TYR   A 1 475  ? -3.72700   83.37200  19.02700  1.000 40.90726  ?  475  TYR   A CG  1 
ATOM   3774  C  CD1 . TYR   A 1 475  ? -4.98900   83.75500  18.58400  1.000 41.13922  ?  475  TYR   A CD1 1 
ATOM   3775  C  CD2 . TYR   A 1 475  ? -2.62000   83.96000  18.43200  1.000 48.75116  ?  475  TYR   A CD2 1 
ATOM   3776  C  CE1 . TYR   A 1 475  ? -5.13800   84.68400  17.56900  1.000 35.59551  ?  475  TYR   A CE1 1 
ATOM   3777  C  CE2 . TYR   A 1 475  ? -2.76000   84.88800  17.41800  1.000 49.89299  ?  475  TYR   A CE2 1 
ATOM   3778  C  CZ  . TYR   A 1 475  ? -4.01800   85.24700  16.99100  1.000 33.92045  ?  475  TYR   A CZ  1 
ATOM   3779  O  OH  . TYR   A 1 475  ? -4.14700   86.17200  15.98200  1.000 45.01194  ?  475  TYR   A OH  1 
ATOM   3780  N  N   . LYS   A 1 476  ? -5.76900   80.09500  20.38100  1.000 39.07200  ?  476  LYS   A N   1 
ATOM   3781  C  CA  . LYS   A 1 476  ? -7.18000   79.77600  20.21200  1.000 41.32411  ?  476  LYS   A CA  1 
ATOM   3782  C  C   . LYS   A 1 476  ? -8.00800   81.05500  20.17600  1.000 46.82189  ?  476  LYS   A C   1 
ATOM   3783  O  O   . LYS   A 1 476  ? -7.73000   82.01200  20.90500  1.000 42.69721  ?  476  LYS   A O   1 
ATOM   3784  C  CB  . LYS   A 1 476  ? -7.66200   78.86600  21.34100  1.000 22.13585  ?  476  LYS   A CB  1 
ATOM   3785  C  CG  . LYS   A 1 476  ? -6.77800   77.65100  21.54500  1.000 36.58269  ?  476  LYS   A CG  1 
ATOM   3786  C  CD  . LYS   A 1 476  ? -7.53200   76.48600  22.16700  1.000 34.87024  ?  476  LYS   A CD  1 
ATOM   3787  C  CE  . LYS   A 1 476  ? -7.56400   76.59000  23.68400  1.000 55.17063  ?  476  LYS   A CE  1 
ATOM   3788  N  NZ  . LYS   A 1 476  ? -7.73800   75.25300  24.32100  1.000 47.32281  ?  476  LYS   A NZ  1 
ATOM   3789  N  N   . LEU   A 1 477  ? -9.02300   81.07000  19.31700  1.000 38.21493  ?  477  LEU   A N   1 
ATOM   3790  C  CA  . LEU   A 1 477  ? -9.88300   82.23400  19.14300  1.000 40.86345  ?  477  LEU   A CA  1 
ATOM   3791  C  C   . LEU   A 1 477  ? -11.21300  82.00300  19.84600  1.000 42.99343  ?  477  LEU   A C   1 
ATOM   3792  O  O   . LEU   A 1 477  ? -11.88200  80.99200  19.60700  1.000 41.03891  ?  477  LEU   A O   1 
ATOM   3793  C  CB  . LEU   A 1 477  ? -10.11600  82.52900  17.66000  1.000 35.60489  ?  477  LEU   A CB  1 
ATOM   3794  C  CG  . LEU   A 1 477  ? -10.84200  83.83400  17.33500  1.000 42.11033  ?  477  LEU   A CG  1 
ATOM   3795  C  CD1 . LEU   A 1 477  ? -10.14300  85.00900  18.00200  1.000 40.76751  ?  477  LEU   A CD1 1 
ATOM   3796  C  CD2 . LEU   A 1 477  ? -10.92300  84.03400  15.82900  1.000 30.66049  ?  477  LEU   A CD2 1 
ATOM   3797  N  N   . TYR   A 1 478  ? -11.59400  82.94200  20.70600  1.000 35.49056  ?  478  TYR   A N   1 
ATOM   3798  C  CA  . TYR   A 1 478  ? -12.83700  82.86000  21.45400  1.000 39.06333  ?  478  TYR   A CA  1 
ATOM   3799  C  C   . TYR   A 1 478  ? -13.70000  84.07600  21.15400  1.000 38.16617  ?  478  TYR   A C   1 
ATOM   3800  O  O   . TYR   A 1 478  ? -13.20600  85.20700  21.11800  1.000 36.25139  ?  478  TYR   A O   1 
ATOM   3801  C  CB  . TYR   A 1 478  ? -12.57500  82.77300  22.95600  1.000 38.66017  ?  478  TYR   A CB  1 
ATOM   3802  C  CG  . TYR   A 1 478  ? -12.12900  81.41100  23.43700  1.000 41.09485  ?  478  TYR   A CG  1 
ATOM   3803  C  CD1 . TYR   A 1 478  ? -10.78100  81.07900  23.49600  1.000 50.60133  ?  478  TYR   A CD1 1 
ATOM   3804  C  CD2 . TYR   A 1 478  ? -13.05400  80.46200  23.84600  1.000 35.66290  ?  478  TYR   A CD2 1 
ATOM   3805  C  CE1 . TYR   A 1 478  ? -10.36900  79.83400  23.94700  1.000 44.16648  ?  478  TYR   A CE1 1 
ATOM   3806  C  CE2 . TYR   A 1 478  ? -12.65400  79.22000  24.29800  1.000 37.44920  ?  478  TYR   A CE2 1 
ATOM   3807  C  CZ  . TYR   A 1 478  ? -11.31200  78.90900  24.34500  1.000 40.73630  ?  478  TYR   A CZ  1 
ATOM   3808  O  OH  . TYR   A 1 478  ? -10.91800  77.66700  24.79500  1.000 45.46445  ?  478  TYR   A OH  1 
ATOM   3809  N  N   . ASN   A 1 479  ? -14.99100  83.83600  20.94000  1.000 32.04386  ?  479  ASN   A N   1 
ATOM   3810  C  CA  . ASN   A 1 479  ? -15.95800  84.89000  20.66400  1.000 30.44758  ?  479  ASN   A CA  1 
ATOM   3811  C  C   . ASN   A 1 479  ? -16.94200  84.96600  21.82400  1.000 37.33609  ?  479  ASN   A C   1 
ATOM   3812  O  O   . ASN   A 1 479  ? -17.58100  83.96500  22.16700  1.000 31.57821  ?  479  ASN   A O   1 
ATOM   3813  C  CB  . ASN   A 1 479  ? -16.69100  84.63000  19.34800  1.000 28.46376  ?  479  ASN   A CB  1 
ATOM   3814  C  CG  . ASN   A 1 479  ? -17.37900  85.86900  18.81000  1.000 34.02869  ?  479  ASN   A CG  1 
ATOM   3815  O  OD1 . ASN   A 1 479  ? -16.87400  86.98400  18.94100  1.000 37.56921  ?  479  ASN   A OD1 1 
ATOM   3816  N  ND2 . ASN   A 1 479  ? -18.54200  85.67800  18.19600  1.000 37.10620  ?  479  ASN   A ND2 1 
ATOM   3817  N  N   . GLY   A 1 480  ? -17.05600  86.15000  22.42400  1.000 31.58814  ?  480  GLY   A N   1 
ATOM   3818  C  CA  . GLY   A 1 480  ? -17.94600  86.36100  23.54800  1.000 28.82810  ?  480  GLY   A CA  1 
ATOM   3819  C  C   . GLY   A 1 480  ? -19.05900  87.35600  23.28500  1.000 43.99633  ?  480  GLY   A C   1 
ATOM   3820  O  O   . GLY   A 1 480  ? -18.99100  88.15200  22.34200  1.000 42.81204  ?  480  GLY   A O   1 
ATOM   3821  N  N   . TYR   A 1 481  ? -20.09600  87.31700  24.12000  1.000 42.15695  ?  481  TYR   A N   1 
ATOM   3822  C  CA  . TYR   A 1 481  ? -21.23600  88.21100  23.99400  1.000 36.14888  ?  481  TYR   A CA  1 
ATOM   3823  C  C   . TYR   A 1 481  ? -21.72800  88.59400  25.37900  1.000 32.30511  ?  481  TYR   A C   1 
ATOM   3824  O  O   . TYR   A 1 481  ? -21.71900  87.77000  26.29800  1.000 34.40009  ?  481  TYR   A O   1 
ATOM   3825  C  CB  . TYR   A 1 481  ? -22.37600  87.56400  23.19800  1.000 36.61584  ?  481  TYR   A CB  1 
ATOM   3826  C  CG  . TYR   A 1 481  ? -23.68500  88.31700  23.28400  1.000 34.30767  ?  481  TYR   A CG  1 
ATOM   3827  C  CD1 . TYR   A 1 481  ? -23.92400  89.42300  22.48000  1.000 28.73150  ?  481  TYR   A CD1 1 
ATOM   3828  C  CD2 . TYR   A 1 481  ? -24.68000  87.92500  24.17100  1.000 30.39968  ?  481  TYR   A CD2 1 
ATOM   3829  C  CE1 . TYR   A 1 481  ? -25.11300  90.11400  22.55300  1.000 28.90827  ?  481  TYR   A CE1 1 
ATOM   3830  C  CE2 . TYR   A 1 481  ? -25.87400  88.61400  24.25400  1.000 28.94380  ?  481  TYR   A CE2 1 
ATOM   3831  C  CZ  . TYR   A 1 481  ? -26.08500  89.70800  23.44100  1.000 34.02999  ?  481  TYR   A CZ  1 
ATOM   3832  O  OH  . TYR   A 1 481  ? -27.27200  90.40200  23.51100  1.000 45.47088  ?  481  TYR   A OH  1 
ATOM   3833  N  N   . GLY   A 1 482  ? -22.16400  89.84200  25.51800  1.000 35.01817  ?  482  GLY   A N   1 
ATOM   3834  C  CA  . GLY   A 1 482  ? -22.71900  90.31700  26.76100  1.000 39.91701  ?  482  GLY   A CA  1 
ATOM   3835  C  C   . GLY   A 1 482  ? -22.93500  91.81500  26.76600  1.000 38.65454  ?  482  GLY   A C   1 
ATOM   3836  O  O   . GLY   A 1 482  ? -22.14600  92.58500  26.20800  1.000 38.31232  ?  482  GLY   A O   1 
ATOM   3837  N  N   . PRO   A 1 483  ? -24.02300  92.25600  27.38700  1.000 37.80751  ?  483  PRO   A N   1 
ATOM   3838  C  CA  . PRO   A 1 483  ? -24.24200  93.69000  27.57600  1.000 35.81964  ?  483  PRO   A CA  1 
ATOM   3839  C  C   . PRO   A 1 483  ? -23.45100  94.19500  28.77200  1.000 47.18960  ?  483  PRO   A C   1 
ATOM   3840  O  O   . PRO   A 1 483  ? -23.03100  93.43000  29.63900  1.000 46.58237  ?  483  PRO   A O   1 
ATOM   3841  C  CB  . PRO   A 1 483  ? -25.75100  93.79300  27.84500  1.000 31.68583  ?  483  PRO   A CB  1 
ATOM   3842  C  CG  . PRO   A 1 483  ? -26.29100  92.36800  27.76700  1.000 32.37284  ?  483  PRO   A CG  1 
ATOM   3843  C  CD  . PRO   A 1 483  ? -25.12000  91.46300  27.95300  1.000 41.59505  ?  483  PRO   A CD  1 
ATOM   3844  N  N   . THR   A 1 484  ? -23.26000  95.51400  28.80800  1.000 33.76989  ?  484  THR   A N   1 
ATOM   3845  C  CA  . THR   A 1 484  ? -22.65500  96.13300  29.97900  1.000 24.77276  ?  484  THR   A CA  1 
ATOM   3846  C  C   . THR   A 1 484  ? -23.55100  96.01800  31.20900  1.000 37.72490  ?  484  THR   A C   1 
ATOM   3847  O  O   . THR   A 1 484  ? -23.04800  96.04500  32.33700  1.000 41.31944  ?  484  THR   A O   1 
ATOM   3848  C  CB  . THR   A 1 484  ? -22.34600  97.60000  29.68500  1.000 21.22939  ?  484  THR   A CB  1 
ATOM   3849  O  OG1 . THR   A 1 484  ? -21.70000  97.69800  28.41300  1.000 49.62404  ?  484  THR   A OG1 1 
ATOM   3850  C  CG2 . THR   A 1 484  ? -21.42000  98.17300  30.74300  1.000 34.33086  ?  484  THR   A CG2 1 
ATOM   3851  N  N   . GLU   A 1 485  ? -24.86400  95.87800  31.00900  1.000 45.04720  ?  485  GLU   A N   1 
ATOM   3852  C  CA  . GLU   A 1 485  ? -25.79600  95.77300  32.12900  1.000 37.20651  ?  485  GLU   A CA  1 
ATOM   3853  C  C   . GLU   A 1 485  ? -25.58700  94.47700  32.89800  1.000 46.66229  ?  485  GLU   A C   1 
ATOM   3854  O  O   . GLU   A 1 485  ? -25.70800  94.44800  34.12900  1.000 46.18512  ?  485  GLU   A O   1 
ATOM   3855  C  CB  . GLU   A 1 485  ? -27.23000  95.88300  31.60900  1.000 29.70922  ?  485  GLU   A CB  1 
ATOM   3856  C  CG  . GLU   A 1 485  ? -27.61800  97.29400  31.15500  1.000 42.47987  ?  485  GLU   A CG  1 
ATOM   3857  C  CD  . GLU   A 1 485  ? -27.00900  97.68700  29.81200  1.000 39.38957  ?  485  GLU   A CD  1 
ATOM   3858  O  OE1 . GLU   A 1 485  ? -26.13600  96.95100  29.30500  1.000 34.88106  ?  485  GLU   A OE1 1 
ATOM   3859  O  OE2 . GLU   A 1 485  ? -27.39300  98.74400  29.26700  1.000 42.10776  -1 485  GLU   A OE2 1 
ATOM   3860  N  N   . CYS   A 1 486  ? -25.30100  93.39500  32.19000  1.000 54.62656  ?  486  CYS   A N   1 
ATOM   3861  C  CA  . CYS   A 1 486  ? -24.72700  92.21400  32.80400  1.000 39.21848  ?  486  CYS   A CA  1 
ATOM   3862  C  C   . CYS   A 1 486  ? -23.21100  92.37800  32.82200  1.000 53.75254  ?  486  CYS   A C   1 
ATOM   3863  O  O   . CYS   A 1 486  ? -22.66200  93.32300  32.25700  1.000 75.95581  ?  486  CYS   A O   1 
ATOM   3864  C  CB  . CYS   A 1 486  ? -25.17800  90.96300  32.05600  1.000 49.87732  ?  486  CYS   A CB  1 
ATOM   3865  S  SG  . CYS   A 1 486  ? -26.97300  90.98400  31.71200  1.000 56.04506  ?  486  CYS   A SG  1 
ATOM   3866  N  N   . THR   A 1 487  ? -22.52300  91.47700  33.50400  1.000 44.52708  ?  487  THR   A N   1 
ATOM   3867  C  CA  . THR   A 1 487  ? -21.10200  91.69500  33.74800  1.000 44.33617  ?  487  THR   A CA  1 
ATOM   3868  C  C   . THR   A 1 487  ? -20.29300  91.24600  32.53800  1.000 47.53843  ?  487  THR   A C   1 
ATOM   3869  O  O   . THR   A 1 487  ? -20.14300  90.04400  32.29400  1.000 46.62915  ?  487  THR   A O   1 
ATOM   3870  C  CB  . THR   A 1 487  ? -20.66200  90.96400  35.00700  1.000 60.86274  ?  487  THR   A CB  1 
ATOM   3871  O  OG1 . THR   A 1 487  ? -21.59400  91.25800  36.04900  1.000 54.61295  ?  487  THR   A OG1 1 
ATOM   3872  C  CG2 . THR   A 1 487  ? -19.27900  91.43300  35.42600  1.000 48.86527  ?  487  THR   A CG2 1 
ATOM   3873  N  N   . ILE   A 1 488  ? -19.77900  92.21800  31.77900  1.000 36.11795  ?  488  ILE   A N   1 
ATOM   3874  C  CA  . ILE   A 1 488  ? -18.82300  91.98200  30.70100  1.000 44.55257  ?  488  ILE   A CA  1 
ATOM   3875  C  C   . ILE   A 1 488  ? -19.42500  91.08700  29.62500  1.000 48.32259  ?  488  ILE   A C   1 
ATOM   3876  O  O   . ILE   A 1 488  ? -19.80000  91.56400  28.54700  1.000 42.22815  ?  488  ILE   A O   1 
ATOM   3877  C  CB  . ILE   A 1 488  ? -17.51200  91.38500  31.24900  1.000 46.34470  ?  488  ILE   A CB  1 
ATOM   3878  C  CG1 . ILE   A 1 488  ? -16.97500  92.25000  32.39300  1.000 29.96723  ?  488  ILE   A CG1 1 
ATOM   3879  C  CG2 . ILE   A 1 488  ? -16.47300  91.24700  30.14200  1.000 36.66088  ?  488  ILE   A CG2 1 
ATOM   3880  C  CD1 . ILE   A 1 488  ? -16.18600  91.47300  33.41500  1.000 35.77089  ?  488  ILE   A CD1 1 
ATOM   3881  N  N   . MET   A 1 489  ? -19.51300  89.78500  29.90000  1.000 38.69509  ?  489  MET   A N   1 
ATOM   3882  C  CA  . MET   A 1 489  ? -19.99200  88.82100  28.91900  1.000 31.46267  ?  489  MET   A CA  1 
ATOM   3883  C  C   . MET   A 1 489  ? -20.82400  87.74500  29.60200  1.000 35.29170  ?  489  MET   A C   1 
ATOM   3884  O  O   . MET   A 1 489  ? -20.63500  87.44300  30.78400  1.000 41.20621  ?  489  MET   A O   1 
ATOM   3885  C  CB  . MET   A 1 489  ? -18.82700  88.18300  28.15500  1.000 39.72145  ?  489  MET   A CB  1 
ATOM   3886  C  CG  . MET   A 1 489  ? -18.05600  89.16800  27.29600  1.000 48.38179  ?  489  MET   A CG  1 
ATOM   3887  S  SD  . MET   A 1 489  ? -16.60500  88.44100  26.52600  1.000 43.50497  ?  489  MET   A SD  1 
ATOM   3888  C  CE  . MET   A 1 489  ? -15.86800  89.89600  25.78500  1.000 49.22549  ?  489  MET   A CE  1 
ATOM   3889  N  N   . VAL   A 1 490  ? -21.75300  87.17300  28.84000  1.000 31.52529  ?  490  VAL   A N   1 
ATOM   3890  C  CA  . VAL   A 1 490  ? -22.62300  86.11900  29.34200  1.000 24.95568  ?  490  VAL   A CA  1 
ATOM   3891  C  C   . VAL   A 1 490  ? -22.52000  84.83000  28.53600  1.000 32.74322  ?  490  VAL   A C   1 
ATOM   3892  O  O   . VAL   A 1 490  ? -22.95800  83.77500  29.02600  1.000 30.36334  ?  490  VAL   A O   1 
ATOM   3893  C  CB  . VAL   A 1 490  ? -24.09000  86.59300  29.39600  1.000 28.00358  ?  490  VAL   A CB  1 
ATOM   3894  C  CG1 . VAL   A 1 490  ? -24.24700  87.73100  30.39300  1.000 30.30474  ?  490  VAL   A CG1 1 
ATOM   3895  C  CG2 . VAL   A 1 490  ? -24.54700  87.02900  28.01900  1.000 27.43285  ?  490  VAL   A CG2 1 
ATOM   3896  N  N   . THR   A 1 491  ? -21.97100  84.86100  27.32300  1.000 29.65248  ?  491  THR   A N   1 
ATOM   3897  C  CA  . THR   A 1 491  ? -21.76400  83.65600  26.53600  1.000 38.07833  ?  491  THR   A CA  1 
ATOM   3898  C  C   . THR   A 1 491  ? -20.37000  83.69100  25.93000  1.000 35.68862  ?  491  THR   A C   1 
ATOM   3899  O  O   . THR   A 1 491  ? -19.84800  84.75800  25.60100  1.000 29.95116  ?  491  THR   A O   1 
ATOM   3900  C  CB  . THR   A 1 491  ? -22.80300  83.51100  25.42000  1.000 31.08225  ?  491  THR   A CB  1 
ATOM   3901  O  OG1 . THR   A 1 491  ? -22.94000  84.76100  24.73300  1.000 41.11026  ?  491  THR   A OG1 1 
ATOM   3902  C  CG2 . THR   A 1 491  ? -24.14300  83.10200  25.99900  1.000 36.67847  ?  491  THR   A CG2 1 
ATOM   3903  N  N   . MET   A 1 492  ? -19.77500  82.50800  25.78600  1.000 25.84716  ?  492  MET   A N   1 
ATOM   3904  C  CA  . MET   A 1 492  ? -18.46100  82.34600  25.18500  1.000 35.41775  ?  492  MET   A CA  1 
ATOM   3905  C  C   . MET   A 1 492  ? -18.50600  81.21600  24.17000  1.000 35.22382  ?  492  MET   A C   1 
ATOM   3906  O  O   . MET   A 1 492  ? -19.21500  80.22400  24.35500  1.000 43.06238  ?  492  MET   A O   1 
ATOM   3907  C  CB  . MET   A 1 492  ? -17.38700  82.05200  26.24600  1.000 33.69783  ?  492  MET   A CB  1 
ATOM   3908  C  CG  . MET   A 1 492  ? -15.96100  82.38700  25.83200  1.000 16.42867  ?  492  MET   A CG  1 
ATOM   3909  S  SD  . MET   A 1 492  ? -15.81500  84.01900  25.10300  1.000 41.19514  ?  492  MET   A SD  1 
ATOM   3910  C  CE  . MET   A 1 492  ? -15.88500  85.03900  26.57200  1.000 48.85674  ?  492  MET   A CE  1 
ATOM   3911  N  N   . PHE   A 1 493  ? -17.73400  81.37200  23.09900  1.000 32.77420  ?  493  PHE   A N   1 
ATOM   3912  C  CA  . PHE   A 1 493  ? -17.65200  80.37200  22.04500  1.000 37.78245  ?  493  PHE   A CA  1 
ATOM   3913  C  C   . PHE   A 1 493  ? -16.20700  80.25700  21.59100  1.000 42.81306  ?  493  PHE   A C   1 
ATOM   3914  O  O   . PHE   A 1 493  ? -15.53000  81.27100  21.39900  1.000 41.88319  ?  493  PHE   A O   1 
ATOM   3915  C  CB  . PHE   A 1 493  ? -18.55100  80.74200  20.85700  1.000 31.48614  ?  493  PHE   A CB  1 
ATOM   3916  C  CG  . PHE   A 1 493  ? -18.51900  79.75000  19.72600  1.000 32.81936  ?  493  PHE   A CG  1 
ATOM   3917  C  CD1 . PHE   A 1 493  ? -19.14200  78.51700  19.84500  1.000 34.68471  ?  493  PHE   A CD1 1 
ATOM   3918  C  CD2 . PHE   A 1 493  ? -17.88900  80.06200  18.53100  1.000 36.54719  ?  493  PHE   A CD2 1 
ATOM   3919  C  CE1 . PHE   A 1 493  ? -19.12300  77.60700  18.79800  1.000 36.39464  ?  493  PHE   A CE1 1 
ATOM   3920  C  CE2 . PHE   A 1 493  ? -17.86600  79.15800  17.48100  1.000 37.25067  ?  493  PHE   A CE2 1 
ATOM   3921  C  CZ  . PHE   A 1 493  ? -18.48500  77.92900  17.61500  1.000 32.41283  ?  493  PHE   A CZ  1 
ATOM   3922  N  N   . GLU   A 1 494  ? -15.73400  79.02500  21.42900  1.000 43.01988  ?  494  GLU   A N   1 
ATOM   3923  C  CA  . GLU   A 1 494  ? -14.41300  78.78200  20.86100  1.000 46.05053  ?  494  GLU   A CA  1 
ATOM   3924  C  C   . GLU   A 1 494  ? -14.57300  78.61300  19.35500  1.000 38.60298  ?  494  GLU   A C   1 
ATOM   3925  O  O   . GLU   A 1 494  ? -15.19500  77.65000  18.89300  1.000 34.35806  ?  494  GLU   A O   1 
ATOM   3926  C  CB  . GLU   A 1 494  ? -13.75000  77.55800  21.48700  1.000 38.06050  ?  494  GLU   A CB  1 
ATOM   3927  C  CG  . GLU   A 1 494  ? -12.28400  77.41100  21.09800  1.000 47.73026  ?  494  GLU   A CG  1 
ATOM   3928  C  CD  . GLU   A 1 494  ? -11.70000  76.05700  21.45400  1.000 60.78002  ?  494  GLU   A CD  1 
ATOM   3929  O  OE1 . GLU   A 1 494  ? -12.27400  75.36700  22.32400  1.000 61.77909  ?  494  GLU   A OE1 1 
ATOM   3930  O  OE2 . GLU   A 1 494  ? -10.66400  75.68400  20.86000  1.000 64.75626  -1 494  GLU   A OE2 1 
ATOM   3931  N  N   . VAL   A 1 495  ? -14.02800  79.55800  18.59200  1.000 38.30571  ?  495  VAL   A N   1 
ATOM   3932  C  CA  . VAL   A 1 495  ? -14.05400  79.48500  17.13700  1.000 36.36762  ?  495  VAL   A CA  1 
ATOM   3933  C  C   . VAL   A 1 495  ? -13.13600  78.35900  16.68400  1.000 50.55947  ?  495  VAL   A C   1 
ATOM   3934  O  O   . VAL   A 1 495  ? -11.91400  78.53100  16.61100  1.000 59.65235  ?  495  VAL   A O   1 
ATOM   3935  C  CB  . VAL   A 1 495  ? -13.64100  80.82300  16.50300  1.000 39.13639  ?  495  VAL   A CB  1 
ATOM   3936  C  CG1 . VAL   A 1 495  ? -14.08800  80.87300  15.06000  1.000 44.39390  ?  495  VAL   A CG1 1 
ATOM   3937  C  CG2 . VAL   A 1 495  ? -14.22900  81.98100  17.28900  1.000 35.30865  ?  495  VAL   A CG2 1 
ATOM   3938  N  N   . ASP   A 1 496  ? -13.72100  77.20100  16.37500  1.000 49.53245  ?  496  ASP   A N   1 
ATOM   3939  C  CA  . ASP   A 1 496  ? -12.96300  76.01800  15.99000  1.000 48.75304  ?  496  ASP   A CA  1 
ATOM   3940  C  C   . ASP   A 1 496  ? -12.84200  75.83700  14.48400  1.000 52.44397  ?  496  ASP   A C   1 
ATOM   3941  O  O   . ASP   A 1 496  ? -11.93600  75.12800  14.03200  1.000 61.65821  ?  496  ASP   A O   1 
ATOM   3942  C  CB  . ASP   A 1 496  ? -13.60700  74.76200  16.59200  1.000 59.39668  ?  496  ASP   A CB  1 
ATOM   3943  C  CG  . ASP   A 1 496  ? -15.04900  74.57000  16.14400  1.000 61.25295  ?  496  ASP   A CG  1 
ATOM   3944  O  OD1 . ASP   A 1 496  ? -15.80600  75.56400  16.12600  1.000 56.24474  ?  496  ASP   A OD1 1 
ATOM   3945  O  OD2 . ASP   A 1 496  ? -15.42700  73.42500  15.81300  1.000 71.88907  -1 496  ASP   A OD2 1 
ATOM   3946  N  N   . LYS   A 1 497  ? -13.72000  76.45500  13.70600  1.000 44.28344  ?  497  LYS   A N   1 
ATOM   3947  C  CA  . LYS   A 1 497  ? -13.76800  76.25400  12.26600  1.000 49.64973  ?  497  LYS   A CA  1 
ATOM   3948  C  C   . LYS   A 1 497  ? -14.38800  77.49100  11.64300  1.000 60.83089  ?  497  LYS   A C   1 
ATOM   3949  O  O   . LYS   A 1 497  ? -14.91400  78.35800  12.35200  1.000 62.63728  ?  497  LYS   A O   1 
ATOM   3950  C  CB  . LYS   A 1 497  ? -14.57400  74.99900  11.90700  1.000 54.10624  ?  497  LYS   A CB  1 
ATOM   3951  C  CG  . LYS   A 1 497  ? -16.05400  75.09600  12.24900  1.000 58.26118  ?  497  LYS   A CG  1 
ATOM   3952  C  CD  . LYS   A 1 497  ? -16.85000  73.94200  11.66100  1.000 62.33000  ?  497  LYS   A CD  1 
ATOM   3953  C  CE  . LYS   A 1 497  ? -17.63800  73.21200  12.74200  1.000 62.73533  ?  497  LYS   A CE  1 
ATOM   3954  N  NZ  . LYS   A 1 497  ? -18.78700  72.44700  12.18100  1.000 66.83266  ?  497  LYS   A NZ  1 
ATOM   3955  N  N   . PRO   A 1 498  ? -14.32000  77.62400  10.31800  1.000 60.78971  ?  498  PRO   A N   1 
ATOM   3956  C  CA  . PRO   A 1 498  ? -15.02800  78.73200  9.66600   1.000 49.86501  ?  498  PRO   A CA  1 
ATOM   3957  C  C   . PRO   A 1 498  ? -16.53400  78.60600  9.84200   1.000 44.24200  ?  498  PRO   A C   1 
ATOM   3958  O  O   . PRO   A 1 498  ? -17.09100  77.50600  9.85300   1.000 44.84335  ?  498  PRO   A O   1 
ATOM   3959  C  CB  . PRO   A 1 498  ? -14.61500  78.60100  8.19700   1.000 45.92855  ?  498  PRO   A CB  1 
ATOM   3960  C  CG  . PRO   A 1 498  ? -13.29500  77.91400  8.24900   1.000 50.61019  ?  498  PRO   A CG  1 
ATOM   3961  C  CD  . PRO   A 1 498  ? -13.38400  76.95600  9.39700   1.000 47.81419  ?  498  PRO   A CD  1 
ATOM   3962  N  N   . TYR   A 1 499  ? -17.18800  79.75400  9.99600   1.000 53.09545  ?  499  TYR   A N   1 
ATOM   3963  C  CA  . TYR   A 1 499  ? -18.63400  79.83100  10.13300  1.000 41.24208  ?  499  TYR   A CA  1 
ATOM   3964  C  C   . TYR   A 1 499  ? -19.14800  80.98900  9.29600   1.000 42.06728  ?  499  TYR   A C   1 
ATOM   3965  O  O   . TYR   A 1 499  ? -18.44800  81.98400  9.09000   1.000 49.94175  ?  499  TYR   A O   1 
ATOM   3966  C  CB  . TYR   A 1 499  ? -19.07300  80.04400  11.59000  1.000 44.35096  ?  499  TYR   A CB  1 
ATOM   3967  C  CG  . TYR   A 1 499  ? -18.92700  78.84400  12.49600  1.000 42.83094  ?  499  TYR   A CG  1 
ATOM   3968  C  CD1 . TYR   A 1 499  ? -19.92200  77.87700  12.56900  1.000 40.64810  ?  499  TYR   A CD1 1 
ATOM   3969  C  CD2 . TYR   A 1 499  ? -17.80300  78.68800  13.29700  1.000 43.02350  ?  499  TYR   A CD2 1 
ATOM   3970  C  CE1 . TYR   A 1 499  ? -19.79400  76.77800  13.40700  1.000 43.54542  ?  499  TYR   A CE1 1 
ATOM   3971  C  CE2 . TYR   A 1 499  ? -17.66600  77.59300  14.13600  1.000 44.24797  ?  499  TYR   A CE2 1 
ATOM   3972  C  CZ  . TYR   A 1 499  ? -18.66400  76.64200  14.18800  1.000 47.78164  ?  499  TYR   A CZ  1 
ATOM   3973  O  OH  . TYR   A 1 499  ? -18.53200  75.55300  15.02100  1.000 43.78417  ?  499  TYR   A OH  1 
ATOM   3974  N  N   . ALA   A 1 500  ? -20.38600  80.86000  8.82200   1.000 45.83690  ?  500  ALA   A N   1 
ATOM   3975  C  CA  . ALA   A 1 500  ? -21.04700  82.00300  8.20400   1.000 35.05671  ?  500  ALA   A CA  1 
ATOM   3976  C  C   . ALA   A 1 500  ? -21.49600  82.99500  9.26700   1.000 50.86715  ?  500  ALA   A C   1 
ATOM   3977  O  O   . ALA   A 1 500  ? -21.23600  84.20000  9.16200   1.000 61.64968  ?  500  ALA   A O   1 
ATOM   3978  C  CB  . ALA   A 1 500  ? -22.23000  81.53900  7.35800   1.000 57.80730  ?  500  ALA   A CB  1 
ATOM   3979  N  N   . ASN   A 1 501  ? -22.17100  82.50300  10.30000  1.000 39.80289  ?  501  ASN   A N   1 
ATOM   3980  C  CA  . ASN   A 1 501  ? -22.51600  83.28500  11.48300  1.000 40.24716  ?  501  ASN   A CA  1 
ATOM   3981  C  C   . ASN   A 1 501  ? -21.89200  82.56600  12.67200  1.000 54.76997  ?  501  ASN   A C   1 
ATOM   3982  O  O   . ASN   A 1 501  ? -22.44900  81.58400  13.17500  1.000 61.82198  ?  501  ASN   A O   1 
ATOM   3983  C  CB  . ASN   A 1 501  ? -24.02800  83.42900  11.63600  1.000 48.38819  ?  501  ASN   A CB  1 
ATOM   3984  C  CG  . ASN   A 1 501  ? -24.41300  84.30400  12.80900  1.000 38.78620  ?  501  ASN   A CG  1 
ATOM   3985  O  OD1 . ASN   A 1 501  ? -24.41900  83.85500  13.95400  1.000 57.51961  ?  501  ASN   A OD1 1 
ATOM   3986  N  ND2 . ASN   A 1 501  ? -24.73800  85.56000  12.53200  1.000 50.68777  ?  501  ASN   A ND2 1 
ATOM   3987  N  N   . ILE   A 1 502  ? -20.72700  83.04200  13.10300  1.000 44.10785  ?  502  ILE   A N   1 
ATOM   3988  C  CA  . ILE   A 1 502  ? -19.99900  82.44600  14.22100  1.000 43.07781  ?  502  ILE   A CA  1 
ATOM   3989  C  C   . ILE   A 1 502  ? -20.83500  82.55900  15.48900  1.000 45.49556  ?  502  ILE   A C   1 
ATOM   3990  O  O   . ILE   A 1 502  ? -21.18900  83.67600  15.89800  1.000 53.06325  ?  502  ILE   A O   1 
ATOM   3991  C  CB  . ILE   A 1 502  ? -18.62800  83.11000  14.40500  1.000 47.07274  ?  502  ILE   A CB  1 
ATOM   3992  C  CG1 . ILE   A 1 502  ? -18.02400  83.44900  13.04300  1.000 39.51360  ?  502  ILE   A CG1 1 
ATOM   3993  C  CG2 . ILE   A 1 502  ? -17.70300  82.19600  15.18500  1.000 54.22125  ?  502  ILE   A CG2 1 
ATOM   3994  C  CD1 . ILE   A 1 502  ? -16.57100  83.85500  13.10600  1.000 42.01247  ?  502  ILE   A CD1 1 
ATOM   3995  N  N   . PRO   A 1 503  ? -21.17100  81.44500  16.13900  1.000 37.08985  ?  503  PRO   A N   1 
ATOM   3996  C  CA  . PRO   A 1 503  ? -22.05300  81.51500  17.30800  1.000 41.51112  ?  503  PRO   A CA  1 
ATOM   3997  C  C   . PRO   A 1 503  ? -21.43100  82.33700  18.42300  1.000 43.35447  ?  503  PRO   A C   1 
ATOM   3998  O  O   . PRO   A 1 503  ? -20.21000  82.37400  18.59200  1.000 51.27525  ?  503  PRO   A O   1 
ATOM   3999  C  CB  . PRO   A 1 503  ? -22.21700  80.04700  17.72100  1.000 35.50149  ?  503  PRO   A CB  1 
ATOM   4000  C  CG  . PRO   A 1 503  ? -21.86500  79.25900  16.50100  1.000 44.01628  ?  503  PRO   A CG  1 
ATOM   4001  C  CD  . PRO   A 1 503  ? -20.81700  80.06000  15.79100  1.000 34.56373  ?  503  PRO   A CD  1 
ATOM   4002  N  N   . ILE   A 1 504  ? -22.28900  83.02000  19.18200  1.000 31.96516  ?  504  ILE   A N   1 
ATOM   4003  C  CA  . ILE   A 1 504  ? -21.79400  83.72600  20.35600  1.000 32.79918  ?  504  ILE   A CA  1 
ATOM   4004  C  C   . ILE   A 1 504  ? -21.55500  82.77000  21.51700  1.000 41.93543  ?  504  ILE   A C   1 
ATOM   4005  O  O   . ILE   A 1 504  ? -20.90600  83.14900  22.49900  1.000 49.60883  ?  504  ILE   A O   1 
ATOM   4006  C  CB  . ILE   A 1 504  ? -22.74500  84.85400  20.78500  1.000 37.85755  ?  504  ILE   A CB  1 
ATOM   4007  C  CG1 . ILE   A 1 504  ? -24.17900  84.33700  20.89200  1.000 43.91039  ?  504  ILE   A CG1 1 
ATOM   4008  C  CG2 . ILE   A 1 504  ? -22.66200  86.01600  19.80300  1.000 30.62663  ?  504  ILE   A CG2 1 
ATOM   4009  C  CD1 . ILE   A 1 504  ? -25.13400  85.34500  21.47500  1.000 30.87128  ?  504  ILE   A CD1 1 
ATOM   4010  N  N   . GLY   A 1 505  ? -22.05900  81.54600  21.43500  1.000 31.64509  ?  505  GLY   A N   1 
ATOM   4011  C  CA  . GLY   A 1 505  ? -21.69000  80.50000  22.36200  1.000 36.23551  ?  505  GLY   A CA  1 
ATOM   4012  C  C   . GLY   A 1 505  ? -22.81800  80.06600  23.27700  1.000 41.29087  ?  505  GLY   A C   1 
ATOM   4013  O  O   . GLY   A 1 505  ? -24.00600  80.24200  22.99300  1.000 36.45590  ?  505  GLY   A O   1 
ATOM   4014  N  N   . LYS   A 1 506  ? -22.42100  79.47000  24.40200  1.000 34.44655  ?  506  LYS   A N   1 
ATOM   4015  C  CA  . LYS   A 1 506  ? -23.27700  78.95200  25.45100  1.000 34.42207  ?  506  LYS   A CA  1 
ATOM   4016  C  C   . LYS   A 1 506  ? -23.14700  79.80000  26.71500  1.000 40.95161  ?  506  LYS   A C   1 
ATOM   4017  O  O   . LYS   A 1 506  ? -22.11300  80.43700  26.93600  1.000 34.71019  ?  506  LYS   A O   1 
ATOM   4018  C  CB  . LYS   A 1 506  ? -22.92400  77.49300  25.76700  1.000 30.95861  ?  506  LYS   A CB  1 
ATOM   4019  C  CG  . LYS   A 1 506  ? -23.05900  76.56400  24.56900  1.000 32.65235  ?  506  LYS   A CG  1 
ATOM   4020  C  CD  . LYS   A 1 506  ? -22.96600  75.10400  24.97700  1.000 38.16510  ?  506  LYS   A CD  1 
ATOM   4021  C  CE  . LYS   A 1 506  ? -23.17800  74.18900  23.78100  1.000 41.07742  ?  506  LYS   A CE  1 
ATOM   4022  N  NZ  . LYS   A 1 506  ? -23.52100  72.80600  24.20400  1.000 50.08415  ?  506  LYS   A NZ  1 
ATOM   4023  N  N   . PRO   A 1 507  ? -24.18400  79.84400  27.55200  1.000 52.00735  ?  507  PRO   A N   1 
ATOM   4024  C  CA  . PRO   A 1 507  ? -24.13000  80.68800  28.75200  1.000 46.60000  ?  507  PRO   A CA  1 
ATOM   4025  C  C   . PRO   A 1 507  ? -23.04700  80.23400  29.72000  1.000 45.43549  ?  507  PRO   A C   1 
ATOM   4026  O  O   . PRO   A 1 507  ? -22.63000  79.07300  29.73500  1.000 47.65058  ?  507  PRO   A O   1 
ATOM   4027  C  CB  . PRO   A 1 507  ? -25.52600  80.52400  29.36600  1.000 27.46948  ?  507  PRO   A CB  1 
ATOM   4028  C  CG  . PRO   A 1 507  ? -26.38500  80.08800  28.23900  1.000 45.39918  ?  507  PRO   A CG  1 
ATOM   4029  C  CD  . PRO   A 1 507  ? -25.51500  79.24300  27.36500  1.000 37.83630  ?  507  PRO   A CD  1 
ATOM   4030  N  N   . ILE   A 1 508  ? -22.60100  81.17900  30.54800  1.000 39.41500  ?  508  ILE   A N   1 
ATOM   4031  C  CA  . ILE   A 1 508  ? -21.51200  80.93800  31.48900  1.000 44.73096  ?  508  ILE   A CA  1 
ATOM   4032  C  C   . ILE   A 1 508  ? -22.07300  80.48100  32.83000  1.000 47.05913  ?  508  ILE   A C   1 
ATOM   4033  O  O   . ILE   A 1 508  ? -23.23700  80.07400  32.92500  1.000 51.85222  ?  508  ILE   A O   1 
ATOM   4034  C  CB  . ILE   A 1 508  ? -20.62900  82.19000  31.66100  1.000 33.47119  ?  508  ILE   A CB  1 
ATOM   4035  C  CG1 . ILE   A 1 508  ? -21.41600  83.33000  32.30900  1.000 34.86524  ?  508  ILE   A CG1 1 
ATOM   4036  C  CG2 . ILE   A 1 508  ? -20.05900  82.64000  30.32300  1.000 27.69218  ?  508  ILE   A CG2 1 
ATOM   4037  C  CD1 . ILE   A 1 508  ? -20.54200  84.48600  32.75100  1.000 26.73830  ?  508  ILE   A CD1 1 
ATOM   4038  N  N   . ASP   A 1 509  ? -21.24200  80.54200  33.87100  1.000 36.02217  ?  509  ASP   A N   1 
ATOM   4039  C  CA  . ASP   A 1 509  ? -21.64500  80.08300  35.19300  1.000 42.08100  ?  509  ASP   A CA  1 
ATOM   4040  C  C   . ASP   A 1 509  ? -22.81700  80.90100  35.72000  1.000 47.18046  ?  509  ASP   A C   1 
ATOM   4041  O  O   . ASP   A 1 509  ? -22.82900  82.13200  35.62000  1.000 43.70493  ?  509  ASP   A O   1 
ATOM   4042  C  CB  . ASP   A 1 509  ? -20.47000  80.17800  36.16900  1.000 42.78041  ?  509  ASP   A CB  1 
ATOM   4043  C  CG  . ASP   A 1 509  ? -19.51500  79.00700  36.05600  1.000 44.63347  ?  509  ASP   A CG  1 
ATOM   4044  O  OD1 . ASP   A 1 509  ? -19.80400  78.06600  35.28600  1.000 50.49205  ?  509  ASP   A OD1 1 
ATOM   4045  O  OD2 . ASP   A 1 509  ? -18.47200  79.03100  36.74200  1.000 50.82930  -1 509  ASP   A OD2 1 
ATOM   4046  N  N   . ARG   A 1 510  ? -23.80500  80.20200  36.28200  1.000 46.91896  ?  510  ARG   A N   1 
ATOM   4047  C  CA  . ARG   A 1 510  ? -24.94400  80.83500  36.94900  1.000 38.36287  ?  510  ARG   A CA  1 
ATOM   4048  C  C   . ARG   A 1 510  ? -25.63800  81.84600  36.03900  1.000 45.67048  ?  510  ARG   A C   1 
ATOM   4049  O  O   . ARG   A 1 510  ? -26.07400  82.91400  36.47600  1.000 36.75919  ?  510  ARG   A O   1 
ATOM   4050  C  CB  . ARG   A 1 510  ? -24.50800  81.49000  38.26100  1.000 29.36496  ?  510  ARG   A CB  1 
ATOM   4051  C  CG  . ARG   A 1 510  ? -24.33400  80.50700  39.40600  1.000 56.98741  ?  510  ARG   A CG  1 
ATOM   4052  C  CD  . ARG   A 1 510  ? -23.64200  81.14700  40.59600  1.000 51.60371  ?  510  ARG   A CD  1 
ATOM   4053  N  NE  . ARG   A 1 510  ? -22.21800  81.33500  40.35300  1.000 63.57237  ?  510  ARG   A NE  1 
ATOM   4054  C  CZ  . ARG   A 1 510  ? -21.25800  80.74300  41.04900  1.000 60.63354  ?  510  ARG   A CZ  1 
ATOM   4055  N  NH1 . ARG   A 1 510  ? -21.53600  79.92100  42.04800  1.000 61.90240  ?  510  ARG   A NH1 1 
ATOM   4056  N  NH2 . ARG   A 1 510  ? -19.98800  80.97800  40.73200  1.000 70.56003  ?  510  ARG   A NH2 1 
ATOM   4057  N  N   . THR   A 1 511  ? -25.74400  81.50300  34.75700  1.000 40.41487  ?  511  THR   A N   1 
ATOM   4058  C  CA  . THR   A 1 511  ? -26.31900  82.38300  33.74900  1.000 32.91011  ?  511  THR   A CA  1 
ATOM   4059  C  C   . THR   A 1 511  ? -27.17400  81.54700  32.81000  1.000 36.06890  ?  511  THR   A C   1 
ATOM   4060  O  O   . THR   A 1 511  ? -26.73800  80.48500  32.36000  1.000 44.74170  ?  511  THR   A O   1 
ATOM   4061  C  CB  . THR   A 1 511  ? -25.21900  83.11200  32.96100  1.000 35.27811  ?  511  THR   A CB  1 
ATOM   4062  O  OG1 . THR   A 1 511  ? -24.52800  84.02300  33.82400  1.000 40.24048  ?  511  THR   A OG1 1 
ATOM   4063  C  CG2 . THR   A 1 511  ? -25.81000  83.88400  31.78700  1.000 41.22797  ?  511  THR   A CG2 1 
ATOM   4064  N  N   . ARG   A 1 512  ? -28.38800  82.01700  32.52300  1.000 37.11978  ?  512  ARG   A N   1 
ATOM   4065  C  CA  . ARG   A 1 512  ? -29.29200  81.32500  31.61400  1.000 36.43448  ?  512  ARG   A CA  1 
ATOM   4066  C  C   . ARG   A 1 512  ? -29.83400  82.30500  30.58300  1.000 39.58444  ?  512  ARG   A C   1 
ATOM   4067  O  O   . ARG   A 1 512  ? -30.15500  83.45300  30.90900  1.000 33.56526  ?  512  ARG   A O   1 
ATOM   4068  C  CB  . ARG   A 1 512  ? -30.44500  80.65800  32.37400  1.000 48.84913  ?  512  ARG   A CB  1 
ATOM   4069  C  CG  . ARG   A 1 512  ? -30.46200  79.14500  32.23400  1.000 56.56327  ?  512  ARG   A CG  1 
ATOM   4070  C  CD  . ARG   A 1 512  ? -31.40500  78.49300  33.23400  1.000 69.49108  ?  512  ARG   A CD  1 
ATOM   4071  N  NE  . ARG   A 1 512  ? -32.80700  78.76300  32.93600  1.000 81.25083  ?  512  ARG   A NE  1 
ATOM   4072  C  CZ  . ARG   A 1 512  ? -33.62300  79.45300  33.72200  1.000 80.40768  ?  512  ARG   A CZ  1 
ATOM   4073  N  NH1 . ARG   A 1 512  ? -33.20800  79.96600  34.86800  1.000 78.03643  ?  512  ARG   A NH1 1 
ATOM   4074  N  NH2 . ARG   A 1 512  ? -34.88800  79.62700  33.35000  1.000 91.02507  ?  512  ARG   A NH2 1 
ATOM   4075  N  N   . ILE   A 1 513  ? -29.93300  81.84400  29.33800  1.000 37.54523  ?  513  ILE   A N   1 
ATOM   4076  C  CA  . ILE   A 1 513  ? -30.36000  82.66400  28.21100  1.000 42.15257  ?  513  ILE   A CA  1 
ATOM   4077  C  C   . ILE   A 1 513  ? -31.64000  82.07000  27.64000  1.000 39.31109  ?  513  ILE   A C   1 
ATOM   4078  O  O   . ILE   A 1 513  ? -31.73200  80.85100  27.45000  1.000 44.00033  ?  513  ILE   A O   1 
ATOM   4079  C  CB  . ILE   A 1 513  ? -29.26400  82.75300  27.13300  1.000 35.76099  ?  513  ILE   A CB  1 
ATOM   4080  C  CG1 . ILE   A 1 513  ? -27.99000  83.37000  27.71600  1.000 33.76676  ?  513  ILE   A CG1 1 
ATOM   4081  C  CG2 . ILE   A 1 513  ? -29.74700  83.55300  25.93500  1.000 40.65633  ?  513  ILE   A CG2 1 
ATOM   4082  C  CD1 . ILE   A 1 513  ? -28.08200  84.87000  27.92600  1.000 36.95199  ?  513  ILE   A CD1 1 
ATOM   4083  N  N   . LEU   A 1 514  ? -32.62500  82.93000  27.37400  1.000 35.53757  ?  514  LEU   A N   1 
ATOM   4084  C  CA  . LEU   A 1 514  ? -33.90200  82.52100  26.80600  1.000 43.87265  ?  514  LEU   A CA  1 
ATOM   4085  C  C   . LEU   A 1 514  ? -34.18100  83.31500  25.54000  1.000 41.39483  ?  514  LEU   A C   1 
ATOM   4086  O  O   . LEU   A 1 514  ? -33.91700  84.52000  25.48100  1.000 46.76623  ?  514  LEU   A O   1 
ATOM   4087  C  CB  . LEU   A 1 514  ? -35.05700  82.72900  27.79700  1.000 22.97391  ?  514  LEU   A CB  1 
ATOM   4088  C  CG  . LEU   A 1 514  ? -35.06300  81.86600  29.05700  1.000 27.35121  ?  514  LEU   A CG  1 
ATOM   4089  C  CD1 . LEU   A 1 514  ? -36.03000  82.43800  30.07500  1.000 38.08842  ?  514  LEU   A CD1 1 
ATOM   4090  C  CD2 . LEU   A 1 514  ? -35.41500  80.42300  28.73100  1.000 35.57130  ?  514  LEU   A CD2 1 
ATOM   4091  N  N   . ILE   A 1 515  ? -34.71700  82.63700  24.53100  1.000 33.96471  ?  515  ILE   A N   1 
ATOM   4092  C  CA  . ILE   A 1 515  ? -35.17300  83.28000  23.30400  1.000 36.37390  ?  515  ILE   A CA  1 
ATOM   4093  C  C   . ILE   A 1 515  ? -36.69100  83.39100  23.38700  1.000 43.21019  ?  515  ILE   A C   1 
ATOM   4094  O  O   . ILE   A 1 515  ? -37.40100  82.37900  23.35400  1.000 36.04898  ?  515  ILE   A O   1 
ATOM   4095  C  CB  . ILE   A 1 515  ? -34.73100  82.50400  22.05700  1.000 33.81412  ?  515  ILE   A CB  1 
ATOM   4096  C  CG1 . ILE   A 1 515  ? -33.20900  82.33300  22.05100  1.000 35.14421  ?  515  ILE   A CG1 1 
ATOM   4097  C  CG2 . ILE   A 1 515  ? -35.19800  83.21800  20.79400  1.000 37.31103  ?  515  ILE   A CG2 1 
ATOM   4098  C  CD1 . ILE   A 1 515  ? -32.44100  83.63500  22.18300  1.000 41.38224  ?  515  ILE   A CD1 1 
ATOM   4099  N  N   . LEU   A 1 516  ? -37.19300  84.61700  23.50500  1.000 35.57517  ?  516  LEU   A N   1 
ATOM   4100  C  CA  . LEU   A 1 516  ? -38.60900  84.86400  23.72400  1.000 40.53478  ?  516  LEU   A CA  1 
ATOM   4101  C  C   . LEU   A 1 516  ? -39.18000  85.72900  22.60700  1.000 42.47164  ?  516  LEU   A C   1 
ATOM   4102  O  O   . LEU   A 1 516  ? -38.45600  86.45700  21.92300  1.000 40.06047  ?  516  LEU   A O   1 
ATOM   4103  C  CB  . LEU   A 1 516  ? -38.84900  85.54200  25.07700  1.000 43.02863  ?  516  LEU   A CB  1 
ATOM   4104  C  CG  . LEU   A 1 516  ? -38.18100  84.87400  26.27800  1.000 46.17652  ?  516  LEU   A CG  1 
ATOM   4105  C  CD1 . LEU   A 1 516  ? -38.50400  85.63800  27.55000  1.000 39.26887  ?  516  LEU   A CD1 1 
ATOM   4106  C  CD2 . LEU   A 1 516  ? -38.60300  83.41400  26.39000  1.000 33.39006  ?  516  LEU   A CD2 1 
ATOM   4107  N  N   . ASP   A 1 517  ? -40.49900  85.64200  22.44000  1.000 42.69892  ?  517  ASP   A N   1 
ATOM   4108  C  CA  . ASP   A 1 517  ? -41.20700  86.37700  21.40300  1.000 45.53452  ?  517  ASP   A CA  1 
ATOM   4109  C  C   . ASP   A 1 517  ? -41.74400  87.68700  21.98200  1.000 61.86651  ?  517  ASP   A C   1 
ATOM   4110  O  O   . ASP   A 1 517  ? -41.40100  88.08400  23.09900  1.000 64.14589  ?  517  ASP   A O   1 
ATOM   4111  C  CB  . ASP   A 1 517  ? -42.31000  85.50500  20.80100  1.000 52.25294  ?  517  ASP   A CB  1 
ATOM   4112  C  CG  . ASP   A 1 517  ? -43.58900  85.51000  21.62800  1.000 64.17547  ?  517  ASP   A CG  1 
ATOM   4113  O  OD1 . ASP   A 1 517  ? -43.50400  85.51200  22.87600  1.000 51.53283  ?  517  ASP   A OD1 1 
ATOM   4114  O  OD2 . ASP   A 1 517  ? -44.68400  85.51500  21.02600  1.000 74.26712  -1 517  ASP   A OD2 1 
ATOM   4115  N  N   . GLU   A 1 518  ? -42.60400  88.37300  21.22200  1.000 51.72265  ?  518  GLU   A N   1 
ATOM   4116  C  CA  . GLU   A 1 518  ? -43.11900  89.66400  21.66700  1.000 45.56602  ?  518  GLU   A CA  1 
ATOM   4117  C  C   . GLU   A 1 518  ? -43.98000  89.53000  22.91700  1.000 47.98031  ?  518  GLU   A C   1 
ATOM   4118  O  O   . GLU   A 1 518  ? -43.98800  90.43400  23.75900  1.000 47.11393  ?  518  GLU   A O   1 
ATOM   4119  C  CB  . GLU   A 1 518  ? -43.91100  90.32200  20.54100  1.000 59.62564  ?  518  GLU   A CB  1 
ATOM   4120  C  CG  . GLU   A 1 518  ? -43.22400  91.52900  19.93100  1.000 62.08947  ?  518  GLU   A CG  1 
ATOM   4121  C  CD  . GLU   A 1 518  ? -43.75700  91.86200  18.55200  1.000 95.52155  ?  518  GLU   A CD  1 
ATOM   4122  O  OE1 . GLU   A 1 518  ? -44.99000  92.00700  18.40900  1.000 123.29021 ?  518  GLU   A OE1 1 
ATOM   4123  O  OE2 . GLU   A 1 518  ? -42.94400  91.97500  17.61000  1.000 92.07030  -1 518  GLU   A OE2 1 
ATOM   4124  N  N   . ALA   A 1 519  ? -44.70400  88.42300  23.05500  1.000 55.98871  ?  519  ALA   A N   1 
ATOM   4125  C  CA  . ALA   A 1 519  ? -45.50600  88.16300  24.24200  1.000 51.21285  ?  519  ALA   A CA  1 
ATOM   4126  C  C   . ALA   A 1 519  ? -44.69300  87.56700  25.38100  1.000 52.80583  ?  519  ALA   A C   1 
ATOM   4127  O  O   . ALA   A 1 519  ? -45.28300  87.10700  26.36600  1.000 55.46291  ?  519  ALA   A O   1 
ATOM   4128  C  CB  . ALA   A 1 519  ? -46.67400  87.23400  23.89700  1.000 61.03516  ?  519  ALA   A CB  1 
ATOM   4129  N  N   . LEU   A 1 520  ? -43.36300  87.56000  25.26000  1.000 48.16351  ?  520  LEU   A N   1 
ATOM   4130  C  CA  . LEU   A 1 520  ? -42.47100  87.02500  26.28900  1.000 45.06857  ?  520  LEU   A CA  1 
ATOM   4131  C  C   . LEU   A 1 520  ? -42.69600  85.52800  26.49500  1.000 38.12913  ?  520  LEU   A C   1 
ATOM   4132  O  O   . LEU   A 1 520  ? -42.62800  85.02000  27.61500  1.000 37.54056  ?  520  LEU   A O   1 
ATOM   4133  C  CB  . LEU   A 1 520  ? -42.61900  87.78600  27.61100  1.000 38.15362  ?  520  LEU   A CB  1 
ATOM   4134  C  CG  . LEU   A 1 520  ? -41.83100  89.08300  27.84100  1.000 51.62979  ?  520  LEU   A CG  1 
ATOM   4135  C  CD1 . LEU   A 1 520  ? -41.69800  89.94100  26.58300  1.000 45.59390  ?  520  LEU   A CD1 1 
ATOM   4136  C  CD2 . LEU   A 1 520  ? -42.46600  89.88400  28.97100  1.000 45.38249  ?  520  LEU   A CD2 1 
ATOM   4137  N  N   . ALA   A 1 521  ? -42.95800  84.81400  25.40400  1.000 43.96366  ?  521  ALA   A N   1 
ATOM   4138  C  CA  . ALA   A 1 521  ? -43.17000  83.37600  25.44200  1.000 51.29828  ?  521  ALA   A CA  1 
ATOM   4139  C  C   . ALA   A 1 521  ? -42.00100  82.65400  24.78500  1.000 53.18534  ?  521  ALA   A C   1 
ATOM   4140  O  O   . ALA   A 1 521  ? -41.33500  83.19200  23.89400  1.000 42.19898  ?  521  ALA   A O   1 
ATOM   4141  C  CB  . ALA   A 1 521  ? -44.48000  82.98900  24.75000  1.000 41.05962  ?  521  ALA   A CB  1 
ATOM   4142  N  N   . LEU   A 1 522  ? -41.76400  81.42300  25.23100  1.000 45.91457  ?  522  LEU   A N   1 
ATOM   4143  C  CA  . LEU   A 1 522  ? -40.60900  80.65700  24.78100  1.000 36.62951  ?  522  LEU   A CA  1 
ATOM   4144  C  C   . LEU   A 1 522  ? -40.73300  80.32200  23.29900  1.000 40.75746  ?  522  LEU   A C   1 
ATOM   4145  O  O   . LEU   A 1 522  ? -41.70600  79.69000  22.87500  1.000 61.01389  ?  522  LEU   A O   1 
ATOM   4146  C  CB  . LEU   A 1 522  ? -40.47800  79.38100  25.60800  1.000 41.41508  ?  522  LEU   A CB  1 
ATOM   4147  C  CG  . LEU   A 1 522  ? -39.09800  78.72800  25.64600  1.000 49.91013  ?  522  LEU   A CG  1 
ATOM   4148  C  CD1 . LEU   A 1 522  ? -38.00000  79.77300  25.81300  1.000 46.48214  ?  522  LEU   A CD1 1 
ATOM   4149  C  CD2 . LEU   A 1 522  ? -39.04500  77.70200  26.76100  1.000 49.48668  ?  522  LEU   A CD2 1 
ATOM   4150  N  N   . GLN   A 1 523  ? -39.74900  80.74800  22.51300  1.000 37.87065  ?  523  GLN   A N   1 
ATOM   4151  C  CA  . GLN   A 1 523  ? -39.69200  80.34900  21.11800  1.000 32.10129  ?  523  GLN   A CA  1 
ATOM   4152  C  C   . GLN   A 1 523  ? -39.07800  78.95400  20.99600  1.000 40.11525  ?  523  GLN   A C   1 
ATOM   4153  O  O   . GLN   A 1 523  ? -38.24900  78.55900  21.82200  1.000 45.25553  ?  523  GLN   A O   1 
ATOM   4154  C  CB  . GLN   A 1 523  ? -38.86800  81.34700  20.30900  1.000 34.88208  ?  523  GLN   A CB  1 
ATOM   4155  C  CG  . GLN   A 1 523  ? -39.46500  82.74300  20.23200  1.000 42.79870  ?  523  GLN   A CG  1 
ATOM   4156  C  CD  . GLN   A 1 523  ? -40.49100  82.88000  19.12500  1.000 44.91568  ?  523  GLN   A CD  1 
ATOM   4157  O  OE1 . GLN   A 1 523  ? -41.42200  82.08100  19.02300  1.000 51.64943  ?  523  GLN   A OE1 1 
ATOM   4158  N  NE2 . GLN   A 1 523  ? -40.32400  83.89600  18.28700  1.000 44.07291  ?  523  GLN   A NE2 1 
ATOM   4159  N  N   . PRO   A 1 524  ? -39.48300  78.18300  19.99000  1.000 44.06663  ?  524  PRO   A N   1 
ATOM   4160  C  CA  . PRO   A 1 524  ? -38.84400  76.88400  19.74900  1.000 35.21187  ?  524  PRO   A CA  1 
ATOM   4161  C  C   . PRO   A 1 524  ? -37.39900  77.05700  19.30400  1.000 41.52415  ?  524  PRO   A C   1 
ATOM   4162  O  O   . PRO   A 1 524  ? -36.95200  78.14500  18.93700  1.000 50.47573  ?  524  PRO   A O   1 
ATOM   4163  C  CB  . PRO   A 1 524  ? -39.69600  76.26300  18.63600  1.000 38.30834  ?  524  PRO   A CB  1 
ATOM   4164  C  CG  . PRO   A 1 524  ? -40.98800  77.00800  18.67400  1.000 30.03947  ?  524  PRO   A CG  1 
ATOM   4165  C  CD  . PRO   A 1 524  ? -40.64100  78.39900  19.10800  1.000 47.42515  ?  524  PRO   A CD  1 
ATOM   4166  N  N   . ILE   A 1 525  ? -36.66100  75.94500  19.33300  1.000 44.46617  ?  525  ILE   A N   1 
ATOM   4167  C  CA  . ILE   A 1 525  ? -35.26600  75.97100  18.90800  1.000 40.62289  ?  525  ILE   A CA  1 
ATOM   4168  C  C   . ILE   A 1 525  ? -35.19500  76.31600  17.42800  1.000 39.04069  ?  525  ILE   A C   1 
ATOM   4169  O  O   . ILE   A 1 525  ? -35.95100  75.77800  16.61000  1.000 50.00684  ?  525  ILE   A O   1 
ATOM   4170  C  CB  . ILE   A 1 525  ? -34.59300  74.62400  19.20400  1.000 39.47520  ?  525  ILE   A CB  1 
ATOM   4171  C  CG1 . ILE   A 1 525  ? -34.49400  74.40600  20.71500  1.000 41.20473  ?  525  ILE   A CG1 1 
ATOM   4172  C  CG2 . ILE   A 1 525  ? -33.21900  74.55900  18.54500  1.000 45.90798  ?  525  ILE   A CG2 1 
ATOM   4173  C  CD1 . ILE   A 1 525  ? -33.35500  73.51400  21.13600  1.000 51.37705  ?  525  ILE   A CD1 1 
ATOM   4174  N  N   . GLY   A 1 526  ? -34.28600  77.22500  17.07700  1.000 44.47900  ?  526  GLY   A N   1 
ATOM   4175  C  CA  . GLY   A 1 526  ? -34.12900  77.67400  15.71500  1.000 36.40754  ?  526  GLY   A CA  1 
ATOM   4176  C  C   . GLY   A 1 526  ? -35.02000  78.83200  15.32300  1.000 38.86228  ?  526  GLY   A C   1 
ATOM   4177  O  O   . GLY   A 1 526  ? -34.74700  79.49500  14.31500  1.000 46.92083  ?  526  GLY   A O   1 
ATOM   4178  N  N   . VAL   A 1 527  ? -36.07700  79.08800  16.07800  1.000 33.10878  ?  527  VAL   A N   1 
ATOM   4179  C  CA  . VAL   A 1 527  ? -36.92200  80.24800  15.83200  1.000 35.09706  ?  527  VAL   A CA  1 
ATOM   4180  C  C   . VAL   A 1 527  ? -36.27900  81.46800  16.47200  1.000 35.19740  ?  527  VAL   A C   1 
ATOM   4181  O  O   . VAL   A 1 527  ? -35.79300  81.41100  17.60800  1.000 37.74712  ?  527  VAL   A O   1 
ATOM   4182  C  CB  . VAL   A 1 527  ? -38.33900  80.00600  16.38000  1.000 36.39796  ?  527  VAL   A CB  1 
ATOM   4183  C  CG1 . VAL   A 1 527  ? -39.29000  81.10000  15.90500  1.000 21.92808  ?  527  VAL   A CG1 1 
ATOM   4184  C  CG2 . VAL   A 1 527  ? -38.82300  78.63000  15.96600  1.000 25.11253  ?  527  VAL   A CG2 1 
ATOM   4185  N  N   . ALA   A 1 528  ? -36.27400  82.57800  15.74300  1.000 34.17545  ?  528  ALA   A N   1 
ATOM   4186  C  CA  . ALA   A 1 528  ? -35.63700  83.78600  16.23400  1.000 28.96249  ?  528  ALA   A CA  1 
ATOM   4187  C  C   . ALA   A 1 528  ? -36.53800  84.51400  17.22800  1.000 44.07368  ?  528  ALA   A C   1 
ATOM   4188  O  O   . ALA   A 1 528  ? -37.76400  84.36200  17.23300  1.000 48.80855  ?  528  ALA   A O   1 
ATOM   4189  C  CB  . ALA   A 1 528  ? -35.27800  84.71300  15.07400  1.000 37.45209  ?  528  ALA   A CB  1 
ATOM   4190  N  N   . GLY   A 1 529  ? -35.90400  85.31100  18.07700  1.000 43.63612  ?  529  GLY   A N   1 
ATOM   4191  C  CA  . GLY   A 1 529  ? -36.61800  86.11000  19.05000  1.000 42.42968  ?  529  GLY   A CA  1 
ATOM   4192  C  C   . GLY   A 1 529  ? -35.67000  87.07900  19.71700  1.000 40.12805  ?  529  GLY   A C   1 
ATOM   4193  O  O   . GLY   A 1 529  ? -34.54100  87.27700  19.26900  1.000 53.04687  ?  529  GLY   A O   1 
ATOM   4194  N  N   . GLU   A 1 530  ? -36.14000  87.68400  20.80400  1.000 42.96030  ?  530  GLU   A N   1 
ATOM   4195  C  CA  . GLU   A 1 530  ? -35.30100  88.57800  21.58800  1.000 40.72057  ?  530  GLU   A CA  1 
ATOM   4196  C  C   . GLU   A 1 530  ? -34.53900  87.78700  22.64100  1.000 42.94909  ?  530  GLU   A C   1 
ATOM   4197  O  O   . GLU   A 1 530  ? -35.10100  86.91300  23.30800  1.000 45.78747  ?  530  GLU   A O   1 
ATOM   4198  C  CB  . GLU   A 1 530  ? -36.13100  89.67200  22.26200  1.000 46.98882  ?  530  GLU   A CB  1 
ATOM   4199  C  CG  . GLU   A 1 530  ? -35.28300  90.65900  23.05100  1.000 50.05422  ?  530  GLU   A CG  1 
ATOM   4200  C  CD  . GLU   A 1 530  ? -36.01600  91.94100  23.37800  1.000 57.63882  ?  530  GLU   A CD  1 
ATOM   4201  O  OE1 . GLU   A 1 530  ? -37.25200  91.98000  23.20700  1.000 83.62675  ?  530  GLU   A OE1 1 
ATOM   4202  O  OE2 . GLU   A 1 530  ? -35.35300  92.91300  23.80000  1.000 57.54712  -1 530  GLU   A OE2 1 
ATOM   4203  N  N   . LEU   A 1 531  ? -33.25200  88.09600  22.78300  1.000 41.53443  ?  531  LEU   A N   1 
ATOM   4204  C  CA  . LEU   A 1 531  ? -32.42100  87.44200  23.78200  1.000 42.05788  ?  531  LEU   A CA  1 
ATOM   4205  C  C   . LEU   A 1 531  ? -32.71300  88.02400  25.15900  1.000 39.10588  ?  531  LEU   A C   1 
ATOM   4206  O  O   . LEU   A 1 531  ? -32.75300  89.24600  25.33200  1.000 30.93171  ?  531  LEU   A O   1 
ATOM   4207  C  CB  . LEU   A 1 531  ? -30.94000  87.60500  23.43600  1.000 39.41576  ?  531  LEU   A CB  1 
ATOM   4208  C  CG  . LEU   A 1 531  ? -29.96900  86.62200  24.09500  1.000 38.20395  ?  531  LEU   A CG  1 
ATOM   4209  C  CD1 . LEU   A 1 531  ? -28.90200  86.17400  23.10800  1.000 32.77175  ?  531  LEU   A CD1 1 
ATOM   4210  C  CD2 . LEU   A 1 531  ? -29.33000  87.23100  25.32900  1.000 32.19771  ?  531  LEU   A CD2 1 
ATOM   4211  N  N   . PHE   A 1 532  ? -32.92800  87.14800  26.13500  1.000 32.35210  ?  532  PHE   A N   1 
ATOM   4212  C  CA  . PHE   A 1 532  ? -33.17700  87.54300  27.51400  1.000 38.39902  ?  532  PHE   A CA  1 
ATOM   4213  C  C   . PHE   A 1 532  ? -32.14400  86.88100  28.41200  1.000 39.90026  ?  532  PHE   A C   1 
ATOM   4214  O  O   . PHE   A 1 532  ? -31.83500  85.69700  28.24700  1.000 46.15426  ?  532  PHE   A O   1 
ATOM   4215  C  CB  . PHE   A 1 532  ? -34.59300  87.15400  27.95500  1.000 44.50078  ?  532  PHE   A CB  1 
ATOM   4216  C  CG  . PHE   A 1 532  ? -35.64700  88.12400  27.51100  1.000 42.36251  ?  532  PHE   A CG  1 
ATOM   4217  C  CD1 . PHE   A 1 532  ? -36.10800  88.11600  26.20500  1.000 42.44815  ?  532  PHE   A CD1 1 
ATOM   4218  C  CD2 . PHE   A 1 532  ? -36.17200  89.04900  28.39700  1.000 43.32274  ?  532  PHE   A CD2 1 
ATOM   4219  C  CE1 . PHE   A 1 532  ? -37.07300  89.01200  25.79000  1.000 48.46082  ?  532  PHE   A CE1 1 
ATOM   4220  C  CE2 . PHE   A 1 532  ? -37.13800  89.94500  27.99000  1.000 39.96521  ?  532  PHE   A CE2 1 
ATOM   4221  C  CZ  . PHE   A 1 532  ? -37.58900  89.92900  26.68300  1.000 48.74560  ?  532  PHE   A CZ  1 
ATOM   4222  N  N   . ILE   A 1 533  ? -31.60900  87.64200  29.36100  1.000 37.56436  ?  533  ILE   A N   1 
ATOM   4223  C  CA  . ILE   A 1 533  ? -30.52500  87.17900  30.22000  1.000 41.67278  ?  533  ILE   A CA  1 
ATOM   4224  C  C   . ILE   A 1 533  ? -31.05300  87.00100  31.63700  1.000 38.78560  ?  533  ILE   A C   1 
ATOM   4225  O  O   . ILE   A 1 533  ? -31.71300  87.89700  32.17800  1.000 41.72504  ?  533  ILE   A O   1 
ATOM   4226  C  CB  . ILE   A 1 533  ? -29.33500  88.15000  30.18900  1.000 34.92113  ?  533  ILE   A CB  1 
ATOM   4227  C  CG1 . ILE   A 1 533  ? -28.94500  88.43600  28.74100  1.000 29.47700  ?  533  ILE   A CG1 1 
ATOM   4228  C  CG2 . ILE   A 1 533  ? -28.15800  87.57600  30.95900  1.000 28.75635  ?  533  ILE   A CG2 1 
ATOM   4229  C  CD1 . ILE   A 1 533  ? -27.61800  89.09700  28.59600  1.000 25.28134  ?  533  ILE   A CD1 1 
ATOM   4230  N  N   . VAL   A 1 534  ? -30.76600  85.84200  32.23000  1.000 29.52599  ?  534  VAL   A N   1 
ATOM   4231  C  CA  . VAL   A 1 534  ? -31.10500  85.53400  33.61500  1.000 33.33372  ?  534  VAL   A CA  1 
ATOM   4232  C  C   . VAL   A 1 534  ? -29.85000  85.00400  34.29100  1.000 43.47737  ?  534  VAL   A C   1 
ATOM   4233  O  O   . VAL   A 1 534  ? -29.16700  84.13500  33.73900  1.000 49.01948  ?  534  VAL   A O   1 
ATOM   4234  C  CB  . VAL   A 1 534  ? -32.24300  84.49600  33.71500  1.000 39.45661  ?  534  VAL   A CB  1 
ATOM   4235  C  CG1 . VAL   A 1 534  ? -32.59100  84.20200  35.17200  1.000 47.23967  ?  534  VAL   A CG1 1 
ATOM   4236  C  CG2 . VAL   A 1 534  ? -33.46200  84.96900  32.96500  1.000 43.71241  ?  534  VAL   A CG2 1 
ATOM   4237  N  N   . GLY   A 1 535  ? -29.54100  85.52100  35.46900  1.000 43.50376  ?  535  GLY   A N   1 
ATOM   4238  C  CA  . GLY   A 1 535  ? -28.43400  84.98200  36.22800  1.000 45.40227  ?  535  GLY   A CA  1 
ATOM   4239  C  C   . GLY   A 1 535  ? -27.76100  86.04800  37.06800  1.000 44.59976  ?  535  GLY   A C   1 
ATOM   4240  O  O   . GLY   A 1 535  ? -28.30500  87.12800  37.28500  1.000 33.92143  ?  535  GLY   A O   1 
ATOM   4241  N  N   . GLU   A 1 536  ? -26.55800  85.70400  37.52800  1.000 50.04020  ?  536  GLU   A N   1 
ATOM   4242  C  CA  . GLU   A 1 536  ? -25.79400  86.53500  38.44900  1.000 40.22671  ?  536  GLU   A CA  1 
ATOM   4243  C  C   . GLU   A 1 536  ? -25.04500  87.66900  37.76500  1.000 38.50517  ?  536  GLU   A C   1 
ATOM   4244  O  O   . GLU   A 1 536  ? -24.36700  88.43500  38.45400  1.000 44.87640  ?  536  GLU   A O   1 
ATOM   4245  C  CB  . GLU   A 1 536  ? -24.80400  85.67100  39.23500  1.000 38.16638  ?  536  GLU   A CB  1 
ATOM   4246  C  CG  . GLU   A 1 536  ? -25.46400  84.70300  40.19800  1.000 54.51836  ?  536  GLU   A CG  1 
ATOM   4247  C  CD  . GLU   A 1 536  ? -25.34000  85.13200  41.64600  1.000 62.69855  ?  536  GLU   A CD  1 
ATOM   4248  O  OE1 . GLU   A 1 536  ? -25.28400  86.35300  41.91200  1.000 48.15291  ?  536  GLU   A OE1 1 
ATOM   4249  O  OE2 . GLU   A 1 536  ? -25.30000  84.24100  42.52200  1.000 73.72877  -1 536  GLU   A OE2 1 
ATOM   4250  N  N   . GLY   A 1 537  ? -25.13900  87.79600  36.43800  1.000 31.96589  ?  537  GLY   A N   1 
ATOM   4251  C  CA  . GLY   A 1 537  ? -24.53300  88.93600  35.77400  1.000 28.25485  ?  537  GLY   A CA  1 
ATOM   4252  C  C   . GLY   A 1 537  ? -25.38600  90.18200  35.82700  1.000 39.83838  ?  537  GLY   A C   1 
ATOM   4253  O  O   . GLY   A 1 537  ? -24.85900  91.29700  35.74400  1.000 53.82305  ?  537  GLY   A O   1 
ATOM   4254  N  N   . LEU   A 1 538  ? -26.69900  90.02200  35.97200  1.000 34.25226  ?  538  LEU   A N   1 
ATOM   4255  C  CA  . LEU   A 1 538  ? -27.61600  91.15400  35.94000  1.000 37.29544  ?  538  LEU   A CA  1 
ATOM   4256  C  C   . LEU   A 1 538  ? -27.36500  92.06200  37.13700  1.000 38.16356  ?  538  LEU   A C   1 
ATOM   4257  O  O   . LEU   A 1 538  ? -27.51600  91.64000  38.28900  1.000 46.19933  ?  538  LEU   A O   1 
ATOM   4258  C  CB  . LEU   A 1 538  ? -29.06500  90.66900  35.93100  1.000 47.47461  ?  538  LEU   A CB  1 
ATOM   4259  C  CG  . LEU   A 1 538  ? -29.62900  90.02000  34.66300  1.000 42.84578  ?  538  LEU   A CG  1 
ATOM   4260  C  CD1 . LEU   A 1 538  ? -29.01500  88.65000  34.38600  1.000 47.63428  ?  538  LEU   A CD1 1 
ATOM   4261  C  CD2 . LEU   A 1 538  ? -31.13800  89.91200  34.77500  1.000 35.38412  ?  538  LEU   A CD2 1 
ATOM   4262  N  N   . GLY   A 1 539  ? -26.98500  93.30900  36.86400  1.000 33.67240  ?  539  GLY   A N   1 
ATOM   4263  C  CA  . GLY   A 1 539  ? -26.69700  94.27400  37.90400  1.000 50.10089  ?  539  GLY   A CA  1 
ATOM   4264  C  C   . GLY   A 1 539  ? -27.95500  94.94600  38.42000  1.000 49.44429  ?  539  GLY   A C   1 
ATOM   4265  O  O   . GLY   A 1 539  ? -29.08100  94.52800  38.14400  1.000 50.50719  ?  539  GLY   A O   1 
ATOM   4266  N  N   . ARG   A 1 540  ? -27.74800  96.02000  39.18900  1.000 42.73989  ?  540  ARG   A N   1 
ATOM   4267  C  CA  . ARG   A 1 540  ? -28.87400  96.75800  39.75800  1.000 54.56652  ?  540  ARG   A CA  1 
ATOM   4268  C  C   . ARG   A 1 540  ? -29.65800  97.48100  38.66700  1.000 46.77441  ?  540  ARG   A C   1 
ATOM   4269  O  O   . ARG   A 1 540  ? -30.88300  97.34500  38.56900  1.000 56.46733  ?  540  ARG   A O   1 
ATOM   4270  C  CB  . ARG   A 1 540  ? -28.38500  97.75400  40.81200  1.000 49.03064  ?  540  ARG   A CB  1 
ATOM   4271  C  CG  . ARG   A 1 540  ? -28.99000  97.59800  42.21400  1.000 63.69667  ?  540  ARG   A CG  1 
ATOM   4272  C  CD  . ARG   A 1 540  ? -28.25800  98.51800  43.19000  1.000 40.54363  ?  540  ARG   A CD  1 
ATOM   4273  N  NE  . ARG   A 1 540  ? -27.35500  97.81700  44.09200  1.000 45.04254  ?  540  ARG   A NE  1 
ATOM   4274  C  CZ  . ARG   A 1 540  ? -26.64900  98.39300  45.05900  1.000 47.12520  ?  540  ARG   A CZ  1 
ATOM   4275  N  NH1 . ARG   A 1 540  ? -26.67500  99.70300  45.25500  1.000 40.62742  ?  540  ARG   A NH1 1 
ATOM   4276  N  NH2 . ARG   A 1 540  ? -25.89100  97.63400  45.84600  1.000 58.99981  ?  540  ARG   A NH2 1 
ATOM   4277  N  N   . GLY   A 1 541  ? -28.97100  98.25500  37.84200  1.000 38.69331  ?  541  GLY   A N   1 
ATOM   4278  C  CA  . GLY   A 1 541  ? -29.61200  98.94800  36.74300  1.000 30.34576  ?  541  GLY   A CA  1 
ATOM   4279  C  C   . GLY   A 1 541  ? -28.86800  100.23500 36.40200  1.000 40.20266  ?  541  GLY   A C   1 
ATOM   4280  O  O   . GLY   A 1 541  ? -27.63800  100.25500 36.32800  1.000 47.99111  ?  541  GLY   A O   1 
ATOM   4281  N  N   . TYR   A 1 542  ? -29.64000  101.29400 36.18000  1.000 37.25692  ?  542  TYR   A N   1 
ATOM   4282  C  CA  . TYR   A 1 542  ? -29.10400  102.57600 35.75300  1.000 45.20927  ?  542  TYR   A CA  1 
ATOM   4283  C  C   . TYR   A 1 542  ? -29.18100  103.59000 36.88800  1.000 50.06265  ?  542  TYR   A C   1 
ATOM   4284  O  O   . TYR   A 1 542  ? -30.07900  103.53800 37.73200  1.000 63.16033  ?  542  TYR   A O   1 
ATOM   4285  C  CB  . TYR   A 1 542  ? -29.85000  103.09600 34.52100  1.000 41.04216  ?  542  TYR   A CB  1 
ATOM   4286  C  CG  . TYR   A 1 542  ? -29.87300  102.12400 33.35900  1.000 53.47915  ?  542  TYR   A CG  1 
ATOM   4287  C  CD1 . TYR   A 1 542  ? -28.74000  101.90800 32.58300  1.000 50.98865  ?  542  TYR   A CD1 1 
ATOM   4288  C  CD2 . TYR   A 1 542  ? -31.02800  101.42100 33.03800  1.000 46.18393  ?  542  TYR   A CD2 1 
ATOM   4289  C  CE1 . TYR   A 1 542  ? -28.75900  101.02300 31.51900  1.000 49.85833  ?  542  TYR   A CE1 1 
ATOM   4290  C  CE2 . TYR   A 1 542  ? -31.05600  100.53400 31.97600  1.000 33.90795  ?  542  TYR   A CE2 1 
ATOM   4291  C  CZ  . TYR   A 1 542  ? -29.92100  100.33900 31.22200  1.000 47.15778  ?  542  TYR   A CZ  1 
ATOM   4292  O  OH  . TYR   A 1 542  ? -29.95300  99.45500  30.16800  1.000 52.60384  ?  542  TYR   A OH  1 
ATOM   4293  N  N   . LEU   A 1 543  ? -28.22500  104.51600 36.89900  1.000 56.22575  ?  543  LEU   A N   1 
ATOM   4294  C  CA  . LEU   A 1 543  ? -28.11300  105.50500 37.96400  1.000 52.39432  ?  543  LEU   A CA  1 
ATOM   4295  C  C   . LEU   A 1 543  ? -29.08800  106.65200 37.72300  1.000 52.24989  ?  543  LEU   A C   1 
ATOM   4296  O  O   . LEU   A 1 543  ? -28.97800  107.36100 36.71700  1.000 59.17338  ?  543  LEU   A O   1 
ATOM   4297  C  CB  . LEU   A 1 543  ? -26.68300  106.03000 38.03800  1.000 61.30154  ?  543  LEU   A CB  1 
ATOM   4298  C  CG  . LEU   A 1 543  ? -26.33100  106.87500 39.26000  1.000 54.50088  ?  543  LEU   A CG  1 
ATOM   4299  C  CD1 . LEU   A 1 543  ? -26.63600  106.12600 40.54700  1.000 36.08720  ?  543  LEU   A CD1 1 
ATOM   4300  C  CD2 . LEU   A 1 543  ? -24.87600  107.31000 39.20100  1.000 50.53884  ?  543  LEU   A CD2 1 
ATOM   4301  N  N   . ASN   A 1 544  ? -30.02900  106.84100 38.65200  1.000 58.33673  ?  544  ASN   A N   1 
ATOM   4302  C  CA  . ASN   A 1 544  ? -31.02100  107.91800 38.60500  1.000 68.18172  ?  544  ASN   A CA  1 
ATOM   4303  C  C   . ASN   A 1 544  ? -31.89100  107.85500 37.35200  1.000 69.77886  ?  544  ASN   A C   1 
ATOM   4304  O  O   . ASN   A 1 544  ? -32.44000  108.87500 36.91900  1.000 74.50619  ?  544  ASN   A O   1 
ATOM   4305  C  CB  . ASN   A 1 544  ? -30.35300  109.29500 38.72100  1.000 68.75717  ?  544  ASN   A CB  1 
ATOM   4306  C  CG  . ASN   A 1 544  ? -29.43200  109.39700 39.92500  1.000 69.64243  ?  544  ASN   A CG  1 
ATOM   4307  O  OD1 . ASN   A 1 544  ? -29.77300  108.95600 41.02400  1.000 68.08765  ?  544  ASN   A OD1 1 
ATOM   4308  N  ND2 . ASN   A 1 544  ? -28.25100  109.96900 39.71800  1.000 55.12596  ?  544  ASN   A ND2 1 
ATOM   4309  N  N   . ARG   A 1 545  ? -32.01500  106.66900 36.75700  1.000 64.67163  ?  545  ARG   A N   1 
ATOM   4310  C  CA  . ARG   A 1 545  ? -32.90400  106.42300 35.62100  1.000 47.28973  ?  545  ARG   A CA  1 
ATOM   4311  C  C   . ARG   A 1 545  ? -33.75300  105.20200 35.94600  1.000 55.84734  ?  545  ARG   A C   1 
ATOM   4312  O  O   . ARG   A 1 545  ? -33.53700  104.11100 35.40300  1.000 48.53862  ?  545  ARG   A O   1 
ATOM   4313  C  CB  . ARG   A 1 545  ? -32.12000  106.21800 34.32300  1.000 41.39675  ?  545  ARG   A CB  1 
ATOM   4314  C  CG  . ARG   A 1 545  ? -30.85800  107.04800 34.21300  1.000 48.48992  ?  545  ARG   A CG  1 
ATOM   4315  C  CD  . ARG   A 1 545  ? -30.81500  107.87400 32.93900  1.000 46.81458  ?  545  ARG   A CD  1 
ATOM   4316  N  NE  . ARG   A 1 545  ? -30.40600  109.24700 33.20900  1.000 77.18222  ?  545  ARG   A NE  1 
ATOM   4317  C  CZ  . ARG   A 1 545  ? -29.16000  109.62500 33.47000  1.000 83.80517  ?  545  ARG   A CZ  1 
ATOM   4318  N  NH1 . ARG   A 1 545  ? -28.16200  108.75600 33.49300  1.000 75.38162  ?  545  ARG   A NH1 1 
ATOM   4319  N  NH2 . ARG   A 1 545  ? -28.90800  110.91000 33.70800  1.000 79.44024  ?  545  ARG   A NH2 1 
ATOM   4320  N  N   . PRO   A 1 546  ? -34.73300  105.35100 36.84100  1.000 67.12739  ?  546  PRO   A N   1 
ATOM   4321  C  CA  . PRO   A 1 546  ? -35.54000  104.19100 37.24300  1.000 63.26769  ?  546  PRO   A CA  1 
ATOM   4322  C  C   . PRO   A 1 546  ? -36.53600  103.75300 36.18600  1.000 52.43518  ?  546  PRO   A C   1 
ATOM   4323  O  O   . PRO   A 1 546  ? -37.01100  102.61100 36.24300  1.000 47.18594  ?  546  PRO   A O   1 
ATOM   4324  C  CB  . PRO   A 1 546  ? -36.24900  104.68700 38.50700  1.000 56.38070  ?  546  PRO   A CB  1 
ATOM   4325  C  CG  . PRO   A 1 546  ? -36.40800  106.15700 38.26700  1.000 65.06563  ?  546  PRO   A CG  1 
ATOM   4326  C  CD  . PRO   A 1 546  ? -35.20000  106.59800 37.47300  1.000 60.08590  ?  546  PRO   A CD  1 
ATOM   4327  N  N   . GLU   A 1 547  ? -36.87100  104.62000 35.22800  1.000 47.26460  ?  547  GLU   A N   1 
ATOM   4328  C  CA  . GLU   A 1 547  ? -37.78900  104.22800 34.16400  1.000 53.57957  ?  547  GLU   A CA  1 
ATOM   4329  C  C   . GLU   A 1 547  ? -37.14500  103.20100 33.24100  1.000 56.56362  ?  547  GLU   A C   1 
ATOM   4330  O  O   . GLU   A 1 547  ? -37.69100  102.11100 33.03000  1.000 57.10227  ?  547  GLU   A O   1 
ATOM   4331  C  CB  . GLU   A 1 547  ? -38.23500  105.46100 33.37400  1.000 47.20869  ?  547  GLU   A CB  1 
ATOM   4332  C  CG  . GLU   A 1 547  ? -39.22900  105.16800 32.25500  1.000 53.26223  ?  547  GLU   A CG  1 
ATOM   4333  C  CD  . GLU   A 1 547  ? -39.61800  106.41700 31.48200  1.000 52.34197  ?  547  GLU   A CD  1 
ATOM   4334  O  OE1 . GLU   A 1 547  ? -39.23100  107.52100 31.91200  1.000 61.70255  ?  547  GLU   A OE1 1 
ATOM   4335  O  OE2 . GLU   A 1 547  ? -40.30400  106.29800 30.44500  1.000 55.31207  -1 547  GLU   A OE2 1 
ATOM   4336  N  N   . LEU   A 1 548  ? -35.97200  103.52900 32.69300  1.000 51.31196  ?  548  LEU   A N   1 
ATOM   4337  C  CA  . LEU   A 1 548  ? -35.28700  102.60300 31.79800  1.000 52.24365  ?  548  LEU   A CA  1 
ATOM   4338  C  C   . LEU   A 1 548  ? -34.93100  101.29400 32.49700  1.000 43.77261  ?  548  LEU   A C   1 
ATOM   4339  O  O   . LEU   A 1 548  ? -34.94300  100.23300 31.86400  1.000 44.31283  ?  548  LEU   A O   1 
ATOM   4340  C  CB  . LEU   A 1 548  ? -34.03500  103.26700 31.22500  1.000 37.18856  ?  548  LEU   A CB  1 
ATOM   4341  C  CG  . LEU   A 1 548  ? -33.34400  102.55200 30.06200  1.000 44.80539  ?  548  LEU   A CG  1 
ATOM   4342  C  CD1 . LEU   A 1 548  ? -34.35900  102.09300 29.02800  1.000 49.50513  ?  548  LEU   A CD1 1 
ATOM   4343  C  CD2 . LEU   A 1 548  ? -32.29600  103.45400 29.42800  1.000 67.56319  ?  548  LEU   A CD2 1 
ATOM   4344  N  N   . THR   A 1 549  ? -34.62000  101.34300 33.79600  1.000 37.01314  ?  549  THR   A N   1 
ATOM   4345  C  CA  . THR   A 1 549  ? -34.30400  100.11600 34.52300  1.000 36.12706  ?  549  THR   A CA  1 
ATOM   4346  C  C   . THR   A 1 549  ? -35.51400  99.19300  34.60200  1.000 43.28412  ?  549  THR   A C   1 
ATOM   4347  O  O   . THR   A 1 549  ? -35.39700  97.98500  34.36400  1.000 43.56012  ?  549  THR   A O   1 
ATOM   4348  C  CB  . THR   A 1 549  ? -33.78300  100.45200 35.92200  1.000 38.05618  ?  549  THR   A CB  1 
ATOM   4349  O  OG1 . THR   A 1 549  ? -32.72600  101.41300 35.81400  1.000 50.29325  ?  549  THR   A OG1 1 
ATOM   4350  C  CG2 . THR   A 1 549  ? -33.25200  99.20600  36.62200  1.000 22.51073  ?  549  THR   A CG2 1 
ATOM   4351  N  N   . ALA   A 1 550  ? -36.68900  99.74400  34.91900  1.000 53.28335  ?  550  ALA   A N   1 
ATOM   4352  C  CA  . ALA   A 1 550  ? -37.90600  98.94100  34.91500  1.000 39.42378  ?  550  ALA   A CA  1 
ATOM   4353  C  C   . ALA   A 1 550  ? -38.28000  98.47900  33.51400  1.000 36.84811  ?  550  ALA   A C   1 
ATOM   4354  O  O   . ALA   A 1 550  ? -39.05600  97.52900  33.37100  1.000 39.26321  ?  550  ALA   A O   1 
ATOM   4355  C  CB  . ALA   A 1 550  ? -39.05600  99.73100  35.53500  1.000 33.63904  ?  550  ALA   A CB  1 
ATOM   4356  N  N   . GLU   A 1 551  ? -37.72800  99.12300  32.48500  1.000 43.90327  ?  551  GLU   A N   1 
ATOM   4357  C  CA  . GLU   A 1 551  ? -38.03400  98.77400  31.10300  1.000 37.10873  ?  551  GLU   A CA  1 
ATOM   4358  C  C   . GLU   A 1 551  ? -37.16800  97.62200  30.60500  1.000 49.54086  ?  551  GLU   A C   1 
ATOM   4359  O  O   . GLU   A 1 551  ? -37.67200  96.70400  29.94800  1.000 61.93587  ?  551  GLU   A O   1 
ATOM   4360  C  CB  . GLU   A 1 551  ? -37.84800  100.00700 30.22000  1.000 41.24086  ?  551  GLU   A CB  1 
ATOM   4361  C  CG  . GLU   A 1 551  ? -38.22000  99.82700  28.76300  1.000 52.35328  ?  551  GLU   A CG  1 
ATOM   4362  C  CD  . GLU   A 1 551  ? -38.02900  101.10800 27.97100  1.000 75.34214  ?  551  GLU   A CD  1 
ATOM   4363  O  OE1 . GLU   A 1 551  ? -38.24100  102.20000 28.54400  1.000 59.55488  ?  551  GLU   A OE1 1 
ATOM   4364  O  OE2 . GLU   A 1 551  ? -37.65100  101.02600 26.78300  1.000 89.73230  -1 551  GLU   A OE2 1 
ATOM   4365  N  N   . LYS   A 1 552  ? -35.86900  97.65200  30.90600  1.000 43.81602  ?  552  LYS   A N   1 
ATOM   4366  C  CA  . LYS   A 1 552  ? -34.95100  96.62200  30.43200  1.000 40.52265  ?  552  LYS   A CA  1 
ATOM   4367  C  C   . LYS   A 1 552  ? -34.77800  95.49100  31.43900  1.000 41.80421  ?  552  LYS   A C   1 
ATOM   4368  O  O   . LYS   A 1 552  ? -34.62600  94.33000  31.04300  1.000 43.97108  ?  552  LYS   A O   1 
ATOM   4369  C  CB  . LYS   A 1 552  ? -33.59200  97.24000  30.10200  1.000 30.11199  ?  552  LYS   A CB  1 
ATOM   4370  C  CG  . LYS   A 1 552  ? -33.66900  98.50800  29.26100  1.000 44.40466  ?  552  LYS   A CG  1 
ATOM   4371  C  CD  . LYS   A 1 552  ? -32.70400  98.44200  28.08500  1.000 57.62787  ?  552  LYS   A CD  1 
ATOM   4372  C  CE  . LYS   A 1 552  ? -33.19800  97.47600  27.01600  1.000 55.16883  ?  552  LYS   A CE  1 
ATOM   4373  N  NZ  . LYS   A 1 552  ? -32.24500  97.32600  25.87500  1.000 42.68770  ?  552  LYS   A NZ  1 
ATOM   4374  N  N   . PHE   A 1 553  ? -34.78500  95.80400  32.73200  1.000 32.86859  ?  553  PHE   A N   1 
ATOM   4375  C  CA  . PHE   A 1 553  ? -34.74800  94.79300  33.78800  1.000 41.94409  ?  553  PHE   A CA  1 
ATOM   4376  C  C   . PHE   A 1 553  ? -36.18800  94.53300  34.21000  1.000 47.54916  ?  553  PHE   A C   1 
ATOM   4377  O  O   . PHE   A 1 553  ? -36.76600  95.29600  34.98800  1.000 51.00550  ?  553  PHE   A O   1 
ATOM   4378  C  CB  . PHE   A 1 553  ? -33.89600  95.24600  34.97000  1.000 37.23929  ?  553  PHE   A CB  1 
ATOM   4379  C  CG  . PHE   A 1 553  ? -32.42900  95.32800  34.66900  1.000 39.18866  ?  553  PHE   A CG  1 
ATOM   4380  C  CD1 . PHE   A 1 553  ? -31.88200  96.48000  34.12500  1.000 32.11537  ?  553  PHE   A CD1 1 
ATOM   4381  C  CD2 . PHE   A 1 553  ? -31.59200  94.25800  34.94500  1.000 48.74275  ?  553  PHE   A CD2 1 
ATOM   4382  C  CE1 . PHE   A 1 553  ? -30.53000  96.55900  33.85100  1.000 34.45323  ?  553  PHE   A CE1 1 
ATOM   4383  C  CE2 . PHE   A 1 553  ? -30.23800  94.33100  34.67500  1.000 35.70195  ?  553  PHE   A CE2 1 
ATOM   4384  C  CZ  . PHE   A 1 553  ? -29.70700  95.48300  34.12800  1.000 35.32264  ?  553  PHE   A CZ  1 
ATOM   4385  N  N   . ILE   A 1 554  ? -36.76900  93.45700  33.69000  1.000 47.23290  ?  554  ILE   A N   1 
ATOM   4386  C  CA  . ILE   A 1 554  ? -38.14800  93.09000  33.97600  1.000 35.48598  ?  554  ILE   A CA  1 
ATOM   4387  C  C   . ILE   A 1 554  ? -38.15700  91.73900  34.67200  1.000 46.20463  ?  554  ILE   A C   1 
ATOM   4388  O  O   . ILE   A 1 554  ? -37.31800  90.87700  34.38500  1.000 67.79640  ?  554  ILE   A O   1 
ATOM   4389  C  CB  . ILE   A 1 554  ? -39.00600  93.05200  32.69300  1.000 38.66896  ?  554  ILE   A CB  1 
ATOM   4390  C  CG1 . ILE   A 1 554  ? -38.60800  91.87200  31.80400  1.000 33.49005  ?  554  ILE   A CG1 1 
ATOM   4391  C  CG2 . ILE   A 1 554  ? -38.86400  94.35500  31.91900  1.000 40.61206  ?  554  ILE   A CG2 1 
ATOM   4392  C  CD1 . ILE   A 1 554  ? -39.71300  91.39400  30.89300  1.000 40.85800  ?  554  ILE   A CD1 1 
ATOM   4393  N  N   . VAL   A 1 555  ? -39.08400  91.56500  35.60600  1.000 51.75482  ?  555  VAL   A N   1 
ATOM   4394  C  CA  . VAL   A 1 555  ? -39.35800  90.25100  36.17300  1.000 69.92341  ?  555  VAL   A CA  1 
ATOM   4395  C  C   . VAL   A 1 555  ? -40.40000  89.57600  35.29100  1.000 56.27291  ?  555  VAL   A C   1 
ATOM   4396  O  O   . VAL   A 1 555  ? -41.39800  90.19500  34.90000  1.000 49.34167  ?  555  VAL   A O   1 
ATOM   4397  C  CB  . VAL   A 1 555  ? -39.80900  90.35300  37.64500  1.000 69.84811  ?  555  VAL   A CB  1 
ATOM   4398  C  CG1 . VAL   A 1 555  ? -41.19800  90.95900  37.78200  1.000 58.88210  ?  555  VAL   A CG1 1 
ATOM   4399  C  CG2 . VAL   A 1 555  ? -39.75000  88.98400  38.32500  1.000 67.55981  ?  555  VAL   A CG2 1 
ATOM   4400  N  N   . HIS   A 1 556  ? -40.13700  88.33200  34.92000  1.000 59.18487  ?  556  HIS   A N   1 
ATOM   4401  C  CA  . HIS   A 1 556  ? -40.97000  87.68100  33.92200  1.000 54.10283  ?  556  HIS   A CA  1 
ATOM   4402  C  C   . HIS   A 1 556  ? -42.37000  87.46300  34.47700  1.000 63.53583  ?  556  HIS   A C   1 
ATOM   4403  O  O   . HIS   A 1 556  ? -42.51500  86.96800  35.60100  1.000 69.69939  ?  556  HIS   A O   1 
ATOM   4404  C  CB  . HIS   A 1 556  ? -40.38200  86.35300  33.48300  1.000 57.05864  ?  556  HIS   A CB  1 
ATOM   4405  C  CG  . HIS   A 1 556  ? -40.96400  85.84700  32.20200  1.000 56.85708  ?  556  HIS   A CG  1 
ATOM   4406  N  ND1 . HIS   A 1 556  ? -41.99300  84.93200  32.16000  1.000 62.15314  ?  556  HIS   A ND1 1 
ATOM   4407  C  CD2 . HIS   A 1 556  ? -40.68400  86.15800  30.91400  1.000 53.06634  ?  556  HIS   A CD2 1 
ATOM   4408  C  CE1 . HIS   A 1 556  ? -42.30800  84.68500  30.90100  1.000 60.25263  ?  556  HIS   A CE1 1 
ATOM   4409  N  NE2 . HIS   A 1 556  ? -41.52900  85.41700  30.12500  1.000 51.69266  ?  556  HIS   A NE2 1 
ATOM   4410  N  N   . PRO   A 1 557  ? -43.41600  87.80800  33.72500  1.000 67.66199  ?  557  PRO   A N   1 
ATOM   4411  C  CA  . PRO   A 1 557  ? -44.78100  87.68400  34.25800  1.000 58.72840  ?  557  PRO   A CA  1 
ATOM   4412  C  C   . PRO   A 1 557  ? -45.15600  86.27100  34.65500  1.000 54.77505  ?  557  PRO   A C   1 
ATOM   4413  O  O   . PRO   A 1 557  ? -46.03800  86.09800  35.50400  1.000 74.54046  ?  557  PRO   A O   1 
ATOM   4414  C  CB  . PRO   A 1 557  ? -45.65600  88.18700  33.10200  1.000 40.37174  ?  557  PRO   A CB  1 
ATOM   4415  C  CG  . PRO   A 1 557  ? -44.74500  89.03500  32.27300  1.000 62.48200  ?  557  PRO   A CG  1 
ATOM   4416  C  CD  . PRO   A 1 557  ? -43.39800  88.39000  32.37300  1.000 65.06091  ?  557  PRO   A CD  1 
ATOM   4417  N  N   . GLN   A 1 558  ? -44.51500  85.25600  34.08400  1.000 55.91619  ?  558  GLN   A N   1 
ATOM   4418  C  CA  . GLN   A 1 558  ? -44.86900  83.87000  34.35700  1.000 55.32205  ?  558  GLN   A CA  1 
ATOM   4419  C  C   . GLN   A 1 558  ? -43.77900  83.10700  35.09300  1.000 65.65099  ?  558  GLN   A C   1 
ATOM   4420  O  O   . GLN   A 1 558  ? -44.05700  82.47800  36.11900  1.000 76.96785  ?  558  GLN   A O   1 
ATOM   4421  C  CB  . GLN   A 1 558  ? -45.22300  83.15900  33.04500  1.000 55.16998  ?  558  GLN   A CB  1 
ATOM   4422  C  CG  . GLN   A 1 558  ? -46.54700  83.62200  32.46100  1.000 52.57837  ?  558  GLN   A CG  1 
ATOM   4423  C  CD  . GLN   A 1 558  ? -46.42100  84.11200  31.03400  1.000 50.46448  ?  558  GLN   A CD  1 
ATOM   4424  O  OE1 . GLN   A 1 558  ? -45.53500  83.68700  30.29300  1.000 60.17618  ?  558  GLN   A OE1 1 
ATOM   4425  N  NE2 . GLN   A 1 558  ? -47.30400  85.02400  30.64500  1.000 40.83681  ?  558  GLN   A NE2 1 
ATOM   4426  N  N   . THR   A 1 559  ? -42.53900  83.14400  34.60500  1.000 63.26305  ?  559  THR   A N   1 
ATOM   4427  C  CA  . THR   A 1 559  ? -41.46100  82.42600  35.27500  1.000 75.93397  ?  559  THR   A CA  1 
ATOM   4428  C  C   . THR   A 1 559  ? -40.98600  83.11600  36.54900  1.000 66.68659  ?  559  THR   A C   1 
ATOM   4429  O  O   . THR   A 1 559  ? -40.18900  82.52700  37.28700  1.000 45.66054  ?  559  THR   A O   1 
ATOM   4430  C  CB  . THR   A 1 559  ? -40.27400  82.22400  34.32200  1.000 75.12296  ?  559  THR   A CB  1 
ATOM   4431  O  OG1 . THR   A 1 559  ? -39.40100  83.35900  34.37700  1.000 69.78111  ?  559  THR   A OG1 1 
ATOM   4432  C  CG2 . THR   A 1 559  ? -40.76000  82.02300  32.89400  1.000 64.25882  ?  559  THR   A CG2 1 
ATOM   4433  N  N   . GLY   A 1 560  ? -41.46100  84.33200  36.82700  1.000 59.19447  ?  560  GLY   A N   1 
ATOM   4434  C  CA  . GLY   A 1 560  ? -41.09700  85.05000  38.03500  1.000 57.77388  ?  560  GLY   A CA  1 
ATOM   4435  C  C   . GLY   A 1 560  ? -39.60400  85.22700  38.21600  1.000 71.10469  ?  560  GLY   A C   1 
ATOM   4436  O  O   . GLY   A 1 560  ? -39.07000  84.99600  39.30600  1.000 72.94207  ?  560  GLY   A O   1 
ATOM   4437  N  N   . GLU   A 1 561  ? -38.91900  85.63800  37.15300  1.000 66.69313  ?  561  GLU   A N   1 
ATOM   4438  C  CA  . GLU   A 1 561  ? -37.47000  85.76200  37.14400  1.000 56.24288  ?  561  GLU   A CA  1 
ATOM   4439  C  C   . GLU   A 1 561  ? -37.08200  87.12100  36.59000  1.000 54.50505  ?  561  GLU   A C   1 
ATOM   4440  O  O   . GLU   A 1 561  ? -37.64800  87.57500  35.59100  1.000 56.42129  ?  561  GLU   A O   1 
ATOM   4441  C  CB  . GLU   A 1 561  ? -36.82200  84.66700  36.29000  1.000 62.31539  ?  561  GLU   A CB  1 
ATOM   4442  C  CG  . GLU   A 1 561  ? -36.78800  83.28700  36.91800  1.000 62.36860  ?  561  GLU   A CG  1 
ATOM   4443  C  CD  . GLU   A 1 561  ? -36.13600  82.26100  36.00700  1.000 89.56629  ?  561  GLU   A CD  1 
ATOM   4444  O  OE1 . GLU   A 1 561  ? -36.44300  82.26000  34.79600  1.000 82.20807  ?  561  GLU   A OE1 1 
ATOM   4445  O  OE2 . GLU   A 1 561  ? -35.30500  81.46700  36.49700  1.000 95.17832  -1 561  GLU   A OE2 1 
ATOM   4446  N  N   . ARG   A 1 562  ? -36.10900  87.76300  37.23000  1.000 49.50324  ?  562  ARG   A N   1 
ATOM   4447  C  CA  . ARG   A 1 562  ? -35.58200  89.00800  36.69400  1.000 55.78395  ?  562  ARG   A CA  1 
ATOM   4448  C  C   . ARG   A 1 562  ? -34.80200  88.71700  35.41700  1.000 48.32728  ?  562  ARG   A C   1 
ATOM   4449  O  O   . ARG   A 1 562  ? -33.94300  87.83200  35.38500  1.000 48.45311  ?  562  ARG   A O   1 
ATOM   4450  C  CB  . ARG   A 1 562  ? -34.69900  89.71300  37.72500  1.000 30.76799  ?  562  ARG   A CB  1 
ATOM   4451  C  CG  . ARG   A 1 562  ? -34.44200  91.17300  37.38900  1.000 38.28420  ?  562  ARG   A CG  1 
ATOM   4452  C  CD  . ARG   A 1 562  ? -34.06800  91.99500  38.61400  1.000 39.12788  ?  562  ARG   A CD  1 
ATOM   4453  N  NE  . ARG   A 1 562  ? -32.64400  91.90800  38.91000  1.000 50.73222  ?  562  ARG   A NE  1 
ATOM   4454  C  CZ  . ARG   A 1 562  ? -31.77200  92.88100  38.68100  1.000 40.25255  ?  562  ARG   A CZ  1 
ATOM   4455  N  NH1 . ARG   A 1 562  ? -32.15100  94.04200  38.16900  1.000 37.52232  ?  562  ARG   A NH1 1 
ATOM   4456  N  NH2 . ARG   A 1 562  ? -30.48800  92.68100  38.96300  1.000 44.80879  ?  562  ARG   A NH2 1 
ATOM   4457  N  N   . MET   A 1 563  ? -35.12800  89.44600  34.35900  1.000 30.69558  ?  563  MET   A N   1 
ATOM   4458  C  CA  . MET   A 1 563  ? -34.54900  89.24100  33.04300  1.000 31.46638  ?  563  MET   A CA  1 
ATOM   4459  C  C   . MET   A 1 563  ? -34.13100  90.58200  32.46800  1.000 48.24955  ?  563  MET   A C   1 
ATOM   4460  O  O   . MET   A 1 563  ? -34.75700  91.60900  32.73900  1.000 42.85962  ?  563  MET   A O   1 
ATOM   4461  C  CB  . MET   A 1 563  ? -35.54500  88.56100  32.09500  1.000 44.86940  ?  563  MET   A CB  1 
ATOM   4462  C  CG  . MET   A 1 563  ? -36.10500  87.24900  32.60800  1.000 43.62709  ?  563  MET   A CG  1 
ATOM   4463  S  SD  . MET   A 1 563  ? -37.00700  86.34300  31.33600  1.000 48.40843  ?  563  MET   A SD  1 
ATOM   4464  C  CE  . MET   A 1 563  ? -37.50100  84.88500  32.24800  1.000 37.97488  ?  563  MET   A CE  1 
ATOM   4465  N  N   . TYR   A 1 564  ? -33.07000  90.56800  31.66800  1.000 38.87517  ?  564  TYR   A N   1 
ATOM   4466  C  CA  . TYR   A 1 564  ? -32.62100  91.76600  30.97600  1.000 38.63515  ?  564  TYR   A CA  1 
ATOM   4467  C  C   . TYR   A 1 564  ? -33.03900  91.69900  29.51000  1.000 52.26878  ?  564  TYR   A C   1 
ATOM   4468  O  O   . TYR   A 1 564  ? -32.74000  90.71900  28.81700  1.000 46.32477  ?  564  TYR   A O   1 
ATOM   4469  C  CB  . TYR   A 1 564  ? -31.10700  91.93900  31.09300  1.000 36.40121  ?  564  TYR   A CB  1 
ATOM   4470  C  CG  . TYR   A 1 564  ? -30.59100  93.12300  30.31000  1.000 27.70948  ?  564  TYR   A CG  1 
ATOM   4471  C  CD1 . TYR   A 1 564  ? -30.86800  94.42200  30.71600  1.000 23.29094  ?  564  TYR   A CD1 1 
ATOM   4472  C  CD2 . TYR   A 1 564  ? -29.84600  92.94300  29.15300  1.000 33.04884  ?  564  TYR   A CD2 1 
ATOM   4473  C  CE1 . TYR   A 1 564  ? -30.40600  95.51100  29.99600  1.000 26.53081  ?  564  TYR   A CE1 1 
ATOM   4474  C  CE2 . TYR   A 1 564  ? -29.37900  94.02600  28.42500  1.000 45.50670  ?  564  TYR   A CE2 1 
ATOM   4475  C  CZ  . TYR   A 1 564  ? -29.66100  95.30700  28.85100  1.000 30.30199  ?  564  TYR   A CZ  1 
ATOM   4476  O  OH  . TYR   A 1 564  ? -29.19800  96.38300  28.12600  1.000 42.69912  ?  564  TYR   A OH  1 
ATOM   4477  N  N   . ARG   A 1 565  ? -33.74200  92.73500  29.05200  1.000 43.03019  ?  565  ARG   A N   1 
ATOM   4478  C  CA  . ARG   A 1 565  ? -34.11300  92.87800  27.64600  1.000 35.54593  ?  565  ARG   A CA  1 
ATOM   4479  C  C   . ARG   A 1 565  ? -32.90200  93.36200  26.86100  1.000 33.01327  ?  565  ARG   A C   1 
ATOM   4480  O  O   . ARG   A 1 565  ? -32.50500  94.52500  26.97700  1.000 39.54073  ?  565  ARG   A O   1 
ATOM   4481  C  CB  . ARG   A 1 565  ? -35.26700  93.86500  27.49500  1.000 59.29608  ?  565  ARG   A CB  1 
ATOM   4482  C  CG  . ARG   A 1 565  ? -36.63600  93.23600  27.53300  1.000 64.86098  ?  565  ARG   A CG  1 
ATOM   4483  C  CD  . ARG   A 1 565  ? -37.72000  94.24900  27.22400  1.000 67.43935  ?  565  ARG   A CD  1 
ATOM   4484  N  NE  . ARG   A 1 565  ? -38.47100  93.88300  26.03100  1.000 64.66912  ?  565  ARG   A NE  1 
ATOM   4485  C  CZ  . ARG   A 1 565  ? -39.72200  93.44300  26.04300  1.000 69.86875  ?  565  ARG   A CZ  1 
ATOM   4486  N  NH1 . ARG   A 1 565  ? -40.39000  93.29100  27.17500  1.000 54.96897  ?  565  ARG   A NH1 1 
ATOM   4487  N  NH2 . ARG   A 1 565  ? -40.31600  93.14500  24.89100  1.000 87.41850  ?  565  ARG   A NH2 1 
ATOM   4488  N  N   . THR   A 1 566  ? -32.32200  92.48700  26.04100  1.000 29.93811  ?  566  THR   A N   1 
ATOM   4489  C  CA  . THR   A 1 566  ? -31.14400  92.88800  25.27900  1.000 31.91473  ?  566  THR   A CA  1 
ATOM   4490  C  C   . THR   A 1 566  ? -31.50700  93.83600  24.14300  1.000 43.91864  ?  566  THR   A C   1 
ATOM   4491  O  O   . THR   A 1 566  ? -30.74000  94.75200  23.82400  1.000 50.85789  ?  566  THR   A O   1 
ATOM   4492  C  CB  . THR   A 1 566  ? -30.42700  91.66000  24.72700  1.000 28.38884  ?  566  THR   A CB  1 
ATOM   4493  O  OG1 . THR   A 1 566  ? -31.33800  90.89400  23.92700  1.000 41.86890  ?  566  THR   A OG1 1 
ATOM   4494  C  CG2 . THR   A 1 566  ? -29.90800  90.79800  25.86500  1.000 42.65008  ?  566  THR   A CG2 1 
ATOM   4495  N  N   . GLY   A 1 567  ? -32.67200  93.64300  23.53000  1.000 40.20435  ?  567  GLY   A N   1 
ATOM   4496  C  CA  . GLY   A 1 567  ? -32.96200  94.29600  22.27200  1.000 39.23973  ?  567  GLY   A CA  1 
ATOM   4497  C  C   . GLY   A 1 567  ? -32.29500  93.65100  21.08100  1.000 46.42062  ?  567  GLY   A C   1 
ATOM   4498  O  O   . GLY   A 1 567  ? -32.37600  94.19200  19.97200  1.000 45.96684  ?  567  GLY   A O   1 
ATOM   4499  N  N   . ASP   A 1 568  ? -31.64200  92.50900  21.28000  1.000 48.56282  ?  568  ASP   A N   1 
ATOM   4500  C  CA  . ASP   A 1 568  ? -30.91300  91.80200  20.24000  1.000 45.56796  ?  568  ASP   A CA  1 
ATOM   4501  C  C   . ASP   A 1 568  ? -31.66700  90.54000  19.84400  1.000 47.44808  ?  568  ASP   A C   1 
ATOM   4502  O  O   . ASP   A 1 568  ? -32.23100  89.84700  20.69800  1.000 39.03193  ?  568  ASP   A O   1 
ATOM   4503  C  CB  . ASP   A 1 568  ? -29.50500  91.43100  20.71500  1.000 42.92838  ?  568  ASP   A CB  1 
ATOM   4504  C  CG  . ASP   A 1 568  ? -28.65800  92.64500  21.05100  1.000 57.89963  ?  568  ASP   A CG  1 
ATOM   4505  O  OD1 . ASP   A 1 568  ? -28.67700  93.63100  20.28200  1.000 62.63641  ?  568  ASP   A OD1 1 
ATOM   4506  O  OD2 . ASP   A 1 568  ? -27.97200  92.60900  22.09300  1.000 69.96638  -1 568  ASP   A OD2 1 
ATOM   4507  N  N   . ARG   A 1 569  ? -31.66800  90.24500  18.54800  1.000 46.41201  ?  569  ARG   A N   1 
ATOM   4508  C  CA  . ARG   A 1 569  ? -32.32600  89.05700  18.02800  1.000 36.51880  ?  569  ARG   A CA  1 
ATOM   4509  C  C   . ARG   A 1 569  ? -31.32100  87.92100  17.90600  1.000 44.13328  ?  569  ARG   A C   1 
ATOM   4510  O  O   . ARG   A 1 569  ? -30.19600  88.11600  17.43500  1.000 45.33062  ?  569  ARG   A O   1 
ATOM   4511  C  CB  . ARG   A 1 569  ? -32.96900  89.34400  16.67100  1.000 43.45273  ?  569  ARG   A CB  1 
ATOM   4512  C  CG  . ARG   A 1 569  ? -33.36300  88.10200  15.87800  1.000 54.96412  ?  569  ARG   A CG  1 
ATOM   4513  C  CD  . ARG   A 1 569  ? -34.13500  88.46900  14.61400  1.000 50.92132  ?  569  ARG   A CD  1 
ATOM   4514  N  NE  . ARG   A 1 569  ? -34.07500  89.90300  14.36500  1.000 55.02649  ?  569  ARG   A NE  1 
ATOM   4515  C  CZ  . ARG   A 1 569  ? -33.21200  90.48200  13.54300  1.000 71.54846  ?  569  ARG   A CZ  1 
ATOM   4516  N  NH1 . ARG   A 1 569  ? -32.37500  89.77000  12.80600  1.000 70.48636  ?  569  ARG   A NH1 1 
ATOM   4517  N  NH2 . ARG   A 1 569  ? -33.17400  91.80700  13.47200  1.000 75.36972  ?  569  ARG   A NH2 1 
ATOM   4518  N  N   . ALA   A 1 570  ? -31.73100  86.73400  18.34300  1.000 36.69401  ?  570  ALA   A N   1 
ATOM   4519  C  CA  . ALA   A 1 570  ? -30.85800  85.57000  18.30800  1.000 36.93079  ?  570  ALA   A CA  1 
ATOM   4520  C  C   . ALA   A 1 570  ? -31.72000  84.31900  18.27100  1.000 44.85916  ?  570  ALA   A C   1 
ATOM   4521  O  O   . ALA   A 1 570  ? -32.93000  84.36400  18.50400  1.000 55.24532  ?  570  ALA   A O   1 
ATOM   4522  C  CB  . ALA   A 1 570  ? -29.90600  85.54800  19.50800  1.000 42.44675  ?  570  ALA   A CB  1 
ATOM   4523  N  N   . ARG   A 1 571  ? -31.07600  83.19500  17.97000  1.000 42.34179  ?  571  ARG   A N   1 
ATOM   4524  C  CA  . ARG   A 1 571  ? -31.74000  81.90300  17.95200  1.000 39.16880  ?  571  ARG   A CA  1 
ATOM   4525  C  C   . ARG   A 1 571  ? -30.81400  80.85600  18.55200  1.000 44.90338  ?  571  ARG   A C   1 
ATOM   4526  O  O   . ARG   A 1 571  ? -29.58900  80.93800  18.42300  1.000 42.88828  ?  571  ARG   A O   1 
ATOM   4527  C  CB  . ARG   A 1 571  ? -32.15600  81.49600  16.52800  1.000 42.58157  ?  571  ARG   A CB  1 
ATOM   4528  C  CG  . ARG   A 1 571  ? -31.07600  80.76100  15.74100  1.000 44.51747  ?  571  ARG   A CG  1 
ATOM   4529  C  CD  . ARG   A 1 571  ? -31.65900  79.96700  14.58700  1.000 50.04178  ?  571  ARG   A CD  1 
ATOM   4530  N  NE  . ARG   A 1 571  ? -32.08600  80.82100  13.48600  1.000 55.83372  ?  571  ARG   A NE  1 
ATOM   4531  C  CZ  . ARG   A 1 571  ? -31.39100  81.00300  12.37200  1.000 69.28674  ?  571  ARG   A CZ  1 
ATOM   4532  N  NH1 . ARG   A 1 571  ? -30.24000  80.38300  12.16900  1.000 69.03940  ?  571  ARG   A NH1 1 
ATOM   4533  N  NH2 . ARG   A 1 571  ? -31.86400  81.82400  11.43800  1.000 63.18818  ?  571  ARG   A NH2 1 
ATOM   4534  N  N   . PHE   A 1 572  ? -31.40900  79.88300  19.23500  1.000 51.41852  ?  572  PHE   A N   1 
ATOM   4535  C  CA  . PHE   A 1 572  ? -30.65900  78.72800  19.70400  1.000 38.90638  ?  572  PHE   A CA  1 
ATOM   4536  C  C   . PHE   A 1 572  ? -30.41400  77.77700  18.54400  1.000 39.68122  ?  572  PHE   A C   1 
ATOM   4537  O  O   . PHE   A 1 572  ? -31.29400  77.55600  17.70700  1.000 50.12227  ?  572  PHE   A O   1 
ATOM   4538  C  CB  . PHE   A 1 572  ? -31.41400  77.99900  20.81800  1.000 33.84822  ?  572  PHE   A CB  1 
ATOM   4539  C  CG  . PHE   A 1 572  ? -30.98200  78.38200  22.20300  1.000 34.94298  ?  572  PHE   A CG  1 
ATOM   4540  C  CD1 . PHE   A 1 572  ? -29.77500  77.93600  22.71700  1.000 42.12123  ?  572  PHE   A CD1 1 
ATOM   4541  C  CD2 . PHE   A 1 572  ? -31.78800  79.18100  22.99800  1.000 31.74908  ?  572  PHE   A CD2 1 
ATOM   4542  C  CE1 . PHE   A 1 572  ? -29.37700  78.28400  23.99600  1.000 52.22650  ?  572  PHE   A CE1 1 
ATOM   4543  C  CE2 . PHE   A 1 572  ? -31.39600  79.53500  24.27600  1.000 47.82651  ?  572  PHE   A CE2 1 
ATOM   4544  C  CZ  . PHE   A 1 572  ? -30.18900  79.08600  24.77600  1.000 53.04945  ?  572  PHE   A CZ  1 
ATOM   4545  N  N   . LEU   A 1 573  ? -29.22300  77.22900  18.48900  1.000 38.15439  ?  573  LEU   A N   1 
ATOM   4546  C  CA  . LEU   A 1 573  ? -28.93700  76.18100  17.52900  1.000 45.44966  ?  573  LEU   A CA  1 
ATOM   4547  C  C   . LEU   A 1 573  ? -29.05600  74.82000  18.20400  1.000 47.83586  ?  573  LEU   A C   1 
ATOM   4548  O  O   . LEU   A 1 573  ? -29.03200  74.72600  19.43400  1.000 52.91626  ?  573  LEU   A O   1 
ATOM   4549  C  CB  . LEU   A 1 573  ? -27.53300  76.36800  16.94100  1.000 39.49133  ?  573  LEU   A CB  1 
ATOM   4550  C  CG  . LEU   A 1 573  ? -27.22400  77.73200  16.32000  1.000 44.48281  ?  573  LEU   A CG  1 
ATOM   4551  C  CD1 . LEU   A 1 573  ? -25.73300  77.89200  16.06900  1.000 44.58241  ?  573  LEU   A CD1 1 
ATOM   4552  C  CD2 . LEU   A 1 573  ? -28.00000  77.92000  15.03500  1.000 49.36953  ?  573  LEU   A CD2 1 
ATOM   4553  N  N   . PRO   A 1 574  ? -29.21000  73.73900  17.43300  1.000 48.56271  ?  574  PRO   A N   1 
ATOM   4554  C  CA  . PRO   A 1 574  ? -29.38900  72.41400  18.05500  1.000 38.30722  ?  574  PRO   A CA  1 
ATOM   4555  C  C   . PRO   A 1 574  ? -28.23000  71.95400  18.93100  1.000 46.72792  ?  574  PRO   A C   1 
ATOM   4556  O  O   . PRO   A 1 574  ? -28.43200  71.05700  19.75800  1.000 58.36882  ?  574  PRO   A O   1 
ATOM   4557  C  CB  . PRO   A 1 574  ? -29.57100  71.48000  16.84900  1.000 30.55751  ?  574  PRO   A CB  1 
ATOM   4558  C  CG  . PRO   A 1 574  ? -29.11700  72.26700  15.66000  1.000 47.32482  ?  574  PRO   A CG  1 
ATOM   4559  C  CD  . PRO   A 1 574  ? -29.43200  73.68600  15.98000  1.000 45.59467  ?  574  PRO   A CD  1 
ATOM   4560  N  N   . ASP   A 1 575  ? -27.03100  72.52200  18.78100  1.000 57.72826  ?  575  ASP   A N   1 
ATOM   4561  C  CA  . ASP   A 1 575  ? -25.88900  72.09900  19.58600  1.000 51.43765  ?  575  ASP   A CA  1 
ATOM   4562  C  C   . ASP   A 1 575  ? -25.92900  72.64700  21.00700  1.000 53.62329  ?  575  ASP   A C   1 
ATOM   4563  O  O   . ASP   A 1 575  ? -25.12400  72.22100  21.84200  1.000 65.63038  ?  575  ASP   A O   1 
ATOM   4564  C  CB  . ASP   A 1 575  ? -24.57900  72.53300  18.92100  1.000 40.16245  ?  575  ASP   A CB  1 
ATOM   4565  C  CG  . ASP   A 1 575  ? -24.61100  73.97500  18.47100  1.000 60.11923  ?  575  ASP   A CG  1 
ATOM   4566  O  OD1 . ASP   A 1 575  ? -25.68200  74.60000  18.60500  1.000 65.99871  ?  575  ASP   A OD1 1 
ATOM   4567  O  OD2 . ASP   A 1 575  ? -23.57600  74.48300  17.98800  1.000 79.49989  -1 575  ASP   A OD2 1 
ATOM   4568  N  N   . GLY   A 1 576  ? -26.83900  73.57100  21.30000  1.000 50.37634  ?  576  GLY   A N   1 
ATOM   4569  C  CA  . GLY   A 1 576  ? -26.87800  74.24800  22.57600  1.000 51.43362  ?  576  GLY   A CA  1 
ATOM   4570  C  C   . GLY   A 1 576  ? -26.31000  75.64800  22.55000  1.000 47.62949  ?  576  GLY   A C   1 
ATOM   4571  O  O   . GLY   A 1 576  ? -26.36900  76.34400  23.57300  1.000 56.54232  ?  576  GLY   A O   1 
ATOM   4572  N  N   . ASN   A 1 577  ? -25.76700  76.07600  21.41500  1.000 33.81332  ?  577  ASN   A N   1 
ATOM   4573  C  CA  . ASN   A 1 577  ? -25.18000  77.39700  21.27100  1.000 47.35139  ?  577  ASN   A CA  1 
ATOM   4574  C  C   . ASN   A 1 577  ? -26.23400  78.41200  20.83600  1.000 46.37689  ?  577  ASN   A C   1 
ATOM   4575  O  O   . ASN   A 1 577  ? -27.33400  78.06900  20.40100  1.000 60.74348  ?  577  ASN   A O   1 
ATOM   4576  C  CB  . ASN   A 1 577  ? -24.02700  77.37100  20.26300  1.000 43.26960  ?  577  ASN   A CB  1 
ATOM   4577  C  CG  . ASN   A 1 577  ? -22.76400  76.72700  20.82100  1.000 47.40502  ?  577  ASN   A CG  1 
ATOM   4578  O  OD1 . ASN   A 1 577  ? -21.99200  77.36600  21.53700  1.000 55.04656  ?  577  ASN   A OD1 1 
ATOM   4579  N  ND2 . ASN   A 1 577  ? -22.53500  75.46800  20.46800  1.000 39.24726  ?  577  ASN   A ND2 1 
ATOM   4580  N  N   . ILE   A 1 578  ? -25.87800  79.68400  20.96800  1.000 40.23202  ?  578  ILE   A N   1 
ATOM   4581  C  CA  . ILE   A 1 578  ? -26.70000  80.78900  20.50000  1.000 44.77499  ?  578  ILE   A CA  1 
ATOM   4582  C  C   . ILE   A 1 578  ? -25.92800  81.51100  19.40700  1.000 38.19550  ?  578  ILE   A C   1 
ATOM   4583  O  O   . ILE   A 1 578  ? -24.69300  81.52000  19.40400  1.000 42.06469  ?  578  ILE   A O   1 
ATOM   4584  C  CB  . ILE   A 1 578  ? -27.07400  81.75900  21.64500  1.000 40.60717  ?  578  ILE   A CB  1 
ATOM   4585  C  CG1 . ILE   A 1 578  ? -27.56700  80.98700  22.86700  1.000 28.62631  ?  578  ILE   A CG1 1 
ATOM   4586  C  CG2 . ILE   A 1 578  ? -28.13700  82.74900  21.19600  1.000 38.01195  ?  578  ILE   A CG2 1 
ATOM   4587  C  CD1 . ILE   A 1 578  ? -26.82600  81.32100  24.13900  1.000 35.94641  ?  578  ILE   A CD1 1 
ATOM   4588  N  N   . GLU   A 1 579  ? -26.65600  82.11000  18.46800  1.000 39.13930  ?  579  GLU   A N   1 
ATOM   4589  C  CA  . GLU   A 1 579  ? -26.02900  82.88200  17.40500  1.000 48.64418  ?  579  GLU   A CA  1 
ATOM   4590  C  C   . GLU   A 1 579  ? -26.73400  84.22300  17.25100  1.000 42.14511  ?  579  GLU   A C   1 
ATOM   4591  O  O   . GLU   A 1 579  ? -27.96600  84.28600  17.20400  1.000 42.36604  ?  579  GLU   A O   1 
ATOM   4592  C  CB  . GLU   A 1 579  ? -26.01700  82.10100  16.08400  1.000 47.32098  ?  579  GLU   A CB  1 
ATOM   4593  C  CG  . GLU   A 1 579  ? -27.37100  81.80400  15.47200  1.000 47.25409  ?  579  GLU   A CG  1 
ATOM   4594  C  CD  . GLU   A 1 579  ? -27.25800  81.32000  14.03600  1.000 51.24446  ?  579  GLU   A CD  1 
ATOM   4595  O  OE1 . GLU   A 1 579  ? -26.13800  80.96900  13.61100  1.000 62.24658  ?  579  GLU   A OE1 1 
ATOM   4596  O  OE2 . GLU   A 1 579  ? -28.28800  81.29000  13.33100  1.000 67.19903  -1 579  GLU   A OE2 1 
ATOM   4597  N  N   . PHE   A 1 580  ? -25.93900  85.28900  17.19600  1.000 46.73240  ?  580  PHE   A N   1 
ATOM   4598  C  CA  . PHE   A 1 580  ? -26.46300  86.64000  17.05300  1.000 40.36138  ?  580  PHE   A CA  1 
ATOM   4599  C  C   . PHE   A 1 580  ? -27.05700  86.82800  15.66100  1.000 44.33445  ?  580  PHE   A C   1 
ATOM   4600  O  O   . PHE   A 1 580  ? -26.40600  86.53900  14.65400  1.000 48.63588  ?  580  PHE   A O   1 
ATOM   4601  C  CB  . PHE   A 1 580  ? -25.33700  87.64500  17.30000  1.000 35.79028  ?  580  PHE   A CB  1 
ATOM   4602  C  CG  . PHE   A 1 580  ? -25.78900  89.07400  17.36100  1.000 27.53677  ?  580  PHE   A CG  1 
ATOM   4603  C  CD1 . PHE   A 1 580  ? -26.60400  89.51600  18.38800  1.000 24.11164  ?  580  PHE   A CD1 1 
ATOM   4604  C  CD2 . PHE   A 1 580  ? -25.37700  89.98200  16.40000  1.000 22.54605  ?  580  PHE   A CD2 1 
ATOM   4605  C  CE1 . PHE   A 1 580  ? -27.01000  90.83500  18.44700  1.000 41.08887  ?  580  PHE   A CE1 1 
ATOM   4606  C  CE2 . PHE   A 1 580  ? -25.77900  91.30100  16.45400  1.000 29.78026  ?  580  PHE   A CE2 1 
ATOM   4607  C  CZ  . PHE   A 1 580  ? -26.59800  91.72900  17.47800  1.000 44.50999  ?  580  PHE   A CZ  1 
ATOM   4608  N  N   . LEU   A 1 581  ? -28.29900  87.31100  15.60300  1.000 43.79137  ?  581  LEU   A N   1 
ATOM   4609  C  CA  . LEU   A 1 581  ? -28.98700  87.52800  14.33500  1.000 43.59626  ?  581  LEU   A CA  1 
ATOM   4610  C  C   . LEU   A 1 581  ? -29.20200  89.00400  14.02700  1.000 44.47616  ?  581  LEU   A C   1 
ATOM   4611  O  O   . LEU   A 1 581  ? -29.86800  89.33000  13.03900  1.000 56.82474  ?  581  LEU   A O   1 
ATOM   4612  C  CB  . LEU   A 1 581  ? -30.33000  86.79200  14.32500  1.000 35.45235  ?  581  LEU   A CB  1 
ATOM   4613  C  CG  . LEU   A 1 581  ? -30.29200  85.28000  14.55000  1.000 34.58984  ?  581  LEU   A CG  1 
ATOM   4614  C  CD1 . LEU   A 1 581  ? -31.66800  84.67600  14.35300  1.000 44.48657  ?  581  LEU   A CD1 1 
ATOM   4615  C  CD2 . LEU   A 1 581  ? -29.29200  84.62800  13.61800  1.000 39.55785  ?  581  LEU   A CD2 1 
ATOM   4616  N  N   . GLY   A 1 582  ? -28.66300  89.89800  14.84200  1.000 40.93969  ?  582  GLY   A N   1 
ATOM   4617  C  CA  . GLY   A 1 582  ? -28.80400  91.32500  14.64100  1.000 40.04151  ?  582  GLY   A CA  1 
ATOM   4618  C  C   . GLY   A 1 582  ? -29.67700  91.96800  15.70600  1.000 43.37323  ?  582  GLY   A C   1 
ATOM   4619  O  O   . GLY   A 1 582  ? -30.29400  91.30700  16.54200  1.000 49.21787  ?  582  GLY   A O   1 
ATOM   4620  N  N   . ARG   A 1 583  ? -29.71300  93.29800  15.65700  1.000 54.05873  ?  583  ARG   A N   1 
ATOM   4621  C  CA  . ARG   A 1 583  ? -30.54100  94.07000  16.57200  1.000 56.20887  ?  583  ARG   A CA  1 
ATOM   4622  C  C   . ARG   A 1 583  ? -31.97000  94.15700  16.05300  1.000 58.10381  ?  583  ARG   A C   1 
ATOM   4623  O  O   . ARG   A 1 583  ? -32.20300  94.25900  14.84500  1.000 67.41878  ?  583  ARG   A O   1 
ATOM   4624  C  CB  . ARG   A 1 583  ? -29.97200  95.47500  16.75900  1.000 55.50254  ?  583  ARG   A CB  1 
ATOM   4625  C  CG  . ARG   A 1 583  ? -28.57600  95.50600  17.34700  1.000 48.40597  ?  583  ARG   A CG  1 
ATOM   4626  C  CD  . ARG   A 1 583  ? -28.46900  96.54100  18.45500  1.000 69.16806  ?  583  ARG   A CD  1 
ATOM   4627  N  NE  . ARG   A 1 583  ? -29.40200  96.27600  19.54300  1.000 66.97497  ?  583  ARG   A NE  1 
ATOM   4628  C  CZ  . ARG   A 1 583  ? -29.22900  96.68200  20.79300  1.000 54.54704  ?  583  ARG   A CZ  1 
ATOM   4629  N  NH1 . ARG   A 1 583  ? -28.17100  97.39200  21.14900  1.000 82.28511  ?  583  ARG   A NH1 1 
ATOM   4630  N  NH2 . ARG   A 1 583  ? -30.13800  96.36500  21.71100  1.000 48.13381  ?  583  ARG   A NH2 1 
ATOM   4631  N  N   . LEU   A 1 584  ? -32.92900  94.13100  16.97900  1.000 51.56087  ?  584  LEU   A N   1 
ATOM   4632  C  CA  . LEU   A 1 584  ? -34.33900  94.15300  16.60700  1.000 51.54313  ?  584  LEU   A CA  1 
ATOM   4633  C  C   . LEU   A 1 584  ? -34.79100  95.49700  16.05200  1.000 57.98443  ?  584  LEU   A C   1 
ATOM   4634  O  O   . LEU   A 1 584  ? -35.96200  95.62900  15.68100  1.000 61.20139  ?  584  LEU   A O   1 
ATOM   4635  C  CB  . LEU   A 1 584  ? -35.20300  93.76300  17.80900  1.000 40.23937  ?  584  LEU   A CB  1 
ATOM   4636  C  CG  . LEU   A 1 584  ? -35.08000  92.29900  18.24000  1.000 50.33378  ?  584  LEU   A CG  1 
ATOM   4637  C  CD1 . LEU   A 1 584  ? -35.45300  92.12300  19.70300  1.000 42.44174  ?  584  LEU   A CD1 1 
ATOM   4638  C  CD2 . LEU   A 1 584  ? -35.93800  91.40500  17.35300  1.000 69.34353  ?  584  LEU   A CD2 1 
ATOM   4639  N  N   . ASP   A 1 585  ? -33.90600  96.48900  15.97900  1.000 68.79099  ?  585  ASP   A N   1 
ATOM   4640  C  CA  . ASP   A 1 585  ? -34.23000  97.76200  15.35700  1.000 70.00412  ?  585  ASP   A CA  1 
ATOM   4641  C  C   . ASP   A 1 585  ? -33.41000  98.07000  14.11500  1.000 78.81753  ?  585  ASP   A C   1 
ATOM   4642  O  O   . ASP   A 1 585  ? -33.80500  98.95000  13.34200  1.000 93.48931  ?  585  ASP   A O   1 
ATOM   4643  C  CB  . ASP   A 1 585  ? -34.08300  98.91000  16.37700  1.000 69.57334  ?  585  ASP   A CB  1 
ATOM   4644  C  CG  . ASP   A 1 585  ? -32.62500  99.23200  16.74100  1.000 103.96657 ?  585  ASP   A CG  1 
ATOM   4645  O  OD1 . ASP   A 1 585  ? -31.69900  99.05100  15.92200  1.000 94.93769  ?  585  ASP   A OD1 1 
ATOM   4646  O  OD2 . ASP   A 1 585  ? -32.40300  99.69000  17.88100  1.000 123.97934 -1 585  ASP   A OD2 1 
ATOM   4647  N  N   . ASN   A 1 586  ? -32.28900  97.37600  13.89800  1.000 75.45155  ?  586  ASN   A N   1 
ATOM   4648  C  CA  . ASN   A 1 586  ? -31.34100  97.71500  12.84300  1.000 82.03960  ?  586  ASN   A CA  1 
ATOM   4649  C  C   . ASN   A 1 586  ? -31.68300  97.07000  11.50700  1.000 72.67902  ?  586  ASN   A C   1 
ATOM   4650  O  O   . ASN   A 1 586  ? -30.77500  96.76500  10.72200  1.000 82.87601  ?  586  ASN   A O   1 
ATOM   4651  C  CB  . ASN   A 1 586  ? -29.92300  97.33200  13.27000  1.000 79.61200  ?  586  ASN   A CB  1 
ATOM   4652  C  CG  . ASN   A 1 586  ? -28.97200  98.51600  13.25900  1.000 81.56008  ?  586  ASN   A CG  1 
ATOM   4653  O  OD1 . ASN   A 1 586  ? -29.36500  99.64400  13.55700  1.000 91.35842  ?  586  ASN   A OD1 1 
ATOM   4654  N  ND2 . ASN   A 1 586  ? -27.71300  98.26400  12.91700  1.000 89.35415  ?  586  ASN   A ND2 1 
ATOM   4655  N  N   . LEU   A 1 587  ? -32.96300  96.85500  11.21900  1.000 57.50236  ?  587  LEU   A N   1 
ATOM   4656  C  CA  . LEU   A 1 587  ? -33.37300  96.35600  9.91600   1.000 59.73317  ?  587  LEU   A CA  1 
ATOM   4657  C  C   . LEU   A 1 587  ? -33.76000  97.53200  9.03200   1.000 65.54856  ?  587  LEU   A C   1 
ATOM   4658  O  O   . LEU   A 1 587  ? -34.55400  98.38800  9.43700   1.000 52.42881  ?  587  LEU   A O   1 
ATOM   4659  C  CB  . LEU   A 1 587  ? -34.54600  95.38600  10.03400  1.000 65.70831  ?  587  LEU   A CB  1 
ATOM   4660  C  CG  . LEU   A 1 587  ? -34.25200  94.05700  10.71800  1.000 70.47217  ?  587  LEU   A CG  1 
ATOM   4661  C  CD1 . LEU   A 1 587  ? -34.67500  94.18200  12.16800  1.000 71.73264  ?  587  LEU   A CD1 1 
ATOM   4662  C  CD2 . LEU   A 1 587  ? -34.97300  92.91800  10.02500  1.000 55.77832  ?  587  LEU   A CD2 1 
ATOM   4663  N  N   . VAL   A 1 588  ? -33.19100  97.57300  7.83400   1.000 58.58620  ?  588  VAL   A N   1 
ATOM   4664  C  CA  . VAL   A 1 588  ? -33.51400  98.59300  6.85200   1.000 49.59557  ?  588  VAL   A CA  1 
ATOM   4665  C  C   . VAL   A 1 588  ? -34.33400  97.94800  5.74500   1.000 62.34673  ?  588  VAL   A C   1 
ATOM   4666  O  O   . VAL   A 1 588  ? -34.32000  96.72900  5.54700   1.000 53.64371  ?  588  VAL   A O   1 
ATOM   4667  C  CB  . VAL   A 1 588  ? -32.25200  99.27100  6.28100   1.000 50.10703  ?  588  VAL   A CB  1 
ATOM   4668  C  CG1 . VAL   A 1 588  ? -31.76500  100.36700 7.21800   1.000 64.16783  ?  588  VAL   A CG1 1 
ATOM   4669  C  CG2 . VAL   A 1 588  ? -31.16600  98.23600  6.05800   1.000 50.48575  ?  588  VAL   A CG2 1 
ATOM   4670  N  N   . LYS   A 1 589  ? -35.06300  98.78600  5.01900   1.000 49.67062  ?  589  LYS   A N   1 
ATOM   4671  C  CA  . LYS   A 1 589  ? -35.91100  98.34700  3.92100   1.000 49.54148  ?  589  LYS   A CA  1 
ATOM   4672  C  C   . LYS   A 1 589  ? -35.24700  98.73500  2.60600   1.000 59.07356  ?  589  LYS   A C   1 
ATOM   4673  O  O   . LYS   A 1 589  ? -34.94400  99.91200  2.38200   1.000 68.72821  ?  589  LYS   A O   1 
ATOM   4674  C  CB  . LYS   A 1 589  ? -37.30700  98.95700  4.04100   1.000 59.61093  ?  589  LYS   A CB  1 
ATOM   4675  C  CG  . LYS   A 1 589  ? -38.03400  99.12500  2.72400   1.000 76.46200  ?  589  LYS   A CG  1 
ATOM   4676  C  CD  . LYS   A 1 589  ? -38.98800  100.30300 2.79000   1.000 75.59034  ?  589  LYS   A CD  1 
ATOM   4677  C  CE  . LYS   A 1 589  ? -40.24300  99.95700  3.57300   1.000 89.39078  ?  589  LYS   A CE  1 
ATOM   4678  N  NZ  . LYS   A 1 589  ? -41.45100  100.57800 2.96400   1.000 77.18619  ?  589  LYS   A NZ  1 
ATOM   4679  N  N   . ILE   A 1 590  ? -35.00600  97.74500  1.75100   1.000 46.10800  ?  590  ILE   A N   1 
ATOM   4680  C  CA  . ILE   A 1 590  ? -34.36400  97.94100  0.45700   1.000 43.20346  ?  590  ILE   A CA  1 
ATOM   4681  C  C   . ILE   A 1 590  ? -35.25900  97.32000  -0.60400  1.000 55.42794  ?  590  ILE   A C   1 
ATOM   4682  O  O   . ILE   A 1 590  ? -35.65600  96.15600  -0.47400  1.000 59.54632  ?  590  ILE   A O   1 
ATOM   4683  C  CB  . ILE   A 1 590  ? -32.95400  97.31500  0.41900   1.000 59.01390  ?  590  ILE   A CB  1 
ATOM   4684  C  CG1 . ILE   A 1 590  ? -32.09500  97.84100  1.57200   1.000 54.88247  ?  590  ILE   A CG1 1 
ATOM   4685  C  CG2 . ILE   A 1 590  ? -32.27600  97.57400  -0.91900  1.000 58.10843  ?  590  ILE   A CG2 1 
ATOM   4686  C  CD1 . ILE   A 1 590  ? -31.69800  99.29200  1.42900   1.000 56.09897  ?  590  ILE   A CD1 1 
ATOM   4687  N  N   . ARG   A 1 591  ? -35.59000  98.09800  -1.64000  1.000 58.34046  ?  591  ARG   A N   1 
ATOM   4688  C  CA  . ARG   A 1 591  ? -36.48300  97.65700  -2.71900  1.000 48.30146  ?  591  ARG   A CA  1 
ATOM   4689  C  C   . ARG   A 1 591  ? -37.82200  97.16600  -2.16900  1.000 55.28288  ?  591  ARG   A C   1 
ATOM   4690  O  O   . ARG   A 1 591  ? -38.52700  96.38400  -2.81400  1.000 70.27429  ?  591  ARG   A O   1 
ATOM   4691  C  CB  . ARG   A 1 591  ? -35.81200  96.57500  -3.58300  1.000 83.55482  ?  591  ARG   A CB  1 
ATOM   4692  C  CG  . ARG   A 1 591  ? -36.40600  96.37400  -4.98400  1.000 60.25271  ?  591  ARG   A CG  1 
ATOM   4693  C  CD  . ARG   A 1 591  ? -35.33200  96.32800  -6.07700  1.000 60.44962  ?  591  ARG   A CD  1 
ATOM   4694  N  NE  . ARG   A 1 591  ? -34.69300  95.02200  -6.21500  1.000 73.02501  ?  591  ARG   A NE  1 
ATOM   4695  C  CZ  . ARG   A 1 591  ? -35.27000  93.94900  -6.74200  1.000 65.56551  ?  591  ARG   A CZ  1 
ATOM   4696  N  NH1 . ARG   A 1 591  ? -36.52900  93.96800  -7.14800  1.000 84.18823  ?  591  ARG   A NH1 1 
ATOM   4697  N  NH2 . ARG   A 1 591  ? -34.56700  92.82600  -6.86000  1.000 46.24196  ?  591  ARG   A NH2 1 
ATOM   4698  N  N   . GLY   A 1 592  ? -38.18100  97.62400  -0.97200  1.000 55.03562  ?  592  GLY   A N   1 
ATOM   4699  C  CA  . GLY   A 1 592  ? -39.37200  97.16100  -0.29500  1.000 47.88014  ?  592  GLY   A CA  1 
ATOM   4700  C  C   . GLY   A 1 592  ? -39.18000  95.96600  0.61000   1.000 55.87999  ?  592  GLY   A C   1 
ATOM   4701  O  O   . GLY   A 1 592  ? -40.17200  95.44800  1.13600   1.000 53.71881  ?  592  GLY   A O   1 
ATOM   4702  N  N   . TYR   A 1 593  ? -37.94300  95.51400  0.81700   1.000 69.01963  ?  593  TYR   A N   1 
ATOM   4703  C  CA  . TYR   A 1 593  ? -37.64800  94.32500  1.60800   1.000 52.00009  ?  593  TYR   A CA  1 
ATOM   4704  C  C   . TYR   A 1 593  ? -36.85500  94.71700  2.84700   1.000 53.60860  ?  593  TYR   A C   1 
ATOM   4705  O  O   . TYR   A 1 593  ? -35.86200  95.44400  2.74600   1.000 56.44215  ?  593  TYR   A O   1 
ATOM   4706  C  CB  . TYR   A 1 593  ? -36.86000  93.29900  0.78400   1.000 33.83637  ?  593  TYR   A CB  1 
ATOM   4707  C  CG  . TYR   A 1 593  ? -37.55700  92.85000  -0.48400  1.000 52.53123  ?  593  TYR   A CG  1 
ATOM   4708  C  CD1 . TYR   A 1 593  ? -37.44500  93.58300  -1.65900  1.000 49.91910  ?  593  TYR   A CD1 1 
ATOM   4709  C  CD2 . TYR   A 1 593  ? -38.31500  91.68600  -0.50800  1.000 57.49219  ?  593  TYR   A CD2 1 
ATOM   4710  C  CE1 . TYR   A 1 593  ? -38.08000  93.17600  -2.81800  1.000 61.39361  ?  593  TYR   A CE1 1 
ATOM   4711  C  CE2 . TYR   A 1 593  ? -38.95200  91.27000  -1.66500  1.000 56.06126  ?  593  TYR   A CE2 1 
ATOM   4712  C  CZ  . TYR   A 1 593  ? -38.83100  92.01900  -2.81600  1.000 64.60129  ?  593  TYR   A CZ  1 
ATOM   4713  O  OH  . TYR   A 1 593  ? -39.46500  91.60600  -3.96600  1.000 86.85991  ?  593  TYR   A OH  1 
ATOM   4714  N  N   . ARG   A 1 594  ? -37.28800  94.23000  4.01000   1.000 61.19431  ?  594  ARG   A N   1 
ATOM   4715  C  CA  . ARG   A 1 594  ? -36.57600  94.47900  5.26000   1.000 61.08641  ?  594  ARG   A CA  1 
ATOM   4716  C  C   . ARG   A 1 594  ? -35.45400  93.45900  5.41700   1.000 58.00777  ?  594  ARG   A C   1 
ATOM   4717  O  O   . ARG   A 1 594  ? -35.71300  92.25300  5.50800   1.000 52.05688  ?  594  ARG   A O   1 
ATOM   4718  C  CB  . ARG   A 1 594  ? -37.53400  94.41400  6.44700   1.000 60.38949  ?  594  ARG   A CB  1 
ATOM   4719  N  N   . ILE   A 1 595  ? -34.21000  93.94000  5.45700   1.000 63.45281  ?  595  ILE   A N   1 
ATOM   4720  C  CA  . ILE   A 1 595  ? -33.03700  93.07700  5.45700   1.000 63.26188  ?  595  ILE   A CA  1 
ATOM   4721  C  C   . ILE   A 1 595  ? -32.10300  93.46900  6.59400   1.000 55.24672  ?  595  ILE   A C   1 
ATOM   4722  O  O   . ILE   A 1 595  ? -32.18500  94.56300  7.15700   1.000 49.66426  ?  595  ILE   A O   1 
ATOM   4723  C  CB  . ILE   A 1 595  ? -32.27500  93.13400  4.11500   1.000 57.34143  ?  595  ILE   A CB  1 
ATOM   4724  C  CG1 . ILE   A 1 595  ? -31.75800  94.55100  3.86200   1.000 34.68425  ?  595  ILE   A CG1 1 
ATOM   4725  C  CG2 . ILE   A 1 595  ? -33.16500  92.67800  2.97100   1.000 44.82747  ?  595  ILE   A CG2 1 
ATOM   4726  C  CD1 . ILE   A 1 595  ? -30.28200  94.61200  3.56700   1.000 37.41364  ?  595  ILE   A CD1 1 
ATOM   4727  N  N   . GLU   A 1 596  ? -31.20200  92.54600  6.92200   1.000 62.33981  ?  596  GLU   A N   1 
ATOM   4728  C  CA  . GLU   A 1 596  ? -30.12500  92.80300  7.87000   1.000 53.99255  ?  596  GLU   A CA  1 
ATOM   4729  C  C   . GLU   A 1 596  ? -28.82300  92.94300  7.09600   1.000 44.36540  ?  596  GLU   A C   1 
ATOM   4730  O  O   . GLU   A 1 596  ? -28.31300  91.94100  6.57000   1.000 45.91294  ?  596  GLU   A O   1 
ATOM   4731  C  CB  . GLU   A 1 596  ? -30.01600  91.67600  8.89700   1.000 46.07068  ?  596  GLU   A CB  1 
ATOM   4732  C  CG  . GLU   A 1 596  ? -28.78900  91.77100  9.79300   1.000 55.27226  ?  596  GLU   A CG  1 
ATOM   4733  C  CD  . GLU   A 1 596  ? -28.79800  93.00500  10.67700  1.000 72.84429  ?  596  GLU   A CD  1 
ATOM   4734  O  OE1 . GLU   A 1 596  ? -29.84100  93.28300  11.30800  1.000 75.05482  ?  596  GLU   A OE1 1 
ATOM   4735  O  OE2 . GLU   A 1 596  ? -27.75900  93.69700  10.74200  1.000 63.20004  -1 596  GLU   A OE2 1 
ATOM   4736  N  N   . PRO   A 1 597  ? -28.25600  94.14700  6.98600   1.000 43.39752  ?  597  PRO   A N   1 
ATOM   4737  C  CA  . PRO   A 1 597  ? -27.04400  94.31600  6.16700   1.000 47.08208  ?  597  PRO   A CA  1 
ATOM   4738  C  C   . PRO   A 1 597  ? -25.87400  93.46000  6.61800   1.000 46.77117  ?  597  PRO   A C   1 
ATOM   4739  O  O   . PRO   A 1 597  ? -24.97300  93.19700  5.81100   1.000 40.77284  ?  597  PRO   A O   1 
ATOM   4740  C  CB  . PRO   A 1 597  ? -26.73300  95.81300  6.30800   1.000 46.00288  ?  597  PRO   A CB  1 
ATOM   4741  C  CG  . PRO   A 1 597  ? -28.04600  96.43700  6.67000   1.000 36.49084  ?  597  PRO   A CG  1 
ATOM   4742  C  CD  . PRO   A 1 597  ? -28.75200  95.42600  7.52100   1.000 42.56007  ?  597  PRO   A CD  1 
ATOM   4743  N  N   . GLY   A 1 598  ? -25.85700  93.00800  7.87100   1.000 50.27522  ?  598  GLY   A N   1 
ATOM   4744  C  CA  . GLY   A 1 598  ? -24.80200  92.12000  8.32300   1.000 49.42367  ?  598  GLY   A CA  1 
ATOM   4745  C  C   . GLY   A 1 598  ? -24.83900  90.73900  7.70500   1.000 39.61493  ?  598  GLY   A C   1 
ATOM   4746  O  O   . GLY   A 1 598  ? -23.87200  89.98700  7.86000   1.000 54.27789  ?  598  GLY   A O   1 
ATOM   4747  N  N   . GLU   A 1 599  ? -25.92600  90.38800  7.02100   1.000 42.32419  ?  599  GLU   A N   1 
ATOM   4748  C  CA  . GLU   A 1 599  ? -26.02400  89.10500  6.34200   1.000 34.19593  ?  599  GLU   A CA  1 
ATOM   4749  C  C   . GLU   A 1 599  ? -25.30700  89.09500  5.00100   1.000 40.15689  ?  599  GLU   A C   1 
ATOM   4750  O  O   . GLU   A 1 599  ? -25.21500  88.03400  4.37400   1.000 45.52023  ?  599  GLU   A O   1 
ATOM   4751  C  CB  . GLU   A 1 599  ? -27.49500  88.73100  6.14100   1.000 29.71971  ?  599  GLU   A CB  1 
ATOM   4752  C  CG  . GLU   A 1 599  ? -28.20600  88.31500  7.41800   1.000 53.77606  ?  599  GLU   A CG  1 
ATOM   4753  C  CD  . GLU   A 1 599  ? -29.64200  87.88200  7.17900   1.000 60.94291  ?  599  GLU   A CD  1 
ATOM   4754  O  OE1 . GLU   A 1 599  ? -30.36400  88.58300  6.43800   1.000 65.16740  ?  599  GLU   A OE1 1 
ATOM   4755  O  OE2 . GLU   A 1 599  ? -30.04700  86.83800  7.73100   1.000 75.30645  -1 599  GLU   A OE2 1 
ATOM   4756  N  N   . ILE   A 1 600  ? -24.80100  90.23900  4.55200   1.000 32.25356  ?  600  ILE   A N   1 
ATOM   4757  C  CA  . ILE   A 1 600  ? -24.11600  90.34600  3.27200   1.000 38.28842  ?  600  ILE   A CA  1 
ATOM   4758  C  C   . ILE   A 1 600  ? -22.60700  90.23200  3.43000   1.000 40.06979  ?  600  ILE   A C   1 
ATOM   4759  O  O   . ILE   A 1 600  ? -21.94800  89.57400  2.62500   1.000 43.81973  ?  600  ILE   A O   1 
ATOM   4760  C  CB  . ILE   A 1 600  ? -24.49900  91.67000  2.57800   1.000 41.42179  ?  600  ILE   A CB  1 
ATOM   4761  C  CG1 . ILE   A 1 600  ? -26.02200  91.80600  2.49600   1.000 34.27452  ?  600  ILE   A CG1 1 
ATOM   4762  C  CG2 . ILE   A 1 600  ? -23.85300  91.75100  1.20600   1.000 41.00283  ?  600  ILE   A CG2 1 
ATOM   4763  C  CD1 . ILE   A 1 600  ? -26.50200  93.23300  2.35700   1.000 34.92108  ?  600  ILE   A CD1 1 
ATOM   4764  N  N   . GLU   A 1 601  ? -22.06100  90.87200  4.46300   1.000 45.06177  ?  601  GLU   A N   1 
ATOM   4765  C  CA  . GLU   A 1 601  ? -20.61600  90.90100  4.67900   1.000 45.63282  ?  601  GLU   A CA  1 
ATOM   4766  C  C   . GLU   A 1 601  ? -19.94500  89.53000  4.66200   1.000 36.81866  ?  601  GLU   A C   1 
ATOM   4767  O  O   . GLU   A 1 601  ? -18.87000  89.41500  4.04900   1.000 41.08393  ?  601  GLU   A O   1 
ATOM   4768  C  CB  . GLU   A 1 601  ? -20.32600  91.62900  6.00100   1.000 48.25868  ?  601  GLU   A CB  1 
ATOM   4769  C  CG  . GLU   A 1 601  ? -21.29900  92.75900  6.31600   1.000 45.07236  ?  601  GLU   A CG  1 
ATOM   4770  C  CD  . GLU   A 1 601  ? -20.92500  93.52800  7.57400   1.000 67.98398  ?  601  GLU   A CD  1 
ATOM   4771  O  OE1 . GLU   A 1 601  ? -20.16000  92.98600  8.40000   1.000 70.43418  ?  601  GLU   A OE1 1 
ATOM   4772  O  OE2 . GLU   A 1 601  ? -21.38900  94.67700  7.73400   1.000 74.32412  -1 601  GLU   A OE2 1 
ATOM   4773  N  N   . PRO   A 1 602  ? -20.48500  88.47700  5.29200   1.000 38.34868  ?  602  PRO   A N   1 
ATOM   4774  C  CA  . PRO   A 1 602  ? -19.80200  87.17100  5.21700   1.000 43.44190  ?  602  PRO   A CA  1 
ATOM   4775  C  C   . PRO   A 1 602  ? -19.56000  86.68800  3.79600   1.000 46.91456  ?  602  PRO   A C   1 
ATOM   4776  O  O   . PRO   A 1 602  ? -18.46400  86.20100  3.49300   1.000 60.12388  ?  602  PRO   A O   1 
ATOM   4777  C  CB  . PRO   A 1 602  ? -20.74900  86.23600  5.99100   1.000 36.14627  ?  602  PRO   A CB  1 
ATOM   4778  C  CG  . PRO   A 1 602  ? -22.03100  86.99000  6.13900   1.000 44.69254  ?  602  PRO   A CG  1 
ATOM   4779  C  CD  . PRO   A 1 602  ? -21.63400  88.42100  6.20900   1.000 51.08249  ?  602  PRO   A CD  1 
ATOM   4780  N  N   . PHE   A 1 603  ? -20.55200  86.81000  2.91000   1.000 41.51742  ?  603  PHE   A N   1 
ATOM   4781  C  CA  . PHE   A 1 603  ? -20.35700  86.37900  1.52800   1.000 49.45120  ?  603  PHE   A CA  1 
ATOM   4782  C  C   . PHE   A 1 603  ? -19.29300  87.22000  0.83300   1.000 46.00327  ?  603  PHE   A C   1 
ATOM   4783  O  O   . PHE   A 1 603  ? -18.49800  86.70100  0.04000   1.000 46.31991  ?  603  PHE   A O   1 
ATOM   4784  C  CB  . PHE   A 1 603  ? -21.67500  86.45000  0.75600   1.000 22.96978  ?  603  PHE   A CB  1 
ATOM   4785  C  CG  . PHE   A 1 603  ? -22.76000  85.58600  1.32500   1.000 31.79024  ?  603  PHE   A CG  1 
ATOM   4786  C  CD1 . PHE   A 1 603  ? -22.90500  84.27100  0.91300   1.000 34.54723  ?  603  PHE   A CD1 1 
ATOM   4787  C  CD2 . PHE   A 1 603  ? -23.63600  86.08600  2.27400   1.000 46.80990  ?  603  PHE   A CD2 1 
ATOM   4788  C  CE1 . PHE   A 1 603  ? -23.90300  83.47200  1.43600   1.000 39.80447  ?  603  PHE   A CE1 1 
ATOM   4789  C  CE2 . PHE   A 1 603  ? -24.63800  85.29300  2.80000   1.000 43.08082  ?  603  PHE   A CE2 1 
ATOM   4790  C  CZ  . PHE   A 1 603  ? -24.77200  83.98400  2.38100   1.000 46.28907  ?  603  PHE   A CZ  1 
ATOM   4791  N  N   . LEU   A 1 604  ? -19.26300  88.52200  1.11800   1.000 39.07800  ?  604  LEU   A N   1 
ATOM   4792  C  CA  . LEU   A 1 604  ? -18.28500  89.39200  0.47900   1.000 39.65829  ?  604  LEU   A CA  1 
ATOM   4793  C  C   . LEU   A 1 604  ? -16.87200  89.10000  0.96900   1.000 45.49230  ?  604  LEU   A C   1 
ATOM   4794  O  O   . LEU   A 1 604  ? -15.91400  89.21300  0.19600   1.000 47.96485  ?  604  LEU   A O   1 
ATOM   4795  C  CB  . LEU   A 1 604  ? -18.65700  90.85400  0.72800   1.000 34.54484  ?  604  LEU   A CB  1 
ATOM   4796  C  CG  . LEU   A 1 604  ? -18.21900  91.87000  -0.32700  1.000 34.89336  ?  604  LEU   A CG  1 
ATOM   4797  C  CD1 . LEU   A 1 604  ? -18.53200  91.36300  -1.72700  1.000 37.26812  ?  604  LEU   A CD1 1 
ATOM   4798  C  CD2 . LEU   A 1 604  ? -18.89500  93.20600  -0.07000  1.000 37.77023  ?  604  LEU   A CD2 1 
ATOM   4799  N  N   . MET   A 1 605  ? -16.72000  88.71200  2.23500   1.000 39.62044  ?  605  MET   A N   1 
ATOM   4800  C  CA  . MET   A 1 605  ? -15.40100  88.36400  2.74700   1.000 54.46584  ?  605  MET   A CA  1 
ATOM   4801  C  C   . MET   A 1 605  ? -14.92100  87.00600  2.25700   1.000 49.94465  ?  605  MET   A C   1 
ATOM   4802  O  O   . MET   A 1 605  ? -13.71200  86.75100  2.27100   1.000 62.62018  ?  605  MET   A O   1 
ATOM   4803  C  CB  . MET   A 1 605  ? -15.39600  88.39000  4.27700   1.000 45.23899  ?  605  MET   A CB  1 
ATOM   4804  C  CG  . MET   A 1 605  ? -14.29300  89.26200  4.85700   1.000 57.64899  ?  605  MET   A CG  1 
ATOM   4805  S  SD  . MET   A 1 605  ? -14.16400  89.14900  6.64900   1.000 67.17092  ?  605  MET   A SD  1 
ATOM   4806  C  CE  . MET   A 1 605  ? -13.73300  87.42300  6.84500   1.000 54.54903  ?  605  MET   A CE  1 
ATOM   4807  N  N   . ASN   A 1 606  ? -15.83300  86.13100  1.82800   1.000 43.10300  ?  606  ASN   A N   1 
ATOM   4808  C  CA  . ASN   A 1 606  ? -15.42700  84.86500  1.23100   1.000 51.87634  ?  606  ASN   A CA  1 
ATOM   4809  C  C   . ASN   A 1 606  ? -14.76700  85.04800  -0.12700  1.000 54.86254  ?  606  ASN   A C   1 
ATOM   4810  O  O   . ASN   A 1 606  ? -14.22300  84.07800  -0.66700  1.000 58.21329  ?  606  ASN   A O   1 
ATOM   4811  C  CB  . ASN   A 1 606  ? -16.63100  83.93000  1.09900   1.000 43.75544  ?  606  ASN   A CB  1 
ATOM   4812  C  CG  . ASN   A 1 606  ? -17.15700  83.46800  2.44100   1.000 55.92952  ?  606  ASN   A CG  1 
ATOM   4813  O  OD1 . ASN   A 1 606  ? -16.40400  83.34900  3.40800   1.000 69.65593  ?  606  ASN   A OD1 1 
ATOM   4814  N  ND2 . ASN   A 1 606  ? -18.45700  83.20200  2.50800   1.000 64.43464  ?  606  ASN   A ND2 1 
ATOM   4815  N  N   . HIS   A 1 607  ? -14.81200  86.25100  -0.68800  1.000 51.37739  ?  607  HIS   A N   1 
ATOM   4816  C  CA  . HIS   A 1 607  ? -14.09800  86.52700  -1.92300  1.000 56.38971  ?  607  HIS   A CA  1 
ATOM   4817  C  C   . HIS   A 1 607  ? -12.60500  86.30700  -1.70400  1.000 65.89751  ?  607  HIS   A C   1 
ATOM   4818  O  O   . HIS   A 1 607  ? -12.06300  86.74400  -0.67700  1.000 60.94123  ?  607  HIS   A O   1 
ATOM   4819  C  CB  . HIS   A 1 607  ? -14.36300  87.95600  -2.39100  1.000 59.44209  ?  607  HIS   A CB  1 
ATOM   4820  C  CG  . HIS   A 1 607  ? -13.82400  88.25700  -3.75500  1.000 62.94241  ?  607  HIS   A CG  1 
ATOM   4821  N  ND1 . HIS   A 1 607  ? -12.56100  88.76900  -3.96000  1.000 68.70260  ?  607  HIS   A ND1 1 
ATOM   4822  C  CD2 . HIS   A 1 607  ? -14.37800  88.11700  -4.98300  1.000 55.36579  ?  607  HIS   A CD2 1 
ATOM   4823  C  CE1 . HIS   A 1 607  ? -12.36000  88.93300  -5.25600  1.000 68.82040  ?  607  HIS   A CE1 1 
ATOM   4824  N  NE2 . HIS   A 1 607  ? -13.44700  88.54500  -5.89800  1.000 58.42088  ?  607  HIS   A NE2 1 
ATOM   4825  N  N   . PRO   A 1 608  ? -11.91000  85.63700  -2.62700  1.000 70.66125  ?  608  PRO   A N   1 
ATOM   4826  C  CA  . PRO   A 1 608  ? -10.50300  85.28300  -2.38100  1.000 58.37213  ?  608  PRO   A CA  1 
ATOM   4827  C  C   . PRO   A 1 608  ? -9.58400   86.47700  -2.18700  1.000 56.02146  ?  608  PRO   A C   1 
ATOM   4828  O  O   . PRO   A 1 608  ? -8.43400   86.28100  -1.77600  1.000 65.69531  ?  608  PRO   A O   1 
ATOM   4829  C  CB  . PRO   A 1 608  ? -10.11700  84.48300  -3.63200  1.000 57.26481  ?  608  PRO   A CB  1 
ATOM   4830  C  CG  . PRO   A 1 608  ? -11.41800  83.98600  -4.18400  1.000 63.64583  ?  608  PRO   A CG  1 
ATOM   4831  C  CD  . PRO   A 1 608  ? -12.41900  85.05800  -3.88100  1.000 68.17223  ?  608  PRO   A CD  1 
ATOM   4832  N  N   . LEU   A 1 609  ? -10.04400  87.70000  -2.45500  1.000 65.28465  ?  609  LEU   A N   1 
ATOM   4833  C  CA  . LEU   A 1 609  ? -9.20400   88.88000  -2.30900  1.000 62.49476  ?  609  LEU   A CA  1 
ATOM   4834  C  C   . LEU   A 1 609  ? -9.58400   89.77100  -1.13700  1.000 67.36851  ?  609  LEU   A C   1 
ATOM   4835  O  O   . LEU   A 1 609  ? -8.75100   90.57100  -0.70100  1.000 63.69583  ?  609  LEU   A O   1 
ATOM   4836  C  CB  . LEU   A 1 609  ? -9.23900   89.72100  -3.59400  1.000 60.90219  ?  609  LEU   A CB  1 
ATOM   4837  C  CG  . LEU   A 1 609  ? -8.11100   89.47300  -4.59700  1.000 58.10705  ?  609  LEU   A CG  1 
ATOM   4838  C  CD1 . LEU   A 1 609  ? -8.23800   88.09300  -5.22500  1.000 52.58618  ?  609  LEU   A CD1 1 
ATOM   4839  C  CD2 . LEU   A 1 609  ? -8.09600   90.55500  -5.66600  1.000 52.06366  ?  609  LEU   A CD2 1 
ATOM   4840  N  N   . ILE   A 1 610  ? -10.80100  89.65700  -0.61800  1.000 68.56254  ?  610  ILE   A N   1 
ATOM   4841  C  CA  . ILE   A 1 610  ? -11.27200  90.52600  0.45300   1.000 53.90768  ?  610  ILE   A CA  1 
ATOM   4842  C  C   . ILE   A 1 610  ? -10.93000  89.89500  1.79400   1.000 63.77497  ?  610  ILE   A C   1 
ATOM   4843  O  O   . ILE   A 1 610  ? -11.17100  88.70000  2.01200   1.000 48.89324  ?  610  ILE   A O   1 
ATOM   4844  C  CB  . ILE   A 1 610  ? -12.78300  90.77900  0.32800   1.000 50.74542  ?  610  ILE   A CB  1 
ATOM   4845  C  CG1 . ILE   A 1 610  ? -13.10000  91.39100  -1.04000  1.000 61.66808  ?  610  ILE   A CG1 1 
ATOM   4846  C  CG2 . ILE   A 1 610  ? -13.27400  91.67400  1.45900   1.000 43.57939  ?  610  ILE   A CG2 1 
ATOM   4847  C  CD1 . ILE   A 1 610  ? -14.53700  91.82500  -1.20900  1.000 52.20223  ?  610  ILE   A CD1 1 
ATOM   4848  N  N   . GLU   A 1 611  ? -10.35900  90.69900  2.69300   1.000 59.86968  ?  611  GLU   A N   1 
ATOM   4849  C  CA  . GLU   A 1 611  ? -10.02900  90.26300  4.04400   1.000 63.53557  ?  611  GLU   A CA  1 
ATOM   4850  C  C   . GLU   A 1 611  ? -10.91600  90.87800  5.11300   1.000 53.42396  ?  611  GLU   A C   1 
ATOM   4851  O  O   . GLU   A 1 611  ? -11.21000  90.21400  6.10800   1.000 66.62768  ?  611  GLU   A O   1 
ATOM   4852  C  CB  . GLU   A 1 611  ? -8.56400   90.59100  4.36700   1.000 79.72149  ?  611  GLU   A CB  1 
ATOM   4853  C  CG  . GLU   A 1 611  ? -7.56500   90.01200  3.37500   1.000 79.36881  ?  611  GLU   A CG  1 
ATOM   4854  C  CD  . GLU   A 1 611  ? -7.34000   88.52500  3.57600   1.000 81.72216  ?  611  GLU   A CD  1 
ATOM   4855  O  OE1 . GLU   A 1 611  ? -7.28700   88.08200  4.74300   1.000 88.88216  ?  611  GLU   A OE1 1 
ATOM   4856  O  OE2 . GLU   A 1 611  ? -7.21700   87.79700  2.56700   1.000 75.79236  -1 611  GLU   A OE2 1 
ATOM   4857  N  N   . LEU   A 1 612  ? -11.34600  92.12400  4.93100   1.000 58.64776  ?  612  LEU   A N   1 
ATOM   4858  C  CA  . LEU   A 1 612  ? -12.22900  92.81500  5.86100   1.000 59.34152  ?  612  LEU   A CA  1 
ATOM   4859  C  C   . LEU   A 1 612  ? -13.38200  93.43000  5.07900   1.000 49.12592  ?  612  LEU   A C   1 
ATOM   4860  O  O   . LEU   A 1 612  ? -13.19000  93.90900  3.95800   1.000 45.93936  ?  612  LEU   A O   1 
ATOM   4861  C  CB  . LEU   A 1 612  ? -11.47600  93.91000  6.63200   1.000 53.75239  ?  612  LEU   A CB  1 
ATOM   4862  C  CG  . LEU   A 1 612  ? -10.96200  93.63600  8.04800   1.000 61.00113  ?  612  LEU   A CG  1 
ATOM   4863  C  CD1 . LEU   A 1 612  ? -10.10000  92.38200  8.11500   1.000 50.27129  ?  612  LEU   A CD1 1 
ATOM   4864  C  CD2 . LEU   A 1 612  ? -10.18800  94.84700  8.55200   1.000 51.76646  ?  612  LEU   A CD2 1 
ATOM   4865  N  N   . THR   A 1 613  ? -14.57700  93.41800  5.66700   1.000 49.07161  ?  613  THR   A N   1 
ATOM   4866  C  CA  . THR   A 1 613  ? -15.74000  93.96100  4.97900   1.000 41.23643  ?  613  THR   A CA  1 
ATOM   4867  C  C   . THR   A 1 613  ? -16.73200  94.53000  5.98200   1.000 43.82195  ?  613  THR   A C   1 
ATOM   4868  O  O   . THR   A 1 613  ? -16.79900  94.09400  7.13500   1.000 48.73999  ?  613  THR   A O   1 
ATOM   4869  C  CB  . THR   A 1 613  ? -16.43700  92.90600  4.11500   1.000 44.03726  ?  613  THR   A CB  1 
ATOM   4870  O  OG1 . THR   A 1 613  ? -17.58800  93.49100  3.49600   1.000 59.44114  ?  613  THR   A OG1 1 
ATOM   4871  C  CG2 . THR   A 1 613  ? -16.87300  91.72800  4.96600   1.000 36.48784  ?  613  THR   A CG2 1 
ATOM   4872  N  N   . THR   A 1 614  ? -17.50800  95.50900  5.51800   1.000 51.03756  ?  614  THR   A N   1 
ATOM   4873  C  CA  . THR   A 1 614  ? -18.54100  96.14500  6.33300   1.000 60.13715  ?  614  THR   A CA  1 
ATOM   4874  C  C   . THR   A 1 614  ? -19.57100  96.75500  5.39600   1.000 56.69280  ?  614  THR   A C   1 
ATOM   4875  O  O   . THR   A 1 614  ? -19.21500  97.54800  4.51700   1.000 52.73896  ?  614  THR   A O   1 
ATOM   4876  C  CB  . THR   A 1 614  ? -17.94200  97.21200  7.25500   1.000 34.18653  ?  614  THR   A CB  1 
ATOM   4877  O  OG1 . THR   A 1 614  ? -17.17300  96.57700  8.28300   1.000 54.69087  ?  614  THR   A OG1 1 
ATOM   4878  C  CG2 . THR   A 1 614  ? -19.04100  98.05000  7.89900   1.000 46.62786  ?  614  THR   A CG2 1 
ATOM   4879  N  N   . VAL   A 1 615  ? -20.83500  96.38600  5.57300   1.000 43.58904  ?  615  VAL   A N   1 
ATOM   4880  C  CA  . VAL   A 1 615  ? -21.92500  96.87400  4.73700   1.000 49.36947  ?  615  VAL   A CA  1 
ATOM   4881  C  C   . VAL   A 1 615  ? -22.75100  97.85300  5.55800   1.000 52.00670  ?  615  VAL   A C   1 
ATOM   4882  O  O   . VAL   A 1 615  ? -23.29600  97.49100  6.60900   1.000 54.21776  ?  615  VAL   A O   1 
ATOM   4883  C  CB  . VAL   A 1 615  ? -22.79600  95.72600  4.20700   1.000 45.50311  ?  615  VAL   A CB  1 
ATOM   4884  C  CG1 . VAL   A 1 615  ? -23.94500  96.28300  3.38800   1.000 43.19883  ?  615  VAL   A CG1 1 
ATOM   4885  C  CG2 . VAL   A 1 615  ? -21.96200  94.76500  3.37000   1.000 51.91362  ?  615  VAL   A CG2 1 
ATOM   4886  N  N   . LEU   A 1 616  ? -22.84000  99.09000  5.08100   1.000 40.51220  ?  616  LEU   A N   1 
ATOM   4887  C  CA  . LEU   A 1 616  ? -23.66500  100.12200 5.69000   1.000 52.64703  ?  616  LEU   A CA  1 
ATOM   4888  C  C   . LEU   A 1 616  ? -24.89600  100.37500 4.83000   1.000 63.12496  ?  616  LEU   A C   1 
ATOM   4889  O  O   . LEU   A 1 616  ? -24.93800  100.02800 3.64600   1.000 63.04476  ?  616  LEU   A O   1 
ATOM   4890  C  CB  . LEU   A 1 616  ? -22.87600  101.42300 5.87200   1.000 55.97785  ?  616  LEU   A CB  1 
ATOM   4891  C  CG  . LEU   A 1 616  ? -21.66300  101.36900 6.80100   1.000 49.29567  ?  616  LEU   A CG  1 
ATOM   4892  C  CD1 . LEU   A 1 616  ? -21.20500  102.77600 7.14900   1.000 56.92625  ?  616  LEU   A CD1 1 
ATOM   4893  C  CD2 . LEU   A 1 616  ? -21.98100  100.57300 8.05900   1.000 59.33799  ?  616  LEU   A CD2 1 
ATOM   4894  N  N   . ALA   A 1 617  ? -25.90900  100.99500 5.44500   1.000 62.72639  ?  617  ALA   A N   1 
ATOM   4895  C  CA  . ALA   A 1 617  ? -27.18500  101.28800 4.78400   1.000 68.38651  ?  617  ALA   A CA  1 
ATOM   4896  C  C   . ALA   A 1 617  ? -27.46800  102.78000 4.93200   1.000 63.58983  ?  617  ALA   A C   1 
ATOM   4897  O  O   . ALA   A 1 617  ? -28.20000  103.20300 5.82800   1.000 76.40052  ?  617  ALA   A O   1 
ATOM   4898  C  CB  . ALA   A 1 617  ? -28.31100  100.43700 5.36400   1.000 53.74233  ?  617  ALA   A CB  1 
ATOM   4899  N  N   . LYS   A 1 618  ? -26.89100  103.57400 4.04000   1.000 57.83485  ?  618  LYS   A N   1 
ATOM   4900  C  CA  . LYS   A 1 618  ? -27.08900  105.01300 4.04500   1.000 77.35309  ?  618  LYS   A CA  1 
ATOM   4901  C  C   . LYS   A 1 618  ? -28.35800  105.38000 3.27500   1.000 82.14695  ?  618  LYS   A C   1 
ATOM   4902  O  O   . LYS   A 1 618  ? -28.99800  104.53800 2.64000   1.000 65.54932  ?  618  LYS   A O   1 
ATOM   4903  C  CB  . LYS   A 1 618  ? -25.86300  105.70500 3.45600   1.000 71.45720  ?  618  LYS   A CB  1 
ATOM   4904  C  CG  . LYS   A 1 618  ? -24.59800  104.87100 3.57300   1.000 69.82066  ?  618  LYS   A CG  1 
ATOM   4905  C  CD  . LYS   A 1 618  ? -23.37900  105.75400 3.63200   1.000 72.91382  ?  618  LYS   A CD  1 
ATOM   4906  C  CE  . LYS   A 1 618  ? -23.11200  106.24700 5.03200   1.000 85.81160  ?  618  LYS   A CE  1 
ATOM   4907  N  NZ  . LYS   A 1 618  ? -22.21000  107.41900 4.93000   1.000 98.53895  ?  618  LYS   A NZ  1 
ATOM   4908  N  N   . GLU   A 1 619  ? -28.72600  106.66000 3.33900   1.000 96.78939  ?  619  GLU   A N   1 
ATOM   4909  C  CA  . GLU   A 1 619  ? -29.95800  107.13700 2.72500   1.000 96.84455  ?  619  GLU   A CA  1 
ATOM   4910  C  C   . GLU   A 1 619  ? -29.70100  108.44700 1.99500   1.000 94.89136  ?  619  GLU   A C   1 
ATOM   4911  O  O   . GLU   A 1 619  ? -28.66400  109.09200 2.16500   1.000 94.60278  ?  619  GLU   A O   1 
ATOM   4912  C  CB  . GLU   A 1 619  ? -31.07000  107.33500 3.76300   1.000 104.02609 ?  619  GLU   A CB  1 
ATOM   4913  C  CG  . GLU   A 1 619  ? -30.92500  108.60700 4.58600   1.000 111.84302 ?  619  GLU   A CG  1 
ATOM   4914  C  CD  . GLU   A 1 619  ? -31.56400  108.49600 5.95500   1.000 113.91306 ?  619  GLU   A CD  1 
ATOM   4915  O  OE1 . GLU   A 1 619  ? -31.77900  107.35800 6.42200   1.000 106.23308 ?  619  GLU   A OE1 1 
ATOM   4916  O  OE2 . GLU   A 1 619  ? -31.84900  109.54800 6.56600   1.000 103.10217 ?  619  GLU   A OE2 1 
ATOM   4917  N  N   . GLN   A 1 620  ? -30.67400  108.83500 1.17800   1.000 95.79665  ?  620  GLN   A N   1 
ATOM   4918  C  CA  . GLN   A 1 620  ? -30.69500  110.12300 0.50200   1.000 110.93098 ?  620  GLN   A CA  1 
ATOM   4919  C  C   . GLN   A 1 620  ? -31.78900  110.99800 1.10200   1.000 118.24013 ?  620  GLN   A C   1 
ATOM   4920  O  O   . GLN   A 1 620  ? -32.63000  110.53600 1.87800   1.000 119.60526 ?  620  GLN   A O   1 
ATOM   4921  C  CB  . GLN   A 1 620  ? -30.91100  109.94000 -1.00400  1.000 93.44328  ?  620  GLN   A CB  1 
ATOM   4922  C  CG  . GLN   A 1 620  ? -29.86900  109.05700 -1.67000  1.000 100.64506 ?  620  GLN   A CG  1 
ATOM   4923  C  CD  . GLN   A 1 620  ? -30.07900  108.94000 -3.16500  1.000 118.27121 ?  620  GLN   A CD  1 
ATOM   4924  O  OE1 . GLN   A 1 620  ? -30.65600  109.82700 -3.79200  1.000 123.64257 ?  620  GLN   A OE1 1 
ATOM   4925  N  NE2 . GLN   A 1 620  ? -29.60600  107.84300 -3.74600  1.000 106.30377 ?  620  GLN   A NE2 1 
ATOM   4926  N  N   . ALA   A 1 621  ? -31.76700  112.28400 0.73600   1.000 117.70098 ?  621  ALA   A N   1 
ATOM   4927  C  CA  . ALA   A 1 621  ? -32.78900  113.20700 1.22600   1.000 116.78961 ?  621  ALA   A CA  1 
ATOM   4928  C  C   . ALA   A 1 621  ? -34.18800  112.76600 0.81500   1.000 115.34693 ?  621  ALA   A C   1 
ATOM   4929  O  O   . ALA   A 1 621  ? -35.15300  112.99200 1.55500   1.000 116.09661 ?  621  ALA   A O   1 
ATOM   4930  C  CB  . ALA   A 1 621  ? -32.51000  114.62300 0.71600   1.000 113.53459 ?  621  ALA   A CB  1 
ATOM   4931  N  N   . ASP   A 1 622  ? -34.31500  112.13500 -0.35400  1.000 115.74974 ?  622  ASP   A N   1 
ATOM   4932  C  CA  . ASP   A 1 622  ? -35.60000  111.60600 -0.79700  1.000 102.66884 ?  622  ASP   A CA  1 
ATOM   4933  C  C   . ASP   A 1 622  ? -36.17700  110.59200 0.18100   1.000 115.83912 ?  622  ASP   A C   1 
ATOM   4934  O  O   . ASP   A 1 622  ? -37.39100  110.35500 0.17000   1.000 108.07438 ?  622  ASP   A O   1 
ATOM   4935  C  CB  . ASP   A 1 622  ? -35.44500  110.96600 -2.17500  1.000 97.97209  ?  622  ASP   A CB  1 
ATOM   4936  C  CG  . ASP   A 1 622  ? -34.50700  111.74300 -3.07200  1.000 108.49527 ?  622  ASP   A CG  1 
ATOM   4937  O  OD1 . ASP   A 1 622  ? -33.33600  111.93200 -2.68200  1.000 106.78518 ?  622  ASP   A OD1 1 
ATOM   4938  O  OD2 . ASP   A 1 622  ? -34.93800  112.16400 -4.16600  1.000 108.51587 -1 622  ASP   A OD2 1 
ATOM   4939  N  N   . GLY   A 1 623  ? -35.33400  109.98100 1.01800   1.000 122.10899 ?  623  GLY   A N   1 
ATOM   4940  C  CA  . GLY   A 1 623  ? -35.75200  109.03000 2.02500   1.000 123.71657 ?  623  GLY   A CA  1 
ATOM   4941  C  C   . GLY   A 1 623  ? -35.31600  107.60600 1.74200   1.000 112.29626 ?  623  GLY   A C   1 
ATOM   4942  O  O   . GLY   A 1 623  ? -35.06300  106.84600 2.68600   1.000 97.14618  ?  623  GLY   A O   1 
ATOM   4943  N  N   . ARG   A 1 624  ? -35.22200  107.23100 0.46700   1.000 97.15451  ?  624  ARG   A N   1 
ATOM   4944  C  CA  . ARG   A 1 624  ? -34.86300  105.86800 0.10500   1.000 85.77060  ?  624  ARG   A CA  1 
ATOM   4945  C  C   . ARG   A 1 624  ? -33.45100  105.53800 0.57700   1.000 79.89241  ?  624  ARG   A C   1 
ATOM   4946  O  O   . ARG   A 1 624  ? -32.58900  106.41300 0.69700   1.000 76.77498  ?  624  ARG   A O   1 
ATOM   4947  C  CB  . ARG   A 1 624  ? -34.97600  105.67500 -1.40700  1.000 76.23362  ?  624  ARG   A CB  1 
ATOM   4948  N  N   . LYS   A 1 625  ? -33.22100  104.25600 0.84900   1.000 73.29561  ?  625  LYS   A N   1 
ATOM   4949  C  CA  . LYS   A 1 625  ? -31.96700  103.78000 1.41600   1.000 77.53146  ?  625  LYS   A CA  1 
ATOM   4950  C  C   . LYS   A 1 625  ? -31.18800  102.97300 0.38700   1.000 70.07596  ?  625  LYS   A C   1 
ATOM   4951  O  O   . LYS   A 1 625  ? -31.77200  102.25500 -0.43100  1.000 42.52485  ?  625  LYS   A O   1 
ATOM   4952  C  CB  . LYS   A 1 625  ? -32.22000  102.92700 2.66300   1.000 67.50621  ?  625  LYS   A CB  1 
ATOM   4953  C  CG  . LYS   A 1 625  ? -33.22800  103.52800 3.62900   1.000 78.43434  ?  625  LYS   A CG  1 
ATOM   4954  C  CD  . LYS   A 1 625  ? -32.77100  103.37400 5.07200   1.000 83.69611  ?  625  LYS   A CD  1 
ATOM   4955  C  CE  . LYS   A 1 625  ? -31.55600  104.23900 5.36100   1.000 85.05441  ?  625  LYS   A CE  1 
ATOM   4956  N  NZ  . LYS   A 1 625  ? -31.19900  104.25900 6.80600   1.000 85.86575  ?  625  LYS   A NZ  1 
ATOM   4957  N  N   . TYR   A 1 626  ? -29.86500  103.09900 0.43100   1.000 59.77617  ?  626  TYR   A N   1 
ATOM   4958  C  CA  . TYR   A 1 626  ? -28.97500  102.33000 -0.42300  1.000 49.59338  ?  626  TYR   A CA  1 
ATOM   4959  C  C   . TYR   A 1 626  ? -27.93200  101.63600 0.44000   1.000 59.20391  ?  626  TYR   A C   1 
ATOM   4960  O  O   . TYR   A 1 626  ? -27.58700  102.10800 1.52700   1.000 62.36044  ?  626  TYR   A O   1 
ATOM   4961  C  CB  . TYR   A 1 626  ? -28.29400  103.20900 -1.50200  1.000 53.43101  ?  626  TYR   A CB  1 
ATOM   4962  C  CG  . TYR   A 1 626  ? -27.42300  104.34900 -0.99200  1.000 60.52927  ?  626  TYR   A CG  1 
ATOM   4963  C  CD1 . TYR   A 1 626  ? -27.94000  105.35100 -0.17800  1.000 68.15458  ?  626  TYR   A CD1 1 
ATOM   4964  C  CD2 . TYR   A 1 626  ? -26.07700  104.41400 -1.32000  1.000 56.32823  ?  626  TYR   A CD2 1 
ATOM   4965  C  CE1 . TYR   A 1 626  ? -27.14000  106.39000 0.28100   1.000 86.32512  ?  626  TYR   A CE1 1 
ATOM   4966  C  CE2 . TYR   A 1 626  ? -25.27200  105.44300 -0.86600  1.000 73.16469  ?  626  TYR   A CE2 1 
ATOM   4967  C  CZ  . TYR   A 1 626  ? -25.80500  106.42900 -0.06500  1.000 86.23986  ?  626  TYR   A CZ  1 
ATOM   4968  O  OH  . TYR   A 1 626  ? -25.00100  107.45400 0.38900   1.000 92.51952  ?  626  TYR   A OH  1 
ATOM   4969  N  N   . LEU   A 1 627  ? -27.44800  100.49500 -0.04300  1.000 59.29060  ?  627  LEU   A N   1 
ATOM   4970  C  CA  . LEU   A 1 627  ? -26.45200  99.70400  0.66700   1.000 43.89883  ?  627  LEU   A CA  1 
ATOM   4971  C  C   . LEU   A 1 627  ? -25.08200  99.94200  0.04800   1.000 49.80617  ?  627  LEU   A C   1 
ATOM   4972  O  O   . LEU   A 1 627  ? -24.93700  99.91100  -1.17800  1.000 52.55409  ?  627  LEU   A O   1 
ATOM   4973  C  CB  . LEU   A 1 627  ? -26.79700  98.21600  0.62000   1.000 47.27506  ?  627  LEU   A CB  1 
ATOM   4974  C  CG  . LEU   A 1 627  ? -28.06700  97.76100  1.33800   1.000 48.09866  ?  627  LEU   A CG  1 
ATOM   4975  C  CD1 . LEU   A 1 627  ? -28.44300  96.36000  0.88600   1.000 39.13632  ?  627  LEU   A CD1 1 
ATOM   4976  C  CD2 . LEU   A 1 627  ? -27.87700  97.80900  2.84100   1.000 55.74652  ?  627  LEU   A CD2 1 
ATOM   4977  N  N   . VAL   A 1 628  ? -24.08300  100.17600 0.89400   1.000 53.11939  ?  628  VAL   A N   1 
ATOM   4978  C  CA  . VAL   A 1 628  ? -22.71500  100.43200 0.45600   1.000 40.61776  ?  628  VAL   A CA  1 
ATOM   4979  C  C   . VAL   A 1 628  ? -21.82100  99.34700  1.03500   1.000 44.15869  ?  628  VAL   A C   1 
ATOM   4980  O  O   . VAL   A 1 628  ? -21.77800  99.15700  2.25700   1.000 57.84163  ?  628  VAL   A O   1 
ATOM   4981  C  CB  . VAL   A 1 628  ? -22.22800  101.82400 0.88300   1.000 47.90652  ?  628  VAL   A CB  1 
ATOM   4982  C  CG1 . VAL   A 1 628  ? -20.83500  102.06600 0.35800   1.000 57.27758  ?  628  VAL   A CG1 1 
ATOM   4983  C  CG2 . VAL   A 1 628  ? -23.17500  102.89300 0.37500   1.000 43.12144  ?  628  VAL   A CG2 1 
ATOM   4984  N  N   . GLY   A 1 629  ? -21.10600  98.64200  0.16500   1.000 45.62315  ?  629  GLY   A N   1 
ATOM   4985  C  CA  . GLY   A 1 629  ? -20.21900  97.58800  0.61300   1.000 49.02486  ?  629  GLY   A CA  1 
ATOM   4986  C  C   . GLY   A 1 629  ? -18.77200  98.02400  0.69600   1.000 51.77339  ?  629  GLY   A C   1 
ATOM   4987  O  O   . GLY   A 1 629  ? -18.09100  98.13100  -0.32700  1.000 52.28819  ?  629  GLY   A O   1 
ATOM   4988  N  N   . TYR   A 1 630  ? -18.29100  98.28400  1.91000   1.000 64.49961  ?  630  TYR   A N   1 
ATOM   4989  C  CA  . TYR   A 1 630  ? -16.89900  98.65000  2.13300   1.000 52.49531  ?  630  TYR   A CA  1 
ATOM   4990  C  C   . TYR   A 1 630  ? -16.06700  97.38600  2.29900   1.000 49.80318  ?  630  TYR   A C   1 
ATOM   4991  O  O   . TYR   A 1 630  ? -16.45500  96.47800  3.04000   1.000 57.60428  ?  630  TYR   A O   1 
ATOM   4992  C  CB  . TYR   A 1 630  ? -16.76500  99.53600  3.37100   1.000 47.14313  ?  630  TYR   A CB  1 
ATOM   4993  C  CG  . TYR   A 1 630  ? -17.56200  100.81700 3.29300   1.000 57.75101  ?  630  TYR   A CG  1 
ATOM   4994  C  CD1 . TYR   A 1 630  ? -17.01600  101.95800 2.72500   1.000 55.03123  ?  630  TYR   A CD1 1 
ATOM   4995  C  CD2 . TYR   A 1 630  ? -18.85900  100.88400 3.78500   1.000 51.81334  ?  630  TYR   A CD2 1 
ATOM   4996  C  CE1 . TYR   A 1 630  ? -17.73600  103.12900 2.64800   1.000 51.24508  ?  630  TYR   A CE1 1 
ATOM   4997  C  CE2 . TYR   A 1 630  ? -19.59000  102.05600 3.71100   1.000 59.71592  ?  630  TYR   A CE2 1 
ATOM   4998  C  CZ  . TYR   A 1 630  ? -19.02200  103.17700 3.14100   1.000 53.34728  ?  630  TYR   A CZ  1 
ATOM   4999  O  OH  . TYR   A 1 630  ? -19.73500  104.35100 3.05900   1.000 58.63753  ?  630  TYR   A OH  1 
ATOM   5000  N  N   . TYR   A 1 631  ? -14.92800  97.32700  1.61000   1.000 47.19249  ?  631  TYR   A N   1 
ATOM   5001  C  CA  . TYR   A 1 631  ? -14.08600  96.14100  1.64700   1.000 53.45428  ?  631  TYR   A CA  1 
ATOM   5002  C  C   . TYR   A 1 631  ? -12.61600  96.53200  1.66200   1.000 59.72328  ?  631  TYR   A C   1 
ATOM   5003  O  O   . TYR   A 1 631  ? -12.21700  97.51700  1.03500   1.000 58.24779  ?  631  TYR   A O   1 
ATOM   5004  C  CB  . TYR   A 1 631  ? -14.37400  95.21200  0.45400   1.000 52.34967  ?  631  TYR   A CB  1 
ATOM   5005  C  CG  . TYR   A 1 631  ? -14.01000  95.77700  -0.90500  1.000 58.78859  ?  631  TYR   A CG  1 
ATOM   5006  C  CD1 . TYR   A 1 631  ? -14.85900  96.65900  -1.56400  1.000 47.77546  ?  631  TYR   A CD1 1 
ATOM   5007  C  CD2 . TYR   A 1 631  ? -12.83100  95.40700  -1.54200  1.000 58.78073  ?  631  TYR   A CD2 1 
ATOM   5008  C  CE1 . TYR   A 1 631  ? -14.53600  97.17100  -2.81000  1.000 60.22202  ?  631  TYR   A CE1 1 
ATOM   5009  C  CE2 . TYR   A 1 631  ? -12.49900  95.91300  -2.79000  1.000 59.20446  ?  631  TYR   A CE2 1 
ATOM   5010  C  CZ  . TYR   A 1 631  ? -13.35500  96.79500  -3.41900  1.000 66.02559  ?  631  TYR   A CZ  1 
ATOM   5011  O  OH  . TYR   A 1 631  ? -13.03100  97.30100  -4.66000  1.000 54.23528  ?  631  TYR   A OH  1 
ATOM   5012  N  N   . VAL   A 1 632  ? -11.81800  95.75100  2.38700   1.000 56.14316  ?  632  VAL   A N   1 
ATOM   5013  C  CA  . VAL   A 1 632  ? -10.36800  95.90400  2.42700   1.000 60.20190  ?  632  VAL   A CA  1 
ATOM   5014  C  C   . VAL   A 1 632  ? -9.75800   94.75700  1.63300   1.000 63.96809  ?  632  VAL   A C   1 
ATOM   5015  O  O   . VAL   A 1 632  ? -9.89700   93.58500  2.00800   1.000 62.21000  ?  632  VAL   A O   1 
ATOM   5016  C  CB  . VAL   A 1 632  ? -9.83500   95.93100  3.86700   1.000 56.38846  ?  632  VAL   A CB  1 
ATOM   5017  C  CG1 . VAL   A 1 632  ? -8.33200   95.69000  3.88200   1.000 58.14714  ?  632  VAL   A CG1 1 
ATOM   5018  C  CG2 . VAL   A 1 632  ? -10.16200  97.26200  4.52600   1.000 52.98877  ?  632  VAL   A CG2 1 
ATOM   5019  N  N   . ALA   A 1 633  ? -9.09300   95.09300  0.53700   1.000 63.75526  ?  633  ALA   A N   1 
ATOM   5020  C  CA  . ALA   A 1 633  ? -8.46400   94.13300  -0.35400  1.000 70.02831  ?  633  ALA   A CA  1 
ATOM   5021  C  C   . ALA   A 1 633  ? -7.14000   94.71400  -0.82500  1.000 72.07751  ?  633  ALA   A C   1 
ATOM   5022  O  O   . ALA   A 1 633  ? -6.91500   95.92400  -0.71500  1.000 64.14483  ?  633  ALA   A O   1 
ATOM   5023  C  CB  . ALA   A 1 633  ? -9.36600   93.81100  -1.55400  1.000 79.58623  ?  633  ALA   A CB  1 
ATOM   5024  N  N   . PRO   A 1 634  ? -6.23000   93.87100  -1.33200  1.000 74.46753  ?  634  PRO   A N   1 
ATOM   5025  C  CA  . PRO   A 1 634  ? -4.95500   94.40300  -1.85200  1.000 53.56023  ?  634  PRO   A CA  1 
ATOM   5026  C  C   . PRO   A 1 634  ? -5.13100   95.52500  -2.86300  1.000 69.70363  ?  634  PRO   A C   1 
ATOM   5027  O  O   . PRO   A 1 634  ? -4.49400   96.57800  -2.73500  1.000 71.65683  ?  634  PRO   A O   1 
ATOM   5028  C  CB  . PRO   A 1 634  ? -4.28900   93.16300  -2.47300  1.000 60.04379  ?  634  PRO   A CB  1 
ATOM   5029  C  CG  . PRO   A 1 634  ? -5.33800   92.07000  -2.45400  1.000 61.51912  ?  634  PRO   A CG  1 
ATOM   5030  C  CD  . PRO   A 1 634  ? -6.23400   92.40100  -1.31800  1.000 73.52275  ?  634  PRO   A CD  1 
ATOM   5031  N  N   . GLU   A 1 635  ? -5.98600   95.33000  -3.86400  1.000 69.95802  ?  635  GLU   A N   1 
ATOM   5032  C  CA  . GLU   A 1 635  ? -6.29400   96.36800  -4.83600  1.000 73.27463  ?  635  GLU   A CA  1 
ATOM   5033  C  C   . GLU   A 1 635  ? -7.80000   96.40300  -5.05000  1.000 73.87298  ?  635  GLU   A C   1 
ATOM   5034  O  O   . GLU   A 1 635  ? -8.54300   95.56700  -4.52900  1.000 74.81678  ?  635  GLU   A O   1 
ATOM   5035  C  CB  . GLU   A 1 635  ? -5.55800   96.13700  -6.16300  1.000 67.36902  ?  635  GLU   A CB  1 
ATOM   5036  N  N   . GLU   A 1 636  ? -8.24900   97.38800  -5.82300  1.000 70.55158  ?  636  GLU   A N   1 
ATOM   5037  C  CA  . GLU   A 1 636  ? -9.66700   97.52100  -6.11900  1.000 49.60125  ?  636  GLU   A CA  1 
ATOM   5038  C  C   . GLU   A 1 636  ? -10.16100  96.32900  -6.93300  1.000 63.28283  ?  636  GLU   A C   1 
ATOM   5039  O  O   . GLU   A 1 636  ? -9.43100   95.75400  -7.74500  1.000 65.33313  ?  636  GLU   A O   1 
ATOM   5040  C  CB  . GLU   A 1 636  ? -9.93700   98.81800  -6.88000  1.000 48.74292  ?  636  GLU   A CB  1 
ATOM   5041  C  CG  . GLU   A 1 636  ? -11.30800  99.41400  -6.61600  1.000 75.27127  ?  636  GLU   A CG  1 
ATOM   5042  C  CD  . GLU   A 1 636  ? -11.78800  100.30600 -7.74500  1.000 87.35693  ?  636  GLU   A CD  1 
ATOM   5043  O  OE1 . GLU   A 1 636  ? -11.72600  99.87400  -8.91500  1.000 91.88473  ?  636  GLU   A OE1 1 
ATOM   5044  O  OE2 . GLU   A 1 636  ? -12.22500  101.44100 -7.46000  1.000 91.63328  -1 636  GLU   A OE2 1 
ATOM   5045  N  N   . ILE   A 1 637  ? -11.41700  95.95800  -6.70100  1.000 65.22093  ?  637  ILE   A N   1 
ATOM   5046  C  CA  . ILE   A 1 637  ? -12.04600  94.85500  -7.42400  1.000 58.55955  ?  637  ILE   A CA  1 
ATOM   5047  C  C   . ILE   A 1 637  ? -13.11500  95.43500  -8.34200  1.000 67.22470  ?  637  ILE   A C   1 
ATOM   5048  O  O   . ILE   A 1 637  ? -13.86600  96.33000  -7.92600  1.000 62.73903  ?  637  ILE   A O   1 
ATOM   5049  C  CB  . ILE   A 1 637  ? -12.63600  93.81600  -6.45800  1.000 56.92860  ?  637  ILE   A CB  1 
ATOM   5050  C  CG1 . ILE   A 1 637  ? -11.61700  93.46300  -5.37300  1.000 57.52627  ?  637  ILE   A CG1 1 
ATOM   5051  C  CG2 . ILE   A 1 637  ? -13.05900  92.55800  -7.20800  1.000 51.69288  ?  637  ILE   A CG2 1 
ATOM   5052  C  CD1 . ILE   A 1 637  ? -12.11300  92.44100  -4.37800  1.000 54.11981  ?  637  ILE   A CD1 1 
ATOM   5053  N  N   . PRO   A 1 638  ? -13.20500  94.97700  -9.59100  1.000 63.93901  ?  638  PRO   A N   1 
ATOM   5054  C  CA  . PRO   A 1 638  ? -14.22900  95.50500  -10.50100 1.000 59.78367  ?  638  PRO   A CA  1 
ATOM   5055  C  C   . PRO   A 1 638  ? -15.63200  95.36700  -9.92600  1.000 58.36886  ?  638  PRO   A C   1 
ATOM   5056  O  O   . PRO   A 1 638  ? -15.96000  94.38300  -9.25900  1.000 52.67340  ?  638  PRO   A O   1 
ATOM   5057  C  CB  . PRO   A 1 638  ? -14.05400  94.65800  -11.77000 1.000 54.64604  ?  638  PRO   A CB  1 
ATOM   5058  C  CG  . PRO   A 1 638  ? -13.09300  93.55500  -11.40300 1.000 62.55601  ?  638  PRO   A CG  1 
ATOM   5059  C  CD  . PRO   A 1 638  ? -12.26800  94.08100  -10.28300 1.000 57.00049  ?  638  PRO   A CD  1 
ATOM   5060  N  N   . HIS   A 1 639  ? -16.45800  96.38000  -10.19900 1.000 53.08514  ?  639  HIS   A N   1 
ATOM   5061  C  CA  . HIS   A 1 639  ? -17.81000  96.42700  -9.65300  1.000 46.09950  ?  639  HIS   A CA  1 
ATOM   5062  C  C   . HIS   A 1 639  ? -18.61800  95.20100  -10.06300 1.000 62.27132  ?  639  HIS   A C   1 
ATOM   5063  O  O   . HIS   A 1 639  ? -19.25600  94.55500  -9.22400  1.000 65.19926  ?  639  HIS   A O   1 
ATOM   5064  C  CB  . HIS   A 1 639  ? -18.49900  97.71300  -10.11100 1.000 48.71584  ?  639  HIS   A CB  1 
ATOM   5065  C  CG  . HIS   A 1 639  ? -19.93900  97.80800  -9.71500  1.000 67.33782  ?  639  HIS   A CG  1 
ATOM   5066  N  ND1 . HIS   A 1 639  ? -20.34300  98.29000  -8.48800  1.000 68.46946  ?  639  HIS   A ND1 1 
ATOM   5067  C  CD2 . HIS   A 1 639  ? -21.07100  97.49500  -10.38800 1.000 69.05817  ?  639  HIS   A CD2 1 
ATOM   5068  C  CE1 . HIS   A 1 639  ? -21.66300  98.26500  -8.42100  1.000 74.09505  ?  639  HIS   A CE1 1 
ATOM   5069  N  NE2 . HIS   A 1 639  ? -22.12900  97.78600  -9.56000  1.000 74.00862  ?  639  HIS   A NE2 1 
ATOM   5070  N  N   . GLY   A 1 640  ? -18.59400  94.86000  -11.35300 1.000 54.25095  ?  640  GLY   A N   1 
ATOM   5071  C  CA  . GLY   A 1 640  ? -19.35300  93.71100  -11.81500 1.000 47.13326  ?  640  GLY   A CA  1 
ATOM   5072  C  C   . GLY   A 1 640  ? -18.88800  92.40400  -11.20600 1.000 53.91670  ?  640  GLY   A C   1 
ATOM   5073  O  O   . GLY   A 1 640  ? -19.67000  91.45700  -11.08800 1.000 53.56934  ?  640  GLY   A O   1 
ATOM   5074  N  N   . GLU   A 1 641  ? -17.61400  92.33300  -10.81000 1.000 57.89379  ?  641  GLU   A N   1 
ATOM   5075  C  CA  . GLU   A 1 641  ? -17.10000  91.12600  -10.17000 1.000 56.50008  ?  641  GLU   A CA  1 
ATOM   5076  C  C   . GLU   A 1 641  ? -17.74100  90.91400  -8.80500  1.000 57.54961  ?  641  GLU   A C   1 
ATOM   5077  O  O   . GLU   A 1 641  ? -18.14500  89.79600  -8.46200  1.000 45.61555  ?  641  GLU   A O   1 
ATOM   5078  C  CB  . GLU   A 1 641  ? -15.58000  91.20500  -10.04300 1.000 52.68090  ?  641  GLU   A CB  1 
ATOM   5079  C  CG  . GLU   A 1 641  ? -14.82000  90.45900  -11.12300 1.000 62.14310  ?  641  GLU   A CG  1 
ATOM   5080  C  CD  . GLU   A 1 641  ? -13.52700  89.85700  -10.60700 1.000 81.29107  ?  641  GLU   A CD  1 
ATOM   5081  O  OE1 . GLU   A 1 641  ? -13.56900  88.75200  -10.02500 1.000 72.36529  ?  641  GLU   A OE1 1 
ATOM   5082  O  OE2 . GLU   A 1 641  ? -12.46700  90.49400  -10.77900 1.000 87.08366  -1 641  GLU   A OE2 1 
ATOM   5083  N  N   . LEU   A 1 642  ? -17.83700  91.97800  -8.00700  1.000 54.56612  ?  642  LEU   A N   1 
ATOM   5084  C  CA  . LEU   A 1 642  ? -18.47900  91.86200  -6.70300  1.000 56.72929  ?  642  LEU   A CA  1 
ATOM   5085  C  C   . LEU   A 1 642  ? -19.97600  91.62300  -6.85100  1.000 52.62846  ?  642  LEU   A C   1 
ATOM   5086  O  O   . LEU   A 1 642  ? -20.57900  90.90100  -6.04700  1.000 51.30304  ?  642  LEU   A O   1 
ATOM   5087  C  CB  . LEU   A 1 642  ? -18.20700  93.11500  -5.87400  1.000 52.98597  ?  642  LEU   A CB  1 
ATOM   5088  C  CG  . LEU   A 1 642  ? -16.73400  93.50400  -5.72400  1.000 52.79045  ?  642  LEU   A CG  1 
ATOM   5089  C  CD1 . LEU   A 1 642  ? -16.60200  94.82800  -4.99700  1.000 59.81161  ?  642  LEU   A CD1 1 
ATOM   5090  C  CD2 . LEU   A 1 642  ? -15.96500  92.42300  -4.99100  1.000 34.66509  ?  642  LEU   A CD2 1 
ATOM   5091  N  N   . ARG   A 1 643  ? -20.59300  92.21900  -7.87600  1.000 52.51274  ?  643  ARG   A N   1 
ATOM   5092  C  CA  . ARG   A 1 643  ? -22.00900  91.97500  -8.13000  1.000 53.03807  ?  643  ARG   A CA  1 
ATOM   5093  C  C   . ARG   A 1 643  ? -22.25300  90.52800  -8.53600  1.000 43.39442  ?  643  ARG   A C   1 
ATOM   5094  O  O   . ARG   A 1 643  ? -23.25100  89.92100  -8.13100  1.000 46.01268  ?  643  ARG   A O   1 
ATOM   5095  C  CB  . ARG   A 1 643  ? -22.52000  92.92700  -9.21100  1.000 46.08304  ?  643  ARG   A CB  1 
ATOM   5096  C  CG  . ARG   A 1 643  ? -22.43800  94.40000  -8.84100  1.000 62.46026  ?  643  ARG   A CG  1 
ATOM   5097  C  CD  . ARG   A 1 643  ? -23.82400  94.97600  -8.62000  1.000 69.18170  ?  643  ARG   A CD  1 
ATOM   5098  N  NE  . ARG   A 1 643  ? -24.76000  94.50300  -9.63200  1.000 59.31723  ?  643  ARG   A NE  1 
ATOM   5099  C  CZ  . ARG   A 1 643  ? -26.07300  94.43100  -9.46300  1.000 73.89845  ?  643  ARG   A CZ  1 
ATOM   5100  N  NH1 . ARG   A 1 643  ? -26.64600  94.80300  -8.32900  1.000 59.19218  ?  643  ARG   A NH1 1 
ATOM   5101  N  NH2 . ARG   A 1 643  ? -26.82900  93.96500  -10.45400 1.000 72.71354  ?  643  ARG   A NH2 1 
ATOM   5102  N  N   . GLU   A 1 644  ? -21.35100  89.96000  -9.33700  1.000 47.08714  ?  644  GLU   A N   1 
ATOM   5103  C  CA  . GLU   A 1 644  ? -21.49100  88.56600  -9.73800  1.000 50.18921  ?  644  GLU   A CA  1 
ATOM   5104  C  C   . GLU   A 1 644  ? -21.15600  87.62700  -8.58600  1.000 56.67707  ?  644  GLU   A C   1 
ATOM   5105  O  O   . GLU   A 1 644  ? -21.80700  86.58900  -8.41300  1.000 57.33994  ?  644  GLU   A O   1 
ATOM   5106  C  CB  . GLU   A 1 644  ? -20.59900  88.28200  -10.94600 1.000 52.09128  ?  644  GLU   A CB  1 
ATOM   5107  C  CG  . GLU   A 1 644  ? -20.22800  86.82300  -11.12200 1.000 77.18715  ?  644  GLU   A CG  1 
ATOM   5108  C  CD  . GLU   A 1 644  ? -19.48600  86.56400  -12.41600 1.000 97.43105  ?  644  GLU   A CD  1 
ATOM   5109  O  OE1 . GLU   A 1 644  ? -18.83600  87.50100  -12.92900 1.000 96.98255  ?  644  GLU   A OE1 1 
ATOM   5110  O  OE2 . GLU   A 1 644  ? -19.55400  85.42300  -12.91900 1.000 106.80561 -1 644  GLU   A OE2 1 
ATOM   5111  N  N   . TRP   A 1 645  ? -20.14500  87.98000  -7.78700  1.000 48.88409  ?  645  TRP   A N   1 
ATOM   5112  C  CA  . TRP   A 1 645  ? -19.75300  87.13300  -6.66600  1.000 48.88549  ?  645  TRP   A CA  1 
ATOM   5113  C  C   . TRP   A 1 645  ? -20.90700  86.95100  -5.69000  1.000 47.62392  ?  645  TRP   A C   1 
ATOM   5114  O  O   . TRP   A 1 645  ? -21.19800  85.83300  -5.25200  1.000 52.42764  ?  645  TRP   A O   1 
ATOM   5115  C  CB  . TRP   A 1 645  ? -18.53400  87.73000  -5.96100  1.000 53.28471  ?  645  TRP   A CB  1 
ATOM   5116  C  CG  . TRP   A 1 645  ? -18.08600  86.93400  -4.77400  1.000 47.28373  ?  645  TRP   A CG  1 
ATOM   5117  C  CD1 . TRP   A 1 645  ? -18.35900  87.19500  -3.46300  1.000 48.83558  ?  645  TRP   A CD1 1 
ATOM   5118  C  CD2 . TRP   A 1 645  ? -17.29100  85.74200  -4.78900  1.000 46.26086  ?  645  TRP   A CD2 1 
ATOM   5119  N  NE1 . TRP   A 1 645  ? -17.78100  86.24100  -2.66000  1.000 58.71681  ?  645  TRP   A NE1 1 
ATOM   5120  C  CE2 . TRP   A 1 645  ? -17.11900  85.33800  -3.45000  1.000 59.22980  ?  645  TRP   A CE2 1 
ATOM   5121  C  CE3 . TRP   A 1 645  ? -16.70500  84.97900  -5.80300  1.000 50.15423  ?  645  TRP   A CE3 1 
ATOM   5122  C  CZ2 . TRP   A 1 645  ? -16.38800  84.20300  -3.10000  1.000 66.08518  ?  645  TRP   A CZ2 1 
ATOM   5123  C  CZ3 . TRP   A 1 645  ? -15.97900  83.85400  -5.45300  1.000 50.01472  ?  645  TRP   A CZ3 1 
ATOM   5124  C  CH2 . TRP   A 1 645  ? -15.82600  83.47700  -4.11400  1.000 61.22019  ?  645  TRP   A CH2 1 
ATOM   5125  N  N   . LEU   A 1 646  ? -21.58500  88.04500  -5.34500  1.000 48.54984  ?  646  LEU   A N   1 
ATOM   5126  C  CA  . LEU   A 1 646  ? -22.72800  87.96600  -4.44900  1.000 43.64826  ?  646  LEU   A CA  1 
ATOM   5127  C  C   . LEU   A 1 646  ? -23.97200  87.41600  -5.13600  1.000 53.89919  ?  646  LEU   A C   1 
ATOM   5128  O  O   . LEU   A 1 646  ? -24.86400  86.89900  -4.45300  1.000 49.40994  ?  646  LEU   A O   1 
ATOM   5129  C  CB  . LEU   A 1 646  ? -23.02200  89.34800  -3.86500  1.000 38.45330  ?  646  LEU   A CB  1 
ATOM   5130  C  CG  . LEU   A 1 646  ? -21.87900  89.97100  -3.06500  1.000 36.49449  ?  646  LEU   A CG  1 
ATOM   5131  C  CD1 . LEU   A 1 646  ? -22.22000  91.39400  -2.65600  1.000 41.65416  ?  646  LEU   A CD1 1 
ATOM   5132  C  CD2 . LEU   A 1 646  ? -21.57500  89.12000  -1.84600  1.000 42.37105  ?  646  LEU   A CD2 1 
ATOM   5133  N  N   . GLY   A 1 647  ? -24.04800  87.50800  -6.46400  1.000 52.78096  ?  647  GLY   A N   1 
ATOM   5134  C  CA  . GLY   A 1 647  ? -25.18900  86.98500  -7.19400  1.000 49.91232  ?  647  GLY   A CA  1 
ATOM   5135  C  C   . GLY   A 1 647  ? -25.31500  85.47800  -7.16000  1.000 48.25213  ?  647  GLY   A C   1 
ATOM   5136  O  O   . GLY   A 1 647  ? -26.35100  84.95000  -7.57900  1.000 56.55169  ?  647  GLY   A O   1 
ATOM   5137  N  N   . ASN   A 1 648  ? -24.29400  84.77900  -6.67000  1.000 40.35031  ?  648  ASN   A N   1 
ATOM   5138  C  CA  . ASN   A 1 648  ? -24.35400  83.32800  -6.57300  1.000 48.69124  ?  648  ASN   A CA  1 
ATOM   5139  C  C   . ASN   A 1 648  ? -25.13000  82.84700  -5.35200  1.000 50.73077  ?  648  ASN   A C   1 
ATOM   5140  O  O   . ASN   A 1 648  ? -25.57400  81.69300  -5.33600  1.000 45.61657  ?  648  ASN   A O   1 
ATOM   5141  C  CB  . ASN   A 1 648  ? -22.93700  82.75000  -6.54700  1.000 41.41568  ?  648  ASN   A CB  1 
ATOM   5142  C  CG  . ASN   A 1 648  ? -22.01500  83.41100  -7.55900  1.000 61.20595  ?  648  ASN   A CG  1 
ATOM   5143  O  OD1 . ASN   A 1 648  ? -22.43300  83.75900  -8.66400  1.000 77.08568  ?  648  ASN   A OD1 1 
ATOM   5144  N  ND2 . ASN   A 1 648  ? -20.75200  83.58600  -7.18400  1.000 63.78063  ?  648  ASN   A ND2 1 
ATOM   5145  N  N   . ASP   A 1 649  ? -25.30100  83.69300  -4.32800  1.000 50.54722  ?  649  ASP   A N   1 
ATOM   5146  C  CA  . ASP   A 1 649  ? -25.95900  83.28700  -3.09500  1.000 52.21386  ?  649  ASP   A CA  1 
ATOM   5147  C  C   . ASP   A 1 649  ? -26.96300  84.30100  -2.55900  1.000 48.65842  ?  649  ASP   A C   1 
ATOM   5148  O  O   . ASP   A 1 649  ? -27.65300  84.00000  -1.57900  1.000 51.14573  ?  649  ASP   A O   1 
ATOM   5149  C  CB  . ASP   A 1 649  ? -24.92200  82.99700  -1.99200  1.000 50.11641  ?  649  ASP   A CB  1 
ATOM   5150  C  CG  . ASP   A 1 649  ? -23.72900  82.19700  -2.49500  1.000 53.06167  ?  649  ASP   A CG  1 
ATOM   5151  O  OD1 . ASP   A 1 649  ? -22.90100  82.75700  -3.24400  1.000 61.90034  ?  649  ASP   A OD1 1 
ATOM   5152  O  OD2 . ASP   A 1 649  ? -23.62200  81.00200  -2.14100  1.000 67.39285  -1 649  ASP   A OD2 1 
ATOM   5153  N  N   . LEU   A 1 650  ? -27.07600  85.47900  -3.16600  1.000 40.16781  ?  650  LEU   A N   1 
ATOM   5154  C  CA  . LEU   A 1 650  ? -27.91300  86.52400  -2.60000  1.000 45.29281  ?  650  LEU   A CA  1 
ATOM   5155  C  C   . LEU   A 1 650  ? -28.84400  87.11600  -3.65000  1.000 50.26488  ?  650  LEU   A C   1 
ATOM   5156  O  O   . LEU   A 1 650  ? -28.53700  87.09600  -4.84700  1.000 44.29441  ?  650  LEU   A O   1 
ATOM   5157  C  CB  . LEU   A 1 650  ? -27.04900  87.63900  -1.99200  1.000 44.42111  ?  650  LEU   A CB  1 
ATOM   5158  C  CG  . LEU   A 1 650  ? -26.33500  87.30200  -0.68100  1.000 43.53710  ?  650  LEU   A CG  1 
ATOM   5159  C  CD1 . LEU   A 1 650  ? -25.36500  88.41400  -0.31100  1.000 27.69473  ?  650  LEU   A CD1 1 
ATOM   5160  C  CD2 . LEU   A 1 650  ? -27.34600  87.06400  0.43400   1.000 48.09248  ?  650  LEU   A CD2 1 
ATOM   5161  N  N   . PRO   A 1 651  ? -29.99400  87.63700  -3.22800  1.000 49.04415  ?  651  PRO   A N   1 
ATOM   5162  C  CA  . PRO   A 1 651  ? -30.90100  88.31700  -4.15900  1.000 46.34017  ?  651  PRO   A CA  1 
ATOM   5163  C  C   . PRO   A 1 651  ? -30.39800  89.70900  -4.51900  1.000 44.60591  ?  651  PRO   A C   1 
ATOM   5164  O  O   . PRO   A 1 651  ? -29.44400  90.23000  -3.94200  1.000 52.79256  ?  651  PRO   A O   1 
ATOM   5165  C  CB  . PRO   A 1 651  ? -32.22300  88.40100  -3.38100  1.000 42.32157  ?  651  PRO   A CB  1 
ATOM   5166  C  CG  . PRO   A 1 651  ? -32.05900  87.49400  -2.20800  1.000 53.77224  ?  651  PRO   A CG  1 
ATOM   5167  C  CD  . PRO   A 1 651  ? -30.60000  87.48000  -1.89900  1.000 52.47960  ?  651  PRO   A CD  1 
ATOM   5168  N  N   . ASP   A 1 652  ? -31.09700  90.32200  -5.47800  1.000 58.08754  ?  652  ASP   A N   1 
ATOM   5169  C  CA  . ASP   A 1 652  ? -30.62600  91.57500  -6.06300  1.000 51.74449  ?  652  ASP   A CA  1 
ATOM   5170  C  C   . ASP   A 1 652  ? -30.58800  92.70400  -5.03800  1.000 42.14224  ?  652  ASP   A C   1 
ATOM   5171  O  O   . ASP   A 1 652  ? -29.64500  93.50400  -5.02800  1.000 56.30507  ?  652  ASP   A O   1 
ATOM   5172  C  CB  . ASP   A 1 652  ? -31.50500  91.95800  -7.25400  1.000 40.35678  ?  652  ASP   A CB  1 
ATOM   5173  C  CG  . ASP   A 1 652  ? -31.13900  93.30900  -7.84000  1.000 63.72140  ?  652  ASP   A CG  1 
ATOM   5174  O  OD1 . ASP   A 1 652  ? -29.93400  93.57200  -8.04700  1.000 70.34173  ?  652  ASP   A OD1 1 
ATOM   5175  O  OD2 . ASP   A 1 652  ? -32.06400  94.11600  -8.07500  1.000 69.27549  -1 652  ASP   A OD2 1 
ATOM   5176  N  N   . TYR   A 1 653  ? -31.60100  92.79400  -4.17100  1.000 38.54293  ?  653  TYR   A N   1 
ATOM   5177  C  CA  . TYR   A 1 653  ? -31.63300  93.89500  -3.21000  1.000 48.79154  ?  653  TYR   A CA  1 
ATOM   5178  C  C   . TYR   A 1 653  ? -30.56200  93.74000  -2.13600  1.000 53.83977  ?  653  TYR   A C   1 
ATOM   5179  O  O   . TYR   A 1 653  ? -30.04900  94.74400  -1.62700  1.000 53.64363  ?  653  TYR   A O   1 
ATOM   5180  C  CB  . TYR   A 1 653  ? -33.01700  94.01700  -2.56500  1.000 44.83339  ?  653  TYR   A CB  1 
ATOM   5181  C  CG  . TYR   A 1 653  ? -33.67700  92.69900  -2.22200  1.000 46.30439  ?  653  TYR   A CG  1 
ATOM   5182  C  CD1 . TYR   A 1 653  ? -34.47600  92.03700  -3.14500  1.000 48.54647  ?  653  TYR   A CD1 1 
ATOM   5183  C  CD2 . TYR   A 1 653  ? -33.51700  92.12600  -0.96800  1.000 44.41707  ?  653  TYR   A CD2 1 
ATOM   5184  C  CE1 . TYR   A 1 653  ? -35.08500  90.83200  -2.83100  1.000 59.63583  ?  653  TYR   A CE1 1 
ATOM   5185  C  CE2 . TYR   A 1 653  ? -34.12100  90.92200  -0.64400  1.000 32.84163  ?  653  TYR   A CE2 1 
ATOM   5186  C  CZ  . TYR   A 1 653  ? -34.90300  90.28000  -1.57600  1.000 51.28178  ?  653  TYR   A CZ  1 
ATOM   5187  O  OH  . TYR   A 1 653  ? -35.49900  89.08400  -1.24300  1.000 52.73994  ?  653  TYR   A OH  1 
ATOM   5188  N  N   . MET   A 1 654  ? -30.20800  92.50300  -1.78500  1.000 53.14867  ?  654  MET   A N   1 
ATOM   5189  C  CA  . MET   A 1 654  ? -29.13100  92.25200  -0.83500  1.000 45.84890  ?  654  MET   A CA  1 
ATOM   5190  C  C   . MET   A 1 654  ? -27.74600  92.45800  -1.44100  1.000 44.19740  ?  654  MET   A C   1 
ATOM   5191  O  O   . MET   A 1 654  ? -26.74900  92.33200  -0.72200  1.000 47.61616  ?  654  MET   A O   1 
ATOM   5192  C  CB  . MET   A 1 654  ? -29.25700  90.83600  -0.26100  1.000 46.51619  ?  654  MET   A CB  1 
ATOM   5193  C  CG  . MET   A 1 654  ? -30.69100  90.45700  0.09800   1.000 35.93503  ?  654  MET   A CG  1 
ATOM   5194  S  SD  . MET   A 1 654  ? -30.87100  89.29300  1.47000   1.000 50.70976  ?  654  MET   A SD  1 
ATOM   5195  C  CE  . MET   A 1 654  ? -29.65500  89.91900  2.62400   1.000 39.32755  ?  654  MET   A CE  1 
ATOM   5196  N  N   . ILE   A 1 655  ? -27.65800  92.77000  -2.73000  1.000 37.27768  ?  655  ILE   A N   1 
ATOM   5197  C  CA  . ILE   A 1 655  ? -26.40200  93.16200  -3.36100  1.000 38.28831  ?  655  ILE   A CA  1 
ATOM   5198  C  C   . ILE   A 1 655  ? -26.25700  94.67200  -3.20500  1.000 40.93796  ?  655  ILE   A C   1 
ATOM   5199  O  O   . ILE   A 1 655  ? -27.16900  95.41100  -3.60700  1.000 45.70907  ?  655  ILE   A O   1 
ATOM   5200  C  CB  . ILE   A 1 655  ? -26.36000  92.75600  -4.83800  1.000 34.14626  ?  655  ILE   A CB  1 
ATOM   5201  C  CG1 . ILE   A 1 655  ? -26.63700  91.25900  -4.98300  1.000 23.42394  ?  655  ILE   A CG1 1 
ATOM   5202  C  CG2 . ILE   A 1 655  ? -25.01700  93.12800  -5.45100  1.000 46.02597  ?  655  ILE   A CG2 1 
ATOM   5203  C  CD1 . ILE   A 1 655  ? -26.66900  90.77600  -6.40900  1.000 36.47207  ?  655  ILE   A CD1 1 
ATOM   5204  N  N   . PRO   A 1 656  ? -25.16400  95.16300  -2.62200  1.000 44.66191  ?  656  PRO   A N   1 
ATOM   5205  C  CA  . PRO   A 1 656  ? -25.04700  96.60500  -2.37800  1.000 49.20486  ?  656  PRO   A CA  1 
ATOM   5206  C  C   . PRO   A 1 656  ? -25.07000  97.40500  -3.67200  1.000 47.88311  ?  656  PRO   A C   1 
ATOM   5207  O  O   . PRO   A 1 656  ? -24.63900  96.94000  -4.73000  1.000 38.62247  ?  656  PRO   A O   1 
ATOM   5208  C  CB  . PRO   A 1 656  ? -23.69900  96.73500  -1.66000  1.000 40.68413  ?  656  PRO   A CB  1 
ATOM   5209  C  CG  . PRO   A 1 656  ? -23.47100  95.39500  -1.04100  1.000 40.53035  ?  656  PRO   A CG  1 
ATOM   5210  C  CD  . PRO   A 1 656  ? -24.06800  94.40400  -1.99800  1.000 44.03470  ?  656  PRO   A CD  1 
ATOM   5211  N  N   . THR   A 1 657  ? -25.59900  98.62700  -3.57000  1.000 54.68095  ?  657  THR   A N   1 
ATOM   5212  C  CA  . THR   A 1 657  ? -25.68300  99.50600  -4.73100  1.000 42.80343  ?  657  THR   A CA  1 
ATOM   5213  C  C   . THR   A 1 657  ? -24.30000  99.96200  -5.18300  1.000 50.61934  ?  657  THR   A C   1 
ATOM   5214  O  O   . THR   A 1 657  ? -24.00200  99.96000  -6.38400  1.000 50.55292  ?  657  THR   A O   1 
ATOM   5215  C  CB  . THR   A 1 657  ? -26.56300  100.71300 -4.40900  1.000 62.96743  ?  657  THR   A CB  1 
ATOM   5216  O  OG1 . THR   A 1 657  ? -27.80300  100.26900 -3.84100  1.000 61.76151  ?  657  THR   A OG1 1 
ATOM   5217  C  CG2 . THR   A 1 657  ? -26.84300  101.50800 -5.67200  1.000 42.63714  ?  657  THR   A CG2 1 
ATOM   5218  N  N   . TYR   A 1 658  ? -23.44500  100.36300 -4.24200  1.000 51.85288  ?  658  TYR   A N   1 
ATOM   5219  C  CA  . TYR   A 1 658  ? -22.08400  100.77900 -4.54600  1.000 53.42246  ?  658  TYR   A CA  1 
ATOM   5220  C  C   . TYR   A 1 658  ? -21.10200  100.02600 -3.65900  1.000 49.14394  ?  658  TYR   A C   1 
ATOM   5221  O  O   . TYR   A 1 658  ? -21.43600  99.60700  -2.54700  1.000 49.40832  ?  658  TYR   A O   1 
ATOM   5222  C  CB  . TYR   A 1 658  ? -21.88800  102.29700 -4.35700  1.000 45.57414  ?  658  TYR   A CB  1 
ATOM   5223  C  CG  . TYR   A 1 658  ? -23.04200  103.14700 -4.83900  1.000 55.85533  ?  658  TYR   A CG  1 
ATOM   5224  C  CD1 . TYR   A 1 658  ? -23.18300  103.47000 -6.18400  1.000 62.47779  ?  658  TYR   A CD1 1 
ATOM   5225  C  CD2 . TYR   A 1 658  ? -23.98900  103.63500 -3.94800  1.000 69.65367  ?  658  TYR   A CD2 1 
ATOM   5226  C  CE1 . TYR   A 1 658  ? -24.24200  104.25200 -6.62700  1.000 67.11275  ?  658  TYR   A CE1 1 
ATOM   5227  C  CE2 . TYR   A 1 658  ? -25.04700  104.41500 -4.38200  1.000 71.98173  ?  658  TYR   A CE2 1 
ATOM   5228  C  CZ  . TYR   A 1 658  ? -25.17000  104.72100 -5.71700  1.000 78.51946  ?  658  TYR   A CZ  1 
ATOM   5229  O  OH  . TYR   A 1 658  ? -26.22900  105.49800 -6.13200  1.000 90.11315  ?  658  TYR   A OH  1 
ATOM   5230  N  N   . PHE   A 1 659  ? -19.88200  99.85900  -4.16200  1.000 41.12804  ?  659  PHE   A N   1 
ATOM   5231  C  CA  . PHE   A 1 659  ? -18.79800  99.24100  -3.41400  1.000 47.10290  ?  659  PHE   A CA  1 
ATOM   5232  C  C   . PHE   A 1 659  ? -17.64800  100.23200 -3.28100  1.000 48.07594  ?  659  PHE   A C   1 
ATOM   5233  O  O   . PHE   A 1 659  ? -17.36700  100.99500 -4.21000  1.000 56.49316  ?  659  PHE   A O   1 
ATOM   5234  C  CB  . PHE   A 1 659  ? -18.31300  97.96200  -4.10000  1.000 42.39354  ?  659  PHE   A CB  1 
ATOM   5235  C  CG  . PHE   A 1 659  ? -19.31300  96.83900  -4.07400  1.000 52.51331  ?  659  PHE   A CG  1 
ATOM   5236  C  CD1 . PHE   A 1 659  ? -19.36800  95.96800  -2.99800  1.000 54.72729  ?  659  PHE   A CD1 1 
ATOM   5237  C  CD2 . PHE   A 1 659  ? -20.19100  96.64700  -5.13000  1.000 59.28715  ?  659  PHE   A CD2 1 
ATOM   5238  C  CE1 . PHE   A 1 659  ? -20.28300  94.92800  -2.97200  1.000 50.12485  ?  659  PHE   A CE1 1 
ATOM   5239  C  CE2 . PHE   A 1 659  ? -21.11100  95.60900  -5.11000  1.000 43.39719  ?  659  PHE   A CE2 1 
ATOM   5240  C  CZ  . PHE   A 1 659  ? -21.15500  94.74900  -4.02900  1.000 44.67761  ?  659  PHE   A CZ  1 
ATOM   5241  N  N   . VAL   A 1 660  ? -16.98900  100.22300 -2.12300  1.000 55.65025  ?  660  VAL   A N   1 
ATOM   5242  C  CA  . VAL   A 1 660  ? -15.89000  101.14000 -1.82800  1.000 56.37715  ?  660  VAL   A CA  1 
ATOM   5243  C  C   . VAL   A 1 660  ? -14.68300  100.32800 -1.37900  1.000 51.04091  ?  660  VAL   A C   1 
ATOM   5244  O  O   . VAL   A 1 660  ? -14.77200  99.56000  -0.41400  1.000 56.86831  ?  660  VAL   A O   1 
ATOM   5245  C  CB  . VAL   A 1 660  ? -16.26700  102.17200 -0.75200  1.000 50.16270  ?  660  VAL   A CB  1 
ATOM   5246  C  CG1 . VAL   A 1 660  ? -15.24100  103.28800 -0.71100  1.000 42.62606  ?  660  VAL   A CG1 1 
ATOM   5247  C  CG2 . VAL   A 1 660  ? -17.64300  102.74300 -1.02500  1.000 54.13607  ?  660  VAL   A CG2 1 
ATOM   5248  N  N   . HIS   A 1 661  ? -13.55400  100.51300 -2.06300  1.000 61.71237  ?  661  HIS   A N   1 
ATOM   5249  C  CA  . HIS   A 1 661  ? -12.30800  99.84900  -1.70400  1.000 59.46117  ?  661  HIS   A CA  1 
ATOM   5250  C  C   . HIS   A 1 661  ? -11.55300  100.66200 -0.66100  1.000 59.08580  ?  661  HIS   A C   1 
ATOM   5251  O  O   . HIS   A 1 661  ? -11.44500  101.88700 -0.76400  1.000 58.27784  ?  661  HIS   A O   1 
ATOM   5252  C  CB  . HIS   A 1 661  ? -11.42400  99.64600  -2.93500  1.000 52.83636  ?  661  HIS   A CB  1 
ATOM   5253  C  CG  . HIS   A 1 661  ? -10.04800  99.14500  -2.61600  1.000 64.16368  ?  661  HIS   A CG  1 
ATOM   5254  N  ND1 . HIS   A 1 661  ? -8.93500   99.95700  -2.64600  1.000 63.78987  ?  661  HIS   A ND1 1 
ATOM   5255  C  CD2 . HIS   A 1 661  ? -9.60400   97.91400  -2.27000  1.000 77.33571  ?  661  HIS   A CD2 1 
ATOM   5256  C  CE1 . HIS   A 1 661  ? -7.86600   99.25000  -2.32800  1.000 61.82846  ?  661  HIS   A CE1 1 
ATOM   5257  N  NE2 . HIS   A 1 661  ? -8.24400   98.00600  -2.09500  1.000 58.36944  ?  661  HIS   A NE2 1 
ATOM   5258  N  N   . MET   A 1 662  ? -11.02800  99.96900  0.34400   1.000 60.28954  ?  662  MET   A N   1 
ATOM   5259  C  CA  . MET   A 1 662  ? -10.22500  100.58700 1.38600   1.000 68.09773  ?  662  MET   A CA  1 
ATOM   5260  C  C   . MET   A 1 662  ? -8.92400   99.81700  1.54300   1.000 70.31818  ?  662  MET   A C   1 
ATOM   5261  O  O   . MET   A 1 662  ? -8.84800   98.62400  1.23500   1.000 66.46378  ?  662  MET   A O   1 
ATOM   5262  C  CB  . MET   A 1 662  ? -10.96400  100.62500 2.73200   1.000 58.03578  ?  662  MET   A CB  1 
ATOM   5263  C  CG  . MET   A 1 662  ? -12.46400  100.80900 2.61900   1.000 62.86652  ?  662  MET   A CG  1 
ATOM   5264  S  SD  . MET   A 1 662  ? -12.94600  102.52200 2.88400   1.000 85.42463  ?  662  MET   A SD  1 
ATOM   5265  C  CE  . MET   A 1 662  ? -12.26100  102.79700 4.51400   1.000 53.25743  ?  662  MET   A CE  1 
ATOM   5266  N  N   . LYS   A 1 663  ? -7.89400   100.51300 2.01900   1.000 65.49134  ?  663  LYS   A N   1 
ATOM   5267  C  CA  . LYS   A 1 663  ? -6.64300   99.85200  2.36200   1.000 60.45765  ?  663  LYS   A CA  1 
ATOM   5268  C  C   . LYS   A 1 663  ? -6.60100   99.42000  3.81900   1.000 61.10712  ?  663  LYS   A C   1 
ATOM   5269  O  O   . LYS   A 1 663  ? -5.93100   98.43400  4.14600   1.000 63.50790  ?  663  LYS   A O   1 
ATOM   5270  C  CB  . LYS   A 1 663  ? -5.45900   100.77100 2.05200   1.000 78.41737  ?  663  LYS   A CB  1 
ATOM   5271  C  CG  . LYS   A 1 663  ? -5.64700   101.60400 0.79500   1.000 85.50169  ?  663  LYS   A CG  1 
ATOM   5272  C  CD  . LYS   A 1 663  ? -4.31600   102.09500 0.25100   1.000 89.69639  ?  663  LYS   A CD  1 
ATOM   5273  C  CE  . LYS   A 1 663  ? -4.24200   101.93300 -1.26200  1.000 81.16989  ?  663  LYS   A CE  1 
ATOM   5274  N  NZ  . LYS   A 1 663  ? -4.26600   100.50200 -1.68300  1.000 83.37255  ?  663  LYS   A NZ  1 
ATOM   5275  N  N   . ALA   A 1 664  ? -7.31400   100.12600 4.69700   1.000 54.46672  ?  664  ALA   A N   1 
ATOM   5276  C  CA  . ALA   A 1 664  ? -7.41100   99.74000  6.10000   1.000 63.95773  ?  664  ALA   A CA  1 
ATOM   5277  C  C   . ALA   A 1 664  ? -8.66300   100.36400 6.69600   1.000 56.46051  ?  664  ALA   A C   1 
ATOM   5278  O  O   . ALA   A 1 664  ? -8.93600   101.54700 6.46900   1.000 58.96177  ?  664  ALA   A O   1 
ATOM   5279  C  CB  . ALA   A 1 664  ? -6.16800   100.17500 6.88500   1.000 58.84622  ?  664  ALA   A CB  1 
ATOM   5280  N  N   . PHE   A 1 665  ? -9.41400   99.57600  7.45300   1.000 56.36932  ?  665  PHE   A N   1 
ATOM   5281  C  CA  . PHE   A 1 665  ? -10.63100  100.08400 8.07500   1.000 57.58325  ?  665  PHE   A CA  1 
ATOM   5282  C  C   . PHE   A 1 665  ? -10.27800  100.99000 9.24900   1.000 62.72205  ?  665  PHE   A C   1 
ATOM   5283  O  O   . PHE   A 1 665  ? -9.47800   100.60000 10.10800  1.000 59.29760  ?  665  PHE   A O   1 
ATOM   5284  C  CB  . PHE   A 1 665  ? -11.51600  98.93300  8.55200   1.000 64.55885  ?  665  PHE   A CB  1 
ATOM   5285  C  CG  . PHE   A 1 665  ? -12.44000  98.39400  7.49700   1.000 70.96073  ?  665  PHE   A CG  1 
ATOM   5286  C  CD1 . PHE   A 1 665  ? -12.59700  99.05200  6.28800   1.000 62.46332  ?  665  PHE   A CD1 1 
ATOM   5287  C  CD2 . PHE   A 1 665  ? -13.15300  97.22600  7.71700   1.000 58.80178  ?  665  PHE   A CD2 1 
ATOM   5288  C  CE1 . PHE   A 1 665  ? -13.44800  98.55400  5.31600   1.000 62.26156  ?  665  PHE   A CE1 1 
ATOM   5289  C  CE2 . PHE   A 1 665  ? -14.00500  96.72200  6.75200   1.000 52.32794  ?  665  PHE   A CE2 1 
ATOM   5290  C  CZ  . PHE   A 1 665  ? -14.15200  97.38700  5.54900   1.000 59.86491  ?  665  PHE   A CZ  1 
ATOM   5291  N  N   . PRO   A 1 666  ? -10.84400  102.19500 9.32700   1.000 60.08553  ?  666  PRO   A N   1 
ATOM   5292  C  CA  . PRO   A 1 666  ? -10.58800  103.05100 10.49300  1.000 48.11933  ?  666  PRO   A CA  1 
ATOM   5293  C  C   . PRO   A 1 666  ? -11.23000  102.46500 11.74200  1.000 62.70244  ?  666  PRO   A C   1 
ATOM   5294  O  O   . PRO   A 1 666  ? -12.39600  102.06600 11.73200  1.000 59.02645  ?  666  PRO   A O   1 
ATOM   5295  C  CB  . PRO   A 1 666  ? -11.22700  104.38900 10.10200  1.000 50.75011  ?  666  PRO   A CB  1 
ATOM   5296  C  CG  . PRO   A 1 666  ? -12.26500  104.02600 9.09100   1.000 62.02583  ?  666  PRO   A CG  1 
ATOM   5297  C  CD  . PRO   A 1 666  ? -11.70700  102.85400 8.33300   1.000 66.15605  ?  666  PRO   A CD  1 
ATOM   5298  N  N   . LEU   A 1 667  ? -10.45300  102.41000 12.81900  1.000 76.98326  ?  667  LEU   A N   1 
ATOM   5299  C  CA  . LEU   A 1 667  ? -10.90600  101.87800 14.09600  1.000 65.76714  ?  667  LEU   A CA  1 
ATOM   5300  C  C   . LEU   A 1 667  ? -11.13200  103.01100 15.08600  1.000 66.18540  ?  667  LEU   A C   1 
ATOM   5301  O  O   . LEU   A 1 667  ? -10.32200  103.94000 15.17800  1.000 68.22609  ?  667  LEU   A O   1 
ATOM   5302  C  CB  . LEU   A 1 667  ? -9.88900   100.88500 14.67000  1.000 53.89639  ?  667  LEU   A CB  1 
ATOM   5303  C  CG  . LEU   A 1 667  ? -10.15000  99.40100  14.40600  1.000 60.98295  ?  667  LEU   A CG  1 
ATOM   5304  C  CD1 . LEU   A 1 667  ? -10.14500  99.12000  12.92300  1.000 66.36054  ?  667  LEU   A CD1 1 
ATOM   5305  C  CD2 . LEU   A 1 667  ? -9.10800   98.54600  15.10700  1.000 51.49255  ?  667  LEU   A CD2 1 
ATOM   5306  N  N   . THR   A 1 668  ? -12.23700  102.93000 15.82400  1.000 63.96681  ?  668  THR   A N   1 
ATOM   5307  C  CA  . THR   A 1 668  ? -12.46400  103.86500 16.91100  1.000 59.50899  ?  668  THR   A CA  1 
ATOM   5308  C  C   . THR   A 1 668  ? -11.41700  103.65700 18.00200  1.000 84.33056  ?  668  THR   A C   1 
ATOM   5309  O  O   . THR   A 1 668  ? -10.62100  102.71300 17.97300  1.000 98.87170  ?  668  THR   A O   1 
ATOM   5310  C  CB  . THR   A 1 668  ? -13.86500  103.69500 17.50100  1.000 59.14305  ?  668  THR   A CB  1 
ATOM   5311  O  OG1 . THR   A 1 668  ? -13.84900  102.65600 18.48800  1.000 60.26027  ?  668  THR   A OG1 1 
ATOM   5312  C  CG2 . THR   A 1 668  ? -14.86300  103.33700 16.41800  1.000 56.88225  ?  668  THR   A CG2 1 
ATOM   5313  N  N   . ALA   A 1 669  ? -11.43300  104.54600 18.98400  1.000 85.20409  ?  669  ALA   A N   1 
ATOM   5314  C  CA  . ALA   A 1 669  ? -10.49300  104.43200 20.09100  1.000 83.45453  ?  669  ALA   A CA  1 
ATOM   5315  C  C   . ALA   A 1 669  ? -10.78100  103.24600 20.99600  1.000 84.69132  ?  669  ALA   A C   1 
ATOM   5316  O  O   . ALA   A 1 669  ? -10.13300  103.13000 22.04700  1.000 98.30496  ?  669  ALA   A O   1 
ATOM   5317  C  CB  . ALA   A 1 669  ? -10.49300  105.72500 20.90900  1.000 100.08423 ?  669  ALA   A CB  1 
ATOM   5318  N  N   . ASN   A 1 670  ? -11.71400  102.35800 20.63400  1.000 62.83951  ?  670  ASN   A N   1 
ATOM   5319  C  CA  . ASN   A 1 670  ? -12.07400  101.23300 21.48700  1.000 80.73992  ?  670  ASN   A CA  1 
ATOM   5320  C  C   . ASN   A 1 670  ? -12.11300  99.91400  20.72400  1.000 72.07396  ?  670  ASN   A C   1 
ATOM   5321  O  O   . ASN   A 1 670  ? -12.74700  98.95900  21.18500  1.000 55.92693  ?  670  ASN   A O   1 
ATOM   5322  C  CB  . ASN   A 1 670  ? -13.41800  101.49200 22.16500  1.000 72.73009  ?  670  ASN   A CB  1 
ATOM   5323  C  CG  . ASN   A 1 670  ? -13.47500  102.85200 22.81200  1.000 75.29578  ?  670  ASN   A CG  1 
ATOM   5324  O  OD1 . ASN   A 1 670  ? -12.87500  103.07500 23.86200  1.000 79.93317  ?  670  ASN   A OD1 1 
ATOM   5325  N  ND2 . ASN   A 1 670  ? -14.18700  103.77900 22.18100  1.000 80.57139  ?  670  ASN   A ND2 1 
ATOM   5326  N  N   . GLY   A 1 671  ? -11.45500  99.84200  19.56800  1.000 62.00835  ?  671  GLY   A N   1 
ATOM   5327  C  CA  . GLY   A 1 671  ? -11.33500  98.59700  18.83900  1.000 52.99606  ?  671  GLY   A CA  1 
ATOM   5328  C  C   . GLY   A 1 671  ? -12.50400  98.23500  17.95400  1.000 50.07523  ?  671  GLY   A C   1 
ATOM   5329  O  O   . GLY   A 1 671  ? -12.52100  97.12600  17.41000  1.000 62.18178  ?  671  GLY   A O   1 
ATOM   5330  N  N   . LYS   A 1 672  ? -13.48500  99.11400  17.80200  1.000 40.55076  ?  672  LYS   A N   1 
ATOM   5331  C  CA  . LYS   A 1 672  ? -14.57100  98.90600  16.85700  1.000 43.43571  ?  672  LYS   A CA  1 
ATOM   5332  C  C   . LYS   A 1 672  ? -14.26200  99.63300  15.55500  1.000 57.48165  ?  672  LYS   A C   1 
ATOM   5333  O  O   . LYS   A 1 672  ? -13.47000  100.57700 15.51700  1.000 64.16123  ?  672  LYS   A O   1 
ATOM   5334  C  CB  . LYS   A 1 672  ? -15.90500  99.39500  17.43100  1.000 57.48411  ?  672  LYS   A CB  1 
ATOM   5335  C  CG  . LYS   A 1 672  ? -16.56100  98.44300  18.42600  1.000 58.24165  ?  672  LYS   A CG  1 
ATOM   5336  C  CD  . LYS   A 1 672  ? -17.97200  98.90700  18.78000  1.000 54.53108  ?  672  LYS   A CD  1 
ATOM   5337  C  CE  . LYS   A 1 672  ? -18.63900  97.96500  19.76900  1.000 49.25016  ?  672  LYS   A CE  1 
ATOM   5338  N  NZ  . LYS   A 1 672  ? -17.82500  97.79900  21.00400  1.000 67.10498  ?  672  LYS   A NZ  1 
ATOM   5339  N  N   . VAL   A 1 673  ? -14.89000  99.17700  14.47800  1.000 59.03539  ?  673  VAL   A N   1 
ATOM   5340  C  CA  . VAL   A 1 673  ? -14.72000  99.81700  13.17800  1.000 66.47895  ?  673  VAL   A CA  1 
ATOM   5341  C  C   . VAL   A 1 673  ? -15.51100  101.12000 13.17600  1.000 68.15396  ?  673  VAL   A C   1 
ATOM   5342  O  O   . VAL   A 1 673  ? -16.72200  101.12200 13.41800  1.000 75.42060  ?  673  VAL   A O   1 
ATOM   5343  C  CB  . VAL   A 1 673  ? -15.17000  98.89100  12.04000  1.000 56.38268  ?  673  VAL   A CB  1 
ATOM   5344  C  CG1 . VAL   A 1 673  ? -15.02900  99.58900  10.69500  1.000 52.52548  ?  673  VAL   A CG1 1 
ATOM   5345  C  CG2 . VAL   A 1 673  ? -14.35800  97.61400  12.06300  1.000 43.50845  ?  673  VAL   A CG2 1 
ATOM   5346  N  N   . ASP   A 1 674  ? -14.82600  102.23100 12.91100  1.000 61.15860  ?  674  ASP   A N   1 
ATOM   5347  C  CA  . ASP   A 1 674  ? -15.47100  103.54300 12.89200  1.000 67.51198  ?  674  ASP   A CA  1 
ATOM   5348  C  C   . ASP   A 1 674  ? -16.37400  103.62800 11.67000  1.000 67.64887  ?  674  ASP   A C   1 
ATOM   5349  O  O   . ASP   A 1 674  ? -15.92400  103.94900 10.56800  1.000 69.35625  ?  674  ASP   A O   1 
ATOM   5350  C  CB  . ASP   A 1 674  ? -14.42900  104.65600 12.89100  1.000 65.82025  ?  674  ASP   A CB  1 
ATOM   5351  C  CG  . ASP   A 1 674  ? -14.97100  105.95800 13.45300  1.000 74.33522  ?  674  ASP   A CG  1 
ATOM   5352  O  OD1 . ASP   A 1 674  ? -16.21000  106.12000 13.48900  1.000 78.03352  ?  674  ASP   A OD1 1 
ATOM   5353  O  OD2 . ASP   A 1 674  ? -14.16100  106.81600 13.86400  1.000 79.57197  -1 674  ASP   A OD2 1 
ATOM   5354  N  N   . ARG   A 1 675  ? -17.66300  103.34600 11.86600  1.000 61.15212  ?  675  ARG   A N   1 
ATOM   5355  C  CA  . ARG   A 1 675  ? -18.58900  103.31600 10.74000  1.000 57.67462  ?  675  ARG   A CA  1 
ATOM   5356  C  C   . ARG   A 1 675  ? -18.84900  104.71000 10.18500  1.000 69.85224  ?  675  ARG   A C   1 
ATOM   5357  O  O   . ARG   A 1 675  ? -19.10200  104.85700 8.98400   1.000 80.08951  ?  675  ARG   A O   1 
ATOM   5358  C  CB  . ARG   A 1 675  ? -19.89800  102.64700 11.15800  1.000 54.15580  ?  675  ARG   A CB  1 
ATOM   5359  C  CG  . ARG   A 1 675  ? -19.69900  101.46600 12.09700  1.000 60.32061  ?  675  ARG   A CG  1 
ATOM   5360  C  CD  . ARG   A 1 675  ? -20.25400  100.17400 11.51600  1.000 65.18565  ?  675  ARG   A CD  1 
ATOM   5361  N  NE  . ARG   A 1 675  ? -21.71000  100.18500 11.43600  1.000 78.47712  ?  675  ARG   A NE  1 
ATOM   5362  C  CZ  . ARG   A 1 675  ? -22.45900  99.10200  11.28100  1.000 97.40212  ?  675  ARG   A CZ  1 
ATOM   5363  N  NH1 . ARG   A 1 675  ? -21.92000  97.89800  11.17300  1.000 100.31451 ?  675  ARG   A NH1 1 
ATOM   5364  N  NH2 . ARG   A 1 675  ? -23.78200  99.22900  11.23500  1.000 94.74884  ?  675  ARG   A NH2 1 
ATOM   5365  N  N   . ARG   A 1 676  ? -18.78100  105.73900 11.02600  1.000 66.40848  ?  676  ARG   A N   1 
ATOM   5366  C  CA  . ARG   A 1 676  ? -19.01100  107.10300 10.57200  1.000 68.03346  ?  676  ARG   A CA  1 
ATOM   5367  C  C   . ARG   A 1 676  ? -17.76000  107.75800 10.00100  1.000 66.98061  ?  676  ARG   A C   1 
ATOM   5368  O  O   . ARG   A 1 676  ? -17.82400  108.91200 9.56500   1.000 81.17801  ?  676  ARG   A O   1 
ATOM   5369  C  CB  . ARG   A 1 676  ? -19.59300  107.95900 11.71000  1.000 71.39731  ?  676  ARG   A CB  1 
ATOM   5370  C  CG  . ARG   A 1 676  ? -21.04400  107.60400 12.13800  1.000 89.21253  ?  676  ARG   A CG  1 
ATOM   5371  C  CD  . ARG   A 1 676  ? -22.11600  107.99100 11.09100  1.000 101.42492 ?  676  ARG   A CD  1 
ATOM   5372  N  NE  . ARG   A 1 676  ? -21.85100  107.36600 9.80100   1.000 96.27273  ?  676  ARG   A NE  1 
ATOM   5373  C  CZ  . ARG   A 1 676  ? -21.78800  108.01000 8.64400   1.000 98.20863  ?  676  ARG   A CZ  1 
ATOM   5374  N  NH1 . ARG   A 1 676  ? -22.14200  109.28100 8.53800   1.000 91.28487  ?  676  ARG   A NH1 1 
ATOM   5375  N  NH2 . ARG   A 1 676  ? -21.33400  107.36900 7.57400   1.000 86.19571  ?  676  ARG   A NH2 1 
ATOM   5376  N  N   . ALA   A 1 677  ? -16.63400  107.05100 9.98600   1.000 66.58315  ?  677  ALA   A N   1 
ATOM   5377  C  CA  . ALA   A 1 677  ? -15.44100  107.48700 9.27900   1.000 59.63303  ?  677  ALA   A CA  1 
ATOM   5378  C  C   . ALA   A 1 677  ? -15.27700  106.78700 7.93900   1.000 62.08239  ?  677  ALA   A C   1 
ATOM   5379  O  O   . ALA   A 1 677  ? -14.27500  107.01100 7.25200   1.000 69.93048  ?  677  ALA   A O   1 
ATOM   5380  C  CB  . ALA   A 1 677  ? -14.19700  107.25500 10.14100  1.000 69.90951  ?  677  ALA   A CB  1 
ATOM   5381  N  N   . LEU   A 1 678  ? -16.22600  105.94700 7.55700   1.000 71.13843  ?  678  LEU   A N   1 
ATOM   5382  C  CA  . LEU   A 1 678  ? -16.15000  105.25800 6.27800   1.000 65.86107  ?  678  LEU   A CA  1 
ATOM   5383  C  C   . LEU   A 1 678  ? -16.53500  106.21700 5.15800   1.000 58.58647  ?  678  LEU   A C   1 
ATOM   5384  O  O   . LEU   A 1 678  ? -17.53300  106.93500 5.28200   1.000 61.74648  ?  678  LEU   A O   1 
ATOM   5385  C  CB  . LEU   A 1 678  ? -17.06400  104.03600 6.27600   1.000 67.20588  ?  678  LEU   A CB  1 
ATOM   5386  C  CG  . LEU   A 1 678  ? -16.59900  102.88500 7.17600   1.000 60.22957  ?  678  LEU   A CG  1 
ATOM   5387  C  CD1 . LEU   A 1 678  ? -17.59100  101.73100 7.16300   1.000 52.11825  ?  678  LEU   A CD1 1 
ATOM   5388  C  CD2 . LEU   A 1 678  ? -15.21200  102.40700 6.77600   1.000 62.38606  ?  678  LEU   A CD2 1 
ATOM   5389  N  N   . PRO   A 1 679  ? -15.76800  106.26800 4.06900   1.000 63.49908  ?  679  PRO   A N   1 
ATOM   5390  C  CA  . PRO   A 1 679  ? -16.03200  107.25000 3.01000   1.000 48.00028  ?  679  PRO   A CA  1 
ATOM   5391  C  C   . PRO   A 1 679  ? -17.44800  107.12900 2.46800   1.000 69.23956  ?  679  PRO   A C   1 
ATOM   5392  O  O   . PRO   A 1 679  ? -17.88700  106.04900 2.07100   1.000 72.95782  ?  679  PRO   A O   1 
ATOM   5393  C  CB  . PRO   A 1 679  ? -14.99300  106.89000 1.94400   1.000 38.46923  ?  679  PRO   A CB  1 
ATOM   5394  C  CG  . PRO   A 1 679  ? -13.85800  106.33300 2.74100   1.000 66.06764  ?  679  PRO   A CG  1 
ATOM   5395  C  CD  . PRO   A 1 679  ? -14.54000  105.50100 3.80000   1.000 64.66806  ?  679  PRO   A CD  1 
ATOM   5396  N  N   . ASP   A 1 680  ? -18.16400  108.24700 2.45300   1.000 66.60488  ?  680  ASP   A N   1 
ATOM   5397  C  CA  . ASP   A 1 680  ? -19.47900  108.27400 1.83300   1.000 65.17847  ?  680  ASP   A CA  1 
ATOM   5398  C  C   . ASP   A 1 680  ? -19.33300  108.28700 0.31800   1.000 73.80307  ?  680  ASP   A C   1 
ATOM   5399  O  O   . ASP   A 1 680  ? -18.39300  108.87700 -0.22400  1.000 67.32243  ?  680  ASP   A O   1 
ATOM   5400  C  CB  . ASP   A 1 680  ? -20.27200  109.49200 2.29900   1.000 67.47654  ?  680  ASP   A CB  1 
ATOM   5401  C  CG  . ASP   A 1 680  ? -21.76200  109.23000 2.33400   1.000 95.76668  ?  680  ASP   A CG  1 
ATOM   5402  O  OD1 . ASP   A 1 680  ? -22.28200  108.60200 1.38600   1.000 86.48985  ?  680  ASP   A OD1 1 
ATOM   5403  O  OD2 . ASP   A 1 680  ? -22.41000  109.63500 3.32100   1.000 95.69488  -1 680  ASP   A OD2 1 
ATOM   5404  N  N   . VAL   A 1 681  ? -20.26500  107.62800 -0.37000  1.000 88.86199  ?  681  VAL   A N   1 
ATOM   5405  C  CA  . VAL   A 1 681  ? -20.15600  107.50600 -1.81800  1.000 88.33788  ?  681  VAL   A CA  1 
ATOM   5406  C  C   . VAL   A 1 681  ? -20.44500  108.85700 -2.46300  1.000 100.67797 ?  681  VAL   A C   1 
ATOM   5407  O  O   . VAL   A 1 681  ? -21.38200  109.56700 -2.07400  1.000 97.26020  ?  681  VAL   A O   1 
ATOM   5408  C  CB  . VAL   A 1 681  ? -21.06300  106.37800 -2.34700  1.000 79.71320  ?  681  VAL   A CB  1 
ATOM   5409  C  CG1 . VAL   A 1 681  ? -20.94000  105.14600 -1.46200  1.000 76.52970  ?  681  VAL   A CG1 1 
ATOM   5410  C  CG2 . VAL   A 1 681  ? -22.52900  106.80500 -2.44800  1.000 92.56364  ?  681  VAL   A CG2 1 
ATOM   5411  N  N   . GLN   A 1 682  ? -19.58000  109.25200 -3.40300  1.000 99.19883  ?  682  GLN   A N   1 
ATOM   5412  C  CA  . GLN   A 1 682  ? -19.75300  110.52000 -4.10600  1.000 112.40457 ?  682  GLN   A CA  1 
ATOM   5413  C  C   . GLN   A 1 682  ? -21.04200  110.51600 -4.91700  1.000 126.44516 ?  682  GLN   A C   1 
ATOM   5414  O  O   . GLN   A 1 682  ? -21.85300  111.44500 -4.82700  1.000 130.53982 ?  682  GLN   A O   1 
ATOM   5415  C  CB  . GLN   A 1 682  ? -18.54100  110.78200 -5.00600  1.000 117.19683 ?  682  GLN   A CB  1 
ATOM   5416  C  CG  . GLN   A 1 682  ? -18.81900  111.57200 -6.28600  1.000 130.94481 ?  682  GLN   A CG  1 
ATOM   5417  C  CD  . GLN   A 1 682  ? -19.42200  112.94500 -6.04500  1.000 128.71374 ?  682  GLN   A CD  1 
ATOM   5418  O  OE1 . GLN   A 1 682  ? -20.52400  113.24300 -6.50700  1.000 137.83351 ?  682  GLN   A OE1 1 
ATOM   5419  N  NE2 . GLN   A 1 682  ? -18.68400  113.79800 -5.35500  1.000 113.80482 ?  682  GLN   A NE2 1 
ATOM   5420  N  N   . ALA   A 1 683  ? -21.25300  109.46400 -5.70500  1.000 135.92567 ?  683  ALA   A N   1 
ATOM   5421  C  CA  . ALA   A 1 683  ? -22.39100  109.36800 -6.61400  1.000 142.29215 ?  683  ALA   A CA  1 
ATOM   5422  C  C   . ALA   A 1 683  ? -23.67300  108.92400 -5.91900  1.000 129.56620 ?  683  ALA   A C   1 
ATOM   5423  O  O   . ALA   A 1 683  ? -24.47100  108.19200 -6.51300  1.000 124.02276 ?  683  ALA   A O   1 
ATOM   5424  C  CB  . ALA   A 1 683  ? -22.04500  108.43500 -7.77100  1.000 113.67461 ?  683  ALA   A CB  1 
ATOM   5425  N  N   . ASP   A 1 684  ? -23.92100  109.34800 -4.67200  1.000 123.48528 ?  684  ASP   A N   1 
ATOM   5426  C  CA  . ASP   A 1 684  ? -25.20400  109.04300 -4.04000  1.000 116.40413 ?  684  ASP   A CA  1 
ATOM   5427  C  C   . ASP   A 1 684  ? -26.35600  109.63800 -4.83900  1.000 130.16041 ?  684  ASP   A C   1 
ATOM   5428  O  O   . ASP   A 1 684  ? -27.40600  109.00200 -4.98400  1.000 131.42276 ?  684  ASP   A O   1 
ATOM   5429  C  CB  . ASP   A 1 684  ? -25.22600  109.54800 -2.59400  1.000 115.41837 ?  684  ASP   A CB  1 
ATOM   5430  C  CG  . ASP   A 1 684  ? -24.95800  111.03900 -2.48400  1.000 131.05673 ?  684  ASP   A CG  1 
ATOM   5431  O  OD1 . ASP   A 1 684  ? -24.25800  111.59300 -3.35700  1.000 135.19682 ?  684  ASP   A OD1 1 
ATOM   5432  O  OD2 . ASP   A 1 684  ? -25.45000  111.65800 -1.51600  1.000 126.31733 ?  684  ASP   A OD2 1 
ATOM   5433  N  N   . ALA   A 1 685  ? -26.16000  110.85900 -5.36300  1.000 141.37224 ?  685  ALA   A N   1 
ATOM   5434  C  CA  . ALA   A 1 685  ? -27.02900  111.57700 -6.29700  1.000 140.99798 ?  685  ALA   A CA  1 
ATOM   5435  C  C   . ALA   A 1 685  ? -28.36100  110.88800 -6.54800  1.000 135.76772 ?  685  ALA   A C   1 
ATOM   5436  O  O   . ALA   A 1 685  ? -29.36000  111.18200 -5.88500  1.000 134.81468 ?  685  ALA   A O   1 
ATOM   5437  C  CB  . ALA   A 1 685  ? -26.30300  111.77800 -7.63100  1.000 125.13823 ?  685  ALA   A CB  1 
ATOM   5438  N  N   . GLU   A 1 686  ? -28.37200  109.96400 -7.50400  1.000 116.66520 ?  686  GLU   A N   1 
ATOM   5439  C  CA  . GLU   A 1 686  ? -29.49000  109.05200 -7.69100  1.000 109.79694 ?  686  GLU   A CA  1 
ATOM   5440  C  C   . GLU   A 1 686  ? -29.03800  107.86400 -8.52200  1.000 114.03169 ?  686  GLU   A C   1 
ATOM   5441  O  O   . GLU   A 1 686  ? -29.85800  107.01400 -8.88500  1.000 119.87077 ?  686  GLU   A O   1 
ATOM   5442  C  CB  . GLU   A 1 686  ? -30.67500  109.74800 -8.36100  1.000 98.77387  ?  686  GLU   A CB  1 
ATOM   5443  C  CG  . GLU   A 1 686  ? -32.02500  109.19500 -7.93200  1.000 101.95442 ?  686  GLU   A CG  1 
ATOM   5444  C  CD  . GLU   A 1 686  ? -32.42400  109.64800 -6.54300  1.000 104.99101 ?  686  GLU   A CD  1 
ATOM   5445  O  OE1 . GLU   A 1 686  ? -32.17100  110.82400 -6.20900  1.000 110.68520 ?  686  GLU   A OE1 1 
ATOM   5446  O  OE2 . GLU   A 1 686  ? -32.99600  108.83200 -5.78800  1.000 86.73296  ?  686  GLU   A OE2 1 
ATOM   5447  N  N   . LEU   A 1 687  ? -27.73500  107.81700 -8.82800  1.000 107.32293 ?  687  LEU   A N   1 
ATOM   5448  C  CA  . LEU   A 1 687  ? -27.13000  106.77300 -9.65000  1.000 112.28896 ?  687  LEU   A CA  1 
ATOM   5449  C  C   . LEU   A 1 687  ? -27.74700  105.41500 -9.36000  1.000 101.02238 ?  687  LEU   A C   1 
ATOM   5450  O  O   . LEU   A 1 687  ? -27.42000  104.77400 -8.35600  1.000 106.24135 ?  687  LEU   A O   1 
ATOM   5451  C  CB  . LEU   A 1 687  ? -25.61400  106.71500 -9.43000  1.000 97.63872  ?  687  LEU   A CB  1 
ATOM   5452  C  CG  . LEU   A 1 687  ? -24.83000  105.78300 -10.36500 1.000 90.33276  ?  687  LEU   A CG  1 
ATOM   5453  C  CD1 . LEU   A 1 687  ? -24.84300  106.29000 -11.80300 1.000 85.66617  ?  687  LEU   A CD1 1 
ATOM   5454  C  CD2 . LEU   A 1 687  ? -23.39900  105.57000 -9.87900  1.000 92.96698  ?  687  LEU   A CD2 1 
ATOM   5455  N  N   . LEU   A 1 688  ? -28.64500  104.97100 -10.23900 1.000 76.81544  ?  688  LEU   A N   1 
ATOM   5456  C  CA  . LEU   A 1 688  ? -29.33000  103.69400 -10.08700 1.000 80.67663  ?  688  LEU   A CA  1 
ATOM   5457  C  C   . LEU   A 1 688  ? -28.35400  102.53100 -10.20100 1.000 85.11828  ?  688  LEU   A C   1 
ATOM   5458  O  O   . LEU   A 1 688  ? -28.76500  101.37500 -10.34900 1.000 81.99402  ?  688  LEU   A O   1 
ATOM   5459  C  CB  . LEU   A 1 688  ? -30.43800  103.57000 -11.13200 1.000 78.14530  ?  688  LEU   A CB  1 
ATOM   5460  C  CG  . LEU   A 1 688  ? -31.31900  104.81200 -11.26200 1.000 68.47805  ?  688  LEU   A CG  1 
ATOM   5461  C  CD1 . LEU   A 1 688  ? -31.03400  105.54200 -12.56400 1.000 61.14880  ?  688  LEU   A CD1 1 
ATOM   5462  C  CD2 . LEU   A 1 688  ? -32.78100  104.42700 -11.16000 1.000 69.31585  ?  688  LEU   A CD2 1 
ATOM   5463  N  N   . GLY   A 1 689  ? -27.06600  102.83300 -10.12900 1.000 66.39213  ?  689  GLY   A N   1 
ATOM   5464  C  CA  . GLY   A 1 689  ? -25.98200  101.88500 -10.23100 1.000 70.31112  ?  689  GLY   A CA  1 
ATOM   5465  C  C   . GLY   A 1 689  ? -25.14600  102.12100 -11.47600 1.000 68.99404  ?  689  GLY   A C   1 
ATOM   5466  O  O   . GLY   A 1 689  ? -25.54300  102.82000 -12.41400 1.000 78.34042  ?  689  GLY   A O   1 
ATOM   5467  N  N   . GLU   A 1 690  ? -23.95100  101.53500 -11.46800 1.000 60.37521  ?  690  GLU   A N   1 
ATOM   5468  C  CA  . GLU   A 1 690  ? -23.14800  101.50300 -12.67900 1.000 64.56771  ?  690  GLU   A CA  1 
ATOM   5469  C  C   . GLU   A 1 690  ? -23.73600  100.55300 -13.71100 1.000 62.44639  ?  690  GLU   A C   1 
ATOM   5470  O  O   . GLU   A 1 690  ? -23.45700  100.69800 -14.90500 1.000 68.10113  ?  690  GLU   A O   1 
ATOM   5471  C  CB  . GLU   A 1 690  ? -21.71400  101.10500 -12.33600 1.000 68.10122  ?  690  GLU   A CB  1 
ATOM   5472  C  CG  . GLU   A 1 690  ? -21.30800  101.50900 -10.92600 1.000 90.06951  ?  690  GLU   A CG  1 
ATOM   5473  C  CD  . GLU   A 1 690  ? -19.83400  101.83700 -10.80700 1.000 87.30466  ?  690  GLU   A CD  1 
ATOM   5474  O  OE1 . GLU   A 1 690  ? -19.02300  101.18600 -11.49800 1.000 70.74255  ?  690  GLU   A OE1 1 
ATOM   5475  O  OE2 . GLU   A 1 690  ? -19.48800  102.74000 -10.01400 1.000 89.54063  -1 690  GLU   A OE2 1 
ATOM   5476  N  N   . ASP   A 1 691  ? -24.55200  99.59500  -13.27200 1.000 69.15782  ?  691  ASP   A N   1 
ATOM   5477  C  CA  . ASP   A 1 691  ? -25.19800  98.64800  -14.16900 1.000 62.56961  ?  691  ASP   A CA  1 
ATOM   5478  C  C   . ASP   A 1 691  ? -26.38300  99.24900  -14.91000 1.000 51.70420  ?  691  ASP   A C   1 
ATOM   5479  O  O   . ASP   A 1 691  ? -26.85800  98.64200  -15.87500 1.000 49.36200  ?  691  ASP   A O   1 
ATOM   5480  C  CB  . ASP   A 1 691  ? -25.66400  97.41800  -13.38600 1.000 68.35411  ?  691  ASP   A CB  1 
ATOM   5481  C  CG  . ASP   A 1 691  ? -24.64000  96.95300  -12.36600 1.000 83.73741  ?  691  ASP   A CG  1 
ATOM   5482  O  OD1 . ASP   A 1 691  ? -24.66500  97.45800  -11.22300 1.000 79.77388  ?  691  ASP   A OD1 1 
ATOM   5483  O  OD2 . ASP   A 1 691  ? -23.81400  96.07900  -12.70700 1.000 74.28016  -1 691  ASP   A OD2 1 
ATOM   5484  N  N   . TYR   A 1 692  ? -26.87200  100.41200 -14.48500 1.000 54.41147  ?  692  TYR   A N   1 
ATOM   5485  C  CA  . TYR   A 1 692  ? -28.04300  101.00900 -15.11300 1.000 43.78618  ?  692  TYR   A CA  1 
ATOM   5486  C  C   . TYR   A 1 692  ? -27.68400  101.54900 -16.49000 1.000 42.89214  ?  692  TYR   A C   1 
ATOM   5487  O  O   . TYR   A 1 692  ? -26.83900  102.44200 -16.61500 1.000 49.15800  ?  692  TYR   A O   1 
ATOM   5488  C  CB  . TYR   A 1 692  ? -28.61500  102.12600 -14.24500 1.000 39.44468  ?  692  TYR   A CB  1 
ATOM   5489  C  CG  . TYR   A 1 692  ? -29.79600  102.83000 -14.88300 1.000 43.21801  ?  692  TYR   A CG  1 
ATOM   5490  C  CD1 . TYR   A 1 692  ? -31.05000  102.23100 -14.92200 1.000 51.99446  ?  692  TYR   A CD1 1 
ATOM   5491  C  CD2 . TYR   A 1 692  ? -29.65300  104.08200 -15.46700 1.000 42.69124  ?  692  TYR   A CD2 1 
ATOM   5492  C  CE1 . TYR   A 1 692  ? -32.13400  102.86900 -15.51200 1.000 56.55587  ?  692  TYR   A CE1 1 
ATOM   5493  C  CE2 . TYR   A 1 692  ? -30.72900  104.72700 -16.05900 1.000 56.24144  ?  692  TYR   A CE2 1 
ATOM   5494  C  CZ  . TYR   A 1 692  ? -31.96700  104.11800 -16.08000 1.000 64.20203  ?  692  TYR   A CZ  1 
ATOM   5495  O  OH  . TYR   A 1 692  ? -33.03800  104.75900 -16.66900 1.000 41.17685  ?  692  TYR   A OH  1 
ATOM   5496  N  N   . VAL   A 1 693  ? -28.32600  101.00700 -17.51800 1.000 42.11588  ?  693  VAL   A N   1 
ATOM   5497  C  CA  . VAL   A 1 693  ? -28.24700  101.52700 -18.87600 1.000 35.57830  ?  693  VAL   A CA  1 
ATOM   5498  C  C   . VAL   A 1 693  ? -29.63000  102.04700 -19.23700 1.000 41.55992  ?  693  VAL   A C   1 
ATOM   5499  O  O   . VAL   A 1 693  ? -30.60100  101.28000 -19.27400 1.000 34.69152  ?  693  VAL   A O   1 
ATOM   5500  C  CB  . VAL   A 1 693  ? -27.77200  100.45700 -19.87000 1.000 38.58078  ?  693  VAL   A CB  1 
ATOM   5501  C  CG1 . VAL   A 1 693  ? -27.43600  101.08800 -21.21700 1.000 48.17826  ?  693  VAL   A CG1 1 
ATOM   5502  C  CG2 . VAL   A 1 693  ? -26.57600  99.71300  -19.30300 1.000 27.45961  ?  693  VAL   A CG2 1 
ATOM   5503  N  N   . ALA   A 1 694  ? -29.72200  103.34800 -19.48800 1.000 50.68110  ?  694  ALA   A N   1 
ATOM   5504  C  CA  . ALA   A 1 694  ? -31.01300  103.97100 -19.71800 1.000 46.78667  ?  694  ALA   A CA  1 
ATOM   5505  C  C   . ALA   A 1 694  ? -31.59500  103.53400 -21.06100 1.000 47.38964  ?  694  ALA   A C   1 
ATOM   5506  O  O   . ALA   A 1 694  ? -30.85400  103.22800 -22.00000 1.000 46.81748  ?  694  ALA   A O   1 
ATOM   5507  C  CB  . ALA   A 1 694  ? -30.88400  105.49100 -19.67800 1.000 45.48376  ?  694  ALA   A CB  1 
ATOM   5508  N  N   . PRO   A 1 695  ? -32.92300  103.47900 -21.16900 1.000 46.47323  ?  695  PRO   A N   1 
ATOM   5509  C  CA  . PRO   A 1 695  ? -33.55000  103.19400 -22.46800 1.000 41.11445  ?  695  PRO   A CA  1 
ATOM   5510  C  C   . PRO   A 1 695  ? -33.13200  104.21600 -23.51700 1.000 36.83204  ?  695  PRO   A C   1 
ATOM   5511  O  O   . PRO   A 1 695  ? -33.13600  105.42200 -23.26500 1.000 45.34225  ?  695  PRO   A O   1 
ATOM   5512  C  CB  . PRO   A 1 695  ? -35.04900  103.27800 -22.16000 1.000 34.12418  ?  695  PRO   A CB  1 
ATOM   5513  C  CG  . PRO   A 1 695  ? -35.14900  102.96000 -20.70300 1.000 41.59080  ?  695  PRO   A CG  1 
ATOM   5514  C  CD  . PRO   A 1 695  ? -33.90800  103.53100 -20.07400 1.000 36.52858  ?  695  PRO   A CD  1 
ATOM   5515  N  N   . THR   A 1 696  ? -32.78800  103.72500 -24.71100 1.000 43.26066  ?  696  THR   A N   1 
ATOM   5516  C  CA  . THR   A 1 696  ? -32.23800  104.57300 -25.76500 1.000 49.55418  ?  696  THR   A CA  1 
ATOM   5517  C  C   . THR   A 1 696  ? -33.19700  104.86100 -26.91800 1.000 43.83985  ?  696  THR   A C   1 
ATOM   5518  O  O   . THR   A 1 696  ? -32.83100  105.60800 -27.83400 1.000 58.49534  ?  696  THR   A O   1 
ATOM   5519  C  CB  . THR   A 1 696  ? -30.94800  103.95100 -26.31700 1.000 42.89971  ?  696  THR   A CB  1 
ATOM   5520  O  OG1 . THR   A 1 696  ? -31.23000  102.66000 -26.87200 1.000 60.78371  ?  696  THR   A OG1 1 
ATOM   5521  C  CG2 . THR   A 1 696  ? -29.91700  103.80200 -25.20400 1.000 44.50276  ?  696  THR   A CG2 1 
ATOM   5522  N  N   . ASP   A 1 697  ? -34.42400  104.35600 -26.86400 1.000 37.77843  ?  697  ASP   A N   1 
ATOM   5523  C  CA  . ASP   A 1 697  ? -35.40900  104.54700 -27.91000 1.000 45.23909  ?  697  ASP   A CA  1 
ATOM   5524  C  C   . ASP   A 1 697  ? -36.78900  104.43400 -27.29700 1.000 52.34105  ?  697  ASP   A C   1 
ATOM   5525  O  O   . ASP   A 1 697  ? -36.93800  104.17900 -26.09900 1.000 55.18421  ?  697  ASP   A O   1 
ATOM   5526  C  CB  . ASP   A 1 697  ? -35.17800  103.49300 -28.97200 1.000 39.00438  ?  697  ASP   A CB  1 
ATOM   5527  C  CG  . ASP   A 1 697  ? -35.40600  102.11200 -28.43400 1.000 60.33653  ?  697  ASP   A CG  1 
ATOM   5528  O  OD1 . ASP   A 1 697  ? -36.57700  101.75700 -28.17900 1.000 66.83818  ?  697  ASP   A OD1 1 
ATOM   5529  O  OD2 . ASP   A 1 697  ? -34.41900  101.33800 -28.41500 1.000 75.28431  -1 697  ASP   A OD2 1 
ATOM   5530  N  N   . GLU   A 1 698  ? -37.80800  104.50200 -28.15000 1.000 42.91141  ?  698  GLU   A N   1 
ATOM   5531  C  CA  . GLU   A 1 698  ? -39.16500  104.53300 -27.62900 1.000 41.68527  ?  698  GLU   A CA  1 
ATOM   5532  C  C   . GLU   A 1 698  ? -39.63600  103.15100 -27.19400 1.000 37.53986  ?  698  GLU   A C   1 
ATOM   5533  O  O   . GLU   A 1 698  ? -40.40100  103.04100 -26.23000 1.000 44.38049  ?  698  GLU   A O   1 
ATOM   5534  C  CB  . GLU   A 1 698  ? -40.10800  105.13500 -28.67100 1.000 40.77024  ?  698  GLU   A CB  1 
ATOM   5535  C  CG  . GLU   A 1 698  ? -40.39500  104.24200 -29.86800 1.000 53.93980  ?  698  GLU   A CG  1 
ATOM   5536  C  CD  . GLU   A 1 698  ? -39.35500  104.35500 -30.97100 1.000 63.72242  ?  698  GLU   A CD  1 
ATOM   5537  O  OE1 . GLU   A 1 698  ? -38.28300  104.95100 -30.73300 1.000 60.31393  ?  698  GLU   A OE1 1 
ATOM   5538  O  OE2 . GLU   A 1 698  ? -39.61300  103.84000 -32.08000 1.000 85.92161  -1 698  GLU   A OE2 1 
ATOM   5539  N  N   . LEU   A 1 699  ? -39.18700  102.09200 -27.87100 1.000 39.05554  ?  699  LEU   A N   1 
ATOM   5540  C  CA  . LEU   A 1 699  ? -39.61700  100.74800 -27.49900 1.000 43.68734  ?  699  LEU   A CA  1 
ATOM   5541  C  C   . LEU   A 1 699  ? -38.95300  100.30100 -26.20400 1.000 40.12329  ?  699  LEU   A C   1 
ATOM   5542  O  O   . LEU   A 1 699  ? -39.60000  99.68700  -25.34700 1.000 35.69307  ?  699  LEU   A O   1 
ATOM   5543  C  CB  . LEU   A 1 699  ? -39.31600  99.76900  -28.63400 1.000 38.92255  ?  699  LEU   A CB  1 
ATOM   5544  C  CG  . LEU   A 1 699  ? -39.73600  98.31100  -28.43500 1.000 45.65328  ?  699  LEU   A CG  1 
ATOM   5545  C  CD1 . LEU   A 1 699  ? -41.20800  98.21800  -28.07100 1.000 35.32082  ?  699  LEU   A CD1 1 
ATOM   5546  C  CD2 . LEU   A 1 699  ? -39.44400  97.49800  -29.68600 1.000 38.22324  ?  699  LEU   A CD2 1 
ATOM   5547  N  N   . GLU   A 1 700  ? -37.66200  100.60200 -26.04200 1.000 41.58858  ?  700  GLU   A N   1 
ATOM   5548  C  CA  . GLU   A 1 700  ? -36.98600  100.27600 -24.79300 1.000 46.08799  ?  700  GLU   A CA  1 
ATOM   5549  C  C   . GLU   A 1 700  ? -37.62700  100.99600 -23.61500 1.000 45.67321  ?  700  GLU   A C   1 
ATOM   5550  O  O   . GLU   A 1 700  ? -37.69800  100.44100 -22.51300 1.000 50.50153  ?  700  GLU   A O   1 
ATOM   5551  C  CB  . GLU   A 1 700  ? -35.49800  100.61600 -24.89500 1.000 37.54941  ?  700  GLU   A CB  1 
ATOM   5552  C  CG  . GLU   A 1 700  ? -34.69500  99.62100  -25.72700 1.000 36.76814  ?  700  GLU   A CG  1 
ATOM   5553  C  CD  . GLU   A 1 700  ? -33.25200  100.05300 -25.93100 1.000 48.62967  ?  700  GLU   A CD  1 
ATOM   5554  O  OE1 . GLU   A 1 700  ? -32.91500  101.19800 -25.56800 1.000 50.11010  ?  700  GLU   A OE1 1 
ATOM   5555  O  OE2 . GLU   A 1 700  ? -32.45100  99.24500  -26.44600 1.000 56.12460  -1 700  GLU   A OE2 1 
ATOM   5556  N  N   . GLN   A 1 701  ? -38.11500  102.22100 -23.83200 1.000 44.98030  ?  701  GLN   A N   1 
ATOM   5557  C  CA  . GLN   A 1 701  ? -38.84000  102.92700 -22.78200 1.000 41.24414  ?  701  GLN   A CA  1 
ATOM   5558  C  C   . GLN   A 1 701  ? -40.20400  102.29400 -22.53400 1.000 39.71837  ?  701  GLN   A C   1 
ATOM   5559  O  O   . GLN   A 1 701  ? -40.60700  102.10800 -21.38000 1.000 46.93451  ?  701  GLN   A O   1 
ATOM   5560  C  CB  . GLN   A 1 701  ? -38.99400  104.40200 -23.15200 1.000 45.37681  ?  701  GLN   A CB  1 
ATOM   5561  C  CG  . GLN   A 1 701  ? -39.77400  105.21700 -22.13000 1.000 47.74131  ?  701  GLN   A CG  1 
ATOM   5562  C  CD  . GLN   A 1 701  ? -38.87800  105.86700 -21.09400 1.000 62.19263  ?  701  GLN   A CD  1 
ATOM   5563  O  OE1 . GLN   A 1 701  ? -38.61400  105.29600 -20.03500 1.000 62.25432  ?  701  GLN   A OE1 1 
ATOM   5564  N  NE2 . GLN   A 1 701  ? -38.40400  107.07000 -21.39600 1.000 70.06931  ?  701  GLN   A NE2 1 
ATOM   5565  N  N   . GLN   A 1 702  ? -40.92700  101.96400 -23.60500 1.000 39.63071  ?  702  GLN   A N   1 
ATOM   5566  C  CA  . GLN   A 1 702  ? -42.21900  101.30300 -23.45700 1.000 45.10225  ?  702  GLN   A CA  1 
ATOM   5567  C  C   . GLN   A 1 702  ? -42.07800  99.96800  -22.73700 1.000 44.95235  ?  702  GLN   A C   1 
ATOM   5568  O  O   . GLN   A 1 702  ? -42.90000  99.62600  -21.87800 1.000 41.57982  ?  702  GLN   A O   1 
ATOM   5569  C  CB  . GLN   A 1 702  ? -42.85800  101.10800 -24.83000 1.000 39.85039  ?  702  GLN   A CB  1 
ATOM   5570  C  CG  . GLN   A 1 702  ? -44.36100  101.27300 -24.85000 1.000 48.67119  ?  702  GLN   A CG  1 
ATOM   5571  C  CD  . GLN   A 1 702  ? -44.91500  101.24500 -26.25600 1.000 62.84074  ?  702  GLN   A CD  1 
ATOM   5572  O  OE1 . GLN   A 1 702  ? -44.38000  100.56500 -27.13200 1.000 62.88554  ?  702  GLN   A OE1 1 
ATOM   5573  N  NE2 . GLN   A 1 702  ? -45.99000  101.99000 -26.48400 1.000 95.23467  ?  702  GLN   A NE2 1 
ATOM   5574  N  N   . LEU   A 1 703  ? -41.03900  99.20000  -23.07500 1.000 41.67798  ?  703  LEU   A N   1 
ATOM   5575  C  CA  . LEU   A 1 703  ? -40.80600  97.93300  -22.39100 1.000 37.03890  ?  703  LEU   A CA  1 
ATOM   5576  C  C   . LEU   A 1 703  ? -40.37500  98.15900  -20.94800 1.000 40.95336  ?  703  LEU   A C   1 
ATOM   5577  O  O   . LEU   A 1 703  ? -40.76100  97.39700  -20.05300 1.000 42.69578  ?  703  LEU   A O   1 
ATOM   5578  C  CB  . LEU   A 1 703  ? -39.75400  97.12000  -23.14500 1.000 39.88878  ?  703  LEU   A CB  1 
ATOM   5579  C  CG  . LEU   A 1 703  ? -40.21700  96.42800  -24.42700 1.000 36.20928  ?  703  LEU   A CG  1 
ATOM   5580  C  CD1 . LEU   A 1 703  ? -39.03100  96.20900  -25.34900 1.000 35.89456  ?  703  LEU   A CD1 1 
ATOM   5581  C  CD2 . LEU   A 1 703  ? -40.90900  95.10800  -24.11500 1.000 49.60857  ?  703  LEU   A CD2 1 
ATOM   5582  N  N   . ALA   A 1 704  ? -39.58100  99.20500  -20.70200 1.000 35.09368  ?  704  ALA   A N   1 
ATOM   5583  C  CA  . ALA   A 1 704  ? -39.13600  99.49200  -19.34200 1.000 38.42659  ?  704  ALA   A CA  1 
ATOM   5584  C  C   . ALA   A 1 704  ? -40.29600  99.89600  -18.44100 1.000 41.38914  ?  704  ALA   A C   1 
ATOM   5585  O  O   . ALA   A 1 704  ? -40.27000  99.61300  -17.23900 1.000 51.55194  ?  704  ALA   A O   1 
ATOM   5586  C  CB  . ALA   A 1 704  ? -38.06800  100.58500 -19.35700 1.000 35.81618  ?  704  ALA   A CB  1 
ATOM   5587  N  N   . GLN   A 1 705  ? -41.31400  100.55600 -18.99300 1.000 44.51929  ?  705  GLN   A N   1 
ATOM   5588  C  CA  . GLN   A 1 705  ? -42.47500  100.91000 -18.18500 1.000 33.95530  ?  705  GLN   A CA  1 
ATOM   5589  C  C   . GLN   A 1 705  ? -43.32400  99.68400  -17.88300 1.000 40.26831  ?  705  GLN   A C   1 
ATOM   5590  O  O   . GLN   A 1 705  ? -43.81600  99.52400  -16.76000 1.000 49.48317  ?  705  GLN   A O   1 
ATOM   5591  C  CB  . GLN   A 1 705  ? -43.30300  101.98100 -18.89200 1.000 35.31513  ?  705  GLN   A CB  1 
ATOM   5592  C  CG  . GLN   A 1 705  ? -42.59600  103.32200 -19.00500 1.000 63.61626  ?  705  GLN   A CG  1 
ATOM   5593  C  CD  . GLN   A 1 705  ? -43.35700  104.31200 -19.86300 1.000 72.37878  ?  705  GLN   A CD  1 
ATOM   5594  O  OE1 . GLN   A 1 705  ? -44.49300  104.05700 -20.26700 1.000 76.63172  ?  705  GLN   A OE1 1 
ATOM   5595  N  NE2 . GLN   A 1 705  ? -42.73200  105.44800 -20.15200 1.000 50.78514  ?  705  GLN   A NE2 1 
ATOM   5596  N  N   . VAL   A 1 706  ? -43.50800  98.80800  -18.87300 1.000 40.84436  ?  706  VAL   A N   1 
ATOM   5597  C  CA  . VAL   A 1 706  ? -44.24400  97.56900  -18.63700 1.000 34.73524  ?  706  VAL   A CA  1 
ATOM   5598  C  C   . VAL   A 1 706  ? -43.52400  96.71900  -17.60100 1.000 38.08217  ?  706  VAL   A C   1 
ATOM   5599  O  O   . VAL   A 1 706  ? -44.14900  96.14300  -16.70200 1.000 35.88034  ?  706  VAL   A O   1 
ATOM   5600  C  CB  . VAL   A 1 706  ? -44.44000  96.80400  -19.95600 1.000 27.70416  ?  706  VAL   A CB  1 
ATOM   5601  C  CG1 . VAL   A 1 706  ? -45.00000  95.42400  -19.68300 1.000 42.38187  ?  706  VAL   A CG1 1 
ATOM   5602  C  CG2 . VAL   A 1 706  ? -45.35700  97.58000  -20.87600 1.000 31.61042  ?  706  VAL   A CG2 1 
ATOM   5603  N  N   . TRP   A 1 707  ? -42.19700  96.63200  -17.71100 1.000 45.74521  ?  707  TRP   A N   1 
ATOM   5604  C  CA  . TRP   A 1 707  ? -41.41500  95.92500  -16.70500 1.000 36.74087  ?  707  TRP   A CA  1 
ATOM   5605  C  C   . TRP   A 1 707  ? -41.58300  96.56600  -15.33400 1.000 39.25585  ?  707  TRP   A C   1 
ATOM   5606  O  O   . TRP   A 1 707  ? -41.66200  95.86600  -14.31800 1.000 48.06897  ?  707  TRP   A O   1 
ATOM   5607  C  CB  . TRP   A 1 707  ? -39.94100  95.89800  -17.11300 1.000 33.48828  ?  707  TRP   A CB  1 
ATOM   5608  C  CG  . TRP   A 1 707  ? -39.60300  94.81900  -18.09400 1.000 39.78511  ?  707  TRP   A CG  1 
ATOM   5609  C  CD1 . TRP   A 1 707  ? -40.36900  94.38900  -19.14000 1.000 43.39322  ?  707  TRP   A CD1 1 
ATOM   5610  C  CD2 . TRP   A 1 707  ? -38.41300  94.02300  -18.11500 1.000 32.80556  ?  707  TRP   A CD2 1 
ATOM   5611  N  NE1 . TRP   A 1 707  ? -39.72600  93.37600  -19.81400 1.000 32.09514  ?  707  TRP   A NE1 1 
ATOM   5612  C  CE2 . TRP   A 1 707  ? -38.52300  93.13300  -19.20300 1.000 42.06176  ?  707  TRP   A CE2 1 
ATOM   5613  C  CE3 . TRP   A 1 707  ? -37.26500  93.97700  -17.31900 1.000 32.73871  ?  707  TRP   A CE3 1 
ATOM   5614  C  CZ2 . TRP   A 1 707  ? -37.52800  92.20800  -19.51500 1.000 37.39443  ?  707  TRP   A CZ2 1 
ATOM   5615  C  CZ3 . TRP   A 1 707  ? -36.27800  93.05800  -17.63200 1.000 37.55256  ?  707  TRP   A CZ3 1 
ATOM   5616  C  CH2 . TRP   A 1 707  ? -36.41500  92.18700  -18.71900 1.000 36.28539  ?  707  TRP   A CH2 1 
ATOM   5617  N  N   . SER   A 1 708  ? -41.64500  97.89800  -15.28600 1.000 34.99371  ?  708  SER   A N   1 
ATOM   5618  C  CA  . SER   A 1 708  ? -41.84200  98.57600  -14.01000 1.000 30.09042  ?  708  SER   A CA  1 
ATOM   5619  C  C   . SER   A 1 708  ? -43.20800  98.25400  -13.42700 1.000 39.21729  ?  708  SER   A C   1 
ATOM   5620  O  O   . SER   A 1 708  ? -43.34700  98.07600  -12.21200 1.000 50.47246  ?  708  SER   A O   1 
ATOM   5621  C  CB  . SER   A 1 708  ? -41.67500  100.08400 -14.18500 1.000 35.47508  ?  708  SER   A CB  1 
ATOM   5622  O  OG  . SER   A 1 708  ? -40.35100  100.40400 -14.57700 1.000 60.88963  ?  708  SER   A OG  1 
ATOM   5623  N  N   . HIS   A 1 709  ? -44.22800  98.16000  -14.28300 1.000 37.21449  ?  709  HIS   A N   1 
ATOM   5624  C  CA  . HIS   A 1 709  ? -45.57600  97.87900  -13.80300 1.000 27.58999  ?  709  HIS   A CA  1 
ATOM   5625  C  C   . HIS   A 1 709  ? -45.68800  96.45600  -13.27400 1.000 36.04349  ?  709  HIS   A C   1 
ATOM   5626  O  O   . HIS   A 1 709  ? -46.31300  96.22000  -12.23400 1.000 59.18532  ?  709  HIS   A O   1 
ATOM   5627  C  CB  . HIS   A 1 709  ? -46.58600  98.12800  -14.92400 1.000 36.48495  ?  709  HIS   A CB  1 
ATOM   5628  C  CG  . HIS   A 1 709  ? -47.96200  97.61400  -14.63000 1.000 52.39550  ?  709  HIS   A CG  1 
ATOM   5629  N  ND1 . HIS   A 1 709  ? -49.00900  98.44500  -14.29300 1.000 48.84378  ?  709  HIS   A ND1 1 
ATOM   5630  C  CD2 . HIS   A 1 709  ? -48.47000  96.35800  -14.64500 1.000 63.14552  ?  709  HIS   A CD2 1 
ATOM   5631  C  CE1 . HIS   A 1 709  ? -50.09700  97.72200  -14.09700 1.000 58.56850  ?  709  HIS   A CE1 1 
ATOM   5632  N  NE2 . HIS   A 1 709  ? -49.79700  96.45200  -14.30400 1.000 69.34182  ?  709  HIS   A NE2 1 
ATOM   5633  N  N   . VAL   A 1 710  ? -45.08200  95.49600  -13.96900 1.000 35.28979  ?  710  VAL   A N   1 
ATOM   5634  C  CA  . VAL   A 1 710  ? -45.24000  94.09700  -13.58900 1.000 40.24681  ?  710  VAL   A CA  1 
ATOM   5635  C  C   . VAL   A 1 710  ? -44.35000  93.74800  -12.40100 1.000 41.42176  ?  710  VAL   A C   1 
ATOM   5636  O  O   . VAL   A 1 710  ? -44.75600  92.99700  -11.50700 1.000 51.92048  ?  710  VAL   A O   1 
ATOM   5637  C  CB  . VAL   A 1 710  ? -44.95700  93.20000  -14.80700 1.000 40.26836  ?  710  VAL   A CB  1 
ATOM   5638  C  CG1 . VAL   A 1 710  ? -44.73300  91.76100  -14.38100 1.000 56.05731  ?  710  VAL   A CG1 1 
ATOM   5639  C  CG2 . VAL   A 1 710  ? -46.09900  93.29700  -15.80400 1.000 35.13403  ?  710  VAL   A CG2 1 
ATOM   5640  N  N   . LEU   A 1 711  ? -43.13400  94.29100  -12.36000 1.000 35.05528  ?  711  LEU   A N   1 
ATOM   5641  C  CA  . LEU   A 1 711  ? -42.17900  93.94000  -11.31700 1.000 34.43648  ?  711  LEU   A CA  1 
ATOM   5642  C  C   . LEU   A 1 711  ? -42.18600  94.90900  -10.14400 1.000 34.93724  ?  711  LEU   A C   1 
ATOM   5643  O  O   . LEU   A 1 711  ? -41.70400  94.55200  -9.06400  1.000 41.63059  ?  711  LEU   A O   1 
ATOM   5644  C  CB  . LEU   A 1 711  ? -40.76700  93.85900  -11.90700 1.000 39.40555  ?  711  LEU   A CB  1 
ATOM   5645  C  CG  . LEU   A 1 711  ? -40.52700  92.74300  -12.92800 1.000 43.78115  ?  711  LEU   A CG  1 
ATOM   5646  C  CD1 . LEU   A 1 711  ? -39.07200  92.71000  -13.36800 1.000 27.35218  ?  711  LEU   A CD1 1 
ATOM   5647  C  CD2 . LEU   A 1 711  ? -40.95000  91.39000  -12.35800 1.000 39.87426  ?  711  LEU   A CD2 1 
ATOM   5648  N  N   . GLY   A 1 712  ? -42.70900  96.11800  -10.32400 1.000 41.24225  ?  712  GLY   A N   1 
ATOM   5649  C  CA  . GLY   A 1 712  ? -42.77400  97.06900  -9.23200  1.000 37.71970  ?  712  GLY   A CA  1 
ATOM   5650  C  C   . GLY   A 1 712  ? -41.50200  97.84000  -8.96600  1.000 36.94567  ?  712  GLY   A C   1 
ATOM   5651  O  O   . GLY   A 1 712  ? -41.36200  98.42200  -7.88800  1.000 53.60779  ?  712  GLY   A O   1 
ATOM   5652  N  N   . ILE   A 1 713  ? -40.57500  97.86900  -9.91000  1.000 44.36598  ?  713  ILE   A N   1 
ATOM   5653  C  CA  . ILE   A 1 713  ? -39.28900  98.54000  -9.73600  1.000 56.27785  ?  713  ILE   A CA  1 
ATOM   5654  C  C   . ILE   A 1 713  ? -39.33800  99.85400  -10.50900 1.000 53.49435  ?  713  ILE   A C   1 
ATOM   5655  O  O   . ILE   A 1 713  ? -39.80500  99.86300  -11.65600 1.000 50.03383  ?  713  ILE   A O   1 
ATOM   5656  C  CB  . ILE   A 1 713  ? -38.12500  97.65000  -10.21600 1.000 38.56227  ?  713  ILE   A CB  1 
ATOM   5657  C  CG1 . ILE   A 1 713  ? -37.96300  96.43500  -9.29500  1.000 44.78198  ?  713  ILE   A CG1 1 
ATOM   5658  C  CG2 . ILE   A 1 713  ? -36.82500  98.43300  -10.29400 1.000 41.65528  ?  713  ILE   A CG2 1 
ATOM   5659  C  CD1 . ILE   A 1 713  ? -37.48200  95.19600  -10.01300 1.000 45.69517  ?  713  ILE   A CD1 1 
ATOM   5660  N  N   . PRO   A 1 714  ? -38.90100  100.97000 -9.93000  1.000 52.55803  ?  714  PRO   A N   1 
ATOM   5661  C  CA  . PRO   A 1 714  ? -38.88100  102.22200 -10.68600 1.000 42.24618  ?  714  PRO   A CA  1 
ATOM   5662  C  C   . PRO   A 1 714  ? -37.60900  102.38300 -11.52100 1.000 52.04610  ?  714  PRO   A C   1 
ATOM   5663  O  O   . PRO   A 1 714  ? -36.49300  102.07400 -11.08300 1.000 61.67943  ?  714  PRO   A O   1 
ATOM   5664  C  CB  . PRO   A 1 714  ? -38.98200  103.28400 -9.57900  1.000 44.43687  ?  714  PRO   A CB  1 
ATOM   5665  C  CG  . PRO   A 1 714  ? -38.45900  102.58400 -8.30800  1.000 61.99664  ?  714  PRO   A CG  1 
ATOM   5666  C  CD  . PRO   A 1 714  ? -38.16100  101.14400 -8.66700  1.000 70.17951  ?  714  PRO   A CD  1 
ATOM   5667  N  N   . GLN   A 1 715  ? -37.79400  102.87600 -12.74600 1.000 39.12377  ?  715  GLN   A N   1 
ATOM   5668  C  CA  . GLN   A 1 715  ? -36.67600  103.15200 -13.63900 1.000 47.59325  ?  715  GLN   A CA  1 
ATOM   5669  C  C   . GLN   A 1 715  ? -35.85100  101.89900 -13.89600 1.000 47.71134  ?  715  GLN   A C   1 
ATOM   5670  O  O   . GLN   A 1 715  ? -34.78200  101.71800 -13.30300 1.000 58.96269  ?  715  GLN   A O   1 
ATOM   5671  C  CB  . GLN   A 1 715  ? -35.78400  104.25400 -13.06100 1.000 55.55004  ?  715  GLN   A CB  1 
ATOM   5672  C  CG  . GLN   A 1 715  ? -36.09600  105.64400 -13.55700 1.000 53.39495  ?  715  GLN   A CG  1 
ATOM   5673  C  CD  . GLN   A 1 715  ? -35.39000  106.71600 -12.75600 1.000 68.27934  ?  715  GLN   A CD  1 
ATOM   5674  O  OE1 . GLN   A 1 715  ? -35.50800  106.76800 -11.53100 1.000 81.58066  ?  715  GLN   A OE1 1 
ATOM   5675  N  NE2 . GLN   A 1 715  ? -34.65200  107.58200 -13.44300 1.000 72.32870  ?  715  GLN   A NE2 1 
ATOM   5676  N  N   . MET   A 1 716  ? -36.34000  101.02600 -14.76500 1.000 49.43781  ?  716  MET   A N   1 
ATOM   5677  C  CA  . MET   A 1 716  ? -35.60800  99.81600  -15.09600 1.000 39.84196  ?  716  MET   A CA  1 
ATOM   5678  C  C   . MET   A 1 716  ? -34.53700  100.11300 -16.14000 1.000 43.55732  ?  716  MET   A C   1 
ATOM   5679  O  O   . MET   A 1 716  ? -34.65400  101.05500 -16.92800 1.000 45.34548  ?  716  MET   A O   1 
ATOM   5680  C  CB  . MET   A 1 716  ? -36.56700  98.73800  -15.60100 1.000 43.75613  ?  716  MET   A CB  1 
ATOM   5681  C  CG  . MET   A 1 716  ? -36.17700  97.33000  -15.19100 1.000 43.04796  ?  716  MET   A CG  1 
ATOM   5682  S  SD  . MET   A 1 716  ? -36.79200  96.87100  -13.56100 1.000 56.75086  ?  716  MET   A SD  1 
ATOM   5683  C  CE  . MET   A 1 716  ? -38.44800  96.32900  -13.95400 1.000 44.66932  ?  716  MET   A CE  1 
ATOM   5684  N  N   . GLY   A 1 717  ? -33.47000  99.31000  -16.12300 1.000 44.71585  ?  717  GLY   A N   1 
ATOM   5685  C  CA  . GLY   A 1 717  ? -32.42200  99.40700  -17.11500 1.000 30.57184  ?  717  GLY   A CA  1 
ATOM   5686  C  C   . GLY   A 1 717  ? -32.59500  98.38000  -18.22000 1.000 45.13646  ?  717  GLY   A C   1 
ATOM   5687  O  O   . GLY   A 1 717  ? -33.21600  97.33600  -18.03500 1.000 53.12328  ?  717  GLY   A O   1 
ATOM   5688  N  N   . ILE   A 1 718  ? -32.02000  98.67400  -19.39200 1.000 41.38111  ?  718  ILE   A N   1 
ATOM   5689  C  CA  . ILE   A 1 718  ? -32.14700  97.74600  -20.51600 1.000 48.08168  ?  718  ILE   A CA  1 
ATOM   5690  C  C   . ILE   A 1 718  ? -31.31400  96.48700  -20.34700 1.000 41.53270  ?  718  ILE   A C   1 
ATOM   5691  O  O   . ILE   A 1 718  ? -31.35700  95.61100  -21.22100 1.000 45.74524  ?  718  ILE   A O   1 
ATOM   5692  C  CB  . ILE   A 1 718  ? -31.78800  98.43300  -21.84800 1.000 43.11054  ?  718  ILE   A CB  1 
ATOM   5693  C  CG1 . ILE   A 1 718  ? -30.30300  98.77600  -21.90700 1.000 35.86045  ?  718  ILE   A CG1 1 
ATOM   5694  C  CG2 . ILE   A 1 718  ? -32.59600  99.67800  -22.01300 1.000 44.88959  ?  718  ILE   A CG2 1 
ATOM   5695  C  CD1 . ILE   A 1 718  ? -29.87300  99.28600  -23.26900 1.000 43.12125  ?  718  ILE   A CD1 1 
ATOM   5696  N  N   . ASP   A 1 719  ? -30.55100  96.36200  -19.25700 1.000 42.73523  ?  719  ASP   A N   1 
ATOM   5697  C  CA  . ASP   A 1 719  ? -29.77100  95.16000  -18.97100 1.000 35.13809  ?  719  ASP   A CA  1 
ATOM   5698  C  C   . ASP   A 1 719  ? -30.24000  94.42700  -17.72200 1.000 42.16165  ?  719  ASP   A C   1 
ATOM   5699  O  O   . ASP   A 1 719  ? -29.65200  93.39900  -17.36000 1.000 49.24926  ?  719  ASP   A O   1 
ATOM   5700  C  CB  . ASP   A 1 719  ? -28.28300  95.50200  -18.82500 1.000 38.75021  ?  719  ASP   A CB  1 
ATOM   5701  C  CG  . ASP   A 1 719  ? -27.64300  95.89200  -20.14100 1.000 50.31273  ?  719  ASP   A CG  1 
ATOM   5702  O  OD1 . ASP   A 1 719  ? -28.31100  95.75700  -21.18800 1.000 49.00919  ?  719  ASP   A OD1 1 
ATOM   5703  O  OD2 . ASP   A 1 719  ? -26.48400  96.36200  -20.12500 1.000 53.88011  -1 719  ASP   A OD2 1 
ATOM   5704  N  N   . ASP   A 1 720  ? -31.26900  94.93600  -17.05000 1.000 50.14668  ?  720  ASP   A N   1 
ATOM   5705  C  CA  . ASP   A 1 720  ? -31.81700  94.26000  -15.88500 1.000 27.20129  ?  720  ASP   A CA  1 
ATOM   5706  C  C   . ASP   A 1 720  ? -32.45100  92.94000  -16.29900 1.000 36.87701  ?  720  ASP   A C   1 
ATOM   5707  O  O   . ASP   A 1 720  ? -33.16600  92.86000  -17.30300 1.000 45.71214  ?  720  ASP   A O   1 
ATOM   5708  C  CB  . ASP   A 1 720  ? -32.84500  95.14800  -15.18500 1.000 38.53439  ?  720  ASP   A CB  1 
ATOM   5709  C  CG  . ASP   A 1 720  ? -32.26300  96.47600  -14.73500 1.000 38.62541  ?  720  ASP   A CG  1 
ATOM   5710  O  OD1 . ASP   A 1 720  ? -31.08700  96.74500  -15.05100 1.000 55.85557  ?  720  ASP   A OD1 1 
ATOM   5711  O  OD2 . ASP   A 1 720  ? -32.97700  97.24800  -14.05800 1.000 46.76462  -1 720  ASP   A OD2 1 
ATOM   5712  N  N   . HIS   A 1 721  ? -32.17400  91.90000  -15.52100 1.000 30.21529  ?  721  HIS   A N   1 
ATOM   5713  C  CA  . HIS   A 1 721  ? -32.64700  90.55600  -15.81300 1.000 27.27096  ?  721  HIS   A CA  1 
ATOM   5714  C  C   . HIS   A 1 721  ? -33.98700  90.32200  -15.12600 1.000 31.76464  ?  721  HIS   A C   1 
ATOM   5715  O  O   . HIS   A 1 721  ? -34.11100  90.51900  -13.91300 1.000 33.72585  ?  721  HIS   A O   1 
ATOM   5716  C  CB  . HIS   A 1 721  ? -31.61000  89.53500  -15.35000 1.000 25.84510  ?  721  HIS   A CB  1 
ATOM   5717  C  CG  . HIS   A 1 721  ? -31.87400  88.13900  -15.81500 1.000 28.99797  ?  721  HIS   A CG  1 
ATOM   5718  N  ND1 . HIS   A 1 721  ? -32.74900  87.29200  -15.16900 1.000 43.33468  ?  721  HIS   A ND1 1 
ATOM   5719  C  CD2 . HIS   A 1 721  ? -31.36000  87.43200  -16.84800 1.000 36.80274  ?  721  HIS   A CD2 1 
ATOM   5720  C  CE1 . HIS   A 1 721  ? -32.77200  86.12700  -15.79100 1.000 39.24764  ?  721  HIS   A CE1 1 
ATOM   5721  N  NE2 . HIS   A 1 721  ? -31.93600  86.18500  -16.81300 1.000 37.69162  ?  721  HIS   A NE2 1 
ATOM   5722  N  N   . PHE   A 1 722  ? -34.98600  89.90100  -15.90900 1.000 28.59468  ?  722  PHE   A N   1 
ATOM   5723  C  CA  . PHE   A 1 722  ? -36.34000  89.71400  -15.39100 1.000 26.67628  ?  722  PHE   A CA  1 
ATOM   5724  C  C   . PHE   A 1 722  ? -36.35500  88.79900  -14.17100 1.000 31.94603  ?  722  PHE   A C   1 
ATOM   5725  O  O   . PHE   A 1 722  ? -36.84600  89.17300  -13.10100 1.000 32.92542  ?  722  PHE   A O   1 
ATOM   5726  C  CB  . PHE   A 1 722  ? -37.23900  89.15300  -16.49400 1.000 22.68987  ?  722  PHE   A CB  1 
ATOM   5727  C  CG  . PHE   A 1 722  ? -38.70100  89.41600  -16.28100 1.000 27.42459  ?  722  PHE   A CG  1 
ATOM   5728  C  CD1 . PHE   A 1 722  ? -39.22400  90.68400  -16.47700 1.000 26.24183  ?  722  PHE   A CD1 1 
ATOM   5729  C  CD2 . PHE   A 1 722  ? -39.55700  88.39200  -15.90800 1.000 29.87372  ?  722  PHE   A CD2 1 
ATOM   5730  C  CE1 . PHE   A 1 722  ? -40.56900  90.92900  -16.29200 1.000 31.53779  ?  722  PHE   A CE1 1 
ATOM   5731  C  CE2 . PHE   A 1 722  ? -40.90800  88.63100  -15.72200 1.000 29.34363  ?  722  PHE   A CE2 1 
ATOM   5732  C  CZ  . PHE   A 1 722  ? -41.41400  89.90100  -15.91400 1.000 37.28988  ?  722  PHE   A CZ  1 
ATOM   5733  N  N   . LEU   A 1 723  ? -35.81000  87.58900  -14.31700 1.000 28.53063  ?  723  LEU   A N   1 
ATOM   5734  C  CA  . LEU   A 1 723  ? -35.84200  86.63300  -13.21600 1.000 31.00992  ?  723  LEU   A CA  1 
ATOM   5735  C  C   . LEU   A 1 723  ? -34.98200  87.08500  -12.04100 1.000 33.78539  ?  723  LEU   A C   1 
ATOM   5736  O  O   . LEU   A 1 723  ? -35.27100  86.72600  -10.89400 1.000 39.78775  ?  723  LEU   A O   1 
ATOM   5737  C  CB  . LEU   A 1 723  ? -35.39900  85.25600  -13.70400 1.000 28.63897  ?  723  LEU   A CB  1 
ATOM   5738  C  CG  . LEU   A 1 723  ? -36.21900  84.71500  -14.87500 1.000 28.10185  ?  723  LEU   A CG  1 
ATOM   5739  C  CD1 . LEU   A 1 723  ? -35.69800  83.35900  -15.30700 1.000 36.79695  ?  723  LEU   A CD1 1 
ATOM   5740  C  CD2 . LEU   A 1 723  ? -37.69200  84.63600  -14.50800 1.000 26.42751  ?  723  LEU   A CD2 1 
ATOM   5741  N  N   . GLU   A 1 724  ? -33.93400  87.87300  -12.29900 1.000 33.54449  ?  724  GLU   A N   1 
ATOM   5742  C  CA  . GLU   A 1 724  ? -33.08000  88.35200  -11.21600 1.000 39.48211  ?  724  GLU   A CA  1 
ATOM   5743  C  C   . GLU   A 1 724  ? -33.74400  89.43900  -10.38200 1.000 38.83154  ?  724  GLU   A C   1 
ATOM   5744  O  O   . GLU   A 1 724  ? -33.38600  89.60900  -9.21100  1.000 45.80944  ?  724  GLU   A O   1 
ATOM   5745  C  CB  . GLU   A 1 724  ? -31.75800  88.88000  -11.77200 1.000 25.17933  ?  724  GLU   A CB  1 
ATOM   5746  C  CG  . GLU   A 1 724  ? -30.84300  87.80200  -12.31500 1.000 44.57542  ?  724  GLU   A CG  1 
ATOM   5747  C  CD  . GLU   A 1 724  ? -29.50300  88.35300  -12.74900 1.000 51.84804  ?  724  GLU   A CD  1 
ATOM   5748  O  OE1 . GLU   A 1 724  ? -29.18400  89.49700  -12.36300 1.000 42.40329  ?  724  GLU   A OE1 1 
ATOM   5749  O  OE2 . GLU   A 1 724  ? -28.77300  87.64900  -13.48100 1.000 56.98859  -1 724  GLU   A OE2 1 
ATOM   5750  N  N   . ARG   A 1 725  ? -34.70000  90.17200  -10.95000 1.000 33.83965  ?  725  ARG   A N   1 
ATOM   5751  C  CA  . ARG   A 1 725  ? -35.34300  91.29600  -10.28000 1.000 41.97182  ?  725  ARG   A CA  1 
ATOM   5752  C  C   . ARG   A 1 725  ? -36.80900  91.00600  -9.96000  1.000 48.37302  ?  725  ARG   A C   1 
ATOM   5753  O  O   . ARG   A 1 725  ? -37.68500  91.85100  -10.15400 1.000 44.14493  ?  725  ARG   A O   1 
ATOM   5754  C  CB  . ARG   A 1 725  ? -35.21400  92.56300  -11.12000 1.000 33.22385  ?  725  ARG   A CB  1 
ATOM   5755  C  CG  . ARG   A 1 725  ? -33.77500  92.91000  -11.48100 1.000 36.56277  ?  725  ARG   A CG  1 
ATOM   5756  C  CD  . ARG   A 1 725  ? -33.60000  94.40800  -11.68000 1.000 33.79971  ?  725  ARG   A CD  1 
ATOM   5757  N  NE  . ARG   A 1 725  ? -33.70900  95.13200  -10.42000 1.000 56.75254  ?  725  ARG   A NE  1 
ATOM   5758  C  CZ  . ARG   A 1 725  ? -33.60700  96.44800  -10.29700 1.000 45.20366  ?  725  ARG   A CZ  1 
ATOM   5759  N  NH1 . ARG   A 1 725  ? -33.41400  97.22900  -11.34700 1.000 35.15704  ?  725  ARG   A NH1 1 
ATOM   5760  N  NH2 . ARG   A 1 725  ? -33.70500  96.99600  -9.08900  1.000 43.50161  ?  725  ARG   A NH2 1 
ATOM   5761  N  N   . GLY   A 1 726  ? -37.08700  89.80500  -9.45500  1.000 44.24599  ?  726  GLY   A N   1 
ATOM   5762  C  CA  . GLY   A 1 726  ? -38.41100  89.44100  -9.00000  1.000 27.17725  ?  726  GLY   A CA  1 
ATOM   5763  C  C   . GLY   A 1 726  ? -39.24100  88.66100  -9.99500  1.000 39.61575  ?  726  GLY   A C   1 
ATOM   5764  O  O   . GLY   A 1 726  ? -40.34600  88.22800  -9.64500  1.000 43.01551  ?  726  GLY   A O   1 
ATOM   5765  N  N   . GLY   A 1 727  ? -38.74800  88.46900  -11.21600 1.000 46.35925  ?  727  GLY   A N   1 
ATOM   5766  C  CA  . GLY   A 1 727  ? -39.50000  87.78100  -12.24500 1.000 30.92028  ?  727  GLY   A CA  1 
ATOM   5767  C  C   . GLY   A 1 727  ? -39.98100  86.40500  -11.84100 1.000 27.44691  ?  727  GLY   A C   1 
ATOM   5768  O  O   . GLY   A 1 727  ? -39.20800  85.57500  -11.35100 1.000 37.61619  ?  727  GLY   A O   1 
ATOM   5769  N  N   . ASP   A 1 728  ? -41.27000  86.16700  -12.03500 1.000 50.30372  ?  728  ASP   A N   1 
ATOM   5770  C  CA  . ASP   A 1 728  ? -41.92300  84.90200  -11.74500 1.000 43.97832  ?  728  ASP   A CA  1 
ATOM   5771  C  C   . ASP   A 1 728  ? -42.54400  84.36900  -13.02700 1.000 40.87256  ?  728  ASP   A C   1 
ATOM   5772  O  O   . ASP   A 1 728  ? -42.55900  85.03900  -14.06100 1.000 50.08368  ?  728  ASP   A O   1 
ATOM   5773  C  CB  . ASP   A 1 728  ? -42.99800  85.07700  -10.66600 1.000 42.53514  ?  728  ASP   A CB  1 
ATOM   5774  C  CG  . ASP   A 1 728  ? -43.03700  83.92500  -9.69300  1.000 74.39058  ?  728  ASP   A CG  1 
ATOM   5775  O  OD1 . ASP   A 1 728  ? -43.58100  82.85600  -10.05000 1.000 77.13923  ?  728  ASP   A OD1 1 
ATOM   5776  O  OD2 . ASP   A 1 728  ? -42.51800  84.09000  -8.57000  1.000 94.50787  -1 728  ASP   A OD2 1 
ATOM   5777  N  N   . SER   A 1 729  ? -43.07200  83.15100  -12.95900 1.000 45.76832  ?  729  SER   A N   1 
ATOM   5778  C  CA  . SER   A 1 729  ? -43.82300  82.64400  -14.10000 1.000 37.53084  ?  729  SER   A CA  1 
ATOM   5779  C  C   . SER   A 1 729  ? -45.11700  83.42000  -14.27800 1.000 45.29434  ?  729  SER   A C   1 
ATOM   5780  O  O   . SER   A 1 729  ? -45.51100  83.73900  -15.40600 1.000 54.87981  ?  729  SER   A O   1 
ATOM   5781  C  CB  . SER   A 1 729  ? -44.11500  81.16200  -13.92000 1.000 34.02232  ?  729  SER   A CB  1 
ATOM   5782  O  OG  . SER   A 1 729  ? -42.92400  80.40800  -13.92000 1.000 37.87670  ?  729  SER   A OG  1 
ATOM   5783  N  N   . ILE   A 1 730  ? -45.79400  83.72600  -13.17100 1.000 45.64288  ?  730  ILE   A N   1 
ATOM   5784  C  CA  . ILE   A 1 730  ? -46.99100  84.55500  -13.23100 1.000 42.86226  ?  730  ILE   A CA  1 
ATOM   5785  C  C   . ILE   A 1 730  ? -46.65200  85.92700  -13.79800 1.000 40.77034  ?  730  ILE   A C   1 
ATOM   5786  O  O   . ILE   A 1 730  ? -47.40300  86.48500  -14.60800 1.000 48.51350  ?  730  ILE   A O   1 
ATOM   5787  C  CB  . ILE   A 1 730  ? -47.63600  84.65300  -11.83500 1.000 39.30655  ?  730  ILE   A CB  1 
ATOM   5788  C  CG1 . ILE   A 1 730  ? -48.36100  83.35000  -11.48100 1.000 37.84004  ?  730  ILE   A CG1 1 
ATOM   5789  C  CG2 . ILE   A 1 730  ? -48.59300  85.82900  -11.76200 1.000 46.13801  ?  730  ILE   A CG2 1 
ATOM   5790  C  CD1 . ILE   A 1 730  ? -49.11900  82.72300  -12.63700 1.000 54.61312  ?  730  ILE   A CD1 1 
ATOM   5791  N  N   . LYS   A 1 731  ? -45.50400  86.48000  -13.40400 1.000 37.18703  ?  731  LYS   A N   1 
ATOM   5792  C  CA  . LYS   A 1 731  ? -45.11000  87.79300  -13.89500 1.000 39.45799  ?  731  LYS   A CA  1 
ATOM   5793  C  C   . LYS   A 1 731  ? -44.66900  87.76100  -15.35300 1.000 42.07364  ?  731  LYS   A C   1 
ATOM   5794  O  O   . LYS   A 1 731  ? -44.75200  88.79000  -16.03200 1.000 42.47736  ?  731  LYS   A O   1 
ATOM   5795  C  CB  . LYS   A 1 731  ? -44.00600  88.36800  -13.01100 1.000 29.98610  ?  731  LYS   A CB  1 
ATOM   5796  C  CG  . LYS   A 1 731  ? -44.54900  89.04800  -11.76600 1.000 27.77471  ?  731  LYS   A CG  1 
ATOM   5797  C  CD  . LYS   A 1 731  ? -43.48100  89.23000  -10.70700 1.000 41.07941  ?  731  LYS   A CD  1 
ATOM   5798  C  CE  . LYS   A 1 731  ? -44.00900  90.06800  -9.55800  1.000 38.24717  ?  731  LYS   A CE  1 
ATOM   5799  N  NZ  . LYS   A 1 731  ? -45.37700  89.62500  -9.16400  1.000 57.54236  ?  731  LYS   A NZ  1 
ATOM   5800  N  N   . VAL   A 1 732  ? -44.20600  86.61300  -15.85300 1.000 38.89716  ?  732  VAL   A N   1 
ATOM   5801  C  CA  . VAL   A 1 732  ? -43.93300  86.50800  -17.28200 1.000 40.56592  ?  732  VAL   A CA  1 
ATOM   5802  C  C   . VAL   A 1 732  ? -45.23100  86.60100  -18.07200 1.000 36.68256  ?  732  VAL   A C   1 
ATOM   5803  O  O   . VAL   A 1 732  ? -45.31200  87.31800  -19.07700 1.000 45.79412  ?  732  VAL   A O   1 
ATOM   5804  C  CB  . VAL   A 1 732  ? -43.16600  85.21100  -17.60000 1.000 45.65087  ?  732  VAL   A CB  1 
ATOM   5805  C  CG1 . VAL   A 1 732  ? -43.21100  84.93300  -19.09100 1.000 41.81552  ?  732  VAL   A CG1 1 
ATOM   5806  C  CG2 . VAL   A 1 732  ? -41.71600  85.31700  -17.13500 1.000 26.13475  ?  732  VAL   A CG2 1 
ATOM   5807  N  N   . MET   A 1 733  ? -46.27000  85.89400  -17.62200 1.000 38.00511  ?  733  MET   A N   1 
ATOM   5808  C  CA  . MET   A 1 733  ? -47.56600  85.98400  -18.28500 1.000 41.04829  ?  733  MET   A CA  1 
ATOM   5809  C  C   . MET   A 1 733  ? -48.13000  87.39600  -18.19600 1.000 42.71817  ?  733  MET   A C   1 
ATOM   5810  O  O   . MET   A 1 733  ? -48.77800  87.87400  -19.13400 1.000 45.18499  ?  733  MET   A O   1 
ATOM   5811  C  CB  . MET   A 1 733  ? -48.53900  84.98000  -17.67300 1.000 32.71375  ?  733  MET   A CB  1 
ATOM   5812  C  CG  . MET   A 1 733  ? -48.33600  83.55400  -18.15100 1.000 47.77097  ?  733  MET   A CG  1 
ATOM   5813  S  SD  . MET   A 1 733  ? -48.35400  83.40900  -19.94500 1.000 71.65411  ?  733  MET   A SD  1 
ATOM   5814  C  CE  . MET   A 1 733  ? -49.96700  84.08900  -20.31800 1.000 64.08309  ?  733  MET   A CE  1 
ATOM   5815  N  N   . GLN   A 1 734  ? -47.89100  88.07900  -17.07300 1.000 31.49772  ?  734  GLN   A N   1 
ATOM   5816  C  CA  . GLN   A 1 734  ? -48.35100  89.45700  -16.94100 1.000 32.90126  ?  734  GLN   A CA  1 
ATOM   5817  C  C   . GLN   A 1 734  ? -47.64200  90.36400  -17.93500 1.000 39.68188  ?  734  GLN   A C   1 
ATOM   5818  O  O   . GLN   A 1 734  ? -48.26600  91.24000  -18.54500 1.000 50.62947  ?  734  GLN   A O   1 
ATOM   5819  C  CB  . GLN   A 1 734  ? -48.13400  89.95100  -15.51100 1.000 42.69980  ?  734  GLN   A CB  1 
ATOM   5820  C  CG  . GLN   A 1 734  ? -49.19900  89.49300  -14.52600 1.000 44.80618  ?  734  GLN   A CG  1 
ATOM   5821  C  CD  . GLN   A 1 734  ? -48.82700  89.79500  -13.08700 1.000 46.46626  ?  734  GLN   A CD  1 
ATOM   5822  O  OE1 . GLN   A 1 734  ? -47.92500  90.59000  -12.82000 1.000 51.55573  ?  734  GLN   A OE1 1 
ATOM   5823  N  NE2 . GLN   A 1 734  ? -49.52100  89.15900  -12.15000 1.000 52.28034  ?  734  GLN   A NE2 1 
ATOM   5824  N  N   . LEU   A 1 735  ? -46.33400  90.16600  -18.11300 1.000 44.94615  ?  735  LEU   A N   1 
ATOM   5825  C  CA  . LEU   A 1 735  ? -45.60600  90.91200  -19.13300 1.000 42.73390  ?  735  LEU   A CA  1 
ATOM   5826  C  C   . LEU   A 1 735  ? -46.17800  90.63900  -20.51900 1.000 39.85401  ?  735  LEU   A C   1 
ATOM   5827  O  O   . LEU   A 1 735  ? -46.34000  91.56100  -21.32800 1.000 36.39981  ?  735  LEU   A O   1 
ATOM   5828  C  CB  . LEU   A 1 735  ? -44.12200  90.55000  -19.08100 1.000 32.32058  ?  735  LEU   A CB  1 
ATOM   5829  C  CG  . LEU   A 1 735  ? -43.28500  90.93500  -20.30100 1.000 32.47093  ?  735  LEU   A CG  1 
ATOM   5830  C  CD1 . LEU   A 1 735  ? -42.94500  92.42000  -20.28400 1.000 28.24226  ?  735  LEU   A CD1 1 
ATOM   5831  C  CD2 . LEU   A 1 735  ? -42.02700  90.08400  -20.38500 1.000 28.30758  ?  735  LEU   A CD2 1 
ATOM   5832  N  N   . ILE   A 1 736  ? -46.51000  89.37700  -20.80000 1.000 33.17180  ?  736  ILE   A N   1 
ATOM   5833  C  CA  . ILE   A 1 736  ? -47.03800  89.01500  -22.11200 1.000 40.33634  ?  736  ILE   A CA  1 
ATOM   5834  C  C   . ILE   A 1 736  ? -48.38500  89.68700  -22.35200 1.000 42.55165  ?  736  ILE   A C   1 
ATOM   5835  O  O   . ILE   A 1 736  ? -48.66600  90.17100  -23.45600 1.000 47.31231  ?  736  ILE   A O   1 
ATOM   5836  C  CB  . ILE   A 1 736  ? -47.13000  87.48200  -22.23600 1.000 34.62251  ?  736  ILE   A CB  1 
ATOM   5837  C  CG1 . ILE   A 1 736  ? -45.72900  86.87500  -22.29900 1.000 39.42819  ?  736  ILE   A CG1 1 
ATOM   5838  C  CG2 . ILE   A 1 736  ? -47.92800  87.08000  -23.46800 1.000 41.90822  ?  736  ILE   A CG2 1 
ATOM   5839  C  CD1 . ILE   A 1 736  ? -45.71700  85.36500  -22.29400 1.000 44.74488  ?  736  ILE   A CD1 1 
ATOM   5840  N  N   . HIS   A 1 737  ? -49.23300  89.74300  -21.32100 1.000 38.87285  ?  737  HIS   A N   1 
ATOM   5841  C  CA  . HIS   A 1 737  ? -50.55100  90.34900  -21.48900 1.000 46.19700  ?  737  HIS   A CA  1 
ATOM   5842  C  C   . HIS   A 1 737  ? -50.45400  91.86500  -21.59600 1.000 48.83985  ?  737  HIS   A C   1 
ATOM   5843  O  O   . HIS   A 1 737  ? -51.15300  92.48300  -22.40800 1.000 59.88247  ?  737  HIS   A O   1 
ATOM   5844  C  CB  . HIS   A 1 737  ? -51.47200  89.94700  -20.33700 1.000 41.65410  ?  737  HIS   A CB  1 
ATOM   5845  C  CG  . HIS   A 1 737  ? -51.80500  88.48600  -20.30900 1.000 63.51045  ?  737  HIS   A CG  1 
ATOM   5846  N  ND1 . HIS   A 1 737  ? -51.98900  87.78600  -19.13500 1.000 62.60775  ?  737  HIS   A ND1 1 
ATOM   5847  C  CD2 . HIS   A 1 737  ? -51.99500  87.59500  -21.31100 1.000 55.10573  ?  737  HIS   A CD2 1 
ATOM   5848  C  CE1 . HIS   A 1 737  ? -52.27500  86.52700  -19.41500 1.000 53.89633  ?  737  HIS   A CE1 1 
ATOM   5849  N  NE2 . HIS   A 1 737  ? -52.28400  86.38400  -20.72800 1.000 57.10251  ?  737  HIS   A NE2 1 
ATOM   5850  N  N   . GLN   A 1 738  ? -49.59000  92.48300  -20.78800 1.000 43.64244  ?  738  GLN   A N   1 
ATOM   5851  C  CA  . GLN   A 1 738  ? -49.36900  93.91800  -20.90700 1.000 43.38371  ?  738  GLN   A CA  1 
ATOM   5852  C  C   . GLN   A 1 738  ? -48.75900  94.29300  -22.25300 1.000 50.47847  ?  738  GLN   A C   1 
ATOM   5853  O  O   . GLN   A 1 738  ? -48.86900  95.44900  -22.67200 1.000 57.16251  ?  738  GLN   A O   1 
ATOM   5854  C  CB  . GLN   A 1 738  ? -48.47200  94.40300  -19.77000 1.000 36.77372  ?  738  GLN   A CB  1 
ATOM   5855  C  CG  . GLN   A 1 738  ? -48.86600  95.75400  -19.21000 1.000 47.05597  ?  738  GLN   A CG  1 
ATOM   5856  C  CD  . GLN   A 1 738  ? -49.79000  95.63000  -18.01600 1.000 69.92728  ?  738  GLN   A CD  1 
ATOM   5857  O  OE1 . GLN   A 1 738  ? -49.50700  94.89100  -17.07300 1.000 66.47492  ?  738  GLN   A OE1 1 
ATOM   5858  N  NE2 . GLN   A 1 738  ? -50.90400  96.35300  -18.05200 1.000 75.93726  ?  738  GLN   A NE2 1 
ATOM   5859  N  N   . LEU   A 1 739  ? -48.11900  93.34200  -22.93600 1.000 44.69617  ?  739  LEU   A N   1 
ATOM   5860  C  CA  . LEU   A 1 739  ? -47.57500  93.61400  -24.26100 1.000 40.37670  ?  739  LEU   A CA  1 
ATOM   5861  C  C   . LEU   A 1 739  ? -48.61700  93.41600  -25.35200 1.000 45.81425  ?  739  LEU   A C   1 
ATOM   5862  O  O   . LEU   A 1 739  ? -48.52600  94.04500  -26.41200 1.000 47.52930  ?  739  LEU   A O   1 
ATOM   5863  C  CB  . LEU   A 1 739  ? -46.35900  92.72300  -24.52100 1.000 32.29904  ?  739  LEU   A CB  1 
ATOM   5864  C  CG  . LEU   A 1 739  ? -45.03000  93.20500  -23.93400 1.000 38.70618  ?  739  LEU   A CG  1 
ATOM   5865  C  CD1 . LEU   A 1 739  ? -43.94700  92.15000  -24.09500 1.000 32.35629  ?  739  LEU   A CD1 1 
ATOM   5866  C  CD2 . LEU   A 1 739  ? -44.60200  94.50500  -24.58900 1.000 39.36351  ?  739  LEU   A CD2 1 
ATOM   5867  N  N   . LYS   A 1 740  ? -49.60800  92.55300  -25.11500 1.000 52.23221  ?  740  LYS   A N   1 
ATOM   5868  C  CA  . LYS   A 1 740  ? -50.67400  92.37600  -26.09300 1.000 39.40665  ?  740  LYS   A CA  1 
ATOM   5869  C  C   . LYS   A 1 740  ? -51.49900  93.64600  -26.25200 1.000 50.47515  ?  740  LYS   A C   1 
ATOM   5870  O  O   . LYS   A 1 740  ? -51.96900  93.94100  -27.35700 1.000 69.45055  ?  740  LYS   A O   1 
ATOM   5871  C  CB  . LYS   A 1 740  ? -51.56700  91.20200  -25.69400 1.000 43.15178  ?  740  LYS   A CB  1 
ATOM   5872  C  CG  . LYS   A 1 740  ? -51.04200  89.85000  -26.14500 1.000 49.28060  ?  740  LYS   A CG  1 
ATOM   5873  C  CD  . LYS   A 1 740  ? -51.74900  88.71000  -25.43000 1.000 66.67311  ?  740  LYS   A CD  1 
ATOM   5874  C  CE  . LYS   A 1 740  ? -51.54600  87.38800  -26.15900 1.000 60.14739  ?  740  LYS   A CE  1 
ATOM   5875  N  NZ  . LYS   A 1 740  ? -52.11700  86.23600  -25.40300 1.000 64.47196  ?  740  LYS   A NZ  1 
ATOM   5876  N  N   . ASN   A 1 741  ? -51.68600  94.40500  -25.16900 1.000 49.91807  ?  741  ASN   A N   1 
ATOM   5877  C  CA  . ASN   A 1 741  ? -52.34800  95.70200  -25.27700 1.000 53.46500  ?  741  ASN   A CA  1 
ATOM   5878  C  C   . ASN   A 1 741  ? -51.52400  96.68800  -26.08900 1.000 53.37054  ?  741  ASN   A C   1 
ATOM   5879  O  O   . ASN   A 1 741  ? -52.08800  97.56500  -26.75300 1.000 70.17549  ?  741  ASN   A O   1 
ATOM   5880  C  CB  . ASN   A 1 741  ? -52.62100  96.27100  -23.88600 1.000 58.12524  ?  741  ASN   A CB  1 
ATOM   5881  C  CG  . ASN   A 1 741  ? -53.59300  95.42700  -23.10000 1.000 82.73114  ?  741  ASN   A CG  1 
ATOM   5882  O  OD1 . ASN   A 1 741  ? -54.48100  94.79500  -23.67100 1.000 90.11226  ?  741  ASN   A OD1 1 
ATOM   5883  N  ND2 . ASN   A 1 741  ? -53.41900  95.39200  -21.78500 1.000 76.41612  ?  741  ASN   A ND2 1 
ATOM   5884  N  N   . ILE   A 1 742  ? -50.19700  96.56800  -26.03900 1.000 55.45701  ?  742  ILE   A N   1 
ATOM   5885  C  CA  . ILE   A 1 742  ? -49.33600  97.43600  -26.83300 1.000 45.45522  ?  742  ILE   A CA  1 
ATOM   5886  C  C   . ILE   A 1 742  ? -49.40500  97.04700  -28.30500 1.000 52.92347  ?  742  ILE   A C   1 
ATOM   5887  O  O   . ILE   A 1 742  ? -49.25400  97.89900  -29.19000 1.000 79.41388  ?  742  ILE   A O   1 
ATOM   5888  C  CB  . ILE   A 1 742  ? -47.89800  97.38200  -26.28000 1.000 47.43215  ?  742  ILE   A CB  1 
ATOM   5889  C  CG1 . ILE   A 1 742  ? -47.78300  98.24100  -25.02100 1.000 44.37118  ?  742  ILE   A CG1 1 
ATOM   5890  C  CG2 . ILE   A 1 742  ? -46.88500  97.84000  -27.31600 1.000 76.88334  ?  742  ILE   A CG2 1 
ATOM   5891  C  CD1 . ILE   A 1 742  ? -48.18400  99.68300  -25.23200 1.000 57.94535  ?  742  ILE   A CD1 1 
ATOM   5892  N  N   . GLY   A 1 743  ? -49.66900  95.77400  -28.59500 1.000 46.19590  ?  743  GLY   A N   1 
ATOM   5893  C  CA  . GLY   A 1 743  ? -49.70200  95.27400  -29.95400 1.000 49.38245  ?  743  GLY   A CA  1 
ATOM   5894  C  C   . GLY   A 1 743  ? -48.57500  94.32700  -30.29500 1.000 68.18755  ?  743  GLY   A C   1 
ATOM   5895  O  O   . GLY   A 1 743  ? -48.46900  93.90600  -31.45400 1.000 63.67470  ?  743  GLY   A O   1 
ATOM   5896  N  N   . LEU   A 1 744  ? -47.73500  93.98000  -29.32600 1.000 66.72507  ?  744  LEU   A N   1 
ATOM   5897  C  CA  . LEU   A 1 744  ? -46.59300  93.09900  -29.52600 1.000 57.60991  ?  744  LEU   A CA  1 
ATOM   5898  C  C   . LEU   A 1 744  ? -46.89600  91.73300  -28.93200 1.000 48.02907  ?  744  LEU   A C   1 
ATOM   5899  O  O   . LEU   A 1 744  ? -47.40000  91.63700  -27.80800 1.000 48.03840  ?  744  LEU   A O   1 
ATOM   5900  C  CB  . LEU   A 1 744  ? -45.33600  93.69100  -28.88800 1.000 42.96724  ?  744  LEU   A CB  1 
ATOM   5901  C  CG  . LEU   A 1 744  ? -45.00400  95.11100  -29.34100 1.000 49.56756  ?  744  LEU   A CG  1 
ATOM   5902  C  CD1 . LEU   A 1 744  ? -43.87200  95.70800  -28.53000 1.000 46.77095  ?  744  LEU   A CD1 1 
ATOM   5903  C  CD2 . LEU   A 1 744  ? -44.61800  95.05800  -30.80100 1.000 58.20434  ?  744  LEU   A CD2 1 
ATOM   5904  N  N   . SER   A 1 745  ? -46.58500  90.68400  -29.68500 1.000 46.48602  ?  745  SER   A N   1 
ATOM   5905  C  CA  . SER   A 1 745  ? -46.81900  89.31500  -29.25200 1.000 46.95482  ?  745  SER   A CA  1 
ATOM   5906  C  C   . SER   A 1 745  ? -45.49500  88.69000  -28.83300 1.000 62.43175  ?  745  SER   A C   1 
ATOM   5907  O  O   . SER   A 1 745  ? -44.55500  88.61800  -29.63200 1.000 66.22608  ?  745  SER   A O   1 
ATOM   5908  C  CB  . SER   A 1 745  ? -47.47600  88.50000  -30.36300 1.000 31.42884  ?  745  SER   A CB  1 
ATOM   5909  O  OG  . SER   A 1 745  ? -48.88500  88.51700  -30.21900 1.000 71.61122  ?  745  SER   A OG  1 
ATOM   5910  N  N   . LEU   A 1 746  ? -45.42400  88.24600  -27.58200 1.000 38.12820  ?  746  LEU   A N   1 
ATOM   5911  C  CA  . LEU   A 1 746  ? -44.25100  87.57800  -27.04300 1.000 29.99966  ?  746  LEU   A CA  1 
ATOM   5912  C  C   . LEU   A 1 746  ? -44.64000  86.18400  -26.57200 1.000 41.46799  ?  746  LEU   A C   1 
ATOM   5913  O  O   . LEU   A 1 746  ? -45.68600  86.00300  -25.94000 1.000 51.53990  ?  746  LEU   A O   1 
ATOM   5914  C  CB  . LEU   A 1 746  ? -43.64700  88.37600  -25.88500 1.000 42.72017  ?  746  LEU   A CB  1 
ATOM   5915  C  CG  . LEU   A 1 746  ? -42.43800  87.76500  -25.17500 1.000 38.43046  ?  746  LEU   A CG  1 
ATOM   5916  C  CD1 . LEU   A 1 746  ? -41.24400  87.69100  -26.11500 1.000 28.63933  ?  746  LEU   A CD1 1 
ATOM   5917  C  CD2 . LEU   A 1 746  ? -42.10000  88.57400  -23.93600 1.000 44.39750  ?  746  LEU   A CD2 1 
ATOM   5918  N  N   . ARG   A 1 747  ? -43.80500  85.20100  -26.89100 1.000 37.60067  ?  747  ARG   A N   1 
ATOM   5919  C  CA  . ARG   A 1 747  ? -44.04400  83.83500  -26.45500 1.000 38.28263  ?  747  ARG   A CA  1 
ATOM   5920  C  C   . ARG   A 1 747  ? -43.39300  83.58700  -25.10000 1.000 47.60559  ?  747  ARG   A C   1 
ATOM   5921  O  O   . ARG   A 1 747  ? -42.37800  84.19800  -24.75400 1.000 58.37688  ?  747  ARG   A O   1 
ATOM   5922  C  CB  . ARG   A 1 747  ? -43.51700  82.83000  -27.47800 1.000 38.34243  ?  747  ARG   A CB  1 
ATOM   5923  C  CG  . ARG   A 1 747  ? -44.60800  82.16700  -28.30200 1.000 52.91948  ?  747  ARG   A CG  1 
ATOM   5924  C  CD  . ARG   A 1 747  ? -44.13300  80.84800  -28.88300 1.000 60.51875  ?  747  ARG   A CD  1 
ATOM   5925  N  NE  . ARG   A 1 747  ? -42.71300  80.88600  -29.21100 1.000 57.67534  ?  747  ARG   A NE  1 
ATOM   5926  C  CZ  . ARG   A 1 747  ? -42.21400  81.42300  -30.31500 1.000 70.60094  ?  747  ARG   A CZ  1 
ATOM   5927  N  NH1 . ARG   A 1 747  ? -42.99700  81.96800  -31.23300 1.000 69.19480  ?  747  ARG   A NH1 1 
ATOM   5928  N  NH2 . ARG   A 1 747  ? -40.89700  81.41700  -30.50200 1.000 64.42736  ?  747  ARG   A NH2 1 
ATOM   5929  N  N   . TYR   A 1 748  ? -43.99800  82.67600  -24.33500 1.000 45.39446  ?  748  TYR   A N   1 
ATOM   5930  C  CA  . TYR   A 1 748  ? -43.51500  82.37900  -22.99000 1.000 37.99193  ?  748  TYR   A CA  1 
ATOM   5931  C  C   . TYR   A 1 748  ? -42.05000  81.95200  -23.00200 1.000 46.63364  ?  748  TYR   A C   1 
ATOM   5932  O  O   . TYR   A 1 748  ? -41.26700  82.36700  -22.13900 1.000 44.20686  ?  748  TYR   A O   1 
ATOM   5933  C  CB  . TYR   A 1 748  ? -44.39000  81.29500  -22.35900 1.000 42.31994  ?  748  TYR   A CB  1 
ATOM   5934  C  CG  . TYR   A 1 748  ? -44.14400  81.07700  -20.88700 1.000 36.77159  ?  748  TYR   A CG  1 
ATOM   5935  C  CD1 . TYR   A 1 748  ? -44.78300  81.85700  -19.93200 1.000 38.18509  ?  748  TYR   A CD1 1 
ATOM   5936  C  CD2 . TYR   A 1 748  ? -43.27700  80.08700  -20.45000 1.000 33.06825  ?  748  TYR   A CD2 1 
ATOM   5937  C  CE1 . TYR   A 1 748  ? -44.55800  81.65900  -18.58400 1.000 31.74818  ?  748  TYR   A CE1 1 
ATOM   5938  C  CE2 . TYR   A 1 748  ? -43.04700  79.88100  -19.10800 1.000 38.19442  ?  748  TYR   A CE2 1 
ATOM   5939  C  CZ  . TYR   A 1 748  ? -43.68800  80.66900  -18.18000 1.000 48.52534  ?  748  TYR   A CZ  1 
ATOM   5940  O  OH  . TYR   A 1 748  ? -43.45100  80.45500  -16.84400 1.000 64.99903  ?  748  TYR   A OH  1 
ATOM   5941  N  N   . ASP   A 1 749  ? -41.65900  81.13200  -23.97900 1.000 44.76926  ?  749  ASP   A N   1 
ATOM   5942  C  CA  . ASP   A 1 749  ? -40.28200  80.65300  -24.03300 1.000 33.96418  ?  749  ASP   A CA  1 
ATOM   5943  C  C   . ASP   A 1 749  ? -39.31300  81.75700  -24.43100 1.000 39.51494  ?  749  ASP   A C   1 
ATOM   5944  O  O   . ASP   A 1 749  ? -38.14600  81.73400  -24.02100 1.000 40.81091  ?  749  ASP   A O   1 
ATOM   5945  C  CB  . ASP   A 1 749  ? -40.17300  79.48700  -25.01300 1.000 38.91486  ?  749  ASP   A CB  1 
ATOM   5946  C  CG  . ASP   A 1 749  ? -40.72400  79.83200  -26.38300 1.000 57.94375  ?  749  ASP   A CG  1 
ATOM   5947  O  OD1 . ASP   A 1 749  ? -41.96400  79.88500  -26.53000 1.000 56.85793  ?  749  ASP   A OD1 1 
ATOM   5948  O  OD2 . ASP   A 1 749  ? -39.91700  80.06700  -27.30800 1.000 48.41672  -1 749  ASP   A OD2 1 
ATOM   5949  N  N   . GLN   A 1 750  ? -39.77200  82.72600  -25.22600 1.000 45.24658  ?  750  GLN   A N   1 
ATOM   5950  C  CA  . GLN   A 1 750  ? -38.87600  83.75900  -25.72900 1.000 50.40304  ?  750  GLN   A CA  1 
ATOM   5951  C  C   . GLN   A 1 750  ? -38.41000  84.70900  -24.63400 1.000 43.56108  ?  750  GLN   A C   1 
ATOM   5952  O  O   . GLN   A 1 750  ? -37.38700  85.37800  -24.80900 1.000 38.07355  ?  750  GLN   A O   1 
ATOM   5953  C  CB  . GLN   A 1 750  ? -39.55500  84.54000  -26.85500 1.000 41.38056  ?  750  GLN   A CB  1 
ATOM   5954  C  CG  . GLN   A 1 750  ? -39.97600  83.67800  -28.03600 1.000 41.11951  ?  750  GLN   A CG  1 
ATOM   5955  C  CD  . GLN   A 1 750  ? -40.54900  84.49200  -29.17800 1.000 27.87670  ?  750  GLN   A CD  1 
ATOM   5956  O  OE1 . GLN   A 1 750  ? -41.55400  85.18500  -29.01800 1.000 40.06301  ?  750  GLN   A OE1 1 
ATOM   5957  N  NE2 . GLN   A 1 750  ? -39.91300  84.41300  -30.34000 1.000 42.41531  ?  750  GLN   A NE2 1 
ATOM   5958  N  N   . LEU   A 1 751  ? -39.13200  84.78200  -23.51300 1.000 36.78301  ?  751  LEU   A N   1 
ATOM   5959  C  CA  . LEU   A 1 751  ? -38.65900  85.59300  -22.39700 1.000 47.41831  ?  751  LEU   A CA  1 
ATOM   5960  C  C   . LEU   A 1 751  ? -37.40500  84.98800  -21.77300 1.000 43.52063  ?  751  LEU   A C   1 
ATOM   5961  O  O   . LEU   A 1 751  ? -36.47200  85.71500  -21.41400 1.000 40.26492  ?  751  LEU   A O   1 
ATOM   5962  C  CB  . LEU   A 1 751  ? -39.76800  85.75000  -21.35400 1.000 35.12044  ?  751  LEU   A CB  1 
ATOM   5963  C  CG  . LEU   A 1 751  ? -39.58700  86.80300  -20.25200 1.000 28.59344  ?  751  LEU   A CG  1 
ATOM   5964  C  CD1 . LEU   A 1 751  ? -38.78800  86.26200  -19.07300 1.000 32.34478  ?  751  LEU   A CD1 1 
ATOM   5965  C  CD2 . LEU   A 1 751  ? -38.93300  88.06200  -20.80000 1.000 25.90417  ?  751  LEU   A CD2 1 
ATOM   5966  N  N   . PHE   A 1 752  ? -37.36200  83.66100  -21.63700 1.000 43.39452  ?  752  PHE   A N   1 
ATOM   5967  C  CA  . PHE   A 1 752  ? -36.19900  83.01900  -21.03600 1.000 38.13069  ?  752  PHE   A CA  1 
ATOM   5968  C  C   . PHE   A 1 752  ? -34.98200  83.06000  -21.94800 1.000 39.64450  ?  752  PHE   A C   1 
ATOM   5969  O  O   . PHE   A 1 752  ? -33.85600  82.91400  -21.46200 1.000 41.30044  ?  752  PHE   A O   1 
ATOM   5970  C  CB  . PHE   A 1 752  ? -36.53600  81.57800  -20.65100 1.000 30.34528  ?  752  PHE   A CB  1 
ATOM   5971  C  CG  . PHE   A 1 752  ? -37.54500  81.47800  -19.54500 1.000 39.09801  ?  752  PHE   A CG  1 
ATOM   5972  C  CD1 . PHE   A 1 752  ? -37.14200  81.49800  -18.21900 1.000 38.09633  ?  752  PHE   A CD1 1 
ATOM   5973  C  CD2 . PHE   A 1 752  ? -38.89800  81.39100  -19.82900 1.000 32.02768  ?  752  PHE   A CD2 1 
ATOM   5974  C  CE1 . PHE   A 1 752  ? -38.07000  81.42000  -17.19700 1.000 40.62028  ?  752  PHE   A CE1 1 
ATOM   5975  C  CE2 . PHE   A 1 752  ? -39.83100  81.31100  -18.81200 1.000 28.84876  ?  752  PHE   A CE2 1 
ATOM   5976  C  CZ  . PHE   A 1 752  ? -39.41700  81.32700  -17.49500 1.000 39.12902  ?  752  PHE   A CZ  1 
ATOM   5977  N  N   . THR   A 1 753  ? -35.18300  83.26300  -23.25000 1.000 40.01809  ?  753  THR   A N   1 
ATOM   5978  C  CA  . THR   A 1 753  ? -34.08400  83.46900  -24.18300 1.000 30.60854  ?  753  THR   A CA  1 
ATOM   5979  C  C   . THR   A 1 753  ? -33.75900  84.94400  -24.39300 1.000 32.11487  ?  753  THR   A C   1 
ATOM   5980  O  O   . THR   A 1 753  ? -32.70700  85.25600  -24.95900 1.000 35.80774  ?  753  THR   A O   1 
ATOM   5981  C  CB  . THR   A 1 753  ? -34.40200  82.81500  -25.53500 1.000 29.53067  ?  753  THR   A CB  1 
ATOM   5982  O  OG1 . THR   A 1 753  ? -35.70200  83.22400  -25.97700 1.000 34.60991  ?  753  THR   A OG1 1 
ATOM   5983  C  CG2 . THR   A 1 753  ? -34.38000  81.30300  -25.41000 1.000 32.81737  ?  753  THR   A CG2 1 
ATOM   5984  N  N   . HIS   A 1 754  ? -34.63100  85.85100  -23.95100 1.000 41.22696  ?  754  HIS   A N   1 
ATOM   5985  C  CA  . HIS   A 1 754  ? -34.39900  87.29600  -24.03400 1.000 42.03513  ?  754  HIS   A CA  1 
ATOM   5986  C  C   . HIS   A 1 754  ? -34.78500  87.93000  -22.70300 1.000 40.51031  ?  754  HIS   A C   1 
ATOM   5987  O  O   . HIS   A 1 754  ? -35.74600  88.70200  -22.61600 1.000 38.21488  ?  754  HIS   A O   1 
ATOM   5988  C  CB  . HIS   A 1 754  ? -35.19300  87.91100  -25.19000 1.000 34.58419  ?  754  HIS   A CB  1 
ATOM   5989  C  CG  . HIS   A 1 754  ? -34.87900  87.31400  -26.52600 1.000 34.24160  ?  754  HIS   A CG  1 
ATOM   5990  N  ND1 . HIS   A 1 754  ? -35.36400  86.08800  -26.92700 1.000 33.81879  ?  754  HIS   A ND1 1 
ATOM   5991  C  CD2 . HIS   A 1 754  ? -34.13100  87.77700  -27.55600 1.000 49.52634  ?  754  HIS   A CD2 1 
ATOM   5992  C  CE1 . HIS   A 1 754  ? -34.92500  85.81800  -28.14300 1.000 41.00501  ?  754  HIS   A CE1 1 
ATOM   5993  N  NE2 . HIS   A 1 754  ? -34.17500  86.82700  -28.54800 1.000 57.25627  ?  754  HIS   A NE2 1 
ATOM   5994  N  N   . PRO   A 1 755  ? -34.04500  87.62600  -21.63500 1.000 39.52687  ?  755  PRO   A N   1 
ATOM   5995  C  CA  . PRO   A 1 755  ? -34.45100  88.05900  -20.29300 1.000 35.34290  ?  755  PRO   A CA  1 
ATOM   5996  C  C   . PRO   A 1 755  ? -34.06600  89.48600  -19.93300 1.000 38.18861  ?  755  PRO   A C   1 
ATOM   5997  O  O   . PRO   A 1 755  ? -34.14000  89.84300  -18.75400 1.000 36.76783  ?  755  PRO   A O   1 
ATOM   5998  C  CB  . PRO   A 1 755  ? -33.71700  87.05400  -19.39400 1.000 33.69027  ?  755  PRO   A CB  1 
ATOM   5999  C  CG  . PRO   A 1 755  ? -32.45600  86.77200  -20.13100 1.000 33.43967  ?  755  PRO   A CG  1 
ATOM   6000  C  CD  . PRO   A 1 755  ? -32.78100  86.86600  -21.60700 1.000 34.27107  ?  755  PRO   A CD  1 
ATOM   6001  N  N   . THR   A 1 756  ? -33.65100  90.30300  -20.89800 1.000 33.48930  ?  756  THR   A N   1 
ATOM   6002  C  CA  . THR   A 1 756  ? -33.37900  91.71400  -20.66900 1.000 35.23300  ?  756  THR   A CA  1 
ATOM   6003  C  C   . THR   A 1 756  ? -34.12900  92.53700  -21.70500 1.000 36.65447  ?  756  THR   A C   1 
ATOM   6004  O  O   . THR   A 1 756  ? -34.55500  92.02800  -22.74400 1.000 45.48380  ?  756  THR   A O   1 
ATOM   6005  C  CB  . THR   A 1 756  ? -31.87400  92.04500  -20.73300 1.000 43.03222  ?  756  THR   A CB  1 
ATOM   6006  O  OG1 . THR   A 1 756  ? -31.41700  91.99400  -22.09200 1.000 36.21153  ?  756  THR   A OG1 1 
ATOM   6007  C  CG2 . THR   A 1 756  ? -31.06900  91.06900  -19.89600 1.000 36.36271  ?  756  THR   A CG2 1 
ATOM   6008  N  N   . ILE   A 1 757  ? -34.28800  93.82800  -21.40600 1.000 38.55309  ?  757  ILE   A N   1 
ATOM   6009  C  CA  . ILE   A 1 757  ? -34.96300  94.72000  -22.34200 1.000 38.48142  ?  757  ILE   A CA  1 
ATOM   6010  C  C   . ILE   A 1 757  ? -34.13800  94.90400  -23.60900 1.000 43.61272  ?  757  ILE   A C   1 
ATOM   6011  O  O   . ILE   A 1 757  ? -34.69700  95.05000  -24.70500 1.000 39.90304  ?  757  ILE   A O   1 
ATOM   6012  C  CB  . ILE   A 1 757  ? -35.26700  96.06200  -21.65400 1.000 39.00256  ?  757  ILE   A CB  1 
ATOM   6013  C  CG1 . ILE   A 1 757  ? -36.26200  95.84400  -20.51100 1.000 43.82476  ?  757  ILE   A CG1 1 
ATOM   6014  C  CG2 . ILE   A 1 757  ? -35.80100  97.07100  -22.65400 1.000 36.31151  ?  757  ILE   A CG2 1 
ATOM   6015  C  CD1 . ILE   A 1 757  ? -36.52200  97.07300  -19.67800 1.000 43.49049  ?  757  ILE   A CD1 1 
ATOM   6016  N  N   . ARG   A 1 758  ? -32.80700  94.89000  -23.48800 1.000 42.66529  ?  758  ARG   A N   1 
ATOM   6017  C  CA  . ARG   A 1 758  ? -31.93900  95.00200  -24.65700 1.000 36.14621  ?  758  ARG   A CA  1 
ATOM   6018  C  C   . ARG   A 1 758  ? -32.24800  93.91400  -25.67700 1.000 46.83687  ?  758  ARG   A C   1 
ATOM   6019  O  O   . ARG   A 1 758  ? -32.34600  94.18200  -26.87900 1.000 53.99988  ?  758  ARG   A O   1 
ATOM   6020  C  CB  . ARG   A 1 758  ? -30.47400  94.92800  -24.22600 1.000 54.87052  ?  758  ARG   A CB  1 
ATOM   6021  C  CG  . ARG   A 1 758  ? -29.52700  95.81000  -25.02500 1.000 48.60820  ?  758  ARG   A CG  1 
ATOM   6022  C  CD  . ARG   A 1 758  ? -28.07900  95.52000  -24.65800 1.000 39.02990  ?  758  ARG   A CD  1 
ATOM   6023  N  NE  . ARG   A 1 758  ? -27.19100  96.62100  -25.01200 1.000 72.41124  ?  758  ARG   A NE  1 
ATOM   6024  C  CZ  . ARG   A 1 758  ? -26.62500  97.44100  -24.13600 1.000 76.04481  ?  758  ARG   A CZ  1 
ATOM   6025  N  NH1 . ARG   A 1 758  ? -26.83100  97.31200  -22.83600 1.000 61.08827  ?  758  ARG   A NH1 1 
ATOM   6026  N  NH2 . ARG   A 1 758  ? -25.83400  98.41700  -24.57700 1.000 69.19964  ?  758  ARG   A NH2 1 
ATOM   6027  N  N   . GLN   A 1 759  ? -32.40900  92.67500  -25.20800 1.000 45.26592  ?  759  GLN   A N   1 
ATOM   6028  C  CA  . GLN   A 1 759  ? -32.68500  91.56300  -26.11000 1.000 41.68048  ?  759  GLN   A CA  1 
ATOM   6029  C  C   . GLN   A 1 759  ? -34.13800  91.55700  -26.57100 1.000 42.43388  ?  759  GLN   A C   1 
ATOM   6030  O  O   . GLN   A 1 759  ? -34.42100  91.21200  -27.72400 1.000 49.19437  ?  759  GLN   A O   1 
ATOM   6031  C  CB  . GLN   A 1 759  ? -32.33800  90.24100  -25.42700 1.000 31.05381  ?  759  GLN   A CB  1 
ATOM   6032  C  CG  . GLN   A 1 759  ? -30.98900  90.25200  -24.72800 1.000 38.85919  ?  759  GLN   A CG  1 
ATOM   6033  C  CD  . GLN   A 1 759  ? -30.72100  88.98000  -23.95000 1.000 40.20460  ?  759  GLN   A CD  1 
ATOM   6034  O  OE1 . GLN   A 1 759  ? -30.92900  87.87400  -24.45100 1.000 49.24518  ?  759  GLN   A OE1 1 
ATOM   6035  N  NE2 . GLN   A 1 759  ? -30.25700  89.13000  -22.71500 1.000 46.80611  ?  759  GLN   A NE2 1 
ATOM   6036  N  N   . LEU   A 1 760  ? -35.06900  91.92600  -25.68600 1.000 38.28083  ?  760  LEU   A N   1 
ATOM   6037  C  CA  . LEU   A 1 760  ? -36.48200  91.90600  -26.04800 1.000 37.65533  ?  760  LEU   A CA  1 
ATOM   6038  C  C   . LEU   A 1 760  ? -36.76200  92.86300  -27.18900 1.000 45.73439  ?  760  LEU   A C   1 
ATOM   6039  O  O   . LEU   A 1 760  ? -37.55700  92.56400  -28.08900 1.000 47.35776  ?  760  LEU   A O   1 
ATOM   6040  C  CB  . LEU   A 1 760  ? -37.34500  92.26600  -24.84100 1.000 46.79767  ?  760  LEU   A CB  1 
ATOM   6041  C  CG  . LEU   A 1 760  ? -37.95800  91.10000  -24.07100 1.000 36.43886  ?  760  LEU   A CG  1 
ATOM   6042  C  CD1 . LEU   A 1 760  ? -39.02700  91.60900  -23.12300 1.000 40.57226  ?  760  LEU   A CD1 1 
ATOM   6043  C  CD2 . LEU   A 1 760  ? -38.53700  90.07100  -25.03000 1.000 45.25698  ?  760  LEU   A CD2 1 
ATOM   6044  N  N   . LYS   A 1 761  ? -36.12100  94.02500  -27.16500 1.000 37.24268  ?  761  LYS   A N   1 
ATOM   6045  C  CA  . LYS   A 1 761  ? -36.29600  94.96200  -28.26000 1.000 39.96868  ?  761  LYS   A CA  1 
ATOM   6046  C  C   . LYS   A 1 761  ? -35.86300  94.37500  -29.60500 1.000 47.26036  ?  761  LYS   A C   1 
ATOM   6047  O  O   . LYS   A 1 761  ? -36.61200  94.44800  -30.58500 1.000 53.65483  ?  761  LYS   A O   1 
ATOM   6048  C  CB  . LYS   A 1 761  ? -35.56400  96.25600  -27.98000 1.000 49.98362  ?  761  LYS   A CB  1 
ATOM   6049  C  CG  . LYS   A 1 761  ? -35.36100  96.89900  -29.33700 1.000 44.96533  ?  761  LYS   A CG  1 
ATOM   6050  C  CD  . LYS   A 1 761  ? -35.46100  98.39900  -29.32300 1.000 52.85256  ?  761  LYS   A CD  1 
ATOM   6051  C  CE  . LYS   A 1 761  ? -34.65300  99.02300  -30.45800 1.000 48.39646  ?  761  LYS   A CE  1 
ATOM   6052  N  NZ  . LYS   A 1 761  ? -33.18800  98.76800  -30.22700 1.000 64.39830  ?  761  LYS   A NZ  1 
ATOM   6053  N  N   . ARG   A 1 762  ? -34.67900  93.75800  -29.66900 1.000 42.59375  ?  762  ARG   A N   1 
ATOM   6054  C  CA  . ARG   A 1 762  ? -34.25000  93.11100  -30.90900 1.000 43.27884  ?  762  ARG   A CA  1 
ATOM   6055  C  C   . ARG   A 1 762  ? -35.26100  92.07600  -31.38700 1.000 40.68612  ?  762  ARG   A C   1 
ATOM   6056  O  O   . ARG   A 1 762  ? -35.39000  91.83900  -32.59400 1.000 55.66334  ?  762  ARG   A O   1 
ATOM   6057  C  CB  . ARG   A 1 762  ? -32.88700  92.45800  -30.70500 1.000 49.24508  ?  762  ARG   A CB  1 
ATOM   6058  C  CG  . ARG   A 1 762  ? -31.94500  93.28500  -29.85400 1.000 58.76663  ?  762  ARG   A CG  1 
ATOM   6059  C  CD  . ARG   A 1 762  ? -30.54100  92.71600  -29.88900 1.000 55.27168  ?  762  ARG   A CD  1 
ATOM   6060  N  NE  . ARG   A 1 762  ? -29.73800  93.35400  -30.92400 1.000 60.98344  ?  762  ARG   A NE  1 
ATOM   6061  C  CZ  . ARG   A 1 762  ? -28.98800  92.70100  -31.80000 1.000 60.28298  ?  762  ARG   A CZ  1 
ATOM   6062  N  NH1 . ARG   A 1 762  ? -28.89000  91.38200  -31.78000 1.000 66.18202  ?  762  ARG   A NH1 1 
ATOM   6063  N  NH2 . ARG   A 1 762  ? -28.31700  93.38900  -32.71700 1.000 66.69043  ?  762  ARG   A NH2 1 
ATOM   6064  N  N   . LEU   A 1 763  ? -35.98800  91.45700  -30.46000 1.000 49.91669  ?  763  LEU   A N   1 
ATOM   6065  C  CA  . LEU   A 1 763  ? -36.98800  90.46900  -30.83500 1.000 44.70388  ?  763  LEU   A CA  1 
ATOM   6066  C  C   . LEU   A 1 763  ? -38.25000  91.13000  -31.37900 1.000 48.33002  ?  763  LEU   A C   1 
ATOM   6067  O  O   . LEU   A 1 763  ? -38.85200  90.63000  -32.33700 1.000 56.54367  ?  763  LEU   A O   1 
ATOM   6068  C  CB  . LEU   A 1 763  ? -37.31200  89.58500  -29.62800 1.000 39.97126  ?  763  LEU   A CB  1 
ATOM   6069  C  CG  . LEU   A 1 763  ? -38.00400  88.24300  -29.88100 1.000 47.22153  ?  763  LEU   A CG  1 
ATOM   6070  C  CD1 . LEU   A 1 763  ? -37.09700  87.30800  -30.66000 1.000 50.45848  ?  763  LEU   A CD1 1 
ATOM   6071  C  CD2 . LEU   A 1 763  ? -38.42200  87.60600  -28.56900 1.000 42.97464  ?  763  LEU   A CD2 1 
ATOM   6072  N  N   . LEU   A 1 764  ? -38.64900  92.26500  -30.80400 1.000 46.27029  ?  764  LEU   A N   1 
ATOM   6073  C  CA  . LEU   A 1 764  ? -39.92300  92.89700  -31.12000 1.000 50.03011  ?  764  LEU   A CA  1 
ATOM   6074  C  C   . LEU   A 1 764  ? -39.79400  94.15100  -31.97400 1.000 54.22039  ?  764  LEU   A C   1 
ATOM   6075  O  O   . LEU   A 1 764  ? -40.81700  94.76900  -32.29200 1.000 64.29889  ?  764  LEU   A O   1 
ATOM   6076  C  CB  . LEU   A 1 764  ? -40.67000  93.24500  -29.82500 1.000 39.90265  ?  764  LEU   A CB  1 
ATOM   6077  C  CG  . LEU   A 1 764  ? -40.78400  92.15900  -28.75400 1.000 35.87645  ?  764  LEU   A CG  1 
ATOM   6078  C  CD1 . LEU   A 1 764  ? -40.96200  92.78500  -27.38100 1.000 34.07036  ?  764  LEU   A CD1 1 
ATOM   6079  C  CD2 . LEU   A 1 764  ? -41.93000  91.21000  -29.06000 1.000 42.04661  ?  764  LEU   A CD2 1 
ATOM   6080  N  N   . THR   A 1 765  ? -38.57700  94.55200  -32.35500 1.000 55.19104  ?  765  THR   A N   1 
ATOM   6081  C  CA  . THR   A 1 765  ? -38.41800  95.82300  -33.05700 1.000 44.52033  ?  765  THR   A CA  1 
ATOM   6082  C  C   . THR   A 1 765  ? -38.99400  95.77200  -34.46600 1.000 70.27389  ?  765  THR   A C   1 
ATOM   6083  O  O   . THR   A 1 765  ? -39.50000  96.78500  -34.96300 1.000 81.22320  ?  765  THR   A O   1 
ATOM   6084  C  CB  . THR   A 1 765  ? -36.94400  96.23400  -33.10100 1.000 53.19103  ?  765  THR   A CB  1 
ATOM   6085  O  OG1 . THR   A 1 765  ? -36.80300  97.44200  -33.86000 1.000 75.70975  ?  765  THR   A OG1 1 
ATOM   6086  C  CG2 . THR   A 1 765  ? -36.08600  95.13700  -33.72400 1.000 54.00781  ?  765  THR   A CG2 1 
ATOM   6087  N  N   . GLU   A 1 766  ? -38.93500  94.61300  -35.12100 1.000 74.60053  ?  766  GLU   A N   1 
ATOM   6088  C  CA  . GLU   A 1 766  ? -39.46200  94.48500  -36.47200 1.000 76.65991  ?  766  GLU   A CA  1 
ATOM   6089  C  C   . GLU   A 1 766  ? -40.95700  94.20500  -36.49900 1.000 76.64903  ?  766  GLU   A C   1 
ATOM   6090  O  O   . GLU   A 1 766  ? -41.55300  94.22500  -37.58200 1.000 96.54089  ?  766  GLU   A O   1 
ATOM   6091  C  CB  . GLU   A 1 766  ? -38.71900  93.37800  -37.22500 1.000 75.84479  ?  766  GLU   A CB  1 
ATOM   6092  C  CG  . GLU   A 1 766  ? -38.60300  92.07400  -36.45200 1.000 87.28088  ?  766  GLU   A CG  1 
ATOM   6093  C  CD  . GLU   A 1 766  ? -37.18500  91.79500  -35.98900 1.000 88.35242  ?  766  GLU   A CD  1 
ATOM   6094  O  OE1 . GLU   A 1 766  ? -36.39200  92.75500  -35.89000 1.000 79.88162  ?  766  GLU   A OE1 1 
ATOM   6095  O  OE2 . GLU   A 1 766  ? -36.86500  90.61700  -35.72100 1.000 82.26885  -1 766  GLU   A OE2 1 
ATOM   6096  N  N   . GLN   A 1 767  ? -41.57300  93.94700  -35.34900 1.000 79.48955  ?  767  GLN   A N   1 
ATOM   6097  C  CA  . GLN   A 1 767  ? -43.00000  93.67100  -35.30500 1.000 71.78910  ?  767  GLN   A CA  1 
ATOM   6098  C  C   . GLN   A 1 767  ? -43.80600  94.94500  -35.53300 1.000 79.34261  ?  767  GLN   A C   1 
ATOM   6099  O  O   . GLN   A 1 767  ? -43.34800  96.05800  -35.25600 1.000 65.25759  ?  767  GLN   A O   1 
ATOM   6100  C  CB  . GLN   A 1 767  ? -43.38400  93.05200  -33.96300 1.000 64.88259  ?  767  GLN   A CB  1 
ATOM   6101  C  CG  . GLN   A 1 767  ? -43.37500  91.53500  -33.94600 1.000 72.25600  ?  767  GLN   A CG  1 
ATOM   6102  C  CD  . GLN   A 1 767  ? -44.01700  90.97000  -32.69500 1.000 72.12962  ?  767  GLN   A CD  1 
ATOM   6103  O  OE1 . GLN   A 1 767  ? -45.13300  91.34500  -32.33300 1.000 68.74599  ?  767  GLN   A OE1 1 
ATOM   6104  N  NE2 . GLN   A 1 767  ? -43.30700  90.07400  -32.01900 1.000 66.16437  ?  767  GLN   A NE2 1 
ATOM   6105  N  N   . LYS   A 1 768  ? -45.02200  94.76900  -36.04200 1.000 87.15512  ?  768  LYS   A N   1 
ATOM   6106  C  CA  . LYS   A 1 768  ? -45.95000  95.86700  -36.26500 1.000 86.50587  ?  768  LYS   A CA  1 
ATOM   6107  C  C   . LYS   A 1 768  ? -47.10800  95.76800  -35.28100 1.000 82.79870  ?  768  LYS   A C   1 
ATOM   6108  O  O   . LYS   A 1 768  ? -47.60600  94.67300  -35.00100 1.000 83.88310  ?  768  LYS   A O   1 
ATOM   6109  C  CB  . LYS   A 1 768  ? -46.47900  95.86300  -37.70200 1.000 79.03892  ?  768  LYS   A CB  1 
ATOM   6110  C  CG  . LYS   A 1 768  ? -45.77500  96.85600  -38.61200 1.000 89.54194  ?  768  LYS   A CG  1 
ATOM   6111  C  CD  . LYS   A 1 768  ? -45.71300  98.23700  -37.97300 1.000 94.29930  ?  768  LYS   A CD  1 
ATOM   6112  C  CE  . LYS   A 1 768  ? -44.67800  99.12100  -38.65500 1.000 95.51928  ?  768  LYS   A CE  1 
ATOM   6113  N  NZ  . LYS   A 1 768  ? -43.31800  98.94300  -38.06700 1.000 83.13008  ?  768  LYS   A NZ  1 
ATOM   6114  N  N   . GLN   A 1 769  ? -47.52500  96.92100  -34.75600 1.000 82.33709  ?  769  GLN   A N   1 
ATOM   6115  C  CA  . GLN   A 1 769  ? -48.60500  96.98700  -33.77700 1.000 76.33664  ?  769  GLN   A CA  1 
ATOM   6116  C  C   . GLN   A 1 769  ? -49.90200  96.42300  -34.34700 1.000 81.84788  ?  769  GLN   A C   1 
ATOM   6117  O  O   . GLN   A 1 769  ? -50.50000  97.01500  -35.25000 1.000 91.24742  ?  769  GLN   A O   1 
ATOM   6118  C  CB  . GLN   A 1 769  ? -48.81500  98.43100  -33.30700 1.000 74.79866  ?  769  GLN   A CB  1 
ATOM   6119  C  CG  . GLN   A 1 769  ? -47.56500  99.13100  -32.77000 1.000 93.02262  ?  769  GLN   A CG  1 
ATOM   6120  C  CD  . GLN   A 1 769  ? -47.00700  98.48500  -31.51000 1.000 93.94160  ?  769  GLN   A CD  1 
ATOM   6121  O  OE1 . GLN   A 1 769  ? -46.59200  97.32400  -31.52000 1.000 84.51077  ?  769  GLN   A OE1 1 
ATOM   6122  N  NE2 . GLN   A 1 769  ? -46.98000  99.24600  -30.41900 1.000 76.26904  ?  769  GLN   A NE2 1 
ATOM   6123  N  N   . VAL   A 1 770  ? -50.34500  95.28200  -33.82400 1.000 70.09692  ?  770  VAL   A N   1 
ATOM   6124  C  CA  . VAL   A 1 770  ? -51.56200  94.61500  -34.27400 1.000 82.56286  ?  770  VAL   A CA  1 
ATOM   6125  C  C   . VAL   A 1 770  ? -52.63900  94.81300  -33.21400 1.000 83.89319  ?  770  VAL   A C   1 
ATOM   6126  O  O   . VAL   A 1 770  ? -52.40600  94.55300  -32.02700 1.000 91.71075  ?  770  VAL   A O   1 
ATOM   6127  C  CB  . VAL   A 1 770  ? -51.31300  93.12100  -34.54700 1.000 72.47262  ?  770  VAL   A CB  1 
ATOM   6128  C  CG1 . VAL   A 1 770  ? -52.61200  92.32800  -34.46400 1.000 67.15860  ?  770  VAL   A CG1 1 
ATOM   6129  C  CG2 . VAL   A 1 770  ? -50.65200  92.93800  -35.90700 1.000 77.52663  ?  770  VAL   A CG2 1 
ATOM   6130  N  N   . ASN   A 1 771  A -53.81000  95.28000  -33.64100 1.000 81.57241  ?  770  ASN   A N   1 
ATOM   6131  C  CA  . ASN   A 1 771  A -54.92400  95.52000  -32.73700 1.000 85.80412  ?  770  ASN   A CA  1 
ATOM   6132  C  C   . ASN   A 1 771  A -55.80400  94.28100  -32.62500 1.000 80.17804  ?  770  ASN   A C   1 
ATOM   6133  O  O   . ASN   A 1 771  A -55.93800  93.50000  -33.57100 1.000 80.88168  ?  770  ASN   A O   1 
ATOM   6134  C  CB  . ASN   A 1 771  A -55.76300  96.70900  -33.21100 1.000 76.75740  ?  770  ASN   A CB  1 
ATOM   6135  C  CG  . ASN   A 1 771  A -54.93300  97.77200  -33.90500 1.000 86.51470  ?  770  ASN   A CG  1 
ATOM   6136  O  OD1 . ASN   A 1 771  A -54.14100  98.47000  -33.27100 1.000 92.66747  ?  770  ASN   A OD1 1 
ATOM   6137  N  ND2 . ASN   A 1 771  A -55.11600  97.90500  -35.21300 1.000 86.41665  ?  770  ASN   A ND2 1 
ATOM   6138  N  N   . GLY   A 1 772  B -56.40700  94.10900  -31.44900 1.000 76.30154  ?  770  GLY   A N   1 
ATOM   6139  C  CA  . GLY   A 1 772  B -57.30900  93.00500  -31.19600 1.000 83.87681  ?  770  GLY   A CA  1 
ATOM   6140  C  C   . GLY   A 1 772  B -56.68500  91.79700  -30.53300 1.000 83.23274  ?  770  GLY   A C   1 
ATOM   6141  O  O   . GLY   A 1 772  B -57.37400  90.78300  -30.36400 1.000 80.47985  ?  770  GLY   A O   1 
ATOM   6142  N  N   . LEU   A 1 773  ? -55.40700  91.86900  -30.15500 1.000 86.87622  ?  771  LEU   A N   1 
ATOM   6143  C  CA  . LEU   A 1 773  ? -54.76400  90.72600  -29.51700 1.000 81.81933  ?  771  LEU   A CA  1 
ATOM   6144  C  C   . LEU   A 1 773  ? -55.38300  90.41900  -28.16100 1.000 80.87684  ?  771  LEU   A C   1 
ATOM   6145  O  O   . LEU   A 1 773  ? -55.42500  89.25400  -27.74800 1.000 95.22098  ?  771  LEU   A O   1 
ATOM   6146  C  CB  . LEU   A 1 773  ? -53.26400  90.98200  -29.37300 1.000 76.92360  ?  771  LEU   A CB  1 
ATOM   6147  C  CG  . LEU   A 1 773  ? -52.47200  91.15700  -30.66900 1.000 63.35782  ?  771  LEU   A CG  1 
ATOM   6148  C  CD1 . LEU   A 1 773  ? -50.99900  91.35300  -30.36100 1.000 61.59190  ?  771  LEU   A CD1 1 
ATOM   6149  C  CD2 . LEU   A 1 773  ? -52.67400  89.95800  -31.57900 1.000 61.66977  ?  771  LEU   A CD2 1 
ATOM   6150  N  N   . LEU   A 1 774  ? -55.87300  91.44000  -27.46100 1.000 85.01260  ?  772  LEU   A N   1 
ATOM   6151  C  CA  . LEU   A 1 774  ? -56.48800  91.28200  -26.14400 1.000 89.21662  ?  772  LEU   A CA  1 
ATOM   6152  C  C   . LEU   A 1 774  ? -57.93600  91.75600  -26.23500 1.000 85.10617  ?  772  LEU   A C   1 
ATOM   6153  O  O   . LEU   A 1 774  ? -58.20700  92.96100  -26.28400 1.000 87.10679  ?  772  LEU   A O   1 
ATOM   6154  C  CB  . LEU   A 1 774  ? -55.69800  92.04100  -25.07700 1.000 74.79313  ?  772  LEU   A CB  1 
ATOM   6155  C  CG  . LEU   A 1 774  ? -55.82300  91.48600  -23.65400 1.000 93.95224  ?  772  LEU   A CG  1 
ATOM   6156  C  CD1 . LEU   A 1 774  ? -54.59300  91.82300  -22.81900 1.000 63.65529  ?  772  LEU   A CD1 1 
ATOM   6157  C  CD2 . LEU   A 1 774  ? -57.09200  92.01000  -22.97400 1.000 96.07986  ?  772  LEU   A CD2 1 
ATOM   6158  N  N   . GLU   A 1 775  ? -58.86800  90.79600  -26.26000 1.000 78.79392  ?  773  GLU   A N   1 
ATOM   6159  C  CA  . GLU   A 1 775  ? -60.29200  91.07000  -26.39500 1.000 69.38756  ?  773  GLU   A CA  1 
ATOM   6160  C  C   . GLU   A 1 775  ? -60.98200  90.91900  -25.05100 1.000 72.61181  ?  773  GLU   A C   1 
ATOM   6161  O  O   . GLU   A 1 775  ? -60.74900  89.92000  -24.35400 1.000 83.56293  ?  773  GLU   A O   1 
ATOM   6162  C  CB  . GLU   A 1 775  ? -60.92200  90.12600  -27.41300 1.000 72.81367  ?  773  GLU   A CB  1 
ATOM   6163  C  CG  . GLU   A 1 775  ? -60.03100  88.95300  -27.79300 1.000 83.66653  ?  773  GLU   A CG  1 
ATOM   6164  C  CD  . GLU   A 1 775  ? -60.79800  87.84200  -28.47700 1.000 104.96287 ?  773  GLU   A CD  1 
ATOM   6165  O  OE1 . GLU   A 1 775  ? -61.30700  86.94800  -27.76900 1.000 89.78711  ?  773  GLU   A OE1 1 
ATOM   6166  O  OE2 . GLU   A 1 775  ? -60.90100  87.87000  -29.72300 1.000 109.44872 -1 773  GLU   A OE2 1 
ATOM   6167  N  N   . PRO   A 1 776  ? -61.82000  91.87700  -24.65900 1.000 72.20205  ?  774  PRO   A N   1 
ATOM   6168  C  CA  . PRO   A 1 776  ? -62.45900  91.80700  -23.34300 1.000 60.45868  ?  774  PRO   A CA  1 
ATOM   6169  C  C   . PRO   A 1 776  ? -63.32500  90.56900  -23.19500 1.000 71.72426  ?  774  PRO   A C   1 
ATOM   6170  O  O   . PRO   A 1 776  ? -63.83000  90.01200  -24.17200 1.000 79.63324  ?  774  PRO   A O   1 
ATOM   6171  C  CB  . PRO   A 1 776  ? -63.30500  93.08100  -23.30900 1.000 62.42192  ?  774  PRO   A CB  1 
ATOM   6172  C  CG  . PRO   A 1 776  ? -62.50400  94.03000  -24.13400 1.000 70.27639  ?  774  PRO   A CG  1 
ATOM   6173  C  CD  . PRO   A 1 776  ? -62.09800  93.16800  -25.30700 1.000 74.21838  ?  774  PRO   A CD  1 
ATOM   6174  N  N   . LEU   A 1 777  ? -63.49200  90.14400  -21.94500 1.000 67.55240  ?  775  LEU   A N   1 
ATOM   6175  C  CA  . LEU   A 1 777  ? -64.38100  89.03800  -21.61600 1.000 70.90686  ?  775  LEU   A CA  1 
ATOM   6176  C  C   . LEU   A 1 777  ? -65.81900  89.54300  -21.64000 1.000 67.71837  ?  775  LEU   A C   1 
ATOM   6177  O  O   . LEU   A 1 777  ? -66.17900  90.44200  -20.87300 1.000 68.14946  ?  775  LEU   A O   1 
ATOM   6178  C  CB  . LEU   A 1 777  ? -64.02700  88.46800  -20.24500 1.000 62.80645  ?  775  LEU   A CB  1 
ATOM   6179  C  CG  . LEU   A 1 777  ? -64.17000  86.95900  -20.02600 1.000 58.36295  ?  775  LEU   A CG  1 
ATOM   6180  C  CD1 . LEU   A 1 777  ? -63.72800  86.57900  -18.61900 1.000 67.92913  ?  775  LEU   A CD1 1 
ATOM   6181  C  CD2 . LEU   A 1 777  ? -65.58000  86.47300  -20.30200 1.000 58.90470  ?  775  LEU   A CD2 1 
ATOM   6182  N  N   . ARG   A 1 778  ? -66.63900  88.97500  -22.52100 1.000 60.03679  ?  776  ARG   A N   1 
ATOM   6183  C  CA  . ARG   A 1 778  ? -68.01200  89.43800  -22.69000 1.000 78.44321  ?  776  ARG   A CA  1 
ATOM   6184  C  C   . ARG   A 1 778  ? -68.86800  88.95400  -21.52600 1.000 70.18801  ?  776  ARG   A C   1 
ATOM   6185  O  O   . ARG   A 1 778  ? -68.93400  87.75000  -21.25400 1.000 77.73048  ?  776  ARG   A O   1 
ATOM   6186  C  CB  . ARG   A 1 778  ? -68.58000  88.94600  -24.01900 1.000 75.60345  ?  776  ARG   A CB  1 
ATOM   6187  N  N   . GLU   A 1 779  ? -69.52200  89.89000  -20.84300 1.000 53.65683  ?  777  GLU   A N   1 
ATOM   6188  C  CA  . GLU   A 1 779  ? -70.39600  89.54100  -19.73100 1.000 72.20321  ?  777  GLU   A CA  1 
ATOM   6189  C  C   . GLU   A 1 779  ? -71.66400  88.88000  -20.25800 1.000 70.83934  ?  777  GLU   A C   1 
ATOM   6190  O  O   . GLU   A 1 779  ? -72.41800  89.49000  -21.02400 1.000 70.11636  ?  777  GLU   A O   1 
ATOM   6191  C  CB  . GLU   A 1 779  ? -70.73500  90.78400  -18.91300 1.000 64.90106  ?  777  GLU   A CB  1 
ATOM   6192  C  CG  . GLU   A 1 779  ? -69.93100  90.93000  -17.62200 1.000 80.70779  ?  777  GLU   A CG  1 
ATOM   6193  C  CD  . GLU   A 1 779  ? -69.47300  89.59700  -17.05200 1.000 86.13437  ?  777  GLU   A CD  1 
ATOM   6194  O  OE1 . GLU   A 1 779  ? -70.32500  88.84100  -16.53500 1.000 68.80574  ?  777  GLU   A OE1 1 
ATOM   6195  O  OE2 . GLU   A 1 779  ? -68.25900  89.30400  -17.12300 1.000 74.41569  -1 777  GLU   A OE2 1 
ATOM   6196  N  N   . LEU   A 1 780  ? -71.89500  87.63300  -19.85100 1.000 66.79487  ?  778  LEU   A N   1 
ATOM   6197  C  CA  . LEU   A 1 780  ? -73.06200  86.89600  -20.31600 1.000 63.72553  ?  778  LEU   A CA  1 
ATOM   6198  C  C   . LEU   A 1 780  ? -74.35000  87.57500  -19.86100 1.000 70.77524  ?  778  LEU   A C   1 
ATOM   6199  O  O   . LEU   A 1 780  ? -74.38700  88.27900  -18.84800 1.000 73.00915  ?  778  LEU   A O   1 
ATOM   6200  C  CB  . LEU   A 1 780  ? -73.02400  85.45700  -19.79900 1.000 57.07762  ?  778  LEU   A CB  1 
ATOM   6201  C  CG  . LEU   A 1 780  ? -72.42600  84.38800  -20.71600 1.000 62.97684  ?  778  LEU   A CG  1 
ATOM   6202  C  CD1 . LEU   A 1 780  ? -72.76500  83.00000  -20.19100 1.000 61.24740  ?  778  LEU   A CD1 1 
ATOM   6203  C  CD2 . LEU   A 1 780  ? -72.91400  84.55900  -22.14700 1.000 76.12566  ?  778  LEU   A CD2 1 
ATOM   6204  N  N   . ASP   A 1 781  ? -75.41400  87.36100  -20.62700 1.000 74.70581  ?  779  ASP   A N   1 
ATOM   6205  C  CA  . ASP   A 1 781  ? -76.72400  87.88100  -20.27200 1.000 73.26177  ?  779  ASP   A CA  1 
ATOM   6206  C  C   . ASP   A 1 781  ? -77.44900  86.90400  -19.35200 1.000 71.29069  ?  779  ASP   A C   1 
ATOM   6207  O  O   . ASP   A 1 781  ? -77.09100  85.73000  -19.24700 1.000 83.91031  ?  779  ASP   A O   1 
ATOM   6208  C  CB  . ASP   A 1 781  ? -77.56000  88.15100  -21.52200 1.000 82.88837  ?  779  ASP   A CB  1 
ATOM   6209  C  CG  . ASP   A 1 781  ? -77.31500  89.53000  -22.09300 1.000 102.34500 ?  779  ASP   A CG  1 
ATOM   6210  O  OD1 . ASP   A 1 781  ? -77.29200  90.50000  -21.30600 1.000 97.88694  ?  779  ASP   A OD1 1 
ATOM   6211  O  OD2 . ASP   A 1 781  ? -77.14400  89.64400  -23.32500 1.000 109.10101 -1 779  ASP   A OD2 1 
ATOM   6212  N  N   . GLU   A 1 782  ? -78.48500  87.40900  -18.68700 1.000 72.00051  ?  780  GLU   A N   1 
ATOM   6213  C  CA  . GLU   A 1 782  ? -79.17000  86.63500  -17.65900 1.000 69.52865  ?  780  GLU   A CA  1 
ATOM   6214  C  C   . GLU   A 1 782  ? -79.88600  85.43200  -18.26400 1.000 62.47617  ?  780  GLU   A C   1 
ATOM   6215  O  O   . GLU   A 1 782  ? -80.62500  85.56100  -19.24500 1.000 72.35240  ?  780  GLU   A O   1 
ATOM   6216  C  CB  . GLU   A 1 782  ? -80.16500  87.51700  -16.90900 1.000 55.73486  ?  780  GLU   A CB  1 
ATOM   6217  C  CG  . GLU   A 1 782  ? -80.30700  87.17900  -15.43300 1.000 76.44627  ?  780  GLU   A CG  1 
ATOM   6218  C  CD  . GLU   A 1 782  ? -80.75900  88.36700  -14.60500 1.000 99.00804  ?  780  GLU   A CD  1 
ATOM   6219  O  OE1 . GLU   A 1 782  ? -81.70600  89.06300  -15.02800 1.000 96.45232  ?  780  GLU   A OE1 1 
ATOM   6220  O  OE2 . GLU   A 1 782  ? -80.16200  88.61100  -13.53600 1.000 98.16676  -1 780  GLU   A OE2 1 
ATOM   6221  N  N   . GLN   A 1 783  ? -79.65800  84.26000  -17.67600 1.000 52.18157  ?  781  GLN   A N   1 
ATOM   6222  C  CA  . GLN   A 1 783  ? -80.32500  83.02600  -18.06500 1.000 67.23437  ?  781  GLN   A CA  1 
ATOM   6223  C  C   . GLN   A 1 783  ? -80.83700  82.32400  -16.81600 1.000 59.05210  ?  781  GLN   A C   1 
ATOM   6224  O  O   . GLN   A 1 783  ? -80.53200  82.71400  -15.68600 1.000 63.76281  ?  781  GLN   A O   1 
ATOM   6225  C  CB  . GLN   A 1 783  ? -79.38800  82.08500  -18.83800 1.000 72.26709  ?  781  GLN   A CB  1 
ATOM   6226  C  CG  . GLN   A 1 783  ? -78.25900  82.77800  -19.58200 1.000 86.79062  ?  781  GLN   A CG  1 
ATOM   6227  C  CD  . GLN   A 1 783  ? -77.77000  81.98300  -20.77700 1.000 90.61069  ?  781  GLN   A CD  1 
ATOM   6228  O  OE1 . GLN   A 1 783  ? -78.55200  81.32400  -21.46300 1.000 107.70019 ?  781  GLN   A OE1 1 
ATOM   6229  N  NE2 . GLN   A 1 783  ? -76.46700  82.04100  -21.03200 1.000 77.47255  ?  781  GLN   A NE2 1 
ATOM   6230  N  N   . ALA   A 1 784  ? -81.62400  81.27100  -17.02900 1.000 53.42012  ?  782  ALA   A N   1 
ATOM   6231  C  CA  . ALA   A 1 784  ? -82.00500  80.41100  -15.91600 1.000 59.55606  ?  782  ALA   A CA  1 
ATOM   6232  C  C   . ALA   A 1 784  ? -80.80600  79.60300  -15.43900 1.000 61.95457  ?  782  ALA   A C   1 
ATOM   6233  O  O   . ALA   A 1 784  ? -80.42900  79.65400  -14.26300 1.000 62.29029  ?  782  ALA   A O   1 
ATOM   6234  C  CB  . ALA   A 1 784  ? -83.15600  79.49100  -16.32900 1.000 40.70923  ?  782  ALA   A CB  1 
ATOM   6235  N  N   . GLU   A 1 785  ? -80.18100  78.86900  -16.35400 1.000 63.85168  ?  783  GLU   A N   1 
ATOM   6236  C  CA  . GLU   A 1 785  ? -78.98100  78.09900  -16.07900 1.000 54.83251  ?  783  GLU   A CA  1 
ATOM   6237  C  C   . GLU   A 1 785  ? -77.85500  78.56500  -16.99000 1.000 57.22829  ?  783  GLU   A C   1 
ATOM   6238  O  O   . GLU   A 1 785  ? -78.08100  78.94300  -18.14300 1.000 68.83493  ?  783  GLU   A O   1 
ATOM   6239  C  CB  . GLU   A 1 785  ? -79.22400  76.60200  -16.28100 1.000 51.07244  ?  783  GLU   A CB  1 
ATOM   6240  C  CG  . GLU   A 1 785  ? -80.42900  76.06600  -15.53200 1.000 57.83811  ?  783  GLU   A CG  1 
ATOM   6241  C  CD  . GLU   A 1 785  ? -80.83900  74.69300  -16.01700 1.000 73.63720  ?  783  GLU   A CD  1 
ATOM   6242  O  OE1 . GLU   A 1 785  ? -80.66200  74.41600  -17.22100 1.000 65.20667  ?  783  GLU   A OE1 1 
ATOM   6243  O  OE2 . GLU   A 1 785  ? -81.33800  73.89100  -15.19700 1.000 76.45782  -1 783  GLU   A OE2 1 
ATOM   6244  N  N   . TYR   A 1 786  ? -76.63700  78.53400  -16.46400 1.000 58.35503  ?  784  TYR   A N   1 
ATOM   6245  C  CA  . TYR   A 1 786  ? -75.45500  78.93600  -17.20700 1.000 50.03969  ?  784  TYR   A CA  1 
ATOM   6246  C  C   . TYR   A 1 786  ? -74.57700  77.72400  -17.49200 1.000 57.80253  ?  784  TYR   A C   1 
ATOM   6247  O  O   . TYR   A 1 786  ? -74.81900  76.61600  -17.00400 1.000 53.96238  ?  784  TYR   A O   1 
ATOM   6248  C  CB  . TYR   A 1 786  ? -74.66600  80.00200  -16.44100 1.000 43.41280  ?  784  TYR   A CB  1 
ATOM   6249  C  CG  . TYR   A 1 786  ? -75.43500  81.27700  -16.18200 1.000 53.49174  ?  784  TYR   A CG  1 
ATOM   6250  C  CD1 . TYR   A 1 786  ? -76.38200  81.34800  -15.16800 1.000 60.02929  ?  784  TYR   A CD1 1 
ATOM   6251  C  CD2 . TYR   A 1 786  ? -75.21000  82.41200  -16.94800 1.000 67.39483  ?  784  TYR   A CD2 1 
ATOM   6252  C  CE1 . TYR   A 1 786  ? -77.08300  82.51300  -14.92500 1.000 67.29726  ?  784  TYR   A CE1 1 
ATOM   6253  C  CE2 . TYR   A 1 786  ? -75.90800  83.58200  -16.71400 1.000 73.72258  ?  784  TYR   A CE2 1 
ATOM   6254  C  CZ  . TYR   A 1 786  ? -76.84200  83.62700  -15.70000 1.000 66.64359  ?  784  TYR   A CZ  1 
ATOM   6255  O  OH  . TYR   A 1 786  ? -77.54200  84.78600  -15.45600 1.000 75.18611  ?  784  TYR   A OH  1 
ATOM   6256  N  N   . GLU   A 1 787  ? -73.54700  77.95100  -18.29900 1.000 64.74862  ?  785  GLU   A N   1 
ATOM   6257  C  CA  . GLU   A 1 787  ? -72.63700  76.88500  -18.68600 1.000 57.38646  ?  785  GLU   A CA  1 
ATOM   6258  C  C   . GLU   A 1 787  ? -71.56000  76.67900  -17.62900 1.000 57.88904  ?  785  GLU   A C   1 
ATOM   6259  O  O   . GLU   A 1 787  ? -71.14500  77.61500  -16.94000 1.000 64.50002  ?  785  GLU   A O   1 
ATOM   6260  C  CB  . GLU   A 1 787  ? -71.98100  77.20100  -20.03000 1.000 73.98011  ?  785  GLU   A CB  1 
ATOM   6261  C  CG  . GLU   A 1 787  ? -72.62700  76.51800  -21.22000 1.000 80.35950  ?  785  GLU   A CG  1 
ATOM   6262  C  CD  . GLU   A 1 787  ? -71.85700  76.75000  -22.50700 1.000 78.09577  ?  785  GLU   A CD  1 
ATOM   6263  O  OE1 . GLU   A 1 787  ? -70.83800  77.47100  -22.47300 1.000 68.05119  ?  785  GLU   A OE1 1 
ATOM   6264  O  OE2 . GLU   A 1 787  ? -72.26700  76.20500  -23.55300 1.000 92.52979  -1 785  GLU   A OE2 1 
ATOM   6265  N  N   . THR   A 1 788  ? -71.10400  75.43700  -17.51100 1.000 43.83032  ?  786  THR   A N   1 
ATOM   6266  C  CA  . THR   A 1 788  ? -70.01600  75.09600  -16.60800 1.000 44.57411  ?  786  THR   A CA  1 
ATOM   6267  C  C   . THR   A 1 788  ? -68.71400  74.94100  -17.38300 1.000 52.23259  ?  786  THR   A C   1 
ATOM   6268  O  O   . THR   A 1 788  ? -68.70500  74.65000  -18.58200 1.000 56.41582  ?  786  THR   A O   1 
ATOM   6269  C  CB  . THR   A 1 788  ? -70.31100  73.80300  -15.84600 1.000 42.82918  ?  786  THR   A CB  1 
ATOM   6270  O  OG1 . THR   A 1 788  ? -70.77900  72.80400  -16.76000 1.000 53.47204  ?  786  THR   A OG1 1 
ATOM   6271  C  CG2 . THR   A 1 788  ? -71.36100  74.04500  -14.77300 1.000 49.92180  ?  786  THR   A CG2 1 
ATOM   6272  N  N   . SER   A 1 789  ? -67.60600  75.12900  -16.67200 1.000 49.51150  ?  787  SER   A N   1 
ATOM   6273  C  CA  . SER   A 1 789  ? -66.28800  74.99100  -17.26700 1.000 40.48387  ?  787  SER   A CA  1 
ATOM   6274  C  C   . SER   A 1 789  ? -65.88400  73.51800  -17.31800 1.000 49.16148  ?  787  SER   A C   1 
ATOM   6275  O  O   . SER   A 1 789  ? -66.59000  72.63100  -16.82800 1.000 43.60439  ?  787  SER   A O   1 
ATOM   6276  C  CB  . SER   A 1 789  ? -65.26600  75.82100  -16.49100 1.000 48.55841  ?  787  SER   A CB  1 
ATOM   6277  O  OG  . SER   A 1 789  ? -64.94500  75.22100  -15.24600 1.000 46.25647  ?  787  SER   A OG  1 
ATOM   6278  N  N   . ALA   A 1 790  ? -64.72500  73.25200  -17.92700 1.000 56.56186  ?  788  ALA   A N   1 
ATOM   6279  C  CA  . ALA   A 1 790  ? -64.24300  71.87800  -18.02900 1.000 46.88730  ?  788  ALA   A CA  1 
ATOM   6280  C  C   . ALA   A 1 790  ? -63.76500  71.35500  -16.67900 1.000 44.74000  ?  788  ALA   A C   1 
ATOM   6281  O  O   . ALA   A 1 790  ? -63.97000  70.17800  -16.35700 1.000 39.03653  ?  788  ALA   A O   1 
ATOM   6282  C  CB  . ALA   A 1 790  ? -63.12800  71.79000  -19.07000 1.000 46.71250  ?  788  ALA   A CB  1 
ATOM   6283  N  N   . VAL   A 1 791  ? -63.12800  72.21200  -15.87500 1.000 32.57744  ?  789  VAL   A N   1 
ATOM   6284  C  CA  . VAL   A 1 791  ? -62.71700  71.80100  -14.53400 1.000 45.72256  ?  789  VAL   A CA  1 
ATOM   6285  C  C   . VAL   A 1 791  ? -63.93300  71.58400  -13.64400 1.000 45.43350  ?  789  VAL   A C   1 
ATOM   6286  O  O   . VAL   A 1 791  ? -63.97800  70.63100  -12.85500 1.000 48.71712  ?  789  VAL   A O   1 
ATOM   6287  C  CB  . VAL   A 1 791  ? -61.75700  72.83200  -13.91400 1.000 28.39286  ?  789  VAL   A CB  1 
ATOM   6288  C  CG1 . VAL   A 1 791  ? -60.39000  72.21600  -13.70800 1.000 31.42184  ?  789  VAL   A CG1 1 
ATOM   6289  C  CG2 . VAL   A 1 791  ? -61.67700  74.08300  -14.77300 1.000 46.72894  ?  789  VAL   A CG2 1 
ATOM   6290  N  N   . GLU   A 1 792  ? -64.92700  72.47200  -13.73900 1.000 44.71263  ?  790  GLU   A N   1 
ATOM   6291  C  CA  . GLU   A 1 792  ? -66.13500  72.32200  -12.93500 1.000 40.16730  ?  790  GLU   A CA  1 
ATOM   6292  C  C   . GLU   A 1 792  ? -66.85300  71.02100  -13.26400 1.000 35.06745  ?  790  GLU   A C   1 
ATOM   6293  O  O   . GLU   A 1 792  ? -67.36700  70.34200  -12.36700 1.000 48.12638  ?  790  GLU   A O   1 
ATOM   6294  C  CB  . GLU   A 1 792  ? -67.06000  73.52100  -13.14500 1.000 32.37113  ?  790  GLU   A CB  1 
ATOM   6295  C  CG  . GLU   A 1 792  ? -66.56400  74.79100  -12.47300 1.000 51.38927  ?  790  GLU   A CG  1 
ATOM   6296  C  CD  . GLU   A 1 792  ? -67.55400  75.93500  -12.56000 1.000 55.10485  ?  790  GLU   A CD  1 
ATOM   6297  O  OE1 . GLU   A 1 792  ? -68.33800  75.97700  -13.53200 1.000 49.49421  ?  790  GLU   A OE1 1 
ATOM   6298  O  OE2 . GLU   A 1 792  ? -67.54400  76.79700  -11.65500 1.000 66.27452  -1 790  GLU   A OE2 1 
ATOM   6299  N  N   . LYS   A 1 793  ? -66.89000  70.65200  -14.54600 1.000 33.63528  ?  791  LYS   A N   1 
ATOM   6300  C  CA  . LYS   A 1 793  ? -67.47100  69.36700  -14.91900 1.000 39.25269  ?  791  LYS   A CA  1 
ATOM   6301  C  C   . LYS   A 1 793  ? -66.67100  68.21300  -14.32900 1.000 41.44706  ?  791  LYS   A C   1 
ATOM   6302  O  O   . LYS   A 1 793  ? -67.24800  67.24300  -13.82500 1.000 50.30199  ?  791  LYS   A O   1 
ATOM   6303  C  CB  . LYS   A 1 793  ? -67.55300  69.24900  -16.44100 1.000 39.11272  ?  791  LYS   A CB  1 
ATOM   6304  C  CG  . LYS   A 1 793  ? -68.58200  70.16900  -17.07900 1.000 55.71498  ?  791  LYS   A CG  1 
ATOM   6305  C  CD  . LYS   A 1 793  ? -68.66000  69.95000  -18.58200 1.000 52.63926  ?  791  LYS   A CD  1 
ATOM   6306  C  CE  . LYS   A 1 793  ? -69.73000  70.82300  -19.21700 1.000 45.68894  ?  791  LYS   A CE  1 
ATOM   6307  N  NZ  . LYS   A 1 793  ? -69.33900  72.26100  -19.19300 1.000 42.41415  ?  791  LYS   A NZ  1 
ATOM   6308  N  N   . ARG   A 1 794  ? -65.34000  68.30500  -14.37600 1.000 40.26012  ?  792  ARG   A N   1 
ATOM   6309  C  CA  . ARG   A 1 794  ? -64.49900  67.27200  -13.77800 1.000 45.52032  ?  792  ARG   A CA  1 
ATOM   6310  C  C   . ARG   A 1 794  ? -64.75500  67.15900  -12.28200 1.000 51.10251  ?  792  ARG   A C   1 
ATOM   6311  O  O   . ARG   A 1 794  ? -65.02700  66.06900  -11.76800 1.000 54.82228  ?  792  ARG   A O   1 
ATOM   6312  C  CB  . ARG   A 1 794  ? -63.02600  67.57900  -14.04200 1.000 53.88214  ?  792  ARG   A CB  1 
ATOM   6313  C  CG  . ARG   A 1 794  ? -62.48800  66.97900  -15.32100 1.000 76.73642  ?  792  ARG   A CG  1 
ATOM   6314  C  CD  . ARG   A 1 794  ? -61.12800  66.33600  -15.10700 1.000 78.25424  ?  792  ARG   A CD  1 
ATOM   6315  N  NE  . ARG   A 1 794  ? -60.22600  67.14300  -14.29000 1.000 67.77541  ?  792  ARG   A NE  1 
ATOM   6316  C  CZ  . ARG   A 1 794  ? -59.66400  68.28100  -14.67700 1.000 86.94836  ?  792  ARG   A CZ  1 
ATOM   6317  N  NH1 . ARG   A 1 794  ? -59.90200  68.80300  -15.87100 1.000 81.74197  ?  792  ARG   A NH1 1 
ATOM   6318  N  NH2 . ARG   A 1 794  ? -58.83800  68.91100  -13.84600 1.000 76.75421  ?  792  ARG   A NH2 1 
ATOM   6319  N  N   . MET   A 1 795  ? -64.66800  68.28500  -11.56800 1.000 43.00231  ?  793  MET   A N   1 
ATOM   6320  C  CA  . MET   A 1 795  ? -64.87800  68.27800  -10.12300 1.000 40.95058  ?  793  MET   A CA  1 
ATOM   6321  C  C   . MET   A 1 795  ? -66.24200  67.70400  -9.76700  1.000 48.30286  ?  793  MET   A C   1 
ATOM   6322  O  O   . MET   A 1 795  ? -66.36600  66.92500  -8.81500  1.000 54.80256  ?  793  MET   A O   1 
ATOM   6323  C  CB  . MET   A 1 795  ? -64.73300  69.69500  -9.56800  1.000 39.34387  ?  793  MET   A CB  1 
ATOM   6324  C  CG  . MET   A 1 795  ? -63.30500  70.22400  -9.54100  1.000 54.21978  ?  793  MET   A CG  1 
ATOM   6325  S  SD  . MET   A 1 795  ? -62.16700  69.18200  -8.60500  1.000 60.38874  ?  793  MET   A SD  1 
ATOM   6326  C  CE  . MET   A 1 795  ? -61.13800  68.52300  -9.91600  1.000 47.71653  ?  793  MET   A CE  1 
ATOM   6327  N  N   . TYR   A 1 796  ? -67.27800  68.08500  -10.52000 1.000 47.58538  ?  794  TYR   A N   1 
ATOM   6328  C  CA  . TYR   A 1 796  ? -68.60400  67.50600  -10.32500 1.000 42.52001  ?  794  TYR   A CA  1 
ATOM   6329  C  C   . TYR   A 1 796  ? -68.55700  65.98800  -10.44700 1.000 51.28188  ?  794  TYR   A C   1 
ATOM   6330  O  O   . TYR   A 1 796  ? -69.03500  65.26600  -9.56500  1.000 51.02637  ?  794  TYR   A O   1 
ATOM   6331  C  CB  . TYR   A 1 796  ? -69.58000  68.10000  -11.34300 1.000 39.75220  ?  794  TYR   A CB  1 
ATOM   6332  C  CG  . TYR   A 1 796  ? -71.04100  67.80700  -11.07100 1.000 45.81463  ?  794  TYR   A CG  1 
ATOM   6333  C  CD1 . TYR   A 1 796  ? -71.61800  66.60900  -11.47900 1.000 38.74056  ?  794  TYR   A CD1 1 
ATOM   6334  C  CD2 . TYR   A 1 796  ? -71.85000  68.74000  -10.43400 1.000 39.88363  ?  794  TYR   A CD2 1 
ATOM   6335  C  CE1 . TYR   A 1 796  ? -72.95300  66.34000  -11.23900 1.000 42.01849  ?  794  TYR   A CE1 1 
ATOM   6336  C  CE2 . TYR   A 1 796  ? -73.18700  68.48100  -10.19300 1.000 49.26867  ?  794  TYR   A CE2 1 
ATOM   6337  C  CZ  . TYR   A 1 796  ? -73.73400  67.28000  -10.59700 1.000 59.31812  ?  794  TYR   A CZ  1 
ATOM   6338  O  OH  . TYR   A 1 796  ? -75.06700  67.02000  -10.35700 1.000 62.23462  ?  794  TYR   A OH  1 
ATOM   6339  N  N   . ILE   A 1 797  ? -67.96000  65.48900  -11.53200 1.000 44.01212  ?  795  ILE   A N   1 
ATOM   6340  C  CA  . ILE   A 1 797  ? -67.87800  64.05000  -11.76600 1.000 43.39945  ?  795  ILE   A CA  1 
ATOM   6341  C  C   . ILE   A 1 797  ? -67.11200  63.36100  -10.64300 1.000 51.50542  ?  795  ILE   A C   1 
ATOM   6342  O  O   . ILE   A 1 797  ? -67.44600  62.23900  -10.24100 1.000 58.48272  ?  795  ILE   A O   1 
ATOM   6343  C  CB  . ILE   A 1 797  ? -67.24200  63.78700  -13.14400 1.000 49.71213  ?  795  ILE   A CB  1 
ATOM   6344  C  CG1 . ILE   A 1 797  ? -68.21700  64.19800  -14.24600 1.000 51.47165  ?  795  ILE   A CG1 1 
ATOM   6345  C  CG2 . ILE   A 1 797  ? -66.84000  62.32800  -13.29900 1.000 68.15390  ?  795  ILE   A CG2 1 
ATOM   6346  C  CD1 . ILE   A 1 797  ? -67.61600  64.19700  -15.61800 1.000 61.73288  ?  795  ILE   A CD1 1 
ATOM   6347  N  N   . ILE   A 1 798  ? -66.08300  64.02500  -10.10900 1.000 55.67428  ?  796  ILE   A N   1 
ATOM   6348  C  CA  . ILE   A 1 798  ? -65.31700  63.45100  -9.00300  1.000 48.72376  ?  796  ILE   A CA  1 
ATOM   6349  C  C   . ILE   A 1 798  ? -66.20500  63.26500  -7.77800  1.000 52.87542  ?  796  ILE   A C   1 
ATOM   6350  O  O   . ILE   A 1 798  ? -66.28500  62.17100  -7.20600  1.000 45.45836  ?  796  ILE   A O   1 
ATOM   6351  C  CB  . ILE   A 1 798  ? -64.09700  64.33100  -8.67800  1.000 51.63808  ?  796  ILE   A CB  1 
ATOM   6352  C  CG1 . ILE   A 1 798  ? -63.19300  64.48100  -9.90300  1.000 52.14778  ?  796  ILE   A CG1 1 
ATOM   6353  C  CG2 . ILE   A 1 798  ? -63.33800  63.75500  -7.49900  1.000 57.33554  ?  796  ILE   A CG2 1 
ATOM   6354  C  CD1 . ILE   A 1 798  ? -62.11300  63.43200  -10.00600 1.000 51.65408  ?  796  ILE   A CD1 1 
ATOM   6355  N  N   . GLN   A 1 799  ? -66.89000  64.33300  -7.36000  1.000 52.77810  ?  797  GLN   A N   1 
ATOM   6356  C  CA  . GLN   A 1 799  ? -67.75600  64.27300  -6.18800  1.000 50.35839  ?  797  GLN   A CA  1 
ATOM   6357  C  C   . GLN   A 1 799  ? -68.94900  63.34600  -6.38300  1.000 47.36054  ?  797  GLN   A C   1 
ATOM   6358  O  O   . GLN   A 1 799  ? -69.67200  63.08700  -5.41500  1.000 58.68942  ?  797  GLN   A O   1 
ATOM   6359  C  CB  . GLN   A 1 799  ? -68.23600  65.68400  -5.82200  1.000 39.25456  ?  797  GLN   A CB  1 
ATOM   6360  C  CG  . GLN   A 1 799  ? -68.76000  65.84100  -4.39300  1.000 41.19302  ?  797  GLN   A CG  1 
ATOM   6361  C  CD  . GLN   A 1 799  ? -67.72400  65.51900  -3.33200  1.000 35.36452  ?  797  GLN   A CD  1 
ATOM   6362  O  OE1 . GLN   A 1 799  ? -66.53300  65.77500  -3.50800  1.000 57.32981  ?  797  GLN   A OE1 1 
ATOM   6363  N  NE2 . GLN   A 1 799  ? -68.17600  64.94400  -2.22300  1.000 42.49501  ?  797  GLN   A NE2 1 
ATOM   6364  N  N   . GLN   A 1 800  ? -69.16600  62.83000  -7.59400  1.000 53.53288  ?  798  GLN   A N   1 
ATOM   6365  C  CA  . GLN   A 1 800  ? -70.28300  61.92700  -7.83800  1.000 48.79692  ?  798  GLN   A CA  1 
ATOM   6366  C  C   . GLN   A 1 800  ? -69.93400  60.46200  -7.61100  1.000 48.26157  ?  798  GLN   A C   1 
ATOM   6367  O  O   . GLN   A 1 800  ? -70.83500  59.66500  -7.32500  1.000 62.82510  ?  798  GLN   A O   1 
ATOM   6368  C  CB  . GLN   A 1 800  ? -70.81100  62.09500  -9.26500  1.000 51.40238  ?  798  GLN   A CB  1 
ATOM   6369  C  CG  . GLN   A 1 800  ? -71.46800  63.43600  -9.55100  1.000 47.07736  ?  798  GLN   A CG  1 
ATOM   6370  C  CD  . GLN   A 1 800  ? -72.30300  63.95100  -8.39500  1.000 45.94021  ?  798  GLN   A CD  1 
ATOM   6371  O  OE1 . GLN   A 1 800  ? -73.12700  63.22700  -7.83500  1.000 54.71017  ?  798  GLN   A OE1 1 
ATOM   6372  N  NE2 . GLN   A 1 800  ? -72.09600  65.21300  -8.03300  1.000 38.05564  ?  798  GLN   A NE2 1 
ATOM   6373  N  N   . GLN   A 1 801  ? -68.66100  60.07700  -7.74700  1.000 52.22373  ?  799  GLN   A N   1 
ATOM   6374  C  CA  . GLN   A 1 801  ? -68.28400  58.68900  -7.48600  1.000 66.38211  ?  799  GLN   A CA  1 
ATOM   6375  C  C   . GLN   A 1 801  ? -68.57800  58.31000  -6.03700  1.000 72.89410  ?  799  GLN   A C   1 
ATOM   6376  O  O   . GLN   A 1 801  ? -69.17500  57.26200  -5.76500  1.000 86.80996  ?  799  GLN   A O   1 
ATOM   6377  C  CB  . GLN   A 1 801  ? -66.80800  58.46200  -7.85200  1.000 69.24739  ?  799  GLN   A CB  1 
ATOM   6378  C  CG  . GLN   A 1 801  ? -65.78700  58.70500  -6.73400  1.000 98.54011  ?  799  GLN   A CG  1 
ATOM   6379  C  CD  . GLN   A 1 801  ? -64.61400  57.73600  -6.74200  1.000 103.36325 ?  799  GLN   A CD  1 
ATOM   6380  O  OE1 . GLN   A 1 801  ? -64.74700  56.58000  -7.13000  1.000 101.75699 ?  799  GLN   A OE1 1 
ATOM   6381  N  NE2 . GLN   A 1 801  ? -63.45600  58.20900  -6.29300  1.000 94.49424  ?  799  GLN   A NE2 1 
ATOM   6382  N  N   . ASP   A 1 802  ? -68.20400  59.17400  -5.09600  1.000 66.86232  ?  800  ASP   A N   1 
ATOM   6383  C  CA  . ASP   A 1 802  ? -68.53400  59.01900  -3.68200  1.000 58.83878  ?  800  ASP   A CA  1 
ATOM   6384  C  C   . ASP   A 1 802  ? -69.17300  60.33700  -3.26700  1.000 56.50940  ?  800  ASP   A C   1 
ATOM   6385  O  O   . ASP   A 1 802  ? -68.47200  61.31900  -3.00400  1.000 54.97512  ?  800  ASP   A O   1 
ATOM   6386  C  CB  . ASP   A 1 802  ? -67.30200  58.69300  -2.84200  1.000 65.96834  ?  800  ASP   A CB  1 
ATOM   6387  C  CG  . ASP   A 1 802  ? -67.65000  58.34000  -1.40500  1.000 73.57109  ?  800  ASP   A CG  1 
ATOM   6388  O  OD1 . ASP   A 1 802  ? -68.83100  58.04000  -1.13300  1.000 66.94662  ?  800  ASP   A OD1 1 
ATOM   6389  O  OD2 . ASP   A 1 802  ? -66.74000  58.36200  -0.54900  1.000 79.96693  -1 800  ASP   A OD2 1 
ATOM   6390  N  N   . VAL   A 1 803  ? -70.50800  60.35800  -3.23400  1.000 51.49425  ?  801  VAL   A N   1 
ATOM   6391  C  CA  . VAL   A 1 803  ? -71.22300  61.59200  -2.94200  1.000 53.63913  ?  801  VAL   A CA  1 
ATOM   6392  C  C   . VAL   A 1 803  ? -70.96700  62.05900  -1.51700  1.000 55.41536  ?  801  VAL   A C   1 
ATOM   6393  O  O   . VAL   A 1 803  ? -71.24100  63.22100  -1.19000  1.000 49.50487  ?  801  VAL   A O   1 
ATOM   6394  C  CB  . VAL   A 1 803  ? -72.72600  61.40200  -3.20500  1.000 33.60992  ?  801  VAL   A CB  1 
ATOM   6395  C  CG1 . VAL   A 1 803  ? -73.39400  62.73500  -3.48500  1.000 39.23478  ?  801  VAL   A CG1 1 
ATOM   6396  C  CG2 . VAL   A 1 803  ? -72.93600  60.45200  -4.36600  1.000 48.71426  ?  801  VAL   A CG2 1 
ATOM   6397  N  N   . GLU   A 1 804  ? -70.42800  61.19000  -0.66000  1.000 49.06492  ?  802  GLU   A N   1 
ATOM   6398  C  CA  . GLU   A 1 804  ? -70.13200  61.52900  0.72500   1.000 63.90152  ?  802  GLU   A CA  1 
ATOM   6399  C  C   . GLU   A 1 804  ? -68.63700  61.70900  0.97500   1.000 54.26130  ?  802  GLU   A C   1 
ATOM   6400  O  O   . GLU   A 1 804  ? -68.18600  61.60200  2.12000   1.000 52.20645  ?  802  GLU   A O   1 
ATOM   6401  C  CB  . GLU   A 1 804  ? -70.70300  60.46400  1.66400   1.000 69.56812  ?  802  GLU   A CB  1 
ATOM   6402  C  CG  . GLU   A 1 804  ? -72.22600  60.41400  1.69700   1.000 57.61907  ?  802  GLU   A CG  1 
ATOM   6403  C  CD  . GLU   A 1 804  ? -72.82100  61.43200  2.65600   1.000 81.33832  ?  802  GLU   A CD  1 
ATOM   6404  O  OE1 . GLU   A 1 804  ? -72.43100  61.43200  3.84300   1.000 77.05921  ?  802  GLU   A OE1 1 
ATOM   6405  O  OE2 . GLU   A 1 804  ? -73.67600  62.23500  2.22200   1.000 83.08287  -1 802  GLU   A OE2 1 
ATOM   6406  N  N   . SER   A 1 805  ? -67.86100  61.99100  -0.06800  1.000 47.55230  ?  803  SER   A N   1 
ATOM   6407  C  CA  . SER   A 1 805  ? -66.42000  62.14000  0.06600   1.000 44.43794  ?  803  SER   A CA  1 
ATOM   6408  C  C   . SER   A 1 805  ? -66.04500  63.58200  0.38200   1.000 45.39799  ?  803  SER   A C   1 
ATOM   6409  O  O   . SER   A 1 805  ? -66.65100  64.52600  -0.13500  1.000 46.25486  ?  803  SER   A O   1 
ATOM   6410  C  CB  . SER   A 1 805  ? -65.70900  61.69500  -1.21100  1.000 40.79252  ?  803  SER   A CB  1 
ATOM   6411  O  OG  . SER   A 1 805  ? -64.34800  62.08600  -1.18300  1.000 28.52765  ?  803  SER   A OG  1 
ATOM   6412  N  N   . ILE   A 1 806  ? -65.03900  63.74300  1.23800   1.000 41.79144  ?  804  ILE   A N   1 
ATOM   6413  C  CA  . ILE   A 1 806  ? -64.48300  65.04800  1.57000   1.000 41.92706  ?  804  ILE   A CA  1 
ATOM   6414  C  C   . ILE   A 1 806  ? -63.07500  65.20900  1.01600   1.000 43.01205  ?  804  ILE   A C   1 
ATOM   6415  O  O   . ILE   A 1 806  ? -62.35500  66.12800  1.42000   1.000 41.50686  ?  804  ILE   A O   1 
ATOM   6416  C  CB  . ILE   A 1 806  ? -64.50100  65.29800  3.08600   1.000 36.54624  ?  804  ILE   A CB  1 
ATOM   6417  C  CG1 . ILE   A 1 806  ? -63.87300  64.11400  3.82400   1.000 37.97870  ?  804  ILE   A CG1 1 
ATOM   6418  C  CG2 . ILE   A 1 806  ? -65.92100  65.55800  3.57500   1.000 37.87224  ?  804  ILE   A CG2 1 
ATOM   6419  C  CD1 . ILE   A 1 806  ? -63.24600  64.49000  5.14600   1.000 33.95805  ?  804  ILE   A CD1 1 
ATOM   6420  N  N   . ALA   A 1 807  ? -62.66700  64.33200  0.09400   1.000 38.50197  ?  805  ALA   A N   1 
ATOM   6421  C  CA  . ALA   A 1 807  ? -61.31000  64.35400  -0.44400  1.000 23.05787  ?  805  ALA   A CA  1 
ATOM   6422  C  C   . ALA   A 1 807  ? -60.98500  65.65100  -1.17600  1.000 26.96348  ?  805  ALA   A C   1 
ATOM   6423  O  O   . ALA   A 1 807  ? -59.80500  65.99600  -1.30200  1.000 41.14232  ?  805  ALA   A O   1 
ATOM   6424  C  CB  . ALA   A 1 807  ? -61.10400  63.16400  -1.38100  1.000 28.26282  ?  805  ALA   A CB  1 
ATOM   6425  N  N   . TYR   A 1 808  ? -61.99300  66.37400  -1.66300  1.000 32.03880  ?  806  TYR   A N   1 
ATOM   6426  C  CA  . TYR   A 1 808  ? -61.79000  67.65200  -2.33300  1.000 38.82600  ?  806  TYR   A CA  1 
ATOM   6427  C  C   . TYR   A 1 808  ? -62.38800  68.80700  -1.53200  1.000 43.98956  ?  806  TYR   A C   1 
ATOM   6428  O  O   . TYR   A 1 808  ? -62.77900  69.83500  -2.09300  1.000 37.88156  ?  806  TYR   A O   1 
ATOM   6429  C  CB  . TYR   A 1 808  ? -62.35100  67.60200  -3.75400  1.000 34.07452  ?  806  TYR   A CB  1 
ATOM   6430  C  CG  . TYR   A 1 808  ? -61.46700  66.79900  -4.68600  1.000 38.17012  ?  806  TYR   A CG  1 
ATOM   6431  C  CD1 . TYR   A 1 808  ? -61.54300  65.40900  -4.72500  1.000 35.25028  ?  806  TYR   A CD1 1 
ATOM   6432  C  CD2 . TYR   A 1 808  ? -60.53500  67.42600  -5.50600  1.000 43.88502  ?  806  TYR   A CD2 1 
ATOM   6433  C  CE1 . TYR   A 1 808  ? -60.72000  64.66700  -5.56200  1.000 36.01578  ?  806  TYR   A CE1 1 
ATOM   6434  C  CE2 . TYR   A 1 808  ? -59.71200  66.69200  -6.34900  1.000 62.30284  ?  806  TYR   A CE2 1 
ATOM   6435  C  CZ  . TYR   A 1 808  ? -59.80900  65.31500  -6.37400  1.000 60.09763  ?  806  TYR   A CZ  1 
ATOM   6436  O  OH  . TYR   A 1 808  ? -58.99000  64.58900  -7.21300  1.000 63.06249  ?  806  TYR   A OH  1 
ATOM   6437  N  N   . ASN   A 1 809  ? -62.45900  68.64400  -0.21400  1.000 37.62552  ?  807  ASN   A N   1 
ATOM   6438  C  CA  . ASN   A 1 809  ? -62.82800  69.72600  0.68400   1.000 40.28913  ?  807  ASN   A CA  1 
ATOM   6439  C  C   . ASN   A 1 809  ? -61.58800  70.53000  1.04600   1.000 35.60495  ?  807  ASN   A C   1 
ATOM   6440  O  O   . ASN   A 1 809  ? -60.52000  69.96700  1.30400   1.000 56.40246  ?  807  ASN   A O   1 
ATOM   6441  C  CB  . ASN   A 1 809  ? -63.48800  69.18300  1.95200   1.000 36.28597  ?  807  ASN   A CB  1 
ATOM   6442  C  CG  . ASN   A 1 809  ? -64.93700  68.80700  1.73900   1.000 39.20453  ?  807  ASN   A CG  1 
ATOM   6443  O  OD1 . ASN   A 1 809  ? -65.34800  68.45800  0.63000   1.000 58.92386  ?  807  ASN   A OD1 1 
ATOM   6444  N  ND2 . ASN   A 1 809  ? -65.72600  68.88800  2.80100   1.000 30.06888  ?  807  ASN   A ND2 1 
ATOM   6445  N  N   . VAL   A 1 810  ? -61.73700  71.84900  1.06800   1.000 33.59998  ?  808  VAL   A N   1 
ATOM   6446  C  CA  . VAL   A 1 810  ? -60.63000  72.77300  1.28400   1.000 42.56430  ?  808  VAL   A CA  1 
ATOM   6447  C  C   . VAL   A 1 810  ? -60.84200  73.44800  2.63200   1.000 39.47667  ?  808  VAL   A C   1 
ATOM   6448  O  O   . VAL   A 1 810  ? -61.72800  74.29900  2.77500   1.000 45.50097  ?  808  VAL   A O   1 
ATOM   6449  C  CB  . VAL   A 1 810  ? -60.53000  73.80700  0.15700   1.000 39.20743  ?  808  VAL   A CB  1 
ATOM   6450  C  CG1 . VAL   A 1 810  ? -59.30100  74.65700  0.34800   1.000 46.34233  ?  808  VAL   A CG1 1 
ATOM   6451  C  CG2 . VAL   A 1 810  ? -60.50900  73.11400  -1.19700  1.000 34.90202  ?  808  VAL   A CG2 1 
ATOM   6452  N  N   . VAL   A 1 811  ? -60.02400  73.08700  3.61900   1.000 43.08895  ?  809  VAL   A N   1 
ATOM   6453  C  CA  . VAL   A 1 811  ? -60.18300  73.56400  4.99000   1.000 40.56614  ?  809  VAL   A CA  1 
ATOM   6454  C  C   . VAL   A 1 811  ? -58.96700  74.39900  5.36200   1.000 34.73423  ?  809  VAL   A C   1 
ATOM   6455  O  O   . VAL   A 1 811  ? -57.82700  73.92600  5.26500   1.000 39.64730  ?  809  VAL   A O   1 
ATOM   6456  C  CB  . VAL   A 1 811  ? -60.37300  72.40700  5.98600   1.000 36.51552  ?  809  VAL   A CB  1 
ATOM   6457  C  CG1 . VAL   A 1 811  ? -61.00900  72.91900  7.26300   1.000 41.10765  ?  809  VAL   A CG1 1 
ATOM   6458  C  CG2 . VAL   A 1 811  ? -61.22800  71.30300  5.37800   1.000 35.77701  ?  809  VAL   A CG2 1 
ATOM   6459  N  N   . TYR   A 1 812  ? -59.21100  75.63400  5.79300   1.000 36.72838  ?  810  TYR   A N   1 
ATOM   6460  C  CA  . TYR   A 1 812  ? -58.17200  76.53200  6.27000   1.000 38.13879  ?  810  TYR   A CA  1 
ATOM   6461  C  C   . TYR   A 1 812  ? -58.55300  77.05500  7.64800   1.000 35.82888  ?  810  TYR   A C   1 
ATOM   6462  O  O   . TYR   A 1 812  ? -59.73500  77.13800  7.99100   1.000 45.59174  ?  810  TYR   A O   1 
ATOM   6463  C  CB  . TYR   A 1 812  ? -57.95600  77.71700  5.31700   1.000 33.90983  ?  810  TYR   A CB  1 
ATOM   6464  C  CG  . TYR   A 1 812  ? -57.12900  77.40400  4.09200   1.000 38.81922  ?  810  TYR   A CG  1 
ATOM   6465  C  CD1 . TYR   A 1 812  ? -55.74700  77.54100  4.11200   1.000 49.11707  ?  810  TYR   A CD1 1 
ATOM   6466  C  CD2 . TYR   A 1 812  ? -57.72600  76.97400  2.91500   1.000 38.20654  ?  810  TYR   A CD2 1 
ATOM   6467  C  CE1 . TYR   A 1 812  ? -54.98200  77.25800  2.99300   1.000 47.04643  ?  810  TYR   A CE1 1 
ATOM   6468  C  CE2 . TYR   A 1 812  ? -56.96700  76.69200  1.79100   1.000 47.76334  ?  810  TYR   A CE2 1 
ATOM   6469  C  CZ  . TYR   A 1 812  ? -55.59600  76.83100  1.83700   1.000 35.93182  ?  810  TYR   A CZ  1 
ATOM   6470  O  OH  . TYR   A 1 812  ? -54.83900  76.55000  0.72200   1.000 48.45646  ?  810  TYR   A OH  1 
ATOM   6471  N  N   . THR   A 1 813  ? -57.54000  77.40900  8.43700   1.000 33.15407  ?  811  THR   A N   1 
ATOM   6472  C  CA  . THR   A 1 813  ? -57.74400  77.98800  9.75700   1.000 33.72618  ?  811  THR   A CA  1 
ATOM   6473  C  C   . THR   A 1 813  ? -56.87700  79.22700  9.91200   1.000 37.80587  ?  811  THR   A C   1 
ATOM   6474  O  O   . THR   A 1 813  ? -55.75600  79.28200  9.39700   1.000 32.48361  ?  811  THR   A O   1 
ATOM   6475  C  CB  . THR   A 1 813  ? -57.41800  76.99200  10.88400  1.000 35.52487  ?  811  THR   A CB  1 
ATOM   6476  O  OG1 . THR   A 1 813  ? -56.10600  76.44800  10.69100  1.000 53.49138  ?  811  THR   A OG1 1 
ATOM   6477  C  CG2 . THR   A 1 813  ? -58.42600  75.86500  10.90000  1.000 32.25604  ?  811  THR   A CG2 1 
ATOM   6478  N  N   . ILE   A 1 814  ? -57.40900  80.22400  10.61500  1.000 37.96844  ?  812  ILE   A N   1 
ATOM   6479  C  CA  . ILE   A 1 814  ? -56.67600  81.43500  10.96500  1.000 34.24907  ?  812  ILE   A CA  1 
ATOM   6480  C  C   . ILE   A 1 814  ? -56.89300  81.69200  12.44900  1.000 43.35827  ?  812  ILE   A C   1 
ATOM   6481  O  O   . ILE   A 1 814  ? -58.04000  81.76900  12.90600  1.000 52.18864  ?  812  ILE   A O   1 
ATOM   6482  C  CB  . ILE   A 1 814  ? -57.12300  82.65500  10.14200  1.000 30.27842  ?  812  ILE   A CB  1 
ATOM   6483  C  CG1 . ILE   A 1 814  ? -57.63500  82.22800  8.76400   1.000 49.42477  ?  812  ILE   A CG1 1 
ATOM   6484  C  CG2 . ILE   A 1 814  ? -55.98200  83.65100  10.01500  1.000 34.87167  ?  812  ILE   A CG2 1 
ATOM   6485  C  CD1 . ILE   A 1 814  ? -58.15700  83.37300  7.92600   1.000 50.62094  ?  812  ILE   A CD1 1 
ATOM   6486  N  N   . ASN   A 1 815  ? -55.80000  81.82300  13.19800  1.000 39.80062  ?  813  ASN   A N   1 
ATOM   6487  C  CA  . ASN   A 1 815  ? -55.86400  82.11400  14.62700  1.000 36.11574  ?  813  ASN   A CA  1 
ATOM   6488  C  C   . ASN   A 1 815  ? -55.85200  83.62700  14.82500  1.000 46.84280  ?  813  ASN   A C   1 
ATOM   6489  O  O   . ASN   A 1 815  ? -54.84500  84.29000  14.55700  1.000 55.32957  ?  813  ASN   A O   1 
ATOM   6490  C  CB  . ASN   A 1 815  ? -54.70600  81.45200  15.36900  1.000 29.76496  ?  813  ASN   A CB  1 
ATOM   6491  C  CG  . ASN   A 1 815  ? -54.78100  79.93500  15.33800  1.000 48.27454  ?  813  ASN   A CG  1 
ATOM   6492  O  OD1 . ASN   A 1 815  ? -55.83400  79.35900  15.06300  1.000 63.74159  ?  813  ASN   A OD1 1 
ATOM   6493  N  ND2 . ASN   A 1 815  ? -53.66100  79.28100  15.62300  1.000 29.76988  ?  813  ASN   A ND2 1 
ATOM   6494  N  N   . PHE   A 1 816  ? -56.98700  84.17800  15.29900  1.000 51.92504  ?  814  PHE   A N   1 
ATOM   6495  C  CA  . PHE   A 1 816  ? -57.15200  85.58800  15.60900  1.000 48.54289  ?  814  PHE   A CA  1 
ATOM   6496  C  C   . PHE   A 1 816  ? -56.98400  85.83000  17.10500  1.000 62.72002  ?  814  PHE   A C   1 
ATOM   6497  O  O   . PHE   A 1 816  ? -57.25200  84.94100  17.91900  1.000 60.52048  ?  814  PHE   A O   1 
ATOM   6498  C  CB  . PHE   A 1 816  ? -58.53700  86.09000  15.18400  1.000 48.38153  ?  814  PHE   A CB  1 
ATOM   6499  C  CG  . PHE   A 1 816  ? -58.72900  86.17700  13.69700  1.000 48.22402  ?  814  PHE   A CG  1 
ATOM   6500  C  CD1 . PHE   A 1 816  ? -58.26100  87.27100  12.98700  1.000 43.95787  ?  814  PHE   A CD1 1 
ATOM   6501  C  CD2 . PHE   A 1 816  ? -59.39800  85.17600  13.01200  1.000 50.49363  ?  814  PHE   A CD2 1 
ATOM   6502  C  CE1 . PHE   A 1 816  ? -58.44300  87.35800  11.61800  1.000 46.15329  ?  814  PHE   A CE1 1 
ATOM   6503  C  CE2 . PHE   A 1 816  ? -59.58400  85.25700  11.64400  1.000 62.11523  ?  814  PHE   A CE2 1 
ATOM   6504  C  CZ  . PHE   A 1 816  ? -59.10600  86.35000  10.94600  1.000 54.45332  ?  814  PHE   A CZ  1 
ATOM   6505  N  N   . PRO   A 1 817  ? -56.53700  87.02100  17.49700  1.000 76.16379  ?  815  PRO   A N   1 
ATOM   6506  C  CA  . PRO   A 1 817  ? -56.55400  87.37800  18.91800  1.000 54.34396  ?  815  PRO   A CA  1 
ATOM   6507  C  C   . PRO   A 1 817  ? -57.98000  87.48700  19.42800  1.000 59.03953  ?  815  PRO   A C   1 
ATOM   6508  O  O   . PRO   A 1 817  ? -58.92600  87.72400  18.67300  1.000 66.36803  ?  815  PRO   A O   1 
ATOM   6509  C  CB  . PRO   A 1 817  ? -55.84500  88.73700  18.95800  1.000 49.14698  ?  815  PRO   A CB  1 
ATOM   6510  C  CG  . PRO   A 1 817  ? -55.08400  88.81600  17.67600  1.000 69.20314  ?  815  PRO   A CG  1 
ATOM   6511  C  CD  . PRO   A 1 817  ? -55.90600  88.06500  16.67500  1.000 69.93909  ?  815  PRO   A CD  1 
ATOM   6512  N  N   . LEU   A 1 818  ? -58.12500  87.31100  20.74300  1.000 67.44513  ?  816  LEU   A N   1 
ATOM   6513  C  CA  . LEU   A 1 818  ? -59.44400  87.34800  21.36600  1.000 63.43024  ?  816  LEU   A CA  1 
ATOM   6514  C  C   . LEU   A 1 818  ? -60.10700  88.71600  21.27300  1.000 65.05210  ?  816  LEU   A C   1 
ATOM   6515  O  O   . LEU   A 1 818  ? -61.31800  88.81400  21.49400  1.000 72.08156  ?  816  LEU   A O   1 
ATOM   6516  C  CB  . LEU   A 1 818  ? -59.34400  86.92000  22.83200  1.000 42.33981  ?  816  LEU   A CB  1 
ATOM   6517  C  CG  . LEU   A 1 818  ? -59.40000  85.41300  23.09300  1.000 54.80334  ?  816  LEU   A CG  1 
ATOM   6518  C  CD1 . LEU   A 1 818  ? -58.90700  85.08400  24.49200  1.000 49.95377  ?  816  LEU   A CD1 1 
ATOM   6519  C  CD2 . LEU   A 1 818  ? -60.80900  84.88300  22.88200  1.000 63.06987  ?  816  LEU   A CD2 1 
ATOM   6520  N  N   . THR   A 1 819  ? -59.35100  89.76400  20.94500  1.000 67.38624  ?  817  THR   A N   1 
ATOM   6521  C  CA  . THR   A 1 819  ? -59.89700  91.11000  20.84400  1.000 49.18689  ?  817  THR   A CA  1 
ATOM   6522  C  C   . THR   A 1 819  ? -60.70300  91.33600  19.57200  1.000 69.40555  ?  817  THR   A C   1 
ATOM   6523  O  O   . THR   A 1 819  ? -61.33200  92.39100  19.43800  1.000 96.70283  ?  817  THR   A O   1 
ATOM   6524  C  CB  . THR   A 1 819  ? -58.76500  92.13800  20.92000  1.000 69.14443  ?  817  THR   A CB  1 
ATOM   6525  O  OG1 . THR   A 1 819  ? -58.48900  92.64500  19.60900  1.000 77.23178  ?  817  THR   A OG1 1 
ATOM   6526  C  CG2 . THR   A 1 819  ? -57.50400  91.49800  21.48400  1.000 58.15031  ?  817  THR   A CG2 1 
ATOM   6527  N  N   . VAL   A 1 820  ? -60.70100  90.38700  18.64400  1.000 61.50455  ?  818  VAL   A N   1 
ATOM   6528  C  CA  . VAL   A 1 820  ? -61.48300  90.51500  17.42000  1.000 62.48278  ?  818  VAL   A CA  1 
ATOM   6529  C  C   . VAL   A 1 820  ? -62.92600  90.12400  17.70300  1.000 68.75795  ?  818  VAL   A C   1 
ATOM   6530  O  O   . VAL   A 1 820  ? -63.19300  89.15400  18.42200  1.000 76.15831  ?  818  VAL   A O   1 
ATOM   6531  C  CB  . VAL   A 1 820  ? -60.87800  89.64700  16.30400  1.000 57.27553  ?  818  VAL   A CB  1 
ATOM   6532  C  CG1 . VAL   A 1 820  ? -61.54400  89.95200  14.97300  1.000 47.49497  ?  818  VAL   A CG1 1 
ATOM   6533  C  CG2 . VAL   A 1 820  ? -59.37800  89.87300  16.22000  1.000 68.11924  ?  818  VAL   A CG2 1 
ATOM   6534  N  N   . ASP   A 1 821  ? -63.86500  90.87900  17.14000  1.000 61.51821  ?  819  ASP   A N   1 
ATOM   6535  C  CA  . ASP   A 1 821  ? -65.27900  90.56700  17.30200  1.000 63.86932  ?  819  ASP   A CA  1 
ATOM   6536  C  C   . ASP   A 1 821  ? -65.65100  89.41700  16.37300  1.000 61.11545  ?  819  ASP   A C   1 
ATOM   6537  O  O   . ASP   A 1 821  ? -65.46300  89.50900  15.15400  1.000 55.25193  ?  819  ASP   A O   1 
ATOM   6538  C  CB  . ASP   A 1 821  ? -66.14100  91.79500  17.01900  1.000 62.58575  ?  819  ASP   A CB  1 
ATOM   6539  C  CG  . ASP   A 1 821  ? -67.60900  91.56500  17.33700  1.000 71.88330  ?  819  ASP   A CG  1 
ATOM   6540  O  OD1 . ASP   A 1 821  ? -67.93400  90.54300  17.98000  1.000 78.97499  ?  819  ASP   A OD1 1 
ATOM   6541  O  OD2 . ASP   A 1 821  ? -68.44000  92.41000  16.94700  1.000 83.43823  -1 819  ASP   A OD2 1 
ATOM   6542  N  N   . THR   A 1 822  ? -66.18000  88.33700  16.95400  1.000 62.66451  ?  820  THR   A N   1 
ATOM   6543  C  CA  . THR   A 1 822  ? -66.55100  87.16700  16.16300  1.000 56.58759  ?  820  THR   A CA  1 
ATOM   6544  C  C   . THR   A 1 822  ? -67.59700  87.51900  15.11100  1.000 58.99825  ?  820  THR   A C   1 
ATOM   6545  O  O   . THR   A 1 822  ? -67.49700  87.08600  13.95600  1.000 68.08950  ?  820  THR   A O   1 
ATOM   6546  C  CB  . THR   A 1 822  ? -67.05900  86.05600  17.08500  1.000 47.24234  ?  820  THR   A CB  1 
ATOM   6547  O  OG1 . THR   A 1 822  ? -65.96100  85.49900  17.81800  1.000 56.45265  ?  820  THR   A OG1 1 
ATOM   6548  C  CG2 . THR   A 1 822  ? -67.72600  84.94700  16.28400  1.000 55.69234  ?  820  THR   A CG2 1 
ATOM   6549  N  N   . GLU   A 1 823  ? -68.60000  88.31900  15.48500  1.000 57.26044  ?  821  GLU   A N   1 
ATOM   6550  C  CA  . GLU   A 1 823  ? -69.65900  88.66600  14.54200  1.000 72.34784  ?  821  GLU   A CA  1 
ATOM   6551  C  C   . GLU   A 1 823  ? -69.14100  89.52900  13.39900  1.000 73.26396  ?  821  GLU   A C   1 
ATOM   6552  O  O   . GLU   A 1 823  ? -69.66000  89.44700  12.27900  1.000 68.91420  ?  821  GLU   A O   1 
ATOM   6553  C  CB  . GLU   A 1 823  ? -70.79900  89.37600  15.26800  1.000 53.85434  ?  821  GLU   A CB  1 
ATOM   6554  C  CG  . GLU   A 1 823  ? -71.44200  88.54100  16.35900  1.000 69.42082  ?  821  GLU   A CG  1 
ATOM   6555  C  CD  . GLU   A 1 823  ? -71.72700  87.12200  15.91000  1.000 67.90030  ?  821  GLU   A CD  1 
ATOM   6556  O  OE1 . GLU   A 1 823  ? -72.57200  86.94800  15.00800  1.000 77.04604  ?  821  GLU   A OE1 1 
ATOM   6557  O  OE2 . GLU   A 1 823  ? -71.11300  86.18300  16.46000  1.000 74.02109  -1 821  GLU   A OE2 1 
ATOM   6558  N  N   . GLN   A 1 824  ? -68.12900  90.36000  13.66000  1.000 54.58744  ?  822  GLN   A N   1 
ATOM   6559  C  CA  . GLN   A 1 824  ? -67.52600  91.14900  12.59100  1.000 52.95332  ?  822  GLN   A CA  1 
ATOM   6560  C  C   . GLN   A 1 824  ? -66.96300  90.25200  11.49700  1.000 62.54090  ?  822  GLN   A C   1 
ATOM   6561  O  O   . GLN   A 1 824  ? -67.09700  90.55400  10.30500  1.000 62.97566  ?  822  GLN   A O   1 
ATOM   6562  C  CB  . GLN   A 1 824  ? -66.43200  92.04900  13.16000  1.000 57.37262  ?  822  GLN   A CB  1 
ATOM   6563  C  CG  . GLN   A 1 824  ? -66.55400  93.50600  12.75700  1.000 82.90943  ?  822  GLN   A CG  1 
ATOM   6564  C  CD  . GLN   A 1 824  ? -65.25800  94.26700  12.95500  1.000 96.29628  ?  822  GLN   A CD  1 
ATOM   6565  O  OE1 . GLN   A 1 824  ? -64.60200  94.13800  13.98900  1.000 93.31805  ?  822  GLN   A OE1 1 
ATOM   6566  N  NE2 . GLN   A 1 824  ? -64.88000  95.06100  11.96000  1.000 79.08524  ?  822  GLN   A NE2 1 
ATOM   6567  N  N   . ILE   A 1 825  ? -66.33300  89.14000  11.88400  1.000 57.70817  ?  823  ILE   A N   1 
ATOM   6568  C  CA  . ILE   A 1 825  ? -65.82000  88.19100  10.89900  1.000 56.01148  ?  823  ILE   A CA  1 
ATOM   6569  C  C   . ILE   A 1 825  ? -66.96200  87.56200  10.11100  1.000 57.11695  ?  823  ILE   A C   1 
ATOM   6570  O  O   . ILE   A 1 825  ? -66.88300  87.41900  8.88500   1.000 55.41898  ?  823  ILE   A O   1 
ATOM   6571  C  CB  . ILE   A 1 825  ? -64.95500  87.12100  11.58800  1.000 48.45251  ?  823  ILE   A CB  1 
ATOM   6572  C  CG1 . ILE   A 1 825  ? -64.00500  87.77600  12.59100  1.000 61.37916  ?  823  ILE   A CG1 1 
ATOM   6573  C  CG2 . ILE   A 1 825  ? -64.19100  86.31300  10.55800  1.000 54.37013  ?  823  ILE   A CG2 1 
ATOM   6574  C  CD1 . ILE   A 1 825  ? -63.39600  86.80700  13.57100  1.000 48.96625  ?  823  ILE   A CD1 1 
ATOM   6575  N  N   . ARG   A 1 826  ? -68.03900  87.17300  10.80000  1.000 54.33175  ?  824  ARG   A N   1 
ATOM   6576  C  CA  . ARG   A 1 826  ? -69.17100  86.56100  10.11000  1.000 55.86879  ?  824  ARG   A CA  1 
ATOM   6577  C  C   . ARG   A 1 826  ? -69.81200  87.53700  9.13200   1.000 62.53571  ?  824  ARG   A C   1 
ATOM   6578  O  O   . ARG   A 1 826  ? -70.17100  87.15800  8.01000   1.000 59.91874  ?  824  ARG   A O   1 
ATOM   6579  C  CB  . ARG   A 1 826  ? -70.20700  86.06800  11.11900  1.000 53.41430  ?  824  ARG   A CB  1 
ATOM   6580  C  CG  . ARG   A 1 826  ? -71.51400  85.62000  10.47300  1.000 72.99740  ?  824  ARG   A CG  1 
ATOM   6581  C  CD  . ARG   A 1 826  ? -72.62900  85.45800  11.49000  1.000 69.14390  ?  824  ARG   A CD  1 
ATOM   6582  N  NE  . ARG   A 1 826  ? -72.86700  86.68900  12.23300  1.000 78.33802  ?  824  ARG   A NE  1 
ATOM   6583  C  CZ  . ARG   A 1 826  ? -73.68300  87.65800  11.83900  1.000 82.54694  ?  824  ARG   A CZ  1 
ATOM   6584  N  NH1 . ARG   A 1 826  ? -74.35300  87.57700  10.70000  1.000 82.60046  ?  824  ARG   A NH1 1 
ATOM   6585  N  NH2 . ARG   A 1 826  ? -73.82800  88.73500  12.60500  1.000 73.98006  ?  824  ARG   A NH2 1 
ATOM   6586  N  N   . VAL   A 1 827  ? -69.96700  88.79700  9.54100   1.000 64.20933  ?  825  VAL   A N   1 
ATOM   6587  C  CA  . VAL   A 1 827  ? -70.52800  89.80800  8.64900   1.000 64.67116  ?  825  VAL   A CA  1 
ATOM   6588  C  C   . VAL   A 1 827  ? -69.66900  89.94500  7.39800   1.000 57.23814  ?  825  VAL   A C   1 
ATOM   6589  O  O   . VAL   A 1 827  ? -70.18000  90.00200  6.27300   1.000 57.18364  ?  825  VAL   A O   1 
ATOM   6590  C  CB  . VAL   A 1 827  ? -70.67400  91.15100  9.38700   1.000 57.61221  ?  825  VAL   A CB  1 
ATOM   6591  C  CG1 . VAL   A 1 827  ? -71.01400  92.26300  8.40800   1.000 60.32193  ?  825  VAL   A CG1 1 
ATOM   6592  C  CG2 . VAL   A 1 827  ? -71.73800  91.04200  10.46300  1.000 64.10835  ?  825  VAL   A CG2 1 
ATOM   6593  N  N   . ALA   A 1 828  ? -68.34700  89.98800  7.57700   1.000 50.87311  ?  826  ALA   A N   1 
ATOM   6594  C  CA  . ALA   A 1 828  ? -67.44800  90.10000  6.43300   1.000 54.18184  ?  826  ALA   A CA  1 
ATOM   6595  C  C   . ALA   A 1 828  ? -67.58100  88.89900  5.50400   1.000 45.73189  ?  826  ALA   A C   1 
ATOM   6596  O  O   . ALA   A 1 828  ? -67.59300  89.05100  4.27700   1.000 55.12016  ?  826  ALA   A O   1 
ATOM   6597  C  CB  . ALA   A 1 828  ? -66.00600  90.25400  6.91300   1.000 45.44520  ?  826  ALA   A CB  1 
ATOM   6598  N  N   . LEU   A 1 829  ? -67.68800  87.69600  6.07000   1.000 31.79723  ?  827  LEU   A N   1 
ATOM   6599  C  CA  . LEU   A 1 829  ? -67.87100  86.51100  5.24100   1.000 37.58514  ?  827  LEU   A CA  1 
ATOM   6600  C  C   . LEU   A 1 829  ? -69.21100  86.53200  4.51400   1.000 49.26239  ?  827  LEU   A C   1 
ATOM   6601  O  O   . LEU   A 1 829  ? -69.30300  86.05500  3.37800   1.000 53.50662  ?  827  LEU   A O   1 
ATOM   6602  C  CB  . LEU   A 1 829  ? -67.75000  85.25100  6.09300   1.000 37.62419  ?  827  LEU   A CB  1 
ATOM   6603  C  CG  . LEU   A 1 829  ? -66.39000  85.00200  6.74000   1.000 39.45754  ?  827  LEU   A CG  1 
ATOM   6604  C  CD1 . LEU   A 1 829  ? -66.50000  83.89700  7.77600   1.000 50.13980  ?  827  LEU   A CD1 1 
ATOM   6605  C  CD2 . LEU   A 1 829  ? -65.35600  84.65600  5.68400   1.000 22.90382  ?  827  LEU   A CD2 1 
ATOM   6606  N  N   . GLU   A 1 830  ? -70.25700  87.06900  5.14800   1.000 57.87605  ?  828  GLU   A N   1 
ATOM   6607  C  CA  . GLU   A 1 830  ? -71.54200  87.18800  4.46700   1.000 50.42398  ?  828  GLU   A CA  1 
ATOM   6608  C  C   . GLU   A 1 830  ? -71.49000  88.24300  3.37100   1.000 54.13466  ?  828  GLU   A C   1 
ATOM   6609  O  O   . GLU   A 1 830  ? -72.25200  88.16500  2.39900   1.000 50.24698  ?  828  GLU   A O   1 
ATOM   6610  C  CB  . GLU   A 1 830  ? -72.64500  87.50100  5.47900   1.000 55.83845  ?  828  GLU   A CB  1 
ATOM   6611  C  CG  . GLU   A 1 830  ? -73.07900  86.28400  6.28700   1.000 75.79202  ?  828  GLU   A CG  1 
ATOM   6612  C  CD  . GLU   A 1 830  ? -73.92600  86.64300  7.49200   1.000 76.36259  ?  828  GLU   A CD  1 
ATOM   6613  O  OE1 . GLU   A 1 830  ? -73.87300  87.81000  7.93400   1.000 70.26056  ?  828  GLU   A OE1 1 
ATOM   6614  O  OE2 . GLU   A 1 830  ? -74.63700  85.75100  8.00400   1.000 70.63821  -1 828  GLU   A OE2 1 
ATOM   6615  N  N   . GLN   A 1 831  ? -70.60000  89.23000  3.50800   1.000 59.11068  ?  829  GLN   A N   1 
ATOM   6616  C  CA  . GLN   A 1 831  ? -70.33900  90.14800  2.40500   1.000 55.89047  ?  829  GLN   A CA  1 
ATOM   6617  C  C   . GLN   A 1 831  ? -69.58300  89.45200  1.28300   1.000 52.13865  ?  829  GLN   A C   1 
ATOM   6618  O  O   . GLN   A 1 831  ? -69.81900  89.72800  0.10300   1.000 58.07670  ?  829  GLN   A O   1 
ATOM   6619  C  CB  . GLN   A 1 831  ? -69.55300  91.36500  2.89100   1.000 57.67227  ?  829  GLN   A CB  1 
ATOM   6620  C  CG  . GLN   A 1 831  ? -70.27000  92.23200  3.90800   1.000 59.19304  ?  829  GLN   A CG  1 
ATOM   6621  C  CD  . GLN   A 1 831  ? -69.41600  93.40000  4.36800   1.000 77.39588  ?  829  GLN   A CD  1 
ATOM   6622  O  OE1 . GLN   A 1 831  ? -69.00400  93.47000  5.52600   1.000 72.97516  ?  829  GLN   A OE1 1 
ATOM   6623  N  NE2 . GLN   A 1 831  ? -69.13800  94.32300  3.45300   1.000 69.27472  ?  829  GLN   A NE2 1 
ATOM   6624  N  N   . LEU   A 1 832  ? -68.66400  88.54900  1.62300   1.000 45.03830  ?  830  LEU   A N   1 
ATOM   6625  C  CA  . LEU   A 1 832  ? -67.96500  87.83100  0.56800   1.000 49.77191  ?  830  LEU   A CA  1 
ATOM   6626  C  C   . LEU   A 1 832  ? -68.88800  86.87500  -0.17800  1.000 51.36282  ?  830  LEU   A C   1 
ATOM   6627  O  O   . LEU   A 1 832  ? -68.61700  86.55900  -1.34100  1.000 62.02022  ?  830  LEU   A O   1 
ATOM   6628  C  CB  . LEU   A 1 832  ? -66.75900  87.08700  1.14100   1.000 47.73444  ?  830  LEU   A CB  1 
ATOM   6629  C  CG  . LEU   A 1 832  ? -65.61700  88.02400  1.54400   1.000 44.72746  ?  830  LEU   A CG  1 
ATOM   6630  C  CD1 . LEU   A 1 832  ? -64.41700  87.23600  2.03900   1.000 51.15992  ?  830  LEU   A CD1 1 
ATOM   6631  C  CD2 . LEU   A 1 832  ? -65.23300  88.92800  0.38200   1.000 41.29130  ?  830  LEU   A CD2 1 
ATOM   6632  N  N   . VAL   A 1 833  ? -69.98600  86.43900  0.44700   1.000 45.08880  ?  831  VAL   A N   1 
ATOM   6633  C  CA  . VAL   A 1 833  ? -70.91400  85.53400  -0.22600  1.000 46.43840  ?  831  VAL   A CA  1 
ATOM   6634  C  C   . VAL   A 1 833  ? -71.62900  86.24600  -1.36900  1.000 52.24807  ?  831  VAL   A C   1 
ATOM   6635  O  O   . VAL   A 1 833  ? -71.76900  85.69500  -2.46800  1.000 57.72369  ?  831  VAL   A O   1 
ATOM   6636  C  CB  . VAL   A 1 833  ? -71.91000  84.93900  0.78600   1.000 42.59763  ?  831  VAL   A CB  1 
ATOM   6637  C  CG1 . VAL   A 1 833  ? -73.08600  84.28900  0.06500   1.000 42.40080  ?  831  VAL   A CG1 1 
ATOM   6638  C  CG2 . VAL   A 1 833  ? -71.20800  83.93000  1.67800   1.000 41.43318  ?  831  VAL   A CG2 1 
ATOM   6639  N  N   . LEU   A 1 834  ? -72.08300  87.48300  -1.14100  1.000 49.04360  ?  832  LEU   A N   1 
ATOM   6640  C  CA  . LEU   A 1 834  ? -72.79500  88.18200  -2.20400  1.000 53.27398  ?  832  LEU   A CA  1 
ATOM   6641  C  C   . LEU   A 1 834  ? -71.83500  88.77500  -3.22800  1.000 54.99038  ?  832  LEU   A C   1 
ATOM   6642  O  O   . LEU   A 1 834  ? -72.20000  88.92500  -4.39900  1.000 59.54432  ?  832  LEU   A O   1 
ATOM   6643  C  CB  . LEU   A 1 834  ? -73.70900  89.27300  -1.62600  1.000 68.63758  ?  832  LEU   A CB  1 
ATOM   6644  C  CG  . LEU   A 1 834  ? -73.33100  90.32500  -0.57000  1.000 78.41743  ?  832  LEU   A CG  1 
ATOM   6645  C  CD1 . LEU   A 1 834  ? -72.14900  91.19500  -0.98700  1.000 59.32391  ?  832  LEU   A CD1 1 
ATOM   6646  C  CD2 . LEU   A 1 834  ? -74.52700  91.19500  -0.25300  1.000 54.02220  ?  832  LEU   A CD2 1 
ATOM   6647  N  N   . ARG   A 1 835  ? -70.60800  89.09600  -2.81100  1.000 56.19122  ?  833  ARG   A N   1 
ATOM   6648  C  CA  . ARG   A 1 835  ? -69.64500  89.71700  -3.71500  1.000 44.45652  ?  833  ARG   A CA  1 
ATOM   6649  C  C   . ARG   A 1 835  ? -69.22600  88.77200  -4.83800  1.000 58.95578  ?  833  ARG   A C   1 
ATOM   6650  O  O   . ARG   A 1 835  ? -68.89000  89.23000  -5.93600  1.000 55.32585  ?  833  ARG   A O   1 
ATOM   6651  C  CB  . ARG   A 1 835  ? -68.43000  90.18400  -2.91100  1.000 36.41370  ?  833  ARG   A CB  1 
ATOM   6652  C  CG  . ARG   A 1 835  ? -67.32000  90.85700  -3.70000  1.000 52.24866  ?  833  ARG   A CG  1 
ATOM   6653  C  CD  . ARG   A 1 835  ? -66.35300  91.54400  -2.74800  1.000 52.17895  ?  833  ARG   A CD  1 
ATOM   6654  N  NE  . ARG   A 1 835  ? -65.14700  92.01300  -3.41600  1.000 62.59464  ?  833  ARG   A NE  1 
ATOM   6655  C  CZ  . ARG   A 1 835  ? -65.03800  93.18500  -4.02500  1.000 71.30968  ?  833  ARG   A CZ  1 
ATOM   6656  N  NH1 . ARG   A 1 835  ? -66.05700  94.02700  -4.08900  1.000 72.62019  ?  833  ARG   A NH1 1 
ATOM   6657  N  NH2 . ARG   A 1 835  ? -63.87700  93.52300  -4.57900  1.000 72.77250  ?  833  ARG   A NH2 1 
ATOM   6658  N  N   . HIS   A 1 836  ? -69.26100  87.46200  -4.59800  1.000 50.61914  ?  834  HIS   A N   1 
ATOM   6659  C  CA  . HIS   A 1 836  ? -68.74900  86.47900  -5.54600  1.000 54.54738  ?  834  HIS   A CA  1 
ATOM   6660  C  C   . HIS   A 1 836  ? -69.83300  85.45900  -5.85700  1.000 46.65032  ?  834  HIS   A C   1 
ATOM   6661  O  O   . HIS   A 1 836  ? -70.29300  84.74300  -4.96200  1.000 49.98457  ?  834  HIS   A O   1 
ATOM   6662  C  CB  . HIS   A 1 836  ? -67.49700  85.80000  -4.98800  1.000 52.01227  ?  834  HIS   A CB  1 
ATOM   6663  C  CG  . HIS   A 1 836  ? -66.46500  86.76700  -4.49900  1.000 39.14348  ?  834  HIS   A CG  1 
ATOM   6664  N  ND1 . HIS   A 1 836  ? -65.60500  87.42700  -5.34900  1.000 43.24709  ?  834  HIS   A ND1 1 
ATOM   6665  C  CD2 . HIS   A 1 836  ? -66.17200  87.20400  -3.25200  1.000 44.57633  ?  834  HIS   A CD2 1 
ATOM   6666  C  CE1 . HIS   A 1 836  ? -64.81500  88.21900  -4.64500  1.000 44.26608  ?  834  HIS   A CE1 1 
ATOM   6667  N  NE2 . HIS   A 1 836  ? -65.13900  88.10300  -3.37000  1.000 43.64611  ?  834  HIS   A NE2 1 
ATOM   6668  N  N   . GLU   A 1 837  ? -70.22800  85.38900  -7.13000  1.000 42.08705  ?  835  GLU   A N   1 
ATOM   6669  C  CA  . GLU   A 1 837  ? -71.30500  84.49200  -7.53100  1.000 42.23377  ?  835  GLU   A CA  1 
ATOM   6670  C  C   . GLU   A 1 837  ? -70.95500  83.03500  -7.27200  1.000 41.86618  ?  835  GLU   A C   1 
ATOM   6671  O  O   . GLU   A 1 837  ? -71.85400  82.19900  -7.12700  1.000 40.89231  ?  835  GLU   A O   1 
ATOM   6672  C  CB  . GLU   A 1 837  ? -71.63100  84.69800  -9.00800  1.000 45.59910  ?  835  GLU   A CB  1 
ATOM   6673  C  CG  . GLU   A 1 837  ? -72.13800  86.08800  -9.33600  1.000 63.88350  ?  835  GLU   A CG  1 
ATOM   6674  C  CD  . GLU   A 1 837  ? -72.74000  86.17000  -10.72100 1.000 61.90550  ?  835  GLU   A CD  1 
ATOM   6675  O  OE1 . GLU   A 1 837  ? -72.63400  85.17600  -11.47300 1.000 51.42549  ?  835  GLU   A OE1 1 
ATOM   6676  O  OE2 . GLU   A 1 837  ? -73.32600  87.22200  -11.05200 1.000 74.75593  -1 835  GLU   A OE2 1 
ATOM   6677  N  N   . GLY   A 1 838  ? -69.66200  82.70700  -7.22600  1.000 45.86676  ?  836  GLY   A N   1 
ATOM   6678  C  CA  . GLY   A 1 838  ? -69.27200  81.34300  -6.91800  1.000 49.41015  ?  836  GLY   A CA  1 
ATOM   6679  C  C   . GLY   A 1 838  ? -69.73700  80.91800  -5.54100  1.000 41.38315  ?  836  GLY   A C   1 
ATOM   6680  O  O   . GLY   A 1 838  ? -70.18400  79.78400  -5.34500  1.000 40.26240  ?  836  GLY   A O   1 
ATOM   6681  N  N   . LEU   A 1 839  ? -69.66300  81.83100  -4.57400  1.000 33.26996  ?  837  LEU   A N   1 
ATOM   6682  C  CA  . LEU   A 1 839  ? -70.19400  81.56800  -3.24500  1.000 42.83010  ?  837  LEU   A CA  1 
ATOM   6683  C  C   . LEU   A 1 839  ? -71.71600  81.51900  -3.22500  1.000 51.43006  ?  837  LEU   A C   1 
ATOM   6684  O  O   . LEU   A 1 839  ? -72.30000  81.35100  -2.14900  1.000 57.91314  ?  837  LEU   A O   1 
ATOM   6685  C  CB  . LEU   A 1 839  ? -69.68500  82.62500  -2.26500  1.000 46.51195  ?  837  LEU   A CB  1 
ATOM   6686  C  CG  . LEU   A 1 839  ? -68.33500  82.29400  -1.62600  1.000 46.12041  ?  837  LEU   A CG  1 
ATOM   6687  C  CD1 . LEU   A 1 839  ? -67.71100  83.51600  -0.97100  1.000 35.89767  ?  837  LEU   A CD1 1 
ATOM   6688  C  CD2 . LEU   A 1 839  ? -68.49700  81.17500  -0.62000  1.000 48.29454  ?  837  LEU   A CD2 1 
ATOM   6689  N  N   . ARG   A 1 840  ? -72.36400  81.66700  -4.38300  1.000 51.52079  ?  838  ARG   A N   1 
ATOM   6690  C  CA  . ARG   A 1 840  ? -73.80700  81.51200  -4.51500  1.000 37.89618  ?  838  ARG   A CA  1 
ATOM   6691  C  C   . ARG   A 1 840  ? -74.16100  80.64500  -5.71800  1.000 40.69973  ?  838  ARG   A C   1 
ATOM   6692  O  O   . ARG   A 1 840  ? -75.30300  80.68400  -6.18800  1.000 53.67503  ?  838  ARG   A O   1 
ATOM   6693  C  CB  . ARG   A 1 840  ? -74.49000  82.87600  -4.63000  1.000 42.36808  ?  838  ARG   A CB  1 
ATOM   6694  C  CG  . ARG   A 1 840  ? -74.54200  83.64900  -3.32600  1.000 52.17133  ?  838  ARG   A CG  1 
ATOM   6695  C  CD  . ARG   A 1 840  ? -75.06700  85.06000  -3.53500  1.000 53.30456  ?  838  ARG   A CD  1 
ATOM   6696  N  NE  . ARG   A 1 840  ? -74.15200  85.89000  -4.30800  1.000 52.48035  ?  838  ARG   A NE  1 
ATOM   6697  C  CZ  . ARG   A 1 840  ? -74.39000  86.32100  -5.54000  1.000 57.23030  ?  838  ARG   A CZ  1 
ATOM   6698  N  NH1 . ARG   A 1 840  ? -75.49600  85.98900  -6.18600  1.000 50.77849  ?  838  ARG   A NH1 1 
ATOM   6699  N  NH2 . ARG   A 1 840  ? -73.49400  87.10300  -6.13900  1.000 45.37591  ?  838  ARG   A NH2 1 
ATOM   6700  N  N   . SER   A 1 841  ? -73.20500  79.87600  -6.22900  1.000 47.45789  ?  839  SER   A N   1 
ATOM   6701  C  CA  . SER   A 1 841  ? -73.39900  79.06100  -7.41900  1.000 47.84185  ?  839  SER   A CA  1 
ATOM   6702  C  C   . SER   A 1 841  ? -73.72000  77.62800  -7.02000  1.000 44.26341  ?  839  SER   A C   1 
ATOM   6703  O  O   . SER   A 1 841  ? -73.12000  77.08400  -6.08900  1.000 64.24952  ?  839  SER   A O   1 
ATOM   6704  C  CB  . SER   A 1 841  ? -72.15200  79.07600  -8.30700  1.000 44.05994  ?  839  SER   A CB  1 
ATOM   6705  O  OG  . SER   A 1 841  ? -71.82300  80.38800  -8.72700  1.000 46.35478  ?  839  SER   A OG  1 
ATOM   6706  N  N   . THR   A 1 842  ? -74.66700  77.02200  -7.73100  1.000 45.99130  ?  840  THR   A N   1 
ATOM   6707  C  CA  . THR   A 1 842  ? -75.03900  75.62900  -7.53500  1.000 46.08123  ?  840  THR   A CA  1 
ATOM   6708  C  C   . THR   A 1 842  ? -74.90600  74.88200  -8.85400  1.000 48.82219  ?  840  THR   A C   1 
ATOM   6709  O  O   . THR   A 1 842  ? -75.05700  75.46300  -9.93300  1.000 48.32211  ?  840  THR   A O   1 
ATOM   6710  C  CB  . THR   A 1 842  ? -76.47300  75.49000  -6.99900  1.000 51.13864  ?  840  THR   A CB  1 
ATOM   6711  O  OG1 . THR   A 1 842  ? -77.39600  76.09100  -7.91600  1.000 55.96703  ?  840  THR   A OG1 1 
ATOM   6712  C  CG2 . THR   A 1 842  ? -76.60200  76.17200  -5.65100  1.000 50.04336  ?  840  THR   A CG2 1 
ATOM   6713  N  N   . TYR   A 1 843  ? -74.62300  73.58600  -8.76200  1.000 45.45650  ?  841  TYR   A N   1 
ATOM   6714  C  CA  . TYR   A 1 843  ? -74.32800  72.76300  -9.92600  1.000 44.55897  ?  841  TYR   A CA  1 
ATOM   6715  C  C   . TYR   A 1 843  ? -75.32300  71.61500  -10.00200 1.000 51.43706  ?  841  TYR   A C   1 
ATOM   6716  O  O   . TYR   A 1 843  ? -75.48100  70.85500  -9.04000  1.000 51.23781  ?  841  TYR   A O   1 
ATOM   6717  C  CB  . TYR   A 1 843  ? -72.89000  72.23200  -9.87300  1.000 44.87734  ?  841  TYR   A CB  1 
ATOM   6718  C  CG  . TYR   A 1 843  ? -71.84400  73.32600  -9.79700  1.000 50.61267  ?  841  TYR   A CG  1 
ATOM   6719  C  CD1 . TYR   A 1 843  ? -71.43100  73.83600  -8.57300  1.000 50.20983  ?  841  TYR   A CD1 1 
ATOM   6720  C  CD2 . TYR   A 1 843  ? -71.27500  73.85400  -10.95000 1.000 47.84161  ?  841  TYR   A CD2 1 
ATOM   6721  C  CE1 . TYR   A 1 843  ? -70.47900  74.83800  -8.49700  1.000 50.96414  ?  841  TYR   A CE1 1 
ATOM   6722  C  CE2 . TYR   A 1 843  ? -70.32000  74.85800  -10.88400 1.000 46.08906  ?  841  TYR   A CE2 1 
ATOM   6723  C  CZ  . TYR   A 1 843  ? -69.92600  75.34500  -9.65500  1.000 47.10782  ?  841  TYR   A CZ  1 
ATOM   6724  O  OH  . TYR   A 1 843  ? -68.97800  76.34200  -9.58000  1.000 41.67771  ?  841  TYR   A OH  1 
ATOM   6725  N  N   . HIS   A 1 844  ? -75.99100  71.49500  -11.14400 1.000 57.02053  ?  842  HIS   A N   1 
ATOM   6726  C  CA  . HIS   A 1 844  ? -77.01800  70.49000  -11.36400 1.000 43.31386  ?  842  HIS   A CA  1 
ATOM   6727  C  C   . HIS   A 1 844  ? -76.76100  69.81000  -12.70000 1.000 47.53273  ?  842  HIS   A C   1 
ATOM   6728  O  O   . HIS   A 1 844  ? -75.83800  70.16900  -13.43600 1.000 60.86423  ?  842  HIS   A O   1 
ATOM   6729  C  CB  . HIS   A 1 844  ? -78.41300  71.12100  -11.31800 1.000 39.07033  ?  842  HIS   A CB  1 
ATOM   6730  C  CG  . HIS   A 1 844  ? -78.54300  72.20400  -10.29500 1.000 42.24361  ?  842  HIS   A CG  1 
ATOM   6731  N  ND1 . HIS   A 1 844  ? -78.94900  71.95900  -9.00100  1.000 55.39433  ?  842  HIS   A ND1 1 
ATOM   6732  C  CD2 . HIS   A 1 844  ? -78.30100  73.53400  -10.36800 1.000 51.65723  ?  842  HIS   A CD2 1 
ATOM   6733  C  CE1 . HIS   A 1 844  ? -78.96200  73.09300  -8.32400  1.000 56.25014  ?  842  HIS   A CE1 1 
ATOM   6734  N  NE2 . HIS   A 1 844  ? -78.57300  74.06400  -9.13100  1.000 54.19803  ?  842  HIS   A NE2 1 
ATOM   6735  N  N   . MET   A 1 845  ? -77.59300  68.82200  -13.02000 1.000 47.67019  ?  843  MET   A N   1 
ATOM   6736  C  CA  . MET   A 1 845  ? -77.43300  68.04200  -14.24000 1.000 65.76257  ?  843  MET   A CA  1 
ATOM   6737  C  C   . MET   A 1 845  ? -78.71800  68.10000  -15.05400 1.000 79.49672  ?  843  MET   A C   1 
ATOM   6738  O  O   . MET   A 1 845  ? -79.77900  67.68000  -14.57800 1.000 68.96599  ?  843  MET   A O   1 
ATOM   6739  C  CB  . MET   A 1 845  ? -77.06200  66.59300  -13.91500 1.000 53.80457  ?  843  MET   A CB  1 
ATOM   6740  C  CG  . MET   A 1 845  ? -76.21800  65.93100  -14.98700 1.000 70.80545  ?  843  MET   A CG  1 
ATOM   6741  S  SD  . MET   A 1 845  ? -75.10300  64.67400  -14.33800 1.000 78.55670  ?  843  MET   A SD  1 
ATOM   6742  C  CE  . MET   A 1 845  ? -74.36600  64.07200  -15.85600 1.000 74.64065  ?  843  MET   A CE  1 
ATOM   6743  N  N   . ARG   A 1 846  ? -78.62000  68.61800  -16.28000 1.000 79.87118  ?  844  ARG   A N   1 
ATOM   6744  C  CA  . ARG   A 1 846  ? -79.73800  68.66600  -17.22300 1.000 62.07527  ?  844  ARG   A CA  1 
ATOM   6745  C  C   . ARG   A 1 846  ? -79.52400  67.56400  -18.25500 1.000 54.95453  ?  844  ARG   A C   1 
ATOM   6746  O  O   . ARG   A 1 846  ? -78.81500  67.75500  -19.24600 1.000 67.15597  ?  844  ARG   A O   1 
ATOM   6747  C  CB  . ARG   A 1 846  ? -79.83500  70.03600  -17.88500 1.000 68.56251  ?  844  ARG   A CB  1 
ATOM   6748  C  CG  . ARG   A 1 846  ? -80.71200  71.02700  -17.14500 1.000 73.57467  ?  844  ARG   A CG  1 
ATOM   6749  C  CD  . ARG   A 1 846  ? -81.97800  71.32400  -17.92800 1.000 61.09757  ?  844  ARG   A CD  1 
ATOM   6750  N  NE  . ARG   A 1 846  ? -82.59900  72.57100  -17.50000 1.000 77.49169  ?  844  ARG   A NE  1 
ATOM   6751  C  CZ  . ARG   A 1 846  ? -83.73600  72.65100  -16.82400 1.000 84.46888  ?  844  ARG   A CZ  1 
ATOM   6752  N  NH1 . ARG   A 1 846  ? -84.41300  71.56800  -16.47800 1.000 84.49535  ?  844  ARG   A NH1 1 
ATOM   6753  N  NH2 . ARG   A 1 846  ? -84.20800  73.84800  -16.48700 1.000 91.55263  ?  844  ARG   A NH2 1 
ATOM   6754  N  N   . GLY   A 1 847  ? -80.14300  66.41000  -18.02400 1.000 53.43061  ?  845  GLY   A N   1 
ATOM   6755  C  CA  . GLY   A 1 847  ? -79.90800  65.25600  -18.86900 1.000 58.99901  ?  845  GLY   A CA  1 
ATOM   6756  C  C   . GLY   A 1 847  ? -78.52400  64.67200  -18.66900 1.000 73.06466  ?  845  GLY   A C   1 
ATOM   6757  O  O   . GLY   A 1 847  ? -78.27500  63.97000  -17.68400 1.000 83.26874  ?  845  GLY   A O   1 
ATOM   6758  N  N   . ASP   A 1 848  ? -77.61200  64.94500  -19.60200 1.000 58.41624  ?  846  ASP   A N   1 
ATOM   6759  C  CA  . ASP   A 1 848  ? -76.21700  64.54800  -19.46200 1.000 70.68026  ?  846  ASP   A CA  1 
ATOM   6760  C  C   . ASP   A 1 848  ? -75.28500  65.74900  -19.37900 1.000 69.15989  ?  846  ASP   A C   1 
ATOM   6761  O  O   . ASP   A 1 848  ? -74.06600  65.58600  -19.50400 1.000 82.34471  ?  846  ASP   A O   1 
ATOM   6762  C  CB  . ASP   A 1 848  ? -75.79200  63.63600  -20.61800 1.000 71.61083  ?  846  ASP   A CB  1 
ATOM   6763  C  CG  . ASP   A 1 848  ? -76.49100  62.29000  -20.58800 1.000 90.26086  ?  846  ASP   A CG  1 
ATOM   6764  O  OD1 . ASP   A 1 848  ? -77.71700  62.26400  -20.35500 1.000 93.19292  ?  846  ASP   A OD1 1 
ATOM   6765  O  OD2 . ASP   A 1 848  ? -75.81400  61.26000  -20.79600 1.000 83.79555  -1 846  ASP   A OD2 1 
ATOM   6766  N  N   . GLU   A 1 849  ? -75.82300  66.94600  -19.16500 1.000 58.74254  ?  847  GLU   A N   1 
ATOM   6767  C  CA  . GLU   A 1 849  ? -75.04200  68.17400  -19.14100 1.000 74.38154  ?  847  GLU   A CA  1 
ATOM   6768  C  C   . GLU   A 1 849  ? -75.03400  68.75600  -17.73400 1.000 76.82948  ?  847  GLU   A C   1 
ATOM   6769  O  O   . GLU   A 1 849  ? -76.09200  68.93100  -17.12200 1.000 73.81040  ?  847  GLU   A O   1 
ATOM   6770  C  CB  . GLU   A 1 849  ? -75.60300  69.19500  -20.13300 1.000 59.34541  ?  847  GLU   A CB  1 
ATOM   6771  C  CG  . GLU   A 1 849  ? -75.06800  70.60100  -19.93500 1.000 72.51366  ?  847  GLU   A CG  1 
ATOM   6772  C  CD  . GLU   A 1 849  ? -74.70200  71.27600  -21.24100 1.000 96.05540  ?  847  GLU   A CD  1 
ATOM   6773  O  OE1 . GLU   A 1 849  ? -74.03200  70.63100  -22.07600 1.000 113.69764 ?  847  GLU   A OE1 1 
ATOM   6774  O  OE2 . GLU   A 1 849  ? -75.08000  72.45100  -21.43200 1.000 99.78847  ?  847  GLU   A OE2 1 
ATOM   6775  N  N   . ILE   A 1 850  ? -73.84200  69.05300  -17.22800 1.000 63.24991  ?  848  ILE   A N   1 
ATOM   6776  C  CA  . ILE   A 1 850  ? -73.68400  69.67700  -15.92000 1.000 58.81108  ?  848  ILE   A CA  1 
ATOM   6777  C  C   . ILE   A 1 850  ? -73.77300  71.18700  -16.09300 1.000 54.28716  ?  848  ILE   A C   1 
ATOM   6778  O  O   . ILE   A 1 850  ? -73.03400  71.77400  -16.89200 1.000 63.57541  ?  848  ILE   A O   1 
ATOM   6779  C  CB  . ILE   A 1 850  ? -72.35200  69.26200  -15.27400 1.000 52.40698  ?  848  ILE   A CB  1 
ATOM   6780  C  CG1 . ILE   A 1 850  ? -72.31800  67.74300  -15.08000 1.000 45.82279  ?  848  ILE   A CG1 1 
ATOM   6781  C  CG2 . ILE   A 1 850  ? -72.14400  69.99000  -13.95300 1.000 47.84833  ?  848  ILE   A CG2 1 
ATOM   6782  C  CD1 . ILE   A 1 850  ? -70.93600  67.13300  -15.18700 1.000 43.24520  ?  848  ILE   A CD1 1 
ATOM   6783  N  N   . VAL   A 1 851  ? -74.68300  71.81900  -15.35100 1.000 53.65654  ?  849  VAL   A N   1 
ATOM   6784  C  CA  . VAL   A 1 851  ? -74.96500  73.23800  -15.51000 1.000 57.93342  ?  849  VAL   A CA  1 
ATOM   6785  C  C   . VAL   A 1 851  ? -74.84200  73.94200  -14.16700 1.000 53.29528  ?  849  VAL   A C   1 
ATOM   6786  O  O   . VAL   A 1 851  ? -74.83000  73.31700  -13.10400 1.000 52.45509  ?  849  VAL   A O   1 
ATOM   6787  C  CB  . VAL   A 1 851  ? -76.36600  73.48300  -16.10800 1.000 55.92547  ?  849  VAL   A CB  1 
ATOM   6788  C  CG1 . VAL   A 1 851  ? -76.32200  73.34800  -17.61700 1.000 61.31674  ?  849  VAL   A CG1 1 
ATOM   6789  C  CG2 . VAL   A 1 851  ? -77.36100  72.50700  -15.51200 1.000 59.57791  ?  849  VAL   A CG2 1 
ATOM   6790  N  N   . LYS   A 1 852  ? -74.76200  75.26800  -14.23200 1.000 50.73304  ?  850  LYS   A N   1 
ATOM   6791  C  CA  . LYS   A 1 852  ? -74.62800  76.11800  -13.05900 1.000 47.61050  ?  850  LYS   A CA  1 
ATOM   6792  C  C   . LYS   A 1 852  ? -75.85600  77.00900  -12.92700 1.000 55.93838  ?  850  LYS   A C   1 
ATOM   6793  O  O   . LYS   A 1 852  ? -76.45500  77.41900  -13.92500 1.000 54.58279  ?  850  LYS   A O   1 
ATOM   6794  C  CB  . LYS   A 1 852  ? -73.35800  76.98000  -13.14400 1.000 45.73448  ?  850  LYS   A CB  1 
ATOM   6795  C  CG  . LYS   A 1 852  ? -72.99800  77.71500  -11.85900 1.000 49.17924  ?  850  LYS   A CG  1 
ATOM   6796  C  CD  . LYS   A 1 852  ? -72.07400  78.89300  -12.13600 1.000 47.24523  ?  850  LYS   A CD  1 
ATOM   6797  C  CE  . LYS   A 1 852  ? -70.60600  78.50500  -12.03200 1.000 50.25357  ?  850  LYS   A CE  1 
ATOM   6798  N  NZ  . LYS   A 1 852  ? -69.75700  79.69600  -11.74000 1.000 48.35899  ?  850  LYS   A NZ  1 
ATOM   6799  N  N   . ARG   A 1 853  ? -76.23300  77.30000  -11.68300 1.000 60.02344  ?  851  ARG   A N   1 
ATOM   6800  C  CA  . ARG   A 1 853  ? -77.35800  78.18100  -11.38800 1.000 61.56404  ?  851  ARG   A CA  1 
ATOM   6801  C  C   . ARG   A 1 853  ? -76.94400  79.14900  -10.29100 1.000 57.73475  ?  851  ARG   A C   1 
ATOM   6802  O  O   . ARG   A 1 853  ? -76.54800  78.72200  -9.20100  1.000 67.81859  ?  851  ARG   A O   1 
ATOM   6803  C  CB  . ARG   A 1 853  ? -78.59700  77.38500  -10.96500 1.000 52.27214  ?  851  ARG   A CB  1 
ATOM   6804  C  CG  . ARG   A 1 853  ? -79.23200  76.57300  -12.08300 1.000 44.71408  ?  851  ARG   A CG  1 
ATOM   6805  C  CD  . ARG   A 1 853  ? -80.49700  75.87000  -11.61200 1.000 48.23601  ?  851  ARG   A CD  1 
ATOM   6806  N  NE  . ARG   A 1 853  ? -80.78100  74.67700  -12.40200 1.000 62.87355  ?  851  ARG   A NE  1 
ATOM   6807  C  CZ  . ARG   A 1 853  ? -81.52500  73.66100  -11.98500 1.000 60.59775  ?  851  ARG   A CZ  1 
ATOM   6808  N  NH1 . ARG   A 1 853  ? -82.09000  73.66300  -10.78900 1.000 59.92716  ?  851  ARG   A NH1 1 
ATOM   6809  N  NH2 . ARG   A 1 853  ? -81.70100  72.61300  -12.78700 1.000 53.15733  ?  851  ARG   A NH2 1 
ATOM   6810  N  N   . ILE   A 1 854  ? -77.03500  80.43700  -10.57400 1.000 54.47007  ?  852  ILE   A N   1 
ATOM   6811  C  CA  . ILE   A 1 854  ? -76.68400  81.46900  -9.60600  1.000 57.83179  ?  852  ILE   A CA  1 
ATOM   6812  C  C   . ILE   A 1 854  ? -77.90400  81.78500  -8.75700  1.000 59.49149  ?  852  ILE   A C   1 
ATOM   6813  O  O   . ILE   A 1 854  ? -79.02400  81.89800  -9.26700  1.000 74.36971  ?  852  ILE   A O   1 
ATOM   6814  C  CB  . ILE   A 1 854  ? -76.15200  82.73100  -10.31000 1.000 53.60643  ?  852  ILE   A CB  1 
ATOM   6815  C  CG1 . ILE   A 1 854  ? -75.14100  82.35300  -11.39100 1.000 55.03807  ?  852  ILE   A CG1 1 
ATOM   6816  C  CG2 . ILE   A 1 854  ? -75.51900  83.67400  -9.29700  1.000 56.45628  ?  852  ILE   A CG2 1 
ATOM   6817  C  CD1 . ILE   A 1 854  ? -73.95200  81.60000  -10.86100 1.000 48.61010  ?  852  ILE   A CD1 1 
ATOM   6818  N  N   . VAL   A 1 855  ? -77.68800  81.92900  -7.45400  1.000 64.64766  ?  853  VAL   A N   1 
ATOM   6819  C  CA  . VAL   A 1 855  ? -78.76400  82.23800  -6.51700  1.000 53.83286  ?  853  VAL   A CA  1 
ATOM   6820  C  C   . VAL   A 1 855  ? -78.53100  83.65200  -5.99500  1.000 56.54753  ?  853  VAL   A C   1 
ATOM   6821  O  O   . VAL   A 1 855  ? -77.38700  84.01300  -5.68500  1.000 65.65428  ?  853  VAL   A O   1 
ATOM   6822  C  CB  . VAL   A 1 855  ? -78.82200  81.20300  -5.38200  1.000 54.63179  ?  853  VAL   A CB  1 
ATOM   6823  C  CG1 . VAL   A 1 855  ? -79.52200  81.77100  -4.17300  1.000 70.50754  ?  853  VAL   A CG1 1 
ATOM   6824  C  CG2 . VAL   A 1 855  ? -79.52600  79.93800  -5.85200  1.000 49.48078  ?  853  VAL   A CG2 1 
ATOM   6825  N  N   . PRO   A 1 856  ? -79.56900  84.48800  -5.90100  1.000 65.05388  ?  854  PRO   A N   1 
ATOM   6826  C  CA  . PRO   A 1 856  ? -79.34500  85.88700  -5.49700  1.000 47.17982  ?  854  PRO   A CA  1 
ATOM   6827  C  C   . PRO   A 1 856  ? -78.79300  86.05100  -4.09000  1.000 54.08376  ?  854  PRO   A C   1 
ATOM   6828  O  O   . PRO   A 1 856  ? -78.02600  86.99300  -3.85300  1.000 62.05445  ?  854  PRO   A O   1 
ATOM   6829  C  CB  . PRO   A 1 856  ? -80.73900  86.51700  -5.63000  1.000 49.43590  ?  854  PRO   A CB  1 
ATOM   6830  C  CG  . PRO   A 1 856  ? -81.69400  85.36200  -5.62200  1.000 70.73214  ?  854  PRO   A CG  1 
ATOM   6831  C  CD  . PRO   A 1 856  ? -80.96800  84.23700  -6.28200  1.000 68.84760  ?  854  PRO   A CD  1 
ATOM   6832  N  N   . ARG   A 1 857  ? -79.15600  85.18100  -3.14800  1.000 59.50676  ?  855  ARG   A N   1 
ATOM   6833  C  CA  . ARG   A 1 857  ? -78.64900  85.28900  -1.78500  1.000 60.46882  ?  855  ARG   A CA  1 
ATOM   6834  C  C   . ARG   A 1 857  ? -78.64200  83.91400  -1.13000  1.000 63.82291  ?  855  ARG   A C   1 
ATOM   6835  O  O   . ARG   A 1 857  ? -79.49800  83.07100  -1.40700  1.000 60.16450  ?  855  ARG   A O   1 
ATOM   6836  C  CB  . ARG   A 1 857  ? -79.47700  86.27200  -0.94300  1.000 63.57810  ?  855  ARG   A CB  1 
ATOM   6837  C  CG  . ARG   A 1 857  ? -80.84300  85.74600  -0.52200  1.000 95.45595  ?  855  ARG   A CG  1 
ATOM   6838  C  CD  . ARG   A 1 857  ? -81.23300  86.23600  0.86800   1.000 99.66610  ?  855  ARG   A CD  1 
ATOM   6839  N  NE  . ARG   A 1 857  ? -80.75300  85.34700  1.92000   1.000 102.17796 ?  855  ARG   A NE  1 
ATOM   6840  C  CZ  . ARG   A 1 857  ? -79.79500  85.65600  2.78400   1.000 96.93963  ?  855  ARG   A CZ  1 
ATOM   6841  N  NH1 . ARG   A 1 857  ? -79.19100  86.83300  2.75400   1.000 99.22593  ?  855  ARG   A NH1 1 
ATOM   6842  N  NH2 . ARG   A 1 857  ? -79.43700  84.76400  3.70400   1.000 79.20255  ?  855  ARG   A NH2 1 
ATOM   6843  N  N   . ALA   A 1 858  ? -77.66600  83.69900  -0.25000  1.000 66.39695  ?  856  ALA   A N   1 
ATOM   6844  C  CA  . ALA   A 1 858  ? -77.52900  82.43700  0.46000   1.000 62.60993  ?  856  ALA   A CA  1 
ATOM   6845  C  C   . ALA   A 1 858  ? -77.08500  82.70600  1.89000   1.000 73.24836  ?  856  ALA   A C   1 
ATOM   6846  O  O   . ALA   A 1 858  ? -76.39900  83.69500  2.16800   1.000 64.94243  ?  856  ALA   A O   1 
ATOM   6847  C  CB  . ALA   A 1 858  ? -76.53400  81.50200  -0.23600  1.000 63.47125  ?  856  ALA   A CB  1 
ATOM   6848  N  N   . GLU   A 1 859  ? -77.48300  81.81500  2.79600   1.000 67.10692  ?  857  GLU   A N   1 
ATOM   6849  C  CA  . GLU   A 1 859  ? -77.19700  81.96000  4.21700   1.000 66.99923  ?  857  GLU   A CA  1 
ATOM   6850  C  C   . GLU   A 1 859  ? -75.97300  81.13100  4.58800   1.000 61.21248  ?  857  GLU   A C   1 
ATOM   6851  O  O   . GLU   A 1 859  ? -75.84700  79.97300  4.17400   1.000 56.73806  ?  857  GLU   A O   1 
ATOM   6852  C  CB  . GLU   A 1 859  ? -78.40600  81.55500  5.06400   1.000 66.64223  ?  857  GLU   A CB  1 
ATOM   6853  C  CG  . GLU   A 1 859  ? -78.77600  80.07900  5.01000   1.000 89.43733  ?  857  GLU   A CG  1 
ATOM   6854  C  CD  . GLU   A 1 859  ? -79.91200  79.72700  5.95400   1.000 107.55814 ?  857  GLU   A CD  1 
ATOM   6855  O  OE1 . GLU   A 1 859  ? -80.58300  80.65700  6.45000   1.000 102.18608 ?  857  GLU   A OE1 1 
ATOM   6856  O  OE2 . GLU   A 1 859  ? -80.13200  78.52300  6.20400   1.000 111.36453 ?  857  GLU   A OE2 1 
ATOM   6857  N  N   . LEU   A 1 860  ? -75.07700  81.73100  5.36600   1.000 57.50102  ?  858  LEU   A N   1 
ATOM   6858  C  CA  . LEU   A 1 860  ? -73.81000  81.11200  5.72600   1.000 45.20806  ?  858  LEU   A CA  1 
ATOM   6859  C  C   . LEU   A 1 860  ? -73.92000  80.39800  7.06600   1.000 50.16724  ?  858  LEU   A C   1 
ATOM   6860  O  O   . LEU   A 1 860  ? -74.57100  80.88500  7.99400   1.000 47.75978  ?  858  LEU   A O   1 
ATOM   6861  C  CB  . LEU   A 1 860  ? -72.70600  82.16900  5.78500   1.000 44.55183  ?  858  LEU   A CB  1 
ATOM   6862  C  CG  . LEU   A 1 860  ? -71.26900  81.71200  6.01800   1.000 46.88131  ?  858  LEU   A CG  1 
ATOM   6863  C  CD1 . LEU   A 1 860  ? -70.85400  80.68800  4.98100   1.000 44.48115  ?  858  LEU   A CD1 1 
ATOM   6864  C  CD2 . LEU   A 1 860  ? -70.35200  82.91400  5.97700   1.000 45.80607  ?  858  LEU   A CD2 1 
ATOM   6865  N  N   . SER   A 1 861  ? -73.27700  79.23800  7.16100   1.000 54.51903  ?  859  SER   A N   1 
ATOM   6866  C  CA  . SER   A 1 861  ? -73.25600  78.45600  8.39400   1.000 30.49172  ?  859  SER   A CA  1 
ATOM   6867  C  C   . SER   A 1 861  ? -72.06700  78.92500  9.22500   1.000 47.52018  ?  859  SER   A C   1 
ATOM   6868  O  O   . SER   A 1 861  ? -70.92300  78.54900  8.96000   1.000 58.79287  ?  859  SER   A O   1 
ATOM   6869  C  CB  . SER   A 1 861  ? -73.17900  76.96600  8.08100   1.000 23.85019  ?  859  SER   A CB  1 
ATOM   6870  O  OG  . SER   A 1 861  ? -72.93500  76.20400  9.24800   1.000 48.31814  ?  859  SER   A OG  1 
ATOM   6871  N  N   . PHE   A 1 862  ? -72.33300  79.75900  10.22800  1.000 53.19556  ?  860  PHE   A N   1 
ATOM   6872  C  CA  . PHE   A 1 862  ? -71.30000  80.28700  11.11800  1.000 47.53622  ?  860  PHE   A CA  1 
ATOM   6873  C  C   . PHE   A 1 862  ? -71.50900  79.69100  12.50600  1.000 46.53526  ?  860  PHE   A C   1 
ATOM   6874  O  O   . PHE   A 1 862  ? -72.30700  80.20100  13.29600  1.000 58.43025  ?  860  PHE   A O   1 
ATOM   6875  C  CB  . PHE   A 1 862  ? -71.33500  81.81000  11.16000  1.000 42.69028  ?  860  PHE   A CB  1 
ATOM   6876  C  CG  . PHE   A 1 862  ? -70.03400  82.42400  11.56900  1.000 50.62348  ?  860  PHE   A CG  1 
ATOM   6877  C  CD1 . PHE   A 1 862  ? -69.05300  82.68000  10.62900  1.000 55.54248  ?  860  PHE   A CD1 1 
ATOM   6878  C  CD2 . PHE   A 1 862  ? -69.78600  82.73400  12.89400  1.000 48.38989  ?  860  PHE   A CD2 1 
ATOM   6879  C  CE1 . PHE   A 1 862  ? -67.85000  83.23900  11.00000  1.000 57.61537  ?  860  PHE   A CE1 1 
ATOM   6880  C  CE2 . PHE   A 1 862  ? -68.58400  83.29400  13.27100  1.000 55.02028  ?  860  PHE   A CE2 1 
ATOM   6881  C  CZ  . PHE   A 1 862  ? -67.61500  83.54700  12.32200  1.000 53.19562  ?  860  PHE   A CZ  1 
ATOM   6882  N  N   . VAL   A 1 863  ? -70.77900  78.62100  12.80300  1.000 46.14576  ?  861  VAL   A N   1 
ATOM   6883  C  CA  . VAL   A 1 863  ? -70.92300  77.89700  14.06100  1.000 42.04630  ?  861  VAL   A CA  1 
ATOM   6884  C  C   . VAL   A 1 863  ? -69.93200  78.46000  15.07300  1.000 50.57346  ?  861  VAL   A C   1 
ATOM   6885  O  O   . VAL   A 1 863  ? -68.71800  78.43900  14.84400  1.000 52.87658  ?  861  VAL   A O   1 
ATOM   6886  C  CB  . VAL   A 1 863  ? -70.70300  76.39100  13.85800  1.000 40.98935  ?  861  VAL   A CB  1 
ATOM   6887  C  CG1 . VAL   A 1 863  ? -70.92900  75.63600  15.16100  1.000 55.04157  ?  861  VAL   A CG1 1 
ATOM   6888  C  CG2 . VAL   A 1 863  ? -71.61700  75.86800  12.76500  1.000 45.92981  ?  861  VAL   A CG2 1 
ATOM   6889  N  N   . ARG   A 1 864  ? -70.44300  78.95400  16.19700  1.000 50.85449  ?  862  ARG   A N   1 
ATOM   6890  C  CA  . ARG   A 1 864  ? -69.60600  79.42600  17.29200  1.000 46.62674  ?  862  ARG   A CA  1 
ATOM   6891  C  C   . ARG   A 1 864  ? -69.46700  78.32300  18.33300  1.000 41.63718  ?  862  ARG   A C   1 
ATOM   6892  O  O   . ARG   A 1 864  ? -70.46900  77.75400  18.77900  1.000 42.95414  ?  862  ARG   A O   1 
ATOM   6893  C  CB  . ARG   A 1 864  ? -70.19000  80.68800  17.92700  1.000 33.97685  ?  862  ARG   A CB  1 
ATOM   6894  C  CG  . ARG   A 1 864  ? -70.18800  81.90100  17.00800  1.000 60.30489  ?  862  ARG   A CG  1 
ATOM   6895  C  CD  . ARG   A 1 864  ? -71.16200  82.96500  17.49500  1.000 56.57161  ?  862  ARG   A CD  1 
ATOM   6896  N  NE  . ARG   A 1 864  ? -71.87700  83.60700  16.39900  1.000 64.19905  ?  862  ARG   A NE  1 
ATOM   6897  C  CZ  . ARG   A 1 864  ? -72.83700  83.02800  15.68800  1.000 72.39550  ?  862  ARG   A CZ  1 
ATOM   6898  N  NH1 . ARG   A 1 864  ? -73.21700  81.78200  15.92400  1.000 53.36845  ?  862  ARG   A NH1 1 
ATOM   6899  N  NH2 . ARG   A 1 864  ? -73.43000  83.71800  14.71700  1.000 62.81960  ?  862  ARG   A NH2 1 
ATOM   6900  N  N   . GLN   A 1 865  ? -68.22900  78.01900  18.71500  1.000 40.70531  ?  863  GLN   A N   1 
ATOM   6901  C  CA  . GLN   A 1 865  ? -67.96300  76.95900  19.67700  1.000 39.98018  ?  863  GLN   A CA  1 
ATOM   6902  C  C   . GLN   A 1 865  ? -66.90000  77.41600  20.66600  1.000 43.26296  ?  863  GLN   A C   1 
ATOM   6903  O  O   . GLN   A 1 865  ? -66.08700  78.29600  20.37600  1.000 48.52730  ?  863  GLN   A O   1 
ATOM   6904  C  CB  . GLN   A 1 865  ? -67.50700  75.66700  18.98400  1.000 33.53684  ?  863  GLN   A CB  1 
ATOM   6905  C  CG  . GLN   A 1 865  ? -68.63000  74.82300  18.41100  1.000 38.80034  ?  863  GLN   A CG  1 
ATOM   6906  C  CD  . GLN   A 1 865  ? -68.11600  73.67700  17.56000  1.000 45.04560  ?  863  GLN   A CD  1 
ATOM   6907  O  OE1 . GLN   A 1 865  ? -68.39800  72.51100  17.83400  1.000 53.15226  ?  863  GLN   A OE1 1 
ATOM   6908  N  NE2 . GLN   A 1 865  ? -67.36100  74.00500  16.51600  1.000 36.92807  ?  863  GLN   A NE2 1 
ATOM   6909  N  N   . THR   A 1 866  ? -66.91500  76.80200  21.84400  1.000 47.60441  ?  864  THR   A N   1 
ATOM   6910  C  CA  . THR   A 1 866  ? -65.88900  77.00800  22.85600  1.000 50.78125  ?  864  THR   A CA  1 
ATOM   6911  C  C   . THR   A 1 866  ? -65.06600  75.73300  22.98700  1.000 53.05987  ?  864  THR   A C   1 
ATOM   6912  O  O   . THR   A 1 866  ? -65.62500  74.63200  23.05600  1.000 38.90230  ?  864  THR   A O   1 
ATOM   6913  C  CB  . THR   A 1 866  ? -66.50700  77.38700  24.20500  1.000 38.83461  ?  864  THR   A CB  1 
ATOM   6914  O  OG1 . THR   A 1 866  ? -67.67500  76.59000  24.43700  1.000 67.60568  ?  864  THR   A OG1 1 
ATOM   6915  C  CG2 . THR   A 1 866  ? -66.89400  78.85900  24.21800  1.000 56.09093  ?  864  THR   A CG2 1 
ATOM   6916  N  N   . GLY   A 1 867  ? -63.74300  75.87900  23.00900  1.000 38.18173  ?  865  GLY   A N   1 
ATOM   6917  C  CA  . GLY   A 1 867  ? -62.88200  74.71700  23.08600  1.000 46.25633  ?  865  GLY   A CA  1 
ATOM   6918  C  C   . GLY   A 1 867  ? -61.57200  75.03000  23.77100  1.000 44.69392  ?  865  GLY   A C   1 
ATOM   6919  O  O   . GLY   A 1 867  ? -61.27600  76.17700  24.11400  1.000 46.14933  ?  865  GLY   A O   1 
ATOM   6920  N  N   . GLU   A 1 868  ? -60.78800  73.97700  23.97200  1.000 49.35968  ?  866  GLU   A N   1 
ATOM   6921  C  CA  . GLU   A 1 868  ? -59.44900  74.05800  24.53300  1.000 39.16385  ?  866  GLU   A CA  1 
ATOM   6922  C  C   . GLU   A 1 868  ? -58.42200  73.72000  23.46000  1.000 50.43296  ?  866  GLU   A C   1 
ATOM   6923  O  O   . GLU   A 1 868  ? -58.75300  73.21000  22.38600  1.000 53.82360  ?  866  GLU   A O   1 
ATOM   6924  C  CB  . GLU   A 1 868  ? -59.30100  73.11100  25.73000  1.000 32.51722  ?  866  GLU   A CB  1 
ATOM   6925  C  CG  . GLU   A 1 868  ? -59.60700  71.65900  25.40500  1.000 52.93426  ?  866  GLU   A CG  1 
ATOM   6926  C  CD  . GLU   A 1 868  ? -59.73500  70.79200  26.64200  1.000 71.77067  ?  866  GLU   A CD  1 
ATOM   6927  O  OE1 . GLU   A 1 868  ? -59.69600  71.34500  27.76100  1.000 63.88956  ?  866  GLU   A OE1 1 
ATOM   6928  O  OE2 . GLU   A 1 868  ? -59.88300  69.55800  26.49500  1.000 82.03350  -1 866  GLU   A OE2 1 
ATOM   6929  N  N   . GLU   A 1 869  ? -57.15600  74.00300  23.77800  1.000 54.93956  ?  867  GLU   A N   1 
ATOM   6930  C  CA  . GLU   A 1 869  ? -56.07900  73.80000  22.81300  1.000 52.46202  ?  867  GLU   A CA  1 
ATOM   6931  C  C   . GLU   A 1 869  ? -56.03700  72.36300  22.31300  1.000 55.06836  ?  867  GLU   A C   1 
ATOM   6932  O  O   . GLU   A 1 869  ? -55.86400  72.11900  21.11200  1.000 68.05196  ?  867  GLU   A O   1 
ATOM   6933  C  CB  . GLU   A 1 869  ? -54.74100  74.18100  23.44100  1.000 49.13289  ?  867  GLU   A CB  1 
ATOM   6934  C  CG  . GLU   A 1 869  ? -54.36200  75.63400  23.25600  1.000 74.19047  ?  867  GLU   A CG  1 
ATOM   6935  C  CD  . GLU   A 1 869  ? -53.27900  75.80800  22.21900  1.000 82.16986  ?  867  GLU   A CD  1 
ATOM   6936  O  OE1 . GLU   A 1 869  ? -53.12900  74.90000  21.37400  1.000 74.98184  ?  867  GLU   A OE1 1 
ATOM   6937  O  OE2 . GLU   A 1 869  ? -52.56800  76.83500  22.25700  1.000 79.11303  -1 867  GLU   A OE2 1 
ATOM   6938  N  N   . GLU   A 1 870  ? -56.19500  71.39800  23.21500  1.000 40.63034  ?  868  GLU   A N   1 
ATOM   6939  C  CA  . GLU   A 1 870  ? -56.11800  69.98700  22.86500  1.000 49.61321  ?  868  GLU   A CA  1 
ATOM   6940  C  C   . GLU   A 1 870  ? -57.45100  69.42900  22.38300  1.000 46.96258  ?  868  GLU   A C   1 
ATOM   6941  O  O   . GLU   A 1 870  ? -57.60900  68.20700  22.29700  1.000 44.34441  ?  868  GLU   A O   1 
ATOM   6942  C  CB  . GLU   A 1 870  ? -55.59100  69.18600  24.06000  1.000 44.99496  ?  868  GLU   A CB  1 
ATOM   6943  C  CG  . GLU   A 1 870  ? -54.39200  69.85700  24.73300  1.000 52.21754  ?  868  GLU   A CG  1 
ATOM   6944  C  CD  . GLU   A 1 870  ? -53.71900  68.99000  25.78700  1.000 52.33855  ?  868  GLU   A CD  1 
ATOM   6945  O  OE1 . GLU   A 1 870  ? -54.26500  67.92200  26.13100  1.000 45.73719  ?  868  GLU   A OE1 1 
ATOM   6946  O  OE2 . GLU   A 1 870  ? -52.63900  69.38600  26.27800  1.000 52.41155  -1 868  GLU   A OE2 1 
ATOM   6947  N  N   . SER   A 1 871  ? -58.40700  70.29800  22.05900  1.000 42.59013  ?  869  SER   A N   1 
ATOM   6948  C  CA  . SER   A 1 871  ? -59.67200  69.87900  21.48000  1.000 42.99053  ?  869  SER   A CA  1 
ATOM   6949  C  C   . SER   A 1 871  ? -60.04200  70.62600  20.20800  1.000 40.49094  ?  869  SER   A C   1 
ATOM   6950  O  O   . SER   A 1 871  ? -60.99800  70.21600  19.54000  1.000 45.57186  ?  869  SER   A O   1 
ATOM   6951  C  CB  . SER   A 1 871  ? -60.80900  70.05100  22.49600  1.000 50.15582  ?  869  SER   A CB  1 
ATOM   6952  O  OG  . SER   A 1 871  ? -61.22100  71.40600  22.54800  1.000 40.79038  ?  869  SER   A OG  1 
ATOM   6953  N  N   . VAL   A 1 872  ? -59.32400  71.69900  19.85300  1.000 33.07345  ?  870  VAL   A N   1 
ATOM   6954  C  CA  . VAL   A 1 872  ? -59.68300  72.50200  18.68400  1.000 38.59492  ?  870  VAL   A CA  1 
ATOM   6955  C  C   . VAL   A 1 872  ? -59.74700  71.62900  17.43800  1.000 44.10088  ?  870  VAL   A C   1 
ATOM   6956  O  O   . VAL   A 1 872  ? -60.68300  71.72600  16.63300  1.000 45.28522  ?  870  VAL   A O   1 
ATOM   6957  C  CB  . VAL   A 1 872  ? -58.69100  73.66800  18.50600  1.000 36.95491  ?  870  VAL   A CB  1 
ATOM   6958  C  CG1 . VAL   A 1 872  ? -58.87100  74.32300  17.14500  1.000 25.61486  ?  870  VAL   A CG1 1 
ATOM   6959  C  CG2 . VAL   A 1 872  ? -58.88500  74.70000  19.60300  1.000 37.12424  ?  870  VAL   A CG2 1 
ATOM   6960  N  N   . GLN   A 1 873  ? -58.75900  70.74900  17.27200  1.000 37.34325  ?  871  GLN   A N   1 
ATOM   6961  C  CA  . GLN   A 1 873  ? -58.73500  69.86800  16.10900  1.000 38.28994  ?  871  GLN   A CA  1 
ATOM   6962  C  C   . GLN   A 1 873  ? -59.95600  68.95700  16.08100  1.000 39.07363  ?  871  GLN   A C   1 
ATOM   6963  O  O   . GLN   A 1 873  ? -60.60100  68.79500  15.03800  1.000 43.98796  ?  871  GLN   A O   1 
ATOM   6964  C  CB  . GLN   A 1 873  ? -57.45200  69.04100  16.11300  1.000 40.16621  ?  871  GLN   A CB  1 
ATOM   6965  C  CG  . GLN   A 1 873  ? -56.19300  69.84600  16.34100  1.000 47.17214  ?  871  GLN   A CG  1 
ATOM   6966  C  CD  . GLN   A 1 873  ? -54.95700  68.97800  16.29200  1.000 48.59582  ?  871  GLN   A CD  1 
ATOM   6967  O  OE1 . GLN   A 1 873  ? -54.40300  68.72500  15.22200  1.000 53.49228  ?  871  GLN   A OE1 1 
ATOM   6968  N  NE2 . GLN   A 1 873  ? -54.52500  68.50000  17.45300  1.000 51.82759  ?  871  GLN   A NE2 1 
ATOM   6969  N  N   . SER   A 1 874  ? -60.29000  68.35500  17.22500  1.000 46.23996  ?  872  SER   A N   1 
ATOM   6970  C  CA  . SER   A 1 874  ? -61.42300  67.43700  17.28700  1.000 45.81865  ?  872  SER   A CA  1 
ATOM   6971  C  C   . SER   A 1 874  ? -62.72400  68.14000  16.92200  1.000 37.43573  ?  872  SER   A C   1 
ATOM   6972  O  O   . SER   A 1 874  ? -63.53500  67.60700  16.15600  1.000 38.28852  ?  872  SER   A O   1 
ATOM   6973  C  CB  . SER   A 1 874  ? -61.51800  66.81800  18.67900  1.000 47.84690  ?  872  SER   A CB  1 
ATOM   6974  O  OG  . SER   A 1 874  ? -60.37700  66.02400  18.94800  1.000 80.58161  ?  872  SER   A OG  1 
ATOM   6975  N  N   . LEU   A 1 875  ? -62.94300  69.33800  17.46800  1.000 26.59028  ?  873  LEU   A N   1 
ATOM   6976  C  CA  . LEU   A 1 875  ? -64.12500  70.11100  17.10100  1.000 38.02111  ?  873  LEU   A CA  1 
ATOM   6977  C  C   . LEU   A 1 875  ? -64.17300  70.34800  15.59900  1.000 41.62888  ?  873  LEU   A C   1 
ATOM   6978  O  O   . LEU   A 1 875  ? -65.19900  70.11000  14.95000  1.000 54.36811  ?  873  LEU   A O   1 
ATOM   6979  C  CB  . LEU   A 1 875  ? -64.14100  71.44400  17.85000  1.000 40.41451  ?  873  LEU   A CB  1 
ATOM   6980  C  CG  . LEU   A 1 875  ? -64.22400  71.42200  19.37500  1.000 41.98123  ?  873  LEU   A CG  1 
ATOM   6981  C  CD1 . LEU   A 1 875  ? -63.65800  72.70800  19.95100  1.000 29.34119  ?  873  LEU   A CD1 1 
ATOM   6982  C  CD2 . LEU   A 1 875  ? -65.66200  71.23000  19.81600  1.000 43.43411  ?  873  LEU   A CD2 1 
ATOM   6983  N  N   . LEU   A 1 876  ? -63.05800  70.80500  15.02700  1.000 34.24803  ?  874  LEU   A N   1 
ATOM   6984  C  CA  . LEU   A 1 876  ? -63.02600  71.12300  13.60400  1.000 37.79860  ?  874  LEU   A CA  1 
ATOM   6985  C  C   . LEU   A 1 876  ? -63.21200  69.87900  12.74500  1.000 37.98717  ?  874  LEU   A C   1 
ATOM   6986  O  O   . LEU   A 1 876  ? -63.79600  69.95700  11.65800  1.000 42.86635  ?  874  LEU   A O   1 
ATOM   6987  C  CB  . LEU   A 1 876  ? -61.70900  71.81900  13.26800  1.000 25.41165  ?  874  LEU   A CB  1 
ATOM   6988  C  CG  . LEU   A 1 876  ? -61.31700  71.99800  11.80400  1.000 44.34705  ?  874  LEU   A CG  1 
ATOM   6989  C  CD1 . LEU   A 1 876  ? -62.37600  72.78800  11.03800  1.000 44.22465  ?  874  LEU   A CD1 1 
ATOM   6990  C  CD2 . LEU   A 1 876  ? -59.97200  72.68800  11.73600  1.000 42.50337  ?  874  LEU   A CD2 1 
ATOM   6991  N  N   . ALA   A 1 877  ? -62.73300  68.72500  13.21500  1.000 33.20627  ?  875  ALA   A N   1 
ATOM   6992  C  CA  . ALA   A 1 877  ? -62.85200  67.50200  12.43000  1.000 29.85446  ?  875  ALA   A CA  1 
ATOM   6993  C  C   . ALA   A 1 877  ? -64.30900  67.10900  12.23600  1.000 40.95578  ?  875  ALA   A C   1 
ATOM   6994  O  O   . ALA   A 1 877  ? -64.70000  66.65700  11.15300  1.000 52.90885  ?  875  ALA   A O   1 
ATOM   6995  C  CB  . ALA   A 1 877  ? -62.07500  66.37000  13.10200  1.000 30.93522  ?  875  ALA   A CB  1 
ATOM   6996  N  N   . GLU   A 1 878  ? -65.13100  67.28000  13.27100  1.000 43.23450  ?  876  GLU   A N   1 
ATOM   6997  C  CA  . GLU   A 1 878  ? -66.54900  66.95900  13.17900  1.000 43.34828  ?  876  GLU   A CA  1 
ATOM   6998  C  C   . GLU   A 1 878  ? -67.32600  67.94600  12.31600  1.000 40.16407  ?  876  GLU   A C   1 
ATOM   6999  O  O   . GLU   A 1 878  ? -68.53600  67.76600  12.14300  1.000 56.34102  ?  876  GLU   A O   1 
ATOM   7000  C  CB  . GLU   A 1 878  ? -67.15900  66.89600  14.58300  1.000 41.03303  ?  876  GLU   A CB  1 
ATOM   7001  C  CG  . GLU   A 1 878  ? -68.10700  65.71900  14.80200  1.000 69.16586  ?  876  GLU   A CG  1 
ATOM   7002  C  CD  . GLU   A 1 878  ? -67.37800  64.39600  14.98400  1.000 82.20033  ?  876  GLU   A CD  1 
ATOM   7003  O  OE1 . GLU   A 1 878  ? -66.13000  64.40300  15.04300  1.000 90.66088  ?  876  GLU   A OE1 1 
ATOM   7004  O  OE2 . GLU   A 1 878  ? -68.05300  63.34700  15.06600  1.000 77.77863  -1 876  GLU   A OE2 1 
ATOM   7005  N  N   . GLN   A 1 879  ? -66.67000  68.97000  11.77000  1.000 39.25987  ?  877  GLN   A N   1 
ATOM   7006  C  CA  . GLN   A 1 879  ? -67.33200  69.97400  10.95200  1.000 48.22775  ?  877  GLN   A CA  1 
ATOM   7007  C  C   . GLN   A 1 879  ? -67.01500  69.84900  9.47100   1.000 44.08102  ?  877  GLN   A C   1 
ATOM   7008  O  O   . GLN   A 1 879  ? -67.68900  70.48800  8.65400   1.000 52.76521  ?  877  GLN   A O   1 
ATOM   7009  C  CB  . GLN   A 1 879  ? -66.95400  71.38100  11.43400  1.000 46.68079  ?  877  GLN   A CB  1 
ATOM   7010  C  CG  . GLN   A 1 879  ? -67.18600  71.59100  12.91500  1.000 40.87303  ?  877  GLN   A CG  1 
ATOM   7011  C  CD  . GLN   A 1 879  ? -68.48500  72.30700  13.19600  1.000 51.32252  ?  877  GLN   A CD  1 
ATOM   7012  O  OE1 . GLN   A 1 879  ? -69.56600  71.74600  13.02000  1.000 62.81047  ?  877  GLN   A OE1 1 
ATOM   7013  N  NE2 . GLN   A 1 879  ? -68.38900  73.55400  13.64200  1.000 55.05171  ?  877  GLN   A NE2 1 
ATOM   7014  N  N   . ILE   A 1 880  ? -66.00700  69.06100  9.10300   1.000 40.40058  ?  878  ILE   A N   1 
ATOM   7015  C  CA  . ILE   A 1 880  ? -65.75800  68.74900  7.70300   1.000 39.09992  ?  878  ILE   A CA  1 
ATOM   7016  C  C   . ILE   A 1 880  ? -66.73700  67.67100  7.26700   1.000 35.19625  ?  878  ILE   A C   1 
ATOM   7017  O  O   . ILE   A 1 880  ? -66.48300  66.47400  7.45500   1.000 27.31660  ?  878  ILE   A O   1 
ATOM   7018  C  CB  . ILE   A 1 880  ? -64.30400  68.30300  7.46500   1.000 22.04896  ?  878  ILE   A CB  1 
ATOM   7019  C  CG1 . ILE   A 1 880  ? -63.32800  69.34600  8.01100   1.000 30.48118  ?  878  ILE   A CG1 1 
ATOM   7020  C  CG2 . ILE   A 1 880  ? -64.07000  68.06900  5.99000   1.000 29.74679  ?  878  ILE   A CG2 1 
ATOM   7021  C  CD1 . ILE   A 1 880  ? -62.07100  68.75100  8.60300   1.000 41.01331  ?  878  ILE   A CD1 1 
ATOM   7022  N  N   . LYS   A 1 881  ? -67.85900  68.08700  6.69800   1.000 46.48355  ?  879  LYS   A N   1 
ATOM   7023  C  CA  . LYS   A 1 881  ? -68.88300  67.19400  6.18400   1.000 52.48220  ?  879  LYS   A CA  1 
ATOM   7024  C  C   . LYS   A 1 881  ? -68.97000  67.31000  4.66700   1.000 47.53673  ?  879  LYS   A C   1 
ATOM   7025  O  O   . LYS   A 1 881  ? -68.57100  68.32800  4.08900   1.000 38.13719  ?  879  LYS   A O   1 
ATOM   7026  C  CB  . LYS   A 1 881  ? -70.24800  67.51400  6.81700   1.000 42.70021  ?  879  LYS   A CB  1 
ATOM   7027  C  CG  . LYS   A 1 881  ? -70.35500  67.13000  8.29200   1.000 41.26214  ?  879  LYS   A CG  1 
ATOM   7028  C  CD  . LYS   A 1 881  ? -70.87800  68.28900  9.13500   1.000 60.31376  ?  879  LYS   A CD  1 
ATOM   7029  C  CE  . LYS   A 1 881  ? -71.37900  67.82200  10.49900  1.000 57.26143  ?  879  LYS   A CE  1 
ATOM   7030  N  NZ  . LYS   A 1 881  ? -71.50800  68.94700  11.47900  1.000 54.32919  ?  879  LYS   A NZ  1 
ATOM   7031  N  N   . PRO   A 1 882  ? -69.46000  66.27300  3.98600   1.000 37.99408  ?  880  PRO   A N   1 
ATOM   7032  C  CA  . PRO   A 1 882  ? -69.57300  66.33700  2.52600   1.000 31.79789  ?  880  PRO   A CA  1 
ATOM   7033  C  C   . PRO   A 1 882  ? -70.45500  67.49200  2.08000   1.000 36.83232  ?  880  PRO   A C   1 
ATOM   7034  O  O   . PRO   A 1 882  ? -71.32100  67.97500  2.81300   1.000 42.45452  ?  880  PRO   A O   1 
ATOM   7035  C  CB  . PRO   A 1 882  ? -70.19500  64.98600  2.15700   1.000 33.10197  ?  880  PRO   A CB  1 
ATOM   7036  C  CG  . PRO   A 1 882  ? -69.80000  64.08200  3.27100   1.000 46.45427  ?  880  PRO   A CG  1 
ATOM   7037  C  CD  . PRO   A 1 882  ? -69.77800  64.93300  4.50700   1.000 49.16915  ?  880  PRO   A CD  1 
ATOM   7038  N  N   . PHE   A 1 883  ? -70.20800  67.94300  0.85500   1.000 39.08099  ?  881  PHE   A N   1 
ATOM   7039  C  CA  . PHE   A 1 883  ? -70.94600  69.03900  0.24800   1.000 38.42774  ?  881  PHE   A CA  1 
ATOM   7040  C  C   . PHE   A 1 883  ? -71.89700  68.49900  -0.80800  1.000 40.10757  ?  881  PHE   A C   1 
ATOM   7041  O  O   . PHE   A 1 883  ? -71.53600  67.60600  -1.58300  1.000 54.91711  ?  881  PHE   A O   1 
ATOM   7042  C  CB  . PHE   A 1 883  ? -69.99900  70.04900  -0.40200  1.000 40.08483  ?  881  PHE   A CB  1 
ATOM   7043  C  CG  . PHE   A 1 883  ? -69.52700  71.12800  0.52300   1.000 38.14560  ?  881  PHE   A CG  1 
ATOM   7044  C  CD1 . PHE   A 1 883  ? -70.30800  72.24600  0.75800   1.000 40.57457  ?  881  PHE   A CD1 1 
ATOM   7045  C  CD2 . PHE   A 1 883  ? -68.29000  71.03600  1.14000   1.000 43.65748  ?  881  PHE   A CD2 1 
ATOM   7046  C  CE1 . PHE   A 1 883  ? -69.87100  73.24900  1.60200   1.000 52.23060  ?  881  PHE   A CE1 1 
ATOM   7047  C  CE2 . PHE   A 1 883  ? -67.84600  72.03600  1.98500   1.000 48.47172  ?  881  PHE   A CE2 1 
ATOM   7048  C  CZ  . PHE   A 1 883  ? -68.63800  73.14300  2.21700   1.000 50.87099  ?  881  PHE   A CZ  1 
ATOM   7049  N  N   . ASP   A 1 884  ? -73.11200  69.03900  -0.83500  1.000 47.59016  ?  882  ASP   A N   1 
ATOM   7050  C  CA  . ASP   A 1 884  ? -74.03400  68.81700  -1.94300  1.000 43.46884  ?  882  ASP   A CA  1 
ATOM   7051  C  C   . ASP   A 1 884  ? -73.85500  69.96800  -2.92100  1.000 49.53026  ?  882  ASP   A C   1 
ATOM   7052  O  O   . ASP   A 1 884  ? -74.18400  71.11600  -2.60500  1.000 51.76081  ?  882  ASP   A O   1 
ATOM   7053  C  CB  . ASP   A 1 884  ? -75.47800  68.73100  -1.45900  1.000 62.34103  ?  882  ASP   A CB  1 
ATOM   7054  C  CG  . ASP   A 1 884  ? -76.42300  68.20500  -2.52800  1.000 64.20228  ?  882  ASP   A CG  1 
ATOM   7055  O  OD1 . ASP   A 1 884  ? -76.15800  68.41400  -3.73200  1.000 61.32627  ?  882  ASP   A OD1 1 
ATOM   7056  O  OD2 . ASP   A 1 884  ? -77.43600  67.57500  -2.15900  1.000 74.66045  -1 882  ASP   A OD2 1 
ATOM   7057  N  N   . LEU   A 1 885  ? -73.33700  69.66000  -4.11100  1.000 38.58498  ?  883  LEU   A N   1 
ATOM   7058  C  CA  . LEU   A 1 885  ? -73.01300  70.71000  -5.06800  1.000 43.30950  ?  883  LEU   A CA  1 
ATOM   7059  C  C   . LEU   A 1 885  ? -74.24600  71.45000  -5.56400  1.000 41.41736  ?  883  LEU   A C   1 
ATOM   7060  O  O   . LEU   A 1 885  ? -74.10900  72.52300  -6.16100  1.000 47.35755  ?  883  LEU   A O   1 
ATOM   7061  C  CB  . LEU   A 1 885  ? -72.23000  70.11100  -6.23800  1.000 38.56166  ?  883  LEU   A CB  1 
ATOM   7062  C  CG  . LEU   A 1 885  ? -70.83200  69.62100  -5.84800  1.000 40.28201  ?  883  LEU   A CG  1 
ATOM   7063  C  CD1 . LEU   A 1 885  ? -70.12600  68.93900  -7.00900  1.000 47.95918  ?  883  LEU   A CD1 1 
ATOM   7064  C  CD2 . LEU   A 1 885  ? -70.00400  70.78400  -5.33600  1.000 41.74375  ?  883  LEU   A CD2 1 
ATOM   7065  N  N   . ALA   A 1 886  ? -75.44000  70.92000  -5.31100  1.000 41.39260  ?  884  ALA   A N   1 
ATOM   7066  C  CA  . ALA   A 1 886  ? -76.66500  71.60000  -5.70000  1.000 50.78821  ?  884  ALA   A CA  1 
ATOM   7067  C  C   . ALA   A 1 886  ? -77.10600  72.65400  -4.69200  1.000 46.27481  ?  884  ALA   A C   1 
ATOM   7068  O  O   . ALA   A 1 886  ? -78.06600  73.38100  -4.96500  1.000 45.58602  ?  884  ALA   A O   1 
ATOM   7069  C  CB  . ALA   A 1 886  ? -77.78200  70.57300  -5.90900  1.000 27.10236  ?  884  ALA   A CB  1 
ATOM   7070  N  N   . LYS   A 1 887  ? -76.42900  72.76800  -3.55100  1.000 43.46469  ?  885  LYS   A N   1 
ATOM   7071  C  CA  . LYS   A 1 887  ? -76.81800  73.69300  -2.49500  1.000 46.85040  ?  885  LYS   A CA  1 
ATOM   7072  C  C   . LYS   A 1 887  ? -75.69300  74.68200  -2.22000  1.000 45.12803  ?  885  LYS   A C   1 
ATOM   7073  O  O   . LYS   A 1 887  ? -74.51500  74.31100  -2.19300  1.000 52.03772  ?  885  LYS   A O   1 
ATOM   7074  C  CB  . LYS   A 1 887  ? -77.18100  72.93900  -1.21200  1.000 43.79647  ?  885  LYS   A CB  1 
ATOM   7075  C  CG  . LYS   A 1 887  ? -78.04100  71.70700  -1.44700  1.000 46.03963  ?  885  LYS   A CG  1 
ATOM   7076  C  CD  . LYS   A 1 887  ? -79.15400  71.59900  -0.41800  1.000 48.20213  ?  885  LYS   A CD  1 
ATOM   7077  C  CE  . LYS   A 1 887  ? -79.32200  70.16700  0.06800   1.000 68.69265  ?  885  LYS   A CE  1 
ATOM   7078  N  NZ  . LYS   A 1 887  ? -80.65900  69.94000  0.68900   1.000 90.08336  ?  885  LYS   A NZ  1 
ATOM   7079  N  N   . ALA   A 1 888  ? -76.06700  75.94200  -2.01300  1.000 43.07039  ?  886  ALA   A N   1 
ATOM   7080  C  CA  . ALA   A 1 888  ? -75.14500  77.04000  -1.79300  1.000 32.53155  ?  886  ALA   A CA  1 
ATOM   7081  C  C   . ALA   A 1 888  ? -75.43700  77.71100  -0.45600  1.000 43.82287  ?  886  ALA   A C   1 
ATOM   7082  O  O   . ALA   A 1 888  ? -76.56700  77.65100  0.03700   1.000 54.20562  ?  886  ALA   A O   1 
ATOM   7083  C  CB  . ALA   A 1 888  ? -75.24400  78.07700  -2.92000  1.000 39.59789  ?  886  ALA   A CB  1 
ATOM   7084  N  N   . PRO   A 1 889  ? -74.44100  78.35700  0.16000   1.000 49.80444  ?  887  PRO   A N   1 
ATOM   7085  C  CA  . PRO   A 1 889  ? -73.05600  78.53700  -0.29100  1.000 43.98557  ?  887  PRO   A CA  1 
ATOM   7086  C  C   . PRO   A 1 889  ? -72.23200  77.26500  -0.13900  1.000 49.63096  ?  887  PRO   A C   1 
ATOM   7087  O  O   . PRO   A 1 889  ? -72.45500  76.46400  0.76800   1.000 48.97261  ?  887  PRO   A O   1 
ATOM   7088  C  CB  . PRO   A 1 889  ? -72.55500  79.66800  0.61300   1.000 34.01656  ?  887  PRO   A CB  1 
ATOM   7089  C  CG  . PRO   A 1 889  ? -73.29600  79.44600  1.89500   1.000 40.95142  ?  887  PRO   A CG  1 
ATOM   7090  C  CD  . PRO   A 1 889  ? -74.66600  78.97600  1.47800   1.000 45.96647  ?  887  PRO   A CD  1 
ATOM   7091  N  N   . LEU   A 1 890  ? -71.27900  77.04400  -1.04000  1.000 50.34508  ?  888  LEU   A N   1 
ATOM   7092  C  CA  . LEU   A 1 890  ? -70.33800  75.93600  -0.91000  1.000 44.33218  ?  888  LEU   A CA  1 
ATOM   7093  C  C   . LEU   A 1 890  ? -69.18000  76.27700  0.01900   1.000 50.59706  ?  888  LEU   A C   1 
ATOM   7094  O  O   . LEU   A 1 890  ? -68.02000  75.96900  -0.26600  1.000 37.74704  ?  888  LEU   A O   1 
ATOM   7095  C  CB  . LEU   A 1 890  ? -69.83800  75.52700  -2.29300  1.000 36.69797  ?  888  LEU   A CB  1 
ATOM   7096  C  CG  . LEU   A 1 890  ? -70.87600  74.80200  -3.15500  1.000 34.06131  ?  888  LEU   A CG  1 
ATOM   7097  C  CD1 . LEU   A 1 890  ? -70.52000  74.90800  -4.62500  1.000 39.02947  ?  888  LEU   A CD1 1 
ATOM   7098  C  CD2 . LEU   A 1 890  ? -71.01600  73.34300  -2.74500  1.000 32.05805  ?  888  LEU   A CD2 1 
ATOM   7099  N  N   . LEU   A 1 891  ? -69.48700  76.93100  1.13800   1.000 51.88959  ?  889  LEU   A N   1 
ATOM   7100  C  CA  . LEU   A 1 891  ? -68.50400  77.27500  2.15300   1.000 46.35737  ?  889  LEU   A CA  1 
ATOM   7101  C  C   . LEU   A 1 891  ? -69.19800  77.29500  3.50600   1.000 48.82290  ?  889  LEU   A C   1 
ATOM   7102  O  O   . LEU   A 1 891  ? -70.26200  77.90400  3.64600   1.000 51.59004  ?  889  LEU   A O   1 
ATOM   7103  C  CB  . LEU   A 1 891  ? -67.85900  78.63500  1.86700   1.000 47.46967  ?  889  LEU   A CB  1 
ATOM   7104  C  CG  . LEU   A 1 891  ? -66.79600  79.10500  2.86000   1.000 40.05951  ?  889  LEU   A CG  1 
ATOM   7105  C  CD1 . LEU   A 1 891  ? -65.51900  79.47200  2.13100   1.000 46.86519  ?  889  LEU   A CD1 1 
ATOM   7106  C  CD2 . LEU   A 1 891  ? -67.30500  80.28300  3.67200   1.000 32.10949  ?  889  LEU   A CD2 1 
ATOM   7107  N  N   . ARG   A 1 892  ? -68.60600  76.61900  4.48700   1.000 52.38433  ?  890  ARG   A N   1 
ATOM   7108  C  CA  . ARG   A 1 892  ? -69.06100  76.66200  5.86800   1.000 39.99482  ?  890  ARG   A CA  1 
ATOM   7109  C  C   . ARG   A 1 892  ? -67.94300  77.22700  6.73100   1.000 42.03185  ?  890  ARG   A C   1 
ATOM   7110  O  O   . ARG   A 1 892  ? -66.76100  77.01900  6.44800   1.000 57.12710  ?  890  ARG   A O   1 
ATOM   7111  C  CB  . ARG   A 1 892  ? -69.47000  75.27200  6.36800   1.000 36.02108  ?  890  ARG   A CB  1 
ATOM   7112  C  CG  . ARG   A 1 892  ? -70.49800  74.58200  5.48100   1.000 38.57606  ?  890  ARG   A CG  1 
ATOM   7113  C  CD  . ARG   A 1 892  ? -70.54800  73.08800  5.74800   1.000 38.34406  ?  890  ARG   A CD  1 
ATOM   7114  N  NE  . ARG   A 1 892  ? -71.37300  72.37900  4.77700   1.000 36.63538  ?  890  ARG   A NE  1 
ATOM   7115  C  CZ  . ARG   A 1 892  ? -71.09400  71.17300  4.30100   1.000 51.14801  ?  890  ARG   A CZ  1 
ATOM   7116  N  NH1 . ARG   A 1 892  ? -70.00600  70.51700  4.67500   1.000 49.59552  ?  890  ARG   A NH1 1 
ATOM   7117  N  NH2 . ARG   A 1 892  ? -71.92600  70.61000  3.42900   1.000 40.20023  ?  890  ARG   A NH2 1 
ATOM   7118  N  N   . ALA   A 1 893  ? -68.31700  77.94800  7.78400   1.000 44.36065  ?  891  ALA   A N   1 
ATOM   7119  C  CA  . ALA   A 1 893  ? -67.34100  78.67900  8.58200   1.000 38.92660  ?  891  ALA   A CA  1 
ATOM   7120  C  C   . ALA   A 1 893  ? -67.69000  78.52800  10.06000  1.000 40.18666  ?  891  ALA   A C   1 
ATOM   7121  O  O   . ALA   A 1 893  ? -68.60200  77.78400  10.43400  1.000 49.69878  ?  891  ALA   A O   1 
ATOM   7122  C  CB  . ALA   A 1 893  ? -67.28300  80.14700  8.14200   1.000 33.25035  ?  891  ALA   A CB  1 
ATOM   7123  N  N   . GLY   A 1 894  ? -66.95300  79.23900  10.89800  1.000 44.42807  ?  892  GLY   A N   1 
ATOM   7124  C  CA  . GLY   A 1 894  ? -67.14800  79.20200  12.33200  1.000 42.91684  ?  892  GLY   A CA  1 
ATOM   7125  C  C   . GLY   A 1 894  ? -65.89500  79.62100  13.06100  1.000 46.34637  ?  892  GLY   A C   1 
ATOM   7126  O  O   . GLY   A 1 894  ? -64.79200  79.62700  12.51200  1.000 55.98762  ?  892  GLY   A O   1 
ATOM   7127  N  N   . VAL   A 1 895  ? -66.07300  79.98200  14.33100  1.000 45.63869  ?  893  VAL   A N   1 
ATOM   7128  C  CA  . VAL   A 1 895  ? -64.97800  80.44800  15.17800  1.000 44.62229  ?  893  VAL   A CA  1 
ATOM   7129  C  C   . VAL   A 1 895  ? -64.96900  79.63000  16.46300  1.000 40.80959  ?  893  VAL   A C   1 
ATOM   7130  O  O   . VAL   A 1 895  ? -65.94600  79.64700  17.22200  1.000 48.78662  ?  893  VAL   A O   1 
ATOM   7131  C  CB  . VAL   A 1 895  ? -65.09100  81.94900  15.50000  1.000 35.06773  ?  893  VAL   A CB  1 
ATOM   7132  C  CG1 . VAL   A 1 895  ? -64.13100  82.32600  16.62400  1.000 43.03182  ?  893  VAL   A CG1 1 
ATOM   7133  C  CG2 . VAL   A 1 895  ? -64.80600  82.77800  14.26200  1.000 37.31513  ?  893  VAL   A CG2 1 
ATOM   7134  N  N   . ILE   A 1 896  ? -63.86900  78.92200  16.70700  1.000 38.45964  ?  894  ILE   A N   1 
ATOM   7135  C  CA  . ILE   A 1 896  ? -63.64800  78.22400  17.96900  1.000 35.42673  ?  894  ILE   A CA  1 
ATOM   7136  C  C   . ILE   A 1 896  ? -62.86900  79.14800  18.89500  1.000 38.95248  ?  894  ILE   A C   1 
ATOM   7137  O  O   . ILE   A 1 896  ? -61.73800  79.54000  18.58600  1.000 46.70470  ?  894  ILE   A O   1 
ATOM   7138  C  CB  . ILE   A 1 896  ? -62.89500  76.90300  17.75800  1.000 28.79972  ?  894  ILE   A CB  1 
ATOM   7139  C  CG1 . ILE   A 1 896  ? -63.73100  75.92400  16.93900  1.000 37.15873  ?  894  ILE   A CG1 1 
ATOM   7140  C  CG2 . ILE   A 1 896  ? -62.51800  76.28300  19.09100  1.000 26.78155  ?  894  ILE   A CG2 1 
ATOM   7141  C  CD1 . ILE   A 1 896  ? -62.92800  74.76500  16.40800  1.000 22.44331  ?  894  ILE   A CD1 1 
ATOM   7142  N  N   . GLU   A 1 897  ? -63.46600  79.48800  20.03200  1.000 48.18517  ?  895  GLU   A N   1 
ATOM   7143  C  CA  . GLU   A 1 897  ? -62.86700  80.41400  20.98500  1.000 47.14690  ?  895  GLU   A CA  1 
ATOM   7144  C  C   . GLU   A 1 897  ? -62.23700  79.63200  22.13000  1.000 46.14951  ?  895  GLU   A C   1 
ATOM   7145  O  O   . GLU   A 1 897  ? -62.92000  78.85800  22.81100  1.000 41.72164  ?  895  GLU   A O   1 
ATOM   7146  C  CB  . GLU   A 1 897  ? -63.90900  81.39500  21.51900  1.000 42.78407  ?  895  GLU   A CB  1 
ATOM   7147  C  CG  . GLU   A 1 897  ? -63.39600  82.28700  22.63500  1.000 51.57021  ?  895  GLU   A CG  1 
ATOM   7148  C  CD  . GLU   A 1 897  ? -64.32500  83.44700  22.92600  1.000 65.96823  ?  895  GLU   A CD  1 
ATOM   7149  O  OE1 . GLU   A 1 897  ? -65.27100  83.66300  22.14000  1.000 72.02641  ?  895  GLU   A OE1 1 
ATOM   7150  O  OE2 . GLU   A 1 897  ? -64.10500  84.14900  23.93500  1.000 77.31498  -1 895  GLU   A OE2 1 
ATOM   7151  N  N   . THR   A 1 898  ? -60.93800  79.82900  22.33100  1.000 43.11915  ?  896  THR   A N   1 
ATOM   7152  C  CA  . THR   A 1 898  ? -60.21500  79.29400  23.47300  1.000 49.34256  ?  896  THR   A CA  1 
ATOM   7153  C  C   . THR   A 1 898  ? -59.89800  80.43600  24.43500  1.000 47.26473  ?  896  THR   A C   1 
ATOM   7154  O  O   . THR   A 1 898  ? -60.32800  81.57800  24.24200  1.000 62.57806  ?  896  THR   A O   1 
ATOM   7155  C  CB  . THR   A 1 898  ? -58.94500  78.56600  23.02200  1.000 44.85624  ?  896  THR   A CB  1 
ATOM   7156  O  OG1 . THR   A 1 898  ? -57.88400  79.51300  22.84400  1.000 57.00815  ?  896  THR   A OG1 1 
ATOM   7157  C  CG2 . THR   A 1 898  ? -59.18500  77.82300  21.71900  1.000 44.22274  ?  896  THR   A CG2 1 
ATOM   7158  N  N   . ALA   A 1 899  ? -59.13300  80.12600  25.47800  1.000 43.15375  ?  897  ALA   A N   1 
ATOM   7159  C  CA  . ALA   A 1 899  ? -58.77100  81.13200  26.46600  1.000 48.74986  ?  897  ALA   A CA  1 
ATOM   7160  C  C   . ALA   A 1 899  ? -57.63900  82.04100  26.00600  1.000 59.63565  ?  897  ALA   A C   1 
ATOM   7161  O  O   . ALA   A 1 899  ? -57.30200  82.98900  26.72200  1.000 68.58235  ?  897  ALA   A O   1 
ATOM   7162  C  CB  . ALA   A 1 899  ? -58.38800  80.45900  27.78600  1.000 38.97910  ?  897  ALA   A CB  1 
ATOM   7163  N  N   . ASP   A 1 900  ? -57.04700  81.78300  24.83800  1.000 62.52997  ?  898  ASP   A N   1 
ATOM   7164  C  CA  . ASP   A 1 900  ? -55.94900  82.59600  24.34000  1.000 53.73748  ?  898  ASP   A CA  1 
ATOM   7165  C  C   . ASP   A 1 900  ? -56.08200  82.99400  22.87600  1.000 57.48581  ?  898  ASP   A C   1 
ATOM   7166  O  O   . ASP   A 1 900  ? -55.30900  83.84600  22.42300  1.000 73.68808  ?  898  ASP   A O   1 
ATOM   7167  C  CB  . ASP   A 1 900  ? -54.60500  81.87100  24.53400  1.000 56.35979  ?  898  ASP   A CB  1 
ATOM   7168  C  CG  . ASP   A 1 900  ? -54.45800  80.65600  23.63400  1.000 87.07123  ?  898  ASP   A CG  1 
ATOM   7169  O  OD1 . ASP   A 1 900  ? -55.37500  79.80600  23.61800  1.000 89.95949  ?  898  ASP   A OD1 1 
ATOM   7170  O  OD2 . ASP   A 1 900  ? -53.42200  80.55000  22.94200  1.000 79.82419  -1 898  ASP   A OD2 1 
ATOM   7171  N  N   . LYS   A 1 901  ? -57.02600  82.42400  22.12900  1.000 55.28095  ?  899  LYS   A N   1 
ATOM   7172  C  CA  . LYS   A 1 901  ? -57.14600  82.72100  20.71000  1.000 53.91920  ?  899  LYS   A CA  1 
ATOM   7173  C  C   . LYS   A 1 901  ? -58.57600  82.48100  20.25000  1.000 54.66051  ?  899  LYS   A C   1 
ATOM   7174  O  O   . LYS   A 1 901  ? -59.36600  81.81100  20.92000  1.000 52.37465  ?  899  LYS   A O   1 
ATOM   7175  C  CB  . LYS   A 1 901  ? -56.18100  81.86900  19.87300  1.000 47.01113  ?  899  LYS   A CB  1 
ATOM   7176  C  CG  . LYS   A 1 901  ? -56.24800  80.37900  20.18400  1.000 52.07918  ?  899  LYS   A CG  1 
ATOM   7177  C  CD  . LYS   A 1 901  ? -55.28500  79.57100  19.32300  1.000 43.40050  ?  899  LYS   A CD  1 
ATOM   7178  C  CE  . LYS   A 1 901  ? -54.74600  78.36800  20.08800  1.000 62.70006  ?  899  LYS   A CE  1 
ATOM   7179  N  NZ  . LYS   A 1 901  ? -54.85600  77.09200  19.32700  1.000 42.05498  ?  899  LYS   A NZ  1 
ATOM   7180  N  N   . LYS   A 1 902  ? -58.89700  83.04600  19.08700  1.000 51.29324  ?  900  LYS   A N   1 
ATOM   7181  C  CA  . LYS   A 1 902  ? -60.13500  82.76600  18.36700  1.000 50.78461  ?  900  LYS   A CA  1 
ATOM   7182  C  C   . LYS   A 1 902  ? -59.74900  82.14900  17.03000  1.000 49.99461  ?  900  LYS   A C   1 
ATOM   7183  O  O   . LYS   A 1 902  ? -59.13000  82.81300  16.19300  1.000 49.84806  ?  900  LYS   A O   1 
ATOM   7184  C  CB  . LYS   A 1 902  ? -60.96700  84.03200  18.17100  1.000 47.85304  ?  900  LYS   A CB  1 
ATOM   7185  C  CG  . LYS   A 1 902  ? -61.77100  84.45500  19.39000  1.000 58.82051  ?  900  LYS   A CG  1 
ATOM   7186  C  CD  . LYS   A 1 902  ? -62.52000  85.75100  19.12400  1.000 56.49760  ?  900  LYS   A CD  1 
ATOM   7187  C  CE  . LYS   A 1 902  ? -63.56600  86.01900  20.19200  1.000 60.30285  ?  900  LYS   A CE  1 
ATOM   7188  N  NZ  . LYS   A 1 902  ? -64.49700  87.11700  19.80400  1.000 69.63408  ?  900  LYS   A NZ  1 
ATOM   7189  N  N   . VAL   A 1 903  ? -60.10100  80.88200  16.83400  1.000 44.95305  ?  901  VAL   A N   1 
ATOM   7190  C  CA  . VAL   A 1 903  ? -59.70000  80.12600  15.65300  1.000 35.23730  ?  901  VAL   A CA  1 
ATOM   7191  C  C   . VAL   A 1 903  ? -60.83900  80.18300  14.64500  1.000 37.14643  ?  901  VAL   A C   1 
ATOM   7192  O  O   . VAL   A 1 903  ? -61.86900  79.52300  14.81600  1.000 38.32636  ?  901  VAL   A O   1 
ATOM   7193  C  CB  . VAL   A 1 903  ? -59.34100  78.67500  16.00300  1.000 42.96118  ?  901  VAL   A CB  1 
ATOM   7194  C  CG1 . VAL   A 1 903  ? -58.87300  77.93100  14.76300  1.000 36.85865  ?  901  VAL   A CG1 1 
ATOM   7195  C  CG2 . VAL   A 1 903  ? -58.26900  78.64000  17.07700  1.000 44.42242  ?  901  VAL   A CG2 1 
ATOM   7196  N  N   . LEU   A 1 904  ? -60.66100  80.97600  13.59400  1.000 41.30324  ?  902  LEU   A N   1 
ATOM   7197  C  CA  . LEU   A 1 904  ? -61.59800  80.96500  12.48000  1.000 42.98101  ?  902  LEU   A CA  1 
ATOM   7198  C  C   . LEU   A 1 904  ? -61.27600  79.79400  11.56300  1.000 42.08633  ?  902  LEU   A C   1 
ATOM   7199  O  O   . LEU   A 1 904  ? -60.12300  79.61000  11.16300  1.000 49.58918  ?  902  LEU   A O   1 
ATOM   7200  C  CB  . LEU   A 1 904  ? -61.53500  82.27800  11.70100  1.000 38.52896  ?  902  LEU   A CB  1 
ATOM   7201  C  CG  . LEU   A 1 904  ? -62.17800  82.23200  10.31200  1.000 37.70666  ?  902  LEU   A CG  1 
ATOM   7202  C  CD1 . LEU   A 1 904  ? -63.69800  82.13600  10.40900  1.000 36.28777  ?  902  LEU   A CD1 1 
ATOM   7203  C  CD2 . LEU   A 1 904  ? -61.75200  83.43500  9.47500   1.000 27.30493  ?  902  LEU   A CD2 1 
ATOM   7204  N  N   . TRP   A 1 905  ? -62.28800  78.99600  11.24600  1.000 38.48154  ?  903  TRP   A N   1 
ATOM   7205  C  CA  . TRP   A 1 905  ? -62.15600  77.90900  10.29200  1.000 34.37988  ?  903  TRP   A CA  1 
ATOM   7206  C  C   . TRP   A 1 905  ? -63.16400  78.11000  9.17000   1.000 39.32333  ?  903  TRP   A C   1 
ATOM   7207  O  O   . TRP   A 1 905  ? -64.26500  78.62000  9.39300   1.000 45.55020  ?  903  TRP   A O   1 
ATOM   7208  C  CB  . TRP   A 1 905  ? -62.36700  76.53900  10.96600  1.000 36.66265  ?  903  TRP   A CB  1 
ATOM   7209  C  CG  . TRP   A 1 905  ? -63.78200  76.27600  11.39300  1.000 38.93155  ?  903  TRP   A CG  1 
ATOM   7210  C  CD1 . TRP   A 1 905  ? -64.33300  76.54500  12.61100  1.000 37.78493  ?  903  TRP   A CD1 1 
ATOM   7211  C  CD2 . TRP   A 1 905  ? -64.82500  75.68800  10.60300  1.000 45.02618  ?  903  TRP   A CD2 1 
ATOM   7212  N  NE1 . TRP   A 1 905  ? -65.65300  76.16800  12.62900  1.000 50.31050  ?  903  TRP   A NE1 1 
ATOM   7213  C  CE2 . TRP   A 1 905  ? -65.98000  75.63800  11.40800  1.000 50.10296  ?  903  TRP   A CE2 1 
ATOM   7214  C  CE3 . TRP   A 1 905  ? -64.89500  75.20200  9.29400   1.000 37.47844  ?  903  TRP   A CE3 1 
ATOM   7215  C  CZ2 . TRP   A 1 905  ? -67.19000  75.12000  10.94800  1.000 46.19537  ?  903  TRP   A CZ2 1 
ATOM   7216  C  CZ3 . TRP   A 1 905  ? -66.09800  74.69000  8.83800   1.000 44.06295  ?  903  TRP   A CZ3 1 
ATOM   7217  C  CH2 . TRP   A 1 905  ? -67.22800  74.65400  9.66200   1.000 48.18858  ?  903  TRP   A CH2 1 
ATOM   7218  N  N   . PHE   A 1 906  ? -62.77800  77.73200  7.95400   1.000 33.97434  ?  904  PHE   A N   1 
ATOM   7219  C  CA  . PHE   A 1 906  ? -63.73400  77.68700  6.85900   1.000 44.16760  ?  904  PHE   A CA  1 
ATOM   7220  C  C   . PHE   A 1 906  ? -63.43400  76.48900  5.97100   1.000 46.70467  ?  904  PHE   A C   1 
ATOM   7221  O  O   . PHE   A 1 906  ? -62.27400  76.10600  5.80000   1.000 51.68506  ?  904  PHE   A O   1 
ATOM   7222  C  CB  . PHE   A 1 906  ? -63.75700  79.00000  6.04800   1.000 42.42466  ?  904  PHE   A CB  1 
ATOM   7223  C  CG  . PHE   A 1 906  ? -62.48500  79.30100  5.29800   1.000 39.34020  ?  904  PHE   A CG  1 
ATOM   7224  C  CD1 . PHE   A 1 906  ? -62.25000  78.75500  4.04500   1.000 43.28696  ?  904  PHE   A CD1 1 
ATOM   7225  C  CD2 . PHE   A 1 906  ? -61.54600  80.16900  5.83000   1.000 37.79143  ?  904  PHE   A CD2 1 
ATOM   7226  C  CE1 . PHE   A 1 906  ? -61.08900  79.04700  3.35000   1.000 51.17962  ?  904  PHE   A CE1 1 
ATOM   7227  C  CE2 . PHE   A 1 906  ? -60.38400  80.46500  5.13900   1.000 61.43624  ?  904  PHE   A CE2 1 
ATOM   7228  C  CZ  . PHE   A 1 906  ? -60.15800  79.90500  3.89700   1.000 51.31263  ?  904  PHE   A CZ  1 
ATOM   7229  N  N   . ASP   A 1 907  ? -64.49400  75.89300  5.43000   1.000 42.38361  ?  905  ASP   A N   1 
ATOM   7230  C  CA  . ASP   A 1 907  ? -64.40800  74.68900  4.61300   1.000 44.47299  ?  905  ASP   A CA  1 
ATOM   7231  C  C   . ASP   A 1 907  ? -65.14600  74.94400  3.30800   1.000 52.05111  ?  905  ASP   A C   1 
ATOM   7232  O  O   . ASP   A 1 907  ? -66.34100  75.25700  3.32200   1.000 47.15808  ?  905  ASP   A O   1 
ATOM   7233  C  CB  . ASP   A 1 907  ? -65.00600  73.48500  5.35300   1.000 46.48745  ?  905  ASP   A CB  1 
ATOM   7234  C  CG  . ASP   A 1 907  ? -64.97200  72.20000  4.53100   1.000 62.58824  ?  905  ASP   A CG  1 
ATOM   7235  O  OD1 . ASP   A 1 907  ? -64.24000  72.14000  3.51900   1.000 71.36125  ?  905  ASP   A OD1 1 
ATOM   7236  O  OD2 . ASP   A 1 907  ? -65.69600  71.24600  4.89700   1.000 53.17691  -1 905  ASP   A OD2 1 
ATOM   7237  N  N   . SER   A 1 908  ? -64.42400  74.84900  2.19100   1.000 47.87326  ?  906  SER   A N   1 
ATOM   7238  C  CA  . SER   A 1 908  ? -65.03200  75.02700  0.84900   1.000 52.31109  ?  906  SER   A CA  1 
ATOM   7239  C  C   . SER   A 1 908  ? -64.80200  73.78000  -0.00300  1.000 47.39930  ?  906  SER   A C   1 
ATOM   7240  O  O   . SER   A 1 908  ? -64.30000  72.78900  0.52600   1.000 46.63408  ?  906  SER   A O   1 
ATOM   7241  C  CB  . SER   A 1 908  ? -64.48700  76.23600  0.15700   1.000 32.50548  ?  906  SER   A CB  1 
ATOM   7242  O  OG  . SER   A 1 908  ? -65.36600  76.67000  -0.86500  1.000 46.24601  ?  906  SER   A OG  1 
ATOM   7243  N  N   . HIS   A 1 909  ? -65.20900  73.83200  -1.26700  1.000 43.95342  ?  907  HIS   A N   1 
ATOM   7244  C  CA  . HIS   A 1 909  ? -64.98300  72.71000  -2.21000  1.000 47.76679  ?  907  HIS   A CA  1 
ATOM   7245  C  C   . HIS   A 1 909  ? -64.05000  73.24300  -3.29800  1.000 49.77293  ?  907  HIS   A C   1 
ATOM   7246  O  O   . HIS   A 1 909  ? -64.03200  74.45900  -3.53300  1.000 48.50789  ?  907  HIS   A O   1 
ATOM   7247  C  CB  . HIS   A 1 909  ? -66.32500  72.20100  -2.74600  1.000 29.97691  ?  907  HIS   A CB  1 
ATOM   7248  C  CG  . HIS   A 1 909  ? -66.28300  70.87300  -3.41700  1.000 26.62324  ?  907  HIS   A CG  1 
ATOM   7249  N  ND1 . HIS   A 1 909  ? -65.94300  70.71500  -4.74100  1.000 38.59236  ?  907  HIS   A ND1 1 
ATOM   7250  C  CD2 . HIS   A 1 909  ? -66.55400  69.65300  -2.95700  1.000 36.31732  ?  907  HIS   A CD2 1 
ATOM   7251  C  CE1 . HIS   A 1 909  ? -65.99900  69.43200  -5.05400  1.000 39.24038  ?  907  HIS   A CE1 1 
ATOM   7252  N  NE2 . HIS   A 1 909  ? -66.36900  68.77100  -3.98400  1.000 33.64697  ?  907  HIS   A NE2 1 
ATOM   7253  N  N   . HIS   A 1 910  ? -63.29500  72.36000  -3.94500  1.000 38.25745  ?  908  HIS   A N   1 
ATOM   7254  C  CA  . HIS   A 1 910  ? -62.32300  72.80800  -4.97100  1.000 45.61576  ?  908  HIS   A CA  1 
ATOM   7255  C  C   . HIS   A 1 910  ? -63.07800  73.42600  -6.14500  1.000 45.82250  ?  908  HIS   A C   1 
ATOM   7256  O  O   . HIS   A 1 910  ? -62.48600  74.23400  -6.86100  1.000 61.04394  ?  908  HIS   A O   1 
ATOM   7257  C  CB  . HIS   A 1 910  ? -61.42800  71.65200  -5.41800  1.000 49.28169  ?  908  HIS   A CB  1 
ATOM   7258  C  CG  . HIS   A 1 910  ? -59.98400  72.00000  -5.49300  1.000 50.56646  ?  908  HIS   A CG  1 
ATOM   7259  N  ND1 . HIS   A 1 910  ? -59.53700  73.29200  -5.64400  1.000 57.80017  ?  908  HIS   A ND1 1 
ATOM   7260  C  CD2 . HIS   A 1 910  ? -58.89400  71.23300  -5.44500  1.000 56.86903  ?  908  HIS   A CD2 1 
ATOM   7261  C  CE1 . HIS   A 1 910  ? -58.21500  73.29400  -5.68500  1.000 70.88492  ?  908  HIS   A CE1 1 
ATOM   7262  N  NE2 . HIS   A 1 910  ? -57.80500  72.05300  -5.56400  1.000 83.35120  ?  908  HIS   A NE2 1 
ATOM   7263  N  N   . ILE   A 1 911  ? -64.34400  73.06200  -6.31900  1.000 45.14168  ?  909  ILE   A N   1 
ATOM   7264  C  CA  . ILE   A 1 911  ? -65.17400  73.62700  -7.41900  1.000 42.53524  ?  909  ILE   A CA  1 
ATOM   7265  C  C   . ILE   A 1 911  ? -65.20500  75.15300  -7.30800  1.000 32.97247  ?  909  ILE   A C   1 
ATOM   7266  O  O   . ILE   A 1 911  ? -65.54200  75.79800  -8.30100  1.000 45.63749  ?  909  ILE   A O   1 
ATOM   7267  C  CB  . ILE   A 1 911  ? -66.58400  73.00500  -7.40800  1.000 53.58704  ?  909  ILE   A CB  1 
ATOM   7268  C  CG1 . ILE   A 1 911  ? -67.23700  73.05900  -8.79200  1.000 53.17888  ?  909  ILE   A CG1 1 
ATOM   7269  C  CG2 . ILE   A 1 911  ? -67.45800  73.63900  -6.33800  1.000 50.43386  ?  909  ILE   A CG2 1 
ATOM   7270  C  CD1 . ILE   A 1 911  ? -67.99500  71.81100  -9.16400  1.000 43.85171  ?  909  ILE   A CD1 1 
ATOM   7271  N  N   . LEU   A 1 912  ? -64.83500  75.70600  -6.15700  1.000 31.55512  ?  910  LEU   A N   1 
ATOM   7272  C  CA  . LEU   A 1 912  ? -64.90100  77.15300  -5.99800  1.000 35.28448  ?  910  LEU   A CA  1 
ATOM   7273  C  C   . LEU   A 1 912  ? -63.59600  77.76400  -5.50800  1.000 44.88878  ?  910  LEU   A C   1 
ATOM   7274  O  O   . LEU   A 1 912  ? -63.21900  78.84100  -5.97500  1.000 59.98863  ?  910  LEU   A O   1 
ATOM   7275  C  CB  . LEU   A 1 912  ? -66.05400  77.51400  -5.03500  1.000 33.17507  ?  910  LEU   A CB  1 
ATOM   7276  C  CG  . LEU   A 1 912  ? -66.00200  78.80700  -4.21200  1.000 41.21130  ?  910  LEU   A CG  1 
ATOM   7277  C  CD1 . LEU   A 1 912  ? -66.01100  80.06300  -5.08400  1.000 43.31212  ?  910  LEU   A CD1 1 
ATOM   7278  C  CD2 . LEU   A 1 912  ? -67.15800  78.84600  -3.22600  1.000 52.66753  ?  910  LEU   A CD2 1 
ATOM   7279  N  N   . LEU   A 1 913  ? -62.88900  77.10400  -4.59400  1.000 41.44489  ?  911  LEU   A N   1 
ATOM   7280  C  CA  . LEU   A 1 913  ? -61.70300  77.67000  -3.95600  1.000 46.88213  ?  911  LEU   A CA  1 
ATOM   7281  C  C   . LEU   A 1 913  ? -60.45100  76.99200  -4.49900  1.000 47.11758  ?  911  LEU   A C   1 
ATOM   7282  O  O   . LEU   A 1 913  ? -60.22900  75.80200  -4.25900  1.000 51.34192  ?  911  LEU   A O   1 
ATOM   7283  C  CB  . LEU   A 1 913  ? -61.78100  77.52500  -2.43800  1.000 45.18889  ?  911  LEU   A CB  1 
ATOM   7284  C  CG  . LEU   A 1 913  ? -61.27600  78.73200  -1.64800  1.000 49.52801  ?  911  LEU   A CG  1 
ATOM   7285  C  CD1 . LEU   A 1 913  ? -62.04500  79.98800  -2.02300  1.000 42.94025  ?  911  LEU   A CD1 1 
ATOM   7286  C  CD2 . LEU   A 1 913  ? -61.37400  78.46200  -0.15600  1.000 57.33393  ?  911  LEU   A CD2 1 
ATOM   7287  N  N   . ASP   A 1 914  ? -59.63600  77.75100  -5.21700  1.000 41.89623  ?  912  ASP   A N   1 
ATOM   7288  C  CA  . ASP   A 1 914  ? -58.33100  77.28900  -5.66200  1.000 37.49090  ?  912  ASP   A CA  1 
ATOM   7289  C  C   . ASP   A 1 914  ? -57.26200  78.19100  -5.04300  1.000 44.17905  ?  912  ASP   A C   1 
ATOM   7290  O  O   . ASP   A 1 914  ? -57.54500  78.99100  -4.14500  1.000 46.28035  ?  912  ASP   A O   1 
ATOM   7291  C  CB  . ASP   A 1 914  ? -58.27100  77.22800  -7.19500  1.000 36.66093  ?  912  ASP   A CB  1 
ATOM   7292  C  CG  . ASP   A 1 914  ? -58.13700  78.59500  -7.85000  1.000 40.72942  ?  912  ASP   A CG  1 
ATOM   7293  O  OD1 . ASP   A 1 914  ? -58.53000  79.60900  -7.24100  1.000 53.03704  ?  912  ASP   A OD1 1 
ATOM   7294  O  OD2 . ASP   A 1 914  ? -57.64600  78.64900  -8.99900  1.000 48.21699  -1 912  ASP   A OD2 1 
ATOM   7295  N  N   . GLY   A 1 915  ? -56.02700  78.04800  -5.52100  1.000 43.65981  ?  913  GLY   A N   1 
ATOM   7296  C  CA  . GLY   A 1 915  ? -54.90300  78.79100  -4.98500  1.000 45.05120  ?  913  GLY   A CA  1 
ATOM   7297  C  C   . GLY   A 1 915  ? -55.11500  80.28900  -4.97400  1.000 37.46087  ?  913  GLY   A C   1 
ATOM   7298  O  O   . GLY   A 1 915  ? -55.05800  80.92400  -3.91600  1.000 41.96487  ?  913  GLY   A O   1 
ATOM   7299  N  N   . LEU   A 1 916  ? -55.37300  80.86600  -6.15000  1.000 40.97205  ?  914  LEU   A N   1 
ATOM   7300  C  CA  . LEU   A 1 916  ? -55.57800  82.30900  -6.22500  1.000 44.81564  ?  914  LEU   A CA  1 
ATOM   7301  C  C   . LEU   A 1 916  ? -56.85100  82.72500  -5.50100  1.000 37.19064  ?  914  LEU   A C   1 
ATOM   7302  O  O   . LEU   A 1 916  ? -56.85200  83.72300  -4.77100  1.000 46.55033  ?  914  LEU   A O   1 
ATOM   7303  C  CB  . LEU   A 1 916  ? -55.60900  82.76500  -7.68400  1.000 37.07827  ?  914  LEU   A CB  1 
ATOM   7304  C  CG  . LEU   A 1 916  ? -55.48200  84.27600  -7.90600  1.000 51.30257  ?  914  LEU   A CG  1 
ATOM   7305  C  CD1 . LEU   A 1 916  ? -54.45700  84.90000  -6.96500  1.000 48.44367  ?  914  LEU   A CD1 1 
ATOM   7306  C  CD2 . LEU   A 1 916  ? -55.11400  84.57000  -9.34600  1.000 51.71578  ?  914  LEU   A CD2 1 
ATOM   7307  N  N   . SER   A 1 917  ? -57.93700  81.96100  -5.67000  1.000 36.22279  ?  915  SER   A N   1 
ATOM   7308  C  CA  . SER   A 1 917  ? -59.18600  82.28200  -4.98200  1.000 42.14044  ?  915  SER   A CA  1 
ATOM   7309  C  C   . SER   A 1 917  ? -58.97500  82.39300  -3.48000  1.000 44.21818  ?  915  SER   A C   1 
ATOM   7310  O  O   . SER   A 1 917  ? -59.58100  83.24400  -2.82100  1.000 59.98010  ?  915  SER   A O   1 
ATOM   7311  C  CB  . SER   A 1 917  ? -60.25300  81.22800  -5.28500  1.000 47.03013  ?  915  SER   A CB  1 
ATOM   7312  O  OG  . SER   A 1 917  ? -60.45400  81.07400  -6.68100  1.000 44.28744  ?  915  SER   A OG  1 
ATOM   7313  N  N   . LYS   A 1 918  ? -58.11000  81.54300  -2.92400  1.000 42.81594  ?  916  LYS   A N   1 
ATOM   7314  C  CA  . LYS   A 1 918  ? -57.78700  81.64300  -1.50600  1.000 34.80560  ?  916  LYS   A CA  1 
ATOM   7315  C  C   . LYS   A 1 918  ? -57.07400  82.95400  -1.19600  1.000 41.32746  ?  916  LYS   A C   1 
ATOM   7316  O  O   . LYS   A 1 918  ? -57.31700  83.56500  -0.14800  1.000 46.86261  ?  916  LYS   A O   1 
ATOM   7317  C  CB  . LYS   A 1 918  ? -56.93500  80.44900  -1.08100  1.000 35.08217  ?  916  LYS   A CB  1 
ATOM   7318  C  CG  . LYS   A 1 918  ? -56.37700  80.54400  0.32400   1.000 39.44916  ?  916  LYS   A CG  1 
ATOM   7319  C  CD  . LYS   A 1 918  ? -55.05100  79.81400  0.42400   1.000 46.85694  ?  916  LYS   A CD  1 
ATOM   7320  C  CE  . LYS   A 1 918  ? -53.90400  80.66400  -0.09500  1.000 44.95795  ?  916  LYS   A CE  1 
ATOM   7321  N  NZ  . LYS   A 1 918  ? -52.69800  79.84000  -0.38700  1.000 55.48085  ?  916  LYS   A NZ  1 
ATOM   7322  N  N   . SER   A 1 919  ? -56.20400  83.41200  -2.10000  1.000 35.46537  ?  917  SER   A N   1 
ATOM   7323  C  CA  . SER   A 1 919  ? -55.47600  84.65300  -1.85100  1.000 52.80373  ?  917  SER   A CA  1 
ATOM   7324  C  C   . SER   A 1 919  ? -56.38700  85.87300  -1.92700  1.000 42.70095  ?  917  SER   A C   1 
ATOM   7325  O  O   . SER   A 1 919  ? -56.16400  86.85200  -1.20700  1.000 54.20881  ?  917  SER   A O   1 
ATOM   7326  C  CB  . SER   A 1 919  ? -54.31200  84.79900  -2.83400  1.000 51.25521  ?  917  SER   A CB  1 
ATOM   7327  O  OG  . SER   A 1 919  ? -53.54400  83.61000  -2.90900  1.000 63.30561  ?  917  SER   A OG  1 
ATOM   7328  N  N   . ILE   A 1 920  ? -57.40900  85.84000  -2.78700  1.000 40.00712  ?  918  ILE   A N   1 
ATOM   7329  C  CA  . ILE   A 1 920  ? -58.34000  86.96400  -2.86600  1.000 51.93931  ?  918  ILE   A CA  1 
ATOM   7330  C  C   . ILE   A 1 920  ? -59.27400  86.97100  -1.66200  1.000 46.70217  ?  918  ILE   A C   1 
ATOM   7331  O  O   . ILE   A 1 920  ? -59.55300  88.02800  -1.08300  1.000 49.40160  ?  918  ILE   A O   1 
ATOM   7332  C  CB  . ILE   A 1 920  ? -59.12200  86.92700  -4.19100  1.000 42.15209  ?  918  ILE   A CB  1 
ATOM   7333  C  CG1 . ILE   A 1 920  ? -58.26400  86.32100  -5.29900  1.000 41.46029  ?  918  ILE   A CG1 1 
ATOM   7334  C  CG2 . ILE   A 1 920  ? -59.56300  88.32300  -4.58000  1.000 68.43133  ?  918  ILE   A CG2 1 
ATOM   7335  C  CD1 . ILE   A 1 920  ? -58.92300  86.32200  -6.65200  1.000 40.51215  ?  918  ILE   A CD1 1 
ATOM   7336  N  N   . LEU   A 1 921  ? -59.77400  85.79600  -1.27100  1.000 41.01895  ?  919  LEU   A N   1 
ATOM   7337  C  CA  . LEU   A 1 921  ? -60.56800  85.69100  -0.05000  1.000 44.77082  ?  919  LEU   A CA  1 
ATOM   7338  C  C   . LEU   A 1 921  ? -59.80400  86.23100  1.15400   1.000 49.50632  ?  919  LEU   A C   1 
ATOM   7339  O  O   . LEU   A 1 921  ? -60.39000  86.87400  2.03400   1.000 46.81621  ?  919  LEU   A O   1 
ATOM   7340  C  CB  . LEU   A 1 921  ? -60.97300  84.23500  0.17700   1.000 33.98895  ?  919  LEU   A CB  1 
ATOM   7341  C  CG  . LEU   A 1 921  ? -62.33200  83.96300  0.81500   1.000 46.49506  ?  919  LEU   A CG  1 
ATOM   7342  C  CD1 . LEU   A 1 921  ? -63.42900  84.08000  -0.21500  1.000 64.44784  ?  919  LEU   A CD1 1 
ATOM   7343  C  CD2 . LEU   A 1 921  ? -62.33400  82.57700  1.44400   1.000 48.36472  ?  919  LEU   A CD2 1 
ATOM   7344  N  N   . ALA   A 1 922  ? -58.49400  85.97900  1.20600   1.000 45.38376  ?  920  ALA   A N   1 
ATOM   7345  C  CA  . ALA   A 1 922  ? -57.65600  86.51000  2.27800   1.000 43.18228  ?  920  ALA   A CA  1 
ATOM   7346  C  C   . ALA   A 1 922  ? -57.66700  88.03000  2.28100   1.000 43.74584  ?  920  ALA   A C   1 
ATOM   7347  O  O   . ALA   A 1 922  ? -58.01200  88.66700  3.28300   1.000 59.78100  ?  920  ALA   A O   1 
ATOM   7348  C  CB  . ALA   A 1 922  ? -56.22200  86.00400  2.11700   1.000 58.31016  ?  920  ALA   A CB  1 
ATOM   7349  N  N   . ARG   A 1 923  ? -57.26700  88.62400  1.15800   1.000 36.30287  ?  921  ARG   A N   1 
ATOM   7350  C  CA  . ARG   A 1 923  ? -57.11700  90.07000  1.08100   1.000 42.61219  ?  921  ARG   A CA  1 
ATOM   7351  C  C   . ARG   A 1 923  ? -58.44600  90.77600  1.31400   1.000 51.89024  ?  921  ARG   A C   1 
ATOM   7352  O  O   . ARG   A 1 923  ? -58.49700  91.81500  1.98500   1.000 57.70162  ?  921  ARG   A O   1 
ATOM   7353  C  CB  . ARG   A 1 923  ? -56.51700  90.43700  -0.27600  1.000 35.54874  ?  921  ARG   A CB  1 
ATOM   7354  C  CG  . ARG   A 1 923  ? -57.15200  91.62400  -0.96500  1.000 71.39621  ?  921  ARG   A CG  1 
ATOM   7355  C  CD  . ARG   A 1 923  ? -56.22900  92.17200  -2.03600  1.000 62.70928  ?  921  ARG   A CD  1 
ATOM   7356  N  NE  . ARG   A 1 923  ? -55.67400  91.10400  -2.85900  1.000 58.80625  ?  921  ARG   A NE  1 
ATOM   7357  C  CZ  . ARG   A 1 923  ? -56.23100  90.64900  -3.97300  1.000 72.40297  ?  921  ARG   A CZ  1 
ATOM   7358  N  NH1 . ARG   A 1 923  ? -57.35900  91.15700  -4.44100  1.000 58.94973  ?  921  ARG   A NH1 1 
ATOM   7359  N  NH2 . ARG   A 1 923  ? -55.64000  89.65600  -4.63400  1.000 64.25568  ?  921  ARG   A NH2 1 
ATOM   7360  N  N   . GLU   A 1 924  ? -59.53800  90.21200  0.79500   1.000 39.62497  ?  922  GLU   A N   1 
ATOM   7361  C  CA  . GLU   A 1 924  ? -60.83500  90.86100  0.93900   1.000 54.93610  ?  922  GLU   A CA  1 
ATOM   7362  C  C   . GLU   A 1 924  ? -61.32900  90.79200  2.38000   1.000 59.04245  ?  922  GLU   A C   1 
ATOM   7363  O  O   . GLU   A 1 924  ? -61.76400  91.80300  2.94300   1.000 62.94366  ?  922  GLU   A O   1 
ATOM   7364  C  CB  . GLU   A 1 924  ? -61.84500  90.23400  -0.01900  1.000 46.84313  ?  922  GLU   A CB  1 
ATOM   7365  C  CG  . GLU   A 1 924  ? -61.95200  90.98200  -1.33500  1.000 46.29805  ?  922  GLU   A CG  1 
ATOM   7366  C  CD  . GLU   A 1 924  ? -62.41900  90.10700  -2.47500  1.000 60.21684  ?  922  GLU   A CD  1 
ATOM   7367  O  OE1 . GLU   A 1 924  ? -62.99200  89.03200  -2.20000  1.000 65.83725  ?  922  GLU   A OE1 1 
ATOM   7368  O  OE2 . GLU   A 1 924  ? -62.22400  90.50000  -3.64500  1.000 64.13032  -1 922  GLU   A OE2 1 
ATOM   7369  N  N   . LEU   A 1 925  ? -61.26800  89.60500  2.99300   1.000 48.15507  ?  923  LEU   A N   1 
ATOM   7370  C  CA  . LEU   A 1 925  ? -61.63700  89.48000  4.40100   1.000 51.46885  ?  923  LEU   A CA  1 
ATOM   7371  C  C   . LEU   A 1 925  ? -60.79300  90.40000  5.27500   1.000 49.04722  ?  923  LEU   A C   1 
ATOM   7372  O  O   . LEU   A 1 925  ? -61.31200  91.05000  6.18900   1.000 58.80177  ?  923  LEU   A O   1 
ATOM   7373  C  CB  . LEU   A 1 925  ? -61.49000  88.02900  4.86100   1.000 41.96432  ?  923  LEU   A CB  1 
ATOM   7374  C  CG  . LEU   A 1 925  ? -61.74700  87.77000  6.34900   1.000 38.11726  ?  923  LEU   A CG  1 
ATOM   7375  C  CD1 . LEU   A 1 925  ? -63.21300  87.95900  6.68000   1.000 45.84315  ?  923  LEU   A CD1 1 
ATOM   7376  C  CD2 . LEU   A 1 925  ? -61.28300  86.38000  6.75800   1.000 32.75744  ?  923  LEU   A CD2 1 
ATOM   7377  N  N   . GLN   A 1 926  ? -59.48800  90.46800  5.00500   1.000 52.78256  ?  924  GLN   A N   1 
ATOM   7378  C  CA  . GLN   A 1 926  ? -58.61700  91.34200  5.78400   1.000 55.59805  ?  924  GLN   A CA  1 
ATOM   7379  C  C   . GLN   A 1 926  ? -58.99500  92.80400  5.59500   1.000 58.67126  ?  924  GLN   A C   1 
ATOM   7380  O  O   . GLN   A 1 926  ? -58.96900  93.58900  6.55100   1.000 63.37657  ?  924  GLN   A O   1 
ATOM   7381  C  CB  . GLN   A 1 926  ? -57.15900  91.11100  5.39300   1.000 48.16022  ?  924  GLN   A CB  1 
ATOM   7382  C  CG  . GLN   A 1 926  ? -56.16100  91.75800  6.33500   1.000 51.51723  ?  924  GLN   A CG  1 
ATOM   7383  C  CD  . GLN   A 1 926  ? -54.77300  91.84800  5.73600   1.000 48.01080  ?  924  GLN   A CD  1 
ATOM   7384  O  OE1 . GLN   A 1 926  ? -54.58300  92.42000  4.66300   1.000 39.19478  ?  924  GLN   A OE1 1 
ATOM   7385  N  NE2 . GLN   A 1 926  ? -53.79300  91.27500  6.42600   1.000 50.20822  ?  924  GLN   A NE2 1 
ATOM   7386  N  N   . ALA   A 1 927  ? -59.34900  93.19000  4.36800   1.000 59.81483  ?  925  ALA   A N   1 
ATOM   7387  C  CA  . ALA   A 1 927  ? -59.78500  94.56000  4.12500   1.000 57.05079  ?  925  ALA   A CA  1 
ATOM   7388  C  C   . ALA   A 1 927  ? -61.10500  94.84900  4.82600   1.000 64.91666  ?  925  ALA   A C   1 
ATOM   7389  O  O   . ALA   A 1 927  ? -61.27500  95.91900  5.42300   1.000 79.36814  ?  925  ALA   A O   1 
ATOM   7390  C  CB  . ALA   A 1 927  ? -59.90800  94.81100  2.62400   1.000 54.00312  ?  925  ALA   A CB  1 
ATOM   7391  N  N   . LEU   A 1 928  ? -62.04800  93.90700  4.76500   1.000 59.33426  ?  926  LEU   A N   1 
ATOM   7392  C  CA  . LEU   A 1 928  ? -63.32000  94.08500  5.45700   1.000 44.89205  ?  926  LEU   A CA  1 
ATOM   7393  C  C   . LEU   A 1 928  ? -63.12700  94.12700  6.96900   1.000 55.64457  ?  926  LEU   A C   1 
ATOM   7394  O  O   . LEU   A 1 928  ? -63.76700  94.92900  7.65900   1.000 69.45656  ?  926  LEU   A O   1 
ATOM   7395  C  CB  . LEU   A 1 928  ? -64.28700  92.96800  5.06700   1.000 42.75635  ?  926  LEU   A CB  1 
ATOM   7396  C  CG  . LEU   A 1 928  ? -64.72100  92.93200  3.60000   1.000 47.70503  ?  926  LEU   A CG  1 
ATOM   7397  C  CD1 . LEU   A 1 928  ? -65.55200  91.69000  3.31600   1.000 46.76564  ?  926  LEU   A CD1 1 
ATOM   7398  C  CD2 . LEU   A 1 928  ? -65.48500  94.19400  3.22200   1.000 50.17380  ?  926  LEU   A CD2 1 
ATOM   7399  N  N   . LEU   A 1 929  ? -62.24700  93.27400  7.50500   1.000 50.85760  ?  927  LEU   A N   1 
ATOM   7400  C  CA  . LEU   A 1 929  ? -61.97900  93.29900  8.93800   1.000 58.39461  ?  927  LEU   A CA  1 
ATOM   7401  C  C   . LEU   A 1 929  ? -61.30900  94.59500  9.37000   1.000 63.14487  ?  927  LEU   A C   1 
ATOM   7402  O  O   . LEU   A 1 929  ? -61.33500  94.92900  10.55900  1.000 72.05027  ?  927  LEU   A O   1 
ATOM   7403  C  CB  . LEU   A 1 929  ? -61.11700  92.10100  9.34100   1.000 40.30062  ?  927  LEU   A CB  1 
ATOM   7404  C  CG  . LEU   A 1 929  ? -61.82300  90.74200  9.32000   1.000 53.03841  ?  927  LEU   A CG  1 
ATOM   7405  C  CD1 . LEU   A 1 929  ? -60.99100  89.69000  10.02900  1.000 61.33439  ?  927  LEU   A CD1 1 
ATOM   7406  C  CD2 . LEU   A 1 929  ? -63.21600  90.82800  9.93300   1.000 60.06728  ?  927  LEU   A CD2 1 
ATOM   7407  N  N   . GLY   A 1 930  ? -60.71200  95.32400  8.43600   1.000 55.78975  ?  928  GLY   A N   1 
ATOM   7408  C  CA  . GLY   A 1 930  ? -60.19200  96.64700  8.68500   1.000 63.79177  ?  928  GLY   A CA  1 
ATOM   7409  C  C   . GLY   A 1 930  ? -61.13500  97.74900  8.27300   1.000 80.97543  ?  928  GLY   A C   1 
ATOM   7410  O  O   . GLY   A 1 930  ? -60.72500  98.91300  8.21500   1.000 87.79673  ?  928  GLY   A O   1 
ATOM   7411  N  N   . GLN   A 1 931  ? -62.38800  97.40600  7.96800   1.000 75.69668  ?  929  GLN   A N   1 
ATOM   7412  C  CA  . GLN   A 1 931  ? -63.42400  98.35500  7.56900   1.000 85.63966  ?  929  GLN   A CA  1 
ATOM   7413  C  C   . GLN   A 1 931  ? -63.03700  99.15600  6.33100   1.000 83.84697  ?  929  GLN   A C   1 
ATOM   7414  O  O   . GLN   A 1 931  ? -63.54600  100.26100 6.11900   1.000 85.72615  ?  929  GLN   A O   1 
ATOM   7415  C  CB  . GLN   A 1 931  ? -63.78600  99.29300  8.72700   1.000 83.68831  ?  929  GLN   A CB  1 
ATOM   7416  C  CG  . GLN   A 1 931  ? -64.25100  98.55700  9.97500   1.000 87.03786  ?  929  GLN   A CG  1 
ATOM   7417  C  CD  . GLN   A 1 931  ? -63.62500  99.09400  11.24600  1.000 96.76524  ?  929  GLN   A CD  1 
ATOM   7418  O  OE1 . GLN   A 1 931  ? -63.24700  98.32900  12.13400  1.000 97.78850  ?  929  GLN   A OE1 1 
ATOM   7419  N  NE2 . GLN   A 1 931  ? -63.51300  100.41500 11.34200  1.000 95.01944  ?  929  GLN   A NE2 1 
ATOM   7420  N  N   . GLN   A 1 932  ? -62.14600  98.61300  5.50500   1.000 78.39631  ?  930  GLN   A N   1 
ATOM   7421  C  CA  . GLN   A 1 932  ? -61.80500  99.23100  4.23300   1.000 78.48576  ?  930  GLN   A CA  1 
ATOM   7422  C  C   . GLN   A 1 932  ? -62.83800  98.85800  3.17500   1.000 76.92431  ?  930  GLN   A C   1 
ATOM   7423  O  O   . GLN   A 1 932  ? -63.41100  97.76500  3.19300   1.000 79.90316  ?  930  GLN   A O   1 
ATOM   7424  C  CB  . GLN   A 1 932  ? -60.40500  98.79900  3.79000   1.000 64.72976  ?  930  GLN   A CB  1 
ATOM   7425  C  CG  . GLN   A 1 932  ? -59.85400  99.53100  2.57000   1.000 93.03932  ?  930  GLN   A CG  1 
ATOM   7426  C  CD  . GLN   A 1 932  ? -59.25800  100.89000 2.90300   1.000 114.55934 ?  930  GLN   A CD  1 
ATOM   7427  O  OE1 . GLN   A 1 932  ? -59.74500  101.60100 3.78300   1.000 106.95134 ?  930  GLN   A OE1 1 
ATOM   7428  N  NE2 . GLN   A 1 932  ? -58.19600  101.25600 2.19400   1.000 105.00171 ?  930  GLN   A NE2 1 
ATOM   7429  N  N   . VAL   A 1 933  ? -63.08200  99.78500  2.25400   1.000 65.83837  ?  931  VAL   A N   1 
ATOM   7430  C  CA  . VAL   A 1 933  ? -64.09100  99.60700  1.21600   1.000 67.94782  ?  931  VAL   A CA  1 
ATOM   7431  C  C   . VAL   A 1 933  ? -63.47900  98.83900  0.05200   1.000 75.76940  ?  931  VAL   A C   1 
ATOM   7432  O  O   . VAL   A 1 933  ? -62.27000  98.90300  -0.19700  1.000 77.86531  ?  931  VAL   A O   1 
ATOM   7433  C  CB  . VAL   A 1 933  ? -64.65800  100.96800 0.76400   1.000 73.29909  ?  931  VAL   A CB  1 
ATOM   7434  C  CG1 . VAL   A 1 933  ? -65.95800  100.78200 -0.00200  1.000 62.49639  ?  931  VAL   A CG1 1 
ATOM   7435  C  CG2 . VAL   A 1 933  ? -64.86600  101.87400 1.96500   1.000 73.56774  ?  931  VAL   A CG2 1 
ATOM   7436  N  N   . LEU   A 1 934  ? -64.32500  98.10700  -0.67200  1.000 63.28174  ?  932  LEU   A N   1 
ATOM   7437  C  CA  . LEU   A 1 934  ? -63.90100  97.24500  -1.76800  1.000 69.63998  ?  932  LEU   A CA  1 
ATOM   7438  C  C   . LEU   A 1 934  ? -64.63200  97.63300  -3.04600  1.000 73.54970  ?  932  LEU   A C   1 
ATOM   7439  O  O   . LEU   A 1 934  ? -65.85800  97.78500  -3.04500  1.000 67.27014  ?  932  LEU   A O   1 
ATOM   7440  C  CB  . LEU   A 1 934  ? -64.16600  95.77400  -1.43400  1.000 57.52082  ?  932  LEU   A CB  1 
ATOM   7441  C  CG  . LEU   A 1 934  ? -63.55500  95.26500  -0.12600  1.000 63.70164  ?  932  LEU   A CG  1 
ATOM   7442  C  CD1 . LEU   A 1 934  ? -63.67400  93.75900  -0.02300  1.000 65.68172  ?  932  LEU   A CD1 1 
ATOM   7443  C  CD2 . LEU   A 1 934  ? -62.09400  95.67600  -0.02800  1.000 73.43837  ?  932  LEU   A CD2 1 
ATOM   7444  N  N   . SER   A 1 935  ? -63.88000  97.78300  -4.12900  1.000 75.13321  ?  933  SER   A N   1 
ATOM   7445  C  CA  . SER   A 1 935  ? -64.48400  98.07500  -5.42200  1.000 63.84675  ?  933  SER   A CA  1 
ATOM   7446  C  C   . SER   A 1 935  ? -65.25700  96.85700  -5.91100  1.000 63.09484  ?  933  SER   A C   1 
ATOM   7447  O  O   . SER   A 1 935  ? -64.69100  95.76000  -5.97600  1.000 67.46847  ?  933  SER   A O   1 
ATOM   7448  C  CB  . SER   A 1 935  ? -63.41100  98.45400  -6.43200  1.000 69.64040  ?  933  SER   A CB  1 
ATOM   7449  O  OG  . SER   A 1 935  ? -62.50900  99.38900  -5.87100  1.000 86.79302  ?  933  SER   A OG  1 
ATOM   7450  N  N   . PRO   A 1 936  ? -66.53400  97.00400  -6.26400  1.000 70.65017  ?  934  PRO   A N   1 
ATOM   7451  C  CA  . PRO   A 1 936  ? -67.32700  95.83400  -6.66000  1.000 91.64882  ?  934  PRO   A CA  1 
ATOM   7452  C  C   . PRO   A 1 936  ? -66.71600  95.11800  -7.85700  1.000 74.95563  ?  934  PRO   A C   1 
ATOM   7453  O  O   . PRO   A 1 936  ? -66.02600  95.71800  -8.68500  1.000 58.25655  ?  934  PRO   A O   1 
ATOM   7454  C  CB  . PRO   A 1 936  ? -68.69900  96.42900  -6.99800  1.000 67.23406  ?  934  PRO   A CB  1 
ATOM   7455  C  CG  . PRO   A 1 936  ? -68.74400  97.72700  -6.25000  1.000 90.24121  ?  934  PRO   A CG  1 
ATOM   7456  C  CD  . PRO   A 1 936  ? -67.33400  98.23900  -6.24600  1.000 86.60741  ?  934  PRO   A CD  1 
ATOM   7457  N  N   . VAL   A 1 937  ? -66.96900  93.80700  -7.92400  1.000 67.31869  ?  935  VAL   A N   1 
ATOM   7458  C  CA  . VAL   A 1 937  ? -66.37500  92.99100  -8.97400  1.000 55.75219  ?  935  VAL   A CA  1 
ATOM   7459  C  C   . VAL   A 1 937  ? -66.90300  93.42500  -10.33800 1.000 61.33387  ?  935  VAL   A C   1 
ATOM   7460  O  O   . VAL   A 1 937  ? -67.96600  94.04600  -10.46400 1.000 91.05196  ?  935  VAL   A O   1 
ATOM   7461  C  CB  . VAL   A 1 937  ? -66.64000  91.49700  -8.73300  1.000 59.38955  ?  935  VAL   A CB  1 
ATOM   7462  C  CG1 . VAL   A 1 937  ? -66.39000  91.14400  -7.27300  1.000 63.62065  ?  935  VAL   A CG1 1 
ATOM   7463  C  CG2 . VAL   A 1 937  ? -68.06100  91.13100  -9.14700  1.000 68.67963  ?  935  VAL   A CG2 1 
ATOM   7464  N  N   . GLU   A 1 938  ? -66.13900  93.09200  -11.37300 1.000 66.00321  ?  936  GLU   A N   1 
ATOM   7465  C  CA  . GLU   A 1 938  ? -66.45800  93.50100  -12.73100 1.000 66.50872  ?  936  GLU   A CA  1 
ATOM   7466  C  C   . GLU   A 1 938  ? -66.78000  92.34400  -13.66300 1.000 62.90202  ?  936  GLU   A C   1 
ATOM   7467  O  O   . GLU   A 1 938  ? -67.57900  92.52200  -14.58500 1.000 70.28253  ?  936  GLU   A O   1 
ATOM   7468  C  CB  . GLU   A 1 938  ? -65.29900  94.31500  -13.32700 1.000 73.96245  ?  936  GLU   A CB  1 
ATOM   7469  C  CG  . GLU   A 1 938  ? -65.66100  95.07700  -14.58900 1.000 89.40452  ?  936  GLU   A CG  1 
ATOM   7470  C  CD  . GLU   A 1 938  ? -66.70400  96.14700  -14.33800 1.000 111.51943 ?  936  GLU   A CD  1 
ATOM   7471  O  OE1 . GLU   A 1 938  ? -66.42100  97.08600  -13.56400 1.000 109.55530 ?  936  GLU   A OE1 1 
ATOM   7472  O  OE2 . GLU   A 1 938  ? -67.81100  96.04600  -14.90900 1.000 111.76026 -1 936  GLU   A OE2 1 
ATOM   7473  N  N   . LYS   A 1 939  ? -66.19200  91.17100  -13.45300 1.000 56.21482  ?  937  LYS   A N   1 
ATOM   7474  C  CA  . LYS   A 1 939  ? -66.42500  90.01300  -14.30100 1.000 49.38008  ?  937  LYS   A CA  1 
ATOM   7475  C  C   . LYS   A 1 939  ? -66.96700  88.86400  -13.46100 1.000 44.32117  ?  937  LYS   A C   1 
ATOM   7476  O  O   . LYS   A 1 939  ? -67.01200  88.93100  -12.23000 1.000 62.89554  ?  937  LYS   A O   1 
ATOM   7477  C  CB  . LYS   A 1 939  ? -65.14000  89.59200  -15.02500 1.000 59.95226  ?  937  LYS   A CB  1 
ATOM   7478  C  CG  . LYS   A 1 939  ? -64.27700  90.75600  -15.49900 1.000 71.37623  ?  937  LYS   A CG  1 
ATOM   7479  C  CD  . LYS   A 1 939  ? -64.98600  91.60600  -16.54300 1.000 75.10313  ?  937  LYS   A CD  1 
ATOM   7480  C  CE  . LYS   A 1 939  ? -65.34900  90.78900  -17.76800 1.000 77.27492  ?  937  LYS   A CE  1 
ATOM   7481  N  NZ  . LYS   A 1 939  ? -65.56400  91.65000  -18.96400 1.000 68.88799  ?  937  LYS   A NZ  1 
ATOM   7482  N  N   . THR   A 1 940  ? -67.38900  87.79900  -14.14100 1.000 45.41994  ?  938  THR   A N   1 
ATOM   7483  C  CA  . THR   A 1 940  ? -67.97400  86.63900  -13.48400 1.000 59.26143  ?  938  THR   A CA  1 
ATOM   7484  C  C   . THR   A 1 940  ? -67.43600  85.36300  -14.11600 1.000 51.97612  ?  938  THR   A C   1 
ATOM   7485  O  O   . THR   A 1 940  ? -67.09400  85.33400  -15.30100 1.000 47.85535  ?  938  THR   A O   1 
ATOM   7486  C  CB  . THR   A 1 940  ? -69.51100  86.63500  -13.56500 1.000 59.32604  ?  938  THR   A CB  1 
ATOM   7487  O  OG1 . THR   A 1 940  ? -69.92400  86.70800  -14.93500 1.000 70.51810  ?  938  THR   A OG1 1 
ATOM   7488  C  CG2 . THR   A 1 940  ? -70.10200  87.80300  -12.79600 1.000 40.49704  ?  938  THR   A CG2 1 
ATOM   7489  N  N   . TYR   A 1 941  ? -67.38200  84.30100  -13.30800 1.000 47.14788  ?  939  TYR   A N   1 
ATOM   7490  C  CA  . TYR   A 1 941  ? -66.84600  83.03000  -13.78600 1.000 36.11630  ?  939  TYR   A CA  1 
ATOM   7491  C  C   . TYR   A 1 941  ? -67.71200  82.44200  -14.89300 1.000 53.34525  ?  939  TYR   A C   1 
ATOM   7492  O  O   . TYR   A 1 941  ? -67.19500  81.82300  -15.83000 1.000 60.07184  ?  939  TYR   A O   1 
ATOM   7493  C  CB  . TYR   A 1 941  ? -66.71600  82.04600  -12.62100 1.000 33.41736  ?  939  TYR   A CB  1 
ATOM   7494  C  CG  . TYR   A 1 941  ? -65.98600  80.75800  -12.95100 1.000 30.98687  ?  939  TYR   A CG  1 
ATOM   7495  C  CD1 . TYR   A 1 941  ? -66.62000  79.73100  -13.64100 1.000 37.23953  ?  939  TYR   A CD1 1 
ATOM   7496  C  CD2 . TYR   A 1 941  ? -64.66700  80.56500  -12.56100 1.000 38.92448  ?  939  TYR   A CD2 1 
ATOM   7497  C  CE1 . TYR   A 1 941  ? -65.96000  78.55500  -13.94200 1.000 44.79107  ?  939  TYR   A CE1 1 
ATOM   7498  C  CE2 . TYR   A 1 941  ? -63.99700  79.38800  -12.85700 1.000 33.48201  ?  939  TYR   A CE2 1 
ATOM   7499  C  CZ  . TYR   A 1 941  ? -64.65300  78.38600  -13.54900 1.000 40.80107  ?  939  TYR   A CZ  1 
ATOM   7500  O  OH  . TYR   A 1 941  ? -64.00900  77.20700  -13.85400 1.000 41.73667  ?  939  TYR   A OH  1 
ATOM   7501  N  N   . LYS   A 1 942  ? -69.03400  82.62300  -14.80100 1.000 57.09060  ?  940  LYS   A N   1 
ATOM   7502  C  CA  . LYS   A 1 942  ? -69.93400  82.04000  -15.79300 1.000 53.86026  ?  940  LYS   A CA  1 
ATOM   7503  C  C   . LYS   A 1 942  ? -69.61400  82.52900  -17.19900 1.000 52.37325  ?  940  LYS   A C   1 
ATOM   7504  O  O   . LYS   A 1 942  ? -69.90700  81.83600  -18.18000 1.000 48.44800  ?  940  LYS   A O   1 
ATOM   7505  C  CB  . LYS   A 1 942  ? -71.38600  82.35800  -15.43500 1.000 57.25084  ?  940  LYS   A CB  1 
ATOM   7506  C  CG  . LYS   A 1 942  ? -71.65900  83.83800  -15.22700 1.000 68.45507  ?  940  LYS   A CG  1 
ATOM   7507  C  CD  . LYS   A 1 942  ? -73.00900  84.07200  -14.57100 1.000 44.00701  ?  940  LYS   A CD  1 
ATOM   7508  C  CE  . LYS   A 1 942  ? -73.57600  85.42400  -14.96500 1.000 55.70309  ?  940  LYS   A CE  1 
ATOM   7509  N  NZ  . LYS   A 1 942  ? -72.52900  86.48500  -14.98600 1.000 75.08214  ?  940  LYS   A NZ  1 
ATOM   7510  N  N   . SER   A 1 943  ? -69.00300  83.70800  -17.31700 1.000 49.59246  ?  941  SER   A N   1 
ATOM   7511  C  CA  . SER   A 1 943  ? -68.63300  84.22700  -18.62700 1.000 55.74073  ?  941  SER   A CA  1 
ATOM   7512  C  C   . SER   A 1 943  ? -67.36600  83.56200  -19.15100 1.000 67.21985  ?  941  SER   A C   1 
ATOM   7513  O  O   . SER   A 1 943  ? -67.28900  83.21900  -20.33700 1.000 70.64510  ?  941  SER   A O   1 
ATOM   7514  C  CB  . SER   A 1 943  ? -68.45200  85.74200  -18.55500 1.000 68.39782  ?  941  SER   A CB  1 
ATOM   7515  O  OG  . SER   A 1 943  ? -69.37200  86.32400  -17.64800 1.000 82.17118  ?  941  SER   A OG  1 
ATOM   7516  N  N   . PHE   A 1 944  ? -66.36600  83.37300  -18.28200 1.000 63.39119  ?  942  PHE   A N   1 
ATOM   7517  C  CA  . PHE   A 1 944  ? -65.13200  82.71200  -18.69700 1.000 52.87342  ?  942  PHE   A CA  1 
ATOM   7518  C  C   . PHE   A 1 944  ? -65.39700  81.30200  -19.21000 1.000 46.50848  ?  942  PHE   A C   1 
ATOM   7519  O  O   . PHE   A 1 944  ? -64.70800  80.83500  -20.12300 1.000 54.92392  ?  942  PHE   A O   1 
ATOM   7520  C  CB  . PHE   A 1 944  ? -64.13200  82.68000  -17.53700 1.000 50.88035  ?  942  PHE   A CB  1 
ATOM   7521  C  CG  . PHE   A 1 944  ? -62.93800  81.79300  -17.78300 1.000 57.15599  ?  942  PHE   A CG  1 
ATOM   7522  C  CD1 . PHE   A 1 944  ? -61.86100  82.24600  -18.52700 1.000 57.92982  ?  942  PHE   A CD1 1 
ATOM   7523  C  CD2 . PHE   A 1 944  ? -62.89500  80.50500  -17.27100 1.000 48.82392  ?  942  PHE   A CD2 1 
ATOM   7524  C  CE1 . PHE   A 1 944  ? -60.76600  81.43200  -18.75700 1.000 59.62165  ?  942  PHE   A CE1 1 
ATOM   7525  C  CE2 . PHE   A 1 944  ? -61.80600  79.68700  -17.50000 1.000 43.36668  ?  942  PHE   A CE2 1 
ATOM   7526  C  CZ  . PHE   A 1 944  ? -60.74100  80.15000  -18.24300 1.000 56.73873  ?  942  PHE   A CZ  1 
ATOM   7527  N  N   . ALA   A 1 945  ? -66.38900  80.61100  -18.64100 1.000 39.12631  ?  943  ALA   A N   1 
ATOM   7528  C  CA  . ALA   A 1 945  ? -66.71600  79.27400  -19.12200 1.000 46.70173  ?  943  ALA   A CA  1 
ATOM   7529  C  C   . ALA   A 1 945  ? -67.21800  79.31700  -20.55800 1.000 49.56242  ?  943  ALA   A C   1 
ATOM   7530  O  O   . ALA   A 1 945  ? -66.89600  78.43600  -21.36400 1.000 47.07917  ?  943  ALA   A O   1 
ATOM   7531  C  CB  . ALA   A 1 945  ? -67.75200  78.62100  -18.20900 1.000 52.08761  ?  943  ALA   A CB  1 
ATOM   7532  N  N   . ARG   A 1 946  ? -68.00500  80.33800  -20.89900 1.000 53.93384  ?  944  ARG   A N   1 
ATOM   7533  C  CA  . ARG   A 1 946  ? -68.46200  80.49400  -22.27600 1.000 65.89785  ?  944  ARG   A CA  1 
ATOM   7534  C  C   . ARG   A 1 946  ? -67.28700  80.73700  -23.21300 1.000 59.90741  ?  944  ARG   A C   1 
ATOM   7535  O  O   . ARG   A 1 946  ? -67.16900  80.09600  -24.26500 1.000 55.54102  ?  944  ARG   A O   1 
ATOM   7536  C  CB  . ARG   A 1 946  ? -69.47000  81.64100  -22.36600 1.000 61.41913  ?  944  ARG   A CB  1 
ATOM   7537  C  CG  . ARG   A 1 946  ? -70.31300  81.64900  -23.63800 1.000 56.18774  ?  944  ARG   A CG  1 
ATOM   7538  C  CD  . ARG   A 1 946  ? -71.28400  80.47200  -23.69800 1.000 79.57300  ?  944  ARG   A CD  1 
ATOM   7539  N  NE  . ARG   A 1 946  ? -70.65500  79.24600  -24.18000 1.000 91.43197  ?  944  ARG   A NE  1 
ATOM   7540  C  CZ  . ARG   A 1 946  ? -70.76400  78.77800  -25.41700 1.000 102.48585 ?  944  ARG   A CZ  1 
ATOM   7541  N  NH1 . ARG   A 1 946  ? -71.48800  79.40300  -26.33200 1.000 87.42858  ?  944  ARG   A NH1 1 
ATOM   7542  N  NH2 . ARG   A 1 946  ? -70.12900  77.65500  -25.74400 1.000 80.22777  ?  944  ARG   A NH2 1 
ATOM   7543  N  N   . TRP   A 1 947  ? -66.40200  81.66000  -22.83700 1.000 55.11749  ?  945  TRP   A N   1 
ATOM   7544  C  CA  . TRP   A 1 947  ? -65.25300  81.99300  -23.67200 1.000 53.08837  ?  945  TRP   A CA  1 
ATOM   7545  C  C   . TRP   A 1 947  ? -64.35100  80.78400  -23.88000 1.000 55.86594  ?  945  TRP   A C   1 
ATOM   7546  O  O   . TRP   A 1 947  ? -63.92600  80.49700  -25.00600 1.000 76.13184  ?  945  TRP   A O   1 
ATOM   7547  C  CB  . TRP   A 1 947  ? -64.48400  83.14500  -23.03000 1.000 42.70313  ?  945  TRP   A CB  1 
ATOM   7548  C  CG  . TRP   A 1 947  ? -63.18800  83.48300  -23.68000 1.000 54.55711  ?  945  TRP   A CG  1 
ATOM   7549  C  CD1 . TRP   A 1 947  ? -62.99000  84.33100  -24.73000 1.000 61.59005  ?  945  TRP   A CD1 1 
ATOM   7550  C  CD2 . TRP   A 1 947  ? -61.89700  82.99800  -23.30500 1.000 70.12520  ?  945  TRP   A CD2 1 
ATOM   7551  N  NE1 . TRP   A 1 947  ? -61.65300  84.40000  -25.03500 1.000 70.11601  ?  945  TRP   A NE1 1 
ATOM   7552  C  CE2 . TRP   A 1 947  ? -60.96100  83.58900  -24.17400 1.000 72.40891  ?  945  TRP   A CE2 1 
ATOM   7553  C  CE3 . TRP   A 1 947  ? -61.44200  82.11600  -22.32100 1.000 54.20251  ?  945  TRP   A CE3 1 
ATOM   7554  C  CZ2 . TRP   A 1 947  ? -59.59700  83.32700  -24.08900 1.000 75.26114  ?  945  TRP   A CZ2 1 
ATOM   7555  C  CZ3 . TRP   A 1 947  ? -60.09100  81.85800  -22.23700 1.000 61.79636  ?  945  TRP   A CZ3 1 
ATOM   7556  C  CH2 . TRP   A 1 947  ? -59.18300  82.46100  -23.11500 1.000 72.67565  ?  945  TRP   A CH2 1 
ATOM   7557  N  N   . GLN   A 1 948  ? -64.05500  80.05400  -22.80300 1.000 42.07041  ?  946  GLN   A N   1 
ATOM   7558  C  CA  . GLN   A 1 948  ? -63.14300  78.92100  -22.91200 1.000 45.99090  ?  946  GLN   A CA  1 
ATOM   7559  C  C   . GLN   A 1 948  ? -63.77500  77.76900  -23.68500 1.000 58.93815  ?  946  GLN   A C   1 
ATOM   7560  O  O   . GLN   A 1 948  ? -63.09500  77.10200  -24.47500 1.000 67.05476  ?  946  GLN   A O   1 
ATOM   7561  C  CB  . GLN   A 1 948  ? -62.70700  78.46100  -21.52300 1.000 65.19711  ?  946  GLN   A CB  1 
ATOM   7562  C  CG  . GLN   A 1 948  ? -61.38700  77.71000  -21.51800 1.000 64.55163  ?  946  GLN   A CG  1 
ATOM   7563  C  CD  . GLN   A 1 948  ? -61.14300  76.98100  -20.21600 1.000 48.95128  ?  946  GLN   A CD  1 
ATOM   7564  O  OE1 . GLN   A 1 948  ? -62.06300  76.41100  -19.63000 1.000 75.57052  ?  946  GLN   A OE1 1 
ATOM   7565  N  NE2 . GLN   A 1 948  ? -59.89800  76.99200  -19.75700 1.000 44.73469  ?  946  GLN   A NE2 1 
ATOM   7566  N  N   . ASN   A 1 949  ? -65.07000  77.51500  -23.47100 1.000 54.01170  ?  947  ASN   A N   1 
ATOM   7567  C  CA  . ASN   A 1 949  ? -65.74500  76.46100  -24.22400 1.000 52.22635  ?  947  ASN   A CA  1 
ATOM   7568  C  C   . ASN   A 1 949  ? -65.75400  76.76300  -25.71600 1.000 52.65310  ?  947  ASN   A C   1 
ATOM   7569  O  O   . ASN   A 1 949  ? -65.76100  75.84000  -26.53800 1.000 58.33227  ?  947  ASN   A O   1 
ATOM   7570  C  CB  . ASN   A 1 949  ? -67.17400  76.27200  -23.70900 1.000 64.63544  ?  947  ASN   A CB  1 
ATOM   7571  C  CG  . ASN   A 1 949  ? -67.22200  75.62900  -22.33100 1.000 58.66893  ?  947  ASN   A CG  1 
ATOM   7572  O  OD1 . ASN   A 1 949  ? -66.29300  74.93200  -21.92200 1.000 62.11918  ?  947  ASN   A OD1 1 
ATOM   7573  N  ND2 . ASN   A 1 949  ? -68.30300  75.87900  -21.60100 1.000 50.82591  ?  947  ASN   A ND2 1 
ATOM   7574  N  N   . GLU   A 1 950  ? -65.75200  78.04500  -26.08600 1.000 52.19268  ?  948  GLU   A N   1 
ATOM   7575  C  CA  . GLU   A 1 950  ? -65.64700  78.41300  -27.49200 1.000 62.22676  ?  948  GLU   A CA  1 
ATOM   7576  C  C   . GLU   A 1 950  ? -64.22300  78.23600  -28.00300 1.000 63.06285  ?  948  GLU   A C   1 
ATOM   7577  O  O   . GLU   A 1 950  ? -64.02000  77.79000  -29.13900 1.000 56.56809  ?  948  GLU   A O   1 
ATOM   7578  C  CB  . GLU   A 1 950  ? -66.11200  79.85500  -27.69100 1.000 65.61955  ?  948  GLU   A CB  1 
ATOM   7579  C  CG  . GLU   A 1 950  ? -67.60900  79.99300  -27.90300 1.000 79.52789  ?  948  GLU   A CG  1 
ATOM   7580  C  CD  . GLU   A 1 950  ? -68.14800  81.32000  -27.40600 1.000 95.67871  ?  948  GLU   A CD  1 
ATOM   7581  O  OE1 . GLU   A 1 950  ? -67.34300  82.25100  -27.19100 1.000 76.61255  ?  948  GLU   A OE1 1 
ATOM   7582  O  OE2 . GLU   A 1 950  ? -69.38000  81.42800  -27.22600 1.000 100.54372 -1 948  GLU   A OE2 1 
ATOM   7583  N  N   . TRP   A 1 951  ? -63.23000  78.57800  -27.17400 1.000 52.51506  ?  949  TRP   A N   1 
ATOM   7584  C  CA  . TRP   A 1 951  ? -61.83700  78.35800  -27.54900 1.000 56.92666  ?  949  TRP   A CA  1 
ATOM   7585  C  C   . TRP   A 1 951  ? -61.55100  76.88200  -27.78900 1.000 60.50641  ?  949  TRP   A C   1 
ATOM   7586  O  O   . TRP   A 1 951  ? -60.62100  76.54300  -28.53100 1.000 64.30468  ?  949  TRP   A O   1 
ATOM   7587  C  CB  . TRP   A 1 951  ? -60.90400  78.91200  -26.46900 1.000 59.39410  ?  949  TRP   A CB  1 
ATOM   7588  C  CG  . TRP   A 1 951  ? -59.44600  78.81600  -26.82400 1.000 57.05242  ?  949  TRP   A CG  1 
ATOM   7589  C  CD1 . TRP   A 1 951  ? -58.76500  79.59000  -27.71800 1.000 52.63361  ?  949  TRP   A CD1 1 
ATOM   7590  C  CD2 . TRP   A 1 951  ? -58.49300  77.88600  -26.29300 1.000 63.47554  ?  949  TRP   A CD2 1 
ATOM   7591  N  NE1 . TRP   A 1 951  ? -57.44800  79.20300  -27.77500 1.000 65.18647  ?  949  TRP   A NE1 1 
ATOM   7592  C  CE2 . TRP   A 1 951  ? -57.25500  78.15800  -26.91000 1.000 65.46794  ?  949  TRP   A CE2 1 
ATOM   7593  C  CE3 . TRP   A 1 951  ? -58.56600  76.85100  -25.35600 1.000 55.60676  ?  949  TRP   A CE3 1 
ATOM   7594  C  CZ2 . TRP   A 1 951  ? -56.10200  77.43200  -26.62100 1.000 60.67116  ?  949  TRP   A CZ2 1 
ATOM   7595  C  CZ3 . TRP   A 1 951  ? -57.42000  76.13100  -25.07100 1.000 57.03375  ?  949  TRP   A CZ3 1 
ATOM   7596  C  CH2 . TRP   A 1 951  ? -56.20500  76.42500  -25.70100 1.000 61.77530  ?  949  TRP   A CH2 1 
ATOM   7597  N  N   . PHE   A 1 952  ? -62.33500  75.99200  -27.17600 1.000 53.34109  ?  950  PHE   A N   1 
ATOM   7598  C  CA  . PHE   A 1 952  ? -62.18900  74.56500  -27.43600 1.000 51.26176  ?  950  PHE   A CA  1 
ATOM   7599  C  C   . PHE   A 1 952  ? -62.58800  74.20100  -28.85800 1.000 60.85261  ?  950  PHE   A C   1 
ATOM   7600  O  O   . PHE   A 1 952  ? -62.25600  73.10500  -29.32400 1.000 61.68791  ?  950  PHE   A O   1 
ATOM   7601  C  CB  . PHE   A 1 952  ? -63.01300  73.76200  -26.42900 1.000 56.35390  ?  950  PHE   A CB  1 
ATOM   7602  C  CG  . PHE   A 1 952  ? -62.54600  73.91200  -25.00700 1.000 65.54446  ?  950  PHE   A CG  1 
ATOM   7603  C  CD1 . PHE   A 1 952  ? -61.23300  74.25900  -24.72700 1.000 59.05902  ?  950  PHE   A CD1 1 
ATOM   7604  C  CD2 . PHE   A 1 952  ? -63.41800  73.70500  -23.95200 1.000 51.91981  ?  950  PHE   A CD2 1 
ATOM   7605  C  CE1 . PHE   A 1 952  ? -60.80000  74.39600  -23.42300 1.000 59.87138  ?  950  PHE   A CE1 1 
ATOM   7606  C  CE2 . PHE   A 1 952  ? -62.99000  73.84100  -22.64500 1.000 67.45288  ?  950  PHE   A CE2 1 
ATOM   7607  C  CZ  . PHE   A 1 952  ? -61.67900  74.18700  -22.38000 1.000 71.47349  ?  950  PHE   A CZ  1 
ATOM   7608  N  N   . ALA   A 1 953  ? -63.28900  75.09400  -29.55300 1.000 68.97897  ?  951  ALA   A N   1 
ATOM   7609  C  CA  . ALA   A 1 953  ? -63.62000  74.92300  -30.95900 1.000 60.50194  ?  951  ALA   A CA  1 
ATOM   7610  C  C   . ALA   A 1 953  ? -62.63800  75.63000  -31.88200 1.000 63.74032  ?  951  ALA   A C   1 
ATOM   7611  O  O   . ALA   A 1 953  ? -62.81300  75.58200  -33.10300 1.000 68.56958  ?  951  ALA   A O   1 
ATOM   7612  C  CB  . ALA   A 1 953  ? -65.04200  75.42600  -31.22900 1.000 62.54462  ?  951  ALA   A CB  1 
ATOM   7613  N  N   . SER   A 1 954  ? -61.61200  76.27800  -31.33400 1.000 56.78887  ?  952  SER   A N   1 
ATOM   7614  C  CA  . SER   A 1 954  ? -60.63600  76.99300  -32.14000 1.000 59.44414  ?  952  SER   A CA  1 
ATOM   7615  C  C   . SER   A 1 954  ? -59.63000  76.02300  -32.75900 1.000 70.57140  ?  952  SER   A C   1 
ATOM   7616  O  O   . SER   A 1 954  ? -59.60200  74.82700  -32.45600 1.000 63.69631  ?  952  SER   A O   1 
ATOM   7617  C  CB  . SER   A 1 954  ? -59.90600  78.04000  -31.29900 1.000 53.53758  ?  952  SER   A CB  1 
ATOM   7618  O  OG  . SER   A 1 954  ? -59.13800  77.43200  -30.27400 1.000 63.45092  ?  952  SER   A OG  1 
ATOM   7619  N  N   . ASP   A 1 955  ? -58.79500  76.56300  -33.65000 1.000 75.88344  ?  953  ASP   A N   1 
ATOM   7620  C  CA  . ASP   A 1 955  ? -57.71400  75.77700  -34.23400 1.000 66.02008  ?  953  ASP   A CA  1 
ATOM   7621  C  C   . ASP   A 1 955  ? -56.52900  75.66300  -33.28700 1.000 63.57913  ?  953  ASP   A C   1 
ATOM   7622  O  O   . ASP   A 1 955  ? -55.80400  74.66100  -33.32200 1.000 53.08182  ?  953  ASP   A O   1 
ATOM   7623  C  CB  . ASP   A 1 955  ? -57.27000  76.39400  -35.56300 1.000 59.19585  ?  953  ASP   A CB  1 
ATOM   7624  C  CG  . ASP   A 1 955  ? -58.42900  76.63600  -36.51100 1.000 77.89150  ?  953  ASP   A CG  1 
ATOM   7625  O  OD1 . ASP   A 1 955  ? -59.52500  76.08800  -36.26700 1.000 98.04819  ?  953  ASP   A OD1 1 
ATOM   7626  O  OD2 . ASP   A 1 955  ? -58.24100  77.36500  -37.50800 1.000 82.17616  -1 953  ASP   A OD2 1 
ATOM   7627  N  N   . GLU   A 1 956  ? -56.32300  76.67300  -32.43800 1.000 62.68525  ?  954  GLU   A N   1 
ATOM   7628  C  CA  . GLU   A 1 956  ? -55.24200  76.61400  -31.46200 1.000 49.94747  ?  954  GLU   A CA  1 
ATOM   7629  C  C   . GLU   A 1 956  ? -55.44300  75.45800  -30.49200 1.000 55.09990  ?  954  GLU   A C   1 
ATOM   7630  O  O   . GLU   A 1 956  ? -54.47400  74.81600  -30.06900 1.000 70.05063  ?  954  GLU   A O   1 
ATOM   7631  C  CB  . GLU   A 1 956  ? -55.15100  77.94200  -30.70900 1.000 33.04228  ?  954  GLU   A CB  1 
ATOM   7632  C  CG  . GLU   A 1 956  ? -54.03900  78.00200  -29.67500 1.000 53.81922  ?  954  GLU   A CG  1 
ATOM   7633  C  CD  . GLU   A 1 956  ? -53.84100  79.39900  -29.11900 1.000 72.49933  ?  954  GLU   A CD  1 
ATOM   7634  O  OE1 . GLU   A 1 956  ? -54.70000  80.26800  -29.37900 1.000 41.49343  ?  954  GLU   A OE1 1 
ATOM   7635  O  OE2 . GLU   A 1 956  ? -52.82500  79.62900  -28.42800 1.000 89.72829  -1 954  GLU   A OE2 1 
ATOM   7636  N  N   . TYR   A 1 957  ? -56.69700  75.16900  -30.13800 1.000 44.99912  ?  955  TYR   A N   1 
ATOM   7637  C  CA  . TYR   A 1 957  ? -56.97400  74.07500  -29.21300 1.000 58.10408  ?  955  TYR   A CA  1 
ATOM   7638  C  C   . TYR   A 1 957  ? -56.55900  72.73500  -29.81100 1.000 56.24326  ?  955  TYR   A C   1 
ATOM   7639  O  O   . TYR   A 1 957  ? -55.93000  71.90900  -29.13800 1.000 63.66818  ?  955  TYR   A O   1 
ATOM   7640  C  CB  . TYR   A 1 957  ? -58.45700  74.07100  -28.83800 1.000 51.32678  ?  955  TYR   A CB  1 
ATOM   7641  C  CG  . TYR   A 1 957  ? -58.85600  72.91000  -27.95900 1.000 44.42421  ?  955  TYR   A CG  1 
ATOM   7642  C  CD1 . TYR   A 1 957  ? -58.55700  72.90400  -26.60300 1.000 42.46085  ?  955  TYR   A CD1 1 
ATOM   7643  C  CD2 . TYR   A 1 957  ? -59.52700  71.81600  -28.48700 1.000 52.80292  ?  955  TYR   A CD2 1 
ATOM   7644  C  CE1 . TYR   A 1 957  ? -58.91800  71.83900  -25.79800 1.000 55.56679  ?  955  TYR   A CE1 1 
ATOM   7645  C  CE2 . TYR   A 1 957  ? -59.89200  70.74900  -27.69200 1.000 57.99082  ?  955  TYR   A CE2 1 
ATOM   7646  C  CZ  . TYR   A 1 957  ? -59.58600  70.76400  -26.35000 1.000 62.63657  ?  955  TYR   A CZ  1 
ATOM   7647  O  OH  . TYR   A 1 957  ? -59.95200  69.69700  -25.56100 1.000 63.91930  ?  955  TYR   A OH  1 
ATOM   7648  N  N   . GLU   A 1 958  ? -56.90100  72.50100  -31.08100 1.000 51.79526  ?  956  GLU   A N   1 
ATOM   7649  C  CA  . GLU   A 1 958  ? -56.49700  71.26100  -31.73500 1.000 49.99201  ?  956  GLU   A CA  1 
ATOM   7650  C  C   . GLU   A 1 958  ? -54.98300  71.16700  -31.84100 1.000 45.54847  ?  956  GLU   A C   1 
ATOM   7651  O  O   . GLU   A 1 958  ? -54.40900  70.07900  -31.70600 1.000 57.25732  ?  956  GLU   A O   1 
ATOM   7652  C  CB  . GLU   A 1 958  ? -57.13900  71.16500  -33.11800 1.000 58.97048  ?  956  GLU   A CB  1 
ATOM   7653  C  CG  . GLU   A 1 958  ? -58.65200  71.22100  -33.09500 1.000 50.67219  ?  956  GLU   A CG  1 
ATOM   7654  C  CD  . GLU   A 1 958  ? -59.26700  69.89400  -32.70500 1.000 75.12110  ?  956  GLU   A CD  1 
ATOM   7655  O  OE1 . GLU   A 1 958  ? -58.62800  68.85200  -32.96200 1.000 69.97408  ?  956  GLU   A OE1 1 
ATOM   7656  O  OE2 . GLU   A 1 958  ? -60.38200  69.89200  -32.14200 1.000 81.69713  -1 956  GLU   A OE2 1 
ATOM   7657  N  N   . GLN   A 1 959  ? -54.31900  72.30000  -32.08600 1.000 49.03801  ?  957  GLN   A N   1 
ATOM   7658  C  CA  . GLN   A 1 959  ? -52.86000  72.32200  -32.11200 1.000 50.33007  ?  957  GLN   A CA  1 
ATOM   7659  C  C   . GLN   A 1 959  ? -52.27900  71.83600  -30.79000 1.000 54.93769  ?  957  GLN   A C   1 
ATOM   7660  O  O   . GLN   A 1 959  ? -51.28800  71.09700  -30.77100 1.000 54.39615  ?  957  GLN   A O   1 
ATOM   7661  C  CB  . GLN   A 1 959  ? -52.37100  73.73600  -32.42400 1.000 42.31958  ?  957  GLN   A CB  1 
ATOM   7662  C  CG  . GLN   A 1 959  ? -51.25300  73.80800  -33.44700 1.000 52.18629  ?  957  GLN   A CG  1 
ATOM   7663  C  CD  . GLN   A 1 959  ? -50.69500  75.21100  -33.58900 1.000 83.59355  ?  957  GLN   A CD  1 
ATOM   7664  O  OE1 . GLN   A 1 959  ? -51.44600  76.18500  -33.65700 1.000 92.78239  ?  957  GLN   A OE1 1 
ATOM   7665  N  NE2 . GLN   A 1 959  ? -49.37200  75.32300  -33.63200 1.000 94.41856  ?  957  GLN   A NE2 1 
ATOM   7666  N  N   . GLN   A 1 960  ? -52.89400  72.23400  -29.67400 1.000 57.46271  ?  958  GLN   A N   1 
ATOM   7667  C  CA  . GLN   A 1 960  ? -52.39500  71.84700  -28.36000 1.000 45.36984  ?  958  GLN   A CA  1 
ATOM   7668  C  C   . GLN   A 1 960  ? -52.73800  70.40000  -28.03000 1.000 44.88912  ?  958  GLN   A C   1 
ATOM   7669  O  O   . GLN   A 1 960  ? -51.93100  69.69600  -27.41200 1.000 57.78735  ?  958  GLN   A O   1 
ATOM   7670  C  CB  . GLN   A 1 960  ? -52.95100  72.78900  -27.29300 1.000 41.02242  ?  958  GLN   A CB  1 
ATOM   7671  C  CG  . GLN   A 1 960  ? -52.55900  74.24300  -27.49500 1.000 54.45994  ?  958  GLN   A CG  1 
ATOM   7672  C  CD  . GLN   A 1 960  ? -52.84900  75.10300  -26.28200 1.000 48.40286  ?  958  GLN   A CD  1 
ATOM   7673  O  OE1 . GLN   A 1 960  ? -53.40000  74.62900  -25.28800 1.000 37.03245  ?  958  GLN   A OE1 1 
ATOM   7674  N  NE2 . GLN   A 1 960  ? -52.47700  76.37600  -26.35600 1.000 41.51964  ?  958  GLN   A NE2 1 
ATOM   7675  N  N   . ILE   A 1 961  ? -53.92800  69.94000  -28.42400 1.000 32.02108  ?  959  ILE   A N   1 
ATOM   7676  C  CA  . ILE   A 1 961  ? -54.28100  68.53600  -28.22600 1.000 43.85540  ?  959  ILE   A CA  1 
ATOM   7677  C  C   . ILE   A 1 961  ? -53.28900  67.63600  -28.95300 1.000 49.61060  ?  959  ILE   A C   1 
ATOM   7678  O  O   . ILE   A 1 961  ? -52.86000  66.60200  -28.42400 1.000 49.85720  ?  959  ILE   A O   1 
ATOM   7679  C  CB  . ILE   A 1 961  ? -55.72800  68.27700  -28.68600 1.000 46.90360  ?  959  ILE   A CB  1 
ATOM   7680  C  CG1 . ILE   A 1 961  ? -56.72200  68.91400  -27.70900 1.000 59.13991  ?  959  ILE   A CG1 1 
ATOM   7681  C  CG2 . ILE   A 1 961  ? -55.98500  66.78300  -28.85000 1.000 51.08080  ?  959  ILE   A CG2 1 
ATOM   7682  C  CD1 . ILE   A 1 961  ? -57.77400  67.95500  -27.16700 1.000 53.77872  ?  959  ILE   A CD1 1 
ATOM   7683  N  N   . ALA   A 1 962  ? -52.89500  68.02500  -30.16700 1.000 49.09524  ?  960  ALA   A N   1 
ATOM   7684  C  CA  . ALA   A 1 962  ? -51.94700  67.22300  -30.93100 1.000 43.78008  ?  960  ALA   A CA  1 
ATOM   7685  C  C   . ALA   A 1 962  ? -50.59500  67.14000  -30.23700 1.000 51.03286  ?  960  ALA   A C   1 
ATOM   7686  O  O   . ALA   A 1 962  ? -49.89500  66.12800  -30.36400 1.000 50.70841  ?  960  ALA   A O   1 
ATOM   7687  C  CB  . ALA   A 1 962  ? -51.78900  67.79700  -32.33800 1.000 34.36183  ?  960  ALA   A CB  1 
ATOM   7688  N  N   . TYR   A 1 963  ? -50.21200  68.18800  -29.50400 1.000 41.23145  ?  961  TYR   A N   1 
ATOM   7689  C  CA  . TYR   A 1 963  ? -48.97200  68.13700  -28.73600 1.000 47.63055  ?  961  TYR   A CA  1 
ATOM   7690  C  C   . TYR   A 1 963  ? -49.01800  67.01500  -27.70800 1.000 46.05411  ?  961  TYR   A C   1 
ATOM   7691  O  O   . TYR   A 1 963  ? -48.08600  66.20900  -27.60900 1.000 45.72992  ?  961  TYR   A O   1 
ATOM   7692  C  CB  . TYR   A 1 963  ? -48.71400  69.47800  -28.04700 1.000 47.37532  ?  961  TYR   A CB  1 
ATOM   7693  C  CG  . TYR   A 1 963  ? -47.60000  69.41500  -27.02200 1.000 48.13260  ?  961  TYR   A CG  1 
ATOM   7694  C  CD1 . TYR   A 1 963  ? -46.27100  69.50200  -27.41100 1.000 44.82947  ?  961  TYR   A CD1 1 
ATOM   7695  C  CD2 . TYR   A 1 963  ? -47.87800  69.25400  -25.66900 1.000 43.72167  ?  961  TYR   A CD2 1 
ATOM   7696  C  CE1 . TYR   A 1 963  ? -45.24600  69.43900  -26.48100 1.000 53.33916  ?  961  TYR   A CE1 1 
ATOM   7697  C  CE2 . TYR   A 1 963  ? -46.85900  69.18900  -24.73300 1.000 46.65938  ?  961  TYR   A CE2 1 
ATOM   7698  C  CZ  . TYR   A 1 963  ? -45.54500  69.28200  -25.14500 1.000 49.37258  ?  961  TYR   A CZ  1 
ATOM   7699  O  OH  . TYR   A 1 963  ? -44.52400  69.22000  -24.22100 1.000 54.95980  ?  961  TYR   A OH  1 
ATOM   7700  N  N   . TRP   A 1 964  ? -50.10300  66.94700  -26.93300 1.000 42.18751  ?  962  TRP   A N   1 
ATOM   7701  C  CA  . TRP   A 1 964  ? -50.21100  65.92400  -25.90000 1.000 44.74257  ?  962  TRP   A CA  1 
ATOM   7702  C  C   . TRP   A 1 964  ? -50.37000  64.53300  -26.49800 1.000 45.46509  ?  962  TRP   A C   1 
ATOM   7703  O  O   . TRP   A 1 964  ? -49.84700  63.56000  -25.94300 1.000 51.72806  ?  962  TRP   A O   1 
ATOM   7704  C  CB  . TRP   A 1 964  ? -51.37900  66.24800  -24.96700 1.000 39.87296  ?  962  TRP   A CB  1 
ATOM   7705  C  CG  . TRP   A 1 964  ? -51.13100  67.47100  -24.14300 1.000 41.09397  ?  962  TRP   A CG  1 
ATOM   7706  C  CD1 . TRP   A 1 964  ? -51.82200  68.64600  -24.19400 1.000 42.59548  ?  962  TRP   A CD1 1 
ATOM   7707  C  CD2 . TRP   A 1 964  ? -50.10700  67.65000  -23.15600 1.000 39.88827  ?  962  TRP   A CD2 1 
ATOM   7708  N  NE1 . TRP   A 1 964  ? -51.29500  69.54400  -23.29700 1.000 44.92969  ?  962  TRP   A NE1 1 
ATOM   7709  C  CE2 . TRP   A 1 964  ? -50.24200  68.95600  -22.64700 1.000 46.24758  ?  962  TRP   A CE2 1 
ATOM   7710  C  CE3 . TRP   A 1 964  ? -49.09300  66.83100  -22.65200 1.000 40.55378  ?  962  TRP   A CE3 1 
ATOM   7711  C  CZ2 . TRP   A 1 964  ? -49.40100  69.46300  -21.65900 1.000 45.03420  ?  962  TRP   A CZ2 1 
ATOM   7712  C  CZ3 . TRP   A 1 964  ? -48.25800  67.33600  -21.67300 1.000 47.48455  ?  962  TRP   A CZ3 1 
ATOM   7713  C  CH2 . TRP   A 1 964  ? -48.41800  68.64000  -21.18600 1.000 45.89007  ?  962  TRP   A CH2 1 
ATOM   7714  N  N   . LYS   A 1 965  ? -51.07800  64.41600  -27.62500 1.000 49.18601  ?  963  LYS   A N   1 
ATOM   7715  C  CA  . LYS   A 1 965  ? -51.28800  63.10700  -28.23400 1.000 53.56485  ?  963  LYS   A CA  1 
ATOM   7716  C  C   . LYS   A 1 965  ? -49.97900  62.50300  -28.72300 1.000 50.79695  ?  963  LYS   A C   1 
ATOM   7717  O  O   . LYS   A 1 965  ? -49.81600  61.27700  -28.70000 1.000 68.90296  ?  963  LYS   A O   1 
ATOM   7718  C  CB  . LYS   A 1 965  ? -52.29100  63.22300  -29.38200 1.000 57.67141  ?  963  LYS   A CB  1 
ATOM   7719  C  CG  . LYS   A 1 965  ? -52.74400  61.89600  -29.97600 1.000 63.26211  ?  963  LYS   A CG  1 
ATOM   7720  C  CD  . LYS   A 1 965  ? -54.14100  62.01400  -30.57200 1.000 62.13312  ?  963  LYS   A CD  1 
ATOM   7721  C  CE  . LYS   A 1 965  ? -54.67200  60.66300  -31.02400 1.000 66.90898  ?  963  LYS   A CE  1 
ATOM   7722  N  NZ  . LYS   A 1 965  ? -54.08800  59.53700  -30.24100 1.000 59.14962  ?  963  LYS   A NZ  1 
ATOM   7723  N  N   . THR   A 1 966  ? -49.03800  63.34100  -29.15900 1.000 48.08111  ?  964  THR   A N   1 
ATOM   7724  C  CA  . THR   A 1 966  ? -47.71500  62.87800  -29.55700 1.000 61.79510  ?  964  THR   A CA  1 
ATOM   7725  C  C   . THR   A 1 966  ? -46.73400  62.85400  -28.39200 1.000 64.97335  ?  964  THR   A C   1 
ATOM   7726  O  O   . THR   A 1 966  ? -45.81700  62.02500  -28.37700 1.000 61.36344  ?  964  THR   A O   1 
ATOM   7727  C  CB  . THR   A 1 966  ? -47.15600  63.76300  -30.67900 1.000 58.93114  ?  964  THR   A CB  1 
ATOM   7728  O  OG1 . THR   A 1 966  ? -48.13200  63.90400  -31.71800 1.000 52.44252  ?  964  THR   A OG1 1 
ATOM   7729  C  CG2 . THR   A 1 966  ? -45.90600  63.13900  -31.27000 1.000 68.21269  ?  964  THR   A CG2 1 
ATOM   7730  N  N   . LEU   A 1 967  ? -46.90900  63.74200  -27.41100 1.000 63.67851  ?  965  LEU   A N   1 
ATOM   7731  C  CA  . LEU   A 1 967  ? -46.03300  63.73800  -26.24400 1.000 56.92999  ?  965  LEU   A CA  1 
ATOM   7732  C  C   . LEU   A 1 967  ? -46.18100  62.44500  -25.44900 1.000 62.14403  ?  965  LEU   A C   1 
ATOM   7733  O  O   . LEU   A 1 967  ? -45.18500  61.85400  -25.01700 1.000 80.34403  ?  965  LEU   A O   1 
ATOM   7734  C  CB  . LEU   A 1 967  ? -46.34000  64.95500  -25.36700 1.000 56.73977  ?  965  LEU   A CB  1 
ATOM   7735  C  CG  . LEU   A 1 967  ? -45.32400  65.43400  -24.33300 1.000 36.03570  ?  965  LEU   A CG  1 
ATOM   7736  C  CD1 . LEU   A 1 967  ? -45.45800  64.66100  -23.02800 1.000 48.33764  ?  965  LEU   A CD1 1 
ATOM   7737  C  CD2 . LEU   A 1 967  ? -43.92100  65.31500  -24.90300 1.000 60.65038  ?  965  LEU   A CD2 1 
ATOM   7738  N  N   . LEU   A 1 968  ? -47.41800  61.98700  -25.25500 1.000 63.41255  ?  966  LEU   A N   1 
ATOM   7739  C  CA  . LEU   A 1 968  ? -47.70500  60.80500  -24.45500 1.000 63.83170  ?  966  LEU   A CA  1 
ATOM   7740  C  C   . LEU   A 1 968  ? -47.97900  59.56500  -25.29600 1.000 64.27646  ?  966  LEU   A C   1 
ATOM   7741  O  O   . LEU   A 1 968  ? -48.51000  58.57900  -24.77300 1.000 61.95092  ?  966  LEU   A O   1 
ATOM   7742  C  CB  . LEU   A 1 968  ? -48.88700  61.07100  -23.52500 1.000 50.80373  ?  966  LEU   A CB  1 
ATOM   7743  C  CG  . LEU   A 1 968  ? -48.74800  62.31800  -22.65600 1.000 59.95000  ?  966  LEU   A CG  1 
ATOM   7744  C  CD1 . LEU   A 1 968  ? -50.11000  62.94600  -22.43000 1.000 48.24019  ?  966  LEU   A CD1 1 
ATOM   7745  C  CD2 . LEU   A 1 968  ? -48.06300  61.98500  -21.33700 1.000 57.56458  ?  966  LEU   A CD2 1 
ATOM   7746  N  N   . GLN   A 1 969  ? -47.64000  59.59100  -26.58000 1.000 70.09779  ?  967  GLN   A N   1 
ATOM   7747  C  CA  . GLN   A 1 969  ? -47.69500  58.38000  -27.37900 1.000 72.20752  ?  967  GLN   A CA  1 
ATOM   7748  C  C   . GLN   A 1 969  ? -46.53700  57.45600  -27.00700 1.000 85.04959  ?  967  GLN   A C   1 
ATOM   7749  O  O   . GLN   A 1 969  ? -45.56900  57.85800  -26.35400 1.000 92.22825  ?  967  GLN   A O   1 
ATOM   7750  C  CB  . GLN   A 1 969  ? -47.64700  58.72500  -28.87100 1.000 80.65156  ?  967  GLN   A CB  1 
ATOM   7751  C  CG  . GLN   A 1 969  ? -46.27000  59.14500  -29.37000 1.000 82.97808  ?  967  GLN   A CG  1 
ATOM   7752  C  CD  . GLN   A 1 969  ? -46.16400  59.13900  -30.88300 1.000 89.66728  ?  967  GLN   A CD  1 
ATOM   7753  O  OE1 . GLN   A 1 969  ? -47.17500  59.14800  -31.58400 1.000 100.11192 ?  967  GLN   A OE1 1 
ATOM   7754  N  NE2 . GLN   A 1 969  ? -44.93800  59.16400  -31.39400 1.000 89.77127  ?  967  GLN   A NE2 1 
ATOM   7755  N  N   . GLY   A 1 970  ? -46.65100  56.19700  -27.42300 1.000 69.04575  ?  968  GLY   A N   1 
ATOM   7756  C  CA  . GLY   A 1 970  ? -45.64200  55.20500  -27.10600 1.000 81.18330  ?  968  GLY   A CA  1 
ATOM   7757  C  C   . GLY   A 1 970  ? -45.63100  54.78200  -25.65000 1.000 84.46795  ?  968  GLY   A C   1 
ATOM   7758  O  O   . GLY   A 1 970  ? -46.37600  55.32700  -24.83000 1.000 88.11730  ?  968  GLY   A O   1 
ATOM   7759  N  N   . GLU   A 1 971  ? -44.78400  53.80600  -25.31600 1.000 77.83241  ?  969  GLU   A N   1 
ATOM   7760  C  CA  . GLU   A 1 971  ? -44.72000  53.30000  -23.95000 1.000 70.90635  ?  969  GLU   A CA  1 
ATOM   7761  C  C   . GLU   A 1 971  ? -44.20400  54.37900  -23.00700 1.000 76.15939  ?  969  GLU   A C   1 
ATOM   7762  O  O   . GLU   A 1 971  ? -43.04100  54.78500  -23.08700 1.000 86.35457  ?  969  GLU   A O   1 
ATOM   7763  C  CB  . GLU   A 1 971  ? -43.83500  52.05500  -23.85700 1.000 72.74264  ?  969  GLU   A CB  1 
ATOM   7764  C  CG  . GLU   A 1 971  ? -43.54400  51.62000  -22.41900 1.000 91.68600  ?  969  GLU   A CG  1 
ATOM   7765  C  CD  . GLU   A 1 971  ? -42.23900  50.86000  -22.28600 1.000 98.28476  ?  969  GLU   A CD  1 
ATOM   7766  O  OE1 . GLU   A 1 971  ? -42.08800  49.81600  -22.95300 1.000 104.81869 ?  969  GLU   A OE1 1 
ATOM   7767  O  OE2 . GLU   A 1 971  ? -41.36100  51.31100  -21.51800 1.000 102.04059 -1 969  GLU   A OE2 1 
ATOM   7768  N  N   . LEU   A 1 972  ? -45.06700  54.84900  -22.11600 1.000 73.83066  ?  970  LEU   A N   1 
ATOM   7769  C  CA  . LEU   A 1 972  ? -44.68200  55.87400  -21.16900 1.000 60.50620  ?  970  LEU   A CA  1 
ATOM   7770  C  C   . LEU   A 1 972  ? -43.83100  55.26700  -20.05800 1.000 59.47898  ?  970  LEU   A C   1 
ATOM   7771  O  O   . LEU   A 1 972  ? -43.87700  54.05800  -19.82100 1.000 67.13757  ?  970  LEU   A O   1 
ATOM   7772  C  CB  . LEU   A 1 972  ? -45.92900  56.54200  -20.60100 1.000 63.75511  ?  970  LEU   A CB  1 
ATOM   7773  C  CG  . LEU   A 1 972  ? -46.30000  57.87000  -21.26000 1.000 72.65094  ?  970  LEU   A CG  1 
ATOM   7774  C  CD1 . LEU   A 1 972  ? -46.14600  57.81400  -22.76600 1.000 85.85863  ?  970  LEU   A CD1 1 
ATOM   7775  C  CD2 . LEU   A 1 972  ? -47.72400  58.18600  -20.92300 1.000 64.63006  ?  970  LEU   A CD2 1 
ATOM   7776  N  N   . PRO   A 1 973  ? -43.02900  56.08000  -19.37100 1.000 52.69163  ?  971  PRO   A N   1 
ATOM   7777  C  CA  . PRO   A 1 973  ? -42.18000  55.54100  -18.30400 1.000 54.53582  ?  971  PRO   A CA  1 
ATOM   7778  C  C   . PRO   A 1 973  ? -43.00800  55.01200  -17.14300 1.000 54.50575  ?  971  PRO   A C   1 
ATOM   7779  O  O   . PRO   A 1 973  ? -44.18900  55.32500  -16.98100 1.000 59.01733  ?  971  PRO   A O   1 
ATOM   7780  C  CB  . PRO   A 1 973  ? -41.33000  56.74400  -17.88100 1.000 57.48883  ?  971  PRO   A CB  1 
ATOM   7781  C  CG  . PRO   A 1 973  ? -42.14800  57.92200  -18.25400 1.000 58.21352  ?  971  PRO   A CG  1 
ATOM   7782  C  CD  . PRO   A 1 973  ? -42.83700  57.53300  -19.53100 1.000 60.97672  ?  971  PRO   A CD  1 
ATOM   7783  N  N   . ALA   A 1 974  ? -42.35900  54.18400  -16.32700 1.000 54.49400  ?  972  ALA   A N   1 
ATOM   7784  C  CA  . ALA   A 1 974  ? -42.98400  53.57300  -15.16100 1.000 61.13947  ?  972  ALA   A CA  1 
ATOM   7785  C  C   . ALA   A 1 974  ? -42.16300  53.92300  -13.93100 1.000 60.87996  ?  972  ALA   A C   1 
ATOM   7786  O  O   . ALA   A 1 974  ? -40.99100  53.54500  -13.83800 1.000 63.74313  ?  972  ALA   A O   1 
ATOM   7787  C  CB  . ALA   A 1 974  ? -43.09000  52.05400  -15.32700 1.000 60.91580  ?  972  ALA   A CB  1 
ATOM   7788  N  N   . VAL   A 1 975  ? -42.77200  54.64200  -12.99300 1.000 53.31580  ?  973  VAL   A N   1 
ATOM   7789  C  CA  . VAL   A 1 975  ? -42.10500  55.06800  -11.76800 1.000 49.66261  ?  973  VAL   A CA  1 
ATOM   7790  C  C   . VAL   A 1 975  ? -42.57500  54.13900  -10.65500 1.000 58.57373  ?  973  VAL   A C   1 
ATOM   7791  O  O   . VAL   A 1 975  ? -43.65900  54.31600  -10.09300 1.000 67.15370  ?  973  VAL   A O   1 
ATOM   7792  C  CB  . VAL   A 1 975  ? -42.38900  56.53900  -11.45200 1.000 43.00550  ?  973  VAL   A CB  1 
ATOM   7793  C  CG1 . VAL   A 1 975  ? -41.54800  57.00700  -10.27400 1.000 48.14515  ?  973  VAL   A CG1 1 
ATOM   7794  C  CG2 . VAL   A 1 975  ? -42.09800  57.39500  -12.66800 1.000 33.70287  ?  973  VAL   A CG2 1 
ATOM   7795  N  N   . GLN   A 1 976  ? -41.75800  53.13300  -10.34100 1.000 59.61732  ?  974  GLN   A N   1 
ATOM   7796  C  CA  . GLN   A 1 976  ? -42.04500  52.20100  -9.25100  1.000 59.47218  ?  974  GLN   A CA  1 
ATOM   7797  C  C   . GLN   A 1 976  ? -41.36000  52.72200  -7.99600  1.000 49.42445  ?  974  GLN   A C   1 
ATOM   7798  O  O   . GLN   A 1 976  ? -40.17500  52.46200  -7.76800  1.000 63.33813  ?  974  GLN   A O   1 
ATOM   7799  C  CB  . GLN   A 1 976  ? -41.57000  50.79100  -9.59300  1.000 52.81904  ?  974  GLN   A CB  1 
ATOM   7800  C  CG  . GLN   A 1 976  ? -42.09200  50.25800  -10.90900 1.000 72.33073  ?  974  GLN   A CG  1 
ATOM   7801  C  CD  . GLN   A 1 976  ? -41.97600  48.74900  -11.01600 1.000 76.13258  ?  974  GLN   A CD  1 
ATOM   7802  O  OE1 . GLN   A 1 976  ? -41.04000  48.22700  -11.62300 1.000 74.12466  ?  974  GLN   A OE1 1 
ATOM   7803  N  NE2 . GLN   A 1 976  ? -42.93000  48.04000  -10.42300 1.000 78.70124  ?  974  GLN   A NE2 1 
ATOM   7804  N  N   . LEU   A 1 977  ? -42.10200  53.45900  -7.18300  1.000 47.33760  ?  975  LEU   A N   1 
ATOM   7805  C  CA  . LEU   A 1 977  ? -41.53700  53.95500  -5.94100  1.000 42.74112  ?  975  LEU   A CA  1 
ATOM   7806  C  C   . LEU   A 1 977  ? -41.49500  52.84300  -4.89500  1.000 44.44490  ?  975  LEU   A C   1 
ATOM   7807  O  O   . LEU   A 1 977  ? -42.33200  51.93600  -4.90900  1.000 39.15807  ?  975  LEU   A O   1 
ATOM   7808  C  CB  . LEU   A 1 977  ? -42.35400  55.12900  -5.41600  1.000 41.20754  ?  975  LEU   A CB  1 
ATOM   7809  C  CG  . LEU   A 1 977  ? -42.18300  56.44000  -6.18400  1.000 44.36955  ?  975  LEU   A CG  1 
ATOM   7810  C  CD1 . LEU   A 1 977  ? -42.60100  57.61200  -5.31400  1.000 41.34210  ?  975  LEU   A CD1 1 
ATOM   7811  C  CD2 . LEU   A 1 977  ? -40.75200  56.61000  -6.68800  1.000 34.23795  ?  975  LEU   A CD2 1 
ATOM   7812  N  N   . PRO   A 1 978  ? -40.51900  52.88300  -3.98100  1.000 47.12607  ?  976  PRO   A N   1 
ATOM   7813  C  CA  . PRO   A 1 978  ? -40.44000  51.84200  -2.94600  1.000 39.03030  ?  976  PRO   A CA  1 
ATOM   7814  C  C   . PRO   A 1 978  ? -41.61400  51.90000  -1.98400  1.000 50.59463  ?  976  PRO   A C   1 
ATOM   7815  O  O   . PRO   A 1 978  ? -41.44300  52.29700  -0.82900  1.000 59.37231  ?  976  PRO   A O   1 
ATOM   7816  C  CB  . PRO   A 1 978  ? -39.11900  52.15600  -2.23100  1.000 28.77161  ?  976  PRO   A CB  1 
ATOM   7817  C  CG  . PRO   A 1 978  ? -38.88600  53.60900  -2.49200  1.000 47.46493  ?  976  PRO   A CG  1 
ATOM   7818  C  CD  . PRO   A 1 978  ? -39.41800  53.85500  -3.87200  1.000 51.20674  ?  976  PRO   A CD  1 
ATOM   7819  N  N   . THR   A 1 979  ? -42.80200  51.51100  -2.43900  1.000 43.70826  ?  977  THR   A N   1 
ATOM   7820  C  CA  . THR   A 1 979  ? -44.00700  51.58000  -1.62700  1.000 44.04410  ?  977  THR   A CA  1 
ATOM   7821  C  C   . THR   A 1 979  ? -44.27700  50.24700  -0.94200  1.000 45.23841  ?  977  THR   A C   1 
ATOM   7822  O  O   . THR   A 1 979  ? -43.62600  49.23300  -1.20300  1.000 51.28585  ?  977  THR   A O   1 
ATOM   7823  C  CB  . THR   A 1 979  ? -45.22200  51.97500  -2.47600  1.000 45.80692  ?  977  THR   A CB  1 
ATOM   7824  O  OG1 . THR   A 1 979  ? -45.61200  50.87400  -3.30900  1.000 46.19907  ?  977  THR   A OG1 1 
ATOM   7825  C  CG2 . THR   A 1 979  ? -44.89200  53.16800  -3.34900  1.000 51.27977  ?  977  THR   A CG2 1 
ATOM   7826  N  N   . LYS   A 1 980  ? -45.25700  50.26800  -0.04400  1.000 52.51336  ?  978  LYS   A N   1 
ATOM   7827  C  CA  . LYS   A 1 980  ? -45.81100  49.04000  0.49600   1.000 37.66097  ?  978  LYS   A CA  1 
ATOM   7828  C  C   . LYS   A 1 980  ? -46.68300  48.37600  -0.57000  1.000 57.93296  ?  978  LYS   A C   1 
ATOM   7829  O  O   . LYS   A 1 980  ? -46.86600  48.89600  -1.67600  1.000 61.31942  ?  978  LYS   A O   1 
ATOM   7830  C  CB  . LYS   A 1 980  ? -46.60000  49.33700  1.76900   1.000 42.12144  ?  978  LYS   A CB  1 
ATOM   7831  C  CG  . LYS   A 1 980  ? -45.84600  49.01700  3.05300   1.000 43.99167  ?  978  LYS   A CG  1 
ATOM   7832  C  CD  . LYS   A 1 980  ? -46.35200  49.84600  4.22600   1.000 49.41573  ?  978  LYS   A CD  1 
ATOM   7833  C  CE  . LYS   A 1 980  ? -47.86500  49.76600  4.35800   1.000 64.92997  ?  978  LYS   A CE  1 
ATOM   7834  N  NZ  . LYS   A 1 980  ? -48.36600  50.56300  5.51300   1.000 64.03221  ?  978  LYS   A NZ  1 
ATOM   7835  N  N   . LYS   A 1 981  ? -47.22700  47.20800  -0.23700  1.000 50.61936  ?  979  LYS   A N   1 
ATOM   7836  C  CA  . LYS   A 1 981  ? -48.01800  46.45000  -1.20000  1.000 49.88595  ?  979  LYS   A CA  1 
ATOM   7837  C  C   . LYS   A 1 981  ? -49.24500  47.24500  -1.62900  1.000 51.44655  ?  979  LYS   A C   1 
ATOM   7838  O  O   . LYS   A 1 981  ? -50.06200  47.64500  -0.79400  1.000 52.48326  ?  979  LYS   A O   1 
ATOM   7839  C  CB  . LYS   A 1 981  ? -48.43000  45.10700  -0.60100  1.000 67.98707  ?  979  LYS   A CB  1 
ATOM   7840  C  CG  . LYS   A 1 981  ? -47.64200  43.92200  -1.14100  1.000 63.28698  ?  979  LYS   A CG  1 
ATOM   7841  C  CD  . LYS   A 1 981  ? -48.40600  43.22200  -2.25500  1.000 77.48337  ?  979  LYS   A CD  1 
ATOM   7842  C  CE  . LYS   A 1 981  ? -47.58300  42.10900  -2.87900  1.000 90.55300  ?  979  LYS   A CE  1 
ATOM   7843  N  NZ  . LYS   A 1 981  ? -48.33200  41.39900  -3.95500  1.000 96.32290  ?  979  LYS   A NZ  1 
ATOM   7844  N  N   . ARG   A 1 982  ? -49.36700  47.47000  -2.92900  1.000 49.50339  ?  980  ARG   A N   1 
ATOM   7845  C  CA  . ARG   A 1 982  ? -50.44500  48.29500  -3.46200  1.000 58.29738  ?  980  ARG   A CA  1 
ATOM   7846  C  C   . ARG   A 1 982  ? -51.79300  47.62400  -3.22900  1.000 50.75621  ?  980  ARG   A C   1 
ATOM   7847  O  O   . ARG   A 1 982  ? -51.98300  46.47800  -3.65600  1.000 59.24606  ?  980  ARG   A O   1 
ATOM   7848  C  CB  . ARG   A 1 982  ? -50.22700  48.54300  -4.95300  1.000 66.99070  ?  980  ARG   A CB  1 
ATOM   7849  C  CG  . ARG   A 1 982  ? -48.87200  49.14900  -5.29500  1.000 60.23365  ?  980  ARG   A CG  1 
ATOM   7850  C  CD  . ARG   A 1 982  ? -48.90200  49.86900  -6.63700  1.000 64.03056  ?  980  ARG   A CD  1 
ATOM   7851  N  NE  . ARG   A 1 982  ? -49.90300  50.93000  -6.65900  1.000 67.44238  ?  980  ARG   A NE  1 
ATOM   7852  C  CZ  . ARG   A 1 982  ? -49.62800  52.22300  -6.55400  1.000 62.87242  ?  980  ARG   A CZ  1 
ATOM   7853  N  NH1 . ARG   A 1 982  ? -48.38400  52.65800  -6.43800  1.000 69.99782  ?  980  ARG   A NH1 1 
ATOM   7854  N  NH2 . ARG   A 1 982  ? -50.62700  53.10100  -6.56100  1.000 56.06338  ?  980  ARG   A NH2 1 
ATOM   7855  N  N   . PRO   A 1 983  ? -52.74300  48.28000  -2.56300  1.000 63.31133  ?  981  PRO   A N   1 
ATOM   7856  C  CA  . PRO   A 1 983  ? -54.05000  47.66100  -2.36300  1.000 65.07448  ?  981  PRO   A CA  1 
ATOM   7857  C  C   . PRO   A 1 983  ? -54.76100  47.47400  -3.69400  1.000 76.94342  ?  981  PRO   A C   1 
ATOM   7858  O  O   . PRO   A 1 983  ? -54.56200  48.26100  -4.63600  1.000 84.55977  ?  981  PRO   A O   1 
ATOM   7859  C  CB  . PRO   A 1 983  ? -54.78700  48.66500  -1.46600  1.000 46.34974  ?  981  PRO   A CB  1 
ATOM   7860  C  CG  . PRO   A 1 983  ? -53.71600  49.51000  -0.85600  1.000 54.96363  ?  981  PRO   A CG  1 
ATOM   7861  C  CD  . PRO   A 1 983  ? -52.62900  49.57800  -1.87900  1.000 65.88152  ?  981  PRO   A CD  1 
ATOM   7862  N  N   . PRO   A 1 984  ? -55.58200  46.41800  -3.81600  1.000 82.46310  ?  982  PRO   A N   1 
ATOM   7863  C  CA  . PRO   A 1 984  ? -56.29900  46.17000  -5.07700  1.000 83.22448  ?  982  PRO   A CA  1 
ATOM   7864  C  C   . PRO   A 1 984  ? -57.05600  47.39000  -5.57600  1.000 77.15053  ?  982  PRO   A C   1 
ATOM   7865  O  O   . PRO   A 1 984  ? -56.84000  47.84500  -6.70300  1.000 79.41443  ?  982  PRO   A O   1 
ATOM   7866  C  CB  . PRO   A 1 984  ? -57.26400  45.03100  -4.72500  1.000 70.88223  ?  982  PRO   A CB  1 
ATOM   7867  C  CG  . PRO   A 1 984  ? -56.82700  44.49400  -3.39900  1.000 75.42508  ?  982  PRO   A CG  1 
ATOM   7868  C  CD  . PRO   A 1 984  ? -55.67000  45.28700  -2.88200  1.000 85.89573  ?  982  PRO   A CD  1 
ATOM   7869  N  N   . GLN   A 1 985  ? -57.94300  47.92700  -4.74600  1.000 78.35892  ?  983  GLN   A N   1 
ATOM   7870  C  CA  . GLN   A 1 985  ? -58.66200  49.14700  -5.07600  1.000 88.98282  ?  983  GLN   A CA  1 
ATOM   7871  C  C   . GLN   A 1 985  ? -57.86700  50.36400  -4.61600  1.000 88.50771  ?  983  GLN   A C   1 
ATOM   7872  O  O   . GLN   A 1 985  ? -57.08200  50.29400  -3.66600  1.000 97.60291  ?  983  GLN   A O   1 
ATOM   7873  C  CB  . GLN   A 1 985  ? -60.04900  49.15200  -4.43100  1.000 97.00337  ?  983  GLN   A CB  1 
ATOM   7874  C  CG  . GLN   A 1 985  ? -60.92300  47.96800  -4.82500  1.000 98.33266  ?  983  GLN   A CG  1 
ATOM   7875  C  CD  . GLN   A 1 985  ? -61.74200  48.23300  -6.07400  1.000 105.27046 ?  983  GLN   A CD  1 
ATOM   7876  O  OE1 . GLN   A 1 985  ? -62.04100  49.38100  -6.40200  1.000 114.02026 ?  983  GLN   A OE1 1 
ATOM   7877  N  NE2 . GLN   A 1 985  ? -62.11300  47.16800  -6.77700  1.000 89.63300  ?  983  GLN   A NE2 1 
ATOM   7878  N  N   . LEU   A 1 986  ? -58.07300  51.48400  -5.30400  1.000 84.89650  ?  984  LEU   A N   1 
ATOM   7879  C  CA  . LEU   A 1 986  ? -57.36200  52.70900  -4.96200  1.000 73.34388  ?  984  LEU   A CA  1 
ATOM   7880  C  C   . LEU   A 1 986  ? -57.87800  53.26700  -3.64000  1.000 74.18581  ?  984  LEU   A C   1 
ATOM   7881  O  O   . LEU   A 1 986  ? -59.09000  53.34500  -3.41700  1.000 77.77427  ?  984  LEU   A O   1 
ATOM   7882  C  CB  . LEU   A 1 986  ? -57.52300  53.74500  -6.07500  1.000 82.44040  ?  984  LEU   A CB  1 
ATOM   7883  C  CG  . LEU   A 1 986  ? -56.37000  53.84500  -7.07800  1.000 76.45346  ?  984  LEU   A CG  1 
ATOM   7884  C  CD1 . LEU   A 1 986  ? -56.67700  54.87700  -8.15000  1.000 70.10431  ?  984  LEU   A CD1 1 
ATOM   7885  C  CD2 . LEU   A 1 986  ? -55.06700  54.17300  -6.37100  1.000 79.40845  ?  984  LEU   A CD2 1 
ATOM   7886  N  N   . THR   A 1 987  ? -56.95600  53.65300  -2.76300  1.000 63.55189  ?  985  THR   A N   1 
ATOM   7887  C  CA  . THR   A 1 987  ? -57.29200  54.19500  -1.45500  1.000 59.59044  ?  985  THR   A CA  1 
ATOM   7888  C  C   . THR   A 1 987  ? -56.84500  55.64700  -1.36300  1.000 56.88718  ?  985  THR   A C   1 
ATOM   7889  O  O   . THR   A 1 987  ? -55.86900  56.05400  -2.00000  1.000 74.10028  ?  985  THR   A O   1 
ATOM   7890  C  CB  . THR   A 1 987  ? -56.64000  53.38400  -0.33700  1.000 58.72524  ?  985  THR   A CB  1 
ATOM   7891  O  OG1 . THR   A 1 987  ? -55.21500  53.44100  -0.48100  1.000 63.68740  ?  985  THR   A OG1 1 
ATOM   7892  C  CG2 . THR   A 1 987  ? -57.09300  51.93700  -0.40700  1.000 59.62618  ?  985  THR   A CG2 1 
ATOM   7893  N  N   . PHE   A 1 988  ? -57.57500  56.43100  -0.56900  1.000 44.04271  ?  986  PHE   A N   1 
ATOM   7894  C  CA  . PHE   A 1 988  ? -57.32400  57.86400  -0.45400  1.000 46.30117  ?  986  PHE   A CA  1 
ATOM   7895  C  C   . PHE   A 1 988  ? -56.97200  58.28700  0.96900   1.000 41.73250  ?  986  PHE   A C   1 
ATOM   7896  O  O   . PHE   A 1 988  ? -56.95000  59.49000  1.25800   1.000 34.63618  ?  986  PHE   A O   1 
ATOM   7897  C  CB  . PHE   A 1 988  ? -58.53500  58.66300  -0.95700  1.000 45.10294  ?  986  PHE   A CB  1 
ATOM   7898  C  CG  . PHE   A 1 988  ? -58.65900  58.72400  -2.46500  1.000 72.80245  ?  986  PHE   A CG  1 
ATOM   7899  C  CD1 . PHE   A 1 988  ? -58.37800  57.61900  -3.25600  1.000 73.01850  ?  986  PHE   A CD1 1 
ATOM   7900  C  CD2 . PHE   A 1 988  ? -59.06600  59.89300  -3.09000  1.000 86.67444  ?  986  PHE   A CD2 1 
ATOM   7901  C  CE1 . PHE   A 1 988  ? -58.49300  57.67800  -4.63200  1.000 82.93492  ?  986  PHE   A CE1 1 
ATOM   7902  C  CE2 . PHE   A 1 988  ? -59.18400  59.95900  -4.46900  1.000 85.14332  ?  986  PHE   A CE2 1 
ATOM   7903  C  CZ  . PHE   A 1 988  ? -58.89700  58.84900  -5.24000  1.000 95.63861  ?  986  PHE   A CZ  1 
ATOM   7904  N  N   . ASP   A 1 989  ? -56.70000  57.33900  1.86400   1.000 41.01431  ?  987  ASP   A N   1 
ATOM   7905  C  CA  . ASP   A 1 989  ? -56.28200  57.67800  3.21900   1.000 38.74655  ?  987  ASP   A CA  1 
ATOM   7906  C  C   . ASP   A 1 989  ? -54.84400  58.18000  3.20800   1.000 40.84149  ?  987  ASP   A C   1 
ATOM   7907  O  O   . ASP   A 1 989  ? -53.97100  57.57400  2.58000   1.000 35.96258  ?  987  ASP   A O   1 
ATOM   7908  C  CB  . ASP   A 1 989  ? -56.39900  56.46200  4.13800   1.000 52.84804  ?  987  ASP   A CB  1 
ATOM   7909  C  CG  . ASP   A 1 989  ? -57.77200  55.82400  4.09900   1.000 57.42077  ?  987  ASP   A CG  1 
ATOM   7910  O  OD1 . ASP   A 1 989  ? -58.13000  55.22500  3.06200   1.000 80.12849  ?  987  ASP   A OD1 1 
ATOM   7911  O  OD2 . ASP   A 1 989  ? -58.49100  55.92000  5.11500   1.000 57.00811  -1 987  ASP   A OD2 1 
ATOM   7912  N  N   . GLY   A 1 990  ? -54.58700  59.28000  3.91800   1.000 45.59037  ?  988  GLY   A N   1 
ATOM   7913  C  CA  . GLY   A 1 990  ? -53.27200  59.88300  3.85000   1.000 44.91902  ?  988  GLY   A CA  1 
ATOM   7914  C  C   . GLY   A 1 990  ? -52.88900  60.65200  5.09500   1.000 29.82549  ?  988  GLY   A C   1 
ATOM   7915  O  O   . GLY   A 1 990  ? -53.69500  60.87300  6.00000   1.000 28.97093  ?  988  GLY   A O   1 
ATOM   7916  N  N   . ALA   A 1 991  ? -51.61800  61.04800  5.12400   1.000 35.38174  ?  989  ALA   A N   1 
ATOM   7917  C  CA  . ALA   A 1 991  ? -51.06000  61.90600  6.15600   1.000 33.31501  ?  989  ALA   A CA  1 
ATOM   7918  C  C   . ALA   A 1 991  ? -50.09000  62.86600  5.48000   1.000 36.63394  ?  989  ALA   A C   1 
ATOM   7919  O  O   . ALA   A 1 991  ? -49.87200  62.79800  4.26500   1.000 36.23763  ?  989  ALA   A O   1 
ATOM   7920  C  CB  . ALA   A 1 991  ? -50.37700  61.08500  7.25600   1.000 29.31327  ?  989  ALA   A CB  1 
ATOM   7921  N  N   . ILE   A 1 992  ? -49.50900  63.77800  6.26300   1.000 30.11412  ?  990  ILE   A N   1 
ATOM   7922  C  CA  . ILE   A 1 992  ? -48.56000  64.74800  5.72900   1.000 38.58117  ?  990  ILE   A CA  1 
ATOM   7923  C  C   . ILE   A 1 992  ? -47.30500  64.77500  6.59200   1.000 38.59971  ?  990  ILE   A C   1 
ATOM   7924  O  O   . ILE   A 1 992  ? -47.34300  64.52800  7.80100   1.000 42.09588  ?  990  ILE   A O   1 
ATOM   7925  C  CB  . ILE   A 1 992  ? -49.15500  66.17700  5.61200   1.000 29.16576  ?  990  ILE   A CB  1 
ATOM   7926  C  CG1 . ILE   A 1 992  ? -49.11300  66.89300  6.96000   1.000 38.63001  ?  990  ILE   A CG1 1 
ATOM   7927  C  CG2 . ILE   A 1 992  ? -50.56700  66.16200  5.03600   1.000 31.12404  ?  990  ILE   A CG2 1 
ATOM   7928  C  CD1 . ILE   A 1 992  ? -49.08500  68.38900  6.84700   1.000 63.42795  ?  990  ILE   A CD1 1 
ATOM   7929  N  N   . GLN   A 1 993  ? -46.17900  65.06100  5.94400   1.000 36.62785  ?  991  GLN   A N   1 
ATOM   7930  C  CA  . GLN   A 1 993  ? -44.92200  65.37000  6.60800   1.000 34.92734  ?  991  GLN   A CA  1 
ATOM   7931  C  C   . GLN   A 1 993  ? -44.39400  66.67300  6.03100   1.000 35.32060  ?  991  GLN   A C   1 
ATOM   7932  O  O   . GLN   A 1 993  ? -44.58700  66.96200  4.84700   1.000 45.43118  ?  991  GLN   A O   1 
ATOM   7933  C  CB  . GLN   A 1 993  ? -43.88600  64.25200  6.42300   1.000 31.94855  ?  991  GLN   A CB  1 
ATOM   7934  C  CG  . GLN   A 1 993  ? -42.80300  64.22000  7.49100   1.000 36.74751  ?  991  GLN   A CG  1 
ATOM   7935  C  CD  . GLN   A 1 993  ? -43.23400  63.46900  8.73300   1.000 50.70123  ?  991  GLN   A CD  1 
ATOM   7936  O  OE1 . GLN   A 1 993  ? -43.21100  64.01100  9.83800   1.000 66.10009  ?  991  GLN   A OE1 1 
ATOM   7937  N  NE2 . GLN   A 1 993  ? -43.63400  62.21400  8.55700   1.000 63.04324  ?  991  GLN   A NE2 1 
ATOM   7938  N  N   . MET   A 1 994  ? -43.73100  67.46600  6.86600   1.000 31.53059  ?  992  MET   A N   1 
ATOM   7939  C  CA  . MET   A 1 994  ? -43.29300  68.79500  6.46800   1.000 39.24545  ?  992  MET   A CA  1 
ATOM   7940  C  C   . MET   A 1 994  ? -41.78000  68.91500  6.58700   1.000 47.49212  ?  992  MET   A C   1 
ATOM   7941  O  O   . MET   A 1 994  ? -41.17600  68.40100  7.53500   1.000 51.69521  ?  992  MET   A O   1 
ATOM   7942  C  CB  . MET   A 1 994  ? -43.97700  69.87500  7.31100   1.000 33.04398  ?  992  MET   A CB  1 
ATOM   7943  C  CG  . MET   A 1 994  ? -44.06000  71.22900  6.62700   1.000 49.90674  ?  992  MET   A CG  1 
ATOM   7944  S  SD  . MET   A 1 994  ? -42.76500  72.37100  7.15500   1.000 96.05266  ?  992  MET   A SD  1 
ATOM   7945  C  CE  . MET   A 1 994  ? -43.31400  72.77500  8.81300   1.000 68.43247  ?  992  MET   A CE  1 
ATOM   7946  N  N   . TYR   A 1 995  ? -41.17400  69.59400  5.61600   1.000 40.45797  ?  993  TYR   A N   1 
ATOM   7947  C  CA  . TYR   A 1 995  ? -39.73700  69.82600  5.58000   1.000 37.79843  ?  993  TYR   A CA  1 
ATOM   7948  C  C   . TYR   A 1 995  ? -39.50500  71.30300  5.30500   1.000 33.08971  ?  993  TYR   A C   1 
ATOM   7949  O  O   . TYR   A 1 995  ? -40.06900  71.85600  4.35600   1.000 37.53522  ?  993  TYR   A O   1 
ATOM   7950  C  CB  . TYR   A 1 995  ? -39.06200  68.94500  4.51500   1.000 28.01548  ?  993  TYR   A CB  1 
ATOM   7951  C  CG  . TYR   A 1 995  ? -37.69600  69.41300  4.05100   1.000 34.52688  ?  993  TYR   A CG  1 
ATOM   7952  C  CD1 . TYR   A 1 995  ? -36.69700  69.73900  4.96200   1.000 41.10511  ?  993  TYR   A CD1 1 
ATOM   7953  C  CD2 . TYR   A 1 995  ? -37.40000  69.51200  2.69600   1.000 38.29652  ?  993  TYR   A CD2 1 
ATOM   7954  C  CE1 . TYR   A 1 995  ? -35.45000  70.16500  4.53700   1.000 35.83431  ?  993  TYR   A CE1 1 
ATOM   7955  C  CE2 . TYR   A 1 995  ? -36.15500  69.93600  2.26200   1.000 32.71774  ?  993  TYR   A CE2 1 
ATOM   7956  C  CZ  . TYR   A 1 995  ? -35.18400  70.26100  3.18800   1.000 34.11142  ?  993  TYR   A CZ  1 
ATOM   7957  O  OH  . TYR   A 1 995  ? -33.94300  70.68400  2.76900   1.000 35.48055  ?  993  TYR   A OH  1 
ATOM   7958  N  N   . ARG   A 1 996  ? -38.69100  71.94000  6.13900   1.000 31.58829  ?  994  ARG   A N   1 
ATOM   7959  C  CA  . ARG   A 1 996  ? -38.43200  73.37100  6.05000   1.000 35.35629  ?  994  ARG   A CA  1 
ATOM   7960  C  C   . ARG   A 1 996  ? -37.04200  73.60600  5.47700   1.000 41.03905  ?  994  ARG   A C   1 
ATOM   7961  O  O   . ARG   A 1 996  ? -36.04900  73.10800  6.01900   1.000 37.59433  ?  994  ARG   A O   1 
ATOM   7962  C  CB  . ARG   A 1 996  ? -38.56400  74.03200  7.42100   1.000 27.84320  ?  994  ARG   A CB  1 
ATOM   7963  C  CG  . ARG   A 1 996  ? -37.91400  75.40300  7.52700   1.000 37.14921  ?  994  ARG   A CG  1 
ATOM   7964  C  CD  . ARG   A 1 996  ? -38.71600  76.46100  6.79800   1.000 44.41341  ?  994  ARG   A CD  1 
ATOM   7965  N  NE  . ARG   A 1 996  ? -38.26300  77.80800  7.12300   1.000 47.15967  ?  994  ARG   A NE  1 
ATOM   7966  C  CZ  . ARG   A 1 996  ? -38.95700  78.90900  6.86900   1.000 49.04962  ?  994  ARG   A CZ  1 
ATOM   7967  N  NH1 . ARG   A 1 996  ? -40.14000  78.85800  6.27800   1.000 35.41677  ?  994  ARG   A NH1 1 
ATOM   7968  N  NH2 . ARG   A 1 996  ? -38.45200  80.08900  7.21800   1.000 43.94803  ?  994  ARG   A NH2 1 
ATOM   7969  N  N   . VAL   A 1 997  ? -36.97600  74.36300  4.38600   1.000 34.89718  ?  995  VAL   A N   1 
ATOM   7970  C  CA  . VAL   A 1 997  ? -35.71500  74.85900  3.85100   1.000 36.31301  ?  995  VAL   A CA  1 
ATOM   7971  C  C   . VAL   A 1 997  ? -35.48900  76.25500  4.42100   1.000 44.23466  ?  995  VAL   A C   1 
ATOM   7972  O  O   . VAL   A 1 997  ? -36.33000  77.14600  4.25300   1.000 32.88088  ?  995  VAL   A O   1 
ATOM   7973  C  CB  . VAL   A 1 997  ? -35.72700  74.87300  2.31500   1.000 24.14349  ?  995  VAL   A CB  1 
ATOM   7974  C  CG1 . VAL   A 1 997  ? -34.32600  75.08700  1.77200   1.000 32.25697  ?  995  VAL   A CG1 1 
ATOM   7975  C  CG2 . VAL   A 1 997  ? -36.30200  73.56900  1.78200   1.000 25.86898  ?  995  VAL   A CG2 1 
ATOM   7976  N  N   . ASN   A 1 998  ? -34.35900  76.44200  5.10600   1.000 37.57757  ?  996  ASN   A N   1 
ATOM   7977  C  CA  . ASN   A 1 998  ? -34.09200  77.68300  5.81700   1.000 30.93683  ?  996  ASN   A CA  1 
ATOM   7978  C  C   . ASN   A 1 998  ? -33.91500  78.84600  4.83900   1.000 36.19085  ?  996  ASN   A C   1 
ATOM   7979  O  O   . ASN   A 1 998  ? -33.69900  78.63800  3.64200   1.000 41.06470  ?  996  ASN   A O   1 
ATOM   7980  C  CB  . ASN   A 1 998  ? -32.84900  77.53200  6.69700   1.000 30.82400  ?  996  ASN   A CB  1 
ATOM   7981  C  CG  . ASN   A 1 998  ? -31.63000  77.08800  5.91800   1.000 37.51745  ?  996  ASN   A CG  1 
ATOM   7982  O  OD1 . ASN   A 1 998  ? -31.03100  77.87000  5.17900   1.000 40.27757  ?  996  ASN   A OD1 1 
ATOM   7983  N  ND2 . ASN   A 1 998  ? -31.25300  75.82400  6.08000   1.000 50.45303  ?  996  ASN   A ND2 1 
ATOM   7984  N  N   . PRO   A 1 999  ? -34.02300  80.08800  5.32800   1.000 34.25557  ?  997  PRO   A N   1 
ATOM   7985  C  CA  . PRO   A 1 999  ? -33.86100  81.24400  4.42900   1.000 35.42688  ?  997  PRO   A CA  1 
ATOM   7986  C  C   . PRO   A 1 999  ? -32.51800  81.29800  3.71900   1.000 39.98969  ?  997  PRO   A C   1 
ATOM   7987  O  O   . PRO   A 1 999  ? -32.45300  81.78400  2.58300   1.000 35.53077  ?  997  PRO   A O   1 
ATOM   7988  C  CB  . PRO   A 1 999  ? -34.04300  82.44100  5.37200   1.000 35.29152  ?  997  PRO   A CB  1 
ATOM   7989  C  CG  . PRO   A 1 999  ? -34.91400  81.92700  6.46000   1.000 39.74030  ?  997  PRO   A CG  1 
ATOM   7990  C  CD  . PRO   A 1 999  ? -34.52200  80.49000  6.65600   1.000 41.80951  ?  997  PRO   A CD  1 
ATOM   7991  N  N   . GLU   A 1 1000 ? -31.44200  80.82000  4.35000   1.000 38.38866  ?  998  GLU   A N   1 
ATOM   7992  C  CA  . GLU   A 1 1000 ? -30.13300  80.86700  3.70500   1.000 36.53597  ?  998  GLU   A CA  1 
ATOM   7993  C  C   . GLU   A 1 1000 ? -30.09500  79.97100  2.47000   1.000 37.52757  ?  998  GLU   A C   1 
ATOM   7994  O  O   . GLU   A 1 1000 ? -29.68700  80.40800  1.38700   1.000 32.50120  ?  998  GLU   A O   1 
ATOM   7995  C  CB  . GLU   A 1 1000 ? -29.03900  80.46700  4.69500   1.000 44.94412  ?  998  GLU   A CB  1 
ATOM   7996  C  CG  . GLU   A 1 1000 ? -27.63200  80.80000  4.21200   1.000 70.95822  ?  998  GLU   A CG  1 
ATOM   7997  C  CD  . GLU   A 1 1000 ? -26.57700  79.85700  4.76200   1.000 80.08946  ?  998  GLU   A CD  1 
ATOM   7998  O  OE1 . GLU   A 1 1000 ? -26.90000  79.05700  5.66600   1.000 87.46134  ?  998  GLU   A OE1 1 
ATOM   7999  O  OE2 . GLU   A 1 1000 ? -25.42300  79.91300  4.28500   1.000 82.59425  -1 998  GLU   A OE2 1 
ATOM   8000  N  N   . ILE   A 1 1001 ? -30.51900  78.71200  2.61100   1.000 31.43823  ?  999  ILE   A N   1 
ATOM   8001  C  CA  . ILE   A 1 1001 ? -30.53600  77.80700  1.46500   1.000 32.50914  ?  999  ILE   A CA  1 
ATOM   8002  C  C   . ILE   A 1 1001 ? -31.54700  78.28000  0.42900   1.000 35.57255  ?  999  ILE   A C   1 
ATOM   8003  O  O   . ILE   A 1 1001 ? -31.28800  78.22600  -0.78000  1.000 35.84124  ?  999  ILE   A O   1 
ATOM   8004  C  CB  . ILE   A 1 1001 ? -30.82500  76.36500  1.91900   1.000 34.34818  ?  999  ILE   A CB  1 
ATOM   8005  C  CG1 . ILE   A 1 1001 ? -29.75400  75.88600  2.90100   1.000 35.23700  ?  999  ILE   A CG1 1 
ATOM   8006  C  CG2 . ILE   A 1 1001 ? -30.88500  75.42900  0.72100   1.000 27.81740  ?  999  ILE   A CG2 1 
ATOM   8007  C  CD1 . ILE   A 1 1001 ? -28.34900  75.87900  2.32100   1.000 50.09892  ?  999  ILE   A CD1 1 
ATOM   8008  N  N   . THR   A 1 1002 ? -32.71000  78.75200  0.88500   1.000 34.89349  ?  1000 THR   A N   1 
ATOM   8009  C  CA  . THR   A 1 1002 ? -33.70500  79.29100  -0.03600  1.000 34.88064  ?  1000 THR   A CA  1 
ATOM   8010  C  C   . THR   A 1 1002 ? -33.11500  80.40300  -0.89300  1.000 41.12501  ?  1000 THR   A C   1 
ATOM   8011  O  O   . THR   A 1 1002 ? -33.38500  80.47800  -2.09800  1.000 34.92105  ?  1000 THR   A O   1 
ATOM   8012  C  CB  . THR   A 1 1002 ? -34.91500  79.81000  0.73700   1.000 32.40120  ?  1000 THR   A CB  1 
ATOM   8013  O  OG1 . THR   A 1 1002 ? -35.35500  78.81600  1.67100   1.000 29.56833  ?  1000 THR   A OG1 1 
ATOM   8014  C  CG2 . THR   A 1 1002 ? -36.04400  80.13200  -0.22300  1.000 26.04802  ?  1000 THR   A CG2 1 
ATOM   8015  N  N   . ARG   A 1 1003 ? -32.29700  81.27200  -0.29200  1.000 33.53857  ?  1001 ARG   A N   1 
ATOM   8016  C  CA  . ARG   A 1 1003 ? -31.68000  82.34900  -1.05800  1.000 40.82188  ?  1001 ARG   A CA  1 
ATOM   8017  C  C   . ARG   A 1 1003 ? -30.72500  81.80100  -2.11000  1.000 44.95910  ?  1001 ARG   A C   1 
ATOM   8018  O  O   . ARG   A 1 1003 ? -30.69800  82.28800  -3.24700  1.000 44.72356  ?  1001 ARG   A O   1 
ATOM   8019  C  CB  . ARG   A 1 1003 ? -30.95500  83.31200  -0.12000  1.000 44.28520  ?  1001 ARG   A CB  1 
ATOM   8020  C  CG  . ARG   A 1 1003 ? -31.84000  84.41900  0.42100   1.000 46.35783  ?  1001 ARG   A CG  1 
ATOM   8021  C  CD  . ARG   A 1 1003 ? -31.08600  85.29900  1.39500   1.000 53.88264  ?  1001 ARG   A CD  1 
ATOM   8022  N  NE  . ARG   A 1 1003 ? -31.90300  85.66200  2.54600   1.000 52.73721  ?  1001 ARG   A NE  1 
ATOM   8023  C  CZ  . ARG   A 1 1003 ? -31.41200  86.05000  3.71400   1.000 57.57273  ?  1001 ARG   A CZ  1 
ATOM   8024  N  NH1 . ARG   A 1 1003 ? -30.10800  86.13200  3.92000   1.000 56.18123  ?  1001 ARG   A NH1 1 
ATOM   8025  N  NH2 . ARG   A 1 1003 ? -32.25000  86.36100  4.69900   1.000 65.85694  ?  1001 ARG   A NH2 1 
ATOM   8026  N  N   . LYS   A 1 1004 ? -29.93800  80.78200  -1.75200  1.000 44.53371  ?  1002 LYS   A N   1 
ATOM   8027  C  CA  . LYS   A 1 1004 ? -29.02000  80.18600  -2.71700  1.000 43.62069  ?  1002 LYS   A CA  1 
ATOM   8028  C  C   . LYS   A 1 1004 ? -29.76500  79.44300  -3.81700  1.000 42.28819  ?  1002 LYS   A C   1 
ATOM   8029  O  O   . LYS   A 1 1004 ? -29.28200  79.37800  -4.95400  1.000 38.66801  ?  1002 LYS   A O   1 
ATOM   8030  C  CB  . LYS   A 1 1004 ? -28.04500  79.24400  -2.00800  1.000 50.16523  ?  1002 LYS   A CB  1 
ATOM   8031  C  CG  . LYS   A 1 1004 ? -26.79600  78.92600  -2.81700  1.000 43.15549  ?  1002 LYS   A CG  1 
ATOM   8032  C  CD  . LYS   A 1 1004 ? -25.94400  77.86400  -2.14100  1.000 42.35992  ?  1002 LYS   A CD  1 
ATOM   8033  C  CE  . LYS   A 1 1004 ? -24.55900  77.79100  -2.76700  1.000 52.04139  ?  1002 LYS   A CE  1 
ATOM   8034  N  NZ  . LYS   A 1 1004 ? -24.48100  78.54800  -4.04900  1.000 58.82115  ?  1002 LYS   A NZ  1 
ATOM   8035  N  N   . LEU   A 1 1005 ? -30.93500  78.88100  -3.50500  1.000 28.59018  ?  1003 LEU   A N   1 
ATOM   8036  C  CA  . LEU   A 1 1005 ? -31.72600  78.20700  -4.52900  1.000 29.16637  ?  1003 LEU   A CA  1 
ATOM   8037  C  C   . LEU   A 1 1005 ? -32.22100  79.19700  -5.57800  1.000 35.51046  ?  1003 LEU   A C   1 
ATOM   8038  O  O   . LEU   A 1 1005 ? -32.06700  78.96600  -6.78400  1.000 35.18715  ?  1003 LEU   A O   1 
ATOM   8039  C  CB  . LEU   A 1 1005 ? -32.90200  77.47200  -3.88500  1.000 30.74178  ?  1003 LEU   A CB  1 
ATOM   8040  C  CG  . LEU   A 1 1005 ? -32.58200  76.27500  -2.98700  1.000 35.57012  ?  1003 LEU   A CG  1 
ATOM   8041  C  CD1 . LEU   A 1 1005 ? -33.81100  75.87900  -2.18500  1.000 32.87194  ?  1003 LEU   A CD1 1 
ATOM   8042  C  CD2 . LEU   A 1 1005 ? -32.06900  75.09500  -3.79900  1.000 20.36517  ?  1003 LEU   A CD2 1 
ATOM   8043  N  N   . LYS   A 1 1006 ? -32.81100  80.31200  -5.13500  1.000 28.80172  ?  1004 LYS   A N   1 
ATOM   8044  C  CA  . LYS   A 1 1006 ? -33.36700  81.28500  -6.07200  1.000 33.77951  ?  1004 LYS   A CA  1 
ATOM   8045  C  C   . LYS   A 1 1006 ? -32.27000  81.97300  -6.87300  1.000 35.77011  ?  1004 LYS   A C   1 
ATOM   8046  O  O   . LYS   A 1 1006 ? -32.38700  82.13100  -8.09500  1.000 37.87614  ?  1004 LYS   A O   1 
ATOM   8047  C  CB  . LYS   A 1 1006 ? -34.21200  82.31800  -5.32500  1.000 44.63493  ?  1004 LYS   A CB  1 
ATOM   8048  C  CG  . LYS   A 1 1006 ? -35.15100  81.72100  -4.29700  1.000 39.61786  ?  1004 LYS   A CG  1 
ATOM   8049  C  CD  . LYS   A 1 1006 ? -36.54400  82.32300  -4.38100  1.000 55.52654  ?  1004 LYS   A CD  1 
ATOM   8050  C  CE  . LYS   A 1 1006 ? -36.71500  83.47100  -3.40100  1.000 59.67875  ?  1004 LYS   A CE  1 
ATOM   8051  N  NZ  . LYS   A 1 1006 ? -38.15200  83.82400  -3.23500  1.000 60.93048  ?  1004 LYS   A NZ  1 
ATOM   8052  N  N   . ALA   A 1 1007 ? -31.20000  82.40000  -6.19800  1.000 36.12733  ?  1005 ALA   A N   1 
ATOM   8053  C  CA  . ALA   A 1 1007 ? -30.09200  83.04500  -6.89400  1.000 37.28746  ?  1005 ALA   A CA  1 
ATOM   8054  C  C   . ALA   A 1 1007 ? -29.50900  82.13200  -7.96400  1.000 41.28642  ?  1005 ALA   A C   1 
ATOM   8055  O  O   . ALA   A 1 1007 ? -29.21400  82.57700  -9.08000  1.000 50.67943  ?  1005 ALA   A O   1 
ATOM   8056  C  CB  . ALA   A 1 1007 ? -29.01400  83.45400  -5.89100  1.000 38.27058  ?  1005 ALA   A CB  1 
ATOM   8057  N  N   . THR   A 1 1008 ? -29.34100  80.84900  -7.64200  1.000 30.38483  ?  1006 THR   A N   1 
ATOM   8058  C  CA  . THR   A 1 1008 ? -28.82600  79.89800  -8.62000  1.000 35.60298  ?  1006 THR   A CA  1 
ATOM   8059  C  C   . THR   A 1 1008 ? -29.74100  79.81100  -9.83700  1.000 39.54768  ?  1006 THR   A C   1 
ATOM   8060  O  O   . THR   A 1 1008 ? -29.27500  79.83700  -10.98200 1.000 41.55387  ?  1006 THR   A O   1 
ATOM   8061  C  CB  . THR   A 1 1008 ? -28.66300  78.52400  -7.96900  1.000 42.37899  ?  1006 THR   A CB  1 
ATOM   8062  O  OG1 . THR   A 1 1008 ? -27.51300  78.53200  -7.11400  1.000 38.15950  ?  1006 THR   A OG1 1 
ATOM   8063  C  CG2 . THR   A 1 1008 ? -28.50900  77.44500  -9.02500  1.000 29.04234  ?  1006 THR   A CG2 1 
ATOM   8064  N  N   . ALA   A 1 1009 ? -31.05300  79.71900  -9.60400  1.000 31.58008  ?  1007 ALA   A N   1 
ATOM   8065  C  CA  . ALA   A 1 1009 ? -31.99600  79.55300  -10.70600 1.000 37.96540  ?  1007 ALA   A CA  1 
ATOM   8066  C  C   . ALA   A 1 1009 ? -31.97800  80.75900  -11.63800 1.000 36.36120  ?  1007 ALA   A C   1 
ATOM   8067  O  O   . ALA   A 1 1009 ? -31.90500  80.61100  -12.86400 1.000 31.77407  ?  1007 ALA   A O   1 
ATOM   8068  C  CB  . ALA   A 1 1009 ? -33.40200  79.31600  -10.15700 1.000 32.93095  ?  1007 ALA   A CB  1 
ATOM   8069  N  N   . ALA   A 1 1010 ? -32.04700  81.96700  -11.07200 1.000 34.71983  ?  1008 ALA   A N   1 
ATOM   8070  C  CA  . ALA   A 1 1010 ? -32.07500  83.16800  -11.90200 1.000 34.85687  ?  1008 ALA   A CA  1 
ATOM   8071  C  C   . ALA   A 1 1010 ? -30.76800  83.34800  -12.66200 1.000 45.11391  ?  1008 ALA   A C   1 
ATOM   8072  O  O   . ALA   A 1 1010 ? -30.77300  83.78500  -13.81900 1.000 51.20097  ?  1008 ALA   A O   1 
ATOM   8073  C  CB  . ALA   A 1 1010 ? -32.36400  84.39700  -11.04100 1.000 35.47028  ?  1008 ALA   A CB  1 
ATOM   8074  N  N   . LYS   A 1 1011 ? -29.64000  83.01700  -12.02800 1.000 49.09532  ?  1009 LYS   A N   1 
ATOM   8075  C  CA  . LYS   A 1 1011 ? -28.34600  83.19100  -12.67900 1.000 44.48587  ?  1009 LYS   A CA  1 
ATOM   8076  C  C   . LYS   A 1 1011 ? -28.23000  82.33700  -13.93400 1.000 37.08927  ?  1009 LYS   A C   1 
ATOM   8077  O  O   . LYS   A 1 1011 ? -27.49800  82.69500  -14.86400 1.000 56.44351  ?  1009 LYS   A O   1 
ATOM   8078  C  CB  . LYS   A 1 1011 ? -27.22100  82.85800  -11.69900 1.000 33.85463  ?  1009 LYS   A CB  1 
ATOM   8079  C  CG  . LYS   A 1 1011 ? -26.25300  84.01000  -11.44400 1.000 71.79208  ?  1009 LYS   A CG  1 
ATOM   8080  C  CD  . LYS   A 1 1011 ? -26.97200  85.35600  -11.38000 1.000 46.75176  ?  1009 LYS   A CD  1 
ATOM   8081  C  CE  . LYS   A 1 1011 ? -25.98100  86.51500  -11.38000 1.000 53.79901  ?  1009 LYS   A CE  1 
ATOM   8082  N  NZ  . LYS   A 1 1011 ? -26.55000  87.76200  -10.79500 1.000 63.32856  ?  1009 LYS   A NZ  1 
ATOM   8083  N  N   . HIS   A 1 1012 ? -28.95000  81.21800  -13.98400 1.000 36.64323  ?  1010 HIS   A N   1 
ATOM   8084  C  CA  . HIS   A 1 1012 ? -28.92700  80.31000  -15.12100 1.000 40.84176  ?  1010 HIS   A CA  1 
ATOM   8085  C  C   . HIS   A 1 1012 ? -30.24100  80.34000  -15.89700 1.000 40.22240  ?  1010 HIS   A C   1 
ATOM   8086  O  O   . HIS   A 1 1012 ? -30.60900  79.35800  -16.54800 1.000 41.66421  ?  1010 HIS   A O   1 
ATOM   8087  C  CB  . HIS   A 1 1012 ? -28.59300  78.89200  -14.65700 1.000 26.15417  ?  1010 HIS   A CB  1 
ATOM   8088  C  CG  . HIS   A 1 1012 ? -27.23600  78.76900  -14.03200 1.000 40.67613  ?  1010 HIS   A CG  1 
ATOM   8089  N  ND1 . HIS   A 1 1012 ? -26.97500  79.15200  -12.73400 1.000 53.20103  ?  1010 HIS   A ND1 1 
ATOM   8090  C  CD2 . HIS   A 1 1012 ? -26.06100  78.32400  -14.53500 1.000 40.03373  ?  1010 HIS   A CD2 1 
ATOM   8091  C  CE1 . HIS   A 1 1012 ? -25.70000  78.93900  -12.46100 1.000 35.86318  ?  1010 HIS   A CE1 1 
ATOM   8092  N  NE2 . HIS   A 1 1012 ? -25.12300  78.43700  -13.53800 1.000 34.20806  ?  1010 HIS   A NE2 1 
ATOM   8093  N  N   . ASP   A 1 1013 ? -30.95200  81.46800  -15.83500 1.000 35.01001  ?  1011 ASP   A N   1 
ATOM   8094  C  CA  . ASP   A 1 1013 ? -32.17400  81.68400  -16.61200 1.000 41.29306  ?  1011 ASP   A CA  1 
ATOM   8095  C  C   . ASP   A 1 1013 ? -33.22300  80.61700  -16.29900 1.000 35.33290  ?  1011 ASP   A C   1 
ATOM   8096  O  O   . ASP   A 1 1013 ? -33.82100  80.01600  -17.19500 1.000 37.34992  ?  1011 ASP   A O   1 
ATOM   8097  C  CB  . ASP   A 1 1013 ? -31.86700  81.73700  -18.11300 1.000 40.58348  ?  1011 ASP   A CB  1 
ATOM   8098  C  CG  . ASP   A 1 1013 ? -31.02100  82.94100  -18.49800 1.000 45.66198  ?  1011 ASP   A CG  1 
ATOM   8099  O  OD1 . ASP   A 1 1013 ? -30.97500  83.91700  -17.72000 1.000 45.82792  ?  1011 ASP   A OD1 1 
ATOM   8100  O  OD2 . ASP   A 1 1013 ? -30.39800  82.91000  -19.58200 1.000 55.35154  -1 1011 ASP   A OD2 1 
ATOM   8101  N  N   . LEU   A 1 1014 ? -33.43900  80.38100  -15.00600 1.000 34.60998  ?  1012 LEU   A N   1 
ATOM   8102  C  CA  . LEU   A 1 1014 ? -34.42600  79.41600  -14.54300 1.000 39.24110  ?  1012 LEU   A CA  1 
ATOM   8103  C  C   . LEU   A 1 1014 ? -35.23600  80.02600  -13.40800 1.000 32.65978  ?  1012 LEU   A C   1 
ATOM   8104  O  O   . LEU   A 1 1014 ? -34.78700  80.94300  -12.71700 1.000 32.79645  ?  1012 LEU   A O   1 
ATOM   8105  C  CB  . LEU   A 1 1014 ? -33.77400  78.11200  -14.06200 1.000 33.40632  ?  1012 LEU   A CB  1 
ATOM   8106  C  CG  . LEU   A 1 1014 ? -32.86500  77.35700  -15.03100 1.000 33.85767  ?  1012 LEU   A CG  1 
ATOM   8107  C  CD1 . LEU   A 1 1014 ? -31.68500  76.78100  -14.27500 1.000 43.54931  ?  1012 LEU   A CD1 1 
ATOM   8108  C  CD2 . LEU   A 1 1014 ? -33.61700  76.25500  -15.76100 1.000 38.57427  ?  1012 LEU   A CD2 1 
ATOM   8109  N  N   . THR   A 1 1015 ? -36.44200  79.50100  -13.22400 1.000 28.65953  ?  1013 THR   A N   1 
ATOM   8110  C  CA  . THR   A 1 1015 ? -37.27000  79.87600  -12.09000 1.000 26.17153  ?  1013 THR   A CA  1 
ATOM   8111  C  C   . THR   A 1 1015 ? -37.04400  78.89400  -10.94400 1.000 31.39203  ?  1013 THR   A C   1 
ATOM   8112  O  O   . THR   A 1 1015 ? -36.47900  77.81300  -11.12200 1.000 38.97045  ?  1013 THR   A O   1 
ATOM   8113  C  CB  . THR   A 1 1015 ? -38.75100  79.91200  -12.48000 1.000 41.21998  ?  1013 THR   A CB  1 
ATOM   8114  O  OG1 . THR   A 1 1015 ? -39.24700  78.57600  -12.63400 1.000 34.95426  ?  1013 THR   A OG1 1 
ATOM   8115  C  CG2 . THR   A 1 1015 ? -38.94500  80.67100  -13.78700 1.000 34.06939  ?  1013 THR   A CG2 1 
ATOM   8116  N  N   . LEU   A 1 1016 ? -37.48600  79.28600  -9.74800  1.000 32.59097  ?  1014 LEU   A N   1 
ATOM   8117  C  CA  . LEU   A 1 1016 ? -37.36500  78.38200  -8.61000  1.000 32.67633  ?  1014 LEU   A CA  1 
ATOM   8118  C  C   . LEU   A 1 1016 ? -38.15500  77.10000  -8.83500  1.000 39.15082  ?  1014 LEU   A C   1 
ATOM   8119  O  O   . LEU   A 1 1016 ? -37.72700  76.02300  -8.40400  1.000 40.14033  ?  1014 LEU   A O   1 
ATOM   8120  C  CB  . LEU   A 1 1016 ? -37.83200  79.07200  -7.32800  1.000 25.28074  ?  1014 LEU   A CB  1 
ATOM   8121  C  CG  . LEU   A 1 1016 ? -37.46700  78.31500  -6.05200  1.000 37.03581  ?  1014 LEU   A CG  1 
ATOM   8122  C  CD1 . LEU   A 1 1016 ? -35.96600  78.09300  -5.99700  1.000 27.67169  ?  1014 LEU   A CD1 1 
ATOM   8123  C  CD2 . LEU   A 1 1016 ? -37.94800  79.05900  -4.82000  1.000 37.58696  ?  1014 LEU   A CD2 1 
ATOM   8124  N  N   . TYR   A 1 1017 ? -39.30300  77.19400  -9.50900  1.000 29.92058  ?  1015 TYR   A N   1 
ATOM   8125  C  CA  . TYR   A 1 1017 ? -40.06900  75.99600  -9.82700  1.000 30.33150  ?  1015 TYR   A CA  1 
ATOM   8126  C  C   . TYR   A 1 1017 ? -39.27400  75.06100  -10.73200 1.000 37.21942  ?  1015 TYR   A C   1 
ATOM   8127  O  O   . TYR   A 1 1017 ? -39.25500  73.84400  -10.51400 1.000 41.00783  ?  1015 TYR   A O   1 
ATOM   8128  C  CB  . TYR   A 1 1017 ? -41.39600  76.38700  -10.47600 1.000 27.25596  ?  1015 TYR   A CB  1 
ATOM   8129  C  CG  . TYR   A 1 1017 ? -42.18800  75.22700  -11.03900 1.000 27.16423  ?  1015 TYR   A CG  1 
ATOM   8130  C  CD1 . TYR   A 1 1017 ? -43.04900  74.49200  -10.23500 1.000 24.84885  ?  1015 TYR   A CD1 1 
ATOM   8131  C  CD2 . TYR   A 1 1017 ? -42.08000  74.87400  -12.38000 1.000 24.55754  ?  1015 TYR   A CD2 1 
ATOM   8132  C  CE1 . TYR   A 1 1017 ? -43.77900  73.43700  -10.74800 1.000 32.78393  ?  1015 TYR   A CE1 1 
ATOM   8133  C  CE2 . TYR   A 1 1017 ? -42.80300  73.81900  -12.90200 1.000 28.41228  ?  1015 TYR   A CE2 1 
ATOM   8134  C  CZ  . TYR   A 1 1017 ? -43.65100  73.10500  -12.08000 1.000 33.90010  ?  1015 TYR   A CZ  1 
ATOM   8135  O  OH  . TYR   A 1 1017 ? -44.37600  72.05400  -12.58900 1.000 35.96084  ?  1015 TYR   A OH  1 
ATOM   8136  N  N   . MET   A 1 1018 ? -38.61400  75.61000  -11.75600 1.000 31.56353  ?  1016 MET   A N   1 
ATOM   8137  C  CA  . MET   A 1 1018 ? -37.78700  74.77900  -12.62500 1.000 33.73566  ?  1016 MET   A CA  1 
ATOM   8138  C  C   . MET   A 1 1018 ? -36.69000  74.08000  -11.83300 1.000 40.17339  ?  1016 MET   A C   1 
ATOM   8139  O  O   . MET   A 1 1018 ? -36.43300  72.88700  -12.03200 1.000 38.92897  ?  1016 MET   A O   1 
ATOM   8140  C  CB  . MET   A 1 1018 ? -37.17700  75.62500  -13.74300 1.000 30.66230  ?  1016 MET   A CB  1 
ATOM   8141  C  CG  . MET   A 1 1018 ? -38.16700  76.08800  -14.79000 1.000 29.88013  ?  1016 MET   A CG  1 
ATOM   8142  S  SD  . MET   A 1 1018 ? -37.51400  77.46400  -15.75000 1.000 51.73446  ?  1016 MET   A SD  1 
ATOM   8143  C  CE  . MET   A 1 1018 ? -38.89800  77.79800  -16.83300 1.000 40.28936  ?  1016 MET   A CE  1 
ATOM   8144  N  N   . LEU   A 1 1019 ? -36.04000  74.80600  -10.92000 1.000 30.50440  ?  1017 LEU   A N   1 
ATOM   8145  C  CA  . LEU   A 1 1019 ? -34.97000  74.21100  -10.12900 1.000 28.40854  ?  1017 LEU   A CA  1 
ATOM   8146  C  C   . LEU   A 1 1019 ? -35.50400  73.12900  -9.19900  1.000 30.46988  ?  1017 LEU   A C   1 
ATOM   8147  O  O   . LEU   A 1 1019 ? -34.87700  72.07400  -9.04100  1.000 34.98059  ?  1017 LEU   A O   1 
ATOM   8148  C  CB  . LEU   A 1 1019 ? -34.24700  75.29800  -9.33800  1.000 31.49709  ?  1017 LEU   A CB  1 
ATOM   8149  C  CG  . LEU   A 1 1019 ? -32.91300  74.91700  -8.70200  1.000 28.94209  ?  1017 LEU   A CG  1 
ATOM   8150  C  CD1 . LEU   A 1 1019 ? -31.88000  76.00300  -8.95400  1.000 30.55467  ?  1017 LEU   A CD1 1 
ATOM   8151  C  CD2 . LEU   A 1 1019 ? -33.10100  74.68600  -7.21600  1.000 29.76506  ?  1017 LEU   A CD2 1 
ATOM   8152  N  N   . MET   A 1 1020 ? -36.66000  73.36900  -8.57900  1.000 34.94758  ?  1018 MET   A N   1 
ATOM   8153  C  CA  . MET   A 1 1020 ? -37.24100  72.36800  -7.69100  1.000 35.02217  ?  1018 MET   A CA  1 
ATOM   8154  C  C   . MET   A 1 1020 ? -37.71300  71.14800  -8.47200  1.000 31.40585  ?  1018 MET   A C   1 
ATOM   8155  O  O   . MET   A 1 1020 ? -37.52000  70.00900  -8.03100  1.000 37.95230  ?  1018 MET   A O   1 
ATOM   8156  C  CB  . MET   A 1 1020 ? -38.39600  72.97700  -6.89300  1.000 37.29251  ?  1018 MET   A CB  1 
ATOM   8157  C  CG  . MET   A 1 1020 ? -37.97700  73.94400  -5.78900  1.000 23.96572  ?  1018 MET   A CG  1 
ATOM   8158  S  SD  . MET   A 1 1020 ? -36.44100  73.44300  -4.99900  1.000 41.31337  ?  1018 MET   A SD  1 
ATOM   8159  C  CE  . MET   A 1 1020 ? -36.90800  73.47400  -3.27300  1.000 28.48586  ?  1018 MET   A CE  1 
ATOM   8160  N  N   . LEU   A 1 1021 ? -38.32900  71.36800  -9.63700  1.000 29.23428  ?  1019 LEU   A N   1 
ATOM   8161  C  CA  . LEU   A 1 1021 ? -38.80300  70.25500  -10.45300 1.000 32.63747  ?  1019 LEU   A CA  1 
ATOM   8162  C  C   . LEU   A 1 1021 ? -37.65700  69.33100  -10.84600 1.000 41.33296  ?  1019 LEU   A C   1 
ATOM   8163  O  O   . LEU   A 1 1021 ? -37.82600  68.10700  -10.90000 1.000 42.48614  ?  1019 LEU   A O   1 
ATOM   8164  C  CB  . LEU   A 1 1021 ? -39.51700  70.79100  -11.69500 1.000 27.13042  ?  1019 LEU   A CB  1 
ATOM   8165  C  CG  . LEU   A 1 1021 ? -40.19900  69.78800  -12.62500 1.000 26.19693  ?  1019 LEU   A CG  1 
ATOM   8166  C  CD1 . LEU   A 1 1021 ? -41.33400  69.06700  -11.91100 1.000 34.41690  ?  1019 LEU   A CD1 1 
ATOM   8167  C  CD2 . LEU   A 1 1021 ? -40.71300  70.49900  -13.86500 1.000 31.21332  ?  1019 LEU   A CD2 1 
ATOM   8168  N  N   . THR   A 1 1022 ? -36.47900  69.89900  -11.11300 1.000 38.34659  ?  1020 THR   A N   1 
ATOM   8169  C  CA  . THR   A 1 1022 ? -35.32300  69.08000  -11.46500 1.000 31.45307  ?  1020 THR   A CA  1 
ATOM   8170  C  C   . THR   A 1 1022 ? -34.89300  68.20700  -10.29400 1.000 37.02272  ?  1020 THR   A C   1 
ATOM   8171  O  O   . THR   A 1 1022 ? -34.65400  67.00400  -10.45700 1.000 47.46077  ?  1020 THR   A O   1 
ATOM   8172  C  CB  . THR   A 1 1022 ? -34.16900  69.97100  -11.92100 1.000 38.45376  ?  1020 THR   A CB  1 
ATOM   8173  O  OG1 . THR   A 1 1022 ? -34.63900  70.88900  -12.91600 1.000 42.32945  ?  1020 THR   A OG1 1 
ATOM   8174  C  CG2 . THR   A 1 1022 ? -33.04700  69.13000  -12.50400 1.000 36.87786  ?  1020 THR   A CG2 1 
ATOM   8175  N  N   . ILE   A 1 1023 ? -34.79000  68.79900  -9.10200  1.000 36.55375  ?  1021 ILE   A N   1 
ATOM   8176  C  CA  . ILE   A 1 1023 ? -34.40500  68.03600  -7.91800  1.000 31.52807  ?  1021 ILE   A CA  1 
ATOM   8177  C  C   . ILE   A 1 1023 ? -35.42100  66.93500  -7.64100  1.000 38.96999  ?  1021 ILE   A C   1 
ATOM   8178  O  O   . ILE   A 1 1023 ? -35.05500  65.79000  -7.35000  1.000 37.70268  ?  1021 ILE   A O   1 
ATOM   8179  C  CB  . ILE   A 1 1023 ? -34.24300  68.97800  -6.71100  1.000 30.40858  ?  1021 ILE   A CB  1 
ATOM   8180  C  CG1 . ILE   A 1 1023 ? -33.14600  70.01300  -6.98200  1.000 29.93617  ?  1021 ILE   A CG1 1 
ATOM   8181  C  CG2 . ILE   A 1 1023 ? -33.93400  68.18200  -5.45700  1.000 37.05571  ?  1021 ILE   A CG2 1 
ATOM   8182  C  CD1 . ILE   A 1 1023 ? -32.96300  71.02200  -5.86100  1.000 17.98181  ?  1021 ILE   A CD1 1 
ATOM   8183  N  N   . VAL   A 1 1024 ? -36.71100  67.26300  -7.73900  1.000 39.47178  ?  1022 VAL   A N   1 
ATOM   8184  C  CA  . VAL   A 1 1024 ? -37.75600  66.25900  -7.55900  1.000 36.37874  ?  1022 VAL   A CA  1 
ATOM   8185  C  C   . VAL   A 1 1024 ? -37.62500  65.15400  -8.59900  1.000 43.51133  ?  1022 VAL   A C   1 
ATOM   8186  O  O   . VAL   A 1 1024 ? -37.78700  63.96600  -8.29100  1.000 49.38197  ?  1022 VAL   A O   1 
ATOM   8187  C  CB  . VAL   A 1 1024 ? -39.14200  66.92400  -7.61500  1.000 35.81700  ?  1022 VAL   A CB  1 
ATOM   8188  C  CG1 . VAL   A 1 1024 ? -40.23000  65.87500  -7.78900  1.000 21.45139  ?  1022 VAL   A CG1 1 
ATOM   8189  C  CG2 . VAL   A 1 1024 ? -39.37200  67.75600  -6.36500  1.000 33.45902  ?  1022 VAL   A CG2 1 
ATOM   8190  N  N   . SER   A 1 1025 ? -37.32700  65.52500  -9.84600  1.000 30.13018  ?  1023 SER   A N   1 
ATOM   8191  C  CA  . SER   A 1 1025 ? -37.18500  64.52500  -10.89900 1.000 33.61334  ?  1023 SER   A CA  1 
ATOM   8192  C  C   . SER   A 1 1025 ? -36.00300  63.60200  -10.63300 1.000 42.68099  ?  1023 SER   A C   1 
ATOM   8193  O  O   . SER   A 1 1025 ? -36.10800  62.38300  -10.81500 1.000 41.03347  ?  1023 SER   A O   1 
ATOM   8194  C  CB  . SER   A 1 1025 ? -37.03600  65.21500  -12.25200 1.000 36.68159  ?  1023 SER   A CB  1 
ATOM   8195  O  OG  . SER   A 1 1025 ? -38.18300  65.99300  -12.53800 1.000 52.42322  ?  1023 SER   A OG  1 
ATOM   8196  N  N   . ILE   A 1 1026 ? -34.86800  64.16400  -10.21400 1.000 41.57420  ?  1024 ILE   A N   1 
ATOM   8197  C  CA  . ILE   A 1 1026 ? -33.71000  63.34000  -9.88000  1.000 46.31777  ?  1024 ILE   A CA  1 
ATOM   8198  C  C   . ILE   A 1 1026 ? -34.02900  62.44300  -8.69500  1.000 40.85147  ?  1024 ILE   A C   1 
ATOM   8199  O  O   . ILE   A 1 1026 ? -33.68300  61.25400  -8.67800  1.000 44.33740  ?  1024 ILE   A O   1 
ATOM   8200  C  CB  . ILE   A 1 1026 ? -32.48800  64.23300  -9.59700  1.000 41.45605  ?  1024 ILE   A CB  1 
ATOM   8201  C  CG1 . ILE   A 1 1026 ? -32.01700  64.91800  -10.88000 1.000 28.42388  ?  1024 ILE   A CG1 1 
ATOM   8202  C  CG2 . ILE   A 1 1026 ? -31.36900  63.42800  -8.95000  1.000 24.05173  ?  1024 ILE   A CG2 1 
ATOM   8203  C  CD1 . ILE   A 1 1026 ? -31.21200  66.16200  -10.62800 1.000 23.73715  ?  1024 ILE   A CD1 1 
ATOM   8204  N  N   . TRP   A 1 1027 ? -34.70100  63.00400  -7.68900  1.000 34.24979  ?  1025 TRP   A N   1 
ATOM   8205  C  CA  . TRP   A 1 1027 ? -35.09000  62.23800  -6.51100  1.000 29.75138  ?  1025 TRP   A CA  1 
ATOM   8206  C  C   . TRP   A 1 1027 ? -35.94400  61.03400  -6.89500  1.000 32.31803  ?  1025 TRP   A C   1 
ATOM   8207  O  O   . TRP   A 1 1027 ? -35.71600  59.91800  -6.41400  1.000 33.95829  ?  1025 TRP   A O   1 
ATOM   8208  C  CB  . TRP   A 1 1027 ? -35.82500  63.16300  -5.53900  1.000 26.06972  ?  1025 TRP   A CB  1 
ATOM   8209  C  CG  . TRP   A 1 1027 ? -36.25100  62.53100  -4.25800  1.000 37.43195  ?  1025 TRP   A CG  1 
ATOM   8210  C  CD1 . TRP   A 1 1027 ? -35.45300  61.91900  -3.33600  1.000 34.76928  ?  1025 TRP   A CD1 1 
ATOM   8211  C  CD2 . TRP   A 1 1027 ? -37.58700  62.45600  -3.74700  1.000 38.64282  ?  1025 TRP   A CD2 1 
ATOM   8212  N  NE1 . TRP   A 1 1027 ? -36.21200  61.46300  -2.28500  1.000 42.74775  ?  1025 TRP   A NE1 1 
ATOM   8213  C  CE2 . TRP   A 1 1027 ? -37.52500  61.78000  -2.51500  1.000 41.49569  ?  1025 TRP   A CE2 1 
ATOM   8214  C  CE3 . TRP   A 1 1027 ? -38.82900  62.89200  -4.21700  1.000 37.84532  ?  1025 TRP   A CE3 1 
ATOM   8215  C  CZ2 . TRP   A 1 1027 ? -38.65800  61.53100  -1.74500  1.000 38.51281  ?  1025 TRP   A CZ2 1 
ATOM   8216  C  CZ3 . TRP   A 1 1027 ? -39.95200  62.64400  -3.45000  1.000 39.74928  ?  1025 TRP   A CZ3 1 
ATOM   8217  C  CH2 . TRP   A 1 1027 ? -39.85900  61.97000  -2.22900  1.000 36.25546  ?  1025 TRP   A CH2 1 
ATOM   8218  N  N   . LEU   A 1 1028 ? -36.92200  61.23500  -7.78100  1.000 39.47606  ?  1026 LEU   A N   1 
ATOM   8219  C  CA  . LEU   A 1 1028 ? -37.75400  60.12100  -8.22700  1.000 35.25279  ?  1026 LEU   A CA  1 
ATOM   8220  C  C   . LEU   A 1 1028 ? -36.94400  59.11300  -9.02900  1.000 41.95645  ?  1026 LEU   A C   1 
ATOM   8221  O  O   . LEU   A 1 1028 ? -37.10400  57.89800  -8.85500  1.000 34.73250  ?  1026 LEU   A O   1 
ATOM   8222  C  CB  . LEU   A 1 1028 ? -38.92700  60.64200  -9.05600  1.000 30.72915  ?  1026 LEU   A CB  1 
ATOM   8223  C  CG  . LEU   A 1 1028 ? -39.99300  61.42600  -8.29300  1.000 39.87332  ?  1026 LEU   A CG  1 
ATOM   8224  C  CD1 . LEU   A 1 1028 ? -41.06300  61.91700  -9.24500  1.000 30.68072  ?  1026 LEU   A CD1 1 
ATOM   8225  C  CD2 . LEU   A 1 1028 ? -40.61000  60.57000  -7.19400  1.000 50.42522  ?  1026 LEU   A CD2 1 
ATOM   8226  N  N   . SER   A 1 1029 ? -36.06900  59.60100  -9.91200  1.000 31.40987  ?  1027 SER   A N   1 
ATOM   8227  C  CA  . SER   A 1 1029 ? -35.26300  58.70800  -10.73600 1.000 36.60034  ?  1027 SER   A CA  1 
ATOM   8228  C  C   . SER   A 1 1029 ? -34.39600  57.80100  -9.87200  1.000 40.25833  ?  1027 SER   A C   1 
ATOM   8229  O  O   . SER   A 1 1029 ? -34.35100  56.58200  -10.07700 1.000 35.62658  ?  1027 SER   A O   1 
ATOM   8230  C  CB  . SER   A 1 1029 ? -34.40300  59.53100  -11.69600 1.000 37.75953  ?  1027 SER   A CB  1 
ATOM   8231  O  OG  . SER   A 1 1029 ? -33.39100  58.74200  -12.29000 1.000 39.02178  ?  1027 SER   A OG  1 
ATOM   8232  N  N   . LYS   A 1 1030 ? -33.71800  58.37800  -8.87900  1.000 35.01156  ?  1028 LYS   A N   1 
ATOM   8233  C  CA  . LYS   A 1 1030 ? -32.82600  57.58400  -8.04200  1.000 35.54942  ?  1028 LYS   A CA  1 
ATOM   8234  C  C   . LYS   A 1 1030 ? -33.59000  56.55000  -7.22400  1.000 40.08642  ?  1028 LYS   A C   1 
ATOM   8235  O  O   . LYS   A 1 1030 ? -33.02500  55.51800  -6.84600  1.000 61.73343  ?  1028 LYS   A O   1 
ATOM   8236  C  CB  . LYS   A 1 1030 ? -32.01100  58.50500  -7.13800  1.000 34.48553  ?  1028 LYS   A CB  1 
ATOM   8237  C  CG  . LYS   A 1 1030 ? -31.04800  59.39600  -7.90900  1.000 28.18397  ?  1028 LYS   A CG  1 
ATOM   8238  C  CD  . LYS   A 1 1030 ? -30.10600  60.13200  -6.97300  1.000 44.01210  ?  1028 LYS   A CD  1 
ATOM   8239  C  CE  . LYS   A 1 1030 ? -29.01000  60.84700  -7.74500  1.000 50.92545  ?  1028 LYS   A CE  1 
ATOM   8240  N  NZ  . LYS   A 1 1030 ? -28.08300  59.88400  -8.41200  1.000 50.98873  ?  1028 LYS   A NZ  1 
ATOM   8241  N  N   . MET   A 1 1031 ? -34.87100  56.79800  -6.95000  1.000 38.90750  ?  1029 MET   A N   1 
ATOM   8242  C  CA  . MET   A 1 1031 ? -35.70300  55.78100  -6.32200  1.000 38.47766  ?  1029 MET   A CA  1 
ATOM   8243  C  C   . MET   A 1 1031 ? -36.28000  54.80400  -7.33700  1.000 43.97718  ?  1029 MET   A C   1 
ATOM   8244  O  O   . MET   A 1 1031 ? -36.61800  53.67400  -6.97000  1.000 41.84288  ?  1029 MET   A O   1 
ATOM   8245  C  CB  . MET   A 1 1031 ? -36.83000  56.43800  -5.52000  1.000 29.59042  ?  1029 MET   A CB  1 
ATOM   8246  C  CG  . MET   A 1 1031 ? -36.34400  57.38000  -4.42200  1.000 49.48306  ?  1029 MET   A CG  1 
ATOM   8247  S  SD  . MET   A 1 1031 ? -37.62000  57.81300  -3.21300  1.000 53.36519  ?  1029 MET   A SD  1 
ATOM   8248  C  CE  . MET   A 1 1031 ? -38.86200  58.53500  -4.27700  1.000 34.93683  ?  1029 MET   A CE  1 
ATOM   8249  N  N   . ASN   A 1 1032 ? -36.39200  55.21000  -8.59900  1.000 36.83011  ?  1030 ASN   A N   1 
ATOM   8250  C  CA  . ASN   A 1 1032 ? -36.80400  54.31600  -9.67800  1.000 43.97269  ?  1030 ASN   A CA  1 
ATOM   8251  C  C   . ASN   A 1 1032 ? -35.61400  53.61600  -10.31800 1.000 51.14412  ?  1030 ASN   A C   1 
ATOM   8252  O  O   . ASN   A 1 1032 ? -35.56100  53.45700  -11.54300 1.000 50.90557  ?  1030 ASN   A O   1 
ATOM   8253  C  CB  . ASN   A 1 1032 ? -37.59900  55.09900  -10.71800 1.000 47.69807  ?  1030 ASN   A CB  1 
ATOM   8254  C  CG  . ASN   A 1 1032 ? -38.48800  54.21100  -11.55800 1.000 44.73278  ?  1030 ASN   A CG  1 
ATOM   8255  O  OD1 . ASN   A 1 1032 ? -38.94600  53.16100  -11.10700 1.000 59.79391  ?  1030 ASN   A OD1 1 
ATOM   8256  N  ND2 . ASN   A 1 1032 ? -38.72000  54.61800  -12.79900 1.000 38.13156  ?  1030 ASN   A ND2 1 
ATOM   8257  N  N   . SER   A 1 1033 ? -34.64200  53.20200  -9.50300  1.000 52.90686  ?  1031 SER   A N   1 
ATOM   8258  C  CA  . SER   A 1 1033 ? -33.44800  52.49400  -9.96900  1.000 37.89809  ?  1031 SER   A CA  1 
ATOM   8259  C  C   . SER   A 1 1033 ? -32.70000  53.30500  -11.02600 1.000 46.50194  ?  1031 SER   A C   1 
ATOM   8260  O  O   . SER   A 1 1033 ? -32.33200  52.79600  -12.08700 1.000 61.82286  ?  1031 SER   A O   1 
ATOM   8261  C  CB  . SER   A 1 1033 ? -33.80500  51.10100  -10.49300 1.000 34.52703  ?  1031 SER   A CB  1 
ATOM   8262  O  OG  . SER   A 1 1033 ? -34.18700  50.24400  -9.43000  1.000 44.16765  ?  1031 SER   A OG  1 
ATOM   8263  N  N   . ASP   A 1 1034 ? -32.48400  54.58500  -10.72000 1.000 49.53906  ?  1032 ASP   A N   1 
ATOM   8264  C  CA  . ASP   A 1 1034 ? -31.72600  55.50500  -11.57200 1.000 42.67056  ?  1032 ASP   A CA  1 
ATOM   8265  C  C   . ASP   A 1 1034 ? -32.22300  55.46900  -13.01600 1.000 44.08331  ?  1032 ASP   A C   1 
ATOM   8266  O  O   . ASP   A 1 1034 ? -31.44900  55.37500  -13.97100 1.000 50.11280  ?  1032 ASP   A O   1 
ATOM   8267  C  CB  . ASP   A 1 1034 ? -30.22900  55.20900  -11.49100 1.000 37.16479  ?  1032 ASP   A CB  1 
ATOM   8268  C  CG  . ASP   A 1 1034 ? -29.67200  55.44600  -10.10300 1.000 45.98014  ?  1032 ASP   A CG  1 
ATOM   8269  O  OD1 . ASP   A 1 1034 ? -29.74700  54.51900  -9.26700  1.000 44.12382  ?  1032 ASP   A OD1 1 
ATOM   8270  O  OD2 . ASP   A 1 1034 ? -29.17800  56.56400  -9.84300  1.000 51.39301  -1 1032 ASP   A OD2 1 
ATOM   8271  N  N   . SER   A 1 1035 ? -33.54300  55.54700  -13.16500 1.000 49.51976  ?  1033 SER   A N   1 
ATOM   8272  C  CA  . SER   A 1 1035 ? -34.15200  55.58300  -14.48500 1.000 39.78103  ?  1033 SER   A CA  1 
ATOM   8273  C  C   . SER   A 1 1035 ? -33.74000  56.84600  -15.23100 1.000 42.98209  ?  1033 SER   A C   1 
ATOM   8274  O  O   . SER   A 1 1035 ? -33.40100  57.87000  -14.63100 1.000 56.54726  ?  1033 SER   A O   1 
ATOM   8275  C  CB  . SER   A 1 1035 ? -35.67300  55.51600  -14.36500 1.000 51.42870  ?  1033 SER   A CB  1 
ATOM   8276  O  OG  . SER   A 1 1035 ? -36.19000  56.71400  -13.81300 1.000 49.29690  ?  1033 SER   A OG  1 
ATOM   8277  N  N   . ASN   A 1 1036 ? -33.76700  56.76500  -16.55800 1.000 43.67528  ?  1034 ASN   A N   1 
ATOM   8278  C  CA  . ASN   A 1 1036 ? -33.40600  57.90400  -17.38800 1.000 46.21709  ?  1034 ASN   A CA  1 
ATOM   8279  C  C   . ASN   A 1 1036 ? -34.58500  58.82000  -17.68100 1.000 52.00319  ?  1034 ASN   A C   1 
ATOM   8280  O  O   . ASN   A 1 1036 ? -34.37400  60.00200  -17.97300 1.000 59.22927  ?  1034 ASN   A O   1 
ATOM   8281  C  CB  . ASN   A 1 1036 ? -32.78700  57.42300  -18.70400 1.000 50.64354  ?  1034 ASN   A CB  1 
ATOM   8282  C  CG  . ASN   A 1 1036 ? -31.35600  56.95100  -18.53200 1.000 77.43035  ?  1034 ASN   A CG  1 
ATOM   8283  O  OD1 . ASN   A 1 1036 ? -30.53400  57.63500  -17.91900 1.000 79.21863  ?  1034 ASN   A OD1 1 
ATOM   8284  N  ND2 . ASN   A 1 1036 ? -31.05100  55.77600  -19.06900 1.000 83.83187  ?  1034 ASN   A ND2 1 
ATOM   8285  N  N   . GLN   A 1 1037 ? -35.81100  58.30700  -17.60700 1.000 45.10624  ?  1035 GLN   A N   1 
ATOM   8286  C  CA  . GLN   A 1 1037 ? -37.00900  59.11100  -17.78700 1.000 42.00990  ?  1035 GLN   A CA  1 
ATOM   8287  C  C   . GLN   A 1 1037 ? -37.91900  58.93800  -16.58100 1.000 44.41096  ?  1035 GLN   A C   1 
ATOM   8288  O  O   . GLN   A 1 1037 ? -37.92400  57.89100  -15.92800 1.000 46.60834  ?  1035 GLN   A O   1 
ATOM   8289  C  CB  . GLN   A 1 1037 ? -37.76600  58.73500  -19.06800 1.000 44.43710  ?  1035 GLN   A CB  1 
ATOM   8290  C  CG  . GLN   A 1 1037 ? -37.12600  59.26800  -20.33900 1.000 56.82387  ?  1035 GLN   A CG  1 
ATOM   8291  C  CD  . GLN   A 1 1037 ? -38.13600  59.49600  -21.44600 1.000 69.40495  ?  1035 GLN   A CD  1 
ATOM   8292  O  OE1 . GLN   A 1 1037 ? -38.72200  58.54900  -21.97100 1.000 81.92397  ?  1035 GLN   A OE1 1 
ATOM   8293  N  NE2 . GLN   A 1 1037 ? -38.34600  60.75800  -21.80500 1.000 64.27789  ?  1035 GLN   A NE2 1 
ATOM   8294  N  N   . VAL   A 1 1038 ? -38.68600  59.98500  -16.28500 1.000 39.21044  ?  1036 VAL   A N   1 
ATOM   8295  C  CA  . VAL   A 1 1038 ? -39.62200  59.97700  -15.17100 1.000 44.67805  ?  1036 VAL   A CA  1 
ATOM   8296  C  C   . VAL   A 1 1038 ? -40.89300  60.68300  -15.62000 1.000 39.60265  ?  1036 VAL   A C   1 
ATOM   8297  O  O   . VAL   A 1 1038 ? -40.90100  61.43500  -16.59600 1.000 37.49341  ?  1036 VAL   A O   1 
ATOM   8298  C  CB  . VAL   A 1 1038 ? -39.03100  60.65000  -13.91000 1.000 48.41041  ?  1036 VAL   A CB  1 
ATOM   8299  C  CG1 . VAL   A 1 1038 ? -39.25500  62.15100  -13.94800 1.000 48.71035  ?  1036 VAL   A CG1 1 
ATOM   8300  C  CG2 . VAL   A 1 1038 ? -39.62600  60.04500  -12.65000 1.000 61.96659  ?  1036 VAL   A CG2 1 
ATOM   8301  N  N   . ILE   A 1 1039 ? -41.98100  60.41800  -14.90100 1.000 41.72027  ?  1037 ILE   A N   1 
ATOM   8302  C  CA  . ILE   A 1 1039 ? -43.27800  61.01600  -15.19800 1.000 39.82016  ?  1037 ILE   A CA  1 
ATOM   8303  C  C   . ILE   A 1 1039 ? -43.92300  61.45300  -13.88900 1.000 39.83830  ?  1037 ILE   A C   1 
ATOM   8304  O  O   . ILE   A 1 1039 ? -43.88600  60.72800  -12.88900 1.000 38.82008  ?  1037 ILE   A O   1 
ATOM   8305  C  CB  . ILE   A 1 1039 ? -44.18800  60.04200  -15.98400 1.000 34.40849  ?  1037 ILE   A CB  1 
ATOM   8306  C  CG1 . ILE   A 1 1039 ? -45.50700  60.71500  -16.36900 1.000 40.78500  ?  1037 ILE   A CG1 1 
ATOM   8307  C  CG2 . ILE   A 1 1039 ? -44.43500  58.76000  -15.20600 1.000 42.27789  ?  1037 ILE   A CG2 1 
ATOM   8308  C  CD1 . ILE   A 1 1039 ? -45.39200  61.64400  -17.55200 1.000 41.79450  ?  1037 ILE   A CD1 1 
ATOM   8309  N  N   . LEU   A 1 1040 ? -44.49800  62.65400  -13.89200 1.000 38.60651  ?  1038 LEU   A N   1 
ATOM   8310  C  CA  . LEU   A 1 1040 ? -45.16400  63.18900  -12.71200 1.000 39.96300  ?  1038 LEU   A CA  1 
ATOM   8311  C  C   . LEU   A 1 1040 ? -46.14100  64.26800  -13.15600 1.000 33.28127  ?  1038 LEU   A C   1 
ATOM   8312  O  O   . LEU   A 1 1040 ? -46.09100  64.75400  -14.28800 1.000 41.19397  ?  1038 LEU   A O   1 
ATOM   8313  C  CB  . LEU   A 1 1040 ? -44.15300  63.73700  -11.69700 1.000 33.64503  ?  1038 LEU   A CB  1 
ATOM   8314  C  CG  . LEU   A 1 1040 ? -43.35600  64.98100  -12.09700 1.000 34.19752  ?  1038 LEU   A CG  1 
ATOM   8315  C  CD1 . LEU   A 1 1040 ? -43.03800  65.82300  -10.87300 1.000 26.26811  ?  1038 LEU   A CD1 1 
ATOM   8316  C  CD2 . LEU   A 1 1040 ? -42.07600  64.61000  -12.83000 1.000 40.30497  ?  1038 LEU   A CD2 1 
ATOM   8317  N  N   . GLY   A 1 1041 ? -47.03900  64.63300  -12.24600 1.000 33.53091  ?  1039 GLY   A N   1 
ATOM   8318  C  CA  . GLY   A 1 1041 ? -48.03300  65.64700  -12.53800 1.000 31.60117  ?  1039 GLY   A CA  1 
ATOM   8319  C  C   . GLY   A 1 1041 ? -47.74800  66.96400  -11.84700 1.000 38.37928  ?  1039 GLY   A C   1 
ATOM   8320  O  O   . GLY   A 1 1041 ? -47.05600  67.00100  -10.82400 1.000 36.76263  ?  1039 GLY   A O   1 
ATOM   8321  N  N   . THR   A 1 1042 ? -48.27200  68.05400  -12.40200 1.000 42.71713  ?  1040 THR   A N   1 
ATOM   8322  C  CA  . THR   A 1 1042 ? -48.12300  69.37600  -11.81400 1.000 35.08121  ?  1040 THR   A CA  1 
ATOM   8323  C  C   . THR   A 1 1042 ? -49.42500  70.14300  -12.00900 1.000 36.89900  ?  1040 THR   A C   1 
ATOM   8324  O  O   . THR   A 1 1042 ? -50.35700  69.66700  -12.66600 1.000 34.11716  ?  1040 THR   A O   1 
ATOM   8325  C  CB  . THR   A 1 1042 ? -46.93700  70.12800  -12.42300 1.000 29.94142  ?  1040 THR   A CB  1 
ATOM   8326  O  OG1 . THR   A 1 1042 ? -46.63500  71.27500  -11.61800 1.000 34.38600  ?  1040 THR   A OG1 1 
ATOM   8327  C  CG2 . THR   A 1 1042 ? -47.26800  70.57600  -13.83700 1.000 37.81788  ?  1040 THR   A CG2 1 
ATOM   8328  N  N   . VAL   A 1 1043 ? -49.48300  71.34400  -11.43800 1.000 32.20712  ?  1041 VAL   A N   1 
ATOM   8329  C  CA  . VAL   A 1 1043 ? -50.69700  72.15000  -11.40700 1.000 29.28303  ?  1041 VAL   A CA  1 
ATOM   8330  C  C   . VAL   A 1 1043 ? -50.35100  73.56200  -11.86000 1.000 38.72952  ?  1041 VAL   A C   1 
ATOM   8331  O  O   . VAL   A 1 1043 ? -49.36400  74.14300  -11.39300 1.000 35.89764  ?  1041 VAL   A O   1 
ATOM   8332  C  CB  . VAL   A 1 1043 ? -51.32400  72.16300  -9.99800  1.000 28.49020  ?  1041 VAL   A CB  1 
ATOM   8333  C  CG1 . VAL   A 1 1043 ? -52.33800  73.29000  -9.85800  1.000 42.40212  ?  1041 VAL   A CG1 1 
ATOM   8334  C  CG2 . VAL   A 1 1043 ? -51.95500  70.81700  -9.68500  1.000 25.71555  ?  1041 VAL   A CG2 1 
ATOM   8335  N  N   . THR   A 1 1044 ? -51.15300  74.10700  -12.77300 1.000 38.36567  ?  1042 THR   A N   1 
ATOM   8336  C  CA  . THR   A 1 1044 ? -51.01300  75.47600  -13.24900 1.000 33.05404  ?  1042 THR   A CA  1 
ATOM   8337  C  C   . THR   A 1 1044 ? -52.18700  76.31800  -12.76100 1.000 43.81092  ?  1042 THR   A C   1 
ATOM   8338  O  O   . THR   A 1 1044 ? -53.22300  75.79300  -12.34500 1.000 46.68657  ?  1042 THR   A O   1 
ATOM   8339  C  CB  . THR   A 1 1044 ? -50.93200  75.52900  -14.78100 1.000 43.40198  ?  1042 THR   A CB  1 
ATOM   8340  O  OG1 . THR   A 1 1044 ? -52.25000  75.63000  -15.33400 1.000 61.25184  ?  1042 THR   A OG1 1 
ATOM   8341  C  CG2 . THR   A 1 1044 ? -50.25500  74.27900  -15.32800 1.000 43.70394  ?  1042 THR   A CG2 1 
ATOM   8342  N  N   . ASP   A 1 1045 ? -52.01500  77.64400  -12.81900 1.000 49.01247  ?  1043 ASP   A N   1 
ATOM   8343  C  CA  . ASP   A 1 1045 ? -53.05100  78.55300  -12.33100 1.000 46.14665  ?  1043 ASP   A CA  1 
ATOM   8344  C  C   . ASP   A 1 1045 ? -54.34100  78.44200  -13.14000 1.000 52.51906  ?  1043 ASP   A C   1 
ATOM   8345  O  O   . ASP   A 1 1045 ? -55.43100  78.65000  -12.59300 1.000 49.42770  ?  1043 ASP   A O   1 
ATOM   8346  C  CB  . ASP   A 1 1045 ? -52.53500  79.99600  -12.34400 1.000 47.68303  ?  1043 ASP   A CB  1 
ATOM   8347  C  CG  . ASP   A 1 1045 ? -52.36400  80.55300  -13.75300 1.000 73.13931  ?  1043 ASP   A CG  1 
ATOM   8348  O  OD1 . ASP   A 1 1045 ? -52.02700  79.78100  -14.67600 1.000 88.48473  ?  1043 ASP   A OD1 1 
ATOM   8349  O  OD2 . ASP   A 1 1045 ? -52.55700  81.77400  -13.93200 1.000 75.42037  -1 1043 ASP   A OD2 1 
ATOM   8350  N  N   . GLY   A 1 1046 ? -54.24000  78.12700  -14.43100 1.000 44.49132  ?  1044 GLY   A N   1 
ATOM   8351  C  CA  . GLY   A 1 1046 ? -55.40300  77.93900  -15.27700 1.000 43.26351  ?  1044 GLY   A CA  1 
ATOM   8352  C  C   . GLY   A 1 1046 ? -56.18200  79.18900  -15.61700 1.000 47.41517  ?  1044 GLY   A C   1 
ATOM   8353  O  O   . GLY   A 1 1046 ? -57.30100  79.08100  -16.12900 1.000 48.22833  ?  1044 GLY   A O   1 
ATOM   8354  N  N   . ARG   A 1 1047 ? -55.63200  80.37400  -15.34900 1.000 52.71879  ?  1045 ARG   A N   1 
ATOM   8355  C  CA  . ARG   A 1 1047 ? -56.31500  81.63500  -15.63700 1.000 38.74059  ?  1045 ARG   A CA  1 
ATOM   8356  C  C   . ARG   A 1 1047 ? -55.91400  82.08500  -17.03800 1.000 37.18590  ?  1045 ARG   A C   1 
ATOM   8357  O  O   . ARG   A 1 1047 ? -55.00500  82.89200  -17.23900 1.000 53.93962  ?  1045 ARG   A O   1 
ATOM   8358  C  CB  . ARG   A 1 1047 ? -55.98400  82.67400  -14.57400 1.000 45.34111  ?  1045 ARG   A CB  1 
ATOM   8359  C  CG  . ARG   A 1 1047 ? -56.11800  82.13300  -13.15800 1.000 45.75210  ?  1045 ARG   A CG  1 
ATOM   8360  C  CD  . ARG   A 1 1047 ? -57.02600  82.99500  -12.29600 1.000 42.17830  ?  1045 ARG   A CD  1 
ATOM   8361  N  NE  . ARG   A 1 1047 ? -57.51800  82.26000  -11.13600 1.000 45.29774  ?  1045 ARG   A NE  1 
ATOM   8362  C  CZ  . ARG   A 1 1047 ? -58.28000  82.78000  -10.18300 1.000 45.03830  ?  1045 ARG   A CZ  1 
ATOM   8363  N  NH1 . ARG   A 1 1047 ? -58.64700  84.05100  -10.20600 1.000 47.03182  ?  1045 ARG   A NH1 1 
ATOM   8364  N  NH2 . ARG   A 1 1047 ? -58.68500  82.00400  -9.18100  1.000 43.91760  ?  1045 ARG   A NH2 1 
ATOM   8365  N  N   . GLN   A 1 1048 ? -56.61700  81.53000  -18.02700 1.000 36.53291  ?  1046 GLN   A N   1 
ATOM   8366  C  CA  . GLN   A 1 1048 ? -56.30400  81.79700  -19.42700 1.000 39.95063  ?  1046 GLN   A CA  1 
ATOM   8367  C  C   . GLN   A 1 1048 ? -56.51300  83.26900  -19.76800 1.000 51.51105  ?  1046 GLN   A C   1 
ATOM   8368  O  O   . GLN   A 1 1048 ? -55.59300  83.95200  -20.23300 1.000 46.37785  ?  1046 GLN   A O   1 
ATOM   8369  C  CB  . GLN   A 1 1048 ? -57.16600  80.90400  -20.32100 1.000 27.74630  ?  1046 GLN   A CB  1 
ATOM   8370  C  CG  . GLN   A 1 1048 ? -56.54600  80.55700  -21.66000 1.000 33.78919  ?  1046 GLN   A CG  1 
ATOM   8371  C  CD  . GLN   A 1 1048 ? -57.29800  79.44700  -22.36600 1.000 49.49987  ?  1046 GLN   A CD  1 
ATOM   8372  O  OE1 . GLN   A 1 1048 ? -58.16100  78.79700  -21.77500 1.000 45.71420  ?  1046 GLN   A OE1 1 
ATOM   8373  N  NE2 . GLN   A 1 1048 ? -56.97300  79.22000  -23.63400 1.000 54.81759  ?  1046 GLN   A NE2 1 
ATOM   8374  N  N   . HIS   A 1 1049 ? -57.72500  83.77300  -19.54100 1.000 62.11279  ?  1047 HIS   A N   1 
ATOM   8375  C  CA  . HIS   A 1 1049 ? -58.05300  85.16800  -19.82400 1.000 54.32180  ?  1047 HIS   A CA  1 
ATOM   8376  C  C   . HIS   A 1 1049 ? -57.48600  86.07000  -18.73200 1.000 51.25026  ?  1047 HIS   A C   1 
ATOM   8377  O  O   . HIS   A 1 1049 ? -57.64600  85.76800  -17.54500 1.000 61.25850  ?  1047 HIS   A O   1 
ATOM   8378  C  CB  . HIS   A 1 1049 ? -59.56600  85.34600  -19.91100 1.000 64.72905  ?  1047 HIS   A CB  1 
ATOM   8379  C  CG  . HIS   A 1 1049 ? -59.99400  86.48700  -20.77900 1.000 70.33657  ?  1047 HIS   A CG  1 
ATOM   8380  N  ND1 . HIS   A 1 1049 ? -59.80800  87.80600  -20.42400 1.000 54.59994  ?  1047 HIS   A ND1 1 
ATOM   8381  C  CD2 . HIS   A 1 1049 ? -60.60700  86.50600  -21.98700 1.000 66.53733  ?  1047 HIS   A CD2 1 
ATOM   8382  C  CE1 . HIS   A 1 1049 ? -60.28400  88.58800  -21.37700 1.000 65.50974  ?  1047 HIS   A CE1 1 
ATOM   8383  N  NE2 . HIS   A 1 1049 ? -60.77500  87.82400  -22.33600 1.000 80.19873  ?  1047 HIS   A NE2 1 
ATOM   8384  N  N   . PRO   A 1 1050 ? -56.83100  87.18200  -19.08600 1.000 53.37463  ?  1048 PRO   A N   1 
ATOM   8385  C  CA  . PRO   A 1 1050 ? -56.24400  88.05000  -18.05100 1.000 62.59242  ?  1048 PRO   A CA  1 
ATOM   8386  C  C   . PRO   A 1 1050 ? -57.26900  88.73900  -17.16300 1.000 55.66953  ?  1048 PRO   A C   1 
ATOM   8387  O  O   . PRO   A 1 1050 ? -56.87900  89.32500  -16.14500 1.000 66.81803  ?  1048 PRO   A O   1 
ATOM   8388  C  CB  . PRO   A 1 1050 ? -55.43900  89.07300  -18.86500 1.000 49.28154  ?  1048 PRO   A CB  1 
ATOM   8389  C  CG  . PRO   A 1 1050 ? -56.09200  89.08500  -20.20400 1.000 57.72986  ?  1048 PRO   A CG  1 
ATOM   8390  C  CD  . PRO   A 1 1050 ? -56.55000  87.67400  -20.44400 1.000 54.67663  ?  1048 PRO   A CD  1 
ATOM   8391  N  N   . ASP   A 1 1051 ? -58.55400  88.68600  -17.50500 1.000 62.48846  ?  1049 ASP   A N   1 
ATOM   8392  C  CA  . ASP   A 1 1051 ? -59.60300  89.30900  -16.70900 1.000 69.27148  ?  1049 ASP   A CA  1 
ATOM   8393  C  C   . ASP   A 1 1051 ? -60.10700  88.42300  -15.57700 1.000 62.59422  ?  1049 ASP   A C   1 
ATOM   8394  O  O   . ASP   A 1 1051 ? -60.99300  88.84700  -14.82800 1.000 65.03372  ?  1049 ASP   A O   1 
ATOM   8395  C  CB  . ASP   A 1 1051 ? -60.78200  89.70400  -17.60600 1.000 70.04430  ?  1049 ASP   A CB  1 
ATOM   8396  C  CG  . ASP   A 1 1051 ? -60.47200  90.89900  -18.48300 1.000 83.85576  ?  1049 ASP   A CG  1 
ATOM   8397  O  OD1 . ASP   A 1 1051 ? -59.43700  91.55900  -18.24600 1.000 73.14656  ?  1049 ASP   A OD1 1 
ATOM   8398  O  OD2 . ASP   A 1 1051 ? -61.26800  91.18000  -19.40700 1.000 73.59259  -1 1049 ASP   A OD2 1 
ATOM   8399  N  N   . THR   A 1 1052 ? -59.56900  87.21500  -15.42600 1.000 64.22395  ?  1050 THR   A N   1 
ATOM   8400  C  CA  . THR   A 1 1052 ? -60.05500  86.26400  -14.43700 1.000 53.17922  ?  1050 THR   A CA  1 
ATOM   8401  C  C   . THR   A 1 1052 ? -59.18300  86.20500  -13.18800 1.000 51.34273  ?  1050 THR   A C   1 
ATOM   8402  O  O   . THR   A 1 1052 ? -59.42700  85.36500  -12.31700 1.000 59.79406  ?  1050 THR   A O   1 
ATOM   8403  C  CB  . THR   A 1 1052 ? -60.15900  84.87300  -15.05900 1.000 40.75981  ?  1050 THR   A CB  1 
ATOM   8404  O  OG1 . THR   A 1 1052 ? -58.85800  84.44400  -15.47600 1.000 52.05819  ?  1050 THR   A OG1 1 
ATOM   8405  C  CG2 . THR   A 1 1052 ? -61.08600  84.89900  -16.26200 1.000 54.48739  ?  1050 THR   A CG2 1 
ATOM   8406  N  N   . ARG   A 1 1053 ? -58.18600  87.07900  -13.07200 1.000 37.84866  ?  1051 ARG   A N   1 
ATOM   8407  C  CA  . ARG   A 1 1053 ? -57.24600  87.01000  -11.96200 1.000 54.49249  ?  1051 ARG   A CA  1 
ATOM   8408  C  C   . ARG   A 1 1053 ? -57.78700  87.61400  -10.67100 1.000 56.53163  ?  1051 ARG   A C   1 
ATOM   8409  O  O   . ARG   A 1 1053 ? -57.07300  87.61300  -9.66200  1.000 57.00011  ?  1051 ARG   A O   1 
ATOM   8410  C  CB  . ARG   A 1 1053 ? -55.93400  87.69500  -12.34800 1.000 63.41303  ?  1051 ARG   A CB  1 
ATOM   8411  C  CG  . ARG   A 1 1053 ? -55.08000  86.85900  -13.28300 1.000 68.88232  ?  1051 ARG   A CG  1 
ATOM   8412  C  CD  . ARG   A 1 1053 ? -53.62100  87.27500  -13.24100 1.000 70.24457  ?  1051 ARG   A CD  1 
ATOM   8413  N  NE  . ARG   A 1 1053 ? -52.89900  86.68000  -12.12100 1.000 68.71262  ?  1051 ARG   A NE  1 
ATOM   8414  C  CZ  . ARG   A 1 1053 ? -52.73000  85.37800  -11.92000 1.000 63.94143  ?  1051 ARG   A CZ  1 
ATOM   8415  N  NH1 . ARG   A 1 1053 ? -53.22100  84.47400  -12.75400 1.000 55.01242  ?  1051 ARG   A NH1 1 
ATOM   8416  N  NH2 . ARG   A 1 1053 ? -52.04000  84.97200  -10.85800 1.000 61.80476  ?  1051 ARG   A NH2 1 
ATOM   8417  N  N   . GLU   A 1 1054 ? -59.02000  88.12200  -10.67000 1.000 55.94430  ?  1052 GLU   A N   1 
ATOM   8418  C  CA  . GLU   A 1 1054 ? -59.64700  88.63100  -9.45700  1.000 48.80495  ?  1052 GLU   A CA  1 
ATOM   8419  C  C   . GLU   A 1 1054 ? -60.92000  87.87500  -9.10500  1.000 44.38781  ?  1052 GLU   A C   1 
ATOM   8420  O  O   . GLU   A 1 1054 ? -61.62100  88.26600  -8.16400  1.000 51.04167  ?  1052 GLU   A O   1 
ATOM   8421  C  CB  . GLU   A 1 1054 ? -59.95100  90.12700  -9.59000  1.000 47.93289  ?  1052 GLU   A CB  1 
ATOM   8422  C  CG  . GLU   A 1 1054 ? -58.79400  90.96300  -10.11300 1.000 57.58704  ?  1052 GLU   A CG  1 
ATOM   8423  C  CD  . GLU   A 1 1054 ? -57.82200  91.37400  -9.02300  1.000 75.89001  ?  1052 GLU   A CD  1 
ATOM   8424  O  OE1 . GLU   A 1 1054 ? -57.82300  90.74400  -7.94400  1.000 88.13968  ?  1052 GLU   A OE1 1 
ATOM   8425  O  OE2 . GLU   A 1 1054 ? -57.05100  92.33100  -9.24900  1.000 106.94422 -1 1052 GLU   A OE2 1 
ATOM   8426  N  N   . LEU   A 1 1055 ? -61.23300  86.80400  -9.82800  1.000 41.47176  ?  1053 LEU   A N   1 
ATOM   8427  C  CA  . LEU   A 1 1055 ? -62.45200  86.04300  -9.61200  1.000 43.66196  ?  1053 LEU   A CA  1 
ATOM   8428  C  C   . LEU   A 1 1055 ? -62.22200  84.90800  -8.61900  1.000 52.44878  ?  1053 LEU   A C   1 
ATOM   8429  O  O   . LEU   A 1 1055 ? -61.09200  84.48400  -8.36500  1.000 49.86440  ?  1053 LEU   A O   1 
ATOM   8430  C  CB  . LEU   A 1 1055 ? -62.97400  85.47300  -10.93200 1.000 43.62924  ?  1053 LEU   A CB  1 
ATOM   8431  C  CG  . LEU   A 1 1055 ? -63.19300  86.47700  -12.06300 1.000 47.97111  ?  1053 LEU   A CG  1 
ATOM   8432  C  CD1 . LEU   A 1 1055 ? -63.56200  85.76600  -13.35400 1.000 42.73587  ?  1053 LEU   A CD1 1 
ATOM   8433  C  CD2 . LEU   A 1 1055 ? -64.25600  87.47800  -11.67700 1.000 53.35319  ?  1053 LEU   A CD2 1 
ATOM   8434  N  N   . LEU   A 1 1056 ? -63.32400  84.41500  -8.06000  1.000 49.21085  ?  1054 LEU   A N   1 
ATOM   8435  C  CA  . LEU   A 1 1056 ? -63.32300  83.28400  -7.13900  1.000 40.38786  ?  1054 LEU   A CA  1 
ATOM   8436  C  C   . LEU   A 1 1056 ? -63.88300  82.07700  -7.87600  1.000 44.31155  ?  1054 LEU   A C   1 
ATOM   8437  O  O   . LEU   A 1 1056 ? -65.08200  82.02600  -8.17100  1.000 58.04765  ?  1054 LEU   A O   1 
ATOM   8438  C  CB  . LEU   A 1 1056 ? -64.15000  83.59200  -5.89500  1.000 38.09078  ?  1054 LEU   A CB  1 
ATOM   8439  C  CG  . LEU   A 1 1056 ? -63.40100  83.92300  -4.61000  1.000 39.42301  ?  1054 LEU   A CG  1 
ATOM   8440  C  CD1 . LEU   A 1 1056 ? -62.47100  85.10700  -4.80800  1.000 58.95837  ?  1054 LEU   A CD1 1 
ATOM   8441  C  CD2 . LEU   A 1 1056 ? -64.41000  84.21400  -3.52700  1.000 38.37258  ?  1054 LEU   A CD2 1 
ATOM   8442  N  N   . GLY   A 1 1057 ? -63.02300  81.11100  -8.17200  1.000 48.80867  ?  1055 GLY   A N   1 
ATOM   8443  C  CA  . GLY   A 1 1057 ? -63.47800  79.93800  -8.89500  1.000 49.92303  ?  1055 GLY   A CA  1 
ATOM   8444  C  C   . GLY   A 1 1057 ? -62.37600  78.90900  -9.00000  1.000 46.03715  ?  1055 GLY   A C   1 
ATOM   8445  O  O   . GLY   A 1 1057 ? -61.26000  79.10300  -8.51100  1.000 43.58054  ?  1055 GLY   A O   1 
ATOM   8446  N  N   . MET   A 1 1058 ? -62.71400  77.80000  -9.65100  1.000 39.64576  ?  1056 MET   A N   1 
ATOM   8447  C  CA  . MET   A 1 1058 ? -61.78200  76.70600  -9.89100  1.000 34.09206  ?  1056 MET   A CA  1 
ATOM   8448  C  C   . MET   A 1 1058 ? -61.20700  76.87300  -11.29200 1.000 46.31945  ?  1056 MET   A C   1 
ATOM   8449  O  O   . MET   A 1 1058 ? -61.89900  76.63600  -12.28800 1.000 39.19412  ?  1056 MET   A O   1 
ATOM   8450  C  CB  . MET   A 1 1058 ? -62.48100  75.35700  -9.73700  1.000 41.62342  ?  1056 MET   A CB  1 
ATOM   8451  C  CG  . MET   A 1 1058 ? -61.63200  74.15500  -10.12200 1.000 35.13866  ?  1056 MET   A CG  1 
ATOM   8452  S  SD  . MET   A 1 1058 ? -60.02600  74.12500  -9.30800  1.000 63.35192  ?  1056 MET   A SD  1 
ATOM   8453  C  CE  . MET   A 1 1058 ? -59.71400  72.36200  -9.28700  1.000 62.32438  ?  1056 MET   A CE  1 
ATOM   8454  N  N   . PHE   A 1 1059 ? -59.94200  77.28600  -11.37000 1.000 47.83509  ?  1057 PHE   A N   1 
ATOM   8455  C  CA  . PHE   A 1 1059 ? -59.27500  77.44800  -12.65100 1.000 46.62206  ?  1057 PHE   A CA  1 
ATOM   8456  C  C   . PHE   A 1 1059 ? -58.14700  76.45700  -12.88800 1.000 47.21714  ?  1057 PHE   A C   1 
ATOM   8457  O  O   . PHE   A 1 1059 ? -57.82900  76.18600  -14.04900 1.000 57.05373  ?  1057 PHE   A O   1 
ATOM   8458  C  CB  . PHE   A 1 1059 ? -58.69800  78.86600  -12.78800 1.000 50.43699  ?  1057 PHE   A CB  1 
ATOM   8459  C  CG  . PHE   A 1 1059 ? -59.73000  79.95700  -12.76300 1.000 47.87425  ?  1057 PHE   A CG  1 
ATOM   8460  C  CD1 . PHE   A 1 1059 ? -60.21700  80.44200  -11.56200 1.000 46.37454  ?  1057 PHE   A CD1 1 
ATOM   8461  C  CD2 . PHE   A 1 1059 ? -60.19900  80.51100  -13.94300 1.000 56.07080  ?  1057 PHE   A CD2 1 
ATOM   8462  C  CE1 . PHE   A 1 1059 ? -61.15700  81.45300  -11.53800 1.000 52.10946  ?  1057 PHE   A CE1 1 
ATOM   8463  C  CE2 . PHE   A 1 1059 ? -61.14100  81.52100  -13.92400 1.000 53.14581  ?  1057 PHE   A CE2 1 
ATOM   8464  C  CZ  . PHE   A 1 1059 ? -61.61800  81.99400  -12.72000 1.000 49.15869  ?  1057 PHE   A CZ  1 
ATOM   8465  N  N   . VAL   A 1 1060 ? -57.55100  75.90300  -11.82600 1.000 42.61866  ?  1058 VAL   A N   1 
ATOM   8466  C  CA  . VAL   A 1 1060 ? -56.28000  75.20000  -11.96700 1.000 53.34398  ?  1058 VAL   A CA  1 
ATOM   8467  C  C   . VAL   A 1 1060 ? -56.42400  74.00100  -12.89300 1.000 47.76270  ?  1058 VAL   A C   1 
ATOM   8468  O  O   . VAL   A 1 1060 ? -57.47200  73.34400  -12.94600 1.000 44.76594  ?  1058 VAL   A O   1 
ATOM   8469  C  CB  . VAL   A 1 1060 ? -55.73200  74.78200  -10.59000 1.000 41.62246  ?  1058 VAL   A CB  1 
ATOM   8470  C  CG1 . VAL   A 1 1060 ? -55.90100  75.90500  -9.58800  1.000 52.46896  ?  1058 VAL   A CG1 1 
ATOM   8471  C  CG2 . VAL   A 1 1060 ? -56.39700  73.51200  -10.08900 1.000 59.25592  ?  1058 VAL   A CG2 1 
ATOM   8472  N  N   . ASN   A 1 1061 ? -55.36700  73.73000  -13.65400 1.000 40.16464  ?  1059 ASN   A N   1 
ATOM   8473  C  CA  . ASN   A 1 1061 ? -55.31800  72.60200  -14.56900 1.000 47.45322  ?  1059 ASN   A CA  1 
ATOM   8474  C  C   . ASN   A 1 1061 ? -54.16700  71.68600  -14.18200 1.000 35.92178  ?  1059 ASN   A C   1 
ATOM   8475  O  O   . ASN   A 1 1061 ? -53.13000  72.13800  -13.68900 1.000 40.78619  ?  1059 ASN   A O   1 
ATOM   8476  C  CB  . ASN   A 1 1061 ? -55.15100  73.05900  -16.02600 1.000 34.72744  ?  1059 ASN   A CB  1 
ATOM   8477  C  CG  . ASN   A 1 1061 ? -55.54900  71.98400  -17.02500 1.000 56.69326  ?  1059 ASN   A CG  1 
ATOM   8478  O  OD1 . ASN   A 1 1061 ? -56.24000  71.02200  -16.68100 1.000 49.96927  ?  1059 ASN   A OD1 1 
ATOM   8479  N  ND2 . ASN   A 1 1061 ? -55.11200  72.14200  -18.27000 1.000 57.92049  ?  1059 ASN   A ND2 1 
ATOM   8480  N  N   . THR   A 1 1062 ? -54.36300  70.39100  -14.40600 1.000 46.55453  ?  1060 THR   A N   1 
ATOM   8481  C  CA  . THR   A 1 1062 ? -53.36100  69.38000  -14.10300 1.000 39.70967  ?  1060 THR   A CA  1 
ATOM   8482  C  C   . THR   A 1 1062 ? -52.65300  68.97300  -15.38800 1.000 44.75221  ?  1060 THR   A C   1 
ATOM   8483  O  O   . THR   A 1 1062 ? -53.30400  68.62100  -16.37800 1.000 46.35904  ?  1060 THR   A O   1 
ATOM   8484  C  CB  . THR   A 1 1062 ? -54.00200  68.16100  -13.43900 1.000 37.89539  ?  1060 THR   A CB  1 
ATOM   8485  O  OG1 . THR   A 1 1062 ? -54.67800  68.57100  -12.24400 1.000 39.74359  ?  1060 THR   A OG1 1 
ATOM   8486  C  CG2 . THR   A 1 1062 ? -52.94400  67.13600  -13.08400 1.000 39.74892  ?  1060 THR   A CG2 1 
ATOM   8487  N  N   . LEU   A 1 1063 ? -51.32100  69.02700  -15.37000 1.000 36.84548  ?  1061 LEU   A N   1 
ATOM   8488  C  CA  . LEU   A 1 1063 ? -50.53400  68.71300  -16.54700 1.000 35.34979  ?  1061 LEU   A CA  1 
ATOM   8489  C  C   . LEU   A 1 1063 ? -49.64500  67.50300  -16.29400 1.000 37.88472  ?  1061 LEU   A C   1 
ATOM   8490  O  O   . LEU   A 1 1063 ? -49.05000  67.38600  -15.21700 1.000 39.60939  ?  1061 LEU   A O   1 
ATOM   8491  C  CB  . LEU   A 1 1063 ? -49.65300  69.90200  -16.95300 1.000 33.06631  ?  1061 LEU   A CB  1 
ATOM   8492  C  CG  . LEU   A 1 1063 ? -50.35200  71.08300  -17.61800 1.000 31.71024  ?  1061 LEU   A CG  1 
ATOM   8493  C  CD1 . LEU   A 1 1063 ? -49.33600  71.90100  -18.38300 1.000 34.99742  ?  1061 LEU   A CD1 1 
ATOM   8494  C  CD2 . LEU   A 1 1063 ? -51.46900  70.60600  -18.53200 1.000 50.88862  ?  1061 LEU   A CD2 1 
ATOM   8495  N  N   . PRO   A 1 1064 ? -49.54200  66.58700  -17.25700 1.000 43.15628  ?  1062 PRO   A N   1 
ATOM   8496  C  CA  . PRO   A 1 1064 ? -48.55700  65.50100  -17.14600 1.000 44.62938  ?  1062 PRO   A CA  1 
ATOM   8497  C  C   . PRO   A 1 1064 ? -47.18800  65.98600  -17.60300 1.000 32.93475  ?  1062 PRO   A C   1 
ATOM   8498  O  O   . PRO   A 1 1064 ? -47.06000  66.62100  -18.65200 1.000 47.07855  ?  1062 PRO   A O   1 
ATOM   8499  C  CB  . PRO   A 1 1064 ? -49.11200  64.42400  -18.08400 1.000 33.81145  ?  1062 PRO   A CB  1 
ATOM   8500  C  CG  . PRO   A 1 1064 ? -49.85300  65.20400  -19.12700 1.000 46.05299  ?  1062 PRO   A CG  1 
ATOM   8501  C  CD  . PRO   A 1 1064 ? -50.40500  66.43600  -18.44100 1.000 44.67954  ?  1062 PRO   A CD  1 
ATOM   8502  N  N   . LEU   A 1 1065 ? -46.16200  65.69500  -16.80700 1.000 26.56057  ?  1063 LEU   A N   1 
ATOM   8503  C  CA  . LEU   A 1 1065 ? -44.80100  66.14000  -17.09600 1.000 31.26645  ?  1063 LEU   A CA  1 
ATOM   8504  C  C   . LEU   A 1 1065 ? -43.92100  64.91900  -17.32500 1.000 37.67950  ?  1063 LEU   A C   1 
ATOM   8505  O  O   . LEU   A 1 1065 ? -43.63400  64.16600  -16.38800 1.000 40.16775  ?  1063 LEU   A O   1 
ATOM   8506  C  CB  . LEU   A 1 1065 ? -44.24700  67.00600  -15.96500 1.000 27.34651  ?  1063 LEU   A CB  1 
ATOM   8507  C  CG  . LEU   A 1 1065 ? -44.87400  68.39200  -15.79600 1.000 32.08836  ?  1063 LEU   A CG  1 
ATOM   8508  C  CD1 . LEU   A 1 1065 ? -44.03300  69.25100  -14.86500 1.000 27.55724  ?  1063 LEU   A CD1 1 
ATOM   8509  C  CD2 . LEU   A 1 1065 ? -45.05800  69.07400  -17.14100 1.000 36.53838  ?  1063 LEU   A CD2 1 
ATOM   8510  N  N   . LEU   A 1 1066 ? -43.49500  64.72800  -18.56700 1.000 33.80553  ?  1064 LEU   A N   1 
ATOM   8511  C  CA  . LEU   A 1 1066 ? -42.58000  63.65500  -18.93400 1.000 36.33769  ?  1064 LEU   A CA  1 
ATOM   8512  C  C   . LEU   A 1 1066 ? -41.18000  64.25200  -19.04500 1.000 35.89862  ?  1064 LEU   A C   1 
ATOM   8513  O  O   . LEU   A 1 1066 ? -40.87500  64.95900  -20.01100 1.000 42.45299  ?  1064 LEU   A O   1 
ATOM   8514  C  CB  . LEU   A 1 1066 ? -43.02800  63.00100  -20.24000 1.000 38.22820  ?  1064 LEU   A CB  1 
ATOM   8515  C  CG  . LEU   A 1 1066 ? -42.08900  62.00400  -20.91300 1.000 54.71406  ?  1064 LEU   A CG  1 
ATOM   8516  C  CD1 . LEU   A 1 1066 ? -41.60900  60.95900  -19.92400 1.000 54.45744  ?  1064 LEU   A CD1 1 
ATOM   8517  C  CD2 . LEU   A 1 1066 ? -42.78700  61.35500  -22.10200 1.000 34.69124  ?  1064 LEU   A CD2 1 
ATOM   8518  N  N   . LEU   A 1 1067 ? -40.33800  63.98200  -18.05100 1.000 34.67671  ?  1065 LEU   A N   1 
ATOM   8519  C  CA  . LEU   A 1 1067 ? -39.01100  64.57300  -17.97500 1.000 45.02002  ?  1065 LEU   A CA  1 
ATOM   8520  C  C   . LEU   A 1 1067 ? -37.93900  63.49100  -18.03800 1.000 41.67206  ?  1065 LEU   A C   1 
ATOM   8521  O  O   . LEU   A 1 1067 ? -38.21200  62.30000  -17.86400 1.000 38.78567  ?  1065 LEU   A O   1 
ATOM   8522  C  CB  . LEU   A 1 1067 ? -38.85100  65.40400  -16.69400 1.000 40.74508  ?  1065 LEU   A CB  1 
ATOM   8523  C  CG  . LEU   A 1 1067 ? -39.95600  66.43800  -16.47500 1.000 36.29667  ?  1065 LEU   A CG  1 
ATOM   8524  C  CD1 . LEU   A 1 1067 ? -39.95100  66.95000  -15.04800 1.000 32.69087  ?  1065 LEU   A CD1 1 
ATOM   8525  C  CD2 . LEU   A 1 1067 ? -39.80000  67.58200  -17.45900 1.000 42.39923  ?  1065 LEU   A CD2 1 
ATOM   8526  N  N   . SER   A 1 1068 ? -36.70400  63.93000  -18.29000 1.000 41.97418  ?  1066 SER   A N   1 
ATOM   8527  C  CA  . SER   A 1 1068 ? -35.56600  63.03900  -18.45900 1.000 41.73372  ?  1066 SER   A CA  1 
ATOM   8528  C  C   . SER   A 1 1068 ? -34.41400  63.48200  -17.57000 1.000 41.55710  ?  1066 SER   A C   1 
ATOM   8529  O  O   . SER   A 1 1068 ? -34.11900  64.67700  -17.46800 1.000 47.98848  ?  1066 SER   A O   1 
ATOM   8530  C  CB  . SER   A 1 1068 ? -35.09700  62.99800  -19.91800 1.000 25.37956  ?  1066 SER   A CB  1 
ATOM   8531  O  OG  . SER   A 1 1068 ? -36.16300  62.66600  -20.79000 1.000 53.65577  ?  1066 SER   A OG  1 
ATOM   8532  N  N   . ILE   A 1 1069 ? -33.76000  62.50900  -16.94100 1.000 46.04661  ?  1067 ILE   A N   1 
ATOM   8533  C  CA  . ILE   A 1 1069 ? -32.60400  62.75200  -16.08700 1.000 43.28837  ?  1067 ILE   A CA  1 
ATOM   8534  C  C   . ILE   A 1 1069 ? -31.40900  62.05000  -16.71200 1.000 41.01524  ?  1067 ILE   A C   1 
ATOM   8535  O  O   . ILE   A 1 1069 ? -31.43300  60.82900  -16.91200 1.000 48.98845  ?  1067 ILE   A O   1 
ATOM   8536  C  CB  . ILE   A 1 1069 ? -32.83700  62.26500  -14.64900 1.000 45.68117  ?  1067 ILE   A CB  1 
ATOM   8537  C  CG1 . ILE   A 1 1069 ? -34.01900  63.00900  -14.02100 1.000 58.47963  ?  1067 ILE   A CG1 1 
ATOM   8538  C  CG2 . ILE   A 1 1069 ? -31.58000  62.45400  -13.81400 1.000 42.97841  ?  1067 ILE   A CG2 1 
ATOM   8539  C  CD1 . ILE   A 1 1069 ? -33.87000  64.52400  -14.03100 1.000 40.26993  ?  1067 ILE   A CD1 1 
ATOM   8540  N  N   . ASP   A 1 1070 ? -30.37500  62.82300  -17.03100 1.000 43.35922  ?  1068 ASP   A N   1 
ATOM   8541  C  CA  . ASP   A 1 1070 ? -29.12100  62.29600  -17.55900 1.000 34.25268  ?  1068 ASP   A CA  1 
ATOM   8542  C  C   . ASP   A 1 1070 ? -28.13500  62.23400  -16.40000 1.000 47.51294  ?  1068 ASP   A C   1 
ATOM   8543  O  O   . ASP   A 1 1070 ? -27.56000  63.25200  -16.00400 1.000 51.04474  ?  1068 ASP   A O   1 
ATOM   8544  C  CB  . ASP   A 1 1070 ? -28.59900  63.16600  -18.69700 1.000 35.57715  ?  1068 ASP   A CB  1 
ATOM   8545  C  CG  . ASP   A 1 1070 ? -27.47300  62.50600  -19.47000 1.000 51.04888  ?  1068 ASP   A CG  1 
ATOM   8546  O  OD1 . ASP   A 1 1070 ? -26.45300  62.13800  -18.84900 1.000 59.15592  ?  1068 ASP   A OD1 1 
ATOM   8547  O  OD2 . ASP   A 1 1070 ? -27.60700  62.35400  -20.70300 1.000 72.12713  -1 1068 ASP   A OD2 1 
ATOM   8548  N  N   . HIS   A 1 1071 ? -27.94000  61.03400  -15.85300 1.000 44.32440  ?  1069 HIS   A N   1 
ATOM   8549  C  CA  . HIS   A 1 1071 ? -27.03900  60.88100  -14.71800 1.000 49.61418  ?  1069 HIS   A CA  1 
ATOM   8550  C  C   . HIS   A 1 1071 ? -25.57800  61.07500  -15.10300 1.000 47.56508  ?  1069 HIS   A C   1 
ATOM   8551  O  O   . HIS   A 1 1071 ? -24.74500  61.30900  -14.22000 1.000 48.98921  ?  1069 HIS   A O   1 
ATOM   8552  C  CB  . HIS   A 1 1071 ? -27.23500  59.50900  -14.07800 1.000 32.50727  ?  1069 HIS   A CB  1 
ATOM   8553  C  CG  . HIS   A 1 1071 ? -28.62600  59.27500  -13.58400 1.000 36.60262  ?  1069 HIS   A CG  1 
ATOM   8554  N  ND1 . HIS   A 1 1071 ? -28.98200  59.43000  -12.26100 1.000 47.72445  ?  1069 HIS   A ND1 1 
ATOM   8555  C  CD2 . HIS   A 1 1071 ? -29.75300  58.90200  -14.23700 1.000 37.51293  ?  1069 HIS   A CD2 1 
ATOM   8556  C  CE1 . HIS   A 1 1071 ? -30.26800  59.16000  -12.12000 1.000 48.55501  ?  1069 HIS   A CE1 1 
ATOM   8557  N  NE2 . HIS   A 1 1071 ? -30.75900  58.83600  -13.30300 1.000 38.55928  ?  1069 HIS   A NE2 1 
ATOM   8558  N  N   . GLU   A 1 1072 ? -25.24800  60.98500  -16.39200 1.000 38.29095  ?  1070 GLU   A N   1 
ATOM   8559  C  CA  . GLU   A 1 1072 ? -23.87400  61.17900  -16.83400 1.000 51.08396  ?  1070 GLU   A CA  1 
ATOM   8560  C  C   . GLU   A 1 1072 ? -23.52200  62.64400  -17.04800 1.000 51.74472  ?  1070 GLU   A C   1 
ATOM   8561  O  O   . GLU   A 1 1072 ? -22.34000  62.96000  -17.22800 1.000 51.39412  ?  1070 GLU   A O   1 
ATOM   8562  C  CB  . GLU   A 1 1072 ? -23.61900  60.39400  -18.12300 1.000 35.86815  ?  1070 GLU   A CB  1 
ATOM   8563  C  CG  . GLU   A 1 1072 ? -24.02100  58.92800  -18.04500 1.000 56.93744  ?  1070 GLU   A CG  1 
ATOM   8564  C  CD  . GLU   A 1 1072 ? -23.00100  58.08200  -17.30500 1.000 61.66987  ?  1070 GLU   A CD  1 
ATOM   8565  O  OE1 . GLU   A 1 1072 ? -21.80400  58.44100  -17.32900 1.000 56.40736  ?  1070 GLU   A OE1 1 
ATOM   8566  O  OE2 . GLU   A 1 1072 ? -23.39500  57.06100  -16.70000 1.000 67.12654  -1 1070 GLU   A OE2 1 
ATOM   8567  N  N   . GLU   A 1 1073 ? -24.50400  63.53700  -17.02600 1.000 49.28311  ?  1071 GLU   A N   1 
ATOM   8568  C  CA  . GLU   A 1 1073 ? -24.28700  64.96400  -17.19200 1.000 38.44400  ?  1071 GLU   A CA  1 
ATOM   8569  C  C   . GLU   A 1 1073 ? -24.46100  65.67400  -15.85200 1.000 44.61557  ?  1071 GLU   A C   1 
ATOM   8570  O  O   . GLU   A 1 1073 ? -24.80200  65.06500  -14.83400 1.000 46.12667  ?  1071 GLU   A O   1 
ATOM   8571  C  CB  . GLU   A 1 1073 ? -25.23000  65.52700  -18.25500 1.000 39.14185  ?  1071 GLU   A CB  1 
ATOM   8572  C  CG  . GLU   A 1 1073 ? -24.81100  65.18600  -19.67600 1.000 43.88560  ?  1071 GLU   A CG  1 
ATOM   8573  C  CD  . GLU   A 1 1073 ? -23.50600  65.85600  -20.07600 1.000 66.36145  ?  1071 GLU   A CD  1 
ATOM   8574  O  OE1 . GLU   A 1 1073 ? -23.18900  66.93200  -19.52400 1.000 59.79016  ?  1071 GLU   A OE1 1 
ATOM   8575  O  OE2 . GLU   A 1 1073 ? -22.79700  65.30500  -20.94500 1.000 69.70036  -1 1071 GLU   A OE2 1 
ATOM   8576  N  N   . SER   A 1 1074 ? -24.22000  66.98100  -15.86100 1.000 53.10200  ?  1072 SER   A N   1 
ATOM   8577  C  CA  . SER   A 1 1074 ? -24.21900  67.76400  -14.63600 1.000 44.00072  ?  1072 SER   A CA  1 
ATOM   8578  C  C   . SER   A 1 1074 ? -25.63700  68.16700  -14.23700 1.000 49.99733  ?  1072 SER   A C   1 
ATOM   8579  O  O   . SER   A 1 1074 ? -26.60100  68.01500  -14.99400 1.000 45.36499  ?  1072 SER   A O   1 
ATOM   8580  C  CB  . SER   A 1 1074 ? -23.35400  69.00800  -14.80300 1.000 35.02051  ?  1072 SER   A CB  1 
ATOM   8581  O  OG  . SER   A 1 1074 ? -23.79800  69.77300  -15.91000 1.000 46.13042  ?  1072 SER   A OG  1 
ATOM   8582  N  N   . PHE   A 1 1075 ? -25.75100  68.69300  -13.01400 1.000 37.40929  ?  1073 PHE   A N   1 
ATOM   8583  C  CA  . PHE   A 1 1075 ? -27.02200  69.24200  -12.55700 1.000 42.53001  ?  1073 PHE   A CA  1 
ATOM   8584  C  C   . PHE   A 1 1075 ? -27.46400  70.39500  -13.44800 1.000 47.09650  ?  1073 PHE   A C   1 
ATOM   8585  O  O   . PHE   A 1 1075 ? -28.64300  70.49500  -13.80900 1.000 46.63196  ?  1073 PHE   A O   1 
ATOM   8586  C  CB  . PHE   A 1 1075 ? -26.89600  69.69500  -11.09900 1.000 42.49629  ?  1073 PHE   A CB  1 
ATOM   8587  C  CG  . PHE   A 1 1075 ? -28.18600  70.17400  -10.49100 1.000 37.65397  ?  1073 PHE   A CG  1 
ATOM   8588  C  CD1 . PHE   A 1 1075 ? -29.33900  69.41100  -10.57800 1.000 33.79500  ?  1073 PHE   A CD1 1 
ATOM   8589  C  CD2 . PHE   A 1 1075 ? -28.24100  71.38800  -9.82500  1.000 36.65424  ?  1073 PHE   A CD2 1 
ATOM   8590  C  CE1 . PHE   A 1 1075 ? -30.52400  69.85300  -10.01700 1.000 36.42159  ?  1073 PHE   A CE1 1 
ATOM   8591  C  CE2 . PHE   A 1 1075 ? -29.42300  71.83500  -9.26300  1.000 36.77709  ?  1073 PHE   A CE2 1 
ATOM   8592  C  CZ  . PHE   A 1 1075 ? -30.56600  71.06600  -9.35900  1.000 39.31205  ?  1073 PHE   A CZ  1 
ATOM   8593  N  N   . LEU   A 1 1076 ? -26.52400  71.26200  -13.83400 1.000 38.79955  ?  1074 LEU   A N   1 
ATOM   8594  C  CA  . LEU   A 1 1076 ? -26.85800  72.38600  -14.70100 1.000 35.95500  ?  1074 LEU   A CA  1 
ATOM   8595  C  C   . LEU   A 1 1076 ? -27.37400  71.91200  -16.05200 1.000 36.61587  ?  1074 LEU   A C   1 
ATOM   8596  O  O   . LEU   A 1 1076 ? -28.26800  72.53600  -16.63400 1.000 51.02097  ?  1074 LEU   A O   1 
ATOM   8597  C  CB  . LEU   A 1 1076 ? -25.63900  73.29000  -14.87800 1.000 39.23319  ?  1074 LEU   A CB  1 
ATOM   8598  C  CG  . LEU   A 1 1076 ? -25.35600  74.19000  -13.67500 1.000 64.13500  ?  1074 LEU   A CG  1 
ATOM   8599  C  CD1 . LEU   A 1 1076 ? -24.25100  75.18300  -13.97900 1.000 61.45051  ?  1074 LEU   A CD1 1 
ATOM   8600  C  CD2 . LEU   A 1 1076 ? -26.63000  74.91900  -13.28600 1.000 69.39157  ?  1074 LEU   A CD2 1 
ATOM   8601  N  N   . HIS   A 1 1077 ? -26.82600  70.81100  -16.56700 1.000 31.65873  ?  1075 HIS   A N   1 
ATOM   8602  C  CA  . HIS   A 1 1077 ? -27.31600  70.27200  -17.83000 1.000 45.31352  ?  1075 HIS   A CA  1 
ATOM   8603  C  C   . HIS   A 1 1077 ? -28.74500  69.76600  -17.68600 1.000 50.09580  ?  1075 HIS   A C   1 
ATOM   8604  O  O   . HIS   A 1 1077 ? -29.61600  70.08500  -18.50500 1.000 41.73175  ?  1075 HIS   A O   1 
ATOM   8605  C  CB  . HIS   A 1 1077 ? -26.39500  69.15500  -18.32200 1.000 32.52606  ?  1075 HIS   A CB  1 
ATOM   8606  C  CG  . HIS   A 1 1077 ? -26.79100  68.59400  -19.65100 1.000 43.15833  ?  1075 HIS   A CG  1 
ATOM   8607  N  ND1 . HIS   A 1 1077 ? -26.26000  69.04700  -20.84000 1.000 41.40297  ?  1075 HIS   A ND1 1 
ATOM   8608  C  CD2 . HIS   A 1 1077 ? -27.68500  67.63100  -19.98000 1.000 42.00897  ?  1075 HIS   A CD2 1 
ATOM   8609  C  CE1 . HIS   A 1 1077 ? -26.80200  68.37900  -21.84300 1.000 55.07318  ?  1075 HIS   A CE1 1 
ATOM   8610  N  NE2 . HIS   A 1 1077 ? -27.67100  67.51500  -21.34800 1.000 49.46223  ?  1075 HIS   A NE2 1 
ATOM   8611  N  N   . ASN   A 1 1078 ? -29.00600  68.97900  -16.63800 1.000 46.60165  ?  1076 ASN   A N   1 
ATOM   8612  C  CA  . ASN   A 1 1078 ? -30.34900  68.45300  -16.42600 1.000 48.71279  ?  1076 ASN   A CA  1 
ATOM   8613  C  C   . ASN   A 1 1078 ? -31.35000  69.57800  -16.19900 1.000 39.54353  ?  1076 ASN   A C   1 
ATOM   8614  O  O   . ASN   A 1 1078 ? -32.50500  69.48400  -16.63000 1.000 35.97300  ?  1076 ASN   A O   1 
ATOM   8615  C  CB  . ASN   A 1 1078 ? -30.34900  67.47800  -15.25000 1.000 46.43244  ?  1076 ASN   A CB  1 
ATOM   8616  C  CG  . ASN   A 1 1078 ? -29.70100  66.15200  -15.59800 1.000 39.16505  ?  1076 ASN   A CG  1 
ATOM   8617  O  OD1 . ASN   A 1 1078 ? -30.38600  65.15600  -15.82900 1.000 49.31213  ?  1076 ASN   A OD1 1 
ATOM   8618  N  ND2 . ASN   A 1 1078 ? -28.37300  66.13300  -15.63300 1.000 39.37666  ?  1076 ASN   A ND2 1 
ATOM   8619  N  N   . LEU   A 1 1079 ? -30.91900  70.65800  -15.54100 1.000 41.78144  ?  1077 LEU   A N   1 
ATOM   8620  C  CA  . LEU   A 1 1079 ? -31.80400  71.79600  -15.31000 1.000 38.94710  ?  1077 LEU   A CA  1 
ATOM   8621  C  C   . LEU   A 1 1079 ? -32.34800  72.34300  -16.62300 1.000 44.28299  ?  1077 LEU   A C   1 
ATOM   8622  O  O   . LEU   A 1 1079 ? -33.55100  72.60000  -16.75200 1.000 51.77345  ?  1077 LEU   A O   1 
ATOM   8623  C  CB  . LEU   A 1 1079 ? -31.06400  72.89000  -14.54300 1.000 30.63468  ?  1077 LEU   A CB  1 
ATOM   8624  C  CG  . LEU   A 1 1079 ? -31.05200  72.75800  -13.02000 1.000 38.44421  ?  1077 LEU   A CG  1 
ATOM   8625  C  CD1 . LEU   A 1 1079 ? -29.90000  73.54400  -12.44200 1.000 33.09589  ?  1077 LEU   A CD1 1 
ATOM   8626  C  CD2 . LEU   A 1 1079 ? -32.35900  73.22700  -12.42000 1.000 40.64885  ?  1077 LEU   A CD2 1 
ATOM   8627  N  N   . GLN   A 1 1080 ? -31.47100  72.52300  -17.61500 1.000 36.84618  ?  1078 GLN   A N   1 
ATOM   8628  C  CA  . GLN   A 1 1080 ? -31.91900  73.01900  -18.91200 1.000 40.41354  ?  1078 GLN   A CA  1 
ATOM   8629  C  C   . GLN   A 1 1080 ? -32.81100  72.01400  -19.62600 1.000 44.79840  ?  1078 GLN   A C   1 
ATOM   8630  O  O   . GLN   A 1 1080 ? -33.73200  72.41100  -20.35100 1.000 48.89556  ?  1078 GLN   A O   1 
ATOM   8631  C  CB  . GLN   A 1 1080 ? -30.71700  73.36700  -19.78800 1.000 36.69931  ?  1078 GLN   A CB  1 
ATOM   8632  C  CG  . GLN   A 1 1080 ? -29.59000  74.05400  -19.04700 1.000 43.71003  ?  1078 GLN   A CG  1 
ATOM   8633  C  CD  . GLN   A 1 1080 ? -29.99800  75.40800  -18.49100 1.000 61.94203  ?  1078 GLN   A CD  1 
ATOM   8634  O  OE1 . GLN   A 1 1080 ? -30.58100  76.23600  -19.19400 1.000 56.36090  ?  1078 GLN   A OE1 1 
ATOM   8635  N  NE2 . GLN   A 1 1080 ? -29.68800  75.64100  -17.22000 1.000 54.42041  ?  1078 GLN   A NE2 1 
ATOM   8636  N  N   . GLN   A 1 1081 ? -32.55500  70.71700  -19.44400 1.000 38.23782  ?  1079 GLN   A N   1 
ATOM   8637  C  CA  . GLN   A 1 1081 ? -33.39600  69.70800  -20.07600 1.000 44.33042  ?  1079 GLN   A CA  1 
ATOM   8638  C  C   . GLN   A 1 1081 ? -34.81700  69.76000  -19.53100 1.000 45.60280  ?  1079 GLN   A C   1 
ATOM   8639  O  O   . GLN   A 1 1081 ? -35.78600  69.66700  -20.29500 1.000 44.24151  ?  1079 GLN   A O   1 
ATOM   8640  C  CB  . GLN   A 1 1081 ? -32.79100  68.32000  -19.87200 1.000 56.97916  ?  1079 GLN   A CB  1 
ATOM   8641  C  CG  . GLN   A 1 1081 ? -31.49000  68.08900  -20.62600 1.000 59.51216  ?  1079 GLN   A CG  1 
ATOM   8642  C  CD  . GLN   A 1 1081 ? -31.46900  68.76500  -21.98400 1.000 73.26335  ?  1079 GLN   A CD  1 
ATOM   8643  O  OE1 . GLN   A 1 1081 ? -30.62800  69.62600  -22.25100 1.000 58.98652  ?  1079 GLN   A OE1 1 
ATOM   8644  N  NE2 . GLN   A 1 1081 ? -32.38900  68.36900  -22.85700 1.000 73.31542  ?  1079 GLN   A NE2 1 
ATOM   8645  N  N   . VAL   A 1 1082 ? -34.95900  69.91000  -18.21100 1.000 34.05556  ?  1080 VAL   A N   1 
ATOM   8646  C  CA  . VAL   A 1 1082 ? -36.28800  69.99900  -17.61300 1.000 43.33513  ?  1080 VAL   A CA  1 
ATOM   8647  C  C   . VAL   A 1 1082 ? -37.02900  71.21600  -18.15400 1.000 40.22587  ?  1080 VAL   A C   1 
ATOM   8648  O  O   . VAL   A 1 1082 ? -38.22900  71.15000  -18.45400 1.000 40.88206  ?  1080 VAL   A O   1 
ATOM   8649  C  CB  . VAL   A 1 1082 ? -36.18400  70.02300  -16.07600 1.000 32.32152  ?  1080 VAL   A CB  1 
ATOM   8650  C  CG1 . VAL   A 1 1082 ? -37.56200  69.97600  -15.44800 1.000 47.18961  ?  1080 VAL   A CG1 1 
ATOM   8651  C  CG2 . VAL   A 1 1082 ? -35.37300  68.84400  -15.59000 1.000 33.20288  ?  1080 VAL   A CG2 1 
ATOM   8652  N  N   . LYS   A 1 1083 ? -36.32400  72.33800  -18.30900 1.000 30.52453  ?  1081 LYS   A N   1 
ATOM   8653  C  CA  . LYS   A 1 1083 ? -36.95600  73.53200  -18.86300 1.000 42.62569  ?  1081 LYS   A CA  1 
ATOM   8654  C  C   . LYS   A 1 1083 ? -37.34200  73.33000  -20.32100 1.000 34.97595  ?  1081 LYS   A C   1 
ATOM   8655  O  O   . LYS   A 1 1083 ? -38.42300  73.75300  -20.74900 1.000 40.61869  ?  1081 LYS   A O   1 
ATOM   8656  C  CB  . LYS   A 1 1083 ? -36.02700  74.73500  -18.72600 1.000 27.76090  ?  1081 LYS   A CB  1 
ATOM   8657  C  CG  . LYS   A 1 1083 ? -36.53300  75.95200  -19.46900 1.000 33.19272  ?  1081 LYS   A CG  1 
ATOM   8658  C  CD  . LYS   A 1 1083 ? -35.73500  77.18800  -19.12600 1.000 32.63278  ?  1081 LYS   A CD  1 
ATOM   8659  C  CE  . LYS   A 1 1083 ? -34.26400  76.98700  -19.41100 1.000 24.11022  ?  1081 LYS   A CE  1 
ATOM   8660  N  NZ  . LYS   A 1 1083 ? -33.47800  78.18400  -19.01100 1.000 44.76464  ?  1081 LYS   A NZ  1 
ATOM   8661  N  N   . ALA   A 1 1084 ? -36.46900  72.68400  -21.09800 1.000 34.71906  ?  1082 ALA   A N   1 
ATOM   8662  C  CA  . ALA   A 1 1084 ? -36.75600  72.41600  -22.50100 1.000 33.08862  ?  1082 ALA   A CA  1 
ATOM   8663  C  C   . ALA   A 1 1084 ? -37.96200  71.50500  -22.68100 1.000 40.92461  ?  1082 ALA   A C   1 
ATOM   8664  O  O   . ALA   A 1 1084 ? -38.51100  71.43400  -23.78600 1.000 43.92719  ?  1082 ALA   A O   1 
ATOM   8665  C  CB  . ALA   A 1 1084 ? -35.53100  71.79800  -23.17100 1.000 25.55293  ?  1082 ALA   A CB  1 
ATOM   8666  N  N   . LYS   A 1 1085 ? -38.37400  70.79600  -21.63200 1.000 40.12231  ?  1083 LYS   A N   1 
ATOM   8667  C  CA  . LYS   A 1 1085 ? -39.58200  69.98700  -21.68000 1.000 41.32000  ?  1083 LYS   A CA  1 
ATOM   8668  C  C   . LYS   A 1 1085 ? -40.75000  70.63200  -20.94900 1.000 36.13818  ?  1083 LYS   A C   1 
ATOM   8669  O  O   . LYS   A 1 1085 ? -41.90300  70.29500  -21.23800 1.000 47.32274  ?  1083 LYS   A O   1 
ATOM   8670  C  CB  . LYS   A 1 1085 ? -39.30800  68.59700  -21.09100 1.000 41.35872  ?  1083 LYS   A CB  1 
ATOM   8671  C  CG  . LYS   A 1 1085 ? -38.15200  67.86800  -21.76800 1.000 38.10900  ?  1083 LYS   A CG  1 
ATOM   8672  C  CD  . LYS   A 1 1085 ? -37.89100  66.50100  -21.14600 1.000 63.33362  ?  1083 LYS   A CD  1 
ATOM   8673  C  CE  . LYS   A 1 1085 ? -36.45200  66.37100  -20.64200 1.000 66.36104  ?  1083 LYS   A CE  1 
ATOM   8674  N  NZ  . LYS   A 1 1085 ? -36.25700  66.87400  -19.24900 1.000 48.80519  ?  1083 LYS   A NZ  1 
ATOM   8675  N  N   . LEU   A 1 1086 ? -40.47900  71.55600  -20.02700 1.000 32.77401  ?  1084 LEU   A N   1 
ATOM   8676  C  CA  . LEU   A 1 1086 ? -41.55300  72.22000  -19.30000 1.000 41.86919  ?  1084 LEU   A CA  1 
ATOM   8677  C  C   . LEU   A 1 1086 ? -42.18900  73.32600  -20.13000 1.000 38.95027  ?  1084 LEU   A C   1 
ATOM   8678  O  O   . LEU   A 1 1086 ? -43.41900  73.44900  -20.16500 1.000 46.44741  ?  1084 LEU   A O   1 
ATOM   8679  C  CB  . LEU   A 1 1086 ? -41.02400  72.78100  -17.98000 1.000 33.75544  ?  1084 LEU   A CB  1 
ATOM   8680  C  CG  . LEU   A 1 1086 ? -41.98400  73.67700  -17.19400 1.000 38.33540  ?  1084 LEU   A CG  1 
ATOM   8681  C  CD1 . LEU   A 1 1086 ? -43.11000  72.86200  -16.56900 1.000 29.20697  ?  1084 LEU   A CD1 1 
ATOM   8682  C  CD2 . LEU   A 1 1086 ? -41.22700  74.45300  -16.13000 1.000 29.85102  ?  1084 LEU   A CD2 1 
ATOM   8683  N  N   . LEU   A 1 1087 ? -41.37100  74.13700  -20.79800 1.000 34.05307  ?  1085 LEU   A N   1 
ATOM   8684  C  CA  . LEU   A 1 1087 ? -41.91000  75.24300  -21.58500 1.000 39.10895  ?  1085 LEU   A CA  1 
ATOM   8685  C  C   . LEU   A 1 1087 ? -42.83900  74.78700  -22.70700 1.000 42.40402  ?  1085 LEU   A C   1 
ATOM   8686  O  O   . LEU   A 1 1087 ? -43.89800  75.41600  -22.88200 1.000 39.34282  ?  1085 LEU   A O   1 
ATOM   8687  C  CB  . LEU   A 1 1087 ? -40.75600  76.09800  -22.12800 1.000 22.17843  ?  1085 LEU   A CB  1 
ATOM   8688  C  CG  . LEU   A 1 1087 ? -39.86300  76.76000  -21.07600 1.000 29.36717  ?  1085 LEU   A CG  1 
ATOM   8689  C  CD1 . LEU   A 1 1087 ? -38.99000  77.82300  -21.70600 1.000 35.68793  ?  1085 LEU   A CD1 1 
ATOM   8690  C  CD2 . LEU   A 1 1087 ? -40.70400  77.36900  -19.97400 1.000 36.93443  ?  1085 LEU   A CD2 1 
ATOM   8691  N  N   . PRO   A 1 1088 ? -42.53300  73.74300  -23.48600 1.000 35.70586  ?  1086 PRO   A N   1 
ATOM   8692  C  CA  . PRO   A 1 1088 ? -43.52500  73.27900  -24.46800 1.000 41.03861  ?  1086 PRO   A CA  1 
ATOM   8693  C  C   . PRO   A 1 1088 ? -44.81300  72.79900  -23.82600 1.000 40.15167  ?  1086 PRO   A C   1 
ATOM   8694  O  O   . PRO   A 1 1088 ? -45.88400  72.93700  -24.43100 1.000 47.58714  ?  1086 PRO   A O   1 
ATOM   8695  C  CB  . PRO   A 1 1088 ? -42.79400  72.14300  -25.19900 1.000 28.82902  ?  1086 PRO   A CB  1 
ATOM   8696  C  CG  . PRO   A 1 1088 ? -41.68600  71.74600  -24.28600 1.000 39.97734  ?  1086 PRO   A CG  1 
ATOM   8697  C  CD  . PRO   A 1 1088 ? -41.26600  73.00500  -23.61500 1.000 40.56373  ?  1086 PRO   A CD  1 
ATOM   8698  N  N   . ALA   A 1 1089 ? -44.74600  72.24800  -22.61200 1.000 37.90901  ?  1087 ALA   A N   1 
ATOM   8699  C  CA  . ALA   A 1 1089 ? -45.96200  71.80500  -21.93800 1.000 46.67417  ?  1087 ALA   A CA  1 
ATOM   8700  C  C   . ALA   A 1 1089 ? -46.79100  72.99100  -21.46100 1.000 44.91848  ?  1087 ALA   A C   1 
ATOM   8701  O  O   . ALA   A 1 1089 ? -48.02400  72.97300  -21.55500 1.000 52.28900  ?  1087 ALA   A O   1 
ATOM   8702  C  CB  . ALA   A 1 1089 ? -45.61200  70.88300  -20.77000 1.000 30.20975  ?  1087 ALA   A CB  1 
ATOM   8703  N  N   . LEU   A 1 1090 ? -46.13300  74.03400  -20.94900 1.000 38.76509  ?  1088 LEU   A N   1 
ATOM   8704  C  CA  . LEU   A 1 1090 ? -46.84900  75.24100  -20.55800 1.000 39.64068  ?  1088 LEU   A CA  1 
ATOM   8705  C  C   . LEU   A 1 1090 ? -47.43900  75.97400  -21.75600 1.000 45.26422  ?  1088 LEU   A C   1 
ATOM   8706  O  O   . LEU   A 1 1090 ? -48.41200  76.71600  -21.59200 1.000 51.95968  ?  1088 LEU   A O   1 
ATOM   8707  C  CB  . LEU   A 1 1090 ? -45.92200  76.17500  -19.77900 1.000 33.68625  ?  1088 LEU   A CB  1 
ATOM   8708  C  CG  . LEU   A 1 1090 ? -45.40800  75.60800  -18.45600 1.000 41.50688  ?  1088 LEU   A CG  1 
ATOM   8709  C  CD1 . LEU   A 1 1090 ? -44.57400  76.63900  -17.71100 1.000 39.00417  ?  1088 LEU   A CD1 1 
ATOM   8710  C  CD2 . LEU   A 1 1090 ? -46.56900  75.12400  -17.59800 1.000 47.34271  ?  1088 LEU   A CD2 1 
ATOM   8711  N  N   . GLN   A 1 1091 ? -46.87500  75.78600  -22.95200 1.000 50.60681  ?  1089 GLN   A N   1 
ATOM   8712  C  CA  . GLN   A 1 1091 ? -47.45400  76.38500  -24.14900 1.000 50.42013  ?  1089 GLN   A CA  1 
ATOM   8713  C  C   . GLN   A 1 1091 ? -48.73900  75.68900  -24.57000 1.000 43.79931  ?  1089 GLN   A C   1 
ATOM   8714  O  O   . GLN   A 1 1091 ? -49.51700  76.26100  -25.33900 1.000 55.63604  ?  1089 GLN   A O   1 
ATOM   8715  C  CB  . GLN   A 1 1091 ? -46.44800  76.35800  -25.30100 1.000 55.72243  ?  1089 GLN   A CB  1 
ATOM   8716  C  CG  . GLN   A 1 1091 ? -46.56700  77.53700  -26.26100 1.000 69.19121  ?  1089 GLN   A CG  1 
ATOM   8717  C  CD  . GLN   A 1 1091 ? -46.01600  78.82700  -25.67600 1.000 84.71765  ?  1089 GLN   A CD  1 
ATOM   8718  O  OE1 . GLN   A 1 1091 ? -44.95000  78.83700  -25.05900 1.000 74.25832  ?  1089 GLN   A OE1 1 
ATOM   8719  N  NE2 . GLN   A 1 1091 ? -46.74000  79.92600  -25.87300 1.000 60.95136  ?  1089 GLN   A NE2 1 
ATOM   8720  N  N   . ASN   A 1 1092 ? -48.97100  74.47300  -24.08800 1.000 40.53740  ?  1090 ASN   A N   1 
ATOM   8721  C  CA  . ASN   A 1 1092 ? -50.19400  73.72300  -24.34100 1.000 50.84655  ?  1090 ASN   A CA  1 
ATOM   8722  C  C   . ASN   A 1 1092 ? -50.87100  73.35300  -23.02700 1.000 45.27413  ?  1090 ASN   A C   1 
ATOM   8723  O  O   . ASN   A 1 1092 ? -51.40100  72.25200  -22.86500 1.000 35.94044  ?  1090 ASN   A O   1 
ATOM   8724  C  CB  . ASN   A 1 1092 ? -49.90300  72.47500  -25.17200 1.000 45.79374  ?  1090 ASN   A CB  1 
ATOM   8725  C  CG  . ASN   A 1 1092 ? -49.04200  72.77000  -26.38400 1.000 47.50339  ?  1090 ASN   A CG  1 
ATOM   8726  O  OD1 . ASN   A 1 1092 ? -49.53900  73.20100  -27.42500 1.000 47.07354  ?  1090 ASN   A OD1 1 
ATOM   8727  N  ND2 . ASN   A 1 1092 ? -47.74100  72.54000  -26.25500 1.000 42.57726  ?  1090 ASN   A ND2 1 
ATOM   8728  N  N   . GLN   A 1 1093 ? -50.85900  74.28400  -22.07300 1.000 42.54522  ?  1091 GLN   A N   1 
ATOM   8729  C  CA  . GLN   A 1 1093 ? -51.33300  74.03500  -20.71700 1.000 47.22439  ?  1091 GLN   A CA  1 
ATOM   8730  C  C   . GLN   A 1 1093 ? -52.84000  74.18000  -20.56300 1.000 55.37149  ?  1091 GLN   A C   1 
ATOM   8731  O  O   . GLN   A 1 1093 ? -53.36000  73.92500  -19.47200 1.000 57.36059  ?  1091 GLN   A O   1 
ATOM   8732  C  CB  . GLN   A 1 1093 ? -50.63900  74.98700  -19.74300 1.000 43.91897  ?  1091 GLN   A CB  1 
ATOM   8733  C  CG  . GLN   A 1 1093 ? -51.13200  76.42200  -19.83200 1.000 37.69550  ?  1091 GLN   A CG  1 
ATOM   8734  C  CD  . GLN   A 1 1093 ? -50.83600  77.21500  -18.57400 1.000 58.07196  ?  1091 GLN   A CD  1 
ATOM   8735  O  OE1 . GLN   A 1 1093 ? -51.64900  77.25900  -17.64800 1.000 55.79266  ?  1091 GLN   A OE1 1 
ATOM   8736  N  NE2 . GLN   A 1 1093 ? -49.66600  77.84500  -18.53300 1.000 37.69985  ?  1091 GLN   A NE2 1 
ATOM   8737  N  N   . TYR   A 1 1094 ? -53.55600  74.58300  -21.61100 1.000 52.39087  ?  1092 TYR   A N   1 
ATOM   8738  C  CA  . TYR   A 1 1094 ? -54.97500  74.88300  -21.49600 1.000 46.13047  ?  1092 TYR   A CA  1 
ATOM   8739  C  C   . TYR   A 1 1094 ? -55.85300  73.80400  -22.11800 1.000 45.74927  ?  1092 TYR   A C   1 
ATOM   8740  O  O   . TYR   A 1 1094 ? -56.99800  74.07600  -22.49200 1.000 52.87851  ?  1092 TYR   A O   1 
ATOM   8741  C  CB  . TYR   A 1 1094 ? -55.26600  76.25300  -22.10700 1.000 38.76011  ?  1092 TYR   A CB  1 
ATOM   8742  C  CG  . TYR   A 1 1094 ? -54.63800  77.37700  -21.31400 1.000 41.05798  ?  1092 TYR   A CG  1 
ATOM   8743  C  CD1 . TYR   A 1 1094 ? -55.01500  77.61300  -19.99900 1.000 46.60429  ?  1092 TYR   A CD1 1 
ATOM   8744  C  CD2 . TYR   A 1 1094 ? -53.65100  78.18100  -21.86700 1.000 37.81006  ?  1092 TYR   A CD2 1 
ATOM   8745  C  CE1 . TYR   A 1 1094 ? -54.44200  78.63200  -19.26100 1.000 47.58500  ?  1092 TYR   A CE1 1 
ATOM   8746  C  CE2 . TYR   A 1 1094 ? -53.06900  79.20500  -21.13400 1.000 38.37582  ?  1092 TYR   A CE2 1 
ATOM   8747  C  CZ  . TYR   A 1 1094 ? -53.47000  79.42400  -19.83100 1.000 43.48773  ?  1092 TYR   A CZ  1 
ATOM   8748  O  OH  . TYR   A 1 1094 ? -52.90300  80.43600  -19.08800 1.000 52.09020  ?  1092 TYR   A OH  1 
ATOM   8749  N  N   . VAL   A 1 1095 ? -55.34400  72.58700  -22.22600 1.000 43.93862  ?  1093 VAL   A N   1 
ATOM   8750  C  CA  . VAL   A 1 1095 ? -56.14600  71.41900  -22.58100 1.000 45.12142  ?  1093 VAL   A CA  1 
ATOM   8751  C  C   . VAL   A 1 1095 ? -56.54400  70.71600  -21.28800 1.000 49.79255  ?  1093 VAL   A C   1 
ATOM   8752  O  O   . VAL   A 1 1095 ? -55.66400  70.41800  -20.46800 1.000 65.12456  ?  1093 VAL   A O   1 
ATOM   8753  C  CB  . VAL   A 1 1095 ? -55.37900  70.46100  -23.50600 1.000 43.09517  ?  1093 VAL   A CB  1 
ATOM   8754  C  CG1 . VAL   A 1 1095 ? -56.22900  69.24200  -23.81300 1.000 49.66099  ?  1093 VAL   A CG1 1 
ATOM   8755  C  CG2 . VAL   A 1 1095 ? -54.97600  71.17600  -24.78400 1.000 55.36742  ?  1093 VAL   A CG2 1 
ATOM   8756  N  N   . PRO   A 1 1096 ? -57.82800  70.45100  -21.06100 1.000 49.82932  ?  1094 PRO   A N   1 
ATOM   8757  C  CA  . PRO   A 1 1096 ? -58.23000  69.80200  -19.80900 1.000 53.41494  ?  1094 PRO   A CA  1 
ATOM   8758  C  C   . PRO   A 1 1096 ? -57.61700  68.41600  -19.67700 1.000 56.01709  ?  1094 PRO   A C   1 
ATOM   8759  O  O   . PRO   A 1 1096 ? -57.34900  67.73200  -20.66800 1.000 58.55962  ?  1094 PRO   A O   1 
ATOM   8760  C  CB  . PRO   A 1 1096 ? -59.75800  69.73500  -19.91600 1.000 59.78379  ?  1094 PRO   A CB  1 
ATOM   8761  C  CG  . PRO   A 1 1096 ? -60.11900  70.78200  -20.91500 1.000 63.54772  ?  1094 PRO   A CG  1 
ATOM   8762  C  CD  . PRO   A 1 1096 ? -58.98500  70.81900  -21.89200 1.000 69.69457  ?  1094 PRO   A CD  1 
ATOM   8763  N  N   . PHE   A 1 1097 ? -57.40000  68.00600  -18.42400 1.000 56.49125  ?  1095 PHE   A N   1 
ATOM   8764  C  CA  . PHE   A 1 1097 ? -56.65400  66.77900  -18.16100 1.000 55.92900  ?  1095 PHE   A CA  1 
ATOM   8765  C  C   . PHE   A 1 1097 ? -57.38900  65.55200  -18.68400 1.000 60.30962  ?  1095 PHE   A C   1 
ATOM   8766  O  O   . PHE   A 1 1097 ? -56.76000  64.62500  -19.21000 1.000 59.84108  ?  1095 PHE   A O   1 
ATOM   8767  C  CB  . PHE   A 1 1097 ? -56.37900  66.63900  -16.66300 1.000 60.11654  ?  1095 PHE   A CB  1 
ATOM   8768  C  CG  . PHE   A 1 1097 ? -55.48400  65.47900  -16.31500 1.000 54.70426  ?  1095 PHE   A CG  1 
ATOM   8769  C  CD1 . PHE   A 1 1097 ? -54.22700  65.35800  -16.88600 1.000 48.68736  ?  1095 PHE   A CD1 1 
ATOM   8770  C  CD2 . PHE   A 1 1097 ? -55.90300  64.50800  -15.42000 1.000 50.51842  ?  1095 PHE   A CD2 1 
ATOM   8771  C  CE1 . PHE   A 1 1097 ? -53.40300  64.29100  -16.56600 1.000 48.66301  ?  1095 PHE   A CE1 1 
ATOM   8772  C  CE2 . PHE   A 1 1097 ? -55.08400  63.44000  -15.09600 1.000 48.98815  ?  1095 PHE   A CE2 1 
ATOM   8773  C  CZ  . PHE   A 1 1097 ? -53.83300  63.33100  -15.67100 1.000 41.58269  ?  1095 PHE   A CZ  1 
ATOM   8774  N  N   . ASP   A 1 1098 ? -58.71900  65.52200  -18.54200 1.000 70.15913  ?  1096 ASP   A N   1 
ATOM   8775  C  CA  . ASP   A 1 1098 ? -59.49200  64.38900  -19.04400 1.000 69.48531  ?  1096 ASP   A CA  1 
ATOM   8776  C  C   . ASP   A 1 1098 ? -59.34100  64.23600  -20.55200 1.000 66.76471  ?  1096 ASP   A C   1 
ATOM   8777  O  O   . ASP   A 1 1098 ? -59.32500  63.11000  -21.06500 1.000 58.30231  ?  1096 ASP   A O   1 
ATOM   8778  C  CB  . ASP   A 1 1098 ? -60.97000  64.53800  -18.66000 1.000 54.50125  ?  1096 ASP   A CB  1 
ATOM   8779  C  CG  . ASP   A 1 1098 ? -61.46900  65.96700  -18.79000 1.000 73.55182  ?  1096 ASP   A CG  1 
ATOM   8780  O  OD1 . ASP   A 1 1098 ? -60.70100  66.81800  -19.28100 1.000 84.07164  ?  1096 ASP   A OD1 1 
ATOM   8781  O  OD2 . ASP   A 1 1098 ? -62.62700  66.24200  -18.40300 1.000 61.22177  -1 1096 ASP   A OD2 1 
ATOM   8782  N  N   . LYS   A 1 1099 ? -59.21400  65.35100  -21.27400 1.000 57.12745  ?  1097 LYS   A N   1 
ATOM   8783  C  CA  . LYS   A 1 1099 ? -59.00000  65.27600  -22.71400 1.000 51.36936  ?  1097 LYS   A CA  1 
ATOM   8784  C  C   . LYS   A 1 1099 ? -57.58200  64.82600  -23.03400 1.000 60.00868  ?  1097 LYS   A C   1 
ATOM   8785  O  O   . LYS   A 1 1099 ? -57.36000  64.10200  -24.01100 1.000 71.07177  ?  1097 LYS   A O   1 
ATOM   8786  C  CB  . LYS   A 1 1099 ? -59.29700  66.63000  -23.35500 1.000 62.69411  ?  1097 LYS   A CB  1 
ATOM   8787  C  CG  . LYS   A 1 1099 ? -60.61100  67.25100  -22.90200 1.000 67.44227  ?  1097 LYS   A CG  1 
ATOM   8788  C  CD  . LYS   A 1 1099 ? -61.78900  66.32900  -23.20100 1.000 80.34852  ?  1097 LYS   A CD  1 
ATOM   8789  C  CE  . LYS   A 1 1099 ? -63.12500  67.03800  -23.01200 1.000 67.58956  ?  1097 LYS   A CE  1 
ATOM   8790  N  NZ  . LYS   A 1 1099 ? -64.24100  66.32100  -23.69400 1.000 49.42281  ?  1097 LYS   A NZ  1 
ATOM   8791  N  N   . ILE   A 1 1100 ? -56.60900  65.24900  -22.22400 1.000 54.64302  ?  1098 ILE   A N   1 
ATOM   8792  C  CA  . ILE   A 1 1100 ? -55.23600  64.78600  -22.40700 1.000 51.36758  ?  1098 ILE   A CA  1 
ATOM   8793  C  C   . ILE   A 1 1100 ? -55.17000  63.27100  -22.26000 1.000 62.06499  ?  1098 ILE   A C   1 
ATOM   8794  O  O   . ILE   A 1 1100 ? -54.53000  62.57700  -23.05900 1.000 63.88271  ?  1098 ILE   A O   1 
ATOM   8795  C  CB  . ILE   A 1 1100 ? -54.29200  65.49100  -21.41700 1.000 51.83005  ?  1098 ILE   A CB  1 
ATOM   8796  C  CG1 . ILE   A 1 1100 ? -54.34500  67.00800  -21.60400 1.000 48.91408  ?  1098 ILE   A CG1 1 
ATOM   8797  C  CG2 . ILE   A 1 1100 ? -52.87300  64.99800  -21.59200 1.000 45.85858  ?  1098 ILE   A CG2 1 
ATOM   8798  C  CD1 . ILE   A 1 1100 ? -53.39700  67.76100  -20.69400 1.000 32.36646  ?  1098 ILE   A CD1 1 
ATOM   8799  N  N   . LEU   A 1 1101 ? -55.83800  62.73700  -21.23400 1.000 65.10580  ?  1099 LEU   A N   1 
ATOM   8800  C  CA  . LEU   A 1 1101 ? -55.87200  61.29000  -21.04100 1.000 68.72068  ?  1099 LEU   A CA  1 
ATOM   8801  C  C   . LEU   A 1 1101 ? -56.51100  60.59200  -22.23200 1.000 68.37077  ?  1099 LEU   A C   1 
ATOM   8802  O  O   . LEU   A 1 1101 ? -56.03600  59.54000  -22.67600 1.000 69.33128  ?  1099 LEU   A O   1 
ATOM   8803  C  CB  . LEU   A 1 1101 ? -56.63200  60.95000  -19.76000 1.000 65.89075  ?  1099 LEU   A CB  1 
ATOM   8804  C  CG  . LEU   A 1 1101 ? -55.97800  61.33300  -18.43600 1.000 67.45990  ?  1099 LEU   A CG  1 
ATOM   8805  C  CD1 . LEU   A 1 1101 ? -57.02000  61.38600  -17.32900 1.000 62.45323  ?  1099 LEU   A CD1 1 
ATOM   8806  C  CD2 . LEU   A 1 1101 ? -54.87200  60.35000  -18.09800 1.000 65.81132  ?  1099 LEU   A CD2 1 
ATOM   8807  N  N   . GLU   A 1 1102 ? -57.59400  61.16500  -22.76000 1.000 71.20760  ?  1100 GLU   A N   1 
ATOM   8808  C  CA  . GLU   A 1 1102 ? -58.25800  60.57400  -23.91500 1.000 77.42128  ?  1100 GLU   A CA  1 
ATOM   8809  C  C   . GLU   A 1 1102 ? -57.37000  60.63700  -25.15000 1.000 79.48493  ?  1100 GLU   A C   1 
ATOM   8810  O  O   . GLU   A 1 1102 ? -57.27900  59.66200  -25.90700 1.000 87.63562  ?  1100 GLU   A O   1 
ATOM   8811  C  CB  . GLU   A 1 1102 ? -59.58900  61.28300  -24.16300 1.000 70.00919  ?  1100 GLU   A CB  1 
ATOM   8812  C  CG  . GLU   A 1 1102 ? -60.14400  61.12200  -25.56500 1.000 86.93507  ?  1100 GLU   A CG  1 
ATOM   8813  C  CD  . GLU   A 1 1102 ? -61.48400  61.81100  -25.73800 1.000 110.59098 ?  1100 GLU   A CD  1 
ATOM   8814  O  OE1 . GLU   A 1 1102 ? -62.14800  62.09000  -24.71700 1.000 97.90378  ?  1100 GLU   A OE1 1 
ATOM   8815  O  OE2 . GLU   A 1 1102 ? -61.87300  62.07600  -26.89600 1.000 108.11423 -1 1100 GLU   A OE2 1 
ATOM   8816  N  N   . ALA   A 1 1103 ? -56.70400  61.77400  -25.36700 1.000 75.83276  ?  1101 ALA   A N   1 
ATOM   8817  C  CA  . ALA   A 1 1103 ? -55.78400  61.88400  -26.49300 1.000 70.93482  ?  1101 ALA   A CA  1 
ATOM   8818  C  C   . ALA   A 1 1103 ? -54.66900  60.85300  -26.38900 1.000 60.30113  ?  1101 ALA   A C   1 
ATOM   8819  O  O   . ALA   A 1 1103 ? -54.26300  60.26000  -27.39500 1.000 75.79948  ?  1101 ALA   A O   1 
ATOM   8820  C  CB  . ALA   A 1 1103 ? -55.20800  63.29800  -26.56500 1.000 72.00358  ?  1101 ALA   A CB  1 
ATOM   8821  N  N   . ALA   A 1 1104 ? -54.17100  60.61600  -25.17700 1.000 59.86432  ?  1102 ALA   A N   1 
ATOM   8822  C  CA  . ALA   A 1 1104 ? -53.15300  59.59800  -24.96400 1.000 78.49483  ?  1102 ALA   A CA  1 
ATOM   8823  C  C   . ALA   A 1 1104 ? -53.73500  58.19600  -24.88300 1.000 75.49158  ?  1102 ALA   A C   1 
ATOM   8824  O  O   . ALA   A 1 1104 ? -52.96700  57.22700  -24.89100 1.000 70.22425  ?  1102 ALA   A O   1 
ATOM   8825  C  CB  . ALA   A 1 1104 ? -52.36300  59.90000  -23.68900 1.000 73.70707  ?  1102 ALA   A CB  1 
ATOM   8826  N  N   . ARG   A 1 1105 ? -55.06100  58.07500  -24.81500 1.000 80.52747  ?  1103 ARG   A N   1 
ATOM   8827  C  CA  . ARG   A 1 1105 ? -55.75000  56.79400  -24.67900 1.000 80.80760  ?  1103 ARG   A CA  1 
ATOM   8828  C  C   . ARG   A 1 1105 ? -55.12800  55.97100  -23.55100 1.000 95.75044  ?  1103 ARG   A C   1 
ATOM   8829  O  O   . ARG   A 1 1105 ? -54.67300  54.84000  -23.73600 1.000 93.03277  ?  1103 ARG   A O   1 
ATOM   8830  C  CB  . ARG   A 1 1105 ? -55.74200  56.02900  -26.00600 1.000 76.43193  ?  1103 ARG   A CB  1 
ATOM   8831  N  N   . VAL   A 1 1106 ? -55.10800  56.57300  -22.36600 1.000 97.90640  ?  1104 VAL   A N   1 
ATOM   8832  C  CA  . VAL   A 1 1106 ? -54.40800  55.99800  -21.22400 1.000 92.32558  ?  1104 VAL   A CA  1 
ATOM   8833  C  C   . VAL   A 1 1106 ? -55.23700  54.85600  -20.65200 1.000 106.94754 ?  1104 VAL   A C   1 
ATOM   8834  O  O   . VAL   A 1 1106 ? -56.42600  55.02200  -20.35100 1.000 83.10238  ?  1104 VAL   A O   1 
ATOM   8835  C  CB  . VAL   A 1 1106 ? -54.12800  57.07400  -20.16300 1.000 82.52154  ?  1104 VAL   A CB  1 
ATOM   8836  C  CG1 . VAL   A 1 1106 ? -54.03600  56.46200  -18.76900 1.000 96.46527  ?  1104 VAL   A CG1 1 
ATOM   8837  C  CG2 . VAL   A 1 1106 ? -52.86100  57.81700  -20.50400 1.000 93.30685  ?  1104 VAL   A CG2 1 
ATOM   8838  N  N   . LYS   A 1 1107 ? -54.61200  53.68900  -20.51900 1.000 104.45679 ?  1105 LYS   A N   1 
ATOM   8839  C  CA  . LYS   A 1 1107 ? -55.28200  52.54600  -19.91900 1.000 117.09791 ?  1105 LYS   A CA  1 
ATOM   8840  C  C   . LYS   A 1 1107 ? -55.50100  52.79100  -18.43100 1.000 125.38196 ?  1105 LYS   A C   1 
ATOM   8841  O  O   . LYS   A 1 1107 ? -54.67800  53.41800  -17.75800 1.000 121.35443 ?  1105 LYS   A O   1 
ATOM   8842  C  CB  . LYS   A 1 1107 ? -54.46600  51.27100  -20.14700 1.000 114.54707 ?  1105 LYS   A CB  1 
ATOM   8843  C  CG  . LYS   A 1 1107 ? -53.52100  50.88600  -19.01400 1.000 104.08846 ?  1105 LYS   A CG  1 
ATOM   8844  C  CD  . LYS   A 1 1107 ? -52.71400  49.64700  -19.36900 1.000 97.82699  ?  1105 LYS   A CD  1 
ATOM   8845  C  CE  . LYS   A 1 1107 ? -53.59700  48.55200  -19.94900 1.000 93.36604  ?  1105 LYS   A CE  1 
ATOM   8846  N  NZ  . LYS   A 1 1107 ? -54.70200  48.16900  -19.02500 1.000 79.13967  ?  1105 LYS   A NZ  1 
ATOM   8847  N  N   . ARG   A 1 1108 ? -56.63000  52.30700  -17.92000 1.000 119.79831 ?  1106 ARG   A N   1 
ATOM   8848  C  CA  . ARG   A 1 1108 ? -57.02100  52.54400  -16.53300 1.000 112.42903 ?  1106 ARG   A CA  1 
ATOM   8849  C  C   . ARG   A 1 1108 ? -56.78300  51.27400  -15.72700 1.000 128.83292 ?  1106 ARG   A C   1 
ATOM   8850  O  O   . ARG   A 1 1108 ? -57.54000  50.30600  -15.83300 1.000 127.93980 ?  1106 ARG   A O   1 
ATOM   8851  C  CB  . ARG   A 1 1108 ? -58.47900  52.97800  -16.43900 1.000 103.60724 ?  1106 ARG   A CB  1 
ATOM   8852  C  CG  . ARG   A 1 1108 ? -58.86600  53.45900  -15.05200 1.000 108.20801 ?  1106 ARG   A CG  1 
ATOM   8853  C  CD  . ARG   A 1 1108 ? -58.40900  54.89100  -14.87400 1.000 105.00340 ?  1106 ARG   A CD  1 
ATOM   8854  N  NE  . ARG   A 1 1108 ? -58.48200  55.59900  -16.14600 1.000 93.69576  ?  1106 ARG   A NE  1 
ATOM   8855  C  CZ  . ARG   A 1 1108 ? -59.27700  56.63300  -16.38300 1.000 91.08876  ?  1106 ARG   A CZ  1 
ATOM   8856  N  NH1 . ARG   A 1 1108 ? -60.04100  57.14900  -15.43500 1.000 96.21967  ?  1106 ARG   A NH1 1 
ATOM   8857  N  NH2 . ARG   A 1 1108 ? -59.31100  57.15800  -17.60500 1.000 90.50878  ?  1106 ARG   A NH2 1 
ATOM   8858  N  N   . GLU   A 1 1109 ? -55.73300  51.28300  -14.91300 1.000 131.55917 ?  1107 GLU   A N   1 
ATOM   8859  C  CA  . GLU   A 1 1109 ? -55.53900  50.23600  -13.92800 1.000 113.54178 ?  1107 GLU   A CA  1 
ATOM   8860  C  C   . GLU   A 1 1109 ? -56.27500  50.61100  -12.64200 1.000 111.82768 ?  1107 GLU   A C   1 
ATOM   8861  O  O   . GLU   A 1 1109 ? -56.88700  51.67700  -12.53400 1.000 105.40715 ?  1107 GLU   A O   1 
ATOM   8862  C  CB  . GLU   A 1 1109 ? -54.05000  49.99600  -13.68700 1.000 87.68363  ?  1107 GLU   A CB  1 
ATOM   8863  C  CG  . GLU   A 1 1109 ? -53.68600  48.52600  -13.65400 1.000 99.35941  ?  1107 GLU   A CG  1 
ATOM   8864  C  CD  . GLU   A 1 1109 ? -52.19100  48.28600  -13.66800 1.000 114.38498 ?  1107 GLU   A CD  1 
ATOM   8865  O  OE1 . GLU   A 1 1109 ? -51.42800  49.27300  -13.72700 1.000 108.71294 ?  1107 GLU   A OE1 1 
ATOM   8866  O  OE2 . GLU   A 1 1109 ? -51.77800  47.10900  -13.62500 1.000 116.47851 -1 1107 GLU   A OE2 1 
ATOM   8867  N  N   . GLY   A 1 1110 ? -56.22800  49.72100  -11.65500 1.000 105.73688 ?  1108 GLY   A N   1 
ATOM   8868  C  CA  . GLY   A 1 1110 ? -56.94200  49.94100  -10.41300 1.000 101.87924 ?  1108 GLY   A CA  1 
ATOM   8869  C  C   . GLY   A 1 1110 ? -56.03600  50.23300  -9.23600  1.000 86.16949  ?  1108 GLY   A C   1 
ATOM   8870  O  O   . GLY   A 1 1110 ? -56.45800  50.85400  -8.25600  1.000 74.43229  ?  1108 GLY   A O   1 
ATOM   8871  N  N   . ASN   A 1 1111 ? -54.78400  49.78300  -9.32000  1.000 85.40066  ?  1109 ASN   A N   1 
ATOM   8872  C  CA  . ASN   A 1 1111 ? -53.82700  50.02300  -8.24900  1.000 97.73346  ?  1109 ASN   A CA  1 
ATOM   8873  C  C   . ASN   A 1 1111 ? -53.16200  51.38800  -8.35700  1.000 93.18766  ?  1109 ASN   A C   1 
ATOM   8874  O  O   . ASN   A 1 1111 ? -52.61600  51.87900  -7.36400  1.000 84.75231  ?  1109 ASN   A O   1 
ATOM   8875  C  CB  . ASN   A 1 1111 ? -52.74700  48.94000  -8.24700  1.000 86.39260  ?  1109 ASN   A CB  1 
ATOM   8876  C  CG  . ASN   A 1 1111 ? -52.33400  48.52900  -9.64600  1.000 93.95868  ?  1109 ASN   A CG  1 
ATOM   8877  O  OD1 . ASN   A 1 1111 ? -53.17600  48.24900  -10.50000 1.000 111.54375 ?  1109 ASN   A OD1 1 
ATOM   8878  N  ND2 . ASN   A 1 1111 ? -51.02900  48.51200  -9.89400  1.000 90.74069  ?  1109 ASN   A ND2 1 
ATOM   8879  N  N   . ARG   A 1 1112 ? -53.19300  52.00700  -9.53200  1.000 82.03519  ?  1110 ARG   A N   1 
ATOM   8880  C  CA  . ARG   A 1 1112 ? -52.49000  53.25400  -9.77800  1.000 68.69510  ?  1110 ARG   A CA  1 
ATOM   8881  C  C   . ARG   A 1 1112 ? -53.47000  54.29800  -10.30000 1.000 79.61337  ?  1110 ARG   A C   1 
ATOM   8882  O  O   . ARG   A 1 1112 ? -54.62000  53.99600  -10.61900 1.000 68.50071  ?  1110 ARG   A O   1 
ATOM   8883  C  CB  . ARG   A 1 1112 ? -51.34400  53.04100  -10.77500 1.000 49.55670  ?  1110 ARG   A CB  1 
ATOM   8884  C  CG  . ARG   A 1 1112 ? -50.30300  52.03700  -10.30200 1.000 57.83437  ?  1110 ARG   A CG  1 
ATOM   8885  C  CD  . ARG   A 1 1112 ? -48.96400  52.19800  -11.01200 1.000 60.38616  ?  1110 ARG   A CD  1 
ATOM   8886  N  NE  . ARG   A 1 1112 ? -47.92200  52.71400  -10.13200 1.000 64.67371  ?  1110 ARG   A NE  1 
ATOM   8887  C  CZ  . ARG   A 1 1112 ? -46.99000  51.96600  -9.55600  1.000 80.33337  ?  1110 ARG   A CZ  1 
ATOM   8888  N  NH1 . ARG   A 1 1112 ? -46.96100  50.65200  -9.71800  1.000 76.99967  ?  1110 ARG   A NH1 1 
ATOM   8889  N  NH2 . ARG   A 1 1112 ? -46.06100  52.55000  -8.80200  1.000 74.28348  ?  1110 ARG   A NH2 1 
ATOM   8890  N  N   A HIS   A 1 1113 ? -52.98900  55.53800  -10.41800 0.460 91.25255  ?  1111 HIS   A N   1 
ATOM   8891  N  N   B HIS   A 1 1113 ? -53.00800  55.55400  -10.35600 0.540 89.66255  ?  1111 HIS   A N   1 
ATOM   8892  C  CA  A HIS   A 1 1113 ? -53.76500  56.68100  -10.89200 0.460 120.88255 ?  1111 HIS   A CA  1 
ATOM   8893  C  CA  B HIS   A 1 1113 ? -53.78500  56.65500  -10.90400 0.540 125.01255 ?  1111 HIS   A CA  1 
ATOM   8894  C  C   A HIS   A 1 1113 ? -53.39200  56.99500  -12.33800 0.460 80.53319  ?  1111 HIS   A C   1 
ATOM   8895  C  C   B HIS   A 1 1113 ? -53.42500  56.87900  -12.36600 0.540 71.77340  ?  1111 HIS   A C   1 
ATOM   8896  O  O   A HIS   A 1 1113 ? -52.21300  56.92500  -12.68800 0.460 72.15966  ?  1111 HIS   A O   1 
ATOM   8897  O  O   B HIS   A 1 1113 ? -52.28100  56.64600  -12.75800 0.540 72.39042  ?  1111 HIS   A O   1 
ATOM   8898  C  CB  A HIS   A 1 1113 ? -53.49400  57.90100  -10.00600 0.460 72.98255  ?  1111 HIS   A CB  1 
ATOM   8899  C  CB  B HIS   A 1 1113 ? -53.52800  57.94600  -10.12200 0.540 75.25255  ?  1111 HIS   A CB  1 
ATOM   8900  C  CG  A HIS   A 1 1113 ? -53.85500  59.21400  -10.63100 0.460 67.53187  ?  1111 HIS   A CG  1 
ATOM   8901  C  CG  B HIS   A 1 1113 ? -53.64800  57.78900  -8.64100  0.540 64.90675  ?  1111 HIS   A CG  1 
ATOM   8902  N  ND1 A HIS   A 1 1113 ? -53.03000  59.87800  -11.51500 0.460 61.85165  ?  1111 HIS   A ND1 1 
ATOM   8903  N  ND1 B HIS   A 1 1113 ? -54.78500  58.14700  -7.95100  0.540 59.71383  ?  1111 HIS   A ND1 1 
ATOM   8904  C  CD2 A HIS   A 1 1113 ? -54.95400  59.99400  -10.48800 0.460 64.79978  ?  1111 HIS   A CD2 1 
ATOM   8905  C  CD2 B HIS   A 1 1113 ? -52.77700  57.32100  -7.71700  0.540 57.30417  ?  1111 HIS   A CD2 1 
ATOM   8906  C  CE1 A HIS   A 1 1113 ? -53.60700  61.00500  -11.89300 0.460 52.91904  ?  1111 HIS   A CE1 1 
ATOM   8907  C  CE1 B HIS   A 1 1113 ? -54.61400  57.89700  -6.66600  0.540 54.86145  ?  1111 HIS   A CE1 1 
ATOM   8908  N  NE2 A HIS   A 1 1113 ? -54.77600  61.09900  -11.28400 0.460 51.02682  ?  1111 HIS   A NE2 1 
ATOM   8909  N  NE2 B HIS   A 1 1113 ? -53.40300  57.39700  -6.49700  0.540 59.86237  ?  1111 HIS   A NE2 1 
ATOM   8910  N  N   . PRO   A 1 1114 ? -54.40300  57.35700  -13.17800 1.000 68.37136  ?  1112 PRO   A N   1 
ATOM   8911  C  CA  . PRO   A 1 1114 ? -54.18800  57.59600  -14.62500 1.000 61.76475  ?  1112 PRO   A CA  1 
ATOM   8912  C  C   . PRO   A 1 1114 ? -52.78700  57.68800  -15.21100 1.000 70.44708  ?  1112 PRO   A C   1 
ATOM   8913  O  O   . PRO   A 1 1114 ? -52.17300  56.65500  -15.49300 1.000 86.27719  ?  1112 PRO   A O   1 
ATOM   8914  C  CB  . PRO   A 1 1114 ? -54.93700  58.92100  -14.83000 1.000 67.97670  ?  1112 PRO   A CB  1 
ATOM   8915  C  CG  . PRO   A 1 1114 ? -56.17100  58.72500  -13.92700 1.000 59.44209  ?  1112 PRO   A CG  1 
ATOM   8916  C  CD  . PRO   A 1 1114 ? -55.76900  57.74400  -12.79800 1.000 76.05967  ?  1112 PRO   A CD  1 
ATOM   8917  N  N   . LEU   A 1 1115 ? -52.29200  58.90500  -15.43800 1.000 56.57394  ?  1113 LEU   A N   1 
ATOM   8918  C  CA  . LEU   A 1 1115 ? -51.03200  59.08900  -16.14900 1.000 42.55320  ?  1113 LEU   A CA  1 
ATOM   8919  C  C   . LEU   A 1 1115 ? -49.83200  59.06900  -15.22300 1.000 42.52251  ?  1113 LEU   A C   1 
ATOM   8920  O  O   . LEU   A 1 1115 ? -48.77500  58.55700  -15.59200 1.000 41.52670  ?  1113 LEU   A O   1 
ATOM   8921  C  CB  . LEU   A 1 1115 ? -51.05400  60.40500  -16.92100 1.000 53.60166  ?  1113 LEU   A CB  1 
ATOM   8922  C  CG  . LEU   A 1 1115 ? -51.26800  60.24800  -18.41600 1.000 52.40960  ?  1113 LEU   A CG  1 
ATOM   8923  C  CD1 . LEU   A 1 1115 ? -51.26500  61.58700  -19.13100 1.000 55.67212  ?  1113 LEU   A CD1 1 
ATOM   8924  C  CD2 . LEU   A 1 1115 ? -50.17000  59.36300  -18.92600 1.000 54.78809  ?  1113 LEU   A CD2 1 
ATOM   8925  N  N   . PHE   A 1 1116 ? -49.97800  59.63200  -14.03300 1.000 49.58341  ?  1114 PHE   A N   1 
ATOM   8926  C  CA  . PHE   A 1 1116 ? -48.90200  59.72900  -13.06700 1.000 36.17507  ?  1114 PHE   A CA  1 
ATOM   8927  C  C   . PHE   A 1 1116 ? -49.43600  59.29700  -11.71300 1.000 36.71445  ?  1114 PHE   A C   1 
ATOM   8928  O  O   . PHE   A 1 1116 ? -50.64700  59.25700  -11.48700 1.000 55.07454  ?  1114 PHE   A O   1 
ATOM   8929  C  CB  . PHE   A 1 1116 ? -48.36400  61.15900  -13.00100 1.000 39.44637  ?  1114 PHE   A CB  1 
ATOM   8930  C  CG  . PHE   A 1 1116 ? -49.43900  62.18900  -12.80000 1.000 41.33418  ?  1114 PHE   A CG  1 
ATOM   8931  C  CD1 . PHE   A 1 1116 ? -49.89400  62.49800  -11.52800 1.000 37.33182  ?  1114 PHE   A CD1 1 
ATOM   8932  C  CD2 . PHE   A 1 1116 ? -50.02000  62.82300  -13.88500 1.000 32.21995  ?  1114 PHE   A CD2 1 
ATOM   8933  C  CE1 . PHE   A 1 1116 ? -50.88600  63.43600  -11.34200 1.000 38.47668  ?  1114 PHE   A CE1 1 
ATOM   8934  C  CE2 . PHE   A 1 1116 ? -51.01400  63.76000  -13.70400 1.000 40.05245  ?  1114 PHE   A CE2 1 
ATOM   8935  C  CZ  . PHE   A 1 1116 ? -51.44800  64.06600  -12.43200 1.000 42.80067  ?  1114 PHE   A CZ  1 
ATOM   8936  N  N   . ASP   A 1 1117 ? -48.51900  58.97000  -10.81100 1.000 41.72532  ?  1115 ASP   A N   1 
ATOM   8937  C  CA  . ASP   A 1 1117 ? -48.88600  58.64000  -9.44700  1.000 38.35816  ?  1115 ASP   A CA  1 
ATOM   8938  C  C   . ASP   A 1 1117 ? -48.29100  59.58600  -8.41800  1.000 42.86551  ?  1115 ASP   A C   1 
ATOM   8939  O  O   . ASP   A 1 1117 ? -48.70000  59.53600  -7.25300  1.000 44.52398  ?  1115 ASP   A O   1 
ATOM   8940  C  CB  . ASP   A 1 1117 ? -48.47100  57.19900  -9.11600  1.000 32.84554  ?  1115 ASP   A CB  1 
ATOM   8941  C  CG  . ASP   A 1 1117 ? -49.41800  56.17900  -9.70700  1.000 54.16941  ?  1115 ASP   A CG  1 
ATOM   8942  O  OD1 . ASP   A 1 1117 ? -50.40400  55.81400  -9.03100  1.000 62.92147  ?  1115 ASP   A OD1 1 
ATOM   8943  O  OD2 . ASP   A 1 1117 ? -49.17900  55.74800  -10.85300 1.000 65.86526  -1 1115 ASP   A OD2 1 
ATOM   8944  N  N   . VAL   A 1 1118 ? -47.35100  60.44600  -8.81100  1.000 34.26303  ?  1116 VAL   A N   1 
ATOM   8945  C  CA  . VAL   A 1 1118 ? -46.74900  61.44300  -7.93600  1.000 28.10149  ?  1116 VAL   A CA  1 
ATOM   8946  C  C   . VAL   A 1 1118 ? -47.02600  62.82300  -8.51600  1.000 28.55731  ?  1116 VAL   A C   1 
ATOM   8947  O  O   . VAL   A 1 1118 ? -46.88800  63.03300  -9.72600  1.000 36.57215  ?  1116 VAL   A O   1 
ATOM   8948  C  CB  . VAL   A 1 1118 ? -45.23200  61.21500  -7.77700  1.000 34.85085  ?  1116 VAL   A CB  1 
ATOM   8949  C  CG1 . VAL   A 1 1118 ? -44.61700  62.28300  -6.87900  1.000 24.96209  ?  1116 VAL   A CG1 1 
ATOM   8950  C  CG2 . VAL   A 1 1118 ? -44.96300  59.82200  -7.23500  1.000 28.18673  ?  1116 VAL   A CG2 1 
ATOM   8951  N  N   . MET   A 1 1119 ? -47.40700  63.76100  -7.65100  1.000 34.75088  ?  1117 MET   A N   1 
ATOM   8952  C  CA  . MET   A 1 1119 ? -47.77700  65.11400  -8.04500  1.000 22.99172  ?  1117 MET   A CA  1 
ATOM   8953  C  C   . MET   A 1 1119 ? -46.88300  66.12900  -7.34300  1.000 26.88035  ?  1117 MET   A C   1 
ATOM   8954  O  O   . MET   A 1 1119 ? -46.60000  65.99800  -6.14800  1.000 37.19795  ?  1117 MET   A O   1 
ATOM   8955  C  CB  . MET   A 1 1119 ? -49.25100  65.38500  -7.71300  1.000 35.45804  ?  1117 MET   A CB  1 
ATOM   8956  C  CG  . MET   A 1 1119 ? -49.62700  66.85200  -7.60400  1.000 36.96441  ?  1117 MET   A CG  1 
ATOM   8957  S  SD  . MET   A 1 1119 ? -50.00000  67.60600  -9.19600  1.000 52.88273  ?  1117 MET   A SD  1 
ATOM   8958  C  CE  . MET   A 1 1119 ? -51.33800  66.56700  -9.77000  1.000 37.30221  ?  1117 MET   A CE  1 
ATOM   8959  N  N   . PHE   A 1 1120 ? -46.44300  67.14300  -8.08800  1.000 28.57118  ?  1118 PHE   A N   1 
ATOM   8960  C  CA  . PHE   A 1 1120 ? -45.59500  68.20300  -7.55100  1.000 26.41589  ?  1118 PHE   A CA  1 
ATOM   8961  C  C   . PHE   A 1 1120 ? -46.23900  69.54700  -7.85300  1.000 35.41336  ?  1118 PHE   A C   1 
ATOM   8962  O  O   . PHE   A 1 1120 ? -46.43600  69.89400  -9.02300  1.000 40.24478  ?  1118 PHE   A O   1 
ATOM   8963  C  CB  . PHE   A 1 1120 ? -44.18400  68.13600  -8.14300  1.000 22.82177  ?  1118 PHE   A CB  1 
ATOM   8964  C  CG  . PHE   A 1 1120 ? -43.32700  69.32900  -7.81700  1.000 27.99570  ?  1118 PHE   A CG  1 
ATOM   8965  C  CD1 . PHE   A 1 1120 ? -42.86900  69.54100  -6.52700  1.000 31.78592  ?  1118 PHE   A CD1 1 
ATOM   8966  C  CD2 . PHE   A 1 1120 ? -42.97000  70.23300  -8.80500  1.000 33.10128  ?  1118 PHE   A CD2 1 
ATOM   8967  C  CE1 . PHE   A 1 1120 ? -42.07300  70.63600  -6.22600  1.000 34.01806  ?  1118 PHE   A CE1 1 
ATOM   8968  C  CE2 . PHE   A 1 1120 ? -42.17600  71.33000  -8.51100  1.000 32.51767  ?  1118 PHE   A CE2 1 
ATOM   8969  C  CZ  . PHE   A 1 1120 ? -41.72700  71.53100  -7.21900  1.000 24.87236  ?  1118 PHE   A CZ  1 
ATOM   8970  N  N   . MET   A 1 1121 ? -46.56900  70.29400  -6.80300  1.000 30.67353  ?  1119 MET   A N   1 
ATOM   8971  C  CA  . MET   A 1 1121 ? -47.15700  71.61800  -6.92400  1.000 19.15694  ?  1119 MET   A CA  1 
ATOM   8972  C  C   . MET   A 1 1121 ? -46.25200  72.64100  -6.25200  1.000 34.61758  ?  1119 MET   A C   1 
ATOM   8973  O  O   . MET   A 1 1121 ? -45.36200  72.29500  -5.46900  1.000 29.41490  ?  1119 MET   A O   1 
ATOM   8974  C  CB  . MET   A 1 1121 ? -48.55300  71.68200  -6.29100  1.000 19.61744  ?  1119 MET   A CB  1 
ATOM   8975  C  CG  . MET   A 1 1121 ? -49.36300  70.40800  -6.40400  1.000 36.37215  ?  1119 MET   A CG  1 
ATOM   8976  S  SD  . MET   A 1 1121 ? -51.02200  70.60000  -5.72000  1.000 47.05397  ?  1119 MET   A SD  1 
ATOM   8977  C  CE  . MET   A 1 1121 ? -50.71800  71.75000  -4.38300  1.000 48.69322  ?  1119 MET   A CE  1 
ATOM   8978  N  N   . MET   A 1 1122 ? -46.49800  73.91300  -6.56200  1.000 34.54300  ?  1120 MET   A N   1 
ATOM   8979  C  CA  . MET   A 1 1122 ? -45.72300  74.99600  -5.97300  1.000 32.24950  ?  1120 MET   A CA  1 
ATOM   8980  C  C   . MET   A 1 1122 ? -46.56800  76.26000  -5.92000  1.000 43.60515  ?  1120 MET   A C   1 
ATOM   8981  O  O   . MET   A 1 1122 ? -47.21100  76.62400  -6.90900  1.000 52.56579  ?  1120 MET   A O   1 
ATOM   8982  C  CB  . MET   A 1 1122 ? -44.43100  75.24300  -6.75900  1.000 29.60517  ?  1120 MET   A CB  1 
ATOM   8983  C  CG  . MET   A 1 1122 ? -43.53500  76.29100  -6.13200  1.000 38.26602  ?  1120 MET   A CG  1 
ATOM   8984  S  SD  . MET   A 1 1122 ? -41.78800  75.96900  -6.42100  1.000 44.16938  ?  1120 MET   A SD  1 
ATOM   8985  C  CE  . MET   A 1 1122 ? -41.06800  77.44200  -5.70400  1.000 33.91014  ?  1120 MET   A CE  1 
ATOM   8986  N  N   . GLN   A 1 1123 ? -46.56800  76.91200  -4.76100  1.000 48.73260  ?  1121 GLN   A N   1 
ATOM   8987  C  CA  . GLN   A 1 1123 ? -47.25900  78.17200  -4.54200  1.000 38.17114  ?  1121 GLN   A CA  1 
ATOM   8988  C  C   . GLN   A 1 1123 ? -46.24700  79.28000  -4.28200  1.000 44.27779  ?  1121 GLN   A C   1 
ATOM   8989  O  O   . GLN   A 1 1123 ? -45.19500  79.05300  -3.68000  1.000 46.08785  ?  1121 GLN   A O   1 
ATOM   8990  C  CB  . GLN   A 1 1123 ? -48.21900  78.07800  -3.35500  1.000 49.67681  ?  1121 GLN   A CB  1 
ATOM   8991  C  CG  . GLN   A 1 1123 ? -49.67500  77.93500  -3.72800  1.000 53.70149  ?  1121 GLN   A CG  1 
ATOM   8992  C  CD  . GLN   A 1 1123 ? -50.56600  77.85400  -2.51000  1.000 53.55608  ?  1121 GLN   A CD  1 
ATOM   8993  O  OE1 . GLN   A 1 1123 ? -50.79500  78.85200  -1.82700  1.000 66.30076  ?  1121 GLN   A OE1 1 
ATOM   8994  N  NE2 . GLN   A 1 1123 ? -51.06700  76.65900  -2.22300  1.000 58.97767  ?  1121 GLN   A NE2 1 
ATOM   8995  N  N   . GLY   A 1 1124 ? -46.57500  80.48500  -4.73200  1.000 47.03792  ?  1122 GLY   A N   1 
ATOM   8996  C  CA  . GLY   A 1 1124 ? -45.73200  81.62400  -4.45700  1.000 36.90827  ?  1122 GLY   A CA  1 
ATOM   8997  C  C   . GLY   A 1 1124 ? -45.91400  82.11500  -3.03000  1.000 53.51804  ?  1122 GLY   A C   1 
ATOM   8998  O  O   . GLY   A 1 1124 ? -46.55700  81.48900  -2.18700  1.000 66.67805  ?  1122 GLY   A O   1 
ATOM   8999  N  N   . ALA   A 1 1125 ? -45.33300  83.28200  -2.77000  1.000 54.59643  ?  1123 ALA   A N   1 
ATOM   9000  C  CA  . ALA   A 1 1125 ? -45.38800  83.85800  -1.43700  1.000 54.47060  ?  1123 ALA   A CA  1 
ATOM   9001  C  C   . ALA   A 1 1125 ? -46.77200  84.44800  -1.16100  1.000 50.04693  ?  1123 ALA   A C   1 
ATOM   9002  O  O   . ALA   A 1 1125 ? -47.48900  84.83000  -2.08900  1.000 54.98393  ?  1123 ALA   A O   1 
ATOM   9003  C  CB  . ALA   A 1 1125 ? -44.32200  84.93800  -1.28200  1.000 46.24416  ?  1123 ALA   A CB  1 
ATOM   9004  N  N   . PRO   A 1 1126 ? -47.17400  84.52800  0.10900   1.000 49.89636  ?  1124 PRO   A N   1 
ATOM   9005  C  CA  . PRO   A 1 1126 ? -48.48200  85.11500  0.42600   1.000 49.33186  ?  1124 PRO   A CA  1 
ATOM   9006  C  C   . PRO   A 1 1126 ? -48.51600  86.60600  0.12000   1.000 55.07122  ?  1124 PRO   A C   1 
ATOM   9007  O  O   . PRO   A 1 1126 ? -47.56000  87.33700  0.38800   1.000 64.06031  ?  1124 PRO   A O   1 
ATOM   9008  C  CB  . PRO   A 1 1126 ? -48.63700  84.84800  1.92900   1.000 43.90289  ?  1124 PRO   A CB  1 
ATOM   9009  C  CG  . PRO   A 1 1126 ? -47.24500  84.66900  2.42900   1.000 56.41935  ?  1124 PRO   A CG  1 
ATOM   9010  C  CD  . PRO   A 1 1126 ? -46.49700  84.01100  1.31100   1.000 46.49286  ?  1124 PRO   A CD  1 
ATOM   9011  N  N   . GLU   A 1 1127 ? -49.64300  87.05400  -0.44300  1.000 52.09239  ?  1125 GLU   A N   1 
ATOM   9012  C  CA  . GLU   A 1 1127 ? -49.78600  88.45500  -0.83000  1.000 57.07515  ?  1125 GLU   A CA  1 
ATOM   9013  C  C   . GLU   A 1 1127 ? -50.17400  89.34600  0.34600   1.000 50.53823  ?  1125 GLU   A C   1 
ATOM   9014  O  O   . GLU   A 1 1127 ? -49.75100  90.50600  0.40300   1.000 52.00861  ?  1125 GLU   A O   1 
ATOM   9015  C  CB  . GLU   A 1 1127 ? -50.81900  88.58600  -1.95000  1.000 54.67791  ?  1125 GLU   A CB  1 
ATOM   9016  C  CG  . GLU   A 1 1127 ? -50.81700  87.42500  -2.93600  1.000 73.82937  ?  1125 GLU   A CG  1 
ATOM   9017  C  CD  . GLU   A 1 1127 ? -50.12500  87.76400  -4.24300  1.000 88.10354  ?  1125 GLU   A CD  1 
ATOM   9018  O  OE1 . GLU   A 1 1127 ? -49.32200  88.72100  -4.26400  1.000 73.24080  ?  1125 GLU   A OE1 1 
ATOM   9019  O  OE2 . GLU   A 1 1127 ? -50.38500  87.06900  -5.24900  1.000 97.93909  -1 1125 GLU   A OE2 1 
ATOM   9020  N  N   . THR   A 1 1128 ? -50.96700  88.83600  1.28000   1.000 43.17733  ?  1126 THR   A N   1 
ATOM   9021  C  CA  . THR   A 1 1128 ? -51.39900  89.58500  2.44900   1.000 45.52268  ?  1126 THR   A CA  1 
ATOM   9022  C  C   . THR   A 1 1128 ? -50.81100  88.97400  3.71400   1.000 43.95343  ?  1126 THR   A C   1 
ATOM   9023  O  O   . THR   A 1 1128 ? -50.18000  87.91500  3.68800   1.000 51.70213  ?  1126 THR   A O   1 
ATOM   9024  C  CB  . THR   A 1 1128 ? -52.92800  89.61400  2.53800   1.000 52.21469  ?  1126 THR   A CB  1 
ATOM   9025  O  OG1 . THR   A 1 1128 ? -53.45300  88.32400  2.19600   1.000 54.48407  ?  1126 THR   A OG1 1 
ATOM   9026  C  CG2 . THR   A 1 1128 ? -53.47900  90.64300  1.58100   1.000 51.00244  ?  1126 THR   A CG2 1 
ATOM   9027  N  N   . GLU   A 1 1129 ? -51.02300  89.66300  4.83700   1.000 47.92352  ?  1127 GLU   A N   1 
ATOM   9028  C  CA  . GLU   A 1 1129 ? -50.60700  89.10400  6.11800   1.000 34.76876  ?  1127 GLU   A CA  1 
ATOM   9029  C  C   . GLU   A 1 1129 ? -51.56900  88.02800  6.59700   1.000 50.39645  ?  1127 GLU   A C   1 
ATOM   9030  O  O   . GLU   A 1 1129 ? -51.15400  87.09800  7.29700   1.000 48.48999  ?  1127 GLU   A O   1 
ATOM   9031  C  CB  . GLU   A 1 1129 ? -50.48700  90.20300  7.17400   1.000 34.31328  ?  1127 GLU   A CB  1 
ATOM   9032  C  CG  . GLU   A 1 1129 ? -49.32600  89.99200  8.13800   1.000 69.84140  ?  1127 GLU   A CG  1 
ATOM   9033  C  CD  . GLU   A 1 1129 ? -49.63600  90.44400  9.55300   1.000 72.77208  ?  1127 GLU   A CD  1 
ATOM   9034  O  OE1 . GLU   A 1 1129 ? -50.47400  91.35400  9.72100   1.000 72.62737  ?  1127 GLU   A OE1 1 
ATOM   9035  O  OE2 . GLU   A 1 1129 ? -49.03900  89.88500  10.49700  1.000 78.69026  -1 1127 GLU   A OE2 1 
ATOM   9036  N  N   . LEU   A 1 1130 ? -52.84900  88.13800  6.23500   1.000 50.61278  ?  1128 LEU   A N   1 
ATOM   9037  C  CA  . LEU   A 1 1130 ? -53.80500  87.10000  6.59800   1.000 39.92796  ?  1128 LEU   A CA  1 
ATOM   9038  C  C   . LEU   A 1 1130 ? -53.46900  85.78600  5.90700   1.000 48.15973  ?  1128 LEU   A C   1 
ATOM   9039  O  O   . LEU   A 1 1130 ? -53.56000  84.71300  6.51500   1.000 56.37913  ?  1128 LEU   A O   1 
ATOM   9040  C  CB  . LEU   A 1 1130 ? -55.22200  87.54800  6.25000   1.000 46.52216  ?  1128 LEU   A CB  1 
ATOM   9041  C  CG  . LEU   A 1 1130 ? -56.35900  86.85900  7.00300   1.000 38.25936  ?  1128 LEU   A CG  1 
ATOM   9042  C  CD1 . LEU   A 1 1130 ? -56.25400  87.12200  8.49700   1.000 57.51311  ?  1128 LEU   A CD1 1 
ATOM   9043  C  CD2 . LEU   A 1 1130 ? -57.69400  87.33700  6.46700   1.000 48.22257  ?  1128 LEU   A CD2 1 
ATOM   9044  N  N   . GLU   A 1 1131 ? -53.06600  85.85300  4.63500   1.000 46.16440  ?  1129 GLU   A N   1 
ATOM   9045  C  CA  . GLU   A 1 1131 ? -52.70800  84.64000  3.91000   1.000 50.31443  ?  1129 GLU   A CA  1 
ATOM   9046  C  C   . GLU   A 1 1131 ? -51.49500  83.95900  4.52800   1.000 45.84780  ?  1129 GLU   A C   1 
ATOM   9047  O  O   . GLU   A 1 1131 ? -51.39500  82.72700  4.50300   1.000 56.05198  ?  1129 GLU   A O   1 
ATOM   9048  C  CB  . GLU   A 1 1131 ? -52.44900  84.96700  2.43900   1.000 42.89377  ?  1129 GLU   A CB  1 
ATOM   9049  C  CG  . GLU   A 1 1131 ? -52.54100  83.76800  1.50800   1.000 42.32347  ?  1129 GLU   A CG  1 
ATOM   9050  C  CD  . GLU   A 1 1131 ? -52.21300  84.12000  0.07100   1.000 52.27513  ?  1129 GLU   A CD  1 
ATOM   9051  O  OE1 . GLU   A 1 1131 ? -52.17200  85.32700  -0.24700  1.000 58.00711  ?  1129 GLU   A OE1 1 
ATOM   9052  O  OE2 . GLU   A 1 1131 ? -51.99700  83.19300  -0.73900  1.000 58.38073  -1 1129 GLU   A OE2 1 
ATOM   9053  N  N   . SER   A 1 1132 ? -50.57200  84.73700  5.09600   1.000 49.65008  ?  1130 SER   A N   1 
ATOM   9054  C  CA  . SER   A 1 1132 ? -49.38200  84.14400  5.69400   1.000 49.21314  ?  1130 SER   A CA  1 
ATOM   9055  C  C   . SER   A 1 1132 ? -49.70700  83.42200  6.99300   1.000 45.49673  ?  1130 SER   A C   1 
ATOM   9056  O  O   . SER   A 1 1132 ? -48.98300  82.49900  7.38400   1.000 44.31697  ?  1130 SER   A O   1 
ATOM   9057  C  CB  . SER   A 1 1132 ? -48.32700  85.21700  5.94400   1.000 40.90805  ?  1130 SER   A CB  1 
ATOM   9058  O  OG  . SER   A 1 1132 ? -48.90000  86.33000  6.60100   1.000 65.20214  ?  1130 SER   A OG  1 
ATOM   9059  N  N   . ASN   A 1 1133 ? -50.77500  83.82800  7.67700   1.000 47.36421  ?  1131 ASN   A N   1 
ATOM   9060  C  CA  . ASN   A 1 1133 ? -51.20100  83.18000  8.90900   1.000 47.31398  ?  1131 ASN   A CA  1 
ATOM   9061  C  C   . ASN   A 1 1133 ? -52.36200  82.22300  8.68900   1.000 41.15383  ?  1131 ASN   A C   1 
ATOM   9062  O  O   . ASN   A 1 1133 ? -52.96100  81.75600  9.66400   1.000 49.04097  ?  1131 ASN   A O   1 
ATOM   9063  C  CB  . ASN   A 1 1133 ? -51.56400  84.22700  9.96100   1.000 49.34180  ?  1131 ASN   A CB  1 
ATOM   9064  C  CG  . ASN   A 1 1133 ? -50.44800  85.22200  10.19200  1.000 46.21185  ?  1131 ASN   A CG  1 
ATOM   9065  O  OD1 . ASN   A 1 1133 ? -50.66700  86.43400  10.18700  1.000 55.25621  ?  1131 ASN   A OD1 1 
ATOM   9066  N  ND2 . ASN   A 1 1133 ? -49.23700  84.71500  10.39100  1.000 52.62558  ?  1131 ASN   A ND2 1 
ATOM   9067  N  N   . MET   A 1 1134 ? -52.70000  81.93600  7.43600   1.000 36.92622  ?  1132 MET   A N   1 
ATOM   9068  C  CA  . MET   A 1 1134 ? -53.61100  80.84700  7.12400   1.000 39.39086  ?  1132 MET   A CA  1 
ATOM   9069  C  C   . MET   A 1 1134 ? -52.87200  79.51700  7.11700   1.000 41.27743  ?  1132 MET   A C   1 
ATOM   9070  O  O   . MET   A 1 1134 ? -51.69800  79.43400  6.74400   1.000 60.27740  ?  1132 MET   A O   1 
ATOM   9071  C  CB  . MET   A 1 1134 ? -54.28300  81.06500  5.77000   1.000 36.68850  ?  1132 MET   A CB  1 
ATOM   9072  C  CG  . MET   A 1 1134 ? -55.47700  81.97700  5.82800   1.000 37.18719  ?  1132 MET   A CG  1 
ATOM   9073  S  SD  . MET   A 1 1134 ? -56.42600  81.97500  4.29900   1.000 50.17794  ?  1132 MET   A SD  1 
ATOM   9074  C  CE  . MET   A 1 1134 ? -57.15500  83.60000  4.40900   1.000 62.67796  ?  1132 MET   A CE  1 
ATOM   9075  N  N   . HIS   A 1 1135 ? -53.57500  78.46600  7.52700   1.000 45.90001  ?  1133 HIS   A N   1 
ATOM   9076  C  CA  . HIS   A 1 1135 ? -52.99200  77.13500  7.62100   1.000 43.14129  ?  1133 HIS   A CA  1 
ATOM   9077  C  C   . HIS   A 1 1135 ? -53.90800  76.14100  6.92800   1.000 44.10897  ?  1133 HIS   A C   1 
ATOM   9078  O  O   . HIS   A 1 1135 ? -55.05200  75.94900  7.35300   1.000 43.98098  ?  1133 HIS   A O   1 
ATOM   9079  C  CB  . HIS   A 1 1135 ? -52.76300  76.74200  9.08200   1.000 48.68833  ?  1133 HIS   A CB  1 
ATOM   9080  C  CG  . HIS   A 1 1135 ? -51.84400  77.67000  9.81100   1.000 57.55828  ?  1133 HIS   A CG  1 
ATOM   9081  N  ND1 . HIS   A 1 1135 ? -52.19400  78.30100  10.98500  1.000 62.05713  ?  1133 HIS   A ND1 1 
ATOM   9082  C  CD2 . HIS   A 1 1135 ? -50.59900  78.10600  9.50600   1.000 67.69015  ?  1133 HIS   A CD2 1 
ATOM   9083  C  CE1 . HIS   A 1 1135 ? -51.19500  79.06500  11.38600  1.000 78.06039  ?  1133 HIS   A CE1 1 
ATOM   9084  N  NE2 . HIS   A 1 1135 ? -50.21500  78.96700  10.50500  1.000 83.27658  ?  1133 HIS   A NE2 1 
ATOM   9085  N  N   . HIS   A 1 1136 ? -53.38500  75.48900  5.89200   1.000 43.29281  ?  1134 HIS   A N   1 
ATOM   9086  C  CA  . HIS   A 1 1136 ? -54.15900  74.44700  5.17800   1.000 37.73368  ?  1134 HIS   A CA  1 
ATOM   9087  C  C   . HIS   A 1 1136 ? -54.25400  73.21400  6.06100   1.000 45.29174  ?  1134 HIS   A C   1 
ATOM   9088  O  O   . HIS   A 1 1136 ? -53.27800  72.82300  6.71700   1.000 47.52779  ?  1134 HIS   A O   1 
ATOM   9089  C  CB  . HIS   A 1 1136 ? -53.53900  74.08000  3.83200   1.000 33.64928  ?  1134 HIS   A CB  1 
ATOM   9090  C  CG  . HIS   A 1 1136 ? -54.45500  73.31200  2.94600   1.000 45.99970  ?  1134 HIS   A CG  1 
ATOM   9091  N  ND1 . HIS   A 1 1136 ? -55.81700  73.51000  2.93600   1.000 65.61574  ?  1134 HIS   A ND1 1 
ATOM   9092  C  CD2 . HIS   A 1 1136 ? -54.21500  72.35100  2.05100   1.000 45.13242  ?  1134 HIS   A CD2 1 
ATOM   9093  C  CE1 . HIS   A 1 1136 ? -56.37100  72.69000  2.05800   1.000 68.57255  ?  1134 HIS   A CE1 1 
ATOM   9094  N  NE2 . HIS   A 1 1136 ? -55.41400  71.97800  1.50800   1.000 52.40255  ?  1134 HIS   A NE2 1 
ATOM   9095  N  N   . ILE   A 1 1137 ? -55.42600  72.60700  6.04700   1.000 46.75153  ?  1135 ILE   A N   1 
ATOM   9096  C  CA  . ILE   A 1 1137 ? -55.69000  71.44300  6.88100   1.000 35.83485  ?  1135 ILE   A CA  1 
ATOM   9097  C  C   . ILE   A 1 1137 ? -55.86600  70.22400  5.99200   1.000 38.85171  ?  1135 ILE   A C   1 
ATOM   9098  O  O   . ILE   A 1 1137 ? -56.56600  70.27800  4.97300   1.000 47.17601  ?  1135 ILE   A O   1 
ATOM   9099  C  CB  . ILE   A 1 1137 ? -56.93600  71.65500  7.76100   1.000 43.74254  ?  1135 ILE   A CB  1 
ATOM   9100  C  CG1 . ILE   A 1 1137 ? -56.83800  73.00100  8.47400   1.000 45.85514  ?  1135 ILE   A CG1 1 
ATOM   9101  C  CG2 . ILE   A 1 1137 ? -57.09500  70.50900  8.75200   1.000 35.29756  ?  1135 ILE   A CG2 1 
ATOM   9102  C  CD1 . ILE   A 1 1137 ? -56.08300  72.93900  9.76800   1.000 44.95853  ?  1135 ILE   A CD1 1 
ATOM   9103  N  N   . ASN   A 1 1138 ? -55.22600  69.12600  6.38000   1.000 31.93911  ?  1136 ASN   A N   1 
ATOM   9104  C  CA  . ASN   A 1 1138 ? -55.42000  67.83300  5.74000   1.000 37.04186  ?  1136 ASN   A CA  1 
ATOM   9105  C  C   . ASN   A 1 1138 ? -56.31400  66.98600  6.63600   1.000 39.00813  ?  1136 ASN   A C   1 
ATOM   9106  O  O   . ASN   A 1 1138 ? -56.01200  66.79600  7.81900   1.000 44.47943  ?  1136 ASN   A O   1 
ATOM   9107  C  CB  . ASN   A 1 1138 ? -54.08400  67.13300  5.49300   1.000 36.35263  ?  1136 ASN   A CB  1 
ATOM   9108  C  CG  . ASN   A 1 1138 ? -54.20600  65.97200  4.52600   1.000 49.82258  ?  1136 ASN   A CG  1 
ATOM   9109  O  OD1 . ASN   A 1 1138 ? -54.21600  64.80900  4.93300   1.000 42.24356  ?  1136 ASN   A OD1 1 
ATOM   9110  N  ND2 . ASN   A 1 1138 ? -54.29900  66.28000  3.23600   1.000 54.90676  ?  1136 ASN   A ND2 1 
ATOM   9111  N  N   . ALA   A 1 1139 ? -57.41900  66.49200  6.07700   1.000 35.31682  ?  1137 ALA   A N   1 
ATOM   9112  C  CA  . ALA   A 1 1139 ? -58.35100  65.65500  6.82100   1.000 35.36003  ?  1137 ALA   A CA  1 
ATOM   9113  C  C   . ALA   A 1 1139 ? -58.00300  64.17500  6.73000   1.000 41.16815  ?  1137 ALA   A C   1 
ATOM   9114  O  O   . ALA   A 1 1139 ? -58.90300  63.32500  6.75300   1.000 46.28121  ?  1137 ALA   A O   1 
ATOM   9115  C  CB  . ALA   A 1 1139 ? -59.78000  65.90200  6.33900   1.000 39.22490  ?  1137 ALA   A CB  1 
ATOM   9116  N  N   . GLY   A 1 1140 ? -56.72000  63.84300  6.64100   1.000 37.96600  ?  1138 GLY   A N   1 
ATOM   9117  C  CA  . GLY   A 1 1140 ? -56.32800  62.45900  6.45400   1.000 40.78945  ?  1138 GLY   A CA  1 
ATOM   9118  C  C   . GLY   A 1 1140 ? -56.59000  61.95900  5.05100   1.000 44.96293  ?  1138 GLY   A C   1 
ATOM   9119  O  O   . GLY   A 1 1140 ? -57.09600  60.84200  4.87900   1.000 54.39015  ?  1138 GLY   A O   1 
ATOM   9120  N  N   . ILE   A 1 1141 ? -56.26000  62.76200  4.04000   1.000 40.97071  ?  1139 ILE   A N   1 
ATOM   9121  C  CA  . ILE   A 1 1141 ? -56.57200  62.46100  2.64900   1.000 46.80723  ?  1139 ILE   A CA  1 
ATOM   9122  C  C   . ILE   A 1 1141 ? -55.31300  62.62300  1.81100   1.000 36.15984  ?  1139 ILE   A C   1 
ATOM   9123  O  O   . ILE   A 1 1141 ? -54.52800  63.55400  2.02300   1.000 29.10462  ?  1139 ILE   A O   1 
ATOM   9124  C  CB  . ILE   A 1 1141 ? -57.69900  63.37000  2.11100   1.000 45.25651  ?  1139 ILE   A CB  1 
ATOM   9125  C  CG1 . ILE   A 1 1141 ? -58.93400  63.27400  3.00700   1.000 38.00771  ?  1139 ILE   A CG1 1 
ATOM   9126  C  CG2 . ILE   A 1 1141 ? -58.04300  63.01300  0.67300   1.000 37.75972  ?  1139 ILE   A CG2 1 
ATOM   9127  C  CD1 . ILE   A 1 1141 ? -59.73600  62.01500  2.79700   1.000 39.67988  ?  1139 ILE   A CD1 1 
ATOM   9128  N  N   . SER   A 1 1142 ? -55.12200  61.70900  0.86000   1.000 36.75547  ?  1140 SER   A N   1 
ATOM   9129  C  CA  . SER   A 1 1142 ? -54.04700  61.79800  -0.12800  1.000 40.48061  ?  1140 SER   A CA  1 
ATOM   9130  C  C   . SER   A 1 1142 ? -54.66100  61.44700  -1.48000  1.000 47.61298  ?  1140 SER   A C   1 
ATOM   9131  O  O   . SER   A 1 1142 ? -54.91100  60.27200  -1.76400  1.000 52.30124  ?  1140 SER   A O   1 
ATOM   9132  C  CB  . SER   A 1 1142 ? -52.89000  60.86800  0.22300   1.000 45.78356  ?  1140 SER   A CB  1 
ATOM   9133  O  OG  . SER   A 1 1142 ? -51.74300  61.13900  -0.56900  1.000 46.10655  ?  1140 SER   A OG  1 
ATOM   9134  N  N   . LYS   A 1 1143 ? -54.90900  62.46900  -2.30700  1.000 44.99958  ?  1141 LYS   A N   1 
ATOM   9135  C  CA  . LYS   A 1 1143 ? -55.52300  62.23400  -3.61200  1.000 50.15493  ?  1141 LYS   A CA  1 
ATOM   9136  C  C   . LYS   A 1 1143 ? -54.64000  61.37100  -4.50800  1.000 42.51573  ?  1141 LYS   A C   1 
ATOM   9137  O  O   . LYS   A 1 1143 ? -55.14600  60.67700  -5.39700  1.000 46.52572  ?  1141 LYS   A O   1 
ATOM   9138  C  CB  . LYS   A 1 1143 ? -55.82900  63.56500  -4.30200  1.000 47.61086  ?  1141 LYS   A CB  1 
ATOM   9139  C  CG  . LYS   A 1 1143 ? -56.69100  64.52200  -3.49000  1.000 54.27597  ?  1141 LYS   A CG  1 
ATOM   9140  C  CD  . LYS   A 1 1143 ? -56.88000  65.84800  -4.22200  1.000 46.38021  ?  1141 LYS   A CD  1 
ATOM   9141  C  CE  . LYS   A 1 1143 ? -56.66900  67.04100  -3.29600  1.000 59.42420  ?  1141 LYS   A CE  1 
ATOM   9142  N  NZ  . LYS   A 1 1143 ? -57.92000  67.45000  -2.59600  1.000 51.75549  ?  1141 LYS   A NZ  1 
ATOM   9143  N  N   . PHE   A 1 1144 ? -53.32700  61.40400  -4.29800  1.000 33.44469  ?  1142 PHE   A N   1 
ATOM   9144  C  CA  . PHE   A 1 1144 ? -52.38600  60.60300  -5.06800  1.000 46.56968  ?  1142 PHE   A CA  1 
ATOM   9145  C  C   . PHE   A 1 1144 ? -51.53100  59.78500  -4.10900  1.000 48.97008  ?  1142 PHE   A C   1 
ATOM   9146  O  O   . PHE   A 1 1144 ? -51.64800  59.89800  -2.88500  1.000 52.42116  ?  1142 PHE   A O   1 
ATOM   9147  C  CB  . PHE   A 1 1144 ? -51.50800  61.48200  -5.97100  1.000 40.34120  ?  1142 PHE   A CB  1 
ATOM   9148  C  CG  . PHE   A 1 1144 ? -52.28500  62.45400  -6.81500  1.000 45.59926  ?  1142 PHE   A CG  1 
ATOM   9149  C  CD1 . PHE   A 1 1144 ? -52.78800  62.07300  -8.04900  1.000 39.94514  ?  1142 PHE   A CD1 1 
ATOM   9150  C  CD2 . PHE   A 1 1144 ? -52.51500  63.74700  -6.37400  1.000 40.18687  ?  1142 PHE   A CD2 1 
ATOM   9151  C  CE1 . PHE   A 1 1144 ? -53.50500  62.96400  -8.82600  1.000 37.81148  ?  1142 PHE   A CE1 1 
ATOM   9152  C  CE2 . PHE   A 1 1144 ? -53.23200  64.64200  -7.14700  1.000 46.20112  ?  1142 PHE   A CE2 1 
ATOM   9153  C  CZ  . PHE   A 1 1144 ? -53.72700  64.24900  -8.37400  1.000 41.64225  ?  1142 PHE   A CZ  1 
ATOM   9154  N  N   . ASP   A 1 1145 ? -50.66400  58.94500  -4.68000  1.000 48.23561  ?  1143 ASP   A N   1 
ATOM   9155  C  CA  . ASP   A 1 1145 ? -49.73400  58.17900  -3.85800  1.000 38.28840  ?  1143 ASP   A CA  1 
ATOM   9156  C  C   . ASP   A 1 1145 ? -48.82000  59.10000  -3.06500  1.000 33.32496  ?  1143 ASP   A C   1 
ATOM   9157  O  O   . ASP   A 1 1145 ? -48.57200  58.87000  -1.87500  1.000 40.82704  ?  1143 ASP   A O   1 
ATOM   9158  C  CB  . ASP   A 1 1145 ? -48.90600  57.23700  -4.73400  1.000 41.70567  ?  1143 ASP   A CB  1 
ATOM   9159  C  CG  . ASP   A 1 1145 ? -49.75600  56.22900  -5.48100  1.000 60.30547  ?  1143 ASP   A CG  1 
ATOM   9160  O  OD1 . ASP   A 1 1145 ? -51.00000  56.27600  -5.35600  1.000 59.21112  ?  1143 ASP   A OD1 1 
ATOM   9161  O  OD2 . ASP   A 1 1145 ? -49.17200  55.38600  -6.19500  1.000 49.86231  -1 1143 ASP   A OD2 1 
ATOM   9162  N  N   . LEU   A 1 1146 ? -48.31500  60.15100  -3.70500  1.000 35.75001  ?  1144 LEU   A N   1 
ATOM   9163  C  CA  . LEU   A 1 1146 ? -47.39800  61.08300  -3.06400  1.000 34.32382  ?  1144 LEU   A CA  1 
ATOM   9164  C  C   . LEU   A 1 1146 ? -47.57800  62.44900  -3.70100  1.000 33.69763  ?  1144 LEU   A C   1 
ATOM   9165  O  O   . LEU   A 1 1146 ? -47.55800  62.56900  -4.93000  1.000 33.98528  ?  1144 LEU   A O   1 
ATOM   9166  C  CB  . LEU   A 1 1146 ? -45.94500  60.61600  -3.20400  1.000 35.87816  ?  1144 LEU   A CB  1 
ATOM   9167  C  CG  . LEU   A 1 1146 ? -44.89200  61.48700  -2.52400  1.000 38.29190  ?  1144 LEU   A CG  1 
ATOM   9168  C  CD1 . LEU   A 1 1146 ? -45.08600  61.46000  -1.01800  1.000 29.93533  ?  1144 LEU   A CD1 1 
ATOM   9169  C  CD2 . LEU   A 1 1146 ? -43.48700  61.03700  -2.90600  1.000 27.98086  ?  1144 LEU   A CD2 1 
ATOM   9170  N  N   . THR   A 1 1147 ? -47.75500  63.46900  -2.86800  1.000 38.31897  ?  1145 THR   A N   1 
ATOM   9171  C  CA  . THR   A 1 1147 ? -47.94100  64.83700  -3.32700  1.000 33.70332  ?  1145 THR   A CA  1 
ATOM   9172  C  C   . THR   A 1 1147 ? -46.92100  65.72000  -2.62800  1.000 31.79699  ?  1145 THR   A C   1 
ATOM   9173  O  O   . THR   A 1 1147 ? -46.74800  65.62600  -1.40900  1.000 33.02861  ?  1145 THR   A O   1 
ATOM   9174  C  CB  . THR   A 1 1147 ? -49.36200  65.33900  -3.04000  1.000 38.40762  ?  1145 THR   A CB  1 
ATOM   9175  O  OG1 . THR   A 1 1147 ? -50.31800  64.36000  -3.47000  1.000 51.37238  ?  1145 THR   A OG1 1 
ATOM   9176  C  CG2 . THR   A 1 1147 ? -49.62300  66.64800  -3.77100  1.000 34.75369  ?  1145 THR   A CG2 1 
ATOM   9177  N  N   . LEU   A 1 1148 ? -46.24300  66.56700  -3.39800  1.000 25.37430  ?  1146 LEU   A N   1 
ATOM   9178  C  CA  . LEU   A 1 1148 ? -45.25800  67.50200  -2.86700  1.000 30.83929  ?  1146 LEU   A CA  1 
ATOM   9179  C  C   . LEU   A 1 1148 ? -45.67200  68.91500  -3.24700  1.000 37.62792  ?  1146 LEU   A C   1 
ATOM   9180  O  O   . LEU   A 1 1148 ? -45.73400  69.25000  -4.43500  1.000 35.51416  ?  1146 LEU   A O   1 
ATOM   9181  C  CB  . LEU   A 1 1148 ? -43.85800  67.19500  -3.40200  1.000 24.91448  ?  1146 LEU   A CB  1 
ATOM   9182  C  CG  . LEU   A 1 1148 ? -42.97600  66.26300  -2.57400  1.000 30.62704  ?  1146 LEU   A CG  1 
ATOM   9183  C  CD1 . LEU   A 1 1148 ? -43.34100  64.82000  -2.85000  1.000 52.08607  ?  1146 LEU   A CD1 1 
ATOM   9184  C  CD2 . LEU   A 1 1148 ? -41.51100  66.50300  -2.89600  1.000 23.89102  ?  1146 LEU   A CD2 1 
ATOM   9185  N  N   . GLU   A 1 1149 ? -45.95700  69.73800  -2.24200  1.000 27.90962  ?  1147 GLU   A N   1 
ATOM   9186  C  CA  . GLU   A 1 1149 ? -46.29000  71.13900  -2.44300  1.000 28.81944  ?  1147 GLU   A CA  1 
ATOM   9187  C  C   . GLU   A 1 1149 ? -45.21900  71.99000  -1.78200  1.000 28.57967  ?  1147 GLU   A C   1 
ATOM   9188  O  O   . GLU   A 1 1149 ? -44.88400  71.77400  -0.61400  1.000 35.16154  ?  1147 GLU   A O   1 
ATOM   9189  C  CB  . GLU   A 1 1149 ? -47.67500  71.47200  -1.87500  1.000 40.88883  ?  1147 GLU   A CB  1 
ATOM   9190  C  CG  . GLU   A 1 1149 ? -48.11200  72.91200  -2.11500  1.000 46.89620  ?  1147 GLU   A CG  1 
ATOM   9191  C  CD  . GLU   A 1 1149 ? -49.45100  73.24500  -1.47700  1.000 59.24809  ?  1147 GLU   A CD  1 
ATOM   9192  O  OE1 . GLU   A 1 1149 ? -49.73600  72.74200  -0.36900  1.000 70.22958  ?  1147 GLU   A OE1 1 
ATOM   9193  O  OE2 . GLU   A 1 1149 ? -50.21600  74.02200  -2.08700  1.000 51.01390  -1 1147 GLU   A OE2 1 
ATOM   9194  N  N   . VAL   A 1 1150 ? -44.67500  72.94100  -2.53400  1.000 33.96730  ?  1148 VAL   A N   1 
ATOM   9195  C  CA  . VAL   A 1 1150 ? -43.67900  73.87700  -2.02600  1.000 35.26542  ?  1148 VAL   A CA  1 
ATOM   9196  C  C   . VAL   A 1 1150 ? -44.35400  75.21600  -1.77400  1.000 33.30022  ?  1148 VAL   A C   1 
ATOM   9197  O  O   . VAL   A 1 1150 ? -44.97700  75.78600  -2.67900  1.000 30.23204  ?  1148 VAL   A O   1 
ATOM   9198  C  CB  . VAL   A 1 1150 ? -42.50800  74.02500  -3.01000  1.000 28.81937  ?  1148 VAL   A CB  1 
ATOM   9199  C  CG1 . VAL   A 1 1150 ? -41.48300  75.02100  -2.47500  1.000 22.75454  ?  1148 VAL   A CG1 1 
ATOM   9200  C  CG2 . VAL   A 1 1150 ? -41.87500  72.66800  -3.26200  1.000 22.05800  ?  1148 VAL   A CG2 1 
ATOM   9201  N  N   . LEU   A 1 1151 ? -44.22900  75.72300  -0.55000  1.000 26.92127  ?  1149 LEU   A N   1 
ATOM   9202  C  CA  . LEU   A 1 1151 ? -44.83800  76.98400  -0.15100  1.000 33.20195  ?  1149 LEU   A CA  1 
ATOM   9203  C  C   . LEU   A 1 1151 ? -43.76200  77.93700  0.35100   1.000 32.53362  ?  1149 LEU   A C   1 
ATOM   9204  O  O   . LEU   A 1 1151 ? -42.98000  77.58200  1.24000   1.000 38.24934  ?  1149 LEU   A O   1 
ATOM   9205  C  CB  . LEU   A 1 1151 ? -45.89400  76.75800  0.93400   1.000 32.54959  ?  1149 LEU   A CB  1 
ATOM   9206  C  CG  . LEU   A 1 1151 ? -47.00200  75.76100  0.59100   1.000 39.25556  ?  1149 LEU   A CG  1 
ATOM   9207  C  CD1 . LEU   A 1 1151 ? -47.42800  74.99700  1.83200   1.000 37.20683  ?  1149 LEU   A CD1 1 
ATOM   9208  C  CD2 . LEU   A 1 1151 ? -48.19400  76.46200  -0.04600  1.000 35.13838  ?  1149 LEU   A CD2 1 
ATOM   9209  N  N   . GLU   A 1 1152 ? -43.72600  79.14400  -0.21400  1.000 32.89666  ?  1150 GLU   A N   1 
ATOM   9210  C  CA  . GLU   A 1 1152 ? -42.78300  80.17200  0.22200   1.000 36.44569  ?  1150 GLU   A CA  1 
ATOM   9211  C  C   . GLU   A 1 1152 ? -43.34900  80.86500  1.45600   1.000 45.62725  ?  1150 GLU   A C   1 
ATOM   9212  O  O   . GLU   A 1 1152 ? -44.34200  81.59300  1.36500   1.000 57.84855  ?  1150 GLU   A O   1 
ATOM   9213  C  CB  . GLU   A 1 1152 ? -42.52300  81.18000  -0.89300  1.000 36.90656  ?  1150 GLU   A CB  1 
ATOM   9214  C  CG  . GLU   A 1 1152 ? -42.00500  80.56800  -2.18300  1.000 47.75405  ?  1150 GLU   A CG  1 
ATOM   9215  C  CD  . GLU   A 1 1152 ? -41.40300  81.59700  -3.12500  1.000 63.73798  ?  1150 GLU   A CD  1 
ATOM   9216  O  OE1 . GLU   A 1 1152 ? -40.71300  82.52500  -2.64400  1.000 51.47944  ?  1150 GLU   A OE1 1 
ATOM   9217  O  OE2 . GLU   A 1 1152 ? -41.62200  81.47900  -4.34900  1.000 63.14984  -1 1150 GLU   A OE2 1 
ATOM   9218  N  N   . ARG   A 1 1153 ? -42.72200  80.64000  2.60900   1.000 42.01404  ?  1151 ARG   A N   1 
ATOM   9219  C  CA  . ARG   A 1 1153 ? -43.18300  81.20200  3.87100   1.000 45.02927  ?  1151 ARG   A CA  1 
ATOM   9220  C  C   . ARG   A 1 1153 ? -41.98500  81.61300  4.71400   1.000 41.78359  ?  1151 ARG   A C   1 
ATOM   9221  O  O   . ARG   A 1 1153 ? -41.00500  80.87000  4.81400   1.000 49.12363  ?  1151 ARG   A O   1 
ATOM   9222  C  CB  . ARG   A 1 1153 ? -44.04600  80.20100  4.66200   1.000 42.10576  ?  1151 ARG   A CB  1 
ATOM   9223  C  CG  . ARG   A 1 1153 ? -45.31900  79.72800  3.96200   1.000 41.61978  ?  1151 ARG   A CG  1 
ATOM   9224  C  CD  . ARG   A 1 1153 ? -46.41200  80.78800  3.99000   1.000 50.68719  ?  1151 ARG   A CD  1 
ATOM   9225  N  NE  . ARG   A 1 1153 ? -47.66300  80.30800  3.41400   1.000 52.76631  ?  1151 ARG   A NE  1 
ATOM   9226  C  CZ  . ARG   A 1 1153 ? -47.91800  80.24500  2.11300   1.000 60.06386  ?  1151 ARG   A CZ  1 
ATOM   9227  N  NH1 . ARG   A 1 1153 ? -47.01600  80.60200  1.21200   1.000 52.09601  ?  1151 ARG   A NH1 1 
ATOM   9228  N  NH2 . ARG   A 1 1153 ? -49.10700  79.80900  1.70400   1.000 72.23244  ?  1151 ARG   A NH2 1 
ATOM   9229  N  N   . GLU   A 1 1154 ? -42.07400  82.80200  5.31500   1.000 46.34148  ?  1152 GLU   A N   1 
ATOM   9230  C  CA  . GLU   A 1 1154 ? -41.08500  83.28300  6.28300   1.000 43.68480  ?  1152 GLU   A CA  1 
ATOM   9231  C  C   . GLU   A 1 1154 ? -39.68100  83.32400  5.68200   1.000 49.71433  ?  1152 GLU   A C   1 
ATOM   9232  O  O   . GLU   A 1 1154 ? -38.70600  82.89800  6.30500   1.000 48.30832  ?  1152 GLU   A O   1 
ATOM   9233  C  CB  . GLU   A 1 1154 ? -41.10600  82.43400  7.55600   1.000 42.79909  ?  1152 GLU   A CB  1 
ATOM   9234  C  CG  . GLU   A 1 1154 ? -42.45900  82.38300  8.25000   1.000 52.31297  ?  1152 GLU   A CG  1 
ATOM   9235  C  CD  . GLU   A 1 1154 ? -42.56100  83.36000  9.40600   1.000 76.87718  ?  1152 GLU   A CD  1 
ATOM   9236  O  OE1 . GLU   A 1 1154 ? -42.57000  84.58300  9.15400   1.000 82.26576  ?  1152 GLU   A OE1 1 
ATOM   9237  O  OE2 . GLU   A 1 1154 ? -42.63100  82.90400  10.56700  1.000 99.00940  -1 1152 GLU   A OE2 1 
ATOM   9238  N  N   . ASN   A 1 1155 ? -39.57900  83.83500  4.45800   1.000 45.98515  ?  1153 ASN   A N   1 
ATOM   9239  C  CA  . ASN   A 1 1155 ? -38.32600  83.92400  3.71400   1.000 46.83995  ?  1153 ASN   A CA  1 
ATOM   9240  C  C   . ASN   A 1 1155 ? -37.66900  82.56600  3.49800   1.000 47.67536  ?  1153 ASN   A C   1 
ATOM   9241  O  O   . ASN   A 1 1155 ? -36.49200  82.50700  3.12300   1.000 55.92943  ?  1153 ASN   A O   1 
ATOM   9242  C  CB  . ASN   A 1 1155 ? -37.33800  84.87800  4.39300   1.000 53.77481  ?  1153 ASN   A CB  1 
ATOM   9243  C  CG  . ASN   A 1 1155 ? -37.68600  86.32600  4.15700   1.000 69.00844  ?  1153 ASN   A CG  1 
ATOM   9244  O  OD1 . ASN   A 1 1155 ? -38.03100  86.71400  3.04100   1.000 74.95046  ?  1153 ASN   A OD1 1 
ATOM   9245  N  ND2 . ASN   A 1 1155 ? -37.59800  87.13800  5.20400   1.000 74.95860  ?  1153 ASN   A ND2 1 
ATOM   9246  N  N   . GLY   A 1 1156 ? -38.39800  81.47600  3.72600   1.000 40.81843  ?  1154 GLY   A N   1 
ATOM   9247  C  CA  . GLY   A 1 1156 ? -37.89700  80.13700  3.49300   1.000 37.91745  ?  1154 GLY   A CA  1 
ATOM   9248  C  C   . GLY   A 1 1156 ? -38.86400  79.31400  2.66800   1.000 40.11769  ?  1154 GLY   A C   1 
ATOM   9249  O  O   . GLY   A 1 1156 ? -39.72100  79.87400  1.97600   1.000 42.14923  ?  1154 GLY   A O   1 
ATOM   9250  N  N   . LEU   A 1 1157 ? -38.74700  77.98900  2.73000   1.000 32.91625  ?  1155 LEU   A N   1 
ATOM   9251  C  CA  . LEU   A 1 1157 ? -39.61000  77.09300  1.97100   1.000 28.34837  ?  1155 LEU   A CA  1 
ATOM   9252  C  C   . LEU   A 1 1157 ? -40.17900  76.02700  2.89300   1.000 36.37646  ?  1155 LEU   A C   1 
ATOM   9253  O  O   . LEU   A 1 1157 ? -39.42700  75.34700  3.59900   1.000 40.35331  ?  1155 LEU   A O   1 
ATOM   9254  C  CB  . LEU   A 1 1157 ? -38.84800  76.42400  0.82500   1.000 21.92105  ?  1155 LEU   A CB  1 
ATOM   9255  C  CG  . LEU   A 1 1157 ? -38.42800  77.31700  -0.33600  1.000 31.48985  ?  1155 LEU   A CG  1 
ATOM   9256  C  CD1 . LEU   A 1 1157 ? -37.65000  76.49200  -1.35300  1.000 21.51636  ?  1155 LEU   A CD1 1 
ATOM   9257  C  CD2 . LEU   A 1 1157 ? -39.64600  77.98400  -0.96300  1.000 33.15826  ?  1155 LEU   A CD2 1 
ATOM   9258  N  N   . ASN   A 1 1158 ? -41.50200  75.88400  2.88200   1.000 28.53824  ?  1156 ASN   A N   1 
ATOM   9259  C  CA  . ASN   A 1 1158 ? -42.19400  74.80800  3.58300   1.000 23.08591  ?  1156 ASN   A CA  1 
ATOM   9260  C  C   . ASN   A 1 1158 ? -42.64700  73.80000  2.53400   1.000 26.31750  ?  1156 ASN   A C   1 
ATOM   9261  O  O   . ASN   A 1 1158 ? -43.54800  74.08800  1.73700   1.000 36.91572  ?  1156 ASN   A O   1 
ATOM   9262  C  CB  . ASN   A 1 1158 ? -43.37500  75.34100  4.39100   1.000 25.49326  ?  1156 ASN   A CB  1 
ATOM   9263  C  CG  . ASN   A 1 1158 ? -42.94200  76.22200  5.55200   1.000 36.41904  ?  1156 ASN   A CG  1 
ATOM   9264  O  OD1 . ASN   A 1 1158 ? -41.76200  76.28900  5.89100   1.000 43.89922  ?  1156 ASN   A OD1 1 
ATOM   9265  N  ND2 . ASN   A 1 1158 ? -43.90000  76.91000  6.16200   1.000 29.98789  ?  1156 ASN   A ND2 1 
ATOM   9266  N  N   . ILE   A 1 1159 ? -42.01300  72.63100  2.52600   1.000 31.92729  ?  1157 ILE   A N   1 
ATOM   9267  C  CA  . ILE   A 1 1159 ? -42.30200  71.57400  1.56300   1.000 32.91356  ?  1157 ILE   A CA  1 
ATOM   9268  C  C   . ILE   A 1 1159 ? -43.13100  70.50400  2.26000   1.000 34.86095  ?  1157 ILE   A C   1 
ATOM   9269  O  O   . ILE   A 1 1159 ? -42.68900  69.91100  3.25200   1.000 39.33198  ?  1157 ILE   A O   1 
ATOM   9270  C  CB  . ILE   A 1 1159 ? -41.01100  70.98200  0.97800   1.000 28.11564  ?  1157 ILE   A CB  1 
ATOM   9271  C  CG1 . ILE   A 1 1159 ? -40.02000  72.10300  0.65600   1.000 23.67326  ?  1157 ILE   A CG1 1 
ATOM   9272  C  CG2 . ILE   A 1 1159 ? -41.31800  70.14700  -0.25200  1.000 25.89918  ?  1157 ILE   A CG2 1 
ATOM   9273  C  CD1 . ILE   A 1 1159 ? -38.87600  71.67400  -0.23100  1.000 29.24481  ?  1157 ILE   A CD1 1 
ATOM   9274  N  N   . VAL   A 1 1160 ? -44.33100  70.26000  1.74000   1.000 31.15537  ?  1158 VAL   A N   1 
ATOM   9275  C  CA  . VAL   A 1 1160 ? -45.26900  69.29400  2.30200   1.000 36.19246  ?  1158 VAL   A CA  1 
ATOM   9276  C  C   . VAL   A 1 1160 ? -45.14300  67.97600  1.55400   1.000 42.72595  ?  1158 VAL   A C   1 
ATOM   9277  O  O   . VAL   A 1 1160 ? -44.96000  67.95800  0.32900   1.000 52.81577  ?  1158 VAL   A O   1 
ATOM   9278  C  CB  . VAL   A 1 1160 ? -46.71000  69.82400  2.23000   1.000 36.35231  ?  1158 VAL   A CB  1 
ATOM   9279  C  CG1 . VAL   A 1 1160 ? -47.67000  68.87600  2.93400   1.000 35.39594  ?  1158 VAL   A CG1 1 
ATOM   9280  C  CG2 . VAL   A 1 1160 ? -46.77700  71.20500  2.83000   1.000 32.29273  ?  1158 VAL   A CG2 1 
ATOM   9281  N  N   . PHE   A 1 1161 ? -45.25300  66.87100  2.28500   1.000 32.46546  ?  1159 PHE   A N   1 
ATOM   9282  C  CA  . PHE   A 1 1161 ? -45.13100  65.52800  1.72300   1.000 31.00103  ?  1159 PHE   A CA  1 
ATOM   9283  C  C   . PHE   A 1 1161 ? -46.41300  64.77400  2.05100   1.000 32.51860  ?  1159 PHE   A C   1 
ATOM   9284  O  O   . PHE   A 1 1161 ? -46.45700  63.97300  2.98600   1.000 50.06866  ?  1159 PHE   A O   1 
ATOM   9285  C  CB  . PHE   A 1 1161 ? -43.89600  64.79800  2.27400   1.000 31.17982  ?  1159 PHE   A CB  1 
ATOM   9286  C  CG  . PHE   A 1 1161 ? -42.58400  65.37400  1.82000   1.000 29.48253  ?  1159 PHE   A CG  1 
ATOM   9287  C  CD1 . PHE   A 1 1161 ? -42.05000  66.49100  2.44400   1.000 35.66798  ?  1159 PHE   A CD1 1 
ATOM   9288  C  CD2 . PHE   A 1 1161 ? -41.86700  64.77700  0.79500   1.000 26.23549  ?  1159 PHE   A CD2 1 
ATOM   9289  C  CE1 . PHE   A 1 1161 ? -40.83700  67.01600  2.03900   1.000 41.92776  ?  1159 PHE   A CE1 1 
ATOM   9290  C  CE2 . PHE   A 1 1161 ? -40.65400  65.29600  0.38600   1.000 28.50844  ?  1159 PHE   A CE2 1 
ATOM   9291  C  CZ  . PHE   A 1 1161 ? -40.13800  66.41800  1.00900   1.000 37.65144  ?  1159 PHE   A CZ  1 
ATOM   9292  N  N   . GLU   A 1 1162 ? -47.46600  65.04700  1.28500   1.000 33.96962  ?  1160 GLU   A N   1 
ATOM   9293  C  CA  . GLU   A 1 1162 ? -48.72700  64.33500  1.44000   1.000 33.42695  ?  1160 GLU   A CA  1 
ATOM   9294  C  C   . GLU   A 1 1162 ? -48.61700  62.96000  0.79100   1.000 39.20432  ?  1160 GLU   A C   1 
ATOM   9295  O  O   . GLU   A 1 1162 ? -48.26700  62.85000  -0.38800  1.000 49.18611  ?  1160 GLU   A O   1 
ATOM   9296  C  CB  . GLU   A 1 1162 ? -49.86400  65.13800  0.81300   1.000 35.28497  ?  1160 GLU   A CB  1 
ATOM   9297  C  CG  . GLU   A 1 1162 ? -51.20000  64.42400  0.78600   1.000 42.84668  ?  1160 GLU   A CG  1 
ATOM   9298  C  CD  . GLU   A 1 1162 ? -52.24600  65.19200  0.00300   1.000 54.27776  ?  1160 GLU   A CD  1 
ATOM   9299  O  OE1 . GLU   A 1 1162 ? -52.59900  66.31200  0.42900   1.000 46.72189  ?  1160 GLU   A OE1 1 
ATOM   9300  O  OE2 . GLU   A 1 1162 ? -52.71500  64.67700  -1.03600  1.000 64.11624  -1 1160 GLU   A OE2 1 
ATOM   9301  N  N   . TYR   A 1 1163 ? -48.91000  61.91200  1.56000   1.000 32.64921  ?  1161 TYR   A N   1 
ATOM   9302  C  CA  . TYR   A 1 1163 ? -48.66700  60.55000  1.10800   1.000 35.72405  ?  1161 TYR   A CA  1 
ATOM   9303  C  C   . TYR   A 1 1163 ? -49.82800  59.64400  1.49200   1.000 46.58156  ?  1161 TYR   A C   1 
ATOM   9304  O  O   . TYR   A 1 1163 ? -50.50700  59.86800  2.49600   1.000 39.12622  ?  1161 TYR   A O   1 
ATOM   9305  C  CB  . TYR   A 1 1163 ? -47.36400  59.99200  1.69500   1.000 32.85647  ?  1161 TYR   A CB  1 
ATOM   9306  C  CG  . TYR   A 1 1163 ? -47.31600  59.95700  3.21400   1.000 38.94092  ?  1161 TYR   A CG  1 
ATOM   9307  C  CD1 . TYR   A 1 1163 ? -46.94700  61.07900  3.94500   1.000 27.24728  ?  1161 TYR   A CD1 1 
ATOM   9308  C  CD2 . TYR   A 1 1163 ? -47.62200  58.79400  3.91600   1.000 35.89528  ?  1161 TYR   A CD2 1 
ATOM   9309  C  CE1 . TYR   A 1 1163 ? -46.89300  61.05200  5.33300   1.000 28.76444  ?  1161 TYR   A CE1 1 
ATOM   9310  C  CE2 . TYR   A 1 1163 ? -47.57100  58.75700  5.30600   1.000 28.69892  ?  1161 TYR   A CE2 1 
ATOM   9311  C  CZ  . TYR   A 1 1163 ? -47.20600  59.89000  6.00800   1.000 38.89065  ?  1161 TYR   A CZ  1 
ATOM   9312  O  OH  . TYR   A 1 1163 ? -47.15200  59.86300  7.38700   1.000 36.46429  ?  1161 TYR   A OH  1 
ATOM   9313  N  N   . ASN   A 1 1164 ? -50.03900  58.61000  0.68100   1.000 37.75394  ?  1162 ASN   A N   1 
ATOM   9314  C  CA  . ASN   A 1 1164 ? -51.03800  57.59400  0.98700   1.000 30.99791  ?  1162 ASN   A CA  1 
ATOM   9315  C  C   . ASN   A 1 1164 ? -50.53000  56.69500  2.10800   1.000 39.65023  ?  1162 ASN   A C   1 
ATOM   9316  O  O   . ASN   A 1 1164 ? -49.44300  56.11600  2.00600   1.000 40.50309  ?  1162 ASN   A O   1 
ATOM   9317  C  CB  . ASN   A 1 1164 ? -51.34700  56.77300  -0.26000  1.000 35.17003  ?  1162 ASN   A CB  1 
ATOM   9318  C  CG  . ASN   A 1 1164 ? -52.55500  55.88200  -0.08200  1.000 39.80723  ?  1162 ASN   A CG  1 
ATOM   9319  O  OD1 . ASN   A 1 1164 ? -52.42200  54.67300  0.08400   1.000 46.78268  ?  1162 ASN   A OD1 1 
ATOM   9320  N  ND2 . ASN   A 1 1164 ? -53.74400  56.47300  -0.13100  1.000 49.81279  ?  1162 ASN   A ND2 1 
ATOM   9321  N  N   . THR   A 1 1165 ? -51.31900  56.56700  3.17600   1.000 44.15383  ?  1163 THR   A N   1 
ATOM   9322  C  CA  . THR   A 1 1165 ? -50.86600  55.81000  4.33800   1.000 35.19461  ?  1163 THR   A CA  1 
ATOM   9323  C  C   . THR   A 1 1165 ? -50.88700  54.30500  4.10400   1.000 46.37454  ?  1163 THR   A C   1 
ATOM   9324  O  O   . THR   A 1 1165 ? -50.27800  53.56400  4.88200   1.000 48.71355  ?  1163 THR   A O   1 
ATOM   9325  C  CB  . THR   A 1 1165 ? -51.71700  56.15700  5.55700   1.000 36.12478  ?  1163 THR   A CB  1 
ATOM   9326  O  OG1 . THR   A 1 1165 ? -53.10200  56.16600  5.18800   1.000 55.60254  ?  1163 THR   A OG1 1 
ATOM   9327  C  CG2 . THR   A 1 1165 ? -51.32800  57.52900  6.09400   1.000 27.78076  ?  1163 THR   A CG2 1 
ATOM   9328  N  N   . HIS   A 1 1166 ? -51.57000  53.83400  3.05900   1.000 44.61494  ?  1164 HIS   A N   1 
ATOM   9329  C  CA  . HIS   A 1 1166 ? -51.51600  52.41700  2.72600   1.000 37.27345  ?  1164 HIS   A CA  1 
ATOM   9330  C  C   . HIS   A 1 1166 ? -50.24900  52.04800  1.96800   1.000 42.26653  ?  1164 HIS   A C   1 
ATOM   9331  O  O   . HIS   A 1 1166 ? -49.91100  50.86200  1.89200   1.000 54.90142  ?  1164 HIS   A O   1 
ATOM   9332  C  CB  . HIS   A 1 1166 ? -52.74100  52.01000  1.90400   1.000 37.08727  ?  1164 HIS   A CB  1 
ATOM   9333  C  CG  . HIS   A 1 1166 ? -54.04000  52.15800  2.63500   1.000 45.22903  ?  1164 HIS   A CG  1 
ATOM   9334  N  ND1 . HIS   A 1 1166 ? -54.63100  51.11800  3.31900   1.000 42.76653  ?  1164 HIS   A ND1 1 
ATOM   9335  C  CD2 . HIS   A 1 1166 ? -54.87100  53.21900  2.77400   1.000 58.81373  ?  1164 HIS   A CD2 1 
ATOM   9336  C  CE1 . HIS   A 1 1166 ? -55.76500  51.53400  3.85500   1.000 66.93909  ?  1164 HIS   A CE1 1 
ATOM   9337  N  NE2 . HIS   A 1 1166 ? -55.93400  52.80500  3.53900   1.000 54.81811  ?  1164 HIS   A NE2 1 
ATOM   9338  N  N   . LEU   A 1 1167 ? -49.53800  53.03200  1.41400   1.000 41.65001  ?  1165 LEU   A N   1 
ATOM   9339  C  CA  . LEU   A 1 1167 ? -48.31000  52.78200  0.67300   1.000 46.53852  ?  1165 LEU   A CA  1 
ATOM   9340  C  C   . LEU   A 1 1167 ? -47.05200  53.22100  1.40600   1.000 39.58574  ?  1165 LEU   A C   1 
ATOM   9341  O  O   . LEU   A 1 1167 ? -45.97300  52.70300  1.10900   1.000 37.74878  ?  1165 LEU   A O   1 
ATOM   9342  C  CB  . LEU   A 1 1167 ? -48.36000  53.48900  -0.68900  1.000 43.91300  ?  1165 LEU   A CB  1 
ATOM   9343  C  CG  . LEU   A 1 1167 ? -49.47300  53.01100  -1.62200  1.000 42.55358  ?  1165 LEU   A CG  1 
ATOM   9344  C  CD1 . LEU   A 1 1167 ? -49.47200  53.82100  -2.90200  1.000 51.02734  ?  1165 LEU   A CD1 1 
ATOM   9345  C  CD2 . LEU   A 1 1167 ? -49.32300  51.52700  -1.92500  1.000 52.32052  ?  1165 LEU   A CD2 1 
ATOM   9346  N  N   . PHE   A 1 1168 ? -47.16300  54.16100  2.34200   1.000 43.46131  ?  1166 PHE   A N   1 
ATOM   9347  C  CA  . PHE   A 1 1168 ? -46.03500  54.62800  3.13200   1.000 34.34708  ?  1166 PHE   A CA  1 
ATOM   9348  C  C   . PHE   A 1 1168 ? -46.47600  54.73300  4.58200   1.000 39.23345  ?  1166 PHE   A C   1 
ATOM   9349  O  O   . PHE   A 1 1168 ? -47.65400  54.96100  4.86600   1.000 44.30762  ?  1166 PHE   A O   1 
ATOM   9350  C  CB  . PHE   A 1 1168 ? -45.52300  55.99400  2.65100   1.000 36.67564  ?  1166 PHE   A CB  1 
ATOM   9351  C  CG  . PHE   A 1 1168 ? -45.33600  56.08900  1.16300   1.000 35.64515  ?  1166 PHE   A CG  1 
ATOM   9352  C  CD1 . PHE   A 1 1168 ? -44.12600  55.75000  0.57800   1.000 42.49718  ?  1166 PHE   A CD1 1 
ATOM   9353  C  CD2 . PHE   A 1 1168 ? -46.37200  56.51400  0.34800   1.000 35.35342  ?  1166 PHE   A CD2 1 
ATOM   9354  C  CE1 . PHE   A 1 1168 ? -43.95400  55.83800  -0.79200  1.000 35.97300  ?  1166 PHE   A CE1 1 
ATOM   9355  C  CE2 . PHE   A 1 1168 ? -46.20700  56.60100  -1.02100  1.000 34.30837  ?  1166 PHE   A CE2 1 
ATOM   9356  C  CZ  . PHE   A 1 1168 ? -44.99700  56.26400  -1.59100  1.000 34.67297  ?  1166 PHE   A CZ  1 
ATOM   9357  N  N   . ASP   A 1 1169 ? -45.52900  54.56900  5.49900   1.000 44.39781  ?  1167 ASP   A N   1 
ATOM   9358  C  CA  . ASP   A 1 1169 ? -45.80400  54.73100  6.92100   1.000 50.28212  ?  1167 ASP   A CA  1 
ATOM   9359  C  C   . ASP   A 1 1169 ? -44.88400  55.80400  7.49700   1.000 46.28875  ?  1167 ASP   A C   1 
ATOM   9360  O  O   . ASP   A 1 1169 ? -44.04300  56.37100  6.79400   1.000 48.08678  ?  1167 ASP   A O   1 
ATOM   9361  C  CB  . ASP   A 1 1169 ? -45.68400  53.39100  7.66400   1.000 53.04384  ?  1167 ASP   A CB  1 
ATOM   9362  C  CG  . ASP   A 1 1169 ? -44.30500  52.75900  7.55200   1.000 67.69930  ?  1167 ASP   A CG  1 
ATOM   9363  O  OD1 . ASP   A 1 1169 ? -43.29500  53.49000  7.52200   1.000 78.69788  ?  1167 ASP   A OD1 1 
ATOM   9364  O  OD2 . ASP   A 1 1169 ? -44.23500  51.51300  7.47200   1.000 58.71025  -1 1167 ASP   A OD2 1 
ATOM   9365  N  N   . GLU   A 1 1170 ? -45.06400  56.08100  8.79200   1.000 57.17282  ?  1168 GLU   A N   1 
ATOM   9366  C  CA  . GLU   A 1 1170 ? -44.34700  57.17800  9.43800   1.000 59.39147  ?  1168 GLU   A CA  1 
ATOM   9367  C  C   . GLU   A 1 1170 ? -42.84300  57.09000  9.19800   1.000 58.68262  ?  1168 GLU   A C   1 
ATOM   9368  O  O   . GLU   A 1 1170 ? -42.18900  58.10300  8.92200   1.000 55.56753  ?  1168 GLU   A O   1 
ATOM   9369  C  CB  . GLU   A 1 1170 ? -44.65900  57.18500  10.93700  1.000 49.36953  ?  1168 GLU   A CB  1 
ATOM   9370  C  CG  . GLU   A 1 1170 ? -45.15800  58.52000  11.47300  1.000 72.53825  ?  1168 GLU   A CG  1 
ATOM   9371  C  CD  . GLU   A 1 1170 ? -44.14300  59.21100  12.37100  1.000 102.88681 ?  1168 GLU   A CD  1 
ATOM   9372  O  OE1 . GLU   A 1 1170 ? -43.36300  58.50600  13.04900  1.000 97.95421  ?  1168 GLU   A OE1 1 
ATOM   9373  O  OE2 . GLU   A 1 1170 ? -44.12600  60.46000  12.40100  1.000 91.54133  -1 1168 GLU   A OE2 1 
ATOM   9374  N  N   . GLY   A 1 1171 ? -42.28300  55.88100  9.26200   1.000 42.49013  ?  1169 GLY   A N   1 
ATOM   9375  C  CA  . GLY   A 1 1171 ? -40.84500  55.73700  9.09700   1.000 59.17014  ?  1169 GLY   A CA  1 
ATOM   9376  C  C   . GLY   A 1 1171 ? -40.38700  55.89300  7.65900   1.000 48.24379  ?  1169 GLY   A C   1 
ATOM   9377  O  O   . GLY   A 1 1171 ? -39.34700  56.50200  7.39400   1.000 51.54162  ?  1169 GLY   A O   1 
ATOM   9378  N  N   . MET   A 1 1172 ? -41.15000  55.34200  6.71300   1.000 54.23704  ?  1170 MET   A N   1 
ATOM   9379  C  CA  . MET   A 1 1172 ? -40.74300  55.38000  5.31100   1.000 45.12307  ?  1170 MET   A CA  1 
ATOM   9380  C  C   . MET   A 1 1172 ? -40.64500  56.81500  4.80100   1.000 48.56628  ?  1170 MET   A C   1 
ATOM   9381  O  O   . MET   A 1 1172 ? -39.63900  57.20300  4.19300   1.000 42.48278  ?  1170 MET   A O   1 
ATOM   9382  C  CB  . MET   A 1 1172 ? -41.73000  54.57600  4.46400   1.000 36.14853  ?  1170 MET   A CB  1 
ATOM   9383  C  CG  . MET   A 1 1172 ? -41.88700  53.12000  4.88000   1.000 46.51391  ?  1170 MET   A CG  1 
ATOM   9384  S  SD  . MET   A 1 1172 ? -42.63900  52.12600  3.58000   1.000 46.71521  ?  1170 MET   A SD  1 
ATOM   9385  C  CE  . MET   A 1 1172 ? -41.91300  52.90500  2.14500   1.000 62.70066  ?  1170 MET   A CE  1 
ATOM   9386  N  N   . ILE   A 1 1173 ? -41.68600  57.61900  5.04000   1.000 38.05842  ?  1171 ILE   A N   1 
ATOM   9387  C  CA  . ILE   A 1 1173 ? -41.69500  58.99400  4.54500   1.000 39.53914  ?  1171 ILE   A CA  1 
ATOM   9388  C  C   . ILE   A 1 1173 ? -40.55900  59.79400  5.16800   1.000 43.81933  ?  1171 ILE   A C   1 
ATOM   9389  O  O   . ILE   A 1 1173 ? -39.87700  60.56900  4.48400   1.000 41.43015  ?  1171 ILE   A O   1 
ATOM   9390  C  CB  . ILE   A 1 1173 ? -43.06700  59.64700  4.80500   1.000 36.79106  ?  1171 ILE   A CB  1 
ATOM   9391  C  CG1 . ILE   A 1 1173 ? -44.10000  59.09500  3.82700   1.000 42.04137  ?  1171 ILE   A CG1 1 
ATOM   9392  C  CG2 . ILE   A 1 1173 ? -42.99100  61.16300  4.66200   1.000 34.81614  ?  1171 ILE   A CG2 1 
ATOM   9393  C  CD1 . ILE   A 1 1173 ? -43.81500  59.44000  2.37700   1.000 42.84551  ?  1171 ILE   A CD1 1 
ATOM   9394  N  N   . LEU   A 1 1174 ? -40.32500  59.60700  6.47100   1.000 36.50090  ?  1172 LEU   A N   1 
ATOM   9395  C  CA  . LEU   A 1 1174 ? -39.23300  60.31100  7.13900   1.000 41.90848  ?  1172 LEU   A CA  1 
ATOM   9396  C  C   . LEU   A 1 1174 ? -37.90000  60.04900  6.44800   1.000 34.28360  ?  1172 LEU   A C   1 
ATOM   9397  O  O   . LEU   A 1 1174 ? -37.05700  60.94700  6.34500   1.000 37.71201  ?  1172 LEU   A O   1 
ATOM   9398  C  CB  . LEU   A 1 1174 ? -39.16400  59.89700  8.61000   1.000 46.86090  ?  1172 LEU   A CB  1 
ATOM   9399  C  CG  . LEU   A 1 1174 ? -39.99700  60.72700  9.58600   1.000 59.70680  ?  1172 LEU   A CG  1 
ATOM   9400  C  CD1 . LEU   A 1 1174 ? -40.39900  59.89800  10.79400  1.000 39.21770  ?  1172 LEU   A CD1 1 
ATOM   9401  C  CD2 . LEU   A 1 1174 ? -39.23000  61.96500  10.01300  1.000 56.72780  ?  1172 LEU   A CD2 1 
ATOM   9402  N  N   . ARG   A 1 1175 ? -37.69900  58.82200  5.95900   1.000 36.06272  ?  1173 ARG   A N   1 
ATOM   9403  C  CA  . ARG   A 1 1175 ? -36.50300  58.51800  5.18100   1.000 30.19962  ?  1173 ARG   A CA  1 
ATOM   9404  C  C   . ARG   A 1 1175 ? -36.48000  59.29800  3.87400   1.000 33.98719  ?  1173 ARG   A C   1 
ATOM   9405  O  O   . ARG   A 1 1175 ? -35.43600  59.82800  3.47700   1.000 39.66246  ?  1173 ARG   A O   1 
ATOM   9406  C  CB  . ARG   A 1 1175 ? -36.42800  57.01800  4.89800   1.000 34.84087  ?  1173 ARG   A CB  1 
ATOM   9407  C  CG  . ARG   A 1 1175 ? -35.28900  56.31000  5.59600   1.000 43.06136  ?  1173 ARG   A CG  1 
ATOM   9408  C  CD  . ARG   A 1 1175 ? -35.22200  54.85200  5.18400   1.000 29.22614  ?  1173 ARG   A CD  1 
ATOM   9409  N  NE  . ARG   A 1 1175 ? -36.17400  54.03400  5.92200   1.000 42.32674  ?  1173 ARG   A NE  1 
ATOM   9410  C  CZ  . ARG   A 1 1175 ? -37.25200  53.47900  5.38700   1.000 50.06415  ?  1173 ARG   A CZ  1 
ATOM   9411  N  NH1 . ARG   A 1 1175 ? -37.54100  53.62700  4.10500   1.000 51.83540  ?  1173 ARG   A NH1 1 
ATOM   9412  N  NH2 . ARG   A 1 1175 ? -38.06100  52.76000  6.15900   1.000 47.96300  ?  1173 ARG   A NH2 1 
ATOM   9413  N  N   . MET   A 1 1176 ? -37.62200  59.37300  3.18500   1.000 32.81321  ?  1174 MET   A N   1 
ATOM   9414  C  CA  . MET   A 1 1176 ? -37.65700  60.05500  1.89600   1.000 35.59549  ?  1174 MET   A CA  1 
ATOM   9415  C  C   . MET   A 1 1176 ? -37.49100  61.55900  2.04900   1.000 38.10630  ?  1174 MET   A C   1 
ATOM   9416  O  O   . MET   A 1 1176 ? -36.93800  62.21500  1.15900   1.000 37.20526  ?  1174 MET   A O   1 
ATOM   9417  C  CB  . MET   A 1 1176 ? -38.96300  59.74600  1.17400   1.000 35.42898  ?  1174 MET   A CB  1 
ATOM   9418  C  CG  . MET   A 1 1176 ? -39.11100  58.30000  0.77100   1.000 41.29419  ?  1174 MET   A CG  1 
ATOM   9419  S  SD  . MET   A 1 1176 ? -40.85200  57.84200  0.74100   1.000 38.46953  ?  1174 MET   A SD  1 
ATOM   9420  C  CE  . MET   A 1 1176 ? -41.37000  58.55200  -0.81900  1.000 22.25831  ?  1174 MET   A CE  1 
ATOM   9421  N  N   . VAL   A 1 1177 ? -37.96600  62.12400  3.15900   1.000 33.93368  ?  1175 VAL   A N   1 
ATOM   9422  C  CA  . VAL   A 1 1177 ? -37.78700  63.55300  3.38700   1.000 41.70693  ?  1175 VAL   A CA  1 
ATOM   9423  C  C   . VAL   A 1 1177 ? -36.31300  63.87900  3.57900   1.000 39.13330  ?  1175 VAL   A C   1 
ATOM   9424  O  O   . VAL   A 1 1177 ? -35.81400  64.89000  3.06800   1.000 35.23371  ?  1175 VAL   A O   1 
ATOM   9425  C  CB  . VAL   A 1 1177 ? -38.63500  64.00900  4.58600   1.000 32.89973  ?  1175 VAL   A CB  1 
ATOM   9426  C  CG1 . VAL   A 1 1177 ? -38.37800  65.46900  4.88700   1.000 24.25153  ?  1175 VAL   A CG1 1 
ATOM   9427  C  CG2 . VAL   A 1 1177 ? -40.10800  63.78000  4.29600   1.000 32.72696  ?  1175 VAL   A CG2 1 
ATOM   9428  N  N   . ALA   A 1 1178 ? -35.59300  63.02400  4.30900   1.000 37.68151  ?  1176 ALA   A N   1 
ATOM   9429  C  CA  . ALA   A 1 1178 ? -34.16800  63.24400  4.52100   1.000 31.80425  ?  1176 ALA   A CA  1 
ATOM   9430  C  C   . ALA   A 1 1178 ? -33.37100  63.02900  3.24200   1.000 38.21231  ?  1176 ALA   A C   1 
ATOM   9431  O  O   . ALA   A 1 1178 ? -32.31100  63.64100  3.06300   1.000 40.94598  ?  1176 ALA   A O   1 
ATOM   9432  C  CB  . ALA   A 1 1178 ? -33.65600  62.32400  5.62600   1.000 31.56039  ?  1176 ALA   A CB  1 
ATOM   9433  N  N   . GLN   A 1 1179 ? -33.86100  62.17000  2.34700   1.000 33.89572  ?  1177 GLN   A N   1 
ATOM   9434  C  CA  . GLN   A 1 1179 ? -33.16800  61.96200  1.08100   1.000 42.02292  ?  1177 GLN   A CA  1 
ATOM   9435  C  C   . GLN   A 1 1179 ? -33.36900  63.14700  0.14600   1.000 40.58407  ?  1177 GLN   A C   1 
ATOM   9436  O  O   . GLN   A 1 1179 ? -32.45500  63.51400  -0.60300  1.000 47.81914  ?  1177 GLN   A O   1 
ATOM   9437  C  CB  . GLN   A 1 1179 ? -33.64200  60.66500  0.42600   1.000 42.70921  ?  1177 GLN   A CB  1 
ATOM   9438  C  CG  . GLN   A 1 1179 ? -33.20100  59.41600  1.17100   1.000 42.02853  ?  1177 GLN   A CG  1 
ATOM   9439  C  CD  . GLN   A 1 1179 ? -33.94300  58.17200  0.72800   1.000 41.51961  ?  1177 GLN   A CD  1 
ATOM   9440  O  OE1 . GLN   A 1 1179 ? -34.72400  58.20300  -0.22500  1.000 48.87138  ?  1177 GLN   A OE1 1 
ATOM   9441  N  NE2 . GLN   A 1 1179 ? -33.70200  57.06500  1.42000   1.000 36.90198  ?  1177 GLN   A NE2 1 
ATOM   9442  N  N   . PHE   A 1 1180 ? -34.55400  63.76000  0.17300   1.000 41.45389  ?  1178 PHE   A N   1 
ATOM   9443  C  CA  . PHE   A 1 1180 ? -34.77500  64.96200  -0.62400  1.000 39.99375  ?  1178 PHE   A CA  1 
ATOM   9444  C  C   . PHE   A 1 1180 ? -33.88500  66.09900  -0.14000  1.000 34.35480  ?  1178 PHE   A C   1 
ATOM   9445  O  O   . PHE   A 1 1180 ? -33.24700  66.79200  -0.94200  1.000 29.48344  ?  1178 PHE   A O   1 
ATOM   9446  C  CB  . PHE   A 1 1180 ? -36.24700  65.37000  -0.57500  1.000 28.47217  ?  1178 PHE   A CB  1 
ATOM   9447  C  CG  . PHE   A 1 1180 ? -36.59100  66.48600  -1.51700  1.000 30.68495  ?  1178 PHE   A CG  1 
ATOM   9448  C  CD1 . PHE   A 1 1180 ? -36.79400  66.23700  -2.86400  1.000 29.53448  ?  1178 PHE   A CD1 1 
ATOM   9449  C  CD2 . PHE   A 1 1180 ? -36.69000  67.78900  -1.06000  1.000 31.38853  ?  1178 PHE   A CD2 1 
ATOM   9450  C  CE1 . PHE   A 1 1180 ? -37.10200  67.26400  -3.73400  1.000 38.18473  ?  1178 PHE   A CE1 1 
ATOM   9451  C  CE2 . PHE   A 1 1180 ? -36.99600  68.82000  -1.92600  1.000 33.96133  ?  1178 PHE   A CE2 1 
ATOM   9452  C  CZ  . PHE   A 1 1180 ? -37.20400  68.55700  -3.26400  1.000 42.32095  ?  1178 PHE   A CZ  1 
ATOM   9453  N  N   . GLU   A 1 1181 ? -33.82700  66.30100  1.17900   1.000 37.51851  ?  1179 GLU   A N   1 
ATOM   9454  C  CA  . GLU   A 1 1181 ? -32.93600  67.31100  1.73900   1.000 33.76560  ?  1179 GLU   A CA  1 
ATOM   9455  C  C   . GLU   A 1 1181 ? -31.48400  67.01400  1.39200   1.000 40.02858  ?  1179 GLU   A C   1 
ATOM   9456  O  O   . GLU   A 1 1181 ? -30.71500  67.92500  1.06100   1.000 36.12900  ?  1179 GLU   A O   1 
ATOM   9457  C  CB  . GLU   A 1 1181 ? -33.11900  67.38200  3.25300   1.000 29.42093  ?  1179 GLU   A CB  1 
ATOM   9458  C  CG  . GLU   A 1 1181 ? -32.14800  68.31100  3.95800   1.000 37.35532  ?  1179 GLU   A CG  1 
ATOM   9459  C  CD  . GLU   A 1 1181 ? -32.27900  68.24700  5.46800   1.000 43.84679  ?  1179 GLU   A CD  1 
ATOM   9460  O  OE1 . GLU   A 1 1181 ? -32.34200  67.12500  6.01600   1.000 42.61140  ?  1179 GLU   A OE1 1 
ATOM   9461  O  OE2 . GLU   A 1 1181 ? -32.32500  69.31900  6.10700   1.000 50.59576  -1 1179 GLU   A OE2 1 
ATOM   9462  N  N   . HIS   A 1 1182 ? -31.09300  65.74000  1.46200   1.000 41.14901  ?  1180 HIS   A N   1 
ATOM   9463  C  CA  . HIS   A 1 1182 ? -29.72700  65.36400  1.12200   1.000 33.96094  ?  1180 HIS   A CA  1 
ATOM   9464  C  C   . HIS   A 1 1182 ? -29.42200  65.67100  -0.33900  1.000 38.86111  ?  1180 HIS   A C   1 
ATOM   9465  O  O   . HIS   A 1 1182 ? -28.33700  66.16600  -0.66500  1.000 46.18621  ?  1180 HIS   A O   1 
ATOM   9466  C  CB  . HIS   A 1 1182 ? -29.51200  63.88300  1.42500   1.000 42.45930  ?  1180 HIS   A CB  1 
ATOM   9467  C  CG  . HIS   A 1 1182 ? -28.07500  63.46800  1.43100   1.000 47.50894  ?  1180 HIS   A CG  1 
ATOM   9468  N  ND1 . HIS   A 1 1182 ? -27.06600  64.28000  1.90200   1.000 56.21460  ?  1180 HIS   A ND1 1 
ATOM   9469  C  CD2 . HIS   A 1 1182 ? -27.47800  62.32200  1.02500   1.000 37.85281  ?  1180 HIS   A CD2 1 
ATOM   9470  C  CE1 . HIS   A 1 1182 ? -25.90900  63.65400  1.78400   1.000 43.16224  ?  1180 HIS   A CE1 1 
ATOM   9471  N  NE2 . HIS   A 1 1182 ? -26.13100  62.46500  1.25400   1.000 43.54322  ?  1180 HIS   A NE2 1 
ATOM   9472  N  N   . LEU   A 1 1183 ? -30.37500  65.39800  -1.23100  1.000 39.84060  ?  1181 LEU   A N   1 
ATOM   9473  C  CA  . LEU   A 1 1183 ? -30.16500  65.68200  -2.64600  1.000 34.64790  ?  1181 LEU   A CA  1 
ATOM   9474  C  C   . LEU   A 1 1183 ? -30.15600  67.18100  -2.91300  1.000 43.59822  ?  1181 LEU   A C   1 
ATOM   9475  O  O   . LEU   A 1 1183 ? -29.36200  67.66700  -3.72800  1.000 48.56279  ?  1181 LEU   A O   1 
ATOM   9476  C  CB  . LEU   A 1 1183 ? -31.24300  64.99300  -3.47800  1.000 32.99077  ?  1181 LEU   A CB  1 
ATOM   9477  C  CG  . LEU   A 1 1183 ? -30.89500  63.59000  -3.97300  1.000 39.87623  ?  1181 LEU   A CG  1 
ATOM   9478  C  CD1 . LEU   A 1 1183 ? -32.09200  62.96500  -4.65400  1.000 44.32416  ?  1181 LEU   A CD1 1 
ATOM   9479  C  CD2 . LEU   A 1 1183 ? -29.71200  63.63800  -4.92000  1.000 38.53001  ?  1181 LEU   A CD2 1 
ATOM   9480  N  N   . LEU   A 1 1184 ? -31.03100  67.92900  -2.23600  1.000 37.12590  ?  1182 LEU   A N   1 
ATOM   9481  C  CA  . LEU   A 1 1184 ? -31.10200  69.37300  -2.44300  1.000 30.54810  ?  1182 LEU   A CA  1 
ATOM   9482  C  C   . LEU   A 1 1184 ? -29.78000  70.04300  -2.09100  1.000 35.01472  ?  1182 LEU   A C   1 
ATOM   9483  O  O   . LEU   A 1 1184 ? -29.21900  70.79700  -2.89500  1.000 37.14075  ?  1182 LEU   A O   1 
ATOM   9484  C  CB  . LEU   A 1 1184 ? -32.24300  69.96200  -1.61300  1.000 42.23263  ?  1182 LEU   A CB  1 
ATOM   9485  C  CG  . LEU   A 1 1184 ? -32.68700  71.39800  -1.90800  1.000 29.17335  ?  1182 LEU   A CG  1 
ATOM   9486  C  CD1 . LEU   A 1 1184 ? -34.17900  71.53100  -1.66900  1.000 26.07555  ?  1182 LEU   A CD1 1 
ATOM   9487  C  CD2 . LEU   A 1 1184 ? -31.92300  72.40300  -1.06300  1.000 22.02633  ?  1182 LEU   A CD2 1 
ATOM   9488  N  N   . LEU   A 1 1185 ? -29.26500  69.77700  -0.88900  1.000 32.87739  ?  1183 LEU   A N   1 
ATOM   9489  C  CA  . LEU   A 1 1185 ? -28.00800  70.39000  -0.47300  1.000 30.94326  ?  1183 LEU   A CA  1 
ATOM   9490  C  C   . LEU   A 1 1185 ? -26.85700  69.95900  -1.37400  1.000 36.29887  ?  1183 LEU   A C   1 
ATOM   9491  O  O   . LEU   A 1 1185 ? -25.98500  70.76900  -1.70900  1.000 42.38676  ?  1183 LEU   A O   1 
ATOM   9492  C  CB  . LEU   A 1 1185 ? -27.71600  70.03900  0.98400   1.000 24.70648  ?  1183 LEU   A CB  1 
ATOM   9493  C  CG  . LEU   A 1 1185 ? -28.78100  70.50300  1.97700   1.000 24.79761  ?  1183 LEU   A CG  1 
ATOM   9494  C  CD1 . LEU   A 1 1185 ? -28.70900  69.69600  3.25700   1.000 22.33735  ?  1183 LEU   A CD1 1 
ATOM   9495  C  CD2 . LEU   A 1 1185 ? -28.62500  71.98500  2.27100   1.000 30.31338  ?  1183 LEU   A CD2 1 
ATOM   9496  N  N   . GLN   A 1 1186 ? -26.83900  68.68600  -1.77700  1.000 39.90418  ?  1184 GLN   A N   1 
ATOM   9497  C  CA  . GLN   A 1 1186 ? -25.81200  68.21700  -2.70200  1.000 41.26077  ?  1184 GLN   A CA  1 
ATOM   9498  C  C   . GLN   A 1 1186 ? -25.89600  68.95300  -4.03000  1.000 47.25877  ?  1184 GLN   A C   1 
ATOM   9499  O  O   . GLN   A 1 1186 ? -24.87100  69.24200  -4.65700  1.000 50.55960  ?  1184 GLN   A O   1 
ATOM   9500  C  CB  . GLN   A 1 1186 ? -25.95200  66.71300  -2.92800  1.000 36.39824  ?  1184 GLN   A CB  1 
ATOM   9501  C  CG  . GLN   A 1 1186 ? -25.27800  65.84700  -1.88400  1.000 28.11318  ?  1184 GLN   A CG  1 
ATOM   9502  C  CD  . GLN   A 1 1186 ? -25.47100  64.36500  -2.14900  1.000 40.49061  ?  1184 GLN   A CD  1 
ATOM   9503  O  OE1 . GLN   A 1 1186 ? -24.75100  63.76400  -2.94500  1.000 46.77886  ?  1184 GLN   A OE1 1 
ATOM   9504  N  NE2 . GLN   A 1 1186 ? -26.45000  63.77000  -1.48000  1.000 36.63034  ?  1184 GLN   A NE2 1 
ATOM   9505  N  N   . ALA   A 1 1187 ? -27.11400  69.26300  -4.47300  1.000 47.18101  ?  1185 ALA   A N   1 
ATOM   9506  C  CA  . ALA   A 1 1187 ? -27.29800  69.88600  -5.77700  1.000 48.23831  ?  1185 ALA   A CA  1 
ATOM   9507  C  C   . ALA   A 1 1187 ? -26.94300  71.36700  -5.74000  1.000 50.72543  ?  1185 ALA   A C   1 
ATOM   9508  O  O   . ALA   A 1 1187 ? -26.19100  71.85300  -6.59200  1.000 48.64545  ?  1185 ALA   A O   1 
ATOM   9509  C  CB  . ALA   A 1 1187 ? -28.73800  69.68600  -6.25000  1.000 40.01602  ?  1185 ALA   A CB  1 
ATOM   9510  N  N   . VAL   A 1 1188 ? -27.46600  72.09700  -4.75100  1.000 47.32773  ?  1186 VAL   A N   1 
ATOM   9511  C  CA  . VAL   A 1 1188 ? -27.23300  73.53400  -4.67700  1.000 41.60135  ?  1186 VAL   A CA  1 
ATOM   9512  C  C   . VAL   A 1 1188 ? -25.75600  73.85300  -4.49700  1.000 48.43687  ?  1186 VAL   A C   1 
ATOM   9513  O  O   . VAL   A 1 1188 ? -25.32900  74.98000  -4.76800  1.000 48.83950  ?  1186 VAL   A O   1 
ATOM   9514  C  CB  . VAL   A 1 1188 ? -28.08200  74.15000  -3.54400  1.000 45.48473  ?  1186 VAL   A CB  1 
ATOM   9515  C  CG1 . VAL   A 1 1188 ? -27.38800  73.98600  -2.19700  1.000 44.05202  ?  1186 VAL   A CG1 1 
ATOM   9516  C  CG2 . VAL   A 1 1188 ? -28.38100  75.61300  -3.83600  1.000 38.34766  ?  1186 VAL   A CG2 1 
ATOM   9517  N  N   . HIS   A 1 1189 ? -24.95900  72.88100  -4.05100  1.000 50.67185  ?  1187 HIS   A N   1 
ATOM   9518  C  CA  . HIS   A 1 1189 ? -23.52100  73.05000  -3.92500  1.000 51.54012  ?  1187 HIS   A CA  1 
ATOM   9519  C  C   . HIS   A 1 1189 ? -22.73800  72.29900  -4.99100  1.000 43.37127  ?  1187 HIS   A C   1 
ATOM   9520  O  O   . HIS   A 1 1189 ? -21.54000  72.55700  -5.15300  1.000 61.24522  ?  1187 HIS   A O   1 
ATOM   9521  C  CB  . HIS   A 1 1189 ? -23.05700  72.60000  -2.53100  1.000 35.76751  ?  1187 HIS   A CB  1 
ATOM   9522  C  CG  . HIS   A 1 1189 ? -23.66800  73.38700  -1.41100  1.000 53.89150  ?  1187 HIS   A CG  1 
ATOM   9523  N  ND1 . HIS   A 1 1189 ? -23.85900  74.75100  -1.47600  1.000 51.27358  ?  1187 HIS   A ND1 1 
ATOM   9524  C  CD2 . HIS   A 1 1189 ? -24.14000  72.99900  -0.20200  1.000 66.15948  ?  1187 HIS   A CD2 1 
ATOM   9525  C  CE1 . HIS   A 1 1189 ? -24.41600  75.17000  -0.35300  1.000 47.65345  ?  1187 HIS   A CE1 1 
ATOM   9526  N  NE2 . HIS   A 1 1189 ? -24.59900  74.12600  0.43600   1.000 48.31348  ?  1187 HIS   A NE2 1 
ATOM   9527  N  N   . GLY   A 1 1190 ? -23.37600  71.38900  -5.72100  1.000 43.23211  ?  1188 GLY   A N   1 
ATOM   9528  C  CA  . GLY   A 1 1190 ? -22.71800  70.68600  -6.80300  1.000 47.74914  ?  1188 GLY   A CA  1 
ATOM   9529  C  C   . GLY   A 1 1190 ? -23.38600  70.95400  -8.13500  1.000 43.27547  ?  1188 GLY   A C   1 
ATOM   9530  O  O   . GLY   A 1 1190 ? -23.91100  70.03600  -8.77100  1.000 52.46445  ?  1188 GLY   A O   1 
ATOM   9531  N  N   . LEU   A 1 1191 ? -23.37900  72.22000  -8.55900  1.000 38.39016  ?  1189 LEU   A N   1 
ATOM   9532  C  CA  . LEU   A 1 1191 ? -24.06800  72.59200  -9.79100  1.000 50.65278  ?  1189 LEU   A CA  1 
ATOM   9533  C  C   . LEU   A 1 1191 ? -23.44200  71.91100  -10.99700 1.000 39.38438  ?  1189 LEU   A C   1 
ATOM   9534  O  O   . LEU   A 1 1191 ? -24.13900  71.54900  -11.95300 1.000 48.25385  ?  1189 LEU   A O   1 
ATOM   9535  C  CB  . LEU   A 1 1191 ? -24.04200  74.10700  -9.96400  1.000 44.38827  ?  1189 LEU   A CB  1 
ATOM   9536  C  CG  . LEU   A 1 1191 ? -25.13600  74.92600  -9.28700  1.000 47.98151  ?  1189 LEU   A CG  1 
ATOM   9537  C  CD1 . LEU   A 1 1191 ? -24.66800  75.43800  -7.93700  1.000 55.30662  ?  1189 LEU   A CD1 1 
ATOM   9538  C  CD2 . LEU   A 1 1191 ? -25.48500  76.08900  -10.18700 1.000 67.16980  ?  1189 LEU   A CD2 1 
ATOM   9539  N  N   . ASP   A 1 1192 ? -22.12900  71.72200  -10.96700 1.000 42.19912  ?  1190 ASP   A N   1 
ATOM   9540  C  CA  . ASP   A 1 1192 ? -21.40300  71.12400  -12.07400 1.000 60.54136  ?  1190 ASP   A CA  1 
ATOM   9541  C  C   . ASP   A 1 1192 ? -21.05400  69.66400  -11.83100 1.000 55.41059  ?  1190 ASP   A C   1 
ATOM   9542  O  O   . ASP   A 1 1192 ? -20.44000  69.03700  -12.69900 1.000 43.14537  ?  1190 ASP   A O   1 
ATOM   9543  C  CB  . ASP   A 1 1192 ? -20.13300  71.93000  -12.35800 1.000 48.12870  ?  1190 ASP   A CB  1 
ATOM   9544  C  CG  . ASP   A 1 1192 ? -20.42800  73.25200  -13.03800 1.000 73.46682  ?  1190 ASP   A CG  1 
ATOM   9545  O  OD1 . ASP   A 1 1192 ? -21.01200  73.23700  -14.14400 1.000 80.76299  ?  1190 ASP   A OD1 1 
ATOM   9546  O  OD2 . ASP   A 1 1192 ? -20.08100  74.30800  -12.46700 1.000 75.41487  -1 1190 ASP   A OD2 1 
ATOM   9547  N  N   . GLN   A 1 1193 ? -21.42800  69.10900  -10.68200 1.000 45.86518  ?  1191 GLN   A N   1 
ATOM   9548  C  CA  . GLN   A 1 1193 ? -21.21700  67.69200  -10.43500 1.000 38.82991  ?  1191 GLN   A CA  1 
ATOM   9549  C  C   . GLN   A 1 1193 ? -22.20400  66.86300  -11.24900 1.000 42.33260  ?  1191 GLN   A C   1 
ATOM   9550  O  O   . GLN   A 1 1193 ? -23.32900  67.28800  -11.52300 1.000 48.35427  ?  1191 GLN   A O   1 
ATOM   9551  C  CB  . GLN   A 1 1193 ? -21.37200  67.37700  -8.94600  1.000 50.17708  ?  1191 GLN   A CB  1 
ATOM   9552  C  CG  . GLN   A 1 1193 ? -20.16800  67.75500  -8.09600  1.000 78.46436  ?  1191 GLN   A CG  1 
ATOM   9553  C  CD  . GLN   A 1 1193 ? -19.92300  66.77300  -6.96300  1.000 97.73152  ?  1191 GLN   A CD  1 
ATOM   9554  O  OE1 . GLN   A 1 1193 ? -19.50300  65.63800  -7.19000  1.000 90.05156  ?  1191 GLN   A OE1 1 
ATOM   9555  N  NE2 . GLN   A 1 1193 ? -20.18500  67.20700  -5.73500  1.000 86.62425  ?  1191 GLN   A NE2 1 
ATOM   9556  N  N   . GLN   A 1 1194 ? -21.76900  65.67200  -11.64700 1.000 42.66493  ?  1192 GLN   A N   1 
ATOM   9557  C  CA  . GLN   A 1 1194 ? -22.65500  64.76700  -12.36500 1.000 44.23015  ?  1192 GLN   A CA  1 
ATOM   9558  C  C   . GLN   A 1 1194 ? -23.73100  64.23300  -11.42700 1.000 53.14325  ?  1192 GLN   A C   1 
ATOM   9559  O  O   . GLN   A 1 1194 ? -23.48700  64.01200  -10.23700 1.000 47.33046  ?  1192 GLN   A O   1 
ATOM   9560  C  CB  . GLN   A 1 1194 ? -21.86100  63.61600  -12.97500 1.000 49.77654  ?  1192 GLN   A CB  1 
ATOM   9561  C  CG  . GLN   A 1 1194 ? -20.97500  64.03400  -14.13100 1.000 51.89778  ?  1192 GLN   A CG  1 
ATOM   9562  C  CD  . GLN   A 1 1194 ? -20.02900  62.93700  -14.56200 1.000 57.62323  ?  1192 GLN   A CD  1 
ATOM   9563  O  OE1 . GLN   A 1 1194 ? -19.14400  62.53200  -13.80700 1.000 69.09591  ?  1192 GLN   A OE1 1 
ATOM   9564  N  NE2 . GLN   A 1 1194 ? -20.21500  62.44100  -15.78000 1.000 44.89212  ?  1192 GLN   A NE2 1 
ATOM   9565  N  N   . VAL   A 1 1195 ? -24.93200  64.02900  -11.97100 1.000 46.33314  ?  1193 VAL   A N   1 
ATOM   9566  C  CA  . VAL   A 1 1195 ? -26.06300  63.61700  -11.14500 1.000 43.20997  ?  1193 VAL   A CA  1 
ATOM   9567  C  C   . VAL   A 1 1195 ? -25.84100  62.21900  -10.57800 1.000 44.36515  ?  1193 VAL   A C   1 
ATOM   9568  O  O   . VAL   A 1 1195 ? -26.33000  61.89800  -9.48700  1.000 48.85397  ?  1193 VAL   A O   1 
ATOM   9569  C  CB  . VAL   A 1 1195 ? -27.36400  63.71900  -11.96400 1.000 49.33491  ?  1193 VAL   A CB  1 
ATOM   9570  C  CG1 . VAL   A 1 1195 ? -28.52400  63.01600  -11.26500 1.000 42.21891  ?  1193 VAL   A CG1 1 
ATOM   9571  C  CG2 . VAL   A 1 1195 ? -27.70200  65.17700  -12.20900 1.000 38.22591  ?  1193 VAL   A CG2 1 
ATOM   9572  N  N   . LYS   A 1 1196 ? -25.08300  61.37800  -11.28500 1.000 47.76277  ?  1194 LYS   A N   1 
ATOM   9573  C  CA  . LYS   A 1 1196 ? -24.75900  60.05500  -10.76100 1.000 42.05813  ?  1194 LYS   A CA  1 
ATOM   9574  C  C   . LYS   A 1 1196 ? -23.94600  60.14400  -9.47600  1.000 40.28443  ?  1194 LYS   A C   1 
ATOM   9575  O  O   . LYS   A 1 1196 ? -23.99200  59.22600  -8.64900  1.000 48.66290  ?  1194 LYS   A O   1 
ATOM   9576  C  CB  . LYS   A 1 1196 ? -23.99600  59.24900  -11.81200 1.000 44.46244  ?  1194 LYS   A CB  1 
ATOM   9577  C  CG  . LYS   A 1 1196 ? -22.63900  59.83700  -12.16100 1.000 54.38213  ?  1194 LYS   A CG  1 
ATOM   9578  C  CD  . LYS   A 1 1196 ? -21.71600  58.80300  -12.77800 1.000 61.77852  ?  1194 LYS   A CD  1 
ATOM   9579  C  CE  . LYS   A 1 1196 ? -21.48000  59.09300  -14.24500 1.000 48.28554  ?  1194 LYS   A CE  1 
ATOM   9580  N  NZ  . LYS   A 1 1196 ? -20.48800  58.15500  -14.83000 1.000 57.79961  ?  1194 LYS   A NZ  1 
ATOM   9581  N  N   . ARG   A 1 1197 ? -23.20400  61.23700  -9.28600  1.000 35.46830  ?  1195 ARG   A N   1 
ATOM   9582  C  CA  . ARG   A 1 1197 ? -22.36600  61.40000  -8.10500  1.000 49.08162  ?  1195 ARG   A CA  1 
ATOM   9583  C  C   . ARG   A 1 1197 ? -23.14400  61.87300  -6.88300  1.000 44.01311  ?  1195 ARG   A C   1 
ATOM   9584  O  O   . ARG   A 1 1197 ? -22.57900  61.91900  -5.78500  1.000 32.19189  ?  1195 ARG   A O   1 
ATOM   9585  C  CB  . ARG   A 1 1197 ? -21.22300  62.37500  -8.40500  1.000 39.89042  ?  1195 ARG   A CB  1 
ATOM   9586  C  CG  . ARG   A 1 1197 ? -20.19900  61.83500  -9.39700  1.000 43.14366  ?  1195 ARG   A CG  1 
ATOM   9587  C  CD  . ARG   A 1 1197 ? -19.30300  60.78400  -8.75100  1.000 71.45098  ?  1195 ARG   A CD  1 
ATOM   9588  N  NE  . ARG   A 1 1197 ? -19.05600  59.64900  -9.63400  1.000 93.83097  ?  1195 ARG   A NE  1 
ATOM   9589  C  CZ  . ARG   A 1 1197 ? -19.48700  58.41400  -9.40900  1.000 87.92394  ?  1195 ARG   A CZ  1 
ATOM   9590  N  NH1 . ARG   A 1 1197 ? -20.19900  58.11500  -8.33300  1.000 61.91255  ?  1195 ARG   A NH1 1 
ATOM   9591  N  NH2 . ARG   A 1 1197 ? -19.19900  57.45600  -10.28500 1.000 92.10240  ?  1195 ARG   A NH2 1 
ATOM   9592  N  N   . PHE   A 1 1198 ? -24.41300  62.22600  -7.04300  1.000 46.63379  ?  1196 PHE   A N   1 
ATOM   9593  C  CA  . PHE   A 1 1198 ? -25.25100  62.55500  -5.90000  1.000 42.32659  ?  1196 PHE   A CA  1 
ATOM   9594  C  C   . PHE   A 1 1198 ? -25.78400  61.26900  -5.28400  1.000 43.70160  ?  1196 PHE   A C   1 
ATOM   9595  O  O   . PHE   A 1 1198 ? -26.39500  60.44900  -5.97600  1.000 51.16880  ?  1196 PHE   A O   1 
ATOM   9596  C  CB  . PHE   A 1 1198 ? -26.40600  63.46000  -6.32400  1.000 42.90671  ?  1196 PHE   A CB  1 
ATOM   9597  C  CG  . PHE   A 1 1198 ? -25.97300  64.76900  -6.92400  1.000 40.61952  ?  1196 PHE   A CG  1 
ATOM   9598  C  CD1 . PHE   A 1 1198 ? -24.80800  65.39400  -6.50700  1.000 49.10476  ?  1196 PHE   A CD1 1 
ATOM   9599  C  CD2 . PHE   A 1 1198 ? -26.74000  65.37900  -7.90300  1.000 39.09588  ?  1196 PHE   A CD2 1 
ATOM   9600  C  CE1 . PHE   A 1 1198 ? -24.41800  66.60300  -7.05800  1.000 53.34471  ?  1196 PHE   A CE1 1 
ATOM   9601  C  CE2 . PHE   A 1 1198 ? -26.35500  66.58500  -8.45800  1.000 31.14913  ?  1196 PHE   A CE2 1 
ATOM   9602  C  CZ  . PHE   A 1 1198 ? -25.19400  67.19800  -8.03500  1.000 33.44286  ?  1196 PHE   A CZ  1 
ATOM   9603  N  N   . GLU   A 1 1199 ? -25.55100  61.08500  -3.98900  1.000 36.77526  ?  1197 GLU   A N   1 
ATOM   9604  C  CA  . GLU   A 1 1199 ? -26.00900  59.88100  -3.31300  1.000 49.93840  ?  1197 GLU   A CA  1 
ATOM   9605  C  C   . GLU   A 1 1199 ? -27.36900  60.12100  -2.66700  1.000 44.31549  ?  1197 GLU   A C   1 
ATOM   9606  O  O   . GLU   A 1 1199 ? -27.61800  61.17600  -2.07400  1.000 49.39846  ?  1197 GLU   A O   1 
ATOM   9607  C  CB  . GLU   A 1 1199 ? -24.97800  59.41200  -2.27800  1.000 48.49119  ?  1197 GLU   A CB  1 
ATOM   9608  C  CG  . GLU   A 1 1199 ? -25.18000  59.91300  -0.85900  1.000 57.22668  ?  1197 GLU   A CG  1 
ATOM   9609  C  CD  . GLU   A 1 1199 ? -24.30000  59.19000  0.14300   1.000 83.74231  ?  1197 GLU   A CD  1 
ATOM   9610  O  OE1 . GLU   A 1 1199 ? -23.36000  58.49000  -0.28800  1.000 86.71872  ?  1197 GLU   A OE1 1 
ATOM   9611  O  OE2 . GLU   A 1 1199 ? -24.54900  59.32100  1.36100   1.000 79.16131  -1 1197 GLU   A OE2 1 
ATOM   9612  N  N   . LEU   A 1 1200 ? -28.26500  59.14600  -2.82300  1.000 35.97784  ?  1198 LEU   A N   1 
ATOM   9613  C  CA  . LEU   A 1 1200 ? -29.60000  59.26600  -2.24800  1.000 35.95585  ?  1198 LEU   A CA  1 
ATOM   9614  C  C   . LEU   A 1 1200 ? -29.59300  58.92500  -0.76400  1.000 44.68096  ?  1198 LEU   A C   1 
ATOM   9615  O  O   . LEU   A 1 1200 ? -30.16200  59.65800  0.05200   1.000 43.81399  ?  1198 LEU   A O   1 
ATOM   9616  C  CB  . LEU   A 1 1200 ? -30.58100  58.36200  -3.00100  1.000 29.50643  ?  1198 LEU   A CB  1 
ATOM   9617  C  CG  . LEU   A 1 1200 ? -32.04400  58.42800  -2.56200  1.000 36.18083  ?  1198 LEU   A CG  1 
ATOM   9618  C  CD1 . LEU   A 1 1200 ? -32.69800  59.69400  -3.08500  1.000 44.61552  ?  1198 LEU   A CD1 1 
ATOM   9619  C  CD2 . LEU   A 1 1200 ? -32.80300  57.20000  -3.03600  1.000 54.58126  ?  1198 LEU   A CD2 1 
ATOM   9620  N  N   . VAL   A 1 1201 ? -28.94900  57.81200  -0.40100  1.000 52.09509  ?  1199 VAL   A N   1 
ATOM   9621  C  CA  . VAL   A 1 1201 ? -28.89500  57.39600  0.99200   1.000 50.29668  ?  1199 VAL   A CA  1 
ATOM   9622  C  C   . VAL   A 1 1201 ? -28.18400  58.46300  1.82300   1.000 46.95755  ?  1199 VAL   A C   1 
ATOM   9623  O  O   . VAL   A 1 1201 ? -27.33100  59.20700  1.32600   1.000 45.61123  ?  1199 VAL   A O   1 
ATOM   9624  C  CB  . VAL   A 1 1201 ? -28.19400  56.03000  1.11200   1.000 44.91185  ?  1199 VAL   A CB  1 
ATOM   9625  C  CG1 . VAL   A 1 1201 ? -26.69500  56.17400  0.90300   1.000 35.43258  ?  1199 VAL   A CG1 1 
ATOM   9626  C  CG2 . VAL   A 1 1201 ? -28.49300  55.38000  2.45100   1.000 47.15379  ?  1199 VAL   A CG2 1 
ATOM   9627  N  N   . THR   A 1 1202 ? -28.55500  58.55400  3.09500   1.000 51.37923  ?  1200 THR   A N   1 
ATOM   9628  C  CA  . THR   A 1 1202 ? -27.97800  59.52600  4.01000   1.000 51.97084  ?  1200 THR   A CA  1 
ATOM   9629  C  C   . THR   A 1 1202 ? -27.01900  58.84100  4.97400   1.000 54.84452  ?  1200 THR   A C   1 
ATOM   9630  O  O   . THR   A 1 1202 ? -27.04200  57.62000  5.14800   1.000 59.62196  ?  1200 THR   A O   1 
ATOM   9631  C  CB  . THR   A 1 1202 ? -29.07200  60.26100  4.79000   1.000 41.89814  ?  1200 THR   A CB  1 
ATOM   9632  O  OG1 . THR   A 1 1202 ? -29.79300  59.32600  5.60200   1.000 49.64004  ?  1200 THR   A OG1 1 
ATOM   9633  C  CG2 . THR   A 1 1202 ? -30.03500  60.93800  3.83300   1.000 39.69549  ?  1200 THR   A CG2 1 
ATOM   9634  N  N   . GLU   A 1 1203 ? -26.16600  59.65200  5.60600   1.000 48.13733  ?  1201 GLU   A N   1 
ATOM   9635  C  CA  . GLU   A 1 1203 ? -25.17300  59.10000  6.52200   1.000 46.09549  ?  1201 GLU   A CA  1 
ATOM   9636  C  C   . GLU   A 1 1203 ? -25.83400  58.46100  7.73600   1.000 51.74146  ?  1201 GLU   A C   1 
ATOM   9637  O  O   . GLU   A 1 1203 ? -25.34600  57.45300  8.25900   1.000 65.63256  ?  1201 GLU   A O   1 
ATOM   9638  C  CB  . GLU   A 1 1203 ? -24.18900  60.18600  6.95000   1.000 39.30624  ?  1201 GLU   A CB  1 
ATOM   9639  C  CG  . GLU   A 1 1203 ? -23.17100  60.54600  5.87700   1.000 65.51387  ?  1201 GLU   A CG  1 
ATOM   9640  C  CD  . GLU   A 1 1203 ? -22.18800  59.42000  5.59600   1.000 76.23892  ?  1201 GLU   A CD  1 
ATOM   9641  O  OE1 . GLU   A 1 1203 ? -21.90400  58.63000  6.52100   1.000 80.10099  ?  1201 GLU   A OE1 1 
ATOM   9642  O  OE2 . GLU   A 1 1203 ? -21.69800  59.32500  4.44900   1.000 63.26982  -1 1201 GLU   A OE2 1 
ATOM   9643  N  N   . ASP   A 1 1204 ? -26.94700  59.03100  8.20100   1.000 55.24506  ?  1202 ASP   A N   1 
ATOM   9644  C  CA  . ASP   A 1 1204 ? -27.69800  58.38900  9.27300   1.000 53.83050  ?  1202 ASP   A CA  1 
ATOM   9645  C  C   . ASP   A 1 1204 ? -28.25600  57.04800  8.81500   1.000 58.15307  ?  1202 ASP   A C   1 
ATOM   9646  O  O   . ASP   A 1 1204 ? -28.27100  56.07700  9.58100   1.000 67.72218  ?  1202 ASP   A O   1 
ATOM   9647  C  CB  . ASP   A 1 1204 ? -28.82200  59.30600  9.75200   1.000 65.81393  ?  1202 ASP   A CB  1 
ATOM   9648  C  CG  . ASP   A 1 1204 ? -28.32600  60.40700  10.67100  1.000 79.03461  ?  1202 ASP   A CG  1 
ATOM   9649  O  OD1 . ASP   A 1 1204 ? -27.09400  60.57700  10.79600  1.000 83.83635  ?  1202 ASP   A OD1 1 
ATOM   9650  O  OD2 . ASP   A 1 1204 ? -29.17400  61.10000  11.27300  1.000 67.23542  -1 1202 ASP   A OD2 1 
ATOM   9651  N  N   . GLU   A 1 1205 ? -28.71100  56.97200  7.56200   1.000 54.99672  ?  1203 GLU   A N   1 
ATOM   9652  C  CA  . GLU   A 1 1205 ? -29.20500  55.70800  7.02900   1.000 52.87712  ?  1203 GLU   A CA  1 
ATOM   9653  C  C   . GLU   A 1 1205 ? -28.08000  54.69400  6.86000   1.000 56.87548  ?  1203 GLU   A C   1 
ATOM   9654  O  O   . GLU   A 1 1205 ? -28.30700  53.48900  7.01200   1.000 61.23502  ?  1203 GLU   A O   1 
ATOM   9655  C  CB  . GLU   A 1 1205 ? -29.90900  55.94200  5.69400   1.000 52.41297  ?  1203 GLU   A CB  1 
ATOM   9656  C  CG  . GLU   A 1 1205 ? -31.32600  56.48200  5.80200   1.000 60.48122  ?  1203 GLU   A CG  1 
ATOM   9657  C  CD  . GLU   A 1 1205 ? -31.88200  56.90100  4.45300   1.000 54.68350  ?  1203 GLU   A CD  1 
ATOM   9658  O  OE1 . GLU   A 1 1205 ? -31.40500  57.91200  3.89700   1.000 56.24496  ?  1203 GLU   A OE1 1 
ATOM   9659  O  OE2 . GLU   A 1 1205 ? -32.78700  56.21300  3.94000   1.000 65.73153  -1 1203 GLU   A OE2 1 
ATOM   9660  N  N   . LYS   A 1 1206 ? -26.86800  55.15900  6.54400   1.000 49.92237  ?  1204 LYS   A N   1 
ATOM   9661  C  CA  . LYS   A 1 1206 ? -25.74200  54.24300  6.38800   1.000 53.56032  ?  1204 LYS   A CA  1 
ATOM   9662  C  C   . LYS   A 1 1206 ? -25.33600  53.63600  7.72500   1.000 56.02535  ?  1204 LYS   A C   1 
ATOM   9663  O  O   . LYS   A 1 1206 ? -25.01800  52.44400  7.80000   1.000 58.20604  ?  1204 LYS   A O   1 
ATOM   9664  C  CB  . LYS   A 1 1206 ? -24.55700  54.96400  5.74500   1.000 45.74577  ?  1204 LYS   A CB  1 
ATOM   9665  C  CG  . LYS   A 1 1206 ? -24.76500  55.31700  4.28100   1.000 52.50127  ?  1204 LYS   A CG  1 
ATOM   9666  C  CD  . LYS   A 1 1206 ? -23.99500  56.57300  3.90200   1.000 61.15568  ?  1204 LYS   A CD  1 
ATOM   9667  C  CE  . LYS   A 1 1206 ? -22.69400  56.24300  3.18700   1.000 63.12549  ?  1204 LYS   A CE  1 
ATOM   9668  N  NZ  . LYS   A 1 1206 ? -22.91900  55.84500  1.77000   1.000 67.53182  ?  1204 LYS   A NZ  1 
ATOM   9669  N  N   . ARG   A 1 1207 ? -25.33600  54.44300  8.78800   1.000 62.48678  ?  1205 ARG   A N   1 
ATOM   9670  C  CA  . ARG   A 1 1207 ? -25.05900  53.91000  10.11800  1.000 65.25473  ?  1205 ARG   A CA  1 
ATOM   9671  C  C   . ARG   A 1 1207 ? -26.14400  52.93500  10.55300  1.000 57.07926  ?  1205 ARG   A C   1 
ATOM   9672  O  O   . ARG   A 1 1207 ? -25.84500  51.88000  11.12500  1.000 69.74702  ?  1205 ARG   A O   1 
ATOM   9673  C  CB  . ARG   A 1 1207 ? -24.93400  55.05000  11.12800  1.000 56.97025  ?  1205 ARG   A CB  1 
ATOM   9674  C  CG  . ARG   A 1 1207 ? -23.57400  55.14200  11.79500  1.000 65.31909  ?  1205 ARG   A CG  1 
ATOM   9675  C  CD  . ARG   A 1 1207 ? -23.43100  54.10900  12.90300  1.000 65.35852  ?  1205 ARG   A CD  1 
ATOM   9676  N  NE  . ARG   A 1 1207 ? -22.14400  54.21200  13.58200  1.000 73.76859  ?  1205 ARG   A NE  1 
ATOM   9677  C  CZ  . ARG   A 1 1207 ? -21.00400  53.72800  13.10700  1.000 92.73409  ?  1205 ARG   A CZ  1 
ATOM   9678  N  NH1 . ARG   A 1 1207 ? -20.95100  53.09600  11.94500  1.000 76.67821  ?  1205 ARG   A NH1 1 
ATOM   9679  N  NH2 . ARG   A 1 1207 ? -19.88900  53.88300  13.81500  1.000 108.34681 ?  1205 ARG   A NH2 1 
ATOM   9680  N  N   . ASP   A 1 1208 ? -27.40900  53.27600  10.29400  1.000 58.79410  ?  1206 ASP   A N   1 
ATOM   9681  C  CA  . ASP   A 1 1208 ? -28.51300  52.38800  10.64100  1.000 61.14045  ?  1206 ASP   A CA  1 
ATOM   9682  C  C   . ASP   A 1 1208 ? -28.38500  51.04600  9.93300   1.000 59.09165  ?  1206 ASP   A C   1 
ATOM   9683  O  O   . ASP   A 1 1208 ? -28.61300  49.99100  10.53700  1.000 65.40626  ?  1206 ASP   A O   1 
ATOM   9684  C  CB  . ASP   A 1 1208 ? -29.84300  53.05900  10.29400  1.000 63.26771  ?  1206 ASP   A CB  1 
ATOM   9685  C  CG  . ASP   A 1 1208 ? -31.04500  52.23200  10.71200  1.000 81.67471  ?  1206 ASP   A CG  1 
ATOM   9686  O  OD1 . ASP   A 1 1208 ? -31.48200  51.37000  9.91900   1.000 88.47987  ?  1206 ASP   A OD1 1 
ATOM   9687  O  OD2 . ASP   A 1 1208 ? -31.55600  52.44500  11.83100  1.000 90.73617  -1 1206 ASP   A OD2 1 
ATOM   9688  N  N   . LEU   A 1 1209 ? -28.01900  51.06800  8.65000   1.000 58.85108  ?  1207 LEU   A N   1 
ATOM   9689  C  CA  . LEU   A 1 1209 ? -27.81500  49.82500  7.91300   1.000 57.59571  ?  1207 LEU   A CA  1 
ATOM   9690  C  C   . LEU   A 1 1209 ? -26.68000  49.00700  8.51600   1.000 61.56961  ?  1207 LEU   A C   1 
ATOM   9691  O  O   . LEU   A 1 1209 ? -26.78400  47.78000  8.63300   1.000 61.13367  ?  1207 LEU   A O   1 
ATOM   9692  C  CB  . LEU   A 1 1209 ? -27.53000  50.13300  6.44400   1.000 54.38749  ?  1207 LEU   A CB  1 
ATOM   9693  C  CG  . LEU   A 1 1209 ? -28.74100  50.39100  5.54700   1.000 49.01998  ?  1207 LEU   A CG  1 
ATOM   9694  C  CD1 . LEU   A 1 1209 ? -28.30400  50.57500  4.09900   1.000 48.69231  ?  1207 LEU   A CD1 1 
ATOM   9695  C  CD2 . LEU   A 1 1209 ? -29.74400  49.25200  5.66800   1.000 40.64259  ?  1207 LEU   A CD2 1 
ATOM   9696  N  N   . PHE   A 1 1210 ? -25.59200  49.67200  8.91200   1.000 56.18916  ?  1208 PHE   A N   1 
ATOM   9697  C  CA  . PHE   A 1 1210 ? -24.43200  48.96700  9.45000   1.000 62.16823  ?  1208 PHE   A CA  1 
ATOM   9698  C  C   . PHE   A 1 1210 ? -24.80200  48.12800  10.66600  1.000 64.73006  ?  1208 PHE   A C   1 
ATOM   9699  O  O   . PHE   A 1 1210 ? -24.52500  46.92300  10.71300  1.000 79.47924  ?  1208 PHE   A O   1 
ATOM   9700  C  CB  . PHE   A 1 1210 ? -23.34000  49.97100  9.81100   1.000 58.64082  ?  1208 PHE   A CB  1 
ATOM   9701  C  CG  . PHE   A 1 1210 ? -22.16600  49.35900  10.50900  1.000 62.64480  ?  1208 PHE   A CG  1 
ATOM   9702  C  CD1 . PHE   A 1 1210 ? -21.21600  48.64400  9.80100   1.000 65.49133  ?  1208 PHE   A CD1 1 
ATOM   9703  C  CD2 . PHE   A 1 1210 ? -22.02200  49.48400  11.87800  1.000 66.04558  ?  1208 PHE   A CD2 1 
ATOM   9704  C  CE1 . PHE   A 1 1210 ? -20.13400  48.08000  10.44800  1.000 63.45049  ?  1208 PHE   A CE1 1 
ATOM   9705  C  CE2 . PHE   A 1 1210 ? -20.94700  48.92000  12.53000  1.000 71.17691  ?  1208 PHE   A CE2 1 
ATOM   9706  C  CZ  . PHE   A 1 1210 ? -20.00100  48.21800  11.81500  1.000 66.64154  ?  1208 PHE   A CZ  1 
ATOM   9707  N  N   . LEU   A 1 1211 ? -25.42000  48.75400  11.66900  1.000 51.65933  ?  1209 LEU   A N   1 
ATOM   9708  C  CA  . LEU   A 1 1211 ? -25.77500  48.04300  12.89200  1.000 52.39646  ?  1209 LEU   A CA  1 
ATOM   9709  C  C   . LEU   A 1 1211 ? -26.75100  46.91200  12.60500  1.000 72.94477  ?  1209 LEU   A C   1 
ATOM   9710  O  O   . LEU   A 1 1211 ? -26.50300  45.75100  12.95800  1.000 96.59297  ?  1209 LEU   A O   1 
ATOM   9711  C  CB  . LEU   A 1 1211 ? -26.37700  49.01700  13.90100  1.000 60.65718  ?  1209 LEU   A CB  1 
ATOM   9712  C  CG  . LEU   A 1 1211 ? -25.66900  50.36000  14.06500  1.000 57.82610  ?  1209 LEU   A CG  1 
ATOM   9713  C  CD1 . LEU   A 1 1211 ? -26.41100  51.21300  15.07500  1.000 44.93678  ?  1209 LEU   A CD1 1 
ATOM   9714  C  CD2 . LEU   A 1 1211 ? -24.23000  50.14800  14.49600  1.000 48.82229  ?  1209 LEU   A CD2 1 
ATOM   9715  N  N   . ARG   A 1 1212 ? -27.86300  47.23400  11.94200  1.000 58.37293  ?  1210 ARG   A N   1 
ATOM   9716  C  CA  . ARG   A 1 1212 ? -28.92800  46.26500  11.74300  1.000 54.44149  ?  1210 ARG   A CA  1 
ATOM   9717  C  C   . ARG   A 1 1212 ? -28.55300  45.15300  10.77500  1.000 69.67131  ?  1210 ARG   A C   1 
ATOM   9718  O  O   . ARG   A 1 1212 ? -29.32100  44.19400  10.64300  1.000 73.67342  ?  1210 ARG   A O   1 
ATOM   9719  C  CB  . ARG   A 1 1212 ? -30.20400  46.95000  11.24500  1.000 51.32344  ?  1210 ARG   A CB  1 
ATOM   9720  C  CG  . ARG   A 1 1212 ? -30.83800  47.85500  12.28300  1.000 61.01360  ?  1210 ARG   A CG  1 
ATOM   9721  C  CD  . ARG   A 1 1212 ? -32.03600  48.61800  11.76500  1.000 64.87938  ?  1210 ARG   A CD  1 
ATOM   9722  N  NE  . ARG   A 1 1212 ? -33.05500  48.55500  12.80400  1.000 92.31797  ?  1210 ARG   A NE  1 
ATOM   9723  C  CZ  . ARG   A 1 1212 ? -33.38700  49.54200  13.62800  1.000 106.60930 ?  1210 ARG   A CZ  1 
ATOM   9724  N  NH1 . ARG   A 1 1212 ? -33.05800  50.80100  13.37100  1.000 96.90083  ?  1210 ARG   A NH1 1 
ATOM   9725  N  NH2 . ARG   A 1 1212 ? -34.12700  49.26700  14.70400  1.000 93.51621  ?  1210 ARG   A NH2 1 
ATOM   9726  N  N   . VAL   A 1 1213 ? -27.41000  45.25100  10.09700  1.000 59.77184  ?  1211 VAL   A N   1 
ATOM   9727  C  CA  . VAL   A 1 1213 ? -27.05000  44.27100  9.08000   1.000 59.07034  ?  1211 VAL   A CA  1 
ATOM   9728  C  C   . VAL   A 1 1213 ? -25.59400  43.83700  9.21900   1.000 61.69352  ?  1211 VAL   A C   1 
ATOM   9729  O  O   . VAL   A 1 1213 ? -25.31000  42.64300  9.35500   1.000 75.55900  ?  1211 VAL   A O   1 
ATOM   9730  C  CB  . VAL   A 1 1213 ? -27.32100  44.82000  7.66500   1.000 62.12786  ?  1211 VAL   A CB  1 
ATOM   9731  C  CG1 . VAL   A 1 1213 ? -26.81700  43.84900  6.60800   1.000 52.61744  ?  1211 VAL   A CG1 1 
ATOM   9732  C  CG2 . VAL   A 1 1213 ? -28.80800  45.10300  7.46600   1.000 54.62826  ?  1211 VAL   A CG2 1 
ATOM   9733  N  N   . ASN   A 1 1214 ? -24.65900  44.79300  9.19200   1.000 43.96698  ?  1212 ASN   A N   1 
ATOM   9734  C  CA  . ASN   A 1 1214 ? -23.25600  44.48800  8.92700   1.000 45.93389  ?  1212 ASN   A CA  1 
ATOM   9735  C  C   . ASN   A 1 1214 ? -22.34500  44.62300  10.14800  1.000 59.83673  ?  1212 ASN   A C   1 
ATOM   9736  O  O   . ASN   A 1 1214 ? -21.12800  44.76700  9.98900   1.000 61.19255  ?  1212 ASN   A O   1 
ATOM   9737  C  CB  . ASN   A 1 1214 ? -22.73200  45.36800  7.79200   1.000 44.46513  ?  1212 ASN   A CB  1 
ATOM   9738  C  CG  . ASN   A 1 1214 ? -23.30700  44.98500  6.44300   1.000 44.99220  ?  1212 ASN   A CG  1 
ATOM   9739  O  OD1 . ASN   A 1 1214 ? -23.57700  43.81300  6.17800   1.000 49.99981  ?  1212 ASN   A OD1 1 
ATOM   9740  N  ND2 . ASN   A 1 1214 ? -23.47700  45.97200  5.57200   1.000 50.05957  ?  1212 ASN   A ND2 1 
ATOM   9741  N  N   . ASP   A 1 1215 ? -22.89300  44.56300  11.36300  1.000 69.25673  ?  1213 ASP   A N   1 
ATOM   9742  C  CA  . ASP   A 1 1215 ? -22.07400  44.51700  12.57600  1.000 76.43628  ?  1213 ASP   A CA  1 
ATOM   9743  C  C   . ASP   A 1 1215 ? -21.97600  43.05700  13.01000  1.000 77.70507  ?  1213 ASP   A C   1 
ATOM   9744  O  O   . ASP   A 1 1215 ? -22.64500  42.60100  13.93900  1.000 68.68902  ?  1213 ASP   A O   1 
ATOM   9745  C  CB  . ASP   A 1 1215 ? -22.66400  45.40400  13.66600  1.000 81.08317  ?  1213 ASP   A CB  1 
ATOM   9746  C  CG  . ASP   A 1 1215 ? -21.64700  45.77200  14.72300  1.000 80.92043  ?  1213 ASP   A CG  1 
ATOM   9747  O  OD1 . ASP   A 1 1215 ? -20.44700  45.50700  14.50100  1.000 85.51704  ?  1213 ASP   A OD1 1 
ATOM   9748  O  OD2 . ASP   A 1 1215 ? -22.04600  46.31700  15.77400  1.000 76.04134  -1 1213 ASP   A OD2 1 
ATOM   9749  N  N   . THR   A 1 1216 ? -21.10700  42.31600  12.31300  1.000 70.09671  ?  1214 THR   A N   1 
ATOM   9750  C  CA  . THR   A 1 1216 ? -21.08800  40.85900  12.37700  1.000 66.36096  ?  1214 THR   A CA  1 
ATOM   9751  C  C   . THR   A 1 1216 ? -19.74000  40.30200  12.82700  1.000 77.39072  ?  1214 THR   A C   1 
ATOM   9752  O  O   . THR   A 1 1216 ? -19.49200  39.10200  12.67600  1.000 75.08538  ?  1214 THR   A O   1 
ATOM   9753  C  CB  . THR   A 1 1216 ? -21.47100  40.26300  11.01900  1.000 57.70201  ?  1214 THR   A CB  1 
ATOM   9754  O  OG1 . THR   A 1 1216 ? -20.55100  40.70500  10.00900  1.000 36.19876  ?  1214 THR   A OG1 1 
ATOM   9755  C  CG2 . THR   A 1 1216 ? -22.88100  40.69000  10.62900  1.000 53.53869  ?  1214 THR   A CG2 1 
ATOM   9756  N  N   . ALA   A 1 1217 ? -18.87000  41.13300  13.39000  1.000 71.63982  ?  1215 ALA   A N   1 
ATOM   9757  C  CA  . ALA   A 1 1217 ? -17.52600  40.67600  13.71600  1.000 47.91003  ?  1215 ALA   A CA  1 
ATOM   9758  C  C   . ALA   A 1 1217 ? -17.54500  39.77100  14.94200  1.000 69.17224  ?  1215 ALA   A C   1 
ATOM   9759  O  O   . ALA   A 1 1217 ? -18.17700  40.08800  15.95500  1.000 66.86765  ?  1215 ALA   A O   1 
ATOM   9760  C  CB  . ALA   A 1 1217 ? -16.60400  41.87000  13.95000  1.000 54.87204  ?  1215 ALA   A CB  1 
ATOM   9761  N  N   . LYS   A 1 1218 ? -16.85100  38.63700  14.84200  1.000 78.30022  ?  1216 LYS   A N   1 
ATOM   9762  C  CA  . LYS   A 1 1218 ? -16.67700  37.71800  15.95800  1.000 69.22712  ?  1216 LYS   A CA  1 
ATOM   9763  C  C   . LYS   A 1 1218 ? -15.32600  37.02800  15.81600  1.000 72.56638  ?  1216 LYS   A C   1 
ATOM   9764  O  O   . LYS   A 1 1218 ? -14.91500  36.68100  14.70600  1.000 71.01545  ?  1216 LYS   A O   1 
ATOM   9765  C  CB  . LYS   A 1 1218 ? -17.80600  36.68100  16.01400  1.000 55.04696  ?  1216 LYS   A CB  1 
ATOM   9766  C  CG  . LYS   A 1 1218 ? -17.71700  35.71500  17.19000  1.000 57.52952  ?  1216 LYS   A CG  1 
ATOM   9767  C  CD  . LYS   A 1 1218 ? -19.03300  35.63400  17.94800  1.000 56.96568  ?  1216 LYS   A CD  1 
ATOM   9768  C  CE  . LYS   A 1 1218 ? -19.13500  34.34300  18.74700  1.000 71.71343  ?  1216 LYS   A CE  1 
ATOM   9769  N  NZ  . LYS   A 1 1218 ? -20.44800  34.22300  19.44400  1.000 83.02467  ?  1216 LYS   A NZ  1 
ATOM   9770  N  N   . ALA   A 1 1219 ? -14.63900  36.84000  16.94300  1.000 76.19566  ?  1217 ALA   A N   1 
ATOM   9771  C  CA  . ALA   A 1 1219 ? -13.33000  36.19300  16.94800  1.000 75.70047  ?  1217 ALA   A CA  1 
ATOM   9772  C  C   . ALA   A 1 1219 ? -13.50500  34.68000  16.92400  1.000 71.50747  ?  1217 ALA   A C   1 
ATOM   9773  O  O   . ALA   A 1 1219 ? -14.15200  34.10900  17.81000  1.000 70.44040  ?  1217 ALA   A O   1 
ATOM   9774  C  CB  . ALA   A 1 1219 ? -12.52200  36.62100  18.17100  1.000 67.07606  ?  1217 ALA   A CB  1 
ATOM   9775  N  N   . TYR   A 1 1220 ? -12.91900  34.02900  15.92100  1.000 60.21738  ?  1218 TYR   A N   1 
ATOM   9776  C  CA  . TYR   A 1 1220 ? -13.10300  32.59900  15.77100  1.000 80.16141  ?  1218 TYR   A CA  1 
ATOM   9777  C  C   . TYR   A 1 1220 ? -11.76600  31.87000  15.81400  1.000 83.28245  ?  1218 TYR   A C   1 
ATOM   9778  O  O   . TYR   A 1 1220 ? -10.76900  32.36800  15.27900  1.000 77.28567  ?  1218 TYR   A O   1 
ATOM   9779  C  CB  . TYR   A 1 1220 ? -13.82800  32.27500  14.45700  1.000 71.18498  ?  1218 TYR   A CB  1 
ATOM   9780  C  CG  . TYR   A 1 1220 ? -15.32800  32.42700  14.56000  1.000 63.94313  ?  1218 TYR   A CG  1 
ATOM   9781  C  CD1 . TYR   A 1 1220 ? -15.97100  32.27500  15.78300  1.000 58.14845  ?  1218 TYR   A CD1 1 
ATOM   9782  C  CD2 . TYR   A 1 1220 ? -16.10200  32.72400  13.44400  1.000 58.61765  ?  1218 TYR   A CD2 1 
ATOM   9783  C  CE1 . TYR   A 1 1220 ? -17.33900  32.41000  15.89500  1.000 64.65895  ?  1218 TYR   A CE1 1 
ATOM   9784  C  CE2 . TYR   A 1 1220 ? -17.47900  32.86200  13.54700  1.000 57.96227  ?  1218 TYR   A CE2 1 
ATOM   9785  C  CZ  . TYR   A 1 1220 ? -18.09000  32.70300  14.77900  1.000 62.35330  ?  1218 TYR   A CZ  1 
ATOM   9786  O  OH  . TYR   A 1 1220 ? -19.45300  32.83500  14.90900  1.000 45.30664  ?  1218 TYR   A OH  1 
ATOM   9787  N  N   . PRO   A 1 1221 ? -11.71400  30.69700  16.44800  1.000 77.61600  ?  1219 PRO   A N   1 
ATOM   9788  C  CA  . PRO   A 1 1221 ? -10.44500  29.96400  16.54700  1.000 46.91980  ?  1219 PRO   A CA  1 
ATOM   9789  C  C   . PRO   A 1 1221 ? -9.91100   29.59400  15.17200  1.000 64.35692  ?  1219 PRO   A C   1 
ATOM   9790  O  O   . PRO   A 1 1221 ? -10.65800  29.17300  14.28600  1.000 78.97792  ?  1219 PRO   A O   1 
ATOM   9791  C  CB  . PRO   A 1 1221 ? -10.80500  28.71500  17.36100  1.000 62.63231  ?  1219 PRO   A CB  1 
ATOM   9792  C  CG  . PRO   A 1 1221 ? -12.15600  28.95200  17.93100  1.000 82.33967  ?  1219 PRO   A CG  1 
ATOM   9793  C  CD  . PRO   A 1 1221 ? -12.81500  30.06500  17.19400  1.000 78.63085  ?  1219 PRO   A CD  1 
ATOM   9794  N  N   . ASN   A 1 1222 ? -8.60100   29.75500  15.00300  1.000 59.71355  ?  1220 ASN   A N   1 
ATOM   9795  C  CA  . ASN   A 1 1222 ? -7.94000   29.53000  13.72600  1.000 75.09374  ?  1220 ASN   A CA  1 
ATOM   9796  C  C   . ASN   A 1 1222 ? -7.43800   28.10000  13.55900  1.000 79.84195  ?  1220 ASN   A C   1 
ATOM   9797  O  O   . ASN   A 1 1222 ? -6.68300   27.82900  12.61900  1.000 82.71956  ?  1220 ASN   A O   1 
ATOM   9798  C  CB  . ASN   A 1 1222 ? -6.77900   30.51500  13.56100  1.000 67.62691  ?  1220 ASN   A CB  1 
ATOM   9799  C  CG  . ASN   A 1 1222 ? -7.07900   31.87000  14.17200  1.000 99.10186  ?  1220 ASN   A CG  1 
ATOM   9800  O  OD1 . ASN   A 1 1222 ? -7.82400   32.67000  13.60400  1.000 103.11435 ?  1220 ASN   A OD1 1 
ATOM   9801  N  ND2 . ASN   A 1 1222 ? -6.50600   32.13100  15.34100  1.000 108.14660 ?  1220 ASN   A ND2 1 
ATOM   9802  N  N   . LYS   A 1 1223 ? -7.83600   27.18700  14.44300  1.000 73.98465  ?  1221 LYS   A N   1 
ATOM   9803  C  CA  . LYS   A 1 1223 ? -7.43800   25.79000  14.31700  1.000 66.45686  ?  1221 LYS   A CA  1 
ATOM   9804  C  C   . LYS   A 1 1223 ? -8.17200   25.15500  13.14300  1.000 76.81335  ?  1221 LYS   A C   1 
ATOM   9805  O  O   . LYS   A 1 1223 ? -9.40700   25.10900  13.12400  1.000 72.93288  ?  1221 LYS   A O   1 
ATOM   9806  C  CB  . LYS   A 1 1223 ? -7.73100   25.03300  15.61000  1.000 79.32320  ?  1221 LYS   A CB  1 
ATOM   9807  C  CG  . LYS   A 1 1223 ? -6.95700   23.72900  15.75100  1.000 79.94758  ?  1221 LYS   A CG  1 
ATOM   9808  C  CD  . LYS   A 1 1223 ? -6.71400   23.38300  17.21100  1.000 69.93869  ?  1221 LYS   A CD  1 
ATOM   9809  C  CE  . LYS   A 1 1223 ? -7.97300   22.84500  17.86900  1.000 64.22147  ?  1221 LYS   A CE  1 
ATOM   9810  N  NZ  . LYS   A 1 1223 ? -7.88200   22.88800  19.35500  1.000 80.00515  ?  1221 LYS   A NZ  1 
ATOM   9811  N  N   . LEU   A 1 1224 ? -7.41100   24.66900  12.16600  1.000 64.13697  ?  1222 LEU   A N   1 
ATOM   9812  C  CA  . LEU   A 1 1224 ? -8.00300   24.11700  10.95800  1.000 63.68443  ?  1222 LEU   A CA  1 
ATOM   9813  C  C   . LEU   A 1 1224 ? -8.81000   22.86100  11.28100  1.000 79.27957  ?  1222 LEU   A C   1 
ATOM   9814  O  O   . LEU   A 1 1224 ? -8.69000   22.26900  12.35800  1.000 88.64670  ?  1222 LEU   A O   1 
ATOM   9815  C  CB  . LEU   A 1 1224 ? -6.91600   23.80700  9.93100   1.000 51.36008  ?  1222 LEU   A CB  1 
ATOM   9816  C  CG  . LEU   A 1 1224 ? -5.93200   24.94400  9.64400   1.000 56.63750  ?  1222 LEU   A CG  1 
ATOM   9817  C  CD1 . LEU   A 1 1224 ? -4.99900   24.56800  8.50500   1.000 62.30840  ?  1222 LEU   A CD1 1 
ATOM   9818  C  CD2 . LEU   A 1 1224 ? -6.66800   26.23600  9.32900   1.000 58.93235  ?  1222 LEU   A CD2 1 
ATOM   9819  N  N   . ILE   A 1 1225 ? -9.64500   22.45300  10.32200  1.000 79.34176  ?  1223 ILE   A N   1 
ATOM   9820  C  CA  . ILE   A 1 1225 ? -10.56100  21.34400  10.57000  1.000 80.01794  ?  1223 ILE   A CA  1 
ATOM   9821  C  C   . ILE   A 1 1225 ? -9.83300   20.00300  10.53800  1.000 71.89533  ?  1223 ILE   A C   1 
ATOM   9822  O  O   . ILE   A 1 1225 ? -10.22000  19.07100  11.25300  1.000 71.19119  ?  1223 ILE   A O   1 
ATOM   9823  C  CB  . ILE   A 1 1225 ? -11.73500  21.38000  9.57200   1.000 77.87036  ?  1223 ILE   A CB  1 
ATOM   9824  C  CG1 . ILE   A 1 1225 ? -12.92000  20.57900  10.11200  1.000 72.60494  ?  1223 ILE   A CG1 1 
ATOM   9825  C  CG2 . ILE   A 1 1225 ? -11.31800  20.87200  8.19500   1.000 68.34466  ?  1223 ILE   A CG2 1 
ATOM   9826  C  CD1 . ILE   A 1 1225 ? -13.92800  21.42200  10.85400  1.000 68.81702  ?  1223 ILE   A CD1 1 
ATOM   9827  N  N   . MET   A 1 1226 ? -8.77100   19.87900  9.73600   1.000 69.55537  ?  1224 MET   A N   1 
ATOM   9828  C  CA  . MET   A 1 1226 ? -8.02600   18.62500  9.70900   1.000 62.15767  ?  1224 MET   A CA  1 
ATOM   9829  C  C   . MET   A 1 1226 ? -7.34000   18.38000  11.04400  1.000 60.12138  ?  1224 MET   A C   1 
ATOM   9830  O  O   . MET   A 1 1226 ? -7.19700   17.23000  11.46900  1.000 73.26027  ?  1224 MET   A O   1 
ATOM   9831  C  CB  . MET   A 1 1226 ? -7.00000   18.64300  8.57800   1.000 54.82223  ?  1224 MET   A CB  1 
ATOM   9832  C  CG  . MET   A 1 1226 ? -5.97800   19.76800  8.67900   1.000 66.70294  ?  1224 MET   A CG  1 
ATOM   9833  S  SD  . MET   A 1 1226 ? -5.80200   20.63800  7.12000   1.000 75.29036  ?  1224 MET   A SD  1 
ATOM   9834  C  CE  . MET   A 1 1226 ? -7.52600   21.04100  6.84000   1.000 83.58712  ?  1224 MET   A CE  1 
ATOM   9835  N  N   . SER   A 1 1227 ? -6.91800   19.44600  11.72200  1.000 62.80641  ?  1225 SER   A N   1 
ATOM   9836  C  CA  . SER   A 1 1227 ? -6.39400   19.28500  13.06900  1.000 58.89809  ?  1225 SER   A CA  1 
ATOM   9837  C  C   . SER   A 1 1227 ? -7.51000   18.93700  14.04700  1.000 61.06870  ?  1225 SER   A C   1 
ATOM   9838  O  O   . SER   A 1 1227 ? -7.34400   18.05000  14.89100  1.000 75.48381  ?  1225 SER   A O   1 
ATOM   9839  C  CB  . SER   A 1 1227 ? -5.65100   20.55200  13.49200  1.000 67.55415  ?  1225 SER   A CB  1 
ATOM   9840  O  OG  . SER   A 1 1227 ? -4.80600   21.00900  12.44500  1.000 72.38219  ?  1225 SER   A OG  1 
ATOM   9841  N  N   . MET   A 1 1228 ? -8.66900   19.59700  13.91700  1.000 69.16700  ?  1226 MET   A N   1 
ATOM   9842  C  CA  . MET   A 1 1228 ? -9.77900   19.37200  14.84400  1.000 76.83120  ?  1226 MET   A CA  1 
ATOM   9843  C  C   . MET   A 1 1228 ? -10.14900  17.89600  14.93700  1.000 77.04651  ?  1226 MET   A C   1 
ATOM   9844  O  O   . MET   A 1 1228 ? -10.38900  17.37800  16.03400  1.000 72.73418  ?  1226 MET   A O   1 
ATOM   9845  C  CB  . MET   A 1 1228 ? -10.99500  20.19500  14.42100  1.000 70.63093  ?  1226 MET   A CB  1 
ATOM   9846  C  CG  . MET   A 1 1228 ? -10.84000  21.69200  14.61900  1.000 79.53620  ?  1226 MET   A CG  1 
ATOM   9847  S  SD  . MET   A 1 1228 ? -12.35500  22.59400  14.24100  1.000 72.83133  ?  1226 MET   A SD  1 
ATOM   9848  C  CE  . MET   A 1 1228 ? -13.02800  22.83500  15.88600  1.000 43.97737  ?  1226 MET   A CE  1 
ATOM   9849  N  N   . LEU   A 1 1229 ? -10.19800  17.19900  13.79900  1.000 58.96635  ?  1227 LEU   A N   1 
ATOM   9850  C  CA  . LEU   A 1 1229 ? -10.50700  15.77200  13.82100  1.000 62.99992  ?  1227 LEU   A CA  1 
ATOM   9851  C  C   . LEU   A 1 1229 ? -9.43100   14.99000  14.56600  1.000 74.51677  ?  1227 LEU   A C   1 
ATOM   9852  O  O   . LEU   A 1 1229 ? -9.73200   14.20000  15.46900  1.000 60.46736  ?  1227 LEU   A O   1 
ATOM   9853  C  CB  . LEU   A 1 1229 ? -10.66300  15.24500  12.39400  1.000 63.68822  ?  1227 LEU   A CB  1 
ATOM   9854  C  CG  . LEU   A 1 1229 ? -10.40500  13.74700  12.21000  1.000 68.91428  ?  1227 LEU   A CG  1 
ATOM   9855  C  CD1 . LEU   A 1 1229 ? -11.58100  12.92700  12.73100  1.000 60.85035  ?  1227 LEU   A CD1 1 
ATOM   9856  C  CD2 . LEU   A 1 1229 ? -10.11200  13.42400  10.75400  1.000 56.76541  ?  1227 LEU   A CD2 1 
ATOM   9857  N  N   . GLU   A 1 1230 ? -8.16300   15.20200  14.19800  1.000 77.79539  ?  1228 GLU   A N   1 
ATOM   9858  C  CA  . GLU   A 1 1230 ? -7.07800   14.47200  14.84300  1.000 72.60939  ?  1228 GLU   A CA  1 
ATOM   9859  C  C   . GLU   A 1 1230 ? -6.97900   14.80900  16.32600  1.000 73.07637  ?  1228 GLU   A C   1 
ATOM   9860  O  O   . GLU   A 1 1230 ? -6.57500   13.95500  17.12400  1.000 91.28202  ?  1228 GLU   A O   1 
ATOM   9861  C  CB  . GLU   A 1 1230 ? -5.75500   14.75100  14.12300  1.000 60.41404  ?  1228 GLU   A CB  1 
ATOM   9862  C  CG  . GLU   A 1 1230 ? -4.94000   15.90400  14.69300  1.000 71.67593  ?  1228 GLU   A CG  1 
ATOM   9863  C  CD  . GLU   A 1 1230 ? -3.73200   16.24200  13.84100  1.000 79.34570  ?  1228 GLU   A CD  1 
ATOM   9864  O  OE1 . GLU   A 1 1230 ? -3.61100   15.68500  12.72800  1.000 61.25510  ?  1228 GLU   A OE1 1 
ATOM   9865  O  OE2 . GLU   A 1 1230 ? -2.90300   17.06400  14.28400  1.000 86.70981  -1 1228 GLU   A OE2 1 
ATOM   9866  N  N   . ASP   A 1 1231 ? -7.34700   16.03600  16.72100  1.000 63.57571  ?  1229 ASP   A N   1 
ATOM   9867  C  CA  . ASP   A 1 1231 ? -7.40600   16.34600  18.14700  1.000 63.07978  ?  1229 ASP   A CA  1 
ATOM   9868  C  C   . ASP   A 1 1231 ? -8.57400   15.62700  18.81000  1.000 73.10462  ?  1229 ASP   A C   1 
ATOM   9869  O  O   . ASP   A 1 1231 ? -8.44100   15.11600  19.92800  1.000 83.98389  ?  1229 ASP   A O   1 
ATOM   9870  C  CB  . ASP   A 1 1231 ? -7.50700   17.86200  18.39900  1.000 73.23012  ?  1229 ASP   A CB  1 
ATOM   9871  C  CG  . ASP   A 1 1231 ? -6.24600   18.63500  17.97900  1.000 89.59640  ?  1229 ASP   A CG  1 
ATOM   9872  O  OD1 . ASP   A 1 1231 ? -5.21700   18.50800  18.68700  1.000 104.96427 ?  1229 ASP   A OD1 1 
ATOM   9873  O  OD2 . ASP   A 1 1231 ? -6.27600   19.34300  16.94100  1.000 97.00773  -1 1229 ASP   A OD2 1 
ATOM   9874  N  N   . TRP   A 1 1232 ? -9.72900   15.58900  18.14100  1.000 77.74769  ?  1230 TRP   A N   1 
ATOM   9875  C  CA  . TRP   A 1 1232 ? -10.90500  14.94700  18.72200  1.000 86.56915  ?  1230 TRP   A CA  1 
ATOM   9876  C  C   . TRP   A 1 1232 ? -10.68600  13.44900  18.89000  1.000 82.02595  ?  1230 TRP   A C   1 
ATOM   9877  O  O   . TRP   A 1 1232 ? -11.03000  12.87100  19.92700  1.000 68.79874  ?  1230 TRP   A O   1 
ATOM   9878  C  CB  . TRP   A 1 1232 ? -12.13300  15.21200  17.85200  1.000 82.11645  ?  1230 TRP   A CB  1 
ATOM   9879  C  CG  . TRP   A 1 1232 ? -12.78600  16.55600  18.04100  1.000 86.75121  ?  1230 TRP   A CG  1 
ATOM   9880  C  CD1 . TRP   A 1 1232 ? -13.32400  17.33700  17.06100  1.000 82.20808  ?  1230 TRP   A CD1 1 
ATOM   9881  C  CD2 . TRP   A 1 1232 ? -12.99300  17.26600  19.27500  1.000 86.00140  ?  1230 TRP   A CD2 1 
ATOM   9882  N  NE1 . TRP   A 1 1232 ? -13.84000  18.48700  17.59900  1.000 86.58022  ?  1230 TRP   A NE1 1 
ATOM   9883  C  CE2 . TRP   A 1 1232 ? -13.65200  18.47000  18.95500  1.000 82.20794  ?  1230 TRP   A CE2 1 
ATOM   9884  C  CE3 . TRP   A 1 1232 ? -12.68100  17.00600  20.61500  1.000 80.77778  ?  1230 TRP   A CE3 1 
ATOM   9885  C  CZ2 . TRP   A 1 1232 ? -14.00500  19.40800  19.92200  1.000 81.13088  ?  1230 TRP   A CZ2 1 
ATOM   9886  C  CZ3 . TRP   A 1 1232 ? -13.03400  17.94000  21.57300  1.000 83.36116  ?  1230 TRP   A CZ3 1 
ATOM   9887  C  CH2 . TRP   A 1 1232 ? -13.68800  19.12500  21.22200  1.000 77.05122  ?  1230 TRP   A CH2 1 
ATOM   9888  N  N   . ALA   A 1 1233 ? -10.11500  12.80300  17.86900  1.000 76.37741  ?  1231 ALA   A N   1 
ATOM   9889  C  CA  . ALA   A 1 1233 ? -9.88100   11.36400  17.93600  1.000 72.38668  ?  1231 ALA   A CA  1 
ATOM   9890  C  C   . ALA   A 1 1233 ? -8.95600   11.00600  19.09200  1.000 86.78229  ?  1231 ALA   A C   1 
ATOM   9891  O  O   . ALA   A 1 1233 ? -9.18300   10.01300  19.79100  1.000 94.02260  ?  1231 ALA   A O   1 
ATOM   9892  C  CB  . ALA   A 1 1233 ? -9.30000   10.86600  16.61300  1.000 75.65058  ?  1231 ALA   A CB  1 
ATOM   9893  N  N   . ALA   A 1 1234 ? -7.91200   11.81000  19.31300  1.000 73.66433  ?  1232 ALA   A N   1 
ATOM   9894  C  CA  . ALA   A 1 1234 ? -6.96400   11.52200  20.38500  1.000 66.40029  ?  1232 ALA   A CA  1 
ATOM   9895  C  C   . ALA   A 1 1234 ? -7.63800   11.48700  21.75100  1.000 72.13857  ?  1232 ALA   A C   1 
ATOM   9896  O  O   . ALA   A 1 1234 ? -7.19900   10.74700  22.63800  1.000 89.13166  ?  1232 ALA   A O   1 
ATOM   9897  C  CB  . ALA   A 1 1234 ? -5.83800   12.55500  20.37700  1.000 70.93485  ?  1232 ALA   A CB  1 
ATOM   9898  N  N   . ALA   A 1 1235 ? -8.70000   12.27000  21.94000  1.000 61.06832  ?  1233 ALA   A N   1 
ATOM   9899  C  CA  . ALA   A 1 1235 ? -9.41600   12.30100  23.21000  1.000 74.65738  ?  1233 ALA   A CA  1 
ATOM   9900  C  C   . ALA   A 1 1235 ? -10.62300  11.37400  23.24600  1.000 83.46665  ?  1233 ALA   A C   1 
ATOM   9901  O  O   . ALA   A 1 1235 ? -10.94100  10.83400  24.31000  1.000 90.61161  ?  1233 ALA   A O   1 
ATOM   9902  C  CB  . ALA   A 1 1235 ? -9.87100   13.72800  23.52900  1.000 92.09576  ?  1233 ALA   A CB  1 
ATOM   9903  N  N   . THR   A 1 1236 ? -11.30600  11.18300  22.11700  1.000 90.77429  ?  1234 THR   A N   1 
ATOM   9904  C  CA  . THR   A 1 1236 ? -12.44300  10.27100  22.01000  1.000 89.29401  ?  1234 THR   A CA  1 
ATOM   9905  C  C   . THR   A 1 1236 ? -12.16100  9.27700   20.89000  1.000 94.43262  ?  1234 THR   A C   1 
ATOM   9906  O  O   . THR   A 1 1236 ? -12.76300  9.35100   19.80900  1.000 97.34191  ?  1234 THR   A O   1 
ATOM   9907  C  CB  . THR   A 1 1236 ? -13.74600  11.02300  21.74800  1.000 74.60373  ?  1234 THR   A CB  1 
ATOM   9908  O  OG1 . THR   A 1 1236 ? -13.57000  11.90900  20.63600  1.000 92.54884  ?  1234 THR   A OG1 1 
ATOM   9909  C  CG2 . THR   A 1 1236 ? -14.15300  11.82600  22.97400  1.000 70.22335  ?  1234 THR   A CG2 1 
ATOM   9910  N  N   . PRO   A 1 1237 ? -11.25000  8.32700   21.11800  1.000 85.48872  ?  1235 PRO   A N   1 
ATOM   9911  C  CA  . PRO   A 1 1237 ? -10.86900  7.42200   20.02200  1.000 87.67399  ?  1235 PRO   A CA  1 
ATOM   9912  C  C   . PRO   A 1 1237 ? -11.98000  6.47500   19.61600  1.000 79.57389  ?  1235 PRO   A C   1 
ATOM   9913  O  O   . PRO   A 1 1237 ? -12.13600  6.19100   18.42200  1.000 69.64103  ?  1235 PRO   A O   1 
ATOM   9914  C  CB  . PRO   A 1 1237 ? -9.65800   6.67700   20.59800  1.000 66.81145  ?  1235 PRO   A CB  1 
ATOM   9915  C  CG  . PRO   A 1 1237 ? -9.88900   6.69000   22.07200  1.000 79.70860  ?  1235 PRO   A CG  1 
ATOM   9916  C  CD  . PRO   A 1 1237 ? -10.56000  8.00000   22.37800  1.000 70.39600  ?  1235 PRO   A CD  1 
ATOM   9917  N  N   . ASP   A 1 1238 ? -12.76900  5.98800   20.57300  1.000 74.99546  ?  1236 ASP   A N   1 
ATOM   9918  C  CA  . ASP   A 1 1238 ? -13.79700  4.98900   20.31000  1.000 87.34371  ?  1236 ASP   A CA  1 
ATOM   9919  C  C   . ASP   A 1 1238 ? -15.20100  5.58800   20.27100  1.000 85.33068  ?  1236 ASP   A C   1 
ATOM   9920  O  O   . ASP   A 1 1238 ? -16.17000  4.92800   20.66300  1.000 69.72946  ?  1236 ASP   A O   1 
ATOM   9921  C  CB  . ASP   A 1 1238 ? -13.71300  3.86600   21.34400  1.000 93.40639  ?  1236 ASP   A CB  1 
ATOM   9922  C  CG  . ASP   A 1 1238 ? -12.31400  3.28100   21.45800  1.000 85.71802  ?  1236 ASP   A CG  1 
ATOM   9923  O  OD1 . ASP   A 1 1238 ? -11.64300  3.12300   20.41500  1.000 81.48196  ?  1236 ASP   A OD1 1 
ATOM   9924  O  OD2 . ASP   A 1 1238 ? -11.88700  2.97700   22.59100  1.000 82.24300  -1 1236 ASP   A OD2 1 
ATOM   9925  N  N   . LYS   A 1 1239 ? -15.33100  6.82400   19.79700  1.000 83.33563  ?  1237 LYS   A N   1 
ATOM   9926  C  CA  . LYS   A 1 1239 ? -16.62900  7.44400   19.58000  1.000 64.53164  ?  1237 LYS   A CA  1 
ATOM   9927  C  C   . LYS   A 1 1239 ? -16.99800  7.36700   18.10400  1.000 69.77616  ?  1237 LYS   A C   1 
ATOM   9928  O  O   . LYS   A 1 1239 ? -16.13200  7.41500   17.22600  1.000 74.01503  ?  1237 LYS   A O   1 
ATOM   9929  C  CB  . LYS   A 1 1239 ? -16.63600  8.90300   20.04300  1.000 66.85260  ?  1237 LYS   A CB  1 
ATOM   9930  C  CG  . LYS   A 1 1239 ? -18.03700  9.47800   20.23700  1.000 79.68239  ?  1237 LYS   A CG  1 
ATOM   9931  C  CD  . LYS   A 1 1239 ? -18.06400  10.98900  20.04500  1.000 71.19735  ?  1237 LYS   A CD  1 
ATOM   9932  C  CE  . LYS   A 1 1239 ? -19.49200  11.52400  20.04700  1.000 65.09433  ?  1237 LYS   A CE  1 
ATOM   9933  N  NZ  . LYS   A 1 1239 ? -20.39900  10.72400  19.17100  1.000 76.72402  ?  1237 LYS   A NZ  1 
ATOM   9934  N  N   . THR   A 1 1240 ? -18.29600  7.24500   17.83900  1.000 65.68896  ?  1238 THR   A N   1 
ATOM   9935  C  CA  . THR   A 1 1240 ? -18.77200  7.11800   16.46800  1.000 61.56683  ?  1238 THR   A CA  1 
ATOM   9936  C  C   . THR   A 1 1240 ? -18.57400  8.42600   15.71000  1.000 64.62029  ?  1238 THR   A C   1 
ATOM   9937  O  O   . THR   A 1 1240 ? -19.01200  9.49000   16.15900  1.000 64.43009  ?  1238 THR   A O   1 
ATOM   9938  C  CB  . THR   A 1 1240 ? -20.24800  6.72300   16.45100  1.000 61.41601  ?  1238 THR   A CB  1 
ATOM   9939  O  OG1 . THR   A 1 1240 ? -20.50100  5.74800   17.47100  1.000 51.41899  ?  1238 THR   A OG1 1 
ATOM   9940  C  CG2 . THR   A 1 1240 ? -20.62300  6.14500   15.09400  1.000 46.98508  ?  1238 THR   A CG2 1 
ATOM   9941  N  N   . ALA   A 1 1241 ? -17.91200  8.34200   14.55700  1.000 54.00822  ?  1239 ALA   A N   1 
ATOM   9942  C  CA  . ALA   A 1 1241 ? -17.68300  9.48800   13.68800  1.000 55.35274  ?  1239 ALA   A CA  1 
ATOM   9943  C  C   . ALA   A 1 1241 ? -18.47700  9.41000   12.39300  1.000 57.69962  ?  1239 ALA   A C   1 
ATOM   9944  O  O   . ALA   A 1 1241 ? -19.11100  10.39300  11.99500  1.000 57.21856  ?  1239 ALA   A O   1 
ATOM   9945  C  CB  . ALA   A 1 1241 ? -16.18500  9.62300   13.37200  1.000 41.34832  ?  1239 ALA   A CB  1 
ATOM   9946  N  N   . LEU   A 1 1242 ? -18.45800  8.26200   11.72100  1.000 47.15484  ?  1240 LEU   A N   1 
ATOM   9947  C  CA  . LEU   A 1 1242 ? -19.19300  8.05800   10.48200  1.000 48.22471  ?  1240 LEU   A CA  1 
ATOM   9948  C  C   . LEU   A 1 1242 ? -20.14400  6.87700   10.62300  1.000 49.10599  ?  1240 LEU   A C   1 
ATOM   9949  O  O   . LEU   A 1 1242 ? -19.86300  5.91600   11.34500  1.000 52.00247  ?  1240 LEU   A O   1 
ATOM   9950  C  CB  . LEU   A 1 1242 ? -18.24300  7.81600   9.30400   1.000 34.36263  ?  1240 LEU   A CB  1 
ATOM   9951  C  CG  . LEU   A 1 1242 ? -17.30700  8.96100   8.92200   1.000 43.66010  ?  1240 LEU   A CG  1 
ATOM   9952  C  CD1 . LEU   A 1 1242 ? -16.75000  8.71500   7.53200   1.000 43.66830  ?  1240 LEU   A CD1 1 
ATOM   9953  C  CD2 . LEU   A 1 1242 ? -18.03800  10.29800  8.98900   1.000 53.08045  ?  1240 LEU   A CD2 1 
ATOM   9954  N  N   . VAL   A 1 1243 ? -21.28100  6.96200   9.93300   1.000 46.45386  ?  1241 VAL   A N   1 
ATOM   9955  C  CA  . VAL   A 1 1243 ? -22.25400  5.87200   9.87500   1.000 40.95768  ?  1241 VAL   A CA  1 
ATOM   9956  C  C   . VAL   A 1 1243 ? -22.71500  5.74000   8.42800   1.000 42.20888  ?  1241 VAL   A C   1 
ATOM   9957  O  O   . VAL   A 1 1243 ? -23.48200  6.57700   7.94000   1.000 46.57989  ?  1241 VAL   A O   1 
ATOM   9958  C  CB  . VAL   A 1 1243 ? -23.46000  6.09700   10.80200  1.000 38.96997  ?  1241 VAL   A CB  1 
ATOM   9959  C  CG1 . VAL   A 1 1243 ? -24.41600  4.91500   10.71800  1.000 50.31394  ?  1241 VAL   A CG1 1 
ATOM   9960  C  CG2 . VAL   A 1 1243 ? -23.01000  6.30900   12.24700  1.000 38.19876  ?  1241 VAL   A CG2 1 
ATOM   9961  N  N   . PHE   A 1 1244 ? -22.25400  4.69800   7.74200   1.000 52.35292  ?  1242 PHE   A N   1 
ATOM   9962  C  CA  . PHE   A 1 1244 ? -22.69300  4.39200   6.38900   1.000 50.94122  ?  1242 PHE   A CA  1 
ATOM   9963  C  C   . PHE   A 1 1244 ? -23.43600  3.06400   6.38000   1.000 55.83601  ?  1242 PHE   A C   1 
ATOM   9964  O  O   . PHE   A 1 1244 ? -22.98600  2.08900   6.99200   1.000 59.00626  ?  1242 PHE   A O   1 
ATOM   9965  C  CB  . PHE   A 1 1244 ? -21.51600  4.33100   5.41100   1.000 37.37009  ?  1242 PHE   A CB  1 
ATOM   9966  C  CG  . PHE   A 1 1244 ? -21.93700  4.28700   3.97100   1.000 39.90635  ?  1242 PHE   A CG  1 
ATOM   9967  C  CD1 . PHE   A 1 1244 ? -23.06300  4.97300   3.54700   1.000 49.55942  ?  1242 PHE   A CD1 1 
ATOM   9968  C  CD2 . PHE   A 1 1244 ? -21.22500  3.54400   3.04500   1.000 45.64212  ?  1242 PHE   A CD2 1 
ATOM   9969  C  CE1 . PHE   A 1 1244 ? -23.46300  4.93200   2.22500   1.000 61.36777  ?  1242 PHE   A CE1 1 
ATOM   9970  C  CE2 . PHE   A 1 1244 ? -21.62200  3.49700   1.71900   1.000 49.99826  ?  1242 PHE   A CE2 1 
ATOM   9971  C  CZ  . PHE   A 1 1244 ? -22.74100  4.19200   1.30900   1.000 49.08953  ?  1242 PHE   A CZ  1 
ATOM   9972  N  N   . ARG   A 1 1245 ? -24.57000  3.03400   5.67400   1.000 62.19460  ?  1243 ARG   A N   1 
ATOM   9973  C  CA  . ARG   A 1 1245 ? -25.44500  1.86600   5.65300   1.000 55.50040  ?  1243 ARG   A CA  1 
ATOM   9974  C  C   . ARG   A 1 1245 ? -25.79100  1.45600   7.07800   1.000 66.31172  ?  1243 ARG   A C   1 
ATOM   9975  O  O   . ARG   A 1 1245 ? -26.45300  2.20600   7.80400   1.000 76.69538  ?  1243 ARG   A O   1 
ATOM   9976  C  CB  . ARG   A 1 1245 ? -24.79000  0.70300   4.90000   1.000 54.95171  ?  1243 ARG   A CB  1 
ATOM   9977  C  CG  . ARG   A 1 1245 ? -25.29300  0.50700   3.47600   1.000 57.79084  ?  1243 ARG   A CG  1 
ATOM   9978  C  CD  . ARG   A 1 1245 ? -25.10500  1.75700   2.63400   1.000 50.95025  ?  1243 ARG   A CD  1 
ATOM   9979  N  NE  . ARG   A 1 1245 ? -25.31400  1.49800   1.21500   1.000 58.15190  ?  1243 ARG   A NE  1 
ATOM   9980  C  CZ  . ARG   A 1 1245 ? -24.41100  0.95400   0.41100   1.000 65.62830  ?  1243 ARG   A CZ  1 
ATOM   9981  N  NH1 . ARG   A 1 1245 ? -23.22000  0.58600   0.85600   1.000 56.55322  ?  1243 ARG   A NH1 1 
ATOM   9982  N  NH2 . ARG   A 1 1245 ? -24.71000  0.77500   -0.87300  1.000 60.09309  ?  1243 ARG   A NH2 1 
ATOM   9983  N  N   . GLU   A 1 1246 ? -25.33600  0.27500   7.49000   1.000 57.64832  ?  1244 GLU   A N   1 
ATOM   9984  C  CA  . GLU   A 1 1246 ? -25.49600  -0.19000  8.86100   1.000 60.66240  ?  1244 GLU   A CA  1 
ATOM   9985  C  C   . GLU   A 1 1246 ? -24.14200  -0.46800  9.50400   1.000 67.59642  ?  1244 GLU   A C   1 
ATOM   9986  O  O   . GLU   A 1 1246 ? -24.02700  -1.30800  10.39800  1.000 72.72206  ?  1244 GLU   A O   1 
ATOM   9987  C  CB  . GLU   A 1 1246 ? -26.38700  -1.43000  8.91700   1.000 72.36248  ?  1244 GLU   A CB  1 
ATOM   9988  C  CG  . GLU   A 1 1246 ? -27.87300  -1.12200  8.78900   1.000 70.28619  ?  1244 GLU   A CG  1 
ATOM   9989  C  CD  . GLU   A 1 1246 ? -28.43200  -0.40600  10.00800  1.000 80.45786  ?  1244 GLU   A CD  1 
ATOM   9990  O  OE1 . GLU   A 1 1246 ? -27.93600  -0.65100  11.12800  1.000 88.43857  ?  1244 GLU   A OE1 1 
ATOM   9991  O  OE2 . GLU   A 1 1246 ? -29.37300  0.40100   9.84400   1.000 71.55439  -1 1244 GLU   A OE2 1 
ATOM   9992  N  N   . GLN   A 1 1247 ? -23.10900  0.23700   9.05200   1.000 66.48825  ?  1245 GLN   A N   1 
ATOM   9993  C  CA  . GLN   A 1 1247 ? -21.76300  0.09100   9.58100   1.000 69.08361  ?  1245 GLN   A CA  1 
ATOM   9994  C  C   . GLN   A 1 1247 ? -21.27300  1.42200   10.13800  1.000 52.71480  ?  1245 GLN   A C   1 
ATOM   9995  O  O   . GLN   A 1 1247 ? -21.64000  2.49300   9.64600   1.000 54.59991  ?  1245 GLN   A O   1 
ATOM   9996  C  CB  . GLN   A 1 1247 ? -20.80300  -0.42900  8.50700   1.000 70.92384  ?  1245 GLN   A CB  1 
ATOM   9997  C  CG  . GLN   A 1 1247 ? -21.20600  -1.78400  7.94500   1.000 71.70126  ?  1245 GLN   A CG  1 
ATOM   9998  C  CD  . GLN   A 1 1247 ? -20.26600  -2.26900  6.86100   1.000 99.32446  ?  1245 GLN   A CD  1 
ATOM   9999  O  OE1 . GLN   A 1 1247 ? -19.06000  -2.02700  6.91500   1.000 80.63054  ?  1245 GLN   A OE1 1 
ATOM   10000 N  NE2 . GLN   A 1 1247 ? -20.81600  -2.96100  5.86900   1.000 107.19155 ?  1245 GLN   A NE2 1 
ATOM   10001 N  N   . ARG   A 1 1248 ? -20.43700  1.34300   11.17100  1.000 51.53068  ?  1246 ARG   A N   1 
ATOM   10002 C  CA  . ARG   A 1 1248 ? -20.00700  2.50900   11.93100  1.000 58.08555  ?  1246 ARG   A CA  1 
ATOM   10003 C  C   . ARG   A 1 1248 ? -18.48700  2.62100   11.93900  1.000 59.54414  ?  1246 ARG   A C   1 
ATOM   10004 O  O   . ARG   A 1 1248 ? -17.77700  1.61800   12.06600  1.000 53.44670  ?  1246 ARG   A O   1 
ATOM   10005 C  CB  . ARG   A 1 1248 ? -20.55100  2.43800   13.36200  1.000 41.75185  ?  1246 ARG   A CB  1 
ATOM   10006 C  CG  . ARG   A 1 1248 ? -22.04800  2.18000   13.39400  1.000 73.38971  ?  1246 ARG   A CG  1 
ATOM   10007 C  CD  . ARG   A 1 1248 ? -22.49400  1.42400   14.63000  1.000 96.45010  ?  1246 ARG   A CD  1 
ATOM   10008 N  NE  . ARG   A 1 1248 ? -23.76000  0.73700   14.39400  1.000 91.71638  ?  1246 ARG   A NE  1 
ATOM   10009 C  CZ  . ARG   A 1 1248 ? -24.94500  1.33200   14.35600  1.000 103.52011 ?  1246 ARG   A CZ  1 
ATOM   10010 N  NH1 . ARG   A 1 1248 ? -25.07300  2.63400   14.56000  1.000 102.32641 ?  1246 ARG   A NH1 1 
ATOM   10011 N  NH2 . ARG   A 1 1248 ? -26.02900  0.60300   14.10800  1.000 100.74848 ?  1246 ARG   A NH2 1 
ATOM   10012 N  N   . VAL   A 1 1249 ? -17.99800  3.85200   11.79700  1.000 54.99620  ?  1247 VAL   A N   1 
ATOM   10013 C  CA  . VAL   A 1 1249 ? -16.57200  4.16200   11.81700  1.000 45.76176  ?  1247 VAL   A CA  1 
ATOM   10014 C  C   . VAL   A 1 1249 ? -16.30000  5.06600   13.01000  1.000 45.39732  ?  1247 VAL   A C   1 
ATOM   10015 O  O   . VAL   A 1 1249 ? -17.01700  6.05000   13.22500  1.000 61.27455  ?  1247 VAL   A O   1 
ATOM   10016 C  CB  . VAL   A 1 1249 ? -16.11100  4.83800   10.51100  1.000 44.40133  ?  1247 VAL   A CB  1 
ATOM   10017 C  CG1 . VAL   A 1 1249 ? -14.60600  5.05300   10.52800  1.000 40.59874  ?  1247 VAL   A CG1 1 
ATOM   10018 C  CG2 . VAL   A 1 1249 ? -16.52400  4.01200   9.29900   1.000 33.40874  ?  1247 VAL   A CG2 1 
ATOM   10019 N  N   . THR   A 1 1250 ? -15.27300  4.73500   13.78100  1.000 47.84035  ?  1248 THR   A N   1 
ATOM   10020 C  CA  . THR   A 1 1250 ? -14.93400  5.54200   14.93900  1.000 63.05024  ?  1248 THR   A CA  1 
ATOM   10021 C  C   . THR   A 1 1250 ? -13.90100  6.60000   14.56200  1.000 63.94509  ?  1248 THR   A C   1 
ATOM   10022 O  O   . THR   A 1 1250 ? -13.27800  6.54400   13.49700  1.000 56.84962  ?  1248 THR   A O   1 
ATOM   10023 C  CB  . THR   A 1 1250 ? -14.42500  4.66100   16.08400  1.000 59.96676  ?  1248 THR   A CB  1 
ATOM   10024 O  OG1 . THR   A 1 1250 ? -14.61800  5.34300   17.32700  1.000 72.17863  ?  1248 THR   A OG1 1 
ATOM   10025 C  CG2 . THR   A 1 1250 ? -12.95600  4.33600   15.91900  1.000 67.93226  ?  1248 THR   A CG2 1 
ATOM   10026 N  N   . TYR   A 1 1251 ? -13.75100  7.59400   15.44300  1.000 54.45441  ?  1249 TYR   A N   1 
ATOM   10027 C  CA  . TYR   A 1 1251 ? -12.79800  8.67200   15.19200  1.000 67.74192  ?  1249 TYR   A CA  1 
ATOM   10028 C  C   . TYR   A 1 1251 ? -11.39500  8.12500   14.97200  1.000 68.28611  ?  1249 TYR   A C   1 
ATOM   10029 O  O   . TYR   A 1 1251 ? -10.68400  8.56300   14.05900  1.000 64.06677  ?  1249 TYR   A O   1 
ATOM   10030 C  CB  . TYR   A 1 1251 ? -12.80500  9.66300   16.35600  1.000 72.28111  ?  1249 TYR   A CB  1 
ATOM   10031 C  CG  . TYR   A 1 1251 ? -13.92800  10.67600  16.30900  1.000 74.09109  ?  1249 TYR   A CG  1 
ATOM   10032 C  CD1 . TYR   A 1 1251 ? -15.16800  10.39000  16.86400  1.000 68.05643  ?  1249 TYR   A CD1 1 
ATOM   10033 C  CD2 . TYR   A 1 1251 ? -13.74500  11.91900  15.71700  1.000 67.98345  ?  1249 TYR   A CD2 1 
ATOM   10034 C  CE1 . TYR   A 1 1251 ? -16.19800  11.31200  16.82700  1.000 73.35918  ?  1249 TYR   A CE1 1 
ATOM   10035 C  CE2 . TYR   A 1 1251 ? -14.77000  12.84900  15.67600  1.000 75.66843  ?  1249 TYR   A CE2 1 
ATOM   10036 C  CZ  . TYR   A 1 1251 ? -15.99400  12.53900  16.23300  1.000 78.02440  ?  1249 TYR   A CZ  1 
ATOM   10037 O  OH  . TYR   A 1 1251 ? -17.01900  13.45800  16.19600  1.000 62.88115  ?  1249 TYR   A OH  1 
ATOM   10038 N  N   . ARG   A 1 1252 ? -10.98400  7.15900   15.79500  1.000 61.99780  ?  1250 ARG   A N   1 
ATOM   10039 C  CA  . ARG   A 1 1252 ? -9.65600   6.57200   15.65500  1.000 63.57400  ?  1250 ARG   A CA  1 
ATOM   10040 C  C   . ARG   A 1 1252 ? -9.52300   5.82500   14.33300  1.000 60.05949  ?  1250 ARG   A C   1 
ATOM   10041 O  O   . ARG   A 1 1252 ? -8.54200   6.00600   13.60200  1.000 52.90450  ?  1250 ARG   A O   1 
ATOM   10042 C  CB  . ARG   A 1 1252 ? -9.37300   5.64200   16.83600  1.000 63.59363  ?  1250 ARG   A CB  1 
ATOM   10043 C  CG  . ARG   A 1 1252 ? -8.02100   5.85000   17.49400  1.000 74.50043  ?  1250 ARG   A CG  1 
ATOM   10044 C  CD  . ARG   A 1 1252 ? -7.42700   4.52200   17.93400  1.000 75.06119  ?  1250 ARG   A CD  1 
ATOM   10045 N  NE  . ARG   A 1 1252 ? -7.14100   3.65900   16.79400  1.000 90.32931  ?  1250 ARG   A NE  1 
ATOM   10046 C  CZ  . ARG   A 1 1252 ? -7.82100   2.56000   16.49600  1.000 101.24276 ?  1250 ARG   A CZ  1 
ATOM   10047 N  NH1 . ARG   A 1 1252 ? -8.83600   2.15300   17.24100  1.000 100.51025 ?  1250 ARG   A NH1 1 
ATOM   10048 N  NH2 . ARG   A 1 1252 ? -7.47900   1.85500   15.42200  1.000 100.58150 ?  1250 ARG   A NH2 1 
ATOM   10049 N  N   . GLU   A 1 1253 ? -10.50500  4.97800   14.01200  1.000 57.73571  ?  1251 GLU   A N   1 
ATOM   10050 C  CA  . GLU   A 1 1253 ? -10.47400  4.23600   12.75400  1.000 60.19503  ?  1251 GLU   A CA  1 
ATOM   10051 C  C   . GLU   A 1 1253 ? -10.44400  5.18000   11.56300  1.000 56.13896  ?  1251 GLU   A C   1 
ATOM   10052 O  O   . GLU   A 1 1253 ? -9.68300   4.97200   10.61000  1.000 58.04097  ?  1251 GLU   A O   1 
ATOM   10053 C  CB  . GLU   A 1 1253 ? -11.68500  3.30900   12.65300  1.000 53.93118  ?  1251 GLU   A CB  1 
ATOM   10054 C  CG  . GLU   A 1 1253 ? -11.63400  2.08600   13.54400  1.000 80.91469  ?  1251 GLU   A CG  1 
ATOM   10055 C  CD  . GLU   A 1 1253 ? -12.99600  1.43900   13.69700  1.000 79.40159  ?  1251 GLU   A CD  1 
ATOM   10056 O  OE1 . GLU   A 1 1253 ? -13.88100  1.72000   12.86100  1.000 76.61686  ?  1251 GLU   A OE1 1 
ATOM   10057 O  OE2 . GLU   A 1 1253 ? -13.18600  0.65400   14.64900  1.000 78.53859  -1 1251 GLU   A OE2 1 
ATOM   10058 N  N   . LEU   A 1 1254 ? -11.28900  6.21200   11.59200  1.000 65.12769  ?  1252 LEU   A N   1 
ATOM   10059 C  CA  . LEU   A 1 1254 ? -11.28700  7.23200   10.55400  1.000 58.24209  ?  1252 LEU   A CA  1 
ATOM   10060 C  C   . LEU   A 1 1254 ? -9.89100   7.82500   10.44500  1.000 59.35703  ?  1252 LEU   A C   1 
ATOM   10061 O  O   . LEU   A 1 1254 ? -9.16700   7.52900   9.49000   1.000 68.45925  ?  1252 LEU   A O   1 
ATOM   10062 C  CB  . LEU   A 1 1254 ? -12.32300  8.31700   10.85400  1.000 49.18450  ?  1252 LEU   A CB  1 
ATOM   10063 C  CG  . LEU   A 1 1254 ? -12.46100  9.41600   9.79700   1.000 50.23536  ?  1252 LEU   A CG  1 
ATOM   10064 C  CD1 . LEU   A 1 1254 ? -12.62100  8.82200   8.39800   1.000 34.61154  ?  1252 LEU   A CD1 1 
ATOM   10065 C  CD2 . LEU   A 1 1254 ? -13.61800  10.34900  10.13800  1.000 41.94853  ?  1252 LEU   A CD2 1 
ATOM   10066 N  N   . ASN   A 1 1255 ? -9.49900   8.60900   11.45500  1.000 45.85560  ?  1253 ASN   A N   1 
ATOM   10067 C  CA  . ASN   A 1 1255 ? -8.20900   9.29700   11.47100  1.000 68.01460  ?  1253 ASN   A CA  1 
ATOM   10068 C  C   . ASN   A 1 1255 ? -7.05500   8.43100   10.96800  1.000 66.97490  ?  1253 ASN   A C   1 
ATOM   10069 O  O   . ASN   A 1 1255 ? -6.24900   8.87400   10.14200  1.000 55.73398  ?  1253 ASN   A O   1 
ATOM   10070 C  CB  . ASN   A 1 1255 ? -7.92500   9.78700   12.89400  1.000 52.25260  ?  1253 ASN   A CB  1 
ATOM   10071 C  CG  . ASN   A 1 1255 ? -6.91800   10.91300  12.93200  1.000 71.89959  ?  1253 ASN   A CG  1 
ATOM   10072 O  OD1 . ASN   A 1 1255 ? -6.54600   11.46500  11.89600  1.000 75.90430  ?  1253 ASN   A OD1 1 
ATOM   10073 N  ND2 . ASN   A 1 1255 ? -6.47100   11.26500  14.13200  1.000 73.94471  ?  1253 ASN   A ND2 1 
ATOM   10074 N  N   . GLU   A 1 1256 ? -6.97400   7.18400   11.44200  1.000 65.01342  ?  1254 GLU   A N   1 
ATOM   10075 C  CA  . GLU   A 1 1256 ? -5.87400   6.30400   11.05300  1.000 52.09251  ?  1254 GLU   A CA  1 
ATOM   10076 C  C   . GLU   A 1 1256 ? -5.89700   6.01100   9.55800   1.000 61.87103  ?  1254 GLU   A C   1 
ATOM   10077 O  O   . GLU   A 1 1256 ? -4.85700   6.05300   8.88900   1.000 64.02729  ?  1254 GLU   A O   1 
ATOM   10078 C  CB  . GLU   A 1 1256 ? -5.93500   5.00400   11.85200  1.000 63.55999  ?  1254 GLU   A CB  1 
ATOM   10079 C  CG  . GLU   A 1 1256 ? -5.43900   5.12400   13.28000  1.000 72.00297  ?  1254 GLU   A CG  1 
ATOM   10080 C  CD  . GLU   A 1 1256 ? -5.38700   3.78600   13.98900  1.000 84.50363  ?  1254 GLU   A CD  1 
ATOM   10081 O  OE1 . GLU   A 1 1256 ? -5.55300   2.74700   13.31400  1.000 72.19620  ?  1254 GLU   A OE1 1 
ATOM   10082 O  OE2 . GLU   A 1 1256 ? -5.18500   3.77400   15.22200  1.000 95.43961  -1 1254 GLU   A OE2 1 
ATOM   10083 N  N   . ARG   A 1 1257 ? -7.07500   5.69200   9.01700   1.000 59.01131  ?  1255 ARG   A N   1 
ATOM   10084 C  CA  . ARG   A 1 1257 ? -7.17700   5.46000   7.57900   1.000 71.94264  ?  1255 ARG   A CA  1 
ATOM   10085 C  C   . ARG   A 1 1257 ? -6.90000   6.73800   6.79700   1.000 70.15530  ?  1255 ARG   A C   1 
ATOM   10086 O  O   . ARG   A 1 1257 ? -6.31000   6.69100   5.71100   1.000 65.16987  ?  1255 ARG   A O   1 
ATOM   10087 C  CB  . ARG   A 1 1257 ? -8.55500   4.90300   7.22600   1.000 61.28108  ?  1255 ARG   A CB  1 
ATOM   10088 C  CG  . ARG   A 1 1257 ? -8.63400   4.34600   5.81400   1.000 75.66671  ?  1255 ARG   A CG  1 
ATOM   10089 C  CD  . ARG   A 1 1257 ? -8.63000   2.82800   5.82900   1.000 92.34860  ?  1255 ARG   A CD  1 
ATOM   10090 N  NE  . ARG   A 1 1257 ? -8.04400   2.26100   4.61900   1.000 86.31851  ?  1255 ARG   A NE  1 
ATOM   10091 C  CZ  . ARG   A 1 1257 ? -6.98700   1.46000   4.60700   1.000 89.67174  ?  1255 ARG   A CZ  1 
ATOM   10092 N  NH1 . ARG   A 1 1257 ? -6.35800   1.12900   5.72400   1.000 78.09924  ?  1255 ARG   A NH1 1 
ATOM   10093 N  NH2 . ARG   A 1 1257 ? -6.55500   0.97300   3.44700   1.000 83.41428  ?  1255 ARG   A NH2 1 
ATOM   10094 N  N   . VAL   A 1 1258 ? -7.33200   7.88500   7.32800   1.000 70.64963  ?  1256 VAL   A N   1 
ATOM   10095 C  CA  . VAL   A 1 1258 ? -6.97000   9.17100   6.73500   1.000 80.07073  ?  1256 VAL   A CA  1 
ATOM   10096 C  C   . VAL   A 1 1258 ? -5.45700   9.34100   6.71400   1.000 68.04692  ?  1256 VAL   A C   1 
ATOM   10097 O  O   . VAL   A 1 1258 ? -4.86900   9.70000   5.68600   1.000 68.19783  ?  1256 VAL   A O   1 
ATOM   10098 C  CB  . VAL   A 1 1258 ? -7.65600   10.32600  7.48600   1.000 76.71685  ?  1256 VAL   A CB  1 
ATOM   10099 C  CG1 . VAL   A 1 1258 ? -7.66900   11.54200  6.62900   1.000 64.01513  ?  1256 VAL   A CG1 1 
ATOM   10100 C  CG2 . VAL   A 1 1258 ? -9.09300   9.97000   7.80100   1.000 68.26555  ?  1256 VAL   A CG2 1 
ATOM   10101 N  N   . ASN   A 1 1259 ? -4.80700   9.08600   7.85400   1.000 57.83034  ?  1257 ASN   A N   1 
ATOM   10102 C  CA  . ASN   A 1 1259 ? -3.36000   9.25100   7.95200   1.000 55.93422  ?  1257 ASN   A CA  1 
ATOM   10103 C  C   . ASN   A 1 1259 ? -2.63100   8.44300   6.88700   1.000 59.34799  ?  1257 ASN   A C   1 
ATOM   10104 O  O   . ASN   A 1 1259 ? -1.67300   8.93200   6.27700   1.000 64.75496  ?  1257 ASN   A O   1 
ATOM   10105 C  CB  . ASN   A 1 1259 ? -2.88300   8.84400   9.34600   1.000 46.25567  ?  1257 ASN   A CB  1 
ATOM   10106 C  CG  . ASN   A 1 1259 ? -3.41700   9.75300   10.43600  1.000 61.31529  ?  1257 ASN   A CG  1 
ATOM   10107 O  OD1 . ASN   A 1 1259 ? -3.84500   10.87700  10.17200  1.000 61.16896  ?  1257 ASN   A OD1 1 
ATOM   10108 N  ND2 . ASN   A 1 1259 ? -3.39700   9.26600   11.67100  1.000 60.27612  ?  1257 ASN   A ND2 1 
ATOM   10109 N  N   . GLN   A 1 1260 ? -3.07400   7.20700   6.64400   1.000 61.19591  ?  1258 GLN   A N   1 
ATOM   10110 C  CA  . GLN   A 1 1260 ? -2.41300   6.35200   5.66200   1.000 59.48505  ?  1258 GLN   A CA  1 
ATOM   10111 C  C   . GLN   A 1 1260 ? -2.47100   6.96800   4.27000   1.000 62.27559  ?  1258 GLN   A C   1 
ATOM   10112 O  O   . GLN   A 1 1260 ? -1.43600   7.22100   3.64400   1.000 79.71068  ?  1258 GLN   A O   1 
ATOM   10113 C  CB  . GLN   A 1 1260 ? -3.05600   4.96700   5.65300   1.000 70.13793  ?  1258 GLN   A CB  1 
ATOM   10114 C  CG  . GLN   A 1 1260 ? -2.79900   4.15300   6.90000   1.000 82.76576  ?  1258 GLN   A CG  1 
ATOM   10115 C  CD  . GLN   A 1 1260 ? -3.74300   2.97600   7.01100   1.000 87.23729  ?  1258 GLN   A CD  1 
ATOM   10116 O  OE1 . GLN   A 1 1260 ? -4.18700   2.42700   6.00200   1.000 79.06008  ?  1258 GLN   A OE1 1 
ATOM   10117 N  NE2 . GLN   A 1 1260 ? -4.06100   2.58400   8.23800   1.000 82.16952  ?  1258 GLN   A NE2 1 
ATOM   10118 N  N   . LEU   A 1 1261 ? -3.68500   7.20700   3.76500   1.000 76.79765  ?  1259 LEU   A N   1 
ATOM   10119 C  CA  . LEU   A 1 1261 ? -3.82800   7.81800   2.44800   1.000 69.16564  ?  1259 LEU   A CA  1 
ATOM   10120 C  C   . LEU   A 1 1261 ? -3.15300   9.18100   2.39000   1.000 71.20024  ?  1259 LEU   A C   1 
ATOM   10121 O  O   . LEU   A 1 1261 ? -2.68600   9.59600   1.32500   1.000 67.31941  ?  1259 LEU   A O   1 
ATOM   10122 C  CB  . LEU   A 1 1261 ? -5.30700   7.93300   2.07700   1.000 61.07604  ?  1259 LEU   A CB  1 
ATOM   10123 C  CG  . LEU   A 1 1261 ? -5.62200   8.39600   0.65300   1.000 63.46465  ?  1259 LEU   A CG  1 
ATOM   10124 C  CD1 . LEU   A 1 1261 ? -4.91800   7.51700   -0.36800  1.000 55.75106  ?  1259 LEU   A CD1 1 
ATOM   10125 C  CD2 . LEU   A 1 1261 ? -7.12500   8.40300   0.41200   1.000 64.41121  ?  1259 LEU   A CD2 1 
ATOM   10126 N  N   . ALA   A 1 1262 ? -3.07900   9.88300   3.52300   1.000 64.50438  ?  1260 ALA   A N   1 
ATOM   10127 C  CA  . ALA   A 1 1262 ? -2.34400   11.14300  3.56100   1.000 68.70101  ?  1260 ALA   A CA  1 
ATOM   10128 C  C   . ALA   A 1 1262 ? -0.85600   10.91200  3.32700   1.000 76.40658  ?  1260 ALA   A C   1 
ATOM   10129 O  O   . ALA   A 1 1262 ? -0.25800   11.52200  2.43200   1.000 67.00978  ?  1260 ALA   A O   1 
ATOM   10130 C  CB  . ALA   A 1 1262 ? -2.57700   11.85000  4.89700   1.000 53.28364  ?  1260 ALA   A CB  1 
ATOM   10131 N  N   . HIS   A 1 1263 ? -0.24500   10.02700  4.12400   1.000 74.22621  ?  1261 HIS   A N   1 
ATOM   10132 C  CA  . HIS   A 1 1263 ? 1.16800    9.70000   3.94400   1.000 53.90294  ?  1261 HIS   A CA  1 
ATOM   10133 C  C   . HIS   A 1 1263 ? 1.44600    9.22900   2.52400   1.000 53.32473  ?  1261 HIS   A C   1 
ATOM   10134 O  O   . HIS   A 1 1263 ? 2.50000    9.53400   1.95400   1.000 79.83552  ?  1261 HIS   A O   1 
ATOM   10135 C  CB  . HIS   A 1 1263 ? 1.59400    8.63200   4.95200   1.000 35.68838  ?  1261 HIS   A CB  1 
ATOM   10136 C  CG  . HIS   A 1 1263 ? 1.71900    9.13700   6.35500   1.000 46.99987  ?  1261 HIS   A CG  1 
ATOM   10137 N  ND1 . HIS   A 1 1263 ? 2.61500    10.12100  6.71500   1.000 75.93389  ?  1261 HIS   A ND1 1 
ATOM   10138 C  CD2 . HIS   A 1 1263 ? 1.06800    8.78800   7.49000   1.000 45.28135  ?  1261 HIS   A CD2 1 
ATOM   10139 C  CE1 . HIS   A 1 1263 ? 2.50600    10.36100  8.01000   1.000 87.34015  ?  1261 HIS   A CE1 1 
ATOM   10140 N  NE2 . HIS   A 1 1263 ? 1.57400    9.56500   8.50400   1.000 66.65526  ?  1261 HIS   A NE2 1 
ATOM   10141 N  N   . THR   A 1 1264 ? 0.50900    8.48300   1.93800   1.000 45.69334  ?  1262 THR   A N   1 
ATOM   10142 C  CA  . THR   A 1 1264 ? 0.61900    8.13100   0.52700   1.000 63.49871  ?  1262 THR   A CA  1 
ATOM   10143 C  C   . THR   A 1 1264 ? 0.54300    9.37300   -0.35200  1.000 70.87215  ?  1262 THR   A C   1 
ATOM   10144 O  O   . THR   A 1 1264 ? 1.37300    9.56700   -1.24700  1.000 73.62485  ?  1262 THR   A O   1 
ATOM   10145 C  CB  . THR   A 1 1264 ? -0.48100   7.13800   0.14300   1.000 70.85016  ?  1262 THR   A CB  1 
ATOM   10146 O  OG1 . THR   A 1 1264 ? -0.68300   6.20100   1.20900   1.000 65.07588  ?  1262 THR   A OG1 1 
ATOM   10147 C  CG2 . THR   A 1 1264 ? -0.10300   6.39200   -1.12500  1.000 60.61338  ?  1262 THR   A CG2 1 
ATOM   10148 N  N   . LEU   A 1 1265 ? -0.45300   10.23200  -0.10600  1.000 79.88992  ?  1263 LEU   A N   1 
ATOM   10149 C  CA  . LEU   A 1 1265 ? -0.61100   11.44600  -0.90200  1.000 87.43849  ?  1263 LEU   A CA  1 
ATOM   10150 C  C   . LEU   A 1 1265 ? 0.58500    12.37800  -0.76300  1.000 85.32180  ?  1263 LEU   A C   1 
ATOM   10151 O  O   . LEU   A 1 1265 ? 0.94400    13.07200  -1.72200  1.000 83.20630  ?  1263 LEU   A O   1 
ATOM   10152 C  CB  . LEU   A 1 1265 ? -1.89500   12.17900  -0.50100  1.000 70.75125  ?  1263 LEU   A CB  1 
ATOM   10153 C  CG  . LEU   A 1 1265 ? -3.23000   11.62100  -1.00300  1.000 70.28125  ?  1263 LEU   A CG  1 
ATOM   10154 C  CD1 . LEU   A 1 1265 ? -4.26500   12.73000  -1.16300  1.000 83.12752  ?  1263 LEU   A CD1 1 
ATOM   10155 C  CD2 . LEU   A 1 1265 ? -3.04100   10.87200  -2.31400  1.000 74.88566  ?  1263 LEU   A CD2 1 
ATOM   10156 N  N   . ARG   A 1 1266 ? 1.21100    12.40900  0.41500   1.000 71.84620  ?  1264 ARG   A N   1 
ATOM   10157 C  CA  . ARG   A 1 1266 ? 2.31400    13.33600  0.65400   1.000 66.43486  ?  1264 ARG   A CA  1 
ATOM   10158 C  C   . ARG   A 1 1266 ? 3.49100    13.03800  -0.26800  1.000 82.68254  ?  1264 ARG   A C   1 
ATOM   10159 O  O   . ARG   A 1 1266 ? 3.96000    13.91500  -1.00300  1.000 88.16572  ?  1264 ARG   A O   1 
ATOM   10160 C  CB  . ARG   A 1 1266 ? 2.74200    13.26900  2.12000   1.000 50.87891  ?  1264 ARG   A CB  1 
ATOM   10161 C  CG  . ARG   A 1 1266 ? 1.74200    13.88800  3.07900   1.000 60.18342  ?  1264 ARG   A CG  1 
ATOM   10162 C  CD  . ARG   A 1 1266 ? 2.17400    13.69200  4.51800   1.000 65.37429  ?  1264 ARG   A CD  1 
ATOM   10163 N  NE  . ARG   A 1 1266 ? 3.37000    14.46800  4.82000   1.000 85.98867  ?  1264 ARG   A NE  1 
ATOM   10164 C  CZ  . ARG   A 1 1266 ? 3.37800    15.59700  5.51400   1.000 85.11634  ?  1264 ARG   A CZ  1 
ATOM   10165 N  NH1 . ARG   A 1 1266 ? 2.26600    16.10400  6.02400   1.000 80.74652  ?  1264 ARG   A NH1 1 
ATOM   10166 N  NH2 . ARG   A 1 1266 ? 4.53000    16.23400  5.70100   1.000 68.90506  ?  1264 ARG   A NH2 1 
ATOM   10167 N  N   . GLU   A 1 1267 ? 3.98100    11.79600  -0.24300  1.000 68.90626  ?  1265 GLU   A N   1 
ATOM   10168 C  CA  . GLU   A 1 1267 ? 5.07800    11.42100  -1.12700  1.000 89.41976  ?  1265 GLU   A CA  1 
ATOM   10169 C  C   . GLU   A 1 1267 ? 4.67500    11.46400  -2.59300  1.000 94.38626  ?  1265 GLU   A C   1 
ATOM   10170 O  O   . GLU   A 1 1267 ? 5.54800    11.50600  -3.46500  1.000 116.23990 ?  1265 GLU   A O   1 
ATOM   10171 C  CB  . GLU   A 1 1267 ? 5.59600    10.02600  -0.77500  1.000 103.45753 ?  1265 GLU   A CB  1 
ATOM   10172 C  CG  . GLU   A 1 1267 ? 4.58300    8.90600   -0.97400  1.000 115.90666 ?  1265 GLU   A CG  1 
ATOM   10173 C  CD  . GLU   A 1 1267 ? 4.79100    8.14500   -2.27600  1.000 120.64569 ?  1265 GLU   A CD  1 
ATOM   10174 O  OE1 . GLU   A 1 1267 ? 5.54700    8.63200   -3.14300  1.000 125.34427 ?  1265 GLU   A OE1 1 
ATOM   10175 O  OE2 . GLU   A 1 1267 ? 4.20100    7.05400   -2.42900  1.000 109.46846 -1 1265 GLU   A OE2 1 
ATOM   10176 N  N   . LYS   A 1 1268 ? 3.37800    11.45900  -2.88400  1.000 81.53587  ?  1266 LYS   A N   1 
ATOM   10177 C  CA  . LYS   A 1 1268 ? 2.91100    11.59200  -4.25600  1.000 82.94158  ?  1266 LYS   A CA  1 
ATOM   10178 C  C   . LYS   A 1 1268 ? 3.15100    12.98200  -4.83400  1.000 85.54275  ?  1266 LYS   A C   1 
ATOM   10179 O  O   . LYS   A 1 1268 ? 2.78500    13.22400  -5.99200  1.000 69.67344  ?  1266 LYS   A O   1 
ATOM   10180 C  CB  . LYS   A 1 1268 ? 1.42400    11.24700  -4.32200  1.000 87.92400  ?  1266 LYS   A CB  1 
ATOM   10181 C  CG  . LYS   A 1 1268 ? 1.11800    9.74600   -4.36600  1.000 85.28189  ?  1266 LYS   A CG  1 
ATOM   10182 C  CD  . LYS   A 1 1268 ? 1.51000    9.09200   -5.68800  1.000 82.99254  ?  1266 LYS   A CD  1 
ATOM   10183 C  CE  . LYS   A 1 1268 ? 1.32500    10.05300  -6.84700  1.000 81.25513  ?  1266 LYS   A CE  1 
ATOM   10184 N  NZ  . LYS   A 1 1268 ? -0.10100   10.12300  -7.25000  1.000 91.21362  ?  1266 LYS   A NZ  1 
ATOM   10185 N  N   . GLY   A 1 1269 ? 3.74900    13.89100  -4.06600  1.000 71.02380  ?  1267 GLY   A N   1 
ATOM   10186 C  CA  . GLY   A 1 1269 ? 4.00700    15.23900  -4.53000  1.000 85.13715  ?  1267 GLY   A CA  1 
ATOM   10187 C  C   . GLY   A 1 1269 ? 2.89200    16.20800  -4.19500  1.000 96.44876  ?  1267 GLY   A C   1 
ATOM   10188 O  O   . GLY   A 1 1269 ? 2.44600    16.97200  -5.05700  1.000 81.13229  ?  1267 GLY   A O   1 
ATOM   10189 N  N   . VAL   A 1 1270 ? 2.43200    16.19000  -2.94700  1.000 91.44616  ?  1268 VAL   A N   1 
ATOM   10190 C  CA  . VAL   A 1 1270 ? 1.34800    17.05400  -2.49400  1.000 86.85841  ?  1268 VAL   A CA  1 
ATOM   10191 C  C   . VAL   A 1 1270 ? 1.93000    18.06800  -1.52000  1.000 87.14235  ?  1268 VAL   A C   1 
ATOM   10192 O  O   . VAL   A 1 1270 ? 2.46900    17.70000  -0.46700  1.000 66.73877  ?  1268 VAL   A O   1 
ATOM   10193 C  CB  . VAL   A 1 1270 ? 0.20600    16.25200  -1.85200  1.000 76.73278  ?  1268 VAL   A CB  1 
ATOM   10194 C  CG1 . VAL   A 1 1270 ? -0.57000   17.11700  -0.86500  1.000 73.81054  ?  1268 VAL   A CG1 1 
ATOM   10195 C  CG2 . VAL   A 1 1270 ? -0.71700   15.70600  -2.92500  1.000 58.70562  ?  1268 VAL   A CG2 1 
ATOM   10196 N  N   . GLN   A 1 1271 ? 1.83500    19.33600  -1.88400  1.000 96.08686  ?  1269 GLN   A N   1 
ATOM   10197 C  CA  . GLN   A 1 1271 ? 2.25900    20.46600  -1.07700  1.000 87.37093  ?  1269 GLN   A CA  1 
ATOM   10198 C  C   . GLN   A 1 1271 ? 1.11200    21.46200  -1.02200  1.000 79.16863  ?  1269 GLN   A C   1 
ATOM   10199 O  O   . GLN   A 1 1271 ? 0.20400    21.41500  -1.86000  1.000 70.96707  ?  1269 GLN   A O   1 
ATOM   10200 C  CB  . GLN   A 1 1271 ? 3.51900    21.12000  -1.66600  1.000 85.54220  ?  1269 GLN   A CB  1 
ATOM   10201 C  CG  . GLN   A 1 1271 ? 4.53200    20.11700  -2.20800  1.000 81.96616  ?  1269 GLN   A CG  1 
ATOM   10202 C  CD  . GLN   A 1 1271 ? 5.22900    20.60500  -3.46200  1.000 95.90609  ?  1269 GLN   A CD  1 
ATOM   10203 O  OE1 . GLN   A 1 1271 ? 5.94100    21.60900  -3.44100  1.000 87.85367  ?  1269 GLN   A OE1 1 
ATOM   10204 N  NE2 . GLN   A 1 1271 ? 5.02700    19.89300  -4.56600  1.000 90.34495  ?  1269 GLN   A NE2 1 
ATOM   10205 N  N   . PRO   A 1 1272 ? 1.10300    22.36000  -0.01600  1.000 63.99189  ?  1270 PRO   A N   1 
ATOM   10206 C  CA  . PRO   A 1 1272 ? 0.02100    23.35100  0.11100   1.000 61.48617  ?  1270 PRO   A CA  1 
ATOM   10207 C  C   . PRO   A 1 1272 ? -0.46200   23.96400  -1.19800  1.000 63.00140  ?  1270 PRO   A C   1 
ATOM   10208 O  O   . PRO   A 1 1272 ? 0.33400    24.25400  -2.09800  1.000 51.25926  ?  1270 PRO   A O   1 
ATOM   10209 C  CB  . PRO   A 1 1272 ? 0.64700    24.42200  1.01500   1.000 50.66644  ?  1270 PRO   A CB  1 
ATOM   10210 C  CG  . PRO   A 1 1272 ? 1.81900    23.74000  1.71100   1.000 61.94760  ?  1270 PRO   A CG  1 
ATOM   10211 C  CD  . PRO   A 1 1272 ? 1.94700    22.33700  1.18800   1.000 60.55031  ?  1270 PRO   A CD  1 
ATOM   10212 N  N   . ASP   A 1 1273 ? -1.78000   24.14800  -1.30000  1.000 62.27075  ?  1271 ASP   A N   1 
ATOM   10213 C  CA  . ASP   A 1 1273 ? -2.45300   24.73800  -2.45800  1.000 66.34727  ?  1271 ASP   A CA  1 
ATOM   10214 C  C   . ASP   A 1 1273 ? -2.29500   23.89900  -3.72400  1.000 71.25119  ?  1271 ASP   A C   1 
ATOM   10215 O  O   . ASP   A 1 1273 ? -2.39300   24.42800  -4.83800  1.000 64.76242  ?  1271 ASP   A O   1 
ATOM   10216 C  CB  . ASP   A 1 1273 ? -1.98500   26.17900  -2.71100  1.000 68.09882  ?  1271 ASP   A CB  1 
ATOM   10217 C  CG  . ASP   A 1 1273 ? -2.35700   27.12200  -1.57700  1.000 62.60942  ?  1271 ASP   A CG  1 
ATOM   10218 O  OD1 . ASP   A 1 1273 ? -3.55000   27.47300  -1.45900  1.000 75.81602  ?  1271 ASP   A OD1 1 
ATOM   10219 O  OD2 . ASP   A 1 1273 ? -1.46000   27.51800  -0.80400  1.000 64.64107  -1 1271 ASP   A OD2 1 
ATOM   10220 N  N   . ASP   A 1 1274 ? -2.05900   22.59800  -3.58100  1.000 75.18480  ?  1272 ASP   A N   1 
ATOM   10221 C  CA  . ASP   A 1 1274 ? -2.09700   21.68400  -4.71200  1.000 77.35928  ?  1272 ASP   A CA  1 
ATOM   10222 C  C   . ASP   A 1 1274 ? -3.49500   21.09300  -4.84800  1.000 70.87827  ?  1272 ASP   A C   1 
ATOM   10223 O  O   . ASP   A 1 1274 ? -4.20500   20.88900  -3.86100  1.000 56.34250  ?  1272 ASP   A O   1 
ATOM   10224 C  CB  . ASP   A 1 1274 ? -1.06700   20.56400  -4.55600  1.000 78.34397  ?  1272 ASP   A CB  1 
ATOM   10225 C  CG  . ASP   A 1 1274 ? 0.25800    20.89100  -5.21900  1.000 95.44440  ?  1272 ASP   A CG  1 
ATOM   10226 O  OD1 . ASP   A 1 1274 ? 0.24000    21.46800  -6.32800  1.000 94.16687  ?  1272 ASP   A OD1 1 
ATOM   10227 O  OD2 . ASP   A 1 1274 ? 1.31500    20.56700  -4.63400  1.000 85.19122  -1 1272 ASP   A OD2 1 
ATOM   10228 N  N   . LEU   A 1 1275 ? -3.88700   20.82300  -6.08600  1.000 68.09317  ?  1273 LEU   A N   1 
ATOM   10229 C  CA  . LEU   A 1 1275 ? -5.22100   20.33000  -6.39600  1.000 70.35345  ?  1273 LEU   A CA  1 
ATOM   10230 C  C   . LEU   A 1 1275 ? -5.14000   18.85100  -6.74300  1.000 83.98946  ?  1273 LEU   A C   1 
ATOM   10231 O  O   . LEU   A 1 1275 ? -4.39100   18.46400  -7.64300  1.000 90.06100  ?  1273 LEU   A O   1 
ATOM   10232 C  CB  . LEU   A 1 1275 ? -5.83000   21.11200  -7.55900  1.000 63.12466  ?  1273 LEU   A CB  1 
ATOM   10233 C  CG  . LEU   A 1 1275 ? -5.82000   22.63400  -7.43200  1.000 68.61018  ?  1273 LEU   A CG  1 
ATOM   10234 C  CD1 . LEU   A 1 1275 ? -6.48900   23.26300  -8.64400  1.000 54.47792  ?  1273 LEU   A CD1 1 
ATOM   10235 C  CD2 . LEU   A 1 1275 ? -6.49800   23.06700  -6.13600  1.000 56.78771  ?  1273 LEU   A CD2 1 
ATOM   10236 N  N   . VAL   A 1 1276 ? -5.90900   18.03100  -6.04100  1.000 84.39428  ?  1274 VAL   A N   1 
ATOM   10237 C  CA  . VAL   A 1 1276 ? -6.10700   16.63200  -6.39600  1.000 75.99431  ?  1274 VAL   A CA  1 
ATOM   10238 C  C   . VAL   A 1 1276 ? -7.59600   16.38600  -6.50000  1.000 61.06287  ?  1274 VAL   A C   1 
ATOM   10239 O  O   . VAL   A 1 1276 ? -8.34800   16.67000  -5.56000  1.000 58.31810  ?  1274 VAL   A O   1 
ATOM   10240 C  CB  . VAL   A 1 1276 ? -5.45100   15.68500  -5.38500  1.000 83.79242  ?  1274 VAL   A CB  1 
ATOM   10241 C  CG1 . VAL   A 1 1276 ? -5.67200   16.22100  -3.98100  1.000 55.84948  ?  1274 VAL   A CG1 1 
ATOM   10242 C  CG2 . VAL   A 1 1276 ? -6.12100   14.30900  -5.44000  1.000 78.63659  ?  1274 VAL   A CG2 1 
ATOM   10243 N  N   . MET   A 1 1277 ? -8.00600   15.84900  -7.63100  1.000 60.85642  ?  1275 MET   A N   1 
ATOM   10244 C  CA  . MET   A 1 1277 ? -9.39300   15.72900  -8.00900  1.000 59.11823  ?  1275 MET   A CA  1 
ATOM   10245 C  C   . MET   A 1 1277 ? -9.95200   14.42500  -7.47000  1.000 79.33676  ?  1275 MET   A C   1 
ATOM   10246 O  O   . MET   A 1 1277 ? -9.23400   13.43200  -7.32700  1.000 75.89162  ?  1275 MET   A O   1 
ATOM   10247 C  CB  . MET   A 1 1277 ? -9.47600   15.79400  -9.52500  1.000 43.76877  ?  1275 MET   A CB  1 
ATOM   10248 C  CG  . MET   A 1 1277 ? -8.30800   16.60900  -10.07500 1.000 63.76646  ?  1275 MET   A CG  1 
ATOM   10249 S  SD  . MET   A 1 1277 ? -8.07300   16.40300  -11.83500 1.000 112.98504 ?  1275 MET   A SD  1 
ATOM   10250 C  CE  . MET   A 1 1277 ? -9.77000   16.53800  -12.31800 1.000 66.73598  ?  1275 MET   A CE  1 
ATOM   10251 N  N   . LEU   A 1 1278 ? -11.23700  14.44700  -7.14900  1.000 75.68486  ?  1276 LEU   A N   1 
ATOM   10252 C  CA  . LEU   A 1 1278 ? -11.91800  13.31100  -6.55600  1.000 51.05879  ?  1276 LEU   A CA  1 
ATOM   10253 C  C   . LEU   A 1 1278 ? -13.00000  12.82200  -7.50600  1.000 63.60004  ?  1276 LEU   A C   1 
ATOM   10254 O  O   . LEU   A 1 1278 ? -13.68800  13.62400  -8.14600  1.000 63.28000  ?  1276 LEU   A O   1 
ATOM   10255 C  CB  . LEU   A 1 1278 ? -12.51900  13.68300  -5.19800  1.000 33.58530  ?  1276 LEU   A CB  1 
ATOM   10256 C  CG  . LEU   A 1 1278 ? -11.67600  13.36600  -3.95900  1.000 48.58483  ?  1276 LEU   A CG  1 
ATOM   10257 C  CD1 . LEU   A 1 1278 ? -10.26300  13.92300  -4.07000  1.000 50.24629  ?  1276 LEU   A CD1 1 
ATOM   10258 C  CD2 . LEU   A 1 1278 ? -12.35700  13.88600  -2.70400  1.000 44.58305  ?  1276 LEU   A CD2 1 
ATOM   10259 N  N   . MET   A 1 1279 ? -13.13100  11.49900  -7.60000  1.000 66.42334  ?  1277 MET   A N   1 
ATOM   10260 C  CA  . MET   A 1 1279 ? -14.14900  10.85200  -8.43300  1.000 66.47025  ?  1277 MET   A CA  1 
ATOM   10261 C  C   . MET   A 1 1279 ? -14.72000  9.69700   -7.61300  1.000 69.51916  ?  1277 MET   A C   1 
ATOM   10262 O  O   . MET   A 1 1279 ? -14.25300  8.56000   -7.72100  1.000 84.82814  ?  1277 MET   A O   1 
ATOM   10263 C  CB  . MET   A 1 1279 ? -13.56300  10.37400  -9.75400  1.000 58.30880  ?  1277 MET   A CB  1 
ATOM   10264 C  CG  . MET   A 1 1279 ? -13.69700  11.36800  -10.88800 1.000 75.84965  ?  1277 MET   A CG  1 
ATOM   10265 S  SD  . MET   A 1 1279 ? -12.98800  10.74600  -12.42100 1.000 95.46083  ?  1277 MET   A SD  1 
ATOM   10266 C  CE  . MET   A 1 1279 ? -14.42400  10.77700  -13.49100 1.000 86.92292  ?  1277 MET   A CE  1 
ATOM   10267 N  N   . ALA   A 1 1280 ? -15.72900  9.99400   -6.79600  1.000 65.72293  ?  1278 ALA   A N   1 
ATOM   10268 C  CA  . ALA   A 1 1280 ? -16.28400  9.00100   -5.88800  1.000 68.28418  ?  1278 ALA   A CA  1 
ATOM   10269 C  C   . ALA   A 1 1280 ? -17.74700  9.30800   -5.60600  1.000 69.34964  ?  1278 ALA   A C   1 
ATOM   10270 O  O   . ALA   A 1 1280 ? -18.17300  10.46600  -5.62700  1.000 72.43500  ?  1278 ALA   A O   1 
ATOM   10271 C  CB  . ALA   A 1 1280 ? -15.50600  8.94900   -4.56800  1.000 41.28822  ?  1278 ALA   A CB  1 
ATOM   10272 N  N   . GLU   A 1 1281 ? -18.51000  8.25300   -5.33800  1.000 66.96042  ?  1279 GLU   A N   1 
ATOM   10273 C  CA  . GLU   A 1 1281 ? -19.87700  8.38400   -4.86400  1.000 52.08484  ?  1279 GLU   A CA  1 
ATOM   10274 C  C   . GLU   A 1 1281 ? -19.90200  8.35100   -3.33900  1.000 49.38445  ?  1279 GLU   A C   1 
ATOM   10275 O  O   . GLU   A 1 1281 ? -18.88500  8.11900   -2.68100  1.000 58.09116  ?  1279 GLU   A O   1 
ATOM   10276 C  CB  . GLU   A 1 1281 ? -20.75700  7.27700   -5.44200  1.000 57.78842  ?  1279 GLU   A CB  1 
ATOM   10277 C  CG  . GLU   A 1 1281 ? -20.96500  7.37000   -6.94100  1.000 72.36867  ?  1279 GLU   A CG  1 
ATOM   10278 C  CD  . GLU   A 1 1281 ? -21.89000  6.29100   -7.45900  1.000 86.92881  ?  1279 GLU   A CD  1 
ATOM   10279 O  OE1 . GLU   A 1 1281 ? -21.61600  5.10000   -7.20300  1.000 93.18822  ?  1279 GLU   A OE1 1 
ATOM   10280 O  OE2 . GLU   A 1 1281 ? -22.89600  6.63400   -8.11700  1.000 99.84760  -1 1279 GLU   A OE2 1 
ATOM   10281 N  N   . ARG   A 1 1282 ? -21.08500  8.59600   -2.77600  1.000 50.42423  ?  1280 ARG   A N   1 
ATOM   10282 C  CA  . ARG   A 1 1282 ? -21.22700  8.65600   -1.32500  1.000 62.43681  ?  1280 ARG   A CA  1 
ATOM   10283 C  C   . ARG   A 1 1282 ? -20.75500  7.35400   -0.69100  1.000 57.91719  ?  1280 ARG   A C   1 
ATOM   10284 O  O   . ARG   A 1 1282 ? -21.23200  6.27100   -1.04500  1.000 70.71462  ?  1280 ARG   A O   1 
ATOM   10285 C  CB  . ARG   A 1 1282 ? -22.67800  8.94600   -0.94600  1.000 62.68330  ?  1280 ARG   A CB  1 
ATOM   10286 C  CG  . ARG   A 1 1282 ? -22.86200  10.26200  -0.21100  1.000 67.99648  ?  1280 ARG   A CG  1 
ATOM   10287 C  CD  . ARG   A 1 1282 ? -24.32100  10.52300  0.11500   1.000 62.38079  ?  1280 ARG   A CD  1 
ATOM   10288 N  NE  . ARG   A 1 1282 ? -24.96200  11.35600  -0.89400  1.000 68.34482  ?  1280 ARG   A NE  1 
ATOM   10289 C  CZ  . ARG   A 1 1282 ? -26.03100  10.99800  -1.59200  1.000 73.99464  ?  1280 ARG   A CZ  1 
ATOM   10290 N  NH1 . ARG   A 1 1282 ? -26.61800  9.82700   -1.40600  1.000 68.15776  ?  1280 ARG   A NH1 1 
ATOM   10291 N  NH2 . ARG   A 1 1282 ? -26.52500  11.83700  -2.49900  1.000 74.40953  ?  1280 ARG   A NH2 1 
ATOM   10292 N  N   . SER   A 1 1283 ? -19.81400  7.46600   0.23900   1.000 58.12130  ?  1281 SER   A N   1 
ATOM   10293 C  CA  . SER   A 1 1283 ? -19.17500  6.31100   0.86100   1.000 61.61046  ?  1281 SER   A CA  1 
ATOM   10294 C  C   . SER   A 1 1283 ? -18.34900  6.81100   2.03900   1.000 59.97872  ?  1281 SER   A C   1 
ATOM   10295 O  O   . SER   A 1 1283 ? -18.28700  8.01300   2.31500   1.000 74.97038  ?  1281 SER   A O   1 
ATOM   10296 C  CB  . SER   A 1 1283 ? -18.30000  5.55500   -0.13900  1.000 65.87190  ?  1281 SER   A CB  1 
ATOM   10297 O  OG  . SER   A 1 1283 ? -17.25000  6.38500   -0.60600  1.000 71.00889  ?  1281 SER   A OG  1 
ATOM   10298 N  N   . VAL   A 1 1284 ? -17.70900  5.87300   2.73600   1.000 47.82036  ?  1282 VAL   A N   1 
ATOM   10299 C  CA  . VAL   A 1 1284 ? -16.71600  6.26500   3.72900   1.000 60.44453  ?  1282 VAL   A CA  1 
ATOM   10300 C  C   . VAL   A 1 1284 ? -15.40600  6.63100   3.04400   1.000 61.44645  ?  1282 VAL   A C   1 
ATOM   10301 O  O   . VAL   A 1 1284 ? -14.62800  7.43700   3.56900   1.000 63.49954  ?  1282 VAL   A O   1 
ATOM   10302 C  CB  . VAL   A 1 1284 ? -16.52100  5.14400   4.76500   1.000 48.37749  ?  1282 VAL   A CB  1 
ATOM   10303 C  CG1 . VAL   A 1 1284 ? -15.62400  5.60800   5.90700   1.000 53.97094  ?  1282 VAL   A CG1 1 
ATOM   10304 C  CG2 . VAL   A 1 1284 ? -17.86500  4.68800   5.29700   1.000 50.58655  ?  1282 VAL   A CG2 1 
ATOM   10305 N  N   . GLU   A 1 1285 ? -15.15200  6.06900   1.86000   1.000 52.39943  ?  1283 GLU   A N   1 
ATOM   10306 C  CA  . GLU   A 1 1285 ? -13.91400  6.36400   1.14600   1.000 68.20709  ?  1283 GLU   A CA  1 
ATOM   10307 C  C   . GLU   A 1 1285 ? -13.86400  7.81800   0.69800   1.000 67.69294  ?  1283 GLU   A C   1 
ATOM   10308 O  O   . GLU   A 1 1285 ? -12.80400  8.45200   0.75500   1.000 63.15636  ?  1283 GLU   A O   1 
ATOM   10309 C  CB  . GLU   A 1 1285 ? -13.76400  5.42700   -0.05200  1.000 66.32609  ?  1283 GLU   A CB  1 
ATOM   10310 C  CG  . GLU   A 1 1285 ? -13.61000  3.96600   0.32200   1.000 71.20164  ?  1283 GLU   A CG  1 
ATOM   10311 C  CD  . GLU   A 1 1285 ? -14.93500  3.23500   0.34900   1.000 93.99786  ?  1283 GLU   A CD  1 
ATOM   10312 O  OE1 . GLU   A 1 1285 ? -15.52300  3.02500   -0.73400  1.000 75.03579  ?  1283 GLU   A OE1 1 
ATOM   10313 O  OE2 . GLU   A 1 1285 ? -15.38900  2.87100   1.45500   1.000 98.62811  -1 1283 GLU   A OE2 1 
ATOM   10314 N  N   . MET   A 1 1286 ? -14.99600  8.36100   0.24000   1.000 59.53011  ?  1284 MET   A N   1 
ATOM   10315 C  CA  . MET   A 1 1286 ? -15.03500  9.77500   -0.11800  1.000 58.38064  ?  1284 MET   A CA  1 
ATOM   10316 C  C   . MET   A 1 1286 ? -14.68300  10.64900  1.07900   1.000 55.48291  ?  1284 MET   A C   1 
ATOM   10317 O  O   . MET   A 1 1286 ? -13.97200  11.65200  0.93900   1.000 65.22011  ?  1284 MET   A O   1 
ATOM   10318 C  CB  . MET   A 1 1286 ? -16.41100  10.14700  -0.66900  1.000 63.47658  ?  1284 MET   A CB  1 
ATOM   10319 C  CG  . MET   A 1 1286 ? -16.66400  11.64800  -0.69400  1.000 72.23816  ?  1284 MET   A CG  1 
ATOM   10320 S  SD  . MET   A 1 1286 ? -18.40500  12.12400  -0.65600  1.000 60.62992  ?  1284 MET   A SD  1 
ATOM   10321 C  CE  . MET   A 1 1286 ? -18.99600  11.45900  -2.21000  1.000 47.79620  ?  1284 MET   A CE  1 
ATOM   10322 N  N   . MET   A 1 1287 ? -15.15300  10.27200  2.27000   1.000 47.92746  ?  1285 MET   A N   1 
ATOM   10323 C  CA  . MET   A 1 1287 ? -14.82700  11.03900  3.46700   1.000 57.82316  ?  1285 MET   A CA  1 
ATOM   10324 C  C   . MET   A 1 1287 ? -13.35600  10.90300  3.83000   1.000 55.55568  ?  1285 MET   A C   1 
ATOM   10325 O  O   . MET   A 1 1287 ? -12.71700  11.88000  4.24100   1.000 64.12664  ?  1285 MET   A O   1 
ATOM   10326 C  CB  . MET   A 1 1287 ? -15.69900  10.58900  4.63600   1.000 51.30148  ?  1285 MET   A CB  1 
ATOM   10327 C  CG  . MET   A 1 1287 ? -17.14600  11.03200  4.54500   1.000 60.58757  ?  1285 MET   A CG  1 
ATOM   10328 S  SD  . MET   A 1 1287 ? -17.28000  12.80600  4.28700   1.000 66.58228  ?  1285 MET   A SD  1 
ATOM   10329 C  CE  . MET   A 1 1287 ? -17.21300  13.37300  5.98400   1.000 48.56678  ?  1285 MET   A CE  1 
ATOM   10330 N  N   . VAL   A 1 1288 ? -12.80900  9.69100   3.71300   1.000 66.06113  ?  1286 VAL   A N   1 
ATOM   10331 C  CA  . VAL   A 1 1288 ? -11.38300  9.49700   3.95600   1.000 66.51821  ?  1286 VAL   A CA  1 
ATOM   10332 C  C   . VAL   A 1 1288 ? -10.56100  10.28400  2.95000   1.000 59.07483  ?  1286 VAL   A C   1 
ATOM   10333 O  O   . VAL   A 1 1288 ? -9.59600   10.96400  3.31600   1.000 55.43508  ?  1286 VAL   A O   1 
ATOM   10334 C  CB  . VAL   A 1 1288 ? -11.01800  8.00400   3.92000   1.000 62.03843  ?  1286 VAL   A CB  1 
ATOM   10335 C  CG1 . VAL   A 1 1288 ? -9.50000   7.83600   3.87900   1.000 77.15923  ?  1286 VAL   A CG1 1 
ATOM   10336 C  CG2 . VAL   A 1 1288 ? -11.60700  7.29300   5.11000   1.000 54.31592  ?  1286 VAL   A CG2 1 
ATOM   10337 N  N   . ALA   A 1 1289 ? -10.90900  10.19300  1.66900   1.000 51.85403  ?  1287 ALA   A N   1 
ATOM   10338 C  CA  . ALA   A 1 1289 ? -10.17700  10.95600  0.66900   1.000 59.45144  ?  1287 ALA   A CA  1 
ATOM   10339 C  C   . ALA   A 1 1289 ? -10.09900  12.43200  1.05800   1.000 75.26533  ?  1287 ALA   A C   1 
ATOM   10340 O  O   . ALA   A 1 1289 ? -9.00600   12.96400  1.29900   1.000 81.85880  ?  1287 ALA   A O   1 
ATOM   10341 C  CB  . ALA   A 1 1289 ? -10.84300  10.76000  -0.68900  1.000 48.95037  ?  1287 ALA   A CB  1 
ATOM   10342 N  N   . ILE   A 1 1290 ? -11.26300  13.08000  1.19000   1.000 70.83915  ?  1288 ILE   A N   1 
ATOM   10343 C  CA  . ILE   A 1 1290 ? -11.32900  14.51700  1.47200   1.000 71.05943  ?  1288 ILE   A CA  1 
ATOM   10344 C  C   . ILE   A 1 1290 ? -10.42100  14.88700  2.64000   1.000 65.41870  ?  1288 ILE   A C   1 
ATOM   10345 O  O   . ILE   A 1 1290 ? -9.53600   15.73900  2.50900   1.000 73.50805  ?  1288 ILE   A O   1 
ATOM   10346 C  CB  . ILE   A 1 1290 ? -12.77700  14.95800  1.74400   1.000 64.18298  ?  1288 ILE   A CB  1 
ATOM   10347 C  CG1 . ILE   A 1 1290 ? -13.59000  14.95300  0.45100   1.000 63.22964  ?  1288 ILE   A CG1 1 
ATOM   10348 C  CG2 . ILE   A 1 1290 ? -12.78900  16.35900  2.35900   1.000 60.13973  ?  1288 ILE   A CG2 1 
ATOM   10349 C  CD1 . ILE   A 1 1290 ? -15.06800  15.15100  0.65800   1.000 51.59263  ?  1288 ILE   A CD1 1 
ATOM   10350 N  N   . PHE   A 1 1291 ? -10.62000  14.24500  3.79600   1.000 53.76766  ?  1289 PHE   A N   1 
ATOM   10351 C  CA  . PHE   A 1 1291 ? -9.81600   14.57900  4.97100   1.000 57.96011  ?  1289 PHE   A CA  1 
ATOM   10352 C  C   . PHE   A 1 1291 ? -8.33200   14.29400  4.74700   1.000 64.68386  ?  1289 PHE   A C   1 
ATOM   10353 O  O   . PHE   A 1 1291 ? -7.47500   14.98200  5.31400   1.000 64.68725  ?  1289 PHE   A O   1 
ATOM   10354 C  CB  . PHE   A 1 1291 ? -10.32500  13.80500  6.19000   1.000 50.07250  ?  1289 PHE   A CB  1 
ATOM   10355 C  CG  . PHE   A 1 1291 ? -11.34400  14.54500  7.01500   1.000 54.46824  ?  1289 PHE   A CG  1 
ATOM   10356 C  CD1 . PHE   A 1 1291 ? -10.94600  15.40000  8.03000   1.000 53.17557  ?  1289 PHE   A CD1 1 
ATOM   10357 C  CD2 . PHE   A 1 1291 ? -12.70100  14.37100  6.78700   1.000 48.19395  ?  1289 PHE   A CD2 1 
ATOM   10358 C  CE1 . PHE   A 1 1291 ? -11.87800  16.07200  8.80000   1.000 61.51965  ?  1289 PHE   A CE1 1 
ATOM   10359 C  CE2 . PHE   A 1 1291 ? -13.64000  15.04300  7.55400   1.000 53.81421  ?  1289 PHE   A CE2 1 
ATOM   10360 C  CZ  . PHE   A 1 1291 ? -13.22700  15.89400  8.56100   1.000 58.76359  ?  1289 PHE   A CZ  1 
ATOM   10361 N  N   . ALA   A 1 1292 ? -8.00900   13.28500  3.93100   1.000 67.57688  ?  1290 ALA   A N   1 
ATOM   10362 C  CA  . ALA   A 1 1292 ? -6.60900   12.94300  3.69200   1.000 65.09908  ?  1290 ALA   A CA  1 
ATOM   10363 C  C   . ALA   A 1 1292 ? -5.94500   13.95600  2.77400   1.000 69.28968  ?  1290 ALA   A C   1 
ATOM   10364 O  O   . ALA   A 1 1292 ? -4.79500   14.35000  3.00800   1.000 64.24390  ?  1290 ALA   A O   1 
ATOM   10365 C  CB  . ALA   A 1 1292 ? -6.50000   11.53800  3.10400   1.000 69.31722  ?  1290 ALA   A CB  1 
ATOM   10366 N  N   . VAL   A 1 1293 ? -6.64000   14.35000  1.69900   1.000 52.08185  ?  1291 VAL   A N   1 
ATOM   10367 C  CA  . VAL   A 1 1293 ? -6.23400   15.53100  0.93400   1.000 60.52831  ?  1291 VAL   A CA  1 
ATOM   10368 C  C   . VAL   A 1 1293 ? -5.83500   16.69300  1.82000   1.000 64.35499  ?  1291 VAL   A C   1 
ATOM   10369 O  O   . VAL   A 1 1293 ? -4.83800   17.38100  1.55800   1.000 67.68490  ?  1291 VAL   A O   1 
ATOM   10370 C  CB  . VAL   A 1 1293 ? -7.32000   15.97200  -0.06000  1.000 70.05202  ?  1291 VAL   A CB  1 
ATOM   10371 C  CG1 . VAL   A 1 1293 ? -6.68300   17.04100  -0.92600  1.000 59.09414  ?  1291 VAL   A CG1 1 
ATOM   10372 C  CG2 . VAL   A 1 1293 ? -7.67400   14.81100  -1.01600  1.000 67.13532  ?  1291 VAL   A CG2 1 
ATOM   10373 N  N   . LEU   A 1 1294 ? -6.64500   16.97800  2.83200   1.000 53.75069  ?  1292 LEU   A N   1 
ATOM   10374 C  CA  . LEU   A 1 1294 ? -6.41500   18.15000  3.65800   1.000 69.27478  ?  1292 LEU   A CA  1 
ATOM   10375 C  C   . LEU   A 1 1294 ? -5.22700   17.93000  4.58000   1.000 65.88889  ?  1292 LEU   A C   1 
ATOM   10376 O  O   . LEU   A 1 1294 ? -4.43200   18.84900  4.80400   1.000 80.58251  ?  1292 LEU   A O   1 
ATOM   10377 C  CB  . LEU   A 1 1294 ? -7.68700   18.46800  4.44500   1.000 69.74793  ?  1292 LEU   A CB  1 
ATOM   10378 C  CG  . LEU   A 1 1294 ? -8.70800   19.42800  3.80900   1.000 51.54829  ?  1292 LEU   A CG  1 
ATOM   10379 C  CD1 . LEU   A 1 1294 ? -9.00800   19.11800  2.33000   1.000 54.34927  ?  1292 LEU   A CD1 1 
ATOM   10380 C  CD2 . LEU   A 1 1294 ? -10.00300  19.42800  4.61500   1.000 50.12104  ?  1292 LEU   A CD2 1 
ATOM   10381 N  N   . LYS   A 1 1295 ? -5.07700   16.70800  5.10100   1.000 68.01829  ?  1293 LYS   A N   1 
ATOM   10382 C  CA  . LYS   A 1 1295 ? -3.93000   16.39200  5.94800   1.000 76.14807  ?  1293 LYS   A CA  1 
ATOM   10383 C  C   . LYS   A 1 1295 ? -2.62900   16.41200  5.15300   1.000 75.24144  ?  1293 LYS   A C   1 
ATOM   10384 O  O   . LYS   A 1 1295 ? -1.58900   16.84600  5.66500   1.000 63.39227  ?  1293 LYS   A O   1 
ATOM   10385 C  CB  . LYS   A 1 1295 ? -4.12600   15.02800  6.61100   1.000 59.45106  ?  1293 LYS   A CB  1 
ATOM   10386 C  CG  . LYS   A 1 1295 ? -5.03600   15.04300  7.82600   1.000 48.47258  ?  1293 LYS   A CG  1 
ATOM   10387 C  CD  . LYS   A 1 1295 ? -4.93000   13.74800  8.61400   1.000 45.02938  ?  1293 LYS   A CD  1 
ATOM   10388 C  CE  . LYS   A 1 1295 ? -5.09700   13.99500  10.10400  1.000 51.23283  ?  1293 LYS   A CE  1 
ATOM   10389 N  NZ  . LYS   A 1 1295 ? -4.10600   14.98500  10.61200  1.000 66.76023  ?  1293 LYS   A NZ  1 
ATOM   10390 N  N   . ALA   A 1 1296 ? -2.66300   15.93700  3.90500   1.000 66.03015  ?  1294 ALA   A N   1 
ATOM   10391 C  CA  . ALA   A 1 1296 ? -1.46200   15.94300  3.07500   1.000 64.39462  ?  1294 ALA   A CA  1 
ATOM   10392 C  C   . ALA   A 1 1296 ? -1.02100   17.36000  2.73400   1.000 75.66959  ?  1294 ALA   A C   1 
ATOM   10393 O  O   . ALA   A 1 1296 ? 0.18200    17.62100  2.61500   1.000 80.95043  ?  1294 ALA   A O   1 
ATOM   10394 C  CB  . ALA   A 1 1296 ? -1.70700   15.13900  1.79700   1.000 66.24358  ?  1294 ALA   A CB  1 
ATOM   10395 N  N   . GLY   A 1 1297 ? -1.97200   18.27700  2.56500   1.000 81.98828  ?  1295 GLY   A N   1 
ATOM   10396 C  CA  . GLY   A 1 1297 ? -1.65100   19.67100  2.32900   1.000 73.57823  ?  1295 GLY   A CA  1 
ATOM   10397 C  C   . GLY   A 1 1297 ? -2.42000   20.32300  1.19700   1.000 68.52233  ?  1295 GLY   A C   1 
ATOM   10398 O  O   . GLY   A 1 1297 ? -2.52200   21.55200  1.13200   1.000 68.96123  ?  1295 GLY   A O   1 
ATOM   10399 N  N   . GLY   A 1 1298 ? -2.97300   19.51100  0.29800   1.000 70.63503  ?  1296 GLY   A N   1 
ATOM   10400 C  CA  . GLY   A 1 1298 ? -3.62300   20.00900  -0.89400  1.000 64.00078  ?  1296 GLY   A CA  1 
ATOM   10401 C  C   . GLY   A 1 1298 ? -5.07200   20.40500  -0.66700  1.000 67.32331  ?  1296 GLY   A C   1 
ATOM   10402 O  O   . GLY   A 1 1298 ? -5.57900   20.44300  0.45600   1.000 52.94529  ?  1296 GLY   A O   1 
ATOM   10403 N  N   . ALA   A 1 1299 ? -5.73900   20.72200  -1.77500  1.000 64.62909  ?  1297 ALA   A N   1 
ATOM   10404 C  CA  . ALA   A 1 1299 ? -7.15900   21.03200  -1.79700  1.000 58.47876  ?  1297 ALA   A CA  1 
ATOM   10405 C  C   . ALA   A 1 1299 ? -7.86900   20.01400  -2.68000  1.000 66.60479  ?  1297 ALA   A C   1 
ATOM   10406 O  O   . ALA   A 1 1299 ? -7.29700   19.51800  -3.65600  1.000 71.98059  ?  1297 ALA   A O   1 
ATOM   10407 C  CB  . ALA   A 1 1299 ? -7.41600   22.45500  -2.31300  1.000 67.36795  ?  1297 ALA   A CB  1 
ATOM   10408 N  N   . TYR   A 1 1300 ? -9.11300   19.69400  -2.33100  1.000 56.44743  ?  1298 TYR   A N   1 
ATOM   10409 C  CA  . TYR   A 1 1300 ? -9.84700   18.63000  -3.00600  1.000 58.88902  ?  1298 TYR   A CA  1 
ATOM   10410 C  C   . TYR   A 1 1300 ? -10.84700  19.21900  -3.99100  1.000 51.04956  ?  1298 TYR   A C   1 
ATOM   10411 O  O   . TYR   A 1 1300 ? -11.55900  20.17400  -3.67000  1.000 60.92095  ?  1298 TYR   A O   1 
ATOM   10412 C  CB  . TYR   A 1 1300 ? -10.53100  17.70500  -1.99100  1.000 58.55469  ?  1298 TYR   A CB  1 
ATOM   10413 C  CG  . TYR   A 1 1300 ? -11.87600  18.14000  -1.43400  1.000 61.60841  ?  1298 TYR   A CG  1 
ATOM   10414 C  CD1 . TYR   A 1 1300 ? -11.95900  18.87500  -0.25600  1.000 58.85960  ?  1298 TYR   A CD1 1 
ATOM   10415 C  CD2 . TYR   A 1 1300 ? -13.06300  17.76200  -2.05100  1.000 57.65200  ?  1298 TYR   A CD2 1 
ATOM   10416 C  CE1 . TYR   A 1 1300 ? -13.18700  19.25200  0.27000   1.000 44.11095  ?  1298 TYR   A CE1 1 
ATOM   10417 C  CE2 . TYR   A 1 1300 ? -14.29000  18.13400  -1.53100  1.000 45.68026  ?  1298 TYR   A CE2 1 
ATOM   10418 C  CZ  . TYR   A 1 1300 ? -14.34800  18.87800  -0.37500  1.000 47.17604  ?  1298 TYR   A CZ  1 
ATOM   10419 O  OH  . TYR   A 1 1300 ? -15.57500  19.24200  0.13200   1.000 53.53963  ?  1298 TYR   A OH  1 
ATOM   10420 N  N   . LEU   A 1 1301 ? -10.87700  18.65500  -5.19600  1.000 48.74259  ?  1299 LEU   A N   1 
ATOM   10421 C  CA  . LEU   A 1 1301 ? -11.72100  19.14000  -6.28600  1.000 50.57302  ?  1299 LEU   A CA  1 
ATOM   10422 C  C   . LEU   A 1 1301 ? -12.74500  18.07000  -6.63900  1.000 67.10754  ?  1299 LEU   A C   1 
ATOM   10423 O  O   . LEU   A 1 1301 ? -12.43300  17.13700  -7.40200  1.000 68.09640  ?  1299 LEU   A O   1 
ATOM   10424 C  CB  . LEU   A 1 1301 ? -10.86700  19.49500  -7.50200  1.000 41.14600  ?  1299 LEU   A CB  1 
ATOM   10425 C  CG  . LEU   A 1 1301 ? -11.48900  20.36400  -8.59400  1.000 58.96318  ?  1299 LEU   A CG  1 
ATOM   10426 C  CD1 . LEU   A 1 1301 ? -10.41600  21.20000  -9.27300  1.000 62.24928  ?  1299 LEU   A CD1 1 
ATOM   10427 C  CD2 . LEU   A 1 1301 ? -12.22700  19.51000  -9.61000  1.000 64.56557  ?  1299 LEU   A CD2 1 
ATOM   10428 N  N   . PRO   A 1 1302 ? -13.97300  18.15800  -6.12900  1.000 60.62414  ?  1300 PRO   A N   1 
ATOM   10429 C  CA  . PRO   A 1 1302 ? -14.93900  17.07200  -6.34600  1.000 43.08631  ?  1300 PRO   A CA  1 
ATOM   10430 C  C   . PRO   A 1 1302 ? -15.44600  17.07400  -7.78000  1.000 50.74027  ?  1300 PRO   A C   1 
ATOM   10431 O  O   . PRO   A 1 1302 ? -15.84600  18.11300  -8.30900  1.000 60.78243  ?  1300 PRO   A O   1 
ATOM   10432 C  CB  . PRO   A 1 1302 ? -16.06600  17.38300  -5.35300  1.000 47.82945  ?  1300 PRO   A CB  1 
ATOM   10433 C  CG  . PRO   A 1 1302 ? -15.62100  18.58300  -4.56700  1.000 62.09957  ?  1300 PRO   A CG  1 
ATOM   10434 C  CD  . PRO   A 1 1302 ? -14.55100  19.26200  -5.35100  1.000 60.99906  ?  1300 PRO   A CD  1 
ATOM   10435 N  N   . ILE   A 1 1303 ? -15.42300  15.90100  -8.40600  1.000 63.03093  ?  1301 ILE   A N   1 
ATOM   10436 C  CA  . ILE   A 1 1303 ? -15.96800  15.70200  -9.74200  1.000 64.10635  ?  1301 ILE   A CA  1 
ATOM   10437 C  C   . ILE   A 1 1303 ? -16.95800  14.54900  -9.68800  1.000 66.41514  ?  1301 ILE   A C   1 
ATOM   10438 O  O   . ILE   A 1 1303 ? -16.66300  13.49500  -9.11200  1.000 60.78561  ?  1301 ILE   A O   1 
ATOM   10439 C  CB  . ILE   A 1 1303 ? -14.86300  15.43200  -10.78200 1.000 64.97808  ?  1301 ILE   A CB  1 
ATOM   10440 C  CG1 . ILE   A 1 1303 ? -14.22800  16.74900  -11.23000 1.000 62.76701  ?  1301 ILE   A CG1 1 
ATOM   10441 C  CG2 . ILE   A 1 1303 ? -15.41000  14.67000  -11.97900 1.000 55.12297  ?  1301 ILE   A CG2 1 
ATOM   10442 C  CD1 . ILE   A 1 1303 ? -13.16600  16.59000  -12.29000 1.000 61.48260  ?  1301 ILE   A CD1 1 
ATOM   10443 N  N   . ASP   A 1 1304 ? -18.13100  14.75800  -10.27000 1.000 76.29176  ?  1302 ASP   A N   1 
ATOM   10444 C  CA  . ASP   A 1 1304 ? -19.12700  13.70500  -10.38200 1.000 74.66488  ?  1302 ASP   A CA  1 
ATOM   10445 C  C   . ASP   A 1 1304 ? -18.54400  12.54200  -11.17500 1.000 85.14736  ?  1302 ASP   A C   1 
ATOM   10446 O  O   . ASP   A 1 1304 ? -18.10600  12.74400  -12.31800 1.000 86.98118  ?  1302 ASP   A O   1 
ATOM   10447 C  CB  . ASP   A 1 1304 ? -20.38100  14.24100  -11.06700 1.000 72.19320  ?  1302 ASP   A CB  1 
ATOM   10448 C  CG  . ASP   A 1 1304 ? -21.58200  13.32600  -10.90200 1.000 85.64096  ?  1302 ASP   A CG  1 
ATOM   10449 O  OD1 . ASP   A 1 1304 ? -21.40200  12.09700  -10.76700 1.000 97.34942  ?  1302 ASP   A OD1 1 
ATOM   10450 O  OD2 . ASP   A 1 1304 ? -22.71700  13.84500  -10.90100 1.000 92.10476  -1 1302 ASP   A OD2 1 
ATOM   10451 N  N   . PRO   A 1 1305 ? -18.49900  11.32800  -10.61600 1.000 90.51186  ?  1303 PRO   A N   1 
ATOM   10452 C  CA  . PRO   A 1 1305 ? -18.00200  10.18900  -11.40700 1.000 71.70636  ?  1303 PRO   A CA  1 
ATOM   10453 C  C   . PRO   A 1 1305 ? -18.80900  9.95300   -12.67000 1.000 80.16353  ?  1303 PRO   A C   1 
ATOM   10454 O  O   . PRO   A 1 1305 ? -18.24300  9.58400   -13.70700 1.000 91.57635  ?  1303 PRO   A O   1 
ATOM   10455 C  CB  . PRO   A 1 1305 ? -18.11000  9.00900   -10.43000 1.000 81.19878  ?  1303 PRO   A CB  1 
ATOM   10456 C  CG  . PRO   A 1 1305 ? -18.12300  9.63000   -9.07300  1.000 81.54558  ?  1303 PRO   A CG  1 
ATOM   10457 C  CD  . PRO   A 1 1305 ? -18.81300  10.95100  -9.22700  1.000 81.77338  ?  1303 PRO   A CD  1 
ATOM   10458 N  N   . HIS   A 1 1306 ? -20.12400  10.17300  -12.61500 1.000 83.19585  ?  1304 HIS   A N   1 
ATOM   10459 C  CA  . HIS   A 1 1306 ? -21.00500  9.98100   -13.76000 1.000 83.57239  ?  1304 HIS   A CA  1 
ATOM   10460 C  C   . HIS   A 1 1306 ? -21.12900  11.23100  -14.62200 1.000 83.82807  ?  1304 HIS   A C   1 
ATOM   10461 O  O   . HIS   A 1 1306 ? -22.18600  11.46600  -15.22300 1.000 82.25316  ?  1304 HIS   A O   1 
ATOM   10462 C  CB  . HIS   A 1 1306 ? -22.38300  9.51800   -13.28300 1.000 77.29581  ?  1304 HIS   A CB  1 
ATOM   10463 C  CG  . HIS   A 1 1306 ? -22.32800  8.45400   -12.23100 1.000 81.00622  ?  1304 HIS   A CG  1 
ATOM   10464 N  ND1 . HIS   A 1 1306 ? -21.43700  7.40400   -12.28200 1.000 78.91739  ?  1304 HIS   A ND1 1 
ATOM   10465 C  CD2 . HIS   A 1 1306 ? -23.05100  8.28000   -11.10000 1.000 87.87861  ?  1304 HIS   A CD2 1 
ATOM   10466 C  CE1 . HIS   A 1 1306 ? -21.61400  6.62800   -11.22700 1.000 85.63244  ?  1304 HIS   A CE1 1 
ATOM   10467 N  NE2 . HIS   A 1 1306 ? -22.58700  7.13700   -10.49400 1.000 86.85879  ?  1304 HIS   A NE2 1 
ATOM   10468 N  N   . SER   A 1 1307 ? -20.07600  12.04000  -14.69600 1.000 89.00501  ?  1305 SER   A N   1 
ATOM   10469 C  CA  . SER   A 1 1307 ? -20.07100  13.22200  -15.54800 1.000 93.94577  ?  1305 SER   A CA  1 
ATOM   10470 C  C   . SER   A 1 1307 ? -19.48800  12.88000  -16.91700 1.000 87.70222  ?  1305 SER   A C   1 
ATOM   10471 O  O   . SER   A 1 1307 ? -18.48600  12.16200  -17.00000 1.000 92.66516  ?  1305 SER   A O   1 
ATOM   10472 C  CB  . SER   A 1 1307 ? -19.25500  14.34500  -14.91200 1.000 92.24218  ?  1305 SER   A CB  1 
ATOM   10473 O  OG  . SER   A 1 1307 ? -18.05700  13.84600  -14.34200 1.000 87.62731  ?  1305 SER   A OG  1 
ATOM   10474 N  N   . PRO   A 1 1308 ? -20.10800  13.37400  -17.98900 1.000 79.66135  ?  1306 PRO   A N   1 
ATOM   10475 C  CA  . PRO   A 1 1308 ? -19.59700  13.09700  -19.33700 1.000 90.92711  ?  1306 PRO   A CA  1 
ATOM   10476 C  C   . PRO   A 1 1308 ? -18.13000  13.48100  -19.47900 1.000 99.97666  ?  1306 PRO   A C   1 
ATOM   10477 O  O   . PRO   A 1 1308 ? -17.65100  14.43200  -18.85700 1.000 110.46052 ?  1306 PRO   A O   1 
ATOM   10478 C  CB  . PRO   A 1 1308 ? -20.49000  13.95900  -20.23600 1.000 80.87217  ?  1306 PRO   A CB  1 
ATOM   10479 C  CG  . PRO   A 1 1308 ? -21.76400  14.08700  -19.47500 1.000 86.43046  ?  1306 PRO   A CG  1 
ATOM   10480 C  CD  . PRO   A 1 1308 ? -21.37500  14.12500  -18.02000 1.000 94.84700  ?  1306 PRO   A CD  1 
ATOM   10481 N  N   . ALA   A 1 1309 ? -17.41600  12.72100  -20.31700 1.000 100.16114 ?  1307 ALA   A N   1 
ATOM   10482 C  CA  . ALA   A 1 1309 ? -15.98500  12.94600  -20.49200 1.000 97.57216  ?  1307 ALA   A CA  1 
ATOM   10483 C  C   . ALA   A 1 1309 ? -15.69100  14.32800  -21.06300 1.000 105.74053 ?  1307 ALA   A C   1 
ATOM   10484 O  O   . ALA   A 1 1309 ? -14.60700  14.87600  -20.83000 1.000 97.77310  ?  1307 ALA   A O   1 
ATOM   10485 C  CB  . ALA   A 1 1309 ? -15.38400  11.85800  -21.38300 1.000 81.67022  ?  1307 ALA   A CB  1 
ATOM   10486 N  N   . GLU   A 1 1310 ? -16.63700  14.90400  -21.81200 1.000 111.69690 ?  1308 GLU   A N   1 
ATOM   10487 C  CA  . GLU   A 1 1310 ? -16.49300  16.28000  -22.27600 1.000 102.62474 ?  1308 GLU   A CA  1 
ATOM   10488 C  C   . GLU   A 1 1310 ? -16.20800  17.22200  -21.11000 1.000 101.31212 ?  1308 GLU   A C   1 
ATOM   10489 O  O   . GLU   A 1 1310 ? -15.24400  17.99500  -21.13600 1.000 91.59855  ?  1308 GLU   A O   1 
ATOM   10490 C  CB  . GLU   A 1 1310 ? -17.75600  16.70900  -23.02800 1.000 81.94111  ?  1308 GLU   A CB  1 
ATOM   10491 N  N   . ARG   A 1 1311 ? -17.02800  17.14700  -20.06000 1.000 93.97348  ?  1309 ARG   A N   1 
ATOM   10492 C  CA  . ARG   A 1 1311 ? -16.80200  17.96900  -18.87700 1.000 89.73047  ?  1309 ARG   A CA  1 
ATOM   10493 C  C   . ARG   A 1 1311 ? -15.46300  17.64900  -18.22000 1.000 94.22154  ?  1309 ARG   A C   1 
ATOM   10494 O  O   . ARG   A 1 1311 ? -14.62100  18.53600  -18.05200 1.000 98.19985  ?  1309 ARG   A O   1 
ATOM   10495 C  CB  . ARG   A 1 1311 ? -17.94600  17.77400  -17.88200 1.000 83.90992  ?  1309 ARG   A CB  1 
ATOM   10496 C  CG  . ARG   A 1 1311 ? -17.90400  18.66200  -16.65700 1.000 83.72845  ?  1309 ARG   A CG  1 
ATOM   10497 C  CD  . ARG   A 1 1311 ? -19.29300  19.16700  -16.34100 1.000 98.12656  ?  1309 ARG   A CD  1 
ATOM   10498 N  NE  . ARG   A 1 1311 ? -19.58100  20.51200  -16.82000 1.000 91.95589  ?  1309 ARG   A NE  1 
ATOM   10499 C  CZ  . ARG   A 1 1311 ? -20.24700  20.78300  -17.93500 1.000 99.67250  ?  1309 ARG   A CZ  1 
ATOM   10500 N  NH1 . ARG   A 1 1311 ? -20.55100  19.83300  -18.80700 1.000 100.08532 ?  1309 ARG   A NH1 1 
ATOM   10501 N  NH2 . ARG   A 1 1311 ? -20.59100  22.04200  -18.19600 1.000 106.59561 ?  1309 ARG   A NH2 1 
ATOM   10502 N  N   . ILE   A 1 1312 ? -15.25200  16.38200  -17.82100 1.000 93.42984  ?  1310 ILE   A N   1 
ATOM   10503 C  CA  . ILE   A 1 1312 ? -14.06100  16.04600  -17.03600 1.000 104.84464 ?  1310 ILE   A CA  1 
ATOM   10504 C  C   . ILE   A 1 1312 ? -12.80500  16.56700  -17.72700 1.000 100.31672 ?  1310 ILE   A C   1 
ATOM   10505 O  O   . ILE   A 1 1312 ? -11.99100  17.26500  -17.11600 1.000 96.51284  ?  1310 ILE   A O   1 
ATOM   10506 C  CB  . ILE   A 1 1312 ? -13.99000  14.53100  -16.75100 1.000 103.33446 ?  1310 ILE   A CB  1 
ATOM   10507 C  CG1 . ILE   A 1 1312 ? -13.74800  13.72200  -18.02300 1.000 93.42977  ?  1310 ILE   A CG1 1 
ATOM   10508 C  CG2 . ILE   A 1 1312 ? -15.26800  14.05300  -16.07600 1.000 93.27137  ?  1310 ILE   A CG2 1 
ATOM   10509 C  CD1 . ILE   A 1 1312 ? -12.86800  12.51200  -17.84100 1.000 108.55446 ?  1310 ILE   A CD1 1 
ATOM   10510 N  N   . ALA   A 1 1313 ? -12.68500  16.32500  -19.03800 1.000 97.79670  ?  1311 ALA   A N   1 
ATOM   10511 C  CA  . ALA   A 1 1313 ? -11.54100  16.82900  -19.79500 1.000 99.45572  ?  1311 ALA   A CA  1 
ATOM   10512 C  C   . ALA   A 1 1313 ? -11.35900  18.32900  -19.59900 1.000 99.12234  ?  1311 ALA   A C   1 
ATOM   10513 O  O   . ALA   A 1 1313 ? -10.22700  18.81800  -19.48000 1.000 84.36919  ?  1311 ALA   A O   1 
ATOM   10514 C  CB  . ALA   A 1 1313 ? -11.71200  16.50100  -21.28000 1.000 99.75793  ?  1311 ALA   A CB  1 
ATOM   10515 N  N   . TYR   A 1 1314 ? -12.46400  19.07200  -19.53900 1.000 102.96044 ?  1312 TYR   A N   1 
ATOM   10516 C  CA  . TYR   A 1 1314 ? -12.39300  20.51100  -19.31600 1.000 100.94038 ?  1312 TYR   A CA  1 
ATOM   10517 C  C   . TYR   A 1 1314 ? -11.76800  20.82600  -17.95800 1.000 96.06080  ?  1312 TYR   A C   1 
ATOM   10518 O  O   . TYR   A 1 1314 ? -10.78300  21.56900  -17.87300 1.000 89.56782  ?  1312 TYR   A O   1 
ATOM   10519 C  CB  . TYR   A 1 1314 ? -13.79300  21.11900  -19.44600 1.000 91.17024  ?  1312 TYR   A CB  1 
ATOM   10520 C  CG  . TYR   A 1 1314 ? -13.88200  22.58800  -19.11800 1.000 97.73633  ?  1312 TYR   A CG  1 
ATOM   10521 C  CD1 . TYR   A 1 1314 ? -13.65200  23.55300  -20.09000 1.000 108.80966 ?  1312 TYR   A CD1 1 
ATOM   10522 C  CD2 . TYR   A 1 1314 ? -14.21900  23.01100  -17.84100 1.000 104.69062 ?  1312 TYR   A CD2 1 
ATOM   10523 C  CE1 . TYR   A 1 1314 ? -13.73700  24.89900  -19.79100 1.000 120.74919 ?  1312 TYR   A CE1 1 
ATOM   10524 C  CE2 . TYR   A 1 1314 ? -14.30700  24.34800  -17.53400 1.000 108.83065 ?  1312 TYR   A CE2 1 
ATOM   10525 C  CZ  . TYR   A 1 1314 ? -14.06800  25.29100  -18.51100 1.000 118.74611 ?  1312 TYR   A CZ  1 
ATOM   10526 O  OH  . TYR   A 1 1314 ? -14.15700  26.63100  -18.20700 1.000 125.01631 ?  1312 TYR   A OH  1 
ATOM   10527 N  N   . ILE   A 1 1315 ? -12.32100  20.25800  -16.87900 1.000 90.60380  ?  1313 ILE   A N   1 
ATOM   10528 C  CA  . ILE   A 1 1315 ? -11.79700  20.55000  -15.54400 1.000 95.23391  ?  1313 ILE   A CA  1 
ATOM   10529 C  C   . ILE   A 1 1315 ? -10.38100  20.01000  -15.39400 1.000 96.15383  ?  1313 ILE   A C   1 
ATOM   10530 O  O   . ILE   A 1 1315 ? -9.51300   20.66700  -14.80600 1.000 87.53123  ?  1313 ILE   A O   1 
ATOM   10531 C  CB  . ILE   A 1 1315 ? -12.72300  19.99400  -14.44400 1.000 82.07264  ?  1313 ILE   A CB  1 
ATOM   10532 C  CG1 . ILE   A 1 1315 ? -14.06000  20.73200  -14.41000 1.000 79.05247  ?  1313 ILE   A CG1 1 
ATOM   10533 C  CG2 . ILE   A 1 1315 ? -12.06800  20.11000  -13.08000 1.000 66.21650  ?  1313 ILE   A CG2 1 
ATOM   10534 C  CD1 . ILE   A 1 1315 ? -15.13600  20.06600  -15.21200 1.000 77.46846  ?  1313 ILE   A CD1 1 
ATOM   10535 N  N   . PHE   A 1 1316 ? -10.13200  18.79700  -15.90400 1.000 106.46682 ?  1314 PHE   A N   1 
ATOM   10536 C  CA  . PHE   A 1 1316 ? -8.78000   18.24300  -15.91800 1.000 101.90825 ?  1314 PHE   A CA  1 
ATOM   10537 C  C   . PHE   A 1 1316 ? -7.78400   19.27100  -16.44300 1.000 95.81376  ?  1314 PHE   A C   1 
ATOM   10538 O  O   . PHE   A 1 1316 ? -6.69700   19.44800  -15.88000 1.000 79.13099  ?  1314 PHE   A O   1 
ATOM   10539 C  CB  . PHE   A 1 1316 ? -8.72700   16.97600  -16.78300 1.000 103.17686 ?  1314 PHE   A CB  1 
ATOM   10540 C  CG  . PHE   A 1 1316 ? -9.24800   15.72200  -16.10200 1.000 109.28608 ?  1314 PHE   A CG  1 
ATOM   10541 C  CD1 . PHE   A 1 1316 ? -10.47100  15.70400  -15.45500 1.000 119.83491 ?  1314 PHE   A CD1 1 
ATOM   10542 C  CD2 . PHE   A 1 1316 ? -8.51100   14.55400  -16.12700 1.000 112.31377 ?  1314 PHE   A CD2 1 
ATOM   10543 C  CE1 . PHE   A 1 1316 ? -10.95200  14.55300  -14.85300 1.000 124.30106 ?  1314 PHE   A CE1 1 
ATOM   10544 C  CE2 . PHE   A 1 1316 ? -8.98600   13.39900  -15.51600 1.000 116.92458 ?  1314 PHE   A CE2 1 
ATOM   10545 C  CZ  . PHE   A 1 1316 ? -10.20400  13.40300  -14.87800 1.000 118.10435 ?  1314 PHE   A CZ  1 
ATOM   10546 N  N   . ALA   A 1 1317 ? -8.16000   19.98300  -17.50800 1.000 97.60656  ?  1315 ALA   A N   1 
ATOM   10547 C  CA  . ALA   A 1 1317 ? -7.27800   20.99000  -18.08800 1.000 95.41731  ?  1315 ALA   A CA  1 
ATOM   10548 C  C   . ALA   A 1 1317 ? -7.28400   22.26800  -17.26000 1.000 93.15254  ?  1315 ALA   A C   1 
ATOM   10549 O  O   . ALA   A 1 1317 ? -6.24200   22.69100  -16.74700 1.000 87.54002  ?  1315 ALA   A O   1 
ATOM   10550 C  CB  . ALA   A 1 1317 ? -7.69000   21.27500  -19.53400 1.000 78.98476  ?  1315 ALA   A CB  1 
ATOM   10551 N  N   . ASP   A 1 1318 ? -8.46100   22.89300  -17.11100 1.000 92.05064  ?  1316 ASP   A N   1 
ATOM   10552 C  CA  . ASP   A 1 1318 ? -8.56500   24.16200  -16.39200 1.000 78.75346  ?  1316 ASP   A CA  1 
ATOM   10553 C  C   . ASP   A 1 1318 ? -7.89800   24.09700  -15.02500 1.000 79.05009  ?  1316 ASP   A C   1 
ATOM   10554 O  O   . ASP   A 1 1318 ? -7.21900   25.04400  -14.60900 1.000 92.17645  ?  1316 ASP   A O   1 
ATOM   10555 C  CB  . ASP   A 1 1318 ? -10.03500  24.55800  -16.24300 1.000 94.96721  ?  1316 ASP   A CB  1 
ATOM   10556 C  CG  . ASP   A 1 1318 ? -10.45400  25.63000  -17.22900 1.000 111.11454 ?  1316 ASP   A CG  1 
ATOM   10557 O  OD1 . ASP   A 1 1318 ? -9.73000   25.85400  -18.22200 1.000 121.08729 ?  1316 ASP   A OD1 1 
ATOM   10558 O  OD2 . ASP   A 1 1318 ? -11.51500  26.24800  -17.00700 1.000 95.46463  ?  1316 ASP   A OD2 1 
ATOM   10559 N  N   . SER   A 1 1319 ? -8.07000   22.98100  -14.31300 1.000 82.02545  ?  1317 SER   A N   1 
ATOM   10560 C  CA  . SER   A 1 1319 ? -7.42200   22.83100  -13.01400 1.000 87.85270  ?  1317 SER   A CA  1 
ATOM   10561 C  C   . SER   A 1 1319 ? -5.92700   22.59700  -13.17000 1.000 93.03110  ?  1317 SER   A C   1 
ATOM   10562 O  O   . SER   A 1 1319 ? -5.12800   23.08700  -12.36100 1.000 83.86171  ?  1317 SER   A O   1 
ATOM   10563 C  CB  . SER   A 1 1319 ? -8.06300   21.68300  -12.23400 1.000 85.07160  ?  1317 SER   A CB  1 
ATOM   10564 O  OG  . SER   A 1 1319 ? -7.82700   20.44100  -12.87700 1.000 87.68312  ?  1317 SER   A OG  1 
ATOM   10565 N  N   . GLY   A 1 1320 ? -5.52900   21.86200  -14.20700 1.000 92.15643  ?  1318 GLY   A N   1 
ATOM   10566 C  CA  . GLY   A 1 1320 ? -4.14500   21.46100  -14.34800 1.000 90.93804  ?  1318 GLY   A CA  1 
ATOM   10567 C  C   . GLY   A 1 1320 ? -3.68300   20.49700  -13.28500 1.000 89.96737  ?  1318 GLY   A C   1 
ATOM   10568 O  O   . GLY   A 1 1320 ? -2.47700   20.34900  -13.07200 1.000 93.77172  ?  1318 GLY   A O   1 
ATOM   10569 N  N   . ALA   A 1 1321 ? -4.61500   19.84200  -12.60200 1.000 89.50030  ?  1319 ALA   A N   1 
ATOM   10570 C  CA  . ALA   A 1 1321 ? -4.27500   18.93600  -11.52100 1.000 93.26429  ?  1319 ALA   A CA  1 
ATOM   10571 C  C   . ALA   A 1 1321 ? -3.73800   17.62100  -12.07400 1.000 98.00182  ?  1319 ALA   A C   1 
ATOM   10572 O  O   . ALA   A 1 1321 ? -3.94800   17.27000  -13.23900 1.000 93.81452  ?  1319 ALA   A O   1 
ATOM   10573 C  CB  . ALA   A 1 1321 ? -5.49300   18.68500  -10.63500 1.000 82.99696  ?  1319 ALA   A CB  1 
ATOM   10574 N  N   . LYS   A 1 1322 ? -3.03200   16.89000  -11.21500 1.000 97.14334  ?  1320 LYS   A N   1 
ATOM   10575 C  CA  . LYS   A 1 1322 ? -2.39800   15.63200  -11.58600 1.000 102.28340 ?  1320 LYS   A CA  1 
ATOM   10576 C  C   . LYS   A 1 1322 ? -3.03900   14.42500  -10.91900 1.000 95.66657  ?  1320 LYS   A C   1 
ATOM   10577 O  O   . LYS   A 1 1322 ? -3.39200   13.45800  -11.60100 1.000 97.56178  ?  1320 LYS   A O   1 
ATOM   10578 C  CB  . LYS   A 1 1322 ? -0.90100   15.68200  -11.24100 1.000 101.97853 ?  1320 LYS   A CB  1 
ATOM   10579 N  N   . LEU   A 1 1323 ? -3.20200   14.45600  -9.59900  1.000 84.56589  ?  1321 LEU   A N   1 
ATOM   10580 C  CA  . LEU   A 1 1323 ? -3.74600   13.31500  -8.87700  1.000 90.30751  ?  1321 LEU   A CA  1 
ATOM   10581 C  C   . LEU   A 1 1323 ? -5.25700   13.22600  -9.05900  1.000 88.20895  ?  1321 LEU   A C   1 
ATOM   10582 O  O   . LEU   A 1 1323 ? -5.95900   14.24200  -9.06500  1.000 78.45481  ?  1321 LEU   A O   1 
ATOM   10583 C  CB  . LEU   A 1 1323 ? -3.40500   13.41500  -7.39100  1.000 66.85004  ?  1321 LEU   A CB  1 
ATOM   10584 C  CG  . LEU   A 1 1323 ? -2.00200   13.02200  -6.93900  1.000 85.54206  ?  1321 LEU   A CG  1 
ATOM   10585 C  CD1 . LEU   A 1 1323 ? -1.16500   14.26400  -6.67300  1.000 73.17999  ?  1321 LEU   A CD1 1 
ATOM   10586 C  CD2 . LEU   A 1 1323 ? -2.09300   12.15800  -5.69200  1.000 69.48340  ?  1321 LEU   A CD2 1 
ATOM   10587 N  N   . VAL   A 1 1324 ? -5.75100   11.99800  -9.22200  1.000 78.23290  ?  1322 VAL   A N   1 
ATOM   10588 C  CA  . VAL   A 1 1324 ? -7.18200   11.73800  -9.34300  1.000 59.17679  ?  1322 VAL   A CA  1 
ATOM   10589 C  C   . VAL   A 1 1324 ? -7.55700   10.60000  -8.40400  1.000 72.30043  ?  1322 VAL   A C   1 
ATOM   10590 O  O   . VAL   A 1 1324 ? -7.61200   9.43600   -8.81500  1.000 91.67300  ?  1322 VAL   A O   1 
ATOM   10591 C  CB  . VAL   A 1 1324 ? -7.58300   11.40000  -10.79300 1.000 62.63700  ?  1322 VAL   A CB  1 
ATOM   10592 C  CG1 . VAL   A 1 1324 ? -9.10000   11.39000  -10.93700 1.000 75.58173  ?  1322 VAL   A CG1 1 
ATOM   10593 C  CG2 . VAL   A 1 1324 ? -6.96500   12.38400  -11.77300 1.000 87.48575  ?  1322 VAL   A CG2 1 
ATOM   10594 N  N   . LEU   A 1 1325 ? -7.81000   10.92300  -7.13500  1.000 68.61465  ?  1323 LEU   A N   1 
ATOM   10595 C  CA  . LEU   A 1 1325 ? -8.26900   9.92600   -6.17300  1.000 59.78951  ?  1323 LEU   A CA  1 
ATOM   10596 C  C   . LEU   A 1 1325 ? -9.66200   9.43300   -6.54300  1.000 65.90977  ?  1323 LEU   A C   1 
ATOM   10597 O  O   . LEU   A 1 1325 ? -10.66300  10.02800  -6.13300  1.000 87.10624  ?  1323 LEU   A O   1 
ATOM   10598 C  CB  . LEU   A 1 1325 ? -8.28000   10.49900  -4.75500  1.000 47.75615  ?  1323 LEU   A CB  1 
ATOM   10599 C  CG  . LEU   A 1 1325 ? -7.05500   10.24300  -3.88100  1.000 55.05464  ?  1323 LEU   A CG  1 
ATOM   10600 C  CD1 . LEU   A 1 1325 ? -5.79600   10.68300  -4.60400  1.000 66.35398  ?  1323 LEU   A CD1 1 
ATOM   10601 C  CD2 . LEU   A 1 1325 ? -7.19600   10.95700  -2.54300  1.000 48.19814  ?  1323 LEU   A CD2 1 
ATOM   10602 N  N   . ALA   A 1 1326 ? -9.73800   8.34700   -7.30600  1.000 71.66398  ?  1324 ALA   A N   1 
ATOM   10603 C  CA  . ALA   A 1 1326 ? -10.99900  7.82300   -7.80700  1.000 76.41984  ?  1324 ALA   A CA  1 
ATOM   10604 C  C   . ALA   A 1 1326 ? -11.29600  6.45800   -7.19800  1.000 84.39271  ?  1324 ALA   A C   1 
ATOM   10605 O  O   . ALA   A 1 1326 ? -10.38900  5.73200   -6.78100  1.000 81.13510  ?  1324 ALA   A O   1 
ATOM   10606 C  CB  . ALA   A 1 1326 ? -10.97500  7.71200   -9.33500  1.000 72.14088  ?  1324 ALA   A CB  1 
ATOM   10607 N  N   . GLN   A 1 1327 ? -12.58200  6.11900   -7.14600  1.000 87.00063  ?  1325 GLN   A N   1 
ATOM   10608 C  CA  . GLN   A 1 1327 ? -12.99600  4.78900   -6.73100  1.000 84.91288  ?  1325 GLN   A CA  1 
ATOM   10609 C  C   . GLN   A 1 1327 ? -12.74900  3.78700   -7.85500  1.000 89.19522  ?  1325 GLN   A C   1 
ATOM   10610 O  O   . GLN   A 1 1327 ? -12.54100  4.15400   -9.01500  1.000 91.72962  ?  1325 GLN   A O   1 
ATOM   10611 C  CB  . GLN   A 1 1327 ? -14.47200  4.78200   -6.32600  1.000 74.46553  ?  1325 GLN   A CB  1 
ATOM   10612 C  CG  . GLN   A 1 1327 ? -14.70900  5.03900   -4.84400  1.000 75.53910  ?  1325 GLN   A CG  1 
ATOM   10613 C  CD  . GLN   A 1 1327 ? -16.18300  5.05100   -4.47500  1.000 74.19822  ?  1325 GLN   A CD  1 
ATOM   10614 O  OE1 . GLN   A 1 1327 ? -17.05300  5.18800   -5.33700  1.000 53.09090  ?  1325 GLN   A OE1 1 
ATOM   10615 N  NE2 . GLN   A 1 1327 ? -16.47100  4.90000   -3.18600  1.000 57.11358  ?  1325 GLN   A NE2 1 
ATOM   10616 N  N   . SER   A 1 1328 ? -12.77400  2.50400   -7.49200  1.000 85.04430  ?  1326 SER   A N   1 
ATOM   10617 C  CA  . SER   A 1 1328 ? -12.46000  1.43600   -8.44200  1.000 72.50030  ?  1326 SER   A CA  1 
ATOM   10618 C  C   . SER   A 1 1328 ? -13.27100  1.49400   -9.73100  1.000 78.58233  ?  1326 SER   A C   1 
ATOM   10619 O  O   . SER   A 1 1328 ? -12.67300  1.35400   -10.81000 1.000 87.00636  ?  1326 SER   A O   1 
ATOM   10620 C  CB  . SER   A 1 1328 ? -12.62400  0.07400   -7.75100  1.000 74.39723  ?  1326 SER   A CB  1 
ATOM   10621 O  OG  . SER   A 1 1328 ? -11.45900  -0.26500  -7.02100  1.000 92.54012  ?  1326 SER   A OG  1 
ATOM   10622 N  N   . PRO   A 1 1329 ? -14.59600  1.69600   -9.71600  1.000 77.28874  ?  1327 PRO   A N   1 
ATOM   10623 C  CA  . PRO   A 1 1329 ? -15.33700  1.74100   -10.98900 1.000 64.74012  ?  1327 PRO   A CA  1 
ATOM   10624 C  C   . PRO   A 1 1329 ? -15.00500  2.94000   -11.86400 1.000 80.32997  ?  1327 PRO   A C   1 
ATOM   10625 O  O   . PRO   A 1 1329 ? -15.46900  2.98400   -13.01100 1.000 78.30526  ?  1327 PRO   A O   1 
ATOM   10626 C  CB  . PRO   A 1 1329 ? -16.80600  1.77800   -10.54400 1.000 52.97397  ?  1327 PRO   A CB  1 
ATOM   10627 C  CG  . PRO   A 1 1329 ? -16.80000  1.26000   -9.14600  1.000 71.39064  ?  1327 PRO   A CG  1 
ATOM   10628 C  CD  . PRO   A 1 1329 ? -15.51600  1.74400   -8.56400  1.000 67.90520  ?  1327 PRO   A CD  1 
ATOM   10629 N  N   . PHE   A 1 1330 ? -14.22200  3.91000   -11.37600 1.000 88.19477  ?  1328 PHE   A N   1 
ATOM   10630 C  CA  . PHE   A 1 1330 ? -13.93900  5.12000   -12.14100 1.000 89.04615  ?  1328 PHE   A CA  1 
ATOM   10631 C  C   . PHE   A 1 1330 ? -12.44700  5.42700   -12.23000 1.000 92.02456  ?  1328 PHE   A C   1 
ATOM   10632 O  O   . PHE   A 1 1330 ? -12.07700  6.57600   -12.48900 1.000 101.88915 ?  1328 PHE   A O   1 
ATOM   10633 C  CB  . PHE   A 1 1330 ? -14.67100  6.32800   -11.54600 1.000 80.10883  ?  1328 PHE   A CB  1 
ATOM   10634 C  CG  . PHE   A 1 1330 ? -16.00300  5.99800   -10.94000 1.000 78.50851  ?  1328 PHE   A CG  1 
ATOM   10635 C  CD1 . PHE   A 1 1330 ? -17.08900  5.69300   -11.74400 1.000 68.52889  ?  1328 PHE   A CD1 1 
ATOM   10636 C  CD2 . PHE   A 1 1330 ? -16.17300  6.00500   -9.56500  1.000 85.96757  ?  1328 PHE   A CD2 1 
ATOM   10637 C  CE1 . PHE   A 1 1330 ? -18.31800  5.39200   -11.18800 1.000 73.03050  ?  1328 PHE   A CE1 1 
ATOM   10638 C  CE2 . PHE   A 1 1330 ? -17.40000  5.70700   -9.00100  1.000 73.32992  ?  1328 PHE   A CE2 1 
ATOM   10639 C  CZ  . PHE   A 1 1330 ? -18.47400  5.40000   -9.81400  1.000 75.43876  ?  1328 PHE   A CZ  1 
ATOM   10640 N  N   . VAL   A 1 1331 ? -11.57700  4.43700   -12.02000 1.000 88.53822  ?  1329 VAL   A N   1 
ATOM   10641 C  CA  . VAL   A 1 1331 ? -10.14200  4.69700   -12.10800 1.000 91.95300  ?  1329 VAL   A CA  1 
ATOM   10642 C  C   . VAL   A 1 1331 ? -9.74800   5.00000   -13.55000 1.000 87.73643  ?  1329 VAL   A C   1 
ATOM   10643 O  O   . VAL   A 1 1331 ? -9.02200   5.96300   -13.82400 1.000 91.50206  ?  1329 VAL   A O   1 
ATOM   10644 C  CB  . VAL   A 1 1331 ? -9.33900   3.51600   -11.53100 1.000 86.60653  ?  1329 VAL   A CB  1 
ATOM   10645 C  CG1 . VAL   A 1 1331 ? -7.96300   3.43900   -12.17500 1.000 71.75515  ?  1329 VAL   A CG1 1 
ATOM   10646 C  CG2 . VAL   A 1 1331 ? -9.20900   3.65100   -10.01900 1.000 81.21159  ?  1329 VAL   A CG2 1 
ATOM   10647 N  N   . GLU   A 1 1332 ? -10.23200  4.19100   -14.49500 1.000 89.97442  ?  1330 GLU   A N   1 
ATOM   10648 C  CA  . GLU   A 1 1332 ? -9.99100   4.45800   -15.90800 1.000 103.24483 ?  1330 GLU   A CA  1 
ATOM   10649 C  C   . GLU   A 1 1332 ? -10.82800  5.61400   -16.43700 1.000 111.30272 ?  1330 GLU   A C   1 
ATOM   10650 O  O   . GLU   A 1 1332 ? -10.58900  6.06300   -17.56300 1.000 107.87424 ?  1330 GLU   A O   1 
ATOM   10651 C  CB  . GLU   A 1 1332 ? -10.26500  3.20300   -16.73900 1.000 107.83740 ?  1330 GLU   A CB  1 
ATOM   10652 N  N   . LYS   A 1 1333 ? -11.80500  6.09600   -15.66100 1.000 106.16695 ?  1331 LYS   A N   1 
ATOM   10653 C  CA  . LYS   A 1 1333 ? -12.56200  7.27300   -16.07200 1.000 99.29523  ?  1331 LYS   A CA  1 
ATOM   10654 C  C   . LYS   A 1 1333 ? -11.66500  8.49600   -16.18400 1.000 106.24373 ?  1331 LYS   A C   1 
ATOM   10655 O  O   . LYS   A 1 1333 ? -11.93000  9.38900   -16.99700 1.000 112.48233 ?  1331 LYS   A O   1 
ATOM   10656 C  CB  . LYS   A 1 1333 ? -13.70100  7.53700   -15.08800 1.000 84.84055  ?  1331 LYS   A CB  1 
ATOM   10657 C  CG  . LYS   A 1 1333 ? -15.06400  7.68600   -15.74100 1.000 92.54216  ?  1331 LYS   A CG  1 
ATOM   10658 C  CD  . LYS   A 1 1333 ? -16.17400  7.26900   -14.79100 1.000 95.79262  ?  1331 LYS   A CD  1 
ATOM   10659 C  CE  . LYS   A 1 1333 ? -17.47100  7.00200   -15.53600 1.000 75.78173  ?  1331 LYS   A CE  1 
ATOM   10660 N  NZ  . LYS   A 1 1333 ? -18.10600  8.26300   -16.00500 1.000 78.57897  ?  1331 LYS   A NZ  1 
ATOM   10661 N  N   . ALA   A 1 1334 ? -10.60100  8.55500   -15.38100 1.000 84.92333  ?  1332 ALA   A N   1 
ATOM   10662 C  CA  . ALA   A 1 1334 ? -9.59900   9.59800   -15.53900 1.000 93.55662  ?  1332 ALA   A CA  1 
ATOM   10663 C  C   . ALA   A 1 1334 ? -8.77900   9.42400   -16.80900 1.000 115.03128 ?  1332 ALA   A C   1 
ATOM   10664 O  O   . ALA   A 1 1334 ? -7.99700   10.31900  -17.14700 1.000 116.81022 ?  1332 ALA   A O   1 
ATOM   10665 C  CB  . ALA   A 1 1334 ? -8.67200   9.62600   -14.32600 1.000 81.06424  ?  1332 ALA   A CB  1 
ATOM   10666 N  N   . SER   A 1 1335 ? -8.93900   8.29800   -17.50900 1.000 122.20276 ?  1333 SER   A N   1 
ATOM   10667 C  CA  . SER   A 1 1335 ? -8.21100   8.00800   -18.74300 1.000 113.20025 ?  1333 SER   A CA  1 
ATOM   10668 C  C   . SER   A 1 1335 ? -6.70100   8.10200   -18.54200 1.000 117.22860 ?  1333 SER   A C   1 
ATOM   10669 O  O   . SER   A 1 1335 ? -5.97200   8.52700   -19.44300 1.000 127.54672 ?  1333 SER   A O   1 
ATOM   10670 C  CB  . SER   A 1 1335 ? -8.65800   8.92800   -19.88200 1.000 117.14347 ?  1333 SER   A CB  1 
ATOM   10671 O  OG  . SER   A 1 1335 ? -10.07000  9.01700   -19.93200 1.000 115.22680 ?  1333 SER   A OG  1 
ATOM   10672 N  N   . MET   A 1 1336 ? -6.23100   7.70200   -17.35900 1.000 117.44791 ?  1334 MET   A N   1 
ATOM   10673 C  CA  . MET   A 1 1336 ? -4.81900   7.80600   -16.98600 1.000 113.27725 ?  1334 MET   A CA  1 
ATOM   10674 C  C   . MET   A 1 1336 ? -4.30900   9.23300   -17.16400 1.000 129.67354 ?  1334 MET   A C   1 
ATOM   10675 O  O   . MET   A 1 1336 ? -3.18900   9.45700   -17.63200 1.000 136.78293 ?  1334 MET   A O   1 
ATOM   10676 C  CB  . MET   A 1 1336 ? -3.96100   6.81500   -17.77600 1.000 104.99748 ?  1334 MET   A CB  1 
ATOM   10677 N  N   . ALA   A 1 1337 ? -5.15100   10.20300  -16.79000 1.000 117.63604 ?  1335 ALA   A N   1 
ATOM   10678 C  CA  . ALA   A 1 1337 ? -4.84100   11.62400  -16.92500 1.000 94.52221  ?  1335 ALA   A CA  1 
ATOM   10679 C  C   . ALA   A 1 1337 ? -3.41700   11.93800  -16.49300 1.000 105.65991 ?  1335 ALA   A C   1 
ATOM   10680 O  O   . ALA   A 1 1337 ? -2.58400   12.36400  -17.29900 1.000 116.64169 ?  1335 ALA   A O   1 
ATOM   10681 C  CB  . ALA   A 1 1337 ? -5.83100   12.44600  -16.10300 1.000 92.60986  ?  1335 ALA   A CB  1 
ATOM   10682 N  N   . GLU   A 1 1338 ? -3.13200   11.74300  -15.21000 1.000 95.44174  ?  1336 GLU   A N   1 
ATOM   10683 C  CA  . GLU   A 1 1338 ? -1.75300   11.70000  -14.75200 1.000 108.15249 ?  1336 GLU   A CA  1 
ATOM   10684 C  C   . GLU   A 1 1338 ? -1.59300   10.50500  -13.82400 1.000 117.08825 ?  1336 GLU   A C   1 
ATOM   10685 O  O   . GLU   A 1 1338 ? -1.68500   9.35700   -14.27200 1.000 120.51170 ?  1336 GLU   A O   1 
ATOM   10686 C  CB  . GLU   A 1 1338 ? -1.35000   13.00500  -14.06700 1.000 114.37606 ?  1336 GLU   A CB  1 
ATOM   10687 C  CG  . GLU   A 1 1338 ? 0.14500    13.27100  -14.13700 1.000 115.36513 ?  1336 GLU   A CG  1 
ATOM   10688 C  CD  . GLU   A 1 1338 ? 0.72800    12.94700  -15.50400 1.000 132.37274 ?  1336 GLU   A CD  1 
ATOM   10689 O  OE1 . GLU   A 1 1338 ? 0.31400    13.57700  -16.50100 1.000 138.53978 ?  1336 GLU   A OE1 1 
ATOM   10690 O  OE2 . GLU   A 1 1338 ? 1.59800    12.05400  -15.58400 1.000 135.62242 -1 1336 GLU   A OE2 1 
ATOM   10691 N  N   . VAL   A 1 1339 ? -1.37800   10.74400  -12.53600 1.000 109.97746 ?  1337 VAL   A N   1 
ATOM   10692 C  CA  . VAL   A 1 1339 ? -1.25900   9.66200   -11.56800 1.000 103.98474 ?  1337 VAL   A CA  1 
ATOM   10693 C  C   . VAL   A 1 1339 ? -2.61900   9.48400   -10.90700 1.000 100.35791 ?  1337 VAL   A C   1 
ATOM   10694 O  O   . VAL   A 1 1339 ? -3.08900   10.36300  -10.17700 1.000 97.65463  ?  1337 VAL   A O   1 
ATOM   10695 C  CB  . VAL   A 1 1339 ? -0.16400   9.93100   -10.53200 1.000 90.15391  ?  1337 VAL   A CB  1 
ATOM   10696 C  CG1 . VAL   A 1 1339 ? 0.28000    8.61300   -9.92100  1.000 115.48954 ?  1337 VAL   A CG1 1 
ATOM   10697 C  CG2 . VAL   A 1 1339 ? 1.00500    10.66600  -11.16500 1.000 88.08932  ?  1337 VAL   A CG2 1 
ATOM   10698 N  N   . VAL   A 1 1340 ? -3.24600   8.34000   -11.16400 1.000 99.34867  ?  1338 VAL   A N   1 
ATOM   10699 C  CA  . VAL   A 1 1340 ? -4.59700   8.04200   -10.70900 1.000 88.65926  ?  1338 VAL   A CA  1 
ATOM   10700 C  C   . VAL   A 1 1340 ? -4.51100   6.92600   -9.67700  1.000 80.85580  ?  1338 VAL   A C   1 
ATOM   10701 O  O   . VAL   A 1 1340 ? -4.03000   5.82700   -9.98000  1.000 98.70336  ?  1338 VAL   A O   1 
ATOM   10702 C  CB  . VAL   A 1 1340 ? -5.50600   7.64200   -11.88100 1.000 78.63394  ?  1338 VAL   A CB  1 
ATOM   10703 C  CG1 . VAL   A 1 1340 ? -6.91200   7.32700   -11.39100 1.000 82.37706  ?  1338 VAL   A CG1 1 
ATOM   10704 C  CG2 . VAL   A 1 1340 ? -5.52000   8.73600   -12.94100 1.000 87.69648  ?  1338 VAL   A CG2 1 
ATOM   10705 N  N   . LEU   A 1 1341 ? -4.96700   7.20700   -8.46200  1.000 71.84743  ?  1339 LEU   A N   1 
ATOM   10706 C  CA  . LEU   A 1 1341 ? -5.01300   6.19900   -7.41600  1.000 82.33770  ?  1339 LEU   A CA  1 
ATOM   10707 C  C   . LEU   A 1 1341 ? -6.38100   5.52000   -7.38900  1.000 96.24067  ?  1339 LEU   A C   1 
ATOM   10708 O  O   . LEU   A 1 1341 ? -7.31800   5.91200   -8.08800  1.000 87.73064  ?  1339 LEU   A O   1 
ATOM   10709 C  CB  . LEU   A 1 1341 ? -4.69500   6.81600   -6.05400  1.000 59.20460  ?  1339 LEU   A CB  1 
ATOM   10710 C  CG  . LEU   A 1 1341 ? -3.29200   7.39800   -5.88000  1.000 69.51961  ?  1339 LEU   A CG  1 
ATOM   10711 C  CD1 . LEU   A 1 1341 ? -2.93700   7.48800   -4.40400  1.000 69.39366  ?  1339 LEU   A CD1 1 
ATOM   10712 C  CD2 . LEU   A 1 1341 ? -2.26000   6.57300   -6.63900  1.000 87.22689  ?  1339 LEU   A CD2 1 
ATOM   10713 N  N   . ASP   A 1 1342 ? -6.48400   4.47700   -6.56900  1.000 94.29660  ?  1340 ASP   A N   1 
ATOM   10714 C  CA  . ASP   A 1 1342 ? -7.72200   3.72500   -6.39000  1.000 83.27337  ?  1340 ASP   A CA  1 
ATOM   10715 C  C   . ASP   A 1 1342 ? -8.04500   3.71200   -4.90300  1.000 87.74630  ?  1340 ASP   A C   1 
ATOM   10716 O  O   . ASP   A 1 1342 ? -7.33300   3.08300   -4.11400  1.000 79.39334  ?  1340 ASP   A O   1 
ATOM   10717 C  CB  . ASP   A 1 1342 ? -7.59200   2.30500   -6.94200  1.000 86.94777  ?  1340 ASP   A CB  1 
ATOM   10718 C  CG  . ASP   A 1 1342 ? -8.92900   1.58700   -7.04200  1.000 103.33860 ?  1340 ASP   A CG  1 
ATOM   10719 O  OD1 . ASP   A 1 1342 ? -9.88600   1.98000   -6.34000  1.000 98.15714  ?  1340 ASP   A OD1 1 
ATOM   10720 O  OD2 . ASP   A 1 1342 ? -9.02100   0.62300   -7.83100  1.000 107.38810 -1 1340 ASP   A OD2 1 
ATOM   10721 N  N   . LEU   A 1 1343 ? -9.12200   4.40200   -4.52400  1.000 90.01241  ?  1341 LEU   A N   1 
ATOM   10722 C  CA  . LEU   A 1 1343 ? -9.51000   4.46400   -3.12100  1.000 84.90174  ?  1341 LEU   A CA  1 
ATOM   10723 C  C   . LEU   A 1 1343 ? -9.93400   3.10600   -2.57600  1.000 80.95836  ?  1341 LEU   A C   1 
ATOM   10724 O  O   . LEU   A 1 1343 ? -9.99000   2.93400   -1.35400  1.000 71.38890  ?  1341 LEU   A O   1 
ATOM   10725 C  CB  . LEU   A 1 1343 ? -10.63600  5.48200   -2.93300  1.000 90.93964  ?  1341 LEU   A CB  1 
ATOM   10726 C  CG  . LEU   A 1 1343 ? -10.32600  6.92500   -3.33600  1.000 71.85706  ?  1341 LEU   A CG  1 
ATOM   10727 C  CD1 . LEU   A 1 1343 ? -11.60300  7.74800   -3.39900  1.000 65.06518  ?  1341 LEU   A CD1 1 
ATOM   10728 C  CD2 . LEU   A 1 1343 ? -9.33200   7.54300   -2.36700  1.000 69.83138  ?  1341 LEU   A CD2 1 
ATOM   10729 N  N   . ASN   A 1 1344 ? -10.22500  2.14000   -3.44800  1.000 86.61008  ?  1342 ASN   A N   1 
ATOM   10730 C  CA  . ASN   A 1 1344 ? -10.63500  0.81200   -3.01400  1.000 88.78064  ?  1342 ASN   A CA  1 
ATOM   10731 C  C   . ASN   A 1 1344 ? -9.49400   -0.19500  -2.98100  1.000 84.82512  ?  1342 ASN   A C   1 
ATOM   10732 O  O   . ASN   A 1 1344 ? -9.62200   -1.22600  -2.31100  1.000 81.74150  ?  1342 ASN   A O   1 
ATOM   10733 C  CB  . ASN   A 1 1344 ? -11.74900  0.28100   -3.92100  1.000 81.30330  ?  1342 ASN   A CB  1 
ATOM   10734 C  CG  . ASN   A 1 1344 ? -12.97700  1.16100   -3.90300  1.000 77.83156  ?  1342 ASN   A CG  1 
ATOM   10735 O  OD1 . ASN   A 1 1344 ? -13.55000  1.47100   -4.94700  1.000 77.48887  ?  1342 ASN   A OD1 1 
ATOM   10736 N  ND2 . ASN   A 1 1344 ? -13.38900  1.57400   -2.71000  1.000 71.78808  ?  1342 ASN   A ND2 1 
ATOM   10737 N  N   . SER   A 1 1345 ? -8.39500   0.07000   -3.68400  1.000 88.25744  ?  1343 SER   A N   1 
ATOM   10738 C  CA  . SER   A 1 1345 ? -7.22400   -0.79600  -3.65400  1.000 79.18661  ?  1343 SER   A CA  1 
ATOM   10739 C  C   . SER   A 1 1345 ? -6.33400   -0.42000  -2.47500  1.000 65.61438  ?  1343 SER   A C   1 
ATOM   10740 O  O   . SER   A 1 1345 ? -5.94400   0.74300   -2.33100  1.000 77.66771  ?  1343 SER   A O   1 
ATOM   10741 C  CB  . SER   A 1 1345 ? -6.43900   -0.69200  -4.96100  1.000 65.10405  ?  1343 SER   A CB  1 
ATOM   10742 O  OG  . SER   A 1 1345 ? -5.22300   -1.41600  -4.88100  1.000 71.25702  ?  1343 SER   A OG  1 
ATOM   10743 N  N   . ALA   A 1 1346 ? -6.01200   -1.40800  -1.63600  1.000 73.32306  ?  1344 ALA   A N   1 
ATOM   10744 C  CA  . ALA   A 1 1346 ? -5.16100   -1.16300  -0.47700  1.000 70.33934  ?  1344 ALA   A CA  1 
ATOM   10745 C  C   . ALA   A 1 1346 ? -3.73200   -0.80900  -0.86100  1.000 78.90140  ?  1344 ALA   A C   1 
ATOM   10746 O  O   . ALA   A 1 1346 ? -2.96400   -0.37900  0.00700   1.000 67.06671  ?  1344 ALA   A O   1 
ATOM   10747 C  CB  . ALA   A 1 1346 ? -5.16200   -2.38100  0.44900   1.000 45.82448  ?  1344 ALA   A CB  1 
ATOM   10748 N  N   . SER   A 1 1347 ? -3.35700   -0.98800  -2.13100  1.000 78.61924  ?  1345 SER   A N   1 
ATOM   10749 C  CA  . SER   A 1 1347 ? -2.04700   -0.53500  -2.58600  1.000 76.55631  ?  1345 SER   A CA  1 
ATOM   10750 C  C   . SER   A 1 1347 ? -1.94700   0.98400   -2.53500  1.000 91.84907  ?  1345 SER   A C   1 
ATOM   10751 O  O   . SER   A 1 1347 ? -0.89100   1.53200   -2.19900  1.000 90.65838  ?  1345 SER   A O   1 
ATOM   10752 C  CB  . SER   A 1 1347 ? -1.77100   -1.04900  -4.00100  1.000 73.07929  ?  1345 SER   A CB  1 
ATOM   10753 O  OG  . SER   A 1 1347 ? -2.45700   -0.28500  -4.97900  1.000 77.00415  ?  1345 SER   A OG  1 
ATOM   10754 N  N   . SER   A 1 1348 ? -3.04100   1.68000   -2.84800  1.000 83.68185  ?  1346 SER   A N   1 
ATOM   10755 C  CA  . SER   A 1 1348 ? -3.05900   3.13700   -2.81500  1.000 75.02242  ?  1346 SER   A CA  1 
ATOM   10756 C  C   . SER   A 1 1348 ? -3.04000   3.70100   -1.39900  1.000 77.37924  ?  1346 SER   A C   1 
ATOM   10757 O  O   . SER   A 1 1348 ? -3.05800   4.92800   -1.24400  1.000 91.22056  ?  1346 SER   A O   1 
ATOM   10758 C  CB  . SER   A 1 1348 ? -4.28300   3.65800   -3.57100  1.000 83.49336  ?  1346 SER   A CB  1 
ATOM   10759 O  OG  . SER   A 1 1348 ? -4.38800   3.05500   -4.85100  1.000 76.81855  ?  1346 SER   A OG  1 
ATOM   10760 N  N   . TYR   A 1 1349 ? -3.00200   2.85300   -0.37700  1.000 59.96479  ?  1347 TYR   A N   1 
ATOM   10761 C  CA  . TYR   A 1 1349 ? -2.87900   3.27300   1.01000   1.000 62.22509  ?  1347 TYR   A CA  1 
ATOM   10762 C  C   . TYR   A 1 1349 ? -1.50100   2.87400   1.53000   1.000 67.72406  ?  1347 TYR   A C   1 
ATOM   10763 O  O   . TYR   A 1 1349 ? -0.70000   2.25200   0.82600   1.000 79.62594  ?  1347 TYR   A O   1 
ATOM   10764 C  CB  . TYR   A 1 1349 ? -4.00100   2.67200   1.86500   1.000 66.21742  ?  1347 TYR   A CB  1 
ATOM   10765 C  CG  . TYR   A 1 1349 ? -5.39500   3.14000   1.48900   1.000 76.03398  ?  1347 TYR   A CG  1 
ATOM   10766 C  CD1 . TYR   A 1 1349 ? -5.95500   2.80600   0.26100   1.000 68.25405  ?  1347 TYR   A CD1 1 
ATOM   10767 C  CD2 . TYR   A 1 1349 ? -6.15200   3.91500   2.36200   1.000 77.76278  ?  1347 TYR   A CD2 1 
ATOM   10768 C  CE1 . TYR   A 1 1349 ? -7.22000   3.22800   -0.08900  1.000 73.94666  ?  1347 TYR   A CE1 1 
ATOM   10769 C  CE2 . TYR   A 1 1349 ? -7.42500   4.34100   2.02000   1.000 79.42828  ?  1347 TYR   A CE2 1 
ATOM   10770 C  CZ  . TYR   A 1 1349 ? -7.95200   3.99300   0.79100   1.000 79.91189  ?  1347 TYR   A CZ  1 
ATOM   10771 O  OH  . TYR   A 1 1349 ? -9.21300   4.40900   0.43500   1.000 72.92694  ?  1347 TYR   A OH  1 
ATOM   10772 N  N   . ALA   A 1 1350 ? -1.22400   3.24200   2.77700   1.000 62.55123  ?  1348 ALA   A N   1 
ATOM   10773 C  CA  . ALA   A 1 1350 ? 0.08300    3.01500   3.37600   1.000 57.42760  ?  1348 ALA   A CA  1 
ATOM   10774 C  C   . ALA   A 1 1350 ? -0.08900   2.34400   4.73000   1.000 68.06536  ?  1348 ALA   A C   1 
ATOM   10775 O  O   . ALA   A 1 1350 ? -1.20300   2.03100   5.16000   1.000 81.52080  ?  1348 ALA   A O   1 
ATOM   10776 C  CB  . ALA   A 1 1350 ? 0.86700    4.32600   3.51600   1.000 57.94848  ?  1348 ALA   A CB  1 
ATOM   10777 N  N   . ALA   A 1 1351 ? 1.03500    2.13200   5.40900   1.000 58.24570  ?  1349 ALA   A N   1 
ATOM   10778 C  CA  . ALA   A 1 1351 ? 1.04700    1.45300   6.69700   1.000 57.48988  ?  1349 ALA   A CA  1 
ATOM   10779 C  C   . ALA   A 1 1351 ? 1.07300    2.40500   7.87900   1.000 67.50506  ?  1349 ALA   A C   1 
ATOM   10780 O  O   . ALA   A 1 1351 ? 0.63800    2.02700   8.97100   1.000 59.01986  ?  1349 ALA   A O   1 
ATOM   10781 C  CB  . ALA   A 1 1351 ? 2.25400    0.51600   6.79100   1.000 61.84958  ?  1349 ALA   A CB  1 
ATOM   10782 N  N   . ASP   A 1 1352 ? 1.57600    3.62100   7.69200   1.000 84.82868  ?  1350 ASP   A N   1 
ATOM   10783 C  CA  . ASP   A 1 1352 ? 1.72000    4.55100   8.80300   1.000 83.16974  ?  1350 ASP   A CA  1 
ATOM   10784 C  C   . ASP   A 1 1352 ? 0.35300    5.08100   9.21500   1.000 77.86717  ?  1350 ASP   A C   1 
ATOM   10785 O  O   . ASP   A 1 1352 ? -0.34600   5.71200   8.41500   1.000 71.54401  ?  1350 ASP   A O   1 
ATOM   10786 C  CB  . ASP   A 1 1352 ? 2.65300    5.69700   8.42200   1.000 87.28948  ?  1350 ASP   A CB  1 
ATOM   10787 C  CG  . ASP   A 1 1352 ? 3.19400    6.43600   9.63500   1.000 91.75888  ?  1350 ASP   A CG  1 
ATOM   10788 O  OD1 . ASP   A 1 1352 ? 2.88300    6.02800   10.77600  1.000 77.25354  ?  1350 ASP   A OD1 1 
ATOM   10789 O  OD2 . ASP   A 1 1352 ? 3.93200    7.42700   9.44700   1.000 95.51938  -1 1350 ASP   A OD2 1 
ATOM   10790 N  N   . THR   A 1 1353 ? -0.02600   4.81600   10.46400  1.000 76.19248  ?  1351 THR   A N   1 
ATOM   10791 C  CA  . THR   A 1 1353 ? -1.27800   5.29400   11.03100  1.000 68.26506  ?  1351 THR   A CA  1 
ATOM   10792 C  C   . THR   A 1 1353 ? -1.07000   6.48000   11.96400  1.000 74.70089  ?  1351 THR   A C   1 
ATOM   10793 O  O   . THR   A 1 1353 ? -1.95300   6.78700   12.77400  1.000 70.50190  ?  1351 THR   A O   1 
ATOM   10794 C  CB  . THR   A 1 1353 ? -1.98900   4.16300   11.77400  1.000 80.34883  ?  1351 THR   A CB  1 
ATOM   10795 O  OG1 . THR   A 1 1353 ? -1.20900   3.77500   12.91200  1.000 80.09654  ?  1351 THR   A OG1 1 
ATOM   10796 C  CG2 . THR   A 1 1353 ? -2.17500   2.96100   10.86000  1.000 57.51821  ?  1351 THR   A CG2 1 
ATOM   10797 N  N   . SER   A 1 1354 ? 0.08100    7.14000   11.87600  1.000 82.30567  ?  1352 SER   A N   1 
ATOM   10798 C  CA  . SER   A 1 1354 ? 0.38400    8.30000   12.69900  1.000 78.21518  ?  1352 SER   A CA  1 
ATOM   10799 C  C   . SER   A 1 1354 ? -0.00400   9.58200   11.97200  1.000 74.42331  ?  1352 SER   A C   1 
ATOM   10800 O  O   . SER   A 1 1354 ? 0.08600    9.67500   10.74300  1.000 62.10562  ?  1352 SER   A O   1 
ATOM   10801 C  CB  . SER   A 1 1354 ? 1.87000    8.33100   13.06200  1.000 94.75172  ?  1352 SER   A CB  1 
ATOM   10802 O  OG  . SER   A 1 1354 ? 2.67700    8.52900   11.91400  1.000 86.71609  ?  1352 SER   A OG  1 
ATOM   10803 N  N   . ASN   A 1 1355 ? -0.43200   10.57200  12.74900  1.000 68.51499  ?  1353 ASN   A N   1 
ATOM   10804 C  CA  . ASN   A 1 1355 ? -0.90600   11.83700  12.20300  1.000 69.04677  ?  1353 ASN   A CA  1 
ATOM   10805 C  C   . ASN   A 1 1355 ? 0.19300    12.52300  11.39800  1.000 71.33953  ?  1353 ASN   A C   1 
ATOM   10806 O  O   . ASN   A 1 1355 ? 1.27300    12.79500  11.94600  1.000 87.78590  ?  1353 ASN   A O   1 
ATOM   10807 C  CB  . ASN   A 1 1355 ? -1.38000   12.75000  13.33300  1.000 54.75136  ?  1353 ASN   A CB  1 
ATOM   10808 C  CG  . ASN   A 1 1355 ? -2.79900   12.44200  13.77200  1.000 68.27721  ?  1353 ASN   A CG  1 
ATOM   10809 O  OD1 . ASN   A 1 1355 ? -3.63400   12.04100  12.96200  1.000 72.30462  ?  1353 ASN   A OD1 1 
ATOM   10810 N  ND2 . ASN   A 1 1355 ? -3.08200   12.63800  15.05600  1.000 55.24433  ?  1353 ASN   A ND2 1 
ATOM   10811 N  N   . PRO   A 1 1356 ? -0.02300   12.81100  10.11100  1.000 71.13001  ?  1354 PRO   A N   1 
ATOM   10812 C  CA  . PRO   A 1 1356 ? 1.00000    13.51600  9.34400   1.000 64.10312  ?  1354 PRO   A CA  1 
ATOM   10813 C  C   . PRO   A 1 1356 ? 1.17700    14.93000  9.87100   1.000 89.49781  ?  1354 PRO   A C   1 
ATOM   10814 O  O   . PRO   A 1 1356 ? 0.24300    15.51300  10.44600  1.000 95.98888  ?  1354 PRO   A O   1 
ATOM   10815 C  CB  . PRO   A 1 1356 ? 0.43700    13.51500  7.91000   1.000 63.35332  ?  1354 PRO   A CB  1 
ATOM   10816 C  CG  . PRO   A 1 1356 ? -0.65500   12.48600  7.90800   1.000 73.76448  ?  1354 PRO   A CG  1 
ATOM   10817 C  CD  . PRO   A 1 1356 ? -1.20700   12.49400  9.29600   1.000 79.54026  ?  1354 PRO   A CD  1 
ATOM   10818 N  N   . PRO   A 1 1357 ? 2.36000    15.51600  9.70600   1.000 94.53978  ?  1355 PRO   A N   1 
ATOM   10819 C  CA  . PRO   A 1 1357 ? 2.60400    16.84900  10.26600  1.000 83.09294  ?  1355 PRO   A CA  1 
ATOM   10820 C  C   . PRO   A 1 1357 ? 1.78500    17.91900  9.56000   1.000 78.20916  ?  1355 PRO   A C   1 
ATOM   10821 O  O   . PRO   A 1 1357 ? 1.37400    17.77800  8.40500   1.000 63.82062  ?  1355 PRO   A O   1 
ATOM   10822 C  CB  . PRO   A 1 1357 ? 4.10400    17.06300  10.03800  1.000 66.59601  ?  1355 PRO   A CB  1 
ATOM   10823 C  CG  . PRO   A 1 1357 ? 4.43800    16.16900  8.89300   1.000 61.37728  ?  1355 PRO   A CG  1 
ATOM   10824 C  CD  . PRO   A 1 1357 ? 3.54300    14.97400  9.01800   1.000 79.65778  ?  1355 PRO   A CD  1 
ATOM   10825 N  N   . LEU   A 1 1358 ? 1.55700    19.01100  10.28700  1.000 75.26145  ?  1356 LEU   A N   1 
ATOM   10826 C  CA  . LEU   A 1 1358 ? 0.78500    20.13000  9.76200   1.000 73.14441  ?  1356 LEU   A CA  1 
ATOM   10827 C  C   . LEU   A 1 1358 ? 1.60600    20.88800  8.72200   1.000 65.70512  ?  1356 LEU   A C   1 
ATOM   10828 O  O   . LEU   A 1 1358 ? 2.77000    21.22000  8.96000   1.000 71.24899  ?  1356 LEU   A O   1 
ATOM   10829 C  CB  . LEU   A 1 1358 ? 0.37700    21.05800  10.90500  1.000 52.75739  ?  1356 LEU   A CB  1 
ATOM   10830 C  CG  . LEU   A 1 1358 ? -0.99700   21.72700  10.83900  1.000 72.62544  ?  1356 LEU   A CG  1 
ATOM   10831 C  CD1 . LEU   A 1 1358 ? -1.26600   22.51000  12.11700  1.000 56.22360  ?  1356 LEU   A CD1 1 
ATOM   10832 C  CD2 . LEU   A 1 1358 ? -1.12500   22.62300  9.62200   1.000 73.26507  ?  1356 LEU   A CD2 1 
ATOM   10833 N  N   . VAL   A 1 1359 ? 1.00100    21.15800  7.56500   1.000 61.05572  ?  1357 VAL   A N   1 
ATOM   10834 C  CA  . VAL   A 1 1359 ? 1.71600    21.79400  6.46400   1.000 58.74415  ?  1357 VAL   A CA  1 
ATOM   10835 C  C   . VAL   A 1 1359 ? 0.84000    22.83900  5.78300   1.000 75.89326  ?  1357 VAL   A C   1 
ATOM   10836 O  O   . VAL   A 1 1359 ? 1.11500    23.24200  4.64800   1.000 62.43989  ?  1357 VAL   A O   1 
ATOM   10837 C  CB  . VAL   A 1 1359 ? 2.20200    20.74800  5.44000   1.000 56.45292  ?  1357 VAL   A CB  1 
ATOM   10838 C  CG1 . VAL   A 1 1359 ? 3.39600    19.97200  5.98000   1.000 64.10127  ?  1357 VAL   A CG1 1 
ATOM   10839 C  CG2 . VAL   A 1 1359 ? 1.07100    19.79900  5.07100   1.000 71.63853  ?  1357 VAL   A CG2 1 
ATOM   10840 N  N   . ASN   A 1 1360 ? -0.21500   23.29100  6.46200   1.000 87.94018  ?  1358 ASN   A N   1 
ATOM   10841 C  CA  . ASN   A 1 1360 ? -1.15800   24.23800  5.87900   1.000 75.71577  ?  1358 ASN   A CA  1 
ATOM   10842 C  C   . ASN   A 1 1360 ? -1.38400   25.42000  6.81100   1.000 77.83253  ?  1358 ASN   A C   1 
ATOM   10843 O  O   . ASN   A 1 1360 ? -1.43000   25.26400  8.03600   1.000 65.50251  ?  1358 ASN   A O   1 
ATOM   10844 C  CB  . ASN   A 1 1360 ? -2.50500   23.57000  5.56400   1.000 62.74730  ?  1358 ASN   A CB  1 
ATOM   10845 C  CG  . ASN   A 1 1360 ? -2.38400   22.46900  4.53100   1.000 64.33507  ?  1358 ASN   A CG  1 
ATOM   10846 O  OD1 . ASN   A 1 1360 ? -2.63500   21.29900  4.82100   1.000 63.79577  ?  1358 ASN   A OD1 1 
ATOM   10847 N  ND2 . ASN   A 1 1360 ? -2.00400   22.83900  3.31300   1.000 68.77953  ?  1358 ASN   A ND2 1 
ATOM   10848 N  N   . GLN   A 1 1361 ? -1.53100   26.59800  6.22000   1.000 71.16117  ?  1359 GLN   A N   1 
ATOM   10849 C  CA  . GLN   A 1 1361 ? -1.82600   27.83000  6.93200   1.000 79.61972  ?  1359 GLN   A CA  1 
ATOM   10850 C  C   . GLN   A 1 1361 ? -3.25400   28.27800  6.63500   1.000 73.46751  ?  1359 GLN   A C   1 
ATOM   10851 O  O   . GLN   A 1 1361 ? -3.82800   27.91200  5.60300   1.000 61.38360  ?  1359 GLN   A O   1 
ATOM   10852 C  CB  . GLN   A 1 1361 ? -0.83000   28.93200  6.53600   1.000 82.10854  ?  1359 GLN   A CB  1 
ATOM   10853 C  CG  . GLN   A 1 1361 ? 0.50000    28.86800  7.28800   1.000 77.97255  ?  1359 GLN   A CG  1 
ATOM   10854 C  CD  . GLN   A 1 1361 ? 0.49000    29.68200  8.57300   1.000 95.05027  ?  1359 GLN   A CD  1 
ATOM   10855 O  OE1 . GLN   A 1 1361 ? 0.74400    30.88700  8.56100   1.000 105.44997 ?  1359 GLN   A OE1 1 
ATOM   10856 N  NE2 . GLN   A 1 1361 ? 0.19500    29.02400  9.69000   1.000 79.61313  ?  1359 GLN   A NE2 1 
ATOM   10857 N  N   . PRO   A 1 1362 ? -3.86700   29.06900  7.52500   1.000 55.57793  ?  1360 PRO   A N   1 
ATOM   10858 C  CA  . PRO   A 1 1362 ? -5.28100   29.44000  7.33300   1.000 55.04976  ?  1360 PRO   A CA  1 
ATOM   10859 C  C   . PRO   A 1 1362 ? -5.57800   30.14800  6.01600   1.000 47.08418  ?  1360 PRO   A C   1 
ATOM   10860 O  O   . PRO   A 1 1362 ? -6.75800   30.35100  5.70300   1.000 56.95026  ?  1360 PRO   A O   1 
ATOM   10861 C  CB  . PRO   A 1 1362 ? -5.57300   30.35200  8.53200   1.000 41.68786  ?  1360 PRO   A CB  1 
ATOM   10862 C  CG  . PRO   A 1 1362 ? -4.59400   29.92000  9.57200   1.000 74.48821  ?  1360 PRO   A CG  1 
ATOM   10863 C  CD  . PRO   A 1 1362 ? -3.34800   29.54000  8.82200   1.000 67.68871  ?  1360 PRO   A CD  1 
ATOM   10864 N  N   . GLY   A 1 1363 ? -4.56800   30.52100  5.23900   1.000 43.27826  ?  1361 GLY   A N   1 
ATOM   10865 C  CA  . GLY   A 1 1363 ? -4.77200   31.12500  3.94100   1.000 51.71895  ?  1361 GLY   A CA  1 
ATOM   10866 C  C   . GLY   A 1 1363 ? -4.58500   30.19200  2.76500   1.000 55.94410  ?  1361 GLY   A C   1 
ATOM   10867 O  O   . GLY   A 1 1363 ? -4.54600   30.66300  1.62200   1.000 43.67740  ?  1361 GLY   A O   1 
ATOM   10868 N  N   . ASP   A 1 1364 ? -4.46800   28.89000  3.00100   1.000 57.18845  ?  1362 ASP   A N   1 
ATOM   10869 C  CA  . ASP   A 1 1364 ? -4.22900   27.93200  1.93300   1.000 63.14396  ?  1362 ASP   A CA  1 
ATOM   10870 C  C   . ASP   A 1 1364 ? -5.54500   27.36500  1.41600   1.000 62.43385  ?  1362 ASP   A C   1 
ATOM   10871 O  O   . ASP   A 1 1364 ? -6.54800   27.31300  2.13300   1.000 69.28845  ?  1362 ASP   A O   1 
ATOM   10872 C  CB  . ASP   A 1 1364 ? -3.32900   26.79500  2.41900   1.000 70.95830  ?  1362 ASP   A CB  1 
ATOM   10873 C  CG  . ASP   A 1 1364 ? -1.93400   27.26700  2.79000   1.000 73.69274  ?  1362 ASP   A CG  1 
ATOM   10874 O  OD1 . ASP   A 1 1364 ? -1.43600   28.22700  2.16400   1.000 76.14131  ?  1362 ASP   A OD1 1 
ATOM   10875 O  OD2 . ASP   A 1 1364 ? -1.33900   26.67900  3.71800   1.000 67.80071  -1 1362 ASP   A OD2 1 
ATOM   10876 N  N   . LEU   A 1 1365 ? -5.52600   26.93400  0.15600   1.000 47.04051  ?  1363 LEU   A N   1 
ATOM   10877 C  CA  . LEU   A 1 1365 ? -6.70900   26.34400  -0.45600  1.000 52.74259  ?  1363 LEU   A CA  1 
ATOM   10878 C  C   . LEU   A 1 1365 ? -7.12600   25.07000  0.27000   1.000 61.41487  ?  1363 LEU   A C   1 
ATOM   10879 O  O   . LEU   A 1 1365 ? -6.29800   24.21000  0.58300   1.000 70.53207  ?  1363 LEU   A O   1 
ATOM   10880 C  CB  . LEU   A 1 1365 ? -6.44600   26.03700  -1.93000  1.000 40.98096  ?  1363 LEU   A CB  1 
ATOM   10881 C  CG  . LEU   A 1 1365 ? -6.49400   27.23200  -2.87900  1.000 48.40786  ?  1363 LEU   A CG  1 
ATOM   10882 C  CD1 . LEU   A 1 1365 ? -6.50400   26.76800  -4.32600  1.000 43.64075  ?  1363 LEU   A CD1 1 
ATOM   10883 C  CD2 . LEU   A 1 1365 ? -7.70000   28.10500  -2.57600  1.000 67.30737  ?  1363 LEU   A CD2 1 
ATOM   10884 N  N   . VAL   A 1 1366 ? -8.42600   24.95400  0.53500   1.000 64.45306  ?  1364 VAL   A N   1 
ATOM   10885 C  CA  . VAL   A 1 1366 ? -8.98400   23.74900  1.12000   1.000 57.24462  ?  1364 VAL   A CA  1 
ATOM   10886 C  C   . VAL   A 1 1366 ? -9.81900   22.95000  0.12000   1.000 51.59050  ?  1364 VAL   A C   1 
ATOM   10887 O  O   . VAL   A 1 1366 ? -9.80500   21.71500  0.17200   1.000 60.88371  ?  1364 VAL   A O   1 
ATOM   10888 C  CB  . VAL   A 1 1366 ? -9.80800   24.08200  2.38400   1.000 57.09870  ?  1364 VAL   A CB  1 
ATOM   10889 C  CG1 . VAL   A 1 1366 ? -10.95400  25.02800  2.05400   1.000 53.55238  ?  1364 VAL   A CG1 1 
ATOM   10890 C  CG2 . VAL   A 1 1366 ? -10.31700  22.81300  3.04900   1.000 51.24204  ?  1364 VAL   A CG2 1 
ATOM   10891 N  N   . TYR   A 1 1367 ? -10.52100  23.61000  -0.80100  1.000 53.28063  ?  1365 TYR   A N   1 
ATOM   10892 C  CA  . TYR   A 1 1367 ? -11.20700  22.91300  -1.88200  1.000 54.94490  ?  1365 TYR   A CA  1 
ATOM   10893 C  C   . TYR   A 1 1367 ? -11.41100  23.87600  -3.04300  1.000 43.59976  ?  1365 TYR   A C   1 
ATOM   10894 O  O   . TYR   A 1 1367 ? -11.19300  25.08400  -2.92400  1.000 45.26497  ?  1365 TYR   A O   1 
ATOM   10895 C  CB  . TYR   A 1 1367 ? -12.54000  22.30500  -1.41500  1.000 61.58840  ?  1365 TYR   A CB  1 
ATOM   10896 C  CG  . TYR   A 1 1367 ? -13.65300  23.28900  -1.10200  1.000 58.46456  ?  1365 TYR   A CG  1 
ATOM   10897 C  CD1 . TYR   A 1 1367 ? -14.49100  23.77100  -2.10300  1.000 55.71874  ?  1365 TYR   A CD1 1 
ATOM   10898 C  CD2 . TYR   A 1 1367 ? -13.88700  23.70500  0.20400   1.000 50.82024  ?  1365 TYR   A CD2 1 
ATOM   10899 C  CE1 . TYR   A 1 1367 ? -15.51300  24.66000  -1.81500  1.000 56.29633  ?  1365 TYR   A CE1 1 
ATOM   10900 C  CE2 . TYR   A 1 1367 ? -14.90900  24.59200  0.50100   1.000 57.15162  ?  1365 TYR   A CE2 1 
ATOM   10901 C  CZ  . TYR   A 1 1367 ? -15.71800  25.06600  -0.51100  1.000 62.89476  ?  1365 TYR   A CZ  1 
ATOM   10902 O  OH  . TYR   A 1 1367 ? -16.73300  25.94900  -0.22100  1.000 53.74061  ?  1365 TYR   A OH  1 
ATOM   10903 N  N   . VAL   A 1 1368 ? -11.82500  23.31500  -4.17700  1.000 47.87235  ?  1366 VAL   A N   1 
ATOM   10904 C  CA  . VAL   A 1 1368 ? -12.12600  24.07900  -5.38400  1.000 46.76816  ?  1366 VAL   A CA  1 
ATOM   10905 C  C   . VAL   A 1 1368 ? -13.42500  23.52300  -5.95500  1.000 58.66377  ?  1366 VAL   A C   1 
ATOM   10906 O  O   . VAL   A 1 1368 ? -13.45300  22.39600  -6.46200  1.000 62.43856  ?  1366 VAL   A O   1 
ATOM   10907 C  CB  . VAL   A 1 1368 ? -11.00100  24.00800  -6.42600  1.000 45.81953  ?  1366 VAL   A CB  1 
ATOM   10908 C  CG1 . VAL   A 1 1368 ? -11.50100  24.48000  -7.78800  1.000 55.95371  ?  1366 VAL   A CG1 1 
ATOM   10909 C  CG2 . VAL   A 1 1368 ? -9.80900   24.83900  -5.97400  1.000 48.46222  ?  1366 VAL   A CG2 1 
ATOM   10910 N  N   . MET   A 1 1369 ? -14.49800  24.30200  -5.86500  1.000 55.55801  ?  1367 MET   A N   1 
ATOM   10911 C  CA  . MET   A 1 1369 ? -15.81000  23.90500  -6.35700  1.000 47.59815  ?  1367 MET   A CA  1 
ATOM   10912 C  C   . MET   A 1 1369 ? -16.07100  24.61200  -7.67900  1.000 52.21237  ?  1367 MET   A C   1 
ATOM   10913 O  O   . MET   A 1 1369 ? -16.10500  25.84600  -7.73000  1.000 61.81447  ?  1367 MET   A O   1 
ATOM   10914 C  CB  . MET   A 1 1369 ? -16.89500  24.25300  -5.33800  1.000 50.23306  ?  1367 MET   A CB  1 
ATOM   10915 C  CG  . MET   A 1 1369 ? -18.21200  23.50200  -5.50000  1.000 46.12376  ?  1367 MET   A CG  1 
ATOM   10916 S  SD  . MET   A 1 1369 ? -18.11000  21.77400  -5.01000  1.000 55.38674  ?  1367 MET   A SD  1 
ATOM   10917 C  CE  . MET   A 1 1369 ? -18.04400  21.93600  -3.22900  1.000 37.91341  ?  1367 MET   A CE  1 
ATOM   10918 N  N   . TYR   A 1 1370 ? -16.25700  23.83600  -8.74000  1.000 51.11604  ?  1368 TYR   A N   1 
ATOM   10919 C  CA  . TYR   A 1 1370 ? -16.60300  24.42100  -10.02400 1.000 59.67831  ?  1368 TYR   A CA  1 
ATOM   10920 C  C   . TYR   A 1 1370 ? -18.07900  24.79700  -10.04800 1.000 58.08270  ?  1368 TYR   A C   1 
ATOM   10921 O  O   . TYR   A 1 1370 ? -18.90600  24.20700  -9.34700  1.000 61.91211  ?  1368 TYR   A O   1 
ATOM   10922 C  CB  . TYR   A 1 1370 ? -16.26900  23.46000  -11.16600 1.000 62.84201  ?  1368 TYR   A CB  1 
ATOM   10923 C  CG  . TYR   A 1 1370 ? -14.87800  23.67600  -11.72100 1.000 60.99279  ?  1368 TYR   A CG  1 
ATOM   10924 C  CD1 . TYR   A 1 1370 ? -13.75800  23.53400  -10.91000 1.000 70.55431  ?  1368 TYR   A CD1 1 
ATOM   10925 C  CD2 . TYR   A 1 1370 ? -14.68400  24.04100  -13.04600 1.000 67.94278  ?  1368 TYR   A CD2 1 
ATOM   10926 C  CE1 . TYR   A 1 1370 ? -12.48200  23.73800  -11.40800 1.000 71.04654  ?  1368 TYR   A CE1 1 
ATOM   10927 C  CE2 . TYR   A 1 1370 ? -13.41100  24.24800  -13.55500 1.000 75.57425  ?  1368 TYR   A CE2 1 
ATOM   10928 C  CZ  . TYR   A 1 1370 ? -12.31400  24.09600  -12.73000 1.000 81.45802  ?  1368 TYR   A CZ  1 
ATOM   10929 O  OH  . TYR   A 1 1370 ? -11.04500  24.29900  -13.22300 1.000 82.50529  ?  1368 TYR   A OH  1 
ATOM   10930 N  N   . THR   A 1 1371 ? -18.40300  25.80200  -10.85900 1.000 67.45530  ?  1369 THR   A N   1 
ATOM   10931 C  CA  . THR   A 1 1371 ? -19.73400  26.39600  -10.86900 1.000 74.44057  ?  1369 THR   A CA  1 
ATOM   10932 C  C   . THR   A 1 1371 ? -20.61300  25.87300  -11.99800 1.000 100.31640 ?  1369 THR   A C   1 
ATOM   10933 O  O   . THR   A 1 1371 ? -21.76100  25.48800  -11.75400 1.000 119.23922 ?  1369 THR   A O   1 
ATOM   10934 C  CB  . THR   A 1 1371 ? -19.62900  27.92200  -10.97000 1.000 84.37532  ?  1369 THR   A CB  1 
ATOM   10935 O  OG1 . THR   A 1 1371 ? -18.84000  28.27100  -12.11500 1.000 91.85990  ?  1369 THR   A OG1 1 
ATOM   10936 C  CG2 . THR   A 1 1371 ? -18.98800  28.49800  -9.71600  1.000 66.82462  ?  1369 THR   A CG2 1 
ATOM   10937 N  N   . SER   A 1 1372 ? -20.09800  25.86200  -13.22900 1.000 108.03837 ?  1370 SER   A N   1 
ATOM   10938 C  CA  . SER   A 1 1372 ? -20.88500  25.49700  -14.41000 1.000 125.98485 ?  1370 SER   A CA  1 
ATOM   10939 C  C   . SER   A 1 1372 ? -22.15400  26.34100  -14.49800 1.000 133.58220 ?  1370 SER   A C   1 
ATOM   10940 O  O   . SER   A 1 1372 ? -23.21900  25.86500  -14.89900 1.000 137.31091 ?  1370 SER   A O   1 
ATOM   10941 C  CB  . SER   A 1 1372 ? -21.21500  24.00200  -14.41700 1.000 126.50952 ?  1370 SER   A CB  1 
ATOM   10942 O  OG  . SER   A 1 1372 ? -22.36000  23.73100  -15.20800 1.000 125.03955 ?  1370 SER   A OG  1 
ATOM   10943 N  N   . GLY   A 1 1373 ? -22.03600  27.60700  -14.11400 1.000 127.41488 ?  1371 GLY   A N   1 
ATOM   10944 C  CA  . GLY   A 1 1373 ? -23.18200  28.49400  -14.08100 1.000 131.21620 ?  1371 GLY   A CA  1 
ATOM   10945 C  C   . GLY   A 1 1373 ? -23.77100  28.73100  -15.45800 1.000 147.39440 ?  1371 GLY   A C   1 
ATOM   10946 O  O   . GLY   A 1 1373 ? -23.19100  28.40900  -16.49600 1.000 149.43914 ?  1371 GLY   A O   1 
ATOM   10947 N  N   . SER   A 1 1374 ? -24.97000  29.30800  -15.45300 1.000 147.78463 ?  1372 SER   A N   1 
ATOM   10948 C  CA  . SER   A 1 1374 ? -25.65200  29.62800  -16.69800 1.000 147.91957 ?  1372 SER   A CA  1 
ATOM   10949 C  C   . SER   A 1 1374 ? -24.85600  30.65600  -17.49200 1.000 151.10613 ?  1372 SER   A C   1 
ATOM   10950 O  O   . SER   A 1 1374 ? -24.15400  31.50100  -16.92800 1.000 150.81991 ?  1372 SER   A O   1 
ATOM   10951 C  CB  . SER   A 1 1374 ? -27.06000  30.15500  -16.41500 1.000 148.69122 ?  1372 SER   A CB  1 
ATOM   10952 O  OG  . SER   A 1 1374 ? -27.71200  30.55100  -17.61000 1.000 151.37333 ?  1372 SER   A OG  1 
ATOM   10953 N  N   . THR   A 1 1375 ? -24.97500  30.57400  -18.81800 1.000 158.97587 ?  1373 THR   A N   1 
ATOM   10954 C  CA  . THR   A 1 1375 ? -24.24200  31.43600  -19.74600 1.000 158.09735 ?  1373 THR   A CA  1 
ATOM   10955 C  C   . THR   A 1 1375 ? -22.75100  31.45400  -19.41200 1.000 152.72399 ?  1373 THR   A C   1 
ATOM   10956 O  O   . THR   A 1 1375 ? -22.10500  32.50300  -19.37000 1.000 155.15826 ?  1373 THR   A O   1 
ATOM   10957 C  CB  . THR   A 1 1375 ? -24.81900  32.85500  -19.76000 1.000 148.86109 ?  1373 THR   A CB  1 
ATOM   10958 O  OG1 . THR   A 1 1375 ? -24.58900  33.48500  -18.49400 1.000 155.40114 ?  1373 THR   A OG1 1 
ATOM   10959 C  CG2 . THR   A 1 1375 ? -26.31600  32.82300  -20.04600 1.000 128.82833 ?  1373 THR   A CG2 1 
ATOM   10960 N  N   . GLY   A 1 1376 ? -22.20500  30.26700  -19.16400 1.000 146.45533 ?  1374 GLY   A N   1 
ATOM   10961 C  CA  . GLY   A 1 1376 ? -20.80400  30.15000  -18.82300 1.000 141.70755 ?  1374 GLY   A CA  1 
ATOM   10962 C  C   . GLY   A 1 1376 ? -20.30400  28.72200  -18.76800 1.000 121.66906 ?  1374 GLY   A C   1 
ATOM   10963 O  O   . GLY   A 1 1376 ? -21.05700  27.79800  -18.44800 1.000 109.25555 ?  1374 GLY   A O   1 
ATOM   10964 N  N   . LYS   A 1 1377 ? -19.03100  28.53300  -19.09600 1.000 113.84139 ?  1375 LYS   A N   1 
ATOM   10965 C  CA  . LYS   A 1 1377 ? -18.40600  27.23000  -18.92400 1.000 103.31885 ?  1375 LYS   A CA  1 
ATOM   10966 C  C   . LYS   A 1 1377 ? -17.80300  27.13500  -17.52500 1.000 103.53067 ?  1375 LYS   A C   1 
ATOM   10967 O  O   . LYS   A 1 1377 ? -17.25800  28.12200  -17.02400 1.000 110.34135 ?  1375 LYS   A O   1 
ATOM   10968 C  CB  . LYS   A 1 1377 ? -17.32500  27.00900  -19.98000 1.000 99.35645  ?  1375 LYS   A CB  1 
ATOM   10969 C  CG  . LYS   A 1 1377 ? -17.17100  25.56100  -20.41400 1.000 109.47682 ?  1375 LYS   A CG  1 
ATOM   10970 C  CD  . LYS   A 1 1377 ? -16.57200  25.44600  -21.80300 1.000 107.73710 ?  1375 LYS   A CD  1 
ATOM   10971 C  CE  . LYS   A 1 1377 ? -16.65500  24.01300  -22.31200 1.000 94.97024  ?  1375 LYS   A CE  1 
ATOM   10972 N  NZ  . LYS   A 1 1377 ? -18.03800  23.45800  -22.21400 1.000 87.63090  ?  1375 LYS   A NZ  1 
ATOM   10973 N  N   . PRO   A 1 1378 ? -17.92700  25.95500  -16.88300 1.000 102.82530 ?  1376 PRO   A N   1 
ATOM   10974 C  CA  . PRO   A 1 1378 ? -17.50200  25.79300  -15.48200 1.000 98.15733  ?  1376 PRO   A CA  1 
ATOM   10975 C  C   . PRO   A 1 1378 ? -16.26900  26.58300  -15.06400 1.000 83.28078  ?  1376 PRO   A C   1 
ATOM   10976 O  O   . PRO   A 1 1378 ? -15.22300  26.52300  -15.71400 1.000 92.01159  ?  1376 PRO   A O   1 
ATOM   10977 C  CB  . PRO   A 1 1378 ? -17.24800  24.28000  -15.37900 1.000 100.08592 ?  1376 PRO   A CB  1 
ATOM   10978 C  CG  . PRO   A 1 1378 ? -17.79700  23.66200  -16.68300 1.000 104.06236 ?  1376 PRO   A CG  1 
ATOM   10979 C  CD  . PRO   A 1 1378 ? -18.57100  24.73200  -17.38200 1.000 102.45448 ?  1376 PRO   A CD  1 
ATOM   10980 N  N   . LYS   A 1 1379 ? -16.39600  27.34600  -13.98000 1.000 69.15050  ?  1377 LYS   A N   1 
ATOM   10981 C  CA  . LYS   A 1 1379 ? -15.30500  28.14100  -13.43600 1.000 73.04896  ?  1377 LYS   A CA  1 
ATOM   10982 C  C   . LYS   A 1 1379 ? -14.99800  27.66800  -12.02200 1.000 62.41025  ?  1377 LYS   A C   1 
ATOM   10983 O  O   . LYS   A 1 1379 ? -15.91000  27.35400  -11.25200 1.000 72.89511  ?  1377 LYS   A O   1 
ATOM   10984 C  CB  . LYS   A 1 1379 ? -15.65300  29.63500  -13.43200 1.000 70.11629  ?  1377 LYS   A CB  1 
ATOM   10985 N  N   . GLY   A 1 1380 ? -13.71200  27.62200  -11.68200 1.000 60.01209  ?  1378 GLY   A N   1 
ATOM   10986 C  CA  . GLY   A 1 1380 ? -13.29700  27.05800  -10.41200 1.000 54.91508  ?  1378 GLY   A CA  1 
ATOM   10987 C  C   . GLY   A 1 1380 ? -13.18900  28.04900  -9.27200  1.000 50.56118  ?  1378 GLY   A C   1 
ATOM   10988 O  O   . GLY   A 1 1380 ? -12.28000  28.88300  -9.25300  1.000 60.68640  ?  1378 GLY   A O   1 
ATOM   10989 N  N   . VAL   A 1 1381 ? -14.10000  27.96000  -8.30900  1.000 40.54967  ?  1379 VAL   A N   1 
ATOM   10990 C  CA  . VAL   A 1 1381 ? -14.06300  28.82500  -7.13400  1.000 43.84525  ?  1379 VAL   A CA  1 
ATOM   10991 C  C   . VAL   A 1 1381 ? -13.06800  28.25000  -6.13300  1.000 51.20722  ?  1379 VAL   A C   1 
ATOM   10992 O  O   . VAL   A 1 1381 ? -13.19700  27.09900  -5.70400  1.000 55.22955  ?  1379 VAL   A O   1 
ATOM   10993 C  CB  . VAL   A 1 1381 ? -15.45800  28.96800  -6.51000  1.000 47.16707  ?  1379 VAL   A CB  1 
ATOM   10994 C  CG1 . VAL   A 1 1381 ? -15.38700  29.78100  -5.22300  1.000 47.87098  ?  1379 VAL   A CG1 1 
ATOM   10995 C  CG2 . VAL   A 1 1381 ? -16.40300  29.61700  -7.50100  1.000 50.14081  ?  1379 VAL   A CG2 1 
ATOM   10996 N  N   . MET   A 1 1382 ? -12.07700  29.05100  -5.75500  1.000 44.50439  ?  1380 MET   A N   1 
ATOM   10997 C  CA  . MET   A 1 1382 ? -11.02400  28.62100  -4.84400  1.000 51.34411  ?  1380 MET   A CA  1 
ATOM   10998 C  C   . MET   A 1 1382 ? -11.32700  29.12300  -3.43700  1.000 47.95846  ?  1380 MET   A C   1 
ATOM   10999 O  O   . MET   A 1 1382 ? -11.35300  30.33500  -3.19600  1.000 58.24327  ?  1380 MET   A O   1 
ATOM   11000 C  CB  . MET   A 1 1382 ? -9.66400   29.12400  -5.32300  1.000 56.52198  ?  1380 MET   A CB  1 
ATOM   11001 C  CG  . MET   A 1 1382 ? -9.55900   29.22900  -6.83200  1.000 70.70458  ?  1380 MET   A CG  1 
ATOM   11002 S  SD  . MET   A 1 1382 ? -7.85900   29.23200  -7.42300  1.000 77.00059  ?  1380 MET   A SD  1 
ATOM   11003 C  CE  . MET   A 1 1382 ? -7.14900   30.52600  -6.42600  1.000 51.74849  ?  1380 MET   A CE  1 
ATOM   11004 N  N   . ILE   A 1 1383 ? -11.54300  28.19000  -2.51300  1.000 33.44842  ?  1381 ILE   A N   1 
ATOM   11005 C  CA  . ILE   A 1 1383 ? -11.89800  28.49700  -1.13300  1.000 40.55769  ?  1381 ILE   A CA  1 
ATOM   11006 C  C   . ILE   A 1 1383 ? -10.72300  28.13300  -0.23600  1.000 50.15003  ?  1381 ILE   A C   1 
ATOM   11007 O  O   . ILE   A 1 1383 ? -10.10100  27.07800  -0.40900  1.000 56.39042  ?  1381 ILE   A O   1 
ATOM   11008 C  CB  . ILE   A 1 1383 ? -13.17600  27.74600  -0.70600  1.000 41.80498  ?  1381 ILE   A CB  1 
ATOM   11009 C  CG1 . ILE   A 1 1383 ? -14.40200  28.32100  -1.41900  1.000 52.14710  ?  1381 ILE   A CG1 1 
ATOM   11010 C  CG2 . ILE   A 1 1383 ? -13.36800  27.81600  0.80300   1.000 37.94174  ?  1381 ILE   A CG2 1 
ATOM   11011 C  CD1 . ILE   A 1 1383 ? -14.46700  29.83200  -1.41300  1.000 59.31199  ?  1381 ILE   A CD1 1 
ATOM   11012 N  N   . GLU   A 1 1384 ? -10.42200  29.00400  0.72100   1.000 50.03990  ?  1382 GLU   A N   1 
ATOM   11013 C  CA  . GLU   A 1 1384 ? -9.31500   28.80100  1.64200   1.000 52.14947  ?  1382 GLU   A CA  1 
ATOM   11014 C  C   . GLU   A 1 1384 ? -9.81900   28.27400  2.98300   1.000 57.37733  ?  1382 GLU   A C   1 
ATOM   11015 O  O   . GLU   A 1 1384 ? -11.02000  28.23400  3.25800   1.000 61.85104  ?  1382 GLU   A O   1 
ATOM   11016 C  CB  . GLU   A 1 1384 ? -8.53000   30.10200  1.83000   1.000 64.27971  ?  1382 GLU   A CB  1 
ATOM   11017 C  CG  . GLU   A 1 1384 ? -7.90700   30.62700  0.54500   1.000 73.85124  ?  1382 GLU   A CG  1 
ATOM   11018 C  CD  . GLU   A 1 1384 ? -7.39600   32.04900  0.68000   1.000 87.66601  ?  1382 GLU   A CD  1 
ATOM   11019 O  OE1 . GLU   A 1 1384 ? -7.83300   32.75300  1.61600   1.000 85.70511  ?  1382 GLU   A OE1 1 
ATOM   11020 O  OE2 . GLU   A 1 1384 ? -6.56500   32.46500  -0.15500  1.000 78.32264  -1 1382 GLU   A OE2 1 
ATOM   11021 N  N   . HIS   A 1 1385 ? -8.86600   27.87300  3.82900   1.000 54.03592  ?  1383 HIS   A N   1 
ATOM   11022 C  CA  . HIS   A 1 1385 ? -9.20200   27.21800  5.09000   1.000 52.48108  ?  1383 HIS   A CA  1 
ATOM   11023 C  C   . HIS   A 1 1385 ? -9.90800   28.17300  6.04400   1.000 59.25647  ?  1383 HIS   A C   1 
ATOM   11024 O  O   . HIS   A 1 1385 ? -11.00100  27.87800  6.54200   1.000 58.22266  ?  1383 HIS   A O   1 
ATOM   11025 C  CB  . HIS   A 1 1385 ? -7.93800   26.65000  5.73700   1.000 62.25919  ?  1383 HIS   A CB  1 
ATOM   11026 C  CG  . HIS   A 1 1385 ? -7.48900   25.35200  5.14600   1.000 74.12659  ?  1383 HIS   A CG  1 
ATOM   11027 N  ND1 . HIS   A 1 1385 ? -6.70500   25.28100  4.01400   1.000 77.27674  ?  1383 HIS   A ND1 1 
ATOM   11028 C  CD2 . HIS   A 1 1385 ? -7.71200   24.07300  5.53100   1.000 49.02407  ?  1383 HIS   A CD2 1 
ATOM   11029 C  CE1 . HIS   A 1 1385 ? -6.46500   24.01400  3.72600   1.000 71.43988  ?  1383 HIS   A CE1 1 
ATOM   11030 N  NE2 . HIS   A 1 1385 ? -7.06500   23.26100  4.63100   1.000 75.18292  ?  1383 HIS   A NE2 1 
ATOM   11031 N  N   . GLY   A 1 1386 ? -9.28500   29.32200  6.32600   1.000 66.86692  ?  1384 GLY   A N   1 
ATOM   11032 C  CA  . GLY   A 1 1386 ? -9.89100   30.28000  7.23700   1.000 58.43468  ?  1384 GLY   A CA  1 
ATOM   11033 C  C   . GLY   A 1 1386 ? -11.25900  30.74100  6.78200   1.000 63.75597  ?  1384 GLY   A C   1 
ATOM   11034 O  O   . GLY   A 1 1386 ? -12.13100  31.02700  7.60900   1.000 46.09620  ?  1384 GLY   A O   1 
ATOM   11035 N  N   . ALA   A 1 1387 ? -11.46900  30.81400  5.46700   1.000 58.22901  ?  1385 ALA   A N   1 
ATOM   11036 C  CA  . ALA   A 1 1387 ? -12.79000  31.12100  4.93500   1.000 38.93531  ?  1385 ALA   A CA  1 
ATOM   11037 C  C   . ALA   A 1 1387 ? -13.79800  30.05300  5.34500   1.000 57.76621  ?  1385 ALA   A C   1 
ATOM   11038 O  O   . ALA   A 1 1387 ? -14.83800  30.35500  5.94100   1.000 51.83137  ?  1385 ALA   A O   1 
ATOM   11039 C  CB  . ALA   A 1 1387 ? -12.71500  31.25300  3.41300   1.000 33.03109  ?  1385 ALA   A CB  1 
ATOM   11040 N  N   . LEU   A 1 1388 ? -13.48900  28.78600  5.04500   1.000 49.97837  ?  1386 LEU   A N   1 
ATOM   11041 C  CA  . LEU   A 1 1388 ? -14.36600  27.68800  5.43900   1.000 45.97547  ?  1386 LEU   A CA  1 
ATOM   11042 C  C   . LEU   A 1 1388 ? -14.55900  27.64400  6.95100   1.000 44.65223  ?  1386 LEU   A C   1 
ATOM   11043 O  O   . LEU   A 1 1388 ? -15.66600  27.37700  7.43400   1.000 50.32590  ?  1386 LEU   A O   1 
ATOM   11044 C  CB  . LEU   A 1 1388 ? -13.79900  26.36200  4.93000   1.000 55.31634  ?  1386 LEU   A CB  1 
ATOM   11045 C  CG  . LEU   A 1 1388 ? -14.45600  25.06600  5.41600   1.000 60.01519  ?  1386 LEU   A CG  1 
ATOM   11046 C  CD1 . LEU   A 1 1388 ? -15.91800  24.99000  4.99600   1.000 53.95915  ?  1386 LEU   A CD1 1 
ATOM   11047 C  CD2 . LEU   A 1 1388 ? -13.68300  23.84700  4.91700   1.000 54.84015  ?  1386 LEU   A CD2 1 
ATOM   11048 N  N   . LEU   A 1 1389 ? -13.49500  27.91100  7.71300   1.000 39.01311  ?  1387 LEU   A N   1 
ATOM   11049 C  CA  . LEU   A 1 1389 ? -13.59100  27.85400  9.16900   1.000 56.37066  ?  1387 LEU   A CA  1 
ATOM   11050 C  C   . LEU   A 1 1389 ? -14.63000  28.83500  9.69200   1.000 53.41641  ?  1387 LEU   A C   1 
ATOM   11051 O  O   . LEU   A 1 1389 ? -15.38700  28.51800  10.61800  1.000 52.56833  ?  1387 LEU   A O   1 
ATOM   11052 C  CB  . LEU   A 1 1389 ? -12.22800  28.14600  9.79800   1.000 50.03561  ?  1387 LEU   A CB  1 
ATOM   11053 C  CG  . LEU   A 1 1389 ? -11.24700  26.99300  10.00100  1.000 58.73849  ?  1387 LEU   A CG  1 
ATOM   11054 C  CD1 . LEU   A 1 1389 ? -10.01800  27.48500  10.74100  1.000 72.67965  ?  1387 LEU   A CD1 1 
ATOM   11055 C  CD2 . LEU   A 1 1389 ? -11.90100  25.86200  10.76900  1.000 66.43743  ?  1387 LEU   A CD2 1 
ATOM   11056 N  N   . ASN   A 1 1390 ? -14.68600  30.02900  9.10000   1.000 53.47177  ?  1388 ASN   A N   1 
ATOM   11057 C  CA  . ASN   A 1 1390 ? -15.57600  31.07500  9.59200   1.000 50.91776  ?  1388 ASN   A CA  1 
ATOM   11058 C  C   . ASN   A 1 1390 ? -17.03900  30.67000  9.44200   1.000 50.88422  ?  1388 ASN   A C   1 
ATOM   11059 O  O   . ASN   A 1 1390 ? -17.84300  30.84400  10.36500  1.000 41.80837  ?  1388 ASN   A O   1 
ATOM   11060 C  CB  . ASN   A 1 1390 ? -15.28700  32.37900  8.84800   1.000 46.19875  ?  1388 ASN   A CB  1 
ATOM   11061 C  CG  . ASN   A 1 1390 ? -16.20300  33.50500  9.26300   1.000 50.06906  ?  1388 ASN   A CG  1 
ATOM   11062 O  OD1 . ASN   A 1 1390 ? -16.01300  34.11500  10.31400  1.000 39.46010  ?  1388 ASN   A OD1 1 
ATOM   11063 N  ND2 . ASN   A 1 1390 ? -17.19900  33.79700  8.43400   1.000 57.02839  ?  1388 ASN   A ND2 1 
ATOM   11064 N  N   . VAL   A 1 1391 ? -17.39700  30.11300  8.28400   1.000 39.07066  ?  1389 VAL   A N   1 
ATOM   11065 C  CA  . VAL   A 1 1391 ? -18.77500  29.68700  8.05500   1.000 43.05470  ?  1389 VAL   A CA  1 
ATOM   11066 C  C   . VAL   A 1 1391 ? -19.13700  28.54500  8.99000   1.000 50.83420  ?  1389 VAL   A C   1 
ATOM   11067 O  O   . VAL   A 1 1391 ? -20.22600  28.51800  9.57600   1.000 58.74214  ?  1389 VAL   A O   1 
ATOM   11068 C  CB  . VAL   A 1 1391 ? -18.96500  29.28400  6.58500   1.000 46.03785  ?  1389 VAL   A CB  1 
ATOM   11069 C  CG1 . VAL   A 1 1391 ? -20.43100  29.35900  6.19400   1.000 59.93087  ?  1389 VAL   A CG1 1 
ATOM   11070 C  CG2 . VAL   A 1 1391 ? -18.12400  30.16600  5.72300   1.000 52.46389  ?  1389 VAL   A CG2 1 
ATOM   11071 N  N   . LEU   A 1 1392 ? -18.23000  27.57600  9.13100   1.000 44.57288  ?  1390 LEU   A N   1 
ATOM   11072 C  CA  . LEU   A 1 1392 ? -18.47500  26.45600  10.03200  1.000 50.31754  ?  1390 LEU   A CA  1 
ATOM   11073 C  C   . LEU   A 1 1392 ? -18.67100  26.94200  11.46100  1.000 50.16248  ?  1390 LEU   A C   1 
ATOM   11074 O  O   . LEU   A 1 1392 ? -19.60900  26.52400  12.15100  1.000 54.20917  ?  1390 LEU   A O   1 
ATOM   11075 C  CB  . LEU   A 1 1392 ? -17.31600  25.46200  9.95500   1.000 56.65861  ?  1390 LEU   A CB  1 
ATOM   11076 C  CG  . LEU   A 1 1392 ? -17.10100  24.75400  8.61700   1.000 55.72603  ?  1390 LEU   A CG  1 
ATOM   11077 C  CD1 . LEU   A 1 1392 ? -15.78700  23.98600  8.62500   1.000 54.89793  ?  1390 LEU   A CD1 1 
ATOM   11078 C  CD2 . LEU   A 1 1392 ? -18.26600  23.83100  8.30800   1.000 45.37534  ?  1390 LEU   A CD2 1 
ATOM   11079 N  N   . HIS   A 1 1393 ? -17.79300  27.83700  11.92100  1.000 39.22465  ?  1391 HIS   A N   1 
ATOM   11080 C  CA  . HIS   A 1 1393 ? -17.92800  28.37400  13.27000  1.000 62.92735  ?  1391 HIS   A CA  1 
ATOM   11081 C  C   . HIS   A 1 1393 ? -19.20700  29.18800  13.41000  1.000 67.55244  ?  1391 HIS   A C   1 
ATOM   11082 O  O   . HIS   A 1 1393 ? -19.88200  29.12500  14.44600  1.000 70.37122  ?  1391 HIS   A O   1 
ATOM   11083 C  CB  . HIS   A 1 1393 ? -16.70700  29.22400  13.62100  1.000 57.40837  ?  1391 HIS   A CB  1 
ATOM   11084 C  CG  . HIS   A 1 1393 ? -15.49100  28.42500  13.97300  1.000 60.50994  ?  1391 HIS   A CG  1 
ATOM   11085 N  ND1 . HIS   A 1 1393 ? -15.44300  27.58200  15.06300  1.000 62.02089  ?  1391 HIS   A ND1 1 
ATOM   11086 C  CD2 . HIS   A 1 1393 ? -14.27600  28.34300  13.38000  1.000 70.52924  ?  1391 HIS   A CD2 1 
ATOM   11087 C  CE1 . HIS   A 1 1393 ? -14.25100  27.01400  15.12500  1.000 78.16962  ?  1391 HIS   A CE1 1 
ATOM   11088 N  NE2 . HIS   A 1 1393 ? -13.52500  27.45800  14.11500  1.000 73.88483  ?  1391 HIS   A NE2 1 
ATOM   11089 N  N   . GLY   A 1 1394 ? -19.56100  29.95100  12.37500  1.000 51.13001  ?  1392 GLY   A N   1 
ATOM   11090 C  CA  . GLY   A 1 1394 ? -20.75800  30.77100  12.45100  1.000 51.56509  ?  1392 GLY   A CA  1 
ATOM   11091 C  C   . GLY   A 1 1394 ? -22.03100  29.95200  12.38900  1.000 60.68973  ?  1392 GLY   A C   1 
ATOM   11092 O  O   . GLY   A 1 1394 ? -22.99500  30.22800  13.11000  1.000 52.32781  ?  1392 GLY   A O   1 
ATOM   11093 N  N   . MET   A 1 1395 ? -22.05500  28.93300  11.52700  1.000 61.81409  ?  1393 MET   A N   1 
ATOM   11094 C  CA  . MET   A 1 1395 ? -23.20900  28.04400  11.46400  1.000 54.12022  ?  1393 MET   A CA  1 
ATOM   11095 C  C   . MET   A 1 1395 ? -23.36700  27.24600  12.75200  1.000 59.72042  ?  1393 MET   A C   1 
ATOM   11096 O  O   . MET   A 1 1395 ? -24.49500  26.94300  13.15900  1.000 67.34383  ?  1393 MET   A O   1 
ATOM   11097 C  CB  . MET   A 1 1395 ? -23.08000  27.10700  10.26300  1.000 39.03095  ?  1393 MET   A CB  1 
ATOM   11098 C  CG  . MET   A 1 1395 ? -23.64000  27.66900  8.96100   1.000 52.94878  ?  1393 MET   A CG  1 
ATOM   11099 S  SD  . MET   A 1 1395 ? -25.23700  28.46400  9.20600   1.000 64.37745  ?  1393 MET   A SD  1 
ATOM   11100 C  CE  . MET   A 1 1395 ? -26.19700  27.73200  7.88700   1.000 54.78733  ?  1393 MET   A CE  1 
ATOM   11101 N  N   . GLN   A 1 1396 ? -22.25100  26.90200  13.40500  1.000 59.67110  ?  1394 GLN   A N   1 
ATOM   11102 C  CA  . GLN   A 1 1396 ? -22.32400  26.22100  14.69500  1.000 67.73738  ?  1394 GLN   A CA  1 
ATOM   11103 C  C   . GLN   A 1 1396 ? -22.86700  27.14300  15.78000  1.000 68.82800  ?  1394 GLN   A C   1 
ATOM   11104 O  O   . GLN   A 1 1396 ? -23.62700  26.70300  16.65100  1.000 78.03118  ?  1394 GLN   A O   1 
ATOM   11105 C  CB  . GLN   A 1 1396 ? -20.94800  25.68100  15.09000  1.000 59.69995  ?  1394 GLN   A CB  1 
ATOM   11106 C  CG  . GLN   A 1 1396 ? -20.99300  24.73000  16.27500  1.000 59.74386  ?  1394 GLN   A CG  1 
ATOM   11107 C  CD  . GLN   A 1 1396 ? -21.30400  23.30500  15.87900  1.000 68.81908  ?  1394 GLN   A CD  1 
ATOM   11108 O  OE1 . GLN   A 1 1396 ? -22.01700  23.05400  14.90700  1.000 68.34757  ?  1394 GLN   A OE1 1 
ATOM   11109 N  NE2 . GLN   A 1 1396 ? -20.77900  22.35800  16.64300  1.000 84.82783  ?  1394 GLN   A NE2 1 
ATOM   11110 N  N   . ASP   A 1 1397 ? -22.48600  28.42200  15.74700  1.000 69.89359  ?  1395 ASP   A N   1 
ATOM   11111 C  CA  . ASP   A 1 1397 ? -23.05500  29.38900  16.67700  1.000 66.10638  ?  1395 ASP   A CA  1 
ATOM   11112 C  C   . ASP   A 1 1397 ? -24.57000  29.48700  16.52600  1.000 64.82497  ?  1395 ASP   A C   1 
ATOM   11113 O  O   . ASP   A 1 1397 ? -25.27300  29.73600  17.51100  1.000 67.60441  ?  1395 ASP   A O   1 
ATOM   11114 C  CB  . ASP   A 1 1397 ? -22.42000  30.76000  16.45700  1.000 69.92791  ?  1395 ASP   A CB  1 
ATOM   11115 C  CG  . ASP   A 1 1397 ? -20.99400  30.82600  16.93700  1.000 84.07300  ?  1395 ASP   A CG  1 
ATOM   11116 O  OD1 . ASP   A 1 1397 ? -20.44100  29.77900  17.33500  1.000 93.64380  ?  1395 ASP   A OD1 1 
ATOM   11117 O  OD2 . ASP   A 1 1397 ? -20.43000  31.93800  16.92000  1.000 75.62397  -1 1395 ASP   A OD2 1 
ATOM   11118 N  N   . GLU   A 1 1398 ? -25.09100  29.27900  15.31500  1.000 59.17373  ?  1396 GLU   A N   1 
ATOM   11119 C  CA  . GLU   A 1 1398 ? -26.51800  29.41900  15.03900  1.000 74.43502  ?  1396 GLU   A CA  1 
ATOM   11120 C  C   . GLU   A 1 1398 ? -27.26800  28.10200  15.22700  1.000 74.48051  ?  1396 GLU   A C   1 
ATOM   11121 O  O   . GLU   A 1 1398 ? -28.31700  28.05800  15.88000  1.000 88.40560  ?  1396 GLU   A O   1 
ATOM   11122 C  CB  . GLU   A 1 1398 ? -26.70500  29.94700  13.61200  1.000 88.88592  ?  1396 GLU   A CB  1 
ATOM   11123 C  CG  . GLU   A 1 1398 ? -26.02800  31.27900  13.43100  1.000 88.49022  ?  1396 GLU   A CG  1 
ATOM   11124 C  CD  . GLU   A 1 1398 ? -26.35800  32.28400  14.56300  1.000 98.02919  ?  1396 GLU   A CD  1 
ATOM   11125 O  OE1 . GLU   A 1 1398 ? -27.51500  32.30500  15.07100  1.000 85.66340  ?  1396 GLU   A OE1 1 
ATOM   11126 O  OE2 . GLU   A 1 1398 ? -25.45300  33.07600  14.93000  1.000 107.37145 -1 1396 GLU   A OE2 1 
ATOM   11127 N  N   . TYR   A 1 1399 ? -26.75400  27.02200  14.64800  1.000 69.75867  ?  1397 TYR   A N   1 
ATOM   11128 C  CA  . TYR   A 1 1399 ? -27.36700  25.70000  14.76600  1.000 64.66940  ?  1397 TYR   A CA  1 
ATOM   11129 C  C   . TYR   A 1 1399 ? -26.28500  24.76400  15.27900  1.000 70.88952  ?  1397 TYR   A C   1 
ATOM   11130 O  O   . TYR   A 1 1399 ? -25.59200  24.10600  14.49000  1.000 72.75146  ?  1397 TYR   A O   1 
ATOM   11131 C  CB  . TYR   A 1 1399 ? -27.94000  25.23600  13.42900  1.000 71.21928  ?  1397 TYR   A CB  1 
ATOM   11132 C  CG  . TYR   A 1 1399 ? -28.51700  26.38900  12.63200  1.000 76.78352  ?  1397 TYR   A CG  1 
ATOM   11133 C  CD1 . TYR   A 1 1399 ? -29.67800  27.03800  13.04400  1.000 63.58351  ?  1397 TYR   A CD1 1 
ATOM   11134 C  CD2 . TYR   A 1 1399 ? -27.88500  26.85100  11.48400  1.000 70.34345  ?  1397 TYR   A CD2 1 
ATOM   11135 C  CE1 . TYR   A 1 1399 ? -30.20200  28.10400  12.31700  1.000 63.93987  ?  1397 TYR   A CE1 1 
ATOM   11136 C  CE2 . TYR   A 1 1399 ? -28.40500  27.91200  10.75100  1.000 65.96541  ?  1397 TYR   A CE2 1 
ATOM   11137 C  CZ  . TYR   A 1 1399 ? -29.56200  28.53600  11.17400  1.000 67.71700  ?  1397 TYR   A CZ  1 
ATOM   11138 O  OH  . TYR   A 1 1399 ? -30.08300  29.59600  10.46300  1.000 58.52641  ?  1397 TYR   A OH  1 
ATOM   11139 N  N   . PRO   A 1 1400 ? -26.09200  24.69700  16.59500  1.000 76.72563  ?  1398 PRO   A N   1 
ATOM   11140 C  CA  . PRO   A 1 1400 ? -24.96600  23.92600  17.13300  1.000 73.43522  ?  1398 PRO   A CA  1 
ATOM   11141 C  C   . PRO   A 1 1400 ? -25.20900  22.42900  17.01600  1.000 75.27068  ?  1398 PRO   A C   1 
ATOM   11142 O  O   . PRO   A 1 1400 ? -26.23800  21.91200  17.45700  1.000 68.74249  ?  1398 PRO   A O   1 
ATOM   11143 C  CB  . PRO   A 1 1400 ? -24.88900  24.38200  18.59500  1.000 67.39315  ?  1398 PRO   A CB  1 
ATOM   11144 C  CG  . PRO   A 1 1400 ? -26.27800  24.81300  18.92000  1.000 71.59962  ?  1398 PRO   A CG  1 
ATOM   11145 C  CD  . PRO   A 1 1400 ? -26.85700  25.37900  17.65200  1.000 69.40499  ?  1398 PRO   A CD  1 
ATOM   11146 N  N   . LEU   A 1 1401 ? -24.25800  21.74300  16.39000  1.000 81.80426  ?  1399 LEU   A N   1 
ATOM   11147 C  CA  . LEU   A 1 1401 ? -24.22300  20.28700  16.35400  1.000 67.96784  ?  1399 LEU   A CA  1 
ATOM   11148 C  C   . LEU   A 1 1401 ? -23.26600  19.84200  17.45200  1.000 69.30910  ?  1399 LEU   A C   1 
ATOM   11149 O  O   . LEU   A 1 1401 ? -22.05000  20.01900  17.33300  1.000 66.29559  ?  1399 LEU   A O   1 
ATOM   11150 C  CB  . LEU   A 1 1401 ? -23.77500  19.78100  14.98400  1.000 71.30753  ?  1399 LEU   A CB  1 
ATOM   11151 C  CG  . LEU   A 1 1401 ? -24.12800  18.34300  14.59800  1.000 65.76477  ?  1399 LEU   A CG  1 
ATOM   11152 C  CD1 . LEU   A 1 1401 ? -24.16800  18.20700  13.08200  1.000 50.68046  ?  1399 LEU   A CD1 1 
ATOM   11153 C  CD2 . LEU   A 1 1401 ? -23.15100  17.34500  15.20100  1.000 57.28919  ?  1399 LEU   A CD2 1 
ATOM   11154 N  N   . LEU   A 1 1402 ? -23.81500  19.28500  18.52400  1.000 70.45705  ?  1400 LEU   A N   1 
ATOM   11155 C  CA  . LEU   A 1 1402 ? -23.01300  18.87000  19.66300  1.000 66.94491  ?  1400 LEU   A CA  1 
ATOM   11156 C  C   . LEU   A 1 1402 ? -22.63500  17.39600  19.51400  1.000 78.08477  ?  1400 LEU   A C   1 
ATOM   11157 O  O   . LEU   A 1 1402 ? -22.83300  16.78200  18.46200  1.000 83.91901  ?  1400 LEU   A O   1 
ATOM   11158 C  CB  . LEU   A 1 1402 ? -23.76600  19.16100  20.95900  1.000 77.43568  ?  1400 LEU   A CB  1 
ATOM   11159 C  CG  . LEU   A 1 1402 ? -24.13400  20.63700  21.14900  1.000 83.09659  ?  1400 LEU   A CG  1 
ATOM   11160 C  CD1 . LEU   A 1 1402 ? -25.19700  20.81500  22.22800  1.000 62.57559  ?  1400 LEU   A CD1 1 
ATOM   11161 C  CD2 . LEU   A 1 1402 ? -22.89400  21.46800  21.46000  1.000 47.22288  ?  1400 LEU   A CD2 1 
ATOM   11162 N  N   . GLN   A 1 1403 ? -22.07700  16.81300  20.57800  1.000 78.58691  ?  1401 GLN   A N   1 
ATOM   11163 C  CA  . GLN   A 1 1403 ? -21.59100  15.43800  20.50600  1.000 72.65481  ?  1401 GLN   A CA  1 
ATOM   11164 C  C   . GLN   A 1 1403 ? -22.72900  14.45300  20.26400  1.000 74.23521  ?  1401 GLN   A C   1 
ATOM   11165 O  O   . GLN   A 1 1403 ? -22.58900  13.51400  19.47100  1.000 76.47968  ?  1401 GLN   A O   1 
ATOM   11166 C  CB  . GLN   A 1 1403 ? -20.83900  15.08900  21.79000  1.000 80.02559  ?  1401 GLN   A CB  1 
ATOM   11167 C  CG  . GLN   A 1 1403 ? -21.43200  15.72900  23.03700  1.000 86.45226  ?  1401 GLN   A CG  1 
ATOM   11168 C  CD  . GLN   A 1 1403 ? -20.49000  15.68800  24.22200  1.000 87.50705  ?  1401 GLN   A CD  1 
ATOM   11169 O  OE1 . GLN   A 1 1403 ? -19.27100  15.67000  24.06100  1.000 93.95399  ?  1401 GLN   A OE1 1 
ATOM   11170 N  NE2 . GLN   A 1 1403 ? -21.05300  15.67500  25.42500  1.000 89.93894  ?  1401 GLN   A NE2 1 
ATOM   11171 N  N   . ASP   A 1 1404 ? -23.86300  14.65100  20.93400  1.000 65.08165  ?  1402 ASP   A N   1 
ATOM   11172 C  CA  . ASP   A 1 1404 ? -25.01300  13.76500  20.80300  1.000 71.08320  ?  1402 ASP   A CA  1 
ATOM   11173 C  C   . ASP   A 1 1404 ? -25.86600  14.07400  19.57900  1.000 70.38660  ?  1402 ASP   A C   1 
ATOM   11174 O  O   . ASP   A 1 1404 ? -27.00200  13.59300  19.49900  1.000 74.63165  ?  1402 ASP   A O   1 
ATOM   11175 C  CB  . ASP   A 1 1404 ? -25.87700  13.83300  22.06600  1.000 76.51371  ?  1402 ASP   A CB  1 
ATOM   11176 C  CG  . ASP   A 1 1404 ? -25.09200  13.52800  23.32700  1.000 94.09345  ?  1402 ASP   A CG  1 
ATOM   11177 O  OD1 . ASP   A 1 1404 ? -23.84500  13.50700  23.26200  1.000 90.54202  ?  1402 ASP   A OD1 1 
ATOM   11178 O  OD2 . ASP   A 1 1404 ? -25.72200  13.30900  24.38400  1.000 99.96522  -1 1402 ASP   A OD2 1 
ATOM   11179 N  N   . ASP   A 1 1405 ? -25.35400  14.85300  18.63400  1.000 64.27446  ?  1403 ASP   A N   1 
ATOM   11180 C  CA  . ASP   A 1 1405 ? -26.09200  15.24900  17.44400  1.000 77.64648  ?  1403 ASP   A CA  1 
ATOM   11181 C  C   . ASP   A 1 1405 ? -25.44900  14.64700  16.20000  1.000 75.02529  ?  1403 ASP   A C   1 
ATOM   11182 O  O   . ASP   A 1 1405 ? -24.37300  14.04400  16.25400  1.000 72.77652  ?  1403 ASP   A O   1 
ATOM   11183 C  CB  . ASP   A 1 1405 ? -26.16200  16.77700  17.33700  1.000 74.34501  ?  1403 ASP   A CB  1 
ATOM   11184 C  CG  . ASP   A 1 1405 ? -26.83800  17.41300  18.53700  1.000 77.88955  ?  1403 ASP   A CG  1 
ATOM   11185 O  OD1 . ASP   A 1 1405 ? -27.75900  16.78700  19.10600  1.000 66.70329  ?  1403 ASP   A OD1 1 
ATOM   11186 O  OD2 . ASP   A 1 1405 ? -26.45600  18.54300  18.91100  1.000 83.04488  -1 1403 ASP   A OD2 1 
ATOM   11187 N  N   . ALA   A 1 1406 ? -26.12800  14.81700  15.06600  1.000 57.90500  ?  1404 ALA   A N   1 
ATOM   11188 C  CA  . ALA   A 1 1406 ? -25.69000  14.19200  13.82700  1.000 54.11743  ?  1404 ALA   A CA  1 
ATOM   11189 C  C   . ALA   A 1 1406 ? -26.15900  15.00600  12.63100  1.000 56.08584  ?  1404 ALA   A C   1 
ATOM   11190 O  O   . ALA   A 1 1406 ? -27.14500  15.74600  12.69900  1.000 60.76035  ?  1404 ALA   A O   1 
ATOM   11191 C  CB  . ALA   A 1 1406 ? -26.20800  12.75400  13.71000  1.000 58.65867  ?  1404 ALA   A CB  1 
ATOM   11192 N  N   . PHE   A 1 1407 ? -25.43200  14.84400  11.52800  1.000 56.71380  ?  1405 PHE   A N   1 
ATOM   11193 C  CA  . PHE   A 1 1407 ? -25.75600  15.42700  10.23700  1.000 55.23091  ?  1405 PHE   A CA  1 
ATOM   11194 C  C   . PHE   A 1 1407 ? -26.03600  14.30100  9.24900   1.000 57.60012  ?  1405 PHE   A C   1 
ATOM   11195 O  O   . PHE   A 1 1407 ? -25.69200  13.13900  9.48700   1.000 59.80439  ?  1405 PHE   A O   1 
ATOM   11196 C  CB  . PHE   A 1 1407 ? -24.60800  16.31800  9.73000   1.000 53.43970  ?  1405 PHE   A CB  1 
ATOM   11197 C  CG  . PHE   A 1 1407 ? -25.05700  17.63500  9.15300   1.000 61.33679  ?  1405 PHE   A CG  1 
ATOM   11198 C  CD1 . PHE   A 1 1407 ? -26.07100  17.69000  8.21100   1.000 67.24659  ?  1405 PHE   A CD1 1 
ATOM   11199 C  CD2 . PHE   A 1 1407 ? -24.46200  18.82100  9.55700   1.000 51.78862  ?  1405 PHE   A CD2 1 
ATOM   11200 C  CE1 . PHE   A 1 1407 ? -26.48400  18.90100  7.68200   1.000 64.64198  ?  1405 PHE   A CE1 1 
ATOM   11201 C  CE2 . PHE   A 1 1407 ? -24.87000  20.03400  9.03400   1.000 35.24947  ?  1405 PHE   A CE2 1 
ATOM   11202 C  CZ  . PHE   A 1 1407 ? -25.88200  20.07400  8.09500   1.000 51.32732  ?  1405 PHE   A CZ  1 
ATOM   11203 N  N   . LEU   A 1 1408 ? -26.67500  14.64700  8.13700   1.000 46.90909  ?  1406 LEU   A N   1 
ATOM   11204 C  CA  . LEU   A 1 1408 ? -26.99600  13.69400  7.08200   1.000 48.76494  ?  1406 LEU   A CA  1 
ATOM   11205 C  C   . LEU   A 1 1408 ? -26.33400  14.13700  5.78600   1.000 53.17392  ?  1406 LEU   A C   1 
ATOM   11206 O  O   . LEU   A 1 1408 ? -26.59900  15.24000  5.29500   1.000 60.78822  ?  1406 LEU   A O   1 
ATOM   11207 C  CB  . LEU   A 1 1408 ? -28.51100  13.55500  6.90600   1.000 53.28159  ?  1406 LEU   A CB  1 
ATOM   11208 C  CG  . LEU   A 1 1408 ? -28.96300  12.53400  5.85400   1.000 53.51168  ?  1406 LEU   A CG  1 
ATOM   11209 C  CD1 . LEU   A 1 1408 ? -28.82000  11.10500  6.33400   1.000 52.37351  ?  1406 LEU   A CD1 1 
ATOM   11210 C  CD2 . LEU   A 1 1408 ? -30.40800  12.79800  5.43700   1.000 59.35433  ?  1406 LEU   A CD2 1 
ATOM   11211 N  N   . LEU   A 1 1409 ? -25.47000  13.28400  5.24200   1.000 43.91720  ?  1407 LEU   A N   1 
ATOM   11212 C  CA  . LEU   A 1 1409 ? -24.80000  13.55900  3.97300   1.000 42.11328  ?  1407 LEU   A CA  1 
ATOM   11213 C  C   . LEU   A 1 1409 ? -25.73200  13.15900  2.83900   1.000 50.98602  ?  1407 LEU   A C   1 
ATOM   11214 O  O   . LEU   A 1 1409 ? -25.82800  11.98200  2.48400   1.000 53.16674  ?  1407 LEU   A O   1 
ATOM   11215 C  CB  . LEU   A 1 1409 ? -23.47600  12.80900  3.88800   1.000 47.84549  ?  1407 LEU   A CB  1 
ATOM   11216 C  CG  . LEU   A 1 1409 ? -22.54700  13.21100  2.74000   1.000 33.02796  ?  1407 LEU   A CG  1 
ATOM   11217 C  CD1 . LEU   A 1 1409 ? -22.16500  14.67200  2.84800   1.000 40.77966  ?  1407 LEU   A CD1 1 
ATOM   11218 C  CD2 . LEU   A 1 1409 ? -21.31100  12.33300  2.73000   1.000 47.37351  ?  1407 LEU   A CD2 1 
ATOM   11219 N  N   . LYS   A 1 1410 ? -26.42100  14.14300  2.26000   1.000 52.74870  ?  1408 LYS   A N   1 
ATOM   11220 C  CA  . LYS   A 1 1410 ? -27.38200  13.89400  1.19100   1.000 46.64405  ?  1408 LYS   A CA  1 
ATOM   11221 C  C   . LYS   A 1 1410 ? -27.21000  14.79500  -0.02000  1.000 49.19917  ?  1408 LYS   A C   1 
ATOM   11222 O  O   . LYS   A 1 1410 ? -27.76200  14.47500  -1.08100  1.000 51.17881  ?  1408 LYS   A O   1 
ATOM   11223 C  CB  . LYS   A 1 1410 ? -28.81800  14.04500  1.71700   1.000 46.43919  ?  1408 LYS   A CB  1 
ATOM   11224 C  CG  . LYS   A 1 1410 ? -29.09900  15.39000  2.36900   1.000 51.68312  ?  1408 LYS   A CG  1 
ATOM   11225 C  CD  . LYS   A 1 1410 ? -30.48900  15.44000  2.99300   1.000 62.36008  ?  1408 LYS   A CD  1 
ATOM   11226 C  CE  . LYS   A 1 1410 ? -31.58400  15.25900  1.95100   1.000 44.57205  ?  1408 LYS   A CE  1 
ATOM   11227 N  NZ  . LYS   A 1 1410 ? -31.60900  16.37700  0.96800   1.000 55.86268  ?  1408 LYS   A NZ  1 
ATOM   11228 N  N   . THR   A 1 1411 ? -26.47900  15.89900  0.09300   1.000 58.30046  ?  1409 THR   A N   1 
ATOM   11229 C  CA  . THR   A 1 1411 ? -26.24500  16.79500  -1.02900  1.000 57.25305  ?  1409 THR   A CA  1 
ATOM   11230 C  C   . THR   A 1 1411 ? -25.04600  16.31100  -1.83200  1.000 52.14113  ?  1409 THR   A C   1 
ATOM   11231 O  O   . THR   A 1 1411 ? -24.03000  15.90000  -1.26300  1.000 60.63681  ?  1409 THR   A O   1 
ATOM   11232 C  CB  . THR   A 1 1411 ? -26.00300  18.22100  -0.53600  1.000 47.95268  ?  1409 THR   A CB  1 
ATOM   11233 O  OG1 . THR   A 1 1411 ? -26.95400  18.54000  0.48700   1.000 54.05824  ?  1409 THR   A OG1 1 
ATOM   11234 C  CG2 . THR   A 1 1411 ? -26.15400  19.20900  -1.68000  1.000 48.65556  ?  1409 THR   A CG2 1 
ATOM   11235 N  N   . THR   A 1 1412 ? -25.17100  16.35800  -3.15700  1.000 39.48198  ?  1410 THR   A N   1 
ATOM   11236 C  CA  . THR   A 1 1412 ? -24.09800  15.88700  -4.02000  1.000 50.52030  ?  1410 THR   A CA  1 
ATOM   11237 C  C   . THR   A 1 1412 ? -22.84800  16.73100  -3.80800  1.000 60.44261  ?  1410 THR   A C   1 
ATOM   11238 O  O   . THR   A 1 1412 ? -22.91800  17.95700  -3.68800  1.000 69.16360  ?  1410 THR   A O   1 
ATOM   11239 C  CB  . THR   A 1 1412 ? -24.53400  15.93100  -5.48400  1.000 55.88125  ?  1410 THR   A CB  1 
ATOM   11240 O  OG1 . THR   A 1 1412 ? -25.76100  15.20700  -5.62600  1.000 87.39515  ?  1410 THR   A OG1 1 
ATOM   11241 C  CG2 . THR   A 1 1412 ? -23.48900  15.27400  -6.36900  1.000 59.20339  ?  1410 THR   A CG2 1 
ATOM   11242 N  N   . TYR   A 1 1413 ? -21.69900  16.06700  -3.75300  1.000 57.73764  ?  1411 TYR   A N   1 
ATOM   11243 C  CA  . TYR   A 1 1413 ? -20.49300  16.77300  -3.34100  1.000 55.54480  ?  1411 TYR   A CA  1 
ATOM   11244 C  C   . TYR   A 1 1413 ? -19.94500  17.73400  -4.41500  1.000 58.73749  ?  1411 TYR   A C   1 
ATOM   11245 O  O   . TYR   A 1 1413 ? -18.86900  18.30200  -4.18200  1.000 46.12707  ?  1411 TYR   A O   1 
ATOM   11246 C  CB  . TYR   A 1 1413 ? -19.43200  15.75600  -2.89000  1.000 48.59631  ?  1411 TYR   A CB  1 
ATOM   11247 C  CG  . TYR   A 1 1413 ? -18.64300  15.02600  -3.97000  1.000 52.77808  ?  1411 TYR   A CG  1 
ATOM   11248 C  CD1 . TYR   A 1 1413 ? -19.15300  14.83600  -5.25100  1.000 49.23115  ?  1411 TYR   A CD1 1 
ATOM   11249 C  CD2 . TYR   A 1 1413 ? -17.38300  14.50700  -3.68700  1.000 52.47233  ?  1411 TYR   A CD2 1 
ATOM   11250 C  CE1 . TYR   A 1 1413 ? -18.42100  14.17000  -6.22100  1.000 55.94792  ?  1411 TYR   A CE1 1 
ATOM   11251 C  CE2 . TYR   A 1 1413 ? -16.64700  13.83800  -4.64800  1.000 54.78341  ?  1411 TYR   A CE2 1 
ATOM   11252 C  CZ  . TYR   A 1 1413 ? -17.17100  13.67300  -5.91200  1.000 62.18402  ?  1411 TYR   A CZ  1 
ATOM   11253 O  OH  . TYR   A 1 1413 ? -16.44200  13.00800  -6.87200  1.000 60.57119  ?  1411 TYR   A OH  1 
ATOM   11254 N  N   . ILE   A 1 1414 ? -20.63000  17.95200  -5.54000  1.000 51.45802  ?  1412 ILE   A N   1 
ATOM   11255 C  CA  . ILE   A 1 1414 ? -20.20500  18.95600  -6.51000  1.000 59.85665  ?  1412 ILE   A CA  1 
ATOM   11256 C  C   . ILE   A 1 1414 ? -20.93400  20.26200  -6.22300  1.000 59.59881  ?  1412 ILE   A C   1 
ATOM   11257 O  O   . ILE   A 1 1414 ? -20.81300  21.23300  -6.97800  1.000 54.88036  ?  1412 ILE   A O   1 
ATOM   11258 C  CB  . ILE   A 1 1414 ? -20.45100  18.49700  -7.95800  1.000 57.70213  ?  1412 ILE   A CB  1 
ATOM   11259 C  CG1 . ILE   A 1 1414 ? -21.82100  17.83000  -8.08800  1.000 50.07907  ?  1412 ILE   A CG1 1 
ATOM   11260 C  CG2 . ILE   A 1 1414 ? -19.33600  17.57000  -8.41500  1.000 52.39474  ?  1412 ILE   A CG2 1 
ATOM   11261 C  CD1 . ILE   A 1 1414 ? -22.36900  17.83700  -9.49700  1.000 42.35017  ?  1412 ILE   A CD1 1 
ATOM   11262 N  N   . PHE   A 1 1415 ? -21.69600  20.28900  -5.13300  1.000 51.82796  ?  1413 PHE   A N   1 
ATOM   11263 C  CA  . PHE   A 1 1415 ? -22.38100  21.48600  -4.66800  1.000 50.20963  ?  1413 PHE   A CA  1 
ATOM   11264 C  C   . PHE   A 1 1415 ? -21.83900  21.86800  -3.29600  1.000 54.44273  ?  1413 PHE   A C   1 
ATOM   11265 O  O   . PHE   A 1 1415 ? -21.58600  20.99800  -2.45600  1.000 51.67128  ?  1413 PHE   A O   1 
ATOM   11266 C  CB  . PHE   A 1 1415 ? -23.89700  21.26800  -4.60300  1.000 54.00153  ?  1413 PHE   A CB  1 
ATOM   11267 C  CG  . PHE   A 1 1415 ? -24.52300  20.96700  -5.93700  1.000 79.28071  ?  1413 PHE   A CG  1 
ATOM   11268 C  CD1 . PHE   A 1 1415 ? -23.93100  21.40400  -7.11200  1.000 76.96534  ?  1413 PHE   A CD1 1 
ATOM   11269 C  CD2 . PHE   A 1 1415 ? -25.70100  20.23900  -6.01700  1.000 85.45104  ?  1413 PHE   A CD2 1 
ATOM   11270 C  CE1 . PHE   A 1 1415 ? -24.50300  21.12700  -8.34200  1.000 86.77729  ?  1413 PHE   A CE1 1 
ATOM   11271 C  CE2 . PHE   A 1 1415 ? -26.27900  19.96000  -7.24400  1.000 83.25744  ?  1413 PHE   A CE2 1 
ATOM   11272 C  CZ  . PHE   A 1 1415 ? -25.67900  20.40300  -8.40700  1.000 82.94099  ?  1413 PHE   A CZ  1 
ATOM   11273 N  N   . ASP   A 1 1416 ? -21.66900  23.17500  -3.07200  1.000 62.53967  ?  1414 ASP   A N   1 
ATOM   11274 C  CA  . ASP   A 1 1416 ? -20.99500  23.64500  -1.86500  1.000 54.41349  ?  1414 ASP   A CA  1 
ATOM   11275 C  C   . ASP   A 1 1416 ? -21.76700  23.32600  -0.58900  1.000 52.14041  ?  1414 ASP   A C   1 
ATOM   11276 O  O   . ASP   A 1 1416 ? -21.15400  23.26000  0.48100   1.000 59.99380  ?  1414 ASP   A O   1 
ATOM   11277 C  CB  . ASP   A 1 1416 ? -20.73200  25.15500  -1.95300  1.000 47.55534  ?  1414 ASP   A CB  1 
ATOM   11278 C  CG  . ASP   A 1 1416 ? -21.99800  25.96500  -2.17600  1.000 78.40749  ?  1414 ASP   A CG  1 
ATOM   11279 O  OD1 . ASP   A 1 1416 ? -23.06400  25.35700  -2.40900  1.000 84.71750  ?  1414 ASP   A OD1 1 
ATOM   11280 O  OD2 . ASP   A 1 1416 ? -21.92600  27.21200  -2.11600  1.000 72.35675  -1 1414 ASP   A OD2 1 
ATOM   11281 N  N   . ILE   A 1 1417 ? -23.08600  23.12700  -0.67200  1.000 48.03933  ?  1415 ILE   A N   1 
ATOM   11282 C  CA  . ILE   A 1 1417 ? -23.86400  22.82000  0.52800   1.000 64.14691  ?  1415 ILE   A CA  1 
ATOM   11283 C  C   . ILE   A 1 1417 ? -23.34700  21.54500  1.18000   1.000 57.71325  ?  1415 ILE   A C   1 
ATOM   11284 O  O   . ILE   A 1 1417 ? -23.29900  21.43200  2.41300   1.000 56.26091  ?  1415 ILE   A O   1 
ATOM   11285 C  CB  . ILE   A 1 1417 ? -25.36500  22.72200  0.18400   1.000 59.35264  ?  1415 ILE   A CB  1 
ATOM   11286 C  CG1 . ILE   A 1 1417 ? -25.94400  24.11100  -0.09600  1.000 44.55185  ?  1415 ILE   A CG1 1 
ATOM   11287 C  CG2 . ILE   A 1 1417 ? -26.15100  22.03900  1.30400   1.000 40.34288  ?  1415 ILE   A CG2 1 
ATOM   11288 C  CD1 . ILE   A 1 1417 ? -26.81500  24.17200  -1.33500  1.000 43.76181  ?  1415 ILE   A CD1 1 
ATOM   11289 N  N   . SER   A 1 1418 ? -22.91900  20.57800  0.36200   1.000 47.65735  ?  1416 SER   A N   1 
ATOM   11290 C  CA  . SER   A 1 1418 ? -22.40600  19.31800  0.89000   1.000 42.65682  ?  1416 SER   A CA  1 
ATOM   11291 C  C   . SER   A 1 1418 ? -21.23900  19.53900  1.84200   1.000 48.16649  ?  1416 SER   A C   1 
ATOM   11292 O  O   . SER   A 1 1418 ? -21.08100  18.78700  2.81100   1.000 53.69107  ?  1416 SER   A O   1 
ATOM   11293 C  CB  . SER   A 1 1418 ? -21.98600  18.40300  -0.26100  1.000 38.72548  ?  1416 SER   A CB  1 
ATOM   11294 O  OG  . SER   A 1 1418 ? -20.85700  18.92200  -0.94300  1.000 50.59927  ?  1416 SER   A OG  1 
ATOM   11295 N  N   . VAL   A 1 1419 ? -20.42400  20.56900  1.59400   1.000 50.37625  ?  1417 VAL   A N   1 
ATOM   11296 C  CA  . VAL   A 1 1419 ? -19.26900  20.83600  2.44800   1.000 44.33396  ?  1417 VAL   A CA  1 
ATOM   11297 C  C   . VAL   A 1 1419 ? -19.71200  21.10700  3.88000   1.000 43.74084  ?  1417 VAL   A C   1 
ATOM   11298 O  O   . VAL   A 1 1419 ? -19.03300  20.72000  4.83900   1.000 40.67161  ?  1417 VAL   A O   1 
ATOM   11299 C  CB  . VAL   A 1 1419 ? -18.44400  22.00800  1.88400   1.000 39.96374  ?  1417 VAL   A CB  1 
ATOM   11300 C  CG1 . VAL   A 1 1419 ? -17.14900  22.16600  2.65900   1.000 35.84113  ?  1417 VAL   A CG1 1 
ATOM   11301 C  CG2 . VAL   A 1 1419 ? -18.16600  21.80800  0.40400   1.000 39.83351  ?  1417 VAL   A CG2 1 
ATOM   11302 N  N   . ALA   A 1 1420 ? -20.85900  21.77300  4.04900   1.000 51.71075  ?  1418 ALA   A N   1 
ATOM   11303 C  CA  . ALA   A 1 1420 ? -21.36700  22.03900  5.39200   1.000 43.66161  ?  1418 ALA   A CA  1 
ATOM   11304 C  C   . ALA   A 1 1420 ? -21.75300  20.75300  6.11000   1.000 51.77922  ?  1418 ALA   A C   1 
ATOM   11305 O  O   . ALA   A 1 1420 ? -21.76700  20.71500  7.34400   1.000 50.62189  ?  1418 ALA   A O   1 
ATOM   11306 C  CB  . ALA   A 1 1420 ? -22.56300  22.98700  5.32700   1.000 42.25583  ?  1418 ALA   A CB  1 
ATOM   11307 N  N   . GLU   A 1 1421 ? -22.08100  19.70300  5.36100   1.000 53.77698  ?  1419 GLU   A N   1 
ATOM   11308 C  CA  . GLU   A 1 1421 ? -22.35900  18.39900  5.94800   1.000 55.45330  ?  1419 GLU   A CA  1 
ATOM   11309 C  C   . GLU   A 1 1421 ? -21.08300  17.59000  6.14700   1.000 49.07778  ?  1419 GLU   A C   1 
ATOM   11310 O  O   . GLU   A 1 1421 ? -20.96400  16.84900  7.13000   1.000 51.29700  ?  1419 GLU   A O   1 
ATOM   11311 C  CB  . GLU   A 1 1421 ? -23.34800  17.63300  5.06300   1.000 57.87397  ?  1419 GLU   A CB  1 
ATOM   11312 C  CG  . GLU   A 1 1421 ? -24.48700  18.50500  4.53700   1.000 60.50310  ?  1419 GLU   A CG  1 
ATOM   11313 C  CD  . GLU   A 1 1421 ? -25.31100  17.83900  3.44300   1.000 60.29582  ?  1419 GLU   A CD  1 
ATOM   11314 O  OE1 . GLU   A 1 1421 ? -24.73500  17.09900  2.61700   1.000 65.60402  ?  1419 GLU   A OE1 1 
ATOM   11315 O  OE2 . GLU   A 1 1421 ? -26.53800  18.07200  3.40000   1.000 51.38162  -1 1419 GLU   A OE2 1 
ATOM   11316 N  N   . ILE   A 1 1422 ? -20.12000  17.73900  5.23500   1.000 49.01915  ?  1420 ILE   A N   1 
ATOM   11317 C  CA  . ILE   A 1 1422 ? -18.86100  17.00600  5.33500   1.000 44.16289  ?  1420 ILE   A CA  1 
ATOM   11318 C  C   . ILE   A 1 1422 ? -18.09800  17.40800  6.59400   1.000 48.80819  ?  1420 ILE   A C   1 
ATOM   11319 O  O   . ILE   A 1 1422 ? -17.52900  16.55700  7.28800   1.000 45.34518  ?  1420 ILE   A O   1 
ATOM   11320 C  CB  . ILE   A 1 1422 ? -18.01800  17.22900  4.06600   1.000 31.10549  ?  1420 ILE   A CB  1 
ATOM   11321 C  CG1 . ILE   A 1 1422 ? -18.68900  16.57000  2.85600   1.000 36.60735  ?  1420 ILE   A CG1 1 
ATOM   11322 C  CG2 . ILE   A 1 1422 ? -16.60700  16.70700  4.26400   1.000 40.57909  ?  1420 ILE   A CG2 1 
ATOM   11323 C  CD1 . ILE   A 1 1422 ? -18.14800  17.03800  1.51800   1.000 38.27428  ?  1420 ILE   A CD1 1 
ATOM   11324 N  N   . PHE   A 1 1423 ? -18.08300  18.70300  6.91600   1.000 46.01900  ?  1421 PHE   A N   1 
ATOM   11325 C  CA  . PHE   A 1 1423 ? -17.29800  19.21800  8.03100   1.000 46.67855  ?  1421 PHE   A CA  1 
ATOM   11326 C  C   . PHE   A 1 1423 ? -18.14000  19.75900  9.18200   1.000 52.99021  ?  1421 PHE   A C   1 
ATOM   11327 O  O   . PHE   A 1 1423 ? -17.57300  20.14900  10.20900  1.000 56.86697  ?  1421 PHE   A O   1 
ATOM   11328 C  CB  . PHE   A 1 1423 ? -16.34700  20.32000  7.54300   1.000 41.16563  ?  1421 PHE   A CB  1 
ATOM   11329 C  CG  . PHE   A 1 1423 ? -15.38900  19.87200  6.47500   1.000 47.22915  ?  1421 PHE   A CG  1 
ATOM   11330 C  CD1 . PHE   A 1 1423 ? -14.37900  18.96900  6.76200   1.000 52.65337  ?  1421 PHE   A CD1 1 
ATOM   11331 C  CD2 . PHE   A 1 1423 ? -15.49200  20.36400  5.18300   1.000 47.08375  ?  1421 PHE   A CD2 1 
ATOM   11332 C  CE1 . PHE   A 1 1423 ? -13.49500  18.55900  5.77900   1.000 59.46797  ?  1421 PHE   A CE1 1 
ATOM   11333 C  CE2 . PHE   A 1 1423 ? -14.61200  19.95900  4.19600   1.000 47.28414  ?  1421 PHE   A CE2 1 
ATOM   11334 C  CZ  . PHE   A 1 1423 ? -13.61200  19.05600  4.49400   1.000 45.80220  ?  1421 PHE   A CZ  1 
ATOM   11335 N  N   . GLY   A 1 1424 ? -19.46600  19.79100  9.05300   1.000 41.77368  ?  1422 GLY   A N   1 
ATOM   11336 C  CA  . GLY   A 1 1424 ? -20.29900  20.41500  10.07100  1.000 38.32686  ?  1422 GLY   A CA  1 
ATOM   11337 C  C   . GLY   A 1 1424 ? -20.42800  19.63700  11.36400  1.000 49.87466  ?  1422 GLY   A C   1 
ATOM   11338 O  O   . GLY   A 1 1424 ? -20.91100  20.19500  12.35600  1.000 58.78300  ?  1422 GLY   A O   1 
ATOM   11339 N  N   . TRP   A 1 1425 ? -20.02100  18.37100  11.37900  1.000 58.70736  ?  1423 TRP   A N   1 
ATOM   11340 C  CA  . TRP   A 1 1425 ? -20.09300  17.56000  12.58700  1.000 49.86568  ?  1423 TRP   A CA  1 
ATOM   11341 C  C   . TRP   A 1 1425 ? -18.81500  17.61500  13.41000  1.000 61.51762  ?  1423 TRP   A C   1 
ATOM   11342 O  O   . TRP   A 1 1425 ? -18.83900  17.25400  14.59400  1.000 45.89560  ?  1423 TRP   A O   1 
ATOM   11343 C  CB  . TRP   A 1 1425 ? -20.39600  16.10600  12.21800  1.000 44.92691  ?  1423 TRP   A CB  1 
ATOM   11344 C  CG  . TRP   A 1 1425 ? -19.41000  15.54300  11.24200  1.000 54.38002  ?  1423 TRP   A CG  1 
ATOM   11345 C  CD1 . TRP   A 1 1425 ? -19.40900  15.71100  9.88600   1.000 44.32741  ?  1423 TRP   A CD1 1 
ATOM   11346 C  CD2 . TRP   A 1 1425 ? -18.26600  14.73700  11.54800  1.000 54.04184  ?  1423 TRP   A CD2 1 
ATOM   11347 N  NE1 . TRP   A 1 1425 ? -18.33900  15.05300  9.33000   1.000 38.17579  ?  1423 TRP   A NE1 1 
ATOM   11348 C  CE2 . TRP   A 1 1425 ? -17.62200  14.44600  10.32900  1.000 46.52809  ?  1423 TRP   A CE2 1 
ATOM   11349 C  CE3 . TRP   A 1 1425 ? -17.72600  14.22800  12.73400  1.000 54.40902  ?  1423 TRP   A CE3 1 
ATOM   11350 C  CZ2 . TRP   A 1 1425 ? -16.46500  13.67000  10.26100  1.000 48.93744  ?  1423 TRP   A CZ2 1 
ATOM   11351 C  CZ3 . TRP   A 1 1425 ? -16.57700  13.45800  12.66500  1.000 50.12331  ?  1423 TRP   A CZ3 1 
ATOM   11352 C  CH2 . TRP   A 1 1425 ? -15.96000  13.18600  11.43700  1.000 47.24174  ?  1423 TRP   A CH2 1 
ATOM   11353 N  N   . VAL   A 1 1426 ? -17.71300  18.06000  12.81300  1.000 55.19405  ?  1424 VAL   A N   1 
ATOM   11354 C  CA  . VAL   A 1 1426 ? -16.40100  18.09400  13.45600  1.000 54.10768  ?  1424 VAL   A CA  1 
ATOM   11355 C  C   . VAL   A 1 1426 ? -16.34100  19.10300  14.60200  1.000 59.06359  ?  1424 VAL   A C   1 
ATOM   11356 O  O   . VAL   A 1 1426 ? -15.80800  18.76200  15.66800  1.000 62.92908  ?  1424 VAL   A O   1 
ATOM   11357 C  CB  . VAL   A 1 1426 ? -15.29600  18.38200  12.42600  1.000 55.31618  ?  1424 VAL   A CB  1 
ATOM   11358 C  CG1 . VAL   A 1 1426 ? -13.94500  18.49800  13.11400  1.000 56.98927  ?  1424 VAL   A CG1 1 
ATOM   11359 C  CG2 . VAL   A 1 1426 ? -15.26700  17.29700  11.36300  1.000 54.03631  ?  1424 VAL   A CG2 1 
ATOM   11360 N  N   . PRO   A 1 1427 ? -16.84000  20.34200  14.44900  1.000 66.99075  ?  1425 PRO   A N   1 
ATOM   11361 C  CA  . PRO   A 1 1427 ? -16.67100  21.31900  15.54500  1.000 54.95367  ?  1425 PRO   A CA  1 
ATOM   11362 C  C   . PRO   A 1 1427 ? -17.21000  20.84500  16.88500  1.000 58.31539  ?  1425 PRO   A C   1 
ATOM   11363 O  O   . PRO   A 1 1427 ? -16.49300  20.90000  17.89200  1.000 66.40869  ?  1425 PRO   A O   1 
ATOM   11364 C  CB  . PRO   A 1 1427 ? -17.42600  22.54900  15.02400  1.000 62.80899  ?  1425 PRO   A CB  1 
ATOM   11365 C  CG  . PRO   A 1 1427 ? -17.32100  22.44400  13.55400  1.000 56.73024  ?  1425 PRO   A CG  1 
ATOM   11366 C  CD  . PRO   A 1 1427 ? -17.45400  20.97900  13.26600  1.000 65.53112  ?  1425 PRO   A CD  1 
ATOM   11367 N  N   . GLY   A 1 1428 ? -18.45400  20.37900  16.93100  1.000 76.44822  ?  1426 GLY   A N   1 
ATOM   11368 C  CA  . GLY   A 1 1428 ? -19.04300  19.88900  18.15900  1.000 69.88466  ?  1426 GLY   A CA  1 
ATOM   11369 C  C   . GLY   A 1 1428 ? -18.78000  18.43100  18.45700  1.000 69.62133  ?  1426 GLY   A C   1 
ATOM   11370 O  O   . GLY   A 1 1428 ? -19.34700  17.89700  19.41700  1.000 68.49815  ?  1426 GLY   A O   1 
ATOM   11371 N  N   . ARG   A 1 1429 ? -17.93700  17.77300  17.65900  1.000 67.82524  ?  1427 ARG   A N   1 
ATOM   11372 C  CA  . ARG   A 1 1429 ? -17.60100  16.36100  17.83700  1.000 72.61990  ?  1427 ARG   A CA  1 
ATOM   11373 C  C   . ARG   A 1 1429 ? -18.85400  15.48600  17.79300  1.000 72.26789  ?  1427 ARG   A C   1 
ATOM   11374 O  O   . ARG   A 1 1429 ? -19.10500  14.66800  18.68000  1.000 67.42378  ?  1427 ARG   A O   1 
ATOM   11375 C  CB  . ARG   A 1 1429 ? -16.81500  16.14100  19.13200  1.000 93.09742  ?  1427 ARG   A CB  1 
ATOM   11376 C  CG  . ARG   A 1 1429 ? -16.00900  14.85400  19.15400  1.000 98.13478  ?  1427 ARG   A CG  1 
ATOM   11377 C  CD  . ARG   A 1 1429 ? -15.20300  14.72100  20.43400  1.000 90.04662  ?  1427 ARG   A CD  1 
ATOM   11378 N  NE  . ARG   A 1 1429 ? -16.04400  14.47900  21.59900  1.000 89.40623  ?  1427 ARG   A NE  1 
ATOM   11379 C  CZ  . ARG   A 1 1429 ? -16.32500  15.38800  22.52200  1.000 90.79208  ?  1427 ARG   A CZ  1 
ATOM   11380 N  NH1 . ARG   A 1 1429 ? -15.85300  16.62200  22.44300  1.000 90.61894  ?  1427 ARG   A NH1 1 
ATOM   11381 N  NH2 . ARG   A 1 1429 ? -17.09800  15.05000  23.55100  1.000 83.57642  ?  1427 ARG   A NH2 1 
ATOM   11382 N  N   . GLY   A 1 1430 ? -19.64800  15.66800  16.74100  1.000 64.87103  ?  1428 GLY   A N   1 
ATOM   11383 C  CA  . GLY   A 1 1430 ? -20.82600  14.84800  16.54100  1.000 66.18011  ?  1428 GLY   A CA  1 
ATOM   11384 C  C   . GLY   A 1 1430 ? -20.55400  13.64300  15.66500  1.000 64.90046  ?  1428 GLY   A C   1 
ATOM   11385 O  O   . GLY   A 1 1430 ? -19.61400  12.88400  15.92000  1.000 75.87708  ?  1428 GLY   A O   1 
ATOM   11386 N  N   . LYS   A 1 1431 ? -21.36700  13.45600  14.62800  1.000 60.08839  ?  1429 LYS   A N   1 
ATOM   11387 C  CA  . LYS   A 1 1431 ? -21.18100  12.35200  13.69700  1.000 58.01251  ?  1429 LYS   A CA  1 
ATOM   11388 C  C   . LYS   A 1 1431 ? -21.85600  12.70600  12.38200  1.000 48.15251  ?  1429 LYS   A C   1 
ATOM   11389 O  O   . LYS   A 1 1431 ? -22.68500  13.61700  12.31500  1.000 57.03241  ?  1429 LYS   A O   1 
ATOM   11390 C  CB  . LYS   A 1 1431 ? -21.74000  11.03800  14.26000  1.000 62.57619  ?  1429 LYS   A CB  1 
ATOM   11391 C  CG  . LYS   A 1 1431 ? -23.16200  11.14500  14.78900  1.000 73.00615  ?  1429 LYS   A CG  1 
ATOM   11392 C  CD  . LYS   A 1 1431 ? -23.81000  9.77600   14.95400  1.000 59.08377  ?  1429 LYS   A CD  1 
ATOM   11393 C  CE  . LYS   A 1 1431 ? -23.54400  9.19600   16.33500  1.000 66.64087  ?  1429 LYS   A CE  1 
ATOM   11394 N  NZ  . LYS   A 1 1431 ? -24.35900  9.86700   17.38600  1.000 68.76240  ?  1429 LYS   A NZ  1 
ATOM   11395 N  N   . LEU   A 1 1432 ? -21.48400  11.97700  11.33200  1.000 46.95374  ?  1430 LEU   A N   1 
ATOM   11396 C  CA  . LEU   A 1 1432 ? -22.07800  12.14400  10.01200  1.000 44.80876  ?  1430 LEU   A CA  1 
ATOM   11397 C  C   . LEU   A 1 1432 ? -22.66500  10.81600  9.55900   1.000 53.91749  ?  1430 LEU   A C   1 
ATOM   11398 O  O   . LEU   A 1 1432 ? -21.95600  9.80500   9.51100   1.000 50.47768  ?  1430 LEU   A O   1 
ATOM   11399 C  CB  . LEU   A 1 1432 ? -21.05700  12.64300  8.98800   1.000 33.80718  ?  1430 LEU   A CB  1 
ATOM   11400 C  CG  . LEU   A 1 1432 ? -21.72100  12.81400  7.61900   1.000 48.05741  ?  1430 LEU   A CG  1 
ATOM   11401 C  CD1 . LEU   A 1 1432 ? -22.75400  13.93400  7.66600   1.000 41.93960  ?  1430 LEU   A CD1 1 
ATOM   11402 C  CD2 . LEU   A 1 1432 ? -20.70700  13.05600  6.51900   1.000 40.47195  ?  1430 LEU   A CD2 1 
ATOM   11403 N  N   . VAL   A 1 1433 ? -23.95200  10.82400  9.23100   1.000 51.84213  ?  1431 VAL   A N   1 
ATOM   11404 C  CA  . VAL   A 1 1433 ? -24.64100  9.66400   8.68000   1.000 39.95024  ?  1431 VAL   A CA  1 
ATOM   11405 C  C   . VAL   A 1 1433 ? -24.63200  9.81400   7.16500   1.000 50.29833  ?  1431 VAL   A C   1 
ATOM   11406 O  O   . VAL   A 1 1433 ? -25.31100  10.68700  6.61300   1.000 61.01640  ?  1431 VAL   A O   1 
ATOM   11407 C  CB  . VAL   A 1 1433 ? -26.06900  9.54000   9.23000   1.000 47.84121  ?  1431 VAL   A CB  1 
ATOM   11408 C  CG1 . VAL   A 1 1433 ? -26.76400  8.32100   8.64800   1.000 47.24126  ?  1431 VAL   A CG1 1 
ATOM   11409 C  CG2 . VAL   A 1 1433 ? -26.04700  9.46000   10.74700  1.000 41.57077  ?  1431 VAL   A CG2 1 
ATOM   11410 N  N   . ILE   A 1 1434 ? -23.85000  8.97700   6.48800   1.000 52.15357  ?  1432 ILE   A N   1 
ATOM   11411 C  CA  . ILE   A 1 1434 ? -23.74700  9.03000   5.03400   1.000 47.91554  ?  1432 ILE   A CA  1 
ATOM   11412 C  C   . ILE   A 1 1434 ? -24.93700  8.29400   4.43300   1.000 48.22546  ?  1432 ILE   A C   1 
ATOM   11413 O  O   . ILE   A 1 1434 ? -25.09600  7.08500   4.62600   1.000 59.12849  ?  1432 ILE   A O   1 
ATOM   11414 C  CB  . ILE   A 1 1434 ? -22.42100  8.42700   4.54600   1.000 52.62509  ?  1432 ILE   A CB  1 
ATOM   11415 C  CG1 . ILE   A 1 1434 ? -21.23900  9.22700   5.09100   1.000 49.04559  ?  1432 ILE   A CG1 1 
ATOM   11416 C  CG2 . ILE   A 1 1434 ? -22.37000  8.41000   3.02400   1.000 57.30344  ?  1432 ILE   A CG2 1 
ATOM   11417 C  CD1 . ILE   A 1 1434 ? -20.12000  8.36800   5.63200   1.000 52.26785  ?  1432 ILE   A CD1 1 
ATOM   11418 N  N   . LEU   A 1 1435 ? -25.77800  9.02500   3.70800   1.000 62.24133  ?  1433 LEU   A N   1 
ATOM   11419 C  CA  . LEU   A 1 1435 ? -26.92100  8.42600   3.04100   1.000 60.12093  ?  1433 LEU   A CA  1 
ATOM   11420 C  C   . LEU   A 1 1435 ? -26.46000  7.56700   1.86500   1.000 61.87866  ?  1433 LEU   A C   1 
ATOM   11421 O  O   . LEU   A 1 1435 ? -25.38700  7.77100   1.29300   1.000 65.29668  ?  1433 LEU   A O   1 
ATOM   11422 C  CB  . LEU   A 1 1435 ? -27.88100  9.51200   2.55500   1.000 59.64186  ?  1433 LEU   A CB  1 
ATOM   11423 C  CG  . LEU   A 1 1435 ? -29.34400  9.14400   2.31500   1.000 61.09962  ?  1433 LEU   A CG  1 
ATOM   11424 C  CD1 . LEU   A 1 1435 ? -29.96700  8.59600   3.58900   1.000 63.56809  ?  1433 LEU   A CD1 1 
ATOM   11425 C  CD2 . LEU   A 1 1435 ? -30.12300  10.34900  1.80300   1.000 64.86670  ?  1433 LEU   A CD2 1 
ATOM   11426 N  N   . GLU   A 1 1436 ? -27.29100  6.59200   1.51100   1.000 63.38021  ?  1434 GLU   A N   1 
ATOM   11427 C  CA  . GLU   A 1 1436 ? -26.99300  5.74100   0.36900   1.000 71.59386  ?  1434 GLU   A CA  1 
ATOM   11428 C  C   . GLU   A 1 1436 ? -27.02600  6.56300   -0.92000  1.000 67.64162  ?  1434 GLU   A C   1 
ATOM   11429 O  O   . GLU   A 1 1436 ? -27.84000  7.48200   -1.04900  1.000 61.33834  ?  1434 GLU   A O   1 
ATOM   11430 C  CB  . GLU   A 1 1436 ? -27.99700  4.58900   0.29100   1.000 68.89636  ?  1434 GLU   A CB  1 
ATOM   11431 C  CG  . GLU   A 1 1436 ? -27.80200  3.66000   -0.89200  1.000 69.11813  ?  1434 GLU   A CG  1 
ATOM   11432 C  CD  . GLU   A 1 1436 ? -28.00000  2.20500   -0.53000  1.000 86.46856  ?  1434 GLU   A CD  1 
ATOM   11433 O  OE1 . GLU   A 1 1436 ? -29.07000  1.86700   0.02000   1.000 95.68289  ?  1434 GLU   A OE1 1 
ATOM   11434 O  OE2 . GLU   A 1 1436 ? -27.08000  1.40100   -0.79000  1.000 89.42017  -1 1434 GLU   A OE2 1 
ATOM   11435 N  N   . PRO   A 1 1437 ? -26.13400  6.28500   -1.87300  1.000 68.55554  ?  1435 PRO   A N   1 
ATOM   11436 C  CA  . PRO   A 1 1437 ? -26.19100  6.98500   -3.16200  1.000 57.72030  ?  1435 PRO   A CA  1 
ATOM   11437 C  C   . PRO   A 1 1437 ? -27.55700  6.84600   -3.81900  1.000 63.26432  ?  1435 PRO   A C   1 
ATOM   11438 O  O   . PRO   A 1 1437 ? -28.17300  5.77900   -3.79500  1.000 81.32978  ?  1435 PRO   A O   1 
ATOM   11439 C  CB  . PRO   A 1 1437 ? -25.09700  6.29800   -3.98500  1.000 52.48704  ?  1435 PRO   A CB  1 
ATOM   11440 C  CG  . PRO   A 1 1437 ? -24.11600  5.82900   -2.96500  1.000 66.01554  ?  1435 PRO   A CG  1 
ATOM   11441 C  CD  . PRO   A 1 1437 ? -24.92300  5.45300   -1.74900  1.000 58.64729  ?  1435 PRO   A CD  1 
ATOM   11442 N  N   . GLU   A 1 1438 ? -28.02700  7.95300   -4.39600  1.000 72.26721  ?  1436 GLU   A N   1 
ATOM   11443 C  CA  . GLU   A 1 1438 ? -29.32000  8.05000   -5.07400  1.000 70.15098  ?  1436 GLU   A CA  1 
ATOM   11444 C  C   . GLU   A 1 1438 ? -30.50100  7.85200   -4.12400  1.000 63.94590  ?  1436 GLU   A C   1 
ATOM   11445 O  O   . GLU   A 1 1438 ? -31.61900  7.57400   -4.56900  1.000 84.56974  ?  1436 GLU   A O   1 
ATOM   11446 C  CB  . GLU   A 1 1438 ? -29.40900  7.07100   -6.25200  1.000 67.14555  ?  1436 GLU   A CB  1 
ATOM   11447 C  CG  . GLU   A 1 1438 ? -28.82800  7.61900   -7.55300  1.000 89.83924  ?  1436 GLU   A CG  1 
ATOM   11448 C  CD  . GLU   A 1 1438 ? -29.50200  8.90600   -8.00500  1.000 98.64137  ?  1436 GLU   A CD  1 
ATOM   11449 O  OE1 . GLU   A 1 1438 ? -30.65800  8.84200   -8.47500  1.000 105.23254 ?  1436 GLU   A OE1 1 
ATOM   11450 O  OE2 . GLU   A 1 1438 ? -28.87900  9.98300   -7.88800  1.000 90.60268  -1 1436 GLU   A OE2 1 
ATOM   11451 N  N   . ALA   A 1 1439 ? -30.28500  7.99600   -2.81700  1.000 61.49162  ?  1437 ALA   A N   1 
ATOM   11452 C  CA  . ALA   A 1 1439 ? -31.38000  7.96500   -1.85800  1.000 57.52797  ?  1437 ALA   A CA  1 
ATOM   11453 C  C   . ALA   A 1 1439 ? -31.89200  9.35300   -1.51200  1.000 73.45998  ?  1437 ALA   A C   1 
ATOM   11454 O  O   . ALA   A 1 1439 ? -32.88500  9.46900   -0.78500  1.000 72.42662  ?  1437 ALA   A O   1 
ATOM   11455 C  CB  . ALA   A 1 1439 ? -30.95200  7.25100   -0.57300  1.000 51.70223  ?  1437 ALA   A CB  1 
ATOM   11456 N  N   . GLU   A 1 1440 ? -31.23200  10.40100  -2.01000  1.000 79.78106  ?  1438 GLU   A N   1 
ATOM   11457 C  CA  . GLU   A 1 1440 ? -31.69800  11.76300  -1.79100  1.000 66.59364  ?  1438 GLU   A CA  1 
ATOM   11458 C  C   . GLU   A 1 1440 ? -33.05500  12.00900  -2.43300  1.000 69.44351  ?  1438 GLU   A C   1 
ATOM   11459 O  O   . GLU   A 1 1440 ? -33.72300  12.99100  -2.09200  1.000 81.44476  ?  1438 GLU   A O   1 
ATOM   11460 C  CB  . GLU   A 1 1440 ? -30.67400  12.75800  -2.33900  1.000 63.55243  ?  1438 GLU   A CB  1 
ATOM   11461 C  CG  . GLU   A 1 1440 ? -30.41900  12.62000  -3.83500  1.000 62.92948  ?  1438 GLU   A CG  1 
ATOM   11462 C  CD  . GLU   A 1 1440 ? -29.33200  11.61600  -4.15600  1.000 74.70891  ?  1438 GLU   A CD  1 
ATOM   11463 O  OE1 . GLU   A 1 1440 ? -28.86700  10.92500  -3.22400  1.000 80.70941  ?  1438 GLU   A OE1 1 
ATOM   11464 O  OE2 . GLU   A 1 1440 ? -28.94800  11.51200  -5.34000  1.000 73.88599  -1 1438 GLU   A OE2 1 
ATOM   11465 N  N   . LYS   A 1 1441 ? -33.47600  11.14000  -3.34800  1.000 68.97013  ?  1439 LYS   A N   1 
ATOM   11466 C  CA  . LYS   A 1 1441 ? -34.74800  11.27300  -4.04000  1.000 63.33868  ?  1439 LYS   A CA  1 
ATOM   11467 C  C   . LYS   A 1 1441 ? -35.85200  10.42500  -3.42100  1.000 70.43154  ?  1439 LYS   A C   1 
ATOM   11468 O  O   . LYS   A 1 1441 ? -36.98000  10.43900  -3.92300  1.000 82.93006  ?  1439 LYS   A O   1 
ATOM   11469 C  CB  . LYS   A 1 1441 ? -34.57200  10.90500  -5.51400  1.000 59.42678  ?  1439 LYS   A CB  1 
ATOM   11470 C  CG  . LYS   A 1 1441 ? -33.24500  11.37100  -6.09300  1.000 65.91658  ?  1439 LYS   A CG  1 
ATOM   11471 C  CD  . LYS   A 1 1441 ? -32.92500  10.66200  -7.39700  1.000 68.11398  ?  1439 LYS   A CD  1 
ATOM   11472 C  CE  . LYS   A 1 1441 ? -32.49200  11.65000  -8.46600  1.000 76.06944  ?  1439 LYS   A CE  1 
ATOM   11473 N  NZ  . LYS   A 1 1441 ? -32.39100  11.01200  -9.80600  1.000 79.46996  ?  1439 LYS   A NZ  1 
ATOM   11474 N  N   . ASN   A 1 1442 ? -35.55700  9.68900   -2.35100  1.000 67.94009  ?  1440 ASN   A N   1 
ATOM   11475 C  CA  . ASN   A 1 1442 ? -36.55600  8.87800   -1.66200  1.000 58.53044  ?  1440 ASN   A CA  1 
ATOM   11476 C  C   . ASN   A 1 1442 ? -36.83100  9.46800   -0.28800  1.000 55.20279  ?  1440 ASN   A C   1 
ATOM   11477 O  O   . ASN   A 1 1442 ? -36.01600  9.30200   0.63300   1.000 56.45065  ?  1440 ASN   A O   1 
ATOM   11478 C  CB  . ASN   A 1 1442 ? -36.08600  7.42600   -1.53300  1.000 78.30753  ?  1440 ASN   A CB  1 
ATOM   11479 C  CG  . ASN   A 1 1442 ? -37.08000  6.56000   -0.78600  1.000 79.30473  ?  1440 ASN   A CG  1 
ATOM   11480 O  OD1 . ASN   A 1 1442 ? -38.28200  6.82500   -0.79900  1.000 74.67846  ?  1440 ASN   A OD1 1 
ATOM   11481 N  ND2 . ASN   A 1 1442 ? -36.58100  5.52300   -0.12400  1.000 75.85475  ?  1440 ASN   A ND2 1 
ATOM   11482 N  N   . PRO   A 1 1443 ? -37.95300  10.16300  -0.09400  1.000 55.89305  ?  1441 PRO   A N   1 
ATOM   11483 C  CA  . PRO   A 1 1443 ? -38.26100  10.68000  1.24800   1.000 62.23719  ?  1441 PRO   A CA  1 
ATOM   11484 C  C   . PRO   A 1 1443 ? -38.43200  9.58000   2.28100   1.000 67.55555  ?  1441 PRO   A C   1 
ATOM   11485 O  O   . PRO   A 1 1443 ? -38.21300  9.82500   3.47500   1.000 61.32193  ?  1441 PRO   A O   1 
ATOM   11486 C  CB  . PRO   A 1 1443 ? -39.55600  11.47600  1.02800   1.000 61.81897  ?  1441 PRO   A CB  1 
ATOM   11487 C  CG  . PRO   A 1 1443 ? -40.15400  10.89400  -0.21700  1.000 61.52006  ?  1441 PRO   A CG  1 
ATOM   11488 C  CD  . PRO   A 1 1443 ? -38.99100  10.50900  -1.07900  1.000 52.93959  ?  1441 PRO   A CD  1 
ATOM   11489 N  N   . LYS   A 1 1444 ? -38.81500  8.37300   1.85500   1.000 68.79170  ?  1442 LYS   A N   1 
ATOM   11490 C  CA  . LYS   A 1 1444 ? -38.81000  7.22700   2.75800   1.000 72.23574  ?  1442 LYS   A CA  1 
ATOM   11491 C  C   . LYS   A 1 1444 ? -37.43900  7.05100   3.39500   1.000 77.38424  ?  1442 LYS   A C   1 
ATOM   11492 O  O   . LYS   A 1 1444 ? -37.31000  7.01100   4.62300   1.000 76.43722  ?  1442 LYS   A O   1 
ATOM   11493 C  CB  . LYS   A 1 1444 ? -39.21100  5.96100   1.99700   1.000 77.47322  ?  1442 LYS   A CB  1 
ATOM   11494 C  CG  . LYS   A 1 1444 ? -40.33900  5.16300   2.62000   1.000 73.89812  ?  1442 LYS   A CG  1 
ATOM   11495 C  CD  . LYS   A 1 1444 ? -41.02200  4.27900   1.58500   1.000 92.64033  ?  1442 LYS   A CD  1 
ATOM   11496 C  CE  . LYS   A 1 1444 ? -42.40900  3.84800   2.04100   1.000 91.86143  ?  1442 LYS   A CE  1 
ATOM   11497 N  NZ  . LYS   A 1 1444 ? -43.31700  3.57600   0.88800   1.000 93.51711  ?  1442 LYS   A NZ  1 
ATOM   11498 N  N   . ALA   A 1 1445 ? -36.39600  6.97800   2.56400   1.000 72.50868  ?  1443 ALA   A N   1 
ATOM   11499 C  CA  . ALA   A 1 1445 ? -35.04600  6.74500   3.06500   1.000 70.44173  ?  1443 ALA   A CA  1 
ATOM   11500 C  C   . ALA   A 1 1445 ? -34.56300  7.90200   3.93100   1.000 76.34340  ?  1443 ALA   A C   1 
ATOM   11501 O  O   . ALA   A 1 1445 ? -34.04100  7.68800   5.03200   1.000 73.45173  ?  1443 ALA   A O   1 
ATOM   11502 C  CB  . ALA   A 1 1445 ? -34.09000  6.51600   1.89500   1.000 58.36471  ?  1443 ALA   A CB  1 
ATOM   11503 N  N   . ILE   A 1 1446 ? -34.71100  9.13700   3.43900   1.000 58.41716  ?  1444 ILE   A N   1 
ATOM   11504 C  CA  . ILE   A 1 1446 ? -34.27800  10.30500  4.20600   1.000 57.97020  ?  1444 ILE   A CA  1 
ATOM   11505 C  C   . ILE   A 1 1446 ? -34.91300  10.28700  5.58800   1.000 59.63046  ?  1444 ILE   A C   1 
ATOM   11506 O  O   . ILE   A 1 1446 ? -34.23400  10.45600  6.60800   1.000 61.74367  ?  1444 ILE   A O   1 
ATOM   11507 C  CB  . ILE   A 1 1446 ? -34.61300  11.60600  3.45400   1.000 57.49258  ?  1444 ILE   A CB  1 
ATOM   11508 C  CG1 . ILE   A 1 1446 ? -34.05800  11.56600  2.02800   1.000 50.87424  ?  1444 ILE   A CG1 1 
ATOM   11509 C  CG2 . ILE   A 1 1446 ? -34.08600  12.81700  4.21800   1.000 54.93815  ?  1444 ILE   A CG2 1 
ATOM   11510 C  CD1 . ILE   A 1 1446 ? -34.66700  12.60300  1.11100   1.000 53.14135  ?  1444 ILE   A CD1 1 
ATOM   11511 N  N   . TRP   A 1 1447 ? -36.22800  10.05900  5.63800   1.000 65.67547  ?  1445 TRP   A N   1 
ATOM   11512 C  CA  . TRP   A 1 1447 ? -36.93000  10.01900  6.91600   1.000 69.68190  ?  1445 TRP   A CA  1 
ATOM   11513 C  C   . TRP   A 1 1447 ? -36.37000  8.92200   7.81400   1.000 66.62226  ?  1445 TRP   A C   1 
ATOM   11514 O  O   . TRP   A 1 1447 ? -36.04600  9.17000   8.98100   1.000 66.18522  ?  1445 TRP   A O   1 
ATOM   11515 C  CB  . TRP   A 1 1447 ? -38.43000  9.82900   6.68100   1.000 64.51221  ?  1445 TRP   A CB  1 
ATOM   11516 C  CG  . TRP   A 1 1447 ? -39.27500  9.78500   7.93300   1.000 66.48881  ?  1445 TRP   A CG  1 
ATOM   11517 C  CD1 . TRP   A 1 1447 ? -40.21300  8.84300   8.24400   1.000 67.08391  ?  1445 TRP   A CD1 1 
ATOM   11518 C  CD2 . TRP   A 1 1447 ? -39.27300  10.72200  9.02500   1.000 62.39923  ?  1445 TRP   A CD2 1 
ATOM   11519 N  NE1 . TRP   A 1 1447 ? -40.78700  9.12700   9.45900   1.000 70.08624  ?  1445 TRP   A NE1 1 
ATOM   11520 C  CE2 . TRP   A 1 1447 ? -40.22900  10.27300  9.95900   1.000 63.30299  ?  1445 TRP   A CE2 1 
ATOM   11521 C  CE3 . TRP   A 1 1447 ? -38.55500  11.89100  9.30500   1.000 64.80741  ?  1445 TRP   A CE3 1 
ATOM   11522 C  CZ2 . TRP   A 1 1447 ? -40.48600  10.95000  11.15200  1.000 59.79968  ?  1445 TRP   A CZ2 1 
ATOM   11523 C  CZ3 . TRP   A 1 1447 ? -38.81200  12.56200  10.49300  1.000 66.83630  ?  1445 TRP   A CZ3 1 
ATOM   11524 C  CH2 . TRP   A 1 1447 ? -39.77000  12.08800  11.40000  1.000 62.84037  ?  1445 TRP   A CH2 1 
ATOM   11525 N  N   . GLN   A 1 1448 ? -36.22400  7.70500   7.27400   1.000 69.03761  ?  1446 GLN   A N   1 
ATOM   11526 C  CA  . GLN   A 1 1448 ? -35.65300  6.59800   8.04200   1.000 71.31174  ?  1446 GLN   A CA  1 
ATOM   11527 C  C   . GLN   A 1 1448 ? -34.33100  6.98200   8.69300   1.000 78.78619  ?  1446 GLN   A C   1 
ATOM   11528 O  O   . GLN   A 1 1448 ? -34.09300  6.66900   9.86600   1.000 73.89131  ?  1446 GLN   A O   1 
ATOM   11529 C  CB  . GLN   A 1 1448 ? -35.44500  5.37700   7.14200   1.000 63.15479  ?  1446 GLN   A CB  1 
ATOM   11530 C  CG  . GLN   A 1 1448 ? -36.71000  4.77700   6.56300   1.000 94.48066  ?  1446 GLN   A CG  1 
ATOM   11531 C  CD  . GLN   A 1 1448 ? -36.45300  3.46100   5.85200   1.000 87.75985  ?  1446 GLN   A CD  1 
ATOM   11532 O  OE1 . GLN   A 1 1448 ? -35.40000  2.84600   6.01900   1.000 74.27125  ?  1446 GLN   A OE1 1 
ATOM   11533 N  NE2 . GLN   A 1 1448 ? -37.40700  3.03700   5.03100   1.000 82.29356  ?  1446 GLN   A NE2 1 
ATOM   11534 N  N   . ALA   A 1 1449 ? -33.45600  7.65800   7.94400   1.000 76.92047  ?  1447 ALA   A N   1 
ATOM   11535 C  CA  . ALA   A 1 1449 ? -32.16900  8.06900   8.49300   1.000 52.75857  ?  1447 ALA   A CA  1 
ATOM   11536 C  C   . ALA   A 1 1449 ? -32.34600  9.02200   9.66900   1.000 62.14773  ?  1447 ALA   A C   1 
ATOM   11537 O  O   . ALA   A 1 1449 ? -31.65500  8.89500   10.68700  1.000 64.26629  ?  1447 ALA   A O   1 
ATOM   11538 C  CB  . ALA   A 1 1449 ? -31.31900  8.71400   7.40000   1.000 49.41658  ?  1447 ALA   A CB  1 
ATOM   11539 N  N   . VAL   A 1 1450 ? -33.27000  9.98000   9.55100   1.000 63.06574  ?  1448 VAL   A N   1 
ATOM   11540 C  CA  . VAL   A 1 1450 ? -33.52400  10.91000  10.64900  1.000 69.55463  ?  1448 VAL   A CA  1 
ATOM   11541 C  C   . VAL   A 1 1450 ? -34.00100  10.16100  11.88800  1.000 66.96300  ?  1448 VAL   A C   1 
ATOM   11542 O  O   . VAL   A 1 1450 ? -33.62000  10.49300  13.01800  1.000 65.03955  ?  1448 VAL   A O   1 
ATOM   11543 C  CB  . VAL   A 1 1450 ? -34.53700  11.98700  10.21400  1.000 63.44252  ?  1448 VAL   A CB  1 
ATOM   11544 C  CG1 . VAL   A 1 1450 ? -34.66400  13.06700  11.28500  1.000 70.28359  ?  1448 VAL   A CG1 1 
ATOM   11545 C  CG2 . VAL   A 1 1450 ? -34.12100  12.59900  8.88700   1.000 47.31008  ?  1448 VAL   A CG2 1 
ATOM   11546 N  N   . VAL   A 1 1451 ? -34.83800  9.13700   11.69700  1.000 64.37449  ?  1449 VAL   A N   1 
ATOM   11547 C  CA  . VAL   A 1 1451 ? -35.40300  8.40300   12.83000  1.000 72.53209  ?  1449 VAL   A CA  1 
ATOM   11548 C  C   . VAL   A 1 1451 ? -34.36200  7.48100   13.45100  1.000 60.48068  ?  1449 VAL   A C   1 
ATOM   11549 O  O   . VAL   A 1 1451 ? -34.05300  7.57900   14.64500  1.000 64.74616  ?  1449 VAL   A O   1 
ATOM   11550 C  CB  . VAL   A 1 1451 ? -36.65500  7.61800   12.40000  1.000 67.91633  ?  1449 VAL   A CB  1 
ATOM   11551 C  CG1 . VAL   A 1 1451 ? -37.44600  7.20800   13.62200  1.000 71.38621  ?  1449 VAL   A CG1 1 
ATOM   11552 C  CG2 . VAL   A 1 1451 ? -37.53800  8.47500   11.50700  1.000 55.79766  ?  1449 VAL   A CG2 1 
ATOM   11553 N  N   . GLY   A 1 1452 ? -33.81900  6.56200   12.65000  1.000 54.06364  ?  1450 GLY   A N   1 
ATOM   11554 C  CA  . GLY   A 1 1452 ? -32.94000  5.54100   13.19600  1.000 53.92363  ?  1450 GLY   A CA  1 
ATOM   11555 C  C   . GLY   A 1 1452 ? -31.64100  6.09500   13.74900  1.000 65.56047  ?  1450 GLY   A C   1 
ATOM   11556 O  O   . GLY   A 1 1452 ? -31.13700  5.61300   14.76700  1.000 58.14607  ?  1450 GLY   A O   1 
ATOM   11557 N  N   . ALA   A 1 1453 ? -31.08100  7.11100   13.09300  1.000 62.59573  ?  1451 ALA   A N   1 
ATOM   11558 C  CA  . ALA   A 1 1453 ? -29.80100  7.67900   13.49400  1.000 45.72994  ?  1451 ALA   A CA  1 
ATOM   11559 C  C   . ALA   A 1 1453 ? -29.94900  8.94200   14.33400  1.000 61.87007  ?  1451 ALA   A C   1 
ATOM   11560 O  O   . ALA   A 1 1453 ? -28.94300  9.60100   14.62200  1.000 82.15984  ?  1451 ALA   A O   1 
ATOM   11561 C  CB  . ALA   A 1 1453 ? -28.94400  7.96700   12.26000  1.000 39.63173  ?  1451 ALA   A CB  1 
ATOM   11562 N  N   . GLY   A 1 1454 ? -31.17100  9.29200   14.73000  1.000 59.22228  ?  1452 GLY   A N   1 
ATOM   11563 C  CA  . GLY   A 1 1454 ? -31.41000  10.46600  15.55900  1.000 78.95273  ?  1452 GLY   A CA  1 
ATOM   11564 C  C   . GLY   A 1 1454 ? -30.84000  11.75400  15.00600  1.000 75.04871  ?  1452 GLY   A C   1 
ATOM   11565 O  O   . GLY   A 1 1454 ? -30.30900  12.57400  15.76600  1.000 68.20510  ?  1452 GLY   A O   1 
ATOM   11566 N  N   . ILE   A 1 1455 ? -30.94600  11.95600  13.69300  1.000 56.71771  ?  1453 ILE   A N   1 
ATOM   11567 C  CA  . ILE   A 1 1455 ? -30.33100  13.10900  13.05100  1.000 54.69172  ?  1453 ILE   A CA  1 
ATOM   11568 C  C   . ILE   A 1 1455 ? -31.04200  14.38700  13.46800  1.000 57.77483  ?  1453 ILE   A C   1 
ATOM   11569 O  O   . ILE   A 1 1455 ? -32.27900  14.45700  13.49400  1.000 70.41768  ?  1453 ILE   A O   1 
ATOM   11570 C  CB  . ILE   A 1 1455 ? -30.35600  12.92700  11.52800  1.000 61.59230  ?  1453 ILE   A CB  1 
ATOM   11571 C  CG1 . ILE   A 1 1455 ? -29.73200  11.58100  11.18200  1.000 67.13503  ?  1453 ILE   A CG1 1 
ATOM   11572 C  CG2 . ILE   A 1 1455 ? -29.61700  14.05900  10.83500  1.000 63.35302  ?  1453 ILE   A CG2 1 
ATOM   11573 C  CD1 . ILE   A 1 1455 ? -29.55200  11.37100  9.72100   1.000 58.36289  ?  1453 ILE   A CD1 1 
ATOM   11574 N  N   . THR   A 1 1456 ? -30.25700  15.41000  13.79100  1.000 49.85339  ?  1454 THR   A N   1 
ATOM   11575 C  CA  . THR   A 1 1456 ? -30.76700  16.71000  14.21000  1.000 69.47629  ?  1454 THR   A CA  1 
ATOM   11576 C  C   . THR   A 1 1456 ? -30.61000  17.78700  13.15000  1.000 61.10622  ?  1454 THR   A C   1 
ATOM   11577 O  O   . THR   A 1 1456 ? -31.49300  18.63400  13.00100  1.000 54.48542  ?  1454 THR   A O   1 
ATOM   11578 C  CB  . THR   A 1 1456 ? -30.05600  17.16200  15.49000  1.000 70.71870  ?  1454 THR   A CB  1 
ATOM   11579 O  OG1 . THR   A 1 1456 ? -28.65400  16.90200  15.36400  1.000 63.30078  ?  1454 THR   A OG1 1 
ATOM   11580 C  CG2 . THR   A 1 1456 ? -30.59100  16.40800  16.69800  1.000 71.51469  ?  1454 THR   A CG2 1 
ATOM   11581 N  N   . HIS   A 1 1457 ? -29.50600  17.77800  12.40900  1.000 53.23753  ?  1455 HIS   A N   1 
ATOM   11582 C  CA  . HIS   A 1 1457 ? -29.23900  18.75700  11.36500  1.000 53.55624  ?  1455 HIS   A CA  1 
ATOM   11583 C  C   . HIS   A 1 1457 ? -29.45300  18.11000  10.00400  1.000 49.81494  ?  1455 HIS   A C   1 
ATOM   11584 O  O   . HIS   A 1 1457 ? -28.93200  17.02000  9.74300   1.000 62.52000  ?  1455 HIS   A O   1 
ATOM   11585 C  CB  . HIS   A 1 1457 ? -27.81100  19.30000  11.47900  1.000 55.74158  ?  1455 HIS   A CB  1 
ATOM   11586 C  CG  . HIS   A 1 1457 ? -27.56000  20.07800  12.73300  1.000 50.37490  ?  1455 HIS   A CG  1 
ATOM   11587 N  ND1 . HIS   A 1 1457 ? -27.78800  19.55800  13.98800  1.000 63.51049  ?  1455 HIS   A ND1 1 
ATOM   11588 C  CD2 . HIS   A 1 1457 ? -27.10100  21.33700  12.92500  1.000 58.41506  ?  1455 HIS   A CD2 1 
ATOM   11589 C  CE1 . HIS   A 1 1457 ? -27.48200  20.46400  14.90000  1.000 69.52925  ?  1455 HIS   A CE1 1 
ATOM   11590 N  NE2 . HIS   A 1 1457 ? -27.06200  21.55200  14.28100  1.000 63.76097  ?  1455 HIS   A NE2 1 
ATOM   11591 N  N   . ILE   A 1 1458 ? -30.21700  18.77500  9.14300   1.000 45.41089  ?  1456 ILE   A N   1 
ATOM   11592 C  CA  . ILE   A 1 1458 ? -30.48800  18.26100  7.80500   1.000 51.24158  ?  1456 ILE   A CA  1 
ATOM   11593 C  C   . ILE   A 1 1458 ? -30.56800  19.43400  6.83700   1.000 55.12414  ?  1456 ILE   A C   1 
ATOM   11594 O  O   . ILE   A 1 1458 ? -31.08600  20.50300  7.17300   1.000 53.41592  ?  1456 ILE   A O   1 
ATOM   11595 C  CB  . ILE   A 1 1458 ? -31.77700  17.40700  7.77900   1.000 65.74725  ?  1456 ILE   A CB  1 
ATOM   11596 C  CG1 . ILE   A 1 1458 ? -31.88600  16.63200  6.46200   1.000 46.97728  ?  1456 ILE   A CG1 1 
ATOM   11597 C  CG2 . ILE   A 1 1458 ? -33.01200  18.26500  8.02900   1.000 62.79980  ?  1456 ILE   A CG2 1 
ATOM   11598 C  CD1 . ILE   A 1 1458 ? -32.82300  15.45300  6.53400   1.000 48.43074  ?  1456 ILE   A CD1 1 
ATOM   11599 N  N   . ASN   A 1 1459 ? -30.02800  19.23500  5.63800   1.000 58.80556  ?  1457 ASN   A N   1 
ATOM   11600 C  CA  . ASN   A 1 1459 ? -30.08700  20.22300  4.57200   1.000 48.39745  ?  1457 ASN   A CA  1 
ATOM   11601 C  C   . ASN   A 1 1459 ? -31.08700  19.76700  3.52100   1.000 48.12016  ?  1457 ASN   A C   1 
ATOM   11602 O  O   . ASN   A 1 1459 ? -31.12900  18.58800  3.15500   1.000 57.49277  ?  1457 ASN   A O   1 
ATOM   11603 C  CB  . ASN   A 1 1459 ? -28.71400  20.43900  3.92300   1.000 43.45455  ?  1457 ASN   A CB  1 
ATOM   11604 C  CG  . ASN   A 1 1459 ? -27.75600  21.20600  4.81700   1.000 49.45145  ?  1457 ASN   A CG  1 
ATOM   11605 O  OD1 . ASN   A 1 1459 ? -28.16400  21.84400  5.78900   1.000 46.11551  ?  1457 ASN   A OD1 1 
ATOM   11606 N  ND2 . ASN   A 1 1459 ? -26.47000  21.15100  4.48700   1.000 46.69571  ?  1457 ASN   A ND2 1 
ATOM   11607 N  N   . PHE   A 1 1460 ? -31.89500  20.70600  3.04500   1.000 55.25628  ?  1458 PHE   A N   1 
ATOM   11608 C  CA  . PHE   A 1 1460 ? -32.91300  20.41800  2.04700   1.000 57.06933  ?  1458 PHE   A CA  1 
ATOM   11609 C  C   . PHE   A 1 1460 ? -32.99000  21.60500  1.10700   1.000 49.80044  ?  1458 PHE   A C   1 
ATOM   11610 O  O   . PHE   A 1 1460 ? -33.34300  22.70900  1.53000   1.000 55.45653  ?  1458 PHE   A O   1 
ATOM   11611 C  CB  . PHE   A 1 1460 ? -34.27900  20.16500  2.69500   1.000 52.81499  ?  1458 PHE   A CB  1 
ATOM   11612 C  CG  . PHE   A 1 1460 ? -34.65900  18.71500  2.77000   1.000 50.31220  ?  1458 PHE   A CG  1 
ATOM   11613 C  CD1 . PHE   A 1 1460 ? -34.89300  17.98900  1.61500   1.000 58.11439  ?  1458 PHE   A CD1 1 
ATOM   11614 C  CD2 . PHE   A 1 1460 ? -34.80200  18.08400  3.99600   1.000 45.05144  ?  1458 PHE   A CD2 1 
ATOM   11615 C  CE1 . PHE   A 1 1460 ? -35.25000  16.65600  1.67700   1.000 64.08676  ?  1458 PHE   A CE1 1 
ATOM   11616 C  CE2 . PHE   A 1 1460 ? -35.16200  16.74800  4.06600   1.000 49.08759  ?  1458 PHE   A CE2 1 
ATOM   11617 C  CZ  . PHE   A 1 1460 ? -35.38600  16.03400  2.90300   1.000 59.11112  ?  1458 PHE   A CZ  1 
ATOM   11618 N  N   . VAL   A 1 1461 ? -32.64100  21.39000  -0.14800  1.000 51.57552  ?  1459 VAL   A N   1 
ATOM   11619 C  CA  . VAL   A 1 1461 ? -33.00800  22.39000  -1.15300  1.000 57.61412  ?  1459 VAL   A CA  1 
ATOM   11620 C  C   . VAL   A 1 1461 ? -34.52400  22.40800  -1.28900  1.000 69.38713  ?  1459 VAL   A C   1 
ATOM   11621 O  O   . VAL   A 1 1461 ? -35.14900  21.33000  -1.31000  1.000 76.22068  ?  1459 VAL   A O   1 
ATOM   11622 C  CB  . VAL   A 1 1461 ? -32.33500  22.07100  -2.48700  1.000 60.57013  ?  1459 VAL   A CB  1 
ATOM   11623 C  CG1 . VAL   A 1 1461 ? -32.50700  20.59500  -2.80900  1.000 66.47010  ?  1459 VAL   A CG1 1 
ATOM   11624 C  CG2 . VAL   A 1 1461 ? -32.89100  22.96500  -3.60200  1.000 62.37255  ?  1459 VAL   A CG2 1 
ATOM   11625 N  N   . PRO   A 1 1462 ? -35.16600  23.57600  -1.34300  1.000 71.33543  ?  1460 PRO   A N   1 
ATOM   11626 C  CA  . PRO   A 1 1462 ? -36.60300  23.60600  -1.62900  1.000 69.79150  ?  1460 PRO   A CA  1 
ATOM   11627 C  C   . PRO   A 1 1462 ? -36.90200  22.87600  -2.92800  1.000 73.23990  ?  1460 PRO   A C   1 
ATOM   11628 O  O   . PRO   A 1 1462 ? -36.02900  22.69500  -3.77800  1.000 89.65326  ?  1460 PRO   A O   1 
ATOM   11629 C  CB  . PRO   A 1 1462 ? -36.91300  25.10200  -1.74300  1.000 53.40554  ?  1460 PRO   A CB  1 
ATOM   11630 C  CG  . PRO   A 1 1462 ? -35.89700  25.74900  -0.88100  1.000 49.88467  ?  1460 PRO   A CG  1 
ATOM   11631 C  CD  . PRO   A 1 1462 ? -34.64400  24.91700  -1.02700  1.000 63.62490  ?  1460 PRO   A CD  1 
ATOM   11632 N  N   . SER   A 1 1463 ? -38.16100  22.44700  -3.05200  1.000 44.78054  ?  1461 SER   A N   1 
ATOM   11633 C  CA  . SER   A 1 1463 ? -38.66300  21.60300  -4.13700  1.000 69.46409  ?  1461 SER   A CA  1 
ATOM   11634 C  C   . SER   A 1 1463 ? -38.30200  20.14200  -3.89200  1.000 69.28015  ?  1461 SER   A C   1 
ATOM   11635 O  O   . SER   A 1 1463 ? -38.88000  19.24800  -4.51500  1.000 75.64854  ?  1461 SER   A O   1 
ATOM   11636 C  CB  . SER   A 1 1463 ? -38.15500  22.05800  -5.51200  1.000 62.20018  ?  1461 SER   A CB  1 
ATOM   11637 O  OG  . SER   A 1 1463 ? -36.83900  21.58700  -5.75000  1.000 62.16652  ?  1461 SER   A OG  1 
ATOM   11638 N  N   . MET   A 1 1464 ? -37.34100  19.88600  -3.00500  1.000 67.36143  ?  1462 MET   A N   1 
ATOM   11639 C  CA  . MET   A 1 1464 ? -37.11800  18.54600  -2.47700  1.000 62.16781  ?  1462 MET   A CA  1 
ATOM   11640 C  C   . MET   A 1 1464 ? -37.62200  18.40600  -1.05100  1.000 61.68628  ?  1462 MET   A C   1 
ATOM   11641 O  O   . MET   A 1 1464 ? -37.74600  17.28100  -0.55500  1.000 63.45847  ?  1462 MET   A O   1 
ATOM   11642 C  CB  . MET   A 1 1464 ? -35.63100  18.17800  -2.54100  1.000 55.36780  ?  1462 MET   A CB  1 
ATOM   11643 C  CG  . MET   A 1 1464 ? -35.00700  18.35300  -3.91600  1.000 61.82960  ?  1462 MET   A CG  1 
ATOM   11644 S  SD  . MET   A 1 1464 ? -35.39500  16.99700  -5.03800  1.000 85.06728  ?  1462 MET   A SD  1 
ATOM   11645 C  CE  . MET   A 1 1464 ? -33.89100  16.02400  -4.94900  1.000 71.13125  ?  1462 MET   A CE  1 
ATOM   11646 N  N   . LEU   A 1 1465 ? -37.90700  19.52700  -0.38800  1.000 64.05129  ?  1463 LEU   A N   1 
ATOM   11647 C  CA  . LEU   A 1 1465 ? -38.56200  19.49600  0.91000   1.000 60.65898  ?  1463 LEU   A CA  1 
ATOM   11648 C  C   . LEU   A 1 1465 ? -40.05000  19.20400  0.77500   1.000 68.75811  ?  1463 LEU   A C   1 
ATOM   11649 O  O   . LEU   A 1 1465 ? -40.62800  18.54500  1.64600   1.000 73.36385  ?  1463 LEU   A O   1 
ATOM   11650 C  CB  . LEU   A 1 1465 ? -38.34100  20.82600  1.63300   1.000 49.31613  ?  1463 LEU   A CB  1 
ATOM   11651 C  CG  . LEU   A 1 1465 ? -38.78300  20.93000  3.09300   1.000 41.69807  ?  1463 LEU   A CG  1 
ATOM   11652 C  CD1 . LEU   A 1 1465 ? -38.16600  19.82600  3.93600   1.000 46.08696  ?  1463 LEU   A CD1 1 
ATOM   11653 C  CD2 . LEU   A 1 1465 ? -38.42100  22.29300  3.65200   1.000 44.96091  ?  1463 LEU   A CD2 1 
ATOM   11654 N  N   . ILE   A 1 1466 ? -40.68100  19.67100  -0.30600  1.000 61.68489  ?  1464 ILE   A N   1 
ATOM   11655 C  CA  . ILE   A 1 1466 ? -42.10800  19.40700  -0.49900  1.000 69.90378  ?  1464 ILE   A CA  1 
ATOM   11656 C  C   . ILE   A 1 1466 ? -42.40000  17.92200  -0.67700  1.000 70.42423  ?  1464 ILE   A C   1 
ATOM   11657 O  O   . ILE   A 1 1466 ? -43.34500  17.42200  -0.04500  1.000 68.12723  ?  1464 ILE   A O   1 
ATOM   11658 C  CB  . ILE   A 1 1466 ? -42.65600  20.26400  -1.65500  1.000 71.14070  ?  1464 ILE   A CB  1 
ATOM   11659 C  CG1 . ILE   A 1 1466 ? -42.05800  21.67000  -1.61000  1.000 65.21196  ?  1464 ILE   A CG1 1 
ATOM   11660 C  CG2 . ILE   A 1 1466 ? -44.17200  20.32300  -1.59600  1.000 91.06535  ?  1464 ILE   A CG2 1 
ATOM   11661 C  CD1 . ILE   A 1 1466 ? -41.94400  22.32000  -2.96100  1.000 96.94255  ?  1464 ILE   A CD1 1 
ATOM   11662 N  N   . PRO   A 1 1467 ? -41.66500  17.16600  -1.50500  1.000 67.58834  ?  1465 PRO   A N   1 
ATOM   11663 C  CA  . PRO   A 1 1467 ? -41.88000  15.71000  -1.51300  1.000 60.15107  ?  1465 PRO   A CA  1 
ATOM   11664 C  C   . PRO   A 1 1467 ? -41.60700  15.07300  -0.16600  1.000 66.57072  ?  1465 PRO   A C   1 
ATOM   11665 O  O   . PRO   A 1 1467 ? -42.24300  14.07000  0.18100   1.000 85.02691  ?  1465 PRO   A O   1 
ATOM   11666 C  CB  . PRO   A 1 1467 ? -40.89500  15.21400  -2.58100  1.000 52.50003  ?  1465 PRO   A CB  1 
ATOM   11667 C  CG  . PRO   A 1 1467 ? -40.65300  16.38500  -3.44700  1.000 56.91417  ?  1465 PRO   A CG  1 
ATOM   11668 C  CD  . PRO   A 1 1467 ? -40.69400  17.57100  -2.53700  1.000 61.73223  ?  1465 PRO   A CD  1 
ATOM   11669 N  N   . PHE   A 1 1468 ? -40.67800  15.63600  0.60700   1.000 52.14098  ?  1466 PHE   A N   1 
ATOM   11670 C  CA  . PHE   A 1 1468 ? -40.38100  15.10200  1.93000   1.000 50.66132  ?  1466 PHE   A CA  1 
ATOM   11671 C  C   . PHE   A 1 1468 ? -41.54500  15.33000  2.88800   1.000 64.11603  ?  1466 PHE   A C   1 
ATOM   11672 O  O   . PHE   A 1 1468 ? -41.96600  14.40900  3.59800   1.000 70.42140  ?  1466 PHE   A O   1 
ATOM   11673 C  CB  . PHE   A 1 1468 ? -39.10000  15.73800  2.46900   1.000 54.16898  ?  1466 PHE   A CB  1 
ATOM   11674 C  CG  . PHE   A 1 1468 ? -38.58400  15.09500  3.72500   1.000 55.23924  ?  1466 PHE   A CG  1 
ATOM   11675 C  CD1 . PHE   A 1 1468 ? -38.11400  13.79100  3.71100   1.000 51.70749  ?  1466 PHE   A CD1 1 
ATOM   11676 C  CD2 . PHE   A 1 1468 ? -38.56100  15.79900  4.91900   1.000 39.05667  ?  1466 PHE   A CD2 1 
ATOM   11677 C  CE1 . PHE   A 1 1468 ? -37.63600  13.19800  4.86500   1.000 43.51118  ?  1466 PHE   A CE1 1 
ATOM   11678 C  CE2 . PHE   A 1 1468 ? -38.08400  15.21200  6.07700   1.000 51.44426  ?  1466 PHE   A CE2 1 
ATOM   11679 C  CZ  . PHE   A 1 1468 ? -37.62000  13.90900  6.05000   1.000 54.37034  ?  1466 PHE   A CZ  1 
ATOM   11680 N  N   . VAL   A 1 1469 ? -42.08200  16.55400  2.92100   1.000 71.53147  ?  1467 VAL   A N   1 
ATOM   11681 C  CA  . VAL   A 1 1469 ? -43.19600  16.84100  3.81800   1.000 75.48530  ?  1467 VAL   A CA  1 
ATOM   11682 C  C   . VAL   A 1 1469 ? -44.48200  16.18000  3.34200   1.000 70.01837  ?  1467 VAL   A C   1 
ATOM   11683 O  O   . VAL   A 1 1469 ? -45.38200  15.93200  4.15300   1.000 70.65623  ?  1467 VAL   A O   1 
ATOM   11684 C  CB  . VAL   A 1 1469 ? -43.39200  18.36200  3.98900   1.000 72.95772  ?  1467 VAL   A CB  1 
ATOM   11685 C  CG1 . VAL   A 1 1469 ? -42.09900  19.02500  4.44600   1.000 52.91697  ?  1467 VAL   A CG1 1 
ATOM   11686 C  CG2 . VAL   A 1 1469 ? -43.88400  18.99100  2.69900   1.000 69.79636  ?  1467 VAL   A CG2 1 
ATOM   11687 N  N   . GLU   A 1 1470 ? -44.59500  15.87800  2.04400   1.000 66.23979  ?  1468 GLU   A N   1 
ATOM   11688 C  CA  . GLU   A 1 1470 ? -45.74700  15.13000  1.55300   1.000 69.81606  ?  1468 GLU   A CA  1 
ATOM   11689 C  C   . GLU   A 1 1470 ? -45.70300  13.67200  1.98400   1.000 76.09058  ?  1468 GLU   A C   1 
ATOM   11690 O  O   . GLU   A 1 1470 ? -46.72800  12.98500  1.91500   1.000 89.41497  ?  1468 GLU   A O   1 
ATOM   11691 C  CB  . GLU   A 1 1470 ? -45.83100  15.21400  0.02800   1.000 62.84443  ?  1468 GLU   A CB  1 
ATOM   11692 C  CG  . GLU   A 1 1470 ? -46.40200  16.52100  -0.49900  1.000 77.63268  ?  1468 GLU   A CG  1 
ATOM   11693 C  CD  . GLU   A 1 1470 ? -46.40900  16.58100  -2.01600  1.000 91.25560  ?  1468 GLU   A CD  1 
ATOM   11694 O  OE1 . GLU   A 1 1470 ? -45.63900  15.82500  -2.64500  1.000 87.54789  ?  1468 GLU   A OE1 1 
ATOM   11695 O  OE2 . GLU   A 1 1470 ? -47.18300  17.38400  -2.57900  1.000 99.69213  -1 1468 GLU   A OE2 1 
ATOM   11696 N  N   . TYR   A 1 1471 ? -44.54100  13.18400  2.41000   1.000 72.74172  ?  1469 TYR   A N   1 
ATOM   11697 C  CA  . TYR   A 1 1471 ? -44.43000  11.84100  2.96000   1.000 71.40681  ?  1469 TYR   A CA  1 
ATOM   11698 C  C   . TYR   A 1 1471 ? -44.64700  11.82000  4.46600   1.000 66.33790  ?  1469 TYR   A C   1 
ATOM   11699 O  O   . TYR   A 1 1471 ? -45.14900  10.82400  5.00000   1.000 78.38576  ?  1469 TYR   A O   1 
ATOM   11700 C  CB  . TYR   A 1 1471 ? -43.05700  11.24500  2.61900   1.000 72.57479  ?  1469 TYR   A CB  1 
ATOM   11701 C  CG  . TYR   A 1 1471 ? -42.79100  9.88800   3.24200   1.000 79.21231  ?  1469 TYR   A CG  1 
ATOM   11702 C  CD1 . TYR   A 1 1471 ? -42.23800  9.78000   4.51500   1.000 76.21429  ?  1469 TYR   A CD1 1 
ATOM   11703 C  CD2 . TYR   A 1 1471 ? -43.09700  8.71700   2.56100   1.000 69.88769  ?  1469 TYR   A CD2 1 
ATOM   11704 C  CE1 . TYR   A 1 1471 ? -42.00200  8.54800   5.09100   1.000 87.76606  ?  1469 TYR   A CE1 1 
ATOM   11705 C  CE2 . TYR   A 1 1471 ? -42.86100  7.47700   3.13000   1.000 75.73777  ?  1469 TYR   A CE2 1 
ATOM   11706 C  CZ  . TYR   A 1 1471 ? -42.31300  7.40000   4.39600   1.000 87.79994  ?  1469 TYR   A CZ  1 
ATOM   11707 O  OH  . TYR   A 1 1471 ? -42.07400  6.17500   4.97600   1.000 99.37286  ?  1469 TYR   A OH  1 
ATOM   11708 N  N   . LEU   A 1 1472 ? -44.29400  12.90200  5.15700   1.000 56.94646  ?  1470 LEU   A N   1 
ATOM   11709 C  CA  . LEU   A 1 1472 ? -44.34300  12.93100  6.61200   1.000 65.57163  ?  1470 LEU   A CA  1 
ATOM   11710 C  C   . LEU   A 1 1472 ? -45.71100  13.30700  7.16300   1.000 76.31712  ?  1470 LEU   A C   1 
ATOM   11711 O  O   . LEU   A 1 1472 ? -45.89800  13.26000  8.38400   1.000 75.31696  ?  1470 LEU   A O   1 
ATOM   11712 C  CB  . LEU   A 1 1472 ? -43.29300  13.90500  7.14900   1.000 65.91171  ?  1470 LEU   A CB  1 
ATOM   11713 C  CG  . LEU   A 1 1472 ? -41.95200  13.28800  7.54500   1.000 59.27825  ?  1470 LEU   A CG  1 
ATOM   11714 C  CD1 . LEU   A 1 1472 ? -41.27200  12.63500  6.35300   1.000 61.10656  ?  1470 LEU   A CD1 1 
ATOM   11715 C  CD2 . LEU   A 1 1472 ? -41.05900  14.33900  8.16000   1.000 62.12721  ?  1470 LEU   A CD2 1 
ATOM   11716 N  N   . GLU   A 1 1473 ? -46.66400  13.67400  6.30300   1.000 90.87437  ?  1471 GLU   A N   1 
ATOM   11717 C  CA  . GLU   A 1 1473 ? -47.98400  14.07100  6.78400   1.000 92.43424  ?  1471 GLU   A CA  1 
ATOM   11718 C  C   . GLU   A 1 1473 ? -48.73700  12.88000  7.36300   1.000 91.92195  ?  1471 GLU   A C   1 
ATOM   11719 O  O   . GLU   A 1 1473 ? -49.26100  12.94700  8.48200   1.000 86.33594  ?  1471 GLU   A O   1 
ATOM   11720 C  CB  . GLU   A 1 1473 ? -48.78300  14.72000  5.65200   1.000 88.72665  ?  1471 GLU   A CB  1 
ATOM   11721 C  CG  . GLU   A 1 1473 ? -48.39000  14.24800  4.26200   1.000 90.45853  ?  1471 GLU   A CG  1 
ATOM   11722 C  CD  . GLU   A 1 1473 ? -49.11700  14.99800  3.15800   1.000 103.29014 ?  1471 GLU   A CD  1 
ATOM   11723 O  OE1 . GLU   A 1 1473 ? -49.09800  16.24700  3.17400   1.000 106.91574 ?  1471 GLU   A OE1 1 
ATOM   11724 O  OE2 . GLU   A 1 1473 ? -49.70000  14.34100  2.27000   1.000 115.39027 ?  1471 GLU   A OE2 1 
ATOM   11725 N  N   . GLY   A 1 1474 ? -48.80100  11.78000  6.61800   1.000 77.29911  ?  1472 GLY   A N   1 
ATOM   11726 C  CA  . GLY   A 1 1474 ? -49.41800  10.57100  7.12400   1.000 90.69709  ?  1472 GLY   A CA  1 
ATOM   11727 C  C   . GLY   A 1 1474 ? -48.42900  9.68700   7.85400   1.000 101.50781 ?  1472 GLY   A C   1 
ATOM   11728 O  O   . GLY   A 1 1474 ? -48.32000  8.49200   7.56200   1.000 105.77031 ?  1472 GLY   A O   1 
ATOM   11729 N  N   . ARG   A 1 1475 ? -47.70200  10.26400  8.81000   1.000 93.60370  ?  1473 ARG   A N   1 
ATOM   11730 C  CA  . ARG   A 1 1475 ? -46.65200  9.55600   9.52500   1.000 79.43333  ?  1473 ARG   A CA  1 
ATOM   11731 C  C   . ARG   A 1 1475 ? -46.66300  9.97900   10.98700  1.000 86.35186  ?  1473 ARG   A C   1 
ATOM   11732 O  O   . ARG   A 1 1475 ? -47.22300  11.01600  11.35300  1.000 88.45308  ?  1473 ARG   A O   1 
ATOM   11733 C  CB  . ARG   A 1 1475 ? -45.27500  9.82400   8.89900   1.000 82.29059  ?  1473 ARG   A CB  1 
ATOM   11734 C  CG  . ARG   A 1 1475 ? -44.37100  8.60600   8.80400   1.000 72.27143  ?  1473 ARG   A CG  1 
ATOM   11735 C  CD  . ARG   A 1 1475 ? -44.77000  7.69200   7.65600   1.000 72.97831  ?  1473 ARG   A CD  1 
ATOM   11736 N  NE  . ARG   A 1 1475 ? -44.27800  6.33400   7.86000   1.000 89.76625  ?  1473 ARG   A NE  1 
ATOM   11737 C  CZ  . ARG   A 1 1475 ? -44.42300  5.34200   6.99200   1.000 90.99482  ?  1473 ARG   A CZ  1 
ATOM   11738 N  NH1 . ARG   A 1 1475 ? -45.04600  5.51700   5.83800   1.000 84.60988  ?  1473 ARG   A NH1 1 
ATOM   11739 N  NH2 . ARG   A 1 1475 ? -43.93300  4.14100   7.29100   1.000 96.09711  ?  1473 ARG   A NH2 1 
ATOM   11740 N  N   . THR   A 1 1476 ? -46.02700  9.15500   11.82700  1.000 86.10038  ?  1474 THR   A N   1 
ATOM   11741 C  CA  . THR   A 1 1476 ? -45.97400  9.45800   13.25300  1.000 84.15942  ?  1474 THR   A CA  1 
ATOM   11742 C  C   . THR   A 1 1476 ? -44.68600  8.99000   13.92400  1.000 81.75512  ?  1474 THR   A C   1 
ATOM   11743 O  O   . THR   A 1 1476 ? -44.63700  8.97000   15.16100  1.000 82.62128  ?  1474 THR   A O   1 
ATOM   11744 C  CB  . THR   A 1 1476 ? -47.17000  8.83100   13.98100  1.000 97.34680  ?  1474 THR   A CB  1 
ATOM   11745 O  OG1 . THR   A 1 1476 ? -47.13100  9.20100   15.36600  1.000 105.89430 ?  1474 THR   A OG1 1 
ATOM   11746 C  CG2 . THR   A 1 1476 ? -47.13000  7.31100   13.86200  1.000 81.42941  ?  1474 THR   A CG2 1 
ATOM   11747 N  N   . GLU   A 1 1477 ? -43.65300  8.61500   13.17100  1.000 79.39723  ?  1475 GLU   A N   1 
ATOM   11748 C  CA  . GLU   A 1 1477 ? -42.41700  8.13700   13.77400  1.000 71.38678  ?  1475 GLU   A CA  1 
ATOM   11749 C  C   . GLU   A 1 1477 ? -41.78400  9.21800   14.64300  1.000 74.39061  ?  1475 GLU   A C   1 
ATOM   11750 O  O   . GLU   A 1 1477 ? -41.89700  10.41600  14.36700  1.000 89.55157  ?  1475 GLU   A O   1 
ATOM   11751 C  CB  . GLU   A 1 1477 ? -41.43100  7.70200   12.68800  1.000 76.38527  ?  1475 GLU   A CB  1 
ATOM   11752 C  CG  . GLU   A 1 1477 ? -41.73700  6.35400   12.04500  1.000 77.94553  ?  1475 GLU   A CG  1 
ATOM   11753 C  CD  . GLU   A 1 1477 ? -42.81900  6.43700   10.98400  1.000 84.29669  ?  1475 GLU   A CD  1 
ATOM   11754 O  OE1 . GLU   A 1 1477 ? -43.96600  6.79700   11.32400  1.000 93.38764  ?  1475 GLU   A OE1 1 
ATOM   11755 O  OE2 . GLU   A 1 1477 ? -42.52000  6.14900   9.80500   1.000 73.76178  -1 1475 GLU   A OE2 1 
ATOM   11756 N  N   . ALA   A 1 1478 ? -41.11800  8.78300   15.71000  1.000 63.56743  ?  1476 ALA   A N   1 
ATOM   11757 C  CA  . ALA   A 1 1478 ? -40.41200  9.71300   16.57900  1.000 83.11707  ?  1476 ALA   A CA  1 
ATOM   11758 C  C   . ALA   A 1 1478 ? -39.23700  10.34200  15.83800  1.000 90.30167  ?  1476 ALA   A C   1 
ATOM   11759 O  O   . ALA   A 1 1478 ? -38.64500  9.74000   14.94000  1.000 82.26664  ?  1476 ALA   A O   1 
ATOM   11760 C  CB  . ALA   A 1 1478 ? -39.91800  9.00200   17.83800  1.000 76.58491  ?  1476 ALA   A CB  1 
ATOM   11761 N  N   . ASN   A 1 1479 ? -38.90300  11.57200  16.21700  1.000 92.02791  ?  1477 ASN   A N   1 
ATOM   11762 C  CA  . ASN   A 1 1479 ? -37.82200  12.28800  15.56100  1.000 69.62457  ?  1477 ASN   A CA  1 
ATOM   11763 C  C   . ASN   A 1 1479 ? -37.01500  13.06200  16.59100  1.000 69.04991  ?  1477 ASN   A C   1 
ATOM   11764 O  O   . ASN   A 1 1479 ? -37.54900  13.55400  17.58800  1.000 78.79926  ?  1477 ASN   A O   1 
ATOM   11765 C  CB  . ASN   A 1 1479 ? -38.34300  13.24800  14.48100  1.000 54.15697  ?  1477 ASN   A CB  1 
ATOM   11766 C  CG  . ASN   A 1 1479 ? -39.67000  13.87300  14.84900  1.000 88.37298  ?  1477 ASN   A CG  1 
ATOM   11767 O  OD1 . ASN   A 1 1479 ? -40.68200  13.18300  14.97400  1.000 104.98493 ?  1477 ASN   A OD1 1 
ATOM   11768 N  ND2 . ASN   A 1 1479 ? -39.67400  15.18900  15.03000  1.000 108.41260 ?  1477 ASN   A ND2 1 
ATOM   11769 N  N   . ARG   A 1 1480 ? -35.71400  13.14600  16.33900  1.000 77.15491  ?  1478 ARG   A N   1 
ATOM   11770 C  CA  . ARG   A 1 1480 ? -34.80700  13.99100  17.09700  1.000 63.61420  ?  1478 ARG   A CA  1 
ATOM   11771 C  C   . ARG   A 1 1480 ? -34.45100  15.26100  16.33800  1.000 63.48763  ?  1478 ARG   A C   1 
ATOM   11772 O  O   . ARG   A 1 1480 ? -33.70400  16.09500  16.86000  1.000 61.54411  ?  1478 ARG   A O   1 
ATOM   11773 C  CB  . ARG   A 1 1480 ? -33.53500  13.20900  17.44500  1.000 59.49775  ?  1478 ARG   A CB  1 
ATOM   11774 C  CG  . ARG   A 1 1480 ? -32.83200  13.67500  18.70600  1.000 65.55043  ?  1478 ARG   A CG  1 
ATOM   11775 C  CD  . ARG   A 1 1480 ? -31.62700  12.80400  19.02100  1.000 69.47043  ?  1478 ARG   A CD  1 
ATOM   11776 N  NE  . ARG   A 1 1480 ? -30.46500  13.59000  19.42100  1.000 64.80628  ?  1478 ARG   A NE  1 
ATOM   11777 C  CZ  . ARG   A 1 1480 ? -30.35100  14.24000  20.57200  1.000 83.71553  ?  1478 ARG   A CZ  1 
ATOM   11778 N  NH1 . ARG   A 1 1480 ? -31.31300  14.21700  21.48100  1.000 83.63677  ?  1478 ARG   A NH1 1 
ATOM   11779 N  NH2 . ARG   A 1 1480 ? -29.24100  14.93100  20.81900  1.000 85.20420  ?  1478 ARG   A NH2 1 
ATOM   11780 N  N   . LEU   A 1 1481 ? -34.99000  15.42600  15.13000  1.000 67.90290  ?  1479 LEU   A N   1 
ATOM   11781 C  CA  . LEU   A 1 1481 ? -34.61200  16.52300  14.24900  1.000 60.11934  ?  1479 LEU   A CA  1 
ATOM   11782 C  C   . LEU   A 1 1481 ? -34.82100  17.87600  14.91900  1.000 64.59408  ?  1479 LEU   A C   1 
ATOM   11783 O  O   . LEU   A 1 1481 ? -35.77500  18.07600  15.67600  1.000 80.33175  ?  1479 LEU   A O   1 
ATOM   11784 C  CB  . LEU   A 1 1481 ? -35.41800  16.44100  12.95200  1.000 56.58076  ?  1479 LEU   A CB  1 
ATOM   11785 C  CG  . LEU   A 1 1481 ? -34.84700  17.12800  11.71200  1.000 67.17599  ?  1479 LEU   A CG  1 
ATOM   11786 C  CD1 . LEU   A 1 1481 ? -33.55900  16.46500  11.24500  1.000 61.26730  ?  1479 LEU   A CD1 1 
ATOM   11787 C  CD2 . LEU   A 1 1481 ? -35.88700  17.12300  10.60100  1.000 49.68634  ?  1479 LEU   A CD2 1 
ATOM   11788 N  N   . ARG   A 1 1482 ? -33.91600  18.80600  14.63400  1.000 61.28942  ?  1480 ARG   A N   1 
ATOM   11789 C  CA  . ARG   A 1 1482 ? -33.91400  20.11500  15.27900  1.000 61.27193  ?  1480 ARG   A CA  1 
ATOM   11790 C  C   . ARG   A 1 1482 ? -33.89700  21.27400  14.29400  1.000 60.31168  ?  1480 ARG   A C   1 
ATOM   11791 O  O   . ARG   A 1 1482 ? -34.58600  22.27100  14.52300  1.000 79.51654  ?  1480 ARG   A O   1 
ATOM   11792 C  CB  . ARG   A 1 1482 ? -32.71100  20.22700  16.23000  1.000 41.47459  ?  1480 ARG   A CB  1 
ATOM   11793 C  CG  . ARG   A 1 1482 ? -33.09700  20.49100  17.67200  1.000 60.94728  ?  1480 ARG   A CG  1 
ATOM   11794 C  CD  . ARG   A 1 1482 ? -32.02800  21.29100  18.38500  1.000 57.21869  ?  1480 ARG   A CD  1 
ATOM   11795 N  NE  . ARG   A 1 1482 ? -30.73700  20.61700  18.36400  1.000 65.30597  ?  1480 ARG   A NE  1 
ATOM   11796 C  CZ  . ARG   A 1 1482 ? -30.36000  19.70300  19.24700  1.000 76.59629  ?  1480 ARG   A CZ  1 
ATOM   11797 N  NH1 . ARG   A 1 1482 ? -31.16400  19.31200  20.22300  1.000 89.03956  ?  1480 ARG   A NH1 1 
ATOM   11798 N  NH2 . ARG   A 1 1482 ? -29.14700  19.17000  19.15000  1.000 71.37888  ?  1480 ARG   A NH2 1 
ATOM   11799 N  N   . TYR   A 1 1483 ? -33.12800  21.17400  13.20900  1.000 54.86883  ?  1481 TYR   A N   1 
ATOM   11800 C  CA  . TYR   A 1 1483 ? -32.99800  22.25000  12.23300  1.000 47.36948  ?  1481 TYR   A CA  1 
ATOM   11801 C  C   . TYR   A 1 1483 ? -33.14700  21.69300  10.82500  1.000 55.76799  ?  1481 TYR   A C   1 
ATOM   11802 O  O   . TYR   A 1 1483 ? -32.48900  20.70900  10.47100  1.000 57.50792  ?  1481 TYR   A O   1 
ATOM   11803 C  CB  . TYR   A 1 1483 ? -31.64300  22.96200  12.34800  1.000 53.26669  ?  1481 TYR   A CB  1 
ATOM   11804 C  CG  . TYR   A 1 1483 ? -31.18400  23.26600  13.75600  1.000 59.85773  ?  1481 TYR   A CG  1 
ATOM   11805 C  CD1 . TYR   A 1 1483 ? -31.64800  24.38400  14.43600  1.000 49.59029  ?  1481 TYR   A CD1 1 
ATOM   11806 C  CD2 . TYR   A 1 1483 ? -30.26400  22.44600  14.39600  1.000 60.96053  ?  1481 TYR   A CD2 1 
ATOM   11807 C  CE1 . TYR   A 1 1483 ? -31.21900  24.66700  15.72200  1.000 50.10217  ?  1481 TYR   A CE1 1 
ATOM   11808 C  CE2 . TYR   A 1 1483 ? -29.83100  22.72000  15.67800  1.000 66.96548  ?  1481 TYR   A CE2 1 
ATOM   11809 C  CZ  . TYR   A 1 1483 ? -30.30900  23.82900  16.33600  1.000 60.15283  ?  1481 TYR   A CZ  1 
ATOM   11810 O  OH  . TYR   A 1 1483 ? -29.87100  24.09200  17.61300  1.000 62.21731  ?  1481 TYR   A OH  1 
ATOM   11811 N  N   . ILE   A 1 1484 ? -33.99500  22.32900  10.02300  1.000 57.69103  ?  1482 ILE   A N   1 
ATOM   11812 C  CA  . ILE   A 1 1484 ? -34.08200  22.06600  8.59200   1.000 46.84892  ?  1482 ILE   A CA  1 
ATOM   11813 C  C   . ILE   A 1 1484 ? -33.51100  23.29600  7.89800   1.000 49.25100  ?  1482 ILE   A C   1 
ATOM   11814 O  O   . ILE   A 1 1484 ? -34.17800  24.33100  7.79300   1.000 56.67801  ?  1482 ILE   A O   1 
ATOM   11815 C  CB  . ILE   A 1 1484 ? -35.51700  21.77300  8.13800   1.000 48.99677  ?  1482 ILE   A CB  1 
ATOM   11816 C  CG1 . ILE   A 1 1484 ? -35.98600  20.43100  8.70200   1.000 52.93427  ?  1482 ILE   A CG1 1 
ATOM   11817 C  CG2 . ILE   A 1 1484 ? -35.60500  21.76200  6.61100   1.000 52.98726  ?  1482 ILE   A CG2 1 
ATOM   11818 C  CD1 . ILE   A 1 1484 ? -37.08800  19.77700  7.90000   1.000 67.18632  ?  1482 ILE   A CD1 1 
ATOM   11819 N  N   . LEU   A 1 1485 ? -32.26400  23.19500  7.43900   1.000 54.67393  ?  1483 LEU   A N   1 
ATOM   11820 C  CA  . LEU   A 1 1485 ? -31.56200  24.31200  6.81400   1.000 43.14485  ?  1483 LEU   A CA  1 
ATOM   11821 C  C   . LEU   A 1 1485 ? -31.79400  24.26100  5.30800   1.000 51.14523  ?  1483 LEU   A C   1 
ATOM   11822 O  O   . LEU   A 1 1485 ? -31.32700  23.33800  4.63200   1.000 51.45710  ?  1483 LEU   A O   1 
ATOM   11823 C  CB  . LEU   A 1 1485 ? -30.07100  24.26100  7.14200   1.000 49.68694  ?  1483 LEU   A CB  1 
ATOM   11824 C  CG  . LEU   A 1 1485 ? -29.65800  24.39000  8.61100   1.000 50.69027  ?  1483 LEU   A CG  1 
ATOM   11825 C  CD1 . LEU   A 1 1485 ? -30.58800  25.34100  9.35700   1.000 48.60623  ?  1483 LEU   A CD1 1 
ATOM   11826 C  CD2 . LEU   A 1 1485 ? -29.59800  23.02600  9.29000   1.000 66.85878  ?  1483 LEU   A CD2 1 
ATOM   11827 N  N   . ALA   A 1 1486 ? -32.50100  25.25900  4.78100   1.000 49.11143  ?  1484 ALA   A N   1 
ATOM   11828 C  CA  . ALA   A 1 1486 ? -32.89600  25.30000  3.37900   1.000 47.01404  ?  1484 ALA   A CA  1 
ATOM   11829 C  C   . ALA   A 1 1486 ? -32.05400  26.31000  2.61000   1.000 37.79618  ?  1484 ALA   A C   1 
ATOM   11830 O  O   . ALA   A 1 1486 ? -31.77300  27.40500  3.10700   1.000 47.20852  ?  1484 ALA   A O   1 
ATOM   11831 C  CB  . ALA   A 1 1486 ? -34.37900  25.65200  3.24200   1.000 46.18335  ?  1484 ALA   A CB  1 
ATOM   11832 N  N   . CYS   A 1 1487 ? -31.66500  25.93600  1.39100   1.000 39.99992  ?  1485 CYS   A N   1 
ATOM   11833 C  CA  . CYS   A 1 1487 ? -30.85300  26.77300  0.51500   1.000 47.67024  ?  1485 CYS   A CA  1 
ATOM   11834 C  C   . CYS   A 1 1487 ? -30.87000  26.17900  -0.88400  1.000 47.42554  ?  1485 CYS   A C   1 
ATOM   11835 O  O   . CYS   A 1 1487 ? -31.05900  24.97100  -1.05300  1.000 60.51552  ?  1485 CYS   A O   1 
ATOM   11836 C  CB  . CYS   A 1 1487 ? -29.40700  26.88900  1.01600   1.000 42.33180  ?  1485 CYS   A CB  1 
ATOM   11837 S  SG  . CYS   A 1 1487 ? -28.30400  27.82400  -0.07800  1.000 56.63706  ?  1485 CYS   A SG  1 
ATOM   11838 N  N   . GLY   A 1 1488 ? -30.66000  27.03700  -1.87900  1.000 45.25196  ?  1486 GLY   A N   1 
ATOM   11839 C  CA  . GLY   A 1 1488 ? -30.61500  26.59100  -3.25800  1.000 40.53470  ?  1486 GLY   A CA  1 
ATOM   11840 C  C   . GLY   A 1 1488 ? -31.57900  27.33200  -4.15800  1.000 52.43234  ?  1486 GLY   A C   1 
ATOM   11841 O  O   . GLY   A 1 1488 ? -31.24500  27.66500  -5.29900  1.000 61.38564  ?  1486 GLY   A O   1 
ATOM   11842 N  N   . GLU   A 1 1489 ? -32.78200  27.59200  -3.65200  1.000 62.17853  ?  1487 GLU   A N   1 
ATOM   11843 C  CA  . GLU   A 1 1489 ? -33.79200  28.32600  -4.39700  1.000 51.83722  ?  1487 GLU   A CA  1 
ATOM   11844 C  C   . GLU   A 1 1489 ? -34.63000  29.12400  -3.41000  1.000 51.63613  ?  1487 GLU   A C   1 
ATOM   11845 O  O   . GLU   A 1 1489 ? -34.46300  29.01900  -2.19200  1.000 51.66978  ?  1487 GLU   A O   1 
ATOM   11846 C  CB  . GLU   A 1 1489 ? -34.67000  27.38400  -5.23300  1.000 57.61300  ?  1487 GLU   A CB  1 
ATOM   11847 C  CG  . GLU   A 1 1489 ? -34.83900  25.99400  -4.63700  1.000 68.36228  ?  1487 GLU   A CG  1 
ATOM   11848 C  CD  . GLU   A 1 1489 ? -35.36300  24.98100  -5.64100  1.000 76.27909  ?  1487 GLU   A CD  1 
ATOM   11849 O  OE1 . GLU   A 1 1489 ? -36.59900  24.87200  -5.79600  1.000 88.53352  ?  1487 GLU   A OE1 1 
ATOM   11850 O  OE2 . GLU   A 1 1489 ? -34.53900  24.28200  -6.26700  1.000 82.71796  -1 1487 GLU   A OE2 1 
ATOM   11851 N  N   . ALA   A 1 1490 ? -35.53300  29.93600  -3.95100  1.000 54.29150  ?  1488 ALA   A N   1 
ATOM   11852 C  CA  . ALA   A 1 1490 ? -36.43900  30.69700  -3.10700  1.000 50.38597  ?  1488 ALA   A CA  1 
ATOM   11853 C  C   . ALA   A 1 1490 ? -37.41900  29.75900  -2.41800  1.000 59.15674  ?  1488 ALA   A C   1 
ATOM   11854 O  O   . ALA   A 1 1490 ? -37.89700  28.78800  -3.01300  1.000 62.75687  ?  1488 ALA   A O   1 
ATOM   11855 C  CB  . ALA   A 1 1490 ? -37.19100  31.73500  -3.93600  1.000 55.85193  ?  1488 ALA   A CB  1 
ATOM   11856 N  N   . MET   A 1 1491 ? -37.70700  30.04000  -1.15400  1.000 47.06796  ?  1489 MET   A N   1 
ATOM   11857 C  CA  . MET   A 1 1491 ? -38.63200  29.20100  -0.40900  1.000 61.61431  ?  1489 MET   A CA  1 
ATOM   11858 C  C   . MET   A 1 1491 ? -40.06200  29.64100  -0.68800  1.000 70.30053  ?  1489 MET   A C   1 
ATOM   11859 O  O   . MET   A 1 1491 ? -40.41200  30.79100  -0.39900  1.000 69.11377  ?  1489 MET   A O   1 
ATOM   11860 C  CB  . MET   A 1 1491 ? -38.35500  29.27000  1.08300   1.000 56.82357  ?  1489 MET   A CB  1 
ATOM   11861 C  CG  . MET   A 1 1491 ? -39.39300  28.52400  1.89900   1.000 60.65996  ?  1489 MET   A CG  1 
ATOM   11862 S  SD  . MET   A 1 1491 ? -38.99400  28.45900  3.64700   1.000 89.00814  ?  1489 MET   A SD  1 
ATOM   11863 C  CE  . MET   A 1 1491 ? -37.51500  27.45300  3.62900   1.000 64.45570  ?  1489 MET   A CE  1 
ATOM   11864 N  N   . PRO   A 1 1492 ? -40.90700  28.77900  -1.24900  1.000 71.80159  ?  1490 PRO   A N   1 
ATOM   11865 C  CA  . PRO   A 1 1492 ? -42.31500  29.14500  -1.43000  1.000 61.43029  ?  1490 PRO   A CA  1 
ATOM   11866 C  C   . PRO   A 1 1492 ? -42.97400  29.42400  -0.08800  1.000 71.02794  ?  1490 PRO   A C   1 
ATOM   11867 O  O   . PRO   A 1 1492 ? -42.77100  28.69700  0.88700   1.000 85.45660  ?  1490 PRO   A O   1 
ATOM   11868 C  CB  . PRO   A 1 1492 ? -42.91800  27.91500  -2.11800  1.000 73.31296  ?  1490 PRO   A CB  1 
ATOM   11869 C  CG  . PRO   A 1 1492 ? -41.74600  27.20200  -2.72800  1.000 67.52009  ?  1490 PRO   A CG  1 
ATOM   11870 C  CD  . PRO   A 1 1492 ? -40.60300  27.44600  -1.79500  1.000 60.75809  ?  1490 PRO   A CD  1 
ATOM   11871 N  N   . ASP   A 1 1493 ? -43.76000  30.50200  -0.04300  1.000 68.95081  ?  1491 ASP   A N   1 
ATOM   11872 C  CA  . ASP   A 1 1493 ? -44.36900  30.92400  1.21500   1.000 71.01379  ?  1491 ASP   A CA  1 
ATOM   11873 C  C   . ASP   A 1 1493 ? -45.28800  29.85200  1.78500   1.000 75.24426  ?  1491 ASP   A C   1 
ATOM   11874 O  O   . ASP   A 1 1493 ? -45.44200  29.75300  3.00900   1.000 73.65451  ?  1491 ASP   A O   1 
ATOM   11875 C  CB  . ASP   A 1 1493 ? -45.13700  32.22700  1.00800   1.000 75.82328  ?  1491 ASP   A CB  1 
ATOM   11876 C  CG  . ASP   A 1 1493 ? -44.39600  33.20300  0.11700   1.000 86.59208  ?  1491 ASP   A CG  1 
ATOM   11877 O  OD1 . ASP   A 1 1493 ? -44.05300  32.82400  -1.02300  1.000 76.27650  ?  1491 ASP   A OD1 1 
ATOM   11878 O  OD2 . ASP   A 1 1493 ? -44.15700  34.34700  0.55500   1.000 103.32049 -1 1491 ASP   A OD2 1 
ATOM   11879 N  N   . GLU   A 1 1494 ? -45.90000  29.04000  0.91900   1.000 71.24920  ?  1492 GLU   A N   1 
ATOM   11880 C  CA  . GLU   A 1 1494 ? -46.78800  27.97500  1.36700   1.000 75.27861  ?  1492 GLU   A CA  1 
ATOM   11881 C  C   . GLU   A 1 1494 ? -46.04000  26.85400  2.07700   1.000 77.81482  ?  1492 GLU   A C   1 
ATOM   11882 O  O   . GLU   A 1 1494 ? -46.66400  26.07000  2.79900   1.000 77.08613  ?  1492 GLU   A O   1 
ATOM   11883 C  CB  . GLU   A 1 1494 ? -47.56000  27.40100  0.17700   1.000 59.76132  ?  1492 GLU   A CB  1 
ATOM   11884 C  CG  . GLU   A 1 1494 ? -46.66800  26.90600  -0.95700  1.000 72.04677  ?  1492 GLU   A CG  1 
ATOM   11885 C  CD  . GLU   A 1 1494 ? -46.43100  27.96100  -2.02300  1.000 78.29023  ?  1492 GLU   A CD  1 
ATOM   11886 O  OE1 . GLU   A 1 1494 ? -46.45900  29.16300  -1.68500  1.000 72.42708  ?  1492 GLU   A OE1 1 
ATOM   11887 O  OE2 . GLU   A 1 1494 ? -46.20600  27.58900  -3.19600  1.000 70.81542  -1 1492 GLU   A OE2 1 
ATOM   11888 N  N   . LEU   A 1 1495 ? -44.72200  26.76200  1.88900   1.000 71.01032  ?  1493 LEU   A N   1 
ATOM   11889 C  CA  . LEU   A 1 1495 ? -43.96600  25.65800  2.46800   1.000 62.01656  ?  1493 LEU   A CA  1 
ATOM   11890 C  C   . LEU   A 1 1495 ? -43.79600  25.80500  3.97500   1.000 67.73936  ?  1493 LEU   A C   1 
ATOM   11891 O  O   . LEU   A 1 1495 ? -43.76500  24.79600  4.68800   1.000 71.89396  ?  1493 LEU   A O   1 
ATOM   11892 C  CB  . LEU   A 1 1495 ? -42.59900  25.55300  1.79100   1.000 69.16058  ?  1493 LEU   A CB  1 
ATOM   11893 C  CG  . LEU   A 1 1495 ? -41.89200  24.20100  1.88000   1.000 64.66722  ?  1493 LEU   A CG  1 
ATOM   11894 C  CD1 . LEU   A 1 1495 ? -42.88600  23.06700  1.67800   1.000 65.76518  ?  1493 LEU   A CD1 1 
ATOM   11895 C  CD2 . LEU   A 1 1495 ? -40.76500  24.13300  0.86300   1.000 65.80171  ?  1493 LEU   A CD2 1 
ATOM   11896 N  N   . VAL   A 1 1496 ? -43.67700  27.04000  4.47600   1.000 62.82087  ?  1494 VAL   A N   1 
ATOM   11897 C  CA  . VAL   A 1 1496 ? -43.42400  27.24500  5.90600   1.000 69.65844  ?  1494 VAL   A CA  1 
ATOM   11898 C  C   . VAL   A 1 1496 ? -44.47900  26.57100  6.78500   1.000 70.13369  ?  1494 VAL   A C   1 
ATOM   11899 O  O   . VAL   A 1 1496 ? -44.10100  25.83100  7.70300   1.000 61.57449  ?  1494 VAL   A O   1 
ATOM   11900 C  CB  . VAL   A 1 1496 ? -43.25900  28.74200  6.20800   1.000 66.64900  ?  1494 VAL   A CB  1 
ATOM   11901 C  CG1 . VAL   A 1 1496 ? -43.20600  28.98700  7.71500   1.000 56.35215  ?  1494 VAL   A CG1 1 
ATOM   11902 C  CG2 . VAL   A 1 1496 ? -42.00800  29.29000  5.53800   1.000 67.84191  ?  1494 VAL   A CG2 1 
ATOM   11903 N  N   . PRO   A 1 1497 ? -45.78800  26.76400  6.56600   1.000 86.27810  ?  1495 PRO   A N   1 
ATOM   11904 C  CA  . PRO   A 1 1497 ? -46.75400  26.03900  7.41100   1.000 82.89777  ?  1495 PRO   A CA  1 
ATOM   11905 C  C   . PRO   A 1 1497 ? -46.77400  24.54400  7.14400   1.000 79.96866  ?  1495 PRO   A C   1 
ATOM   11906 O  O   . PRO   A 1 1497 ? -46.93300  23.75800  8.08600   1.000 75.82272  ?  1495 PRO   A O   1 
ATOM   11907 C  CB  . PRO   A 1 1497 ? -48.09800  26.70200  7.06600   1.000 80.09005  ?  1495 PRO   A CB  1 
ATOM   11908 C  CG  . PRO   A 1 1497 ? -47.75000  27.97000  6.35200   1.000 70.42425  ?  1495 PRO   A CG  1 
ATOM   11909 C  CD  . PRO   A 1 1497 ? -46.47000  27.68900  5.64400   1.000 78.05718  ?  1495 PRO   A CD  1 
ATOM   11910 N  N   . LYS   A 1 1498 ? -46.61900  24.13000  5.88100   1.000 72.58800  ?  1496 LYS   A N   1 
ATOM   11911 C  CA  . LYS   A 1 1498 ? -46.54700  22.70700  5.55900   1.000 69.29346  ?  1496 LYS   A CA  1 
ATOM   11912 C  C   . LYS   A 1 1498 ? -45.46000  22.00700  6.36700   1.000 79.15883  ?  1496 LYS   A C   1 
ATOM   11913 O  O   . LYS   A 1 1498 ? -45.63200  20.86000  6.79500   1.000 80.40814  ?  1496 LYS   A O   1 
ATOM   11914 C  CB  . LYS   A 1 1498 ? -46.28400  22.51700  4.06400   1.000 65.45563  ?  1496 LYS   A CB  1 
ATOM   11915 C  CG  . LYS   A 1 1498 ? -47.45000  22.84600  3.15100   1.000 61.53175  ?  1496 LYS   A CG  1 
ATOM   11916 C  CD  . LYS   A 1 1498 ? -47.34300  22.05800  1.85300   1.000 71.95916  ?  1496 LYS   A CD  1 
ATOM   11917 C  CE  . LYS   A 1 1498 ? -47.78700  22.88100  0.65200   1.000 87.82946  ?  1496 LYS   A CE  1 
ATOM   11918 N  NZ  . LYS   A 1 1498 ? -46.94600  22.60500  -0.55000  1.000 75.94165  ?  1496 LYS   A NZ  1 
ATOM   11919 N  N   . VAL   A 1 1499 ? -44.33000  22.68400  6.58000   1.000 79.46918  ?  1497 VAL   A N   1 
ATOM   11920 C  CA  . VAL   A 1 1499 ? -43.23000  22.08400  7.32900   1.000 71.48822  ?  1497 VAL   A CA  1 
ATOM   11921 C  C   . VAL   A 1 1499 ? -43.57800  21.99600  8.81000   1.000 64.15418  ?  1497 VAL   A C   1 
ATOM   11922 O  O   . VAL   A 1 1499 ? -43.47300  20.92900  9.42700   1.000 65.35553  ?  1497 VAL   A O   1 
ATOM   11923 C  CB  . VAL   A 1 1499 ? -41.93100  22.87900  7.09600   1.000 58.54530  ?  1497 VAL   A CB  1 
ATOM   11924 C  CG1 . VAL   A 1 1499 ? -40.82900  22.39000  8.02200   1.000 56.37079  ?  1497 VAL   A CG1 1 
ATOM   11925 C  CG2 . VAL   A 1 1499 ? -41.49700  22.76000  5.64400   1.000 49.10696  ?  1497 VAL   A CG2 1 
ATOM   11926 N  N   . TYR   A 1 1500 ? -44.00900  23.11100  9.40000   1.000 55.77125  ?  1498 TYR   A N   1 
ATOM   11927 C  CA  . TYR   A 1 1500 ? -44.28900  23.13500  10.83000  1.000 67.38025  ?  1498 TYR   A CA  1 
ATOM   11928 C  C   . TYR   A 1 1500 ? -45.51000  22.30900  11.21600  1.000 77.02166  ?  1498 TYR   A C   1 
ATOM   11929 O  O   . TYR   A 1 1500 ? -45.76100  22.13600  12.41300  1.000 74.88728  ?  1498 TYR   A O   1 
ATOM   11930 C  CB  . TYR   A 1 1500 ? -44.46800  24.57800  11.30400  1.000 75.61901  ?  1498 TYR   A CB  1 
ATOM   11931 C  CG  . TYR   A 1 1500 ? -43.16900  25.32900  11.50500  1.000 79.19769  ?  1498 TYR   A CG  1 
ATOM   11932 C  CD1 . TYR   A 1 1500 ? -42.38400  25.10800  12.62900  1.000 78.94417  ?  1498 TYR   A CD1 1 
ATOM   11933 C  CD2 . TYR   A 1 1500 ? -42.73200  26.26400  10.57500  1.000 72.96299  ?  1498 TYR   A CD2 1 
ATOM   11934 C  CE1 . TYR   A 1 1500 ? -41.20000  25.79500  12.82000  1.000 77.84296  ?  1498 TYR   A CE1 1 
ATOM   11935 C  CE2 . TYR   A 1 1500 ? -41.54700  26.95600  10.75900  1.000 74.33281  ?  1498 TYR   A CE2 1 
ATOM   11936 C  CZ  . TYR   A 1 1500 ? -40.78600  26.71700  11.88300  1.000 70.49147  ?  1498 TYR   A CZ  1 
ATOM   11937 O  OH  . TYR   A 1 1500 ? -39.60700  27.40100  12.07300  1.000 71.04982  ?  1498 TYR   A OH  1 
ATOM   11938 N  N   . GLU   A 1 1501 ? -46.27100  21.79600  10.24800  1.000 74.97258  ?  1499 GLU   A N   1 
ATOM   11939 C  CA  . GLU   A 1 1501 ? -47.39100  20.91800  10.56300  1.000 73.43940  ?  1499 GLU   A CA  1 
ATOM   11940 C  C   . GLU   A 1 1501 ? -46.99200  19.44800  10.56900  1.000 77.98631  ?  1499 GLU   A C   1 
ATOM   11941 O  O   . GLU   A 1 1501 ? -47.53200  18.67300  11.36800  1.000 82.07357  ?  1499 GLU   A O   1 
ATOM   11942 C  CB  . GLU   A 1 1501 ? -48.54700  21.15100  9.58000   1.000 71.82301  ?  1499 GLU   A CB  1 
ATOM   11943 C  CG  . GLU   A 1 1501 ? -48.53500  20.26200  8.34200   1.000 80.31859  ?  1499 GLU   A CG  1 
ATOM   11944 C  CD  . GLU   A 1 1501 ? -49.84000  20.30500  7.57200   1.000 98.72363  ?  1499 GLU   A CD  1 
ATOM   11945 O  OE1 . GLU   A 1 1501 ? -50.87600  19.88900  8.13400   1.000 105.58411 ?  1499 GLU   A OE1 1 
ATOM   11946 O  OE2 . GLU   A 1 1501 ? -49.83000  20.74800  6.40300   1.000 84.21890  ?  1499 GLU   A OE2 1 
ATOM   11947 N  N   . VAL   A 1 1502 ? -46.05100  19.04800  9.71300   1.000 79.58976  ?  1500 VAL   A N   1 
ATOM   11948 C  CA  . VAL   A 1 1502 ? -45.55500  17.67800  9.73200   1.000 68.94226  ?  1500 VAL   A CA  1 
ATOM   11949 C  C   . VAL   A 1 1502 ? -44.42600  17.49500  10.73700  1.000 68.29737  ?  1500 VAL   A C   1 
ATOM   11950 O  O   . VAL   A 1 1502 ? -44.17600  16.36300  11.17500  1.000 82.17311  ?  1500 VAL   A O   1 
ATOM   11951 C  CB  . VAL   A 1 1502 ? -45.08200  17.23600  8.33500   1.000 71.12280  ?  1500 VAL   A CB  1 
ATOM   11952 C  CG1 . VAL   A 1 1502 ? -46.20600  17.38200  7.32400   1.000 66.10537  ?  1500 VAL   A CG1 1 
ATOM   11953 C  CG2 . VAL   A 1 1502 ? -43.86000  18.03400  7.90200   1.000 69.89439  ?  1500 VAL   A CG2 1 
ATOM   11954 N  N   . LEU   A 1 1503 ? -43.74200  18.57200  11.11700  1.000 66.56647  ?  1501 LEU   A N   1 
ATOM   11955 C  CA  . LEU   A 1 1503 ? -42.65300  18.51300  12.09100  1.000 76.63116  ?  1501 LEU   A CA  1 
ATOM   11956 C  C   . LEU   A 1 1503 ? -42.73100  19.72100  13.00900  1.000 74.68177  ?  1501 LEU   A C   1 
ATOM   11957 O  O   . LEU   A 1 1503 ? -41.96300  20.67900  12.86700  1.000 73.34091  ?  1501 LEU   A O   1 
ATOM   11958 C  CB  . LEU   A 1 1503 ? -41.28900  18.46600  11.40000  1.000 67.71446  ?  1501 LEU   A CB  1 
ATOM   11959 C  CG  . LEU   A 1 1503 ? -40.85800  17.20100  10.66600  1.000 58.12635  ?  1501 LEU   A CG  1 
ATOM   11960 C  CD1 . LEU   A 1 1503 ? -40.30100  17.58100  9.30700   1.000 63.24335  ?  1501 LEU   A CD1 1 
ATOM   11961 C  CD2 . LEU   A 1 1503 ? -39.82600  16.44500  11.47900  1.000 65.09150  ?  1501 LEU   A CD2 1 
ATOM   11962 N  N   . PRO   A 1 1504 ? -43.65200  19.71600  13.96900  1.000 75.62789  ?  1502 PRO   A N   1 
ATOM   11963 C  CA  . PRO   A 1 1504 ? -43.53700  20.67300  15.07100  1.000 69.95620  ?  1502 PRO   A CA  1 
ATOM   11964 C  C   . PRO   A 1 1504 ? -42.26100  20.39300  15.84700  1.000 77.99630  ?  1502 PRO   A C   1 
ATOM   11965 O  O   . PRO   A 1 1504 ? -41.70800  19.29100  15.80500  1.000 84.66537  ?  1502 PRO   A O   1 
ATOM   11966 C  CB  . PRO   A 1 1504 ? -44.78900  20.41000  15.91600  1.000 71.30789  ?  1502 PRO   A CB  1 
ATOM   11967 C  CG  . PRO   A 1 1504 ? -45.20800  19.02500  15.55800  1.000 75.58138  ?  1502 PRO   A CG  1 
ATOM   11968 C  CD  . PRO   A 1 1504 ? -44.82100  18.83200  14.12000  1.000 65.04150  ?  1502 PRO   A CD  1 
ATOM   11969 N  N   . GLU   A 1 1505 ? -41.77600  21.42100  16.53900  1.000 77.02777  ?  1503 GLU   A N   1 
ATOM   11970 C  CA  . GLU   A 1 1505 ? -40.54200  21.45300  17.31400  1.000 78.84405  ?  1503 GLU   A CA  1 
ATOM   11971 C  C   . GLU   A 1 1505 ? -39.30200  21.54200  16.41900  1.000 75.06287  ?  1503 GLU   A C   1 
ATOM   11972 O  O   . GLU   A 1 1505 ? -38.19500  21.65300  16.94500  1.000 76.30217  ?  1503 GLU   A O   1 
ATOM   11973 C  CB  . GLU   A 1 1505 ? -40.38500  20.24900  18.26600  1.000 76.10418  ?  1503 GLU   A CB  1 
ATOM   11974 C  CG  . GLU   A 1 1505 ? -41.52900  20.08900  19.25800  1.000 86.90274  ?  1503 GLU   A CG  1 
ATOM   11975 C  CD  . GLU   A 1 1505 ? -41.25600  20.77000  20.58200  1.000 109.18638 ?  1503 GLU   A CD  1 
ATOM   11976 O  OE1 . GLU   A 1 1505 ? -40.39300  20.27300  21.33600  1.000 105.95169 ?  1503 GLU   A OE1 1 
ATOM   11977 O  OE2 . GLU   A 1 1505 ? -41.90200  21.80100  20.86700  1.000 107.17614 -1 1503 GLU   A OE2 1 
ATOM   11978 N  N   . VAL   A 1 1506 ? -39.44100  21.48600  15.09100  1.000 71.47196  ?  1504 VAL   A N   1 
ATOM   11979 C  CA  . VAL   A 1 1506 ? -38.31000  21.75800  14.21300  1.000 63.31315  ?  1504 VAL   A CA  1 
ATOM   11980 C  C   . VAL   A 1 1506 ? -38.18100  23.26500  14.02400  1.000 65.26456  ?  1504 VAL   A C   1 
ATOM   11981 O  O   . VAL   A 1 1506 ? -39.10300  24.03400  14.29900  1.000 77.33716  ?  1504 VAL   A O   1 
ATOM   11982 C  CB  . VAL   A 1 1506 ? -38.45700  21.03900  12.85700  1.000 59.89691  ?  1504 VAL   A CB  1 
ATOM   11983 C  CG1 . VAL   A 1 1506 ? -39.29600  21.87000  11.90000  1.000 56.51726  ?  1504 VAL   A CG1 1 
ATOM   11984 C  CG2 . VAL   A 1 1506 ? -37.09400  20.73700  12.24800  1.000 56.14152  ?  1504 VAL   A CG2 1 
ATOM   11985 N  N   . LYS   A 1 1507 ? -37.01900  23.69200  13.54600  1.000 61.00441  ?  1505 LYS   A N   1 
ATOM   11986 C  CA  . LYS   A 1 1507 ? -36.75300  25.10200  13.27600  1.000 64.12273  ?  1505 LYS   A CA  1 
ATOM   11987 C  C   . LYS   A 1 1507 ? -36.35900  25.23200  11.80800  1.000 68.16643  ?  1505 LYS   A C   1 
ATOM   11988 O  O   . LYS   A 1 1507 ? -35.22800  24.91000  11.43100  1.000 78.57073  ?  1505 LYS   A O   1 
ATOM   11989 C  CB  . LYS   A 1 1507 ? -35.66600  25.63800  14.20200  1.000 57.70962  ?  1505 LYS   A CB  1 
ATOM   11990 C  CG  . LYS   A 1 1507 ? -36.06600  25.67200  15.66600  1.000 66.34483  ?  1505 LYS   A CG  1 
ATOM   11991 C  CD  . LYS   A 1 1507 ? -36.26000  27.10000  16.14400  1.000 76.42622  ?  1505 LYS   A CD  1 
ATOM   11992 C  CE  . LYS   A 1 1507 ? -36.06100  27.21300  17.64800  1.000 90.50482  ?  1505 LYS   A CE  1 
ATOM   11993 N  NZ  . LYS   A 1 1507 ? -34.71300  27.74000  18.01100  1.000 77.52132  ?  1505 LYS   A NZ  1 
ATOM   11994 N  N   . LEU   A 1 1508 ? -37.29500  25.69000  10.98000  1.000 59.39982  ?  1506 LEU   A N   1 
ATOM   11995 C  CA  . LEU   A 1 1508 ? -37.02100  25.89900  9.56600   1.000 51.06805  ?  1506 LEU   A CA  1 
ATOM   11996 C  C   . LEU   A 1 1508 ? -36.25000  27.19800  9.37400   1.000 59.10597  ?  1506 LEU   A C   1 
ATOM   11997 O  O   . LEU   A 1 1508 ? -36.59200  28.22700  9.96500   1.000 52.72750  ?  1506 LEU   A O   1 
ATOM   11998 C  CB  . LEU   A 1 1508 ? -38.31900  25.93000  8.76500   1.000 54.28403  ?  1506 LEU   A CB  1 
ATOM   11999 C  CG  . LEU   A 1 1508 ? -38.15000  26.13200  7.26100   1.000 49.06745  ?  1506 LEU   A CG  1 
ATOM   12000 C  CD1 . LEU   A 1 1508 ? -37.31600  25.01400  6.67000   1.000 37.00490  ?  1506 LEU   A CD1 1 
ATOM   12001 C  CD2 . LEU   A 1 1508 ? -39.50800  26.20500  6.58500   1.000 61.68008  ?  1506 LEU   A CD2 1 
ATOM   12002 N  N   . GLU   A 1 1509 ? -35.19900  27.14300  8.55800   1.000 56.31882  ?  1507 GLU   A N   1 
ATOM   12003 C  CA  . GLU   A 1 1509 ? -34.33000  28.28900  8.32800   1.000 48.97098  ?  1507 GLU   A CA  1 
ATOM   12004 C  C   . GLU   A 1 1509 ? -34.03700  28.40200  6.84200   1.000 51.72312  ?  1507 GLU   A C   1 
ATOM   12005 O  O   . GLU   A 1 1509 ? -33.65100  27.41700  6.20500   1.000 51.09088  ?  1507 GLU   A O   1 
ATOM   12006 C  CB  . GLU   A 1 1509 ? -33.02000  28.16100  9.11900   1.000 39.90908  ?  1507 GLU   A CB  1 
ATOM   12007 C  CG  . GLU   A 1 1509 ? -33.20700  27.71800  10.56600  1.000 53.19943  ?  1507 GLU   A CG  1 
ATOM   12008 C  CD  . GLU   A 1 1509 ? -33.38300  28.88300  11.52100  1.000 57.52533  ?  1507 GLU   A CD  1 
ATOM   12009 O  OE1 . GLU   A 1 1509 ? -32.65800  29.88900  11.36900  1.000 56.72596  ?  1507 GLU   A OE1 1 
ATOM   12010 O  OE2 . GLU   A 1 1509 ? -34.25200  28.79800  12.41500  1.000 59.27509  -1 1507 GLU   A OE2 1 
ATOM   12011 N  N   . ASN   A 1 1510 ? -34.22900  29.59600  6.29200   1.000 48.01483  ?  1508 ASN   A N   1 
ATOM   12012 C  CA  . ASN   A 1 1510 ? -33.88200  29.88600  4.90800   1.000 45.88302  ?  1508 ASN   A CA  1 
ATOM   12013 C  C   . ASN   A 1 1510 ? -32.50000  30.52500  4.88500   1.000 50.55232  ?  1508 ASN   A C   1 
ATOM   12014 O  O   . ASN   A 1 1510 ? -32.26900  31.53600  5.55900   1.000 49.21585  ?  1508 ASN   A O   1 
ATOM   12015 C  CB  . ASN   A 1 1510 ? -34.91700  30.80500  4.26300   1.000 49.59955  ?  1508 ASN   A CB  1 
ATOM   12016 C  CG  . ASN   A 1 1510 ? -34.83600  30.79800  2.75500   1.000 43.10067  ?  1508 ASN   A CG  1 
ATOM   12017 O  OD1 . ASN   A 1 1510 ? -34.71400  29.74200  2.13400   1.000 51.94315  ?  1508 ASN   A OD1 1 
ATOM   12018 N  ND2 . ASN   A 1 1510 ? -34.90200  31.97900  2.15400   1.000 51.99715  ?  1508 ASN   A ND2 1 
ATOM   12019 N  N   . ILE   A 1 1511 ? -31.58500  29.93300  4.12300   1.000 43.26161  ?  1509 ILE   A N   1 
ATOM   12020 C  CA  . ILE   A 1 1511 ? -30.19600  30.37000  4.08100   1.000 48.94502  ?  1509 ILE   A CA  1 
ATOM   12021 C  C   . ILE   A 1 1511 ? -29.80700  30.62800  2.63100   1.000 45.26023  ?  1509 ILE   A C   1 
ATOM   12022 O  O   . ILE   A 1 1511 ? -30.24700  29.91700  1.72100   1.000 38.94522  ?  1509 ILE   A O   1 
ATOM   12023 C  CB  . ILE   A 1 1511 ? -29.26300  29.33000  4.73800   1.000 46.48874  ?  1509 ILE   A CB  1 
ATOM   12024 C  CG1 . ILE   A 1 1511 ? -29.60700  29.18400  6.21700   1.000 51.92198  ?  1509 ILE   A CG1 1 
ATOM   12025 C  CG2 . ILE   A 1 1511 ? -27.82600  29.76200  4.64500   1.000 47.50008  ?  1509 ILE   A CG2 1 
ATOM   12026 C  CD1 . ILE   A 1 1511 ? -29.61800  27.76600  6.69700   1.000 56.44752  ?  1509 ILE   A CD1 1 
ATOM   12027 N  N   . TYR   A 1 1512 ? -28.99600  31.66200  2.41900   1.000 40.71600  ?  1510 TYR   A N   1 
ATOM   12028 C  CA  . TYR   A 1 1512 ? -28.55000  32.06800  1.09600   1.000 40.10060  ?  1510 TYR   A CA  1 
ATOM   12029 C  C   . TYR   A 1 1512 ? -27.03400  32.20400  1.10400   1.000 51.77956  ?  1510 TYR   A C   1 
ATOM   12030 O  O   . TYR   A 1 1512 ? -26.42600  32.48200  2.14200   1.000 43.12151  ?  1510 TYR   A O   1 
ATOM   12031 C  CB  . TYR   A 1 1512 ? -29.21800  33.39300  0.67800   1.000 35.46075  ?  1510 TYR   A CB  1 
ATOM   12032 C  CG  . TYR   A 1 1512 ? -28.51900  34.15900  -0.42400  1.000 30.85793  ?  1510 TYR   A CG  1 
ATOM   12033 C  CD1 . TYR   A 1 1512 ? -28.76300  33.87100  -1.75900  1.000 29.90798  ?  1510 TYR   A CD1 1 
ATOM   12034 C  CD2 . TYR   A 1 1512 ? -27.62800  35.18300  -0.12700  1.000 37.70876  ?  1510 TYR   A CD2 1 
ATOM   12035 C  CE1 . TYR   A 1 1512 ? -28.13200  34.57400  -2.76800  1.000 34.83088  ?  1510 TYR   A CE1 1 
ATOM   12036 C  CE2 . TYR   A 1 1512 ? -26.99000  35.88900  -1.12800  1.000 37.26127  ?  1510 TYR   A CE2 1 
ATOM   12037 C  CZ  . TYR   A 1 1512 ? -27.24600  35.58100  -2.44700  1.000 43.81454  ?  1510 TYR   A CZ  1 
ATOM   12038 O  OH  . TYR   A 1 1512 ? -26.61700  36.28000  -3.45200  1.000 44.55437  ?  1510 TYR   A OH  1 
ATOM   12039 N  N   . GLY   A 1 1513 ? -26.42500  31.99300  -0.05900  1.000 44.76281  ?  1511 GLY   A N   1 
ATOM   12040 C  CA  . GLY   A 1 1513 ? -24.99800  32.15200  -0.19100  1.000 42.57811  ?  1511 GLY   A CA  1 
ATOM   12041 C  C   . GLY   A 1 1513 ? -24.46800  31.67500  -1.52500  1.000 44.40285  ?  1511 GLY   A C   1 
ATOM   12042 O  O   . GLY   A 1 1513 ? -24.71000  30.54100  -1.95100  1.000 63.69034  ?  1511 GLY   A O   1 
ATOM   12043 N  N   . PRO   A 1 1514 ? -23.73200  32.54200  -2.21300  1.000 44.66738  ?  1512 PRO   A N   1 
ATOM   12044 C  CA  . PRO   A 1 1514 ? -23.05800  32.12300  -3.44400  1.000 50.57595  ?  1512 PRO   A CA  1 
ATOM   12045 C  C   . PRO   A 1 1514 ? -21.84700  31.25900  -3.13000  1.000 56.88499  ?  1512 PRO   A C   1 
ATOM   12046 O  O   . PRO   A 1 1514 ? -21.28600  31.29800  -2.03200  1.000 44.39577  ?  1512 PRO   A O   1 
ATOM   12047 C  CB  . PRO   A 1 1514 ? -22.64400  33.44900  -4.08800  1.000 40.13013  ?  1512 PRO   A CB  1 
ATOM   12048 C  CG  . PRO   A 1 1514 ? -22.46600  34.37400  -2.92300  1.000 44.62579  ?  1512 PRO   A CG  1 
ATOM   12049 C  CD  . PRO   A 1 1514 ? -23.49600  33.96300  -1.90300  1.000 47.09551  ?  1512 PRO   A CD  1 
ATOM   12050 N  N   . THR   A 1 1515 ? -21.45200  30.45700  -4.12400  1.000 57.64971  ?  1513 THR   A N   1 
ATOM   12051 C  CA  . THR   A 1 1515 ? -20.28100  29.59900  -3.96100  1.000 66.50716  ?  1513 THR   A CA  1 
ATOM   12052 C  C   . THR   A 1 1515 ? -19.02700  30.42000  -3.68500  1.000 62.89512  ?  1513 THR   A C   1 
ATOM   12053 O  O   . THR   A 1 1515 ? -18.13100  29.96900  -2.96100  1.000 49.75672  ?  1513 THR   A O   1 
ATOM   12054 C  CB  . THR   A 1 1515 ? -20.08300  28.73000  -5.20600  1.000 52.59238  ?  1513 THR   A CB  1 
ATOM   12055 O  OG1 . THR   A 1 1515 ? -21.33500  28.14700  -5.59200  1.000 57.78301  ?  1513 THR   A OG1 1 
ATOM   12056 C  CG2 . THR   A 1 1515 ? -19.08100  27.61900  -4.93200  1.000 45.13714  ?  1513 THR   A CG2 1 
ATOM   12057 N  N   . GLU   A 1 1516 ? -18.95800  31.63300  -4.23600  1.000 56.59933  ?  1514 GLU   A N   1 
ATOM   12058 C  CA  . GLU   A 1 1516 ? -17.82500  32.53000  -4.05800  1.000 41.36464  ?  1514 GLU   A CA  1 
ATOM   12059 C  C   . GLU   A 1 1516 ? -17.77200  33.15200  -2.67000  1.000 40.55038  ?  1514 GLU   A C   1 
ATOM   12060 O  O   . GLU   A 1 1516 ? -16.81700  33.87600  -2.36800  1.000 45.07110  ?  1514 GLU   A O   1 
ATOM   12061 C  CB  . GLU   A 1 1516 ? -17.86400  33.61700  -5.13300  1.000 36.33969  ?  1514 GLU   A CB  1 
ATOM   12062 C  CG  . GLU   A 1 1516 ? -17.78600  33.07400  -6.56000  1.000 38.89646  ?  1514 GLU   A CG  1 
ATOM   12063 C  CD  . GLU   A 1 1516 ? -19.13300  32.63700  -7.11300  1.000 46.16275  ?  1514 GLU   A CD  1 
ATOM   12064 O  OE1 . GLU   A 1 1516 ? -20.01400  32.24200  -6.31800  1.000 48.27574  ?  1514 GLU   A OE1 1 
ATOM   12065 O  OE2 . GLU   A 1 1516 ? -19.31000  32.68000  -8.35000  1.000 57.68995  -1 1514 GLU   A OE2 1 
ATOM   12066 N  N   . ALA   A 1 1517 ? -18.76900  32.89500  -1.82700  1.000 38.77852  ?  1515 ALA   A N   1 
ATOM   12067 C  CA  . ALA   A 1 1517 ? -18.68000  33.21900  -0.41000  1.000 40.82918  ?  1515 ALA   A CA  1 
ATOM   12068 C  C   . ALA   A 1 1517 ? -18.63900  31.92300  0.38900   1.000 61.04922  ?  1515 ALA   A C   1 
ATOM   12069 O  O   . ALA   A 1 1517 ? -19.38700  31.75900  1.35900   1.000 55.43408  ?  1515 ALA   A O   1 
ATOM   12070 C  CB  . ALA   A 1 1517 ? -19.85500  34.09500  0.02500   1.000 57.11095  ?  1515 ALA   A CB  1 
ATOM   12071 N  N   . THR   A 1 1518 ? -17.75700  31.00400  -0.01900  1.000 67.97830  ?  1516 THR   A N   1 
ATOM   12072 C  CA  . THR   A 1 1518 ? -17.68600  29.64000  0.50000   1.000 71.38967  ?  1516 THR   A CA  1 
ATOM   12073 C  C   . THR   A 1 1518 ? -19.01500  28.91200  0.34100   1.000 72.68441  ?  1516 THR   A C   1 
ATOM   12074 O  O   . THR   A 1 1518 ? -19.34300  28.44800  -0.75600  1.000 79.43230  ?  1516 THR   A O   1 
ATOM   12075 C  CB  . THR   A 1 1518 ? -17.25600  29.62200  1.96800   1.000 61.31056  ?  1516 THR   A CB  1 
ATOM   12076 O  OG1 . THR   A 1 1518 ? -18.26800  30.25100  2.76100   1.000 75.01874  ?  1516 THR   A OG1 1 
ATOM   12077 C  CG2 . THR   A 1 1518 ? -15.93600  30.34800  2.14200   1.000 29.54588  ?  1516 THR   A CG2 1 
ATOM   12078 N  N   . ILE   A 1 1519 ? -19.78300  28.80000  1.42500   1.000 37.62279  ?  1517 ILE   A N   1 
ATOM   12079 C  CA  . ILE   A 1 1519 ? -21.02200  28.02800  1.40200   1.000 57.61375  ?  1517 ILE   A CA  1 
ATOM   12080 C  C   . ILE   A 1 1519 ? -22.22200  28.95900  1.46600   1.000 61.76990  ?  1517 ILE   A C   1 
ATOM   12081 O  O   . ILE   A 1 1519 ? -23.00400  29.05700  0.51300   1.000 47.72450  ?  1517 ILE   A O   1 
ATOM   12082 C  CB  . ILE   A 1 1519 ? -21.07500  27.01400  2.56000   1.000 65.68192  ?  1517 ILE   A CB  1 
ATOM   12083 C  CG1 . ILE   A 1 1519 ? -19.68000  26.46700  2.86900   1.000 41.45265  ?  1517 ILE   A CG1 1 
ATOM   12084 C  CG2 . ILE   A 1 1519 ? -22.06600  25.90100  2.24100   1.000 57.54300  ?  1517 ILE   A CG2 1 
ATOM   12085 C  CD1 . ILE   A 1 1519 ? -19.18300  25.47700  1.85500   1.000 43.34656  ?  1517 ILE   A CD1 1 
ATOM   12086 N  N   . TYR   A 1 1520 ? -22.38100  29.63300  2.59700   1.000 57.40113  ?  1518 TYR   A N   1 
ATOM   12087 C  CA  . TYR   A 1 1520 ? -23.53100  30.47400  2.87900   1.000 42.39491  ?  1518 TYR   A CA  1 
ATOM   12088 C  C   . TYR   A 1 1520 ? -23.06800  31.90800  3.11100   1.000 51.16095  ?  1518 TYR   A C   1 
ATOM   12089 O  O   . TYR   A 1 1520 ? -21.87300  32.20700  3.11600   1.000 59.93950  ?  1518 TYR   A O   1 
ATOM   12090 C  CB  . TYR   A 1 1520 ? -24.29900  29.94000  4.09000   1.000 38.98459  ?  1518 TYR   A CB  1 
ATOM   12091 C  CG  . TYR   A 1 1520 ? -24.75000  28.50100  3.94700   1.000 58.41276  ?  1518 TYR   A CG  1 
ATOM   12092 C  CD1 . TYR   A 1 1520 ? -25.48200  28.08400  2.84100   1.000 54.75720  ?  1518 TYR   A CD1 1 
ATOM   12093 C  CD2 . TYR   A 1 1520 ? -24.45200  27.55900  4.92400   1.000 57.14084  ?  1518 TYR   A CD2 1 
ATOM   12094 C  CE1 . TYR   A 1 1520 ? -25.90200  26.76800  2.71300   1.000 49.18615  ?  1518 TYR   A CE1 1 
ATOM   12095 C  CE2 . TYR   A 1 1520 ? -24.86800  26.24300  4.80500   1.000 45.03557  ?  1518 TYR   A CE2 1 
ATOM   12096 C  CZ  . TYR   A 1 1520 ? -25.59100  25.85300  3.69700   1.000 53.31883  ?  1518 TYR   A CZ  1 
ATOM   12097 O  OH  . TYR   A 1 1520 ? -26.00400  24.54500  3.57400   1.000 56.18261  ?  1518 TYR   A OH  1 
ATOM   12098 N  N   . ALA   A 1 1521 ? -24.03200  32.80400  3.31000   1.000 53.98244  ?  1519 ALA   A N   1 
ATOM   12099 C  CA  . ALA   A 1 1521 ? -23.71200  34.20100  3.57100   1.000 38.02678  ?  1519 ALA   A CA  1 
ATOM   12100 C  C   . ALA   A 1 1521 ? -24.73000  34.82400  4.51800   1.000 49.75039  ?  1519 ALA   A C   1 
ATOM   12101 O  O   . ALA   A 1 1521 ? -24.36200  35.58400  5.41800   1.000 54.50491  ?  1519 ALA   A O   1 
ATOM   12102 C  CB  . ALA   A 1 1521 ? -23.64600  34.98600  2.26000   1.000 25.22555  ?  1519 ALA   A CB  1 
ATOM   12103 N  N   . SER   A 1 1522 ? -26.00800  34.49700  4.33400   1.000 51.56076  ?  1520 SER   A N   1 
ATOM   12104 C  CA  . SER   A 1 1522 ? -27.08600  35.08100  5.12000   1.000 43.46330  ?  1520 SER   A CA  1 
ATOM   12105 C  C   . SER   A 1 1522 ? -28.09800  34.00500  5.48800   1.000 51.95922  ?  1520 SER   A C   1 
ATOM   12106 O  O   . SER   A 1 1522 ? -28.19300  32.96700  4.83000   1.000 49.25625  ?  1520 SER   A O   1 
ATOM   12107 C  CB  . SER   A 1 1522 ? -27.79200  36.20300  4.35400   1.000 46.06286  ?  1520 SER   A CB  1 
ATOM   12108 O  OG  . SER   A 1 1522 ? -28.47800  35.68400  3.22400   1.000 47.52485  ?  1520 SER   A OG  1 
ATOM   12109 N  N   . ARG   A 1 1523 ? -28.88000  34.27000  6.53200   1.000 42.73035  ?  1521 ARG   A N   1 
ATOM   12110 C  CA  . ARG   A 1 1523 ? -29.87100  33.31000  6.98800   1.000 46.64879  ?  1521 ARG   A CA  1 
ATOM   12111 C  C   . ARG   A 1 1523 ? -31.08700  34.07800  7.48000   1.000 49.80352  ?  1521 ARG   A C   1 
ATOM   12112 O  O   . ARG   A 1 1523 ? -30.99500  35.25500  7.83500   1.000 53.70696  ?  1521 ARG   A O   1 
ATOM   12113 C  CB  . ARG   A 1 1523 ? -29.33100  32.42800  8.12300   1.000 44.75465  ?  1521 ARG   A CB  1 
ATOM   12114 C  CG  . ARG   A 1 1523 ? -29.79000  32.93200  9.47000   1.000 57.68962  ?  1521 ARG   A CG  1 
ATOM   12115 C  CD  . ARG   A 1 1523 ? -28.83100  32.72500  10.60200  1.000 72.98539  ?  1521 ARG   A CD  1 
ATOM   12116 N  NE  . ARG   A 1 1523 ? -29.48400  33.02800  11.87400  1.000 83.06185  ?  1521 ARG   A NE  1 
ATOM   12117 C  CZ  . ARG   A 1 1523 ? -28.86900  33.60800  12.89800  1.000 95.68435  ?  1521 ARG   A CZ  1 
ATOM   12118 N  NH1 . ARG   A 1 1523 ? -27.64300  34.09700  12.78000  1.000 86.75284  ?  1521 ARG   A NH1 1 
ATOM   12119 N  NH2 . ARG   A 1 1523 ? -29.53000  33.78600  14.03700  1.000 106.59222 ?  1521 ARG   A NH2 1 
ATOM   12120 N  N   . TYR   A 1 1524 ? -32.23000  33.39600  7.51000   1.000 43.46810  ?  1522 TYR   A N   1 
ATOM   12121 C  CA  . TYR   A 1 1524 ? -33.45700  33.95600  8.06300   1.000 46.30140  ?  1522 TYR   A CA  1 
ATOM   12122 C  C   . TYR   A 1 1524 ? -34.21100  32.84500  8.77800   1.000 51.37258  ?  1522 TYR   A C   1 
ATOM   12123 O  O   . TYR   A 1 1524 ? -34.53400  31.82300  8.16500   1.000 52.09970  ?  1522 TYR   A O   1 
ATOM   12124 C  CB  . TYR   A 1 1524 ? -34.31700  34.58300  6.96400   1.000 52.89687  ?  1522 TYR   A CB  1 
ATOM   12125 C  CG  . TYR   A 1 1524 ? -35.59700  35.17900  7.47600   1.000 58.97150  ?  1522 TYR   A CG  1 
ATOM   12126 C  CD1 . TYR   A 1 1524 ? -35.59600  36.38600  8.15900   1.000 63.84999  ?  1522 TYR   A CD1 1 
ATOM   12127 C  CD2 . TYR   A 1 1524 ? -36.80600  34.53600  7.27400   1.000 64.34576  ?  1522 TYR   A CD2 1 
ATOM   12128 C  CE1 . TYR   A 1 1524 ? -36.76300  36.93200  8.62700   1.000 65.56135  ?  1522 TYR   A CE1 1 
ATOM   12129 C  CE2 . TYR   A 1 1524 ? -37.97700  35.07200  7.73700   1.000 68.19106  ?  1522 TYR   A CE2 1 
ATOM   12130 C  CZ  . TYR   A 1 1524 ? -37.95300  36.27200  8.41200   1.000 62.81242  ?  1522 TYR   A CZ  1 
ATOM   12131 O  OH  . TYR   A 1 1524 ? -39.12600  36.81200  8.87800   1.000 82.33812  ?  1522 TYR   A OH  1 
ATOM   12132 N  N   . SER   A 1 1525 ? -34.47400  33.03600  10.07000  1.000 62.94955  ?  1523 SER   A N   1 
ATOM   12133 C  CA  . SER   A 1 1525 ? -35.20400  32.06000  10.87200  1.000 54.86878  ?  1523 SER   A CA  1 
ATOM   12134 C  C   . SER   A 1 1525 ? -36.70100  32.28600  10.69600  1.000 60.84737  ?  1523 SER   A C   1 
ATOM   12135 O  O   . SER   A 1 1525 ? -37.21600  33.35500  11.03800  1.000 74.23213  ?  1523 SER   A O   1 
ATOM   12136 C  CB  . SER   A 1 1525 ? -34.82200  32.16600  12.34900  1.000 42.55405  ?  1523 SER   A CB  1 
ATOM   12137 O  OG  . SER   A 1 1525 ? -33.44700  32.46700  12.50700  1.000 61.13271  ?  1523 SER   A OG  1 
ATOM   12138 N  N   . LEU   A 1 1526 ? -37.39200  31.28700  10.16100  1.000 65.43440  ?  1524 LEU   A N   1 
ATOM   12139 C  CA  . LEU   A 1 1526 ? -38.83400  31.35700  9.99000   1.000 64.87496  ?  1524 LEU   A CA  1 
ATOM   12140 C  C   . LEU   A 1 1526 ? -39.53800  30.82600  11.23200  1.000 69.80907  ?  1524 LEU   A C   1 
ATOM   12141 O  O   . LEU   A 1 1526 ? -39.03800  29.93100  11.91800  1.000 76.40247  ?  1524 LEU   A O   1 
ATOM   12142 C  CB  . LEU   A 1 1526 ? -39.25900  30.56400  8.75700   1.000 50.53289  ?  1524 LEU   A CB  1 
ATOM   12143 C  CG  . LEU   A 1 1526 ? -38.68500  31.16300  7.47500   1.000 62.96268  ?  1524 LEU   A CG  1 
ATOM   12144 C  CD1 . LEU   A 1 1526 ? -38.23500  30.06500  6.54600   1.000 62.21349  ?  1524 LEU   A CD1 1 
ATOM   12145 C  CD2 . LEU   A 1 1526 ? -39.71500  32.05600  6.79500   1.000 63.20108  ?  1524 LEU   A CD2 1 
ATOM   12146 N  N   . ALA   A 1 1527 ? -40.70600  31.39300  11.51800  1.000 90.64884  ?  1525 ALA   A N   1 
ATOM   12147 C  CA  . ALA   A 1 1527 ? -41.46400  31.06300  12.71400  1.000 87.95056  ?  1525 ALA   A CA  1 
ATOM   12148 C  C   . ALA   A 1 1527 ? -42.78300  30.40100  12.33900  1.000 80.48908  ?  1525 ALA   A C   1 
ATOM   12149 O  O   . ALA   A 1 1527 ? -43.25100  30.49400  11.20000  1.000 82.34821  ?  1525 ALA   A O   1 
ATOM   12150 C  CB  . ALA   A 1 1527 ? -41.72900  32.31000  13.56500  1.000 76.61377  ?  1525 ALA   A CB  1 
ATOM   12151 N  N   . LYS   A 1 1528 ? -43.38100  29.73400  13.32800  1.000 85.41455  ?  1526 LYS   A N   1 
ATOM   12152 C  CA  . LYS   A 1 1528 ? -44.62700  29.00700  13.10500  1.000 90.84994  ?  1526 LYS   A CA  1 
ATOM   12153 C  C   . LYS   A 1 1528 ? -45.74700  29.95200  12.68200  1.000 97.51493  ?  1526 LYS   A C   1 
ATOM   12154 O  O   . LYS   A 1 1528 ? -46.30000  29.83200  11.58200  1.000 91.85059  ?  1526 LYS   A O   1 
ATOM   12155 C  CB  . LYS   A 1 1528 ? -45.01000  28.23900  14.37100  1.000 78.98512  ?  1526 LYS   A CB  1 
ATOM   12156 C  CG  . LYS   A 1 1528 ? -43.81800  27.70600  15.15100  1.000 89.11811  ?  1526 LYS   A CG  1 
ATOM   12157 C  CD  . LYS   A 1 1528 ? -44.11900  27.63800  16.64000  1.000 97.11859  ?  1526 LYS   A CD  1 
ATOM   12158 C  CE  . LYS   A 1 1528 ? -43.43900  26.44600  17.29200  1.000 85.56305  ?  1526 LYS   A CE  1 
ATOM   12159 N  NZ  . LYS   A 1 1528 ? -44.04400  26.12400  18.61300  1.000 71.46437  ?  1526 LYS   A NZ  1 
ATOM   12160 N  N   . GLY   A 1 1529 ? -46.09500  30.90000  13.54900  1.000 92.51306  ?  1527 GLY   A N   1 
ATOM   12161 C  CA  . GLY   A 1 1529 ? -47.12000  31.87400  13.23400  1.000 96.69862  ?  1527 GLY   A CA  1 
ATOM   12162 C  C   . GLY   A 1 1529 ? -46.59000  33.02100  12.39900  1.000 92.72367  ?  1527 GLY   A C   1 
ATOM   12163 O  O   . GLY   A 1 1529 ? -46.42800  34.13900  12.89800  1.000 91.34181  ?  1527 GLY   A O   1 
ATOM   12164 N  N   . SER   A 1 1530 ? -46.31800  32.75400  11.12300  1.000 81.70646  ?  1528 SER   A N   1 
ATOM   12165 C  CA  . SER   A 1 1530 ? -45.72500  33.73800  10.23200  1.000 76.15232  ?  1528 SER   A CA  1 
ATOM   12166 C  C   . SER   A 1 1530 ? -46.30000  33.57800  8.83400   1.000 89.58634  ?  1528 SER   A C   1 
ATOM   12167 O  O   . SER   A 1 1530 ? -46.75100  32.49600  8.44800   1.000 89.71215  ?  1528 SER   A O   1 
ATOM   12168 C  CB  . SER   A 1 1530 ? -44.19700  33.60000  10.18200  1.000 98.92586  ?  1528 SER   A CB  1 
ATOM   12169 O  OG  . SER   A 1 1530 ? -43.78700  32.84600  9.05300   1.000 96.67733  ?  1528 SER   A OG  1 
ATOM   12170 N  N   . GLN   A 1 1531 ? -46.26800  34.67400  8.06900   1.000 91.96472  ?  1529 GLN   A N   1 
ATOM   12171 C  CA  . GLN   A 1 1531 ? -46.67500  34.66200  6.67200   1.000 109.75180 ?  1529 GLN   A CA  1 
ATOM   12172 C  C   . GLN   A 1 1531 ? -45.85600  35.72500  5.93500   1.000 106.33493 ?  1529 GLN   A C   1 
ATOM   12173 O  O   . GLN   A 1 1531 ? -46.35900  36.76400  5.50200   1.000 113.23153 ?  1529 GLN   A O   1 
ATOM   12174 C  CB  . GLN   A 1 1531 ? -48.18000  34.89500  6.51400   1.000 104.84489 ?  1529 GLN   A CB  1 
ATOM   12175 C  CG  . GLN   A 1 1531 ? -49.05400  33.62900  6.41700   1.000 114.79532 ?  1529 GLN   A CG  1 
ATOM   12176 C  CD  . GLN   A 1 1531 ? -48.57200  32.54200  5.44300   1.000 116.91973 ?  1529 GLN   A CD  1 
ATOM   12177 O  OE1 . GLN   A 1 1531 ? -47.61200  32.70900  4.68600   1.000 106.88060 ?  1529 GLN   A OE1 1 
ATOM   12178 N  NE2 . GLN   A 1 1531 ? -49.26100  31.40800  5.47400   1.000 96.88391  ?  1529 GLN   A NE2 1 
ATOM   12179 N  N   . GLU   A 1 1532 ? -44.56000  35.45000  5.79600   1.000 84.36181  ?  1530 GLU   A N   1 
ATOM   12180 C  CA  . GLU   A 1 1532 ? -43.66400  36.36900  5.10800   1.000 81.49359  ?  1530 GLU   A CA  1 
ATOM   12181 C  C   . GLU   A 1 1532 ? -44.12200  36.57900  3.67200   1.000 79.19650  ?  1530 GLU   A C   1 
ATOM   12182 O  O   . GLU   A 1 1532 ? -44.57800  35.64600  3.00400   1.000 71.62624  ?  1530 GLU   A O   1 
ATOM   12183 C  CB  . GLU   A 1 1532 ? -42.23300  35.83200  5.13100   1.000 94.80246  ?  1530 GLU   A CB  1 
ATOM   12184 C  CG  . GLU   A 1 1532 ? -41.69100  35.56900  6.52700   1.000 100.13839 ?  1530 GLU   A CG  1 
ATOM   12185 C  CD  . GLU   A 1 1532 ? -42.21400  36.54800  7.56200   1.000 99.93382  ?  1530 GLU   A CD  1 
ATOM   12186 O  OE1 . GLU   A 1 1532 ? -43.33300  36.33100  8.07400   1.000 103.52835 ?  1530 GLU   A OE1 1 
ATOM   12187 O  OE2 . GLU   A 1 1532 ? -41.50200  37.52800  7.87000   1.000 102.27451 -1 1530 GLU   A OE2 1 
ATOM   12188 N  N   . SER   A 1 1533 ? -44.00200  37.81500  3.19800   1.000 82.65576  ?  1531 SER   A N   1 
ATOM   12189 C  CA  . SER   A 1 1533 ? -44.54200  38.12000  1.88200   1.000 84.25154  ?  1531 SER   A CA  1 
ATOM   12190 C  C   . SER   A 1 1533 ? -43.62100  37.63400  0.75800   1.000 83.63503  ?  1531 SER   A C   1 
ATOM   12191 O  O   . SER   A 1 1533 ? -44.12700  37.09200  -0.22900  1.000 94.33681  ?  1531 SER   A O   1 
ATOM   12192 C  CB  . SER   A 1 1533 ? -44.87100  39.62000  1.75800   1.000 106.65184 ?  1531 SER   A CB  1 
ATOM   12193 O  OG  . SER   A 1 1533 ? -43.83900  40.46600  2.23200   1.000 92.99355  ?  1531 SER   A OG  1 
ATOM   12194 N  N   . PRO   A 1 1534 ? -42.28500  37.77100  0.84400   1.000 85.09210  ?  1532 PRO   A N   1 
ATOM   12195 C  CA  . PRO   A 1 1534 ? -41.45100  37.12800  -0.18100  1.000 74.06710  ?  1532 PRO   A CA  1 
ATOM   12196 C  C   . PRO   A 1 1534 ? -40.53200  36.05600  0.38300   1.000 82.02466  ?  1532 PRO   A C   1 
ATOM   12197 O  O   . PRO   A 1 1534 ? -39.84800  35.37200  -0.38400  1.000 99.99486  ?  1532 PRO   A O   1 
ATOM   12198 C  CB  . PRO   A 1 1534 ? -40.63800  38.30400  -0.74800  1.000 49.80377  ?  1532 PRO   A CB  1 
ATOM   12199 C  CG  . PRO   A 1 1534 ? -40.86400  39.46800  0.25300   1.000 73.03812  ?  1532 PRO   A CG  1 
ATOM   12200 C  CD  . PRO   A 1 1534 ? -41.51600  38.85600  1.46200   1.000 78.21171  ?  1532 PRO   A CD  1 
ATOM   12201 N  N   . VAL   A 1 1535 ? -40.52100  35.90400  1.70700   1.000 68.58104  ?  1533 VAL   A N   1 
ATOM   12202 C  CA  . VAL   A 1 1535 ? -39.57700  35.05800  2.43900   1.000 67.72114  ?  1533 VAL   A CA  1 
ATOM   12203 C  C   . VAL   A 1 1535 ? -38.16400  35.59200  2.23400   1.000 57.47339  ?  1533 VAL   A C   1 
ATOM   12204 O  O   . VAL   A 1 1535 ? -37.55000  35.34800  1.18400   1.000 53.56922  ?  1533 VAL   A O   1 
ATOM   12205 C  CB  . VAL   A 1 1535 ? -39.68200  33.58300  2.02200   1.000 61.15277  ?  1533 VAL   A CB  1 
ATOM   12206 C  CG1 . VAL   A 1 1535 ? -38.73700  32.74100  2.85400   1.000 64.26086  ?  1533 VAL   A CG1 1 
ATOM   12207 C  CG2 . VAL   A 1 1535 ? -41.11100  33.09500  2.16800   1.000 54.26327  ?  1533 VAL   A CG2 1 
ATOM   12208 N  N   . PRO   A 1 1536 ? -37.60500  36.30600  3.20400   1.000 55.01695  ?  1534 PRO   A N   1 
ATOM   12209 C  CA  . PRO   A 1 1536 ? -36.31100  36.96000  2.99700   1.000 56.71809  ?  1534 PRO   A CA  1 
ATOM   12210 C  C   . PRO   A 1 1536 ? -35.14000  36.00400  3.17600   1.000 53.84598  ?  1534 PRO   A C   1 
ATOM   12211 O  O   . PRO   A 1 1536 ? -35.21800  34.99300  3.87400   1.000 52.35431  ?  1534 PRO   A O   1 
ATOM   12212 C  CB  . PRO   A 1 1536 ? -36.29600  38.05000  4.07300   1.000 53.09713  ?  1534 PRO   A CB  1 
ATOM   12213 C  CG  . PRO   A 1 1536 ? -37.13100  37.48500  5.17300   1.000 54.74484  ?  1534 PRO   A CG  1 
ATOM   12214 C  CD  . PRO   A 1 1536 ? -38.18300  36.61700  4.52500   1.000 55.14294  ?  1534 PRO   A CD  1 
ATOM   12215 N  N   . ILE   A 1 1537 ? -34.03300  36.35500  2.51800   1.000 55.90960  ?  1535 ILE   A N   1 
ATOM   12216 C  CA  . ILE   A 1 1537 ? -32.80000  35.60000  2.70700   1.000 43.80647  ?  1535 ILE   A CA  1 
ATOM   12217 C  C   . ILE   A 1 1537 ? -32.10800  35.96100  4.01500   1.000 43.79931  ?  1535 ILE   A C   1 
ATOM   12218 O  O   . ILE   A 1 1537 ? -31.23200  35.21300  4.46600   1.000 53.13082  ?  1535 ILE   A O   1 
ATOM   12219 C  CB  . ILE   A 1 1537 ? -31.83300  35.80300  1.52900   1.000 39.82311  ?  1535 ILE   A CB  1 
ATOM   12220 C  CG1 . ILE   A 1 1537 ? -31.33500  37.24300  1.47600   1.000 47.46579  ?  1535 ILE   A CG1 1 
ATOM   12221 C  CG2 . ILE   A 1 1537 ? -32.51100  35.45000  0.22000   1.000 36.86096  ?  1535 ILE   A CG2 1 
ATOM   12222 C  CD1 . ILE   A 1 1537 ? -30.51800  37.53900  0.24100   1.000 40.47627  ?  1535 ILE   A CD1 1 
ATOM   12223 N  N   . GLY   A 1 1538 ? -32.46400  37.08700  4.63100   1.000 42.76422  ?  1536 GLY   A N   1 
ATOM   12224 C  CA  . GLY   A 1 1538 ? -32.02400  37.38700  5.98000   1.000 42.75185  ?  1536 GLY   A CA  1 
ATOM   12225 C  C   . GLY   A 1 1538 ? -30.85400  38.34200  6.10700   1.000 48.21848  ?  1536 GLY   A C   1 
ATOM   12226 O  O   . GLY   A 1 1538 ? -30.60700  39.16300  5.21700   1.000 46.46171  ?  1536 GLY   A O   1 
ATOM   12227 N  N   . LYS   A 1 1539 ? -30.13400  38.24600  7.22000   1.000 51.76460  ?  1537 LYS   A N   1 
ATOM   12228 C  CA  . LYS   A 1 1539 ? -28.97800  39.07600  7.52400   1.000 48.64994  ?  1537 LYS   A CA  1 
ATOM   12229 C  C   . LYS   A 1 1539 ? -27.69300  38.25700  7.43800   1.000 53.44223  ?  1537 LYS   A C   1 
ATOM   12230 O  O   . LYS   A 1 1539 ? -27.72000  37.03000  7.57500   1.000 60.21925  ?  1537 LYS   A O   1 
ATOM   12231 C  CB  . LYS   A 1 1539 ? -29.11800  39.68800  8.92600   1.000 45.05078  ?  1537 LYS   A CB  1 
ATOM   12232 C  CG  . LYS   A 1 1539 ? -30.29600  40.63700  9.04500   1.000 55.58689  ?  1537 LYS   A CG  1 
ATOM   12233 C  CD  . LYS   A 1 1539 ? -30.43200  41.19500  10.44500  1.000 49.94914  ?  1537 LYS   A CD  1 
ATOM   12234 C  CE  . LYS   A 1 1539 ? -31.65600  42.08700  10.56400  1.000 66.89303  ?  1537 LYS   A CE  1 
ATOM   12235 N  NZ  . LYS   A 1 1539 ? -31.60700  42.90400  11.80900  1.000 52.20965  ?  1537 LYS   A NZ  1 
ATOM   12236 N  N   . PRO   A 1 1540 ? -26.54700  38.89800  7.20300   1.000 56.03406  ?  1538 PRO   A N   1 
ATOM   12237 C  CA  . PRO   A 1 1540 ? -25.31000  38.13800  6.98700   1.000 62.78762  ?  1538 PRO   A CA  1 
ATOM   12238 C  C   . PRO   A 1 1540 ? -24.83100  37.42500  8.24500   1.000 59.38795  ?  1538 PRO   A C   1 
ATOM   12239 O  O   . PRO   A 1 1540 ? -25.12900  37.81200  9.37700   1.000 55.08551  ?  1538 PRO   A O   1 
ATOM   12240 C  CB  . PRO   A 1 1540 ? -24.30600  39.20700  6.54100   1.000 48.39527  ?  1538 PRO   A CB  1 
ATOM   12241 C  CG  . PRO   A 1 1540 ? -24.84500  40.47700  7.08500   1.000 57.88141  ?  1538 PRO   A CG  1 
ATOM   12242 C  CD  . PRO   A 1 1540 ? -26.33500  40.34400  7.02000   1.000 55.43921  ?  1538 PRO   A CD  1 
ATOM   12243 N  N   . LEU   A 1 1541 ? -24.06300  36.35800  8.01500   1.000 61.52892  ?  1539 LEU   A N   1 
ATOM   12244 C  CA  . LEU   A 1 1541 ? -23.51400  35.53200  9.07700   1.000 58.33370  ?  1539 LEU   A CA  1 
ATOM   12245 C  C   . LEU   A 1 1541 ? -22.40300  36.28600  9.80600   1.000 52.98222  ?  1539 LEU   A C   1 
ATOM   12246 O  O   . LEU   A 1 1541 ? -22.02000  37.38600  9.40100   1.000 60.20208  ?  1539 LEU   A O   1 
ATOM   12247 C  CB  . LEU   A 1 1541 ? -22.99700  34.21900  8.48900   1.000 45.60846  ?  1539 LEU   A CB  1 
ATOM   12248 C  CG  . LEU   A 1 1541 ? -24.05900  33.17600  8.13700   1.000 43.70119  ?  1539 LEU   A CG  1 
ATOM   12249 C  CD1 . LEU   A 1 1541 ? -23.46300  32.07400  7.27700   1.000 52.66384  ?  1539 LEU   A CD1 1 
ATOM   12250 C  CD2 . LEU   A 1 1541 ? -24.68100  32.59800  9.39900   1.000 39.43913  ?  1539 LEU   A CD2 1 
ATOM   12251 N  N   . PRO   A 1 1542 ? -21.88500  35.73300  10.90600  1.000 57.79148  ?  1540 PRO   A N   1 
ATOM   12252 C  CA  . PRO   A 1 1542 ? -20.73000  36.35500  11.56500  1.000 55.67719  ?  1540 PRO   A CA  1 
ATOM   12253 C  C   . PRO   A 1 1542 ? -19.56800  36.57700  10.60600  1.000 47.09221  ?  1540 PRO   A C   1 
ATOM   12254 O  O   . PRO   A 1 1542 ? -19.26100  35.73400  9.76100   1.000 47.88393  ?  1540 PRO   A O   1 
ATOM   12255 C  CB  . PRO   A 1 1542 ? -20.37500  35.34800  12.66100  1.000 37.44312  ?  1540 PRO   A CB  1 
ATOM   12256 C  CG  . PRO   A 1 1542 ? -21.68800  34.76000  13.03500  1.000 46.27123  ?  1540 PRO   A CG  1 
ATOM   12257 C  CD  . PRO   A 1 1542 ? -22.50300  34.70100  11.76200  1.000 54.41904  ?  1540 PRO   A CD  1 
ATOM   12258 N  N   . ASN   A 1 1543 ? -18.93200  37.74200  10.74100  1.000 48.83031  ?  1541 ASN   A N   1 
ATOM   12259 C  CA  . ASN   A 1 1543 ? -17.81400  38.17900  9.90500   1.000 44.33097  ?  1541 ASN   A CA  1 
ATOM   12260 C  C   . ASN   A 1 1543 ? -18.17800  38.24100  8.42500   1.000 51.86565  ?  1541 ASN   A C   1 
ATOM   12261 O  O   . ASN   A 1 1543 ? -17.29600  38.19000  7.56000   1.000 44.77683  ?  1541 ASN   A O   1 
ATOM   12262 C  CB  . ASN   A 1 1543 ? -16.58200  37.29800  10.12200  1.000 47.70666  ?  1541 ASN   A CB  1 
ATOM   12263 C  CG  . ASN   A 1 1543 ? -15.95700  37.51300  11.48400  1.000 58.20152  ?  1541 ASN   A CG  1 
ATOM   12264 O  OD1 . ASN   A 1 1543 ? -15.19200  38.45500  11.68400  1.000 73.21860  ?  1541 ASN   A OD1 1 
ATOM   12265 N  ND2 . ASN   A 1 1543 ? -16.29200  36.64700  12.43400  1.000 60.38626  ?  1541 ASN   A ND2 1 
ATOM   12266 N  N   . TYR   A 1 1544 ? -19.46800  38.35500  8.12300   1.000 47.85050  ?  1542 TYR   A N   1 
ATOM   12267 C  CA  . TYR   A 1 1544 ? -19.96000  38.59800  6.77700   1.000 43.18567  ?  1542 TYR   A CA  1 
ATOM   12268 C  C   . TYR   A 1 1544 ? -20.50800  40.01600  6.68900   1.000 50.03505  ?  1542 TYR   A C   1 
ATOM   12269 O  O   . TYR   A 1 1544 ? -20.97400  40.58200  7.68200   1.000 40.41227  ?  1542 TYR   A O   1 
ATOM   12270 C  CB  . TYR   A 1 1544 ? -21.06500  37.60600  6.40200   1.000 53.17282  ?  1542 TYR   A CB  1 
ATOM   12271 C  CG  . TYR   A 1 1544 ? -20.59900  36.29800  5.80600   1.000 41.65805  ?  1542 TYR   A CG  1 
ATOM   12272 C  CD1 . TYR   A 1 1544 ? -20.22100  35.23700  6.61800   1.000 50.53646  ?  1542 TYR   A CD1 1 
ATOM   12273 C  CD2 . TYR   A 1 1544 ? -20.56800  36.11300  4.43000   1.000 44.63047  ?  1542 TYR   A CD2 1 
ATOM   12274 C  CE1 . TYR   A 1 1544 ? -19.80900  34.03400  6.07500   1.000 41.22428  ?  1542 TYR   A CE1 1 
ATOM   12275 C  CE2 . TYR   A 1 1544 ? -20.15800  34.91700  3.87900   1.000 46.28799  ?  1542 TYR   A CE2 1 
ATOM   12276 C  CZ  . TYR   A 1 1544 ? -19.77900  33.88100  4.70600   1.000 44.71736  ?  1542 TYR   A CZ  1 
ATOM   12277 O  OH  . TYR   A 1 1544 ? -19.37300  32.68800  4.15800   1.000 43.94061  ?  1542 TYR   A OH  1 
ATOM   12278 N  N   . ARG   A 1 1545 ? -20.45700  40.58600  5.48700   1.000 46.33922  ?  1543 ARG   A N   1 
ATOM   12279 C  CA  . ARG   A 1 1545 ? -21.02500  41.90300  5.23600   1.000 36.10435  ?  1543 ARG   A CA  1 
ATOM   12280 C  C   . ARG   A 1 1545 ? -21.62100  41.92400  3.83800   1.000 45.48311  ?  1543 ARG   A C   1 
ATOM   12281 O  O   . ARG   A 1 1545 ? -20.96700  41.51400  2.87500   1.000 41.37681  ?  1543 ARG   A O   1 
ATOM   12282 C  CB  . ARG   A 1 1545 ? -19.96900  43.00500  5.38400   1.000 48.03418  ?  1543 ARG   A CB  1 
ATOM   12283 C  CG  . ARG   A 1 1545 ? -19.65800  43.37700  6.82600   1.000 41.76290  ?  1543 ARG   A CG  1 
ATOM   12284 C  CD  . ARG   A 1 1545 ? -18.57500  44.43300  6.89200   1.000 51.14007  ?  1543 ARG   A CD  1 
ATOM   12285 N  NE  . ARG   A 1 1545 ? -17.36800  44.02200  6.18500   1.000 57.91434  ?  1543 ARG   A NE  1 
ATOM   12286 C  CZ  . ARG   A 1 1545 ? -16.44300  43.21800  6.69100   1.000 57.70492  ?  1543 ARG   A CZ  1 
ATOM   12287 N  NH1 . ARG   A 1 1545 ? -16.56700  42.69800  7.90200   1.000 53.92230  ?  1543 ARG   A NH1 1 
ATOM   12288 N  NH2 . ARG   A 1 1545 ? -15.36600  42.93200  5.96500   1.000 41.07123  ?  1543 ARG   A NH2 1 
ATOM   12289 N  N   . MET   A 1 1546 ? -22.86000  42.39800  3.73200   1.000 53.90023  ?  1544 MET   A N   1 
ATOM   12290 C  CA  . MET   A 1 1546 ? -23.58600  42.43600  2.47100   1.000 56.64025  ?  1544 MET   A CA  1 
ATOM   12291 C  C   . MET   A 1 1546 ? -23.96400  43.87200  2.13400   1.000 54.83562  ?  1544 MET   A C   1 
ATOM   12292 O  O   . MET   A 1 1546 ? -24.43200  44.62000  2.99800   1.000 46.95701  ?  1544 MET   A O   1 
ATOM   12293 C  CB  . MET   A 1 1546 ? -24.83900  41.55800  2.54100   1.000 48.15795  ?  1544 MET   A CB  1 
ATOM   12294 C  CG  . MET   A 1 1546 ? -24.53800  40.11000  2.89300   1.000 50.35656  ?  1544 MET   A CG  1 
ATOM   12295 S  SD  . MET   A 1 1546 ? -25.99700  39.05300  2.90700   1.000 63.49753  ?  1544 MET   A SD  1 
ATOM   12296 C  CE  . MET   A 1 1546 ? -26.03900  38.48800  1.21400   1.000 33.03442  ?  1544 MET   A CE  1 
ATOM   12297 N  N   . TYR   A 1 1547 ? -23.75200  44.25300  0.87600   1.000 47.13371  ?  1545 TYR   A N   1 
ATOM   12298 C  CA  . TYR   A 1 1547 ? -24.04600  45.59400  0.39400   1.000 35.50717  ?  1545 TYR   A CA  1 
ATOM   12299 C  C   . TYR   A 1 1547 ? -24.89600  45.50400  -0.86200  1.000 39.09698  ?  1545 TYR   A C   1 
ATOM   12300 O  O   . TYR   A 1 1547 ? -24.61200  44.70200  -1.75700  1.000 52.43329  ?  1545 TYR   A O   1 
ATOM   12301 C  CB  . TYR   A 1 1547 ? -22.76200  46.38400  0.08100   1.000 42.94110  ?  1545 TYR   A CB  1 
ATOM   12302 C  CG  . TYR   A 1 1547 ? -21.80400  46.53500  1.24300   1.000 35.89651  ?  1545 TYR   A CG  1 
ATOM   12303 C  CD1 . TYR   A 1 1547 ? -22.19800  47.15800  2.42000   1.000 43.37181  ?  1545 TYR   A CD1 1 
ATOM   12304 C  CD2 . TYR   A 1 1547 ? -20.49900  46.06400  1.15700   1.000 40.99310  ?  1545 TYR   A CD2 1 
ATOM   12305 C  CE1 . TYR   A 1 1547 ? -21.32300  47.30100  3.48200   1.000 51.05524  ?  1545 TYR   A CE1 1 
ATOM   12306 C  CE2 . TYR   A 1 1547 ? -19.61600  46.20300  2.21400   1.000 43.08561  ?  1545 TYR   A CE2 1 
ATOM   12307 C  CZ  . TYR   A 1 1547 ? -20.03400  46.82200  3.37400   1.000 46.43466  ?  1545 TYR   A CZ  1 
ATOM   12308 O  OH  . TYR   A 1 1547 ? -19.16300  46.96400  4.42900   1.000 44.67593  ?  1545 TYR   A OH  1 
ATOM   12309 N  N   . ILE   A 1 1548 ? -25.93300  46.33000  -0.93000  1.000 46.11914  ?  1546 ILE   A N   1 
ATOM   12310 C  CA  . ILE   A 1 1548 ? -26.76900  46.45100  -2.11900  1.000 46.82748  ?  1546 ILE   A CA  1 
ATOM   12311 C  C   . ILE   A 1 1548 ? -26.44200  47.78800  -2.76900  1.000 42.80120  ?  1546 ILE   A C   1 
ATOM   12312 O  O   . ILE   A 1 1548 ? -26.60600  48.84500  -2.14700  1.000 47.73869  ?  1546 ILE   A O   1 
ATOM   12313 C  CB  . ILE   A 1 1548 ? -28.26200  46.34000  -1.78000  1.000 37.91964  ?  1546 ILE   A CB  1 
ATOM   12314 C  CG1 . ILE   A 1 1548 ? -28.56200  44.98900  -1.12900  1.000 31.81410  ?  1546 ILE   A CG1 1 
ATOM   12315 C  CG2 . ILE   A 1 1548 ? -29.09600  46.52100  -3.02900  1.000 39.63425  ?  1546 ILE   A CG2 1 
ATOM   12316 C  CD1 . ILE   A 1 1548 ? -29.97700  44.86500  -0.61100  1.000 32.99466  ?  1546 ILE   A CD1 1 
ATOM   12317 N  N   . ILE   A 1 1549 ? -25.96500  47.74400  -4.01300  1.000 43.42357  ?  1547 ILE   A N   1 
ATOM   12318 C  CA  . ILE   A 1 1549 ? -25.45200  48.92600  -4.68900  1.000 42.06523  ?  1547 ILE   A CA  1 
ATOM   12319 C  C   . ILE   A 1 1549 ? -26.20700  49.13200  -5.99500  1.000 41.08097  ?  1547 ILE   A C   1 
ATOM   12320 O  O   . ILE   A 1 1549 ? -26.81700  48.21200  -6.54700  1.000 37.87031  ?  1547 ILE   A O   1 
ATOM   12321 C  CB  . ILE   A 1 1549 ? -23.93300  48.83300  -4.95000  1.000 54.50406  ?  1547 ILE   A CB  1 
ATOM   12322 C  CG1 . ILE   A 1 1549 ? -23.63600  47.77100  -6.00800  1.000 51.24587  ?  1547 ILE   A CG1 1 
ATOM   12323 C  CG2 . ILE   A 1 1549 ? -23.17900  48.52900  -3.66100  1.000 36.14300  ?  1547 ILE   A CG2 1 
ATOM   12324 C  CD1 . ILE   A 1 1549 ? -22.18400  47.72500  -6.43100  1.000 53.39632  ?  1547 ILE   A CD1 1 
ATOM   12325 N  N   . ASN   A 1 1550 ? -26.15600  50.36500  -6.49000  1.000 49.31679  ?  1548 ASN   A N   1 
ATOM   12326 C  CA  . ASN   A 1 1550 ? -26.82700  50.72900  -7.72900  1.000 55.54401  ?  1548 ASN   A CA  1 
ATOM   12327 C  C   . ASN   A 1 1550 ? -25.85300  50.57300  -8.89800  1.000 61.02424  ?  1548 ASN   A C   1 
ATOM   12328 O  O   . ASN   A 1 1550 ? -24.71600  50.12200  -8.73200  1.000 57.86381  ?  1548 ASN   A O   1 
ATOM   12329 C  CB  . ASN   A 1 1550 ? -27.38900  52.14600  -7.62800  1.000 45.82248  ?  1548 ASN   A CB  1 
ATOM   12330 C  CG  . ASN   A 1 1550 ? -26.30500  53.20500  -7.64400  1.000 46.53574  ?  1548 ASN   A CG  1 
ATOM   12331 O  OD1 . ASN   A 1 1550 ? -25.15600  52.94100  -7.28900  1.000 60.91165  ?  1548 ASN   A OD1 1 
ATOM   12332 N  ND2 . ASN   A 1 1550 ? -26.66400  54.41200  -8.06600  1.000 37.44586  ?  1548 ASN   A ND2 1 
ATOM   12333 N  N   . ARG   A 1 1551 ? -26.28700  50.96000  -10.10000 1.000 60.63842  ?  1549 ARG   A N   1 
ATOM   12334 C  CA  . ARG   A 1 1551 ? -25.45900  50.82700  -11.29400 1.000 49.01728  ?  1549 ARG   A CA  1 
ATOM   12335 C  C   . ARG   A 1 1551 ? -24.23400  51.73700  -11.28900 1.000 48.47587  ?  1549 ARG   A C   1 
ATOM   12336 O  O   . ARG   A 1 1551 ? -23.39400  51.61400  -12.18800 1.000 53.12293  ?  1549 ARG   A O   1 
ATOM   12337 C  CB  . ARG   A 1 1551 ? -26.30300  51.10300  -12.53800 1.000 48.63827  ?  1549 ARG   A CB  1 
ATOM   12338 C  CG  . ARG   A 1 1551 ? -27.22900  52.29900  -12.39400 1.000 78.00264  ?  1549 ARG   A CG  1 
ATOM   12339 C  CD  . ARG   A 1 1551 ? -28.62800  51.98500  -12.90800 1.000 90.52519  ?  1549 ARG   A CD  1 
ATOM   12340 N  NE  . ARG   A 1 1551 ? -28.71600  52.06600  -14.36200 1.000 74.70746  ?  1549 ARG   A NE  1 
ATOM   12341 C  CZ  . ARG   A 1 1551 ? -29.85100  52.03600  -15.04600 1.000 84.60431  ?  1549 ARG   A CZ  1 
ATOM   12342 N  NH1 . ARG   A 1 1551 ? -31.02300  51.93100  -14.44000 1.000 74.32916  ?  1549 ARG   A NH1 1 
ATOM   12343 N  NH2 . ARG   A 1 1551 ? -29.81100  52.11000  -16.37400 1.000 97.42051  ?  1549 ARG   A NH2 1 
ATOM   12344 N  N   . HIS   A 1 1552 ? -24.11000  52.64100  -10.31800 1.000 46.56372  ?  1550 HIS   A N   1 
ATOM   12345 C  CA  . HIS   A 1 1552 ? -22.96200  53.53400  -10.22000 1.000 43.34341  ?  1550 HIS   A CA  1 
ATOM   12346 C  C   . HIS   A 1 1552 ? -22.10300  53.23700  -8.99800  1.000 49.39048  ?  1550 HIS   A C   1 
ATOM   12347 O  O   . HIS   A 1 1552 ? -21.13700  53.96300  -8.73500  1.000 58.53133  ?  1550 HIS   A O   1 
ATOM   12348 C  CB  . HIS   A 1 1552 ? -23.42300  54.99400  -10.20400 1.000 58.88947  ?  1550 HIS   A CB  1 
ATOM   12349 C  CG  . HIS   A 1 1552 ? -24.28700  55.37000  -11.36900 1.000 59.41120  ?  1550 HIS   A CG  1 
ATOM   12350 N  ND1 . HIS   A 1 1552 ? -23.79700  55.47900  -12.65400 1.000 58.39431  ?  1550 HIS   A ND1 1 
ATOM   12351 C  CD2 . HIS   A 1 1552 ? -25.60700  55.66200  -11.44500 1.000 54.72624  ?  1550 HIS   A CD2 1 
ATOM   12352 C  CE1 . HIS   A 1 1552 ? -24.77900  55.82100  -13.47000 1.000 52.26411  ?  1550 HIS   A CE1 1 
ATOM   12353 N  NE2 . HIS   A 1 1552 ? -25.88800  55.93800  -12.76100 1.000 56.67622  ?  1550 HIS   A NE2 1 
ATOM   12354 N  N   . GLY   A 1 1553 ? -22.43600  52.19000  -8.24500  1.000 56.32961  ?  1551 GLY   A N   1 
ATOM   12355 C  CA  . GLY   A 1 1553 ? -21.62900  51.77900  -7.11700  1.000 54.20101  ?  1551 GLY   A CA  1 
ATOM   12356 C  C   . GLY   A 1 1553 ? -21.95800  52.45400  -5.80800  1.000 48.63427  ?  1551 GLY   A C   1 
ATOM   12357 O  O   . GLY   A 1 1553 ? -21.07300  52.58600  -4.95500  1.000 60.63845  ?  1551 GLY   A O   1 
ATOM   12358 N  N   . GLN   A 1 1554 ? -23.20200  52.88100  -5.61300  1.000 48.72816  ?  1552 GLN   A N   1 
ATOM   12359 C  CA  . GLN   A 1 1554 ? -23.61200  53.58000  -4.40400  1.000 54.99510  ?  1552 GLN   A CA  1 
ATOM   12360 C  C   . GLN   A 1 1554 ? -24.57200  52.71400  -3.60100  1.000 45.25105  ?  1552 GLN   A C   1 
ATOM   12361 O  O   . GLN   A 1 1554 ? -25.43400  52.03700  -4.17100  1.000 48.13107  ?  1552 GLN   A O   1 
ATOM   12362 C  CB  . GLN   A 1 1554 ? -24.27400  54.91700  -4.74400  1.000 55.66246  ?  1552 GLN   A CB  1 
ATOM   12363 C  CG  . GLN   A 1 1554 ? -23.43600  55.81200  -5.64300  1.000 57.72735  ?  1552 GLN   A CG  1 
ATOM   12364 C  CD  . GLN   A 1 1554 ? -24.01200  57.20600  -5.76200  1.000 63.43983  ?  1552 GLN   A CD  1 
ATOM   12365 O  OE1 . GLN   A 1 1554 ? -25.16100  57.44600  -5.39300  1.000 58.63321  ?  1552 GLN   A OE1 1 
ATOM   12366 N  NE2 . GLN   A 1 1554 ? -23.21600  58.13500  -6.28000  1.000 63.33632  ?  1552 GLN   A NE2 1 
ATOM   12367 N  N   . LEU   A 1 1555 ? -24.41700  52.74100  -2.27800  1.000 36.13743  ?  1553 LEU   A N   1 
ATOM   12368 C  CA  . LEU   A 1 1555 ? -25.28600  51.96300  -1.40300  1.000 44.88488  ?  1553 LEU   A CA  1 
ATOM   12369 C  C   . LEU   A 1 1555 ? -26.73800  52.40000  -1.55300  1.000 43.77625  ?  1553 LEU   A C   1 
ATOM   12370 O  O   . LEU   A 1 1555 ? -27.06100  53.58400  -1.42000  1.000 57.35628  ?  1553 LEU   A O   1 
ATOM   12371 C  CB  . LEU   A 1 1555 ? -24.83900  52.11400  0.05100   1.000 39.88912  ?  1553 LEU   A CB  1 
ATOM   12372 C  CG  . LEU   A 1 1555 ? -25.36500  51.04400  1.00800   1.000 53.14794  ?  1553 LEU   A CG  1 
ATOM   12373 C  CD1 . LEU   A 1 1555 ? -24.76100  49.68700  0.67900   1.000 52.73511  ?  1553 LEU   A CD1 1 
ATOM   12374 C  CD2 . LEU   A 1 1555 ? -25.09000  51.43300  2.45600   1.000 48.79408  ?  1553 LEU   A CD2 1 
ATOM   12375 N  N   . GLN   A 1 1556 ? -27.61500  51.43500  -1.83600  1.000 40.13438  ?  1554 GLN   A N   1 
ATOM   12376 C  CA  . GLN   A 1 1556 ? -29.03300  51.72900  -1.98100  1.000 42.14756  ?  1554 GLN   A CA  1 
ATOM   12377 C  C   . GLN   A 1 1556 ? -29.70600  51.75900  -0.61000  1.000 49.00364  ?  1554 GLN   A C   1 
ATOM   12378 O  O   . GLN   A 1 1556 ? -29.34400  50.98000  0.27600   1.000 51.48430  ?  1554 GLN   A O   1 
ATOM   12379 C  CB  . GLN   A 1 1556 ? -29.71200  50.68500  -2.86500  1.000 39.74121  ?  1554 GLN   A CB  1 
ATOM   12380 C  CG  . GLN   A 1 1556 ? -29.20500  50.65800  -4.29500  1.000 51.47986  ?  1554 GLN   A CG  1 
ATOM   12381 C  CD  . GLN   A 1 1556 ? -29.87400  51.69400  -5.17300  1.000 48.22703  ?  1554 GLN   A CD  1 
ATOM   12382 O  OE1 . GLN   A 1 1556 ? -29.82400  52.89100  -4.89000  1.000 58.03627  ?  1554 GLN   A OE1 1 
ATOM   12383 N  NE2 . GLN   A 1 1556 ? -30.50400  51.23800  -6.25000  1.000 55.16630  ?  1554 GLN   A NE2 1 
ATOM   12384 N  N   . PRO   A 1 1557 ? -30.67400  52.64300  -0.40800  1.000 46.20554  ?  1555 PRO   A N   1 
ATOM   12385 C  CA  . PRO   A 1 1557 ? -31.41300  52.67900  0.85600   1.000 51.06554  ?  1555 PRO   A CA  1 
ATOM   12386 C  C   . PRO   A 1 1557 ? -32.45300  51.56400  0.90400   1.000 45.07999  ?  1555 PRO   A C   1 
ATOM   12387 O  O   . PRO   A 1 1557 ? -32.57000  50.74400  -0.00500  1.000 42.18769  ?  1555 PRO   A O   1 
ATOM   12388 C  CB  . PRO   A 1 1557 ? -32.06800  54.06100  0.83200   1.000 46.65502  ?  1555 PRO   A CB  1 
ATOM   12389 C  CG  . PRO   A 1 1557 ? -32.27000  54.33800  -0.61700  1.000 47.17700  ?  1555 PRO   A CG  1 
ATOM   12390 C  CD  . PRO   A 1 1557 ? -31.11200  53.69800  -1.33800  1.000 49.90579  ?  1555 PRO   A CD  1 
ATOM   12391 N  N   . ILE   A 1 1558 ? -33.21800  51.55300  1.99800   1.000 39.29527  ?  1556 ILE   A N   1 
ATOM   12392 C  CA  . ILE   A 1 1558 ? -34.24500  50.53700  2.18300   1.000 35.65303  ?  1556 ILE   A CA  1 
ATOM   12393 C  C   . ILE   A 1 1558 ? -35.27200  50.63300  1.06400   1.000 33.32443  ?  1556 ILE   A C   1 
ATOM   12394 O  O   . ILE   A 1 1558 ? -35.64800  51.72900  0.63100   1.000 40.46981  ?  1556 ILE   A O   1 
ATOM   12395 C  CB  . ILE   A 1 1558 ? -34.90000  50.70100  3.56500   1.000 39.61104  ?  1556 ILE   A CB  1 
ATOM   12396 C  CG1 . ILE   A 1 1558 ? -33.84300  50.60300  4.66500   1.000 31.51495  ?  1556 ILE   A CG1 1 
ATOM   12397 C  CG2 . ILE   A 1 1558 ? -35.99100  49.66500  3.78300   1.000 43.32793  ?  1556 ILE   A CG2 1 
ATOM   12398 C  CD1 . ILE   A 1 1558 ? -34.40700  50.69400  6.06200   1.000 32.91280  ?  1556 ILE   A CD1 1 
ATOM   12399 N  N   . GLY   A 1 1559 ? -35.71500  49.47900  0.57300   1.000 38.18373  ?  1557 GLY   A N   1 
ATOM   12400 C  CA  . GLY   A 1 1559 ? -36.77800  49.45400  -0.41100  1.000 29.58473  ?  1557 GLY   A CA  1 
ATOM   12401 C  C   . GLY   A 1 1559 ? -36.28500  49.56200  -1.83700  1.000 34.58956  ?  1557 GLY   A C   1 
ATOM   12402 O  O   . GLY   A 1 1559 ? -36.84400  48.93100  -2.74000  1.000 32.88562  ?  1557 GLY   A O   1 
ATOM   12403 N  N   . VAL   A 1 1560 ? -35.23400  50.34400  -2.04800  1.000 36.77671  ?  1558 VAL   A N   1 
ATOM   12404 C  CA  . VAL   A 1 1560 ? -34.70000  50.56500  -3.39500  1.000 39.69589  ?  1558 VAL   A CA  1 
ATOM   12405 C  C   . VAL   A 1 1560 ? -33.83100  49.37000  -3.78300  1.000 41.88233  ?  1558 VAL   A C   1 
ATOM   12406 O  O   . VAL   A 1 1560 ? -32.91100  49.01300  -3.03000  1.000 44.91021  ?  1558 VAL   A O   1 
ATOM   12407 C  CB  . VAL   A 1 1560 ? -33.90500  51.86600  -3.44800  1.000 49.42505  ?  1558 VAL   A CB  1 
ATOM   12408 C  CG1 . VAL   A 1 1560 ? -33.40000  52.12700  -4.86200  1.000 41.87541  ?  1558 VAL   A CG1 1 
ATOM   12409 C  CG2 . VAL   A 1 1560 ? -34.76000  53.03200  -2.95100  1.000 45.48130  ?  1558 VAL   A CG2 1 
ATOM   12410 N  N   . PRO   A 1 1561 ? -34.08100  48.74100  -4.92700  1.000 43.69126  ?  1559 PRO   A N   1 
ATOM   12411 C  CA  . PRO   A 1 1561 ? -33.35100  47.52200  -5.28400  1.000 39.96960  ?  1559 PRO   A CA  1 
ATOM   12412 C  C   . PRO   A 1 1561 ? -31.99900  47.80600  -5.92300  1.000 44.67935  ?  1559 PRO   A C   1 
ATOM   12413 O  O   . PRO   A 1 1561 ? -31.73000  48.88900  -6.44500  1.000 45.01664  ?  1559 PRO   A O   1 
ATOM   12414 C  CB  . PRO   A 1 1561 ? -34.29100  46.84000  -6.28300  1.000 37.77645  ?  1559 PRO   A CB  1 
ATOM   12415 C  CG  . PRO   A 1 1561 ? -34.97600  47.97200  -6.95100  1.000 45.55780  ?  1559 PRO   A CG  1 
ATOM   12416 C  CD  . PRO   A 1 1561 ? -35.13800  49.05300  -5.90500  1.000 53.02976  ?  1559 PRO   A CD  1 
ATOM   12417 N  N   . GLY   A 1 1562 ? -31.15000  46.78600  -5.87800  1.000 51.91579  ?  1560 GLY   A N   1 
ATOM   12418 C  CA  . GLY   A 1 1562 ? -29.82700  46.86900  -6.46000  1.000 42.29300  ?  1560 GLY   A CA  1 
ATOM   12419 C  C   . GLY   A 1 1562 ? -29.15700  45.51200  -6.44900  1.000 46.81698  ?  1560 GLY   A C   1 
ATOM   12420 O  O   . GLY   A 1 1562 ? -29.78400  44.49200  -6.16100  1.000 49.22445  ?  1560 GLY   A O   1 
ATOM   12421 N  N   . GLU   A 1 1563 ? -27.86100  45.51400  -6.76300  1.000 48.24314  ?  1561 GLU   A N   1 
ATOM   12422 C  CA  . GLU   A 1 1563 ? -27.08400  44.28200  -6.83900  1.000 41.85656  ?  1561 GLU   A CA  1 
ATOM   12423 C  C   . GLU   A 1 1563 ? -26.53500  43.91000  -5.47000  1.000 53.64943  ?  1561 GLU   A C   1 
ATOM   12424 O  O   . GLU   A 1 1563 ? -25.91500  44.73800  -4.79300  1.000 50.08337  ?  1561 GLU   A O   1 
ATOM   12425 C  CB  . GLU   A 1 1563 ? -25.92700  44.41200  -7.83000  1.000 55.34602  ?  1561 GLU   A CB  1 
ATOM   12426 C  CG  . GLU   A 1 1563 ? -25.12800  43.11800  -7.98100  1.000 58.78815  ?  1561 GLU   A CG  1 
ATOM   12427 C  CD  . GLU   A 1 1563 ? -23.95900  43.24500  -8.93600  1.000 63.47903  ?  1561 GLU   A CD  1 
ATOM   12428 O  OE1 . GLU   A 1 1563 ? -23.43200  44.36600  -9.08900  1.000 82.18758  ?  1561 GLU   A OE1 1 
ATOM   12429 O  OE2 . GLU   A 1 1563 ? -23.56700  42.22000  -9.53700  1.000 62.61386  -1 1561 GLU   A OE2 1 
ATOM   12430 N  N   . LEU   A 1 1564 ? -26.74700  42.65800  -5.07700  1.000 49.90291  ?  1562 LEU   A N   1 
ATOM   12431 C  CA  . LEU   A 1 1564 ? -26.19100  42.16200  -3.82800  1.000 42.63780  ?  1562 LEU   A CA  1 
ATOM   12432 C  C   . LEU   A 1 1564 ? -24.69000  41.94900  -3.97100  1.000 44.33697  ?  1562 LEU   A C   1 
ATOM   12433 O  O   . LEU   A 1 1564 ? -24.21100  41.43900  -4.98800  1.000 49.03994  ?  1562 LEU   A O   1 
ATOM   12434 C  CB  . LEU   A 1 1564 ? -26.88100  40.86200  -3.42600  1.000 38.07584  ?  1562 LEU   A CB  1 
ATOM   12435 C  CG  . LEU   A 1 1564 ? -26.73000  40.39700  -1.97900  1.000 36.53321  ?  1562 LEU   A CG  1 
ATOM   12436 C  CD1 . LEU   A 1 1564 ? -26.72300  41.57300  -1.01600  1.000 38.20043  ?  1562 LEU   A CD1 1 
ATOM   12437 C  CD2 . LEU   A 1 1564 ? -27.86200  39.44500  -1.65000  1.000 37.25914  ?  1562 LEU   A CD2 1 
ATOM   12438 N  N   . CYS   A 1 1565 ? -23.94300  42.35500  -2.94800  1.000 42.87368  ?  1563 CYS   A N   1 
ATOM   12439 C  CA  . CYS   A 1 1565 ? -22.49000  42.25700  -2.96200  1.000 41.35842  ?  1563 CYS   A CA  1 
ATOM   12440 C  C   . CYS   A 1 1565 ? -22.01600  41.73100  -1.61900  1.000 48.05962  ?  1563 CYS   A C   1 
ATOM   12441 O  O   . CYS   A 1 1565 ? -22.47400  42.20000  -0.57400  1.000 50.37932  ?  1563 CYS   A O   1 
ATOM   12442 C  CB  . CYS   A 1 1565 ? -21.84600  43.61400  -3.26200  1.000 43.46016  ?  1563 CYS   A CB  1 
ATOM   12443 S  SG  . CYS   A 1 1565 ? -22.16200  44.21100  -4.93600  1.000 55.35209  ?  1563 CYS   A SG  1 
ATOM   12444 N  N   . ILE   A 1 1566 ? -21.09900  40.76400  -1.64700  1.000 39.66908  ?  1564 ILE   A N   1 
ATOM   12445 C  CA  . ILE   A 1 1566 ? -20.63900  40.09300  -0.43800  1.000 46.20930  ?  1564 ILE   A CA  1 
ATOM   12446 C  C   . ILE   A 1 1566 ? -19.24000  40.58100  -0.09600  1.000 48.56739  ?  1564 ILE   A C   1 
ATOM   12447 O  O   . ILE   A 1 1566 ? -18.43100  40.89600  -0.97600  1.000 47.06840  ?  1564 ILE   A O   1 
ATOM   12448 C  CB  . ILE   A 1 1566 ? -20.64700  38.55500  -0.57700  1.000 54.02700  ?  1564 ILE   A CB  1 
ATOM   12449 C  CG1 . ILE   A 1 1566 ? -21.82400  38.09000  -1.43000  1.000 47.41750  ?  1564 ILE   A CG1 1 
ATOM   12450 C  CG2 . ILE   A 1 1566 ? -20.70900  37.89400  0.79500   1.000 41.89863  ?  1564 ILE   A CG2 1 
ATOM   12451 C  CD1 . ILE   A 1 1566 ? -23.16600  38.38500  -0.82300  1.000 45.08074  ?  1564 ILE   A CD1 1 
ATOM   12452 N  N   . ALA   A 1 1567 ? -18.95500  40.62700  1.20200   1.000 43.65878  ?  1565 ALA   A N   1 
ATOM   12453 C  CA  . ALA   A 1 1567 ? -17.64100  41.01400  1.69200   1.000 49.42750  ?  1565 ALA   A CA  1 
ATOM   12454 C  C   . ALA   A 1 1567 ? -17.44900  40.42100  3.07800   1.000 48.63800  ?  1565 ALA   A C   1 
ATOM   12455 O  O   . ALA   A 1 1567 ? -18.41500  40.11000  3.78000   1.000 56.91099  ?  1565 ALA   A O   1 
ATOM   12456 C  CB  . ALA   A 1 1567 ? -17.47600  42.53500  1.72700   1.000 59.97710  ?  1565 ALA   A CB  1 
ATOM   12457 N  N   . GLY   A 1 1568 ? -16.18600  40.26300  3.46200   1.000 50.83896  ?  1566 GLY   A N   1 
ATOM   12458 C  CA  . GLY   A 1 1568 ? -15.86300  39.74300  4.77000   1.000 57.63121  ?  1566 GLY   A CA  1 
ATOM   12459 C  C   . GLY   A 1 1568 ? -14.78600  38.68500  4.68700   1.000 63.82483  ?  1566 GLY   A C   1 
ATOM   12460 O  O   . GLY   A 1 1568 ? -14.01500  38.62400  3.72300   1.000 43.54093  ?  1566 GLY   A O   1 
ATOM   12461 N  N   . ALA   A 1 1569 ? -14.75200  37.83600  5.71600   1.000 56.79784  ?  1567 ALA   A N   1 
ATOM   12462 C  CA  . ALA   A 1 1569 ? -13.66900  36.87300  5.87200   1.000 44.69444  ?  1567 ALA   A CA  1 
ATOM   12463 C  C   . ALA   A 1 1569 ? -13.79300  35.71100  4.89300   1.000 52.80016  ?  1567 ALA   A C   1 
ATOM   12464 O  O   . ALA   A 1 1569 ? -12.82700  35.36400  4.20400   1.000 66.80366  ?  1567 ALA   A O   1 
ATOM   12465 C  CB  . ALA   A 1 1569 ? -13.63900  36.35700  7.31100   1.000 42.61591  ?  1567 ALA   A CB  1 
ATOM   12466 N  N   . SER   A 1 1570 ? -14.97100  35.10000  4.81600   1.000 55.23688  ?  1568 SER   A N   1 
ATOM   12467 C  CA  . SER   A 1 1570 ? -15.15800  33.87900  4.03300   1.000 43.49013  ?  1568 SER   A CA  1 
ATOM   12468 C  C   . SER   A 1 1570 ? -15.34800  34.13800  2.54600   1.000 40.79432  ?  1568 SER   A C   1 
ATOM   12469 O  O   . SER   A 1 1570 ? -16.20500  33.52000  1.90900   1.000 57.70790  ?  1568 SER   A O   1 
ATOM   12470 C  CB  . SER   A 1 1570 ? -16.33900  33.09800  4.60100   1.000 33.29874  ?  1568 SER   A CB  1 
ATOM   12471 O  OG  . SER   A 1 1570 ? -16.34600  33.15400  6.01600   1.000 52.19328  ?  1568 SER   A OG  1 
ATOM   12472 N  N   . LEU   A 1 1571 ? -14.56400  35.03700  1.96700   1.000 36.60300  ?  1569 LEU   A N   1 
ATOM   12473 C  CA  . LEU   A 1 1571 ? -14.63400  35.30100  0.54000   1.000 47.28440  ?  1569 LEU   A CA  1 
ATOM   12474 C  C   . LEU   A 1 1571 ? -13.64800  34.41100  -0.20200  1.000 44.46159  ?  1569 LEU   A C   1 
ATOM   12475 O  O   . LEU   A 1 1571 ? -12.60900  34.01800  0.33600   1.000 60.35563  ?  1569 LEU   A O   1 
ATOM   12476 C  CB  . LEU   A 1 1571 ? -14.34100  36.77500  0.25200   1.000 59.18921  ?  1569 LEU   A CB  1 
ATOM   12477 C  CG  . LEU   A 1 1571 ? -15.32200  37.50700  -0.66600  1.000 56.69324  ?  1569 LEU   A CG  1 
ATOM   12478 C  CD1 . LEU   A 1 1571 ? -16.74400  37.40500  -0.13900  1.000 50.90295  ?  1569 LEU   A CD1 1 
ATOM   12479 C  CD2 . LEU   A 1 1571 ? -14.91500  38.96000  -0.80900  1.000 52.89139  ?  1569 LEU   A CD2 1 
ATOM   12480 N  N   . ALA   A 1 1572 ? -13.98700  34.08400  -1.44500  1.000 44.09447  ?  1570 ALA   A N   1 
ATOM   12481 C  CA  . ALA   A 1 1572 ? -13.11800  33.23900  -2.25100  1.000 59.06359  ?  1570 ALA   A CA  1 
ATOM   12482 C  C   . ALA   A 1 1572 ? -11.85800  33.99400  -2.65700  1.000 67.58525  ?  1570 ALA   A C   1 
ATOM   12483 O  O   . ALA   A 1 1572 ? -11.87800  35.20800  -2.87400  1.000 69.23768  ?  1570 ALA   A O   1 
ATOM   12484 C  CB  . ALA   A 1 1572 ? -13.85200  32.75000  -3.49900  1.000 48.38271  ?  1570 ALA   A CB  1 
ATOM   12485 N  N   . ARG   A 1 1573 ? -10.74500  33.25900  -2.75700  1.000 69.53431  ?  1571 ARG   A N   1 
ATOM   12486 C  CA  . ARG   A 1 1573 ? -9.52400   33.86500  -3.27700  1.000 62.37200  ?  1571 ARG   A CA  1 
ATOM   12487 C  C   . ARG   A 1 1573 ? -9.72100   34.34500  -4.70900  1.000 60.01287  ?  1571 ARG   A C   1 
ATOM   12488 O  O   . ARG   A 1 1573 ? -9.14600   35.36400  -5.10900  1.000 76.52590  ?  1571 ARG   A O   1 
ATOM   12489 C  CB  . ARG   A 1 1573 ? -8.35700   32.87400  -3.20800  1.000 69.17372  ?  1571 ARG   A CB  1 
ATOM   12490 C  CG  . ARG   A 1 1573 ? -7.06400   33.42900  -3.80200  1.000 77.15787  ?  1571 ARG   A CG  1 
ATOM   12491 C  CD  . ARG   A 1 1573 ? -5.94400   32.40600  -3.85800  1.000 62.64356  ?  1571 ARG   A CD  1 
ATOM   12492 N  NE  . ARG   A 1 1573 ? -5.56600   31.88500  -2.55100  1.000 67.62793  ?  1571 ARG   A NE  1 
ATOM   12493 C  CZ  . ARG   A 1 1573 ? -4.81700   30.80500  -2.37100  1.000 59.50981  ?  1571 ARG   A CZ  1 
ATOM   12494 N  NH1 . ARG   A 1 1573 ? -4.36200   30.10300  -3.39800  1.000 47.66919  ?  1571 ARG   A NH1 1 
ATOM   12495 N  NH2 . ARG   A 1 1573 ? -4.51000   30.42600  -1.13300  1.000 37.02368  ?  1571 ARG   A NH2 1 
ATOM   12496 N  N   . GLY   A 1 1574 ? -10.53400  33.64400  -5.47900  1.000 43.73856  ?  1572 GLY   A N   1 
ATOM   12497 C  CA  . GLY   A 1 1574 ? -10.82800  34.03500  -6.83900  1.000 51.36687  ?  1572 GLY   A CA  1 
ATOM   12498 C  C   . GLY   A 1 1574 ? -11.20400  32.81600  -7.65500  1.000 61.94185  ?  1572 GLY   A C   1 
ATOM   12499 O  O   . GLY   A 1 1574 ? -11.39700  31.72800  -7.12200  1.000 62.78476  ?  1572 GLY   A O   1 
ATOM   12500 N  N   . TYR   A 1 1575 ? -11.30700  33.02300  -8.96500  1.000 63.25610  ?  1573 TYR   A N   1 
ATOM   12501 C  CA  . TYR   A 1 1575 ? -11.56500  31.93400  -9.89800  1.000 58.92552  ?  1573 TYR   A CA  1 
ATOM   12502 C  C   . TYR   A 1 1575 ? -10.24100  31.36000  -10.39100 1.000 81.45651  ?  1573 TYR   A C   1 
ATOM   12503 O  O   . TYR   A 1 1575 ? -9.32600   32.11000  -10.74600 1.000 90.14371  ?  1573 TYR   A O   1 
ATOM   12504 C  CB  . TYR   A 1 1575 ? -12.41100  32.41700  -11.07500 1.000 64.29073  ?  1573 TYR   A CB  1 
ATOM   12505 C  CG  . TYR   A 1 1575 ? -13.77400  32.93200  -10.67400 1.000 71.13554  ?  1573 TYR   A CG  1 
ATOM   12506 C  CD1 . TYR   A 1 1575 ? -14.79200  32.05600  -10.32200 1.000 69.45301  ?  1573 TYR   A CD1 1 
ATOM   12507 C  CD2 . TYR   A 1 1575 ? -14.04400  34.29500  -10.64600 1.000 72.01360  ?  1573 TYR   A CD2 1 
ATOM   12508 C  CE1 . TYR   A 1 1575 ? -16.04100  32.52100  -9.95500  1.000 76.07055  ?  1573 TYR   A CE1 1 
ATOM   12509 C  CE2 . TYR   A 1 1575 ? -15.29000  34.77000  -10.28000 1.000 66.34272  ?  1573 TYR   A CE2 1 
ATOM   12510 C  CZ  . TYR   A 1 1575 ? -16.28500  33.87700  -9.93600  1.000 71.09239  ?  1573 TYR   A CZ  1 
ATOM   12511 O  OH  . TYR   A 1 1575 ? -17.52800  34.34100  -9.57100  1.000 75.22420  ?  1573 TYR   A OH  1 
ATOM   12512 N  N   . LEU   A 1 1576 ? -10.14400  30.03100  -10.40600 1.000 83.04444  ?  1574 LEU   A N   1 
ATOM   12513 C  CA  . LEU   A 1 1576 ? -8.89700   29.36200  -10.76100 1.000 67.19829  ?  1574 LEU   A CA  1 
ATOM   12514 C  C   . LEU   A 1 1576 ? -8.58000   29.57300  -12.23600 1.000 81.46368  ?  1574 LEU   A C   1 
ATOM   12515 O  O   . LEU   A 1 1576 ? -9.38400   29.22500  -13.10800 1.000 81.07760  ?  1574 LEU   A O   1 
ATOM   12516 C  CB  . LEU   A 1 1576 ? -8.99000   27.87200  -10.44100 1.000 74.01703  ?  1574 LEU   A CB  1 
ATOM   12517 C  CG  . LEU   A 1 1576 ? -7.80700   26.98300  -10.83000 1.000 77.71364  ?  1574 LEU   A CG  1 
ATOM   12518 C  CD1 . LEU   A 1 1576 ? -6.60900   27.18600  -9.91800  1.000 75.60122  ?  1574 LEU   A CD1 1 
ATOM   12519 C  CD2 . LEU   A 1 1576 ? -8.24700   25.53400  -10.80600 1.000 77.29056  ?  1574 LEU   A CD2 1 
ATOM   12520 N  N   . ASN   A 1 1577 ? -7.40200   30.14000  -12.50600 1.000 82.80949  ?  1575 ASN   A N   1 
ATOM   12521 C  CA  . ASN   A 1 1577 ? -6.92000   30.37000  -13.86900 1.000 83.67633  ?  1575 ASN   A CA  1 
ATOM   12522 C  C   . ASN   A 1 1577 ? -7.92100   31.18400  -14.68500 1.000 83.62823  ?  1575 ASN   A C   1 
ATOM   12523 O  O   . ASN   A 1 1577 ? -8.20400   30.87800  -15.84500 1.000 79.72789  ?  1575 ASN   A O   1 
ATOM   12524 C  CB  . ASN   A 1 1577 ? -6.58400   29.04800  -14.56300 1.000 94.96359  ?  1575 ASN   A CB  1 
ATOM   12525 C  CG  . ASN   A 1 1577 ? -5.42500   28.32500  -13.90200 1.000 96.35012  ?  1575 ASN   A CG  1 
ATOM   12526 O  OD1 . ASN   A 1 1577 ? -4.54300   28.95200  -13.31400 1.000 112.33525 ?  1575 ASN   A OD1 1 
ATOM   12527 N  ND2 . ASN   A 1 1577 ? -5.42400   27.00000  -13.99000 1.000 63.95644  ?  1575 ASN   A ND2 1 
ATOM   12528 N  N   . ASN   A 1 1578 ? -8.47000   32.22900  -14.06300 1.000 90.14333  ?  1576 ASN   A N   1 
ATOM   12529 C  CA  . ASN   A 1 1578 ? -9.32400   33.19600  -14.75500 1.000 86.60457  ?  1576 ASN   A CA  1 
ATOM   12530 C  C   . ASN   A 1 1578 ? -9.22900   34.53200  -14.03100 1.000 89.55476  ?  1576 ASN   A C   1 
ATOM   12531 O  O   . ASN   A 1 1578 ? -10.20500  35.01500  -13.44500 1.000 80.53277  ?  1576 ASN   A O   1 
ATOM   12532 C  CB  . ASN   A 1 1578 ? -10.76900  32.70300  -14.82000 1.000 63.45866  ?  1576 ASN   A CB  1 
ATOM   12533 C  CG  . ASN   A 1 1578 ? -11.51600  33.24100  -16.02900 1.000 74.65577  ?  1576 ASN   A CG  1 
ATOM   12534 O  OD1 . ASN   A 1 1578 ? -11.25600  34.35200  -16.49100 1.000 78.16148  ?  1576 ASN   A OD1 1 
ATOM   12535 N  ND2 . ASN   A 1 1578 ? -12.45200  32.45100  -16.54500 1.000 81.15707  ?  1576 ASN   A ND2 1 
ATOM   12536 N  N   . PRO   A 1 1579 ? -8.04700   35.16200  -14.04700 1.000 95.58654  ?  1577 PRO   A N   1 
ATOM   12537 C  CA  . PRO   A 1 1579 ? -7.90300   36.45700  -13.36400 1.000 78.27045  ?  1577 PRO   A CA  1 
ATOM   12538 C  C   . PRO   A 1 1579 ? -8.73700   37.55500  -13.99100 1.000 75.79359  ?  1577 PRO   A C   1 
ATOM   12539 O  O   . PRO   A 1 1579 ? -9.03200   38.54700  -13.31300 1.000 63.10433  ?  1577 PRO   A O   1 
ATOM   12540 C  CB  . PRO   A 1 1579 ? -6.40200   36.76300  -13.48600 1.000 56.90555  ?  1577 PRO   A CB  1 
ATOM   12541 C  CG  . PRO   A 1 1579 ? -5.76500   35.47900  -13.93600 1.000 66.09676  ?  1577 PRO   A CG  1 
ATOM   12542 C  CD  . PRO   A 1 1579 ? -6.80700   34.77500  -14.73700 1.000 74.42692  ?  1577 PRO   A CD  1 
ATOM   12543 N  N   . ALA   A 1 1580 ? -9.11300   37.41800  -15.26300 1.000 78.04416  ?  1578 ALA   A N   1 
ATOM   12544 C  CA  . ALA   A 1 1580 ? -10.04600  38.36300  -15.86200 1.000 68.50420  ?  1578 ALA   A CA  1 
ATOM   12545 C  C   . ALA   A 1 1580 ? -11.35900  38.37300  -15.09200 1.000 77.65670  ?  1578 ALA   A C   1 
ATOM   12546 O  O   . ALA   A 1 1580 ? -11.75700  39.39800  -14.53000 1.000 86.04304  ?  1578 ALA   A O   1 
ATOM   12547 C  CB  . ALA   A 1 1580 ? -10.27400  38.01700  -17.33400 1.000 75.22771  ?  1578 ALA   A CB  1 
ATOM   12548 N  N   . LEU   A 1 1581 ? -12.02900  37.21700  -15.02500 1.000 80.10273  ?  1579 LEU   A N   1 
ATOM   12549 C  CA  . LEU   A 1 1581 ? -13.29300  37.12300  -14.30200 1.000 71.47406  ?  1579 LEU   A CA  1 
ATOM   12550 C  C   . LEU   A 1 1581 ? -13.13600  37.49900  -12.83400 1.000 68.49210  ?  1579 LEU   A C   1 
ATOM   12551 O  O   . LEU   A 1 1581 ? -14.06400  38.05600  -12.23700 1.000 79.91982  ?  1579 LEU   A O   1 
ATOM   12552 C  CB  . LEU   A 1 1581 ? -13.86600  35.71100  -14.42100 1.000 67.20300  ?  1579 LEU   A CB  1 
ATOM   12553 C  CG  . LEU   A 1 1581 ? -15.38900  35.59300  -14.36500 1.000 68.11987  ?  1579 LEU   A CG  1 
ATOM   12554 C  CD1 . LEU   A 1 1581 ? -15.98000  35.79400  -15.75100 1.000 75.17896  ?  1579 LEU   A CD1 1 
ATOM   12555 C  CD2 . LEU   A 1 1581 ? -15.80700  34.25000  -13.78500 1.000 73.88089  ?  1579 LEU   A CD2 1 
ATOM   12556 N  N   . THR   A 1 1582 ? -11.98000  37.20300  -12.23500 1.000 60.33693  ?  1580 THR   A N   1 
ATOM   12557 C  CA  . THR   A 1 1582 ? -11.77100  37.55200  -10.83300 1.000 66.28107  ?  1580 THR   A CA  1 
ATOM   12558 C  C   . THR   A 1 1582 ? -11.73500  39.06200  -10.63400 1.000 75.92743  ?  1580 THR   A C   1 
ATOM   12559 O  O   . THR   A 1 1582 ? -12.14400  39.55700  -9.57700  1.000 81.78570  ?  1580 THR   A O   1 
ATOM   12560 C  CB  . THR   A 1 1582 ? -10.48300  36.90900  -10.31500 1.000 69.26219  ?  1580 THR   A CB  1 
ATOM   12561 O  OG1 . THR   A 1 1582 ? -10.49300  35.50900  -10.62000 1.000 56.73789  ?  1580 THR   A OG1 1 
ATOM   12562 C  CG2 . THR   A 1 1582 ? -10.35700  37.09200  -8.80600  1.000 60.63429  ?  1580 THR   A CG2 1 
ATOM   12563 N  N   . GLU   A 1 1583 ? -11.26700  39.80800  -11.63700 1.000 82.70829  ?  1581 GLU   A N   1 
ATOM   12564 C  CA  . GLU   A 1 1583 ? -11.25800  41.26200  -11.53700 1.000 77.86927  ?  1581 GLU   A CA  1 
ATOM   12565 C  C   . GLU   A 1 1583 ? -12.64200  41.86400  -11.75200 1.000 70.62034  ?  1581 GLU   A C   1 
ATOM   12566 O  O   . GLU   A 1 1583 ? -12.96700  42.88200  -11.13200 1.000 64.64334  ?  1581 GLU   A O   1 
ATOM   12567 C  CB  . GLU   A 1 1583 ? -10.26800  41.85500  -12.54100 1.000 89.03379  ?  1581 GLU   A CB  1 
ATOM   12568 C  CG  . GLU   A 1 1583 ? -8.96700   42.33900  -11.91800 1.000 94.44713  ?  1581 GLU   A CG  1 
ATOM   12569 C  CD  . GLU   A 1 1583 ? -8.09900   43.10300  -12.90000 1.000 121.52956 ?  1581 GLU   A CD  1 
ATOM   12570 O  OE1 . GLU   A 1 1583 ? -8.65700   43.71700  -13.83400 1.000 109.74988 ?  1581 GLU   A OE1 1 
ATOM   12571 O  OE2 . GLU   A 1 1583 ? -6.86000   43.09200  -12.73500 1.000 129.71956 -1 1581 GLU   A OE2 1 
ATOM   12572 N  N   . GLU   A 1 1584 ? -13.46700  41.26400  -12.61700 1.000 69.67151  ?  1582 GLU   A N   1 
ATOM   12573 C  CA  . GLU   A 1 1584 ? -14.81100  41.78800  -12.84200 1.000 69.81500  ?  1582 GLU   A CA  1 
ATOM   12574 C  C   . GLU   A 1 1584 ? -15.75200  41.49100  -11.68300 1.000 68.49992  ?  1582 GLU   A C   1 
ATOM   12575 O  O   . GLU   A 1 1584 ? -16.73000  42.22100  -11.48700 1.000 85.64912  ?  1582 GLU   A O   1 
ATOM   12576 C  CB  . GLU   A 1 1584 ? -15.40500  41.21700  -14.13300 1.000 55.87212  ?  1582 GLU   A CB  1 
ATOM   12577 C  CG  . GLU   A 1 1584 ? -14.37900  40.73300  -15.12900 1.000 85.61359  ?  1582 GLU   A CG  1 
ATOM   12578 C  CD  . GLU   A 1 1584 ? -14.99100  40.25700  -16.43300 1.000 106.77415 ?  1582 GLU   A CD  1 
ATOM   12579 O  OE1 . GLU   A 1 1584 ? -16.23200  40.12100  -16.50400 1.000 110.06662 ?  1582 GLU   A OE1 1 
ATOM   12580 O  OE2 . GLU   A 1 1584 ? -14.22300  39.99500  -17.38200 1.000 113.20142 -1 1582 GLU   A OE2 1 
ATOM   12581 N  N   . LYS   A 1 1585 ? -15.48800  40.43400  -10.91600 1.000 59.20932  ?  1583 LYS   A N   1 
ATOM   12582 C  CA  . LYS   A 1 1585 ? -16.40500  40.00400  -9.86800  1.000 59.75010  ?  1583 LYS   A CA  1 
ATOM   12583 C  C   . LYS   A 1 1585 ? -15.91000  40.28600  -8.46000  1.000 55.55419  ?  1583 LYS   A C   1 
ATOM   12584 O  O   . LYS   A 1 1585 ? -16.73000  40.51600  -7.57000  1.000 51.07047  ?  1583 LYS   A O   1 
ATOM   12585 C  CB  . LYS   A 1 1585 ? -16.69900  38.50300  -9.99600  1.000 52.08573  ?  1583 LYS   A CB  1 
ATOM   12586 C  CG  . LYS   A 1 1585 ? -17.15300  38.06700  -11.38400 1.000 59.32942  ?  1583 LYS   A CG  1 
ATOM   12587 C  CD  . LYS   A 1 1585 ? -18.17100  39.02600  -11.98200 1.000 62.25071  ?  1583 LYS   A CD  1 
ATOM   12588 C  CE  . LYS   A 1 1585 ? -19.09400  38.31500  -12.95900 1.000 73.93677  ?  1583 LYS   A CE  1 
ATOM   12589 N  NZ  . LYS   A 1 1585 ? -19.60000  39.24000  -14.01200 1.000 98.43131  ?  1583 LYS   A NZ  1 
ATOM   12590 N  N   . PHE   A 1 1586 ? -14.59900  40.27000  -8.23200  1.000 54.85938  ?  1584 PHE   A N   1 
ATOM   12591 C  CA  . PHE   A 1 1586 ? -14.01500  40.55200  -6.92100  1.000 61.22033  ?  1584 PHE   A CA  1 
ATOM   12592 C  C   . PHE   A 1 1586 ? -13.30100  41.89700  -7.01700  1.000 66.27576  ?  1584 PHE   A C   1 
ATOM   12593 O  O   . PHE   A 1 1586 ? -12.08600  41.97300  -7.20900  1.000 75.33387  ?  1584 PHE   A O   1 
ATOM   12594 C  CB  . PHE   A 1 1586 ? -13.06000  39.42600  -6.47700  1.000 66.78165  ?  1584 PHE   A CB  1 
ATOM   12595 C  CG  . PHE   A 1 1586 ? -13.73900  38.10300  -6.25800  1.000 50.27063  ?  1584 PHE   A CG  1 
ATOM   12596 C  CD1 . PHE   A 1 1586 ? -13.95500  37.23600  -7.31700  1.000 68.13244  ?  1584 PHE   A CD1 1 
ATOM   12597 C  CD2 . PHE   A 1 1586 ? -14.15400  37.72300  -4.99200  1.000 48.37055  ?  1584 PHE   A CD2 1 
ATOM   12598 C  CE1 . PHE   A 1 1586 ? -14.57900  36.01700  -7.11900  1.000 64.79572  ?  1584 PHE   A CE1 1 
ATOM   12599 C  CE2 . PHE   A 1 1586 ? -14.77800  36.50500  -4.78700  1.000 51.01896  ?  1584 PHE   A CE2 1 
ATOM   12600 C  CZ  . PHE   A 1 1586 ? -14.99000  35.65100  -5.85300  1.000 53.82982  ?  1584 PHE   A CZ  1 
ATOM   12601 N  N   . THR   A 1 1587 ? -14.07400  42.96900  -6.87300  1.000 74.46561  ?  1585 THR   A N   1 
ATOM   12602 C  CA  . THR   A 1 1587 ? -13.62400  44.34000  -7.06500  1.000 56.33470  ?  1585 THR   A CA  1 
ATOM   12603 C  C   . THR   A 1 1587 ? -13.40500  45.03900  -5.72900  1.000 61.19114  ?  1585 THR   A C   1 
ATOM   12604 O  O   . THR   A 1 1587 ? -14.16000  44.81000  -4.77700  1.000 60.10865  ?  1585 THR   A O   1 
ATOM   12605 C  CB  . THR   A 1 1587 ? -14.65200  45.12700  -7.87800  1.000 45.28578  ?  1585 THR   A CB  1 
ATOM   12606 O  OG1 . THR   A 1 1587 ? -15.82300  45.34700  -7.08200  1.000 58.16255  ?  1585 THR   A OG1 1 
ATOM   12607 C  CG2 . THR   A 1 1587 ? -15.04400  44.35800  -9.13000  1.000 34.89473  ?  1585 THR   A CG2 1 
ATOM   12608 N  N   . PRO   A 1 1588 ? -12.38100  45.88300  -5.62200  1.000 69.37876  ?  1586 PRO   A N   1 
ATOM   12609 C  CA  . PRO   A 1 1588 ? -12.24100  46.71500  -4.42500  1.000 63.97732  ?  1586 PRO   A CA  1 
ATOM   12610 C  C   . PRO   A 1 1588 ? -13.27500  47.82700  -4.43600  1.000 64.95377  ?  1586 PRO   A C   1 
ATOM   12611 O  O   . PRO   A 1 1588 ? -13.63800  48.35700  -5.48800  1.000 64.79384  ?  1586 PRO   A O   1 
ATOM   12612 C  CB  . PRO   A 1 1588 ? -10.81800  47.27800  -4.53800  1.000 42.20798  ?  1586 PRO   A CB  1 
ATOM   12613 C  CG  . PRO   A 1 1588 ? -10.16100  46.51100  -5.65500  1.000 59.97685  ?  1586 PRO   A CG  1 
ATOM   12614 C  CD  . PRO   A 1 1588 ? -11.26800  46.08100  -6.56100  1.000 64.78310  ?  1586 PRO   A CD  1 
ATOM   12615 N  N   . HIS   A 1 1589 ? -13.75500  48.17800  -3.24800  1.000 48.89622  ?  1587 HIS   A N   1 
ATOM   12616 C  CA  . HIS   A 1 1589 ? -14.81200  49.16900  -3.14100  1.000 49.87164  ?  1587 HIS   A CA  1 
ATOM   12617 C  C   . HIS   A 1 1589 ? -14.57300  50.06800  -1.93900  1.000 63.86583  ?  1587 HIS   A C   1 
ATOM   12618 O  O   . HIS   A 1 1589 ? -14.05600  49.61400  -0.91100  1.000 61.45175  ?  1587 HIS   A O   1 
ATOM   12619 C  CB  . HIS   A 1 1589 ? -16.19300  48.50900  -3.02000  1.000 60.03237  ?  1587 HIS   A CB  1 
ATOM   12620 C  CG  . HIS   A 1 1589 ? -17.32400  49.41900  -3.37900  1.000 65.00252  ?  1587 HIS   A CG  1 
ATOM   12621 N  ND1 . HIS   A 1 1589 ? -17.94900  50.22900  -2.45500  1.000 55.37012  ?  1587 HIS   A ND1 1 
ATOM   12622 C  CD2 . HIS   A 1 1589 ? -17.93100  49.66200  -4.56500  1.000 61.77738  ?  1587 HIS   A CD2 1 
ATOM   12623 C  CE1 . HIS   A 1 1589 ? -18.89900  50.92400  -3.05400  1.000 66.77248  ?  1587 HIS   A CE1 1 
ATOM   12624 N  NE2 . HIS   A 1 1589 ? -18.90900  50.59900  -4.33500  1.000 63.86557  ?  1587 HIS   A NE2 1 
ATOM   12625 N  N   . PRO   A 1 1590 ? -14.93500  51.35100  -2.04400  1.000 65.24606  ?  1588 PRO   A N   1 
ATOM   12626 C  CA  . PRO   A 1 1590 ? -14.78500  52.25200  -0.89000  1.000 51.57238  ?  1588 PRO   A CA  1 
ATOM   12627 C  C   . PRO   A 1 1590 ? -15.56500  51.80900  0.33100   1.000 59.05698  ?  1588 PRO   A C   1 
ATOM   12628 O  O   . PRO   A 1 1590 ? -15.18500  52.16000  1.45600   1.000 58.77606  ?  1588 PRO   A O   1 
ATOM   12629 C  CB  . PRO   A 1 1590 ? -15.30300  53.59300  -1.42800  1.000 41.24977  ?  1588 PRO   A CB  1 
ATOM   12630 C  CG  . PRO   A 1 1590 ? -15.09800  53.51300  -2.89800  1.000 53.02004  ?  1588 PRO   A CG  1 
ATOM   12631 C  CD  . PRO   A 1 1590 ? -15.31400  52.07500  -3.27000  1.000 62.54464  ?  1588 PRO   A CD  1 
ATOM   12632 N  N   . LEU   A 1 1591 ? -16.65300  51.05700  0.14700   1.000 58.37313  ?  1589 LEU   A N   1 
ATOM   12633 C  CA  . LEU   A 1 1591 ? -17.41200  50.56300  1.29300   1.000 60.32442  ?  1589 LEU   A CA  1 
ATOM   12634 C  C   . LEU   A 1 1591 ? -16.55200  49.66600  2.17400   1.000 66.13535  ?  1589 LEU   A C   1 
ATOM   12635 O  O   . LEU   A 1 1591 ? -16.64800  49.71500  3.40700   1.000 59.04566  ?  1589 LEU   A O   1 
ATOM   12636 C  CB  . LEU   A 1 1591 ? -18.65500  49.81600  0.81300   1.000 59.92618  ?  1589 LEU   A CB  1 
ATOM   12637 C  CG  . LEU   A 1 1591 ? -19.89800  50.67000  0.56200   1.000 52.72453  ?  1589 LEU   A CG  1 
ATOM   12638 C  CD1 . LEU   A 1 1591 ? -20.87600  49.93400  -0.34000  1.000 42.98581  ?  1589 LEU   A CD1 1 
ATOM   12639 C  CD2 . LEU   A 1 1591 ? -20.55600  51.05200  1.87800   1.000 50.56639  ?  1589 LEU   A CD2 1 
ATOM   12640 N  N   . GLU   A 1 1592 ? -15.70500  48.84000  1.56100   1.000 76.65428  ?  1590 GLU   A N   1 
ATOM   12641 C  CA  . GLU   A 1 1592 ? -14.77100  47.99000  2.28400   1.000 75.54885  ?  1590 GLU   A CA  1 
ATOM   12642 C  C   . GLU   A 1 1592 ? -13.39100  48.62000  2.40900   1.000 77.07950  ?  1590 GLU   A C   1 
ATOM   12643 O  O   . GLU   A 1 1592 ? -12.45500  47.95300  2.86300   1.000 86.84632  ?  1590 GLU   A O   1 
ATOM   12644 C  CB  . GLU   A 1 1592 ? -14.66500  46.62300  1.60400   1.000 58.38694  ?  1590 GLU   A CB  1 
ATOM   12645 C  CG  . GLU   A 1 1592 ? -15.85000  45.71500  1.86600   1.000 52.27820  ?  1590 GLU   A CG  1 
ATOM   12646 C  CD  . GLU   A 1 1592 ? -15.92700  45.25600  3.31100   1.000 62.87413  ?  1590 GLU   A CD  1 
ATOM   12647 O  OE1 . GLU   A 1 1592 ? -15.07700  44.44100  3.72800   1.000 73.19203  ?  1590 GLU   A OE1 1 
ATOM   12648 O  OE2 . GLU   A 1 1592 ? -16.84200  45.71000  4.03100   1.000 65.42154  -1 1590 GLU   A OE2 1 
ATOM   12649 N  N   . LYS   A 1 1593 ? -13.24900  49.88700  2.01200   1.000 68.45574  ?  1591 LYS   A N   1 
ATOM   12650 C  CA  . LYS   A 1 1593 ? -12.00300  50.64100  2.13800   1.000 66.23321  ?  1591 LYS   A CA  1 
ATOM   12651 C  C   . LYS   A 1 1593 ? -10.86000  49.93500  1.40600   1.000 72.08201  ?  1591 LYS   A C   1 
ATOM   12652 O  O   . LYS   A 1 1593 ? -9.84100   49.56300  1.99000   1.000 91.63900  ?  1591 LYS   A O   1 
ATOM   12653 C  CB  . LYS   A 1 1593 ? -11.65800  50.88000  3.61300   1.000 66.24671  ?  1591 LYS   A CB  1 
ATOM   12654 C  CG  . LYS   A 1 1593 ? -12.79800  51.47800  4.42200   1.000 69.12540  ?  1591 LYS   A CG  1 
ATOM   12655 C  CD  . LYS   A 1 1593 ? -12.32500  51.97600  5.77600   1.000 62.53173  ?  1591 LYS   A CD  1 
ATOM   12656 C  CE  . LYS   A 1 1593 ? -13.42100  52.75700  6.48200   1.000 71.91713  ?  1591 LYS   A CE  1 
ATOM   12657 N  NZ  . LYS   A 1 1593 ? -14.70500  52.00200  6.52500   1.000 88.20285  ?  1591 LYS   A NZ  1 
ATOM   12658 N  N   . GLY   A 1 1594 ? -11.05300  49.75500  0.09900   1.000 66.87283  ?  1592 GLY   A N   1 
ATOM   12659 C  CA  . GLY   A 1 1594 ? -10.10100  49.04500  -0.72500  1.000 75.09008  ?  1592 GLY   A CA  1 
ATOM   12660 C  C   . GLY   A 1 1594 ? -10.21700  47.53700  -0.69000  1.000 79.09737  ?  1592 GLY   A C   1 
ATOM   12661 O  O   . GLY   A 1 1594 ? -9.74200   46.87500  -1.62000  1.000 76.49238  ?  1592 GLY   A O   1 
ATOM   12662 N  N   . GLU   A 1 1595 ? -10.82300  46.96800  0.35000   1.000 74.81095  ?  1593 GLU   A N   1 
ATOM   12663 C  CA  . GLU   A 1 1595 ? -11.04100  45.53100  0.39200   1.000 82.22946  ?  1593 GLU   A CA  1 
ATOM   12664 C  C   . GLU   A 1 1595 ? -12.07200  45.12100  -0.65700  1.000 80.81069  ?  1593 GLU   A C   1 
ATOM   12665 O  O   . GLU   A 1 1595 ? -12.90600  45.91700  -1.09800  1.000 80.91301  ?  1593 GLU   A O   1 
ATOM   12666 C  CB  . GLU   A 1 1595 ? -11.49500  45.09100  1.78500   1.000 89.25367  ?  1593 GLU   A CB  1 
ATOM   12667 C  CG  . GLU   A 1 1595 ? -10.44500  45.27800  2.86800   1.000 83.20960  ?  1593 GLU   A CG  1 
ATOM   12668 C  CD  . GLU   A 1 1595 ? -9.13200   44.60600  2.52200   1.000 86.97520  ?  1593 GLU   A CD  1 
ATOM   12669 O  OE1 . GLU   A 1 1595 ? -9.10800   43.36200  2.41200   1.000 90.81533  ?  1593 GLU   A OE1 1 
ATOM   12670 O  OE2 . GLU   A 1 1595 ? -8.12400   45.32400  2.35500   1.000 106.85511 -1 1593 GLU   A OE2 1 
ATOM   12671 N  N   . ARG   A 1 1596 ? -12.00600  43.85600  -1.05500  1.000 78.01398  ?  1594 ARG   A N   1 
ATOM   12672 C  CA  . ARG   A 1 1596 ? -12.78500  43.38800  -2.18800  1.000 70.23797  ?  1594 ARG   A CA  1 
ATOM   12673 C  C   . ARG   A 1 1596 ? -14.24500  43.16700  -1.80900  1.000 58.46684  ?  1594 ARG   A C   1 
ATOM   12674 O  O   . ARG   A 1 1596 ? -14.60300  43.00700  -0.63800  1.000 57.40722  ?  1594 ARG   A O   1 
ATOM   12675 C  CB  . ARG   A 1 1596 ? -12.20300  42.08900  -2.74000  1.000 68.61668  ?  1594 ARG   A CB  1 
ATOM   12676 C  CG  . ARG   A 1 1596 ? -10.86800  42.23600  -3.44100  1.000 73.57873  ?  1594 ARG   A CG  1 
ATOM   12677 C  CD  . ARG   A 1 1596 ? -10.37500  40.87300  -3.86600  1.000 64.85112  ?  1594 ARG   A CD  1 
ATOM   12678 N  NE  . ARG   A 1 1596 ? -10.59100  39.90100  -2.80300  1.000 66.87984  ?  1594 ARG   A NE  1 
ATOM   12679 C  CZ  . ARG   A 1 1596 ? -10.70800  38.59400  -2.99200  1.000 61.67874  ?  1594 ARG   A CZ  1 
ATOM   12680 N  NH1 . ARG   A 1 1596 ? -10.63100  38.06100  -4.20100  1.000 62.17194  ?  1594 ARG   A NH1 1 
ATOM   12681 N  NH2 . ARG   A 1 1596 ? -10.91600  37.80300  -1.94300  1.000 48.65130  ?  1594 ARG   A NH2 1 
ATOM   12682 N  N   . ILE   A 1 1597 ? -15.09200  43.16400  -2.83400  1.000 45.18647  ?  1595 ILE   A N   1 
ATOM   12683 C  CA  . ILE   A 1 1597 ? -16.49000  42.77500  -2.71800  1.000 54.54518  ?  1595 ILE   A CA  1 
ATOM   12684 C  C   . ILE   A 1 1597 ? -16.81000  41.87200  -3.90100  1.000 54.09989  ?  1595 ILE   A C   1 
ATOM   12685 O  O   . ILE   A 1 1597 ? -16.31800  42.09500  -5.01300  1.000 42.86328  ?  1595 ILE   A O   1 
ATOM   12686 C  CB  . ILE   A 1 1597 ? -17.43500  43.99800  -2.68200  1.000 55.82222  ?  1595 ILE   A CB  1 
ATOM   12687 C  CG1 . ILE   A 1 1597 ? -17.19800  44.90300  -3.89300  1.000 45.61420  ?  1595 ILE   A CG1 1 
ATOM   12688 C  CG2 . ILE   A 1 1597 ? -17.26200  44.77900  -1.38300  1.000 43.47689  ?  1595 ILE   A CG2 1 
ATOM   12689 C  CD1 . ILE   A 1 1597 ? -18.45900  45.52800  -4.44300  1.000 48.96039  ?  1595 ILE   A CD1 1 
ATOM   12690 N  N   . TYR   A 1 1598 ? -17.61400  40.83900  -3.66300  1.000 44.40642  ?  1596 TYR   A N   1 
ATOM   12691 C  CA  . TYR   A 1 1598 ? -18.03700  39.93500  -4.72500  1.000 40.00145  ?  1596 TYR   A CA  1 
ATOM   12692 C  C   . TYR   A 1 1598 ? -19.40600  40.37200  -5.22900  1.000 45.84750  ?  1596 TYR   A C   1 
ATOM   12693 O  O   . TYR   A 1 1598 ? -20.36200  40.45400  -4.45000  1.000 46.15170  ?  1596 TYR   A O   1 
ATOM   12694 C  CB  . TYR   A 1 1598 ? -18.08100  38.48100  -4.25400  1.000 40.78207  ?  1596 TYR   A CB  1 
ATOM   12695 C  CG  . TYR   A 1 1598 ? -18.76800  37.58300  -5.26200  1.000 39.13739  ?  1596 TYR   A CG  1 
ATOM   12696 C  CD1 . TYR   A 1 1598 ? -18.21900  37.37500  -6.52200  1.000 37.26415  ?  1596 TYR   A CD1 1 
ATOM   12697 C  CD2 . TYR   A 1 1598 ? -19.98300  36.97400  -4.97000  1.000 38.63576  ?  1596 TYR   A CD2 1 
ATOM   12698 C  CE1 . TYR   A 1 1598 ? -18.85100  36.57200  -7.45700  1.000 40.73301  ?  1596 TYR   A CE1 1 
ATOM   12699 C  CE2 . TYR   A 1 1598 ? -20.62300  36.16900  -5.89800  1.000 42.76964  ?  1596 TYR   A CE2 1 
ATOM   12700 C  CZ  . TYR   A 1 1598 ? -20.05200  35.97100  -7.14000  1.000 44.81352  ?  1596 TYR   A CZ  1 
ATOM   12701 O  OH  . TYR   A 1 1598 ? -20.68800  35.17100  -8.06600  1.000 58.33001  ?  1596 TYR   A OH  1 
ATOM   12702 N  N   . ARG   A 1 1599 ? -19.49800  40.64800  -6.52800  1.000 49.53622  ?  1597 ARG   A N   1 
ATOM   12703 C  CA  . ARG   A 1 1599 ? -20.75200  41.04500  -7.16000  1.000 41.37625  ?  1597 ARG   A CA  1 
ATOM   12704 C  C   . ARG   A 1 1599 ? -21.52900  39.78900  -7.53100  1.000 44.12783  ?  1597 ARG   A C   1 
ATOM   12705 O  O   . ARG   A 1 1599 ? -21.17600  39.08800  -8.48600  1.000 50.00280  ?  1597 ARG   A O   1 
ATOM   12706 C  CB  . ARG   A 1 1599 ? -20.48300  41.91900  -8.38100  1.000 59.13360  ?  1597 ARG   A CB  1 
ATOM   12707 C  CG  . ARG   A 1 1599 ? -20.13200  43.34400  -8.00900  1.000 62.63380  ?  1597 ARG   A CG  1 
ATOM   12708 C  CD  . ARG   A 1 1599 ? -18.90100  43.84000  -8.73900  1.000 55.42539  ?  1597 ARG   A CD  1 
ATOM   12709 N  NE  . ARG   A 1 1599 ? -18.47100  45.13000  -8.21500  1.000 64.10380  ?  1597 ARG   A NE  1 
ATOM   12710 C  CZ  . ARG   A 1 1599 ? -19.05000  46.28700  -8.51000  1.000 71.82176  ?  1597 ARG   A CZ  1 
ATOM   12711 N  NH1 . ARG   A 1 1599 ? -20.08300  46.35300  -9.33600  1.000 51.17810  ?  1597 ARG   A NH1 1 
ATOM   12712 N  NH2 . ARG   A 1 1599 ? -18.58200  47.40500  -7.96100  1.000 62.75800  ?  1597 ARG   A NH2 1 
ATOM   12713 N  N   . THR   A 1 1600 ? -22.59700  39.51200  -6.77600  1.000 40.25915  ?  1598 THR   A N   1 
ATOM   12714 C  CA  . THR   A 1 1600 ? -23.33400  38.26500  -6.94800  1.000 33.61468  ?  1598 THR   A CA  1 
ATOM   12715 C  C   . THR   A 1 1600 ? -24.09800  38.22200  -8.26300  1.000 39.51478  ?  1598 THR   A C   1 
ATOM   12716 O  O   . THR   A 1 1600 ? -24.36200  37.13500  -8.78800  1.000 55.18408  ?  1598 THR   A O   1 
ATOM   12717 C  CB  . THR   A 1 1600 ? -24.30900  38.06500  -5.78800  1.000 46.28237  ?  1598 THR   A CB  1 
ATOM   12718 O  OG1 . THR   A 1 1600 ? -25.39800  38.98900  -5.91100  1.000 40.03762  ?  1598 THR   A OG1 1 
ATOM   12719 C  CG2 . THR   A 1 1600 ? -23.61100  38.29600  -4.46300  1.000 41.63339  ?  1598 THR   A CG2 1 
ATOM   12720 N  N   . GLY   A 1 1601 ? -24.46300  39.37800  -8.81000  1.000 43.30358  ?  1599 GLY   A N   1 
ATOM   12721 C  CA  . GLY   A 1 1601 ? -25.36200  39.37600  -9.94400  1.000 41.42775  ?  1599 GLY   A CA  1 
ATOM   12722 C  C   . GLY   A 1 1601 ? -26.80500  39.11900  -9.58700  1.000 50.02787  ?  1599 GLY   A C   1 
ATOM   12723 O  O   . GLY   A 1 1601 ? -27.62000  38.88500  -10.48400 1.000 56.24231  ?  1599 GLY   A O   1 
ATOM   12724 N  N   . ASP   A 1 1602 ? -27.14200  39.14700  -8.30100  1.000 45.63775  ?  1600 ASP   A N   1 
ATOM   12725 C  CA  . ASP   A 1 1602 ? -28.50800  38.96700  -7.83400  1.000 54.30726  ?  1600 ASP   A CA  1 
ATOM   12726 C  C   . ASP   A 1 1602 ? -29.11400  40.31700  -7.47600  1.000 57.12626  ?  1600 ASP   A C   1 
ATOM   12727 O  O   . ASP   A 1 1602 ? -28.45600  41.16300  -6.86200  1.000 50.37914  ?  1600 ASP   A O   1 
ATOM   12728 C  CB  . ASP   A 1 1602 ? -28.56000  38.04600  -6.61200  1.000 60.11642  ?  1600 ASP   A CB  1 
ATOM   12729 C  CG  . ASP   A 1 1602 ? -28.00300  36.66400  -6.89300  1.000 56.09200  ?  1600 ASP   A CG  1 
ATOM   12730 O  OD1 . ASP   A 1 1602 ? -28.10100  36.20000  -8.04800  1.000 58.89128  ?  1600 ASP   A OD1 1 
ATOM   12731 O  OD2 . ASP   A 1 1602 ? -27.47800  36.03700  -5.94800  1.000 50.82736  -1 1600 ASP   A OD2 1 
ATOM   12732 N  N   . LEU   A 1 1603 ? -30.37100  40.51300  -7.86200  1.000 53.74946  ?  1601 LEU   A N   1 
ATOM   12733 C  CA  . LEU   A 1 1603 ? -31.10200  41.71100  -7.47800  1.000 47.16787  ?  1601 LEU   A CA  1 
ATOM   12734 C  C   . LEU   A 1 1603 ? -31.69800  41.52000  -6.09000  1.000 51.80952  ?  1601 LEU   A C   1 
ATOM   12735 O  O   . LEU   A 1 1603 ? -32.28100  40.47200  -5.79500  1.000 55.12844  ?  1601 LEU   A O   1 
ATOM   12736 C  CB  . LEU   A 1 1603 ? -32.20000  42.01500  -8.49500  1.000 56.56361  ?  1601 LEU   A CB  1 
ATOM   12737 C  CG  . LEU   A 1 1603 ? -32.92100  43.35300  -8.33000  1.000 58.53048  ?  1601 LEU   A CG  1 
ATOM   12738 C  CD1 . LEU   A 1 1603 ? -31.98900  44.50200  -8.67500  1.000 42.83474  ?  1601 LEU   A CD1 1 
ATOM   12739 C  CD2 . LEU   A 1 1603 ? -34.17700  43.39100  -9.18800  1.000 48.33845  ?  1601 LEU   A CD2 1 
ATOM   12740 N  N   . ALA   A 1 1604 ? -31.55400  42.53200  -5.23800  1.000 50.52427  ?  1602 ALA   A N   1 
ATOM   12741 C  CA  . ALA   A 1 1604 ? -32.00500  42.42600  -3.85900  1.000 49.91833  ?  1602 ALA   A CA  1 
ATOM   12742 C  C   . ALA   A 1 1604 ? -32.39800  43.80600  -3.34600  1.000 49.09833  ?  1602 ALA   A C   1 
ATOM   12743 O  O   . ALA   A 1 1604 ? -32.09200  44.83300  -3.95800  1.000 45.95802  ?  1602 ALA   A O   1 
ATOM   12744 C  CB  . ALA   A 1 1604 ? -30.92600  41.79400  -2.97300  1.000 42.74737  ?  1602 ALA   A CB  1 
ATOM   12745 N  N   . ARG   A 1 1605 ? -33.09100  43.81600  -2.20900  1.000 46.04803  ?  1603 ARG   A N   1 
ATOM   12746 C  CA  . ARG   A 1 1605 ? -33.53700  45.04900  -1.57800  1.000 55.67342  ?  1603 ARG   A CA  1 
ATOM   12747 C  C   . ARG   A 1 1605 ? -33.41300  44.90800  -0.06900  1.000 50.34201  ?  1603 ARG   A C   1 
ATOM   12748 O  O   . ARG   A 1 1605 ? -33.60900  43.82000  0.47900   1.000 42.81497  ?  1603 ARG   A O   1 
ATOM   12749 C  CB  . ARG   A 1 1605 ? -34.98900  45.38800  -1.96400  1.000 47.27844  ?  1603 ARG   A CB  1 
ATOM   12750 C  CG  . ARG   A 1 1605 ? -36.02800  44.44900  -1.36600  1.000 55.03760  ?  1603 ARG   A CG  1 
ATOM   12751 C  CD  . ARG   A 1 1605 ? -37.39200  44.59600  -2.02600  1.000 65.53398  ?  1603 ARG   A CD  1 
ATOM   12752 N  NE  . ARG   A 1 1605 ? -38.10300  45.78700  -1.57900  1.000 59.81249  ?  1603 ARG   A NE  1 
ATOM   12753 C  CZ  . ARG   A 1 1605 ? -39.36300  46.06300  -1.88800  1.000 75.03485  ?  1603 ARG   A CZ  1 
ATOM   12754 N  NH1 . ARG   A 1 1605 ? -40.08300  45.25000  -2.64500  1.000 72.92924  ?  1603 ARG   A NH1 1 
ATOM   12755 N  NH2 . ARG   A 1 1605 ? -39.91700  47.18000  -1.42100  1.000 76.32648  ?  1603 ARG   A NH2 1 
ATOM   12756 N  N   . TYR   A 1 1606 ? -33.05900  46.00500  0.59400   1.000 53.86224  ?  1604 TYR   A N   1 
ATOM   12757 C  CA  . TYR   A 1 1606 ? -33.10600  46.03100  2.04500   1.000 48.82543  ?  1604 TYR   A CA  1 
ATOM   12758 C  C   . TYR   A 1 1606 ? -34.54900  46.17300  2.51900   1.000 56.36916  ?  1604 TYR   A C   1 
ATOM   12759 O  O   . TYR   A 1 1606 ? -35.42200  46.67700  1.80700   1.000 58.44367  ?  1604 TYR   A O   1 
ATOM   12760 C  CB  . TYR   A 1 1606 ? -32.26400  47.17700  2.60800   1.000 49.88879  ?  1604 TYR   A CB  1 
ATOM   12761 C  CG  . TYR   A 1 1606 ? -30.77000  46.99600  2.46200   1.000 53.23425  ?  1604 TYR   A CG  1 
ATOM   12762 C  CD1 . TYR   A 1 1606 ? -30.09500  46.00200  3.16100   1.000 49.23957  ?  1604 TYR   A CD1 1 
ATOM   12763 C  CD2 . TYR   A 1 1606 ? -30.03200  47.83000  1.63400   1.000 54.54241  ?  1604 TYR   A CD2 1 
ATOM   12764 C  CE1 . TYR   A 1 1606 ? -28.72600  45.84100  3.03100   1.000 35.49415  ?  1604 TYR   A CE1 1 
ATOM   12765 C  CE2 . TYR   A 1 1606 ? -28.66800  47.67700  1.49700   1.000 47.43973  ?  1604 TYR   A CE2 1 
ATOM   12766 C  CZ  . TYR   A 1 1606 ? -28.01900  46.68300  2.19500   1.000 39.96926  ?  1604 TYR   A CZ  1 
ATOM   12767 O  OH  . TYR   A 1 1606 ? -26.65800  46.54300  2.04800   1.000 43.36981  ?  1604 TYR   A OH  1 
ATOM   12768 N  N   . ARG   A 1 1607 ? -34.78800  45.71900  3.74200   1.000 59.67442  ?  1605 ARG   A N   1 
ATOM   12769 C  CA  . ARG   A 1 1607 ? -36.10200  45.77200  4.36000   1.000 67.54364  ?  1605 ARG   A CA  1 
ATOM   12770 C  C   . ARG   A 1 1607 ? -36.00200  46.56300  5.65600   1.000 67.62176  ?  1605 ARG   A C   1 
ATOM   12771 O  O   . ARG   A 1 1607 ? -34.93000  46.64700  6.26400   1.000 64.47480  ?  1605 ARG   A O   1 
ATOM   12772 C  CB  . ARG   A 1 1607 ? -36.63500  44.35500  4.61600   1.000 63.43553  ?  1605 ARG   A CB  1 
ATOM   12773 C  CG  . ARG   A 1 1607 ? -38.13200  44.23300  4.79700   1.000 77.17402  ?  1605 ARG   A CG  1 
ATOM   12774 C  CD  . ARG   A 1 1607 ? -38.51700  42.76600  4.87300   1.000 67.55137  ?  1605 ARG   A CD  1 
ATOM   12775 N  NE  . ARG   A 1 1607 ? -38.29300  42.21400  6.20300   1.000 77.94335  ?  1605 ARG   A NE  1 
ATOM   12776 C  CZ  . ARG   A 1 1607 ? -38.83200  41.08800  6.64900   1.000 76.19140  ?  1605 ARG   A CZ  1 
ATOM   12777 N  NH1 . ARG   A 1 1607 ? -39.62300  40.35000  5.88600   1.000 66.40254  ?  1605 ARG   A NH1 1 
ATOM   12778 N  NH2 . ARG   A 1 1607 ? -38.56400  40.68800  7.88800   1.000 63.98269  ?  1605 ARG   A NH2 1 
ATOM   12779 N  N   . GLU   A 1 1608 ? -37.12500  47.16700  6.06100   1.000 66.87248  ?  1606 GLU   A N   1 
ATOM   12780 C  CA  . GLU   A 1 1608 ? -37.13300  47.97600  7.27600   1.000 66.58096  ?  1606 GLU   A CA  1 
ATOM   12781 C  C   . GLU   A 1 1608 ? -36.61100  47.18900  8.46900   1.000 83.28648  ?  1606 GLU   A C   1 
ATOM   12782 O  O   . GLU   A 1 1608 ? -35.94900  47.75400  9.34800   1.000 78.12646  ?  1606 GLU   A O   1 
ATOM   12783 C  CB  . GLU   A 1 1608 ? -38.54500  48.49600  7.55500   1.000 71.01301  ?  1606 GLU   A CB  1 
ATOM   12784 C  CG  . GLU   A 1 1608 ? -38.58600  49.77900  8.37700   1.000 85.30787  ?  1606 GLU   A CG  1 
ATOM   12785 C  CD  . GLU   A 1 1608 ? -39.63500  50.76000  7.87800   1.000 99.62279  ?  1606 GLU   A CD  1 
ATOM   12786 O  OE1 . GLU   A 1 1608 ? -40.38900  50.40500  6.94700   1.000 95.35968  ?  1606 GLU   A OE1 1 
ATOM   12787 O  OE2 . GLU   A 1 1608 ? -39.70500  51.88800  8.41300   1.000 81.24255  -1 1606 GLU   A OE2 1 
ATOM   12788 N  N   . ASP   A 1 1609 ? -36.88600  45.88200  8.50500   1.000 79.78034  ?  1607 ASP   A N   1 
ATOM   12789 C  CA  . ASP   A 1 1609 ? -36.31100  45.02200  9.53400   1.000 74.67428  ?  1607 ASP   A CA  1 
ATOM   12790 C  C   . ASP   A 1 1609 ? -34.79300  44.97800  9.43000   1.000 72.96805  ?  1607 ASP   A C   1 
ATOM   12791 O  O   . ASP   A 1 1609 ? -34.09200  44.92900  10.44800  1.000 70.77412  ?  1607 ASP   A O   1 
ATOM   12792 C  CB  . ASP   A 1 1609 ? -36.89300  43.61300  9.41500   1.000 74.96460  ?  1607 ASP   A CB  1 
ATOM   12793 C  CG  . ASP   A 1 1609 ? -37.33000  43.04700  10.74900  1.000 99.66564  ?  1607 ASP   A CG  1 
ATOM   12794 O  OD1 . ASP   A 1 1609 ? -36.79400  43.48800  11.78700  1.000 108.25634 ?  1607 ASP   A OD1 1 
ATOM   12795 O  OD2 . ASP   A 1 1609 ? -38.20800  42.15800  10.75900  1.000 96.93472  -1 1607 ASP   A OD2 1 
ATOM   12796 N  N   . GLY   A 1 1610 ? -34.26900  45.01000  8.21000   1.000 74.57483  ?  1608 GLY   A N   1 
ATOM   12797 C  CA  . GLY   A 1 1610 ? -32.86000  44.79700  7.95500   1.000 58.46966  ?  1608 GLY   A CA  1 
ATOM   12798 C  C   . GLY   A 1 1610 ? -32.56900  43.53900  7.17000   1.000 69.48043  ?  1608 GLY   A C   1 
ATOM   12799 O  O   . GLY   A 1 1610 ? -31.44700  43.38800  6.66900   1.000 64.92892  ?  1608 GLY   A O   1 
ATOM   12800 N  N   . ASN   A 1 1611 ? -33.54000  42.63800  7.03800   1.000 54.32405  ?  1609 ASN   A N   1 
ATOM   12801 C  CA  . ASN   A 1 1611 ? -33.33900  41.40400  6.29300   1.000 58.50576  ?  1609 ASN   A CA  1 
ATOM   12802 C  C   . ASN   A 1 1611 ? -33.43500  41.66600  4.79500   1.000 54.77510  ?  1609 ASN   A C   1 
ATOM   12803 O  O   . ASN   A 1 1611 ? -34.33600  42.36500  4.32700   1.000 65.38635  ?  1609 ASN   A O   1 
ATOM   12804 C  CB  . ASN   A 1 1611 ? -34.36900  40.35300  6.71000   1.000 63.63994  ?  1609 ASN   A CB  1 
ATOM   12805 C  CG  . ASN   A 1 1611 ? -34.19100  39.90000  8.14800   1.000 61.13955  ?  1609 ASN   A CG  1 
ATOM   12806 O  OD1 . ASN   A 1 1611 ? -33.21800  39.22500  8.48400   1.000 60.15788  ?  1609 ASN   A OD1 1 
ATOM   12807 N  ND2 . ASN   A 1 1611 ? -35.13400  40.27300  9.00500   1.000 77.79252  ?  1609 ASN   A ND2 1 
ATOM   12808 N  N   . ILE   A 1 1612 ? -32.50100  41.09700  4.04500   1.000 46.21834  ?  1610 ILE   A N   1 
ATOM   12809 C  CA  . ILE   A 1 1612 ? -32.44200  41.31200  2.60500   1.000 44.95651  ?  1610 ILE   A CA  1 
ATOM   12810 C  C   . ILE   A 1 1612 ? -33.45400  40.40700  1.91600   1.000 49.41442  ?  1610 ILE   A C   1 
ATOM   12811 O  O   . ILE   A 1 1612 ? -33.66700  39.26000  2.32700   1.000 49.32876  ?  1610 ILE   A O   1 
ATOM   12812 C  CB  . ILE   A 1 1612 ? -31.01300  41.06900  2.08800   1.000 33.60082  ?  1610 ILE   A CB  1 
ATOM   12813 C  CG1 . ILE   A 1 1612 ? -30.05200  42.08800  2.70200   1.000 41.40983  ?  1610 ILE   A CG1 1 
ATOM   12814 C  CG2 . ILE   A 1 1612 ? -30.96200  41.14900  0.57200   1.000 27.61194  ?  1610 ILE   A CG2 1 
ATOM   12815 C  CD1 . ILE   A 1 1612 ? -28.99000  41.47600  3.58200   1.000 58.20179  ?  1610 ILE   A CD1 1 
ATOM   12816 N  N   . GLU   A 1 1613 ? -34.09400  40.93000  0.87400   1.000 43.85743  ?  1611 GLU   A N   1 
ATOM   12817 C  CA  . GLU   A 1 1613 ? -35.05900  40.18200  0.08100   1.000 51.04670  ?  1611 GLU   A CA  1 
ATOM   12818 C  C   . GLU   A 1 1613 ? -34.45700  39.88700  -1.28500  1.000 50.51930  ?  1611 GLU   A C   1 
ATOM   12819 O  O   . GLU   A 1 1613 ? -33.90400  40.78300  -1.93000  1.000 47.00964  ?  1611 GLU   A O   1 
ATOM   12820 C  CB  . GLU   A 1 1613 ? -36.37100  40.95700  -0.06800  1.000 44.93545  ?  1611 GLU   A CB  1 
ATOM   12821 C  CG  . GLU   A 1 1613 ? -37.00300  41.37500  1.25400   1.000 52.79251  ?  1611 GLU   A CG  1 
ATOM   12822 C  CD  . GLU   A 1 1613 ? -38.48100  41.69500  1.12500   1.000 63.39172  ?  1611 GLU   A CD  1 
ATOM   12823 O  OE1 . GLU   A 1 1613 ? -38.88700  42.24400  0.07700   1.000 57.91777  ?  1611 GLU   A OE1 1 
ATOM   12824 O  OE2 . GLU   A 1 1613 ? -39.24100  41.38900  2.07000   1.000 65.64743  -1 1611 GLU   A OE2 1 
ATOM   12825 N  N   . TYR   A 1 1614 ? -34.55800  38.63200  -1.71400  1.000 48.65558  ?  1612 TYR   A N   1 
ATOM   12826 C  CA  . TYR   A 1 1614 ? -34.03300  38.21500  -3.00700  1.000 41.59019  ?  1612 TYR   A CA  1 
ATOM   12827 C  C   . TYR   A 1 1614 ? -35.02700  38.57200  -4.10400  1.000 48.67577  ?  1612 TYR   A C   1 
ATOM   12828 O  O   . TYR   A 1 1614 ? -36.21000  38.22900  -4.01600  1.000 65.25255  ?  1612 TYR   A O   1 
ATOM   12829 C  CB  . TYR   A 1 1614 ? -33.75400  36.71200  -2.99500  1.000 42.26332  ?  1612 TYR   A CB  1 
ATOM   12830 C  CG  . TYR   A 1 1614 ? -33.15700  36.16000  -4.26900  1.000 50.16595  ?  1612 TYR   A CG  1 
ATOM   12831 C  CD1 . TYR   A 1 1614 ? -31.82100  36.36900  -4.58200  1.000 44.98638  ?  1612 TYR   A CD1 1 
ATOM   12832 C  CD2 . TYR   A 1 1614 ? -33.92500  35.40800  -5.14900  1.000 53.22237  ?  1612 TYR   A CD2 1 
ATOM   12833 C  CE1 . TYR   A 1 1614 ? -31.27000  35.85700  -5.74400  1.000 59.66738  ?  1612 TYR   A CE1 1 
ATOM   12834 C  CE2 . TYR   A 1 1614 ? -33.38300  34.89000  -6.31100  1.000 49.52427  ?  1612 TYR   A CE2 1 
ATOM   12835 C  CZ  . TYR   A 1 1614 ? -32.05700  35.11800  -6.60500  1.000 58.59175  ?  1612 TYR   A CZ  1 
ATOM   12836 O  OH  . TYR   A 1 1614 ? -31.51700  34.60500  -7.76200  1.000 60.10748  ?  1612 TYR   A OH  1 
ATOM   12837 N  N   . LEU   A 1 1615 ? -34.55000  39.27000  -5.13500  1.000 46.10579  ?  1613 LEU   A N   1 
ATOM   12838 C  CA  . LEU   A 1 1615 ? -35.40300  39.70900  -6.23200  1.000 51.91937  ?  1613 LEU   A CA  1 
ATOM   12839 C  C   . LEU   A 1 1615 ? -35.03800  39.05300  -7.55800  1.000 57.22715  ?  1613 LEU   A C   1 
ATOM   12840 O  O   . LEU   A 1 1615 ? -35.59900  39.42200  -8.59500  1.000 61.31529  ?  1613 LEU   A O   1 
ATOM   12841 C  CB  . LEU   A 1 1615 ? -35.34900  41.23200  -6.36900  1.000 50.06993  ?  1613 LEU   A CB  1 
ATOM   12842 C  CG  . LEU   A 1 1615 ? -35.78900  42.04200  -5.14800  1.000 47.05158  ?  1613 LEU   A CG  1 
ATOM   12843 C  CD1 . LEU   A 1 1615 ? -35.44400  43.50800  -5.32800  1.000 49.75429  ?  1613 LEU   A CD1 1 
ATOM   12844 C  CD2 . LEU   A 1 1615 ? -37.27300  41.87500  -4.88200  1.000 37.06218  ?  1613 LEU   A CD2 1 
ATOM   12845 N  N   . GLY   A 1 1616 ? -34.11300  38.10000  -7.55500  1.000 48.12923  ?  1614 GLY   A N   1 
ATOM   12846 C  CA  . GLY   A 1 1616 ? -33.75300  37.38200  -8.76200  1.000 45.21697  ?  1614 GLY   A CA  1 
ATOM   12847 C  C   . GLY   A 1 1616 ? -32.42500  37.83900  -9.33000  1.000 60.87729  ?  1614 GLY   A C   1 
ATOM   12848 O  O   . GLY   A 1 1616 ? -31.73700  38.71400  -8.79400  1.000 66.88238  ?  1614 GLY   A O   1 
ATOM   12849 N  N   . ARG   A 1 1617 ? -32.06400  37.21100  -10.44400 1.000 56.92488  ?  1615 ARG   A N   1 
ATOM   12850 C  CA  . ARG   A 1 1617 ? -30.85400  37.58200  -11.15900 1.000 61.71526  ?  1615 ARG   A CA  1 
ATOM   12851 C  C   . ARG   A 1 1617 ? -31.01000  38.96500  -11.78100 1.000 67.73349  ?  1615 ARG   A C   1 
ATOM   12852 O  O   . ARG   A 1 1617 ? -32.11800  39.40600  -12.09800 1.000 73.99080  ?  1615 ARG   A O   1 
ATOM   12853 C  CB  . ARG   A 1 1617 ? -30.53900  36.55300  -12.24400 1.000 68.05676  ?  1615 ARG   A CB  1 
ATOM   12854 C  CG  . ARG   A 1 1617 ? -30.35500  35.14100  -11.72800 1.000 63.13087  ?  1615 ARG   A CG  1 
ATOM   12855 C  CD  . ARG   A 1 1617 ? -29.07300  35.02800  -10.92700 1.000 58.33626  ?  1615 ARG   A CD  1 
ATOM   12856 N  NE  . ARG   A 1 1617 ? -27.89700  35.26900  -11.75500 1.000 62.27911  ?  1615 ARG   A NE  1 
ATOM   12857 C  CZ  . ARG   A 1 1617 ? -26.69200  35.55200  -11.27800 1.000 65.45476  ?  1615 ARG   A CZ  1 
ATOM   12858 N  NH1 . ARG   A 1 1617 ? -26.46800  35.64600  -9.97700  1.000 48.02140  ?  1615 ARG   A NH1 1 
ATOM   12859 N  NH2 . ARG   A 1 1617 ? -25.68800  35.74800  -12.12800 1.000 54.74862  ?  1615 ARG   A NH2 1 
ATOM   12860 N  N   . MET   A 1 1618 ? -29.88100  39.65400  -11.95300 1.000 78.42793  ?  1616 MET   A N   1 
ATOM   12861 C  CA  . MET   A 1 1618 ? -29.91400  40.97200  -12.57900 1.000 71.72134  ?  1616 MET   A CA  1 
ATOM   12862 C  C   . MET   A 1 1618 ? -30.25700  40.86400  -14.05900 1.000 77.15110  ?  1616 MET   A C   1 
ATOM   12863 O  O   . MET   A 1 1618 ? -31.14500  41.56800  -14.55300 1.000 84.98615  ?  1616 MET   A O   1 
ATOM   12864 C  CB  . MET   A 1 1618 ? -28.58000  41.68400  -12.36900 1.000 74.84404  ?  1616 MET   A CB  1 
ATOM   12865 C  CG  . MET   A 1 1618 ? -28.32100  42.04500  -10.91900 1.000 54.25356  ?  1616 MET   A CG  1 
ATOM   12866 S  SD  . MET   A 1 1618 ? -27.40600  43.58500  -10.76900 1.000 71.18754  ?  1616 MET   A SD  1 
ATOM   12867 C  CE  . MET   A 1 1618 ? -26.35800  43.51400  -12.21900 1.000 68.23415  ?  1616 MET   A CE  1 
ATOM   12868 N  N   . ASP   A 1 1619 ? -29.55900  39.99500  -14.78500 1.000 81.71532  ?  1617 ASP   A N   1 
ATOM   12869 C  CA  . ASP   A 1 1619 ? -30.09600  39.50500  -16.04200 1.000 71.64587  ?  1617 ASP   A CA  1 
ATOM   12870 C  C   . ASP   A 1 1619 ? -31.31000  38.62300  -15.75500 1.000 90.17849  ?  1617 ASP   A C   1 
ATOM   12871 O  O   . ASP   A 1 1619 ? -31.58000  38.25200  -14.61100 1.000 93.32279  ?  1617 ASP   A O   1 
ATOM   12872 C  CB  . ASP   A 1 1619 ? -29.03100  38.73200  -16.82000 1.000 61.90763  ?  1617 ASP   A CB  1 
ATOM   12873 C  CG  . ASP   A 1 1619 ? -28.37700  37.64300  -15.98700 1.000 97.78965  ?  1617 ASP   A CG  1 
ATOM   12874 O  OD1 . ASP   A 1 1619 ? -28.41700  37.73900  -14.74100 1.000 98.84683  ?  1617 ASP   A OD1 1 
ATOM   12875 O  OD2 . ASP   A 1 1619 ? -27.82700  36.68800  -16.57400 1.000 96.14764  -1 1617 ASP   A OD2 1 
ATOM   12876 N  N   . HIS   A 1 1620 ? -32.05200  38.28600  -16.80700 1.000 80.02077  ?  1618 HIS   A N   1 
ATOM   12877 C  CA  . HIS   A 1 1620 ? -33.27900  37.49900  -16.66900 1.000 87.81008  ?  1618 HIS   A CA  1 
ATOM   12878 C  C   . HIS   A 1 1620 ? -34.27500  38.21200  -15.74900 1.000 88.30722  ?  1618 HIS   A C   1 
ATOM   12879 O  O   . HIS   A 1 1620 ? -34.87700  37.60900  -14.85900 1.000 87.93660  ?  1618 HIS   A O   1 
ATOM   12880 C  CB  . HIS   A 1 1620 ? -32.99100  36.07900  -16.15700 1.000 86.28288  ?  1618 HIS   A CB  1 
ATOM   12881 C  CG  . HIS   A 1 1620 ? -31.80100  35.41700  -16.78700 1.000 98.93498  ?  1618 HIS   A CG  1 
ATOM   12882 N  ND1 . HIS   A 1 1620 ? -31.28000  34.23200  -16.31200 1.000 92.81016  ?  1618 HIS   A ND1 1 
ATOM   12883 C  CD2 . HIS   A 1 1620 ? -31.04300  35.75700  -17.85700 1.000 97.87241  ?  1618 HIS   A CD2 1 
ATOM   12884 C  CE1 . HIS   A 1 1620 ? -30.24500  33.87800  -17.05300 1.000 87.02458  ?  1618 HIS   A CE1 1 
ATOM   12885 N  NE2 . HIS   A 1 1620 ? -30.08000  34.78600  -17.99700 1.000 93.29902  ?  1618 HIS   A NE2 1 
ATOM   12886 N  N   . GLN   A 1 1621 ? -34.42900  39.51700  -15.95500 1.000 83.80391  ?  1619 GLN   A N   1 
ATOM   12887 C  CA  . GLN   A 1 1621 ? -35.40800  40.32200  -15.23100 1.000 76.29130  ?  1619 GLN   A CA  1 
ATOM   12888 C  C   . GLN   A 1 1621 ? -36.57300  40.61300  -16.16600 1.000 74.42355  ?  1619 GLN   A C   1 
ATOM   12889 O  O   . GLN   A 1 1621 ? -36.37400  41.15600  -17.25700 1.000 88.63845  ?  1619 GLN   A O   1 
ATOM   12890 C  CB  . GLN   A 1 1621 ? -34.78900  41.62100  -14.71800 1.000 76.86486  ?  1619 GLN   A CB  1 
ATOM   12891 C  CG  . GLN   A 1 1621 ? -34.10800  41.50100  -13.36300 1.000 73.75697  ?  1619 GLN   A CG  1 
ATOM   12892 C  CD  . GLN   A 1 1621 ? -35.08400  41.21400  -12.24000 1.000 66.85805  ?  1619 GLN   A CD  1 
ATOM   12893 O  OE1 . GLN   A 1 1621 ? -36.22700  41.66600  -12.27000 1.000 83.14355  ?  1619 GLN   A OE1 1 
ATOM   12894 N  NE2 . GLN   A 1 1621 ? -34.63800  40.45900  -11.24200 1.000 49.23029  ?  1619 GLN   A NE2 1 
ATOM   12895 N  N   . VAL   A 1 1622 ? -37.78300  40.25900  -15.74000 1.000 85.90773  ?  1620 VAL   A N   1 
ATOM   12896 C  CA  . VAL   A 1 1622 ? -38.96900  40.33900  -16.58600 1.000 92.81609  ?  1620 VAL   A CA  1 
ATOM   12897 C  C   . VAL   A 1 1622 ? -39.72300  41.61800  -16.24300 1.000 100.75686 ?  1620 VAL   A C   1 
ATOM   12898 O  O   . VAL   A 1 1622 ? -40.02500  41.87300  -15.07000 1.000 102.10638 ?  1620 VAL   A O   1 
ATOM   12899 C  CB  . VAL   A 1 1622 ? -39.85700  39.09500  -16.40500 1.000 97.50055  ?  1620 VAL   A CB  1 
ATOM   12900 C  CG1 . VAL   A 1 1622 ? -41.31100  39.40700  -16.70400 1.000 99.21568  ?  1620 VAL   A CG1 1 
ATOM   12901 C  CG2 . VAL   A 1 1622 ? -39.36000  37.96200  -17.27900 1.000 92.77301  ?  1620 VAL   A CG2 1 
ATOM   12902 N  N   . LYS   A 1 1623 ? -40.00500  42.43300  -17.26300 1.000 96.99957  ?  1621 LYS   A N   1 
ATOM   12903 C  CA  . LYS   A 1 1623 ? -40.65400  43.73000  -17.08100 1.000 95.32722  ?  1621 LYS   A CA  1 
ATOM   12904 C  C   . LYS   A 1 1623 ? -41.71300  43.92000  -18.15900 1.000 105.31428 ?  1621 LYS   A C   1 
ATOM   12905 O  O   . LYS   A 1 1623 ? -41.40300  43.84100  -19.35100 1.000 109.74687 ?  1621 LYS   A O   1 
ATOM   12906 C  CB  . LYS   A 1 1623 ? -39.64000  44.88200  -17.13800 1.000 84.02721  ?  1621 LYS   A CB  1 
ATOM   12907 C  CG  . LYS   A 1 1623 ? -38.34700  44.64700  -16.36800 1.000 92.30004  ?  1621 LYS   A CG  1 
ATOM   12908 C  CD  . LYS   A 1 1623 ? -37.33700  45.76900  -16.60200 1.000 81.26368  ?  1621 LYS   A CD  1 
ATOM   12909 C  CE  . LYS   A 1 1623 ? -37.60400  46.97300  -15.70700 1.000 82.89129  ?  1621 LYS   A CE  1 
ATOM   12910 N  NZ  . LYS   A 1 1623 ? -36.52700  48.00300  -15.80600 1.000 80.60433  ?  1621 LYS   A NZ  1 
ATOM   12911 N  N   . ILE   A 1 1624 ? -42.95200  44.17800  -17.74400 1.000 107.09920 ?  1622 ILE   A N   1 
ATOM   12912 C  CA  . ILE   A 1 1624 ? -44.03400  44.53400  -18.65800 1.000 92.72102  ?  1622 ILE   A CA  1 
ATOM   12913 C  C   . ILE   A 1 1624 ? -44.26300  46.03300  -18.53200 1.000 88.86860  ?  1622 ILE   A C   1 
ATOM   12914 O  O   . ILE   A 1 1624 ? -44.51700  46.54200  -17.43200 1.000 86.67413  ?  1622 ILE   A O   1 
ATOM   12915 C  CB  . ILE   A 1 1624 ? -45.31600  43.72900  -18.36900 1.000 92.76459  ?  1622 ILE   A CB  1 
ATOM   12916 C  CG1 . ILE   A 1 1624 ? -45.42700  42.53300  -19.31000 1.000 98.70568  ?  1622 ILE   A CG1 1 
ATOM   12917 C  CG2 . ILE   A 1 1624 ? -46.56400  44.54600  -18.62300 1.000 85.62158  ?  1622 ILE   A CG2 1 
ATOM   12918 C  CD1 . ILE   A 1 1624 ? -44.19100  41.69200  -19.38500 1.000 90.95255  ?  1622 ILE   A CD1 1 
ATOM   12919 N  N   . ARG   A 1 1625 ? -44.12600  46.74200  -19.65400 1.000 92.77047  ?  1623 ARG   A N   1 
ATOM   12920 C  CA  . ARG   A 1 1625 ? -44.34000  48.18800  -19.71300 1.000 80.15097  ?  1623 ARG   A CA  1 
ATOM   12921 C  C   . ARG   A 1 1625 ? -43.51000  48.91700  -18.65900 1.000 86.52160  ?  1623 ARG   A C   1 
ATOM   12922 O  O   . ARG   A 1 1625 ? -43.96300  49.87800  -18.03400 1.000 94.76147  ?  1623 ARG   A O   1 
ATOM   12923 C  CB  . ARG   A 1 1625 ? -45.82600  48.52300  -19.57000 1.000 82.73705  ?  1623 ARG   A CB  1 
ATOM   12924 C  CG  . ARG   A 1 1625 ? -46.73400  47.79700  -20.56000 1.000 75.77052  ?  1623 ARG   A CG  1 
ATOM   12925 C  CD  . ARG   A 1 1625 ? -48.20000  48.11700  -20.29400 1.000 61.51043  ?  1623 ARG   A CD  1 
ATOM   12926 N  NE  . ARG   A 1 1625 ? -48.98100  46.92900  -19.96800 1.000 72.59241  ?  1623 ARG   A NE  1 
ATOM   12927 C  CZ  . ARG   A 1 1625 ? -49.89300  46.87100  -19.00500 1.000 86.23052  ?  1623 ARG   A CZ  1 
ATOM   12928 N  NH1 . ARG   A 1 1625 ? -50.15400  47.91500  -18.23500 1.000 79.34333  ?  1623 ARG   A NH1 1 
ATOM   12929 N  NH2 . ARG   A 1 1625 ? -50.55700  45.73600  -18.80900 1.000 89.67350  ?  1623 ARG   A NH2 1 
ATOM   12930 N  N   . GLY   A 1 1626 ? -42.28200  48.44400  -18.44800 1.000 81.26162  ?  1624 GLY   A N   1 
ATOM   12931 C  CA  . GLY   A 1 1626 ? -41.36900  49.06400  -17.51200 1.000 84.71152  ?  1624 GLY   A CA  1 
ATOM   12932 C  C   . GLY   A 1 1626 ? -41.50400  48.61900  -16.07100 1.000 71.29525  ?  1624 GLY   A C   1 
ATOM   12933 O  O   . GLY   A 1 1626 ? -40.62700  48.94000  -15.25900 1.000 79.68926  ?  1624 GLY   A O   1 
ATOM   12934 N  N   . TYR   A 1 1627 ? -42.56400  47.89400  -15.72400 1.000 76.61347  ?  1625 TYR   A N   1 
ATOM   12935 C  CA  . TYR   A 1 1627 ? -42.78300  47.45500  -14.35300 1.000 88.91294  ?  1625 TYR   A CA  1 
ATOM   12936 C  C   . TYR   A 1 1627 ? -42.19400  46.06900  -14.13600 1.000 87.92949  ?  1625 TYR   A C   1 
ATOM   12937 O  O   . TYR   A 1 1627 ? -42.35900  45.17600  -14.97000 1.000 92.37830  ?  1625 TYR   A O   1 
ATOM   12938 C  CB  . TYR   A 1 1627 ? -44.27500  47.42900  -14.02700 1.000 86.09459  ?  1625 TYR   A CB  1 
ATOM   12939 C  CG  . TYR   A 1 1627 ? -44.94300  48.78200  -14.01500 1.000 78.59847  ?  1625 TYR   A CG  1 
ATOM   12940 C  CD1 . TYR   A 1 1627 ? -44.86600  49.60700  -12.90200 1.000 77.36188  ?  1625 TYR   A CD1 1 
ATOM   12941 C  CD2 . TYR   A 1 1627 ? -45.66900  49.22700  -15.11200 1.000 73.68278  ?  1625 TYR   A CD2 1 
ATOM   12942 C  CE1 . TYR   A 1 1627 ? -45.48000  50.84200  -12.88400 1.000 78.45647  ?  1625 TYR   A CE1 1 
ATOM   12943 C  CE2 . TYR   A 1 1627 ? -46.28700  50.46200  -15.10400 1.000 86.65461  ?  1625 TYR   A CE2 1 
ATOM   12944 C  CZ  . TYR   A 1 1627 ? -46.19000  51.26500  -13.98600 1.000 75.04741  ?  1625 TYR   A CZ  1 
ATOM   12945 O  OH  . TYR   A 1 1627 ? -46.80000  52.49700  -13.96500 1.000 76.00943  ?  1625 TYR   A OH  1 
ATOM   12946 N  N   . ARG   A 1 1628 ? -41.52200  45.88800  -13.00200 1.000 76.69276  ?  1626 ARG   A N   1 
ATOM   12947 C  CA  . ARG   A 1 1628 ? -40.93800  44.59300  -12.68700 1.000 71.47148  ?  1626 ARG   A CA  1 
ATOM   12948 C  C   . ARG   A 1 1628 ? -42.03000  43.58800  -12.33400 1.000 90.73561  ?  1626 ARG   A C   1 
ATOM   12949 O  O   . ARG   A 1 1628 ? -42.97900  43.90100  -11.60800 1.000 83.62908  ?  1626 ARG   A O   1 
ATOM   12950 C  CB  . ARG   A 1 1628 ? -39.94500  44.72100  -11.53400 1.000 73.70093  ?  1626 ARG   A CB  1 
ATOM   12951 C  CG  . ARG   A 1 1628 ? -39.76800  43.44100  -10.74600 1.000 92.50558  ?  1626 ARG   A CG  1 
ATOM   12952 C  CD  . ARG   A 1 1628 ? -38.44800  43.41300  -9.99200  1.000 73.15310  ?  1626 ARG   A CD  1 
ATOM   12953 N  NE  . ARG   A 1 1628 ? -38.19400  42.14700  -9.30900  1.000 71.01436  ?  1626 ARG   A NE  1 
ATOM   12954 C  CZ  . ARG   A 1 1628 ? -39.01900  41.53300  -8.46700  1.000 86.71868  ?  1626 ARG   A CZ  1 
ATOM   12955 N  NH1 . ARG   A 1 1628 ? -40.18200  42.06000  -8.11400  1.000 95.88712  ?  1626 ARG   A NH1 1 
ATOM   12956 N  NH2 . ARG   A 1 1628 ? -38.65800  40.36100  -7.95400  1.000 78.94270  ?  1626 ARG   A NH2 1 
ATOM   12957 N  N   . ILE   A 1 1629 ? -41.88800  42.37200  -12.85400 1.000 92.85545  ?  1627 ILE   A N   1 
ATOM   12958 C  CA  . ILE   A 1 1629 ? -42.87500  41.30900  -12.70000 1.000 96.74159  ?  1627 ILE   A CA  1 
ATOM   12959 C  C   . ILE   A 1 1629 ? -42.28900  40.22700  -11.80400 1.000 101.67304 ?  1627 ILE   A C   1 
ATOM   12960 O  O   . ILE   A 1 1629 ? -41.26200  39.62300  -12.13900 1.000 95.83272  ?  1627 ILE   A O   1 
ATOM   12961 C  CB  . ILE   A 1 1629 ? -43.28600  40.73100  -14.06200 1.000 93.11789  ?  1627 ILE   A CB  1 
ATOM   12962 C  CG1 . ILE   A 1 1629 ? -43.28300  41.83200  -15.12500 1.000 97.49268  ?  1627 ILE   A CG1 1 
ATOM   12963 C  CG2 . ILE   A 1 1629 ? -44.62900  40.03700  -13.97800 1.000 96.47717  ?  1627 ILE   A CG2 1 
ATOM   12964 C  CD1 . ILE   A 1 1629 ? -44.46200  42.77300  -15.00900 1.000 105.13288 ?  1627 ILE   A CD1 1 
ATOM   12965 N  N   . GLU   A 1 1630 ? -42.94100  39.97700  -10.67100 1.000 106.70396 ?  1628 GLU   A N   1 
ATOM   12966 C  CA  . GLU   A 1 1630 ? -42.57400  38.88000  -9.77800  1.000 104.78109 ?  1628 GLU   A CA  1 
ATOM   12967 C  C   . GLU   A 1 1630 ? -43.52600  37.72300  -10.04900 1.000 100.82592 ?  1628 GLU   A C   1 
ATOM   12968 O  O   . GLU   A 1 1630 ? -44.67000  37.72100  -9.58700  1.000 98.17157  ?  1628 GLU   A O   1 
ATOM   12969 C  CB  . GLU   A 1 1630 ? -42.62800  39.31300  -8.32000  1.000 103.01505 ?  1628 GLU   A CB  1 
ATOM   12970 C  CG  . GLU   A 1 1630 ? -42.11000  38.27000  -7.34000  1.000 103.66494 ?  1628 GLU   A CG  1 
ATOM   12971 C  CD  . GLU   A 1 1630 ? -40.67700  38.51000  -6.91900  1.000 106.90580 ?  1628 GLU   A CD  1 
ATOM   12972 O  OE1 . GLU   A 1 1630 ? -39.75500  38.06000  -7.63500  1.000 101.77693 ?  1628 GLU   A OE1 1 
ATOM   12973 O  OE2 . GLU   A 1 1630 ? -40.47400  39.15500  -5.86800  1.000 94.69485  ?  1628 GLU   A OE2 1 
ATOM   12974 N  N   . LEU   A 1 1631 ? -43.03600  36.72800  -10.78700 1.000 91.08991  ?  1629 LEU   A N   1 
ATOM   12975 C  CA  . LEU   A 1 1631 ? -43.86600  35.60600  -11.20200 1.000 85.83196  ?  1629 LEU   A CA  1 
ATOM   12976 C  C   . LEU   A 1 1631 ? -44.37000  34.78200  -10.02300 1.000 97.24724  ?  1629 LEU   A C   1 
ATOM   12977 O  O   . LEU   A 1 1631 ? -45.32900  34.01800  -10.18000 1.000 96.12337  ?  1629 LEU   A O   1 
ATOM   12978 C  CB  . LEU   A 1 1631 ? -43.06800  34.73300  -12.16900 1.000 81.58479  ?  1629 LEU   A CB  1 
ATOM   12979 C  CG  . LEU   A 1 1631 ? -42.32700  35.55000  -13.23100 1.000 79.89893  ?  1629 LEU   A CG  1 
ATOM   12980 C  CD1 . LEU   A 1 1631 ? -40.84200  35.67800  -12.90100 1.000 78.32900  ?  1629 LEU   A CD1 1 
ATOM   12981 C  CD2 . LEU   A 1 1631 ? -42.51500  34.93600  -14.60000 1.000 96.74272  ?  1629 LEU   A CD2 1 
ATOM   12982 N  N   . ASP   A 1 1632 ? -43.75100  34.92100  -8.84800  1.000 114.44108 ?  1630 ASP   A N   1 
ATOM   12983 C  CA  . ASP   A 1 1632 ? -44.19800  34.16700  -7.68100  1.000 114.91050 ?  1630 ASP   A CA  1 
ATOM   12984 C  C   . ASP   A 1 1632 ? -45.50200  34.72500  -7.12700  1.000 105.88893 ?  1630 ASP   A C   1 
ATOM   12985 O  O   . ASP   A 1 1632 ? -46.38000  33.95900  -6.71100  1.000 113.59938 ?  1630 ASP   A O   1 
ATOM   12986 C  CB  . ASP   A 1 1632 ? -43.11600  34.17100  -6.60000  1.000 111.91297 ?  1630 ASP   A CB  1 
ATOM   12987 C  CG  . ASP   A 1 1632 ? -42.01300  33.16400  -6.87000  1.000 119.20682 ?  1630 ASP   A CG  1 
ATOM   12988 O  OD1 . ASP   A 1 1632 ? -41.79100  32.82100  -8.04900  1.000 109.19233 ?  1630 ASP   A OD1 1 
ATOM   12989 O  OD2 . ASP   A 1 1632 ? -41.36500  32.71600  -5.89900  1.000 108.55584 ?  1630 ASP   A OD2 1 
ATOM   12990 N  N   . GLU   A 1 1633 ? -45.64000  36.05600  -7.09700  1.000 94.77006  ?  1631 GLU   A N   1 
ATOM   12991 C  CA  . GLU   A 1 1633 ? -46.88700  36.66000  -6.63200  1.000 101.20169 ?  1631 GLU   A CA  1 
ATOM   12992 C  C   . GLU   A 1 1633 ? -48.08000  36.15300  -7.42800  1.000 98.93618  ?  1631 GLU   A C   1 
ATOM   12993 O  O   . GLU   A 1 1633 ? -49.13600  35.86000  -6.85500  1.000 92.84804  ?  1631 GLU   A O   1 
ATOM   12994 C  CB  . GLU   A 1 1633 ? -46.81500  38.18600  -6.71200  1.000 101.01446 ?  1631 GLU   A CB  1 
ATOM   12995 C  CG  . GLU   A 1 1633 ? -46.36700  38.87300  -5.42400  1.000 101.04101 ?  1631 GLU   A CG  1 
ATOM   12996 C  CD  . GLU   A 1 1633 ? -45.54400  40.12400  -5.67400  1.000 113.23939 ?  1631 GLU   A CD  1 
ATOM   12997 O  OE1 . GLU   A 1 1633 ? -44.34800  39.99700  -6.00000  1.000 115.62885 ?  1631 GLU   A OE1 1 
ATOM   12998 O  OE2 . GLU   A 1 1633 ? -46.10800  41.23600  -5.56800  1.000 107.04392 ?  1631 GLU   A OE2 1 
ATOM   12999 N  N   . ILE   A 1 1634 ? -47.93500  36.04300  -8.74900  1.000 93.65137  ?  1632 ILE   A N   1 
ATOM   13000 C  CA  . ILE   A 1 1634 ? -49.05000  35.59100  -9.57300  1.000 99.62983  ?  1632 ILE   A CA  1 
ATOM   13001 C  C   . ILE   A 1 1634 ? -49.28500  34.09600  -9.38300  1.000 106.02152 ?  1632 ILE   A C   1 
ATOM   13002 O  O   . ILE   A 1 1634 ? -50.43200  33.63100  -9.38000  1.000 107.98526 ?  1632 ILE   A O   1 
ATOM   13003 C  CB  . ILE   A 1 1634 ? -48.80600  35.96700  -11.04800 1.000 84.37263  ?  1632 ILE   A CB  1 
ATOM   13004 C  CG1 . ILE   A 1 1634 ? -49.20700  34.83000  -11.98700 1.000 82.89126  ?  1632 ILE   A CG1 1 
ATOM   13005 C  CG2 . ILE   A 1 1634 ? -47.35600  36.37000  -11.26900 1.000 78.43230  ?  1632 ILE   A CG2 1 
ATOM   13006 C  CD1 . ILE   A 1 1634 ? -48.88400  35.11200  -13.43200 1.000 101.94308 ?  1632 ILE   A CD1 1 
ATOM   13007 N  N   . ARG   A 1 1635 ? -48.21200  33.32000  -9.20200  1.000 109.09304 ?  1633 ARG   A N   1 
ATOM   13008 C  CA  . ARG   A 1 1635 ? -48.37300  31.89900  -8.90700  1.000 107.50618 ?  1633 ARG   A CA  1 
ATOM   13009 C  C   . ARG   A 1 1635 ? -49.07200  31.69400  -7.57000  1.000 101.89299 ?  1633 ARG   A C   1 
ATOM   13010 O  O   . ARG   A 1 1635 ? -50.01700  30.90400  -7.46400  1.000 95.45298  ?  1633 ARG   A O   1 
ATOM   13011 C  CB  . ARG   A 1 1635 ? -47.01700  31.19200  -8.90500  1.000 103.59944 ?  1633 ARG   A CB  1 
ATOM   13012 C  CG  . ARG   A 1 1635 ? -47.09200  29.78600  -8.33200  1.000 109.58121 ?  1633 ARG   A CG  1 
ATOM   13013 C  CD  . ARG   A 1 1635 ? -45.84900  28.95900  -8.60400  1.000 99.51181  ?  1633 ARG   A CD  1 
ATOM   13014 N  NE  . ARG   A 1 1635 ? -46.17200  27.53700  -8.63600  1.000 89.65501  ?  1633 ARG   A NE  1 
ATOM   13015 C  CZ  . ARG   A 1 1635 ? -46.24600  26.76100  -7.56300  1.000 102.06949 ?  1633 ARG   A CZ  1 
ATOM   13016 N  NH1 . ARG   A 1 1635 ? -46.00600  27.23300  -6.35000  1.000 89.39042  ?  1633 ARG   A NH1 1 
ATOM   13017 N  NH2 . ARG   A 1 1635 ? -46.57000  25.47900  -7.71100  1.000 89.68059  ?  1633 ARG   A NH2 1 
ATOM   13018 N  N   . SER   A 1 1636 ? -48.60700  32.39400  -6.53200  1.000 97.37940  ?  1634 SER   A N   1 
ATOM   13019 C  CA  . SER   A 1 1636 ? -49.22000  32.27000  -5.21500  1.000 92.46651  ?  1634 SER   A CA  1 
ATOM   13020 C  C   . SER   A 1 1636 ? -50.70600  32.59800  -5.26800  1.000 97.54309  ?  1634 SER   A C   1 
ATOM   13021 O  O   . SER   A 1 1636 ? -51.52200  31.91200  -4.64300  1.000 92.05983  ?  1634 SER   A O   1 
ATOM   13022 C  CB  . SER   A 1 1636 ? -48.50200  33.17600  -4.21700  1.000 86.73702  ?  1634 SER   A CB  1 
ATOM   13023 O  OG  . SER   A 1 1636 ? -49.29200  33.39200  -3.06200  1.000 97.97378  ?  1634 SER   A OG  1 
ATOM   13024 N  N   . LYS   A 1 1637 ? -51.08000  33.63200  -6.02600  1.000 107.37838 ?  1635 LYS   A N   1 
ATOM   13025 C  CA  . LYS   A 1 1637 ? -52.49000  33.98300  -6.14900  1.000 108.52549 ?  1635 LYS   A CA  1 
ATOM   13026 C  C   . LYS   A 1 1637 ? -53.24900  32.97200  -7.00100  1.000 113.91948 ?  1635 LYS   A C   1 
ATOM   13027 O  O   . LYS   A 1 1637 ? -54.46300  32.80800  -6.83300  1.000 121.23301 ?  1635 LYS   A O   1 
ATOM   13028 C  CB  . LYS   A 1 1637 ? -52.63200  35.38900  -6.73400  1.000 85.06971  ?  1635 LYS   A CB  1 
ATOM   13029 N  N   . LEU   A 1 1638 ? -52.55800  32.28600  -7.90900  1.000 92.79922  ?  1636 LEU   A N   1 
ATOM   13030 C  CA  . LEU   A 1 1638 ? -53.16800  31.28400  -8.77000  1.000 94.46785  ?  1636 LEU   A CA  1 
ATOM   13031 C  C   . LEU   A 1 1638 ? -53.14500  29.88900  -8.15300  1.000 101.73869 ?  1636 LEU   A C   1 
ATOM   13032 O  O   . LEU   A 1 1638 ? -53.38300  28.90700  -8.86100  1.000 107.50557 ?  1636 LEU   A O   1 
ATOM   13033 C  CB  . LEU   A 1 1638 ? -52.46100  31.27200  -10.13200 1.000 92.70719  ?  1636 LEU   A CB  1 
ATOM   13034 C  CG  . LEU   A 1 1638 ? -53.17100  30.68700  -11.35700 1.000 81.95735  ?  1636 LEU   A CG  1 
ATOM   13035 C  CD1 . LEU   A 1 1638 ? -54.48500  31.40400  -11.62300 1.000 94.84493  ?  1636 LEU   A CD1 1 
ATOM   13036 C  CD2 . LEU   A 1 1638 ? -52.26800  30.74900  -12.57700 1.000 81.89798  ?  1636 LEU   A CD2 1 
ATOM   13037 N  N   . ILE   A 1 1639 ? -52.87700  29.77600  -6.85300  1.000 101.44383 ?  1637 ILE   A N   1 
ATOM   13038 C  CA  . ILE   A 1 1639 ? -52.69100  28.46900  -6.23100  1.000 109.10777 ?  1637 ILE   A CA  1 
ATOM   13039 C  C   . ILE   A 1 1639 ? -53.67700  28.26100  -5.08800  1.000 111.65135 ?  1637 ILE   A C   1 
ATOM   13040 O  O   . ILE   A 1 1639 ? -54.09100  27.12800  -4.81500  1.000 119.96397 ?  1637 ILE   A O   1 
ATOM   13041 C  CB  . ILE   A 1 1639 ? -51.24300  28.29600  -5.73800  1.000 97.27784  ?  1637 ILE   A CB  1 
ATOM   13042 N  N   . GLN   A 1 1640 ? -54.06200  29.34900  -4.41400  1.000 114.98543 ?  1638 GLN   A N   1 
ATOM   13043 C  CA  . GLN   A 1 1640 ? -54.91600  29.23300  -3.23400  1.000 111.25734 ?  1638 GLN   A CA  1 
ATOM   13044 C  C   . GLN   A 1 1640 ? -56.28800  28.65200  -3.55700  1.000 114.68676 ?  1638 GLN   A C   1 
ATOM   13045 O  O   . GLN   A 1 1640 ? -56.98600  28.20200  -2.64200  1.000 89.06317  ?  1638 GLN   A O   1 
ATOM   13046 C  CB  . GLN   A 1 1640 ? -55.07600  30.59700  -2.55700  1.000 94.89487  ?  1638 GLN   A CB  1 
ATOM   13047 C  CG  . GLN   A 1 1640 ? -53.95900  31.57400  -2.86800  1.000 101.35214 ?  1638 GLN   A CG  1 
ATOM   13048 C  CD  . GLN   A 1 1640 ? -53.83400  32.68000  -1.84000  1.000 112.35783 ?  1638 GLN   A CD  1 
ATOM   13049 O  OE1 . GLN   A 1 1640 ? -54.82800  33.27400  -1.42300  1.000 115.38517 ?  1638 GLN   A OE1 1 
ATOM   13050 N  NE2 . GLN   A 1 1640 ? -52.60400  32.96400  -1.42500  1.000 94.85866  ?  1638 GLN   A NE2 1 
ATOM   13051 N  N   . GLU   A 1 1641 ? -56.69000  28.65100  -4.82500  1.000 121.14671 ?  1639 GLU   A N   1 
ATOM   13052 C  CA  . GLU   A 1 1641 ? -57.94300  28.02200  -5.21800  1.000 125.21217 ?  1639 GLU   A CA  1 
ATOM   13053 C  C   . GLU   A 1 1641 ? -57.76400  26.51100  -5.30600  1.000 132.70552 ?  1639 GLU   A C   1 
ATOM   13054 O  O   . GLU   A 1 1641 ? -56.74100  26.01800  -5.79000  1.000 134.69702 ?  1639 GLU   A O   1 
ATOM   13055 C  CB  . GLU   A 1 1641 ? -58.42800  28.58000  -6.55700  1.000 117.71660 ?  1639 GLU   A CB  1 
ATOM   13056 C  CG  . GLU   A 1 1641 ? -59.24000  29.86400  -6.43400  1.000 111.50542 ?  1639 GLU   A CG  1 
ATOM   13057 C  CD  . GLU   A 1 1641 ? -60.42000  29.72600  -5.48700  1.000 124.97392 ?  1639 GLU   A CD  1 
ATOM   13058 O  OE1 . GLU   A 1 1641 ? -61.04300  28.64300  -5.45900  1.000 119.41299 ?  1639 GLU   A OE1 1 
ATOM   13059 O  OE2 . GLU   A 1 1641 ? -60.72100  30.70000  -4.76400  1.000 120.85200 ?  1639 GLU   A OE2 1 
ATOM   13060 N  N   . GLU   A 1 1642 ? -58.77200  25.77500  -4.82700  1.000 128.70463 ?  1640 GLU   A N   1 
ATOM   13061 C  CA  . GLU   A 1 1642 ? -58.65700  24.32200  -4.74300  1.000 120.16381 ?  1640 GLU   A CA  1 
ATOM   13062 C  C   . GLU   A 1 1642 ? -58.55700  23.68600  -6.12400  1.000 121.70942 ?  1640 GLU   A C   1 
ATOM   13063 O  O   . GLU   A 1 1642 ? -57.85200  22.68600  -6.30300  1.000 126.26583 ?  1640 GLU   A O   1 
ATOM   13064 C  CB  . GLU   A 1 1642 ? -59.85100  23.74100  -3.98600  1.000 114.96622 ?  1640 GLU   A CB  1 
ATOM   13065 C  CG  . GLU   A 1 1642 ? -60.48700  24.68100  -2.98100  1.000 119.46278 ?  1640 GLU   A CG  1 
ATOM   13066 C  CD  . GLU   A 1 1642 ? -61.78100  24.12300  -2.41700  1.000 119.18862 ?  1640 GLU   A CD  1 
ATOM   13067 O  OE1 . GLU   A 1 1642 ? -62.11300  22.96000  -2.73100  1.000 97.74213  ?  1640 GLU   A OE1 1 
ATOM   13068 O  OE2 . GLU   A 1 1642 ? -62.46600  24.84600  -1.66400  1.000 119.99839 ?  1640 GLU   A OE2 1 
ATOM   13069 N  N   . THR   A 1 1643 ? -59.26200  24.25000  -7.11100  1.000 128.43066 ?  1641 THR   A N   1 
ATOM   13070 C  CA  . THR   A 1 1643 ? -59.31200  23.64300  -8.43900  1.000 125.49879 ?  1641 THR   A CA  1 
ATOM   13071 C  C   . THR   A 1 1643 ? -57.92900  23.51200  -9.06100  1.000 128.62313 ?  1641 THR   A C   1 
ATOM   13072 O  O   . THR   A 1 1643 ? -57.66400  22.54300  -9.78300  1.000 133.53593 ?  1641 THR   A O   1 
ATOM   13073 C  CB  . THR   A 1 1643 ? -60.21600  24.46000  -9.36600  1.000 119.63051 ?  1641 THR   A CB  1 
ATOM   13074 O  OG1 . THR   A 1 1643 ? -59.95900  24.08900  -10.72700 1.000 109.24534 ?  1641 THR   A OG1 1 
ATOM   13075 C  CG2 . THR   A 1 1643 ? -59.95700  25.95400  -9.19800  1.000 107.69722 ?  1641 THR   A CG2 1 
ATOM   13076 N  N   . ILE   A 1 1644 ? -57.03900  24.46400  -8.79500  1.000 129.06395 ?  1642 ILE   A N   1 
ATOM   13077 C  CA  . ILE   A 1 1644 ? -55.71300  24.49400  -9.39800  1.000 112.14187 ?  1642 ILE   A CA  1 
ATOM   13078 C  C   . ILE   A 1 1644 ? -54.68900  24.04300  -8.36700  1.000 115.50831 ?  1642 ILE   A C   1 
ATOM   13079 O  O   . ILE   A 1 1644 ? -54.63200  24.58100  -7.25200  1.000 92.55970  ?  1642 ILE   A O   1 
ATOM   13080 C  CB  . ILE   A 1 1644 ? -55.37600  25.89600  -9.93500  1.000 105.74911 ?  1642 ILE   A CB  1 
ATOM   13081 C  CG1 . ILE   A 1 1644 ? -53.86400  26.05000  -10.12200 1.000 115.22500 ?  1642 ILE   A CG1 1 
ATOM   13082 C  CG2 . ILE   A 1 1644 ? -55.93000  26.97000  -9.00900  1.000 109.73680 ?  1642 ILE   A CG2 1 
ATOM   13083 C  CD1 . ILE   A 1 1644 ? -53.47900  26.81500  -11.37100 1.000 109.55400 ?  1642 ILE   A CD1 1 
ATOM   13084 N  N   . GLN   A 1 1645 ? -53.86400  23.07200  -8.76900  1.000 124.54657 ?  1643 GLN   A N   1 
ATOM   13085 C  CA  . GLN   A 1 1645 ? -52.76200  22.59800  -7.89900  1.000 115.43682 ?  1643 GLN   A CA  1 
ATOM   13086 C  C   . GLN   A 1 1645 ? -51.45900  22.85800  -8.66400  1.000 119.16129 ?  1643 GLN   A C   1 
ATOM   13087 O  O   . GLN   A 1 1645 ? -50.42800  23.12300  -8.01100  1.000 114.65129 ?  1643 GLN   A O   1 
ATOM   13088 C  CB  . GLN   A 1 1645 ? -52.93500  21.11000  -7.60300  1.000 101.85937 ?  1643 GLN   A CB  1 
ATOM   13089 C  CG  . GLN   A 1 1645 ? -54.28900  20.74100  -7.00500  1.000 116.22560 ?  1643 GLN   A CG  1 
ATOM   13090 C  CD  . GLN   A 1 1645 ? -55.36500  20.50000  -8.04200  1.000 130.96665 ?  1643 GLN   A CD  1 
ATOM   13091 O  OE1 . GLN   A 1 1645 ? -55.08700  20.14000  -9.19100  1.000 127.47307 ?  1643 GLN   A OE1 1 
ATOM   13092 N  NE2 . GLN   A 1 1645 ? -56.61200  20.71300  -7.64800  1.000 115.93388 ?  1643 GLN   A NE2 1 
ATOM   13093 N  N   . ASP   A 1 1646 ? -51.52100  22.82000  -9.99700  1.000 117.21878 ?  1644 ASP   A N   1 
ATOM   13094 C  CA  . ASP   A 1 1646 ? -50.31200  23.00500  -10.84500 1.000 121.14526 ?  1644 ASP   A CA  1 
ATOM   13095 C  C   . ASP   A 1 1646 ? -50.25000  24.44400  -11.36100 1.000 119.47156 ?  1644 ASP   A C   1 
ATOM   13096 O  O   . ASP   A 1 1646 ? -51.18400  24.84100  -12.07200 1.000 131.93471 ?  1644 ASP   A O   1 
ATOM   13097 C  CB  . ASP   A 1 1646 ? -50.33600  22.02200  -12.00300 1.000 114.77393 ?  1644 ASP   A CB  1 
ATOM   13098 C  CG  . ASP   A 1 1646 ? -51.68200  21.88800  -12.70000 1.000 123.76600 ?  1644 ASP   A CG  1 
ATOM   13099 O  OD1 . ASP   A 1 1646 ? -52.68200  21.61600  -12.00200 1.000 118.80352 ?  1644 ASP   A OD1 1 
ATOM   13100 O  OD2 . ASP   A 1 1646 ? -51.72400  22.07700  -13.93300 1.000 117.84628 -1 1644 ASP   A OD2 1 
ATOM   13101 N  N   . ALA   A 1 1647 ? -49.17400  25.17800  -11.07100 1.000 112.01626 ?  1645 ALA   A N   1 
ATOM   13102 C  CA  . ALA   A 1 1647 ? -49.11400  26.60700  -11.46200 1.000 105.88350 ?  1645 ALA   A CA  1 
ATOM   13103 C  C   . ALA   A 1 1647 ? -47.86600  26.92200  -12.28800 1.000 113.02961 ?  1645 ALA   A C   1 
ATOM   13104 O  O   . ALA   A 1 1647 ? -46.77700  27.06200  -11.69300 1.000 113.71255 ?  1645 ALA   A O   1 
ATOM   13105 C  CB  . ALA   A 1 1647 ? -49.14700  27.45300  -10.22000 1.000 110.77964 ?  1645 ALA   A CB  1 
ATOM   13106 N  N   . VAL   A 1 1648 ? -48.02200  27.07300  -13.60600 1.000 119.14255 ?  1646 VAL   A N   1 
ATOM   13107 C  CA  . VAL   A 1 1648 ? -46.87400  27.45200  -14.48600 1.000 113.41081 ?  1646 VAL   A CA  1 
ATOM   13108 C  C   . VAL   A 1 1648 ? -46.82900  28.98200  -14.63500 1.000 125.26255 ?  1646 VAL   A C   1 
ATOM   13109 O  O   . VAL   A 1 1648 ? -47.83700  29.55000  -15.09900 1.000 133.95354 ?  1646 VAL   A O   1 
ATOM   13110 C  CB  . VAL   A 1 1648 ? -47.04800  26.78100  -15.85800 1.000 112.28172 ?  1646 VAL   A CB  1 
ATOM   13111 C  CG1 . VAL   A 1 1648 ? -45.82200  26.96800  -16.74300 1.000 84.30866  ?  1646 VAL   A CG1 1 
ATOM   13112 C  CG2 . VAL   A 1 1648 ? -47.40900  25.30700  -15.72400 1.000 101.20916 ?  1646 VAL   A CG2 1 
ATOM   13113 N  N   . VAL   A 1 1649 ? -45.71200  29.62200  -14.27700 1.000 110.74136 ?  1647 VAL   A N   1 
ATOM   13114 C  CA  . VAL   A 1 1649 ? -45.63700  31.11600  -14.32300 1.000 102.12122 ?  1647 VAL   A CA  1 
ATOM   13115 C  C   . VAL   A 1 1649 ? -44.29300  31.55100  -14.92700 1.000 97.20437  ?  1647 VAL   A C   1 
ATOM   13116 O  O   . VAL   A 1 1649 ? -43.28900  31.57500  -14.19100 1.000 102.35751 ?  1647 VAL   A O   1 
ATOM   13117 C  CB  . VAL   A 1 1649 ? -45.83300  31.68300  -12.90700 1.000 99.47263  ?  1647 VAL   A CB  1 
ATOM   13118 C  CG1 . VAL   A 1 1649 ? -47.30700  31.87000  -12.58200 1.000 88.39210  ?  1647 VAL   A CG1 1 
ATOM   13119 C  CG2 . VAL   A 1 1649 ? -45.17300  30.80000  -11.85600 1.000 101.18253 ?  1647 VAL   A CG2 1 
ATOM   13120 N  N   . VAL   A 1 1650 ? -44.27700  31.89500  -16.21200 1.000 85.08345  ?  1648 VAL   A N   1 
ATOM   13121 C  CA  . VAL   A 1 1650 ? -42.98100  32.23200  -16.86700 1.000 96.45369  ?  1648 VAL   A CA  1 
ATOM   13122 C  C   . VAL   A 1 1650 ? -43.23400  33.21000  -18.02300 1.000 108.03147 ?  1648 VAL   A C   1 
ATOM   13123 O  O   . VAL   A 1 1650 ? -44.40900  33.40700  -18.38300 1.000 115.08854 ?  1648 VAL   A O   1 
ATOM   13124 C  CB  . VAL   A 1 1650 ? -42.27700  30.94900  -17.34500 1.000 107.90304 ?  1648 VAL   A CB  1 
ATOM   13125 C  CG1 . VAL   A 1 1650 ? -42.73800  30.51600  -18.73100 1.000 108.70806 ?  1648 VAL   A CG1 1 
ATOM   13126 C  CG2 . VAL   A 1 1650 ? -40.75900  31.06900  -17.28000 1.000 98.31114  ?  1648 VAL   A CG2 1 
ATOM   13127 N  N   . ALA   A 1 1651 ? -42.17200  33.79000  -18.58100 1.000 95.58971  ?  1649 ALA   A N   1 
ATOM   13128 C  CA  . ALA   A 1 1651 ? -42.35000  34.80900  -19.63500 1.000 90.97442  ?  1649 ALA   A CA  1 
ATOM   13129 C  C   . ALA   A 1 1651 ? -41.87000  34.29700  -20.98400 1.000 103.22367 ?  1649 ALA   A C   1 
ATOM   13130 O  O   . ALA   A 1 1651 ? -40.82700  33.61800  -21.03500 1.000 104.09437 ?  1649 ALA   A O   1 
ATOM   13131 C  CB  . ALA   A 1 1651 ? -41.58700  36.04300  -19.26200 1.000 90.75436  ?  1649 ALA   A CB  1 
ATOM   13132 N  N   . ARG   A 1 1652 ? -42.61300  34.61700  -22.04000 1.000 106.33644 ?  1650 ARG   A N   1 
ATOM   13133 C  CA  . ARG   A 1 1652 ? -42.19800  34.26400  -23.39100 1.000 110.72699 ?  1650 ARG   A CA  1 
ATOM   13134 C  C   . ARG   A 1 1652 ? -42.05300  35.53200  -24.21900 1.000 115.32689 ?  1650 ARG   A C   1 
ATOM   13135 O  O   . ARG   A 1 1652 ? -42.93200  36.39900  -24.19000 1.000 126.69754 ?  1650 ARG   A O   1 
ATOM   13136 C  CB  . ARG   A 1 1652 ? -43.20500  33.31800  -24.05500 1.000 107.90427 ?  1650 ARG   A CB  1 
ATOM   13137 C  CG  . ARG   A 1 1652 ? -43.19300  33.38400  -25.57700 1.000 119.04054 ?  1650 ARG   A CG  1 
ATOM   13138 C  CD  . ARG   A 1 1652 ? -44.26500  32.50400  -26.20100 1.000 112.65608 ?  1650 ARG   A CD  1 
ATOM   13139 N  NE  . ARG   A 1 1652 ? -44.05600  31.08800  -25.92200 1.000 108.04118 ?  1650 ARG   A NE  1 
ATOM   13140 C  CZ  . ARG   A 1 1652 ? -43.11600  30.34100  -26.48400 1.000 103.97044 ?  1650 ARG   A CZ  1 
ATOM   13141 N  NH1 . ARG   A 1 1652 ? -42.26100  30.84600  -27.36000 1.000 110.27984 ?  1650 ARG   A NH1 1 
ATOM   13142 N  NH2 . ARG   A 1 1652 ? -43.03200  29.05300  -26.16200 1.000 96.95246  ?  1650 ARG   A NH2 1 
ATOM   13143 N  N   . ASN   A 1 1653 ? -40.94500  35.64000  -24.94900 1.000 115.92098 ?  1651 ASN   A N   1 
ATOM   13144 C  CA  . ASN   A 1 1653 ? -40.78000  36.73700  -25.89200 1.000 126.04842 ?  1651 ASN   A CA  1 
ATOM   13145 C  C   . ASN   A 1 1653 ? -41.66100  36.50400  -27.11400 1.000 132.19085 ?  1651 ASN   A C   1 
ATOM   13146 O  O   . ASN   A 1 1653 ? -41.61900  35.43200  -27.72600 1.000 124.27325 ?  1651 ASN   A O   1 
ATOM   13147 C  CB  . ASN   A 1 1653 ? -39.31500  36.87000  -26.30400 1.000 114.89204 ?  1651 ASN   A CB  1 
ATOM   13148 C  CG  . ASN   A 1 1653 ? -38.51800  37.72900  -25.34400 1.000 126.67228 ?  1651 ASN   A CG  1 
ATOM   13149 O  OD1 . ASN   A 1 1653 ? -38.63800  37.59400  -24.12600 1.000 126.78837 ?  1651 ASN   A OD1 1 
ATOM   13150 N  ND2 . ASN   A 1 1653 ? -37.69800  38.62100  -25.88900 1.000 128.25770 ?  1651 ASN   A ND2 1 
ATOM   13151 N  N   . ASP   A 1 1654 ? -42.46300  37.50800  -27.46700 1.000 148.02975 ?  1652 ASP   A N   1 
ATOM   13152 C  CA  . ASP   A 1 1654 ? -43.44900  37.38100  -28.53000 1.000 145.54152 ?  1652 ASP   A CA  1 
ATOM   13153 C  C   . ASP   A 1 1654 ? -43.29600  38.51200  -29.54000 1.000 152.36828 ?  1652 ASP   A C   1 
ATOM   13154 O  O   . ASP   A 1 1654 ? -42.80500  39.59800  -29.22300 1.000 160.05678 ?  1652 ASP   A O   1 
ATOM   13155 C  CB  . ASP   A 1 1654 ? -44.88300  37.36500  -27.96400 1.000 140.88756 ?  1652 ASP   A CB  1 
ATOM   13156 C  CG  . ASP   A 1 1654 ? -45.36400  38.74300  -27.52800 1.000 147.75027 ?  1652 ASP   A CG  1 
ATOM   13157 O  OD1 . ASP   A 1 1654 ? -44.55800  39.51800  -26.97100 1.000 144.17949 ?  1652 ASP   A OD1 1 
ATOM   13158 O  OD2 . ASP   A 1 1654 ? -46.55600  39.05300  -27.74300 1.000 151.80979 ?  1652 ASP   A OD2 1 
ATOM   13159 N  N   . GLN   A 1 1655 ? -43.73100  38.23300  -30.77100 1.000 148.80650 ?  1653 GLN   A N   1 
ATOM   13160 C  CA  . GLN   A 1 1655 ? -43.74400  39.20800  -31.85800 1.000 146.47574 ?  1653 GLN   A CA  1 
ATOM   13161 C  C   . GLN   A 1 1655 ? -42.38300  39.86800  -32.05400 1.000 153.18183 ?  1653 GLN   A C   1 
ATOM   13162 O  O   . GLN   A 1 1655 ? -41.39700  39.18900  -32.36000 1.000 143.25625 ?  1653 GLN   A O   1 
ATOM   13163 C  CB  . GLN   A 1 1655 ? -44.82400  40.26700  -31.60900 1.000 132.29173 ?  1653 GLN   A CB  1 
ATOM   13164 C  CG  . GLN   A 1 1655 ? -46.19000  39.69100  -31.25100 1.000 140.22354 ?  1653 GLN   A CG  1 
ATOM   13165 C  CD  . GLN   A 1 1655 ? -46.60300  38.54400  -32.15600 1.000 139.81373 ?  1653 GLN   A CD  1 
ATOM   13166 O  OE1 . GLN   A 1 1655 ? -46.74100  37.40500  -31.71000 1.000 131.60807 ?  1653 GLN   A OE1 1 
ATOM   13167 N  NE2 . GLN   A 1 1655 ? -46.80200  38.84100  -33.43400 1.000 138.24263 ?  1653 GLN   A NE2 1 
ATOM   13168 N  N   . ASN   A 1 1656 ? -42.32000  41.19100  -31.87900 1.000 160.47429 ?  1654 ASN   A N   1 
ATOM   13169 C  CA  . ASN   A 1 1656 ? -41.09300  41.96200  -32.09900 1.000 165.23109 ?  1654 ASN   A CA  1 
ATOM   13170 C  C   . ASN   A 1 1656 ? -40.17500  41.91200  -30.87400 1.000 165.65504 ?  1654 ASN   A C   1 
ATOM   13171 O  O   . ASN   A 1 1656 ? -39.83800  42.92600  -30.26200 1.000 162.61794 ?  1654 ASN   A O   1 
ATOM   13172 C  CB  . ASN   A 1 1656 ? -41.43400  43.40300  -32.45800 1.000 154.80126 ?  1654 ASN   A CB  1 
ATOM   13173 C  CG  . ASN   A 1 1656 ? -40.20600  44.21500  -32.83000 1.000 160.82242 ?  1654 ASN   A CG  1 
ATOM   13174 O  OD1 . ASN   A 1 1656 ? -39.34500  43.75300  -33.57900 1.000 172.53805 ?  1654 ASN   A OD1 1 
ATOM   13175 N  ND2 . ASN   A 1 1656 ? -40.10800  45.42100  -32.28300 1.000 154.41873 ?  1654 ASN   A ND2 1 
ATOM   13176 N  N   . GLY   A 1 1657 ? -39.77600  40.69600  -30.51000 1.000 160.62345 ?  1655 GLY   A N   1 
ATOM   13177 C  CA  . GLY   A 1 1657 ? -38.91500  40.50200  -29.35700 1.000 147.81331 ?  1655 GLY   A CA  1 
ATOM   13178 C  C   . GLY   A 1 1657 ? -39.49900  41.00100  -28.04900 1.000 148.49499 ?  1655 GLY   A C   1 
ATOM   13179 O  O   . GLY   A 1 1657 ? -38.89400  40.83100  -26.98500 1.000 151.16352 ?  1655 GLY   A O   1 
ATOM   13180 N  N   . GLN   A 1 1658 ? -40.66500  41.64200  -28.12200 1.000 145.00002 ?  1656 GLN   A N   1 
ATOM   13181 C  CA  . GLN   A 1 1658 ? -41.41200  42.01800  -26.93700 1.000 138.47633 ?  1656 GLN   A CA  1 
ATOM   13182 C  C   . GLN   A 1 1658 ? -41.76700  40.76400  -26.14600 1.000 130.78613 ?  1656 GLN   A C   1 
ATOM   13183 O  O   . GLN   A 1 1658 ? -41.81200  39.65400  -26.68000 1.000 141.50174 ?  1656 GLN   A O   1 
ATOM   13184 C  CB  . GLN   A 1 1658 ? -42.67800  42.78400  -27.33000 1.000 141.53961 ?  1656 GLN   A CB  1 
ATOM   13185 C  CG  . GLN   A 1 1658 ? -42.57500  44.30200  -27.20500 1.000 129.97879 ?  1656 GLN   A CG  1 
ATOM   13186 C  CD  . GLN   A 1 1658 ? -42.01100  44.96100  -28.45600 1.000 129.01852 ?  1656 GLN   A CD  1 
ATOM   13187 O  OE1 . GLN   A 1 1658 ? -42.61000  44.89600  -29.53100 1.000 130.67307 ?  1656 GLN   A OE1 1 
ATOM   13188 N  NE2 . GLN   A 1 1658 ? -40.85400  45.60100  -28.31900 1.000 120.79051 ?  1656 GLN   A NE2 1 
ATOM   13189 N  N   . ALA   A 1 1659 ? -42.00400  40.94100  -24.85500 1.000 118.22653 ?  1657 ALA   A N   1 
ATOM   13190 C  CA  . ALA   A 1 1659 ? -42.25300  39.81600  -23.97000 1.000 123.50818 ?  1657 ALA   A CA  1 
ATOM   13191 C  C   . ALA   A 1 1659 ? -43.69400  39.83400  -23.48700 1.000 124.43769 ?  1657 ALA   A C   1 
ATOM   13192 O  O   . ALA   A 1 1659 ? -44.36500  40.87000  -23.49800 1.000 126.33890 ?  1657 ALA   A O   1 
ATOM   13193 C  CB  . ALA   A 1 1659 ? -41.29700  39.83700  -22.77300 1.000 117.65185 ?  1657 ALA   A CB  1 
ATOM   13194 N  N   . TYR   A 1 1660 ? -44.16800  38.66400  -23.06900 1.000 115.59042 ?  1658 TYR   A N   1 
ATOM   13195 C  CA  . TYR   A 1 1660 ? -45.47900  38.57500  -22.44900 1.000 109.74090 ?  1658 TYR   A CA  1 
ATOM   13196 C  C   . TYR   A 1 1660 ? -45.55500  37.31800  -21.60000 1.000 108.86809 ?  1658 TYR   A C   1 
ATOM   13197 O  O   . TYR   A 1 1660 ? -45.06500  36.25800  -21.99800 1.000 108.61847 ?  1658 TYR   A O   1 
ATOM   13198 C  CB  . TYR   A 1 1660 ? -46.60100  38.59700  -23.48900 1.000 126.34928 ?  1658 TYR   A CB  1 
ATOM   13199 C  CG  . TYR   A 1 1660 ? -47.28700  39.93700  -23.52700 1.000 139.21413 ?  1658 TYR   A CG  1 
ATOM   13200 C  CD1 . TYR   A 1 1660 ? -48.00900  40.39200  -22.43200 1.000 128.72209 ?  1658 TYR   A CD1 1 
ATOM   13201 C  CD2 . TYR   A 1 1660 ? -47.19500  40.75900  -24.64200 1.000 141.22498 ?  1658 TYR   A CD2 1 
ATOM   13202 C  CE1 . TYR   A 1 1660 ? -48.63100  41.62000  -22.44900 1.000 130.70640 ?  1658 TYR   A CE1 1 
ATOM   13203 C  CE2 . TYR   A 1 1660 ? -47.81500  41.99200  -24.66800 1.000 140.07955 ?  1658 TYR   A CE2 1 
ATOM   13204 C  CZ  . TYR   A 1 1660 ? -48.53100  42.41600  -23.56800 1.000 138.21751 ?  1658 TYR   A CZ  1 
ATOM   13205 O  OH  . TYR   A 1 1660 ? -49.15200  43.64200  -23.58400 1.000 137.45852 ?  1658 TYR   A OH  1 
ATOM   13206 N  N   . LEU   A 1 1661 ? -46.17200  37.45700  -20.42900 1.000 107.92296 ?  1659 LEU   A N   1 
ATOM   13207 C  CA  . LEU   A 1 1661 ? -46.28500  36.34900  -19.49200 1.000 106.10001 ?  1659 LEU   A CA  1 
ATOM   13208 C  C   . LEU   A 1 1661 ? -47.24700  35.29600  -20.02300 1.000 121.60234 ?  1659 LEU   A C   1 
ATOM   13209 O  O   . LEU   A 1 1661 ? -48.34800  35.61600  -20.48100 1.000 123.44832 ?  1659 LEU   A O   1 
ATOM   13210 C  CB  . LEU   A 1 1661 ? -46.76600  36.85000  -18.13000 1.000 100.63804 ?  1659 LEU   A CB  1 
ATOM   13211 C  CG  . LEU   A 1 1661 ? -45.74000  37.47100  -17.18000 1.000 105.75634 ?  1659 LEU   A CG  1 
ATOM   13212 C  CD1 . LEU   A 1 1661 ? -44.49300  36.61000  -17.10300 1.000 107.65413 ?  1659 LEU   A CD1 1 
ATOM   13213 C  CD2 . LEU   A 1 1661 ? -45.39500  38.89000  -17.59900 1.000 106.67847 ?  1659 LEU   A CD2 1 
ATOM   13214 N  N   . CYS   A 1 1662 ? -46.83500  34.03400  -19.94100 1.000 127.03193 ?  1660 CYS   A N   1 
ATOM   13215 C  CA  . CYS   A 1 1662 ? -47.65600  32.91000  -20.36100 1.000 121.32814 ?  1660 CYS   A CA  1 
ATOM   13216 C  C   . CYS   A 1 1662 ? -47.79600  31.91100  -19.22000 1.000 108.41958 ?  1660 CYS   A C   1 
ATOM   13217 O  O   . CYS   A 1 1662 ? -46.90900  31.78300  -18.37000 1.000 84.90069  ?  1660 CYS   A O   1 
ATOM   13218 C  CB  . CYS   A 1 1662 ? -47.06300  32.21600  -21.59300 1.000 111.56305 ?  1660 CYS   A CB  1 
ATOM   13219 S  SG  . CYS   A 1 1662 ? -48.19800  31.07900  -22.41400 1.000 114.90359 ?  1660 CYS   A SG  1 
ATOM   13220 N  N   . ALA   A 1 1663 ? -48.92100  31.20200  -19.21000 1.000 107.98118 ?  1661 ALA   A N   1 
ATOM   13221 C  CA  . ALA   A 1 1663 ? -49.18500  30.20000  -18.18400 1.000 97.75281  ?  1661 ALA   A CA  1 
ATOM   13222 C  C   . ALA   A 1 1663 ? -49.63100  28.88400  -18.81200 1.000 93.72130  ?  1661 ALA   A C   1 
ATOM   13223 O  O   . ALA   A 1 1663 ? -50.68800  28.35000  -18.47500 1.000 106.81392 ?  1661 ALA   A O   1 
ATOM   13224 C  CB  . ALA   A 1 1663 ? -50.23400  30.70500  -17.20400 1.000 89.41129  ?  1661 ALA   A CB  1 
ATOM   13225 N  N   . THR   A 1 1672 ? -61.19800  28.38500  -19.21900 1.000 73.32718  ?  1670 THR   A N   1 
ATOM   13226 C  CA  . THR   A 1 1672 ? -61.47200  29.58400  -18.43500 1.000 101.64037 ?  1670 THR   A CA  1 
ATOM   13227 C  C   . THR   A 1 1672 ? -60.31400  30.57500  -18.52800 1.000 109.13617 ?  1670 THR   A C   1 
ATOM   13228 O  O   . THR   A 1 1672 ? -59.27300  30.38500  -17.89900 1.000 122.64136 ?  1670 THR   A O   1 
ATOM   13229 C  CB  . THR   A 1 1672 ? -61.73200  29.24000  -16.95400 1.000 110.63422 ?  1670 THR   A CB  1 
ATOM   13230 O  OG1 . THR   A 1 1672 ? -60.86900  28.16800  -16.55100 1.000 109.08428 ?  1670 THR   A OG1 1 
ATOM   13231 C  CG2 . THR   A 1 1672 ? -63.18400  28.82800  -16.74800 1.000 71.60112  ?  1670 THR   A CG2 1 
ATOM   13232 N  N   . VAL   A 1 1673 ? -60.50000  31.63400  -19.31600 1.000 105.91368 ?  1671 VAL   A N   1 
ATOM   13233 C  CA  . VAL   A 1 1673 ? -59.47500  32.65500  -19.53200 1.000 111.59081 ?  1671 VAL   A CA  1 
ATOM   13234 C  C   . VAL   A 1 1673 ? -59.87600  33.98400  -18.89200 1.000 113.00676 ?  1671 VAL   A C   1 
ATOM   13235 O  O   . VAL   A 1 1673 ? -59.14400  34.52800  -18.06300 1.000 112.57768 ?  1671 VAL   A O   1 
ATOM   13236 C  CB  . VAL   A 1 1673 ? -59.16400  32.82500  -21.03700 1.000 105.70825 ?  1671 VAL   A CB  1 
ATOM   13237 C  CG1 . VAL   A 1 1673 ? -58.67000  34.23800  -21.33900 1.000 88.41223  ?  1671 VAL   A CG1 1 
ATOM   13238 C  CG2 . VAL   A 1 1673 ? -58.14300  31.78900  -21.48900 1.000 101.16501 ?  1671 VAL   A CG2 1 
ATOM   13239 N  N   . GLY   A 1 1674 ? -61.04100  34.52100  -19.26500 1.000 106.50717 ?  1672 GLY   A N   1 
ATOM   13240 C  CA  . GLY   A 1 1674 ? -61.51900  35.73500  -18.62600 1.000 102.86024 ?  1672 GLY   A CA  1 
ATOM   13241 C  C   . GLY   A 1 1674 ? -61.83400  35.53400  -17.15800 1.000 118.64208 ?  1672 GLY   A C   1 
ATOM   13242 O  O   . GLY   A 1 1674 ? -61.64900  36.44500  -16.34600 1.000 116.41591 ?  1672 GLY   A O   1 
ATOM   13243 N  N   . GLN   A 1 1675 ? -62.31300  34.34100  -16.79700 1.000 119.48482 ?  1673 GLN   A N   1 
ATOM   13244 C  CA  . GLN   A 1 1675 ? -62.50400  34.01200  -15.39000 1.000 127.24667 ?  1673 GLN   A CA  1 
ATOM   13245 C  C   . GLN   A 1 1675 ? -61.16500  33.89400  -14.67200 1.000 134.04544 ?  1673 GLN   A C   1 
ATOM   13246 O  O   . GLN   A 1 1675 ? -61.02600  34.34200  -13.52800 1.000 136.70795 ?  1673 GLN   A O   1 
ATOM   13247 C  CB  . GLN   A 1 1675 ? -63.30500  32.71600  -15.26000 1.000 123.09566 ?  1673 GLN   A CB  1 
ATOM   13248 C  CG  . GLN   A 1 1675 ? -64.24400  32.67900  -14.06300 1.000 122.29827 ?  1673 GLN   A CG  1 
ATOM   13249 C  CD  . GLN   A 1 1675 ? -63.50300  32.64800  -12.74000 1.000 142.16654 ?  1673 GLN   A CD  1 
ATOM   13250 O  OE1 . GLN   A 1 1675 ? -62.85300  31.65900  -12.40300 1.000 148.76582 ?  1673 GLN   A OE1 1 
ATOM   13251 N  NE2 . GLN   A 1 1675 ? -63.59600  33.73600  -11.98300 1.000 130.55955 ?  1673 GLN   A NE2 1 
ATOM   13252 N  N   . LEU   A 1 1676 ? -60.17000  33.29000  -15.32800 1.000 128.39142 ?  1674 LEU   A N   1 
ATOM   13253 C  CA  . LEU   A 1 1676 ? -58.82600  33.25500  -14.76200 1.000 116.85463 ?  1674 LEU   A CA  1 
ATOM   13254 C  C   . LEU   A 1 1676 ? -58.26000  34.66100  -14.61800 1.000 116.14308 ?  1674 LEU   A C   1 
ATOM   13255 O  O   . LEU   A 1 1676 ? -57.59200  34.97200  -13.62400 1.000 112.71220 ?  1674 LEU   A O   1 
ATOM   13256 C  CB  . LEU   A 1 1676 ? -57.91200  32.39200  -15.63200 1.000 109.17848 ?  1674 LEU   A CB  1 
ATOM   13257 N  N   . ARG   A 1 1677 ? -58.51700  35.52600  -15.60300 1.000 110.47602 ?  1675 ARG   A N   1 
ATOM   13258 C  CA  . ARG   A 1 1677 ? -58.13800  36.92900  -15.47200 1.000 107.88907 ?  1675 ARG   A CA  1 
ATOM   13259 C  C   . ARG   A 1 1677 ? -58.89200  37.59500  -14.32800 1.000 117.36448 ?  1675 ARG   A C   1 
ATOM   13260 O  O   . ARG   A 1 1677 ? -58.33800  38.44800  -13.62500 1.000 127.30867 ?  1675 ARG   A O   1 
ATOM   13261 C  CB  . ARG   A 1 1677 ? -58.39500  37.66900  -16.78600 1.000 96.16376  ?  1675 ARG   A CB  1 
ATOM   13262 C  CG  . ARG   A 1 1677 ? -57.37200  37.39000  -17.87500 1.000 96.71938  ?  1675 ARG   A CG  1 
ATOM   13263 C  CD  . ARG   A 1 1677 ? -57.75200  38.08500  -19.17300 1.000 100.15561 ?  1675 ARG   A CD  1 
ATOM   13264 N  NE  . ARG   A 1 1677 ? -57.91500  39.52300  -18.99500 1.000 108.53876 ?  1675 ARG   A NE  1 
ATOM   13265 C  CZ  . ARG   A 1 1677 ? -57.09100  40.43600  -19.49100 1.000 115.64273 ?  1675 ARG   A CZ  1 
ATOM   13266 N  NH1 . ARG   A 1 1677 ? -56.03500  40.09600  -20.21000 1.000 106.35645 ?  1675 ARG   A NH1 1 
ATOM   13267 N  NH2 . ARG   A 1 1677 ? -57.33400  41.72400  -19.25900 1.000 119.53266 ?  1675 ARG   A NH2 1 
ATOM   13268 N  N   . GLU   A 1 1678 ? -60.15700  37.21500  -14.12300 1.000 118.85480 ?  1676 GLU   A N   1 
ATOM   13269 C  CA  . GLU   A 1 1678 ? -60.94100  37.78700  -13.03000 1.000 124.46562 ?  1676 GLU   A CA  1 
ATOM   13270 C  C   . GLU   A 1 1678 ? -60.37400  37.38900  -11.67300 1.000 121.83948 ?  1676 GLU   A C   1 
ATOM   13271 O  O   . GLU   A 1 1678 ? -60.29000  38.22100  -10.76100 1.000 110.33854 ?  1676 GLU   A O   1 
ATOM   13272 C  CB  . GLU   A 1 1678 ? -62.40400  37.35500  -13.15400 1.000 126.25658 ?  1676 GLU   A CB  1 
ATOM   13273 C  CG  . GLU   A 1 1678 ? -63.13400  37.18100  -11.82400 1.000 130.12036 ?  1676 GLU   A CG  1 
ATOM   13274 C  CD  . GLU   A 1 1678 ? -63.39500  38.49800  -11.11200 1.000 136.66492 ?  1676 GLU   A CD  1 
ATOM   13275 O  OE1 . GLU   A 1 1678 ? -63.32000  39.56000  -11.76500 1.000 135.83736 ?  1676 GLU   A OE1 1 
ATOM   13276 O  OE2 . GLU   A 1 1678 ? -63.67200  38.46800  -9.89300  1.000 124.54740 ?  1676 GLU   A OE2 1 
ATOM   13277 N  N   . LEU   A 1 1679 ? -59.98800  36.11900  -11.51900 1.000 114.49871 ?  1677 LEU   A N   1 
ATOM   13278 C  CA  . LEU   A 1 1679 ? -59.32200  35.68900  -10.29500 1.000 107.80789 ?  1677 LEU   A CA  1 
ATOM   13279 C  C   . LEU   A 1 1679 ? -58.06400  36.51000  -10.04100 1.000 109.75772 ?  1677 LEU   A C   1 
ATOM   13280 O  O   . LEU   A 1 1679 ? -57.73000  36.81400  -8.89000  1.000 101.33761 ?  1677 LEU   A O   1 
ATOM   13281 C  CB  . LEU   A 1 1679 ? -58.98800  34.20000  -10.38200 1.000 103.31386 ?  1677 LEU   A CB  1 
ATOM   13282 C  CG  . LEU   A 1 1679 ? -58.73700  33.45500  -9.07100  1.000 98.47514  ?  1677 LEU   A CG  1 
ATOM   13283 C  CD1 . LEU   A 1 1679 ? -60.04300  32.93400  -8.48800  1.000 92.66157  ?  1677 LEU   A CD1 1 
ATOM   13284 C  CD2 . LEU   A 1 1679 ? -57.74800  32.32000  -9.28800  1.000 85.46128  ?  1677 LEU   A CD2 1 
ATOM   13285 N  N   . LEU   A 1 1680 ? -57.36300  36.89000  -11.10800 1.000 113.68265 ?  1678 LEU   A N   1 
ATOM   13286 C  CA  . LEU   A 1 1680 ? -56.18300  37.73700  -11.01800 1.000 112.89832 ?  1678 LEU   A CA  1 
ATOM   13287 C  C   . LEU   A 1 1680 ? -56.49500  39.21300  -11.23400 1.000 118.69128 ?  1678 LEU   A C   1 
ATOM   13288 O  O   . LEU   A 1 1680 ? -55.58700  40.04300  -11.12100 1.000 121.44805 ?  1678 LEU   A O   1 
ATOM   13289 C  CB  . LEU   A 1 1680 ? -55.12900  37.27600  -12.02900 1.000 111.50713 ?  1678 LEU   A CB  1 
ATOM   13290 C  CG  . LEU   A 1 1680 ? -54.78600  35.78500  -11.97500 1.000 110.96134 ?  1678 LEU   A CG  1 
ATOM   13291 C  CD1 . LEU   A 1 1680 ? -53.68200  35.44800  -12.96100 1.000 93.94934  ?  1678 LEU   A CD1 1 
ATOM   13292 C  CD2 . LEU   A 1 1680 ? -54.39300  35.36700  -10.56400 1.000 99.85043  ?  1678 LEU   A CD2 1 
ATOM   13293 N  N   . ARG   A 1 1681 ? -57.74700  39.56100  -11.54900 1.000 122.56075 ?  1679 ARG   A N   1 
ATOM   13294 C  CA  . ARG   A 1 1681 ? -58.12100  40.97000  -11.63800 1.000 110.02669 ?  1679 ARG   A CA  1 
ATOM   13295 C  C   . ARG   A 1 1681 ? -57.98100  41.64800  -10.28400 1.000 108.40067 ?  1679 ARG   A C   1 
ATOM   13296 O  O   . ARG   A 1 1681 ? -57.35300  42.70600  -10.16500 1.000 105.17113 ?  1679 ARG   A O   1 
ATOM   13297 C  CB  . ARG   A 1 1681 ? -59.54800  41.11000  -12.17000 1.000 119.26518 ?  1679 ARG   A CB  1 
ATOM   13298 C  CG  . ARG   A 1 1681 ? -59.69000  42.18000  -13.23800 1.000 117.48448 ?  1679 ARG   A CG  1 
ATOM   13299 C  CD  . ARG   A 1 1681 ? -61.07900  42.19400  -13.86200 1.000 98.39659  ?  1679 ARG   A CD  1 
ATOM   13300 N  NE  . ARG   A 1 1681 ? -61.21500  41.26300  -14.97900 1.000 100.41852 ?  1679 ARG   A NE  1 
ATOM   13301 C  CZ  . ARG   A 1 1681 ? -60.56800  41.36300  -16.13400 1.000 117.69543 ?  1679 ARG   A CZ  1 
ATOM   13302 N  NH1 . ARG   A 1 1681 ? -59.69100  42.32900  -16.35800 1.000 109.12299 ?  1679 ARG   A NH1 1 
ATOM   13303 N  NH2 . ARG   A 1 1681 ? -60.80800  40.46900  -17.09000 1.000 112.20449 ?  1679 ARG   A NH2 1 
ATOM   13304 N  N   . ARG   A 1 1682 ? -58.56700  41.05300  -9.24900  1.000 108.60339 ?  1680 ARG   A N   1 
ATOM   13305 C  CA  . ARG   A 1 1682 ? -58.24300  41.45300  -7.89300  1.000 107.06710 ?  1680 ARG   A CA  1 
ATOM   13306 C  C   . ARG   A 1 1682 ? -56.84300  40.96200  -7.53600  1.000 122.87761 ?  1680 ARG   A C   1 
ATOM   13307 O  O   . ARG   A 1 1682 ? -56.27400  40.09100  -8.20200  1.000 121.59758 ?  1680 ARG   A O   1 
ATOM   13308 C  CB  . ARG   A 1 1682 ? -59.27200  40.90100  -6.90400  1.000 92.65808  ?  1680 ARG   A CB  1 
ATOM   13309 C  CG  . ARG   A 1 1682 ? -60.65400  40.66600  -7.50600  1.000 117.63236 ?  1680 ARG   A CG  1 
ATOM   13310 C  CD  . ARG   A 1 1682 ? -61.61100  41.80700  -7.18200  1.000 123.28431 ?  1680 ARG   A CD  1 
ATOM   13311 N  NE  . ARG   A 1 1682 ? -62.98300  41.50200  -7.57300  1.000 115.20256 ?  1680 ARG   A NE  1 
ATOM   13312 C  CZ  . ARG   A 1 1682 ? -63.56600  41.94600  -8.67800  1.000 113.67994 ?  1680 ARG   A CZ  1 
ATOM   13313 N  NH1 . ARG   A 1 1682 ? -62.92400  42.72500  -9.53400  1.000 104.72984 ?  1680 ARG   A NH1 1 
ATOM   13314 N  NH2 . ARG   A 1 1682 ? -64.82500  41.60000  -8.93200  1.000 102.28936 ?  1680 ARG   A NH2 1 
ATOM   13315 N  N   . GLU   A 1 1683 ? -56.28100  41.55400  -6.47800  1.000 120.96996 ?  1681 GLU   A N   1 
ATOM   13316 C  CA  . GLU   A 1 1683 ? -54.95900  41.21200  -5.95100  1.000 112.70330 ?  1681 GLU   A CA  1 
ATOM   13317 C  C   . GLU   A 1 1683 ? -53.82100  41.62300  -6.88400  1.000 100.92596 ?  1681 GLU   A C   1 
ATOM   13318 O  O   . GLU   A 1 1683 ? -52.82100  42.18700  -6.42900  1.000 101.08869 ?  1681 GLU   A O   1 
ATOM   13319 C  CB  . GLU   A 1 1683 ? -54.86000  39.71000  -5.64600  1.000 117.41780 ?  1681 GLU   A CB  1 
ATOM   13320 C  CG  . GLU   A 1 1683 ? -56.02500  39.13500  -4.84700  1.000 131.46631 ?  1681 GLU   A CG  1 
ATOM   13321 C  CD  . GLU   A 1 1683 ? -55.83100  39.25400  -3.34700  1.000 144.26643 ?  1681 GLU   A CD  1 
ATOM   13322 O  OE1 . GLU   A 1 1683 ? -55.66900  40.39000  -2.85100  1.000 141.21552 ?  1681 GLU   A OE1 1 
ATOM   13323 O  OE2 . GLU   A 1 1683 ? -55.84400  38.21000  -2.66200  1.000 128.32560 ?  1681 GLU   A OE2 1 
ATOM   13324 N  N   . LEU   A 1 1684 ? -53.95100  41.34700  -8.19300  1.000 104.75169 ?  1682 LEU   A N   1 
ATOM   13325 C  CA  . LEU   A 1 1684 ? -52.82400  41.53800  -9.09800  1.000 104.81427 ?  1682 LEU   A CA  1 
ATOM   13326 C  C   . LEU   A 1 1684 ? -53.04400  42.72100  -10.03500 1.000 109.38414 ?  1682 LEU   A C   1 
ATOM   13327 O  O   . LEU   A 1 1684 ? -54.16100  42.92700  -10.52400 1.000 92.04074  ?  1682 LEU   A O   1 
ATOM   13328 C  CB  . LEU   A 1 1684 ? -52.58000  40.27700  -9.93500  1.000 101.96985 ?  1682 LEU   A CB  1 
ATOM   13329 C  CG  . LEU   A 1 1684 ? -51.51100  39.29800  -9.45000  1.000 96.56496  ?  1682 LEU   A CG  1 
ATOM   13330 C  CD1 . LEU   A 1 1684 ? -51.54100  39.13200  -7.93700  1.000 103.38128 ?  1682 LEU   A CD1 1 
ATOM   13331 C  CD2 . LEU   A 1 1684 ? -51.70400  37.96300  -10.13800 1.000 94.98297  ?  1682 LEU   A CD2 1 
ATOM   13332 N  N   . PRO   A 1 1685 ? -52.00100  43.49800  -10.31400 1.000 109.34545 ?  1683 PRO   A N   1 
ATOM   13333 C  CA  . PRO   A 1 1685 ? -52.13800  44.63600  -11.22600 1.000 100.21172 ?  1683 PRO   A CA  1 
ATOM   13334 C  C   . PRO   A 1 1685 ? -52.14800  44.18800  -12.68000 1.000 98.29572  ?  1683 PRO   A C   1 
ATOM   13335 O  O   . PRO   A 1 1685 ? -51.63900  43.12500  -13.03500 1.000 101.88241 ?  1683 PRO   A O   1 
ATOM   13336 C  CB  . PRO   A 1 1685 ? -50.89600  45.48600  -10.92900 1.000 80.87287  ?  1683 PRO   A CB  1 
ATOM   13337 C  CG  . PRO   A 1 1685 ? -50.18600  44.81100  -9.77600  1.000 86.43508  ?  1683 PRO   A CG  1 
ATOM   13338 C  CD  . PRO   A 1 1685 ? -50.63600  43.39100  -9.78200  1.000 98.43351  ?  1683 PRO   A CD  1 
ATOM   13339 N  N   . GLU   A 1 1686 ? -52.71800  45.04600  -13.53100 1.000 99.44105  ?  1684 GLU   A N   1 
ATOM   13340 C  CA  . GLU   A 1 1686 ? -52.98100  44.64900  -14.91100 1.000 102.51355 ?  1684 GLU   A CA  1 
ATOM   13341 C  C   . GLU   A 1 1686 ? -51.72000  44.48100  -15.74700 1.000 97.28162  ?  1684 GLU   A C   1 
ATOM   13342 O  O   . GLU   A 1 1686 ? -51.81700  43.99000  -16.87700 1.000 101.11197 ?  1684 GLU   A O   1 
ATOM   13343 C  CB  . GLU   A 1 1686 ? -53.93000  45.63900  -15.58500 1.000 106.27160 ?  1684 GLU   A CB  1 
ATOM   13344 C  CG  . GLU   A 1 1686 ? -55.06200  44.95700  -16.35100 1.000 104.18312 ?  1684 GLU   A CG  1 
ATOM   13345 C  CD  . GLU   A 1 1686 ? -55.91900  44.06200  -15.46400 1.000 116.57211 ?  1684 GLU   A CD  1 
ATOM   13346 O  OE1 . GLU   A 1 1686 ? -56.11600  44.40300  -14.27800 1.000 111.22522 ?  1684 GLU   A OE1 1 
ATOM   13347 O  OE2 . GLU   A 1 1686 ? -56.39100  43.01100  -15.94900 1.000 107.86354 ?  1684 GLU   A OE2 1 
ATOM   13348 N  N   . TYR   A 1 1687 ? -50.55200  44.86200  -15.24000 1.000 95.22405  ?  1685 TYR   A N   1 
ATOM   13349 C  CA  . TYR   A 1 1687 ? -49.31100  44.51300  -15.91500 1.000 85.90492  ?  1685 TYR   A CA  1 
ATOM   13350 C  C   . TYR   A 1 1687 ? -48.77800  43.15200  -15.48700 1.000 94.91206  ?  1685 TYR   A C   1 
ATOM   13351 O  O   . TYR   A 1 1687 ? -47.74400  42.71700  -16.00600 1.000 85.19234  ?  1685 TYR   A O   1 
ATOM   13352 C  CB  . TYR   A 1 1687 ? -48.23700  45.58300  -15.68100 1.000 87.37133  ?  1685 TYR   A CB  1 
ATOM   13353 C  CG  . TYR   A 1 1687 ? -47.89900  45.86700  -14.23400 1.000 98.48735  ?  1685 TYR   A CG  1 
ATOM   13354 C  CD1 . TYR   A 1 1687 ? -48.59900  46.82400  -13.50600 1.000 100.29411 ?  1685 TYR   A CD1 1 
ATOM   13355 C  CD2 . TYR   A 1 1687 ? -46.82700  45.23400  -13.62000 1.000 94.10338  ?  1685 TYR   A CD2 1 
ATOM   13356 C  CE1 . TYR   A 1 1687 ? -48.26600  47.10500  -12.18900 1.000 103.74842 ?  1685 TYR   A CE1 1 
ATOM   13357 C  CE2 . TYR   A 1 1687 ? -46.49400  45.50000  -12.30300 1.000 97.81451  ?  1685 TYR   A CE2 1 
ATOM   13358 C  CZ  . TYR   A 1 1687 ? -47.21500  46.43900  -11.59300 1.000 104.61332 ?  1685 TYR   A CZ  1 
ATOM   13359 O  OH  . TYR   A 1 1687 ? -46.88400  46.71400  -10.28300 1.000 92.11577  ?  1685 TYR   A OH  1 
ATOM   13360 N  N   . MET   A 1 1688 ? -49.46300  42.47000  -14.56500 1.000 96.77301  ?  1686 MET   A N   1 
ATOM   13361 C  CA  . MET   A 1 1688 ? -49.04000  41.16700  -14.06800 1.000 90.19961  ?  1686 MET   A CA  1 
ATOM   13362 C  C   . MET   A 1 1688 ? -50.07400  40.08400  -14.37100 1.000 102.40874 ?  1686 MET   A C   1 
ATOM   13363 O  O   . MET   A 1 1688 ? -50.18400  39.10300  -13.63200 1.000 94.57960  ?  1686 MET   A O   1 
ATOM   13364 C  CB  . MET   A 1 1688 ? -48.75400  41.22400  -12.56500 1.000 92.21074  ?  1686 MET   A CB  1 
ATOM   13365 C  CG  . MET   A 1 1688 ? -47.27800  41.42300  -12.24000 1.000 86.15020  ?  1686 MET   A CG  1 
ATOM   13366 S  SD  . MET   A 1 1688 ? -46.80300  41.40900  -10.49600 1.000 123.72961 ?  1686 MET   A SD  1 
ATOM   13367 C  CE  . MET   A 1 1688 ? -48.26500  40.73100  -9.72000  1.000 97.03778  ?  1686 MET   A CE  1 
ATOM   13368 N  N   . ILE   A 1 1689 ? -50.84200  40.25000  -15.43900 1.000 102.01120 ?  1687 ILE   A N   1 
ATOM   13369 C  CA  . ILE   A 1 1689 ? -51.78500  39.23100  -15.90600 1.000 95.68265  ?  1687 ILE   A CA  1 
ATOM   13370 C  C   . ILE   A 1 1689 ? -51.13000  38.41900  -17.01600 1.000 104.28905 ?  1687 ILE   A C   1 
ATOM   13371 O  O   . ILE   A 1 1689 ? -50.53500  39.01000  -17.93100 1.000 101.28592 ?  1687 ILE   A O   1 
ATOM   13372 C  CB  . ILE   A 1 1689 ? -53.12100  39.83400  -16.39000 1.000 103.66508 ?  1687 ILE   A CB  1 
ATOM   13373 C  CG1 . ILE   A 1 1689 ? -54.05200  40.14800  -15.21700 1.000 101.04390 ?  1687 ILE   A CG1 1 
ATOM   13374 C  CG2 . ILE   A 1 1689 ? -53.84000  38.88400  -17.32400 1.000 106.83525 ?  1687 ILE   A CG2 1 
ATOM   13375 C  CD1 . ILE   A 1 1689 ? -53.71100  41.35900  -14.46200 1.000 99.44154  ?  1687 ILE   A CD1 1 
ATOM   13376 N  N   . PRO   A 1 1690 ? -51.20800  37.09000  -16.97400 1.000 106.99711 ?  1688 PRO   A N   1 
ATOM   13377 C  CA  . PRO   A 1 1690 ? -50.71600  36.28800  -18.10200 1.000 101.05808 ?  1688 PRO   A CA  1 
ATOM   13378 C  C   . PRO   A 1 1690 ? -51.52400  36.59600  -19.35200 1.000 104.11242 ?  1688 PRO   A C   1 
ATOM   13379 O  O   . PRO   A 1 1690 ? -52.73700  36.38600  -19.39600 1.000 106.99851 ?  1688 PRO   A O   1 
ATOM   13380 C  CB  . PRO   A 1 1690 ? -50.92200  34.84400  -17.62700 1.000 106.67918 ?  1688 PRO   A CB  1 
ATOM   13381 C  CG  . PRO   A 1 1690 ? -51.13400  34.93000  -16.14500 1.000 88.76930  ?  1688 PRO   A CG  1 
ATOM   13382 C  CD  . PRO   A 1 1690 ? -51.74900  36.26100  -15.88700 1.000 103.50650 ?  1688 PRO   A CD  1 
ATOM   13383 N  N   . ALA   A 1 1691 ? -50.83900  37.13200  -20.36700 1.000 109.88380 ?  1689 ALA   A N   1 
ATOM   13384 C  CA  . ALA   A 1 1691 ? -51.49900  37.40800  -21.63900 1.000 113.02125 ?  1689 ALA   A CA  1 
ATOM   13385 C  C   . ALA   A 1 1691 ? -52.10600  36.14600  -22.24100 1.000 120.98070 ?  1689 ALA   A C   1 
ATOM   13386 O  O   . ALA   A 1 1691 ? -53.16500  36.20800  -22.87700 1.000 119.01684 ?  1689 ALA   A O   1 
ATOM   13387 C  CB  . ALA   A 1 1691 ? -50.50900  38.04100  -22.61500 1.000 96.70628  ?  1689 ALA   A CB  1 
ATOM   13388 N  N   . HIS   A 1 1692 ? -51.45400  34.99900  -22.05600 1.000 119.33690 ?  1690 HIS   A N   1 
ATOM   13389 C  CA  . HIS   A 1 1692 ? -51.96500  33.71400  -22.51500 1.000 112.62409 ?  1690 HIS   A CA  1 
ATOM   13390 C  C   . HIS   A 1 1692 ? -51.91600  32.72500  -21.36100 1.000 106.50103 ?  1690 HIS   A C   1 
ATOM   13391 O  O   . HIS   A 1 1692 ? -50.89200  32.61000  -20.68100 1.000 99.42963  ?  1690 HIS   A O   1 
ATOM   13392 C  CB  . HIS   A 1 1692 ? -51.15800  33.18100  -23.70700 1.000 110.49111 ?  1690 HIS   A CB  1 
ATOM   13393 C  CG  . HIS   A 1 1692 ? -51.01200  34.16500  -24.82700 1.000 125.45972 ?  1690 HIS   A CG  1 
ATOM   13394 N  ND1 . HIS   A 1 1692 ? -49.88600  34.94300  -24.98900 1.000 134.18035 ?  1690 HIS   A ND1 1 
ATOM   13395 C  CD2 . HIS   A 1 1692 ? -51.84700  34.49600  -25.84100 1.000 114.49617 ?  1690 HIS   A CD2 1 
ATOM   13396 C  CE1 . HIS   A 1 1692 ? -50.03500  35.71500  -26.05000 1.000 123.43636 ?  1690 HIS   A CE1 1 
ATOM   13397 N  NE2 . HIS   A 1 1692 ? -51.21600  35.46300  -26.58600 1.000 116.15027 ?  1690 HIS   A NE2 1 
ATOM   13398 N  N   . PHE   A 1 1693 ? -53.02200  32.02100  -21.13500 1.000 113.44709 ?  1691 PHE   A N   1 
ATOM   13399 C  CA  . PHE   A 1 1693 ? -53.08600  31.02500  -20.07000 1.000 102.81075 ?  1691 PHE   A CA  1 
ATOM   13400 C  C   . PHE   A 1 1693 ? -52.88100  29.62400  -20.63200 1.000 97.48051  ?  1691 PHE   A C   1 
ATOM   13401 O  O   . PHE   A 1 1693 ? -52.91700  29.42500  -21.84600 1.000 97.21089  ?  1691 PHE   A O   1 
ATOM   13402 C  CB  . PHE   A 1 1693 ? -54.42300  31.10800  -19.32700 1.000 91.83289  ?  1691 PHE   A CB  1 
ATOM   13403 C  CG  . PHE   A 1 1693 ? -54.54800  32.31100  -18.43400 1.000 112.09798 ?  1691 PHE   A CG  1 
ATOM   13404 C  CD1 . PHE   A 1 1693 ? -54.96900  33.52900  -18.94200 1.000 120.70393 ?  1691 PHE   A CD1 1 
ATOM   13405 C  CD2 . PHE   A 1 1693 ? -54.24100  32.22300  -17.08600 1.000 106.18581 ?  1691 PHE   A CD2 1 
ATOM   13406 C  CE1 . PHE   A 1 1693 ? -55.08300  34.63700  -18.12100 1.000 122.03892 ?  1691 PHE   A CE1 1 
ATOM   13407 C  CE2 . PHE   A 1 1693 ? -54.35300  33.32600  -16.26000 1.000 105.95575 ?  1691 PHE   A CE2 1 
ATOM   13408 C  CZ  . PHE   A 1 1693 ? -54.77400  34.53400  -16.77800 1.000 115.32498 ?  1691 PHE   A CZ  1 
ATOM   13409 N  N   . ALA   A 1 1726 ? -73.73700  38.54500  -23.42900 1.000 102.20396 ?  1724 ALA   A N   1 
ATOM   13410 C  CA  . ALA   A 1 1726 ? -74.31100  37.62700  -24.40100 1.000 103.53784 ?  1724 ALA   A CA  1 
ATOM   13411 C  C   . ALA   A 1 1726 ? -75.47600  36.90900  -23.76400 1.000 114.03525 ?  1724 ALA   A C   1 
ATOM   13412 O  O   . ALA   A 1 1726 ? -76.29900  36.30600  -24.44400 1.000 122.19226 ?  1724 ALA   A O   1 
ATOM   13413 C  CB  . ALA   A 1 1726 ? -73.26500  36.63300  -24.89100 1.000 95.54510  ?  1724 ALA   A CB  1 
ATOM   13414 N  N   . ALA   A 1 1727 ? -75.54200  36.96800  -22.43600 1.000 113.25633 ?  1725 ALA   A N   1 
ATOM   13415 C  CA  . ALA   A 1 1727 ? -76.57600  36.24200  -21.69300 1.000 111.20953 ?  1725 ALA   A CA  1 
ATOM   13416 C  C   . ALA   A 1 1727 ? -77.25400  37.07700  -20.60200 1.000 105.42482 ?  1725 ALA   A C   1 
ATOM   13417 O  O   . ALA   A 1 1727 ? -77.34100  36.64400  -19.45400 1.000 102.77855 ?  1725 ALA   A O   1 
ATOM   13418 C  CB  . ALA   A 1 1727 ? -75.96500  34.98000  -21.09700 1.000 106.63301 ?  1725 ALA   A CB  1 
ATOM   13419 N  N   . PRO   A 1 1728 ? -77.75900  38.27700  -20.92500 1.000 105.06745 ?  1726 PRO   A N   1 
ATOM   13420 C  CA  . PRO   A 1 1728 ? -78.67400  38.95500  -19.99600 1.000 100.62219 ?  1726 PRO   A CA  1 
ATOM   13421 C  C   . PRO   A 1 1728 ? -79.80900  38.03300  -19.57400 1.000 92.47516  ?  1726 PRO   A C   1 
ATOM   13422 O  O   . PRO   A 1 1728 ? -80.46600  37.40900  -20.41100 1.000 92.30533  ?  1726 PRO   A O   1 
ATOM   13423 C  CB  . PRO   A 1 1728 ? -79.20000  40.14200  -20.81600 1.000 87.79391  ?  1726 PRO   A CB  1 
ATOM   13424 C  CG  . PRO   A 1 1728 ? -78.25900  40.31600  -21.96300 1.000 82.60007  ?  1726 PRO   A CG  1 
ATOM   13425 C  CD  . PRO   A 1 1728 ? -77.21900  39.24100  -21.90300 1.000 103.55848 ?  1726 PRO   A CD  1 
ATOM   13426 N  N   . ARG   A 1 1729 ? -80.03700  37.94700  -18.26300 1.000 89.31753  ?  1727 ARG   A N   1 
ATOM   13427 C  CA  . ARG   A 1 1729 ? -81.03400  37.03800  -17.70800 1.000 95.23652  ?  1727 ARG   A CA  1 
ATOM   13428 C  C   . ARG   A 1 1729 ? -82.27600  37.71700  -17.14900 1.000 102.13636 ?  1727 ARG   A C   1 
ATOM   13429 O  O   . ARG   A 1 1729 ? -83.35700  37.13300  -17.22800 1.000 104.34366 ?  1727 ARG   A O   1 
ATOM   13430 C  CB  . ARG   A 1 1729 ? -80.41600  36.16200  -16.60900 1.000 86.43678  ?  1727 ARG   A CB  1 
ATOM   13431 C  CG  . ARG   A 1 1729 ? -79.23600  35.32900  -17.07700 1.000 97.80902  ?  1727 ARG   A CG  1 
ATOM   13432 C  CD  . ARG   A 1 1729 ? -78.00200  35.60100  -16.24800 1.000 100.89696 ?  1727 ARG   A CD  1 
ATOM   13433 N  NE  . ARG   A 1 1729 ? -78.11000  35.03900  -14.90800 1.000 107.61803 ?  1727 ARG   A NE  1 
ATOM   13434 C  CZ  . ARG   A 1 1729 ? -77.39200  35.44500  -13.87000 1.000 116.06442 ?  1727 ARG   A CZ  1 
ATOM   13435 N  NH1 . ARG   A 1 1729 ? -76.51700  36.43100  -13.97800 1.000 103.73275 ?  1727 ARG   A NH1 1 
ATOM   13436 N  NH2 . ARG   A 1 1729 ? -77.56100  34.84900  -12.69300 1.000 116.91573 ?  1727 ARG   A NH2 1 
ATOM   13437 N  N   . THR   A 1 1730 ? -82.16800  38.91100  -16.57300 1.000 108.11692 ?  1728 THR   A N   1 
ATOM   13438 C  CA  . THR   A 1 1730 ? -83.35900  39.65700  -16.19300 1.000 108.66616 ?  1728 THR   A CA  1 
ATOM   13439 C  C   . THR   A 1 1730 ? -83.40400  40.98600  -16.93800 1.000 106.84745 ?  1728 THR   A C   1 
ATOM   13440 O  O   . THR   A 1 1730 ? -82.44000  41.40400  -17.58700 1.000 93.85893  ?  1728 THR   A O   1 
ATOM   13441 C  CB  . THR   A 1 1730 ? -83.45000  39.87800  -14.67000 1.000 94.75444  ?  1728 THR   A CB  1 
ATOM   13442 O  OG1 . THR   A 1 1730 ? -84.54000  40.76200  -14.37900 1.000 102.23070 ?  1728 THR   A OG1 1 
ATOM   13443 C  CG2 . THR   A 1 1730 ? -82.18300  40.46000  -14.10600 1.000 74.24137  ?  1728 THR   A CG2 1 
ATOM   13444 N  N   . GLU   A 1 1731 ? -84.57700  41.62200  -16.86100 1.000 100.22506 ?  1729 GLU   A N   1 
ATOM   13445 C  CA  . GLU   A 1 1731 ? -84.79900  42.89000  -17.54600 1.000 99.55798  ?  1729 GLU   A CA  1 
ATOM   13446 C  C   . GLU   A 1 1731 ? -83.74300  43.91300  -17.16100 1.000 87.00762  ?  1729 GLU   A C   1 
ATOM   13447 O  O   . GLU   A 1 1731 ? -83.26600  44.68000  -18.00600 1.000 73.23951  ?  1729 GLU   A O   1 
ATOM   13448 C  CB  . GLU   A 1 1731 ? -86.18900  43.41800  -17.20400 1.000 95.05656  ?  1729 GLU   A CB  1 
ATOM   13449 C  CG  . GLU   A 1 1731 ? -87.32200  42.72200  -17.92400 1.000 99.19501  ?  1729 GLU   A CG  1 
ATOM   13450 C  CD  . GLU   A 1 1731 ? -88.58900  43.54800  -17.91900 1.000 114.85070 ?  1729 GLU   A CD  1 
ATOM   13451 O  OE1 . GLU   A 1 1731 ? -88.85600  44.21200  -16.89500 1.000 118.73021 ?  1729 GLU   A OE1 1 
ATOM   13452 O  OE2 . GLU   A 1 1731 ? -89.31900  43.53100  -18.93300 1.000 128.95931 -1 1729 GLU   A OE2 1 
ATOM   13453 N  N   . LEU   A 1 1732 ? -83.37200  43.93100  -15.88300 1.000 81.00485  ?  1730 LEU   A N   1 
ATOM   13454 C  CA  . LEU   A 1 1732 ? -82.37900  44.87700  -15.39500 1.000 74.52924  ?  1730 LEU   A CA  1 
ATOM   13455 C  C   . LEU   A 1 1732 ? -81.05900  44.72500  -16.14000 1.000 86.04638  ?  1730 LEU   A C   1 
ATOM   13456 O  O   . LEU   A 1 1732 ? -80.50900  45.70300  -16.65500 1.000 88.29454  ?  1730 LEU   A O   1 
ATOM   13457 C  CB  . LEU   A 1 1732 ? -82.19200  44.66800  -13.89600 1.000 67.88503  ?  1730 LEU   A CB  1 
ATOM   13458 C  CG  . LEU   A 1 1732 ? -81.45100  45.71100  -13.07900 1.000 59.72632  ?  1730 LEU   A CG  1 
ATOM   13459 C  CD1 . LEU   A 1 1732 ? -81.83500  47.10700  -13.54900 1.000 66.96596  ?  1730 LEU   A CD1 1 
ATOM   13460 C  CD2 . LEU   A 1 1732 ? -81.84200  45.48100  -11.63400 1.000 40.19754  ?  1730 LEU   A CD2 1 
ATOM   13461 N  N   . GLU   A 1 1733 ? -80.54100  43.49700  -16.21800 1.000 87.59927  ?  1731 GLU   A N   1 
ATOM   13462 C  CA  . GLU   A 1 1733 ? -79.27100  43.27400  -16.90400 1.000 83.10611  ?  1731 GLU   A CA  1 
ATOM   13463 C  C   . GLU   A 1 1733 ? -79.38500  43.59300  -18.38900 1.000 86.49356  ?  1731 GLU   A C   1 
ATOM   13464 O  O   . GLU   A 1 1733 ? -78.44100  44.11500  -18.99300 1.000 86.80577  ?  1731 GLU   A O   1 
ATOM   13465 C  CB  . GLU   A 1 1733 ? -78.81400  41.83100  -16.68800 1.000 91.48693  ?  1731 GLU   A CB  1 
ATOM   13466 C  CG  . GLU   A 1 1733 ? -79.24700  41.29900  -15.34300 1.000 105.75320 ?  1731 GLU   A CG  1 
ATOM   13467 C  CD  . GLU   A 1 1733 ? -78.54500  40.02800  -14.90000 1.000 112.43896 ?  1731 GLU   A CD  1 
ATOM   13468 O  OE1 . GLU   A 1 1733 ? -77.98900  39.29900  -15.74800 1.000 104.93266 ?  1731 GLU   A OE1 1 
ATOM   13469 O  OE2 . GLU   A 1 1733 ? -78.60600  39.73100  -13.68900 1.000 110.94681 ?  1731 GLU   A OE2 1 
ATOM   13470 N  N   . ALA   A 1 1734 ? -80.53500  43.28900  -18.99700 1.000 84.50020  ?  1732 ALA   A N   1 
ATOM   13471 C  CA  . ALA   A 1 1734 ? -80.77000  43.71000  -20.37400 1.000 78.09786  ?  1732 ALA   A CA  1 
ATOM   13472 C  C   . ALA   A 1 1734 ? -80.73900  45.22800  -20.48600 1.000 71.11929  ?  1732 ALA   A C   1 
ATOM   13473 O  O   . ALA   A 1 1734 ? -80.11000  45.78700  -21.39300 1.000 74.52205  ?  1732 ALA   A O   1 
ATOM   13474 C  CB  . ALA   A 1 1734 ? -82.10600  43.16000  -20.87500 1.000 73.73136  ?  1732 ALA   A CB  1 
ATOM   13475 N  N   . THR   A 1 1735 ? -81.41300  45.91200  -19.55900 1.000 75.14166  ?  1733 THR   A N   1 
ATOM   13476 C  CA  . THR   A 1 1735 ? -81.37300  47.37000  -19.53100 1.000 81.63501  ?  1733 THR   A CA  1 
ATOM   13477 C  C   . THR   A 1 1735 ? -79.95800  47.87600  -19.28600 1.000 74.57206  ?  1733 THR   A C   1 
ATOM   13478 O  O   . THR   A 1 1735 ? -79.51300  48.83700  -19.92600 1.000 69.97388  ?  1733 THR   A O   1 
ATOM   13479 C  CB  . THR   A 1 1735 ? -82.32500  47.89800  -18.45600 1.000 76.07823  ?  1733 THR   A CB  1 
ATOM   13480 O  OG1 . THR   A 1 1735 ? -83.58800  47.22800  -18.56100 1.000 66.73050  ?  1733 THR   A OG1 1 
ATOM   13481 C  CG2 . THR   A 1 1735 ? -82.53400  49.39600  -18.61200 1.000 68.60508  ?  1733 THR   A CG2 1 
ATOM   13482 N  N   . LEU   A 1 1736 ? -79.23200  47.23800  -18.36300 1.000 75.17490  ?  1734 LEU   A N   1 
ATOM   13483 C  CA  . LEU   A 1 1736 ? -77.85800  47.64900  -18.09100 1.000 71.88854  ?  1734 LEU   A CA  1 
ATOM   13484 C  C   . LEU   A 1 1736 ? -76.95900  47.39000  -19.29200 1.000 73.68851  ?  1734 LEU   A C   1 
ATOM   13485 O  O   . LEU   A 1 1736 ? -76.08000  48.20200  -19.60500 1.000 70.46656  ?  1734 LEU   A O   1 
ATOM   13486 C  CB  . LEU   A 1 1736 ? -77.32700  46.92300  -16.85400 1.000 65.29441  ?  1734 LEU   A CB  1 
ATOM   13487 C  CG  . LEU   A 1 1736 ? -78.01500  47.23500  -15.52300 1.000 57.73990  ?  1734 LEU   A CG  1 
ATOM   13488 C  CD1 . LEU   A 1 1736 ? -77.78400  46.11800  -14.51500 1.000 57.85607  ?  1734 LEU   A CD1 1 
ATOM   13489 C  CD2 . LEU   A 1 1736 ? -77.54000  48.56500  -14.96800 1.000 49.19638  ?  1734 LEU   A CD2 1 
ATOM   13490 N  N   . ALA   A 1 1737 ? -77.17000  46.26600  -19.98300 1.000 71.42158  ?  1735 ALA   A N   1 
ATOM   13491 C  CA  . ALA   A 1 1737 ? -76.37000  45.95800  -21.16400 1.000 71.46612  ?  1735 ALA   A CA  1 
ATOM   13492 C  C   . ALA   A 1 1737 ? -76.60900  46.97400  -22.27200 1.000 69.85921  ?  1735 ALA   A C   1 
ATOM   13493 O  O   . ALA   A 1 1737 ? -75.67800  47.34600  -22.99700 1.000 68.31890  ?  1735 ALA   A O   1 
ATOM   13494 C  CB  . ALA   A 1 1737 ? -76.68200  44.54600  -21.65900 1.000 64.29037  ?  1735 ALA   A CB  1 
ATOM   13495 N  N   . HIS   A 1 1738 ? -77.85100  47.43500  -22.41900 1.000 64.01289  ?  1736 HIS   A N   1 
ATOM   13496 C  CA  . HIS   A 1 1738 ? -78.14600  48.44000  -23.43300 1.000 74.88231  ?  1736 HIS   A CA  1 
ATOM   13497 C  C   . HIS   A 1 1738 ? -77.50900  49.78000  -23.07800 1.000 76.61280  ?  1736 HIS   A C   1 
ATOM   13498 O  O   . HIS   A 1 1738 ? -76.89900  50.43400  -23.93300 1.000 86.26412  ?  1736 HIS   A O   1 
ATOM   13499 C  CB  . HIS   A 1 1738 ? -79.65800  48.58600  -23.60300 1.000 74.46578  ?  1736 HIS   A CB  1 
ATOM   13500 C  CG  . HIS   A 1 1738 ? -80.05300  49.67400  -24.55100 1.000 80.65464  ?  1736 HIS   A CG  1 
ATOM   13501 N  ND1 . HIS   A 1 1738 ? -80.69400  50.82200  -24.14000 1.000 75.01721  ?  1736 HIS   A ND1 1 
ATOM   13502 C  CD2 . HIS   A 1 1738 ? -79.88900  49.79400  -25.89000 1.000 73.05867  ?  1736 HIS   A CD2 1 
ATOM   13503 C  CE1 . HIS   A 1 1738 ? -80.91100  51.60200  -25.18500 1.000 75.73643  ?  1736 HIS   A CE1 1 
ATOM   13504 N  NE2 . HIS   A 1 1738 ? -80.43200  51.00100  -26.25900 1.000 78.72653  ?  1736 HIS   A NE2 1 
ATOM   13505 N  N   . ILE   A 1 1739 ? -77.63300  50.20100  -21.81600 1.000 74.25899  ?  1737 ILE   A N   1 
ATOM   13506 C  CA  . ILE   A 1 1739 ? -77.08100  51.48800  -21.40200 1.000 80.99485  ?  1737 ILE   A CA  1 
ATOM   13507 C  C   . ILE   A 1 1739 ? -75.55800  51.46900  -21.46900 1.000 82.05780  ?  1737 ILE   A C   1 
ATOM   13508 O  O   . ILE   A 1 1739 ? -74.93100  52.43800  -21.91500 1.000 82.29394  ?  1737 ILE   A O   1 
ATOM   13509 C  CB  . ILE   A 1 1739 ? -77.58500  51.85600  -19.99400 1.000 60.18120  ?  1737 ILE   A CB  1 
ATOM   13510 C  CG1 . ILE   A 1 1739 ? -79.10200  52.06000  -20.01300 1.000 52.04001  ?  1737 ILE   A CG1 1 
ATOM   13511 C  CG2 . ILE   A 1 1739 ? -76.87600  53.10200  -19.47800 1.000 59.36439  ?  1737 ILE   A CG2 1 
ATOM   13512 C  CD1 . ILE   A 1 1739 ? -79.65200  52.77400  -18.79300 1.000 51.46728  ?  1737 ILE   A CD1 1 
ATOM   13513 N  N   . TRP   A 1 1740 ? -74.94000  50.36900  -21.03000 1.000 76.68489  ?  1738 TRP   A N   1 
ATOM   13514 C  CA  . TRP   A 1 1740 ? -73.48800  50.25300  -21.12400 1.000 80.29366  ?  1738 TRP   A CA  1 
ATOM   13515 C  C   . TRP   A 1 1740 ? -73.02400  50.32700  -22.57300 1.000 86.11628  ?  1738 TRP   A C   1 
ATOM   13516 O  O   . TRP   A 1 1740 ? -72.05000  51.02100  -22.88700 1.000 89.60658  ?  1738 TRP   A O   1 
ATOM   13517 C  CB  . TRP   A 1 1740 ? -73.02100  48.94700  -20.48100 1.000 79.26929  ?  1738 TRP   A CB  1 
ATOM   13518 C  CG  . TRP   A 1 1740 ? -72.97000  48.98100  -18.98400 1.000 80.01807  ?  1738 TRP   A CG  1 
ATOM   13519 C  CD1 . TRP   A 1 1740 ? -73.64100  49.83400  -18.15500 1.000 81.53676  ?  1738 TRP   A CD1 1 
ATOM   13520 C  CD2 . TRP   A 1 1740 ? -72.19800  48.12400  -18.13600 1.000 86.03272  ?  1738 TRP   A CD2 1 
ATOM   13521 N  NE1 . TRP   A 1 1740 ? -73.33800  49.55800  -16.84400 1.000 64.94725  ?  1738 TRP   A NE1 1 
ATOM   13522 C  CE2 . TRP   A 1 1740 ? -72.45200  48.51200  -16.80500 1.000 87.41432  ?  1738 TRP   A CE2 1 
ATOM   13523 C  CE3 . TRP   A 1 1740 ? -71.31600  47.06500  -18.37300 1.000 98.71416  ?  1738 TRP   A CE3 1 
ATOM   13524 C  CZ2 . TRP   A 1 1740 ? -71.85700  47.87900  -15.71700 1.000 84.77104  ?  1738 TRP   A CZ2 1 
ATOM   13525 C  CZ3 . TRP   A 1 1740 ? -70.72500  46.43800  -17.29100 1.000 93.54337  ?  1738 TRP   A CZ3 1 
ATOM   13526 C  CH2 . TRP   A 1 1740 ? -70.99900  46.84600  -15.98000 1.000 84.14793  ?  1738 TRP   A CH2 1 
ATOM   13527 N  N   . GLY   A 1 1741 ? -73.71800  49.62500  -23.47300 1.000 72.49872  ?  1739 GLY   A N   1 
ATOM   13528 C  CA  . GLY   A 1 1741 ? -73.33400  49.63900  -24.87300 1.000 67.23543  ?  1739 GLY   A CA  1 
ATOM   13529 C  C   . GLY   A 1 1741 ? -73.40200  51.01400  -25.50600 1.000 77.17928  ?  1739 GLY   A C   1 
ATOM   13530 O  O   . GLY   A 1 1741 ? -72.66800  51.29900  -26.45600 1.000 79.72895  ?  1739 GLY   A O   1 
ATOM   13531 N  N   . GLU   A 1 1742 ? -74.27900  51.88100  -24.99900 1.000 78.36456  ?  1740 GLU   A N   1 
ATOM   13532 C  CA  . GLU   A 1 1742 ? -74.35300  53.24400  -25.51400 1.000 77.92904  ?  1740 GLU   A CA  1 
ATOM   13533 C  C   . GLU   A 1 1742 ? -73.16800  54.07200  -25.03800 1.000 86.21278  ?  1740 GLU   A C   1 
ATOM   13534 O  O   . GLU   A 1 1742 ? -72.46500  54.69300  -25.84400 1.000 94.98535  ?  1740 GLU   A O   1 
ATOM   13535 C  CB  . GLU   A 1 1742 ? -75.66200  53.90000  -25.07900 1.000 84.24798  ?  1740 GLU   A CB  1 
ATOM   13536 C  CG  . GLU   A 1 1742 ? -76.86200  53.54900  -25.93300 1.000 92.18227  ?  1740 GLU   A CG  1 
ATOM   13537 C  CD  . GLU   A 1 1742 ? -78.01800  54.50400  -25.71000 1.000 102.67190 ?  1740 GLU   A CD  1 
ATOM   13538 O  OE1 . GLU   A 1 1742 ? -78.24500  54.89900  -24.54600 1.000 99.73474  ?  1740 GLU   A OE1 1 
ATOM   13539 O  OE2 . GLU   A 1 1742 ? -78.69400  54.86300  -26.69600 1.000 102.80122 -1 1740 GLU   A OE2 1 
ATOM   13540 N  N   . VAL   A 1 1743 ? -72.93400  54.09100  -23.72500 1.000 87.35312  ?  1741 VAL   A N   1 
ATOM   13541 C  CA  . VAL   A 1 1743 ? -71.87600  54.92400  -23.16200 1.000 87.04233  ?  1741 VAL   A CA  1 
ATOM   13542 C  C   . VAL   A 1 1743 ? -70.50500  54.37400  -23.53800 1.000 80.71946  ?  1741 VAL   A C   1 
ATOM   13543 O  O   . VAL   A 1 1743 ? -69.62600  55.11100  -24.00100 1.000 71.65357  ?  1741 VAL   A O   1 
ATOM   13544 C  CB  . VAL   A 1 1743 ? -72.04600  55.03600  -21.63700 1.000 82.60645  ?  1741 VAL   A CB  1 
ATOM   13545 C  CG1 . VAL   A 1 1743 ? -70.95700  55.90700  -21.04600 1.000 79.78339  ?  1741 VAL   A CG1 1 
ATOM   13546 C  CG2 . VAL   A 1 1743 ? -73.42400  55.58500  -21.29100 1.000 60.83085  ?  1741 VAL   A CG2 1 
ATOM   13547 N  N   . LEU   A 1 1744 ? -70.30200  53.06700  -23.35000 1.000 82.15615  ?  1742 LEU   A N   1 
ATOM   13548 C  CA  . LEU   A 1 1744 ? -69.00100  52.47200  -23.63500 1.000 84.69157  ?  1742 LEU   A CA  1 
ATOM   13549 C  C   . LEU   A 1 1744 ? -68.75500  52.33300  -25.13200 1.000 93.27147  ?  1742 LEU   A C   1 
ATOM   13550 O  O   . LEU   A 1 1744 ? -67.59700  52.29500  -25.56600 1.000 117.52235 ?  1742 LEU   A O   1 
ATOM   13551 C  CB  . LEU   A 1 1744 ? -68.88900  51.10900  -22.95300 1.000 83.05849  ?  1742 LEU   A CB  1 
ATOM   13552 C  CG  . LEU   A 1 1744 ? -68.94300  51.13600  -21.42500 1.000 81.94955  ?  1742 LEU   A CG  1 
ATOM   13553 C  CD1 . LEU   A 1 1744 ? -68.91200  49.72300  -20.86100 1.000 78.61405  ?  1742 LEU   A CD1 1 
ATOM   13554 C  CD2 . LEU   A 1 1744 ? -67.80000  51.97400  -20.86600 1.000 77.19599  ?  1742 LEU   A CD2 1 
ATOM   13555 N  N   . GLY   A 1 1745 ? -69.81600  52.26000  -25.93200 1.000 91.98740  ?  1743 GLY   A N   1 
ATOM   13556 C  CA  . GLY   A 1 1745 ? -69.66200  52.07700  -27.36100 1.000 86.11372  ?  1743 GLY   A CA  1 
ATOM   13557 C  C   . GLY   A 1 1745 ? -69.43900  50.64800  -27.79400 1.000 91.24235  ?  1743 GLY   A C   1 
ATOM   13558 O  O   . GLY   A 1 1745 ? -68.95900  50.41600  -28.90800 1.000 89.12883  ?  1743 GLY   A O   1 
ATOM   13559 N  N   . ILE   A 1 1746 ? -69.76800  49.68000  -26.94600 1.000 98.93505  ?  1744 ILE   A N   1 
ATOM   13560 C  CA  . ILE   A 1 1746 ? -69.59300  48.26700  -27.25100 1.000 96.68851  ?  1744 ILE   A CA  1 
ATOM   13561 C  C   . ILE   A 1 1746 ? -70.96300  47.70600  -27.60200 1.000 95.02156  ?  1744 ILE   A C   1 
ATOM   13562 O  O   . ILE   A 1 1746 ? -71.82300  47.55200  -26.72800 1.000 107.22044 ?  1744 ILE   A O   1 
ATOM   13563 C  CB  . ILE   A 1 1746 ? -68.95800  47.50800  -26.07800 1.000 95.05721  ?  1744 ILE   A CB  1 
ATOM   13564 C  CG1 . ILE   A 1 1746 ? -67.86500  48.35400  -25.41800 1.000 97.93815  ?  1744 ILE   A CG1 1 
ATOM   13565 C  CG2 . ILE   A 1 1746 ? -68.39700  46.17400  -26.54800 1.000 95.49862  ?  1744 ILE   A CG2 1 
ATOM   13566 C  CD1 . ILE   A 1 1746 ? -66.71100  48.70500  -26.34100 1.000 98.47103  ?  1744 ILE   A CD1 1 
ATOM   13567 N  N   . GLU   A 1 1747 ? -71.16700  47.40900  -28.88900 1.000 101.98859 ?  1745 GLU   A N   1 
ATOM   13568 C  CA  . GLU   A 1 1747 ? -72.44200  46.87000  -29.35000 1.000 111.75080 ?  1745 GLU   A CA  1 
ATOM   13569 C  C   . GLU   A 1 1747 ? -72.86000  45.63500  -28.56800 1.000 117.40964 ?  1745 GLU   A C   1 
ATOM   13570 O  O   . GLU   A 1 1747 ? -74.05800  45.39700  -28.37200 1.000 123.31424 ?  1745 GLU   A O   1 
ATOM   13571 C  CB  . GLU   A 1 1747 ? -72.35700  46.52400  -30.83600 1.000 106.76812 ?  1745 GLU   A CB  1 
ATOM   13572 C  CG  . GLU   A 1 1747 ? -73.54000  46.99300  -31.66100 1.000 122.53713 ?  1745 GLU   A CG  1 
ATOM   13573 C  CD  . GLU   A 1 1747 ? -73.47200  46.49300  -33.09000 1.000 120.35730 ?  1745 GLU   A CD  1 
ATOM   13574 O  OE1 . GLU   A 1 1747 ? -72.50500  46.84600  -33.79800 1.000 115.82219 ?  1745 GLU   A OE1 1 
ATOM   13575 O  OE2 . GLU   A 1 1747 ? -74.38000  45.74200  -33.50500 1.000 107.32116 ?  1745 GLU   A OE2 1 
ATOM   13576 N  N   . ARG   A 1 1748 ? -71.89800  44.83600  -28.11800 1.000 103.62077 ?  1746 ARG   A N   1 
ATOM   13577 C  CA  . ARG   A 1 1748 ? -72.18400  43.57500  -27.44900 1.000 105.33993 ?  1746 ARG   A CA  1 
ATOM   13578 C  C   . ARG   A 1 1748 ? -71.55400  43.58800  -26.06200 1.000 102.85998 ?  1746 ARG   A C   1 
ATOM   13579 O  O   . ARG   A 1 1748 ? -70.32600  43.54400  -25.93300 1.000 119.46465 ?  1746 ARG   A O   1 
ATOM   13580 C  CB  . ARG   A 1 1748 ? -71.67100  42.39400  -28.28000 1.000 117.57690 ?  1746 ARG   A CB  1 
ATOM   13581 C  CG  . ARG   A 1 1748 ? -72.60300  41.93900  -29.43100 1.000 116.39712 ?  1746 ARG   A CG  1 
ATOM   13582 C  CD  . ARG   A 1 1748 ? -73.97000  41.42900  -28.93300 1.000 119.36228 ?  1746 ARG   A CD  1 
ATOM   13583 N  NE  . ARG   A 1 1748 ? -73.92600  41.19800  -27.49800 1.000 116.00648 ?  1746 ARG   A NE  1 
ATOM   13584 C  CZ  . ARG   A 1 1748 ? -73.48100  40.09400  -26.91800 1.000 119.81594 ?  1746 ARG   A CZ  1 
ATOM   13585 N  NH1 . ARG   A 1 1748 ? -73.29500  38.97700  -27.60300 1.000 112.44490 ?  1746 ARG   A NH1 1 
ATOM   13586 N  NH2 . ARG   A 1 1748 ? -73.18500  40.12800  -25.62700 1.000 120.17132 ?  1746 ARG   A NH2 1 
ATOM   13587 N  N   . ILE   A 1 1749 ? -72.39400  43.63600  -25.03000 1.000 92.66020  ?  1747 ILE   A N   1 
ATOM   13588 C  CA  . ILE   A 1 1749 ? -71.95400  43.65500  -23.64000 1.000 94.93799  ?  1747 ILE   A CA  1 
ATOM   13589 C  C   . ILE   A 1 1749 ? -72.51400  42.42300  -22.94600 1.000 90.69930  ?  1747 ILE   A C   1 
ATOM   13590 O  O   . ILE   A 1 1749 ? -73.71600  42.14800  -23.03700 1.000 87.08628  ?  1747 ILE   A O   1 
ATOM   13591 C  CB  . ILE   A 1 1749 ? -72.40700  44.93500  -22.91300 1.000 81.07103  ?  1747 ILE   A CB  1 
ATOM   13592 C  CG1 . ILE   A 1 1749 ? -71.70500  46.16300  -23.49400 1.000 93.00969  ?  1747 ILE   A CG1 1 
ATOM   13593 C  CG2 . ILE   A 1 1749 ? -72.13700  44.82200  -21.42000 1.000 75.63845  ?  1747 ILE   A CG2 1 
ATOM   13594 C  CD1 . ILE   A 1 1749 ? -70.32100  46.38900  -22.95500 1.000 80.39125  ?  1747 ILE   A CD1 1 
ATOM   13595 N  N   . GLY   A 1 1750 ? -71.64600  41.68600  -22.25700 1.000 96.66331  ?  1748 GLY   A N   1 
ATOM   13596 C  CA  . GLY   A 1 1750 ? -72.05900  40.54800  -21.47000 1.000 87.58927  ?  1748 GLY   A CA  1 
ATOM   13597 C  C   . GLY   A 1 1750 ? -72.18400  40.89400  -19.99900 1.000 84.86280  ?  1748 GLY   A C   1 
ATOM   13598 O  O   . GLY   A 1 1750 ? -71.62200  41.87400  -19.51600 1.000 92.03428  ?  1748 GLY   A O   1 
ATOM   13599 N  N   . ILE   A 1 1751 ? -72.94000  40.06000  -19.28200 1.000 84.23011  ?  1749 ILE   A N   1 
ATOM   13600 C  CA  . ILE   A 1 1751 ? -73.14800  40.29100  -17.86000 1.000 92.91306  ?  1749 ILE   A CA  1 
ATOM   13601 C  C   . ILE   A 1 1751 ? -71.86200  40.12300  -17.07000 1.000 98.79425  ?  1749 ILE   A C   1 
ATOM   13602 O  O   . ILE   A 1 1751 ? -71.76900  40.60300  -15.93500 1.000 101.20115 ?  1749 ILE   A O   1 
ATOM   13603 C  CB  . ILE   A 1 1751 ? -74.22400  39.34100  -17.32200 1.000 88.89508  ?  1749 ILE   A CB  1 
ATOM   13604 C  CG1 . ILE   A 1 1751 ? -74.10900  37.99400  -18.03000 1.000 98.15002  ?  1749 ILE   A CG1 1 
ATOM   13605 C  CG2 . ILE   A 1 1751 ? -75.59200  39.94600  -17.55000 1.000 86.57268  ?  1749 ILE   A CG2 1 
ATOM   13606 C  CD1 . ILE   A 1 1751 ? -75.03700  36.96300  -17.49400 1.000 95.05925  ?  1749 ILE   A CD1 1 
ATOM   13607 N  N   . ARG   A 1 1752 ? -70.86600  39.44600  -17.64000 1.000 107.38628 ?  1750 ARG   A N   1 
ATOM   13608 C  CA  . ARG   A 1 1752 ? -69.59000  39.20700  -16.98000 1.000 107.26895 ?  1750 ARG   A CA  1 
ATOM   13609 C  C   . ARG   A 1 1752 ? -68.44500  39.94600  -17.66400 1.000 93.85807  ?  1750 ARG   A C   1 
ATOM   13610 O  O   . ARG   A 1 1752 ? -67.31000  39.46600  -17.67800 1.000 100.70490 ?  1750 ARG   A O   1 
ATOM   13611 C  CB  . ARG   A 1 1752 ? -69.30200  37.70700  -16.91500 1.000 104.41479 ?  1750 ARG   A CB  1 
ATOM   13612 C  CG  . ARG   A 1 1752 ? -70.06900  37.00100  -15.81600 1.000 95.17987  ?  1750 ARG   A CG  1 
ATOM   13613 C  CD  . ARG   A 1 1752 ? -70.32200  35.53700  -16.12100 1.000 93.55839  ?  1750 ARG   A CD  1 
ATOM   13614 N  NE  . ARG   A 1 1752 ? -71.65500  35.13300  -15.69000 1.000 101.10909 ?  1750 ARG   A NE  1 
ATOM   13615 C  CZ  . ARG   A 1 1752 ? -71.92000  34.53400  -14.53700 1.000 102.91922 ?  1750 ARG   A CZ  1 
ATOM   13616 N  NH1 . ARG   A 1 1752 ? -70.96200  34.24800  -13.67100 1.000 104.99911 ?  1750 ARG   A NH1 1 
ATOM   13617 N  NH2 . ARG   A 1 1752 ? -73.17800  34.21600  -14.24500 1.000 103.31845 ?  1750 ARG   A NH2 1 
ATOM   13618 N  N   . ASP   A 1 1753 ? -68.72700  41.11400  -18.23400 1.000 102.31926 ?  1751 ASP   A N   1 
ATOM   13619 C  CA  . ASP   A 1 1753 ? -67.70600  41.95200  -18.84800 1.000 94.86997  ?  1751 ASP   A CA  1 
ATOM   13620 C  C   . ASP   A 1 1753 ? -67.32500  43.07200  -17.88800 1.000 92.24955  ?  1751 ASP   A C   1 
ATOM   13621 O  O   . ASP   A 1 1753 ? -68.18200  43.62900  -17.19600 1.000 87.85544  ?  1751 ASP   A O   1 
ATOM   13622 C  CB  . ASP   A 1 1753 ? -68.19300  42.53400  -20.17800 1.000 88.36418  ?  1751 ASP   A CB  1 
ATOM   13623 C  CG  . ASP   A 1 1753 ? -68.68600  41.46500  -21.13900 1.000 97.23289  ?  1751 ASP   A CG  1 
ATOM   13624 O  OD1 . ASP   A 1 1753 ? -68.77500  40.28700  -20.73000 1.000 85.26826  ?  1751 ASP   A OD1 1 
ATOM   13625 O  OD2 . ASP   A 1 1753 ? -68.98800  41.80200  -22.30500 1.000 84.44933  -1 1751 ASP   A OD2 1 
ATOM   13626 N  N   . ASN   A 1 1754 ? -66.03500  43.39300  -17.84800 1.000 89.55931  ?  1752 ASN   A N   1 
ATOM   13627 C  CA  . ASN   A 1 1754 ? -65.50500  44.35000  -16.88600 1.000 95.63962  ?  1752 ASN   A CA  1 
ATOM   13628 C  C   . ASN   A 1 1754 ? -65.62600  45.76300  -17.44500 1.000 86.28545  ?  1752 ASN   A C   1 
ATOM   13629 O  O   . ASN   A 1 1754 ? -65.10100  46.05300  -18.52400 1.000 81.15644  ?  1752 ASN   A O   1 
ATOM   13630 C  CB  . ASN   A 1 1754 ? -64.05100  44.02400  -16.55000 1.000 86.75281  ?  1752 ASN   A CB  1 
ATOM   13631 C  CG  . ASN   A 1 1754 ? -63.44400  45.01200  -15.57500 1.000 84.94318  ?  1752 ASN   A CG  1 
ATOM   13632 O  OD1 . ASN   A 1 1754 ? -63.05700  46.11900  -15.95100 1.000 87.62161  ?  1752 ASN   A OD1 1 
ATOM   13633 N  ND2 . ASN   A 1 1754 ? -63.36200  44.61700  -14.31100 1.000 78.35054  ?  1752 ASN   A ND2 1 
ATOM   13634 N  N   . PHE   A 1 1755 ? -66.30400  46.63400  -16.69200 1.000 82.06889  ?  1753 PHE   A N   1 
ATOM   13635 C  CA  . PHE   A 1 1755 ? -66.53100  48.02000  -17.09300 1.000 90.50123  ?  1753 PHE   A CA  1 
ATOM   13636 C  C   . PHE   A 1 1755 ? -65.25400  48.68300  -17.60700 1.000 83.46973  ?  1753 PHE   A C   1 
ATOM   13637 O  O   . PHE   A 1 1755 ? -65.21600  49.20600  -18.72700 1.000 79.25802  ?  1753 PHE   A O   1 
ATOM   13638 C  CB  . PHE   A 1 1755 ? -67.11400  48.79000  -15.90200 1.000 80.81754  ?  1753 PHE   A CB  1 
ATOM   13639 C  CG  . PHE   A 1 1755 ? -67.35100  50.24800  -16.16600 1.000 72.12287  ?  1753 PHE   A CG  1 
ATOM   13640 C  CD1 . PHE   A 1 1755 ? -68.22300  50.65800  -17.16000 1.000 67.46889  ?  1753 PHE   A CD1 1 
ATOM   13641 C  CD2 . PHE   A 1 1755 ? -66.71300  51.21200  -15.40200 1.000 75.76817  ?  1753 PHE   A CD2 1 
ATOM   13642 C  CE1 . PHE   A 1 1755 ? -68.44000  52.00300  -17.39600 1.000 67.46838  ?  1753 PHE   A CE1 1 
ATOM   13643 C  CE2 . PHE   A 1 1755 ? -66.92900  52.55700  -15.63100 1.000 83.61192  ?  1753 PHE   A CE2 1 
ATOM   13644 C  CZ  . PHE   A 1 1755 ? -67.79400  52.95400  -16.62900 1.000 74.95438  ?  1753 PHE   A CZ  1 
ATOM   13645 N  N   . PHE   A 1 1756 ? -64.18800  48.65200  -16.80400 1.000 91.24052  ?  1754 PHE   A N   1 
ATOM   13646 C  CA  . PHE   A 1 1756 ? -62.94600  49.31400  -17.19400 1.000 93.66773  ?  1754 PHE   A CA  1 
ATOM   13647 C  C   . PHE   A 1 1756 ? -62.27500  48.62200  -18.37300 1.000 85.83983  ?  1754 PHE   A C   1 
ATOM   13648 O  O   . PHE   A 1 1756 ? -61.52700  49.26400  -19.12000 1.000 76.56853  ?  1754 PHE   A O   1 
ATOM   13649 C  CB  . PHE   A 1 1756 ? -61.99200  49.37500  -16.00300 1.000 88.34820  ?  1754 PHE   A CB  1 
ATOM   13650 C  CG  . PHE   A 1 1756 ? -62.60800  49.96700  -14.77600 1.000 94.99094  ?  1754 PHE   A CG  1 
ATOM   13651 C  CD1 . PHE   A 1 1756 ? -62.92000  51.31400  -14.72700 1.000 96.98406  ?  1754 PHE   A CD1 1 
ATOM   13652 C  CD2 . PHE   A 1 1756 ? -62.88500  49.17800  -13.67400 1.000 94.08703  ?  1754 PHE   A CD2 1 
ATOM   13653 C  CE1 . PHE   A 1 1756 ? -63.49100  51.86400  -13.60400 1.000 85.64834  ?  1754 PHE   A CE1 1 
ATOM   13654 C  CE2 . PHE   A 1 1756 ? -63.45700  49.72500  -12.54700 1.000 95.06936  ?  1754 PHE   A CE2 1 
ATOM   13655 C  CZ  . PHE   A 1 1756 ? -63.75700  51.06600  -12.51700 1.000 81.40830  ?  1754 PHE   A CZ  1 
ATOM   13656 N  N   . GLU   A 1 1757 ? -62.52500  47.32500  -18.56000 1.000 90.71989  ?  1755 GLU   A N   1 
ATOM   13657 C  CA  . GLU   A 1 1757 ? -61.94400  46.61700  -19.69400 1.000 88.07151  ?  1755 GLU   A CA  1 
ATOM   13658 C  C   . GLU   A 1 1757 ? -62.56900  47.03100  -21.01800 1.000 80.84932  ?  1755 GLU   A C   1 
ATOM   13659 O  O   . GLU   A 1 1757 ? -61.96200  46.81400  -22.07000 1.000 87.15828  ?  1755 GLU   A O   1 
ATOM   13660 C  CB  . GLU   A 1 1757 ? -62.08800  45.10700  -19.50400 1.000 75.94160  ?  1755 GLU   A CB  1 
ATOM   13661 C  CG  . GLU   A 1 1757 ? -61.12900  44.51800  -18.48600 1.000 95.01895  ?  1755 GLU   A CG  1 
ATOM   13662 C  CD  . GLU   A 1 1757 ? -60.09400  43.60600  -19.11400 1.000 113.03183 ?  1755 GLU   A CD  1 
ATOM   13663 O  OE1 . GLU   A 1 1757 ? -59.29600  44.08600  -19.94700 1.000 115.05244 ?  1755 GLU   A OE1 1 
ATOM   13664 O  OE2 . GLU   A 1 1757 ? -60.07900  42.40500  -18.77300 1.000 119.89938 -1 1755 GLU   A OE2 1 
ATOM   13665 N  N   . LEU   A 1 1758 ? -63.76100  47.62000  -20.98900 1.000 72.09624  ?  1756 LEU   A N   1 
ATOM   13666 C  CA  . LEU   A 1 1758 ? -64.46100  48.04800  -22.19000 1.000 68.89532  ?  1756 LEU   A CA  1 
ATOM   13667 C  C   . LEU   A 1 1758 ? -64.32500  49.54200  -22.44000 1.000 75.94196  ?  1756 LEU   A C   1 
ATOM   13668 O  O   . LEU   A 1 1758 ? -65.05000  50.09000  -23.27700 1.000 83.68913  ?  1756 LEU   A O   1 
ATOM   13669 C  CB  . LEU   A 1 1758 ? -65.93700  47.66600  -22.08500 1.000 81.47316  ?  1756 LEU   A CB  1 
ATOM   13670 C  CG  . LEU   A 1 1758 ? -66.17300  46.34700  -21.34400 1.000 86.85984  ?  1756 LEU   A CG  1 
ATOM   13671 C  CD1 . LEU   A 1 1758 ? -67.59300  46.24700  -20.81600 1.000 78.18346  ?  1756 LEU   A CD1 1 
ATOM   13672 C  CD2 . LEU   A 1 1758 ? -65.85300  45.15300  -22.23300 1.000 88.72298  ?  1756 LEU   A CD2 1 
ATOM   13673 N  N   . GLY   A 1 1759 ? -63.42200  50.21000  -21.73400 1.000 78.98990  ?  1757 GLY   A N   1 
ATOM   13674 C  CA  . GLY   A 1 1759 ? -63.29800  51.64600  -21.80000 1.000 81.30999  ?  1757 GLY   A CA  1 
ATOM   13675 C  C   . GLY   A 1 1759 ? -63.93100  52.39100  -20.64700 1.000 84.41988  ?  1757 GLY   A C   1 
ATOM   13676 O  O   . GLY   A 1 1759 ? -64.31400  53.55400  -20.82100 1.000 68.67806  ?  1757 GLY   A O   1 
ATOM   13677 N  N   . GLY   A 1 1760 ? -64.05300  51.76200  -19.48000 1.000 85.85971  ?  1758 GLY   A N   1 
ATOM   13678 C  CA  . GLY   A 1 1760 ? -64.72400  52.36000  -18.34400 1.000 74.93479  ?  1758 GLY   A CA  1 
ATOM   13679 C  C   . GLY   A 1 1760 ? -63.96000  53.49100  -17.68900 1.000 76.72777  ?  1758 GLY   A C   1 
ATOM   13680 O  O   . GLY   A 1 1760 ? -62.93600  53.26800  -17.03900 1.000 89.47098  ?  1758 GLY   A O   1 
ATOM   13681 N  N   . ASP   A 1 1761 ? -64.44800  54.71300  -17.85800 1.000 84.54595  ?  1759 ASP   A N   1 
ATOM   13682 C  CA  . ASP   A 1 1761 ? -63.87500  55.87600  -17.20600 1.000 79.25795  ?  1759 ASP   A CA  1 
ATOM   13683 C  C   . ASP   A 1 1761 ? -64.77200  56.30900  -16.05200 1.000 76.49384  ?  1759 ASP   A C   1 
ATOM   13684 O  O   . ASP   A 1 1761 ? -65.84600  55.75500  -15.81100 1.000 58.73001  ?  1759 ASP   A O   1 
ATOM   13685 C  CB  . ASP   A 1 1761 ? -63.68500  57.02400  -18.20200 1.000 76.96525  ?  1759 ASP   A CB  1 
ATOM   13686 C  CG  . ASP   A 1 1761 ? -62.78200  56.65300  -19.36600 1.000 103.64569 ?  1759 ASP   A CG  1 
ATOM   13687 O  OD1 . ASP   A 1 1761 ? -63.26400  55.98800  -20.30800 1.000 96.40337  ?  1759 ASP   A OD1 1 
ATOM   13688 O  OD2 . ASP   A 1 1761 ? -61.59100  57.03300  -19.34100 1.000 102.03930 -1 1759 ASP   A OD2 1 
ATOM   13689 N  N   . SER   A 1 1762 ? -64.31700  57.32100  -15.32000 1.000 91.46633  ?  1760 SER   A N   1 
ATOM   13690 C  CA  . SER   A 1 1762 ? -65.19100  57.93900  -14.33400 1.000 72.13861  ?  1760 SER   A CA  1 
ATOM   13691 C  C   . SER   A 1 1762 ? -66.27600  58.76500  -14.99800 1.000 68.37917  ?  1760 SER   A C   1 
ATOM   13692 O  O   . SER   A 1 1762 ? -67.36300  58.92600  -14.43100 1.000 68.48433  ?  1760 SER   A O   1 
ATOM   13693 C  CB  . SER   A 1 1762 ? -64.38300  58.80900  -13.39000 1.000 88.14757  ?  1760 SER   A CB  1 
ATOM   13694 O  OG  . SER   A 1 1762 ? -63.21700  59.26700  -14.02600 1.000 89.25722  ?  1760 SER   A OG  1 
ATOM   13695 N  N   . ILE   A 1 1763 ? -65.97900  59.33500  -16.16900 1.000 79.88660  ?  1761 ILE   A N   1 
ATOM   13696 C  CA  . ILE   A 1 1763 ? -66.98300  60.07200  -16.92900 1.000 69.88350  ?  1761 ILE   A CA  1 
ATOM   13697 C  C   . ILE   A 1 1763 ? -68.11500  59.14100  -17.33900 1.000 72.65847  ?  1761 ILE   A C   1 
ATOM   13698 O  O   . ILE   A 1 1763 ? -69.29200  59.51900  -17.31100 1.000 68.63133  ?  1761 ILE   A O   1 
ATOM   13699 C  CB  . ILE   A 1 1763 ? -66.33800  60.74100  -18.16000 1.000 66.29095  ?  1761 ILE   A CB  1 
ATOM   13700 C  CG1 . ILE   A 1 1763 ? -64.92300  61.23900  -17.84200 1.000 63.40237  ?  1761 ILE   A CG1 1 
ATOM   13701 C  CG2 . ILE   A 1 1763 ? -67.22000  61.87200  -18.70000 1.000 58.41143  ?  1761 ILE   A CG2 1 
ATOM   13702 C  CD1 . ILE   A 1 1763 ? -64.86800  62.56400  -17.12700 1.000 59.49418  ?  1761 ILE   A CD1 1 
ATOM   13703 N  N   . LYS   A 1 1764 ? -67.77400  57.90800  -17.72500 1.000 71.34629  ?  1762 LYS   A N   1 
ATOM   13704 C  CA  . LYS   A 1 1764 ? -68.77900  56.96600  -18.21000 1.000 70.46162  ?  1762 LYS   A CA  1 
ATOM   13705 C  C   . LYS   A 1 1764 ? -69.76900  56.58800  -17.11300 1.000 65.38167  ?  1762 LYS   A C   1 
ATOM   13706 O  O   . LYS   A 1 1764 ? -70.98100  56.54200  -17.35400 1.000 77.40349  ?  1762 LYS   A O   1 
ATOM   13707 C  CB  . LYS   A 1 1764 ? -68.09800  55.71200  -18.75800 1.000 70.29095  ?  1762 LYS   A CB  1 
ATOM   13708 C  CG  . LYS   A 1 1764 ? -66.93900  55.98600  -19.70100 1.000 74.48169  ?  1762 LYS   A CG  1 
ATOM   13709 C  CD  . LYS   A 1 1764 ? -67.41400  56.17300  -21.13200 1.000 75.22557  ?  1762 LYS   A CD  1 
ATOM   13710 C  CE  . LYS   A 1 1764 ? -66.27500  56.62100  -22.03500 1.000 74.31918  ?  1762 LYS   A CE  1 
ATOM   13711 N  NZ  . LYS   A 1 1764 ? -65.24900  55.55200  -22.21000 1.000 85.63191  ?  1762 LYS   A NZ  1 
ATOM   13712 N  N   . GLY   A 1 1765 ? -69.26900  56.30900  -15.90800 1.000 60.25612  ?  1763 GLY   A N   1 
ATOM   13713 C  CA  . GLY   A 1 1765 ? -70.14700  55.88600  -14.82700 1.000 55.80973  ?  1763 GLY   A CA  1 
ATOM   13714 C  C   . GLY   A 1 1765 ? -71.23700  56.89300  -14.51300 1.000 64.30742  ?  1763 GLY   A C   1 
ATOM   13715 O  O   . GLY   A 1 1765 ? -72.36900  56.51500  -14.20100 1.000 72.25609  ?  1763 GLY   A O   1 
ATOM   13716 N  N   . LEU   A 1 1766 ? -70.91400  58.18800  -14.58500 1.000 61.93762  ?  1764 LEU   A N   1 
ATOM   13717 C  CA  . LEU   A 1 1766 ? -71.93400  59.21000  -14.36500 1.000 58.39917  ?  1764 LEU   A CA  1 
ATOM   13718 C  C   . LEU   A 1 1766 ? -73.00700  59.15500  -15.44300 1.000 64.33526  ?  1764 LEU   A C   1 
ATOM   13719 O  O   . LEU   A 1 1766 ? -74.20200  59.27400  -15.14700 1.000 74.50563  ?  1764 LEU   A O   1 
ATOM   13720 C  CB  . LEU   A 1 1766 ? -71.30000  60.60000  -14.32200 1.000 55.70734  ?  1764 LEU   A CB  1 
ATOM   13721 C  CG  . LEU   A 1 1766 ? -72.26200  61.74700  -13.99300 1.000 59.58263  ?  1764 LEU   A CG  1 
ATOM   13722 C  CD1 . LEU   A 1 1766 ? -73.15400  61.39400  -12.81500 1.000 60.39889  ?  1764 LEU   A CD1 1 
ATOM   13723 C  CD2 . LEU   A 1 1766 ? -71.50900  63.03500  -13.71600 1.000 64.44125  ?  1764 LEU   A CD2 1 
ATOM   13724 N  N   . GLN   A 1 1767 ? -72.59900  58.98500  -16.70200 1.000 60.44425  ?  1765 GLN   A N   1 
ATOM   13725 C  CA  . GLN   A 1 1767 ? -73.57300  58.87500  -17.78100 1.000 59.58750  ?  1765 GLN   A CA  1 
ATOM   13726 C  C   . GLN   A 1 1767 ? -74.46100  57.65200  -17.58800 1.000 62.39086  ?  1765 GLN   A C   1 
ATOM   13727 O  O   . GLN   A 1 1767 ? -75.68800  57.74500  -17.68600 1.000 67.22065  ?  1765 GLN   A O   1 
ATOM   13728 C  CB  . GLN   A 1 1767 ? -72.86200  58.82900  -19.13300 1.000 58.29712  ?  1765 GLN   A CB  1 
ATOM   13729 C  CG  . GLN   A 1 1767 ? -72.18700  60.13800  -19.51500 1.000 58.82311  ?  1765 GLN   A CG  1 
ATOM   13730 C  CD  . GLN   A 1 1767 ? -71.46700  60.05800  -20.84600 1.000 85.19518  ?  1765 GLN   A CD  1 
ATOM   13731 O  OE1 . GLN   A 1 1767 ? -70.75100  59.09600  -21.12100 1.000 77.35697  ?  1765 GLN   A OE1 1 
ATOM   13732 N  NE2 . GLN   A 1 1767 ? -71.65600  61.07200  -21.68400 1.000 95.73188  ?  1765 GLN   A NE2 1 
ATOM   13733 N  N   . ILE   A 1 1768 ? -73.85700  56.49900  -17.28700 1.000 51.23346  ?  1766 ILE   A N   1 
ATOM   13734 C  CA  . ILE   A 1 1768 ? -74.63500  55.27800  -17.08600 1.000 55.15928  ?  1766 ILE   A CA  1 
ATOM   13735 C  C   . ILE   A 1 1768 ? -75.62400  55.45700  -15.94000 1.000 64.72462  ?  1766 ILE   A C   1 
ATOM   13736 O  O   . ILE   A 1 1768 ? -76.80300  55.09700  -16.04800 1.000 64.82505  ?  1766 ILE   A O   1 
ATOM   13737 C  CB  . ILE   A 1 1768 ? -73.70200  54.08000  -16.83900 1.000 45.09063  ?  1766 ILE   A CB  1 
ATOM   13738 C  CG1 . ILE   A 1 1768 ? -73.00800  53.67800  -18.14000 1.000 59.74244  ?  1766 ILE   A CG1 1 
ATOM   13739 C  CG2 . ILE   A 1 1768 ? -74.47700  52.91000  -16.24900 1.000 36.73545  ?  1766 ILE   A CG2 1 
ATOM   13740 C  CD1 . ILE   A 1 1768 ? -71.53200  53.44100  -17.99200 1.000 58.74232  ?  1766 ILE   A CD1 1 
ATOM   13741 N  N   . ALA   A 1 1769 ? -75.15800  56.02300  -14.82600 1.000 62.22314  ?  1767 ALA   A N   1 
ATOM   13742 C  CA  . ALA   A 1 1769 ? -76.02900  56.20600  -13.67100 1.000 59.76829  ?  1767 ALA   A CA  1 
ATOM   13743 C  C   . ALA   A 1 1769 ? -77.13400  57.21600  -13.96100 1.000 62.47128  ?  1767 ALA   A C   1 
ATOM   13744 O  O   . ALA   A 1 1769 ? -78.26300  57.06300  -13.47900 1.000 60.84334  ?  1767 ALA   A O   1 
ATOM   13745 C  CB  . ALA   A 1 1769 ? -75.20500  56.63900  -12.45900 1.000 59.47218  ?  1767 ALA   A CB  1 
ATOM   13746 N  N   . SER   A 1 1770 ? -76.83200  58.25200  -14.75000 1.000 48.82799  ?  1768 SER   A N   1 
ATOM   13747 C  CA  . SER   A 1 1770 ? -77.84000  59.26600  -15.05100 1.000 57.00428  ?  1768 SER   A CA  1 
ATOM   13748 C  C   . SER   A 1 1770 ? -78.92500  58.71400  -15.96900 1.000 68.94335  ?  1768 SER   A C   1 
ATOM   13749 O  O   . SER   A 1 1770 ? -80.11500  58.98300  -15.76200 1.000 58.92748  ?  1768 SER   A O   1 
ATOM   13750 C  CB  . SER   A 1 1770 ? -77.18200  60.49900  -15.67300 1.000 53.69710  ?  1768 SER   A CB  1 
ATOM   13751 O  OG  . SER   A 1 1770 ? -77.18600  60.43400  -17.08900 1.000 73.39797  ?  1768 SER   A OG  1 
ATOM   13752 N  N   . ARG   A 1 1771 ? -78.53800  57.94300  -16.99000 1.000 63.66183  ?  1769 ARG   A N   1 
ATOM   13753 C  CA  . ARG   A 1 1771 ? -79.53300  57.30600  -17.84500 1.000 52.50616  ?  1769 ARG   A CA  1 
ATOM   13754 C  C   . ARG   A 1 1771 ? -80.35000  56.28000  -17.07300 1.000 56.29886  ?  1769 ARG   A C   1 
ATOM   13755 O  O   . ARG   A 1 1771 ? -81.53400  56.08100  -17.36700 1.000 70.20641  ?  1769 ARG   A O   1 
ATOM   13756 C  CB  . ARG   A 1 1771 ? -78.86000  56.65000  -19.05100 1.000 57.64685  ?  1769 ARG   A CB  1 
ATOM   13757 C  CG  . ARG   A 1 1771 ? -77.85000  57.53300  -19.75700 1.000 59.40125  ?  1769 ARG   A CG  1 
ATOM   13758 C  CD  . ARG   A 1 1771 ? -78.29500  57.93500  -21.14800 1.000 74.97843  ?  1769 ARG   A CD  1 
ATOM   13759 N  NE  . ARG   A 1 1771 ? -77.23500  58.65200  -21.84600 1.000 80.25252  ?  1769 ARG   A NE  1 
ATOM   13760 C  CZ  . ARG   A 1 1771 ? -76.25900  58.06600  -22.52600 1.000 81.06305  ?  1769 ARG   A CZ  1 
ATOM   13761 N  NH1 . ARG   A 1 1771 ? -76.19500  56.75000  -22.64700 1.000 78.04292  ?  1769 ARG   A NH1 1 
ATOM   13762 N  NH2 . ARG   A 1 1771 ? -75.32400  58.81900  -23.09900 1.000 106.00653 ?  1769 ARG   A NH2 1 
ATOM   13763 N  N   . LEU   A 1 1772 ? -79.73900  55.62200  -16.08800 1.000 50.25638  ?  1770 LEU   A N   1 
ATOM   13764 C  CA  . LEU   A 1 1772 ? -80.48500  54.68800  -15.25400 1.000 44.96713  ?  1770 LEU   A CA  1 
ATOM   13765 C  C   . LEU   A 1 1772 ? -81.44700  55.42300  -14.33000 1.000 61.43076  ?  1770 LEU   A C   1 
ATOM   13766 O  O   . LEU   A 1 1772 ? -82.54900  54.93400  -14.05400 1.000 64.99236  ?  1770 LEU   A O   1 
ATOM   13767 C  CB  . LEU   A 1 1772 ? -79.51800  53.82800  -14.44300 1.000 54.44668  ?  1770 LEU   A CB  1 
ATOM   13768 C  CG  . LEU   A 1 1772 ? -78.91200  52.61200  -15.13800 1.000 57.61011  ?  1770 LEU   A CG  1 
ATOM   13769 C  CD1 . LEU   A 1 1772 ? -77.70800  52.12700  -14.35300 1.000 60.33829  ?  1770 LEU   A CD1 1 
ATOM   13770 C  CD2 . LEU   A 1 1772 ? -79.94800  51.51100  -15.28100 1.000 40.42656  ?  1770 LEU   A CD2 1 
ATOM   13771 N  N   . GLN   A 1 1773 ? -81.04500  56.59800  -13.83600 1.000 60.51822  ?  1771 GLN   A N   1 
ATOM   13772 C  CA  . GLN   A 1 1773 ? -81.91600  57.37000  -12.95500 1.000 59.17271  ?  1771 GLN   A CA  1 
ATOM   13773 C  C   . GLN   A 1 1773 ? -83.14600  57.87300  -13.70000 1.000 71.17073  ?  1771 GLN   A C   1 
ATOM   13774 O  O   . GLN   A 1 1773 ? -84.24400  57.93400  -13.13300 1.000 76.68638  ?  1771 GLN   A O   1 
ATOM   13775 C  CB  . GLN   A 1 1773 ? -81.13900  58.53700  -12.34300 1.000 69.21688  ?  1771 GLN   A CB  1 
ATOM   13776 C  CG  . GLN   A 1 1773 ? -82.00600  59.58500  -11.65600 1.000 67.33466  ?  1771 GLN   A CG  1 
ATOM   13777 C  CD  . GLN   A 1 1773 ? -82.14600  60.85200  -12.48000 1.000 86.92074  ?  1771 GLN   A CD  1 
ATOM   13778 O  OE1 . GLN   A 1 1773 ? -81.22700  61.24000  -13.20200 1.000 81.92063  ?  1771 GLN   A OE1 1 
ATOM   13779 N  NE2 . GLN   A 1 1773 ? -83.30300  61.50100  -12.38000 1.000 62.81636  ?  1771 GLN   A NE2 1 
ATOM   13780 N  N   . ARG   A 1 1774 ? -82.98600  58.22700  -14.97700 1.000 65.79587  ?  1772 ARG   A N   1 
ATOM   13781 C  CA  . ARG   A 1 1774 ? -84.10600  58.71300  -15.77100 1.000 56.15182  ?  1772 ARG   A CA  1 
ATOM   13782 C  C   . ARG   A 1 1774 ? -85.13600  57.63200  -16.07100 1.000 55.02224  ?  1772 ARG   A C   1 
ATOM   13783 O  O   . ARG   A 1 1774 ? -86.23600  57.96400  -16.52600 1.000 72.24859  ?  1772 ARG   A O   1 
ATOM   13784 C  CB  . ARG   A 1 1774 ? -83.59400  59.32100  -17.07700 1.000 62.07909  ?  1772 ARG   A CB  1 
ATOM   13785 C  CG  . ARG   A 1 1774 ? -82.79100  60.59400  -16.88400 1.000 59.84679  ?  1772 ARG   A CG  1 
ATOM   13786 C  CD  . ARG   A 1 1774 ? -82.65000  61.35600  -18.18900 1.000 54.16009  ?  1772 ARG   A CD  1 
ATOM   13787 N  NE  . ARG   A 1 1774 ? -81.26000  61.43200  -18.62000 1.000 68.15237  ?  1772 ARG   A NE  1 
ATOM   13788 C  CZ  . ARG   A 1 1774 ? -80.77400  60.82700  -19.69600 1.000 79.27691  ?  1772 ARG   A CZ  1 
ATOM   13789 N  NH1 . ARG   A 1 1774 ? -81.54700  60.10300  -20.48900 1.000 85.00492  ?  1772 ARG   A NH1 1 
ATOM   13790 N  NH2 . ARG   A 1 1774 ? -79.48200  60.95300  -19.98200 1.000 64.84215  ?  1772 ARG   A NH2 1 
ATOM   13791 N  N   . ILE   A 1 1775 ? -84.81800  56.36000  -15.83500 1.000 42.20705  ?  1773 ILE   A N   1 
ATOM   13792 C  CA  . ILE   A 1 1775 ? -85.79800  55.28900  -15.97700 1.000 50.66098  ?  1773 ILE   A CA  1 
ATOM   13793 C  C   . ILE   A 1 1775 ? -86.03200  54.64700  -14.61600 1.000 52.03065  ?  1773 ILE   A C   1 
ATOM   13794 O  O   . ILE   A 1 1775 ? -86.41400  53.47400  -14.52600 1.000 45.85857  ?  1773 ILE   A O   1 
ATOM   13795 C  CB  . ILE   A 1 1775 ? -85.35300  54.25000  -17.02200 1.000 42.65833  ?  1773 ILE   A CB  1 
ATOM   13796 C  CG1 . ILE   A 1 1775 ? -83.93000  53.77800  -16.74400 1.000 51.12028  ?  1773 ILE   A CG1 1 
ATOM   13797 C  CG2 . ILE   A 1 1775 ? -85.43400  54.83400  -18.41800 1.000 41.78309  ?  1773 ILE   A CG2 1 
ATOM   13798 C  CD1 . ILE   A 1 1775 ? -83.41300  52.81400  -17.77800 1.000 39.71555  ?  1773 ILE   A CD1 1 
ATOM   13799 N  N   . ASN   A 1 1776 ? -85.79700  55.41900  -13.55100 1.000 44.39279  ?  1774 ASN   A N   1 
ATOM   13800 C  CA  . ASN   A 1 1776 ? -86.07800  55.00600  -12.17300 1.000 54.83128  ?  1774 ASN   A CA  1 
ATOM   13801 C  C   . ASN   A 1 1776 ? -85.29500  53.75000  -11.78800 1.000 61.89504  ?  1774 ASN   A C   1 
ATOM   13802 O  O   . ASN   A 1 1776 ? -85.85000  52.76600  -11.29400 1.000 56.06497  ?  1774 ASN   A O   1 
ATOM   13803 C  CB  . ASN   A 1 1776 ? -87.58100  54.81000  -11.95400 1.000 64.46170  ?  1774 ASN   A CB  1 
ATOM   13804 C  CG  . ASN   A 1 1776 ? -88.32400  56.12500  -11.79800 1.000 69.83049  ?  1774 ASN   A CG  1 
ATOM   13805 O  OD1 . ASN   A 1 1776 ? -88.71200  56.50400  -10.69300 1.000 81.15645  ?  1774 ASN   A OD1 1 
ATOM   13806 N  ND2 . ASN   A 1 1776 ? -88.52300  56.82900  -12.90700 1.000 72.76738  ?  1774 ASN   A ND2 1 
ATOM   13807 N  N   . TRP   A 1 1777 ? -83.98300  53.79600  -12.01600 1.000 63.55586  ?  1775 TRP   A N   1 
ATOM   13808 C  CA  . TRP   A 1 1777 ? -83.05800  52.73600  -11.61400 1.000 55.83526  ?  1775 TRP   A CA  1 
ATOM   13809 C  C   . TRP   A 1 1777 ? -81.87900  53.41700  -10.92700 1.000 61.15154  ?  1775 TRP   A C   1 
ATOM   13810 O  O   . TRP   A 1 1777 ? -81.02300  54.00500  -11.59300 1.000 68.33970  ?  1775 TRP   A O   1 
ATOM   13811 C  CB  . TRP   A 1 1777 ? -82.59700  51.90800  -12.81100 1.000 52.50471  ?  1775 TRP   A CB  1 
ATOM   13812 C  CG  . TRP   A 1 1777 ? -83.57600  50.86500  -13.26800 1.000 55.29568  ?  1775 TRP   A CG  1 
ATOM   13813 C  CD1 . TRP   A 1 1777 ? -84.22600  50.81900  -14.46900 1.000 54.02320  ?  1775 TRP   A CD1 1 
ATOM   13814 C  CD2 . TRP   A 1 1777 ? -84.01000  49.71500  -12.53200 1.000 49.23358  ?  1775 TRP   A CD2 1 
ATOM   13815 N  NE1 . TRP   A 1 1777 ? -85.03800  49.71100  -14.52500 1.000 60.44911  ?  1775 TRP   A NE1 1 
ATOM   13816 C  CE2 . TRP   A 1 1777 ? -84.92400  49.01800  -13.34800 1.000 51.52236  ?  1775 TRP   A CE2 1 
ATOM   13817 C  CE3 . TRP   A 1 1777 ? -83.71700  49.20900  -11.26300 1.000 58.43507  ?  1775 TRP   A CE3 1 
ATOM   13818 C  CZ2 . TRP   A 1 1777 ? -85.54600  47.84200  -12.93500 1.000 45.27356  ?  1775 TRP   A CZ2 1 
ATOM   13819 C  CZ3 . TRP   A 1 1777 ? -84.33500  48.04200  -10.85500 1.000 67.64559  ?  1775 TRP   A CZ3 1 
ATOM   13820 C  CH2 . TRP   A 1 1777 ? -85.23900  47.37200  -11.68800 1.000 57.61669  ?  1775 TRP   A CH2 1 
ATOM   13821 N  N   . THR   A 1 1778 ? -81.83300  53.34700  -9.60000  1.000 59.28812  ?  1776 THR   A N   1 
ATOM   13822 C  CA  . THR   A 1 1778 ? -80.80800  54.04000  -8.82900  1.000 72.85393  ?  1776 THR   A CA  1 
ATOM   13823 C  C   . THR   A 1 1778 ? -79.56600  53.16100  -8.72000  1.000 64.76749  ?  1776 THR   A C   1 
ATOM   13824 O  O   . THR   A 1 1778 ? -79.62700  52.05700  -8.17000  1.000 63.68385  ?  1776 THR   A O   1 
ATOM   13825 C  CB  . THR   A 1 1778 ? -81.33500  54.41600  -7.44400  1.000 67.84920  ?  1776 THR   A CB  1 
ATOM   13826 O  OG1 . THR   A 1 1778 ? -82.21700  53.39000  -6.96800  1.000 86.41228  ?  1776 THR   A OG1 1 
ATOM   13827 C  CG2 . THR   A 1 1778 ? -82.09000  55.73900  -7.50400  1.000 61.89216  ?  1776 THR   A CG2 1 
ATOM   13828 N  N   . MET   A 1 1779 ? -78.44200  53.65700  -9.24000  1.000 61.10203  ?  1777 MET   A N   1 
ATOM   13829 C  CA  . MET   A 1 1779 ? -77.17000  52.94700  -9.23600  1.000 65.12345  ?  1777 MET   A CA  1 
ATOM   13830 C  C   . MET   A 1 1779 ? -76.06400  53.87200  -8.75500  1.000 60.45982  ?  1777 MET   A C   1 
ATOM   13831 O  O   . MET   A 1 1779 ? -75.98200  55.02800  -9.18100  1.000 61.24959  ?  1777 MET   A O   1 
ATOM   13832 C  CB  . MET   A 1 1779 ? -76.83500  52.42600  -10.63300 1.000 67.27890  ?  1777 MET   A CB  1 
ATOM   13833 C  CG  . MET   A 1 1779 ? -75.54800  51.62700  -10.75300 1.000 67.54373  ?  1777 MET   A CG  1 
ATOM   13834 S  SD  . MET   A 1 1779 ? -74.61300  52.13400  -12.20500 1.000 68.43848  ?  1777 MET   A SD  1 
ATOM   13835 C  CE  . MET   A 1 1779 ? -73.53600  50.72700  -12.41600 1.000 59.71183  ?  1777 MET   A CE  1 
ATOM   13836 N  N   . VAL   A 1 1780 ? -75.20500  53.35700  -7.88400  1.000 63.37654  ?  1778 VAL   A N   1 
ATOM   13837 C  CA  . VAL   A 1 1780 ? -74.11500  54.14200  -7.31800  1.000 72.84106  ?  1778 VAL   A CA  1 
ATOM   13838 C  C   . VAL   A 1 1780 ? -72.87900  53.98100  -8.19000  1.000 68.20689  ?  1778 VAL   A C   1 
ATOM   13839 O  O   . VAL   A 1 1780 ? -72.49300  52.85900  -8.54000  1.000 63.15425  ?  1778 VAL   A O   1 
ATOM   13840 C  CB  . VAL   A 1 1780 ? -73.82500  53.72300  -5.86900  1.000 70.88538  ?  1778 VAL   A CB  1 
ATOM   13841 C  CG1 . VAL   A 1 1780 ? -72.98500  54.78600  -5.17100  1.000 74.88429  ?  1778 VAL   A CG1 1 
ATOM   13842 C  CG2 . VAL   A 1 1780 ? -75.12400  53.48800  -5.12300  1.000 56.20833  ?  1778 VAL   A CG2 1 
ATOM   13843 N  N   . ILE   A 1 1781 ? -72.25500  55.10900  -8.53700  1.000 65.48287  ?  1779 ILE   A N   1 
ATOM   13844 C  CA  . ILE   A 1 1781 ? -71.05900  55.07700  -9.37300  1.000 65.66472  ?  1779 ILE   A CA  1 
ATOM   13845 C  C   . ILE   A 1 1781 ? -69.92700  54.35700  -8.65100  1.000 82.13455  ?  1779 ILE   A C   1 
ATOM   13846 O  O   . ILE   A 1 1781 ? -69.12500  53.64700  -9.27400  1.000 78.89406  ?  1779 ILE   A O   1 
ATOM   13847 C  CB  . ILE   A 1 1781 ? -70.66300  56.50800  -9.78100  1.000 51.86168  ?  1779 ILE   A CB  1 
ATOM   13848 C  CG1 . ILE   A 1 1781 ? -71.76500  57.13500  -10.63500 1.000 45.59494  ?  1779 ILE   A CG1 1 
ATOM   13849 C  CG2 . ILE   A 1 1781 ? -69.33900  56.51100  -10.53100 1.000 56.55206  ?  1779 ILE   A CG2 1 
ATOM   13850 C  CD1 . ILE   A 1 1781 ? -71.70500  58.64000  -10.68800 1.000 54.91776  ?  1779 ILE   A CD1 1 
ATOM   13851 N  N   . ASN   A 1 1782 ? -69.85200  54.51700  -7.32500  1.000 92.73794  ?  1780 ASN   A N   1 
ATOM   13852 C  CA  . ASN   A 1 1782 ? -68.83600  53.82300  -6.53900  1.000 83.24948  ?  1780 ASN   A CA  1 
ATOM   13853 C  C   . ASN   A 1 1782 ? -68.96100  52.31200  -6.69200  1.000 88.80845  ?  1780 ASN   A C   1 
ATOM   13854 O  O   . ASN   A 1 1782 ? -67.95100  51.60100  -6.75800  1.000 92.15408  ?  1780 ASN   A O   1 
ATOM   13855 C  CB  . ASN   A 1 1782 ? -68.94700  54.23500  -5.06600  1.000 79.72498  ?  1780 ASN   A CB  1 
ATOM   13856 C  CG  . ASN   A 1 1782 ? -67.91900  53.54900  -4.17000  1.000 89.15795  ?  1780 ASN   A CG  1 
ATOM   13857 O  OD1 . ASN   A 1 1782 ? -67.87600  52.32300  -4.06000  1.000 101.87495 ?  1780 ASN   A OD1 1 
ATOM   13858 N  ND2 . ASN   A 1 1782 ? -67.08400  54.35300  -3.52200  1.000 86.31390  ?  1780 ASN   A ND2 1 
ATOM   13859 N  N   . HIS   A 1 1783 ? -70.19300  51.80600  -6.76100  1.000 76.27240  ?  1781 HIS   A N   1 
ATOM   13860 C  CA  . HIS   A 1 1783 ? -70.40000  50.36600  -6.84400  1.000 73.67491  ?  1781 HIS   A CA  1 
ATOM   13861 C  C   . HIS   A 1 1783 ? -69.75300  49.77200  -8.08900  1.000 70.12418  ?  1781 HIS   A C   1 
ATOM   13862 O  O   . HIS   A 1 1783 ? -69.38700  48.59200  -8.09400  1.000 82.44758  ?  1781 HIS   A O   1 
ATOM   13863 C  CB  . HIS   A 1 1783 ? -71.89600  50.06000  -6.82800  1.000 85.27493  ?  1781 HIS   A CB  1 
ATOM   13864 C  CG  . HIS   A 1 1783 ? -72.53100  50.19800  -5.48100  1.000 83.86655  ?  1781 HIS   A CG  1 
ATOM   13865 N  ND1 . HIS   A 1 1783 ? -73.86700  49.94200  -5.26200  1.000 89.20432  ?  1781 HIS   A ND1 1 
ATOM   13866 C  CD2 . HIS   A 1 1783 ? -72.01600  50.56500  -4.28400  1.000 81.87011  ?  1781 HIS   A CD2 1 
ATOM   13867 C  CE1 . HIS   A 1 1783 ? -74.14900  50.14700  -3.98800  1.000 84.77803  ?  1781 HIS   A CE1 1 
ATOM   13868 N  NE2 . HIS   A 1 1783 ? -73.04300  50.52500  -3.37200  1.000 96.08337  ?  1781 HIS   A NE2 1 
ATOM   13869 N  N   . LEU   A 1 1784 ? -69.60200  50.57000  -9.14800  1.000 65.53875  ?  1782 LEU   A N   1 
ATOM   13870 C  CA  . LEU   A 1 1784 ? -69.04400  50.06600  -10.39800 1.000 81.77767  ?  1782 LEU   A CA  1 
ATOM   13871 C  C   . LEU   A 1 1784 ? -67.57600  49.67600  -10.27100 1.000 92.71577  ?  1782 LEU   A C   1 
ATOM   13872 O  O   . LEU   A 1 1784 ? -67.08700  48.89000  -11.08900 1.000 93.90647  ?  1782 LEU   A O   1 
ATOM   13873 C  CB  . LEU   A 1 1784 ? -69.21800  51.10900  -11.50500 1.000 74.23164  ?  1782 LEU   A CB  1 
ATOM   13874 C  CG  . LEU   A 1 1784 ? -69.36900  50.57900  -12.93300 1.000 72.75150  ?  1782 LEU   A CG  1 
ATOM   13875 C  CD1 . LEU   A 1 1784 ? -70.24400  49.33400  -12.96600 1.000 70.23795  ?  1782 LEU   A CD1 1 
ATOM   13876 C  CD2 . LEU   A 1 1784 ? -69.94000  51.66000  -13.83500 1.000 68.44806  ?  1782 LEU   A CD2 1 
ATOM   13877 N  N   . PHE   A 1 1785 ? -66.86400  50.20400  -9.27500  1.000 105.42029 ?  1783 PHE   A N   1 
ATOM   13878 C  CA  . PHE   A 1 1785 ? -65.48200  49.81000  -9.02800  1.000 93.58347  ?  1783 PHE   A CA  1 
ATOM   13879 C  C   . PHE   A 1 1785 ? -65.37600  48.58800  -8.12900  1.000 93.94366  ?  1783 PHE   A C   1 
ATOM   13880 O  O   . PHE   A 1 1785 ? -64.36800  47.87400  -8.18900  1.000 104.41792 ?  1783 PHE   A O   1 
ATOM   13881 C  CB  . PHE   A 1 1785 ? -64.70400  50.97700  -8.41000  1.000 87.31334  ?  1783 PHE   A CB  1 
ATOM   13882 C  CG  . PHE   A 1 1785 ? -65.17400  52.32400  -8.87700  1.000 97.07117  ?  1783 PHE   A CG  1 
ATOM   13883 C  CD1 . PHE   A 1 1785 ? -65.15100  52.65200  -10.21900 1.000 98.82162  ?  1783 PHE   A CD1 1 
ATOM   13884 C  CD2 . PHE   A 1 1785 ? -65.67000  53.24800  -7.98300  1.000 96.99167  ?  1783 PHE   A CD2 1 
ATOM   13885 C  CE1 . PHE   A 1 1785 ? -65.59000  53.87800  -10.66200 1.000 100.95470 ?  1783 PHE   A CE1 1 
ATOM   13886 C  CE2 . PHE   A 1 1785 ? -66.11700  54.47500  -8.42200  1.000 106.20507 ?  1783 PHE   A CE2 1 
ATOM   13887 C  CZ  . PHE   A 1 1785 ? -66.07600  54.79200  -9.76100  1.000 111.66978 ?  1783 PHE   A CZ  1 
ATOM   13888 N  N   . LEU   A 1 1786 ? -66.38900  48.33200  -7.30600  1.000 97.23551  ?  1784 LEU   A N   1 
ATOM   13889 C  CA  . LEU   A 1 1786 ? -66.44800  47.11300  -6.51200  1.000 103.97596 ?  1784 LEU   A CA  1 
ATOM   13890 C  C   . LEU   A 1 1786 ? -67.12800  45.97500  -7.26100  1.000 96.23122  ?  1784 LEU   A C   1 
ATOM   13891 O  O   . LEU   A 1 1786 ? -66.76700  44.80800  -7.06700  1.000 92.20010  ?  1784 LEU   A O   1 
ATOM   13892 C  CB  . LEU   A 1 1786 ? -67.18400  47.38100  -5.19500  1.000 105.16826 ?  1784 LEU   A CB  1 
ATOM   13893 C  CG  . LEU   A 1 1786 ? -66.85100  48.69400  -4.47500  1.000 97.54650  ?  1784 LEU   A CG  1 
ATOM   13894 C  CD1 . LEU   A 1 1786 ? -67.63100  48.80500  -3.17300  1.000 98.28923  ?  1784 LEU   A CD1 1 
ATOM   13895 C  CD2 . LEU   A 1 1786 ? -65.35300  48.82300  -4.21700  1.000 85.87380  ?  1784 LEU   A CD2 1 
ATOM   13896 N  N   . TYR   A 1 1787 ? -68.09800  46.29500  -8.11600  1.000 97.66263  ?  1785 TYR   A N   1 
ATOM   13897 C  CA  . TYR   A 1 1787 ? -68.81600  45.31200  -8.92800  1.000 89.62744  ?  1785 TYR   A CA  1 
ATOM   13898 C  C   . TYR   A 1 1787 ? -68.77000  45.78600  -10.37400 1.000 88.82658  ?  1785 TYR   A C   1 
ATOM   13899 O  O   . TYR   A 1 1787 ? -69.72100  46.40400  -10.87100 1.000 83.07119  ?  1785 TYR   A O   1 
ATOM   13900 C  CB  . TYR   A 1 1787 ? -70.25300  45.13700  -8.43800  1.000 86.66384  ?  1785 TYR   A CB  1 
ATOM   13901 C  CG  . TYR   A 1 1787 ? -70.37700  45.09900  -6.93400  1.000 94.07434  ?  1785 TYR   A CG  1 
ATOM   13902 C  CD1 . TYR   A 1 1787 ? -69.89500  44.02000  -6.20600  1.000 91.11308  ?  1785 TYR   A CD1 1 
ATOM   13903 C  CD2 . TYR   A 1 1787 ? -70.97000  46.14600  -6.24000  1.000 91.19361  ?  1785 TYR   A CD2 1 
ATOM   13904 C  CE1 . TYR   A 1 1787 ? -70.00400  43.98100  -4.82800  1.000 92.87676  ?  1785 TYR   A CE1 1 
ATOM   13905 C  CE2 . TYR   A 1 1787 ? -71.08400  46.11700  -4.86200  1.000 95.66240  ?  1785 TYR   A CE2 1 
ATOM   13906 C  CZ  . TYR   A 1 1787 ? -70.59800  45.03200  -4.16100  1.000 94.62449  ?  1785 TYR   A CZ  1 
ATOM   13907 O  OH  . TYR   A 1 1787 ? -70.70700  44.99200  -2.78900  1.000 82.10511  ?  1785 TYR   A OH  1 
ATOM   13908 N  N   . PRO   A 1 1788 ? -67.67000  45.51600  -11.08000 1.000 91.39066  ?  1786 PRO   A N   1 
ATOM   13909 C  CA  . PRO   A 1 1788 ? -67.48800  46.04900  -12.43600 1.000 89.04233  ?  1786 PRO   A CA  1 
ATOM   13910 C  C   . PRO   A 1 1788 ? -68.22300  45.29100  -13.53000 1.000 86.53936  ?  1786 PRO   A C   1 
ATOM   13911 O  O   . PRO   A 1 1788 ? -68.04000  45.61900  -14.70500 1.000 92.47754  ?  1786 PRO   A O   1 
ATOM   13912 C  CB  . PRO   A 1 1788 ? -65.96500  45.94400  -12.64400 1.000 90.19167  ?  1786 PRO   A CB  1 
ATOM   13913 C  CG  . PRO   A 1 1788 ? -65.38400  45.57800  -11.30300 1.000 89.30921  ?  1786 PRO   A CG  1 
ATOM   13914 C  CD  . PRO   A 1 1788 ? -66.46100  44.83900  -10.59300 1.000 86.09166  ?  1786 PRO   A CD  1 
ATOM   13915 N  N   . THR   A 1 1789 ? -69.02900  44.29000  -13.19600 1.000 84.81330  ?  1787 THR   A N   1 
ATOM   13916 C  CA  . THR   A 1 1789 ? -69.81000  43.55600  -14.17900 1.000 93.68209  ?  1787 THR   A CA  1 
ATOM   13917 C  C   . THR   A 1 1789 ? -71.29800  43.80300  -13.96100 1.000 91.38692  ?  1787 THR   A C   1 
ATOM   13918 O  O   . THR   A 1 1789 ? -71.72900  44.22700  -12.88500 1.000 91.20955  ?  1787 THR   A O   1 
ATOM   13919 C  CB  . THR   A 1 1789 ? -69.50800  42.05500  -14.11300 1.000 92.83871  ?  1787 THR   A CB  1 
ATOM   13920 O  OG1 . THR   A 1 1789 ? -70.53900  41.38800  -13.37500 1.000 97.76347  ?  1787 THR   A OG1 1 
ATOM   13921 C  CG2 . THR   A 1 1789 ? -68.17500  41.81600  -13.43500 1.000 78.68711  ?  1787 THR   A CG2 1 
ATOM   13922 N  N   . ILE   A 1 1790 ? -72.08300  43.53600  -15.00900 1.000 92.11191  ?  1788 ILE   A N   1 
ATOM   13923 C  CA  . ILE   A 1 1790 ? -73.52600  43.76100  -14.94300 1.000 85.12418  ?  1788 ILE   A CA  1 
ATOM   13924 C  C   . ILE   A 1 1790 ? -74.15300  42.89000  -13.86200 1.000 91.95048  ?  1788 ILE   A C   1 
ATOM   13925 O  O   . ILE   A 1 1790 ? -74.90800  43.37200  -13.00800 1.000 91.55628  ?  1788 ILE   A O   1 
ATOM   13926 C  CB  . ILE   A 1 1790 ? -74.17500  43.50200  -16.31400 1.000 77.89195  ?  1788 ILE   A CB  1 
ATOM   13927 C  CG1 . ILE   A 1 1790 ? -73.62700  44.47200  -17.35900 1.000 81.31582  ?  1788 ILE   A CG1 1 
ATOM   13928 C  CG2 . ILE   A 1 1790 ? -75.68700  43.61200  -16.22100 1.000 81.22943  ?  1788 ILE   A CG2 1 
ATOM   13929 C  CD1 . ILE   A 1 1790 ? -74.34600  44.39500  -18.67700 1.000 79.84821  ?  1788 ILE   A CD1 1 
ATOM   13930 N  N   . GLU   A 1 1791 ? -73.84900  41.59000  -13.88300 1.000 88.89205  ?  1789 GLU   A N   1 
ATOM   13931 C  CA  . GLU   A 1 1791 ? -74.43600  40.67200  -12.91300 1.000 90.12726  ?  1789 GLU   A CA  1 
ATOM   13932 C  C   . GLU   A 1 1791 ? -73.94400  40.95100  -11.49800 1.000 81.45801  ?  1789 GLU   A C   1 
ATOM   13933 O  O   . GLU   A 1 1791 ? -74.66200  40.68000  -10.53000 1.000 82.13595  ?  1789 GLU   A O   1 
ATOM   13934 C  CB  . GLU   A 1 1791 ? -74.12100  39.22800  -13.30000 1.000 97.25638  ?  1789 GLU   A CB  1 
ATOM   13935 C  CG  . GLU   A 1 1791 ? -72.63500  38.93800  -13.37900 1.000 103.61701 ?  1789 GLU   A CG  1 
ATOM   13936 C  CD  . GLU   A 1 1791 ? -72.28200  37.56400  -12.85300 1.000 114.52348 ?  1789 GLU   A CD  1 
ATOM   13937 O  OE1 . GLU   A 1 1791 ? -73.05600  37.02400  -12.03600 1.000 104.74789 ?  1789 GLU   A OE1 1 
ATOM   13938 O  OE2 . GLU   A 1 1791 ? -71.21700  37.03600  -13.23300 1.000 114.62202 -1 1789 GLU   A OE2 1 
ATOM   13939 N  N   . GLN   A 1 1792 ? -72.72700  41.48300  -11.35700 1.000 83.79159  ?  1790 GLN   A N   1 
ATOM   13940 C  CA  . GLN   A 1 1792 ? -72.20400  41.79100  -10.03000 1.000 78.04827  ?  1790 GLN   A CA  1 
ATOM   13941 C  C   . GLN   A 1 1792 ? -72.90200  43.00400  -9.42900  1.000 90.25706  ?  1790 GLN   A C   1 
ATOM   13942 O  O   . GLN   A 1 1792 ? -73.13800  43.05500  -8.21700  1.000 86.79106  ?  1790 GLN   A O   1 
ATOM   13943 C  CB  . GLN   A 1 1792 ? -70.69700  42.02700  -10.10200 1.000 92.78130  ?  1790 GLN   A CB  1 
ATOM   13944 C  CG  . GLN   A 1 1792 ? -69.86500  40.76300  -10.12200 1.000 100.37110 ?  1790 GLN   A CG  1 
ATOM   13945 C  CD  . GLN   A 1 1792 ? -68.48200  40.98100  -9.54800  1.000 96.48821  ?  1790 GLN   A CD  1 
ATOM   13946 O  OE1 . GLN   A 1 1792 ? -67.53500  41.27600  -10.27700 1.000 83.92744  ?  1790 GLN   A OE1 1 
ATOM   13947 N  NE2 . GLN   A 1 1792 ? -68.35900  40.84200  -8.23300  1.000 91.55268  ?  1790 GLN   A NE2 1 
ATOM   13948 N  N   . ILE   A 1 1793 ? -73.23500  43.99300  -10.26500 1.000 89.14430  ?  1791 ILE   A N   1 
ATOM   13949 C  CA  . ILE   A 1 1793 ? -73.91200  45.19900  -9.79700  1.000 80.58406  ?  1791 ILE   A CA  1 
ATOM   13950 C  C   . ILE   A 1 1793 ? -75.42600  45.10500  -9.92700  1.000 84.82812  ?  1791 ILE   A C   1 
ATOM   13951 O  O   . ILE   A 1 1793 ? -76.13800  45.99000  -9.42600  1.000 85.07639  ?  1791 ILE   A O   1 
ATOM   13952 C  CB  . ILE   A 1 1793 ? -73.37500  46.42700  -10.56000 1.000 68.48043  ?  1791 ILE   A CB  1 
ATOM   13953 C  CG1 . ILE   A 1 1793 ? -73.47600  47.67700  -9.69300  1.000 75.28323  ?  1791 ILE   A CG1 1 
ATOM   13954 C  CG2 . ILE   A 1 1793 ? -74.11400  46.61600  -11.88200 1.000 79.94808  ?  1791 ILE   A CG2 1 
ATOM   13955 C  CD1 . ILE   A 1 1793 ? -72.34900  48.62400  -9.92200  1.000 77.78000  ?  1791 ILE   A CD1 1 
ATOM   13956 N  N   . ALA   A 1 1794 ? -75.93900  44.05700  -10.57100 1.000 70.57672  ?  1792 ALA   A N   1 
ATOM   13957 C  CA  . ALA   A 1 1794 ? -77.38300  43.86700  -10.70600 1.000 74.91692  ?  1792 ALA   A CA  1 
ATOM   13958 C  C   . ALA   A 1 1794 ? -78.14000  43.93300  -9.38300  1.000 85.47329  ?  1792 ALA   A C   1 
ATOM   13959 O  O   . ALA   A 1 1794 ? -79.13300  44.67400  -9.31000  1.000 86.86106  ?  1792 ALA   A O   1 
ATOM   13960 C  CB  . ALA   A 1 1794 ? -77.65400  42.54100  -11.43000 1.000 91.84876  ?  1792 ALA   A CB  1 
ATOM   13961 N  N   . PRO   A 1 1795 ? -77.74800  43.22200  -8.31700  1.000 87.83192  ?  1793 PRO   A N   1 
ATOM   13962 C  CA  . PRO   A 1 1795 ? -78.52700  43.30200  -7.07100  1.000 89.14409  ?  1793 PRO   A CA  1 
ATOM   13963 C  C   . PRO   A 1 1795 ? -78.38600  44.62500  -6.33800  1.000 76.62284  ?  1793 PRO   A C   1 
ATOM   13964 O  O   . PRO   A 1 1795 ? -78.99600  44.78900  -5.27600  1.000 86.78909  ?  1793 PRO   A O   1 
ATOM   13965 C  CB  . PRO   A 1 1795 ? -77.95600  42.15100  -6.23400  1.000 89.74816  ?  1793 PRO   A CB  1 
ATOM   13966 C  CG  . PRO   A 1 1795 ? -76.54400  42.07100  -6.66500  1.000 88.20553  ?  1793 PRO   A CG  1 
ATOM   13967 C  CD  . PRO   A 1 1795 ? -76.56300  42.35800  -8.14600  1.000 83.92750  ?  1793 PRO   A CD  1 
ATOM   13968 N  N   . PHE   A 1 1796 ? -77.61100  45.57300  -6.86700  1.000 74.02446  ?  1794 PHE   A N   1 
ATOM   13969 C  CA  . PHE   A 1 1796 ? -77.32900  46.81500  -6.16600  1.000 83.57881  ?  1794 PHE   A CA  1 
ATOM   13970 C  C   . PHE   A 1 1796 ? -78.00700  48.03100  -6.77100  1.000 80.63150  ?  1794 PHE   A C   1 
ATOM   13971 O  O   . PHE   A 1 1796 ? -78.16200  49.03900  -6.07400  1.000 77.33397  ?  1794 PHE   A O   1 
ATOM   13972 C  CB  . PHE   A 1 1796 ? -75.81500  47.05400  -6.11000  1.000 87.96838  ?  1794 PHE   A CB  1 
ATOM   13973 C  CG  . PHE   A 1 1796 ? -75.09100  46.04800  -5.27100  1.000 96.14924  ?  1794 PHE   A CG  1 
ATOM   13974 C  CD1 . PHE   A 1 1796 ? -75.05000  46.17700  -3.89200  1.000 90.34701  ?  1794 PHE   A CD1 1 
ATOM   13975 C  CD2 . PHE   A 1 1796 ? -74.48100  44.95200  -5.85700  1.000 96.53700  ?  1794 PHE   A CD2 1 
ATOM   13976 C  CE1 . PHE   A 1 1796 ? -74.39400  45.24100  -3.11500  1.000 74.55604  ?  1794 PHE   A CE1 1 
ATOM   13977 C  CE2 . PHE   A 1 1796 ? -73.82600  44.01300  -5.08700  1.000 93.89087  ?  1794 PHE   A CE2 1 
ATOM   13978 C  CZ  . PHE   A 1 1796 ? -73.78200  44.15700  -3.71400  1.000 84.52565  ?  1794 PHE   A CZ  1 
ATOM   13979 N  N   . VAL   A 1 1797 ? -78.41500  47.97200  -8.03300  1.000 79.79579  ?  1795 VAL   A N   1 
ATOM   13980 C  CA  . VAL   A 1 1797 ? -79.21100  49.05400  -8.59100  1.000 66.97187  ?  1795 VAL   A CA  1 
ATOM   13981 C  C   . VAL   A 1 1797 ? -80.65300  48.82500  -8.14300  1.000 75.78151  ?  1795 VAL   A C   1 
ATOM   13982 O  O   . VAL   A 1 1797 ? -81.24800  47.77600  -8.41200  1.000 75.11885  ?  1795 VAL   A O   1 
ATOM   13983 C  CB  . VAL   A 1 1797 ? -79.05800  49.14200  -10.12100 1.000 66.93304  ?  1795 VAL   A CB  1 
ATOM   13984 C  CG1 . VAL   A 1 1797 ? -77.60500  48.97100  -10.49300 1.000 79.48772  ?  1795 VAL   A CG1 1 
ATOM   13985 C  CG2 . VAL   A 1 1797 ? -79.86200  48.12700  -10.85700 1.000 69.86282  ?  1795 VAL   A CG2 1 
ATOM   13986 N  N   . THR   A 1 1798 ? -81.17500  49.75800  -7.35700  1.000 85.04095  ?  1796 THR   A N   1 
ATOM   13987 C  CA  . THR   A 1 1798 ? -82.49800  49.62100  -6.76900  1.000 80.80206  ?  1796 THR   A CA  1 
ATOM   13988 C  C   . THR   A 1 1798 ? -83.52100  50.36000  -7.61800  1.000 77.93586  ?  1796 THR   A C   1 
ATOM   13989 O  O   . THR   A 1 1798 ? -83.19000  51.26100  -8.39300  1.000 74.64526  ?  1796 THR   A O   1 
ATOM   13990 C  CB  . THR   A 1 1798 ? -82.52500  50.14600  -5.32700  1.000 75.58282  ?  1796 THR   A CB  1 
ATOM   13991 O  OG1 . THR   A 1 1798 ? -82.29800  51.56200  -5.31500  1.000 78.97367  ?  1796 THR   A OG1 1 
ATOM   13992 C  CG2 . THR   A 1 1798 ? -81.44900  49.46500  -4.50100  1.000 72.61398  ?  1796 THR   A CG2 1 
ATOM   13993 N  N   . SER   A 1 1799 ? -84.77300  49.94600  -7.48200  1.000 77.58373  ?  1797 SER   A N   1 
ATOM   13994 C  CA  . SER   A 1 1799 ? -85.85800  50.59200  -8.19500  1.000 80.08697  ?  1797 SER   A CA  1 
ATOM   13995 C  C   . SER   A 1 1799 ? -86.42200  51.73200  -7.36100  1.000 90.66205  ?  1797 SER   A C   1 
ATOM   13996 O  O   . SER   A 1 1799 ? -86.34100  51.72900  -6.13000  1.000 91.63448  ?  1797 SER   A O   1 
ATOM   13997 C  CB  . SER   A 1 1799 ? -86.96600  49.59400  -8.52800  1.000 69.69941  ?  1797 SER   A CB  1 
ATOM   13998 O  OG  . SER   A 1 1799 ? -87.84700  50.14800  -9.48600  1.000 74.97458  ?  1797 SER   A OG  1 
ATOM   13999 N  N   . GLU   A 1 1800 ? -86.99000  52.71500  -8.04900  1.000 88.64353  ?  1798 GLU   A N   1 
ATOM   14000 C  CA  . GLU   A 1 1800 ? -87.60300  53.87200  -7.40400  1.000 92.54743  ?  1798 GLU   A CA  1 
ATOM   14001 C  C   . GLU   A 1 1800 ? -89.10800  53.62900  -7.39100  1.000 92.24209  ?  1798 GLU   A C   1 
ATOM   14002 O  O   . GLU   A 1 1800 ? -89.80900  53.92000  -8.36000  1.000 105.34989 ?  1798 GLU   A O   1 
ATOM   14003 C  CB  . GLU   A 1 1800 ? -87.23500  55.15800  -8.13200  1.000 89.00865  ?  1798 GLU   A CB  1 
ATOM   14004 C  CG  . GLU   A 1 1800 ? -85.85800  55.69600  -7.77700  1.000 102.89493 ?  1798 GLU   A CG  1 
ATOM   14005 C  CD  . GLU   A 1 1800 ? -85.79500  56.25700  -6.37100  1.000 118.77487 ?  1798 GLU   A CD  1 
ATOM   14006 O  OE1 . GLU   A 1 1800 ? -86.45600  57.28500  -6.11100  1.000 135.93421 ?  1798 GLU   A OE1 1 
ATOM   14007 O  OE2 . GLU   A 1 1800 ? -85.08800  55.66900  -5.52400  1.000 95.92715  ?  1798 GLU   A OE2 1 
ATOM   14008 N  N   . GLN   A 1 1801 ? -89.59900  53.07700  -6.28200  1.000 90.23486  ?  1799 GLN   A N   1 
ATOM   14009 C  CA  . GLN   A 1 1801 ? -91.01700  52.75900  -6.15000  1.000 99.13378  ?  1799 GLN   A CA  1 
ATOM   14010 C  C   . GLN   A 1 1801 ? -91.86200  54.01500  -6.32500  1.000 93.13495  ?  1799 GLN   A C   1 
ATOM   14011 O  O   . GLN   A 1 1801 ? -91.70400  54.99000  -5.58300  1.000 94.56915  ?  1799 GLN   A O   1 
ATOM   14012 C  CB  . GLN   A 1 1801 ? -91.28500  52.11900  -4.78900  1.000 93.56422  ?  1799 GLN   A CB  1 
ATOM   14013 C  CG  . GLN   A 1 1801 ? -90.53800  50.81400  -4.54900  1.000 97.45273  ?  1799 GLN   A CG  1 
ATOM   14014 C  CD  . GLN   A 1 1801 ? -91.10800  49.65900  -5.35000  1.000 109.20586 ?  1799 GLN   A CD  1 
ATOM   14015 O  OE1 . GLN   A 1 1801 ? -90.44100  49.10100  -6.22200  1.000 100.76304 ?  1799 GLN   A OE1 1 
ATOM   14016 N  NE2 . GLN   A 1 1801 ? -92.35000  49.29300  -5.05600  1.000 97.39842  ?  1799 GLN   A NE2 1 
ATOM   14017 N  N   . VAL   A 1 1802 ? -92.75700  53.99000  -7.31100  1.000 80.81574  ?  1800 VAL   A N   1 
ATOM   14018 C  CA  . VAL   A 1 1802 ? -93.58800  55.13900  -7.64700  1.000 77.14145  ?  1800 VAL   A CA  1 
ATOM   14019 C  C   . VAL   A 1 1802 ? -94.95400  54.96900  -7.00300  1.000 82.15904  ?  1800 VAL   A C   1 
ATOM   14020 O  O   . VAL   A 1 1802 ? -95.47500  53.85500  -6.87200  1.000 81.18106  ?  1800 VAL   A O   1 
ATOM   14021 C  CB  . VAL   A 1 1802 ? -93.72100  55.32100  -9.17500  1.000 67.11711  ?  1800 VAL   A CB  1 
ATOM   14022 C  CG1 . VAL   A 1 1802 ? -94.10300  56.75600  -9.51000  1.000 71.12587  ?  1800 VAL   A CG1 1 
ATOM   14023 C  CG2 . VAL   A 1 1802 ? -92.43400  54.93200  -9.87600  1.000 71.09702  ?  1800 VAL   A CG2 1 
ATOM   14024 N  N   . VAL   A 1 1803 ? -95.54000  56.08900  -6.59300  1.000 85.53615  ?  1801 VAL   A N   1 
ATOM   14025 C  CA  . VAL   A 1 1803 ? -96.89600  56.12500  -6.06100  1.000 84.38678  ?  1801 VAL   A CA  1 
ATOM   14026 C  C   . VAL   A 1 1803 ? -97.81000  56.58000  -7.18900  1.000 73.59065  ?  1801 VAL   A C   1 
ATOM   14027 O  O   . VAL   A 1 1803 ? -97.73900  57.73000  -7.63500  1.000 68.78719  ?  1801 VAL   A O   1 
ATOM   14028 C  CB  . VAL   A 1 1803 ? -97.00400  57.05000  -4.84200  1.000 95.43744  ?  1801 VAL   A CB  1 
ATOM   14029 C  CG1 . VAL   A 1 1803 ? -98.23900  56.70200  -4.02300  1.000 66.02104  ?  1801 VAL   A CG1 1 
ATOM   14030 C  CG2 . VAL   A 1 1803 ? -95.74400  56.95600  -3.99200  1.000 89.69532  ?  1801 VAL   A CG2 1 
ATOM   14031 N  N   . ILE   A 1 1804 ? -98.66700  55.67500  -7.65800  1.000 69.27637  ?  1802 ILE   A N   1 
ATOM   14032 C  CA  . ILE   A 1 1804 ? -99.52500  55.99200  -8.79400  1.000 72.35591  ?  1802 ILE   A CA  1 
ATOM   14033 C  C   . ILE   A 1 1804 ? -100.76700 56.75000  -8.34200  1.000 72.77746  ?  1802 ILE   A C   1 
ATOM   14034 O  O   . ILE   A 1 1804 ? -101.21000 57.69000  -9.01100  1.000 73.73943  ?  1802 ILE   A O   1 
ATOM   14035 C  CB  . ILE   A 1 1804 ? -99.87900  54.70400  -9.56000  1.000 66.51436  ?  1802 ILE   A CB  1 
ATOM   14036 C  CG1 . ILE   A 1 1804 ? -98.64000  54.14300  -10.25700 1.000 54.75368  ?  1802 ILE   A CG1 1 
ATOM   14037 C  CG2 . ILE   A 1 1804 ? -100.97200 54.95800  -10.58000 1.000 58.18739  ?  1802 ILE   A CG2 1 
ATOM   14038 C  CD1 . ILE   A 1 1804 ? -98.82800  52.74200  -10.78700 1.000 53.92416  ?  1802 ILE   A CD1 1 
ATOM   14039 N  N   . GLU   A 1 1805 ? -101.34100 56.37200  -7.20500  1.000 68.35497  ?  1803 GLU   A N   1 
ATOM   14040 C  CA  . GLU   A 1 1805 ? -102.54500 57.01900  -6.70400  1.000 73.87091  ?  1803 GLU   A CA  1 
ATOM   14041 C  C   . GLU   A 1 1805 ? -102.19200 58.23700  -5.85900  1.000 68.82846  ?  1803 GLU   A C   1 
ATOM   14042 O  O   . GLU   A 1 1805 ? -101.15900 58.27400  -5.18300  1.000 77.64075  ?  1803 GLU   A O   1 
ATOM   14043 C  CB  . GLU   A 1 1805 ? -103.38300 56.03700  -5.88400  1.000 77.71757  ?  1803 GLU   A CB  1 
ATOM   14044 C  CG  . GLU   A 1 1805 ? -103.39400 54.62200  -6.44100  1.000 89.70473  ?  1803 GLU   A CG  1 
ATOM   14045 C  CD  . GLU   A 1 1805 ? -102.50100 53.67600  -5.65700  1.000 115.90036 ?  1803 GLU   A CD  1 
ATOM   14046 O  OE1 . GLU   A 1 1805 ? -101.76500 54.15000  -4.76500  1.000 117.12762 ?  1803 GLU   A OE1 1 
ATOM   14047 O  OE2 . GLU   A 1 1805 ? -102.53600 52.45800  -5.93200  1.000 131.02375 -1 1803 GLU   A OE2 1 
ATOM   14048 N  N   . ALA   A 1 1806 ? -103.06400 59.23800  -5.90400  1.000 67.26737  ?  1804 ALA   A N   1 
ATOM   14049 C  CA  . ALA   A 1 1806 ? -102.88600 60.47400  -5.15800  1.000 43.22996  ?  1804 ALA   A CA  1 
ATOM   14050 C  C   . ALA   A 1 1806 ? -103.68600 60.43700  -3.86200  1.000 44.93869  ?  1804 ALA   A C   1 
ATOM   14051 O  O   . ALA   A 1 1806 ? -104.52500 59.56000  -3.63800  1.000 56.50129  ?  1804 ALA   A O   1 
ATOM   14052 C  CB  . ALA   A 1 1806 ? -103.30300 61.68000  -6.00300  1.000 49.70426  ?  1804 ALA   A CB  1 
ATOM   14053 N  N   . ALA   A 1 1807 ? -103.40900 61.41400  -2.99600  1.000 42.44172  ?  1805 ALA   A N   1 
ATOM   14054 C  CA  . ALA   A 1 1807 ? -104.18900 61.54800  -1.77200  1.000 47.26026  ?  1805 ALA   A CA  1 
ATOM   14055 C  C   . ALA   A 1 1807 ? -105.63600 61.88700  -2.09100  1.000 54.74749  ?  1805 ALA   A C   1 
ATOM   14056 O  O   . ALA   A 1 1807 ? -106.56300 61.31200  -1.50900  1.000 71.79169  ?  1805 ALA   A O   1 
ATOM   14057 C  CB  . ALA   A 1 1807 ? -103.57100 62.61400  -0.86800  1.000 56.30098  ?  1805 ALA   A CB  1 
ATOM   14058 N  N   . ALA   A 1 1808 ? -105.84700 62.81100  -3.02100  1.000 54.95400  ?  1806 ALA   A N   1 
ATOM   14059 C  CA  . ALA   A 1 1808 ? -107.17800 63.15900  -3.49700  1.000 47.74409  ?  1806 ALA   A CA  1 
ATOM   14060 C  C   . ALA   A 1 1808 ? -107.37100 62.51300  -4.86400  1.000 56.43574  ?  1806 ALA   A C   1 
ATOM   14061 O  O   . ALA   A 1 1808 ? -106.74200 62.92200  -5.84600  1.000 53.13158  ?  1806 ALA   A O   1 
ATOM   14062 C  CB  . ALA   A 1 1808 ? -107.35300 64.67300  -3.56500  1.000 46.12563  ?  1806 ALA   A CB  1 
ATOM   14063 N  N   . GLU   A 1 1809 ? -108.22600 61.49300  -4.92100  1.000 67.72974  ?  1807 GLU   A N   1 
ATOM   14064 C  CA  . GLU   A 1 1809 ? -108.57400 60.84400  -6.17800  1.000 72.04870  ?  1807 GLU   A CA  1 
ATOM   14065 C  C   . GLU   A 1 1809 ? -109.95000 61.23900  -6.69100  1.000 65.41489  ?  1807 GLU   A C   1 
ATOM   14066 O  O   . GLU   A 1 1809 ? -110.15600 61.27600  -7.90900  1.000 73.14225  ?  1807 GLU   A O   1 
ATOM   14067 C  CB  . GLU   A 1 1809 ? -108.50800 59.31900  -6.03000  1.000 80.62805  ?  1807 GLU   A CB  1 
ATOM   14068 C  CG  . GLU   A 1 1809 ? -107.10700 58.78100  -5.78800  1.000 83.17716  ?  1807 GLU   A CG  1 
ATOM   14069 C  CD  . GLU   A 1 1809 ? -107.06100 57.26700  -5.75800  1.000 103.37098 ?  1807 GLU   A CD  1 
ATOM   14070 O  OE1 . GLU   A 1 1809 ? -107.78600 56.63500  -6.55500  1.000 107.18613 ?  1807 GLU   A OE1 1 
ATOM   14071 O  OE2 . GLU   A 1 1809 ? -106.30000 56.70900  -4.93800  1.000 105.14815 -1 1807 GLU   A OE2 1 
ATOM   14072 N  N   . ASN   A 1 1810 ? -110.89000 61.53700  -5.79800  1.000 54.50591  ?  1808 ASN   A N   1 
ATOM   14073 C  CA  . ASN   A 1 1810 ? -112.21200 62.02100  -6.16600  1.000 70.57377  ?  1808 ASN   A CA  1 
ATOM   14074 C  C   . ASN   A 1 1810 ? -112.43900 63.38000  -5.52100  1.000 52.11509  ?  1808 ASN   A C   1 
ATOM   14075 O  O   . ASN   A 1 1810 ? -112.12400 63.57700  -4.34400  1.000 58.49082  ?  1808 ASN   A O   1 
ATOM   14076 C  CB  . ASN   A 1 1810 ? -113.31200 61.04000  -5.73400  1.000 76.35595  ?  1808 ASN   A CB  1 
ATOM   14077 C  CG  . ASN   A 1 1810 ? -112.92400 59.58900  -5.96000  1.000 92.32436  ?  1808 ASN   A CG  1 
ATOM   14078 O  OD1 . ASN   A 1 1810 ? -112.62800 58.85800  -5.01400  1.000 84.98261  ?  1808 ASN   A OD1 1 
ATOM   14079 N  ND2 . ASN   A 1 1810 ? -112.93000 59.16300  -7.21900  1.000 85.13351  ?  1808 ASN   A ND2 1 
ATOM   14080 N  N   . LEU   A 1 1811 ? -112.98000 64.31600  -6.29600  1.000 47.61533  ?  1809 LEU   A N   1 
ATOM   14081 C  CA  . LEU   A 1 1811 ? -113.18100 65.68700  -5.84500  1.000 37.01084  ?  1809 LEU   A CA  1 
ATOM   14082 C  C   . LEU   A 1 1811 ? -114.64100 66.06600  -6.02600  1.000 46.97700  ?  1809 LEU   A C   1 
ATOM   14083 O  O   . LEU   A 1 1811 ? -115.20400 65.88100  -7.11100  1.000 64.08679  ?  1809 LEU   A O   1 
ATOM   14084 C  CB  . LEU   A 1 1811 ? -112.28100 66.65400  -6.61800  1.000 45.96806  ?  1809 LEU   A CB  1 
ATOM   14085 C  CG  . LEU   A 1 1811 ? -111.52800 67.69700  -5.79700  1.000 43.60105  ?  1809 LEU   A CG  1 
ATOM   14086 C  CD1 . LEU   A 1 1811 ? -110.57100 67.02500  -4.82800  1.000 39.94753  ?  1809 LEU   A CD1 1 
ATOM   14087 C  CD2 . LEU   A 1 1811 ? -110.78300 68.65000  -6.71700  1.000 38.08368  ?  1809 LEU   A CD2 1 
ATOM   14088 N  N   . TYR   A 1 1812 ? -115.25100 66.59600  -4.96900  1.000 47.70736  ?  1810 TYR   A N   1 
ATOM   14089 C  CA  . TYR   A 1 1812 ? -116.65400 66.99200  -4.98200  1.000 46.80887  ?  1810 TYR   A CA  1 
ATOM   14090 C  C   . TYR   A 1 1812 ? -116.74900 68.47000  -4.63100  1.000 39.25652  ?  1810 TYR   A C   1 
ATOM   14091 O  O   . TYR   A 1 1812 ? -116.39000 68.87000  -3.51900  1.000 50.69844  ?  1810 TYR   A O   1 
ATOM   14092 C  CB  . TYR   A 1 1812 ? -117.47600 66.14600  -4.00500  1.000 40.57614  ?  1810 TYR   A CB  1 
ATOM   14093 C  CG  . TYR   A 1 1812 ? -117.35000 64.65500  -4.23900  1.000 47.95745  ?  1810 TYR   A CG  1 
ATOM   14094 C  CD1 . TYR   A 1 1812 ? -118.20000 63.99300  -5.11900  1.000 41.73175  ?  1810 TYR   A CD1 1 
ATOM   14095 C  CD2 . TYR   A 1 1812 ? -116.37700 63.91000  -3.58400  1.000 52.92089  ?  1810 TYR   A CD2 1 
ATOM   14096 C  CE1 . TYR   A 1 1812 ? -118.08200 62.62900  -5.33800  1.000 39.54426  ?  1810 TYR   A CE1 1 
ATOM   14097 C  CE2 . TYR   A 1 1812 ? -116.25200 62.54800  -3.79600  1.000 62.38158  ?  1810 TYR   A CE2 1 
ATOM   14098 C  CZ  . TYR   A 1 1812 ? -117.10600 61.91300  -4.67300  1.000 53.02507  ?  1810 TYR   A CZ  1 
ATOM   14099 O  OH  . TYR   A 1 1812 ? -116.97800 60.55900  -4.88200  1.000 55.67523  ?  1810 TYR   A OH  1 
ATOM   14100 N  N   . PHE   A 1 1813 ? -117.21900 69.27500  -5.58200  1.000 45.21291  ?  1811 PHE   A N   1 
ATOM   14101 C  CA  . PHE   A 1 1813 ? -117.42100 70.69800  -5.34300  1.000 48.68748  ?  1811 PHE   A CA  1 
ATOM   14102 C  C   . PHE   A 1 1813 ? -118.77700 70.92100  -4.68500  1.000 55.59972  ?  1811 PHE   A C   1 
ATOM   14103 O  O   . PHE   A 1 1813 ? -119.79400 70.39100  -5.14400  1.000 65.52301  ?  1811 PHE   A O   1 
ATOM   14104 C  CB  . PHE   A 1 1813 ? -117.33600 71.48500  -6.65300  1.000 41.46030  ?  1811 PHE   A CB  1 
ATOM   14105 C  CG  . PHE   A 1 1813 ? -115.93200 71.81800  -7.07700  1.000 43.27560  ?  1811 PHE   A CG  1 
ATOM   14106 C  CD1 . PHE   A 1 1813 ? -114.98100 70.82000  -7.22800  1.000 53.63711  ?  1811 PHE   A CD1 1 
ATOM   14107 C  CD2 . PHE   A 1 1813 ? -115.56400 73.13000  -7.33100  1.000 42.72559  ?  1811 PHE   A CD2 1 
ATOM   14108 C  CE1 . PHE   A 1 1813 ? -113.68800 71.12300  -7.62200  1.000 46.29474  ?  1811 PHE   A CE1 1 
ATOM   14109 C  CE2 . PHE   A 1 1813 ? -114.27200 73.44100  -7.72500  1.000 49.73176  ?  1811 PHE   A CE2 1 
ATOM   14110 C  CZ  . PHE   A 1 1813 ? -113.33300 72.43600  -7.87000  1.000 52.09422  ?  1811 PHE   A CZ  1 
ATOM   14111 N  N   . GLN   A 1 1814 ? -118.79100 71.70200  -3.60900  1.000 61.26356  ?  1812 GLN   A N   1 
ATOM   14112 C  CA  . GLN   A 1 1814 ? -120.03700 72.02200  -2.92000  1.000 75.57483  ?  1812 GLN   A CA  1 
ATOM   14113 C  C   . GLN   A 1 1814 ? -120.32700 73.52400  -2.96300  1.000 84.52136  ?  1812 GLN   A C   1 
ATOM   14114 O  O   . GLN   A 1 1814 ? -119.43400 74.35200  -3.15300  1.000 67.59268  ?  1812 GLN   A O   1 
ATOM   14115 C  CB  . GLN   A 1 1814 ? -119.99000 71.53200  -1.47000  1.000 56.88720  ?  1812 GLN   A CB  1 
ATOM   14116 C  CG  . GLN   A 1 1814 ? -119.65300 72.61300  -0.46000  1.000 49.62414  ?  1812 GLN   A CG  1 
ATOM   14117 C  CD  . GLN   A 1 1814 ? -119.13000 72.04600  0.84000   1.000 67.84605  ?  1812 GLN   A CD  1 
ATOM   14118 O  OE1 . GLN   A 1 1814 ? -118.55800 70.95500  0.86900   1.000 49.01494  ?  1812 GLN   A OE1 1 
ATOM   14119 N  NE2 . GLN   A 1 1814 ? -119.32100 72.78600  1.92800   1.000 71.90547  ?  1812 GLN   A NE2 1 
ATOM   14120 O  OXT . GLN   A 1 1814 ? -121.47100 73.95300  -2.81700  1.000 106.38293 ?  1812 GLN   A OXT 1 
ATOM   14121 N  N   . MET   B 1 1    ? 98.47400   50.34900  -22.19700 1.000 84.75782  ?  1    MET   B N   1 
ATOM   14122 C  CA  . MET   B 1 1    ? 97.26600   50.18900  -23.00000 1.000 94.13633  ?  1    MET   B CA  1 
ATOM   14123 C  C   . MET   B 1 1    ? 97.23000   51.18600  -24.15600 1.000 105.74499 ?  1    MET   B C   1 
ATOM   14124 O  O   . MET   B 1 1    ? 98.03700   51.10400  -25.08300 1.000 113.87757 ?  1    MET   B O   1 
ATOM   14125 C  CB  . MET   B 1 1    ? 96.01900   50.35400  -22.13000 1.000 79.67135  ?  1    MET   B CB  1 
ATOM   14126 C  CG  . MET   B 1 1    ? 94.79500   49.61800  -22.65200 1.000 88.26769  ?  1    MET   B CG  1 
ATOM   14127 S  SD  . MET   B 1 1    ? 94.56700   48.01500  -21.86600 1.000 110.91736 ?  1    MET   B SD  1 
ATOM   14128 C  CE  . MET   B 1 1    ? 94.58400   48.48900  -20.13900 1.000 65.90116  ?  1    MET   B CE  1 
ATOM   14129 N  N   . GLY   B 1 2    ? 96.29200   52.12100  -24.09500 1.000 83.18323  ?  2    GLY   B N   1 
ATOM   14130 C  CA  . GLY   B 1 2    ? 96.14200   53.11400  -25.14200 1.000 63.89496  ?  2    GLY   B CA  1 
ATOM   14131 C  C   . GLY   B 1 2    ? 95.90700   54.48900  -24.55500 1.000 66.55402  ?  2    GLY   B C   1 
ATOM   14132 O  O   . GLY   B 1 2    ? 95.31500   54.63800  -23.48400 1.000 62.50122  ?  2    GLY   B O   1 
ATOM   14133 N  N   . ARG   B 1 3    ? 96.38300   55.50100  -25.27900 1.000 69.65747  ?  3    ARG   B N   1 
ATOM   14134 C  CA  . ARG   B 1 3    ? 96.23900   56.88700  -24.85300 1.000 64.57953  ?  3    ARG   B CA  1 
ATOM   14135 C  C   . ARG   B 1 3    ? 94.87200   57.41900  -25.26700 1.000 67.99434  ?  3    ARG   B C   1 
ATOM   14136 O  O   . ARG   B 1 3    ? 94.46200   57.27200  -26.42300 1.000 67.00059  ?  3    ARG   B O   1 
ATOM   14137 C  CB  . ARG   B 1 3    ? 97.35200   57.74300  -25.45600 1.000 68.24437  ?  3    ARG   B CB  1 
ATOM   14138 C  CG  . ARG   B 1 3    ? 97.85800   58.85600  -24.55200 1.000 68.28815  ?  3    ARG   B CG  1 
ATOM   14139 C  CD  . ARG   B 1 3    ? 99.27300   59.27100  -24.93600 1.000 62.29343  ?  3    ARG   B CD  1 
ATOM   14140 N  NE  . ARG   B 1 3    ? 99.59900   60.61000  -24.46100 1.000 65.68372  ?  3    ARG   B NE  1 
ATOM   14141 C  CZ  . ARG   B 1 3    ? 99.61700   61.69100  -25.22900 1.000 74.65452  ?  3    ARG   B CZ  1 
ATOM   14142 N  NH1 . ARG   B 1 3    ? 99.33700   61.62600  -26.52100 1.000 67.41329  ?  3    ARG   B NH1 1 
ATOM   14143 N  NH2 . ARG   B 1 3    ? 99.92100   62.86700  -24.68800 1.000 82.54501  ?  3    ARG   B NH2 1 
ATOM   14144 N  N   . ILE   B 1 4    ? 94.16900   58.03900  -24.32300 1.000 65.93920  ?  4    ILE   B N   1 
ATOM   14145 C  CA  . ILE   B 1 4    ? 92.79600   58.48800  -24.52200 1.000 57.54698  ?  4    ILE   B CA  1 
ATOM   14146 C  C   . ILE   B 1 4    ? 92.75100   60.00300  -24.39100 1.000 53.23667  ?  4    ILE   B C   1 
ATOM   14147 O  O   . ILE   B 1 4    ? 93.24700   60.56100  -23.40600 1.000 54.67313  ?  4    ILE   B O   1 
ATOM   14148 C  CB  . ILE   B 1 4    ? 91.83500   57.83000  -23.51700 1.000 56.44202  ?  4    ILE   B CB  1 
ATOM   14149 C  CG1 . ILE   B 1 4    ? 91.68100   56.34100  -23.81500 1.000 53.68451  ?  4    ILE   B CG1 1 
ATOM   14150 C  CG2 . ILE   B 1 4    ? 90.48100   58.51700  -23.53800 1.000 62.58142  ?  4    ILE   B CG2 1 
ATOM   14151 C  CD1 . ILE   B 1 4    ? 90.93300   55.60000  -22.73800 1.000 63.31106  ?  4    ILE   B CD1 1 
ATOM   14152 N  N   . LEU   B 1 5    ? 92.14800   60.66200  -25.37700 1.000 54.50953  ?  5    LEU   B N   1 
ATOM   14153 C  CA  . LEU   B 1 5    ? 91.90500   62.09900  -25.33200 1.000 50.54504  ?  5    LEU   B CA  1 
ATOM   14154 C  C   . LEU   B 1 5    ? 90.44600   62.32200  -24.95300 1.000 54.75204  ?  5    LEU   B C   1 
ATOM   14155 O  O   . LEU   B 1 5    ? 89.53900   61.96900  -25.71400 1.000 62.74783  ?  5    LEU   B O   1 
ATOM   14156 C  CB  . LEU   B 1 5    ? 92.22800   62.75000  -26.67400 1.000 42.01462  ?  5    LEU   B CB  1 
ATOM   14157 C  CG  . LEU   B 1 5    ? 91.68900   64.16700  -26.86300 1.000 49.49907  ?  5    LEU   B CG  1 
ATOM   14158 C  CD1 . LEU   B 1 5    ? 92.44200   65.14700  -25.97700 1.000 48.50363  ?  5    LEU   B CD1 1 
ATOM   14159 C  CD2 . LEU   B 1 5    ? 91.78000   64.57500  -28.32200 1.000 65.02776  ?  5    LEU   B CD2 1 
ATOM   14160 N  N   . PHE   B 1 6    ? 90.21900   62.89900  -23.77700 1.000 55.89553  ?  6    PHE   B N   1 
ATOM   14161 C  CA  . PHE   B 1 6    ? 88.87000   63.19600  -23.31800 1.000 48.42760  ?  6    PHE   B CA  1 
ATOM   14162 C  C   . PHE   B 1 6    ? 88.48500   64.61000  -23.72800 1.000 55.17014  ?  6    PHE   B C   1 
ATOM   14163 O  O   . PHE   B 1 6    ? 89.25300   65.55600  -23.52300 1.000 50.25707  ?  6    PHE   B O   1 
ATOM   14164 C  CB  . PHE   B 1 6    ? 88.76000   63.04300  -21.80300 1.000 41.32753  ?  6    PHE   B CB  1 
ATOM   14165 C  CG  . PHE   B 1 6    ? 87.34700   62.97000  -21.31000 1.000 47.30458  ?  6    PHE   B CG  1 
ATOM   14166 C  CD1 . PHE   B 1 6    ? 86.58600   61.83300  -21.51900 1.000 39.16898  ?  6    PHE   B CD1 1 
ATOM   14167 C  CD2 . PHE   B 1 6    ? 86.77200   64.04600  -20.65500 1.000 63.31487  ?  6    PHE   B CD2 1 
ATOM   14168 C  CE1 . PHE   B 1 6    ? 85.28200   61.76500  -21.07000 1.000 43.28463  ?  6    PHE   B CE1 1 
ATOM   14169 C  CE2 . PHE   B 1 6    ? 85.46800   63.98600  -20.20400 1.000 48.48710  ?  6    PHE   B CE2 1 
ATOM   14170 C  CZ  . PHE   B 1 6    ? 84.72200   62.84500  -20.41200 1.000 50.41266  ?  6    PHE   B CZ  1 
ATOM   14171 N  N   . LEU   B 1 7    ? 87.28800   64.75200  -24.29300 1.000 51.98708  ?  7    LEU   B N   1 
ATOM   14172 C  CA  . LEU   B 1 7    ? 86.80100   66.03200  -24.79300 1.000 44.93514  ?  7    LEU   B CA  1 
ATOM   14173 C  C   . LEU   B 1 7    ? 85.52600   66.39800  -24.04600 1.000 49.37414  ?  7    LEU   B C   1 
ATOM   14174 O  O   . LEU   B 1 7    ? 84.49000   65.74700  -24.22100 1.000 57.71669  ?  7    LEU   B O   1 
ATOM   14175 C  CB  . LEU   B 1 7    ? 86.56100   65.96800  -26.29900 1.000 49.78310  ?  7    LEU   B CB  1 
ATOM   14176 C  CG  . LEU   B 1 7    ? 87.80700   66.11400  -27.17300 1.000 48.15201  ?  7    LEU   B CG  1 
ATOM   14177 C  CD1 . LEU   B 1 7    ? 87.41200   66.16200  -28.63600 1.000 51.58896  ?  7    LEU   B CD1 1 
ATOM   14178 C  CD2 . LEU   B 1 7    ? 88.60800   67.35000  -26.78400 1.000 54.49252  ?  7    LEU   B CD2 1 
ATOM   14179 N  N   . THR   B 1 8    ? 85.60200   67.43400  -23.21400 1.000 39.13220  ?  8    THR   B N   1 
ATOM   14180 C  CA  . THR   B 1 8    ? 84.43700   67.94800  -22.51000 1.000 49.68010  ?  8    THR   B CA  1 
ATOM   14181 C  C   . THR   B 1 8    ? 84.50200   69.46800  -22.48100 1.000 50.36419  ?  8    THR   B C   1 
ATOM   14182 O  O   . THR   B 1 8    ? 85.54100   70.07500  -22.75000 1.000 56.94510  ?  8    THR   B O   1 
ATOM   14183 C  CB  . THR   B 1 8    ? 84.33900   67.39800  -21.08400 1.000 48.49712  ?  8    THR   B CB  1 
ATOM   14184 O  OG1 . THR   B 1 8    ? 83.14300   67.89100  -20.47000 1.000 50.82280  ?  8    THR   B OG1 1 
ATOM   14185 C  CG2 . THR   B 1 8    ? 85.53500   67.84200  -20.26300 1.000 47.31267  ?  8    THR   B CG2 1 
ATOM   14186 N  N   . THR   B 1 9    ? 83.37000   70.08400  -22.14900 1.000 41.37817  ?  9    THR   B N   1 
ATOM   14187 C  CA  . THR   B 1 9    ? 83.29900   71.53500  -22.03700 1.000 44.56423  ?  9    THR   B CA  1 
ATOM   14188 C  C   . THR   B 1 9    ? 82.46000   71.92200  -20.82800 1.000 50.56525  ?  9    THR   B C   1 
ATOM   14189 O  O   . THR   B 1 9    ? 82.85900   72.77400  -20.02800 1.000 61.21851  ?  9    THR   B O   1 
ATOM   14190 C  CB  . THR   B 1 9    ? 82.71100   72.15400  -23.30700 1.000 44.88951  ?  9    THR   B CB  1 
ATOM   14191 O  OG1 . THR   B 1 9    ? 83.42100   71.66800  -24.45300 1.000 63.28994  ?  9    THR   B OG1 1 
ATOM   14192 C  CG2 . THR   B 1 9    ? 82.81700   73.67200  -23.25900 1.000 46.82707  ?  9    THR   B CG2 1 
ATOM   14193 N  N   . PHE   B 1 10   ? 81.29600   71.29000  -20.68900 1.000 46.11633  ?  10   PHE   B N   1 
ATOM   14194 C  CA  . PHE   B 1 10   ? 80.36900   71.58200  -19.60700 1.000 38.36075  ?  10   PHE   B CA  1 
ATOM   14195 C  C   . PHE   B 1 10   ? 80.40800   70.54800  -18.49100 1.000 41.47222  ?  10   PHE   B C   1 
ATOM   14196 O  O   . PHE   B 1 10   ? 79.79600   70.77100  -17.44100 1.000 44.74099  ?  10   PHE   B O   1 
ATOM   14197 C  CB  . PHE   B 1 10   ? 78.94100   71.69800  -20.15700 1.000 39.36317  ?  10   PHE   B CB  1 
ATOM   14198 C  CG  . PHE   B 1 10   ? 78.85200   72.48700  -21.43400 1.000 41.20824  ?  10   PHE   B CG  1 
ATOM   14199 C  CD1 . PHE   B 1 10   ? 79.13100   73.84500  -21.44400 1.000 36.84549  ?  10   PHE   B CD1 1 
ATOM   14200 C  CD2 . PHE   B 1 10   ? 78.50100   71.87100  -22.62400 1.000 39.48507  ?  10   PHE   B CD2 1 
ATOM   14201 C  CE1 . PHE   B 1 10   ? 79.05700   74.57400  -22.61400 1.000 40.41700  ?  10   PHE   B CE1 1 
ATOM   14202 C  CE2 . PHE   B 1 10   ? 78.42500   72.59600  -23.80000 1.000 47.48925  ?  10   PHE   B CE2 1 
ATOM   14203 C  CZ  . PHE   B 1 10   ? 78.70300   73.94900  -23.79500 1.000 50.68435  ?  10   PHE   B CZ  1 
ATOM   14204 N  N   . MET   B 1 11   ? 81.09900   69.42900  -18.69000 1.000 42.55493  ?  11   MET   B N   1 
ATOM   14205 C  CA  . MET   B 1 11   ? 81.34300   68.47200  -17.62100 1.000 45.42479  ?  11   MET   B CA  1 
ATOM   14206 C  C   . MET   B 1 11   ? 82.71100   68.75800  -17.00000 1.000 47.37215  ?  11   MET   B C   1 
ATOM   14207 O  O   . MET   B 1 11   ? 83.34500   69.78000  -17.28200 1.000 41.08930  ?  11   MET   B O   1 
ATOM   14208 C  CB  . MET   B 1 11   ? 81.22400   67.04500  -18.14800 1.000 44.66064  ?  11   MET   B CB  1 
ATOM   14209 C  CG  . MET   B 1 11   ? 79.80200   66.62700  -18.48100 1.000 42.24833  ?  11   MET   B CG  1 
ATOM   14210 S  SD  . MET   B 1 11   ? 78.81600   66.32600  -17.00300 1.000 61.38802  ?  11   MET   B SD  1 
ATOM   14211 C  CE  . MET   B 1 11   ? 77.17700   66.19600  -17.70800 1.000 50.83094  ?  11   MET   B CE  1 
ATOM   14212 N  N   . SER   B 1 12   ? 83.18600   67.85800  -16.14600 1.000 52.37144  ?  12   SER   B N   1 
ATOM   14213 C  CA  . SER   B 1 12   ? 84.37700   68.09600  -15.34700 1.000 45.05013  ?  12   SER   B CA  1 
ATOM   14214 C  C   . SER   B 1 12   ? 85.51200   67.16900  -15.75700 1.000 58.25010  ?  12   SER   B C   1 
ATOM   14215 O  O   . SER   B 1 12   ? 85.30100   66.09300  -16.32500 1.000 60.62374  ?  12   SER   B O   1 
ATOM   14216 C  CB  . SER   B 1 12   ? 84.07700   67.91100  -13.85600 1.000 39.55436  ?  12   SER   B CB  1 
ATOM   14217 O  OG  . SER   B 1 12   ? 82.98200   67.03300  -13.67100 1.000 75.29945  ?  12   SER   B OG  1 
ATOM   14218 N  N   . LYS   B 1 13   ? 86.73600   67.61200  -15.45600 1.000 63.09952  ?  13   LYS   B N   1 
ATOM   14219 C  CA  . LYS   B 1 13   ? 87.90700   66.77300  -15.68200 1.000 48.79623  ?  13   LYS   B CA  1 
ATOM   14220 C  C   . LYS   B 1 13   ? 87.94400   65.60400  -14.71100 1.000 49.98582  ?  13   LYS   B C   1 
ATOM   14221 O  O   . LYS   B 1 13   ? 88.55800   64.57200  -15.00400 1.000 56.47693  ?  13   LYS   B O   1 
ATOM   14222 C  CB  . LYS   B 1 13   ? 89.18000   67.60500  -15.55800 1.000 46.18161  ?  13   LYS   B CB  1 
ATOM   14223 C  CG  . LYS   B 1 13   ? 89.09900   68.96500  -16.23800 1.000 71.75313  ?  13   LYS   B CG  1 
ATOM   14224 C  CD  . LYS   B 1 13   ? 90.23000   69.87700  -15.78200 1.000 76.83751  ?  13   LYS   B CD  1 
ATOM   14225 C  CE  . LYS   B 1 13   ? 90.87900   70.59600  -16.95600 1.000 76.97979  ?  13   LYS   B CE  1 
ATOM   14226 N  NZ  . LYS   B 1 13   ? 92.36800   70.61100  -16.84500 1.000 85.33137  ?  13   LYS   B NZ  1 
ATOM   14227 N  N   . GLY   B 1 14   ? 87.29300   65.74300  -13.56000 1.000 47.52209  ?  14   GLY   B N   1 
ATOM   14228 C  CA  . GLY   B 1 14   ? 87.24500   64.67300  -12.59000 1.000 50.73013  ?  14   GLY   B CA  1 
ATOM   14229 C  C   . GLY   B 1 14   ? 85.93600   63.91800  -12.64300 1.000 64.28248  ?  14   GLY   B C   1 
ATOM   14230 O  O   . GLY   B 1 14   ? 85.35700   63.59900  -11.60200 1.000 78.03773  ?  14   GLY   B O   1 
ATOM   14231 N  N   . ASN   B 1 15   ? 85.45900   63.62600  -13.85000 1.000 65.46568  ?  15   ASN   B N   1 
ATOM   14232 C  CA  . ASN   B 1 15   ? 84.20600   62.91000  -14.00900 1.000 57.36043  ?  15   ASN   B CA  1 
ATOM   14233 C  C   . ASN   B 1 15   ? 84.39200   61.42300  -13.71300 1.000 53.75726  ?  15   ASN   B C   1 
ATOM   14234 O  O   . ASN   B 1 15   ? 85.50300   60.88700  -13.75000 1.000 52.04517  ?  15   ASN   B O   1 
ATOM   14235 C  CB  . ASN   B 1 15   ? 83.65600   63.10400  -15.42300 1.000 57.03923  ?  15   ASN   B CB  1 
ATOM   14236 C  CG  . ASN   B 1 15   ? 82.18400   62.76300  -15.52500 1.000 88.01516  ?  15   ASN   B CG  1 
ATOM   14237 O  OD1 . ASN   B 1 15   ? 81.79500   61.85500  -16.25900 1.000 80.03601  ?  15   ASN   B OD1 1 
ATOM   14238 N  ND2 . ASN   B 1 15   ? 81.35400   63.48900  -14.78400 1.000 93.56173  ?  15   ASN   B ND2 1 
ATOM   14239 N  N   . LYS   B 1 16   ? 83.27300   60.75900  -13.41100 1.000 47.64951  ?  16   LYS   B N   1 
ATOM   14240 C  CA  . LYS   B 1 16   ? 83.29700   59.32400  -13.14300 1.000 42.82913  ?  16   LYS   B CA  1 
ATOM   14241 C  C   . LYS   B 1 16   ? 83.89300   58.55000  -14.31200 1.000 51.00937  ?  16   LYS   B C   1 
ATOM   14242 O  O   . LYS   B 1 16   ? 84.61400   57.56500  -14.11100 1.000 58.46945  ?  16   LYS   B O   1 
ATOM   14243 C  CB  . LYS   B 1 16   ? 81.88200   58.82900  -12.84100 1.000 42.25094  ?  16   LYS   B CB  1 
ATOM   14244 C  CG  . LYS   B 1 16   ? 81.81600   57.55400  -12.01800 1.000 56.66865  ?  16   LYS   B CG  1 
ATOM   14245 C  CD  . LYS   B 1 16   ? 80.38300   57.05700  -11.88700 1.000 60.86704  ?  16   LYS   B CD  1 
ATOM   14246 C  CE  . LYS   B 1 16   ? 80.23800   56.07300  -10.73400 1.000 63.07185  ?  16   LYS   B CE  1 
ATOM   14247 N  NZ  . LYS   B 1 16   ? 79.19400   56.50000  -9.75900  1.000 56.66155  ?  16   LYS   B NZ  1 
ATOM   14248 N  N   . VAL   B 1 17   ? 83.60700   58.98000  -15.54300 1.000 41.93388  ?  17   VAL   B N   1 
ATOM   14249 C  CA  . VAL   B 1 17   ? 84.13700   58.27600  -16.70500 1.000 51.87642  ?  17   VAL   B CA  1 
ATOM   14250 C  C   . VAL   B 1 17   ? 85.65100   58.43200  -16.78000 1.000 46.94368  ?  17   VAL   B C   1 
ATOM   14251 O  O   . VAL   B 1 17   ? 86.36700   57.49400  -17.15100 1.000 51.18091  ?  17   VAL   B O   1 
ATOM   14252 C  CB  . VAL   B 1 17   ? 83.44300   58.76200  -17.99300 1.000 54.80107  ?  17   VAL   B CB  1 
ATOM   14253 C  CG1 . VAL   B 1 17   ? 81.94500   58.53800  -17.90000 1.000 52.81730  ?  17   VAL   B CG1 1 
ATOM   14254 C  CG2 . VAL   B 1 17   ? 83.73700   60.22900  -18.25400 1.000 63.62732  ?  17   VAL   B CG2 1 
ATOM   14255 N  N   . VAL   B 1 18   ? 86.16500   59.60800  -16.40800 1.000 51.13063  ?  18   VAL   B N   1 
ATOM   14256 C  CA  . VAL   B 1 18   ? 87.60500   59.83900  -16.45400 1.000 54.87082  ?  18   VAL   B CA  1 
ATOM   14257 C  C   . VAL   B 1 18   ? 88.31300   58.99800  -15.40200 1.000 50.13676  ?  18   VAL   B C   1 
ATOM   14258 O  O   . VAL   B 1 18   ? 89.36000   58.39700  -15.66800 1.000 52.78016  ?  18   VAL   B O   1 
ATOM   14259 C  CB  . VAL   B 1 18   ? 87.90900   61.33800  -16.28000 1.000 36.42898  ?  18   VAL   B CB  1 
ATOM   14260 C  CG1 . VAL   B 1 18   ? 89.40100   61.57800  -16.34000 1.000 40.34561  ?  18   VAL   B CG1 1 
ATOM   14261 C  CG2 . VAL   B 1 18   ? 87.20100   62.14900  -17.34900 1.000 45.55934  ?  18   VAL   B CG2 1 
ATOM   14262 N  N   . ARG   B 1 19   ? 87.75300   58.93700  -14.19200 1.000 50.76492  ?  19   ARG   B N   1 
ATOM   14263 C  CA  . ARG   B 1 19   ? 88.36400   58.13700  -13.13800 1.000 60.83963  ?  19   ARG   B CA  1 
ATOM   14264 C  C   . ARG   B 1 19   ? 88.24700   56.64600  -13.42800 1.000 54.20673  ?  19   ARG   B C   1 
ATOM   14265 O  O   . ARG   B 1 19   ? 89.11900   55.86900  -13.02200 1.000 53.66535  ?  19   ARG   B O   1 
ATOM   14266 C  CB  . ARG   B 1 19   ? 87.73300   58.48300  -11.78900 1.000 52.28198  ?  19   ARG   B CB  1 
ATOM   14267 C  CG  . ARG   B 1 19   ? 87.71300   59.97700  -11.49500 1.000 55.96834  ?  19   ARG   B CG  1 
ATOM   14268 C  CD  . ARG   B 1 19   ? 87.17900   60.27400  -10.10300 1.000 60.72251  ?  19   ARG   B CD  1 
ATOM   14269 N  NE  . ARG   B 1 19   ? 85.83400   59.74700  -9.90800  1.000 65.16170  ?  19   ARG   B NE  1 
ATOM   14270 C  CZ  . ARG   B 1 19   ? 84.77500   60.48600  -9.60300  1.000 66.76516  ?  19   ARG   B CZ  1 
ATOM   14271 N  NH1 . ARG   B 1 19   ? 84.86400   61.79800  -9.46200  1.000 69.43240  ?  19   ARG   B NH1 1 
ATOM   14272 N  NH2 . ARG   B 1 19   ? 83.59700   59.89300  -9.43600  1.000 69.05935  ?  19   ARG   B NH2 1 
ATOM   14273 N  N   . TYR   B 1 20   ? 87.19000   56.22700  -14.12600 1.000 48.41871  ?  20   TYR   B N   1 
ATOM   14274 C  CA  . TYR   B 1 20   ? 87.10100   54.83000  -14.53400 1.000 52.90320  ?  20   TYR   B CA  1 
ATOM   14275 C  C   . TYR   B 1 20   ? 88.17100   54.49700  -15.56400 1.000 50.65457  ?  20   TYR   B C   1 
ATOM   14276 O  O   . TYR   B 1 20   ? 88.78500   53.42500  -15.50700 1.000 50.62660  ?  20   TYR   B O   1 
ATOM   14277 C  CB  . TYR   B 1 20   ? 85.71000   54.52200  -15.08800 1.000 50.51586  ?  20   TYR   B CB  1 
ATOM   14278 C  CG  . TYR   B 1 20   ? 85.60000   53.14700  -15.70800 1.000 42.38294  ?  20   TYR   B CG  1 
ATOM   14279 C  CD1 . TYR   B 1 20   ? 85.54400   52.00700  -14.91400 1.000 39.93958  ?  20   TYR   B CD1 1 
ATOM   14280 C  CD2 . TYR   B 1 20   ? 85.56000   52.98700  -17.08600 1.000 46.22843  ?  20   TYR   B CD2 1 
ATOM   14281 C  CE1 . TYR   B 1 20   ? 85.44800   50.74500  -15.47800 1.000 37.54819  ?  20   TYR   B CE1 1 
ATOM   14282 C  CE2 . TYR   B 1 20   ? 85.46400   51.73000  -17.66000 1.000 47.04585  ?  20   TYR   B CE2 1 
ATOM   14283 C  CZ  . TYR   B 1 20   ? 85.40700   50.61400  -16.85200 1.000 51.56343  ?  20   TYR   B CZ  1 
ATOM   14284 O  OH  . TYR   B 1 20   ? 85.31000   49.36400  -17.42200 1.000 65.52015  ?  20   TYR   B OH  1 
ATOM   14285 N  N   . LEU   B 1 21   ? 88.40800   55.40500  -16.51300 1.000 44.66869  ?  21   LEU   B N   1 
ATOM   14286 C  CA  . LEU   B 1 21   ? 89.46400   55.18500  -17.49400 1.000 48.76204  ?  21   LEU   B CA  1 
ATOM   14287 C  C   . LEU   B 1 21   ? 90.83500   55.18700  -16.83200 1.000 58.65798  ?  21   LEU   B C   1 
ATOM   14288 O  O   . LEU   B 1 21   ? 91.69600   54.36600  -17.17100 1.000 51.94994  ?  21   LEU   B O   1 
ATOM   14289 C  CB  . LEU   B 1 21   ? 89.39000   56.24700  -18.59000 1.000 47.45608  ?  21   LEU   B CB  1 
ATOM   14290 C  CG  . LEU   B 1 21   ? 88.17100   56.14600  -19.50600 1.000 49.68119  ?  21   LEU   B CG  1 
ATOM   14291 C  CD1 . LEU   B 1 21   ? 88.19300   57.24900  -20.55400 1.000 46.20453  ?  21   LEU   B CD1 1 
ATOM   14292 C  CD2 . LEU   B 1 21   ? 88.11000   54.77300  -20.15700 1.000 42.41235  ?  21   LEU   B CD2 1 
ATOM   14293 N  N   . GLU   B 1 22   ? 91.05300   56.10200  -15.88300 1.000 57.62939  ?  22   GLU   B N   1 
ATOM   14294 C  CA  . GLU   B 1 22   ? 92.30600   56.10400  -15.13600 1.000 40.20017  ?  22   GLU   B CA  1 
ATOM   14295 C  C   . GLU   B 1 22   ? 92.44600   54.85000  -14.28600 1.000 52.68408  ?  22   GLU   B C   1 
ATOM   14296 O  O   . GLU   B 1 22   ? 93.56700   54.40300  -14.01900 1.000 65.50699  ?  22   GLU   B O   1 
ATOM   14297 C  CB  . GLU   B 1 22   ? 92.39600   57.35500  -14.26200 1.000 33.76187  ?  22   GLU   B CB  1 
ATOM   14298 C  CG  . GLU   B 1 22   ? 92.53700   58.65000  -15.04800 1.000 37.10368  ?  22   GLU   B CG  1 
ATOM   14299 C  CD  . GLU   B 1 22   ? 92.58900   59.88100  -14.16000 1.000 63.62329  ?  22   GLU   B CD  1 
ATOM   14300 O  OE1 . GLU   B 1 22   ? 92.38700   59.74900  -12.93400 1.000 73.72460  ?  22   GLU   B OE1 1 
ATOM   14301 O  OE2 . GLU   B 1 22   ? 92.83300   60.98500  -14.69400 1.000 67.38075  -1 22   GLU   B OE2 1 
ATOM   14302 N  N   . SER   B 1 23   ? 91.32300   54.26600  -13.85800 1.000 49.44918  ?  23   SER   B N   1 
ATOM   14303 C  CA  . SER   B 1 23   ? 91.38400   53.03400  -13.08300 1.000 44.52104  ?  23   SER   B CA  1 
ATOM   14304 C  C   . SER   B 1 23   ? 91.89700   51.86900  -13.92200 1.000 42.91289  ?  23   SER   B C   1 
ATOM   14305 O  O   . SER   B 1 23   ? 92.59800   50.99600  -13.40100 1.000 49.45346  ?  23   SER   B O   1 
ATOM   14306 C  CB  . SER   B 1 23   ? 90.00800   52.71200  -12.50100 1.000 42.26453  ?  23   SER   B CB  1 
ATOM   14307 O  OG  . SER   B 1 23   ? 89.21800   51.98300  -13.42300 1.000 54.74641  ?  23   SER   B OG  1 
ATOM   14308 N  N   . LEU   B 1 24   ? 91.57100   51.84200  -15.21400 1.000 49.88477  ?  24   LEU   B N   1 
ATOM   14309 C  CA  . LEU   B 1 24   ? 92.03200   50.79700  -16.12100 1.000 50.52201  ?  24   LEU   B CA  1 
ATOM   14310 C  C   . LEU   B 1 24   ? 93.46200   51.01700  -16.59400 1.000 52.13446  ?  24   LEU   B C   1 
ATOM   14311 O  O   . LEU   B 1 24   ? 93.91100   50.32200  -17.51400 1.000 53.44957  ?  24   LEU   B O   1 
ATOM   14312 C  CB  . LEU   B 1 24   ? 91.09600   50.69400  -17.33000 1.000 57.20230  ?  24   LEU   B CB  1 
ATOM   14313 C  CG  . LEU   B 1 24   ? 89.62400   50.38400  -17.04000 1.000 52.30913  ?  24   LEU   B CG  1 
ATOM   14314 C  CD1 . LEU   B 1 24   ? 88.88500   50.06200  -18.32800 1.000 59.98343  ?  24   LEU   B CD1 1 
ATOM   14315 C  CD2 . LEU   B 1 24   ? 89.49400   49.24000  -16.04600 1.000 36.08106  ?  24   LEU   B CD2 1 
ATOM   14316 N  N   . HIS   B 1 25   ? 94.17200   51.96700  -15.98500 1.000 51.09793  ?  25   HIS   B N   1 
ATOM   14317 C  CA  . HIS   B 1 25   ? 95.55500   52.28900  -16.33100 1.000 53.37917  ?  25   HIS   B CA  1 
ATOM   14318 C  C   . HIS   B 1 25   ? 95.67500   52.83200  -17.75100 1.000 46.32971  ?  25   HIS   B C   1 
ATOM   14319 O  O   . HIS   B 1 25   ? 96.72300   52.71100  -18.38700 1.000 58.21507  ?  25   HIS   B O   1 
ATOM   14320 C  CB  . HIS   B 1 25   ? 96.47800   51.08300  -16.12500 1.000 54.42476  ?  25   HIS   B CB  1 
ATOM   14321 C  CG  . HIS   B 1 25   ? 96.51200   50.58900  -14.71200 1.000 54.73843  ?  25   HIS   B CG  1 
ATOM   14322 N  ND1 . HIS   B 1 25   ? 96.78300   51.41700  -13.64300 1.000 54.50279  ?  25   HIS   B ND1 1 
ATOM   14323 C  CD2 . HIS   B 1 25   ? 96.30600   49.35700  -14.19000 1.000 49.54019  ?  25   HIS   B CD2 1 
ATOM   14324 C  CE1 . HIS   B 1 25   ? 96.74400   50.71500  -12.52400 1.000 62.66255  ?  25   HIS   B CE1 1 
ATOM   14325 N  NE2 . HIS   B 1 25   ? 96.45700   49.46200  -12.82800 1.000 51.38486  ?  25   HIS   B NE2 1 
ATOM   14326 N  N   . HIS   B 1 26   ? 94.59700   53.42400  -18.25900 1.000 55.60039  ?  26   HIS   B N   1 
ATOM   14327 C  CA  . HIS   B 1 26   ? 94.69800   54.27200  -19.43400 1.000 52.15368  ?  26   HIS   B CA  1 
ATOM   14328 C  C   . HIS   B 1 26   ? 95.34600   55.59800  -19.05200 1.000 52.92247  ?  26   HIS   B C   1 
ATOM   14329 O  O   . HIS   B 1 26   ? 95.36500   55.99500  -17.88300 1.000 54.20805  ?  26   HIS   B O   1 
ATOM   14330 C  CB  . HIS   B 1 26   ? 93.31700   54.54000  -20.03900 1.000 57.38113  ?  26   HIS   B CB  1 
ATOM   14331 C  CG  . HIS   B 1 26   ? 92.73400   53.38100  -20.78700 1.000 66.26844  ?  26   HIS   B CG  1 
ATOM   14332 N  ND1 . HIS   B 1 26   ? 93.10000   53.06500  -22.07800 1.000 64.60939  ?  26   HIS   B ND1 1 
ATOM   14333 C  CD2 . HIS   B 1 26   ? 91.79000   52.47600  -20.43200 1.000 57.48901  ?  26   HIS   B CD2 1 
ATOM   14334 C  CE1 . HIS   B 1 26   ? 92.41400   52.01100  -22.48300 1.000 56.93682  ?  26   HIS   B CE1 1 
ATOM   14335 N  NE2 . HIS   B 1 26   ? 91.61400   51.63300  -21.50200 1.000 52.39849  ?  26   HIS   B NE2 1 
ATOM   14336 N  N   . GLU   B 1 27   ? 95.87800   56.29300  -20.05100 1.000 47.21283  ?  27   GLU   B N   1 
ATOM   14337 C  CA  . GLU   B 1 27   ? 96.38700   57.64700  -19.86900 1.000 51.98665  ?  27   GLU   B CA  1 
ATOM   14338 C  C   . GLU   B 1 27   ? 95.39600   58.61100  -20.50400 1.000 56.24489  ?  27   GLU   B C   1 
ATOM   14339 O  O   . GLU   B 1 27   ? 95.11600   58.51700  -21.70400 1.000 69.92061  ?  27   GLU   B O   1 
ATOM   14340 C  CB  . GLU   B 1 27   ? 97.78000   57.81300  -20.47600 1.000 61.88273  ?  27   GLU   B CB  1 
ATOM   14341 C  CG  . GLU   B 1 27   ? 98.52800   59.03500  -19.95100 1.000 68.54222  ?  27   GLU   B CG  1 
ATOM   14342 C  CD  . GLU   B 1 27   ? 99.55200   59.57200  -20.93300 1.000 80.63696  ?  27   GLU   B CD  1 
ATOM   14343 O  OE1 . GLU   B 1 27   ? 100.06700  58.78200  -21.75200 1.000 75.10559  ?  27   GLU   B OE1 1 
ATOM   14344 O  OE2 . GLU   B 1 27   ? 99.84200   60.78700  -20.88700 1.000 74.58046  -1 27   GLU   B OE2 1 
ATOM   14345 N  N   . VAL   B 1 28   ? 94.86700   59.52900  -19.70200 1.000 53.65851  ?  28   VAL   B N   1 
ATOM   14346 C  CA  . VAL   B 1 28   ? 93.74900   60.37600  -20.09700 1.000 52.67035  ?  28   VAL   B CA  1 
ATOM   14347 C  C   . VAL   B 1 28   ? 94.22600   61.82000  -20.15500 1.000 54.21031  ?  28   VAL   B C   1 
ATOM   14348 O  O   . VAL   B 1 28   ? 94.54100   62.42600  -19.12300 1.000 52.21412  ?  28   VAL   B O   1 
ATOM   14349 C  CB  . VAL   B 1 28   ? 92.56100   60.22900  -19.13700 1.000 47.25147  ?  28   VAL   B CB  1 
ATOM   14350 C  CG1 . VAL   B 1 28   ? 91.28000   60.67800  -19.81900 1.000 58.39530  ?  28   VAL   B CG1 1 
ATOM   14351 C  CG2 . VAL   B 1 28   ? 92.44300   58.78700  -18.66300 1.000 50.18222  ?  28   VAL   B CG2 1 
ATOM   14352 N  N   . VAL   B 1 29   ? 94.26400   62.37800  -21.36000 1.000 49.50853  ?  29   VAL   B N   1 
ATOM   14353 C  CA  . VAL   B 1 29   ? 94.47000   63.80500  -21.56500 1.000 48.91046  ?  29   VAL   B CA  1 
ATOM   14354 C  C   . VAL   B 1 29   ? 93.10300   64.45800  -21.70300 1.000 61.88648  ?  29   VAL   B C   1 
ATOM   14355 O  O   . VAL   B 1 29   ? 92.27600   64.01900  -22.51300 1.000 58.08901  ?  29   VAL   B O   1 
ATOM   14356 C  CB  . VAL   B 1 29   ? 95.33800   64.07200  -22.80500 1.000 32.44726  ?  29   VAL   B CB  1 
ATOM   14357 C  CG1 . VAL   B 1 29   ? 95.74400   65.53800  -22.86000 1.000 41.19741  ?  29   VAL   B CG1 1 
ATOM   14358 C  CG2 . VAL   B 1 29   ? 96.55600   63.16800  -22.79400 1.000 37.75475  ?  29   VAL   B CG2 1 
ATOM   14359 N  N   . ILE   B 1 30   ? 92.86000   65.49800  -20.91300 1.000 53.62817  ?  30   ILE   B N   1 
ATOM   14360 C  CA  . ILE   B 1 30   ? 91.56100   66.15600  -20.85100 1.000 49.11216  ?  30   ILE   B CA  1 
ATOM   14361 C  C   . ILE   B 1 30   ? 91.70400   67.51900  -21.51500 1.000 50.59382  ?  30   ILE   B C   1 
ATOM   14362 O  O   . ILE   B 1 30   ? 92.27500   68.45000  -20.93700 1.000 66.88189  ?  30   ILE   B O   1 
ATOM   14363 C  CB  . ILE   B 1 30   ? 91.05100   66.28000  -19.41100 1.000 37.71408  ?  30   ILE   B CB  1 
ATOM   14364 C  CG1 . ILE   B 1 30   ? 90.96400   64.89700  -18.76200 1.000 53.36669  ?  30   ILE   B CG1 1 
ATOM   14365 C  CG2 . ILE   B 1 30   ? 89.69100   66.96000  -19.38400 1.000 57.76206  ?  30   ILE   B CG2 1 
ATOM   14366 C  CD1 . ILE   B 1 30   ? 91.68200   64.79200  -17.43600 1.000 63.41730  ?  30   ILE   B CD1 1 
ATOM   14367 N  N   . CYS   B 1 31   ? 91.18200   67.64100  -22.73000 1.000 57.97749  ?  31   CYS   B N   1 
ATOM   14368 C  CA  . CYS   B 1 31   ? 91.11600   68.91500  -23.43000 1.000 65.35401  ?  31   CYS   B CA  1 
ATOM   14369 C  C   . CYS   B 1 31   ? 89.72000   69.50500  -23.28100 1.000 61.41176  ?  31   CYS   B C   1 
ATOM   14370 O  O   . CYS   B 1 31   ? 88.72600   68.77400  -23.26800 1.000 56.39614  ?  31   CYS   B O   1 
ATOM   14371 C  CB  . CYS   B 1 31   ? 91.46100   68.74400  -24.90900 1.000 65.71088  ?  31   CYS   B CB  1 
ATOM   14372 S  SG  . CYS   B 1 31   ? 92.33600   70.14700  -25.62200 1.000 79.30024  ?  31   CYS   B SG  1 
ATOM   14373 N  N   . GLN   B 1 32   ? 89.64800   70.83300  -23.16400 1.000 66.79826  ?  32   GLN   B N   1 
ATOM   14374 C  CA  . GLN   B 1 32   ? 88.37200   71.51400  -22.98900 1.000 55.79259  ?  32   GLN   B CA  1 
ATOM   14375 C  C   . GLN   B 1 32   ? 88.10500   72.61800  -24.00000 1.000 71.40359  ?  32   GLN   B C   1 
ATOM   14376 O  O   . GLN   B 1 32   ? 86.95800   73.06900  -24.09700 1.000 70.77879  ?  32   GLN   B O   1 
ATOM   14377 C  CB  . GLN   B 1 32   ? 88.26900   72.11000  -21.57700 1.000 44.22846  ?  32   GLN   B CB  1 
ATOM   14378 C  CG  . GLN   B 1 32   ? 88.46200   71.08700  -20.47600 1.000 61.67690  ?  32   GLN   B CG  1 
ATOM   14379 C  CD  . GLN   B 1 32   ? 87.45300   71.23400  -19.35900 1.000 61.55428  ?  32   GLN   B CD  1 
ATOM   14380 O  OE1 . GLN   B 1 32   ? 87.81400   71.26400  -18.18200 1.000 51.83539  ?  32   GLN   B OE1 1 
ATOM   14381 N  NE2 . GLN   B 1 32   ? 86.17800   71.32600  -19.72000 1.000 70.39775  ?  32   GLN   B NE2 1 
ATOM   14382 N  N   . GLU   B 1 33   ? 89.10900   73.07000  -24.74100 1.000 68.69604  ?  33   GLU   B N   1 
ATOM   14383 C  CA  . GLU   B 1 33   ? 88.92000   74.07800  -25.76700 1.000 52.57648  ?  33   GLU   B CA  1 
ATOM   14384 C  C   . GLU   B 1 33   ? 88.81200   73.40300  -27.13000 1.000 58.39766  ?  33   GLU   B C   1 
ATOM   14385 O  O   . GLU   B 1 33   ? 88.85600   72.17600  -27.25200 1.000 48.03156  ?  33   GLU   B O   1 
ATOM   14386 C  CB  . GLU   B 1 33   ? 90.06500   75.09400  -25.73500 1.000 81.40106  ?  33   GLU   B CB  1 
ATOM   14387 N  N   . LYS   B 1 34   ? 88.66600   74.22400  -28.17000 1.000 74.77043  ?  34   LYS   B N   1 
ATOM   14388 C  CA  . LYS   B 1 34   ? 88.56800   73.73300  -29.53900 1.000 76.60763  ?  34   LYS   B CA  1 
ATOM   14389 C  C   . LYS   B 1 34   ? 89.85600   73.03400  -29.95900 1.000 58.77597  ?  34   LYS   B C   1 
ATOM   14390 O  O   . LYS   B 1 34   ? 90.87400   73.69000  -30.20000 1.000 67.53511  ?  34   LYS   B O   1 
ATOM   14391 C  CB  . LYS   B 1 34   ? 88.25000   74.88800  -30.49400 1.000 74.90957  ?  34   LYS   B CB  1 
ATOM   14392 C  CG  . LYS   B 1 34   ? 87.41800   74.49800  -31.70800 1.000 75.47381  ?  34   LYS   B CG  1 
ATOM   14393 C  CD  . LYS   B 1 34   ? 87.20500   75.68900  -32.63000 1.000 67.13741  ?  34   LYS   B CD  1 
ATOM   14394 C  CE  . LYS   B 1 34   ? 85.90900   75.56400  -33.41300 1.000 72.39842  ?  34   LYS   B CE  1 
ATOM   14395 N  NZ  . LYS   B 1 34   ? 85.24100   76.88500  -33.57800 1.000 71.62866  ?  34   LYS   B NZ  1 
ATOM   14396 N  N   . VAL   B 1 35   ? 89.82500   71.70400  -30.04000 1.000 62.84109  ?  35   VAL   B N   1 
ATOM   14397 C  CA  . VAL   B 1 35   ? 90.99600   70.95400  -30.47700 1.000 75.28528  ?  35   VAL   B CA  1 
ATOM   14398 C  C   . VAL   B 1 35   ? 91.18300   71.13900  -31.97700 1.000 87.32919  ?  35   VAL   B C   1 
ATOM   14399 O  O   . VAL   B 1 35   ? 90.21200   71.19000  -32.74400 1.000 88.94032  ?  35   VAL   B O   1 
ATOM   14400 C  CB  . VAL   B 1 35   ? 90.85300   69.46800  -30.09900 1.000 54.00548  ?  35   VAL   B CB  1 
ATOM   14401 C  CG1 . VAL   B 1 35   ? 89.53300   68.92000  -30.59100 1.000 62.19647  ?  35   VAL   B CG1 1 
ATOM   14402 C  CG2 . VAL   B 1 35   ? 92.00600   68.64800  -30.65600 1.000 66.47626  ?  35   VAL   B CG2 1 
ATOM   14403 N  N   . HIS   B 1 36   ? 92.43800   71.26000  -32.40200 1.000 87.94300  ?  36   HIS   B N   1 
ATOM   14404 C  CA  . HIS   B 1 36   ? 92.77800   71.47500  -33.79900 1.000 90.10233  ?  36   HIS   B CA  1 
ATOM   14405 C  C   . HIS   B 1 36   ? 93.66800   70.34400  -34.29600 1.000 104.02734 ?  36   HIS   B C   1 
ATOM   14406 O  O   . HIS   B 1 36   ? 94.37100   69.69800  -33.51400 1.000 113.27643 ?  36   HIS   B O   1 
ATOM   14407 C  CB  . HIS   B 1 36   ? 93.47900   72.82200  -33.99000 1.000 96.09229  ?  36   HIS   B CB  1 
ATOM   14408 C  CG  . HIS   B 1 36   ? 92.72800   73.97600  -33.40200 1.000 110.81111 ?  36   HIS   B CG  1 
ATOM   14409 N  ND1 . HIS   B 1 36   ? 91.44700   74.30400  -33.79200 1.000 101.21788 ?  36   HIS   B ND1 1 
ATOM   14410 C  CD2 . HIS   B 1 36   ? 93.07000   74.86800  -32.44200 1.000 109.26267 ?  36   HIS   B CD2 1 
ATOM   14411 C  CE1 . HIS   B 1 36   ? 91.03600   75.35400  -33.10400 1.000 88.38903  ?  36   HIS   B CE1 1 
ATOM   14412 N  NE2 . HIS   B 1 36   ? 92.00100   75.71600  -32.27800 1.000 95.21076  ?  36   HIS   B NE2 1 
ATOM   14413 N  N   . ALA   B 1 37   ? 93.62800   70.10900  -35.61100 1.000 99.86883  ?  37   ALA   B N   1 
ATOM   14414 C  CA  . ALA   B 1 37   ? 94.41500   69.02700  -36.19400 1.000 95.55460  ?  37   ALA   B CA  1 
ATOM   14415 C  C   . ALA   B 1 37   ? 95.90800   69.24500  -35.99200 1.000 109.51565 ?  37   ALA   B C   1 
ATOM   14416 O  O   . ALA   B 1 37   ? 96.68000   68.27900  -35.96300 1.000 113.91387 ?  37   ALA   B O   1 
ATOM   14417 C  CB  . ALA   B 1 37   ? 94.09700   68.88500  -37.68200 1.000 91.35719  ?  37   ALA   B CB  1 
ATOM   14418 N  N   . GLN   B 1 38   ? 96.33200   70.50100  -35.85000 1.000 102.75361 ?  38   GLN   B N   1 
ATOM   14419 C  CA  . GLN   B 1 38   ? 97.73200   70.82300  -35.61100 1.000 109.30581 ?  38   GLN   B CA  1 
ATOM   14420 C  C   . GLN   B 1 38   ? 98.13900   70.67000  -34.15100 1.000 103.74181 ?  38   GLN   B C   1 
ATOM   14421 O  O   . GLN   B 1 38   ? 99.33800   70.72000  -33.85500 1.000 104.78255 ?  38   GLN   B O   1 
ATOM   14422 C  CB  . GLN   B 1 38   ? 98.02200   72.25400  -36.07100 1.000 123.45327 ?  38   GLN   B CB  1 
ATOM   14423 C  CG  . GLN   B 1 38   ? 96.99900   73.27500  -35.59000 1.000 125.86825 ?  38   GLN   B CG  1 
ATOM   14424 C  CD  . GLN   B 1 38   ? 97.39300   73.93000  -34.27800 1.000 135.73001 ?  38   GLN   B CD  1 
ATOM   14425 O  OE1 . GLN   B 1 38   ? 96.76900   73.69500  -33.24200 1.000 139.22956 ?  38   GLN   B OE1 1 
ATOM   14426 N  NE2 . GLN   B 1 38   ? 98.43000   74.75900  -34.31700 1.000 119.44982 ?  38   GLN   B NE2 1 
ATOM   14427 N  N   . SER   B 1 39   ? 97.18300   70.48600  -33.24300 1.000 99.87069  ?  39   SER   B N   1 
ATOM   14428 C  CA  . SER   B 1 39   ? 97.49200   70.42500  -31.82100 1.000 101.17398 ?  39   SER   B CA  1 
ATOM   14429 C  C   . SER   B 1 39   ? 98.30100   69.17600  -31.48600 1.000 96.55690  ?  39   SER   B C   1 
ATOM   14430 O  O   . SER   B 1 39   ? 98.13600   68.11600  -32.09500 1.000 97.69860  ?  39   SER   B O   1 
ATOM   14431 C  CB  . SER   B 1 39   ? 96.20500   70.44600  -30.99300 1.000 101.47250 ?  39   SER   B CB  1 
ATOM   14432 O  OG  . SER   B 1 39   ? 96.46200   70.15400  -29.62900 1.000 95.53520  ?  39   SER   B OG  1 
ATOM   14433 N  N   . ALA   B 1 40   ? 99.19100   69.31800  -30.49900 1.000 89.12386  ?  40   ALA   B N   1 
ATOM   14434 C  CA  . ALA   B 1 40   ? 99.95600   68.17800  -30.00700 1.000 87.84961  ?  40   ALA   B CA  1 
ATOM   14435 C  C   . ALA   B 1 40   ? 99.10000   67.23400  -29.17700 1.000 93.93986  ?  40   ALA   B C   1 
ATOM   14436 O  O   . ALA   B 1 40   ? 99.42900   66.04700  -29.07000 1.000 86.72351  ?  40   ALA   B O   1 
ATOM   14437 C  CB  . ALA   B 1 40   ? 101.15400  68.65800  -29.18700 1.000 85.54562  ?  40   ALA   B CB  1 
ATOM   14438 N  N   . ASN   B 1 41   ? 98.00200   67.73000  -28.60200 1.000 97.46688  ?  41   ASN   B N   1 
ATOM   14439 C  CA  . ASN   B 1 41   ? 97.05300   66.88900  -27.88700 1.000 85.69773  ?  41   ASN   B CA  1 
ATOM   14440 C  C   . ASN   B 1 41   ? 96.39300   65.84900  -28.78900 1.000 82.83534  ?  41   ASN   B C   1 
ATOM   14441 O  O   . ASN   B 1 41   ? 95.62700   65.01600  -28.28800 1.000 92.28674  ?  41   ASN   B O   1 
ATOM   14442 C  CB  . ASN   B 1 41   ? 95.98300   67.76600  -27.23200 1.000 82.91007  ?  41   ASN   B CB  1 
ATOM   14443 C  CG  . ASN   B 1 41   ? 96.42800   68.32900  -25.90800 1.000 96.51330  ?  41   ASN   B CG  1 
ATOM   14444 O  OD1 . ASN   B 1 41   ? 97.62200   68.37900  -25.61700 1.000 96.25193  ?  41   ASN   B OD1 1 
ATOM   14445 N  ND2 . ASN   B 1 41   ? 95.47200   68.75600  -25.09200 1.000 84.93038  ?  41   ASN   B ND2 1 
ATOM   14446 N  N   . LEU   B 1 42   ? 96.66100   65.88300  -30.09800 1.000 80.70465  ?  42   LEU   B N   1 
ATOM   14447 C  CA  . LEU   B 1 42   ? 96.12900   64.92200  -31.05900 1.000 80.81883  ?  42   LEU   B CA  1 
ATOM   14448 C  C   . LEU   B 1 42   ? 97.14700   63.87200  -31.48600 1.000 79.03864  ?  42   LEU   B C   1 
ATOM   14449 O  O   . LEU   B 1 42   ? 96.77800   62.91500  -32.17600 1.000 68.93803  ?  42   LEU   B O   1 
ATOM   14450 C  CB  . LEU   B 1 42   ? 95.62000   65.65400  -32.30500 1.000 84.02913  ?  42   LEU   B CB  1 
ATOM   14451 C  CG  . LEU   B 1 42   ? 94.11600   65.87700  -32.42100 1.000 86.09391  ?  42   LEU   B CG  1 
ATOM   14452 C  CD1 . LEU   B 1 42   ? 93.75100   65.99600  -33.88400 1.000 98.05454  ?  42   LEU   B CD1 1 
ATOM   14453 C  CD2 . LEU   B 1 42   ? 93.35200   64.74500  -31.75600 1.000 86.98247  ?  42   LEU   B CD2 1 
ATOM   14454 N  N   . GLN   B 1 43   ? 98.40900   64.03000  -31.10600 1.000 77.63449  ?  43   GLN   B N   1 
ATOM   14455 C  CA  . GLN   B 1 43   ? 99.45800   63.10800  -31.50900 1.000 72.79022  ?  43   GLN   B CA  1 
ATOM   14456 C  C   . GLN   B 1 43   ? 99.62600   62.00800  -30.47000 1.000 83.94546  ?  43   GLN   B C   1 
ATOM   14457 O  O   . GLN   B 1 43   ? 99.55500   62.26000  -29.26300 1.000 79.78834  ?  43   GLN   B O   1 
ATOM   14458 C  CB  . GLN   B 1 43   ? 100.77400  63.85900  -31.71400 1.000 74.86754  ?  43   GLN   B CB  1 
ATOM   14459 C  CG  . GLN   B 1 43   ? 100.66300  65.02200  -32.69100 1.000 84.46491  ?  43   GLN   B CG  1 
ATOM   14460 C  CD  . GLN   B 1 43   ? 101.67400  66.12100  -32.42300 1.000 92.25633  ?  43   GLN   B CD  1 
ATOM   14461 O  OE1 . GLN   B 1 43   ? 102.59500  65.95300  -31.62300 1.000 95.75078  ?  43   GLN   B OE1 1 
ATOM   14462 N  NE2 . GLN   B 1 43   ? 101.50100  67.25800  -33.08700 1.000 82.60505  ?  43   GLN   B NE2 1 
ATOM   14463 N  N   . GLU   B 1 44   ? 99.83900   60.78200  -30.95700 1.000 73.44517  ?  44   GLU   B N   1 
ATOM   14464 C  CA  . GLU   B 1 44   ? 99.98900   59.59100  -30.11900 1.000 80.65358  ?  44   GLU   B CA  1 
ATOM   14465 C  C   . GLU   B 1 44   ? 98.72200   59.29300  -29.32200 1.000 78.10798  ?  44   GLU   B C   1 
ATOM   14466 O  O   . GLU   B 1 44   ? 98.77900   58.71400  -28.23400 1.000 72.63010  ?  44   GLU   B O   1 
ATOM   14467 C  CB  . GLU   B 1 44   ? 101.19600  59.71100  -29.18100 1.000 88.95383  ?  44   GLU   B CB  1 
ATOM   14468 N  N   . ILE   B 1 45   ? 97.56800   59.68100  -29.85800 1.000 77.01412  ?  45   ILE   B N   1 
ATOM   14469 C  CA  . ILE   B 1 45   ? 96.27700   59.42300  -29.23200 1.000 65.05472  ?  45   ILE   B CA  1 
ATOM   14470 C  C   . ILE   B 1 45   ? 95.64100   58.22400  -29.91900 1.000 65.95484  ?  45   ILE   B C   1 
ATOM   14471 O  O   . ILE   B 1 45   ? 95.51800   58.19600  -31.15000 1.000 72.15996  ?  45   ILE   B O   1 
ATOM   14472 C  CB  . ILE   B 1 45   ? 95.36200   60.65700  -29.31200 1.000 63.49730  ?  45   ILE   B CB  1 
ATOM   14473 C  CG1 . ILE   B 1 45   ? 95.78700   61.70600  -28.28100 1.000 60.62512  ?  45   ILE   B CG1 1 
ATOM   14474 C  CG2 . ILE   B 1 45   ? 93.90900   60.25700  -29.10400 1.000 73.59901  ?  45   ILE   B CG2 1 
ATOM   14475 C  CD1 . ILE   B 1 45   ? 95.68100   61.23500  -26.84500 1.000 55.33201  ?  45   ILE   B CD1 1 
ATOM   14476 N  N   . ASP   B 1 46   ? 95.23900   57.23100  -29.12600 1.000 60.50638  ?  46   ASP   B N   1 
ATOM   14477 C  CA  . ASP   B 1 46   ? 94.64900   56.01200  -29.66300 1.000 71.05352  ?  46   ASP   B CA  1 
ATOM   14478 C  C   . ASP   B 1 46   ? 93.12900   55.99100  -29.59500 1.000 66.31115  ?  46   ASP   B C   1 
ATOM   14479 O  O   . ASP   B 1 46   ? 92.50500   55.22500  -30.33700 1.000 60.66419  ?  46   ASP   B O   1 
ATOM   14480 C  CB  . ASP   B 1 46   ? 95.19800   54.78500  -28.92400 1.000 76.92526  ?  46   ASP   B CB  1 
ATOM   14481 C  CG  . ASP   B 1 46   ? 96.69300   54.86600  -28.68900 1.000 77.56460  ?  46   ASP   B CG  1 
ATOM   14482 O  OD1 . ASP   B 1 46   ? 97.38100   55.57600  -29.45400 1.000 88.90630  ?  46   ASP   B OD1 1 
ATOM   14483 O  OD2 . ASP   B 1 46   ? 97.17900   54.21400  -27.74200 1.000 79.08443  -1 46   ASP   B OD2 1 
ATOM   14484 N  N   . TRP   B 1 47   ? 92.52200   56.79800  -28.72900 1.000 69.19957  ?  47   TRP   B N   1 
ATOM   14485 C  CA  . TRP   B 1 47   ? 91.07200   56.87500  -28.63500 1.000 59.16491  ?  47   TRP   B CA  1 
ATOM   14486 C  C   . TRP   B 1 47   ? 90.68000   58.29100  -28.24800 1.000 56.66407  ?  47   TRP   B C   1 
ATOM   14487 O  O   . TRP   B 1 47   ? 91.35700   58.92700  -27.43600 1.000 62.69426  ?  47   TRP   B O   1 
ATOM   14488 C  CB  . TRP   B 1 47   ? 90.51000   55.88900  -27.60500 1.000 54.06652  ?  47   TRP   B CB  1 
ATOM   14489 C  CG  . TRP   B 1 47   ? 90.50300   54.45900  -28.04300 1.000 57.60421  ?  47   TRP   B CG  1 
ATOM   14490 C  CD1 . TRP   B 1 47   ? 91.43700   53.51000  -27.75200 1.000 63.24434  ?  47   TRP   B CD1 1 
ATOM   14491 C  CD2 . TRP   B 1 47   ? 89.50300   53.80900  -28.83400 1.000 63.99317  ?  47   TRP   B CD2 1 
ATOM   14492 N  NE1 . TRP   B 1 47   ? 91.08500   52.31000  -28.31800 1.000 73.35803  ?  47   TRP   B NE1 1 
ATOM   14493 C  CE2 . TRP   B 1 47   ? 89.90100   52.46700  -28.98900 1.000 68.17575  ?  47   TRP   B CE2 1 
ATOM   14494 C  CE3 . TRP   B 1 47   ? 88.31200   54.23300  -29.43100 1.000 76.22135  ?  47   TRP   B CE3 1 
ATOM   14495 C  CZ2 . TRP   B 1 47   ? 89.15200   51.54500  -29.71600 1.000 72.26399  ?  47   TRP   B CZ2 1 
ATOM   14496 C  CZ3 . TRP   B 1 47   ? 87.56900   53.31600  -30.15200 1.000 76.27645  ?  47   TRP   B CZ3 1 
ATOM   14497 C  CH2 . TRP   B 1 47   ? 87.99200   51.98800  -30.28800 1.000 78.78985  ?  47   TRP   B CH2 1 
ATOM   14498 N  N   . ILE   B 1 48   ? 89.58700   58.77500  -28.82800 1.000 68.61912  ?  48   ILE   B N   1 
ATOM   14499 C  CA  . ILE   B 1 48   ? 89.00900   60.06600  -28.47400 1.000 56.64671  ?  48   ILE   B CA  1 
ATOM   14500 C  C   . ILE   B 1 48   ? 87.62500   59.80900  -27.89700 1.000 58.63550  ?  48   ILE   B C   1 
ATOM   14501 O  O   . ILE   B 1 48   ? 86.75300   59.26300  -28.58300 1.000 62.37287  ?  48   ILE   B O   1 
ATOM   14502 C  CB  . ILE   B 1 48   ? 88.93500   61.01500  -29.68000 1.000 52.79114  ?  48   ILE   B CB  1 
ATOM   14503 C  CG1 . ILE   B 1 48   ? 90.33500   61.25900  -30.25000 1.000 70.88022  ?  48   ILE   B CG1 1 
ATOM   14504 C  CG2 . ILE   B 1 48   ? 88.28000   62.32800  -29.27800 1.000 52.34025  ?  48   ILE   B CG2 1 
ATOM   14505 C  CD1 . ILE   B 1 48   ? 90.39900   62.36700  -31.28200 1.000 53.48142  ?  48   ILE   B CD1 1 
ATOM   14506 N  N   . VAL   B 1 49   ? 87.42800   60.18800  -26.63900 1.000 51.16469  ?  49   VAL   B N   1 
ATOM   14507 C  CA  . VAL   B 1 49   ? 86.14800   60.03200  -25.96000 1.000 48.15064  ?  49   VAL   B CA  1 
ATOM   14508 C  C   . VAL   B 1 49   ? 85.61100   61.42200  -25.64900 1.000 47.84831  ?  49   VAL   B C   1 
ATOM   14509 O  O   . VAL   B 1 49   ? 86.28800   62.22200  -24.99000 1.000 53.42867  ?  49   VAL   B O   1 
ATOM   14510 C  CB  . VAL   B 1 49   ? 86.27800   59.18900  -24.68300 1.000 52.29671  ?  49   VAL   B CB  1 
ATOM   14511 C  CG1 . VAL   B 1 49   ? 84.97900   59.21500  -23.89700 1.000 43.37345  ?  49   VAL   B CG1 1 
ATOM   14512 C  CG2 . VAL   B 1 49   ? 86.66500   57.76200  -25.03500 1.000 47.71062  ?  49   VAL   B CG2 1 
ATOM   14513 N  N   . SER   B 1 50   ? 84.40400   61.71100  -26.12500 1.000 49.53151  ?  50   SER   B N   1 
ATOM   14514 C  CA  . SER   B 1 50   ? 83.77700   63.00700  -25.91900 1.000 48.31647  ?  50   SER   B CA  1 
ATOM   14515 C  C   . SER   B 1 50   ? 82.55100   62.86700  -25.02600 1.000 46.18325  ?  50   SER   B C   1 
ATOM   14516 O  O   . SER   B 1 50   ? 81.92200   61.80700  -24.95800 1.000 45.55351  ?  50   SER   B O   1 
ATOM   14517 C  CB  . SER   B 1 50   ? 83.38200   63.65400  -27.25100 1.000 37.81886  ?  50   SER   B CB  1 
ATOM   14518 O  OG  . SER   B 1 50   ? 82.36500   62.91700  -27.90600 1.000 55.20337  ?  50   SER   B OG  1 
ATOM   14519 N  N   . TYR   B 1 51   ? 82.22100   63.96000  -24.34300 1.000 48.78600  ?  51   TYR   B N   1 
ATOM   14520 C  CA  . TYR   B 1 51   ? 81.11600   63.99700  -23.39500 1.000 33.09816  ?  51   TYR   B CA  1 
ATOM   14521 C  C   . TYR   B 1 51   ? 80.81800   65.45200  -23.05500 1.000 41.35594  ?  51   TYR   B C   1 
ATOM   14522 O  O   . TYR   B 1 51   ? 81.60500   66.10200  -22.35900 1.000 46.78348  ?  51   TYR   B O   1 
ATOM   14523 C  CB  . TYR   B 1 51   ? 81.46000   63.18900  -22.14100 1.000 43.43869  ?  51   TYR   B CB  1 
ATOM   14524 C  CG  . TYR   B 1 51   ? 80.32600   63.02100  -21.15400 1.000 49.23383  ?  51   TYR   B CG  1 
ATOM   14525 C  CD1 . TYR   B 1 51   ? 79.00100   63.09400  -21.56200 1.000 55.98344  ?  51   TYR   B CD1 1 
ATOM   14526 C  CD2 . TYR   B 1 51   ? 80.58500   62.78400  -19.81100 1.000 40.72843  ?  51   TYR   B CD2 1 
ATOM   14527 C  CE1 . TYR   B 1 51   ? 77.96500   62.93900  -20.65600 1.000 45.30713  ?  51   TYR   B CE1 1 
ATOM   14528 C  CE2 . TYR   B 1 51   ? 79.55800   62.62800  -18.90000 1.000 48.74698  ?  51   TYR   B CE2 1 
ATOM   14529 C  CZ  . TYR   B 1 51   ? 78.25100   62.70600  -19.32700 1.000 45.67619  ?  51   TYR   B CZ  1 
ATOM   14530 O  OH  . TYR   B 1 51   ? 77.22900   62.55100  -18.42000 1.000 58.16170  ?  51   TYR   B OH  1 
ATOM   14531 N  N   . ALA   B 1 52   ? 79.70200   65.97100  -23.56200 1.000 36.34738  ?  52   ALA   B N   1 
ATOM   14532 C  CA  . ALA   B 1 52   ? 79.33100   67.37500  -23.40400 1.000 35.38648  ?  52   ALA   B CA  1 
ATOM   14533 C  C   . ALA   B 1 52   ? 80.43500   68.29000  -23.93400 1.000 41.59419  ?  52   ALA   B C   1 
ATOM   14534 O  O   . ALA   B 1 52   ? 80.95500   69.16300  -23.23600 1.000 43.89945  ?  52   ALA   B O   1 
ATOM   14535 C  CB  . ALA   B 1 52   ? 78.99600   67.69600  -21.94400 1.000 29.41581  ?  52   ALA   B CB  1 
ATOM   14536 N  N   . TYR   B 1 53   ? 80.79800   68.06500  -25.19500 1.000 44.06628  ?  53   TYR   B N   1 
ATOM   14537 C  CA  . TYR   B 1 53   ? 81.79000   68.88100  -25.88300 1.000 43.68406  ?  53   TYR   B CA  1 
ATOM   14538 C  C   . TYR   B 1 53   ? 81.07200   69.97300  -26.66600 1.000 41.66360  ?  53   TYR   B C   1 
ATOM   14539 O  O   . TYR   B 1 53   ? 80.24500   69.67600  -27.53500 1.000 43.33009  ?  53   TYR   B O   1 
ATOM   14540 C  CB  . TYR   B 1 53   ? 82.65600   68.03300  -26.81300 1.000 48.24955  ?  53   TYR   B CB  1 
ATOM   14541 C  CG  . TYR   B 1 53   ? 83.87100   68.76800  -27.32800 1.000 53.98692  ?  53   TYR   B CG  1 
ATOM   14542 C  CD1 . TYR   B 1 53   ? 84.73700   69.41000  -26.45200 1.000 51.47404  ?  53   TYR   B CD1 1 
ATOM   14543 C  CD2 . TYR   B 1 53   ? 84.14900   68.83000  -28.68700 1.000 58.35546  ?  53   TYR   B CD2 1 
ATOM   14544 C  CE1 . TYR   B 1 53   ? 85.85100   70.08900  -26.91400 1.000 59.43544  ?  53   TYR   B CE1 1 
ATOM   14545 C  CE2 . TYR   B 1 53   ? 85.26100   69.50700  -29.16000 1.000 64.74818  ?  53   TYR   B CE2 1 
ATOM   14546 C  CZ  . TYR   B 1 53   ? 86.10900   70.13500  -28.27000 1.000 64.34817  ?  53   TYR   B CZ  1 
ATOM   14547 O  OH  . TYR   B 1 53   ? 87.21500   70.80800  -28.74000 1.000 50.53980  ?  53   TYR   B OH  1 
ATOM   14548 N  N   . GLY   B 1 54   ? 81.39500   71.22900  -26.36600 1.000 40.31737  ?  54   GLY   B N   1 
ATOM   14549 C  CA  . GLY   B 1 54   ? 80.66600   72.35000  -26.93000 1.000 51.90070  ?  54   GLY   B CA  1 
ATOM   14550 C  C   . GLY   B 1 54   ? 81.23100   72.91000  -28.21800 1.000 55.60125  ?  54   GLY   B C   1 
ATOM   14551 O  O   . GLY   B 1 54   ? 80.97900   74.07000  -28.55900 1.000 64.13649  ?  54   GLY   B O   1 
ATOM   14552 N  N   . TYR   B 1 55   ? 81.99600   72.10100  -28.94600 1.000 55.64864  ?  55   TYR   B N   1 
ATOM   14553 C  CA  . TYR   B 1 55   ? 82.55200   72.51400  -30.22400 1.000 46.07524  ?  55   TYR   B CA  1 
ATOM   14554 C  C   . TYR   B 1 55   ? 82.39500   71.37500  -31.21700 1.000 47.97636  ?  55   TYR   B C   1 
ATOM   14555 O  O   . TYR   B 1 55   ? 82.13400   70.22900  -30.84300 1.000 49.64397  ?  55   TYR   B O   1 
ATOM   14556 C  CB  . TYR   B 1 55   ? 84.02900   72.91800  -30.10500 1.000 52.46689  ?  55   TYR   B CB  1 
ATOM   14557 C  CG  . TYR   B 1 55   ? 84.29600   74.00600  -29.08600 1.000 56.61495  ?  55   TYR   B CG  1 
ATOM   14558 C  CD1 . TYR   B 1 55   ? 83.91200   75.31900  -29.32500 1.000 55.10618  ?  55   TYR   B CD1 1 
ATOM   14559 C  CD2 . TYR   B 1 55   ? 84.93900   73.72000  -27.88800 1.000 60.18313  ?  55   TYR   B CD2 1 
ATOM   14560 C  CE1 . TYR   B 1 55   ? 84.15800   76.31700  -28.39500 1.000 64.34708  ?  55   TYR   B CE1 1 
ATOM   14561 C  CE2 . TYR   B 1 55   ? 85.18800   74.71000  -26.95300 1.000 61.50296  ?  55   TYR   B CE2 1 
ATOM   14562 C  CZ  . TYR   B 1 55   ? 84.79700   76.00600  -27.21100 1.000 58.23463  ?  55   TYR   B CZ  1 
ATOM   14563 O  OH  . TYR   B 1 55   ? 85.04600   76.99000  -26.28100 1.000 48.20302  ?  55   TYR   B OH  1 
ATOM   14564 N  N   . ILE   B 1 56   ? 82.55400   71.70400  -32.49400 1.000 54.07349  ?  56   ILE   B N   1 
ATOM   14565 C  CA  . ILE   B 1 56   ? 82.48200   70.72900  -33.57500 1.000 56.26252  ?  56   ILE   B CA  1 
ATOM   14566 C  C   . ILE   B 1 56   ? 83.89900   70.41600  -34.03300 1.000 68.19853  ?  56   ILE   B C   1 
ATOM   14567 O  O   . ILE   B 1 56   ? 84.69400   71.33100  -34.28700 1.000 60.10638  ?  56   ILE   B O   1 
ATOM   14568 C  CB  . ILE   B 1 56   ? 81.62400   71.25000  -34.74100 1.000 52.71663  ?  56   ILE   B CB  1 
ATOM   14569 C  CG1 . ILE   B 1 56   ? 80.14100   71.20500  -34.36900 1.000 56.53791  ?  56   ILE   B CG1 1 
ATOM   14570 C  CG2 . ILE   B 1 56   ? 81.87900   70.43700  -35.99900 1.000 46.32295  ?  56   ILE   B CG2 1 
ATOM   14571 C  CD1 . ILE   B 1 56   ? 79.21100   71.31800  -35.55500 1.000 59.21130  ?  56   ILE   B CD1 1 
ATOM   14572 N  N   . LEU   B 1 57   ? 84.21900   69.12700  -34.12600 1.000 73.43124  ?  57   LEU   B N   1 
ATOM   14573 C  CA  . LEU   B 1 57   ? 85.53100   68.70800  -34.59800 1.000 63.49231  ?  57   LEU   B CA  1 
ATOM   14574 C  C   . LEU   B 1 57   ? 85.67200   68.96200  -36.09400 1.000 75.74697  ?  57   LEU   B C   1 
ATOM   14575 O  O   . LEU   B 1 57   ? 84.70700   68.86300  -36.85800 1.000 81.83281  ?  57   LEU   B O   1 
ATOM   14576 C  CB  . LEU   B 1 57   ? 85.75900   67.22500  -34.30900 1.000 54.21483  ?  57   LEU   B CB  1 
ATOM   14577 C  CG  . LEU   B 1 57   ? 85.64100   66.79400  -32.85000 1.000 61.01614  ?  57   LEU   B CG  1 
ATOM   14578 C  CD1 . LEU   B 1 57   ? 86.00400   65.32500  -32.69200 1.000 52.19480  ?  57   LEU   B CD1 1 
ATOM   14579 C  CD2 . LEU   B 1 57   ? 86.52300   67.66600  -31.98200 1.000 50.91393  ?  57   LEU   B CD2 1 
ATOM   14580 N  N   . ASP   B 1 58   ? 86.89300   69.28800  -36.50900 1.000 71.25038  ?  58   ASP   B N   1 
ATOM   14581 C  CA  . ASP   B 1 58   ? 87.17100   69.45900  -37.92700 1.000 74.00330  ?  58   ASP   B CA  1 
ATOM   14582 C  C   . ASP   B 1 58   ? 86.98700   68.13600  -38.66300 1.000 81.23511  ?  58   ASP   B C   1 
ATOM   14583 O  O   . ASP   B 1 58   ? 87.16100   67.05300  -38.09500 1.000 59.74969  ?  58   ASP   B O   1 
ATOM   14584 C  CB  . ASP   B 1 58   ? 88.59100   69.98800  -38.13300 1.000 65.40618  ?  58   ASP   B CB  1 
ATOM   14585 C  CG  . ASP   B 1 58   ? 88.79900   70.57700  -39.51600 1.000 102.25148 ?  58   ASP   B CG  1 
ATOM   14586 O  OD1 . ASP   B 1 58   ? 88.80900   69.80700  -40.50100 1.000 94.20556  ?  58   ASP   B OD1 1 
ATOM   14587 O  OD2 . ASP   B 1 58   ? 88.95000   71.81200  -39.61800 1.000 123.72168 -1 58   ASP   B OD2 1 
ATOM   14588 N  N   . LYS   B 1 59   ? 86.61900   68.23400  -39.94500 1.000 87.51042  ?  59   LYS   B N   1 
ATOM   14589 C  CA  . LYS   B 1 59   ? 86.38500   67.03500  -40.74500 1.000 68.31367  ?  59   LYS   B CA  1 
ATOM   14590 C  C   . LYS   B 1 59   ? 87.64400   66.18700  -40.86800 1.000 71.44996  ?  59   LYS   B C   1 
ATOM   14591 O  O   . LYS   B 1 59   ? 87.55600   64.95500  -40.94300 1.000 59.65703  ?  59   LYS   B O   1 
ATOM   14592 C  CB  . LYS   B 1 59   ? 85.86700   67.42200  -42.13000 1.000 68.31095  ?  59   LYS   B CB  1 
ATOM   14593 N  N   . GLU   B 1 60   ? 88.81800   66.82400  -40.88500 1.000 81.14512  ?  60   GLU   B N   1 
ATOM   14594 C  CA  . GLU   B 1 60   ? 90.07000   66.07600  -40.95100 1.000 71.85427  ?  60   GLU   B CA  1 
ATOM   14595 C  C   . GLU   B 1 60   ? 90.28600   65.24800  -39.68900 1.000 75.29858  ?  60   GLU   B C   1 
ATOM   14596 O  O   . GLU   B 1 60   ? 90.77900   64.11600  -39.76000 1.000 66.50661  ?  60   GLU   B O   1 
ATOM   14597 C  CB  . GLU   B 1 60   ? 91.24000   67.03500  -41.17400 1.000 64.37296  ?  60   GLU   B CB  1 
ATOM   14598 N  N   . ILE   B 1 61   ? 89.91800   65.79400  -38.52800 1.000 76.41354  ?  61   ILE   B N   1 
ATOM   14599 C  CA  . ILE   B 1 61   ? 90.06700   65.05600  -37.27700 1.000 67.32758  ?  61   ILE   B CA  1 
ATOM   14600 C  C   . ILE   B 1 61   ? 89.17400   63.82200  -37.27800 1.000 61.98076  ?  61   ILE   B C   1 
ATOM   14601 O  O   . ILE   B 1 61   ? 89.56700   62.75000  -36.80200 1.000 64.98189  ?  61   ILE   B O   1 
ATOM   14602 C  CB  . ILE   B 1 61   ? 89.76500   65.97300  -36.07800 1.000 62.77250  ?  61   ILE   B CB  1 
ATOM   14603 C  CG1 . ILE   B 1 61   ? 90.78700   67.11100  -36.00600 1.000 56.93153  ?  61   ILE   B CG1 1 
ATOM   14604 C  CG2 . ILE   B 1 61   ? 89.76900   65.17200  -34.78400 1.000 51.08563  ?  61   ILE   B CG2 1 
ATOM   14605 C  CD1 . ILE   B 1 61   ? 90.80100   67.84700  -34.68200 1.000 63.14092  ?  61   ILE   B CD1 1 
ATOM   14606 N  N   . VAL   B 1 62   ? 87.95900   63.95200  -37.81900 1.000 66.12307  ?  62   VAL   B N   1 
ATOM   14607 C  CA  . VAL   B 1 62   ? 87.03700   62.82000  -37.86000 1.000 61.70622  ?  62   VAL   B CA  1 
ATOM   14608 C  C   . VAL   B 1 62   ? 87.58600   61.71500  -38.75100 1.000 68.91362  ?  62   VAL   B C   1 
ATOM   14609 O  O   . VAL   B 1 62   ? 87.43400   60.52400  -38.45500 1.000 68.59107  ?  62   VAL   B O   1 
ATOM   14610 C  CB  . VAL   B 1 62   ? 85.64500   63.28000  -38.33100 1.000 60.67287  ?  62   VAL   B CB  1 
ATOM   14611 C  CG1 . VAL   B 1 62   ? 84.64000   62.15200  -38.17500 1.000 55.55415  ?  62   VAL   B CG1 1 
ATOM   14612 C  CG2 . VAL   B 1 62   ? 85.19900   64.50800  -37.55700 1.000 58.73822  ?  62   VAL   B CG2 1 
ATOM   14613 N  N   . SER   B 1 63   ? 88.23000   62.09000  -39.85900 1.000 77.93587  ?  63   SER   B N   1 
ATOM   14614 C  CA  . SER   B 1 63   ? 88.77700   61.08700  -40.76600 1.000 79.86620  ?  63   SER   B CA  1 
ATOM   14615 C  C   . SER   B 1 63   ? 90.02800   60.44200  -40.18500 1.000 83.33881  ?  63   SER   B C   1 
ATOM   14616 O  O   . SER   B 1 63   ? 90.24100   59.23400  -40.34700 1.000 83.60214  ?  63   SER   B O   1 
ATOM   14617 C  CB  . SER   B 1 63   ? 89.07800   61.71800  -42.12400 1.000 73.38133  ?  63   SER   B CB  1 
ATOM   14618 O  OG  . SER   B 1 63   ? 89.66500   62.99800  -41.96700 1.000 78.35607  ?  63   SER   B OG  1 
ATOM   14619 N  N   . ARG   B 1 64   ? 90.86900   61.23400  -39.51200 1.000 64.14919  ?  64   ARG   B N   1 
ATOM   14620 C  CA  . ARG   B 1 64   ? 92.06100   60.68500  -38.87400 1.000 61.80854  ?  64   ARG   B CA  1 
ATOM   14621 C  C   . ARG   B 1 64   ? 91.69400   59.58600  -37.88700 1.000 68.81885  ?  64   ARG   B C   1 
ATOM   14622 O  O   . ARG   B 1 64   ? 92.28400   58.49900  -37.89700 1.000 65.84732  ?  64   ARG   B O   1 
ATOM   14623 C  CB  . ARG   B 1 64   ? 92.83400   61.79600  -38.16400 1.000 71.75886  ?  64   ARG   B CB  1 
ATOM   14624 C  CG  . ARG   B 1 64   ? 93.75000   62.62100  -39.04500 1.000 72.19767  ?  64   ARG   B CG  1 
ATOM   14625 C  CD  . ARG   B 1 64   ? 94.87200   63.21800  -38.20700 1.000 79.33333  ?  64   ARG   B CD  1 
ATOM   14626 N  NE  . ARG   B 1 64   ? 95.39600   62.24700  -37.25300 1.000 83.84466  ?  64   ARG   B NE  1 
ATOM   14627 C  CZ  . ARG   B 1 64   ? 96.46700   62.43800  -36.49600 1.000 90.25778  ?  64   ARG   B CZ  1 
ATOM   14628 N  NH1 . ARG   B 1 64   ? 97.15800   63.56600  -36.54700 1.000 83.75387  ?  64   ARG   B NH1 1 
ATOM   14629 N  NH2 . ARG   B 1 64   ? 96.85600   61.47400  -35.66500 1.000 85.81466  ?  64   ARG   B NH2 1 
ATOM   14630 N  N   . PHE   B 1 65   ? 90.70700   59.84900  -37.03200 1.000 64.51571  ?  65   PHE   B N   1 
ATOM   14631 C  CA  . PHE   B 1 65   ? 90.32500   58.94100  -35.96000 1.000 65.96574  ?  65   PHE   B CA  1 
ATOM   14632 C  C   . PHE   B 1 65   ? 88.99400   58.25300  -36.24400 1.000 63.49278  ?  65   PHE   B C   1 
ATOM   14633 O  O   . PHE   B 1 65   ? 88.22700   57.97400  -35.32000 1.000 63.83323  ?  65   PHE   B O   1 
ATOM   14634 C  CB  . PHE   B 1 65   ? 90.26700   59.68800  -34.62900 1.000 58.42402  ?  65   PHE   B CB  1 
ATOM   14635 C  CG  . PHE   B 1 65   ? 91.55400   60.37100  -34.25200 1.000 67.38434  ?  65   PHE   B CG  1 
ATOM   14636 C  CD1 . PHE   B 1 65   ? 91.88900   61.60500  -34.79100 1.000 70.94948  ?  65   PHE   B CD1 1 
ATOM   14637 C  CD2 . PHE   B 1 65   ? 92.42500   59.78300  -33.34900 1.000 61.17806  ?  65   PHE   B CD2 1 
ATOM   14638 C  CE1 . PHE   B 1 65   ? 93.07200   62.23300  -34.44300 1.000 71.56013  ?  65   PHE   B CE1 1 
ATOM   14639 C  CE2 . PHE   B 1 65   ? 93.60700   60.40700  -32.99600 1.000 67.48117  ?  65   PHE   B CE2 1 
ATOM   14640 C  CZ  . PHE   B 1 65   ? 93.93100   61.63400  -33.54400 1.000 79.25048  ?  65   PHE   B CZ  1 
ATOM   14641 N  N   . ARG   B 1 66   ? 88.70500   57.98200  -37.51600 1.000 61.25159  ?  66   ARG   B N   1 
ATOM   14642 C  CA  . ARG   B 1 66   ? 87.46700   57.30200  -37.87300 1.000 59.87694  ?  66   ARG   B CA  1 
ATOM   14643 C  C   . ARG   B 1 66   ? 87.39400   55.94800  -37.17600 1.000 56.42363  ?  66   ARG   B C   1 
ATOM   14644 O  O   . ARG   B 1 66   ? 88.31600   55.13400  -37.27100 1.000 62.46283  ?  66   ARG   B O   1 
ATOM   14645 C  CB  . ARG   B 1 66   ? 87.37700   57.13500  -39.39000 1.000 51.52155  ?  66   ARG   B CB  1 
ATOM   14646 N  N   . GLY   B 1 67   ? 86.29500   55.71600  -36.46100 1.000 60.25271  ?  67   GLY   B N   1 
ATOM   14647 C  CA  . GLY   B 1 67   ? 86.17500   54.54800  -35.61600 1.000 64.66844  ?  67   GLY   B CA  1 
ATOM   14648 C  C   . GLY   B 1 67   ? 86.81300   54.68700  -34.25300 1.000 72.27957  ?  67   GLY   B C   1 
ATOM   14649 O  O   . GLY   B 1 67   ? 86.75100   53.73900  -33.45800 1.000 64.07746  ?  67   GLY   B O   1 
ATOM   14650 N  N   . ARG   B 1 68   ? 87.41700   55.83800  -33.95100 1.000 73.18846  ?  68   ARG   B N   1 
ATOM   14651 C  CA  . ARG   B 1 68   ? 88.11000   56.05300  -32.69000 1.000 67.70055  ?  68   ARG   B CA  1 
ATOM   14652 C  C   . ARG   B 1 68   ? 87.60200   57.25900  -31.90800 1.000 68.64921  ?  68   ARG   B C   1 
ATOM   14653 O  O   . ARG   B 1 68   ? 88.12700   57.53600  -30.82300 1.000 69.38323  ?  68   ARG   B O   1 
ATOM   14654 C  CB  . ARG   B 1 68   ? 89.61900   56.20500  -32.93500 1.000 81.20367  ?  68   ARG   B CB  1 
ATOM   14655 C  CG  . ARG   B 1 68   ? 90.25900   55.03200  -33.67400 1.000 80.43278  ?  68   ARG   B CG  1 
ATOM   14656 C  CD  . ARG   B 1 68   ? 91.78500   55.09100  -33.61800 1.000 82.78371  ?  68   ARG   B CD  1 
ATOM   14657 N  NE  . ARG   B 1 68   ? 92.33600   56.20000  -34.39200 1.000 82.93953  ?  68   ARG   B NE  1 
ATOM   14658 C  CZ  . ARG   B 1 68   ? 93.62100   56.52900  -34.42100 1.000 79.65831  ?  68   ARG   B CZ  1 
ATOM   14659 N  NH1 . ARG   B 1 68   ? 94.52300   55.86000  -33.72100 1.000 79.30487  ?  68   ARG   B NH1 1 
ATOM   14660 N  NH2 . ARG   B 1 68   ? 94.01200   57.55600  -35.17100 1.000 68.70408  ?  68   ARG   B NH2 1 
ATOM   14661 N  N   . ILE   B 1 69   ? 86.61100   57.98800  -32.42000 1.000 65.31383  ?  69   ILE   B N   1 
ATOM   14662 C  CA  . ILE   B 1 69   ? 85.98600   59.09000  -31.69200 1.000 62.34732  ?  69   ILE   B CA  1 
ATOM   14663 C  C   . ILE   B 1 69   ? 84.63200   58.61400  -31.18400 1.000 64.34795  ?  69   ILE   B C   1 
ATOM   14664 O  O   . ILE   B 1 69   ? 83.74000   58.28300  -31.97600 1.000 60.91694  ?  69   ILE   B O   1 
ATOM   14665 C  CB  . ILE   B 1 69   ? 85.83500   60.34500  -32.56600 1.000 48.23026  ?  69   ILE   B CB  1 
ATOM   14666 C  CG1 . ILE   B 1 69   ? 87.14200   60.67900  -33.27700 1.000 63.03902  ?  69   ILE   B CG1 1 
ATOM   14667 C  CG2 . ILE   B 1 69   ? 85.40900   61.53100  -31.71900 1.000 45.23003  ?  69   ILE   B CG2 1 
ATOM   14668 C  CD1 . ILE   B 1 69   ? 87.08100   61.96600  -34.06900 1.000 58.07465  ?  69   ILE   B CD1 1 
ATOM   14669 N  N   . ILE   B 1 70   ? 84.47400   58.58300  -29.86400 1.000 69.44915  ?  70   ILE   B N   1 
ATOM   14670 C  CA  . ILE   B 1 70   ? 83.29100   58.03800  -29.21000 1.000 53.03946  ?  70   ILE   B CA  1 
ATOM   14671 C  C   . ILE   B 1 70   ? 82.59600   59.17100  -28.46500 1.000 56.10375  ?  70   ILE   B C   1 
ATOM   14672 O  O   . ILE   B 1 70   ? 83.25000   59.95100  -27.76200 1.000 46.46301  ?  70   ILE   B O   1 
ATOM   14673 C  CB  . ILE   B 1 70   ? 83.65400   56.89600  -28.23800 1.000 51.41988  ?  70   ILE   B CB  1 
ATOM   14674 C  CG1 . ILE   B 1 70   ? 84.41600   55.73300  -28.90500 1.000 73.77910  ?  70   ILE   B CG1 1 
ATOM   14675 C  CG2 . ILE   B 1 70   ? 82.39900   56.33500  -27.60300 1.000 63.61683  ?  70   ILE   B CG2 1 
ATOM   14676 C  CD1 . ILE   B 1 70   ? 84.08000   55.42800  -30.36200 1.000 67.31291  ?  70   ILE   B CD1 1 
ATOM   14677 N  N   . ASN   B 1 71   ? 81.27500   59.25800  -28.60700 1.000 53.27198  ?  71   ASN   B N   1 
ATOM   14678 C  CA  . ASN   B 1 71   ? 80.49100   60.25800  -27.90200 1.000 41.57210  ?  71   ASN   B CA  1 
ATOM   14679 C  C   . ASN   B 1 71   ? 79.59800   59.60000  -26.86000 1.000 44.80976  ?  71   ASN   B C   1 
ATOM   14680 O  O   . ASN   B 1 71   ? 79.13100   58.47100  -27.03800 1.000 50.19050  ?  71   ASN   B O   1 
ATOM   14681 C  CB  . ASN   B 1 71   ? 79.63300   61.08200  -28.86100 1.000 44.04942  ?  71   ASN   B CB  1 
ATOM   14682 C  CG  . ASN   B 1 71   ? 79.08800   62.33400  -28.20900 1.000 45.99053  ?  71   ASN   B CG  1 
ATOM   14683 O  OD1 . ASN   B 1 71   ? 79.81000   63.03700  -27.50600 1.000 40.66202  ?  71   ASN   B OD1 1 
ATOM   14684 N  ND2 . ASN   B 1 71   ? 77.80600   62.61100  -28.42400 1.000 59.95420  ?  71   ASN   B ND2 1 
ATOM   14685 N  N   . LEU   B 1 72   ? 79.37000   60.32400  -25.77000 1.000 36.09736  ?  72   LEU   B N   1 
ATOM   14686 C  CA  . LEU   B 1 72   ? 78.52700   59.86800  -24.67200 1.000 50.87109  ?  72   LEU   B CA  1 
ATOM   14687 C  C   . LEU   B 1 72   ? 77.25300   60.70800  -24.65000 1.000 50.39788  ?  72   LEU   B C   1 
ATOM   14688 O  O   . LEU   B 1 72   ? 77.05000   61.54900  -23.77300 1.000 54.97947  ?  72   LEU   B O   1 
ATOM   14689 C  CB  . LEU   B 1 72   ? 79.29200   59.96800  -23.33800 1.000 50.90006  ?  72   LEU   B CB  1 
ATOM   14690 C  CG  . LEU   B 1 72   ? 80.11700   58.77100  -22.86000 1.000 48.97767  ?  72   LEU   B CG  1 
ATOM   14691 C  CD1 . LEU   B 1 72   ? 81.39100   58.63000  -23.66900 1.000 48.17601  ?  72   LEU   B CD1 1 
ATOM   14692 C  CD2 . LEU   B 1 72   ? 80.43800   58.89300  -21.38000 1.000 51.83626  ?  72   LEU   B CD2 1 
ATOM   14693 N  N   . HIS   B 1 73   ? 76.39300   60.48100  -25.63300 1.000 46.40784  ?  73   HIS   B N   1 
ATOM   14694 C  CA  . HIS   B 1 73   ? 75.16600   61.26700  -25.74300 1.000 56.71758  ?  73   HIS   B CA  1 
ATOM   14695 C  C   . HIS   B 1 73   ? 74.15400   60.84600  -24.68300 1.000 59.51528  ?  73   HIS   B C   1 
ATOM   14696 O  O   . HIS   B 1 73   ? 73.68400   59.70000  -24.70900 1.000 50.78392  ?  73   HIS   B O   1 
ATOM   14697 C  CB  . HIS   B 1 73   ? 74.55800   61.11800  -27.12700 1.000 57.47408  ?  73   HIS   B CB  1 
ATOM   14698 C  CG  . HIS   B 1 73   ? 73.60900   62.21700  -27.48200 1.000 63.81358  ?  73   HIS   B CG  1 
ATOM   14699 N  ND1 . HIS   B 1 73   ? 73.95100   63.55000  -27.39600 1.000 54.50010  ?  73   HIS   B ND1 1 
ATOM   14700 C  CD2 . HIS   B 1 73   ? 72.32400   62.18500  -27.90700 1.000 72.81698  ?  73   HIS   B CD2 1 
ATOM   14701 C  CE1 . HIS   B 1 73   ? 72.92100   64.29100  -27.76300 1.000 54.47366  ?  73   HIS   B CE1 1 
ATOM   14702 N  NE2 . HIS   B 1 73   ? 71.92100   63.48800  -28.07800 1.000 60.67971  ?  73   HIS   B NE2 1 
ATOM   14703 N  N   . PRO   B 1 74   ? 73.76400   61.73300  -23.76600 1.000 47.39203  ?  74   PRO   B N   1 
ATOM   14704 C  CA  . PRO   B 1 74   ? 72.90400   61.33300  -22.64800 1.000 59.09041  ?  74   PRO   B CA  1 
ATOM   14705 C  C   . PRO   B 1 74   ? 71.43400   61.18000  -23.00100 1.000 64.97731  ?  74   PRO   B C   1 
ATOM   14706 O  O   . PRO   B 1 74   ? 70.60800   61.05000  -22.09400 1.000 85.41014  ?  74   PRO   B O   1 
ATOM   14707 C  CB  . PRO   B 1 74   ? 73.10700   62.48300  -21.65000 1.000 63.84491  ?  74   PRO   B CB  1 
ATOM   14708 C  CG  . PRO   B 1 74   ? 73.33500   63.67000  -22.51700 1.000 53.35757  ?  74   PRO   B CG  1 
ATOM   14709 C  CD  . PRO   B 1 74   ? 74.06600   63.17500  -23.74500 1.000 35.31701  ?  74   PRO   B CD  1 
ATOM   14710 N  N   . SER   B 1 75   ? 71.09000   61.19200  -24.28000 1.000 65.32985  ?  75   SER   B N   1 
ATOM   14711 C  CA  . SER   B 1 75   ? 69.73300   60.95300  -24.73500 1.000 58.52916  ?  75   SER   B CA  1 
ATOM   14712 C  C   . SER   B 1 75   ? 69.72100   59.76500  -25.68600 1.000 52.63910  ?  75   SER   B C   1 
ATOM   14713 O  O   . SER   B 1 75   ? 70.76600   59.27900  -26.12500 1.000 63.00066  ?  75   SER   B O   1 
ATOM   14714 C  CB  . SER   B 1 75   ? 69.16000   62.18900  -25.42900 1.000 73.90272  ?  75   SER   B CB  1 
ATOM   14715 O  OG  . SER   B 1 75   ? 69.40700   62.12000  -26.82200 1.000 60.78041  ?  75   SER   B OG  1 
ATOM   14716 N  N   . LEU   B 1 76   ? 68.52000   59.29000  -25.99800 1.000 68.84623  ?  76   LEU   B N   1 
ATOM   14717 C  CA  . LEU   B 1 76   ? 68.38000   58.27400  -27.03000 1.000 60.13272  ?  76   LEU   B CA  1 
ATOM   14718 C  C   . LEU   B 1 76   ? 68.59100   58.89700  -28.40200 1.000 69.46339  ?  76   LEU   B C   1 
ATOM   14719 O  O   . LEU   B 1 76   ? 68.37500   60.09500  -28.60700 1.000 81.43297  ?  76   LEU   B O   1 
ATOM   14720 C  CB  . LEU   B 1 76   ? 67.00300   57.61500  -26.96500 1.000 48.03293  ?  76   LEU   B CB  1 
ATOM   14721 C  CG  . LEU   B 1 76   ? 66.92600   56.16400  -27.44400 1.000 49.93665  ?  76   LEU   B CG  1 
ATOM   14722 C  CD1 . LEU   B 1 76   ? 67.85900   55.28700  -26.63400 1.000 62.42376  ?  76   LEU   B CD1 1 
ATOM   14723 C  CD2 . LEU   B 1 76   ? 65.50400   55.65000  -27.34500 1.000 50.93877  ?  76   LEU   B CD2 1 
ATOM   14724 N  N   . LEU   B 1 77   ? 69.02200   58.07200  -29.34900 1.000 60.75443  ?  77   LEU   B N   1 
ATOM   14725 C  CA  . LEU   B 1 77   ? 69.30600   58.58700  -30.67200 1.000 58.06676  ?  77   LEU   B CA  1 
ATOM   14726 C  C   . LEU   B 1 77   ? 68.41500   57.90900  -31.70200 1.000 62.18077  ?  77   LEU   B C   1 
ATOM   14727 O  O   . LEU   B 1 77   ? 68.12100   56.71600  -31.57600 1.000 56.58339  ?  77   LEU   B O   1 
ATOM   14728 C  CB  . LEU   B 1 77   ? 70.78400   58.37900  -31.04100 1.000 55.16767  ?  77   LEU   B CB  1 
ATOM   14729 C  CG  . LEU   B 1 77   ? 71.72700   59.52300  -30.65200 1.000 58.54934  ?  77   LEU   B CG  1 
ATOM   14730 C  CD1 . LEU   B 1 77   ? 73.02000   59.48800  -31.45600 1.000 59.12242  ?  77   LEU   B CD1 1 
ATOM   14731 C  CD2 . LEU   B 1 77   ? 71.03000   60.86100  -30.82500 1.000 49.99668  ?  77   LEU   B CD2 1 
ATOM   14732 N  N   . PRO   B 1 78   ? 67.97600   58.63500  -32.73700 1.000 63.11947  ?  78   PRO   B N   1 
ATOM   14733 C  CA  . PRO   B 1 78   ? 68.32500   60.01700  -33.09300 1.000 61.03085  ?  78   PRO   B CA  1 
ATOM   14734 C  C   . PRO   B 1 78   ? 67.44600   61.10000  -32.47300 1.000 59.20271  ?  78   PRO   B C   1 
ATOM   14735 O  O   . PRO   B 1 78   ? 66.89700   61.91100  -33.20400 1.000 54.99392  ?  78   PRO   B O   1 
ATOM   14736 C  CB  . PRO   B 1 78   ? 68.17100   60.01300  -34.61800 1.000 57.34856  ?  78   PRO   B CB  1 
ATOM   14737 C  CG  . PRO   B 1 78   ? 67.15400   58.91600  -34.92200 1.000 63.34317  ?  78   PRO   B CG  1 
ATOM   14738 C  CD  . PRO   B 1 78   ? 66.99300   58.07200  -33.67600 1.000 56.53033  ?  78   PRO   B CD  1 
ATOM   14739 N  N   . TRP   B 1 79   ? 67.31300   61.18300  -31.15300 1.000 70.56408  ?  79   TRP   B N   1 
ATOM   14740 C  CA  . TRP   B 1 79   ? 66.41700   62.13700  -30.51900 1.000 52.91026  ?  79   TRP   B CA  1 
ATOM   14741 C  C   . TRP   B 1 79   ? 67.19900   63.25500  -29.84300 1.000 59.34298  ?  79   TRP   B C   1 
ATOM   14742 O  O   . TRP   B 1 79   ? 68.24200   63.01500  -29.22400 1.000 71.24260  ?  79   TRP   B O   1 
ATOM   14743 C  CB  . TRP   B 1 79   ? 65.52200   61.43900  -29.50100 1.000 68.73933  ?  79   TRP   B CB  1 
ATOM   14744 C  CG  . TRP   B 1 79   ? 64.73700   60.32300  -30.09700 1.000 69.71201  ?  79   TRP   B CG  1 
ATOM   14745 C  CD1 . TRP   B 1 79   ? 64.96400   58.98800  -29.94600 1.000 80.08978  ?  79   TRP   B CD1 1 
ATOM   14746 C  CD2 . TRP   B 1 79   ? 63.59600   60.44300  -30.95400 1.000 79.67390  ?  79   TRP   B CD2 1 
ATOM   14747 N  NE1 . TRP   B 1 79   ? 64.02800   58.26500  -30.64900 1.000 74.56293  ?  79   TRP   B NE1 1 
ATOM   14748 C  CE2 . TRP   B 1 79   ? 63.17800   59.13600  -31.27800 1.000 67.83610  ?  79   TRP   B CE2 1 
ATOM   14749 C  CE3 . TRP   B 1 79   ? 62.88500   61.52800  -31.47600 1.000 75.67599  ?  79   TRP   B CE3 1 
ATOM   14750 C  CZ2 . TRP   B 1 79   ? 62.08200   58.88600  -32.09900 1.000 54.23192  ?  79   TRP   B CZ2 1 
ATOM   14751 C  CZ3 . TRP   B 1 79   ? 61.79700   61.27800  -32.29200 1.000 63.79555  ?  79   TRP   B CZ3 1 
ATOM   14752 C  CH2 . TRP   B 1 79   ? 61.40600   59.96800  -32.59500 1.000 55.88864  ?  79   TRP   B CH2 1 
ATOM   14753 N  N   . ASN   B 1 80   ? 66.67800   64.47300  -29.97300 1.000 55.77564  ?  80   ASN   B N   1 
ATOM   14754 C  CA  . ASN   B 1 80   ? 67.24100   65.67600  -29.36200 1.000 69.23196  ?  80   ASN   B CA  1 
ATOM   14755 C  C   . ASN   B 1 80   ? 68.74900   65.75900  -29.58700 1.000 69.25159  ?  80   ASN   B C   1 
ATOM   14756 O  O   . ASN   B 1 80   ? 69.53400   66.05700  -28.68300 1.000 89.04622  ?  80   ASN   B O   1 
ATOM   14757 C  CB  . ASN   B 1 80   ? 66.87900   65.73400  -27.88500 1.000 77.86771  ?  80   ASN   B CB  1 
ATOM   14758 C  CG  . ASN   B 1 80   ? 65.60300   64.97300  -27.58900 1.000 59.18111  ?  80   ASN   B CG  1 
ATOM   14759 O  OD1 . ASN   B 1 80   ? 65.64500   63.83900  -27.10200 1.000 48.96361  ?  80   ASN   B OD1 1 
ATOM   14760 N  ND2 . ASN   B 1 80   ? 64.46300   65.55000  -27.97700 1.000 57.44255  ?  80   ASN   B ND2 1 
ATOM   14761 N  N   . LYS   B 1 81   ? 69.15000   65.48300  -30.82500 1.000 55.28322  ?  81   LYS   B N   1 
ATOM   14762 C  CA  . LYS   B 1 81   ? 70.54500   65.63600  -31.20300 1.000 52.98593  ?  81   LYS   B CA  1 
ATOM   14763 C  C   . LYS   B 1 81   ? 70.94100   67.10300  -31.11700 1.000 61.28854  ?  81   LYS   B C   1 
ATOM   14764 O  O   . LYS   B 1 81   ? 70.23500   67.98000  -31.62000 1.000 61.64572  ?  81   LYS   B O   1 
ATOM   14765 C  CB  . LYS   B 1 81   ? 70.77800   65.10500  -32.61900 1.000 56.43114  ?  81   LYS   B CB  1 
ATOM   14766 C  CG  . LYS   B 1 81   ? 70.02900   63.82300  -32.94600 1.000 60.14016  ?  81   LYS   B CG  1 
ATOM   14767 C  CD  . LYS   B 1 81   ? 70.15600   63.47200  -34.42200 1.000 50.18573  ?  81   LYS   B CD  1 
ATOM   14768 C  CE  . LYS   B 1 81   ? 68.81400   63.57400  -35.12900 1.000 66.42573  ?  81   LYS   B CE  1 
ATOM   14769 N  NZ  . LYS   B 1 81   ? 68.91400   63.27900  -36.58500 1.000 66.61909  ?  81   LYS   B NZ  1 
ATOM   14770 N  N   . GLY   B 1 82   ? 72.06300   67.36900  -30.45800 1.000 58.99517  ?  82   GLY   B N   1 
ATOM   14771 C  CA  . GLY   B 1 82   ? 72.55000   68.72700  -30.35600 1.000 65.31303  ?  82   GLY   B CA  1 
ATOM   14772 C  C   . GLY   B 1 82   ? 72.62500   69.23000  -28.93300 1.000 70.85852  ?  82   GLY   B C   1 
ATOM   14773 O  O   . GLY   B 1 82   ? 73.46400   68.77800  -28.14800 1.000 97.91187  ?  82   GLY   B O   1 
ATOM   14774 N  N   . ARG   B 1 83   ? 71.74900   70.16800  -28.59700 1.000 38.73863  ?  83   ARG   B N   1 
ATOM   14775 C  CA  . ARG   B 1 83   ? 71.73900   70.79700  -27.29000 1.000 41.72527  ?  83   ARG   B CA  1 
ATOM   14776 C  C   . ARG   B 1 83   ? 70.48800   70.39100  -26.52200 1.000 46.10038  ?  83   ARG   B C   1 
ATOM   14777 O  O   . ARG   B 1 83   ? 69.50400   69.91700  -27.08600 1.000 48.91494  ?  83   ARG   B O   1 
ATOM   14778 C  CB  . ARG   B 1 83   ? 71.80600   72.32200  -27.40700 1.000 46.35761  ?  83   ARG   B CB  1 
ATOM   14779 C  CG  . ARG   B 1 83   ? 73.14500   72.85600  -27.90800 1.000 44.78971  ?  83   ARG   B CG  1 
ATOM   14780 C  CD  . ARG   B 1 83   ? 74.30100   72.37500  -27.03800 1.000 50.48593  ?  83   ARG   B CD  1 
ATOM   14781 N  NE  . ARG   B 1 83   ? 75.17400   73.46400  -26.61200 1.000 49.64839  ?  83   ARG   B NE  1 
ATOM   14782 C  CZ  . ARG   B 1 83   ? 76.21100   73.90800  -27.30900 1.000 65.30421  ?  83   ARG   B CZ  1 
ATOM   14783 N  NH1 . ARG   B 1 83   ? 76.52200   73.39400  -28.48800 1.000 68.86339  ?  83   ARG   B NH1 1 
ATOM   14784 N  NH2 . ARG   B 1 83   ? 76.95400   74.89500  -26.81200 1.000 60.17762  ?  83   ARG   B NH2 1 
ATOM   14785 N  N   . ASP   B 1 84   ? 70.55900   70.58600  -25.21300 1.000 44.04305  ?  84   ASP   B N   1 
ATOM   14786 C  CA  . ASP   B 1 84   ? 69.50800   70.27800  -24.24500 1.000 35.53129  ?  84   ASP   B CA  1 
ATOM   14787 C  C   . ASP   B 1 84   ? 68.82800   68.93000  -24.53800 1.000 48.99892  ?  84   ASP   B C   1 
ATOM   14788 O  O   . ASP   B 1 84   ? 67.62600   68.89200  -24.81300 1.000 43.09022  ?  84   ASP   B O   1 
ATOM   14789 C  CB  . ASP   B 1 84   ? 68.48700   71.41400  -24.18900 1.000 38.03436  ?  84   ASP   B CB  1 
ATOM   14790 C  CG  . ASP   B 1 84   ? 69.10900   72.68200  -23.66900 1.000 50.35639  ?  84   ASP   B CG  1 
ATOM   14791 O  OD1 . ASP   B 1 84   ? 69.17500   72.83400  -22.43500 1.000 63.04041  ?  84   ASP   B OD1 1 
ATOM   14792 O  OD2 . ASP   B 1 84   ? 69.55000   73.53400  -24.48200 1.000 45.86114  -1 84   ASP   B OD2 1 
ATOM   14793 N  N   . PRO   B 1 85   ? 69.56400   67.83600  -24.52500 1.000 46.89382  ?  85   PRO   B N   1 
ATOM   14794 C  CA  . PRO   B 1 85   ? 68.97400   66.54500  -24.93400 1.000 47.66742  ?  85   PRO   B CA  1 
ATOM   14795 C  C   . PRO   B 1 85   ? 67.85500   66.06700  -24.03200 1.000 46.31135  ?  85   PRO   B C   1 
ATOM   14796 O  O   . PRO   B 1 85   ? 66.78600   65.72700  -24.52600 1.000 33.30891  ?  85   PRO   B O   1 
ATOM   14797 C  CB  . PRO   B 1 85   ? 70.17700   65.56200  -24.92100 1.000 35.11670  ?  85   PRO   B CB  1 
ATOM   14798 C  CG  . PRO   B 1 85   ? 71.36300   66.33300  -24.44700 1.000 61.44993  ?  85   PRO   B CG  1 
ATOM   14799 C  CD  . PRO   B 1 85   ? 70.91700   67.67700  -23.95000 1.000 60.41765  ?  85   PRO   B CD  1 
ATOM   14800 N  N   . VAL   B 1 86   ? 68.08700   66.02400  -22.71300 1.000 49.26255  ?  86   VAL   B N   1 
ATOM   14801 C  CA  . VAL   B 1 86   ? 67.08600   65.44900  -21.82100 1.000 47.60064  ?  86   VAL   B CA  1 
ATOM   14802 C  C   . VAL   B 1 86   ? 65.83500   66.31400  -21.79100 1.000 47.03338  ?  86   VAL   B C   1 
ATOM   14803 O  O   . VAL   B 1 86   ? 64.71100   65.80000  -21.75800 1.000 30.70672  ?  86   VAL   B O   1 
ATOM   14804 C  CB  . VAL   B 1 86   ? 67.66600   65.25700  -20.40900 1.000 38.42607  ?  86   VAL   B CB  1 
ATOM   14805 C  CG1 . VAL   B 1 86   ? 66.59500   64.73400  -19.46000 1.000 33.02334  ?  86   VAL   B CG1 1 
ATOM   14806 C  CG2 . VAL   B 1 86   ? 68.85800   64.32700  -20.45000 1.000 47.16737  ?  86   VAL   B CG2 1 
ATOM   14807 N  N   . PHE   B 1 87   ? 66.00700   67.63800  -21.79700 1.000 39.79778  ?  87   PHE   B N   1 
ATOM   14808 C  CA  . PHE   B 1 87   ? 64.85200   68.52700  -21.73500 1.000 38.39995  ?  87   PHE   B CA  1 
ATOM   14809 C  C   . PHE   B 1 87   ? 63.91200   68.28500  -22.90600 1.000 42.34286  ?  87   PHE   B C   1 
ATOM   14810 O  O   . PHE   B 1 87   ? 62.70500   68.08900  -22.72400 1.000 38.15476  ?  87   PHE   B O   1 
ATOM   14811 C  CB  . PHE   B 1 87   ? 65.28900   69.98800  -21.71400 1.000 39.45494  ?  87   PHE   B CB  1 
ATOM   14812 C  CG  . PHE   B 1 87   ? 64.15000   70.94700  -21.89600 1.000 52.28868  ?  87   PHE   B CG  1 
ATOM   14813 C  CD1 . PHE   B 1 87   ? 63.25300   71.17000  -20.86700 1.000 67.50714  ?  87   PHE   B CD1 1 
ATOM   14814 C  CD2 . PHE   B 1 87   ? 63.95300   71.59300  -23.10600 1.000 53.12741  ?  87   PHE   B CD2 1 
ATOM   14815 C  CE1 . PHE   B 1 87   ? 62.19400   72.03900  -21.03000 1.000 58.55834  ?  87   PHE   B CE1 1 
ATOM   14816 C  CE2 . PHE   B 1 87   ? 62.89400   72.46200  -23.27700 1.000 40.69919  ?  87   PHE   B CE2 1 
ATOM   14817 C  CZ  . PHE   B 1 87   ? 62.01400   72.68400  -22.23700 1.000 55.79046  ?  87   PHE   B CZ  1 
ATOM   14818 N  N   . TRP   B 1 88   ? 64.45000   68.30300  -24.12300 1.000 52.32005  ?  88   TRP   B N   1 
ATOM   14819 C  CA  . TRP   B 1 88   ? 63.61900   68.06900  -25.29200 1.000 35.87058  ?  88   TRP   B CA  1 
ATOM   14820 C  C   . TRP   B 1 88   ? 63.05400   66.66200  -25.30600 1.000 40.65875  ?  88   TRP   B C   1 
ATOM   14821 O  O   . TRP   B 1 88   ? 61.95200   66.44600  -25.81900 1.000 50.76699  ?  88   TRP   B O   1 
ATOM   14822 C  CB  . TRP   B 1 88   ? 64.42300   68.32500  -26.55400 1.000 35.20187  ?  88   TRP   B CB  1 
ATOM   14823 C  CG  . TRP   B 1 88   ? 64.74500   69.76500  -26.76900 1.000 34.70027  ?  88   TRP   B CG  1 
ATOM   14824 C  CD1 . TRP   B 1 88   ? 65.98400   70.33200  -26.81900 1.000 50.72927  ?  88   TRP   B CD1 1 
ATOM   14825 C  CD2 . TRP   B 1 88   ? 63.81200   70.82700  -26.97100 1.000 34.70972  ?  88   TRP   B CD2 1 
ATOM   14826 N  NE1 . TRP   B 1 88   ? 65.88100   71.68300  -27.04900 1.000 50.20252  ?  88   TRP   B NE1 1 
ATOM   14827 C  CE2 . TRP   B 1 88   ? 64.55600   72.01100  -27.14600 1.000 33.98503  ?  88   TRP   B CE2 1 
ATOM   14828 C  CE3 . TRP   B 1 88   ? 62.41800   70.89100  -27.02800 1.000 36.38527  ?  88   TRP   B CE3 1 
ATOM   14829 C  CZ2 . TRP   B 1 88   ? 63.95300   73.23900  -27.37300 1.000 42.67309  ?  88   TRP   B CZ2 1 
ATOM   14830 C  CZ3 . TRP   B 1 88   ? 61.82600   72.10400  -27.25100 1.000 35.55132  ?  88   TRP   B CZ3 1 
ATOM   14831 C  CH2 . TRP   B 1 88   ? 62.58800   73.26400  -27.42200 1.000 50.11860  ?  88   TRP   B CH2 1 
ATOM   14832 N  N   . SER   B 1 89   ? 63.79200   65.69200  -24.75900 1.000 44.69046  ?  89   SER   B N   1 
ATOM   14833 C  CA  . SER   B 1 89   ? 63.25300   64.34300  -24.64200 1.000 43.37092  ?  89   SER   B CA  1 
ATOM   14834 C  C   . SER   B 1 89   ? 62.00700   64.32100  -23.77100 1.000 50.84116  ?  89   SER   B C   1 
ATOM   14835 O  O   . SER   B 1 89   ? 61.11100   63.50000  -23.99100 1.000 47.12178  ?  89   SER   B O   1 
ATOM   14836 C  CB  . SER   B 1 89   ? 64.31500   63.39000  -24.08300 1.000 53.24571  ?  89   SER   B CB  1 
ATOM   14837 O  OG  . SER   B 1 89   ? 64.22900   63.27200  -22.67300 1.000 55.37838  ?  89   SER   B OG  1 
ATOM   14838 N  N   . VAL   B 1 90   ? 61.92200   65.21500  -22.79100 1.000 47.23636  ?  90   VAL   B N   1 
ATOM   14839 C  CA  . VAL   B 1 90   ? 60.75200   65.28100  -21.92400 1.000 43.06047  ?  90   VAL   B CA  1 
ATOM   14840 C  C   . VAL   B 1 90   ? 59.66500   66.15800  -22.52900 1.000 43.78345  ?  90   VAL   B C   1 
ATOM   14841 O  O   . VAL   B 1 90   ? 58.49800   65.76400  -22.59200 1.000 38.74202  ?  90   VAL   B O   1 
ATOM   14842 C  CB  . VAL   B 1 90   ? 61.16200   65.77500  -20.52000 1.000 36.78776  ?  90   VAL   B CB  1 
ATOM   14843 C  CG1 . VAL   B 1 90   ? 59.95600   66.29900  -19.76700 1.000 38.68328  ?  90   VAL   B CG1 1 
ATOM   14844 C  CG2 . VAL   B 1 90   ? 61.83600   64.66000  -19.73900 1.000 48.99745  ?  90   VAL   B CG2 1 
ATOM   14845 N  N   . TRP   B 1 91   ? 60.03400   67.35200  -22.99900 1.000 51.64320  ?  91   TRP   B N   1 
ATOM   14846 C  CA  . TRP   B 1 91   ? 59.04200   68.30000  -23.50100 1.000 42.84037  ?  91   TRP   B CA  1 
ATOM   14847 C  C   . TRP   B 1 91   ? 58.31300   67.74500  -24.71900 1.000 53.89339  ?  91   TRP   B C   1 
ATOM   14848 O  O   . TRP   B 1 91   ? 57.08700   67.58700  -24.70900 1.000 68.29939  ?  91   TRP   B O   1 
ATOM   14849 C  CB  . TRP   B 1 91   ? 59.70900   69.63300  -23.83700 1.000 40.69271  ?  91   TRP   B CB  1 
ATOM   14850 C  CG  . TRP   B 1 91   ? 58.77000   70.60300  -24.47500 1.000 48.45297  ?  91   TRP   B CG  1 
ATOM   14851 C  CD1 . TRP   B 1 91   ? 58.56300   70.78500  -25.81000 1.000 45.98229  ?  91   TRP   B CD1 1 
ATOM   14852 C  CD2 . TRP   B 1 91   ? 57.90000   71.52200  -23.80400 1.000 54.06729  ?  91   TRP   B CD2 1 
ATOM   14853 N  NE1 . TRP   B 1 91   ? 57.62000   71.76300  -26.01400 1.000 37.87756  ?  91   TRP   B NE1 1 
ATOM   14854 C  CE2 . TRP   B 1 91   ? 57.19800   72.23200  -24.79800 1.000 42.64274  ?  91   TRP   B CE2 1 
ATOM   14855 C  CE3 . TRP   B 1 91   ? 57.64800   71.81500  -22.46000 1.000 48.97604  ?  91   TRP   B CE3 1 
ATOM   14856 C  CZ2 . TRP   B 1 91   ? 56.26300   73.21700  -24.49100 1.000 41.50329  ?  91   TRP   B CZ2 1 
ATOM   14857 C  CZ3 . TRP   B 1 91   ? 56.71900   72.79400  -22.15800 1.000 53.02269  ?  91   TRP   B CZ3 1 
ATOM   14858 C  CH2 . TRP   B 1 91   ? 56.03700   73.48200  -23.16900 1.000 48.17645  ?  91   TRP   B CH2 1 
ATOM   14859 N  N   . ASP   B 1 92   ? 59.05300   67.45300  -25.78600 1.000 64.79475  ?  92   ASP   B N   1 
ATOM   14860 C  CA  . ASP   B 1 92   ? 58.46500   66.86600  -26.98300 1.000 52.09595  ?  92   ASP   B CA  1 
ATOM   14861 C  C   . ASP   B 1 92   ? 58.10500   65.39500  -26.80900 1.000 48.24306  ?  92   ASP   B C   1 
ATOM   14862 O  O   . ASP   B 1 92   ? 57.61100   64.78300  -27.76100 1.000 49.60739  ?  92   ASP   B O   1 
ATOM   14863 C  CB  . ASP   B 1 92   ? 59.41900   67.02000  -28.17200 1.000 34.21650  ?  92   ASP   B CB  1 
ATOM   14864 C  CG  . ASP   B 1 92   ? 59.54200   68.45700  -28.64000 1.000 63.39072  ?  92   ASP   B CG  1 
ATOM   14865 O  OD1 . ASP   B 1 92   ? 58.57400   69.22700  -28.46100 1.000 72.89367  ?  92   ASP   B OD1 1 
ATOM   14866 O  OD2 . ASP   B 1 92   ? 60.60500   68.81500  -29.19300 1.000 61.49293  -1 92   ASP   B OD2 1 
ATOM   14867 N  N   . GLU   B 1 93   ? 58.33600   64.81800  -25.62700 1.000 67.31560  ?  93   GLU   B N   1 
ATOM   14868 C  CA  . GLU   B 1 93   ? 58.03500   63.41100  -25.35100 1.000 71.33775  ?  93   GLU   B CA  1 
ATOM   14869 C  C   . GLU   B 1 93   ? 58.72200   62.47500  -26.34100 1.000 67.88447  ?  93   GLU   B C   1 
ATOM   14870 O  O   . GLU   B 1 93   ? 58.17000   61.43600  -26.71400 1.000 43.24619  ?  93   GLU   B O   1 
ATOM   14871 C  CB  . GLU   B 1 93   ? 56.52500   63.15700  -25.33100 1.000 49.15846  ?  93   GLU   B CB  1 
ATOM   14872 C  CG  . GLU   B 1 93   ? 55.72900   64.27400  -24.67800 1.000 68.72035  ?  93   GLU   B CG  1 
ATOM   14873 C  CD  . GLU   B 1 93   ? 54.23900   64.00200  -24.67100 1.000 73.45927  ?  93   GLU   B CD  1 
ATOM   14874 O  OE1 . GLU   B 1 93   ? 53.84200   62.86100  -24.35600 1.000 79.46616  ?  93   GLU   B OE1 1 
ATOM   14875 O  OE2 . GLU   B 1 93   ? 53.46500   64.93100  -24.98200 1.000 66.95180  -1 93   GLU   B OE2 1 
ATOM   14876 N  N   . THR   B 1 94   ? 59.92900   62.84200  -26.77200 1.000 78.21513  ?  94   THR   B N   1 
ATOM   14877 C  CA  . THR   B 1 94   ? 60.71900   61.95600  -27.61200 1.000 39.19247  ?  94   THR   B CA  1 
ATOM   14878 C  C   . THR   B 1 94   ? 61.26200   60.80700  -26.76500 1.000 53.35142  ?  94   THR   B C   1 
ATOM   14879 O  O   . THR   B 1 94   ? 61.57800   61.00600  -25.58800 1.000 77.59864  ?  94   THR   B O   1 
ATOM   14880 C  CB  . THR   B 1 94   ? 61.87600   62.71000  -28.27800 1.000 64.22936  ?  94   THR   B CB  1 
ATOM   14881 O  OG1 . THR   B 1 94   ? 63.00700   62.75700  -27.39500 1.000 69.65488  ?  94   THR   B OG1 1 
ATOM   14882 C  CG2 . THR   B 1 94   ? 61.46000   64.12800  -28.64200 1.000 66.59163  ?  94   THR   B CG2 1 
ATOM   14883 N  N   . PRO   B 1 95   ? 61.35500   59.60100  -27.32400 1.000 67.91032  ?  95   PRO   B N   1 
ATOM   14884 C  CA  . PRO   B 1 95   ? 61.84000   58.44700  -26.55100 1.000 58.25481  ?  95   PRO   B CA  1 
ATOM   14885 C  C   . PRO   B 1 95   ? 63.14100   58.75600  -25.82200 1.000 57.94192  ?  95   PRO   B C   1 
ATOM   14886 O  O   . PRO   B 1 95   ? 64.11000   59.23400  -26.41500 1.000 67.05449  ?  95   PRO   B O   1 
ATOM   14887 C  CB  . PRO   B 1 95   ? 62.03600   57.37100  -27.62400 1.000 54.35783  ?  95   PRO   B CB  1 
ATOM   14888 C  CG  . PRO   B 1 95   ? 61.03500   57.72600  -28.67900 1.000 56.12621  ?  95   PRO   B CG  1 
ATOM   14889 C  CD  . PRO   B 1 95   ? 60.92600   59.22400  -28.68100 1.000 60.67794  ?  95   PRO   B CD  1 
ATOM   14890 N  N   . LYS   B 1 96   ? 63.14600   58.49500  -24.51700 1.000 52.41370  ?  96   LYS   B N   1 
ATOM   14891 C  CA  . LYS   B 1 96   ? 64.26700   58.84000  -23.65300 1.000 83.68877  ?  96   LYS   B CA  1 
ATOM   14892 C  C   . LYS   B 1 96   ? 65.19300   57.64400  -23.46300 1.000 73.66499  ?  96   LYS   B C   1 
ATOM   14893 O  O   . LYS   B 1 96   ? 64.73900   56.51200  -23.27100 1.000 49.52745  ?  96   LYS   B O   1 
ATOM   14894 C  CB  . LYS   B 1 96   ? 63.77600   59.33900  -22.29100 1.000 60.84721  ?  96   LYS   B CB  1 
ATOM   14895 C  CG  . LYS   B 1 96   ? 62.26100   59.38100  -22.14400 1.000 36.37026  ?  96   LYS   B CG  1 
ATOM   14896 C  CD  . LYS   B 1 96   ? 61.74100   60.81500  -22.17100 1.000 41.73454  ?  96   LYS   B CD  1 
ATOM   14897 C  CE  . LYS   B 1 96   ? 60.25500   60.86100  -22.50400 1.000 50.13787  ?  96   LYS   B CE  1 
ATOM   14898 N  NZ  . LYS   B 1 96   ? 59.96700   60.40500  -23.89600 1.000 53.47697  ?  96   LYS   B NZ  1 
ATOM   14899 N  N   . GLY   B 1 97   ? 66.48900   57.90900  -23.51500 1.000 53.70404  ?  97   GLY   B N   1 
ATOM   14900 C  CA  . GLY   B 1 97   ? 67.46700   56.87600  -23.27600 1.000 44.35091  ?  97   GLY   B CA  1 
ATOM   14901 C  C   . GLY   B 1 97   ? 68.85100   57.46600  -23.14600 1.000 53.47820  ?  97   GLY   B C   1 
ATOM   14902 O  O   . GLY   B 1 97   ? 69.01500   58.63300  -22.79100 1.000 60.35525  ?  97   GLY   B O   1 
ATOM   14903 N  N   . VAL   B 1 98   ? 69.84900   56.63300  -23.43100 1.000 52.06737  ?  98   VAL   B N   1 
ATOM   14904 C  CA  . VAL   B 1 98   ? 71.24400   57.05100  -23.46500 1.000 42.43610  ?  98   VAL   B CA  1 
ATOM   14905 C  C   . VAL   B 1 98   ? 71.92500   56.29300  -24.59300 1.000 42.90017  ?  98   VAL   B C   1 
ATOM   14906 O  O   . VAL   B 1 98   ? 71.60600   55.13200  -24.86400 1.000 45.74835  ?  98   VAL   B O   1 
ATOM   14907 C  CB  . VAL   B 1 98   ? 71.96900   56.80200  -22.12200 1.000 50.22058  ?  98   VAL   B CB  1 
ATOM   14908 C  CG1 . VAL   B 1 98   ? 71.68200   57.92400  -21.13700 1.000 41.70819  ?  98   VAL   B CG1 1 
ATOM   14909 C  CG2 . VAL   B 1 98   ? 71.56700   55.46100  -21.54000 1.000 53.30533  ?  98   VAL   B CG2 1 
ATOM   14910 N  N   . THR   B 1 99   ? 72.87300   56.95400  -25.25400 1.000 42.96546  ?  99   THR   B N   1 
ATOM   14911 C  CA  . THR   B 1 99   ? 73.48300   56.40600  -26.46100 1.000 51.14456  ?  99   THR   B CA  1 
ATOM   14912 C  C   . THR   B 1 99   ? 74.98100   56.66900  -26.46200 1.000 51.26760  ?  99   THR   B C   1 
ATOM   14913 O  O   . THR   B 1 99   ? 75.41700   57.82400  -26.41200 1.000 35.75695  ?  99   THR   B O   1 
ATOM   14914 C  CB  . THR   B 1 99   ? 72.83400   57.00100  -27.71500 1.000 50.56166  ?  99   THR   B CB  1 
ATOM   14915 O  OG1 . THR   B 1 99   ? 71.41200   56.85400  -27.62900 1.000 58.02863  ?  99   THR   B OG1 1 
ATOM   14916 C  CG2 . THR   B 1 99   ? 73.33200   56.29300  -28.96200 1.000 49.76926  ?  99   THR   B CG2 1 
ATOM   14917 N  N   . ILE   B 1 100  ? 75.76100   55.59500  -26.51900 1.000 44.88912  ?  100  ILE   B N   1 
ATOM   14918 C  CA  . ILE   B 1 100  ? 77.19600   55.66000  -26.76400 1.000 49.55302  ?  100  ILE   B CA  1 
ATOM   14919 C  C   . ILE   B 1 100  ? 77.39400   55.38500  -28.24900 1.000 49.54404  ?  100  ILE   B C   1 
ATOM   14920 O  O   . ILE   B 1 100  ? 77.14800   54.26900  -28.71800 1.000 55.77994  ?  100  ILE   B O   1 
ATOM   14921 C  CB  . ILE   B 1 100  ? 77.96600   54.64900  -25.90400 1.000 51.13237  ?  100  ILE   B CB  1 
ATOM   14922 C  CG1 . ILE   B 1 100  ? 77.62400   54.82700  -24.42100 1.000 64.34319  ?  100  ILE   B CG1 1 
ATOM   14923 C  CG2 . ILE   B 1 100  ? 79.46000   54.77400  -26.15400 1.000 47.47936  ?  100  ILE   B CG2 1 
ATOM   14924 C  CD1 . ILE   B 1 100  ? 78.58100   55.70900  -23.65700 1.000 67.87721  ?  100  ILE   B CD1 1 
ATOM   14925 N  N   . HIS   B 1 101  ? 77.83100   56.39200  -29.00200 1.000 47.22270  ?  101  HIS   B N   1 
ATOM   14926 C  CA  . HIS   B 1 101  ? 77.86500   56.28300  -30.45400 1.000 47.84559  ?  101  HIS   B CA  1 
ATOM   14927 C  C   . HIS   B 1 101  ? 79.18200   56.83100  -30.99200 1.000 58.05403  ?  101  HIS   B C   1 
ATOM   14928 O  O   . HIS   B 1 101  ? 80.05800   57.27200  -30.24100 1.000 61.30248  ?  101  HIS   B O   1 
ATOM   14929 C  CB  . HIS   B 1 101  ? 76.67300   57.01000  -31.08400 1.000 47.88935  ?  101  HIS   B CB  1 
ATOM   14930 C  CG  . HIS   B 1 101  ? 76.72300   58.49800  -30.93200 1.000 49.89484  ?  101  HIS   B CG  1 
ATOM   14931 N  ND1 . HIS   B 1 101  ? 77.17500   59.33300  -31.93200 1.000 59.99600  ?  101  HIS   B ND1 1 
ATOM   14932 C  CD2 . HIS   B 1 101  ? 76.37200   59.30300  -29.90100 1.000 52.87965  ?  101  HIS   B CD2 1 
ATOM   14933 C  CE1 . HIS   B 1 101  ? 77.10300   60.58700  -31.52300 1.000 42.61991  ?  101  HIS   B CE1 1 
ATOM   14934 N  NE2 . HIS   B 1 101  ? 76.61800   60.59700  -30.29500 1.000 42.56626  ?  101  HIS   B NE2 1 
ATOM   14935 N  N   . LEU   B 1 102  ? 79.30700   56.79800  -32.31600 1.000 59.94744  ?  102  LEU   B N   1 
ATOM   14936 C  CA  . LEU   B 1 102  ? 80.47000   57.28400  -33.04300 1.000 52.98040  ?  102  LEU   B CA  1 
ATOM   14937 C  C   . LEU   B 1 102  ? 80.21500   58.68800  -33.58000 1.000 49.04533  ?  102  LEU   B C   1 
ATOM   14938 O  O   . LEU   B 1 102  ? 79.07400   59.10100  -33.79300 1.000 70.76237  ?  102  LEU   B O   1 
ATOM   14939 C  CB  . LEU   B 1 102  ? 80.81400   56.34000  -34.19800 1.000 57.05419  ?  102  LEU   B CB  1 
ATOM   14940 C  CG  . LEU   B 1 102  ? 81.69100   55.13900  -33.84400 1.000 60.48211  ?  102  LEU   B CG  1 
ATOM   14941 C  CD1 . LEU   B 1 102  ? 81.43300   53.98500  -34.80100 1.000 45.67029  ?  102  LEU   B CD1 1 
ATOM   14942 C  CD2 . LEU   B 1 102  ? 83.16200   55.53200  -33.85300 1.000 55.29904  ?  102  LEU   B CD2 1 
ATOM   14943 N  N   . ILE   B 1 103  ? 81.30300   59.41500  -33.81400 1.000 43.25394  ?  103  ILE   B N   1 
ATOM   14944 C  CA  . ILE   B 1 103  ? 81.24600   60.80800  -34.24600 1.000 54.58614  ?  103  ILE   B CA  1 
ATOM   14945 C  C   . ILE   B 1 103  ? 81.49200   60.87700  -35.74500 1.000 56.80253  ?  103  ILE   B C   1 
ATOM   14946 O  O   . ILE   B 1 103  ? 82.39800   60.21700  -36.26800 1.000 67.25233  ?  103  ILE   B O   1 
ATOM   14947 C  CB  . ILE   B 1 103  ? 82.27000   61.66300  -33.47400 1.000 47.13173  ?  103  ILE   B CB  1 
ATOM   14948 C  CG1 . ILE   B 1 103  ? 81.69200   62.10800  -32.12900 1.000 53.77722  ?  103  ILE   B CG1 1 
ATOM   14949 C  CG2 . ILE   B 1 103  ? 82.70600   62.86700  -34.29700 1.000 43.99877  ?  103  ILE   B CG2 1 
ATOM   14950 C  CD1 . ILE   B 1 103  ? 80.81400   63.34700  -32.21000 1.000 53.68056  ?  103  ILE   B CD1 1 
ATOM   14951 N  N   . ASP   B 1 104  ? 80.68100   61.67100  -36.44600 1.000 73.67043  ?  104  ASP   B N   1 
ATOM   14952 C  CA  . ASP   B 1 104  ? 80.91500   61.90200  -37.86500 1.000 65.81451  ?  104  ASP   B CA  1 
ATOM   14953 C  C   . ASP   B 1 104  ? 81.07600   63.39300  -38.15300 1.000 71.71623  ?  104  ASP   B C   1 
ATOM   14954 O  O   . ASP   B 1 104  ? 81.53100   64.15000  -37.28900 1.000 68.60368  ?  104  ASP   B O   1 
ATOM   14955 C  CB  . ASP   B 1 104  ? 79.79100   61.28400  -38.71000 1.000 63.14837  ?  104  ASP   B CB  1 
ATOM   14956 C  CG  . ASP   B 1 104  ? 78.43300   61.94100  -38.48900 1.000 79.68264  ?  104  ASP   B CG  1 
ATOM   14957 O  OD1 . ASP   B 1 104  ? 78.34100   62.97800  -37.79800 1.000 91.78484  ?  104  ASP   B OD1 1 
ATOM   14958 O  OD2 . ASP   B 1 104  ? 77.44100   61.41400  -39.03600 1.000 78.24183  -1 104  ASP   B OD2 1 
ATOM   14959 N  N   . GLU   B 1 105  ? 80.70700   63.81900  -39.35900 1.000 77.61575  ?  105  GLU   B N   1 
ATOM   14960 C  CA  . GLU   B 1 105  ? 80.82700   65.20800  -39.78200 1.000 71.19844  ?  105  GLU   B CA  1 
ATOM   14961 C  C   . GLU   B 1 105  ? 79.56700   66.02200  -39.51300 1.000 73.81573  ?  105  GLU   B C   1 
ATOM   14962 O  O   . GLU   B 1 105  ? 79.53000   67.21100  -39.84900 1.000 74.30977  ?  105  GLU   B O   1 
ATOM   14963 C  CB  . GLU   B 1 105  ? 81.17300   65.27500  -41.27600 1.000 83.04715  ?  105  GLU   B CB  1 
ATOM   14964 C  CG  . GLU   B 1 105  ? 82.01800   64.10300  -41.79000 1.000 96.81933  ?  105  GLU   B CG  1 
ATOM   14965 C  CD  . GLU   B 1 105  ? 81.19300   62.87000  -42.15100 1.000 95.98061  ?  105  GLU   B CD  1 
ATOM   14966 O  OE1 . GLU   B 1 105  ? 80.13800   62.64300  -41.52000 1.000 95.26463  ?  105  GLU   B OE1 1 
ATOM   14967 O  OE2 . GLU   B 1 105  ? 81.60700   62.12000  -43.06200 1.000 104.36277 -1 105  GLU   B OE2 1 
ATOM   14968 N  N   . HIS   B 1 106  ? 78.54300   65.41900  -38.92400 1.000 74.14478  ?  106  HIS   B N   1 
ATOM   14969 C  CA  . HIS   B 1 106  ? 77.30800   66.10300  -38.57600 1.000 75.83055  ?  106  HIS   B CA  1 
ATOM   14970 C  C   . HIS   B 1 106  ? 77.03900   65.93200  -37.08300 1.000 83.13074  ?  106  HIS   B C   1 
ATOM   14971 O  O   . HIS   B 1 106  ? 77.84000   65.35000  -36.34600 1.000 86.39235  ?  106  HIS   B O   1 
ATOM   14972 C  CB  . HIS   B 1 106  ? 76.14700   65.58600  -39.43000 1.000 79.97055  ?  106  HIS   B CB  1 
ATOM   14973 C  CG  . HIS   B 1 106  ? 76.33100   65.82300  -40.89700 1.000 89.52494  ?  106  HIS   B CG  1 
ATOM   14974 N  ND1 . HIS   B 1 106  ? 76.15400   64.83400  -41.84200 1.000 79.60089  ?  106  HIS   B ND1 1 
ATOM   14975 C  CD2 . HIS   B 1 106  ? 76.68500   66.93700  -41.58100 1.000 76.41557  ?  106  HIS   B CD2 1 
ATOM   14976 C  CE1 . HIS   B 1 106  ? 76.38700   65.33000  -43.04400 1.000 79.38243  ?  106  HIS   B CE1 1 
ATOM   14977 N  NE2 . HIS   B 1 106  ? 76.71100   66.60400  -42.91300 1.000 67.02102  ?  106  HIS   B NE2 1 
ATOM   14978 N  N   . VAL   B 1 107  ? 75.90000   66.44900  -36.63500 1.000 71.24975  ?  107  VAL   B N   1 
ATOM   14979 C  CA  . VAL   B 1 107  ? 75.59200   66.52700  -35.21100 1.000 59.23854  ?  107  VAL   B CA  1 
ATOM   14980 C  C   . VAL   B 1 107  ? 74.84500   65.26600  -34.79000 1.000 53.25008  ?  107  VAL   B C   1 
ATOM   14981 O  O   . VAL   B 1 107  ? 73.65800   65.10500  -35.08800 1.000 62.96765  ?  107  VAL   B O   1 
ATOM   14982 C  CB  . VAL   B 1 107  ? 74.78500   67.78600  -34.88200 1.000 53.47288  ?  107  VAL   B CB  1 
ATOM   14983 C  CG1 . VAL   B 1 107  ? 74.29900   67.73500  -33.44400 1.000 66.73823  ?  107  VAL   B CG1 1 
ATOM   14984 C  CG2 . VAL   B 1 107  ? 75.63500   69.02200  -35.12100 1.000 51.02044  ?  107  VAL   B CG2 1 
ATOM   14985 N  N   . ASP   B 1 108  ? 75.55000   64.37400  -34.08800 1.000 50.66764  ?  108  ASP   B N   1 
ATOM   14986 C  CA  . ASP   B 1 108  ? 74.96200   63.18400  -33.47000 1.000 50.56399  ?  108  ASP   B CA  1 
ATOM   14987 C  C   . ASP   B 1 108  ? 74.24100   62.30900  -34.49300 1.000 52.11875  ?  108  ASP   B C   1 
ATOM   14988 O  O   . ASP   B 1 108  ? 73.21800   61.68700  -34.19900 1.000 58.36880  ?  108  ASP   B O   1 
ATOM   14989 C  CB  . ASP   B 1 108  ? 74.02900   63.56700  -32.31800 1.000 60.78162  ?  108  ASP   B CB  1 
ATOM   14990 C  CG  . ASP   B 1 108  ? 74.69700   64.48200  -31.30400 1.000 64.44856  ?  108  ASP   B CG  1 
ATOM   14991 O  OD1 . ASP   B 1 108  ? 75.94100   64.43800  -31.18900 1.000 69.66240  ?  108  ASP   B OD1 1 
ATOM   14992 O  OD2 . ASP   B 1 108  ? 73.98200   65.24900  -30.62600 1.000 63.65526  -1 108  ASP   B OD2 1 
ATOM   14993 N  N   . THR   B 1 109  ? 74.78500   62.25400  -35.70600 1.000 60.28762  ?  109  THR   B N   1 
ATOM   14994 C  CA  . THR   B 1 109  ? 74.27700   61.37400  -36.74900 1.000 68.65534  ?  109  THR   B CA  1 
ATOM   14995 C  C   . THR   B 1 109  ? 75.13900   60.13200  -36.92800 1.000 73.07756  ?  109  THR   B C   1 
ATOM   14996 O  O   . THR   B 1 109  ? 74.97200   59.41100  -37.91700 1.000 79.58229  ?  109  THR   B O   1 
ATOM   14997 C  CB  . THR   B 1 109  ? 74.16800   62.12900  -38.07400 1.000 57.57403  ?  109  THR   B CB  1 
ATOM   14998 O  OG1 . THR   B 1 109  ? 75.47000   62.26800  -38.65500 1.000 73.10376  ?  109  THR   B OG1 1 
ATOM   14999 C  CG2 . THR   B 1 109  ? 73.58200   63.50300  -37.85000 1.000 70.41868  ?  109  THR   B CG2 1 
ATOM   15000 N  N   . GLY   B 1 110  ? 76.05300   59.86500  -35.99500 1.000 75.79071  ?  110  GLY   B N   1 
ATOM   15001 C  CA  . GLY   B 1 110  ? 76.95700   58.74600  -36.13100 1.000 63.55388  ?  110  GLY   B CA  1 
ATOM   15002 C  C   . GLY   B 1 110  ? 76.29000   57.41600  -35.85800 1.000 61.42749  ?  110  GLY   B C   1 
ATOM   15003 O  O   . GLY   B 1 110  ? 75.12900   57.33700  -35.45800 1.000 79.04026  ?  110  GLY   B O   1 
ATOM   15004 N  N   . ASP   B 1 111  ? 77.05100   56.35000  -36.08500 1.000 57.86044  ?  111  ASP   B N   1 
ATOM   15005 C  CA  . ASP   B 1 111  ? 76.54400   55.00300  -35.87900 1.000 69.90845  ?  111  ASP   B CA  1 
ATOM   15006 C  C   . ASP   B 1 111  ? 76.54100   54.65200  -34.39800 1.000 60.36103  ?  111  ASP   B C   1 
ATOM   15007 O  O   . ASP   B 1 111  ? 77.42200   55.06500  -33.63800 1.000 55.68976  ?  111  ASP   B O   1 
ATOM   15008 C  CB  . ASP   B 1 111  ? 77.38200   53.98800  -36.65400 1.000 76.45724  ?  111  ASP   B CB  1 
ATOM   15009 C  CG  . ASP   B 1 111  ? 77.26300   54.16200  -38.15100 1.000 95.05047  ?  111  ASP   B CG  1 
ATOM   15010 O  OD1 . ASP   B 1 111  ? 76.34500   53.56200  -38.74500 1.000 100.80815 ?  111  ASP   B OD1 1 
ATOM   15011 O  OD2 . ASP   B 1 111  ? 78.08500   54.90300  -38.73200 1.000 97.61234  -1 111  ASP   B OD2 1 
ATOM   15012 N  N   . ILE   B 1 112  ? 75.54200   53.87400  -33.99700 1.000 55.88186  ?  112  ILE   B N   1 
ATOM   15013 C  CA  . ILE   B 1 112  ? 75.35100   53.53300  -32.59200 1.000 59.15458  ?  112  ILE   B CA  1 
ATOM   15014 C  C   . ILE   B 1 112  ? 76.25300   52.36400  -32.22600 1.000 60.40492  ?  112  ILE   B C   1 
ATOM   15015 O  O   . ILE   B 1 112  ? 76.24500   51.32400  -32.89400 1.000 71.01313  ?  112  ILE   B O   1 
ATOM   15016 C  CB  . ILE   B 1 112  ? 73.87800   53.20200  -32.30800 1.000 59.94898  ?  112  ILE   B CB  1 
ATOM   15017 C  CG1 . ILE   B 1 112  ? 72.96800   54.26600  -32.92600 1.000 72.99550  ?  112  ILE   B CG1 1 
ATOM   15018 C  CG2 . ILE   B 1 112  ? 73.63900   53.07100  -30.80800 1.000 62.75493  ?  112  ILE   B CG2 1 
ATOM   15019 C  CD1 . ILE   B 1 112  ? 71.59400   54.33900  -32.30500 1.000 60.74141  ?  112  ILE   B CD1 1 
ATOM   15020 N  N   . LEU   B 1 113  ? 77.03600   52.53300  -31.16300 1.000 54.29262  ?  113  LEU   B N   1 
ATOM   15021 C  CA  . LEU   B 1 113  ? 77.79000   51.41900  -30.60100 1.000 50.23003  ?  113  LEU   B CA  1 
ATOM   15022 C  C   . LEU   B 1 113  ? 76.93700   50.65800  -29.59000 1.000 49.56571  ?  113  LEU   B C   1 
ATOM   15023 O  O   . LEU   B 1 113  ? 76.60800   49.48700  -29.80200 1.000 64.14401  ?  113  LEU   B O   1 
ATOM   15024 C  CB  . LEU   B 1 113  ? 79.08800   51.92700  -29.96400 1.000 59.42417  ?  113  LEU   B CB  1 
ATOM   15025 C  CG  . LEU   B 1 113  ? 80.01100   52.73100  -30.88200 1.000 56.73213  ?  113  LEU   B CG  1 
ATOM   15026 C  CD1 . LEU   B 1 113  ? 80.93500   53.63300  -30.07300 1.000 55.58630  ?  113  LEU   B CD1 1 
ATOM   15027 C  CD2 . LEU   B 1 113  ? 80.80800   51.79800  -31.77800 1.000 53.14609  ?  113  LEU   B CD2 1 
ATOM   15028 N  N   . VAL   B 1 114  ? 76.56800   51.31400  -28.49000 1.000 57.36079  ?  114  VAL   B N   1 
ATOM   15029 C  CA  . VAL   B 1 114  ? 75.66900   50.74400  -27.49300 1.000 66.54809  ?  114  VAL   B CA  1 
ATOM   15030 C  C   . VAL   B 1 114  ? 74.61400   51.78100  -27.12800 1.000 61.48407  ?  114  VAL   B C   1 
ATOM   15031 O  O   . VAL   B 1 114  ? 74.87000   52.98900  -27.13100 1.000 50.93588  ?  114  VAL   B O   1 
ATOM   15032 C  CB  . VAL   B 1 114  ? 76.41400   50.26500  -26.22300 1.000 65.03559  ?  114  VAL   B CB  1 
ATOM   15033 C  CG1 . VAL   B 1 114  ? 75.57300   49.24100  -25.46800 1.000 59.82683  ?  114  VAL   B CG1 1 
ATOM   15034 C  CG2 . VAL   B 1 114  ? 77.77700   49.67800  -26.57500 1.000 75.72598  ?  114  VAL   B CG2 1 
ATOM   15035 N  N   . GLN   B 1 115  ? 73.41700   51.29300  -26.81300 1.000 67.75597  ?  115  GLN   B N   1 
ATOM   15036 C  CA  . GLN   B 1 115  ? 72.29700   52.13000  -26.41200 1.000 53.93640  ?  115  GLN   B CA  1 
ATOM   15037 C  C   . GLN   B 1 115  ? 71.62800   51.52200  -25.18700 1.000 53.25361  ?  115  GLN   B C   1 
ATOM   15038 O  O   . GLN   B 1 115  ? 71.81100   50.34200  -24.87600 1.000 75.04591  ?  115  GLN   B O   1 
ATOM   15039 C  CB  . GLN   B 1 115  ? 71.27400   52.27500  -27.54200 1.000 58.01724  ?  115  GLN   B CB  1 
ATOM   15040 C  CG  . GLN   B 1 115  ? 70.97800   53.70300  -27.94100 1.000 52.91784  ?  115  GLN   B CG  1 
ATOM   15041 C  CD  . GLN   B 1 115  ? 69.99900   53.78100  -29.09300 1.000 62.23020  ?  115  GLN   B CD  1 
ATOM   15042 O  OE1 . GLN   B 1 115  ? 69.42100   52.77200  -29.50000 1.000 71.82602  ?  115  GLN   B OE1 1 
ATOM   15043 N  NE2 . GLN   B 1 115  ? 69.80200   54.98200  -29.62200 1.000 56.05264  ?  115  GLN   B NE2 1 
ATOM   15044 N  N   . GLU   B 1 116  ? 70.84600   52.34200  -24.48800 1.000 49.72307  ?  116  GLU   B N   1 
ATOM   15045 C  CA  . GLU   B 1 116  ? 70.11400   51.87300  -23.31800 1.000 48.11639  ?  116  GLU   B CA  1 
ATOM   15046 C  C   . GLU   B 1 116  ? 68.90700   52.76900  -23.09900 1.000 56.28602  ?  116  GLU   B C   1 
ATOM   15047 O  O   . GLU   B 1 116  ? 69.03000   53.99800  -23.11800 1.000 42.49869  ?  116  GLU   B O   1 
ATOM   15048 C  CB  . GLU   B 1 116  ? 71.00000   51.85700  -22.06400 1.000 51.80743  ?  116  GLU   B CB  1 
ATOM   15049 C  CG  . GLU   B 1 116  ? 70.35700   51.15400  -20.87000 1.000 52.47352  ?  116  GLU   B CG  1 
ATOM   15050 C  CD  . GLU   B 1 116  ? 70.98100   51.53800  -19.53600 1.000 71.01546  ?  116  GLU   B CD  1 
ATOM   15051 O  OE1 . GLU   B 1 116  ? 71.80200   52.47900  -19.50100 1.000 68.08907  ?  116  GLU   B OE1 1 
ATOM   15052 O  OE2 . GLU   B 1 116  ? 70.64900   50.89400  -18.51800 1.000 77.01063  -1 116  GLU   B OE2 1 
ATOM   15053 N  N   . GLU   B 1 117  ? 67.75000   52.14800  -22.89100 1.000 57.19214  ?  117  GLU   B N   1 
ATOM   15054 C  CA  . GLU   B 1 117  ? 66.51600   52.88000  -22.65700 1.000 57.65777  ?  117  GLU   B CA  1 
ATOM   15055 C  C   . GLU   B 1 117  ? 66.38100   53.22500  -21.18200 1.000 54.11485  ?  117  GLU   B C   1 
ATOM   15056 O  O   . GLU   B 1 117  ? 66.67700   52.40600  -20.30700 1.000 62.20625  ?  117  GLU   B O   1 
ATOM   15057 C  CB  . GLU   B 1 117  ? 65.31700   52.05000  -23.11200 1.000 68.66186  ?  117  GLU   B CB  1 
ATOM   15058 C  CG  . GLU   B 1 117  ? 64.03700   52.84300  -23.28600 1.000 81.91273  ?  117  GLU   B CG  1 
ATOM   15059 C  CD  . GLU   B 1 117  ? 63.28700   52.46200  -24.54800 1.000 92.85889  ?  117  GLU   B CD  1 
ATOM   15060 O  OE1 . GLU   B 1 117  ? 63.50200   51.34000  -25.05300 1.000 82.50753  ?  117  GLU   B OE1 1 
ATOM   15061 O  OE2 . GLU   B 1 117  ? 62.47800   53.28200  -25.03100 1.000 104.17367 -1 117  GLU   B OE2 1 
ATOM   15062 N  N   . ILE   B 1 118  ? 65.93900   54.45000  -20.90700 1.000 59.04110  ?  118  ILE   B N   1 
ATOM   15063 C  CA  . ILE   B 1 118  ? 65.76100   54.92900  -19.54500 1.000 56.07490  ?  118  ILE   B CA  1 
ATOM   15064 C  C   . ILE   B 1 118  ? 64.31500   55.38700  -19.37700 1.000 58.86316  ?  118  ILE   B C   1 
ATOM   15065 O  O   . ILE   B 1 118  ? 63.55700   55.49100  -20.34100 1.000 59.65520  ?  118  ILE   B O   1 
ATOM   15066 C  CB  . ILE   B 1 118  ? 66.75200   56.05400  -19.18500 1.000 46.37901  ?  118  ILE   B CB  1 
ATOM   15067 C  CG1 . ILE   B 1 118  ? 66.20900   57.42000  -19.60400 1.000 50.02737  ?  118  ILE   B CG1 1 
ATOM   15068 C  CG2 . ILE   B 1 118  ? 68.10400   55.80500  -19.83600 1.000 60.14586  ?  118  ILE   B CG2 1 
ATOM   15069 C  CD1 . ILE   B 1 118  ? 67.18500   58.55200  -19.36200 1.000 52.32022  ?  118  ILE   B CD1 1 
ATOM   15070 N  N   . ALA   B 1 119  ? 63.93800   55.65400  -18.12700 1.000 57.07344  ?  119  ALA   B N   1 
ATOM   15071 C  CA  . ALA   B 1 119  ? 62.55700   55.98300  -17.79800 1.000 49.58795  ?  119  ALA   B CA  1 
ATOM   15072 C  C   . ALA   B 1 119  ? 62.50400   57.12100  -16.78900 1.000 54.96758  ?  119  ALA   B C   1 
ATOM   15073 O  O   . ALA   B 1 119  ? 63.17500   57.06900  -15.75400 1.000 51.62725  ?  119  ALA   B O   1 
ATOM   15074 C  CB  . ALA   B 1 119  ? 61.82300   54.75800  -17.24200 1.000 55.51973  ?  119  ALA   B CB  1 
ATOM   15075 N  N   . PHE   B 1 120  ? 61.69500   58.13400  -17.09000 1.000 47.97400  ?  120  PHE   B N   1 
ATOM   15076 C  CA  . PHE   B 1 120  ? 61.42100   59.23400  -16.17600 1.000 44.58884  ?  120  PHE   B CA  1 
ATOM   15077 C  C   . PHE   B 1 120  ? 60.02900   59.08100  -15.57200 1.000 44.71934  ?  120  PHE   B C   1 
ATOM   15078 O  O   . PHE   B 1 120  ? 59.12100   58.52300  -16.19200 1.000 57.93844  ?  120  PHE   B O   1 
ATOM   15079 C  CB  . PHE   B 1 120  ? 61.52000   60.58300  -16.89000 1.000 43.27007  ?  120  PHE   B CB  1 
ATOM   15080 C  CG  . PHE   B 1 120  ? 62.86500   60.85700  -17.49500 1.000 50.84309  ?  120  PHE   B CG  1 
ATOM   15081 C  CD1 . PHE   B 1 120  ? 64.02700   60.53100  -16.81600 1.000 66.76016  ?  120  PHE   B CD1 1 
ATOM   15082 C  CD2 . PHE   B 1 120  ? 62.96600   61.44100  -18.74700 1.000 38.12450  ?  120  PHE   B CD2 1 
ATOM   15083 C  CE1 . PHE   B 1 120  ? 65.26700   60.78700  -17.37500 1.000 57.75465  ?  120  PHE   B CE1 1 
ATOM   15084 C  CE2 . PHE   B 1 120  ? 64.20000   61.69600  -19.31200 1.000 43.63711  ?  120  PHE   B CE2 1 
ATOM   15085 C  CZ  . PHE   B 1 120  ? 65.35200   61.37100  -18.62500 1.000 43.81057  ?  120  PHE   B CZ  1 
ATOM   15086 N  N   . ALA   B 1 121  ? 59.86700   59.59500  -14.35900 1.000 49.30563  ?  121  ALA   B N   1 
ATOM   15087 C  CA  . ALA   B 1 121  ? 58.60100   59.53600  -13.64500 1.000 42.31772  ?  121  ALA   B CA  1 
ATOM   15088 C  C   . ALA   B 1 121  ? 57.81600   60.82800  -13.83900 1.000 59.32532  ?  121  ALA   B C   1 
ATOM   15089 O  O   . ALA   B 1 121  ? 58.37400   61.88600  -14.14000 1.000 62.78614  ?  121  ALA   B O   1 
ATOM   15090 C  CB  . ALA   B 1 121  ? 58.83000   59.28200  -12.15200 1.000 33.38157  ?  121  ALA   B CB  1 
ATOM   15091 N  N   . ASP   B 1 122  ? 56.49600   60.72800  -13.66100 1.000 56.95895  ?  122  ASP   B N   1 
ATOM   15092 C  CA  . ASP   B 1 122  ? 55.64800   61.90400  -13.81900 1.000 59.14205  ?  122  ASP   B CA  1 
ATOM   15093 C  C   . ASP   B 1 122  ? 55.89200   62.91900  -12.71200 1.000 51.96393  ?  122  ASP   B C   1 
ATOM   15094 O  O   . ASP   B 1 122  ? 55.75300   64.12700  -12.93600 1.000 52.19353  ?  122  ASP   B O   1 
ATOM   15095 C  CB  . ASP   B 1 122  ? 54.17500   61.49600  -13.85200 1.000 68.07056  ?  122  ASP   B CB  1 
ATOM   15096 C  CG  . ASP   B 1 122  ? 53.85600   60.54100  -14.98900 1.000 75.60062  ?  122  ASP   B CG  1 
ATOM   15097 O  OD1 . ASP   B 1 122  ? 54.57000   59.52600  -15.14100 1.000 89.01587  ?  122  ASP   B OD1 1 
ATOM   15098 O  OD2 . ASP   B 1 122  ? 52.88500   60.80400  -15.72800 1.000 69.78473  -1 122  ASP   B OD2 1 
ATOM   15099 N  N   . GLU   B 1 123  ? 56.25300   62.45400  -11.52000 1.000 46.23676  ?  123  GLU   B N   1 
ATOM   15100 C  CA  . GLU   B 1 123  ? 56.55500   63.34000  -10.40600 1.000 52.17365  ?  123  GLU   B CA  1 
ATOM   15101 C  C   . GLU   B 1 123  ? 58.01900   63.74600  -10.36100 1.000 52.23734  ?  123  GLU   B C   1 
ATOM   15102 O  O   . GLU   B 1 123  ? 58.42600   64.44500  -9.42700  1.000 51.36469  ?  123  GLU   B O   1 
ATOM   15103 C  CB  . GLU   B 1 123  ? 56.15400   62.68000  -9.08300  1.000 53.05821  ?  123  GLU   B CB  1 
ATOM   15104 C  CG  . GLU   B 1 123  ? 54.67500   62.34300  -8.99300  1.000 68.44785  ?  123  GLU   B CG  1 
ATOM   15105 C  CD  . GLU   B 1 123  ? 53.78200   63.56800  -9.12300  1.000 85.84080  ?  123  GLU   B CD  1 
ATOM   15106 O  OE1 . GLU   B 1 123  ? 54.14800   64.64200  -8.59700  1.000 79.31457  ?  123  GLU   B OE1 1 
ATOM   15107 O  OE2 . GLU   B 1 123  ? 52.70800   63.45500  -9.75300  1.000 86.47121  -1 123  GLU   B OE2 1 
ATOM   15108 N  N   . ASP   B 1 124  ? 58.81300   63.33000  -11.34300 1.000 44.09172  ?  124  ASP   B N   1 
ATOM   15109 C  CA  . ASP   B 1 124  ? 60.20600   63.73700  -11.42000 1.000 46.15478  ?  124  ASP   B CA  1 
ATOM   15110 C  C   . ASP   B 1 124  ? 60.31700   65.13800  -12.00300 1.000 47.79510  ?  124  ASP   B C   1 
ATOM   15111 O  O   . ASP   B 1 124  ? 59.61200   65.48700  -12.95400 1.000 43.95821  ?  124  ASP   B O   1 
ATOM   15112 C  CB  . ASP   B 1 124  ? 60.99800   62.75500  -12.28000 1.000 41.17561  ?  124  ASP   B CB  1 
ATOM   15113 C  CG  . ASP   B 1 124  ? 61.71900   61.71700  -11.45900 1.000 58.00007  ?  124  ASP   B CG  1 
ATOM   15114 O  OD1 . ASP   B 1 124  ? 62.01100   61.99500  -10.27500 1.000 67.15118  ?  124  ASP   B OD1 1 
ATOM   15115 O  OD2 . ASP   B 1 124  ? 61.99100   60.62400  -11.99800 1.000 55.63609  -1 124  ASP   B OD2 1 
ATOM   15116 N  N   . THR   B 1 125  ? 61.20600   65.94400  -11.43000 1.000 37.90039  ?  125  THR   B N   1 
ATOM   15117 C  CA  . THR   B 1 125  ? 61.46400   67.25600  -11.99700 1.000 38.49504  ?  125  THR   B CA  1 
ATOM   15118 C  C   . THR   B 1 125  ? 62.45200   67.14800  -13.15400 1.000 41.37079  ?  125  THR   B C   1 
ATOM   15119 O  O   . THR   B 1 125  ? 63.11900   66.12600  -13.34200 1.000 33.99998  ?  125  THR   B O   1 
ATOM   15120 C  CB  . THR   B 1 125  ? 62.01100   68.21700  -10.94000 1.000 46.86812  ?  125  THR   B CB  1 
ATOM   15121 O  OG1 . THR   B 1 125  ? 63.43000   68.04600  -10.82000 1.000 52.91767  ?  125  THR   B OG1 1 
ATOM   15122 C  CG2 . THR   B 1 125  ? 61.36000   67.95300  -9.60000  1.000 56.16529  ?  125  THR   B CG2 1 
ATOM   15123 N  N   . LEU   B 1 126  ? 62.52900   68.22400  -13.94200 1.000 34.38672  ?  126  LEU   B N   1 
ATOM   15124 C  CA  . LEU   B 1 126  ? 63.49400   68.25800  -15.03600 1.000 36.22097  ?  126  LEU   B CA  1 
ATOM   15125 C  C   . LEU   B 1 126  ? 64.91000   68.05900  -14.51500 1.000 39.92617  ?  126  LEU   B C   1 
ATOM   15126 O  O   . LEU   B 1 126  ? 65.68700   67.28700  -15.08900 1.000 44.70212  ?  126  LEU   B O   1 
ATOM   15127 C  CB  . LEU   B 1 126  ? 63.38200   69.57700  -15.80300 1.000 38.60919  ?  126  LEU   B CB  1 
ATOM   15128 C  CG  . LEU   B 1 126  ? 62.53100   69.58200  -17.07700 1.000 46.50737  ?  126  LEU   B CG  1 
ATOM   15129 C  CD1 . LEU   B 1 126  ? 62.97200   68.49200  -18.05000 1.000 47.97166  ?  126  LEU   B CD1 1 
ATOM   15130 C  CD2 . LEU   B 1 126  ? 61.06200   69.43700  -16.74000 1.000 53.08785  ?  126  LEU   B CD2 1 
ATOM   15131 N  N   . LEU   B 1 127  ? 65.25700   68.73600  -13.41700 1.000 42.73069  ?  127  LEU   B N   1 
ATOM   15132 C  CA  . LEU   B 1 127  ? 66.56400   68.53500  -12.80200 1.000 36.83438  ?  127  LEU   B CA  1 
ATOM   15133 C  C   . LEU   B 1 127  ? 66.75000   67.08700  -12.37100 1.000 39.37686  ?  127  LEU   B C   1 
ATOM   15134 O  O   . LEU   B 1 127  ? 67.84400   66.52600  -12.50600 1.000 47.55228  ?  127  LEU   B O   1 
ATOM   15135 C  CB  . LEU   B 1 127  ? 66.72900   69.47800  -11.61100 1.000 22.95734  ?  127  LEU   B CB  1 
ATOM   15136 C  CG  . LEU   B 1 127  ? 66.73100   70.96000  -11.98800 1.000 37.61537  ?  127  LEU   B CG  1 
ATOM   15137 C  CD1 . LEU   B 1 127  ? 66.91500   71.84200  -10.76500 1.000 30.80861  ?  127  LEU   B CD1 1 
ATOM   15138 C  CD2 . LEU   B 1 127  ? 67.81100   71.24000  -13.02000 1.000 43.95142  ?  127  LEU   B CD2 1 
ATOM   15139 N  N   . ASP   B 1 128  ? 65.68800   66.46100  -11.85700 1.000 37.76408  ?  128  ASP   B N   1 
ATOM   15140 C  CA  . ASP   B 1 128  ? 65.77500   65.05300  -11.48700 1.000 43.20415  ?  128  ASP   B CA  1 
ATOM   15141 C  C   . ASP   B 1 128  ? 65.99600   64.16900  -12.70600 1.000 47.30990  ?  128  ASP   B C   1 
ATOM   15142 O  O   . ASP   B 1 128  ? 66.70000   63.15700  -12.61600 1.000 43.07693  ?  128  ASP   B O   1 
ATOM   15143 C  CB  . ASP   B 1 128  ? 64.51300   64.62700  -10.73800 1.000 45.72347  ?  128  ASP   B CB  1 
ATOM   15144 C  CG  . ASP   B 1 128  ? 64.38200   65.29800  -9.38500  1.000 50.55691  ?  128  ASP   B CG  1 
ATOM   15145 O  OD1 . ASP   B 1 128  ? 65.41800   65.70500  -8.81700  1.000 65.36276  ?  128  ASP   B OD1 1 
ATOM   15146 O  OD2 . ASP   B 1 128  ? 63.24100   65.42400  -8.89200  1.000 58.59346  -1 128  ASP   B OD2 1 
ATOM   15147 N  N   . CYS   B 1 129  ? 65.41500   64.53500  -13.85200 1.000 52.70755  ?  129  CYS   B N   1 
ATOM   15148 C  CA  . CYS   B 1 129  ? 65.62000   63.75300  -15.06700 1.000 48.16890  ?  129  CYS   B CA  1 
ATOM   15149 C  C   . CYS   B 1 129  ? 67.04400   63.90100  -15.58800 1.000 45.56786  ?  129  CYS   B C   1 
ATOM   15150 O  O   . CYS   B 1 129  ? 67.64800   62.91900  -16.03500 1.000 51.29487  ?  129  CYS   B O   1 
ATOM   15151 C  CB  . CYS   B 1 129  ? 64.61800   64.17000  -16.14300 1.000 37.46974  ?  129  CYS   B CB  1 
ATOM   15152 S  SG  . CYS   B 1 129  ? 62.88900   63.89900  -15.70900 1.000 51.01085  ?  129  CYS   B SG  1 
ATOM   15153 N  N   . TYR   B 1 130  ? 67.59200   65.12200  -15.55100 1.000 39.39454  ?  130  TYR   B N   1 
ATOM   15154 C  CA  . TYR   B 1 130  ? 68.95900   65.33300  -16.02000 1.000 35.14556  ?  130  TYR   B CA  1 
ATOM   15155 C  C   . TYR   B 1 130  ? 69.93100   64.42700  -15.28100 1.000 41.25717  ?  130  TYR   B C   1 
ATOM   15156 O  O   . TYR   B 1 130  ? 70.83600   63.84500  -15.89100 1.000 47.11233  ?  130  TYR   B O   1 
ATOM   15157 C  CB  . TYR   B 1 130  ? 69.37900   66.79500  -15.83900 1.000 32.60868  ?  130  TYR   B CB  1 
ATOM   15158 C  CG  . TYR   B 1 130  ? 68.47000   67.81700  -16.47500 1.000 37.96979  ?  130  TYR   B CG  1 
ATOM   15159 C  CD1 . TYR   B 1 130  ? 67.62500   67.47000  -17.51600 1.000 39.76079  ?  130  TYR   B CD1 1 
ATOM   15160 C  CD2 . TYR   B 1 130  ? 68.45000   69.13200  -16.02100 1.000 31.62737  ?  130  TYR   B CD2 1 
ATOM   15161 C  CE1 . TYR   B 1 130  ? 66.79100   68.39200  -18.08900 1.000 40.82660  ?  130  TYR   B CE1 1 
ATOM   15162 C  CE2 . TYR   B 1 130  ? 67.61500   70.06700  -16.59000 1.000 32.95186  ?  130  TYR   B CE2 1 
ATOM   15163 C  CZ  . TYR   B 1 130  ? 66.78700   69.68700  -17.62700 1.000 43.12752  ?  130  TYR   B CZ  1 
ATOM   15164 O  OH  . TYR   B 1 130  ? 65.94200   70.59000  -18.22100 1.000 58.52946  ?  130  TYR   B OH  1 
ATOM   15165 N  N   . ASN   B 1 131  ? 69.75400   64.29000  -13.96500 1.000 38.26904  ?  131  ASN   B N   1 
ATOM   15166 C  CA  . ASN   B 1 131  ? 70.65900   63.46000  -13.17700 1.000 51.20507  ?  131  ASN   B CA  1 
ATOM   15167 C  C   . ASN   B 1 131  ? 70.55900   61.99600  -13.58800 1.000 45.91413  ?  131  ASN   B C   1 
ATOM   15168 O  O   . ASN   B 1 131  ? 71.57800   61.31800  -13.76400 1.000 53.27784  ?  131  ASN   B O   1 
ATOM   15169 C  CB  . ASN   B 1 131  ? 70.35800   63.62300  -11.68500 1.000 47.92658  ?  131  ASN   B CB  1 
ATOM   15170 C  CG  . ASN   B 1 131  ? 70.83500   64.95300  -11.12700 1.000 45.65422  ?  131  ASN   B CG  1 
ATOM   15171 O  OD1 . ASN   B 1 131  ? 71.80800   65.53600  -11.60900 1.000 66.54465  ?  131  ASN   B OD1 1 
ATOM   15172 N  ND2 . ASN   B 1 131  ? 70.14900   65.43900  -10.10000 1.000 43.18217  ?  131  ASN   B ND2 1 
ATOM   15173 N  N   . LYS   B 1 132  ? 69.33200   61.49200  -13.75100 1.000 43.48589  ?  132  LYS   B N   1 
ATOM   15174 C  CA  . LYS   B 1 132  ? 69.14500   60.08600  -14.09600 1.000 45.29268  ?  132  LYS   B CA  1 
ATOM   15175 C  C   . LYS   B 1 132  ? 69.79300   59.74800  -15.43300 1.000 46.56591  ?  132  LYS   B C   1 
ATOM   15176 O  O   . LYS   B 1 132  ? 70.37800   58.67000  -15.59400 1.000 48.69415  ?  132  LYS   B O   1 
ATOM   15177 C  CB  . LYS   B 1 132  ? 67.65500   59.74800  -14.12600 1.000 44.20199  ?  132  LYS   B CB  1 
ATOM   15178 C  CG  . LYS   B 1 132  ? 66.93600   60.00400  -12.81700 1.000 48.38430  ?  132  LYS   B CG  1 
ATOM   15179 C  CD  . LYS   B 1 132  ? 65.43400   60.05600  -13.02800 1.000 62.18389  ?  132  LYS   B CD  1 
ATOM   15180 C  CE  . LYS   B 1 132  ? 64.77500   58.73800  -12.66200 1.000 63.34693  ?  132  LYS   B CE  1 
ATOM   15181 N  NZ  . LYS   B 1 132  ? 64.10600   58.80800  -11.33500 1.000 53.23737  ?  132  LYS   B NZ  1 
ATOM   15182 N  N   . ALA   B 1 133  ? 69.70100   60.65900  -16.40200 1.000 49.25108  ?  133  ALA   B N   1 
ATOM   15183 C  CA  . ALA   B 1 133  ? 70.30000   60.41300  -17.70900 1.000 47.75650  ?  133  ALA   B CA  1 
ATOM   15184 C  C   . ALA   B 1 133  ? 71.82000   60.46700  -17.63500 1.000 49.45852  ?  133  ALA   B C   1 
ATOM   15185 O  O   . ALA   B 1 133  ? 72.50800   59.57100  -18.13900 1.000 53.21705  ?  133  ALA   B O   1 
ATOM   15186 C  CB  . ALA   B 1 133  ? 69.77200   61.42600  -18.72100 1.000 40.12574  ?  133  ALA   B CB  1 
ATOM   15187 N  N   . ASN   B 1 134  ? 72.36400   61.51500  -17.01000 1.000 50.85954  ?  134  ASN   B N   1 
ATOM   15188 C  CA  . ASN   B 1 134  ? 73.81100   61.61900  -16.86100 1.000 47.74986  ?  134  ASN   B CA  1 
ATOM   15189 C  C   . ASN   B 1 134  ? 74.38000   60.43900  -16.08500 1.000 50.31756  ?  134  ASN   B C   1 
ATOM   15190 O  O   . ASN   B 1 134  ? 75.50800   60.00800  -16.35000 1.000 62.98831  ?  134  ASN   B O   1 
ATOM   15191 C  CB  . ASN   B 1 134  ? 74.17700   62.93500  -16.17900 1.000 37.81995  ?  134  ASN   B CB  1 
ATOM   15192 C  CG  . ASN   B 1 134  ? 74.09600   64.11700  -17.12200 1.000 53.17286  ?  134  ASN   B CG  1 
ATOM   15193 O  OD1 . ASN   B 1 134  ? 74.40100   63.99900  -18.30800 1.000 59.02926  ?  134  ASN   B OD1 1 
ATOM   15194 N  ND2 . ASN   B 1 134  ? 73.68900   65.26800  -16.59800 1.000 57.25235  ?  134  ASN   B ND2 1 
ATOM   15195 N  N   . GLN   B 1 135  ? 73.61900   59.89800  -15.13300 1.000 35.17787  ?  135  GLN   B N   1 
ATOM   15196 C  CA  . GLN   B 1 135  ? 74.07100   58.70000  -14.43600 1.000 42.71190  ?  135  GLN   B CA  1 
ATOM   15197 C  C   . GLN   B 1 135  ? 73.99400   57.47800  -15.34200 1.000 43.07179  ?  135  GLN   B C   1 
ATOM   15198 O  O   . GLN   B 1 135  ? 74.88900   56.62600  -15.32200 1.000 49.81045  ?  135  GLN   B O   1 
ATOM   15199 C  CB  . GLN   B 1 135  ? 73.24500   58.48400  -13.16800 1.000 44.81174  ?  135  GLN   B CB  1 
ATOM   15200 C  CG  . GLN   B 1 135  ? 73.77800   59.21800  -11.94500 1.000 69.54249  ?  135  GLN   B CG  1 
ATOM   15201 C  CD  . GLN   B 1 135  ? 72.76100   59.29800  -10.81900 1.000 95.70029  ?  135  GLN   B CD  1 
ATOM   15202 O  OE1 . GLN   B 1 135  ? 71.84600   58.47800  -10.73200 1.000 88.87467  ?  135  GLN   B OE1 1 
ATOM   15203 N  NE2 . GLN   B 1 135  ? 72.91700   60.29100  -9.94900  1.000 89.62968  ?  135  GLN   B NE2 1 
ATOM   15204 N  N   . ALA   B 1 136  ? 72.94100   57.38100  -16.15600 1.000 43.76960  ?  136  ALA   B N   1 
ATOM   15205 C  CA  . ALA   B 1 136  ? 72.76500   56.20500  -17.00200 1.000 41.67099  ?  136  ALA   B CA  1 
ATOM   15206 C  C   . ALA   B 1 136  ? 73.82600   56.13800  -18.09300 1.000 46.26250  ?  136  ALA   B C   1 
ATOM   15207 O  O   . ALA   B 1 136  ? 74.35100   55.05800  -18.39000 1.000 47.67799  ?  136  ALA   B O   1 
ATOM   15208 C  CB  . ALA   B 1 136  ? 71.36400   56.20600  -17.61400 1.000 33.37414  ?  136  ALA   B CB  1 
ATOM   15209 N  N   . ILE   B 1 137  ? 74.15300   57.28000  -18.70500 1.000 46.62794  ?  137  ILE   B N   1 
ATOM   15210 C  CA  . ILE   B 1 137  ? 75.19300   57.29700  -19.72500 1.000 49.07123  ?  137  ILE   B CA  1 
ATOM   15211 C  C   . ILE   B 1 137  ? 76.56400   57.02100  -19.12400 1.000 44.53688  ?  137  ILE   B C   1 
ATOM   15212 O  O   . ILE   B 1 137  ? 77.46000   56.54300  -19.82900 1.000 49.02631  ?  137  ILE   B O   1 
ATOM   15213 C  CB  . ILE   B 1 137  ? 75.17700   58.63600  -20.49000 1.000 39.68695  ?  137  ILE   B CB  1 
ATOM   15214 C  CG1 . ILE   B 1 137  ? 75.94100   58.51600  -21.81100 1.000 37.21357  ?  137  ILE   B CG1 1 
ATOM   15215 C  CG2 . ILE   B 1 137  ? 75.75700   59.75400  -19.64000 1.000 43.19017  ?  137  ILE   B CG2 1 
ATOM   15216 C  CD1 . ILE   B 1 137  ? 75.49000   57.36800  -22.68000 1.000 41.19115  ?  137  ILE   B CD1 1 
ATOM   15217 N  N   . GLU   B 1 138  ? 76.74800   57.28800  -17.82800 1.000 42.33405  ?  138  GLU   B N   1 
ATOM   15218 C  CA  . GLU   B 1 138  ? 78.03400   57.02800  -17.19200 1.000 43.17324  ?  138  GLU   B CA  1 
ATOM   15219 C  C   . GLU   B 1 138  ? 78.17700   55.56300  -16.79100 1.000 49.76116  ?  138  GLU   B C   1 
ATOM   15220 O  O   . GLU   B 1 138  ? 79.25500   54.97800  -16.95200 1.000 54.40157  ?  138  GLU   B O   1 
ATOM   15221 C  CB  . GLU   B 1 138  ? 78.21800   57.94400  -15.98200 1.000 34.76776  ?  138  GLU   B CB  1 
ATOM   15222 C  CG  . GLU   B 1 138  ? 78.68200   59.34900  -16.34800 1.000 46.48045  ?  138  GLU   B CG  1 
ATOM   15223 C  CD  . GLU   B 1 138  ? 78.45800   60.34900  -15.23300 1.000 66.16930  ?  138  GLU   B CD  1 
ATOM   15224 O  OE1 . GLU   B 1 138  ? 78.11600   59.91600  -14.11200 1.000 56.98225  ?  138  GLU   B OE1 1 
ATOM   15225 O  OE2 . GLU   B 1 138  ? 78.61700   61.56500  -15.47800 1.000 65.19432  -1 138  GLU   B OE2 1 
ATOM   15226 N  N   . GLU   B 1 139  ? 77.10800   54.95200  -16.27300 1.000 44.84958  ?  139  GLU   B N   1 
ATOM   15227 C  CA  . GLU   B 1 139  ? 77.16400   53.52700  -15.95800 1.000 49.29265  ?  139  GLU   B CA  1 
ATOM   15228 C  C   . GLU   B 1 139  ? 77.29200   52.69100  -17.22600 1.000 55.35159  ?  139  GLU   B C   1 
ATOM   15229 O  O   . GLU   B 1 139  ? 77.98700   51.66800  -17.23600 1.000 52.71395  ?  139  GLU   B O   1 
ATOM   15230 C  CB  . GLU   B 1 139  ? 75.92400   53.10400  -15.16700 1.000 53.34979  ?  139  GLU   B CB  1 
ATOM   15231 C  CG  . GLU   B 1 139  ? 75.60800   53.96100  -13.94600 1.000 66.94744  ?  139  GLU   B CG  1 
ATOM   15232 C  CD  . GLU   B 1 139  ? 76.75200   54.04300  -12.94900 1.000 90.29272  ?  139  GLU   B CD  1 
ATOM   15233 O  OE1 . GLU   B 1 139  ? 77.53100   53.07100  -12.83900 1.000 93.31640  ?  139  GLU   B OE1 1 
ATOM   15234 O  OE2 . GLU   B 1 139  ? 76.87000   55.08500  -12.26800 1.000 85.98310  -1 139  GLU   B OE2 1 
ATOM   15235 N  N   . LEU   B 1 140  ? 76.62700   53.11300  -18.30400 1.000 50.66363  ?  140  LEU   B N   1 
ATOM   15236 C  CA  . LEU   B 1 140  ? 76.68500   52.36400  -19.55400 1.000 46.28817  ?  140  LEU   B CA  1 
ATOM   15237 C  C   . LEU   B 1 140  ? 78.10200   52.34600  -20.11100 1.000 52.50728  ?  140  LEU   B C   1 
ATOM   15238 O  O   . LEU   B 1 140  ? 78.59900   51.29800  -20.53900 1.000 50.36149  ?  140  LEU   B O   1 
ATOM   15239 C  CB  . LEU   B 1 140  ? 75.71000   52.96300  -20.56600 1.000 51.72828  ?  140  LEU   B CB  1 
ATOM   15240 C  CG  . LEU   B 1 140  ? 75.51100   52.18100  -21.86500 1.000 57.61854  ?  140  LEU   B CG  1 
ATOM   15241 C  CD1 . LEU   B 1 140  ? 74.74400   50.89100  -21.60900 1.000 57.35607  ?  140  LEU   B CD1 1 
ATOM   15242 C  CD2 . LEU   B 1 140  ? 74.80200   53.03700  -22.90300 1.000 47.40513  ?  140  LEU   B CD2 1 
ATOM   15243 N  N   . PHE   B 1 141  ? 78.76800   53.50500  -20.11300 1.000 43.02888  ?  141  PHE   B N   1 
ATOM   15244 C  CA  . PHE   B 1 141  ? 80.16400   53.56100  -20.53400 1.000 39.96968  ?  141  PHE   B CA  1 
ATOM   15245 C  C   . PHE   B 1 141  ? 81.01500   52.59600  -19.71700 1.000 47.39347  ?  141  PHE   B C   1 
ATOM   15246 O  O   . PHE   B 1 141  ? 81.79000   51.81000  -20.27300 1.000 51.56213  ?  141  PHE   B O   1 
ATOM   15247 C  CB  . PHE   B 1 141  ? 80.69200   54.99200  -20.40700 1.000 39.19114  ?  141  PHE   B CB  1 
ATOM   15248 C  CG  . PHE   B 1 141  ? 82.10700   55.16600  -20.89300 1.000 55.23410  ?  141  PHE   B CG  1 
ATOM   15249 C  CD1 . PHE   B 1 141  ? 83.18000   54.97200  -20.03600 1.000 50.00831  ?  141  PHE   B CD1 1 
ATOM   15250 C  CD2 . PHE   B 1 141  ? 82.36400   55.53000  -22.20600 1.000 55.61157  ?  141  PHE   B CD2 1 
ATOM   15251 C  CE1 . PHE   B 1 141  ? 84.48200   55.13100  -20.47900 1.000 53.76708  ?  141  PHE   B CE1 1 
ATOM   15252 C  CE2 . PHE   B 1 141  ? 83.66700   55.69200  -22.65600 1.000 56.91029  ?  141  PHE   B CE2 1 
ATOM   15253 C  CZ  . PHE   B 1 141  ? 84.72600   55.49200  -21.79000 1.000 47.59329  ?  141  PHE   B CZ  1 
ATOM   15254 N  N   . ILE   B 1 142  ? 80.87200   52.63600  -18.38900 1.000 45.63499  ?  142  ILE   B N   1 
ATOM   15255 C  CA  . ILE   B 1 142  ? 81.62400   51.73700  -17.51900 1.000 42.36921  ?  142  ILE   B CA  1 
ATOM   15256 C  C   . ILE   B 1 142  ? 81.30100   50.28500  -17.84000 1.000 48.42349  ?  142  ILE   B C   1 
ATOM   15257 O  O   . ILE   B 1 142  ? 82.16500   49.40500  -17.73300 1.000 63.65688  ?  142  ILE   B O   1 
ATOM   15258 C  CB  . ILE   B 1 142  ? 81.33900   52.08200  -16.04000 1.000 40.37460  ?  142  ILE   B CB  1 
ATOM   15259 C  CG1 . ILE   B 1 142  ? 81.94100   53.44300  -15.68400 1.000 44.91539  ?  142  ILE   B CG1 1 
ATOM   15260 C  CG2 . ILE   B 1 142  ? 81.88500   51.01800  -15.10600 1.000 35.39543  ?  142  ILE   B CG2 1 
ATOM   15261 C  CD1 . ILE   B 1 142  ? 81.42000   54.02700  -14.38400 1.000 40.70114  ?  142  ILE   B CD1 1 
ATOM   15262 N  N   . ARG   B 1 143  ? 80.07200   50.01300  -18.27700 1.000 50.74905  ?  143  ARG   B N   1 
ATOM   15263 C  CA  . ARG   B 1 143  ? 79.66400   48.63800  -18.53100 1.000 46.05887  ?  143  ARG   B CA  1 
ATOM   15264 C  C   . ARG   B 1 143  ? 80.17400   48.10700  -19.86600 1.000 44.07032  ?  143  ARG   B C   1 
ATOM   15265 O  O   . ARG   B 1 143  ? 80.37400   46.89500  -20.00100 1.000 57.27353  ?  143  ARG   B O   1 
ATOM   15266 C  CB  . ARG   B 1 143  ? 78.14000   48.53000  -18.47900 1.000 52.70608  ?  143  ARG   B CB  1 
ATOM   15267 C  CG  . ARG   B 1 143  ? 77.62600   47.51100  -17.47600 1.000 61.14155  ?  143  ARG   B CG  1 
ATOM   15268 C  CD  . ARG   B 1 143  ? 76.10500   47.46300  -17.46000 1.000 51.98402  ?  143  ARG   B CD  1 
ATOM   15269 N  NE  . ARG   B 1 143  ? 75.51700   48.77000  -17.19000 1.000 66.35590  ?  143  ARG   B NE  1 
ATOM   15270 C  CZ  . ARG   B 1 143  ? 74.63400   49.37100  -17.97700 1.000 69.66661  ?  143  ARG   B CZ  1 
ATOM   15271 N  NH1 . ARG   B 1 143  ? 74.20800   48.80500  -19.09500 1.000 57.09380  ?  143  ARG   B NH1 1 
ATOM   15272 N  NH2 . ARG   B 1 143  ? 74.16600   50.56700  -17.63100 1.000 64.61913  ?  143  ARG   B NH2 1 
ATOM   15273 N  N   . GLU   B 1 144  ? 80.39200   48.97400  -20.85800 1.000 40.11914  ?  144  GLU   B N   1 
ATOM   15274 C  CA  . GLU   B 1 144  ? 80.67800   48.51700  -22.21200 1.000 54.38965  ?  144  GLU   B CA  1 
ATOM   15275 C  C   . GLU   B 1 144  ? 81.96900   49.06300  -22.80900 1.000 57.01136  ?  144  GLU   B C   1 
ATOM   15276 O  O   . GLU   B 1 144  ? 82.24300   48.79500  -23.98500 1.000 64.96184  ?  144  GLU   B O   1 
ATOM   15277 C  CB  . GLU   B 1 144  ? 79.51400   48.87000  -23.15100 1.000 62.49676  ?  144  GLU   B CB  1 
ATOM   15278 C  CG  . GLU   B 1 144  ? 78.13200   48.55300  -22.59800 1.000 70.44515  ?  144  GLU   B CG  1 
ATOM   15279 C  CD  . GLU   B 1 144  ? 77.77900   47.08100  -22.70400 1.000 76.75133  ?  144  GLU   B CD  1 
ATOM   15280 O  OE1 . GLU   B 1 144  ? 78.44100   46.36300  -23.48400 1.000 67.30773  ?  144  GLU   B OE1 1 
ATOM   15281 O  OE2 . GLU   B 1 144  ? 76.84000   46.64300  -22.00500 1.000 84.77777  -1 144  GLU   B OE2 1 
ATOM   15282 N  N   . TRP   B 1 145  ? 82.76700   49.81700  -22.04900 1.000 55.91922  ?  145  TRP   B N   1 
ATOM   15283 C  CA  . TRP   B 1 145  ? 84.00100   50.36600  -22.60600 1.000 56.61460  ?  145  TRP   B CA  1 
ATOM   15284 C  C   . TRP   B 1 145  ? 84.96300   49.25900  -23.01500 1.000 67.07305  ?  145  TRP   B C   1 
ATOM   15285 O  O   . TRP   B 1 145  ? 85.56800   49.31900  -24.09200 1.000 68.90391  ?  145  TRP   B O   1 
ATOM   15286 C  CB  . TRP   B 1 145  ? 84.66500   51.30700  -21.60100 1.000 55.21147  ?  145  TRP   B CB  1 
ATOM   15287 C  CG  . TRP   B 1 145  ? 86.04400   51.76000  -22.00200 1.000 56.38767  ?  145  TRP   B CG  1 
ATOM   15288 C  CD1 . TRP   B 1 145  ? 87.21500   51.48900  -21.35200 1.000 51.96569  ?  145  TRP   B CD1 1 
ATOM   15289 C  CD2 . TRP   B 1 145  ? 86.39400   52.57100  -23.13300 1.000 46.40019  ?  145  TRP   B CD2 1 
ATOM   15290 N  NE1 . TRP   B 1 145  ? 88.27000   52.07400  -22.01000 1.000 52.15613  ?  145  TRP   B NE1 1 
ATOM   15291 C  CE2 . TRP   B 1 145  ? 87.79400   52.74500  -23.10500 1.000 59.72346  ?  145  TRP   B CE2 1 
ATOM   15292 C  CE3 . TRP   B 1 145  ? 85.66200   53.16300  -24.16600 1.000 44.14736  ?  145  TRP   B CE3 1 
ATOM   15293 C  CZ2 . TRP   B 1 145  ? 88.47400   53.49000  -24.06900 1.000 48.07125  ?  145  TRP   B CZ2 1 
ATOM   15294 C  CZ3 . TRP   B 1 145  ? 86.34200   53.90000  -25.12500 1.000 58.74870  ?  145  TRP   B CZ3 1 
ATOM   15295 C  CH2 . TRP   B 1 145  ? 87.73300   54.05400  -25.07000 1.000 47.72346  ?  145  TRP   B CH2 1 
ATOM   15296 N  N   . GLU   B 1 146  ? 85.11100   48.23600  -22.16900 1.000 64.10968  ?  146  GLU   B N   1 
ATOM   15297 C  CA  . GLU   B 1 146  ? 86.02000   47.13800  -22.47800 1.000 68.03402  ?  146  GLU   B CA  1 
ATOM   15298 C  C   . GLU   B 1 146  ? 85.60500   46.42800  -23.76100 1.000 75.24778  ?  146  GLU   B C   1 
ATOM   15299 O  O   . GLU   B 1 146  ? 86.43500   46.17500  -24.64100 1.000 82.83535  ?  146  GLU   B O   1 
ATOM   15300 C  CB  . GLU   B 1 146  ? 86.06900   46.15500  -21.30800 1.000 82.19046  ?  146  GLU   B CB  1 
ATOM   15301 C  CG  . GLU   B 1 146  ? 86.30800   46.81300  -19.95900 1.000 96.79921  ?  146  GLU   B CG  1 
ATOM   15302 C  CD  . GLU   B 1 146  ? 87.51300   46.24300  -19.23600 1.000 91.97138  ?  146  GLU   B CD  1 
ATOM   15303 O  OE1 . GLU   B 1 146  ? 88.63400   46.34400  -19.77700 1.000 94.67824  ?  146  GLU   B OE1 1 
ATOM   15304 O  OE2 . GLU   B 1 146  ? 87.34000   45.69200  -18.12800 1.000 85.94355  -1 146  GLU   B OE2 1 
ATOM   15305 N  N   . ASN   B 1 147  ? 84.31700   46.10600  -23.88800 1.000 70.39151  ?  147  ASN   B N   1 
ATOM   15306 C  CA  . ASN   B 1 147  ? 83.84000   45.46500  -25.10700 1.000 64.43329  ?  147  ASN   B CA  1 
ATOM   15307 C  C   . ASN   B 1 147  ? 83.98500   46.36800  -26.32200 1.000 63.58160  ?  147  ASN   B C   1 
ATOM   15308 O  O   . ASN   B 1 147  ? 83.91800   45.87900  -27.45400 1.000 70.96324  ?  147  ASN   B O   1 
ATOM   15309 C  CB  . ASN   B 1 147  ? 82.38200   45.04200  -24.94100 1.000 57.45705  ?  147  ASN   B CB  1 
ATOM   15310 C  CG  . ASN   B 1 147  ? 82.13000   44.34100  -23.62400 1.000 77.29291  ?  147  ASN   B CG  1 
ATOM   15311 O  OD1 . ASN   B 1 147  ? 82.07300   44.97700  -22.57100 1.000 81.97848  ?  147  ASN   B OD1 1 
ATOM   15312 N  ND2 . ASN   B 1 147  ? 81.97800   43.02300  -23.67400 1.000 73.62857  ?  147  ASN   B ND2 1 
ATOM   15313 N  N   . ILE   B 1 148  ? 84.18900   47.66900  -26.11600 1.000 55.83175  ?  148  ILE   B N   1 
ATOM   15314 C  CA  . ILE   B 1 148  ? 84.35500   48.58400  -27.23900 1.000 64.15633  ?  148  ILE   B CA  1 
ATOM   15315 C  C   . ILE   B 1 148  ? 85.80000   48.59200  -27.72100 1.000 66.24404  ?  148  ILE   B C   1 
ATOM   15316 O  O   . ILE   B 1 148  ? 86.06700   48.48700  -28.92300 1.000 74.15555  ?  148  ILE   B O   1 
ATOM   15317 C  CB  . ILE   B 1 148  ? 83.87500   49.99600  -26.85400 1.000 59.72806  ?  148  ILE   B CB  1 
ATOM   15318 C  CG1 . ILE   B 1 148  ? 82.34600   50.06600  -26.89300 1.000 52.97668  ?  148  ILE   B CG1 1 
ATOM   15319 C  CG2 . ILE   B 1 148  ? 84.48600   51.04200  -27.77700 1.000 55.68973  ?  148  ILE   B CG2 1 
ATOM   15320 C  CD1 . ILE   B 1 148  ? 81.77900   51.35600  -26.34800 1.000 51.92359  ?  148  ILE   B CD1 1 
ATOM   15321 N  N   . VAL   B 1 149  ? 86.75700   48.71300  -26.79500 1.000 74.21377  ?  149  VAL   B N   1 
ATOM   15322 C  CA  . VAL   B 1 149  ? 88.16200   48.76400  -27.19200 1.000 76.26645  ?  149  VAL   B CA  1 
ATOM   15323 C  C   . VAL   B 1 149  ? 88.61600   47.41700  -27.73900 1.000 69.27875  ?  149  VAL   B C   1 
ATOM   15324 O  O   . VAL   B 1 149  ? 89.44100   47.35300  -28.65700 1.000 64.48340  ?  149  VAL   B O   1 
ATOM   15325 C  CB  . VAL   B 1 149  ? 89.04500   49.21800  -26.01700 1.000 66.51802  ?  149  VAL   B CB  1 
ATOM   15326 C  CG1 . VAL   B 1 149  ? 89.03300   50.72500  -25.90700 1.000 65.61874  ?  149  VAL   B CG1 1 
ATOM   15327 C  CG2 . VAL   B 1 149  ? 88.58800   48.57100  -24.72100 1.000 58.40571  ?  149  VAL   B CG2 1 
ATOM   15328 N  N   . HIS   B 1 150  ? 88.09500   46.32500  -27.18800 1.000 75.01158  ?  150  HIS   B N   1 
ATOM   15329 C  CA  . HIS   B 1 150  ? 88.44100   44.99200  -27.66100 1.000 74.51336  ?  150  HIS   B CA  1 
ATOM   15330 C  C   . HIS   B 1 150  ? 87.71800   44.61400  -28.94900 1.000 79.87795  ?  150  HIS   B C   1 
ATOM   15331 O  O   . HIS   B 1 150  ? 87.84500   43.47000  -29.39700 1.000 100.25094 ?  150  HIS   B O   1 
ATOM   15332 C  CB  . HIS   B 1 150  ? 88.15100   43.95500  -26.57100 1.000 81.93342  ?  150  HIS   B CB  1 
ATOM   15333 C  CG  . HIS   B 1 150  ? 88.93700   44.16600  -25.31400 1.000 87.81010  ?  150  HIS   B CG  1 
ATOM   15334 N  ND1 . HIS   B 1 150  ? 88.42800   43.89700  -24.06200 1.000 89.71662  ?  150  HIS   B ND1 1 
ATOM   15335 C  CD2 . HIS   B 1 150  ? 90.19600   44.62400  -25.11700 1.000 72.04025  ?  150  HIS   B CD2 1 
ATOM   15336 C  CE1 . HIS   B 1 150  ? 89.33900   44.17700  -23.14800 1.000 82.08323  ?  150  HIS   B CE1 1 
ATOM   15337 N  NE2 . HIS   B 1 150  ? 90.42200   44.62100  -23.76200 1.000 81.80238  ?  150  HIS   B NE2 1 
ATOM   15338 N  N   . GLY   B 1 151  ? 86.97300   45.54000  -29.54600 1.000 73.98914  ?  151  GLY   B N   1 
ATOM   15339 C  CA  . GLY   B 1 151  ? 86.32200   45.28500  -30.82400 1.000 80.17050  ?  151  GLY   B CA  1 
ATOM   15340 C  C   . GLY   B 1 151  ? 85.28100   44.18800  -30.78900 1.000 77.15470  ?  151  GLY   B C   1 
ATOM   15341 O  O   . GLY   B 1 151  ? 85.20400   43.37800  -31.72100 1.000 101.78220 ?  151  GLY   B O   1 
ATOM   15342 N  N   . ARG   B 1 152  ? 84.47100   44.14500  -29.73400 1.000 73.69254  ?  152  ARG   B N   1 
ATOM   15343 C  CA  . ARG   B 1 152  ? 83.43500   43.13200  -29.58400 1.000 86.59396  ?  152  ARG   B CA  1 
ATOM   15344 C  C   . ARG   B 1 152  ? 82.03600   43.66300  -29.86500 1.000 76.42840  ?  152  ARG   B C   1 
ATOM   15345 O  O   . ARG   B 1 152  ? 81.06400   42.91400  -29.71700 1.000 84.64082  ?  152  ARG   B O   1 
ATOM   15346 C  CB  . ARG   B 1 152  ? 83.48100   42.53900  -28.17100 1.000 83.30002  ?  152  ARG   B CB  1 
ATOM   15347 C  CG  . ARG   B 1 152  ? 84.28900   41.25900  -28.05500 1.000 84.17216  ?  152  ARG   B CG  1 
ATOM   15348 C  CD  . ARG   B 1 152  ? 84.11900   40.63600  -26.68300 1.000 63.22746  ?  152  ARG   B CD  1 
ATOM   15349 N  NE  . ARG   B 1 152  ? 84.47400   41.57000  -25.62100 1.000 74.56435  ?  152  ARG   B NE  1 
ATOM   15350 C  CZ  . ARG   B 1 152  ? 85.62700   41.55900  -24.96600 1.000 86.94103  ?  152  ARG   B CZ  1 
ATOM   15351 N  NH1 . ARG   B 1 152  ? 86.57000   40.67200  -25.24100 1.000 95.56885  ?  152  ARG   B NH1 1 
ATOM   15352 N  NH2 . ARG   B 1 152  ? 85.83900   42.46100  -24.01300 1.000 80.71390  ?  152  ARG   B NH2 1 
ATOM   15353 N  N   . ILE   B 1 153  ? 81.90600   44.92500  -30.26600 1.000 61.46724  ?  153  ILE   B N   1 
ATOM   15354 C  CA  . ILE   B 1 153  ? 80.61100   45.56700  -30.46300 1.000 69.66531  ?  153  ILE   B CA  1 
ATOM   15355 C  C   . ILE   B 1 153  ? 80.48900   45.94800  -31.93100 1.000 70.84584  ?  153  ILE   B C   1 
ATOM   15356 O  O   . ILE   B 1 153  ? 81.34100   46.67000  -32.46500 1.000 69.99723  ?  153  ILE   B O   1 
ATOM   15357 C  CB  . ILE   B 1 153  ? 80.44000   46.79800  -29.55800 1.000 66.81899  ?  153  ILE   B CB  1 
ATOM   15358 C  CG1 . ILE   B 1 153  ? 80.18500   46.37200  -28.10800 1.000 60.55078  ?  153  ILE   B CG1 1 
ATOM   15359 C  CG2 . ILE   B 1 153  ? 79.31500   47.69100  -30.06000 1.000 52.98715  ?  153  ILE   B CG2 1 
ATOM   15360 C  CD1 . ILE   B 1 153  ? 79.30000   45.14900  -27.96700 1.000 83.67911  ?  153  ILE   B CD1 1 
ATOM   15361 N  N   . ALA   B 1 154  ? 79.43200   45.46400  -32.58200 1.000 68.45615  ?  154  ALA   B N   1 
ATOM   15362 C  CA  . ALA   B 1 154  ? 79.20100   45.76300  -33.98800 1.000 69.14571  ?  154  ALA   B CA  1 
ATOM   15363 C  C   . ALA   B 1 154  ? 78.43300   47.07100  -34.11300 1.000 71.98925  ?  154  ALA   B C   1 
ATOM   15364 O  O   . ALA   B 1 154  ? 77.29400   47.15400  -33.63400 1.000 74.48220  ?  154  ALA   B O   1 
ATOM   15365 C  CB  . ALA   B 1 154  ? 78.42700   44.64100  -34.65600 1.000 76.77946  ?  154  ALA   B CB  1 
ATOM   15366 N  N   . PRO   B 1 155  ? 79.00500   48.10700  -34.72500 1.000 60.51583  ?  155  PRO   B N   1 
ATOM   15367 C  CA  . PRO   B 1 155  ? 78.26000   49.35900  -34.89900 1.000 68.67449  ?  155  PRO   B CA  1 
ATOM   15368 C  C   . PRO   B 1 155  ? 77.07400   49.16600  -35.83100 1.000 75.38318  ?  155  PRO   B C   1 
ATOM   15369 O  O   . PRO   B 1 155  ? 77.16000   48.46400  -36.84100 1.000 87.85042  ?  155  PRO   B O   1 
ATOM   15370 C  CB  . PRO   B 1 155  ? 79.29700   50.31300  -35.50700 1.000 54.15851  ?  155  PRO   B CB  1 
ATOM   15371 C  CG  . PRO   B 1 155  ? 80.62100   49.68900  -35.22200 1.000 56.02941  ?  155  PRO   B CG  1 
ATOM   15372 C  CD  . PRO   B 1 155  ? 80.38600   48.21200  -35.22200 1.000 54.27740  ?  155  PRO   B CD  1 
ATOM   15373 N  N   . TYR   B 1 156  ? 75.95500   49.79600  -35.47900 1.000 69.45794  ?  156  TYR   B N   1 
ATOM   15374 C  CA  . TYR   B 1 156  ? 74.75500   49.76300  -36.30100 1.000 51.29858  ?  156  TYR   B CA  1 
ATOM   15375 C  C   . TYR   B 1 156  ? 74.24600   51.18100  -36.51500 1.000 63.59518  ?  156  TYR   B C   1 
ATOM   15376 O  O   . TYR   B 1 156  ? 74.31800   52.01900  -35.61200 1.000 79.62624  ?  156  TYR   B O   1 
ATOM   15377 C  CB  . TYR   B 1 156  ? 73.65900   48.88000  -35.67600 1.000 69.03095  ?  156  TYR   B CB  1 
ATOM   15378 C  CG  . TYR   B 1 156  ? 73.26300   49.21100  -34.24900 1.000 75.97573  ?  156  TYR   B CG  1 
ATOM   15379 C  CD1 . TYR   B 1 156  ? 74.04100   48.79800  -33.17300 1.000 80.16540  ?  156  TYR   B CD1 1 
ATOM   15380 C  CD2 . TYR   B 1 156  ? 72.08900   49.90300  -33.97700 1.000 59.23612  ?  156  TYR   B CD2 1 
ATOM   15381 C  CE1 . TYR   B 1 156  ? 73.67300   49.08600  -31.86900 1.000 76.90594  ?  156  TYR   B CE1 1 
ATOM   15382 C  CE2 . TYR   B 1 156  ? 71.71300   50.19400  -32.67700 1.000 57.69999  ?  156  TYR   B CE2 1 
ATOM   15383 C  CZ  . TYR   B 1 156  ? 72.50800   49.78300  -31.62800 1.000 77.12087  ?  156  TYR   B CZ  1 
ATOM   15384 O  OH  . TYR   B 1 156  ? 72.13700   50.07000  -30.33300 1.000 82.51031  ?  156  TYR   B OH  1 
ATOM   15385 N  N   . ARG   B 1 157  ? 73.74000   51.44100  -37.71800 1.000 71.10811  ?  157  ARG   B N   1 
ATOM   15386 C  CA  . ARG   B 1 157  ? 73.30600   52.78200  -38.08600 1.000 76.50329  ?  157  ARG   B CA  1 
ATOM   15387 C  C   . ARG   B 1 157  ? 72.02500   53.16800  -37.35400 1.000 73.77958  ?  157  ARG   B C   1 
ATOM   15388 O  O   . ARG   B 1 157  ? 71.21900   52.31700  -36.96700 1.000 58.79935  ?  157  ARG   B O   1 
ATOM   15389 C  CB  . ARG   B 1 157  ? 73.08500   52.87600  -39.59600 1.000 72.07363  ?  157  ARG   B CB  1 
ATOM   15390 N  N   . GLN   B 1 158  ? 71.84500   54.47500  -37.17400 1.000 75.24792  ?  158  GLN   B N   1 
ATOM   15391 C  CA  . GLN   B 1 158  ? 70.65500   54.98200  -36.50400 1.000 67.60336  ?  158  GLN   B CA  1 
ATOM   15392 C  C   . GLN   B 1 158  ? 69.41400   54.69300  -37.33700 1.000 75.64687  ?  158  GLN   B C   1 
ATOM   15393 O  O   . GLN   B 1 158  ? 69.43700   54.77800  -38.56800 1.000 88.36442  ?  158  GLN   B O   1 
ATOM   15394 C  CB  . GLN   B 1 158  ? 70.78000   56.48800  -36.26500 1.000 66.78209  ?  158  GLN   B CB  1 
ATOM   15395 C  CG  . GLN   B 1 158  ? 71.61400   56.88300  -35.05700 1.000 65.77756  ?  158  GLN   B CG  1 
ATOM   15396 C  CD  . GLN   B 1 158  ? 71.93400   58.36800  -35.03800 1.000 78.15031  ?  158  GLN   B CD  1 
ATOM   15397 O  OE1 . GLN   B 1 158  ? 71.09100   59.19900  -35.37100 1.000 74.02365  ?  158  GLN   B OE1 1 
ATOM   15398 N  NE2 . GLN   B 1 158  ? 73.16200   58.70600  -34.65900 1.000 77.77991  ?  158  GLN   B NE2 1 
ATOM   15399 N  N   . THR   B 1 159  ? 68.32600   54.34400  -36.65600 1.000 77.84457  ?  159  THR   B N   1 
ATOM   15400 C  CA  . THR   B 1 159  ? 67.05000   54.18000  -37.33600 1.000 72.72353  ?  159  THR   B CA  1 
ATOM   15401 C  C   . THR   B 1 159  ? 66.59500   55.51600  -37.91200 1.000 77.90742  ?  159  THR   B C   1 
ATOM   15402 O  O   . THR   B 1 159  ? 66.94000   56.58600  -37.40400 1.000 86.14557  ?  159  THR   B O   1 
ATOM   15403 C  CB  . THR   B 1 159  ? 65.99500   53.63000  -36.37600 1.000 73.77308  ?  159  THR   B CB  1 
ATOM   15404 O  OG1 . THR   B 1 159  ? 66.61600   52.72600  -35.45300 1.000 99.43567  ?  159  THR   B OG1 1 
ATOM   15405 C  CG2 . THR   B 1 159  ? 64.90700   52.89000  -37.14300 1.000 72.28280  ?  159  THR   B CG2 1 
ATOM   15406 N  N   . ALA   B 1 160  ? 65.81800   55.44600  -38.98900 1.000 74.89497  ?  160  ALA   B N   1 
ATOM   15407 C  CA  . ALA   B 1 160  ? 65.41200   56.65500  -39.69000 1.000 87.64701  ?  160  ALA   B CA  1 
ATOM   15408 C  C   . ALA   B 1 160  ? 64.51400   57.52100  -38.81200 1.000 84.12180  ?  160  ALA   B C   1 
ATOM   15409 O  O   . ALA   B 1 160  ? 63.73500   57.02400  -37.99300 1.000 63.71748  ?  160  ALA   B O   1 
ATOM   15410 C  CB  . ALA   B 1 160  ? 64.69100   56.29500  -40.98900 1.000 94.09959  ?  160  ALA   B CB  1 
ATOM   15411 N  N   . GLY   B 1 161  ? 64.64000   58.83600  -38.98400 1.000 76.83463  ?  161  GLY   B N   1 
ATOM   15412 C  CA  . GLY   B 1 161  ? 63.80500   59.78000  -38.26800 1.000 73.41949  ?  161  GLY   B CA  1 
ATOM   15413 C  C   . GLY   B 1 161  ? 64.54700   60.58200  -37.21800 1.000 70.69543  ?  161  GLY   B C   1 
ATOM   15414 O  O   . GLY   B 1 161  ? 65.72500   60.91000  -37.38900 1.000 77.43249  ?  161  GLY   B O   1 
ATOM   15415 N  N   . GLY   B 1 162  ? 63.85500   60.91400  -36.13400 1.000 75.49920  ?  162  GLY   B N   1 
ATOM   15416 C  CA  . GLY   B 1 162  ? 64.44800   61.58900  -34.99800 1.000 60.75075  ?  162  GLY   B CA  1 
ATOM   15417 C  C   . GLY   B 1 162  ? 64.29200   63.10100  -35.05700 1.000 57.45651  ?  162  GLY   B C   1 
ATOM   15418 O  O   . GLY   B 1 162  ? 63.86000   63.68500  -36.05300 1.000 78.21700  ?  162  GLY   B O   1 
ATOM   15419 N  N   . THR   B 1 163  ? 64.66200   63.73600  -33.94600 1.000 70.38279  ?  163  THR   B N   1 
ATOM   15420 C  CA  . THR   B 1 163  ? 64.61400   65.18400  -33.79900 1.000 63.44843  ?  163  THR   B CA  1 
ATOM   15421 C  C   . THR   B 1 163  ? 66.00500   65.71700  -33.48800 1.000 63.21683  ?  163  THR   B C   1 
ATOM   15422 O  O   . THR   B 1 163  ? 66.85000   65.00900  -32.93500 1.000 67.52194  ?  163  THR   B O   1 
ATOM   15423 C  CB  . THR   B 1 163  ? 63.64400   65.60800  -32.68500 1.000 55.57008  ?  163  THR   B CB  1 
ATOM   15424 O  OG1 . THR   B 1 163  ? 64.06800   65.04400  -31.43800 1.000 63.30688  ?  163  THR   B OG1 1 
ATOM   15425 C  CG2 . THR   B 1 163  ? 62.23700   65.12800  -32.99300 1.000 54.28759  ?  163  THR   B CG2 1 
ATOM   15426 N  N   . LEU   B 1 164  ? 66.23400   66.97800  -33.84500 1.000 55.50315  ?  164  LEU   B N   1 
ATOM   15427 C  CA  . LEU   B 1 164  ? 67.50300   67.64200  -33.58400 1.000 44.29048  ?  164  LEU   B CA  1 
ATOM   15428 C  C   . LEU   B 1 164  ? 67.22300   69.06900  -33.14100 1.000 50.43077  ?  164  LEU   B C   1 
ATOM   15429 O  O   . LEU   B 1 164  ? 66.37600   69.75000  -33.72400 1.000 56.18957  ?  164  LEU   B O   1 
ATOM   15430 C  CB  . LEU   B 1 164  ? 68.41200   67.61600  -34.82300 1.000 48.07674  ?  164  LEU   B CB  1 
ATOM   15431 C  CG  . LEU   B 1 164  ? 69.60200   68.57600  -34.87600 1.000 56.47688  ?  164  LEU   B CG  1 
ATOM   15432 C  CD1 . LEU   B 1 164  ? 70.78200   67.92800  -35.56000 1.000 69.57334  ?  164  LEU   B CD1 1 
ATOM   15433 C  CD2 . LEU   B 1 164  ? 69.20400   69.81000  -35.65200 1.000 57.26948  ?  164  LEU   B CD2 1 
ATOM   15434 N  N   . HIS   B 1 165  ? 67.92900   69.51200  -32.10200 1.000 55.79870  ?  165  HIS   B N   1 
ATOM   15435 C  CA  . HIS   B 1 165  ? 67.69700   70.82000  -31.50900 1.000 51.46911  ?  165  HIS   B CA  1 
ATOM   15436 C  C   . HIS   B 1 165  ? 69.01300   71.57000  -31.35400 1.000 39.54587  ?  165  HIS   B C   1 
ATOM   15437 O  O   . HIS   B 1 165  ? 70.09800   70.98400  -31.37700 1.000 44.27542  ?  165  HIS   B O   1 
ATOM   15438 C  CB  . HIS   B 1 165  ? 66.99900   70.70500  -30.14800 1.000 42.58074  ?  165  HIS   B CB  1 
ATOM   15439 C  CG  . HIS   B 1 165  ? 65.57000   70.27100  -30.23900 1.000 41.82851  ?  165  HIS   B CG  1 
ATOM   15440 N  ND1 . HIS   B 1 165  ? 65.17900   68.95900  -30.07900 1.000 44.99689  ?  165  HIS   B ND1 1 
ATOM   15441 C  CD2 . HIS   B 1 165  ? 64.43700   70.97600  -30.47200 1.000 40.25563  ?  165  HIS   B CD2 1 
ATOM   15442 C  CE1 . HIS   B 1 165  ? 63.86700   68.87400  -30.20800 1.000 61.49835  ?  165  HIS   B CE1 1 
ATOM   15443 N  NE2 . HIS   B 1 165  ? 63.39300   70.08400  -30.44700 1.000 54.49481  ?  165  HIS   B NE2 1 
ATOM   15444 N  N   . PHE   B 1 166  ? 68.90000   72.88400  -31.18800 1.000 42.53758  ?  166  PHE   B N   1 
ATOM   15445 C  CA  . PHE   B 1 166  ? 70.04900   73.77400  -31.14200 1.000 46.27258  ?  166  PHE   B CA  1 
ATOM   15446 C  C   . PHE   B 1 166  ? 70.14800   74.46500  -29.79100 1.000 43.50900  ?  166  PHE   B C   1 
ATOM   15447 O  O   . PHE   B 1 166  ? 69.26900   74.36000  -28.93300 1.000 48.21861  ?  166  PHE   B O   1 
ATOM   15448 C  CB  . PHE   B 1 166  ? 69.98000   74.84800  -32.23600 1.000 51.95246  ?  166  PHE   B CB  1 
ATOM   15449 C  CG  . PHE   B 1 166  ? 70.25500   74.33400  -33.61100 1.000 68.72122  ?  166  PHE   B CG  1 
ATOM   15450 C  CD1 . PHE   B 1 166  ? 69.35100   73.50500  -34.24900 1.000 66.75098  ?  166  PHE   B CD1 1 
ATOM   15451 C  CD2 . PHE   B 1 166  ? 71.41000   74.70600  -34.27900 1.000 72.64771  ?  166  PHE   B CD2 1 
ATOM   15452 C  CE1 . PHE   B 1 166  ? 69.60400   73.04100  -35.51600 1.000 58.06255  ?  166  PHE   B CE1 1 
ATOM   15453 C  CE2 . PHE   B 1 166  ? 71.67200   74.23800  -35.54100 1.000 77.75367  ?  166  PHE   B CE2 1 
ATOM   15454 C  CZ  . PHE   B 1 166  ? 70.76300   73.40700  -36.16600 1.000 88.55625  ?  166  PHE   B CZ  1 
ATOM   15455 N  N   . LYS   B 1 167  ? 71.25400   75.18300  -29.62700 1.000 37.35068  ?  167  LYS   B N   1 
ATOM   15456 C  CA  . LYS   B 1 167  ? 71.37100   76.15800  -28.55800 1.000 36.90914  ?  167  LYS   B CA  1 
ATOM   15457 C  C   . LYS   B 1 167  ? 70.29200   77.22500  -28.71400 1.000 51.87473  ?  167  LYS   B C   1 
ATOM   15458 O  O   . LYS   B 1 167  ? 69.78300   77.46500  -29.81300 1.000 74.11125  ?  167  LYS   B O   1 
ATOM   15459 C  CB  . LYS   B 1 167  ? 72.76200   76.78900  -28.59300 1.000 53.04377  ?  167  LYS   B CB  1 
ATOM   15460 C  CG  . LYS   B 1 167  ? 73.25600   77.37100  -27.28600 1.000 66.78847  ?  167  LYS   B CG  1 
ATOM   15461 C  CD  . LYS   B 1 167  ? 74.61900   78.01100  -27.50000 1.000 55.72975  ?  167  LYS   B CD  1 
ATOM   15462 C  CE  . LYS   B 1 167  ? 75.14200   78.67000  -26.23700 1.000 70.07382  ?  167  LYS   B CE  1 
ATOM   15463 N  NZ  . LYS   B 1 167  ? 76.31400   79.54500  -26.52700 1.000 67.06442  ?  167  LYS   B NZ  1 
ATOM   15464 N  N   . ALA   B 1 168  ? 69.92100   77.84500  -27.59000 1.000 55.73751  ?  168  ALA   B N   1 
ATOM   15465 C  CA  . ALA   B 1 168  ? 68.95100   78.93800  -27.54100 1.000 50.33965  ?  168  ALA   B CA  1 
ATOM   15466 C  C   . ALA   B 1 168  ? 67.53100   78.49700  -27.88200 1.000 39.88463  ?  168  ALA   B C   1 
ATOM   15467 O  O   . ALA   B 1 168  ? 66.59200   79.29200  -27.76600 1.000 72.49956  ?  168  ALA   B O   1 
ATOM   15468 C  CB  . ALA   B 1 168  ? 69.37300   80.08500  -28.46600 1.000 47.77888  ?  168  ALA   B CB  1 
ATOM   15469 N  N   . ASP   B 1 169  ? 67.35000   77.24200  -28.29400 1.000 34.98929  ?  169  ASP   B N   1 
ATOM   15470 C  CA  . ASP   B 1 169  ? 66.00400   76.72700  -28.52300 1.000 43.55499  ?  169  ASP   B CA  1 
ATOM   15471 C  C   . ASP   B 1 169  ? 65.21800   76.55100  -27.23200 1.000 46.00482  ?  169  ASP   B C   1 
ATOM   15472 O  O   . ASP   B 1 169  ? 64.01200   76.29100  -27.29200 1.000 48.84470  ?  169  ASP   B O   1 
ATOM   15473 C  CB  . ASP   B 1 169  ? 66.06100   75.39000  -29.26100 1.000 44.05905  ?  169  ASP   B CB  1 
ATOM   15474 C  CG  . ASP   B 1 169  ? 66.36000   75.54900  -30.73600 1.000 47.65043  ?  169  ASP   B CG  1 
ATOM   15475 O  OD1 . ASP   B 1 169  ? 66.54000   76.69900  -31.19400 1.000 47.68698  ?  169  ASP   B OD1 1 
ATOM   15476 O  OD2 . ASP   B 1 169  ? 66.41400   74.51600  -31.43600 1.000 45.17188  -1 169  ASP   B OD2 1 
ATOM   15477 N  N   . ARG   B 1 170  ? 65.86600   76.68300  -26.07800 1.000 54.73201  ?  170  ARG   B N   1 
ATOM   15478 C  CA  . ARG   B 1 170  ? 65.21400   76.50500  -24.79400 1.000 45.06645  ?  170  ARG   B CA  1 
ATOM   15479 C  C   . ARG   B 1 170  ? 65.03300   77.82000  -24.04300 1.000 42.12352  ?  170  ARG   B C   1 
ATOM   15480 O  O   . ARG   B 1 170  ? 64.32100   77.84900  -23.03200 1.000 60.36777  ?  170  ARG   B O   1 
ATOM   15481 C  CB  . ARG   B 1 170  ? 66.02500   75.49900  -23.95200 1.000 62.00469  ?  170  ARG   B CB  1 
ATOM   15482 C  CG  . ARG   B 1 170  ? 65.56300   75.30000  -22.53200 1.000 67.33340  ?  170  ARG   B CG  1 
ATOM   15483 C  CD  . ARG   B 1 170  ? 66.70100   74.84100  -21.65000 1.000 75.78931  ?  170  ARG   B CD  1 
ATOM   15484 N  NE  . ARG   B 1 170  ? 66.22200   74.13300  -20.47300 1.000 52.67744  ?  170  ARG   B NE  1 
ATOM   15485 C  CZ  . ARG   B 1 170  ? 66.78300   73.04000  -19.97800 1.000 64.02932  ?  170  ARG   B CZ  1 
ATOM   15486 N  NH1 . ARG   B 1 170  ? 67.81200   72.45400  -20.57400 1.000 59.40867  ?  170  ARG   B NH1 1 
ATOM   15487 N  NH2 . ARG   B 1 170  ? 66.32200   72.54100  -18.83800 1.000 62.27005  ?  170  ARG   B NH2 1 
ATOM   15488 N  N   . ASP   B 1 171  ? 65.59800   78.92300  -24.54700 1.000 44.41739  ?  171  ASP   B N   1 
ATOM   15489 C  CA  . ASP   B 1 171  ? 65.54700   80.21200  -23.85600 1.000 47.14846  ?  171  ASP   B CA  1 
ATOM   15490 C  C   . ASP   B 1 171  ? 64.13000   80.65600  -23.50100 1.000 44.92446  ?  171  ASP   B C   1 
ATOM   15491 O  O   . ASP   B 1 171  ? 63.97300   81.56500  -22.67800 1.000 50.87259  ?  171  ASP   B O   1 
ATOM   15492 C  CB  . ASP   B 1 171  ? 66.23300   81.28200  -24.71000 1.000 42.05691  ?  171  ASP   B CB  1 
ATOM   15493 C  CG  . ASP   B 1 171  ? 67.72800   81.06200  -24.82000 1.000 67.97113  ?  171  ASP   B CG  1 
ATOM   15494 O  OD1 . ASP   B 1 171  ? 68.23400   80.10100  -24.20000 1.000 61.15851  ?  171  ASP   B OD1 1 
ATOM   15495 O  OD2 . ASP   B 1 171  ? 68.39600   81.84200  -25.53100 1.000 74.60339  -1 171  ASP   B OD2 1 
ATOM   15496 N  N   . PHE   B 1 172  ? 63.10400   80.03600  -24.08300 1.000 54.11060  ?  172  PHE   B N   1 
ATOM   15497 C  CA  . PHE   B 1 172  ? 61.72100   80.32300  -23.72700 1.000 49.69917  ?  172  PHE   B CA  1 
ATOM   15498 C  C   . PHE   B 1 172  ? 61.24700   79.48500  -22.54700 1.000 51.40186  ?  172  PHE   B C   1 
ATOM   15499 O  O   . PHE   B 1 172  ? 60.39600   79.93800  -21.77100 1.000 54.60103  ?  172  PHE   B O   1 
ATOM   15500 C  CB  . PHE   B 1 172  ? 60.81900   80.08900  -24.94400 1.000 46.19294  ?  172  PHE   B CB  1 
ATOM   15501 C  CG  . PHE   B 1 172  ? 59.38500   80.49000  -24.73400 1.000 52.45255  ?  172  PHE   B CG  1 
ATOM   15502 C  CD1 . PHE   B 1 172  ? 59.06300   81.74900  -24.25300 1.000 52.83695  ?  172  PHE   B CD1 1 
ATOM   15503 C  CD2 . PHE   B 1 172  ? 58.35700   79.61100  -25.03500 1.000 42.44382  ?  172  PHE   B CD2 1 
ATOM   15504 C  CE1 . PHE   B 1 172  ? 57.74300   82.12000  -24.06600 1.000 43.17917  ?  172  PHE   B CE1 1 
ATOM   15505 C  CE2 . PHE   B 1 172  ? 57.03600   79.97400  -24.84900 1.000 40.84447  ?  172  PHE   B CE2 1 
ATOM   15506 C  CZ  . PHE   B 1 172  ? 56.72900   81.23100  -24.36400 1.000 47.89710  ?  172  PHE   B CZ  1 
ATOM   15507 N  N   . TYR   B 1 173  ? 61.79800   78.28500  -22.38100 1.000 42.22197  ?  173  TYR   B N   1 
ATOM   15508 C  CA  . TYR   B 1 173  ? 61.43200   77.37900  -21.29700 1.000 36.47317  ?  173  TYR   B CA  1 
ATOM   15509 C  C   . TYR   B 1 173  ? 62.46700   77.38700  -20.18200 1.000 45.63105  ?  173  TYR   B C   1 
ATOM   15510 O  O   . TYR   B 1 173  ? 62.81500   76.33900  -19.62900 1.000 53.22120  ?  173  TYR   B O   1 
ATOM   15511 C  CB  . TYR   B 1 173  ? 61.24300   75.96900  -21.84100 1.000 41.40896  ?  173  TYR   B CB  1 
ATOM   15512 C  CG  . TYR   B 1 173  ? 60.55100   75.91200  -23.18400 1.000 49.16284  ?  173  TYR   B CG  1 
ATOM   15513 C  CD1 . TYR   B 1 173  ? 59.16500   75.87600  -23.27200 1.000 55.55890  ?  173  TYR   B CD1 1 
ATOM   15514 C  CD2 . TYR   B 1 173  ? 61.28100   75.89000  -24.36400 1.000 52.91009  ?  173  TYR   B CD2 1 
ATOM   15515 C  CE1 . TYR   B 1 173  ? 58.52800   75.81900  -24.49500 1.000 54.38796  ?  173  TYR   B CE1 1 
ATOM   15516 C  CE2 . TYR   B 1 173  ? 60.65200   75.83500  -25.59300 1.000 53.87880  ?  173  TYR   B CE2 1 
ATOM   15517 C  CZ  . TYR   B 1 173  ? 59.27600   75.79900  -25.65300 1.000 51.11761  ?  173  TYR   B CZ  1 
ATOM   15518 O  OH  . TYR   B 1 173  ? 58.64600   75.74300  -26.87400 1.000 73.53061  ?  173  TYR   B OH  1 
ATOM   15519 N  N   . LYS   B 1 174  ? 62.98400   78.56500  -19.83600 1.000 47.20674  ?  174  LYS   B N   1 
ATOM   15520 C  CA  . LYS   B 1 174  ? 64.05000   78.63800  -18.84700 1.000 35.83541  ?  174  LYS   B CA  1 
ATOM   15521 C  C   . LYS   B 1 174  ? 63.52800   78.47100  -17.42600 1.000 49.77363  ?  174  LYS   B C   1 
ATOM   15522 O  O   . LYS   B 1 174  ? 64.25300   77.96600  -16.56000 1.000 63.77067  ?  174  LYS   B O   1 
ATOM   15523 C  CB  . LYS   B 1 174  ? 64.80000   79.96500  -18.98500 1.000 30.06195  ?  174  LYS   B CB  1 
ATOM   15524 C  CG  . LYS   B 1 174  ? 63.95900   81.18400  -18.66400 1.000 43.65928  ?  174  LYS   B CG  1 
ATOM   15525 C  CD  . LYS   B 1 174  ? 64.78100   82.46300  -18.65500 1.000 37.79898  ?  174  LYS   B CD  1 
ATOM   15526 C  CE  . LYS   B 1 174  ? 64.30900   83.39700  -17.54300 1.000 63.54992  ?  174  LYS   B CE  1 
ATOM   15527 N  NZ  . LYS   B 1 174  ? 64.22300   84.82200  -17.97200 1.000 56.79648  ?  174  LYS   B NZ  1 
ATOM   15528 N  N   . ASN   B 1 175  ? 62.28500   78.86600  -17.16800 1.000 41.01231  ?  175  ASN   B N   1 
ATOM   15529 C  CA  . ASN   B 1 175  ? 61.73000   78.83100  -15.82400 1.000 26.91588  ?  175  ASN   B CA  1 
ATOM   15530 C  C   . ASN   B 1 175  ? 61.07200   77.50100  -15.48300 1.000 32.29015  ?  175  ASN   B C   1 
ATOM   15531 O  O   . ASN   B 1 175  ? 60.36300   77.41700  -14.47600 1.000 43.82540  ?  175  ASN   B O   1 
ATOM   15532 C  CB  . ASN   B 1 175  ? 60.72500   79.96900  -15.64400 1.000 26.74806  ?  175  ASN   B CB  1 
ATOM   15533 C  CG  . ASN   B 1 175  ? 61.33300   81.32600  -15.92300 1.000 43.23248  ?  175  ASN   B CG  1 
ATOM   15534 O  OD1 . ASN   B 1 175  ? 62.52100   81.54200  -15.68500 1.000 47.10127  ?  175  ASN   B OD1 1 
ATOM   15535 N  ND2 . ASN   B 1 175  ? 60.52200   82.25200  -16.42000 1.000 51.97630  ?  175  ASN   B ND2 1 
ATOM   15536 N  N   . LEU   B 1 176  ? 61.29600   76.45800  -16.28100 1.000 27.34566  ?  176  LEU   B N   1 
ATOM   15537 C  CA  . LEU   B 1 176  ? 60.62000   75.18100  -16.08900 1.000 40.88397  ?  176  LEU   B CA  1 
ATOM   15538 C  C   . LEU   B 1 176  ? 61.58200   74.07800  -15.65700 1.000 43.80635  ?  176  LEU   B C   1 
ATOM   15539 O  O   . LEU   B 1 176  ? 61.40100   72.91300  -16.01900 1.000 51.20886  ?  176  LEU   B O   1 
ATOM   15540 C  CB  . LEU   B 1 176  ? 59.88200   74.77700  -17.36300 1.000 39.17879  ?  176  LEU   B CB  1 
ATOM   15541 C  CG  . LEU   B 1 176  ? 59.10200   75.88700  -18.07100 1.000 35.73429  ?  176  LEU   B CG  1 
ATOM   15542 C  CD1 . LEU   B 1 176  ? 58.59900   75.42300  -19.42900 1.000 33.20692  ?  176  LEU   B CD1 1 
ATOM   15543 C  CD2 . LEU   B 1 176  ? 57.94800   76.35000  -17.20300 1.000 35.33325  ?  176  LEU   B CD2 1 
ATOM   15544 N  N   . ASN   B 1 177  ? 62.60600   74.43100  -14.87600 1.000 46.52361  ?  177  ASN   B N   1 
ATOM   15545 C  CA  . ASN   B 1 177  ? 63.63500   73.45800  -14.52300 1.000 43.29983  ?  177  ASN   B CA  1 
ATOM   15546 C  C   . ASN   B 1 177  ? 63.24600   72.63800  -13.30100 1.000 53.09433  ?  177  ASN   B C   1 
ATOM   15547 O  O   . ASN   B 1 177  ? 63.57600   71.45000  -13.21800 1.000 44.45175  ?  177  ASN   B O   1 
ATOM   15548 C  CB  . ASN   B 1 177  ? 64.97000   74.16300  -14.28900 1.000 43.66380  ?  177  ASN   B CB  1 
ATOM   15549 C  CG  . ASN   B 1 177  ? 65.91900   74.02900  -15.47300 1.000 71.22323  ?  177  ASN   B CG  1 
ATOM   15550 O  OD1 . ASN   B 1 177  ? 65.58100   73.43100  -16.49700 1.000 59.56954  ?  177  ASN   B OD1 1 
ATOM   15551 N  ND2 . ASN   B 1 177  ? 67.11700   74.58600  -15.33400 1.000 76.27720  ?  177  ASN   B ND2 1 
ATOM   15552 N  N   . MET   B 1 178  ? 62.55200   73.25000  -12.34300 1.000 53.48088  ?  178  MET   B N   1 
ATOM   15553 C  CA  . MET   B 1 178  ? 62.09200   72.55200  -11.15000 1.000 45.57650  ?  178  MET   B CA  1 
ATOM   15554 C  C   . MET   B 1 178  ? 60.61800   72.16400  -11.24400 1.000 46.16764  ?  178  MET   B C   1 
ATOM   15555 O  O   . MET   B 1 178  ? 59.94400   72.02100  -10.21900 1.000 56.14542  ?  178  MET   B O   1 
ATOM   15556 C  CB  . MET   B 1 178  ? 62.35500   73.40300  -9.90800  1.000 60.20119  ?  178  MET   B CB  1 
ATOM   15557 C  CG  . MET   B 1 178  ? 63.52300   72.90400  -9.06100  1.000 69.18109  ?  178  MET   B CG  1 
ATOM   15558 S  SD  . MET   B 1 178  ? 64.24100   74.16500  -7.98800  1.000 69.52194  ?  178  MET   B SD  1 
ATOM   15559 C  CE  . MET   B 1 178  ? 62.76900   74.86700  -7.24500  1.000 86.35260  ?  178  MET   B CE  1 
ATOM   15560 N  N   . THR   B 1 179  ? 60.11000   71.98100  -12.45900 1.000 47.89175  ?  179  THR   B N   1 
ATOM   15561 C  CA  . THR   B 1 179  ? 58.72800   71.59100  -12.69300 1.000 43.09942  ?  179  THR   B CA  1 
ATOM   15562 C  C   . THR   B 1 179  ? 58.66000   70.10100  -13.00700 1.000 34.66758  ?  179  THR   B C   1 
ATOM   15563 O  O   . THR   B 1 179  ? 59.49600   69.57600  -13.74700 1.000 44.85110  ?  179  THR   B O   1 
ATOM   15564 C  CB  . THR   B 1 179  ? 58.13000   72.41200  -13.84100 1.000 45.65550  ?  179  THR   B CB  1 
ATOM   15565 O  OG1 . THR   B 1 179  ? 57.86500   73.74600  -13.38600 1.000 50.77840  ?  179  THR   B OG1 1 
ATOM   15566 C  CG2 . THR   B 1 179  ? 56.84400   71.79200  -14.36000 1.000 37.59438  ?  179  THR   B CG2 1 
ATOM   15567 N  N   . THR   B 1 180  ? 57.67300   69.42000  -12.42700 1.000 39.24474  ?  180  THR   B N   1 
ATOM   15568 C  CA  . THR   B 1 180  ? 57.52100   67.98900  -12.65300 1.000 49.33405  ?  180  THR   B CA  1 
ATOM   15569 C  C   . THR   B 1 180  ? 57.20200   67.69700  -14.11800 1.000 47.06104  ?  180  THR   B C   1 
ATOM   15570 O  O   . THR   B 1 180  ? 56.74200   68.56200  -14.86900 1.000 48.43086  ?  180  THR   B O   1 
ATOM   15571 C  CB  . THR   B 1 180  ? 56.42100   67.42100  -11.76000 1.000 48.19784  ?  180  THR   B CB  1 
ATOM   15572 O  OG1 . THR   B 1 180  ? 55.14400   67.85800  -12.24200 1.000 57.12228  ?  180  THR   B OG1 1 
ATOM   15573 C  CG2 . THR   B 1 180  ? 56.60700   67.90600  -10.33700 1.000 55.17567  ?  180  THR   B CG2 1 
ATOM   15574 N  N   . VAL   B 1 181  ? 57.45800   66.44900  -14.51900 1.000 44.65607  ?  181  VAL   B N   1 
ATOM   15575 C  CA  . VAL   B 1 181  ? 57.18700   66.03000  -15.89200 1.000 42.76173  ?  181  VAL   B CA  1 
ATOM   15576 C  C   . VAL   B 1 181  ? 55.70700   66.19000  -16.21000 1.000 50.63337  ?  181  VAL   B C   1 
ATOM   15577 O  O   . VAL   B 1 181  ? 55.33100   66.70700  -17.26900 1.000 54.58596  ?  181  VAL   B O   1 
ATOM   15578 C  CB  . VAL   B 1 181  ? 57.65600   64.57900  -16.11100 1.000 44.73976  ?  181  VAL   B CB  1 
ATOM   15579 C  CG1 . VAL   B 1 181  ? 57.02400   63.99400  -17.36500 1.000 45.13683  ?  181  VAL   B CG1 1 
ATOM   15580 C  CG2 . VAL   B 1 181  ? 59.16900   64.52200  -16.20000 1.000 32.01221  ?  181  VAL   B CG2 1 
ATOM   15581 N  N   . ARG   B 1 182  ? 54.84700   65.75600  -15.28800 1.000 45.61063  ?  182  ARG   B N   1 
ATOM   15582 C  CA  . ARG   B 1 182  ? 53.40800   65.83200  -15.51300 1.000 42.46267  ?  182  ARG   B CA  1 
ATOM   15583 C  C   . ARG   B 1 182  ? 52.95300   67.27800  -15.66100 1.000 45.93892  ?  182  ARG   B C   1 
ATOM   15584 O  O   . ARG   B 1 182  ? 52.21800   67.61900  -16.59600 1.000 59.20500  ?  182  ARG   B O   1 
ATOM   15585 C  CB  . ARG   B 1 182  ? 52.67000   65.14200  -14.36600 1.000 59.07894  ?  182  ARG   B CB  1 
ATOM   15586 C  CG  . ARG   B 1 182  ? 51.17300   65.00500  -14.57200 1.000 75.12056  ?  182  ARG   B CG  1 
ATOM   15587 C  CD  . ARG   B 1 182  ? 50.48300   64.58400  -13.28400 1.000 66.76038  ?  182  ARG   B CD  1 
ATOM   15588 N  NE  . ARG   B 1 182  ? 51.00500   65.30600  -12.13000 1.000 80.36397  ?  182  ARG   B NE  1 
ATOM   15589 C  CZ  . ARG   B 1 182  ? 50.66300   66.54400  -11.79700 1.000 81.52744  ?  182  ARG   B CZ  1 
ATOM   15590 N  NH1 . ARG   B 1 182  ? 49.78700   67.23600  -12.50900 1.000 68.15143  ?  182  ARG   B NH1 1 
ATOM   15591 N  NH2 . ARG   B 1 182  ? 51.21500   67.10300  -10.72300 1.000 79.48315  ?  182  ARG   B NH2 1 
ATOM   15592 N  N   . GLU   B 1 183  ? 53.38900   68.14800  -14.74900 1.000 47.24741  ?  183  GLU   B N   1 
ATOM   15593 C  CA  . GLU   B 1 183  ? 53.02100   69.55600  -14.83600 1.000 40.74672  ?  183  GLU   B CA  1 
ATOM   15594 C  C   . GLU   B 1 183  ? 53.62800   70.23500  -16.05400 1.000 42.03778  ?  183  GLU   B C   1 
ATOM   15595 O  O   . GLU   B 1 183  ? 53.09300   71.25200  -16.51100 1.000 48.63878  ?  183  GLU   B O   1 
ATOM   15596 C  CB  . GLU   B 1 183  ? 53.44500   70.29300  -13.56600 1.000 42.08553  ?  183  GLU   B CB  1 
ATOM   15597 C  CG  . GLU   B 1 183  ? 52.57900   69.99200  -12.35600 1.000 61.31408  ?  183  GLU   B CG  1 
ATOM   15598 C  CD  . GLU   B 1 183  ? 53.25800   70.35700  -11.05200 1.000 76.48915  ?  183  GLU   B CD  1 
ATOM   15599 O  OE1 . GLU   B 1 183  ? 54.50700   70.40000  -11.02400 1.000 72.38752  ?  183  GLU   B OE1 1 
ATOM   15600 O  OE2 . GLU   B 1 183  ? 52.54400   70.59900  -10.05600 1.000 80.83100  -1 183  GLU   B OE2 1 
ATOM   15601 N  N   . LEU   B 1 184  ? 54.72900   69.70200  -16.58600 1.000 54.63657  ?  184  LEU   B N   1 
ATOM   15602 C  CA  . LEU   B 1 184  ? 55.33300   70.28700  -17.77800 1.000 47.86752  ?  184  LEU   B CA  1 
ATOM   15603 C  C   . LEU   B 1 184  ? 54.54200   69.93700  -19.03200 1.000 45.93577  ?  184  LEU   B C   1 
ATOM   15604 O  O   . LEU   B 1 184  ? 54.31400   70.80200  -19.88500 1.000 39.24495  ?  184  LEU   B O   1 
ATOM   15605 C  CB  . LEU   B 1 184  ? 56.78200   69.82600  -17.91800 1.000 36.54881  ?  184  LEU   B CB  1 
ATOM   15606 C  CG  . LEU   B 1 184  ? 57.55100   70.52200  -19.04000 1.000 46.20016  ?  184  LEU   B CG  1 
ATOM   15607 C  CD1 . LEU   B 1 184  ? 58.21600   71.79500  -18.53600 1.000 40.69215  ?  184  LEU   B CD1 1 
ATOM   15608 C  CD2 . LEU   B 1 184  ? 58.57200   69.58100  -19.65100 1.000 39.41006  ?  184  LEU   B CD2 1 
ATOM   15609 N  N   . LEU   B 1 185  ? 54.11300   68.67900  -19.15500 1.000 43.36590  ?  185  LEU   B N   1 
ATOM   15610 C  CA  . LEU   B 1 185  ? 53.30600   68.28100  -20.30400 1.000 47.57055  ?  185  LEU   B CA  1 
ATOM   15611 C  C   . LEU   B 1 185  ? 51.92700   68.92900  -20.26300 1.000 51.63897  ?  185  LEU   B C   1 
ATOM   15612 O  O   . LEU   B 1 185  ? 51.37700   69.29400  -21.31000 1.000 50.63543  ?  185  LEU   B O   1 
ATOM   15613 C  CB  . LEU   B 1 185  ? 53.19000   66.76000  -20.36000 1.000 44.35692  ?  185  LEU   B CB  1 
ATOM   15614 C  CG  . LEU   B 1 185  ? 54.51900   66.01000  -20.42200 1.000 37.78999  ?  185  LEU   B CG  1 
ATOM   15615 C  CD1 . LEU   B 1 185  ? 54.27700   64.53400  -20.65600 1.000 42.20284  ?  185  LEU   B CD1 1 
ATOM   15616 C  CD2 . LEU   B 1 185  ? 55.39600   66.59000  -21.51700 1.000 46.43427  ?  185  LEU   B CD2 1 
ATOM   15617 N  N   . ALA   B 1 186  ? 51.34900   69.06800  -19.06600 1.000 42.64798  ?  186  ALA   B N   1 
ATOM   15618 C  CA  . ALA   B 1 186  ? 50.10800   69.82400  -18.91900 1.000 49.35746  ?  186  ALA   B CA  1 
ATOM   15619 C  C   . ALA   B 1 186  ? 50.27000   71.23900  -19.45300 1.000 46.03894  ?  186  ALA   B C   1 
ATOM   15620 O  O   . ALA   B 1 186  ? 49.49600   71.68700  -20.30700 1.000 59.37609  ?  186  ALA   B O   1 
ATOM   15621 C  CB  . ALA   B 1 186  ? 49.68300   69.85800  -17.45100 1.000 28.47313  ?  186  ALA   B CB  1 
ATOM   15622 N  N   . LEU   B 1 187  ? 51.28400   71.95400  -18.96100 1.000 46.23999  ?  187  LEU   B N   1 
ATOM   15623 C  CA  . LEU   B 1 187  ? 51.56500   73.30300  -19.43900 1.000 43.01424  ?  187  LEU   B CA  1 
ATOM   15624 C  C   . LEU   B 1 187  ? 51.74300   73.35000  -20.95200 1.000 51.88045  ?  187  LEU   B C   1 
ATOM   15625 O  O   . LEU   B 1 187  ? 51.37800   74.34500  -21.58900 1.000 51.61667  ?  187  LEU   B O   1 
ATOM   15626 C  CB  . LEU   B 1 187  ? 52.81400   73.84700  -18.74600 1.000 40.05139  ?  187  LEU   B CB  1 
ATOM   15627 C  CG  . LEU   B 1 187  ? 53.41200   75.11900  -19.34700 1.000 33.53457  ?  187  LEU   B CG  1 
ATOM   15628 C  CD1 . LEU   B 1 187  ? 52.74300   76.33700  -18.75200 1.000 30.05870  ?  187  LEU   B CD1 1 
ATOM   15629 C  CD2 . LEU   B 1 187  ? 54.91400   75.17700  -19.13400 1.000 44.03304  ?  187  LEU   B CD2 1 
ATOM   15630 N  N   . LYS   B 1 188  ? 52.29300   72.28600  -21.54600 1.000 53.74117  ?  188  LYS   B N   1 
ATOM   15631 C  CA  . LYS   B 1 188  ? 52.49700   72.27200  -22.99200 1.000 45.03588  ?  188  LYS   B CA  1 
ATOM   15632 C  C   . LYS   B 1 188  ? 51.17000   72.37000  -23.73400 1.000 53.92465  ?  188  LYS   B C   1 
ATOM   15633 O  O   . LYS   B 1 188  ? 51.00200   73.22000  -24.61500 1.000 65.77128  ?  188  LYS   B O   1 
ATOM   15634 C  CB  . LYS   B 1 188  ? 53.25300   71.01100  -23.41200 1.000 40.91491  ?  188  LYS   B CB  1 
ATOM   15635 C  CG  . LYS   B 1 188  ? 53.56300   70.96500  -24.90300 1.000 43.92422  ?  188  LYS   B CG  1 
ATOM   15636 C  CD  . LYS   B 1 188  ? 54.48800   69.81200  -25.25400 1.000 57.15527  ?  188  LYS   B CD  1 
ATOM   15637 C  CE  . LYS   B 1 188  ? 53.71200   68.52500  -25.48000 1.000 50.66614  ?  188  LYS   B CE  1 
ATOM   15638 N  NZ  . LYS   B 1 188  ? 54.25300   67.74200  -26.62600 1.000 42.26855  ?  188  LYS   B NZ  1 
ATOM   15639 N  N   . ARG   B 1 189  ? 50.21100   71.50800  -23.38600 1.000 46.63770  ?  189  ARG   B N   1 
ATOM   15640 C  CA  . ARG   B 1 189  ? 48.91300   71.52400  -24.05600 1.000 58.61076  ?  189  ARG   B CA  1 
ATOM   15641 C  C   . ARG   B 1 189  ? 48.20000   72.85500  -23.85500 1.000 51.94413  ?  189  ARG   B C   1 
ATOM   15642 O  O   . ARG   B 1 189  ? 47.65700   73.43300  -24.80400 1.000 59.93527  ?  189  ARG   B O   1 
ATOM   15643 C  CB  . ARG   B 1 189  ? 48.04700   70.37400  -23.54600 1.000 36.77883  ?  189  ARG   B CB  1 
ATOM   15644 C  CG  . ARG   B 1 189  ? 48.72700   69.02300  -23.62600 1.000 48.25244  ?  189  ARG   B CG  1 
ATOM   15645 C  CD  . ARG   B 1 189  ? 48.37000   68.16500  -22.43200 1.000 61.30094  ?  189  ARG   B CD  1 
ATOM   15646 N  NE  . ARG   B 1 189  ? 49.09300   66.89900  -22.43700 1.000 79.96188  ?  189  ARG   B NE  1 
ATOM   15647 C  CZ  . ARG   B 1 189  ? 49.13600   66.06100  -21.41000 1.000 92.38333  ?  189  ARG   B CZ  1 
ATOM   15648 N  NH1 . ARG   B 1 189  ? 48.50100   66.32200  -20.27800 1.000 86.56622  ?  189  ARG   B NH1 1 
ATOM   15649 N  NH2 . ARG   B 1 189  ? 49.83400   64.93300  -21.52000 1.000 75.59904  ?  189  ARG   B NH2 1 
ATOM   15650 N  N   . LEU   B 1 190  ? 48.19700   73.36000  -22.62100 1.000 48.71379  ?  190  LEU   B N   1 
ATOM   15651 C  CA  . LEU   B 1 190  ? 47.56000   74.63700  -22.32600 1.000 49.69169  ?  190  LEU   B CA  1 
ATOM   15652 C  C   . LEU   B 1 190  ? 48.22700   75.81400  -23.02700 1.000 56.51793  ?  190  LEU   B C   1 
ATOM   15653 O  O   . LEU   B 1 190  ? 47.68000   76.92100  -22.98300 1.000 79.21373  ?  190  LEU   B O   1 
ATOM   15654 C  CB  . LEU   B 1 190  ? 47.55500   74.88600  -20.81600 1.000 38.87653  ?  190  LEU   B CB  1 
ATOM   15655 C  CG  . LEU   B 1 190  ? 46.46800   74.22500  -19.96800 1.000 56.61260  ?  190  LEU   B CG  1 
ATOM   15656 C  CD1 . LEU   B 1 190  ? 46.69300   72.73300  -19.79900 1.000 64.04349  ?  190  LEU   B CD1 1 
ATOM   15657 C  CD2 . LEU   B 1 190  ? 46.41000   74.90500  -18.60900 1.000 57.43546  ?  190  LEU   B CD2 1 
ATOM   15658 N  N   . CYS   B 1 191  ? 49.37600   75.61500  -23.66800 1.000 51.41125  ?  191  CYS   B N   1 
ATOM   15659 C  CA  . CYS   B 1 191  ? 50.12300   76.71000  -24.28100 1.000 66.17327  ?  191  CYS   B CA  1 
ATOM   15660 C  C   . CYS   B 1 191  ? 50.77300   76.25300  -25.58400 1.000 68.92431  ?  191  CYS   B C   1 
ATOM   15661 O  O   . CYS   B 1 191  ? 51.93800   76.53900  -25.86000 1.000 76.27298  ?  191  CYS   B O   1 
ATOM   15662 C  CB  . CYS   B 1 191  ? 51.17000   77.25600  -23.31100 1.000 66.83997  ?  191  CYS   B CB  1 
ATOM   15663 S  SG  . CYS   B 1 191  ? 50.48300   78.11400  -21.87400 1.000 89.71278  ?  191  CYS   B SG  1 
ATOM   15664 N  N   . ALA   B 1 192  ? 50.01200   75.53500  -26.40900 1.000 79.08867  ?  192  ALA   B N   1 
ATOM   15665 C  CA  . ALA   B 1 192  ? 50.50300   75.10800  -27.71200 1.000 85.21917  ?  192  ALA   B CA  1 
ATOM   15666 C  C   . ALA   B 1 192  ? 49.32300   74.88100  -28.64400 1.000 84.55896  ?  192  ALA   B C   1 
ATOM   15667 O  O   . ALA   B 1 192  ? 48.21600   74.55600  -28.20500 1.000 61.06711  ?  192  ALA   B O   1 
ATOM   15668 C  CB  . ALA   B 1 192  ? 51.35500   73.83800  -27.61900 1.000 82.71307  ?  192  ALA   B CB  1 
ATOM   15669 N  N   . GLU   B 1 193  ? 49.58500   75.04800  -29.93600 1.000 82.70327  ?  193  GLU   B N   1 
ATOM   15670 C  CA  . GLU   B 1 193  ? 48.57000   74.94300  -30.97600 1.000 73.40385  ?  193  GLU   B CA  1 
ATOM   15671 C  C   . GLU   B 1 193  ? 48.01900   73.52600  -31.09000 1.000 74.00215  ?  193  GLU   B C   1 
ATOM   15672 O  O   . GLU   B 1 193  ? 47.98800   72.95100  -32.17800 1.000 79.67683  ?  193  GLU   B O   1 
ATOM   15673 C  CB  . GLU   B 1 193  ? 49.15200   75.38900  -32.32100 1.000 70.15572  ?  193  GLU   B CB  1 
ATOM   15674 C  CG  . GLU   B 1 193  ? 49.98700   76.67400  -32.26000 1.000 86.90678  ?  193  GLU   B CG  1 
ATOM   15675 C  CD  . GLU   B 1 193  ? 51.43000   76.44200  -31.82000 1.000 106.23149 ?  193  GLU   B CD  1 
ATOM   15676 O  OE1 . GLU   B 1 193  ? 51.66100   75.59500  -30.92900 1.000 107.82555 ?  193  GLU   B OE1 1 
ATOM   15677 O  OE2 . GLU   B 1 193  ? 52.33400   77.11200  -32.36300 1.000 99.18691  -1 193  GLU   B OE2 1 
ATOM   15678 N  N   . GLU   B 1 198  ? 42.03300   73.79700  -37.64000 1.000 101.63313 ?  198  GLU   B N   1 
ATOM   15679 C  CA  . GLU   B 1 198  ? 42.19800   75.24500  -37.66300 1.000 105.76951 ?  198  GLU   B CA  1 
ATOM   15680 C  C   . GLU   B 1 198  ? 41.86500   75.81600  -39.03900 1.000 114.17239 ?  198  GLU   B C   1 
ATOM   15681 O  O   . GLU   B 1 198  ? 42.74200   75.95500  -39.89100 1.000 120.18963 ?  198  GLU   B O   1 
ATOM   15682 C  CB  . GLU   B 1 198  ? 43.62700   75.62900  -37.26700 1.000 72.89490  ?  198  GLU   B CB  1 
ATOM   15683 N  N   . LYS   B 1 199  ? 40.59000   76.14000  -39.25200 1.000 92.33959  ?  199  LYS   B N   1 
ATOM   15684 C  CA  . LYS   B 1 199  ? 40.21900   76.76300  -40.51700 1.000 88.78006  ?  199  LYS   B CA  1 
ATOM   15685 C  C   . LYS   B 1 199  ? 40.37300   78.28000  -40.42300 1.000 96.30937  ?  199  LYS   B C   1 
ATOM   15686 O  O   . LYS   B 1 199  ? 40.09500   78.86800  -39.37400 1.000 87.52984  ?  199  LYS   B O   1 
ATOM   15687 C  CB  . LYS   B 1 199  ? 38.78000   76.41700  -40.89200 1.000 75.80825  ?  199  LYS   B CB  1 
ATOM   15688 N  N   . PRO   B 1 200  ? 40.82700   78.93300  -41.48900 1.000 90.74672  ?  200  PRO   B N   1 
ATOM   15689 C  CA  . PRO   B 1 200  ? 40.97200   80.39000  -41.45600 1.000 79.97739  ?  200  PRO   B CA  1 
ATOM   15690 C  C   . PRO   B 1 200  ? 39.66100   81.10400  -41.75300 1.000 76.57479  ?  200  PRO   B C   1 
ATOM   15691 O  O   . PRO   B 1 200  ? 38.81500   80.62100  -42.50800 1.000 80.41747  ?  200  PRO   B O   1 
ATOM   15692 C  CB  . PRO   B 1 200  ? 42.00600   80.66000  -42.55500 1.000 72.19023  ?  200  PRO   B CB  1 
ATOM   15693 C  CG  . PRO   B 1 200  ? 41.77800   79.55900  -43.53900 1.000 71.77481  ?  200  PRO   B CG  1 
ATOM   15694 C  CD  . PRO   B 1 200  ? 41.34500   78.35100  -42.74100 1.000 67.37169  ?  200  PRO   B CD  1 
ATOM   15695 N  N   . ILE   B 1 201  ? 39.50300   82.27300  -41.13500 1.000 64.53052  ?  201  ILE   B N   1 
ATOM   15696 C  CA  . ILE   B 1 201  ? 38.32600   83.10400  -41.37200 1.000 52.23968  ?  201  ILE   B CA  1 
ATOM   15697 C  C   . ILE   B 1 201  ? 38.39100   83.65100  -42.79300 1.000 50.47901  ?  201  ILE   B C   1 
ATOM   15698 O  O   . ILE   B 1 201  ? 39.36000   84.31700  -43.17300 1.000 58.90175  ?  201  ILE   B O   1 
ATOM   15699 C  CB  . ILE   B 1 201  ? 38.23700   84.23700  -40.34100 1.000 51.51538  ?  201  ILE   B CB  1 
ATOM   15700 C  CG1 . ILE   B 1 201  ? 38.17100   83.66600  -38.92000 1.000 45.37648  ?  201  ILE   B CG1 1 
ATOM   15701 C  CG2 . ILE   B 1 201  ? 37.04600   85.14100  -40.63100 1.000 43.57746  ?  201  ILE   B CG2 1 
ATOM   15702 C  CD1 . ILE   B 1 201  ? 36.88500   82.93400  -38.61200 1.000 48.81105  ?  201  ILE   B CD1 1 
ATOM   15703 N  N   . ASP   B 1 202  ? 37.35400   83.37100  -43.58600 1.000 54.88914  ?  202  ASP   B N   1 
ATOM   15704 C  CA  . ASP   B 1 202  ? 37.31400   83.76600  -44.99100 1.000 58.04006  ?  202  ASP   B CA  1 
ATOM   15705 C  C   . ASP   B 1 202  ? 36.08600   84.60700  -45.32100 1.000 54.13849  ?  202  ASP   B C   1 
ATOM   15706 O  O   . ASP   B 1 202  ? 35.69200   84.68900  -46.48900 1.000 62.02177  ?  202  ASP   B O   1 
ATOM   15707 C  CB  . ASP   B 1 202  ? 37.35300   82.52900  -45.88900 1.000 64.27265  ?  202  ASP   B CB  1 
ATOM   15708 C  CG  . ASP   B 1 202  ? 36.43000   81.43100  -45.39800 1.000 92.54580  ?  202  ASP   B CG  1 
ATOM   15709 O  OD1 . ASP   B 1 202  ? 36.09000   81.44000  -44.19500 1.000 79.35189  ?  202  ASP   B OD1 1 
ATOM   15710 O  OD2 . ASP   B 1 202  ? 36.04600   80.56300  -46.21000 1.000 103.81924 -1 202  ASP   B OD2 1 
ATOM   15711 N  N   . LYS   B 1 203  ? 35.47200   85.23400  -44.32200 1.000 41.83832  ?  203  LYS   B N   1 
ATOM   15712 C  CA  . LYS   B 1 203  ? 34.23000   85.96400  -44.52200 1.000 51.24566  ?  203  LYS   B CA  1 
ATOM   15713 C  C   . LYS   B 1 203  ? 34.29100   87.29700  -43.79400 1.000 36.69224  ?  203  LYS   B C   1 
ATOM   15714 O  O   . LYS   B 1 203  ? 35.00300   87.44800  -42.79900 1.000 36.13620  ?  203  LYS   B O   1 
ATOM   15715 C  CB  . LYS   B 1 203  ? 33.01800   85.16300  -44.02100 1.000 48.87125  ?  203  LYS   B CB  1 
ATOM   15716 C  CG  . LYS   B 1 203  ? 32.76200   83.86700  -44.77100 1.000 56.11256  ?  203  LYS   B CG  1 
ATOM   15717 C  CD  . LYS   B 1 203  ? 32.35000   84.13900  -46.20700 1.000 57.34949  ?  203  LYS   B CD  1 
ATOM   15718 C  CE  . LYS   B 1 203  ? 32.23700   82.85000  -47.00200 1.000 71.40525  ?  203  LYS   B CE  1 
ATOM   15719 N  NZ  . LYS   B 1 203  ? 31.21000   81.93500  -46.43000 1.000 84.90597  ?  203  LYS   B NZ  1 
ATOM   15720 N  N   . THR   B 1 204  ? 33.54400   88.26500  -44.31100 1.000 32.94953  ?  204  THR   B N   1 
ATOM   15721 C  CA  . THR   B 1 204  ? 33.27000   89.49700  -43.59300 1.000 31.57073  ?  204  THR   B CA  1 
ATOM   15722 C  C   . THR   B 1 204  ? 31.95100   89.35100  -42.83900 1.000 39.16648  ?  204  THR   B C   1 
ATOM   15723 O  O   . THR   B 1 204  ? 31.22500   88.36700  -42.99800 1.000 48.29546  ?  204  THR   B O   1 
ATOM   15724 C  CB  . THR   B 1 204  ? 33.22500   90.68500  -44.55700 1.000 38.58191  ?  204  THR   B CB  1 
ATOM   15725 O  OG1 . THR   B 1 204  ? 32.16900   90.49600  -45.50700 1.000 33.50942  ?  204  THR   B OG1 1 
ATOM   15726 C  CG2 . THR   B 1 204  ? 34.54700   90.81300  -45.30200 1.000 35.11468  ?  204  THR   B CG2 1 
ATOM   15727 N  N   . PHE   B 1 205  ? 31.64000   90.33900  -41.99900 1.000 28.62301  ?  205  PHE   B N   1 
ATOM   15728 C  CA  . PHE   B 1 205  ? 30.41300   90.24600  -41.21300 1.000 36.27742  ?  205  PHE   B CA  1 
ATOM   15729 C  C   . PHE   B 1 205  ? 29.17900   90.43100  -42.08700 1.000 41.73678  ?  205  PHE   B C   1 
ATOM   15730 O  O   . PHE   B 1 205  ? 28.25600   89.60700  -42.05400 1.000 42.55915  ?  205  PHE   B O   1 
ATOM   15731 C  CB  . PHE   B 1 205  ? 30.41000   91.26700  -40.07800 1.000 41.06488  ?  205  PHE   B CB  1 
ATOM   15732 C  CG  . PHE   B 1 205  ? 29.15500   91.23100  -39.25600 1.000 35.64610  ?  205  PHE   B CG  1 
ATOM   15733 C  CD1 . PHE   B 1 205  ? 28.99400   90.28000  -38.26500 1.000 32.63960  ?  205  PHE   B CD1 1 
ATOM   15734 C  CD2 . PHE   B 1 205  ? 28.12400   92.12600  -39.49400 1.000 42.75025  ?  205  PHE   B CD2 1 
ATOM   15735 C  CE1 . PHE   B 1 205  ? 27.83500   90.23300  -37.51400 1.000 39.39687  ?  205  PHE   B CE1 1 
ATOM   15736 C  CE2 . PHE   B 1 205  ? 26.96300   92.08300  -38.74700 1.000 37.32918  ?  205  PHE   B CE2 1 
ATOM   15737 C  CZ  . PHE   B 1 205  ? 26.82000   91.13500  -37.75600 1.000 38.91671  ?  205  PHE   B CZ  1 
ATOM   15738 N  N   . HIS   B 1 206  ? 29.13400   91.51900  -42.86400 1.000 32.32829  ?  206  HIS   B N   1 
ATOM   15739 C  CA  . HIS   B 1 206  ? 27.96300   91.77000  -43.69700 1.000 30.40182  ?  206  HIS   B CA  1 
ATOM   15740 C  C   . HIS   B 1 206  ? 27.74200   90.64600  -44.69900 1.000 31.37930  ?  206  HIS   B C   1 
ATOM   15741 O  O   . HIS   B 1 206  ? 26.60400   90.39400  -45.10800 1.000 42.75335  ?  206  HIS   B O   1 
ATOM   15742 C  CB  . HIS   B 1 206  ? 28.09000   93.11700  -44.41400 1.000 40.02860  ?  206  HIS   B CB  1 
ATOM   15743 C  CG  . HIS   B 1 206  ? 29.39700   93.31800  -45.11500 1.000 37.76683  ?  206  HIS   B CG  1 
ATOM   15744 N  ND1 . HIS   B 1 206  ? 30.57100   93.58100  -44.44200 1.000 38.73031  ?  206  HIS   B ND1 1 
ATOM   15745 C  CD2 . HIS   B 1 206  ? 29.71200   93.31700  -46.43200 1.000 30.18382  ?  206  HIS   B CD2 1 
ATOM   15746 C  CE1 . HIS   B 1 206  ? 31.55400   93.72200  -45.31300 1.000 41.61225  ?  206  HIS   B CE1 1 
ATOM   15747 N  NE2 . HIS   B 1 206  ? 31.05900   93.56700  -46.52800 1.000 43.94166  ?  206  HIS   B NE2 1 
ATOM   15748 N  N   . GLN   B 1 207  ? 28.80800   89.95200  -45.09400 1.000 32.42604  ?  207  GLN   B N   1 
ATOM   15749 C  CA  . GLN   B 1 207  ? 28.64500   88.75700  -45.91200 1.000 44.70387  ?  207  GLN   B CA  1 
ATOM   15750 C  C   . GLN   B 1 207  ? 27.84500   87.69500  -45.16500 1.000 34.58409  ?  207  GLN   B C   1 
ATOM   15751 O  O   . GLN   B 1 207  ? 26.83800   87.18600  -45.67100 1.000 31.64195  ?  207  GLN   B O   1 
ATOM   15752 C  CB  . GLN   B 1 207  ? 30.01600   88.21800  -46.31900 1.000 47.55073  ?  207  GLN   B CB  1 
ATOM   15753 C  CG  . GLN   B 1 207  ? 30.05500   87.56200  -47.68300 1.000 66.24235  ?  207  GLN   B CG  1 
ATOM   15754 C  CD  . GLN   B 1 207  ? 31.41900   86.98100  -47.99800 1.000 69.97553  ?  207  GLN   B CD  1 
ATOM   15755 O  OE1 . GLN   B 1 207  ? 32.39100   87.22800  -47.28300 1.000 59.50927  ?  207  GLN   B OE1 1 
ATOM   15756 N  NE2 . GLN   B 1 207  ? 31.49600   86.19500  -49.06600 1.000 73.96400  ?  207  GLN   B NE2 1 
ATOM   15757 N  N   . LEU   B 1 208  ? 28.27600   87.35500  -43.94800 1.000 38.24099  ?  208  LEU   B N   1 
ATOM   15758 C  CA  . LEU   B 1 208  ? 27.55900   86.36000  -43.15900 1.000 37.47366  ?  208  LEU   B CA  1 
ATOM   15759 C  C   . LEU   B 1 208  ? 26.19400   86.86900  -42.72100 1.000 40.54980  ?  208  LEU   B C   1 
ATOM   15760 O  O   . LEU   B 1 208  ? 25.24800   86.08100  -42.60700 1.000 33.63479  ?  208  LEU   B O   1 
ATOM   15761 C  CB  . LEU   B 1 208  ? 28.38800   85.95700  -41.93900 1.000 35.28166  ?  208  LEU   B CB  1 
ATOM   15762 C  CG  . LEU   B 1 208  ? 29.67200   85.17500  -42.21500 1.000 34.13117  ?  208  LEU   B CG  1 
ATOM   15763 C  CD1 . LEU   B 1 208  ? 30.54300   85.11900  -40.97100 1.000 22.45152  ?  208  LEU   B CD1 1 
ATOM   15764 C  CD2 . LEU   B 1 208  ? 29.35200   83.77600  -42.71400 1.000 26.87662  ?  208  LEU   B CD2 1 
ATOM   15765 N  N   . PHE   B 1 209  ? 26.07000   88.17200  -42.46300 1.000 35.06460  ?  209  PHE   B N   1 
ATOM   15766 C  CA  . PHE   B 1 209  ? 24.76600   88.72500  -42.12200 1.000 30.16657  ?  209  PHE   B CA  1 
ATOM   15767 C  C   . PHE   B 1 209  ? 23.79500   88.56300  -43.28000 1.000 39.74171  ?  209  PHE   B C   1 
ATOM   15768 O  O   . PHE   B 1 209  ? 22.66600   88.08800  -43.10000 1.000 40.56594  ?  209  PHE   B O   1 
ATOM   15769 C  CB  . PHE   B 1 209  ? 24.89600   90.19700  -41.74000 1.000 38.70860  ?  209  PHE   B CB  1 
ATOM   15770 C  CG  . PHE   B 1 209  ? 23.57600   90.89300  -41.57200 1.000 38.61026  ?  209  PHE   B CG  1 
ATOM   15771 C  CD1 . PHE   B 1 209  ? 22.81300   90.69200  -40.43300 1.000 31.28821  ?  209  PHE   B CD1 1 
ATOM   15772 C  CD2 . PHE   B 1 209  ? 23.09600   91.74300  -42.55400 1.000 30.11112  ?  209  PHE   B CD2 1 
ATOM   15773 C  CE1 . PHE   B 1 209  ? 21.59900   91.33000  -40.27500 1.000 36.72084  ?  209  PHE   B CE1 1 
ATOM   15774 C  CE2 . PHE   B 1 209  ? 21.88300   92.38300  -42.40200 1.000 36.64871  ?  209  PHE   B CE2 1 
ATOM   15775 C  CZ  . PHE   B 1 209  ? 21.13300   92.17700  -41.26200 1.000 37.82590  ?  209  PHE   B CZ  1 
ATOM   15776 N  N   . GLU   B 1 210  ? 24.22300   88.95700  -44.48200 1.000 41.89076  ?  210  GLU   B N   1 
ATOM   15777 C  CA  . GLU   B 1 210  ? 23.38500   88.78400  -45.66300 1.000 36.46503  ?  210  GLU   B CA  1 
ATOM   15778 C  C   . GLU   B 1 210  ? 22.98700   87.32600  -45.84100 1.000 33.16609  ?  210  GLU   B C   1 
ATOM   15779 O  O   . GLU   B 1 210  ? 21.85500   87.02900  -46.23800 1.000 45.37282  ?  210  GLU   B O   1 
ATOM   15780 C  CB  . GLU   B 1 210  ? 24.11000   89.30600  -46.90400 1.000 28.07471  ?  210  GLU   B CB  1 
ATOM   15781 C  CG  . GLU   B 1 210  ? 24.13800   90.82800  -47.00300 1.000 32.68234  ?  210  GLU   B CG  1 
ATOM   15782 C  CD  . GLU   B 1 210  ? 25.16100   91.32400  -48.00300 1.000 43.72370  ?  210  GLU   B CD  1 
ATOM   15783 O  OE1 . GLU   B 1 210  ? 25.66900   90.48900  -48.77800 1.000 44.76600  ?  210  GLU   B OE1 1 
ATOM   15784 O  OE2 . GLU   B 1 210  ? 25.46600   92.53800  -48.00900 1.000 46.16578  -1 210  GLU   B OE2 1 
ATOM   15785 N  N   . GLN   B 1 211  ? 23.89700   86.40100  -45.53000 1.000 31.44285  ?  211  GLN   B N   1 
ATOM   15786 C  CA  . GLN   B 1 211  ? 23.56300   84.98400  -45.61100 1.000 35.92991  ?  211  GLN   B CA  1 
ATOM   15787 C  C   . GLN   B 1 211  ? 22.47800   84.62200  -44.60600 1.000 36.01235  ?  211  GLN   B C   1 
ATOM   15788 O  O   . GLN   B 1 211  ? 21.61900   83.77700  -44.88200 1.000 39.78157  ?  211  GLN   B O   1 
ATOM   15789 C  CB  . GLN   B 1 211  ? 24.81400   84.13800  -45.38600 1.000 42.66031  ?  211  GLN   B CB  1 
ATOM   15790 C  CG  . GLN   B 1 211  ? 24.68800   82.70300  -45.85700 1.000 62.45241  ?  211  GLN   B CG  1 
ATOM   15791 C  CD  . GLN   B 1 211  ? 26.00800   81.95700  -45.81300 1.000 87.74081  ?  211  GLN   B CD  1 
ATOM   15792 O  OE1 . GLN   B 1 211  ? 27.08100   82.56400  -45.81000 1.000 89.46255  ?  211  GLN   B OE1 1 
ATOM   15793 N  NE2 . GLN   B 1 211  ? 25.93600   80.63200  -45.76800 1.000 107.56398 ?  211  GLN   B NE2 1 
ATOM   15794 N  N   . GLN   B 1 212  ? 22.49600   85.25900  -43.43300 1.000 31.61161  ?  212  GLN   B N   1 
ATOM   15795 C  CA  . GLN   B 1 212  ? 21.45900   84.99200  -42.44200 1.000 40.48538  ?  212  GLN   B CA  1 
ATOM   15796 C  C   . GLN   B 1 212  ? 20.11800   85.56300  -42.87700 1.000 46.89713  ?  212  GLN   B C   1 
ATOM   15797 O  O   . GLN   B 1 212  ? 19.06900   84.99000  -42.56000 1.000 36.99425  ?  212  GLN   B O   1 
ATOM   15798 C  CB  . GLN   B 1 212  ? 21.87000   85.56100  -41.08300 1.000 26.72632  ?  212  GLN   B CB  1 
ATOM   15799 C  CG  . GLN   B 1 212  ? 20.87800   85.28900  -39.96200 1.000 31.91745  ?  212  GLN   B CG  1 
ATOM   15800 C  CD  . GLN   B 1 212  ? 20.71700   83.81000  -39.65300 1.000 44.70291  ?  212  GLN   B CD  1 
ATOM   15801 O  OE1 . GLN   B 1 212  ? 21.69900   83.07700  -39.52800 1.000 47.46084  ?  212  GLN   B OE1 1 
ATOM   15802 N  NE2 . GLN   B 1 212  ? 19.47100   83.36400  -39.52700 1.000 33.24836  ?  212  GLN   B NE2 1 
ATOM   15803 N  N   . VAL   B 1 213  ? 20.13400   86.68000  -43.60900 1.000 38.05293  ?  213  VAL   B N   1 
ATOM   15804 C  CA  . VAL   B 1 213  ? 18.89000   87.27500  -44.08700 1.000 35.19455  ?  213  VAL   B CA  1 
ATOM   15805 C  C   . VAL   B 1 213  ? 18.15400   86.30200  -44.99700 1.000 38.18526  ?  213  VAL   B C   1 
ATOM   15806 O  O   . VAL   B 1 213  ? 16.93400   86.13100  -44.89000 1.000 35.91921  ?  213  VAL   B O   1 
ATOM   15807 C  CB  . VAL   B 1 213  ? 19.17200   88.61200  -44.79800 1.000 41.12108  ?  213  VAL   B CB  1 
ATOM   15808 C  CG1 . VAL   B 1 213  ? 17.89300   89.16400  -45.39700 1.000 25.56869  ?  213  VAL   B CG1 1 
ATOM   15809 C  CG2 . VAL   B 1 213  ? 19.80000   89.61800  -43.83400 1.000 37.56653  ?  213  VAL   B CG2 1 
ATOM   15810 N  N   . GLU   B 1 214  ? 18.88500   85.63700  -45.89600 1.000 44.75513  ?  214  GLU   B N   1 
ATOM   15811 C  CA  . GLU   B 1 214  ? 18.26600   84.67400  -46.80000 1.000 46.40437  ?  214  GLU   B CA  1 
ATOM   15812 C  C   . GLU   B 1 214  ? 17.64900   83.49800  -46.05700 1.000 35.42579  ?  214  GLU   B C   1 
ATOM   15813 O  O   . GLU   B 1 214  ? 16.72200   82.86900  -46.57900 1.000 42.39071  ?  214  GLU   B O   1 
ATOM   15814 C  CB  . GLU   B 1 214  ? 19.29500   84.17200  -47.82100 1.000 30.14841  ?  214  GLU   B CB  1 
ATOM   15815 C  CG  . GLU   B 1 214  ? 19.12300   84.75700  -49.22400 1.000 47.39666  ?  214  GLU   B CG  1 
ATOM   15816 C  CD  . GLU   B 1 214  ? 19.30700   86.26400  -49.26000 1.000 63.50108  ?  214  GLU   B CD  1 
ATOM   15817 O  OE1 . GLU   B 1 214  ? 20.14800   86.77200  -48.48900 1.000 58.02852  ?  214  GLU   B OE1 1 
ATOM   15818 O  OE2 . GLU   B 1 214  ? 18.60800   86.93800  -50.05400 1.000 58.93331  -1 214  GLU   B OE2 1 
ATOM   15819 N  N   . MET   B 1 215  ? 18.12600   83.19700  -44.85000 1.000 38.88981  ?  215  MET   B N   1 
ATOM   15820 C  CA  . MET   B 1 215  ? 17.63500   82.04400  -44.10600 1.000 50.63221  ?  215  MET   B CA  1 
ATOM   15821 C  C   . MET   B 1 215  ? 16.45900   82.37400  -43.19900 1.000 51.61733  ?  215  MET   B C   1 
ATOM   15822 O  O   . MET   B 1 215  ? 15.57700   81.52800  -43.01200 1.000 62.12716  ?  215  MET   B O   1 
ATOM   15823 C  CB  . MET   B 1 215  ? 18.76500   81.43700  -43.27100 1.000 52.69332  ?  215  MET   B CB  1 
ATOM   15824 C  CG  . MET   B 1 215  ? 19.76000   80.62500  -44.07600 1.000 43.23204  ?  215  MET   B CG  1 
ATOM   15825 S  SD  . MET   B 1 215  ? 20.20300   79.09900  -43.22800 1.000 105.48573 ?  215  MET   B SD  1 
ATOM   15826 C  CE  . MET   B 1 215  ? 18.80400   78.05600  -43.64300 1.000 57.59152  ?  215  MET   B CE  1 
ATOM   15827 N  N   . THR   B 1 216  ? 16.43200   83.57400  -42.62100 1.000 45.51522  ?  216  THR   B N   1 
ATOM   15828 C  CA  . THR   B 1 216  ? 15.34100   84.02300  -41.75600 1.000 31.62003  ?  216  THR   B CA  1 
ATOM   15829 C  C   . THR   B 1 216  ? 14.92600   85.42500  -42.18400 1.000 42.37130  ?  216  THR   B C   1 
ATOM   15830 O  O   . THR   B 1 216  ? 15.15000   86.40200  -41.46000 1.000 41.54077  ?  216  THR   B O   1 
ATOM   15831 C  CB  . THR   B 1 216  ? 15.75400   84.00300  -40.28300 1.000 37.48957  ?  216  THR   B CB  1 
ATOM   15832 O  OG1 . THR   B 1 216  ? 16.97100   84.74000  -40.10900 1.000 49.67276  ?  216  THR   B OG1 1 
ATOM   15833 C  CG2 . THR   B 1 216  ? 15.95800   82.57400  -39.80200 1.000 43.08502  ?  216  THR   B CG2 1 
ATOM   15834 N  N   . PRO   B 1 217  ? 14.30300   85.55700  -43.36100 1.000 45.77633  ?  217  PRO   B N   1 
ATOM   15835 C  CA  . PRO   B 1 217  ? 14.00900   86.90600  -43.87400 1.000 33.69456  ?  217  PRO   B CA  1 
ATOM   15836 C  C   . PRO   B 1 217  ? 12.94200   87.63100  -43.08200 1.000 39.69716  ?  217  PRO   B C   1 
ATOM   15837 O  O   . PRO   B 1 217  ? 13.03100   88.85200  -42.90300 1.000 35.61493  ?  217  PRO   B O   1 
ATOM   15838 C  CB  . PRO   B 1 217  ? 13.55700   86.64600  -45.32100 1.000 26.12700  ?  217  PRO   B CB  1 
ATOM   15839 C  CG  . PRO   B 1 217  ? 13.84100   85.18600  -45.58800 1.000 38.07053  ?  217  PRO   B CG  1 
ATOM   15840 C  CD  . PRO   B 1 217  ? 13.79800   84.51000  -44.26100 1.000 45.07081  ?  217  PRO   B CD  1 
ATOM   15841 N  N   . ASP   B 1 218  ? 11.92900   86.91600  -42.60400 1.000 37.68185  ?  218  ASP   B N   1 
ATOM   15842 C  CA  . ASP   B 1 218  ? 10.78100   87.54100  -41.96900 1.000 38.18002  ?  218  ASP   B CA  1 
ATOM   15843 C  C   . ASP   B 1 218  ? 10.84900   87.51200  -40.44800 1.000 42.24395  ?  218  ASP   B C   1 
ATOM   15844 O  O   . ASP   B 1 218  ? 9.93400    88.02000  -39.79300 1.000 43.35753  ?  218  ASP   B O   1 
ATOM   15845 C  CB  . ASP   B 1 218  ? 9.49000    86.87300  -42.45700 1.000 37.39787  ?  218  ASP   B CB  1 
ATOM   15846 C  CG  . ASP   B 1 218  ? 9.37900    86.85100  -43.98000 1.000 41.72333  ?  218  ASP   B CG  1 
ATOM   15847 O  OD1 . ASP   B 1 218  ? 9.83100    87.81700  -44.63500 1.000 38.41371  ?  218  ASP   B OD1 1 
ATOM   15848 O  OD2 . ASP   B 1 218  ? 8.84100    85.86300  -44.52300 1.000 44.95633  -1 218  ASP   B OD2 1 
ATOM   15849 N  N   . HIS   B 1 219  ? 11.90200   86.93900  -39.87100 1.000 42.64027  ?  219  HIS   B N   1 
ATOM   15850 C  CA  . HIS   B 1 219  ? 12.07500   86.99400  -38.42700 1.000 38.15491  ?  219  HIS   B CA  1 
ATOM   15851 C  C   . HIS   B 1 219  ? 12.34700   88.42700  -37.98400 1.000 40.45236  ?  219  HIS   B C   1 
ATOM   15852 O  O   . HIS   B 1 219  ? 12.93700   89.22500  -38.71500 1.000 39.09079  ?  219  HIS   B O   1 
ATOM   15853 C  CB  . HIS   B 1 219  ? 13.22700   86.09300  -37.98200 1.000 33.88187  ?  219  HIS   B CB  1 
ATOM   15854 C  CG  . HIS   B 1 219  ? 12.88700   84.63500  -37.95100 1.000 39.23726  ?  219  HIS   B CG  1 
ATOM   15855 N  ND1 . HIS   B 1 219  ? 12.60100   83.91000  -39.08800 1.000 40.99730  ?  219  HIS   B ND1 1 
ATOM   15856 C  CD2 . HIS   B 1 219  ? 12.80200   83.76300  -36.91800 1.000 36.89702  ?  219  HIS   B CD2 1 
ATOM   15857 C  CE1 . HIS   B 1 219  ? 12.35000   82.65600  -38.75700 1.000 19.96926  ?  219  HIS   B CE1 1 
ATOM   15858 N  NE2 . HIS   B 1 219  ? 12.46400   82.54100  -37.44600 1.000 44.54048  ?  219  HIS   B NE2 1 
ATOM   15859 N  N   . VAL   B 1 220  ? 11.91200   88.75000  -36.76800 1.000 35.64612  ?  220  VAL   B N   1 
ATOM   15860 C  CA  . VAL   B 1 220  ? 12.18700   90.06500  -36.20500 1.000 41.14412  ?  220  VAL   B CA  1 
ATOM   15861 C  C   . VAL   B 1 220  ? 13.67300   90.18000  -35.89300 1.000 45.66284  ?  220  VAL   B C   1 
ATOM   15862 O  O   . VAL   B 1 220  ? 14.25500   89.30800  -35.23400 1.000 46.28149  ?  220  VAL   B O   1 
ATOM   15863 C  CB  . VAL   B 1 220  ? 11.33500   90.29800  -34.95100 1.000 35.73274  ?  220  VAL   B CB  1 
ATOM   15864 C  CG1 . VAL   B 1 220  ? 11.63500   91.66200  -34.35200 1.000 38.38122  ?  220  VAL   B CG1 1 
ATOM   15865 C  CG2 . VAL   B 1 220  ? 9.86200    90.16100  -35.29200 1.000 41.51670  ?  220  VAL   B CG2 1 
ATOM   15866 N  N   . ALA   B 1 221  ? 14.29600   91.26100  -36.36500 1.000 39.28931  ?  221  ALA   B N   1 
ATOM   15867 C  CA  . ALA   B 1 221  ? 15.72400   91.48800  -36.16800 1.000 32.99369  ?  221  ALA   B CA  1 
ATOM   15868 C  C   . ALA   B 1 221  ? 16.01100   92.55300  -35.11500 1.000 33.19150  ?  221  ALA   B C   1 
ATOM   15869 O  O   . ALA   B 1 221  ? 16.86000   92.34600  -34.24300 1.000 38.04583  ?  221  ALA   B O   1 
ATOM   15870 C  CB  . ALA   B 1 221  ? 16.38600   91.87300  -37.49500 1.000 31.01857  ?  221  ALA   B CB  1 
ATOM   15871 N  N   . VAL   B 1 222  ? 15.32900   93.69500  -35.18200 1.000 29.24102  ?  222  VAL   B N   1 
ATOM   15872 C  CA  . VAL   B 1 222  ? 15.49700   94.77400  -34.21400 1.000 37.35084  ?  222  VAL   B CA  1 
ATOM   15873 C  C   . VAL   B 1 222  ? 14.12900   95.20500  -33.70400 1.000 43.48569  ?  222  VAL   B C   1 
ATOM   15874 O  O   . VAL   B 1 222  ? 13.15800   95.26100  -34.46700 1.000 43.84319  ?  222  VAL   B O   1 
ATOM   15875 C  CB  . VAL   B 1 222  ? 16.24300   95.98200  -34.81600 1.000 24.95607  ?  222  VAL   B CB  1 
ATOM   15876 C  CG1 . VAL   B 1 222  ? 16.77300   96.88500  -33.70900 1.000 32.59686  ?  222  VAL   B CG1 1 
ATOM   15877 C  CG2 . VAL   B 1 222  ? 17.37000   95.52200  -35.72000 1.000 23.13821  ?  222  VAL   B CG2 1 
ATOM   15878 N  N   . VAL   B 1 223  ? 14.05900   95.52000  -32.41300 1.000 43.00254  ?  223  VAL   B N   1 
ATOM   15879 C  CA  . VAL   B 1 223  ? 12.85600   96.05300  -31.78300 1.000 34.36960  ?  223  VAL   B CA  1 
ATOM   15880 C  C   . VAL   B 1 223  ? 13.24400   97.33000  -31.04900 1.000 38.83571  ?  223  VAL   B C   1 
ATOM   15881 O  O   . VAL   B 1 223  ? 14.13700   97.30900  -30.19300 1.000 39.85600  ?  223  VAL   B O   1 
ATOM   15882 C  CB  . VAL   B 1 223  ? 12.21400   95.04400  -30.81500 1.000 30.14643  ?  223  VAL   B CB  1 
ATOM   15883 C  CG1 . VAL   B 1 223  ? 11.29000   95.75700  -29.84700 1.000 30.02319  ?  223  VAL   B CG1 1 
ATOM   15884 C  CG2 . VAL   B 1 223  ? 11.45800   93.97400  -31.58600 1.000 37.58990  ?  223  VAL   B CG2 1 
ATOM   15885 N  N   . ASP   B 1 224  ? 12.58300   98.43600  -31.38600 1.000 42.61312  ?  224  ASP   B N   1 
ATOM   15886 C  CA  . ASP   B 1 224  ? 12.84100   99.72400  -30.75000 1.000 40.47491  ?  224  ASP   B CA  1 
ATOM   15887 C  C   . ASP   B 1 224  ? 11.51000   100.37500 -30.41200 1.000 56.87122  ?  224  ASP   B C   1 
ATOM   15888 O  O   . ASP   B 1 224  ? 10.68800   100.60500 -31.30500 1.000 56.04640  ?  224  ASP   B O   1 
ATOM   15889 C  CB  . ASP   B 1 224  ? 13.66900   100.63700 -31.65800 1.000 48.75913  ?  224  ASP   B CB  1 
ATOM   15890 C  CG  . ASP   B 1 224  ? 14.01900   101.95600 -30.99500 1.000 56.27074  ?  224  ASP   B CG  1 
ATOM   15891 O  OD1 . ASP   B 1 224  ? 14.09000   101.99700 -29.74700 1.000 43.17876  ?  224  ASP   B OD1 1 
ATOM   15892 O  OD2 . ASP   B 1 224  ? 14.22400   102.95200 -31.72300 1.000 58.06901  -1 224  ASP   B OD2 1 
ATOM   15893 N  N   . ARG   B 1 225  ? 11.31100   100.68300 -29.12800 1.000 70.99290  ?  225  ARG   B N   1 
ATOM   15894 C  CA  . ARG   B 1 225  ? 10.05000   101.21900 -28.62800 1.000 58.48914  ?  225  ARG   B CA  1 
ATOM   15895 C  C   . ARG   B 1 225  ? 8.89900    100.30100 -29.01600 1.000 60.36814  ?  225  ARG   B C   1 
ATOM   15896 O  O   . ARG   B 1 225  ? 8.76300    99.19700  -28.47900 1.000 57.71561  ?  225  ARG   B O   1 
ATOM   15897 C  CB  . ARG   B 1 225  ? 9.79900    102.63600 -29.15500 1.000 63.08597  ?  225  ARG   B CB  1 
ATOM   15898 C  CG  . ARG   B 1 225  ? 10.95300   103.62200 -28.97500 1.000 73.06196  ?  225  ARG   B CG  1 
ATOM   15899 C  CD  . ARG   B 1 225  ? 11.63200   103.50000 -27.61200 1.000 68.97693  ?  225  ARG   B CD  1 
ATOM   15900 N  NE  . ARG   B 1 225  ? 12.38900   104.69700 -27.25600 1.000 83.02549  ?  225  ARG   B NE  1 
ATOM   15901 C  CZ  . ARG   B 1 225  ? 13.51300   105.09000 -27.84400 1.000 79.40158  ?  225  ARG   B CZ  1 
ATOM   15902 N  NH1 . ARG   B 1 225  ? 14.05500   104.40200 -28.83600 1.000 61.00862  ?  225  ARG   B NH1 1 
ATOM   15903 N  NH2 . ARG   B 1 225  ? 14.11100   106.20000 -27.42200 1.000 81.21981  ?  225  ARG   B NH2 1 
ATOM   15904 N  N   . GLY   B 1 226  ? 8.07700    100.74000 -29.96200 1.000 60.23391  ?  226  GLY   B N   1 
ATOM   15905 C  CA  . GLY   B 1 226  ? 6.95900    99.93100  -30.40000 1.000 72.60774  ?  226  GLY   B CA  1 
ATOM   15906 C  C   . GLY   B 1 226  ? 7.14500    99.31400  -31.77100 1.000 64.37274  ?  226  GLY   B C   1 
ATOM   15907 O  O   . GLY   B 1 226  ? 6.49600    98.31600  -32.09200 1.000 66.02218  ?  226  GLY   B O   1 
ATOM   15908 N  N   . GLN   B 1 227  ? 8.02500    99.89000  -32.58600 1.000 62.49947  ?  227  GLN   B N   1 
ATOM   15909 C  CA  . GLN   B 1 227  ? 8.22200    99.44400  -33.95800 1.000 59.38682  ?  227  GLN   B CA  1 
ATOM   15910 C  C   . GLN   B 1 227  ? 9.21200    98.28000  -34.02200 1.000 51.84677  ?  227  GLN   B C   1 
ATOM   15911 O  O   . GLN   B 1 227  ? 9.88700    97.94300  -33.04700 1.000 46.80654  ?  227  GLN   B O   1 
ATOM   15912 C  CB  . GLN   B 1 227  ? 8.70200    100.60600 -34.82900 1.000 55.39049  ?  227  GLN   B CB  1 
ATOM   15913 C  CG  . GLN   B 1 227  ? 7.86200    101.86900 -34.70100 1.000 67.82411  ?  227  GLN   B CG  1 
ATOM   15914 C  CD  . GLN   B 1 227  ? 8.40300    102.82600 -33.65500 1.000 87.31243  ?  227  GLN   B CD  1 
ATOM   15915 O  OE1 . GLN   B 1 227  ? 9.61500    102.92600 -33.45600 1.000 80.35614  ?  227  GLN   B OE1 1 
ATOM   15916 N  NE2 . GLN   B 1 227  ? 7.50500    103.53600 -32.97900 1.000 79.40404  ?  227  GLN   B NE2 1 
ATOM   15917 N  N   . SER   B 1 228  ? 9.29400    97.66100  -35.19900 1.000 46.36300  ?  228  SER   B N   1 
ATOM   15918 C  CA  . SER   B 1 228  ? 10.15900   96.50700  -35.39200 1.000 32.38022  ?  228  SER   B CA  1 
ATOM   15919 C  C   . SER   B 1 228  ? 10.65200   96.46100  -36.83000 1.000 48.87084  ?  228  SER   B C   1 
ATOM   15920 O  O   . SER   B 1 228  ? 10.09400   97.10000  -37.72600 1.000 49.74790  ?  228  SER   B O   1 
ATOM   15921 C  CB  . SER   B 1 228  ? 9.44100    95.20300  -35.04300 1.000 28.27124  ?  228  SER   B CB  1 
ATOM   15922 O  OG  . SER   B 1 228  ? 9.07400    95.19800  -33.67900 1.000 51.14056  ?  228  SER   B OG  1 
ATOM   15923 N  N   . LEU   B 1 229  ? 11.71200   95.68500  -37.03700 1.000 43.11684  ?  229  LEU   B N   1 
ATOM   15924 C  CA  . LEU   B 1 229  ? 12.29400   95.48300  -38.35500 1.000 33.93792  ?  229  LEU   B CA  1 
ATOM   15925 C  C   . LEU   B 1 229  ? 12.63400   94.01200  -38.50800 1.000 35.39154  ?  229  LEU   B C   1 
ATOM   15926 O  O   . LEU   B 1 229  ? 13.28200   93.43100  -37.63300 1.000 33.26984  ?  229  LEU   B O   1 
ATOM   15927 C  CB  . LEU   B 1 229  ? 13.55600   96.32900  -38.54600 1.000 34.51266  ?  229  LEU   B CB  1 
ATOM   15928 C  CG  . LEU   B 1 229  ? 13.38900   97.82500  -38.78200 1.000 33.63544  ?  229  LEU   B CG  1 
ATOM   15929 C  CD1 . LEU   B 1 229  ? 14.75400   98.50800  -38.79500 1.000 21.89108  ?  229  LEU   B CD1 1 
ATOM   15930 C  CD2 . LEU   B 1 229  ? 12.64000   98.05900  -40.08100 1.000 32.11876  ?  229  LEU   B CD2 1 
ATOM   15931 N  N   . THR   B 1 230  ? 12.19400   93.41100  -39.60700 1.000 37.85275  ?  230  THR   B N   1 
ATOM   15932 C  CA  . THR   B 1 230  ? 12.61000   92.05000  -39.88700 1.000 33.99978  ?  230  THR   B CA  1 
ATOM   15933 C  C   . THR   B 1 230  ? 14.00700   92.05000  -40.49700 1.000 37.97608  ?  230  THR   B C   1 
ATOM   15934 O  O   . THR   B 1 230  ? 14.54600   93.08900  -40.89000 1.000 31.62978  ?  230  THR   B O   1 
ATOM   15935 C  CB  . THR   B 1 230  ? 11.62300   91.35300  -40.82000 1.000 36.43043  ?  230  THR   B CB  1 
ATOM   15936 O  OG1 . THR   B 1 230  ? 11.68700   91.95100  -42.12000 1.000 37.61393  ?  230  THR   B OG1 1 
ATOM   15937 C  CG2 . THR   B 1 230  ? 10.20800   91.46100  -40.27400 1.000 26.55523  ?  230  THR   B CG2 1 
ATOM   15938 N  N   . TYR   B 1 231  ? 14.60200   90.85800  -40.56600 1.000 43.45514  ?  231  TYR   B N   1 
ATOM   15939 C  CA  . TYR   B 1 231  ? 15.93400   90.73600  -41.14600 1.000 34.33361  ?  231  TYR   B CA  1 
ATOM   15940 C  C   . TYR   B 1 231  ? 15.95300   91.23100  -42.58600 1.000 37.91936  ?  231  TYR   B C   1 
ATOM   15941 O  O   . TYR   B 1 231  ? 16.89900   91.90700  -43.00700 1.000 43.07287  ?  231  TYR   B O   1 
ATOM   15942 C  CB  . TYR   B 1 231  ? 16.41000   89.28800  -41.06700 1.000 28.00361  ?  231  TYR   B CB  1 
ATOM   15943 C  CG  . TYR   B 1 231  ? 17.10000   88.93900  -39.77000 1.000 36.45453  ?  231  TYR   B CG  1 
ATOM   15944 C  CD1 . TYR   B 1 231  ? 16.37000   88.56200  -38.65100 1.000 37.22294  ?  231  TYR   B CD1 1 
ATOM   15945 C  CD2 . TYR   B 1 231  ? 18.48500   88.97900  -39.66700 1.000 33.46521  ?  231  TYR   B CD2 1 
ATOM   15946 C  CE1 . TYR   B 1 231  ? 16.99800   88.24000  -37.46300 1.000 37.10282  ?  231  TYR   B CE1 1 
ATOM   15947 C  CE2 . TYR   B 1 231  ? 19.12300   88.65700  -38.48500 1.000 26.36125  ?  231  TYR   B CE2 1 
ATOM   15948 C  CZ  . TYR   B 1 231  ? 18.37500   88.28900  -37.38500 1.000 41.14505  ?  231  TYR   B CZ  1 
ATOM   15949 O  OH  . TYR   B 1 231  ? 19.00300   87.97000  -36.20300 1.000 30.11816  ?  231  TYR   B OH  1 
ATOM   15950 N  N   . LYS   B 1 232  ? 14.90700   90.91700  -43.35300 1.000 40.27266  ?  232  LYS   B N   1 
ATOM   15951 C  CA  . LYS   B 1 232  ? 14.83500   91.39000  -44.73100 1.000 36.15098  ?  232  LYS   B CA  1 
ATOM   15952 C  C   . LYS   B 1 232  ? 14.70500   92.90800  -44.78800 1.000 35.34979  ?  232  LYS   B C   1 
ATOM   15953 O  O   . LYS   B 1 232  ? 15.29300   93.55400  -45.66200 1.000 39.89238  ?  232  LYS   B O   1 
ATOM   15954 C  CB  . LYS   B 1 232  ? 13.66500   90.72000  -45.45100 1.000 28.09679  ?  232  LYS   B CB  1 
ATOM   15955 C  CG  . LYS   B 1 232  ? 13.38700   91.26500  -46.83700 1.000 33.16585  ?  232  LYS   B CG  1 
ATOM   15956 C  CD  . LYS   B 1 232  ? 12.51300   90.30800  -47.62600 1.000 45.38849  ?  232  LYS   B CD  1 
ATOM   15957 C  CE  . LYS   B 1 232  ? 11.89200   91.00200  -48.81800 1.000 56.85615  ?  232  LYS   B CE  1 
ATOM   15958 N  NZ  . LYS   B 1 232  ? 10.82700   91.93000  -48.36100 1.000 65.51734  ?  232  LYS   B NZ  1 
ATOM   15959 N  N   . GLN   B 1 233  ? 13.94900   93.49600  -43.85800 1.000 35.26517  ?  233  GLN   B N   1 
ATOM   15960 C  CA  . GLN   B 1 233  ? 13.75800   94.94300  -43.87300 1.000 39.18778  ?  233  GLN   B CA  1 
ATOM   15961 C  C   . GLN   B 1 233  ? 15.01800   95.67400  -43.43200 1.000 36.60918  ?  233  GLN   B C   1 
ATOM   15962 O  O   . GLN   B 1 233  ? 15.38800   96.69600  -44.02100 1.000 31.84252  ?  233  GLN   B O   1 
ATOM   15963 C  CB  . GLN   B 1 233  ? 12.57500   95.32200  -42.98600 1.000 32.97365  ?  233  GLN   B CB  1 
ATOM   15964 C  CG  . GLN   B 1 233  ? 11.25400   94.77200  -43.48700 1.000 42.56425  ?  233  GLN   B CG  1 
ATOM   15965 C  CD  . GLN   B 1 233  ? 10.17500   94.78800  -42.42900 1.000 44.01663  ?  233  GLN   B CD  1 
ATOM   15966 O  OE1 . GLN   B 1 233  ? 10.44500   94.59000  -41.24400 1.000 46.93052  ?  233  GLN   B OE1 1 
ATOM   15967 N  NE2 . GLN   B 1 233  ? 8.94000    95.03600  -42.85000 1.000 46.10506  ?  233  GLN   B NE2 1 
ATOM   15968 N  N   . LEU   B 1 234  ? 15.68700   95.16800  -42.39400 1.000 40.69928  ?  234  LEU   B N   1 
ATOM   15969 C  CA  . LEU   B 1 234  ? 16.94400   95.76900  -41.96200 1.000 30.48776  ?  234  LEU   B CA  1 
ATOM   15970 C  C   . LEU   B 1 234  ? 17.98800   95.70600  -43.06800 1.000 43.21821  ?  234  LEU   B C   1 
ATOM   15971 O  O   . LEU   B 1 234  ? 18.70200   96.68600  -43.31600 1.000 37.42767  ?  234  LEU   B O   1 
ATOM   15972 C  CB  . LEU   B 1 234  ? 17.44400   95.06600  -40.70100 1.000 31.51578  ?  234  LEU   B CB  1 
ATOM   15973 C  CG  . LEU   B 1 234  ? 18.85400   95.38300  -40.20500 1.000 36.79380  ?  234  LEU   B CG  1 
ATOM   15974 C  CD1 . LEU   B 1 234  ? 19.01300   96.87100  -39.92700 1.000 32.09973  ?  234  LEU   B CD1 1 
ATOM   15975 C  CD2 . LEU   B 1 234  ? 19.16300   94.55800  -38.96300 1.000 21.53043  ?  234  LEU   B CD2 1 
ATOM   15976 N  N   . ASN   B 1 235  ? 18.08100   94.56200  -43.75300 1.000 38.39982  ?  235  ASN   B N   1 
ATOM   15977 C  CA  . ASN   B 1 235  ? 19.04800   94.41400  -44.83600 1.000 30.38091  ?  235  ASN   B CA  1 
ATOM   15978 C  C   . ASN   B 1 235  ? 18.74200   95.37200  -45.97800 1.000 44.36668  ?  235  ASN   B C   1 
ATOM   15979 O  O   . ASN   B 1 235  ? 19.62700   96.09300  -46.45400 1.000 48.29650  ?  235  ASN   B O   1 
ATOM   15980 C  CB  . ASN   B 1 235  ? 19.05400   92.96800  -45.33500 1.000 36.54696  ?  235  ASN   B CB  1 
ATOM   15981 C  CG  . ASN   B 1 235  ? 20.26500   92.65200  -46.19400 1.000 38.15910  ?  235  ASN   B CG  1 
ATOM   15982 O  OD1 . ASN   B 1 235  ? 21.40100   92.91300  -45.80600 1.000 47.40782  ?  235  ASN   B OD1 1 
ATOM   15983 N  ND2 . ASN   B 1 235  ? 20.02400   92.08400  -47.36900 1.000 39.02139  ?  235  ASN   B ND2 1 
ATOM   15984 N  N   . GLU   B 1 236  ? 17.48400   95.39400  -46.42900 1.000 44.32110  ?  236  GLU   B N   1 
ATOM   15985 C  CA  . GLU   B 1 236  ? 17.10600   96.26400  -47.53700 1.000 34.79224  ?  236  GLU   B CA  1 
ATOM   15986 C  C   . GLU   B 1 236  ? 17.31000   97.73200  -47.18200 1.000 41.19078  ?  236  GLU   B C   1 
ATOM   15987 O  O   . GLU   B 1 236  ? 17.84000   98.50400  -47.98900 1.000 37.90103  ?  236  GLU   B O   1 
ATOM   15988 C  CB  . GLU   B 1 236  ? 15.65300   96.00600  -47.93900 1.000 31.78681  ?  236  GLU   B CB  1 
ATOM   15989 C  CG  . GLU   B 1 236  ? 15.42900   94.69800  -48.68700 1.000 39.85775  ?  236  GLU   B CG  1 
ATOM   15990 C  CD  . GLU   B 1 236  ? 14.04600   94.60800  -49.30900 1.000 57.74749  ?  236  GLU   B CD  1 
ATOM   15991 O  OE1 . GLU   B 1 236  ? 13.15800   95.39300  -48.91100 1.000 56.25021  ?  236  GLU   B OE1 1 
ATOM   15992 O  OE2 . GLU   B 1 236  ? 13.84600   93.75400  -50.19900 1.000 70.63842  -1 236  GLU   B OE2 1 
ATOM   15993 N  N   . ARG   B 1 237  ? 16.90400   98.13400  -45.97500 1.000 36.75281  ?  237  ARG   B N   1 
ATOM   15994 C  CA  . ARG   B 1 237  ? 17.07500   99.52600  -45.57200 1.000 42.13170  ?  237  ARG   B CA  1 
ATOM   15995 C  C   . ARG   B 1 237  ? 18.55000   99.89200  -45.46400 1.000 42.89299  ?  237  ARG   B C   1 
ATOM   15996 O  O   . ARG   B 1 237  ? 18.94600   101.00900 -45.81800 1.000 42.71598  ?  237  ARG   B O   1 
ATOM   15997 C  CB  . ARG   B 1 237  ? 16.35500   99.78800  -44.25000 1.000 31.66457  ?  237  ARG   B CB  1 
ATOM   15998 C  CG  . ARG   B 1 237  ? 16.03500   101.25400 -44.01200 1.000 39.55318  ?  237  ARG   B CG  1 
ATOM   15999 C  CD  . ARG   B 1 237  ? 15.18300   101.81700 -45.14200 1.000 64.73450  ?  237  ARG   B CD  1 
ATOM   16000 N  NE  . ARG   B 1 237  ? 15.16400   103.27500 -45.14600 1.000 61.49604  ?  237  ARG   B NE  1 
ATOM   16001 C  CZ  . ARG   B 1 237  ? 14.46600   104.01500 -45.99700 1.000 63.44759  ?  237  ARG   B CZ  1 
ATOM   16002 N  NH1 . ARG   B 1 237  ? 13.71500   103.46400 -46.93800 1.000 67.34977  ?  237  ARG   B NH1 1 
ATOM   16003 N  NH2 . ARG   B 1 237  ? 14.52500   105.34100 -45.90400 1.000 46.35486  ?  237  ARG   B NH2 1 
ATOM   16004 N  N   . ALA   B 1 238  ? 19.38100   98.96300  -44.98700 1.000 44.16537  ?  238  ALA   B N   1 
ATOM   16005 C  CA  . ALA   B 1 238  ? 20.81400   99.22800  -44.92900 1.000 40.43386  ?  238  ALA   B CA  1 
ATOM   16006 C  C   . ALA   B 1 238  ? 21.41500   99.30400  -46.32600 1.000 43.79585  ?  238  ALA   B C   1 
ATOM   16007 O  O   . ALA   B 1 238  ? 22.25700   100.16800 -46.59800 1.000 41.60941  ?  238  ALA   B O   1 
ATOM   16008 C  CB  . ALA   B 1 238  ? 21.51700   98.15600  -44.09800 1.000 39.50416  ?  238  ALA   B CB  1 
ATOM   16009 N  N   . ASN   B 1 239  ? 20.98800   98.41200  -47.22500 1.000 38.02562  ?  239  ASN   B N   1 
ATOM   16010 C  CA  . ASN   B 1 239  ? 21.50600   98.42500  -48.59000 1.000 41.84812  ?  239  ASN   B CA  1 
ATOM   16011 C  C   . ASN   B 1 239  ? 21.25900   99.76900  -49.26300 1.000 54.17122  ?  239  ASN   B C   1 
ATOM   16012 O  O   . ASN   B 1 239  ? 22.09500   100.24700 -50.03900 1.000 52.28392  ?  239  ASN   B O   1 
ATOM   16013 C  CB  . ASN   B 1 239  ? 20.87300   97.29700  -49.40300 1.000 42.24076  ?  239  ASN   B CB  1 
ATOM   16014 C  CG  . ASN   B 1 239  ? 21.46600   95.94500  -49.07700 1.000 40.46967  ?  239  ASN   B CG  1 
ATOM   16015 O  OD1 . ASN   B 1 239  ? 22.53400   95.85800  -48.47400 1.000 50.38334  ?  239  ASN   B OD1 1 
ATOM   16016 N  ND2 . ASN   B 1 239  ? 20.77800   94.88100  -49.47600 1.000 34.62340  ?  239  ASN   B ND2 1 
ATOM   16017 N  N   . GLN   B 1 240  ? 20.11700   100.39600 -48.97200 1.000 50.77517  ?  240  GLN   B N   1 
ATOM   16018 C  CA  . GLN   B 1 240  ? 19.81400   101.69400 -49.56200 1.000 45.26198  ?  240  GLN   B CA  1 
ATOM   16019 C  C   . GLN   B 1 240  ? 20.82400   102.74200 -49.11600 1.000 44.36272  ?  240  GLN   B C   1 
ATOM   16020 O  O   . GLN   B 1 240  ? 21.35000   103.50600 -49.93400 1.000 49.43473  ?  240  GLN   B O   1 
ATOM   16021 C  CB  . GLN   B 1 240  ? 18.39000   102.11400 -49.19400 1.000 56.48649  ?  240  GLN   B CB  1 
ATOM   16022 C  CG  . GLN   B 1 240  ? 17.31100   101.18900 -49.74400 1.000 54.79154  ?  240  GLN   B CG  1 
ATOM   16023 C  CD  . GLN   B 1 240  ? 15.91300   101.58200 -49.30300 1.000 53.02475  ?  240  GLN   B CD  1 
ATOM   16024 O  OE1 . GLN   B 1 240  ? 15.49900   102.73200 -49.45700 1.000 51.06500  ?  240  GLN   B OE1 1 
ATOM   16025 N  NE2 . GLN   B 1 240  ? 15.17600   100.62500 -48.75000 1.000 52.44260  ?  240  GLN   B NE2 1 
ATOM   16026 N  N   . LEU   B 1 241  ? 21.11800   102.78500 -47.81600 1.000 48.30595  ?  241  LEU   B N   1 
ATOM   16027 C  CA  . LEU   B 1 241  ? 22.10500   103.73600 -47.32100 1.000 42.23085  ?  241  LEU   B CA  1 
ATOM   16028 C  C   . LEU   B 1 241  ? 23.51200   103.36500 -47.77100 1.000 45.94846  ?  241  LEU   B C   1 
ATOM   16029 O  O   . LEU   B 1 241  ? 24.37000   104.24500 -47.90500 1.000 46.39335  ?  241  LEU   B O   1 
ATOM   16030 C  CB  . LEU   B 1 241  ? 22.02800   103.82000 -45.79700 1.000 34.72055  ?  241  LEU   B CB  1 
ATOM   16031 C  CG  . LEU   B 1 241  ? 22.85000   104.91800 -45.11900 1.000 39.49950  ?  241  LEU   B CG  1 
ATOM   16032 C  CD1 . LEU   B 1 241  ? 22.49800   106.28200 -45.68400 1.000 41.43929  ?  241  LEU   B CD1 1 
ATOM   16033 C  CD2 . LEU   B 1 241  ? 22.63800   104.89400 -43.61700 1.000 38.37160  ?  241  LEU   B CD2 1 
ATOM   16034 N  N   . ALA   B 1 242  ? 23.76400   102.07800 -48.02200 1.000 36.20639  ?  242  ALA   B N   1 
ATOM   16035 C  CA  . ALA   B 1 242  ? 25.09100   101.65400 -48.45600 1.000 37.19593  ?  242  ALA   B CA  1 
ATOM   16036 C  C   . ALA   B 1 242  ? 25.37800   102.11800 -49.87800 1.000 47.22090  ?  242  ALA   B C   1 
ATOM   16037 O  O   . ALA   B 1 242  ? 26.46200   102.64400 -50.16300 1.000 36.14108  ?  242  ALA   B O   1 
ATOM   16038 C  CB  . ALA   B 1 242  ? 25.21900   100.13500 -48.34700 1.000 40.85196  ?  242  ALA   B CB  1 
ATOM   16039 N  N   . HIS   B 1 243  ? 24.42000   101.91800 -50.78800 1.000 49.55182  ?  243  HIS   B N   1 
ATOM   16040 C  CA  . HIS   B 1 243  ? 24.55600   102.42600 -52.15000 1.000 46.36195  ?  243  HIS   B CA  1 
ATOM   16041 C  C   . HIS   B 1 243  ? 24.87600   103.91500 -52.14600 1.000 47.01964  ?  243  HIS   B C   1 
ATOM   16042 O  O   . HIS   B 1 243  ? 25.77300   104.37700 -52.86000 1.000 49.76280  ?  243  HIS   B O   1 
ATOM   16043 C  CB  . HIS   B 1 243  ? 23.26900   102.16600 -52.93500 1.000 54.94002  ?  243  HIS   B CB  1 
ATOM   16044 C  CG  . HIS   B 1 243  ? 23.11200   100.75300 -53.40200 1.000 46.20734  ?  243  HIS   B CG  1 
ATOM   16045 N  ND1 . HIS   B 1 243  ? 23.88700   100.20900 -54.40300 1.000 44.58854  ?  243  HIS   B ND1 1 
ATOM   16046 C  CD2 . HIS   B 1 243  ? 22.25300   99.77900  -53.02000 1.000 40.64026  ?  243  HIS   B CD2 1 
ATOM   16047 C  CE1 . HIS   B 1 243  ? 23.51900   98.95700  -54.61100 1.000 49.22298  ?  243  HIS   B CE1 1 
ATOM   16048 N  NE2 . HIS   B 1 243  ? 22.52900   98.67200  -53.78400 1.000 44.90799  ?  243  HIS   B NE2 1 
ATOM   16049 N  N   . HIS   B 1 244  ? 24.14300   104.68200 -51.33700 1.000 41.68832  ?  244  HIS   B N   1 
ATOM   16050 C  CA  . HIS   B 1 244  ? 24.40400   106.11100 -51.22600 1.000 38.68256  ?  244  HIS   B CA  1 
ATOM   16051 C  C   . HIS   B 1 244  ? 25.78200   106.37400 -50.63200 1.000 45.37223  ?  244  HIS   B C   1 
ATOM   16052 O  O   . HIS   B 1 244  ? 26.48500   107.29800 -51.05800 1.000 44.42315  ?  244  HIS   B O   1 
ATOM   16053 C  CB  . HIS   B 1 244  ? 23.31200   106.76600 -50.38100 1.000 37.27644  ?  244  HIS   B CB  1 
ATOM   16054 C  CG  . HIS   B 1 244  ? 23.51500   108.23000 -50.15400 1.000 41.63737  ?  244  HIS   B CG  1 
ATOM   16055 N  ND1 . HIS   B 1 244  ? 23.26600   109.17600 -51.12500 1.000 43.31742  ?  244  HIS   B ND1 1 
ATOM   16056 C  CD2 . HIS   B 1 244  ? 23.93600   108.91200 -49.06200 1.000 45.16149  ?  244  HIS   B CD2 1 
ATOM   16057 C  CE1 . HIS   B 1 244  ? 23.53000   110.37800 -50.64300 1.000 59.23971  ?  244  HIS   B CE1 1 
ATOM   16058 N  NE2 . HIS   B 1 244  ? 23.93800   110.24500 -49.39300 1.000 48.59706  ?  244  HIS   B NE2 1 
ATOM   16059 N  N   . LEU   B 1 245  ? 26.19000   105.56500 -49.65000 1.000 52.27555  ?  245  LEU   B N   1 
ATOM   16060 C  CA  . LEU   B 1 245  ? 27.48900   105.76600 -49.01500 1.000 41.64217  ?  245  LEU   B CA  1 
ATOM   16061 C  C   . LEU   B 1 245  ? 28.62700   105.44400 -49.97200 1.000 41.82298  ?  245  LEU   B C   1 
ATOM   16062 O  O   . LEU   B 1 245  ? 29.61000   106.19100 -50.05000 1.000 36.66414  ?  245  LEU   B O   1 
ATOM   16063 C  CB  . LEU   B 1 245  ? 27.59800   104.91000 -47.75300 1.000 46.12999  ?  245  LEU   B CB  1 
ATOM   16064 C  CG  . LEU   B 1 245  ? 27.08700   105.51500 -46.44500 1.000 44.24421  ?  245  LEU   B CG  1 
ATOM   16065 C  CD1 . LEU   B 1 245  ? 27.32700   104.55000 -45.29600 1.000 32.77032  ?  245  LEU   B CD1 1 
ATOM   16066 C  CD2 . LEU   B 1 245  ? 27.75000   106.86100 -46.17600 1.000 37.09675  ?  245  LEU   B CD2 1 
ATOM   16067 N  N   . ARG   B 1 246  ? 28.51500   104.33300 -50.70500 1.000 51.66815  ?  246  ARG   B N   1 
ATOM   16068 C  CA  . ARG   B 1 246  ? 29.55500   103.97500 -51.66400 1.000 41.39000  ?  246  ARG   B CA  1 
ATOM   16069 C  C   . ARG   B 1 246  ? 29.70300   105.04500 -52.73700 1.000 52.01514  ?  246  ARG   B C   1 
ATOM   16070 O  O   . ARG   B 1 246  ? 30.82200   105.37500 -53.14600 1.000 57.05749  ?  246  ARG   B O   1 
ATOM   16071 C  CB  . ARG   B 1 246  ? 29.24300   102.61900 -52.29400 1.000 28.72795  ?  246  ARG   B CB  1 
ATOM   16072 C  CG  . ARG   B 1 246  ? 30.47600   101.84900 -52.72100 1.000 35.94882  ?  246  ARG   B CG  1 
ATOM   16073 C  CD  . ARG   B 1 246  ? 30.13200   100.43200 -53.14200 1.000 24.84605  ?  246  ARG   B CD  1 
ATOM   16074 N  NE  . ARG   B 1 246  ? 30.34900   99.48000  -52.05900 1.000 30.40308  ?  246  ARG   B NE  1 
ATOM   16075 C  CZ  . ARG   B 1 246  ? 30.41200   98.16500  -52.21900 1.000 41.26906  ?  246  ARG   B CZ  1 
ATOM   16076 N  NH1 . ARG   B 1 246  ? 30.29800   97.60700  -53.41400 1.000 32.66120  ?  246  ARG   B NH1 1 
ATOM   16077 N  NH2 . ARG   B 1 246  ? 30.59100   97.39100  -51.15300 1.000 45.35347  ?  246  ARG   B NH2 1 
ATOM   16078 N  N   . GLY   B 1 247  ? 28.58100   105.60400 -53.19800 1.000 45.14691  ?  247  GLY   B N   1 
ATOM   16079 C  CA  . GLY   B 1 247  ? 28.64400   106.66600 -54.18600 1.000 37.66556  ?  247  GLY   B CA  1 
ATOM   16080 C  C   . GLY   B 1 247  ? 29.32300   107.91900 -53.67500 1.000 34.07118  ?  247  GLY   B C   1 
ATOM   16081 O  O   . GLY   B 1 247  ? 29.91300   108.67000 -54.45600 1.000 48.47424  ?  247  GLY   B O   1 
ATOM   16082 N  N   . LYS   B 1 248  ? 29.25400   108.16500 -52.36600 1.000 31.57357  ?  248  LYS   B N   1 
ATOM   16083 C  CA  . LYS   B 1 248  ? 29.92400   109.32300 -51.78800 1.000 45.54096  ?  248  LYS   B CA  1 
ATOM   16084 C  C   . LYS   B 1 248  ? 31.43100   109.13100 -51.67600 1.000 54.22546  ?  248  LYS   B C   1 
ATOM   16085 O  O   . LYS   B 1 248  ? 32.13300   110.08200 -51.31400 1.000 52.46473  ?  248  LYS   B O   1 
ATOM   16086 C  CB  . LYS   B 1 248  ? 29.33500   109.63700 -50.41100 1.000 55.97992  ?  248  LYS   B CB  1 
ATOM   16087 C  CG  . LYS   B 1 248  ? 27.95100   110.28100 -50.44700 1.000 51.22369  ?  248  LYS   B CG  1 
ATOM   16088 C  CD  . LYS   B 1 248  ? 28.02500   111.74100 -50.86400 1.000 55.74613  ?  248  LYS   B CD  1 
ATOM   16089 C  CE  . LYS   B 1 248  ? 28.62700   112.59700 -49.76000 1.000 64.82556  ?  248  LYS   B CE  1 
ATOM   16090 N  NZ  . LYS   B 1 248  ? 29.68800   113.50800 -50.27400 1.000 69.96546  ?  248  LYS   B NZ  1 
ATOM   16091 N  N   . GLY   B 1 249  ? 31.93900   107.94200 -51.96900 1.000 52.01105  ?  249  GLY   B N   1 
ATOM   16092 C  CA  . GLY   B 1 249  ? 33.35800   107.68300 -51.98900 1.000 53.01433  ?  249  GLY   B CA  1 
ATOM   16093 C  C   . GLY   B 1 249  ? 33.89000   106.77700 -50.89700 1.000 53.41355  ?  249  GLY   B C   1 
ATOM   16094 O  O   . GLY   B 1 249  ? 35.09600   106.81800 -50.62300 1.000 65.21680  ?  249  GLY   B O   1 
ATOM   16095 N  N   . VAL   B 1 250  ? 33.04500   105.96800 -50.27000 1.000 55.76038  ?  250  VAL   B N   1 
ATOM   16096 C  CA  . VAL   B 1 250  ? 33.49100   105.10600 -49.18200 1.000 46.47027  ?  250  VAL   B CA  1 
ATOM   16097 C  C   . VAL   B 1 250  ? 34.21600   103.90300 -49.77200 1.000 45.23329  ?  250  VAL   B C   1 
ATOM   16098 O  O   . VAL   B 1 250  ? 33.63300   103.12000 -50.53000 1.000 38.35645  ?  250  VAL   B O   1 
ATOM   16099 C  CB  . VAL   B 1 250  ? 32.31200   104.67100 -48.30200 1.000 35.21584  ?  250  VAL   B CB  1 
ATOM   16100 C  CG1 . VAL   B 1 250  ? 32.72100   103.50700 -47.41600 1.000 37.73106  ?  250  VAL   B CG1 1 
ATOM   16101 C  CG2 . VAL   B 1 250  ? 31.82900   105.84500 -47.46000 1.000 31.07519  ?  250  VAL   B CG2 1 
ATOM   16102 N  N   . LYS   B 1 251  ? 35.48900   103.76100 -49.43100 1.000 40.69800  ?  251  LYS   B N   1 
ATOM   16103 C  CA  . LYS   B 1 251  ? 36.33000   102.66800 -49.88500 1.000 42.61093  ?  251  LYS   B CA  1 
ATOM   16104 C  C   . LYS   B 1 251  ? 36.71700   101.77700 -48.71100 1.000 38.01564  ?  251  LYS   B C   1 
ATOM   16105 O  O   . LYS   B 1 251  ? 36.54300   102.16000 -47.54900 1.000 38.09795  ?  251  LYS   B O   1 
ATOM   16106 C  CB  . LYS   B 1 251  ? 37.59300   103.21500 -50.56700 1.000 51.94012  ?  251  LYS   B CB  1 
ATOM   16107 C  CG  . LYS   B 1 251  ? 37.34200   103.83400 -51.93600 1.000 52.46929  ?  251  LYS   B CG  1 
ATOM   16108 C  CD  . LYS   B 1 251  ? 37.05200   102.77100 -52.98700 1.000 48.09707  ?  251  LYS   B CD  1 
ATOM   16109 C  CE  . LYS   B 1 251  ? 36.25200   103.34100 -54.15300 1.000 68.39461  ?  251  LYS   B CE  1 
ATOM   16110 N  NZ  . LYS   B 1 251  ? 36.89500   104.54300 -54.76000 1.000 57.50904  ?  251  LYS   B NZ  1 
ATOM   16111 N  N   . PRO   B 1 252  ? 37.21500   100.56600 -48.97100 1.000 30.97539  ?  252  PRO   B N   1 
ATOM   16112 C  CA  . PRO   B 1 252  ? 37.68500   99.71500  -47.87100 1.000 31.41647  ?  252  PRO   B CA  1 
ATOM   16113 C  C   . PRO   B 1 252  ? 38.70600   100.42800 -46.99500 1.000 37.96680  ?  252  PRO   B C   1 
ATOM   16114 O  O   . PRO   B 1 252  ? 39.50700   101.23700 -47.47100 1.000 44.41979  ?  252  PRO   B O   1 
ATOM   16115 C  CB  . PRO   B 1 252  ? 38.30000   98.51600  -48.59700 1.000 36.15767  ?  252  PRO   B CB  1 
ATOM   16116 C  CG  . PRO   B 1 252  ? 37.49800   98.41000  -49.84700 1.000 43.07714  ?  252  PRO   B CG  1 
ATOM   16117 C  CD  . PRO   B 1 252  ? 37.17100   99.83100  -50.24800 1.000 39.05433  ?  252  PRO   B CD  1 
ATOM   16118 N  N   . ASP   B 1 253  ? 38.65400   100.12500 -45.69700 1.000 40.05845  ?  253  ASP   B N   1 
ATOM   16119 C  CA  . ASP   B 1 253  ? 39.46400   100.69600 -44.62200 1.000 36.03904  ?  253  ASP   B CA  1 
ATOM   16120 C  C   . ASP   B 1 253  ? 39.15900   102.16700 -44.35200 1.000 40.99719  ?  253  ASP   B C   1 
ATOM   16121 O  O   . ASP   B 1 253  ? 39.81400   102.76600 -43.49000 1.000 36.29943  ?  253  ASP   B O   1 
ATOM   16122 C  CB  . ASP   B 1 253  ? 40.97200   100.53700 -44.86700 1.000 35.06159  ?  253  ASP   B CB  1 
ATOM   16123 C  CG  . ASP   B 1 253  ? 41.50800   99.21300  -44.35500 1.000 48.54681  ?  253  ASP   B CG  1 
ATOM   16124 O  OD1 . ASP   B 1 253  ? 40.84000   98.59800  -43.49700 1.000 48.87962  ?  253  ASP   B OD1 1 
ATOM   16125 O  OD2 . ASP   B 1 253  ? 42.59600   98.79000  -44.80400 1.000 51.28491  -1 253  ASP   B OD2 1 
ATOM   16126 N  N   . ASP   B 1 254  ? 38.19600   102.76900 -45.04900 1.000 45.19682  ?  254  ASP   B N   1 
ATOM   16127 C  CA  . ASP   B 1 254  ? 37.78600   104.13000 -44.73200 1.000 39.55729  ?  254  ASP   B CA  1 
ATOM   16128 C  C   . ASP   B 1 254  ? 36.98800   104.14900 -43.43500 1.000 47.58861  ?  254  ASP   B C   1 
ATOM   16129 O  O   . ASP   B 1 254  ? 36.32100   103.17600 -43.07300 1.000 49.97572  ?  254  ASP   B O   1 
ATOM   16130 C  CB  . ASP   B 1 254  ? 36.94000   104.72400 -45.86000 1.000 49.81164  ?  254  ASP   B CB  1 
ATOM   16131 C  CG  . ASP   B 1 254  ? 37.77400   105.39800 -46.93100 1.000 61.02378  ?  254  ASP   B CG  1 
ATOM   16132 O  OD1 . ASP   B 1 254  ? 38.92800   105.77800 -46.64000 1.000 76.37436  ?  254  ASP   B OD1 1 
ATOM   16133 O  OD2 . ASP   B 1 254  ? 37.27200   105.55000 -48.06700 1.000 58.81542  -1 254  ASP   B OD2 1 
ATOM   16134 N  N   . GLN   B 1 255  ? 37.05500   105.27400 -42.73400 1.000 45.51727  ?  255  GLN   B N   1 
ATOM   16135 C  CA  . GLN   B 1 255  ? 36.33300   105.45300 -41.48400 1.000 42.30302  ?  255  GLN   B CA  1 
ATOM   16136 C  C   . GLN   B 1 255  ? 35.14200   106.37000 -41.71700 1.000 44.72334  ?  255  GLN   B C   1 
ATOM   16137 O  O   . GLN   B 1 255  ? 35.28400   107.44400 -42.31100 1.000 46.85834  ?  255  GLN   B O   1 
ATOM   16138 C  CB  . GLN   B 1 255  ? 37.24700   106.02000 -40.39700 1.000 33.82740  ?  255  GLN   B CB  1 
ATOM   16139 C  CG  . GLN   B 1 255  ? 38.27800   105.02600 -39.89800 1.000 30.58523  ?  255  GLN   B CG  1 
ATOM   16140 C  CD  . GLN   B 1 255  ? 39.44400   105.69400 -39.20000 1.000 56.49217  ?  255  GLN   B CD  1 
ATOM   16141 O  OE1 . GLN   B 1 255  ? 39.37300   106.86600 -38.82800 1.000 61.28122  ?  255  GLN   B OE1 1 
ATOM   16142 N  NE2 . GLN   B 1 255  ? 40.53000   104.95100 -39.02100 1.000 59.22231  ?  255  GLN   B NE2 1 
ATOM   16143 N  N   . VAL   B 1 256  ? 33.97200   105.93400 -41.26100 1.000 38.01019  ?  256  VAL   B N   1 
ATOM   16144 C  CA  . VAL   B 1 256  ? 32.74700   106.71900 -41.31600 1.000 40.33924  ?  256  VAL   B CA  1 
ATOM   16145 C  C   . VAL   B 1 256  ? 32.21800   106.83800 -39.89500 1.000 32.12289  ?  256  VAL   B C   1 
ATOM   16146 O  O   . VAL   B 1 256  ? 31.91000   105.82400 -39.25600 1.000 35.72067  ?  256  VAL   B O   1 
ATOM   16147 C  CB  . VAL   B 1 256  ? 31.70000   106.08200 -42.24100 1.000 32.96413  ?  256  VAL   B CB  1 
ATOM   16148 C  CG1 . VAL   B 1 256  ? 30.41000   106.88600 -42.21600 1.000 38.07076  ?  256  VAL   B CG1 1 
ATOM   16149 C  CG2 . VAL   B 1 256  ? 32.24400   105.97500 -43.65000 1.000 27.57647  ?  256  VAL   B CG2 1 
ATOM   16150 N  N   . ALA   B 1 257  ? 32.11700   108.06500 -39.40000 1.000 28.62078  ?  257  ALA   B N   1 
ATOM   16151 C  CA  . ALA   B 1 257  ? 31.63900   108.28300 -38.04400 1.000 37.35268  ?  257  ALA   B CA  1 
ATOM   16152 C  C   . ALA   B 1 257  ? 30.12100   108.16600 -37.97400 1.000 37.86299  ?  257  ALA   B C   1 
ATOM   16153 O  O   . ALA   B 1 257  ? 29.40300   108.48100 -38.92800 1.000 36.18501  ?  257  ALA   B O   1 
ATOM   16154 C  CB  . ALA   B 1 257  ? 32.07700   109.65500 -37.53000 1.000 38.66041  ?  257  ALA   B CB  1 
ATOM   16155 N  N   . ILE   B 1 258  ? 29.63900   107.69700 -36.82600 1.000 35.96146  ?  258  ILE   B N   1 
ATOM   16156 C  CA  . ILE   B 1 258  ? 28.21500   107.62100 -36.52700 1.000 32.73385  ?  258  ILE   B CA  1 
ATOM   16157 C  C   . ILE   B 1 258  ? 27.99400   108.22200 -35.14700 1.000 40.26043  ?  258  ILE   B C   1 
ATOM   16158 O  O   . ILE   B 1 258  ? 28.62600   107.79700 -34.17400 1.000 53.82093  ?  258  ILE   B O   1 
ATOM   16159 C  CB  . ILE   B 1 258  ? 27.68700   106.17400 -36.56900 1.000 26.23696  ?  258  ILE   B CB  1 
ATOM   16160 C  CG1 . ILE   B 1 258  ? 28.06200   105.48900 -37.88200 1.000 29.19752  ?  258  ILE   B CG1 1 
ATOM   16161 C  CG2 . ILE   B 1 258  ? 26.18100   106.15200 -36.38100 1.000 36.23153  ?  258  ILE   B CG2 1 
ATOM   16162 C  CD1 . ILE   B 1 258  ? 27.60100   104.04800 -37.95400 1.000 32.27889  ?  258  ILE   B CD1 1 
ATOM   16163 N  N   . MET   B 1 259  ? 27.11000   109.21400 -35.06300 1.000 40.79100  ?  259  MET   B N   1 
ATOM   16164 C  CA  . MET   B 1 259  ? 26.72600   109.82700 -33.79100 1.000 45.64221  ?  259  MET   B CA  1 
ATOM   16165 C  C   . MET   B 1 259  ? 25.20700   109.79200 -33.70800 1.000 33.14958  ?  259  MET   B C   1 
ATOM   16166 O  O   . MET   B 1 259  ? 24.52700   110.70200 -34.19000 1.000 50.45278  ?  259  MET   B O   1 
ATOM   16167 C  CB  . MET   B 1 259  ? 27.26000   111.24500 -33.66000 1.000 47.27750  ?  259  MET   B CB  1 
ATOM   16168 C  CG  . MET   B 1 259  ? 27.28300   111.74400 -32.22600 1.000 42.47747  ?  259  MET   B CG  1 
ATOM   16169 S  SD  . MET   B 1 259  ? 27.92700   113.41700 -32.08200 1.000 56.36414  ?  259  MET   B SD  1 
ATOM   16170 C  CE  . MET   B 1 259  ? 27.43400   114.09800 -33.66300 1.000 35.95678  ?  259  MET   B CE  1 
ATOM   16171 N  N   . LEU   B 1 260  ? 24.68100   108.74000 -33.09100 1.000 35.20457  ?  260  LEU   B N   1 
ATOM   16172 C  CA  . LEU   B 1 260  ? 23.24600   108.54200 -32.98100 1.000 37.61788  ?  260  LEU   B CA  1 
ATOM   16173 C  C   . LEU   B 1 260  ? 22.92000   107.98600 -31.60400 1.000 46.74785  ?  260  LEU   B C   1 
ATOM   16174 O  O   . LEU   B 1 260  ? 23.76900   107.39300 -30.93100 1.000 40.07052  ?  260  LEU   B O   1 
ATOM   16175 C  CB  . LEU   B 1 260  ? 22.72700   107.58800 -34.06200 1.000 29.07625  ?  260  LEU   B CB  1 
ATOM   16176 C  CG  . LEU   B 1 260  ? 22.85600   108.06900 -35.50200 1.000 30.59103  ?  260  LEU   B CG  1 
ATOM   16177 C  CD1 . LEU   B 1 260  ? 22.37000   107.00500 -36.47300 1.000 29.57963  ?  260  LEU   B CD1 1 
ATOM   16178 C  CD2 . LEU   B 1 260  ? 22.07400   109.34800 -35.66500 1.000 33.96293  ?  260  LEU   B CD2 1 
ATOM   16179 N  N   . ASP   B 1 261  ? 21.67500   108.19000 -31.18900 1.000 47.76021  ?  261  ASP   B N   1 
ATOM   16180 C  CA  . ASP   B 1 261  ? 21.16800   107.50500 -30.01400 1.000 43.73172  ?  261  ASP   B CA  1 
ATOM   16181 C  C   . ASP   B 1 261  ? 20.70900   106.10200 -30.39700 1.000 44.29388  ?  261  ASP   B C   1 
ATOM   16182 O  O   . ASP   B 1 261  ? 20.45400   105.80400 -31.56700 1.000 42.22033  ?  261  ASP   B O   1 
ATOM   16183 C  CB  . ASP   B 1 261  ? 20.01800   108.29100 -29.38200 1.000 43.17442  ?  261  ASP   B CB  1 
ATOM   16184 C  CG  . ASP   B 1 261  ? 20.50000   109.33900 -28.39700 1.000 63.18619  ?  261  ASP   B CG  1 
ATOM   16185 O  OD1 . ASP   B 1 261  ? 21.31800   108.99900 -27.51500 1.000 80.51817  ?  261  ASP   B OD1 1 
ATOM   16186 O  OD2 . ASP   B 1 261  ? 20.06700   110.50600 -28.51100 1.000 55.16622  -1 261  ASP   B OD2 1 
ATOM   16187 N  N   . LYS   B 1 262  ? 20.62000   105.23000 -29.39400 1.000 33.31541  ?  262  LYS   B N   1 
ATOM   16188 C  CA  . LYS   B 1 262  ? 20.19900   103.85500 -29.64200 1.000 39.91502  ?  262  LYS   B CA  1 
ATOM   16189 C  C   . LYS   B 1 262  ? 18.80500   103.83300 -30.26000 1.000 43.58461  ?  262  LYS   B C   1 
ATOM   16190 O  O   . LYS   B 1 262  ? 17.82800   104.24800 -29.62900 1.000 42.16770  ?  262  LYS   B O   1 
ATOM   16191 C  CB  . LYS   B 1 262  ? 20.22000   103.05300 -28.34200 1.000 41.00275  ?  262  LYS   B CB  1 
ATOM   16192 C  CG  . LYS   B 1 262  ? 21.59200   102.90600 -27.72300 1.000 35.97676  ?  262  LYS   B CG  1 
ATOM   16193 C  CD  . LYS   B 1 262  ? 21.74900   101.55500 -27.05000 1.000 34.44530  ?  262  LYS   B CD  1 
ATOM   16194 C  CE  . LYS   B 1 262  ? 22.69600   101.63700 -25.86200 1.000 47.28215  ?  262  LYS   B CE  1 
ATOM   16195 N  NZ  . LYS   B 1 262  ? 21.97400   101.82500 -24.57100 1.000 63.58315  ?  262  LYS   B NZ  1 
ATOM   16196 N  N   . SER   B 1 263  ? 18.71900   103.34600 -31.49400 1.000 39.24221  ?  263  SER   B N   1 
ATOM   16197 C  CA  . SER   B 1 263  ? 17.46500   103.34200 -32.23700 1.000 35.99796  ?  263  SER   B CA  1 
ATOM   16198 C  C   . SER   B 1 263  ? 17.59100   102.37800 -33.40800 1.000 40.47572  ?  263  SER   B C   1 
ATOM   16199 O  O   . SER   B 1 263  ? 18.61700   101.71500 -33.58800 1.000 43.72341  ?  263  SER   B O   1 
ATOM   16200 C  CB  . SER   B 1 263  ? 17.12000   104.74500 -32.73000 1.000 44.52393  ?  263  SER   B CB  1 
ATOM   16201 O  OG  . SER   B 1 263  ? 18.09800   105.17300 -33.66200 1.000 40.40587  ?  263  SER   B OG  1 
ATOM   16202 N  N   . LEU   B 1 264  ? 16.53100   102.31600 -34.21800 1.000 42.89880  ?  264  LEU   B N   1 
ATOM   16203 C  CA  . LEU   B 1 264  ? 16.57900   101.51100 -35.43400 1.000 35.29168  ?  264  LEU   B CA  1 
ATOM   16204 C  C   . LEU   B 1 264  ? 17.60500   102.06500 -36.41300 1.000 44.71095  ?  264  LEU   B C   1 
ATOM   16205 O  O   . LEU   B 1 264  ? 18.28000   101.30400 -37.11700 1.000 40.48413  ?  264  LEU   B O   1 
ATOM   16206 C  CB  . LEU   B 1 264  ? 15.19700   101.45600 -36.08400 1.000 26.33759  ?  264  LEU   B CB  1 
ATOM   16207 C  CG  . LEU   B 1 264  ? 14.08800   100.77900 -35.27900 1.000 36.33851  ?  264  LEU   B CG  1 
ATOM   16208 C  CD1 . LEU   B 1 264  ? 12.75000   100.95700 -35.96600 1.000 48.34460  ?  264  LEU   B CD1 1 
ATOM   16209 C  CD2 . LEU   B 1 264  ? 14.39200   99.30800  -35.09700 1.000 43.15779  ?  264  LEU   B CD2 1 
ATOM   16210 N  N   . ASP   B 1 265  ? 17.74300   103.39200 -36.46400 1.000 46.15877  ?  265  ASP   B N   1 
ATOM   16211 C  CA  . ASP   B 1 265  ? 18.68000   104.00200 -37.40000 1.000 44.51513  ?  265  ASP   B CA  1 
ATOM   16212 C  C   . ASP   B 1 265  ? 20.12600   103.68900 -37.03800 1.000 46.22839  ?  265  ASP   B C   1 
ATOM   16213 O  O   . ASP   B 1 265  ? 20.99100   103.67100 -37.92200 1.000 43.79932  ?  265  ASP   B O   1 
ATOM   16214 C  CB  . ASP   B 1 265  ? 18.45700   105.51100 -37.45100 1.000 43.47464  ?  265  ASP   B CB  1 
ATOM   16215 C  CG  . ASP   B 1 265  ? 17.03500   105.87000 -37.82000 1.000 50.98112  ?  265  ASP   B CG  1 
ATOM   16216 O  OD1 . ASP   B 1 265  ? 16.50700   105.27000 -38.77900 1.000 47.36412  ?  265  ASP   B OD1 1 
ATOM   16217 O  OD2 . ASP   B 1 265  ? 16.44400   106.74400 -37.14800 1.000 66.19924  -1 265  ASP   B OD2 1 
ATOM   16218 N  N   . MET   B 1 266  ? 20.40900   103.44100 -35.75700 1.000 37.11203  ?  266  MET   B N   1 
ATOM   16219 C  CA  . MET   B 1 266  ? 21.76700   103.07600 -35.37000 1.000 37.09148  ?  266  MET   B CA  1 
ATOM   16220 C  C   . MET   B 1 266  ? 22.15100   101.71900 -35.94200 1.000 39.97413  ?  266  MET   B C   1 
ATOM   16221 O  O   . MET   B 1 266  ? 23.27800   101.53600 -36.41700 1.000 42.15974  ?  266  MET   B O   1 
ATOM   16222 C  CB  . MET   B 1 266  ? 21.90300   103.07500 -33.84800 1.000 38.33916  ?  266  MET   B CB  1 
ATOM   16223 C  CG  . MET   B 1 266  ? 23.23200   103.61500 -33.34400 1.000 38.16360  ?  266  MET   B CG  1 
ATOM   16224 S  SD  . MET   B 1 266  ? 23.46200   103.36100 -31.57200 1.000 52.62917  ?  266  MET   B SD  1 
ATOM   16225 C  CE  . MET   B 1 266  ? 23.09600   101.61700 -31.43400 1.000 27.22152  ?  266  MET   B CE  1 
ATOM   16226 N  N   . ILE   B 1 267  ? 21.22700   100.75700 -35.91100 1.000 35.14549  ?  267  ILE   B N   1 
ATOM   16227 C  CA  . ILE   B 1 267  ? 21.51900   99.44700  -36.48100 1.000 28.29322  ?  267  ILE   B CA  1 
ATOM   16228 C  C   . ILE   B 1 267  ? 21.61300   99.53500  -37.99700 1.000 40.29700  ?  267  ILE   B C   1 
ATOM   16229 O  O   . ILE   B 1 267  ? 22.39400   98.80600  -38.62300 1.000 42.86022  ?  267  ILE   B O   1 
ATOM   16230 C  CB  . ILE   B 1 267  ? 20.46000   98.42200  -36.03800 1.000 31.41248  ?  267  ILE   B CB  1 
ATOM   16231 C  CG1 . ILE   B 1 267  ? 20.25300   98.48900  -34.52400 1.000 33.90834  ?  267  ILE   B CG1 1 
ATOM   16232 C  CG2 . ILE   B 1 267  ? 20.86700   97.02200  -36.45800 1.000 30.60128  ?  267  ILE   B CG2 1 
ATOM   16233 C  CD1 . ILE   B 1 267  ? 21.49900   98.17200  -33.72200 1.000 21.82672  ?  267  ILE   B CD1 1 
ATOM   16234 N  N   . VAL   B 1 268  ? 20.83600   100.42500 -38.61300 1.000 41.41239  ?  268  VAL   B N   1 
ATOM   16235 C  CA  . VAL   B 1 268  ? 20.89700   100.58300 -40.06100 1.000 38.66371  ?  268  VAL   B CA  1 
ATOM   16236 C  C   . VAL   B 1 268  ? 22.20100   101.25700 -40.46500 1.000 40.57213  ?  268  VAL   B C   1 
ATOM   16237 O  O   . VAL   B 1 268  ? 22.87700   100.82600 -41.40700 1.000 40.90966  ?  268  VAL   B O   1 
ATOM   16238 C  CB  . VAL   B 1 268  ? 19.67500   101.36800 -40.56700 1.000 43.09974  ?  268  VAL   B CB  1 
ATOM   16239 C  CG1 . VAL   B 1 268  ? 19.83300   101.69700 -42.04000 1.000 40.95450  ?  268  VAL   B CG1 1 
ATOM   16240 C  CG2 . VAL   B 1 268  ? 18.40300   100.57400 -40.33000 1.000 30.82084  ?  268  VAL   B CG2 1 
ATOM   16241 N  N   . SER   B 1 269  ? 22.57800   102.32100 -39.75000 1.000 39.27980  ?  269  SER   B N   1 
ATOM   16242 C  CA  . SER   B 1 269  ? 23.79200   103.05700 -40.09300 1.000 44.31510  ?  269  SER   B CA  1 
ATOM   16243 C  C   . SER   B 1 269  ? 25.03700   102.19600 -39.91700 1.000 49.51133  ?  269  SER   B C   1 
ATOM   16244 O  O   . SER   B 1 269  ? 25.98900   102.30400 -40.69900 1.000 47.78977  ?  269  SER   B O   1 
ATOM   16245 C  CB  . SER   B 1 269  ? 23.89200   104.32200 -39.24200 1.000 44.65807  ?  269  SER   B CB  1 
ATOM   16246 O  OG  . SER   B 1 269  ? 22.73600   105.12600 -39.39200 1.000 52.14632  ?  269  SER   B OG  1 
ATOM   16247 N  N   . ILE   B 1 270  ? 25.05100   101.33600 -38.89600 1.000 46.44922  ?  270  ILE   B N   1 
ATOM   16248 C  CA  . ILE   B 1 270  ? 26.21500   100.48700 -38.65800 1.000 40.80161  ?  270  ILE   B CA  1 
ATOM   16249 C  C   . ILE   B 1 270  ? 26.39700   99.50000  -39.80400 1.000 39.46664  ?  270  ILE   B C   1 
ATOM   16250 O  O   . ILE   B 1 270  ? 27.49600   99.35400  -40.35100 1.000 41.22473  ?  270  ILE   B O   1 
ATOM   16251 C  CB  . ILE   B 1 270  ? 26.08500   99.76500  -37.30600 1.000 33.80810  ?  270  ILE   B CB  1 
ATOM   16252 C  CG1 . ILE   B 1 270  ? 26.40200   100.72000 -36.15400 1.000 37.03648  ?  270  ILE   B CG1 1 
ATOM   16253 C  CG2 . ILE   B 1 270  ? 27.00800   98.56500  -37.25600 1.000 30.87471  ?  270  ILE   B CG2 1 
ATOM   16254 C  CD1 . ILE   B 1 270  ? 26.16100   100.11700 -34.78800 1.000 16.93432  ?  270  ILE   B CD1 1 
ATOM   16255 N  N   . LEU   B 1 271  ? 25.32200   98.80700  -40.18600 1.000 37.20597  ?  271  LEU   B N   1 
ATOM   16256 C  CA  . LEU   B 1 271  ? 25.42300   97.84800  -41.28000 1.000 31.78421  ?  271  LEU   B CA  1 
ATOM   16257 C  C   . LEU   B 1 271  ? 25.60000   98.54500  -42.62200 1.000 38.90677  ?  271  LEU   B C   1 
ATOM   16258 O  O   . LEU   B 1 271  ? 26.16300   97.95800  -43.55300 1.000 33.65641  ?  271  LEU   B O   1 
ATOM   16259 C  CB  . LEU   B 1 271  ? 24.18800   96.94900  -41.30600 1.000 34.79644  ?  271  LEU   B CB  1 
ATOM   16260 C  CG  . LEU   B 1 271  ? 23.94400   96.11700  -40.04500 1.000 34.21919  ?  271  LEU   B CG  1 
ATOM   16261 C  CD1 . LEU   B 1 271  ? 22.61700   95.37800  -40.13100 1.000 23.67295  ?  271  LEU   B CD1 1 
ATOM   16262 C  CD2 . LEU   B 1 271  ? 25.09000   95.14300  -39.82400 1.000 24.64621  ?  271  LEU   B CD2 1 
ATOM   16263 N  N   . ALA   B 1 272  ? 25.13200   99.79100  -42.74100 1.000 41.66149  ?  272  ALA   B N   1 
ATOM   16264 C  CA  . ALA   B 1 272  ? 25.30500   100.52400 -43.99000 1.000 32.99709  ?  272  ALA   B CA  1 
ATOM   16265 C  C   . ALA   B 1 272  ? 26.76700   100.87400 -44.22400 1.000 40.18927  ?  272  ALA   B C   1 
ATOM   16266 O  O   . ALA   B 1 272  ? 27.25700   100.79300 -45.35700 1.000 41.50311  ?  272  ALA   B O   1 
ATOM   16267 C  CB  . ALA   B 1 272  ? 24.44800   101.78700 -43.98300 1.000 30.31551  ?  272  ALA   B CB  1 
ATOM   16268 N  N   . VAL   B 1 273  ? 27.47800   101.27000 -43.16600 1.000 39.66787  ?  273  VAL   B N   1 
ATOM   16269 C  CA  . VAL   B 1 273  ? 28.90600   101.54100 -43.29500 1.000 36.49706  ?  273  VAL   B CA  1 
ATOM   16270 C  C   . VAL   B 1 273  ? 29.64700   100.27400 -43.69900 1.000 35.03137  ?  273  VAL   B C   1 
ATOM   16271 O  O   . VAL   B 1 273  ? 30.57000   100.31000 -44.52200 1.000 37.63077  ?  273  VAL   B O   1 
ATOM   16272 C  CB  . VAL   B 1 273  ? 29.45800   102.13200 -41.98300 1.000 34.57179  ?  273  VAL   B CB  1 
ATOM   16273 C  CG1 . VAL   B 1 273  ? 30.96800   102.25200 -42.05200 1.000 32.57623  ?  273  VAL   B CG1 1 
ATOM   16274 C  CG2 . VAL   B 1 273  ? 28.83200   103.48900 -41.71100 1.000 34.53304  ?  273  VAL   B CG2 1 
ATOM   16275 N  N   . MET   B 1 274  ? 29.23800   99.13200  -43.14400 1.000 33.71730  ?  274  MET   B N   1 
ATOM   16276 C  CA  . MET   B 1 274  ? 29.89500   97.86700  -43.45500 1.000 33.69137  ?  274  MET   B CA  1 
ATOM   16277 C  C   . MET   B 1 274  ? 29.66800   97.46600  -44.90800 1.000 31.81453  ?  274  MET   B C   1 
ATOM   16278 O  O   . MET   B 1 274  ? 30.61200   97.09000  -45.61300 1.000 32.47668  ?  274  MET   B O   1 
ATOM   16279 C  CB  . MET   B 1 274  ? 29.38700   96.77700  -42.51600 1.000 32.95578  ?  274  MET   B CB  1 
ATOM   16280 C  CG  . MET   B 1 274  ? 30.41100   96.29700  -41.51700 1.000 38.45324  ?  274  MET   B CG  1 
ATOM   16281 S  SD  . MET   B 1 274  ? 29.69600   95.11700  -40.36200 1.000 44.77652  ?  274  MET   B SD  1 
ATOM   16282 C  CE  . MET   B 1 274  ? 28.84700   96.21800  -39.24100 1.000 42.89958  ?  274  MET   B CE  1 
ATOM   16283 N  N   . LYS   B 1 275  ? 28.41700   97.53300  -45.36900 1.000 38.45891  ?  275  LYS   B N   1 
ATOM   16284 C  CA  . LYS   B 1 275  ? 28.11100   97.11600  -46.73300 1.000 26.79567  ?  275  LYS   B CA  1 
ATOM   16285 C  C   . LYS   B 1 275  ? 28.74900   98.04800  -47.75300 1.000 37.79238  ?  275  LYS   B C   1 
ATOM   16286 O  O   . LYS   B 1 275  ? 29.21200   97.59600  -48.80700 1.000 41.61426  ?  275  LYS   B O   1 
ATOM   16287 C  CB  . LYS   B 1 275  ? 26.60000   97.05100  -46.93200 1.000 33.74865  ?  275  LYS   B CB  1 
ATOM   16288 C  CG  . LYS   B 1 275  ? 25.94400   95.87600  -46.24000 1.000 32.19676  ?  275  LYS   B CG  1 
ATOM   16289 C  CD  . LYS   B 1 275  ? 24.52300   96.21400  -45.84200 1.000 45.29528  ?  275  LYS   B CD  1 
ATOM   16290 C  CE  . LYS   B 1 275  ? 23.74700   94.95900  -45.51000 1.000 41.85843  ?  275  LYS   B CE  1 
ATOM   16291 N  NZ  . LYS   B 1 275  ? 23.62800   94.07200  -46.70000 1.000 42.40397  ?  275  LYS   B NZ  1 
ATOM   16292 N  N   . ALA   B 1 276  ? 28.78700   99.35200  -47.46000 1.000 27.02075  ?  276  ALA   B N   1 
ATOM   16293 C  CA  . ALA   B 1 276  ? 29.49400   100.27600 -48.33900 1.000 35.83597  ?  276  ALA   B CA  1 
ATOM   16294 C  C   . ALA   B 1 276  ? 30.96300   99.89300  -48.48500 1.000 41.30309  ?  276  ALA   B C   1 
ATOM   16295 O  O   . ALA   B 1 276  ? 31.55800   100.11500 -49.54600 1.000 42.53473  ?  276  ALA   B O   1 
ATOM   16296 C  CB  . ALA   B 1 276  ? 29.36300   101.70600 -47.81700 1.000 32.88883  ?  276  ALA   B CB  1 
ATOM   16297 N  N   . GLY   B 1 277  ? 31.55600   99.31100  -47.44100 1.000 29.31038  ?  277  GLY   B N   1 
ATOM   16298 C  CA  . GLY   B 1 277  ? 32.92300   98.82800  -47.50300 1.000 40.07133  ?  277  GLY   B CA  1 
ATOM   16299 C  C   . GLY   B 1 277  ? 33.83300   99.34800  -46.40700 1.000 39.10414  ?  277  GLY   B C   1 
ATOM   16300 O  O   . GLY   B 1 277  ? 34.91600   98.79900  -46.17400 1.000 29.58310  ?  277  GLY   B O   1 
ATOM   16301 N  N   . GLY   B 1 278  ? 33.40600   100.40900 -45.72600 1.000 29.89847  ?  278  GLY   B N   1 
ATOM   16302 C  CA  . GLY   B 1 278  ? 34.22100   101.06000 -44.72400 1.000 30.46468  ?  278  GLY   B CA  1 
ATOM   16303 C  C   . GLY   B 1 278  ? 34.05500   100.45700 -43.34300 1.000 31.51574  ?  278  GLY   B C   1 
ATOM   16304 O  O   . GLY   B 1 278  ? 33.51200   99.36600  -43.15900 1.000 28.57869  ?  278  GLY   B O   1 
ATOM   16305 N  N   . ALA   B 1 279  ? 34.55500   101.19700 -42.35400 1.000 31.43170  ?  279  ALA   B N   1 
ATOM   16306 C  CA  . ALA   B 1 279  ? 34.46700   100.83900 -40.94700 1.000 25.80725  ?  279  ALA   B CA  1 
ATOM   16307 C  C   . ALA   B 1 279  ? 33.84200   102.00200 -40.19500 1.000 36.42859  ?  279  ALA   B C   1 
ATOM   16308 O  O   . ALA   B 1 279  ? 34.09900   103.16600 -40.51700 1.000 38.92715  ?  279  ALA   B O   1 
ATOM   16309 C  CB  . ALA   B 1 279  ? 35.84500   100.51500 -40.36400 1.000 35.71439  ?  279  ALA   B CB  1 
ATOM   16310 N  N   . TYR   B 1 280  ? 33.02200   101.69200 -39.19700 1.000 37.58200  ?  280  TYR   B N   1 
ATOM   16311 C  CA  . TYR   B 1 280  ? 32.25300   102.71400 -38.50300 1.000 35.08051  ?  280  TYR   B CA  1 
ATOM   16312 C  C   . TYR   B 1 280  ? 32.93400   103.11100 -37.20100 1.000 35.43570  ?  280  TYR   B C   1 
ATOM   16313 O  O   . TYR   B 1 280  ? 33.47100   102.26500 -36.48000 1.000 31.05015  ?  280  TYR   B O   1 
ATOM   16314 C  CB  . TYR   B 1 280  ? 30.81700   102.24200 -38.24800 1.000 35.82203  ?  280  TYR   B CB  1 
ATOM   16315 C  CG  . TYR   B 1 280  ? 30.59100   101.34800 -37.04400 1.000 30.93831  ?  280  TYR   B CG  1 
ATOM   16316 C  CD1 . TYR   B 1 280  ? 30.74200   99.96900  -37.13700 1.000 33.47811  ?  280  TYR   B CD1 1 
ATOM   16317 C  CD2 . TYR   B 1 280  ? 30.17800   101.87900 -35.82600 1.000 29.43444  ?  280  TYR   B CD2 1 
ATOM   16318 C  CE1 . TYR   B 1 280  ? 30.51200   99.14400  -36.04300 1.000 29.42089  ?  280  TYR   B CE1 1 
ATOM   16319 C  CE2 . TYR   B 1 280  ? 29.94800   101.06400 -34.72600 1.000 32.61541  ?  280  TYR   B CE2 1 
ATOM   16320 C  CZ  . TYR   B 1 280  ? 30.11600   99.69700  -34.84100 1.000 37.70446  ?  280  TYR   B CZ  1 
ATOM   16321 O  OH  . TYR   B 1 280  ? 29.88700   98.87900  -33.75600 1.000 36.70673  ?  280  TYR   B OH  1 
ATOM   16322 N  N   . VAL   B 1 281  ? 32.92600   104.41200 -36.92300 1.000 34.09950  ?  281  VAL   B N   1 
ATOM   16323 C  CA  . VAL   B 1 281  ? 33.51000   104.97300 -35.70800 1.000 27.93925  ?  281  VAL   B CA  1 
ATOM   16324 C  C   . VAL   B 1 281  ? 32.37900   105.49000 -34.83000 1.000 40.19032  ?  281  VAL   B C   1 
ATOM   16325 O  O   . VAL   B 1 281  ? 31.90500   106.61900 -35.02300 1.000 41.70304  ?  281  VAL   B O   1 
ATOM   16326 C  CB  . VAL   B 1 281  ? 34.51700   106.08800 -36.02800 1.000 32.40137  ?  281  VAL   B CB  1 
ATOM   16327 C  CG1 . VAL   B 1 281  ? 35.27000   106.48700 -34.77100 1.000 27.92078  ?  281  VAL   B CG1 1 
ATOM   16328 C  CG2 . VAL   B 1 281  ? 35.48300   105.63800 -37.11300 1.000 41.92554  ?  281  VAL   B CG2 1 
ATOM   16329 N  N   . PRO   B 1 282  ? 31.91800   104.70500 -33.86100 1.000 44.12650  ?  282  PRO   B N   1 
ATOM   16330 C  CA  . PRO   B 1 282  ? 30.76900   105.12800 -33.05300 1.000 32.37018  ?  282  PRO   B CA  1 
ATOM   16331 C  C   . PRO   B 1 282  ? 31.13800   106.25100 -32.09700 1.000 41.68519  ?  282  PRO   B C   1 
ATOM   16332 O  O   . PRO   B 1 282  ? 32.22000   106.25700 -31.50400 1.000 55.34951  ?  282  PRO   B O   1 
ATOM   16333 C  CB  . PRO   B 1 282  ? 30.38800   103.85300 -32.29700 1.000 38.31003  ?  282  PRO   B CB  1 
ATOM   16334 C  CG  . PRO   B 1 282  ? 31.67300   103.08900 -32.20300 1.000 34.68280  ?  282  PRO   B CG  1 
ATOM   16335 C  CD  . PRO   B 1 282  ? 32.42400   103.38000 -33.46700 1.000 36.45717  ?  282  PRO   B CD  1 
ATOM   16336 N  N   . ILE   B 1 283  ? 30.22100   107.20700 -31.95400 1.000 44.13672  ?  283  ILE   B N   1 
ATOM   16337 C  CA  . ILE   B 1 283  ? 30.41100   108.37200 -31.09100 1.000 38.30918  ?  283  ILE   B CA  1 
ATOM   16338 C  C   . ILE   B 1 283  ? 29.12300   108.57800 -30.30200 1.000 45.54946  ?  283  ILE   B C   1 
ATOM   16339 O  O   . ILE   B 1 283  ? 28.08400   108.91700 -30.88100 1.000 46.17251  ?  283  ILE   B O   1 
ATOM   16340 C  CB  . ILE   B 1 283  ? 30.76700   109.63800 -31.88300 1.000 36.15187  ?  283  ILE   B CB  1 
ATOM   16341 C  CG1 . ILE   B 1 283  ? 32.11800   109.46300 -32.57900 1.000 41.46850  ?  283  ILE   B CG1 1 
ATOM   16342 C  CG2 . ILE   B 1 283  ? 30.79800   110.85200 -30.97000 1.000 36.97566  ?  283  ILE   B CG2 1 
ATOM   16343 C  CD1 . ILE   B 1 283  ? 32.30500   110.35900 -33.77300 1.000 35.51818  ?  283  ILE   B CD1 1 
ATOM   16344 N  N   . ASP   B 1 284  ? 29.18700   108.37400 -28.99300 1.000 59.38420  ?  284  ASP   B N   1 
ATOM   16345 C  CA  . ASP   B 1 284  ? 28.00900   108.51200 -28.14200 1.000 49.45181  ?  284  ASP   B CA  1 
ATOM   16346 C  C   . ASP   B 1 284  ? 27.61800   109.97900 -28.03800 1.000 56.19699  ?  284  ASP   B C   1 
ATOM   16347 O  O   . ASP   B 1 284  ? 28.44300   110.80400 -27.62300 1.000 61.67420  ?  284  ASP   B O   1 
ATOM   16348 C  CB  . ASP   B 1 284  ? 28.28400   107.93200 -26.75700 1.000 45.04829  ?  284  ASP   B CB  1 
ATOM   16349 C  CG  . ASP   B 1 284  ? 27.03000   107.77800 -25.92600 1.000 57.91537  ?  284  ASP   B CG  1 
ATOM   16350 O  OD1 . ASP   B 1 284  ? 26.34300   108.79200 -25.67600 1.000 55.96976  ?  284  ASP   B OD1 1 
ATOM   16351 O  OD2 . ASP   B 1 284  ? 26.73100   106.63600 -25.52000 1.000 59.93895  -1 284  ASP   B OD2 1 
ATOM   16352 N  N   . PRO   B 1 285  ? 26.38500   110.35200 -28.39300 1.000 55.20217  ?  285  PRO   B N   1 
ATOM   16353 C  CA  . PRO   B 1 285  ? 26.01100   111.77500 -28.37800 1.000 55.53492  ?  285  PRO   B CA  1 
ATOM   16354 C  C   . PRO   B 1 285  ? 25.94900   112.38400 -26.98700 1.000 58.31325  ?  285  PRO   B C   1 
ATOM   16355 O  O   . PRO   B 1 285  ? 25.86600   113.61400 -26.87700 1.000 60.64411  ?  285  PRO   B O   1 
ATOM   16356 C  CB  . PRO   B 1 285  ? 24.62900   111.78400 -29.04700 1.000 50.49048  ?  285  PRO   B CB  1 
ATOM   16357 C  CG  . PRO   B 1 285  ? 24.51800   110.46200 -29.75000 1.000 50.63174  ?  285  PRO   B CG  1 
ATOM   16358 C  CD  . PRO   B 1 285  ? 25.30400   109.50400 -28.91600 1.000 56.95420  ?  285  PRO   B CD  1 
ATOM   16359 N  N   . ASP   B 1 286  ? 25.98400   111.58100 -25.92800 1.000 55.12727  ?  286  ASP   B N   1 
ATOM   16360 C  CA  . ASP   B 1 286  ? 25.96000   112.10600 -24.57000 1.000 63.14493  ?  286  ASP   B CA  1 
ATOM   16361 C  C   . ASP   B 1 286  ? 27.35300   112.34400 -24.00500 1.000 62.35575  ?  286  ASP   B C   1 
ATOM   16362 O  O   . ASP   B 1 286  ? 27.47100   112.79300 -22.85900 1.000 68.10808  ?  286  ASP   B O   1 
ATOM   16363 C  CB  . ASP   B 1 286  ? 25.18000   111.16200 -23.65100 1.000 49.11169  ?  286  ASP   B CB  1 
ATOM   16364 C  CG  . ASP   B 1 286  ? 23.72000   111.04900 -24.04000 1.000 66.61813  ?  286  ASP   B CG  1 
ATOM   16365 O  OD1 . ASP   B 1 286  ? 23.20000   111.98500 -24.68500 1.000 69.67435  ?  286  ASP   B OD1 1 
ATOM   16366 O  OD2 . ASP   B 1 286  ? 23.09100   110.02400 -23.70000 1.000 64.97189  -1 286  ASP   B OD2 1 
ATOM   16367 N  N   . TYR   B 1 287  ? 28.40400   112.04900 -24.77600 1.000 67.09431  ?  287  TYR   B N   1 
ATOM   16368 C  CA  . TYR   B 1 287  ? 29.76600   112.34800 -24.36400 1.000 52.72276  ?  287  TYR   B CA  1 
ATOM   16369 C  C   . TYR   B 1 287  ? 29.95200   113.85700 -24.23100 1.000 51.55692  ?  287  TYR   B C   1 
ATOM   16370 O  O   . TYR   B 1 287  ? 29.23700   114.63900 -24.86300 1.000 63.99603  ?  287  TYR   B O   1 
ATOM   16371 C  CB  . TYR   B 1 287  ? 30.76700   111.80300 -25.38400 1.000 52.81025  ?  287  TYR   B CB  1 
ATOM   16372 C  CG  . TYR   B 1 287  ? 31.24100   110.38600 -25.14000 1.000 52.39808  ?  287  TYR   B CG  1 
ATOM   16373 C  CD1 . TYR   B 1 287  ? 31.72000   109.98800 -23.90000 1.000 68.17206  ?  287  TYR   B CD1 1 
ATOM   16374 C  CD2 . TYR   B 1 287  ? 31.21000   109.44700 -26.15900 1.000 55.28809  ?  287  TYR   B CD2 1 
ATOM   16375 C  CE1 . TYR   B 1 287  ? 32.15500   108.68700 -23.68600 1.000 69.07386  ?  287  TYR   B CE1 1 
ATOM   16376 C  CE2 . TYR   B 1 287  ? 31.64300   108.15000 -25.95700 1.000 51.44702  ?  287  TYR   B CE2 1 
ATOM   16377 C  CZ  . TYR   B 1 287  ? 32.11300   107.77400 -24.72100 1.000 52.03681  ?  287  TYR   B CZ  1 
ATOM   16378 O  OH  . TYR   B 1 287  ? 32.53900   106.48000 -24.52400 1.000 72.27332  ?  287  TYR   B OH  1 
ATOM   16379 N  N   . PRO   B 1 288  ? 30.90500   114.29100 -23.40800 1.000 51.73047  ?  288  PRO   B N   1 
ATOM   16380 C  CA  . PRO   B 1 288  ? 31.28300   115.70700 -23.41300 1.000 49.77479  ?  288  PRO   B CA  1 
ATOM   16381 C  C   . PRO   B 1 288  ? 31.76300   116.12800 -24.79400 1.000 66.53522  ?  288  PRO   B C   1 
ATOM   16382 O  O   . PRO   B 1 288  ? 32.35500   115.34000 -25.53600 1.000 78.14452  ?  288  PRO   B O   1 
ATOM   16383 C  CB  . PRO   B 1 288  ? 32.41000   115.78100 -22.37700 1.000 48.04372  ?  288  PRO   B CB  1 
ATOM   16384 C  CG  . PRO   B 1 288  ? 32.18600   114.59600 -21.49000 1.000 45.56224  ?  288  PRO   B CG  1 
ATOM   16385 C  CD  . PRO   B 1 288  ? 31.61500   113.52600 -22.36800 1.000 52.33013  ?  288  PRO   B CD  1 
ATOM   16386 N  N   . GLY   B 1 289  ? 31.48600   117.38800 -25.14200 1.000 60.35483  ?  289  GLY   B N   1 
ATOM   16387 C  CA  . GLY   B 1 289  ? 31.85200   117.88100 -26.45900 1.000 63.41996  ?  289  GLY   B CA  1 
ATOM   16388 C  C   . GLY   B 1 289  ? 33.34100   117.81000 -26.72900 1.000 70.94407  ?  289  GLY   B C   1 
ATOM   16389 O  O   . GLY   B 1 289  ? 33.76200   117.66100 -27.88100 1.000 64.50089  ?  289  GLY   B O   1 
ATOM   16390 N  N   . GLU   B 1 290  ? 34.15600   117.91500 -25.67800 1.000 78.80692  ?  290  GLU   B N   1 
ATOM   16391 C  CA  . GLU   B 1 290  ? 35.60000   117.79200 -25.83500 1.000 69.83007  ?  290  GLU   B CA  1 
ATOM   16392 C  C   . GLU   B 1 290  ? 35.97200   116.43600 -26.41700 1.000 62.97415  ?  290  GLU   B C   1 
ATOM   16393 O  O   . GLU   B 1 290  ? 36.79100   116.34400 -27.33800 1.000 74.33776  ?  290  GLU   B O   1 
ATOM   16394 C  CB  . GLU   B 1 290  ? 36.28500   118.00400 -24.48600 1.000 76.55453  ?  290  GLU   B CB  1 
ATOM   16395 C  CG  . GLU   B 1 290  ? 35.42900   117.56500 -23.30800 1.000 89.54238  ?  290  GLU   B CG  1 
ATOM   16396 C  CD  . GLU   B 1 290  ? 36.01200   117.96800 -21.96900 1.000 102.31002 ?  290  GLU   B CD  1 
ATOM   16397 O  OE1 . GLU   B 1 290  ? 37.24200   117.84300 -21.79000 1.000 96.71831  ?  290  GLU   B OE1 1 
ATOM   16398 O  OE2 . GLU   B 1 290  ? 35.23600   118.40700 -21.09200 1.000 89.05004  -1 290  GLU   B OE2 1 
ATOM   16399 N  N   . ARG   B 1 291  ? 35.37100   115.36600 -25.89400 1.000 53.59484  ?  291  ARG   B N   1 
ATOM   16400 C  CA  . ARG   B 1 291  ? 35.71800   114.03900 -26.38600 1.000 58.66547  ?  291  ARG   B CA  1 
ATOM   16401 C  C   . ARG   B 1 291  ? 35.17100   113.81500 -27.78900 1.000 58.98688  ?  291  ARG   B C   1 
ATOM   16402 O  O   . ARG   B 1 291  ? 35.84500   113.21000 -28.63000 1.000 60.72009  ?  291  ARG   B O   1 
ATOM   16403 C  CB  . ARG   B 1 291  ? 35.21100   112.95900 -25.43000 1.000 50.54740  ?  291  ARG   B CB  1 
ATOM   16404 C  CG  . ARG   B 1 291  ? 35.78400   111.58800 -25.75100 1.000 59.90502  ?  291  ARG   B CG  1 
ATOM   16405 C  CD  . ARG   B 1 291  ? 35.78000   110.61800 -24.58400 1.000 59.84348  ?  291  ARG   B CD  1 
ATOM   16406 N  NE  . ARG   B 1 291  ? 35.68500   109.24900 -25.07900 1.000 66.23926  ?  291  ARG   B NE  1 
ATOM   16407 C  CZ  . ARG   B 1 291  ? 36.65200   108.34600 -24.99300 1.000 65.93252  ?  291  ARG   B CZ  1 
ATOM   16408 N  NH1 . ARG   B 1 291  ? 37.81600   108.63000 -24.43000 1.000 65.42492  ?  291  ARG   B NH1 1 
ATOM   16409 N  NH2 . ARG   B 1 291  ? 36.44600   107.12600 -25.48400 1.000 70.76490  ?  291  ARG   B NH2 1 
ATOM   16410 N  N   . ILE   B 1 292  ? 33.95500   114.29800 -28.06200 1.000 57.37228  ?  292  ILE   B N   1 
ATOM   16411 C  CA  . ILE   B 1 292  ? 33.40200   114.19400 -29.41000 1.000 46.90910  ?  292  ILE   B CA  1 
ATOM   16412 C  C   . ILE   B 1 292  ? 34.33000   114.86400 -30.41300 1.000 50.89415  ?  292  ILE   B C   1 
ATOM   16413 O  O   . ILE   B 1 292  ? 34.57600   114.33800 -31.50600 1.000 55.75852  ?  292  ILE   B O   1 
ATOM   16414 C  CB  . ILE   B 1 292  ? 31.98700   114.79900 -29.46200 1.000 41.41391  ?  292  ILE   B CB  1 
ATOM   16415 C  CG1 . ILE   B 1 292  ? 31.07800   114.14000 -28.42200 1.000 54.37209  ?  292  ILE   B CG1 1 
ATOM   16416 C  CG2 . ILE   B 1 292  ? 31.40000   114.66100 -30.85900 1.000 43.07689  ?  292  ILE   B CG2 1 
ATOM   16417 C  CD1 . ILE   B 1 292  ? 29.62000   114.52600 -28.55700 1.000 55.35464  ?  292  ILE   B CD1 1 
ATOM   16418 N  N   . ALA   B 1 293  ? 34.87100   116.02900 -30.05100 1.000 57.04893  ?  293  ALA   B N   1 
ATOM   16419 C  CA  . ALA   B 1 293  ? 35.80500   116.71700 -30.93500 1.000 58.45159  ?  293  ALA   B CA  1 
ATOM   16420 C  C   . ALA   B 1 293  ? 37.08500   115.91100 -31.11600 1.000 64.06856  ?  293  ALA   B C   1 
ATOM   16421 O  O   . ALA   B 1 293  ? 37.61800   115.81900 -32.22900 1.000 65.10780  ?  293  ALA   B O   1 
ATOM   16422 C  CB  . ALA   B 1 293  ? 36.11500   118.10700 -30.38300 1.000 52.41109  ?  293  ALA   B CB  1 
ATOM   16423 N  N   . TYR   B 1 294  ? 37.58400   115.30800 -30.03500 1.000 55.22783  ?  294  TYR   B N   1 
ATOM   16424 C  CA  . TYR   B 1 294  ? 38.81400   114.52700 -30.12000 1.000 49.60313  ?  294  TYR   B CA  1 
ATOM   16425 C  C   . TYR   B 1 294  ? 38.63600   113.31200 -31.02300 1.000 53.94739  ?  294  TYR   B C   1 
ATOM   16426 O  O   . TYR   B 1 294  ? 39.46700   113.05300 -31.90100 1.000 61.59442  ?  294  TYR   B O   1 
ATOM   16427 C  CB  . TYR   B 1 294  ? 39.26200   114.10500 -28.72000 1.000 61.77760  ?  294  TYR   B CB  1 
ATOM   16428 C  CG  . TYR   B 1 294  ? 40.47300   113.19800 -28.70600 1.000 68.52145  ?  294  TYR   B CG  1 
ATOM   16429 C  CD1 . TYR   B 1 294  ? 41.75700   113.72300 -28.74900 1.000 52.12252  ?  294  TYR   B CD1 1 
ATOM   16430 C  CD2 . TYR   B 1 294  ? 40.33000   111.81800 -28.64100 1.000 63.43894  ?  294  TYR   B CD2 1 
ATOM   16431 C  CE1 . TYR   B 1 294  ? 42.86500   112.89700 -28.73400 1.000 69.08942  ?  294  TYR   B CE1 1 
ATOM   16432 C  CE2 . TYR   B 1 294  ? 41.43000   110.98700 -28.62700 1.000 61.63022  ?  294  TYR   B CE2 1 
ATOM   16433 C  CZ  . TYR   B 1 294  ? 42.69500   111.53100 -28.67300 1.000 63.37198  ?  294  TYR   B CZ  1 
ATOM   16434 O  OH  . TYR   B 1 294  ? 43.79100   110.70100 -28.65800 1.000 67.63905  ?  294  TYR   B OH  1 
ATOM   16435 N  N   . MET   B 1 295  ? 37.55400   112.55300 -30.82200 1.000 49.44475  ?  295  MET   B N   1 
ATOM   16436 C  CA  . MET   B 1 295  ? 37.32200   111.36600 -31.64300 1.000 45.34728  ?  295  MET   B CA  1 
ATOM   16437 C  C   . MET   B 1 295  ? 37.16600   111.73500 -33.11200 1.000 57.19000  ?  295  MET   B C   1 
ATOM   16438 O  O   . MET   B 1 295  ? 37.75500   111.09300 -33.99000 1.000 66.72285  ?  295  MET   B O   1 
ATOM   16439 C  CB  . MET   B 1 295  ? 36.08600   110.61000 -31.16200 1.000 55.29604  ?  295  MET   B CB  1 
ATOM   16440 C  CG  . MET   B 1 295  ? 36.01800   110.34600 -29.67800 1.000 49.53915  ?  295  MET   B CG  1 
ATOM   16441 S  SD  . MET   B 1 295  ? 34.77700   109.08300 -29.37100 1.000 53.94412  ?  295  MET   B SD  1 
ATOM   16442 C  CE  . MET   B 1 295  ? 33.93300   109.79700 -27.98100 1.000 56.68755  ?  295  MET   B CE  1 
ATOM   16443 N  N   . LEU   B 1 296  ? 36.36300   112.76300 -33.40100 1.000 48.45733  ?  296  LEU   B N   1 
ATOM   16444 C  CA  . LEU   B 1 296  ? 36.17100   113.18700 -34.78500 1.000 51.07545  ?  296  LEU   B CA  1 
ATOM   16445 C  C   . LEU   B 1 296  ? 37.48700   113.60800 -35.42200 1.000 50.70799  ?  296  LEU   B C   1 
ATOM   16446 O  O   . LEU   B 1 296  ? 37.73500   113.32600 -36.60100 1.000 47.49436  ?  296  LEU   B O   1 
ATOM   16447 C  CB  . LEU   B 1 296  ? 35.16000   114.33100 -34.84700 1.000 44.20426  ?  296  LEU   B CB  1 
ATOM   16448 C  CG  . LEU   B 1 296  ? 33.68300   113.94800 -34.85600 1.000 40.12125  ?  296  LEU   B CG  1 
ATOM   16449 C  CD1 . LEU   B 1 296  ? 32.82900   115.18700 -35.04100 1.000 52.69947  ?  296  LEU   B CD1 1 
ATOM   16450 C  CD2 . LEU   B 1 296  ? 33.41100   112.94100 -35.96400 1.000 44.93719  ?  296  LEU   B CD2 1 
ATOM   16451 N  N   . ALA   B 1 297  ? 38.34700   114.28000 -34.65300 1.000 49.92047  ?  297  ALA   B N   1 
ATOM   16452 C  CA  . ALA   B 1 297  ? 39.61800   114.75100 -35.19300 1.000 56.33182  ?  297  ALA   B CA  1 
ATOM   16453 C  C   . ALA   B 1 297  ? 40.58800   113.59800 -35.41700 1.000 51.65585  ?  297  ALA   B C   1 
ATOM   16454 O  O   . ALA   B 1 297  ? 41.12000   113.43000 -36.52200 1.000 51.58064  ?  297  ALA   B O   1 
ATOM   16455 C  CB  . ALA   B 1 297  ? 40.22800   115.79300 -34.25500 1.000 47.14374  ?  297  ALA   B CB  1 
ATOM   16456 N  N   . ASP   B 1 298  ? 40.83500   112.79600 -34.37500 1.000 44.53950  ?  298  ASP   B N   1 
ATOM   16457 C  CA  . ASP   B 1 298  ? 41.79400   111.70000 -34.48800 1.000 50.74898  ?  298  ASP   B CA  1 
ATOM   16458 C  C   . ASP   B 1 298  ? 41.38400   110.71800 -35.57500 1.000 47.62367  ?  298  ASP   B C   1 
ATOM   16459 O  O   . ASP   B 1 298  ? 42.22700   110.24300 -36.34500 1.000 58.66985  ?  298  ASP   B O   1 
ATOM   16460 C  CB  . ASP   B 1 298  ? 41.93600   110.98300 -33.14500 1.000 49.98649  ?  298  ASP   B CB  1 
ATOM   16461 C  CG  . ASP   B 1 298  ? 43.01400   109.91200 -33.16300 1.000 59.78178  ?  298  ASP   B CG  1 
ATOM   16462 O  OD1 . ASP   B 1 298  ? 44.00800   110.06700 -33.90700 1.000 61.02734  ?  298  ASP   B OD1 1 
ATOM   16463 O  OD2 . ASP   B 1 298  ? 42.86400   108.91000 -32.43300 1.000 69.62759  -1 298  ASP   B OD2 1 
ATOM   16464 N  N   . SER   B 1 299  ? 40.09900   110.40000 -35.65700 1.000 50.69249  ?  299  SER   B N   1 
ATOM   16465 C  CA  . SER   B 1 299  ? 39.62300   109.55900 -36.74200 1.000 58.49400  ?  299  SER   B CA  1 
ATOM   16466 C  C   . SER   B 1 299  ? 39.74100   110.29600 -38.07200 1.000 58.29009  ?  299  SER   B C   1 
ATOM   16467 O  O   . SER   B 1 299  ? 39.44500   111.49100 -38.16400 1.000 62.06077  ?  299  SER   B O   1 
ATOM   16468 C  CB  . SER   B 1 299  ? 38.17500   109.14900 -36.49000 1.000 40.22243  ?  299  SER   B CB  1 
ATOM   16469 O  OG  . SER   B 1 299  ? 37.59200   108.61300 -37.66100 1.000 50.62686  ?  299  SER   B OG  1 
ATOM   16470 N  N   . SER   B 1 300  ? 40.18900   109.57700 -39.10700 1.000 58.20131  ?  300  SER   B N   1 
ATOM   16471 C  CA  . SER   B 1 300  ? 40.22200   110.09500 -40.47100 1.000 58.67170  ?  300  SER   B CA  1 
ATOM   16472 C  C   . SER   B 1 300  ? 38.85500   110.06000 -41.14100 1.000 60.99949  ?  300  SER   B C   1 
ATOM   16473 O  O   . SER   B 1 300  ? 38.77300   109.90000 -42.36700 1.000 72.50595  ?  300  SER   B O   1 
ATOM   16474 C  CB  . SER   B 1 300  ? 41.24800   109.33100 -41.31200 1.000 59.20453  ?  300  SER   B CB  1 
ATOM   16475 O  OG  . SER   B 1 300  ? 41.48500   108.03400 -40.79000 1.000 56.82963  ?  300  SER   B OG  1 
ATOM   16476 N  N   . ALA   B 1 301  ? 37.77500   110.20400 -40.37200 1.000 59.93761  ?  301  ALA   B N   1 
ATOM   16477 C  CA  . ALA   B 1 301  ? 36.42900   110.12400 -40.92700 1.000 55.41088  ?  301  ALA   B CA  1 
ATOM   16478 C  C   . ALA   B 1 301  ? 36.06600   111.44500 -41.59500 1.000 61.17323  ?  301  ALA   B C   1 
ATOM   16479 O  O   . ALA   B 1 301  ? 36.11700   112.50400 -40.95900 1.000 68.77310  ?  301  ALA   B O   1 
ATOM   16480 C  CB  . ALA   B 1 301  ? 35.41400   109.77400 -39.84000 1.000 51.97215  ?  301  ALA   B CB  1 
ATOM   16481 N  N   . ALA   B 1 302  ? 35.71400   111.38200 -42.87500 1.000 62.40694  ?  302  ALA   B N   1 
ATOM   16482 C  CA  . ALA   B 1 302  ? 35.23000   112.55400 -43.59000 1.000 63.85727  ?  302  ALA   B CA  1 
ATOM   16483 C  C   . ALA   B 1 302  ? 33.71100   112.64700 -43.58400 1.000 63.87256  ?  302  ALA   B C   1 
ATOM   16484 O  O   . ALA   B 1 302  ? 33.16100   113.74900 -43.69200 1.000 65.17829  ?  302  ALA   B O   1 
ATOM   16485 C  CB  . ALA   B 1 302  ? 35.74300   112.54200 -45.03400 1.000 55.84800  ?  302  ALA   B CB  1 
ATOM   16486 N  N   . ILE   B 1 303  ? 33.02800   111.51300 -43.44100 1.000 62.61025  ?  303  ILE   B N   1 
ATOM   16487 C  CA  . ILE   B 1 303  ? 31.57200   111.44100 -43.44700 1.000 50.89590  ?  303  ILE   B CA  1 
ATOM   16488 C  C   . ILE   B 1 303  ? 31.09500   111.09600 -42.04300 1.000 42.54167  ?  303  ILE   B C   1 
ATOM   16489 O  O   . ILE   B 1 303  ? 31.67500   110.23100 -41.37500 1.000 49.92818  ?  303  ILE   B O   1 
ATOM   16490 C  CB  . ILE   B 1 303  ? 31.07300   110.39900 -44.46900 1.000 49.93655  ?  303  ILE   B CB  1 
ATOM   16491 C  CG1 . ILE   B 1 303  ? 31.45600   110.81400 -45.88900 1.000 39.57398  ?  303  ILE   B CG1 1 
ATOM   16492 C  CG2 . ILE   B 1 303  ? 29.56800   110.20100 -44.36400 1.000 32.63787  ?  303  ILE   B CG2 1 
ATOM   16493 C  CD1 . ILE   B 1 303  ? 31.21700   109.72900 -46.91600 1.000 44.58962  ?  303  ILE   B CD1 1 
ATOM   16494 N  N   . LEU   B 1 304  ? 30.03800   111.77100 -41.59700 1.000 41.64335  ?  304  LEU   B N   1 
ATOM   16495 C  CA  . LEU   B 1 304  ? 29.42400   111.50700 -40.29800 1.000 43.26196  ?  304  LEU   B CA  1 
ATOM   16496 C  C   . LEU   B 1 304  ? 27.92600   111.30000 -40.49100 1.000 43.93652  ?  304  LEU   B C   1 
ATOM   16497 O  O   . LEU   B 1 304  ? 27.21200   112.22900 -40.88100 1.000 41.26103  ?  304  LEU   B O   1 
ATOM   16498 C  CB  . LEU   B 1 304  ? 29.69200   112.65100 -39.32000 1.000 48.52038  ?  304  LEU   B CB  1 
ATOM   16499 C  CG  . LEU   B 1 304  ? 28.76600   112.74800 -38.10600 1.000 38.36548  ?  304  LEU   B CG  1 
ATOM   16500 C  CD1 . LEU   B 1 304  ? 28.98200   111.57200 -37.17200 1.000 46.11941  ?  304  LEU   B CD1 1 
ATOM   16501 C  CD2 . LEU   B 1 304  ? 28.97600   114.06500 -37.37700 1.000 39.28278  ?  304  LEU   B CD2 1 
ATOM   16502 N  N   . LEU   B 1 305  ? 27.45300   110.08500 -40.22000 1.000 35.37426  ?  305  LEU   B N   1 
ATOM   16503 C  CA  . LEU   B 1 305  ? 26.02300   109.80900 -40.19800 1.000 29.01146  ?  305  LEU   B CA  1 
ATOM   16504 C  C   . LEU   B 1 305  ? 25.46300   110.23000 -38.84300 1.000 38.30325  ?  305  LEU   B C   1 
ATOM   16505 O  O   . LEU   B 1 305  ? 25.88900   109.71000 -37.80600 1.000 42.32401  ?  305  LEU   B O   1 
ATOM   16506 C  CB  . LEU   B 1 305  ? 25.75900   108.32700 -40.45300 1.000 33.72284  ?  305  LEU   B CB  1 
ATOM   16507 C  CG  . LEU   B 1 305  ? 26.41400   107.68200 -41.67500 1.000 36.49169  ?  305  LEU   B CG  1 
ATOM   16508 C  CD1 . LEU   B 1 305  ? 26.30500   106.17000 -41.60000 1.000 39.10408  ?  305  LEU   B CD1 1 
ATOM   16509 C  CD2 . LEU   B 1 305  ? 25.77500   108.18700 -42.94800 1.000 45.30677  ?  305  LEU   B CD2 1 
ATOM   16510 N  N   . THR   B 1 306  ? 24.51900   111.16900 -38.84200 1.000 42.48697  ?  306  THR   B N   1 
ATOM   16511 C  CA  . THR   B 1 306  ? 23.97900   111.68500 -37.58900 1.000 41.87126  ?  306  THR   B CA  1 
ATOM   16512 C  C   . THR   B 1 306  ? 22.56500   112.21100 -37.82600 1.000 44.78806  ?  306  THR   B C   1 
ATOM   16513 O  O   . THR   B 1 306  ? 21.99500   112.05300 -38.91100 1.000 40.14769  ?  306  THR   B O   1 
ATOM   16514 C  CB  . THR   B 1 306  ? 24.89800   112.76600 -37.00400 1.000 43.62420  ?  306  THR   B CB  1 
ATOM   16515 O  OG1 . THR   B 1 306  ? 24.32600   113.27600 -35.79300 1.000 36.65884  ?  306  THR   B OG1 1 
ATOM   16516 C  CG2 . THR   B 1 306  ? 25.08900   113.90800 -37.99700 1.000 37.01974  ?  306  THR   B CG2 1 
ATOM   16517 N  N   . ASN   B 1 307  ? 21.99700   112.82700 -36.79500 1.000 54.43757  ?  307  ASN   B N   1 
ATOM   16518 C  CA  . ASN   B 1 307  ? 20.66200   113.40600 -36.82200 1.000 41.16625  ?  307  ASN   B CA  1 
ATOM   16519 C  C   . ASN   B 1 307  ? 20.75000   114.92300 -36.85600 1.000 56.90910  ?  307  ASN   B C   1 
ATOM   16520 O  O   . ASN   B 1 307  ? 21.81300   115.51900 -36.66600 1.000 55.96615  ?  307  ASN   B O   1 
ATOM   16521 C  CB  . ASN   B 1 307  ? 19.84900   112.97600 -35.59500 1.000 39.66434  ?  307  ASN   B CB  1 
ATOM   16522 C  CG  . ASN   B 1 307  ? 19.45900   111.52000 -35.63400 1.000 69.60219  ?  307  ASN   B CG  1 
ATOM   16523 O  OD1 . ASN   B 1 307  ? 19.43400   110.90300 -36.69700 1.000 79.28840  ?  307  ASN   B OD1 1 
ATOM   16524 N  ND2 . ASN   B 1 307  ? 19.16400   110.95500 -34.46900 1.000 77.52746  ?  307  ASN   B ND2 1 
ATOM   16525 N  N   . ALA   B 1 308  ? 19.59500   115.54700 -37.08800 1.000 56.41209  ?  308  ALA   B N   1 
ATOM   16526 C  CA  . ALA   B 1 308  ? 19.50000   116.98900 -36.92300 1.000 58.53572  ?  308  ALA   B CA  1 
ATOM   16527 C  C   . ALA   B 1 308  ? 19.63200   117.39900 -35.46200 1.000 66.68396  ?  308  ALA   B C   1 
ATOM   16528 O  O   . ALA   B 1 308  ? 20.01300   118.54100 -35.18000 1.000 66.18003  ?  308  ALA   B O   1 
ATOM   16529 C  CB  . ALA   B 1 308  ? 18.17800   117.49200 -37.50100 1.000 42.00527  ?  308  ALA   B CB  1 
ATOM   16530 N  N   . LEU   B 1 309  ? 19.34000   116.48800 -34.53000 1.000 60.14873  ?  309  LEU   B N   1 
ATOM   16531 C  CA  . LEU   B 1 309  ? 19.45400   116.80200 -33.11000 1.000 45.48404  ?  309  LEU   B CA  1 
ATOM   16532 C  C   . LEU   B 1 309  ? 20.90800   116.99100 -32.70000 1.000 61.14519  ?  309  LEU   B C   1 
ATOM   16533 O  O   . LEU   B 1 309  ? 21.23300   117.91900 -31.95100 1.000 81.09658  ?  309  LEU   B O   1 
ATOM   16534 C  CB  . LEU   B 1 309  ? 18.80300   115.69300 -32.28300 1.000 53.68253  ?  309  LEU   B CB  1 
ATOM   16535 C  CG  . LEU   B 1 309  ? 18.04500   116.08200 -31.01300 1.000 66.08513  ?  309  LEU   B CG  1 
ATOM   16536 C  CD1 . LEU   B 1 309  ? 17.32300   114.86800 -30.44800 1.000 56.87841  ?  309  LEU   B CD1 1 
ATOM   16537 C  CD2 . LEU   B 1 309  ? 18.97200   116.69100 -29.96600 1.000 66.00283  ?  309  LEU   B CD2 1 
ATOM   16538 N  N   . HIS   B 1 310  ? 21.79600   116.12300 -33.17700 1.000 64.48320  ?  310  HIS   B N   1 
ATOM   16539 C  CA  . HIS   B 1 310  ? 23.19700   116.14800 -32.78500 1.000 57.15858  ?  310  HIS   B CA  1 
ATOM   16540 C  C   . HIS   B 1 310  ? 24.10000   116.73500 -33.86300 1.000 63.21129  ?  310  HIS   B C   1 
ATOM   16541 O  O   . HIS   B 1 310  ? 25.32300   116.58800 -33.77700 1.000 62.76252  ?  310  HIS   B O   1 
ATOM   16542 C  CB  . HIS   B 1 310  ? 23.65900   114.73600 -32.42300 1.000 54.21104  ?  310  HIS   B CB  1 
ATOM   16543 C  CG  . HIS   B 1 310  ? 22.64900   113.95200 -31.64300 1.000 57.98330  ?  310  HIS   B CG  1 
ATOM   16544 N  ND1 . HIS   B 1 310  ? 22.55600   114.01500 -30.26900 1.000 49.85592  ?  310  HIS   B ND1 1 
ATOM   16545 C  CD2 . HIS   B 1 310  ? 21.68500   113.09000 -32.04600 1.000 59.57850  ?  310  HIS   B CD2 1 
ATOM   16546 C  CE1 . HIS   B 1 310  ? 21.58100   113.22200 -29.85900 1.000 44.56785  ?  310  HIS   B CE1 1 
ATOM   16547 N  NE2 . HIS   B 1 310  ? 21.03700   112.65000 -30.91800 1.000 49.14805  ?  310  HIS   B NE2 1 
ATOM   16548 N  N   . GLU   B 1 311  ? 23.52700   117.40200 -34.86800 1.000 66.16040  ?  311  GLU   B N   1 
ATOM   16549 C  CA  . GLU   B 1 311  ? 24.32800   117.94600 -35.96100 1.000 55.57721  ?  311  GLU   B CA  1 
ATOM   16550 C  C   . GLU   B 1 311  ? 25.35200   118.95400 -35.45000 1.000 69.45319  ?  311  GLU   B C   1 
ATOM   16551 O  O   . GLU   B 1 311  ? 26.52800   118.90900 -35.83100 1.000 63.38377  ?  311  GLU   B O   1 
ATOM   16552 C  CB  . GLU   B 1 311  ? 23.41200   118.59200 -37.00000 1.000 67.39193  ?  311  GLU   B CB  1 
ATOM   16553 C  CG  . GLU   B 1 311  ? 23.80100   118.31600 -38.44100 1.000 79.67618  ?  311  GLU   B CG  1 
ATOM   16554 C  CD  . GLU   B 1 311  ? 23.11900   119.25900 -39.41300 1.000 94.06528  ?  311  GLU   B CD  1 
ATOM   16555 O  OE1 . GLU   B 1 311  ? 21.94400   119.00800 -39.76000 1.000 81.67772  ?  311  GLU   B OE1 1 
ATOM   16556 O  OE2 . GLU   B 1 311  ? 23.75600   120.25200 -39.82600 1.000 95.78928  -1 311  GLU   B OE2 1 
ATOM   16557 N  N   . GLU   B 1 312  ? 24.92200   119.86800 -34.57600 1.000 80.95630  ?  312  GLU   B N   1 
ATOM   16558 C  CA  . GLU   B 1 312  ? 25.80000   120.93700 -34.10900 1.000 75.03059  ?  312  GLU   B CA  1 
ATOM   16559 C  C   . GLU   B 1 312  ? 26.97600   120.41500 -33.29600 1.000 75.88509  ?  312  GLU   B C   1 
ATOM   16560 O  O   . GLU   B 1 312  ? 27.96900   121.13300 -33.13400 1.000 91.39862  ?  312  GLU   B O   1 
ATOM   16561 C  CB  . GLU   B 1 312  ? 25.00600   121.94500 -33.27600 1.000 83.39508  ?  312  GLU   B CB  1 
ATOM   16562 C  CG  . GLU   B 1 312  ? 24.38000   123.07100 -34.08500 1.000 97.28676  ?  312  GLU   B CG  1 
ATOM   16563 C  CD  . GLU   B 1 312  ? 23.07800   123.56700 -33.48400 1.000 115.97957 ?  312  GLU   B CD  1 
ATOM   16564 O  OE1 . GLU   B 1 312  ? 22.89200   123.42100 -32.25700 1.000 109.68255 ?  312  GLU   B OE1 1 
ATOM   16565 O  OE2 . GLU   B 1 312  ? 22.24000   124.10400 -34.23900 1.000 124.53668 -1 312  GLU   B OE2 1 
ATOM   16566 N  N   . LYS   B 1 313  ? 26.89300   119.18700 -32.78600 1.000 55.30394  ?  313  LYS   B N   1 
ATOM   16567 C  CA  . LYS   B 1 313  ? 27.97800   118.65400 -31.97200 1.000 66.56908  ?  313  LYS   B CA  1 
ATOM   16568 C  C   . LYS   B 1 313  ? 29.22800   118.35800 -32.79100 1.000 72.29817  ?  313  LYS   B C   1 
ATOM   16569 O  O   . LYS   B 1 313  ? 30.30500   118.18500 -32.21000 1.000 73.59443  ?  313  LYS   B O   1 
ATOM   16570 C  CB  . LYS   B 1 313  ? 27.51300   117.39400 -31.24200 1.000 71.70215  ?  313  LYS   B CB  1 
ATOM   16571 C  CG  . LYS   B 1 313  ? 26.56100   117.66600 -30.08700 1.000 72.69798  ?  313  LYS   B CG  1 
ATOM   16572 C  CD  . LYS   B 1 313  ? 25.91300   116.38400 -29.58300 1.000 62.77346  ?  313  LYS   B CD  1 
ATOM   16573 C  CE  . LYS   B 1 313  ? 25.08300   116.63700 -28.33300 1.000 61.96241  ?  313  LYS   B CE  1 
ATOM   16574 N  NZ  . LYS   B 1 313  ? 23.63500   116.36800 -28.56400 1.000 50.51420  ?  313  LYS   B NZ  1 
ATOM   16575 N  N   . ALA   B 1 314  ? 29.11500   118.29700 -34.11900 1.000 76.64259  ?  314  ALA   B N   1 
ATOM   16576 C  CA  . ALA   B 1 314  ? 30.27500   118.06300 -34.97000 1.000 62.35543  ?  314  ALA   B CA  1 
ATOM   16577 C  C   . ALA   B 1 314  ? 31.06900   119.33000 -35.25000 1.000 76.58180  ?  314  ALA   B C   1 
ATOM   16578 O  O   . ALA   B 1 314  ? 32.20000   119.23200 -35.73900 1.000 88.08750  ?  314  ALA   B O   1 
ATOM   16579 C  CB  . ALA   B 1 314  ? 29.84300   117.43800 -36.29800 1.000 59.05539  ?  314  ALA   B CB  1 
ATOM   16580 N  N   . ASN   B 1 315  ? 30.50200   120.50300 -34.95900 1.000 90.09367  ?  315  ASN   B N   1 
ATOM   16581 C  CA  . ASN   B 1 315  ? 31.15200   121.79200 -35.19700 1.000 89.37991  ?  315  ASN   B CA  1 
ATOM   16582 C  C   . ASN   B 1 315  ? 31.56400   121.95800 -36.65700 1.000 81.82181  ?  315  ASN   B C   1 
ATOM   16583 O  O   . ASN   B 1 315  ? 32.57200   122.60300 -36.95800 1.000 82.12094  ?  315  ASN   B O   1 
ATOM   16584 C  CB  . ASN   B 1 315  ? 32.36000   121.98500 -34.27400 1.000 73.38000  ?  315  ASN   B CB  1 
ATOM   16585 C  CG  . ASN   B 1 315  ? 32.48600   123.40900 -33.76800 1.000 91.61236  ?  315  ASN   B CG  1 
ATOM   16586 O  OD1 . ASN   B 1 315  ? 31.68600   124.27800 -34.11600 1.000 105.64982 ?  315  ASN   B OD1 1 
ATOM   16587 N  ND2 . ASN   B 1 315  ? 33.49900   123.65600 -32.94600 1.000 85.65105  ?  315  ASN   B ND2 1 
ATOM   16588 N  N   . GLY   B 1 316  ? 30.78900   121.37900 -37.56900 1.000 81.61012  ?  316  GLY   B N   1 
ATOM   16589 C  CA  . GLY   B 1 316  ? 31.07700   121.50400 -38.99000 1.000 102.46825 ?  316  GLY   B CA  1 
ATOM   16590 C  C   . GLY   B 1 316  ? 32.41200   120.92100 -39.39900 1.000 91.80892  ?  316  GLY   B C   1 
ATOM   16591 O  O   . GLY   B 1 316  ? 33.10400   121.49400 -40.25000 1.000 93.40476  ?  316  GLY   B O   1 
ATOM   16592 N  N   . ALA   B 1 317  ? 32.79100   119.78800 -38.81000 1.000 88.56305  ?  317  ALA   B N   1 
ATOM   16593 C  CA  . ALA   B 1 317  ? 34.07700   119.16600 -39.08700 1.000 84.30108  ?  317  ALA   B CA  1 
ATOM   16594 C  C   . ALA   B 1 317  ? 33.98700   117.99600 -40.05700 1.000 86.74138  ?  317  ALA   B C   1 
ATOM   16595 O  O   . ALA   B 1 317  ? 35.02900   117.49600 -40.49400 1.000 90.84344  ?  317  ALA   B O   1 
ATOM   16596 C  CB  . ALA   B 1 317  ? 34.72600   118.69100 -37.78100 1.000 62.26331  ?  317  ALA   B CB  1 
ATOM   16597 N  N   . CYS   B 1 318  ? 32.78200   117.55000 -40.40700 1.000 87.09696  ?  318  CYS   B N   1 
ATOM   16598 C  CA  . CYS   B 1 318  ? 32.61000   116.39400 -41.27300 1.000 84.25569  ?  318  CYS   B CA  1 
ATOM   16599 C  C   . CYS   B 1 318  ? 31.52500   116.67900 -42.29900 1.000 65.84049  ?  318  CYS   B C   1 
ATOM   16600 O  O   . CYS   B 1 318  ? 30.72100   117.60200 -42.14800 1.000 73.11066  ?  318  CYS   B O   1 
ATOM   16601 C  CB  . CYS   B 1 318  ? 32.24300   115.13300 -40.47400 1.000 81.75697  ?  318  CYS   B CB  1 
ATOM   16602 S  SG  . CYS   B 1 318  ? 33.57800   114.42100 -39.48200 1.000 91.04053  ?  318  CYS   B SG  1 
ATOM   16603 N  N   . ASP   B 1 319  ? 31.51400   115.86700 -43.35200 1.000 61.01681  ?  319  ASP   B N   1 
ATOM   16604 C  CA  . ASP   B 1 319  ? 30.42200   115.87000 -44.32100 1.000 68.32785  ?  319  ASP   B CA  1 
ATOM   16605 C  C   . ASP   B 1 319  ? 29.22100   115.19500 -43.67200 1.000 67.46528  ?  319  ASP   B C   1 
ATOM   16606 O  O   . ASP   B 1 319  ? 29.16100   113.96800 -43.57200 1.000 71.98835  ?  319  ASP   B O   1 
ATOM   16607 C  CB  . ASP   B 1 319  ? 30.84100   115.15300 -45.60000 1.000 72.82132  ?  319  ASP   B CB  1 
ATOM   16608 C  CG  . ASP   B 1 319  ? 29.77900   115.21100 -46.68800 1.000 83.69890  ?  319  ASP   B CG  1 
ATOM   16609 O  OD1 . ASP   B 1 319  ? 28.68500   115.76700 -46.44800 1.000 95.45744  ?  319  ASP   B OD1 1 
ATOM   16610 O  OD2 . ASP   B 1 319  ? 30.04100   114.69000 -47.79300 1.000 90.87163  -1 319  ASP   B OD2 1 
ATOM   16611 N  N   . ILE   B 1 320  ? 28.25800   115.99900 -43.22100 1.000 62.34472  ?  320  ILE   B N   1 
ATOM   16612 C  CA  . ILE   B 1 320  ? 27.09200   115.46000 -42.53600 1.000 56.57107  ?  320  ILE   B CA  1 
ATOM   16613 C  C   . ILE   B 1 320  ? 26.20100   114.72600 -43.52900 1.000 55.93537  ?  320  ILE   B C   1 
ATOM   16614 O  O   . ILE   B 1 320  ? 26.01900   115.16200 -44.67400 1.000 57.16661  ?  320  ILE   B O   1 
ATOM   16615 C  CB  . ILE   B 1 320  ? 26.32500   116.58800 -41.82400 1.000 55.83734  ?  320  ILE   B CB  1 
ATOM   16616 C  CG1 . ILE   B 1 320  ? 27.26500   117.37200 -40.90500 1.000 52.89203  ?  320  ILE   B CG1 1 
ATOM   16617 C  CG2 . ILE   B 1 320  ? 25.14200   116.03000 -41.04300 1.000 41.64040  ?  320  ILE   B CG2 1 
ATOM   16618 C  CD1 . ILE   B 1 320  ? 27.44700   116.75100 -39.53700 1.000 59.62905  ?  320  ILE   B CD1 1 
ATOM   16619 N  N   . ILE   B 1 321  ? 25.65400   113.59100 -43.09700 1.000 56.91791  ?  321  ILE   B N   1 
ATOM   16620 C  CA  . ILE   B 1 321  ? 24.65300   112.84600 -43.85200 1.000 47.54835  ?  321  ILE   B CA  1 
ATOM   16621 C  C   . ILE   B 1 321  ? 23.51200   112.53900 -42.89200 1.000 53.96068  ?  321  ILE   B C   1 
ATOM   16622 O  O   . ILE   B 1 321  ? 23.68000   111.74600 -41.95500 1.000 44.03133  ?  321  ILE   B O   1 
ATOM   16623 C  CB  . ILE   B 1 321  ? 25.21300   111.55600 -44.46300 1.000 42.37980  ?  321  ILE   B CB  1 
ATOM   16624 C  CG1 . ILE   B 1 321  ? 26.17200   111.88300 -45.60600 1.000 50.98214  ?  321  ILE   B CG1 1 
ATOM   16625 C  CG2 . ILE   B 1 321  ? 24.07800   110.66600 -44.96000 1.000 37.40981  ?  321  ILE   B CG2 1 
ATOM   16626 C  CD1 . ILE   B 1 321  ? 26.61400   110.67200 -46.38800 1.000 44.23710  ?  321  ILE   B CD1 1 
ATOM   16627 N  N   . ASP   B 1 322  ? 22.35800   113.16400 -43.11600 1.000 55.57101  ?  322  ASP   B N   1 
ATOM   16628 C  CA  . ASP   B 1 322  ? 21.20600   112.98200 -42.24100 1.000 51.58474  ?  322  ASP   B CA  1 
ATOM   16629 C  C   . ASP   B 1 322  ? 20.55500   111.63600 -42.53000 1.000 52.37913  ?  322  ASP   B C   1 
ATOM   16630 O  O   . ASP   B 1 322  ? 20.19300   111.34700 -43.67600 1.000 56.92894  ?  322  ASP   B O   1 
ATOM   16631 C  CB  . ASP   B 1 322  ? 20.20300   114.11800 -42.43200 1.000 57.12485  ?  322  ASP   B CB  1 
ATOM   16632 C  CG  . ASP   B 1 322  ? 19.03300   114.03500 -41.46400 1.000 72.36620  ?  322  ASP   B CG  1 
ATOM   16633 O  OD1 . ASP   B 1 322  ? 19.20600   114.38900 -40.27700 1.000 73.02151  ?  322  ASP   B OD1 1 
ATOM   16634 O  OD2 . ASP   B 1 322  ? 17.93700   113.61600 -41.89200 1.000 79.87971  -1 322  ASP   B OD2 1 
ATOM   16635 N  N   . VAL   B 1 323  ? 20.40700   110.80900 -41.48900 1.000 51.34333  ?  323  VAL   B N   1 
ATOM   16636 C  CA  . VAL   B 1 323  ? 19.79000   109.49500 -41.65700 1.000 55.30479  ?  323  VAL   B CA  1 
ATOM   16637 C  C   . VAL   B 1 323  ? 18.27300   109.55800 -41.65600 1.000 57.15655  ?  323  VAL   B C   1 
ATOM   16638 O  O   . VAL   B 1 323  ? 17.62200   108.52200 -41.84600 1.000 53.75889  ?  323  VAL   B O   1 
ATOM   16639 C  CB  . VAL   B 1 323  ? 20.26700   108.52100 -40.56200 1.000 53.22823  ?  323  VAL   B CB  1 
ATOM   16640 C  CG1 . VAL   B 1 323  ? 21.79100   108.41200 -40.56600 1.000 48.63990  ?  323  VAL   B CG1 1 
ATOM   16641 C  CG2 . VAL   B 1 323  ? 19.76200   108.96700 -39.20800 1.000 56.51245  ?  323  VAL   B CG2 1 
ATOM   16642 N  N   . HIS   B 1 324  ? 17.68500   110.73800 -41.44400 1.000 62.73373  ?  324  HIS   B N   1 
ATOM   16643 C  CA  . HIS   B 1 324  ? 16.24100   110.91400 -41.54300 1.000 60.83388  ?  324  HIS   B CA  1 
ATOM   16644 C  C   . HIS   B 1 324  ? 15.79600   111.46200 -42.89200 1.000 59.62550  ?  324  HIS   B C   1 
ATOM   16645 O  O   . HIS   B 1 324  ? 14.63500   111.26900 -43.26800 1.000 69.34464  ?  324  HIS   B O   1 
ATOM   16646 C  CB  . HIS   B 1 324  ? 15.73300   111.84800 -40.43500 1.000 66.67031  ?  324  HIS   B CB  1 
ATOM   16647 C  CG  . HIS   B 1 324  ? 15.78500   111.24900 -39.06400 1.000 81.94629  ?  324  HIS   B CG  1 
ATOM   16648 N  ND1 . HIS   B 1 324  ? 15.79500   112.01300 -37.91600 1.000 81.66136  ?  324  HIS   B ND1 1 
ATOM   16649 C  CD2 . HIS   B 1 324  ? 15.83000   109.95800 -38.65600 1.000 87.12664  ?  324  HIS   B CD2 1 
ATOM   16650 C  CE1 . HIS   B 1 324  ? 15.84400   111.21900 -36.86100 1.000 76.09882  ?  324  HIS   B CE1 1 
ATOM   16651 N  NE2 . HIS   B 1 324  ? 15.86700   109.96700 -37.28200 1.000 95.36398  ?  324  HIS   B NE2 1 
ATOM   16652 N  N   . ASP   B 1 325  ? 16.68500   112.13100 -43.61900 1.000 63.06475  ?  325  ASP   B N   1 
ATOM   16653 C  CA  . ASP   B 1 325  ? 16.35000   112.67900 -44.92800 1.000 73.37737  ?  325  ASP   B CA  1 
ATOM   16654 C  C   . ASP   B 1 325  ? 16.29200   111.55800 -45.96100 1.000 73.35481  ?  325  ASP   B C   1 
ATOM   16655 O  O   . ASP   B 1 325  ? 17.26600   110.81400 -46.11400 1.000 77.93193  ?  325  ASP   B O   1 
ATOM   16656 C  CB  . ASP   B 1 325  ? 17.37900   113.73200 -45.34100 1.000 71.09181  ?  325  ASP   B CB  1 
ATOM   16657 C  CG  . ASP   B 1 325  ? 17.40200   113.97600 -46.83800 1.000 80.67623  ?  325  ASP   B CG  1 
ATOM   16658 O  OD1 . ASP   B 1 325  ? 16.32100   114.18500 -47.42900 1.000 83.59713  ?  325  ASP   B OD1 1 
ATOM   16659 O  OD2 . ASP   B 1 325  ? 18.50500   113.96600 -47.42200 1.000 93.57761  -1 325  ASP   B OD2 1 
ATOM   16660 N  N   . PRO   B 1 326  ? 15.17600   111.40500 -46.68100 1.000 72.21402  ?  326  PRO   B N   1 
ATOM   16661 C  CA  . PRO   B 1 326  ? 15.06500   110.29200 -47.64000 1.000 67.49168  ?  326  PRO   B CA  1 
ATOM   16662 C  C   . PRO   B 1 326  ? 16.03200   110.38400 -48.80600 1.000 62.53487  ?  326  PRO   B C   1 
ATOM   16663 O  O   . PRO   B 1 326  ? 16.27600   109.36400 -49.46100 1.000 59.25729  ?  326  PRO   B O   1 
ATOM   16664 C  CB  . PRO   B 1 326  ? 13.60900   110.38200 -48.11900 1.000 68.56185  ?  326  PRO   B CB  1 
ATOM   16665 C  CG  . PRO   B 1 326  ? 12.90500   111.18800 -47.06800 1.000 74.79352  ?  326  PRO   B CG  1 
ATOM   16666 C  CD  . PRO   B 1 326  ? 13.92000   112.16200 -46.56500 1.000 64.61935  ?  326  PRO   B CD  1 
ATOM   16667 N  N   . ASP   B 1 327  ? 16.58700   111.56500 -49.09200 1.000 63.94007  ?  327  ASP   B N   1 
ATOM   16668 C  CA  . ASP   B 1 327  ? 17.55900   111.68300 -50.17300 1.000 79.96561  ?  327  ASP   B CA  1 
ATOM   16669 C  C   . ASP   B 1 327  ? 18.85600   110.94800 -49.86400 1.000 74.17302  ?  327  ASP   B C   1 
ATOM   16670 O  O   . ASP   B 1 327  ? 19.60200   110.61400 -50.79100 1.000 62.71346  ?  327  ASP   B O   1 
ATOM   16671 C  CB  . ASP   B 1 327  ? 17.85100   113.15600 -50.46700 1.000 81.43745  ?  327  ASP   B CB  1 
ATOM   16672 C  CG  . ASP   B 1 327  ? 16.73700   113.82700 -51.24800 1.000 87.37872  ?  327  ASP   B CG  1 
ATOM   16673 O  OD1 . ASP   B 1 327  ? 16.31000   113.26400 -52.27900 1.000 79.61071  ?  327  ASP   B OD1 1 
ATOM   16674 O  OD2 . ASP   B 1 327  ? 16.29100   114.91700 -50.83200 1.000 86.06157  -1 327  ASP   B OD2 1 
ATOM   16675 N  N   . SER   B 1 328  ? 19.13900   110.68800 -48.58600 1.000 70.63937  ?  328  SER   B N   1 
ATOM   16676 C  CA  . SER   B 1 328  ? 20.31500   109.92000 -48.20300 1.000 52.61485  ?  328  SER   B CA  1 
ATOM   16677 C  C   . SER   B 1 328  ? 20.16300   108.43100 -48.48000 1.000 50.62183  ?  328  SER   B C   1 
ATOM   16678 O  O   . SER   B 1 328  ? 21.13300   107.68700 -48.30300 1.000 56.22062  ?  328  SER   B O   1 
ATOM   16679 C  CB  . SER   B 1 328  ? 20.62100   110.13400 -46.71900 1.000 39.12283  ?  328  SER   B CB  1 
ATOM   16680 O  OG  . SER   B 1 328  ? 20.82500   111.50600 -46.43300 1.000 57.59810  ?  328  SER   B OG  1 
ATOM   16681 N  N   . TYR   B 1 329  ? 18.98500   107.98400 -48.90500 1.000 43.83073  ?  329  TYR   B N   1 
ATOM   16682 C  CA  . TYR   B 1 329  ? 18.70900   106.57400 -49.14900 1.000 51.25929  ?  329  TYR   B CA  1 
ATOM   16683 C  C   . TYR   B 1 329  ? 18.45200   106.35300 -50.63200 1.000 60.89834  ?  329  TYR   B C   1 
ATOM   16684 O  O   . TYR   B 1 329  ? 17.58200   107.00500 -51.22000 1.000 68.71809  ?  329  TYR   B O   1 
ATOM   16685 C  CB  . TYR   B 1 329  ? 17.50400   106.10100 -48.32700 1.000 47.16320  ?  329  TYR   B CB  1 
ATOM   16686 C  CG  . TYR   B 1 329  ? 17.74100   106.11700 -46.83300 1.000 47.36533  ?  329  TYR   B CG  1 
ATOM   16687 C  CD1 . TYR   B 1 329  ? 17.68300   107.30400 -46.11500 1.000 43.17214  ?  329  TYR   B CD1 1 
ATOM   16688 C  CD2 . TYR   B 1 329  ? 18.03000   104.94600 -46.14300 1.000 40.95973  ?  329  TYR   B CD2 1 
ATOM   16689 C  CE1 . TYR   B 1 329  ? 17.90400   107.32800 -44.75100 1.000 43.53194  ?  329  TYR   B CE1 1 
ATOM   16690 C  CE2 . TYR   B 1 329  ? 18.25200   104.95900 -44.77700 1.000 43.08395  ?  329  TYR   B CE2 1 
ATOM   16691 C  CZ  . TYR   B 1 329  ? 18.18700   106.15300 -44.08600 1.000 55.21319  ?  329  TYR   B CZ  1 
ATOM   16692 O  OH  . TYR   B 1 329  ? 18.40700   106.17500 -42.72700 1.000 56.08527  ?  329  TYR   B OH  1 
ATOM   16693 N  N   . SER   B 1 330  ? 19.20800   105.43900 -51.23200 1.000 53.99844  ?  330  SER   B N   1 
ATOM   16694 C  CA  . SER   B 1 330  ? 18.99300   105.09400 -52.62600 1.000 56.30691  ?  330  SER   B CA  1 
ATOM   16695 C  C   . SER   B 1 330  ? 17.78500   104.17100 -52.76400 1.000 45.14963  ?  330  SER   B C   1 
ATOM   16696 O  O   . SER   B 1 330  ? 17.20700   103.70100 -51.78200 1.000 55.67500  ?  330  SER   B O   1 
ATOM   16697 C  CB  . SER   B 1 330  ? 20.23500   104.43000 -53.21700 1.000 57.34741  ?  330  SER   B CB  1 
ATOM   16698 O  OG  . SER   B 1 330  ? 19.93100   103.12700 -53.68500 1.000 59.18588  ?  330  SER   B OG  1 
ATOM   16699 N  N   . GLU   B 1 331  ? 17.40400   103.91300 -54.01100 1.000 55.96226  ?  331  GLU   B N   1 
ATOM   16700 C  CA  . GLU   B 1 331  ? 16.26400   103.05500 -54.30000 1.000 56.30634  ?  331  GLU   B CA  1 
ATOM   16701 C  C   . GLU   B 1 331  ? 16.65800   101.60000 -54.49000 1.000 52.76778  ?  331  GLU   B C   1 
ATOM   16702 O  O   . GLU   B 1 331  ? 15.78100   100.72800 -54.47300 1.000 62.72393  ?  331  GLU   B O   1 
ATOM   16703 C  CB  . GLU   B 1 331  ? 15.52500   103.55500 -55.54900 1.000 63.38101  ?  331  GLU   B CB  1 
ATOM   16704 C  CG  . GLU   B 1 331  ? 16.43100   103.97800 -56.70400 1.000 74.83659  ?  331  GLU   B CG  1 
ATOM   16705 C  CD  . GLU   B 1 331  ? 17.02600   105.36600 -56.51800 1.000 94.50846  ?  331  GLU   B CD  1 
ATOM   16706 O  OE1 . GLU   B 1 331  ? 16.25700   106.31200 -56.24700 1.000 96.52960  ?  331  GLU   B OE1 1 
ATOM   16707 O  OE2 . GLU   B 1 331  ? 18.26400   105.50600 -56.63000 1.000 86.71409  -1 331  GLU   B OE2 1 
ATOM   16708 N  N   . ASN   B 1 332  ? 17.94600   101.31900 -54.66700 1.000 47.62872  ?  332  ASN   B N   1 
ATOM   16709 C  CA  . ASN   B 1 332  ? 18.42500   99.95200  -54.82800 1.000 48.53830  ?  332  ASN   B CA  1 
ATOM   16710 C  C   . ASN   B 1 332  ? 18.45300   99.28500  -53.45900 1.000 49.47200  ?  332  ASN   B C   1 
ATOM   16711 O  O   . ASN   B 1 332  ? 19.26000   99.64700  -52.59700 1.000 57.81422  ?  332  ASN   B O   1 
ATOM   16712 C  CB  . ASN   B 1 332  ? 19.80500   99.94100  -55.48200 1.000 39.22162  ?  332  ASN   B CB  1 
ATOM   16713 C  CG  . ASN   B 1 332  ? 20.17100   98.58100  -56.04900 1.000 52.62831  ?  332  ASN   B CG  1 
ATOM   16714 O  OD1 . ASN   B 1 332  ? 19.58300   97.56400  -55.68100 1.000 58.95213  ?  332  ASN   B OD1 1 
ATOM   16715 N  ND2 . ASN   B 1 332  ? 21.14600   98.55600  -56.95200 1.000 72.04190  ?  332  ASN   B ND2 1 
ATOM   16716 N  N   . THR   B 1 333  ? 17.56100   98.32200  -53.24900 1.000 47.88553  ?  333  THR   B N   1 
ATOM   16717 C  CA  . THR   B 1 333  ? 17.51200   97.57600  -52.00300 1.000 50.47138  ?  333  THR   B CA  1 
ATOM   16718 C  C   . THR   B 1 333  ? 18.28200   96.26700  -52.08300 1.000 44.36718  ?  333  THR   B C   1 
ATOM   16719 O  O   . THR   B 1 333  ? 18.20300   95.45400  -51.15800 1.000 53.46569  ?  333  THR   B O   1 
ATOM   16720 C  CB  . THR   B 1 333  ? 16.05900   97.30500  -51.60000 1.000 42.02899  ?  333  THR   B CB  1 
ATOM   16721 O  OG1 . THR   B 1 333  ? 15.44800   96.42500  -52.55300 1.000 43.70553  ?  333  THR   B OG1 1 
ATOM   16722 C  CG2 . THR   B 1 333  ? 15.27200   98.60600  -51.53300 1.000 34.05490  ?  333  THR   B CG2 1 
ATOM   16723 N  N   . ASN   B 1 334  ? 19.02100   96.04500  -53.16100 1.000 44.37978  ?  334  ASN   B N   1 
ATOM   16724 C  CA  . ASN   B 1 334  ? 19.75400   94.80200  -53.32200 1.000 52.56850  ?  334  ASN   B CA  1 
ATOM   16725 C  C   . ASN   B 1 334  ? 21.11300   94.89400  -52.63900 1.000 50.59226  ?  334  ASN   B C   1 
ATOM   16726 O  O   . ASN   B 1 334  ? 21.63700   95.98100  -52.37900 1.000 47.22674  ?  334  ASN   B O   1 
ATOM   16727 C  CB  . ASN   B 1 334  ? 19.92800   94.46200  -54.80300 1.000 53.44160  ?  334  ASN   B CB  1 
ATOM   16728 C  CG  . ASN   B 1 334  ? 18.61500   94.12300  -55.48500 1.000 66.48714  ?  334  ASN   B CG  1 
ATOM   16729 O  OD1 . ASN   B 1 334  ? 17.56100   94.66200  -55.14100 1.000 65.27262  ?  334  ASN   B OD1 1 
ATOM   16730 N  ND2 . ASN   B 1 334  ? 18.67400   93.23000  -56.46500 1.000 84.43791  ?  334  ASN   B ND2 1 
ATOM   16731 N  N   . ASN   B 1 335  ? 21.67900   93.72700  -52.34400 1.000 46.73091  ?  335  ASN   B N   1 
ATOM   16732 C  CA  . ASN   B 1 335  ? 22.98200   93.67300  -51.69900 1.000 38.57910  ?  335  ASN   B CA  1 
ATOM   16733 C  C   . ASN   B 1 335  ? 24.05000   94.30000  -52.58500 1.000 48.72666  ?  335  ASN   B C   1 
ATOM   16734 O  O   . ASN   B 1 335  ? 24.04800   94.13100  -53.80700 1.000 53.85684  ?  335  ASN   B O   1 
ATOM   16735 C  CB  . ASN   B 1 335  ? 23.34800   92.22800  -51.37900 1.000 29.82909  ?  335  ASN   B CB  1 
ATOM   16736 C  CG  . ASN   B 1 335  ? 22.58400   91.69100  -50.19800 1.000 26.71084  ?  335  ASN   B CG  1 
ATOM   16737 O  OD1 . ASN   B 1 335  ? 21.96300   92.44900  -49.45300 1.000 30.10842  ?  335  ASN   B OD1 1 
ATOM   16738 N  ND2 . ASN   B 1 335  ? 22.62700   90.37900  -50.01100 1.000 29.06649  ?  335  ASN   B ND2 1 
ATOM   16739 N  N   . LEU   B 1 336  ? 24.96500   95.03100  -51.95800 1.000 51.46198  ?  336  LEU   B N   1 
ATOM   16740 C  CA  . LEU   B 1 336  ? 26.05400   95.64400  -52.69800 1.000 46.60461  ?  336  LEU   B CA  1 
ATOM   16741 C  C   . LEU   B 1 336  ? 27.02100   94.56900  -53.19600 1.000 48.79098  ?  336  LEU   B C   1 
ATOM   16742 O  O   . LEU   B 1 336  ? 27.10200   93.47800  -52.62100 1.000 42.18948  ?  336  LEU   B O   1 
ATOM   16743 C  CB  . LEU   B 1 336  ? 26.80300   96.64100  -51.81600 1.000 46.08138  ?  336  LEU   B CB  1 
ATOM   16744 C  CG  . LEU   B 1 336  ? 26.31100   98.08500  -51.68900 1.000 38.43718  ?  336  LEU   B CG  1 
ATOM   16745 C  CD1 . LEU   B 1 336  ? 26.62300   98.86500  -52.95200 1.000 48.53688  ?  336  LEU   B CD1 1 
ATOM   16746 C  CD2 . LEU   B 1 336  ? 24.82800   98.13800  -51.37200 1.000 48.47403  ?  336  LEU   B CD2 1 
ATOM   16747 N  N   . PRO   B 1 337  ? 27.75700   94.84300  -54.27300 1.000 44.26490  ?  337  PRO   B N   1 
ATOM   16748 C  CA  . PRO   B 1 337  ? 28.83500   93.92900  -54.67500 1.000 47.37530  ?  337  PRO   B CA  1 
ATOM   16749 C  C   . PRO   B 1 337  ? 29.97800   93.99100  -53.67300 1.000 46.34596  ?  337  PRO   B C   1 
ATOM   16750 O  O   . PRO   B 1 337  ? 30.43800   95.07400  -53.30400 1.000 38.97970  ?  337  PRO   B O   1 
ATOM   16751 C  CB  . PRO   B 1 337  ? 29.26300   94.45600  -56.05000 1.000 39.18318  ?  337  PRO   B CB  1 
ATOM   16752 C  CG  . PRO   B 1 337  ? 28.15700   95.36600  -56.49000 1.000 47.03973  ?  337  PRO   B CG  1 
ATOM   16753 C  CD  . PRO   B 1 337  ? 27.58400   95.94100  -55.23600 1.000 43.88832  ?  337  PRO   B CD  1 
ATOM   16754 N  N   . HIS   B 1 338  ? 30.44000   92.81900  -53.24100 1.000 43.30206  ?  338  HIS   B N   1 
ATOM   16755 C  CA  . HIS   B 1 338  ? 31.41700   92.75500  -52.16100 1.000 48.82460  ?  338  HIS   B CA  1 
ATOM   16756 C  C   . HIS   B 1 338  ? 32.77900   93.25700  -52.63000 1.000 42.92089  ?  338  HIS   B C   1 
ATOM   16757 O  O   . HIS   B 1 338  ? 33.26900   92.85900  -53.69100 1.000 39.68516  ?  338  HIS   B O   1 
ATOM   16758 C  CB  . HIS   B 1 338  ? 31.52000   91.32600  -51.63300 1.000 34.39082  ?  338  HIS   B CB  1 
ATOM   16759 C  CG  . HIS   B 1 338  ? 30.29000   90.86400  -50.91600 1.000 61.92653  ?  338  HIS   B CG  1 
ATOM   16760 N  ND1 . HIS   B 1 338  ? 29.54200   91.70000  -50.11400 1.000 75.28538  ?  338  HIS   B ND1 1 
ATOM   16761 C  CD2 . HIS   B 1 338  ? 29.67400   89.65900  -50.88300 1.000 55.53198  ?  338  HIS   B CD2 1 
ATOM   16762 C  CE1 . HIS   B 1 338  ? 28.51900   91.02900  -49.61600 1.000 57.22829  ?  338  HIS   B CE1 1 
ATOM   16763 N  NE2 . HIS   B 1 338  ? 28.57600   89.78800  -50.06600 1.000 74.20238  ?  338  HIS   B NE2 1 
ATOM   16764 N  N   . VAL   B 1 339  ? 33.38900   94.13700  -51.83400 1.000 32.67700  ?  339  VAL   B N   1 
ATOM   16765 C  CA  . VAL   B 1 339  ? 34.67700   94.72800  -52.18300 1.000 46.17596  ?  339  VAL   B CA  1 
ATOM   16766 C  C   . VAL   B 1 339  ? 35.65400   94.60500  -51.02000 1.000 47.98912  ?  339  VAL   B C   1 
ATOM   16767 O  O   . VAL   B 1 339  ? 36.73600   95.20400  -51.03900 1.000 42.52078  ?  339  VAL   B O   1 
ATOM   16768 C  CB  . VAL   B 1 339  ? 34.51200   96.20200  -52.59100 1.000 38.80370  ?  339  VAL   B CB  1 
ATOM   16769 C  CG1 . VAL   B 1 339  ? 33.65100   96.30800  -53.82900 1.000 40.96504  ?  339  VAL   B CG1 1 
ATOM   16770 C  CG2 . VAL   B 1 339  ? 33.91200   96.99900  -51.44700 1.000 32.12253  ?  339  VAL   B CG2 1 
ATOM   16771 N  N   . ASN   B 1 340  ? 35.28600   93.82700  -50.00700 1.000 47.09332  ?  340  ASN   B N   1 
ATOM   16772 C  CA  . ASN   B 1 340  ? 36.03000   93.76100  -48.75900 1.000 32.62368  ?  340  ASN   B CA  1 
ATOM   16773 C  C   . ASN   B 1 340  ? 36.74600   92.42800  -48.61300 1.000 41.28484  ?  340  ASN   B C   1 
ATOM   16774 O  O   . ASN   B 1 340  ? 36.26900   91.38900  -49.07900 1.000 33.72828  ?  340  ASN   B O   1 
ATOM   16775 C  CB  . ASN   B 1 340  ? 35.10500   93.95900  -47.55900 1.000 35.32959  ?  340  ASN   B CB  1 
ATOM   16776 C  CG  . ASN   B 1 340  ? 34.90800   95.41100  -47.21400 1.000 40.68741  ?  340  ASN   B CG  1 
ATOM   16777 O  OD1 . ASN   B 1 340  ? 33.78000   95.86500  -47.03200 1.000 53.35003  ?  340  ASN   B OD1 1 
ATOM   16778 N  ND2 . ASN   B 1 340  ? 36.00600   96.15300  -47.11800 1.000 27.28278  ?  340  ASN   B ND2 1 
ATOM   16779 N  N   . ARG   B 1 341  ? 37.89600   92.47500  -47.94600 1.000 46.47700  ?  341  ARG   B N   1 
ATOM   16780 C  CA  . ARG   B 1 341  ? 38.66100   91.33000  -47.49100 1.000 35.59366  ?  341  ARG   B CA  1 
ATOM   16781 C  C   . ARG   B 1 341  ? 38.56800   91.22300  -45.97100 1.000 37.99160  ?  341  ARG   B C   1 
ATOM   16782 O  O   . ARG   B 1 341  ? 38.39800   92.23700  -45.28400 1.000 30.03866  ?  341  ARG   B O   1 
ATOM   16783 C  CB  . ARG   B 1 341  ? 40.13400   91.44400  -47.90800 1.000 51.15585  ?  341  ARG   B CB  1 
ATOM   16784 C  CG  . ARG   B 1 341  ? 40.39300   91.17100  -49.38600 1.000 66.46763  ?  341  ARG   B CG  1 
ATOM   16785 C  CD  . ARG   B 1 341  ? 41.61200   91.94000  -49.90600 1.000 82.61820  ?  341  ARG   B CD  1 
ATOM   16786 N  NE  . ARG   B 1 341  ? 41.64400   93.32600  -49.44800 1.000 96.85157  ?  341  ARG   B NE  1 
ATOM   16787 C  CZ  . ARG   B 1 341  ? 41.09300   94.34900  -50.09100 1.000 85.43457  ?  341  ARG   B CZ  1 
ATOM   16788 N  NH1 . ARG   B 1 341  ? 40.44600   94.18000  -51.23300 1.000 71.32949  ?  341  ARG   B NH1 1 
ATOM   16789 N  NH2 . ARG   B 1 341  ? 41.19400   95.57100  -49.57500 1.000 59.12954  ?  341  ARG   B NH2 1 
ATOM   16790 N  N   . PRO   B 1 342  ? 38.66800   90.01300  -45.41400 1.000 31.42970  ?  342  PRO   B N   1 
ATOM   16791 C  CA  . PRO   B 1 342  ? 38.47400   89.85400  -43.96200 1.000 24.03079  ?  342  PRO   B CA  1 
ATOM   16792 C  C   . PRO   B 1 342  ? 39.45500   90.63900  -43.10700 1.000 29.86820  ?  342  PRO   B C   1 
ATOM   16793 O  O   . PRO   B 1 342  ? 39.16600   90.87200  -41.92700 1.000 35.50022  ?  342  PRO   B O   1 
ATOM   16794 C  CB  . PRO   B 1 342  ? 38.64000   88.34400  -43.75300 1.000 30.86885  ?  342  PRO   B CB  1 
ATOM   16795 C  CG  . PRO   B 1 342  ? 38.28300   87.74800  -45.06700 1.000 27.55434  ?  342  PRO   B CG  1 
ATOM   16796 C  CD  . PRO   B 1 342  ? 38.78700   88.71500  -46.09700 1.000 32.37099  ?  342  PRO   B CD  1 
ATOM   16797 N  N   . ASP   B 1 343  ? 40.59900   91.05500  -43.64500 1.000 36.00848  ?  343  ASP   B N   1 
ATOM   16798 C  CA  . ASP   B 1 343  ? 41.56100   91.83600  -42.88000 1.000 33.87955  ?  343  ASP   B CA  1 
ATOM   16799 C  C   . ASP   B 1 343  ? 41.30400   93.33800  -42.95700 1.000 36.93565  ?  343  ASP   B C   1 
ATOM   16800 O  O   . ASP   B 1 343  ? 42.12400   94.11800  -42.46400 1.000 43.19942  ?  343  ASP   B O   1 
ATOM   16801 C  CB  . ASP   B 1 343  ? 42.98400   91.52900  -43.34800 1.000 39.83728  ?  343  ASP   B CB  1 
ATOM   16802 C  CG  . ASP   B 1 343  ? 43.05900   91.27700  -44.83200 1.000 50.93563  ?  343  ASP   B CG  1 
ATOM   16803 O  OD1 . ASP   B 1 343  ? 42.50200   90.25600  -45.28800 1.000 51.28540  ?  343  ASP   B OD1 1 
ATOM   16804 O  OD2 . ASP   B 1 343  ? 43.66700   92.10500  -45.54200 1.000 63.60006  -1 343  ASP   B OD2 1 
ATOM   16805 N  N   . ASP   B 1 344  ? 40.19400   93.75900  -43.55900 1.000 39.89285  ?  344  ASP   B N   1 
ATOM   16806 C  CA  . ASP   B 1 344  ? 39.84400   95.17100  -43.60500 1.000 37.48444  ?  344  ASP   B CA  1 
ATOM   16807 C  C   . ASP   B 1 344  ? 39.19000   95.60200  -42.29700 1.000 32.84570  ?  344  ASP   B C   1 
ATOM   16808 O  O   . ASP   B 1 344  ? 38.55600   94.80200  -41.60200 1.000 43.50455  ?  344  ASP   B O   1 
ATOM   16809 C  CB  . ASP   B 1 344  ? 38.90000   95.45600  -44.77500 1.000 32.75280  ?  344  ASP   B CB  1 
ATOM   16810 C  CG  . ASP   B 1 344  ? 39.56800   95.26200  -46.12200 1.000 51.38487  ?  344  ASP   B CG  1 
ATOM   16811 O  OD1 . ASP   B 1 344  ? 40.79400   95.49100  -46.21300 1.000 68.43591  ?  344  ASP   B OD1 1 
ATOM   16812 O  OD2 . ASP   B 1 344  ? 38.86800   94.88600  -47.08900 1.000 43.57981  -1 344  ASP   B OD2 1 
ATOM   16813 N  N   . LEU   B 1 345  ? 39.34900   96.88100  -41.96200 1.000 22.93030  ?  345  LEU   B N   1 
ATOM   16814 C  CA  . LEU   B 1 345  ? 38.74400   97.40800  -40.74600 1.000 33.38757  ?  345  LEU   B CA  1 
ATOM   16815 C  C   . LEU   B 1 345  ? 37.23000   97.21700  -40.76400 1.000 40.57212  ?  345  LEU   B C   1 
ATOM   16816 O  O   . LEU   B 1 345  ? 36.58900   97.23400  -41.81900 1.000 35.86769  ?  345  LEU   B O   1 
ATOM   16817 C  CB  . LEU   B 1 345  ? 39.07100   98.89300  -40.58800 1.000 30.30348  ?  345  LEU   B CB  1 
ATOM   16818 C  CG  . LEU   B 1 345  ? 40.50800   99.28200  -40.24200 1.000 34.66359  ?  345  LEU   B CG  1 
ATOM   16819 C  CD1 . LEU   B 1 345  ? 40.58500   100.76200 -39.89300 1.000 32.11922  ?  345  LEU   B CD1 1 
ATOM   16820 C  CD2 . LEU   B 1 345  ? 41.04200   98.43100  -39.10300 1.000 34.07860  ?  345  LEU   B CD2 1 
ATOM   16821 N  N   . VAL   B 1 346  ? 36.65800   97.02600  -39.57100 1.000 40.57413  ?  346  VAL   B N   1 
ATOM   16822 C  CA  . VAL   B 1 346  ? 35.21700   96.92100  -39.39300 1.000 30.53906  ?  346  VAL   B CA  1 
ATOM   16823 C  C   . VAL   B 1 346  ? 34.68300   97.97600  -38.43200 1.000 27.61187  ?  346  VAL   B C   1 
ATOM   16824 O  O   . VAL   B 1 346  ? 33.57100   98.48100  -38.62300 1.000 42.79690  ?  346  VAL   B O   1 
ATOM   16825 C  CB  . VAL   B 1 346  ? 34.80300   95.50400  -38.93000 1.000 29.30415  ?  346  VAL   B CB  1 
ATOM   16826 C  CG1 . VAL   B 1 346  ? 35.36000   95.18400  -37.53600 1.000 26.06391  ?  346  VAL   B CG1 1 
ATOM   16827 C  CG2 . VAL   B 1 346  ? 33.28300   95.35200  -38.97000 1.000 26.83611  ?  346  VAL   B CG2 1 
ATOM   16828 N  N   . TYR   B 1 347  ? 35.44800   98.32900  -37.40100 1.000 31.32259  ?  347  TYR   B N   1 
ATOM   16829 C  CA  . TYR   B 1 347  ? 35.09100   99.44200  -36.53100 1.000 40.71208  ?  347  TYR   B CA  1 
ATOM   16830 C  C   . TYR   B 1 347  ? 36.34300   99.93400  -35.82100 1.000 32.04532  ?  347  TYR   B C   1 
ATOM   16831 O  O   . TYR   B 1 347  ? 37.34100   99.21800  -35.71300 1.000 23.10189  ?  347  TYR   B O   1 
ATOM   16832 C  CB  . TYR   B 1 347  ? 33.98400   99.07800  -35.51400 1.000 35.76027  ?  347  TYR   B CB  1 
ATOM   16833 C  CG  . TYR   B 1 347  ? 34.33400   98.02900  -34.46800 1.000 21.93553  ?  347  TYR   B CG  1 
ATOM   16834 C  CD1 . TYR   B 1 347  ? 35.18200   98.32100  -33.40800 1.000 22.48017  ?  347  TYR   B CD1 1 
ATOM   16835 C  CD2 . TYR   B 1 347  ? 33.79000   96.75100  -34.53300 1.000 22.74361  ?  347  TYR   B CD2 1 
ATOM   16836 C  CE1 . TYR   B 1 347  ? 35.50100   97.36700  -32.46600 1.000 31.16377  ?  347  TYR   B CE1 1 
ATOM   16837 C  CE2 . TYR   B 1 347  ? 34.09900   95.78900  -33.58400 1.000 22.35222  ?  347  TYR   B CE2 1 
ATOM   16838 C  CZ  . TYR   B 1 347  ? 34.95600   96.10700  -32.55100 1.000 25.97972  ?  347  TYR   B CZ  1 
ATOM   16839 O  OH  . TYR   B 1 347  ? 35.28300   95.17200  -31.59600 1.000 43.24600  ?  347  TYR   B OH  1 
ATOM   16840 N  N   . VAL   B 1 348  ? 36.27900   101.17700 -35.34800 1.000 30.61231  ?  348  VAL   B N   1 
ATOM   16841 C  CA  . VAL   B 1 348  ? 37.35300   101.78600 -34.57200 1.000 31.38846  ?  348  VAL   B CA  1 
ATOM   16842 C  C   . VAL   B 1 348  ? 36.72700   102.26000 -33.26700 1.000 43.07684  ?  348  VAL   B C   1 
ATOM   16843 O  O   . VAL   B 1 348  ? 35.99400   103.25700 -33.23900 1.000 32.85563  ?  348  VAL   B O   1 
ATOM   16844 C  CB  . VAL   B 1 348  ? 38.03900   102.93600 -35.31700 1.000 25.79311  ?  348  VAL   B CB  1 
ATOM   16845 C  CG1 . VAL   B 1 348  ? 39.00400   103.65800 -34.39300 1.000 21.13677  ?  348  VAL   B CG1 1 
ATOM   16846 C  CG2 . VAL   B 1 348  ? 38.77200   102.40900 -36.54200 1.000 37.58352  ?  348  VAL   B CG2 1 
ATOM   16847 N  N   . MET   B 1 349  ? 36.98800   101.52900 -32.19000 1.000 42.42694  ?  349  MET   B N   1 
ATOM   16848 C  CA  . MET   B 1 349  ? 36.56400   101.91500 -30.85500 1.000 36.62640  ?  349  MET   B CA  1 
ATOM   16849 C  C   . MET   B 1 349  ? 37.69200   102.65400 -30.14400 1.000 34.30310  ?  349  MET   B C   1 
ATOM   16850 O  O   . MET   B 1 349  ? 38.86800   102.52300 -30.49000 1.000 46.65736  ?  349  MET   B O   1 
ATOM   16851 C  CB  . MET   B 1 349  ? 36.15400   100.68400 -30.04900 1.000 47.11634  ?  349  MET   B CB  1 
ATOM   16852 C  CG  . MET   B 1 349  ? 34.89400   100.86600 -29.24000 1.000 40.59691  ?  349  MET   B CG  1 
ATOM   16853 S  SD  . MET   B 1 349  ? 33.42200   100.39800 -30.16500 1.000 49.00767  ?  349  MET   B SD  1 
ATOM   16854 C  CE  . MET   B 1 349  ? 33.53200   98.62100  -30.15100 1.000 22.42560  ?  349  MET   B CE  1 
ATOM   16855 N  N   . TYR   B 1 350  ? 37.32000   103.43500 -29.13500 1.000 34.59367  ?  350  TYR   B N   1 
ATOM   16856 C  CA  . TYR   B 1 350  ? 38.26700   104.23700 -28.37800 1.000 35.86003  ?  350  TYR   B CA  1 
ATOM   16857 C  C   . TYR   B 1 350  ? 38.29800   103.77800 -26.92600 1.000 41.49619  ?  350  TYR   B C   1 
ATOM   16858 O  O   . TYR   B 1 350  ? 37.30300   103.27600 -26.39400 1.000 52.87819  ?  350  TYR   B O   1 
ATOM   16859 C  CB  . TYR   B 1 350  ? 37.91600   105.73200 -28.44600 1.000 35.22514  ?  350  TYR   B CB  1 
ATOM   16860 C  CG  . TYR   B 1 350  ? 38.41800   106.41700 -29.69700 1.000 39.27304  ?  350  TYR   B CG  1 
ATOM   16861 C  CD1 . TYR   B 1 350  ? 37.79900   106.20900 -30.92500 1.000 41.10702  ?  350  TYR   B CD1 1 
ATOM   16862 C  CD2 . TYR   B 1 350  ? 39.52000   107.26100 -29.65600 1.000 45.14240  ?  350  TYR   B CD2 1 
ATOM   16863 C  CE1 . TYR   B 1 350  ? 38.25900   106.82900 -32.07400 1.000 46.02802  ?  350  TYR   B CE1 1 
ATOM   16864 C  CE2 . TYR   B 1 350  ? 39.98900   107.88400 -30.79900 1.000 49.15755  ?  350  TYR   B CE2 1 
ATOM   16865 C  CZ  . TYR   B 1 350  ? 39.35500   107.66500 -32.00500 1.000 51.67155  ?  350  TYR   B CZ  1 
ATOM   16866 O  OH  . TYR   B 1 350  ? 39.81800   108.28200 -33.14300 1.000 51.05702  ?  350  TYR   B OH  1 
ATOM   16867 N  N   . THR   B 1 351  ? 39.45100   103.95300 -26.29100 1.000 50.90895  ?  351  THR   B N   1 
ATOM   16868 C  CA  . THR   B 1 351  ? 39.62700   103.58100 -24.89800 1.000 47.74894  ?  351  THR   B CA  1 
ATOM   16869 C  C   . THR   B 1 351  ? 39.26600   104.74600 -23.97900 1.000 68.85624  ?  351  THR   B C   1 
ATOM   16870 O  O   . THR   B 1 351  ? 39.08200   105.88600 -24.41200 1.000 59.33602  ?  351  THR   B O   1 
ATOM   16871 C  CB  . THR   B 1 351  ? 41.06200   103.13300 -24.63900 1.000 49.08808  ?  351  THR   B CB  1 
ATOM   16872 O  OG1 . THR   B 1 351  ? 41.93100   104.27000 -24.70000 1.000 58.19845  ?  351  THR   B OG1 1 
ATOM   16873 C  CG2 . THR   B 1 351  ? 41.49300   102.11600 -25.67600 1.000 48.16876  ?  351  THR   B CG2 1 
ATOM   16874 N  N   . SER   B 1 352  ? 39.17800   104.44300 -22.68800 1.000 72.41919  ?  352  SER   B N   1 
ATOM   16875 C  CA  . SER   B 1 352  ? 38.78500   105.44100 -21.70800 1.000 77.11118  ?  352  SER   B CA  1 
ATOM   16876 C  C   . SER   B 1 352  ? 39.90600   106.45500 -21.49500 1.000 94.37620  ?  352  SER   B C   1 
ATOM   16877 O  O   . SER   B 1 352  ? 41.05600   106.25500 -21.89800 1.000 92.02094  ?  352  SER   B O   1 
ATOM   16878 C  CB  . SER   B 1 352  ? 38.42100   104.77300 -20.38500 1.000 89.12532  ?  352  SER   B CB  1 
ATOM   16879 O  OG  . SER   B 1 352  ? 39.59100   104.40500 -19.67600 1.000 83.22903  ?  352  SER   B OG  1 
ATOM   16880 N  N   . GLY   B 1 353  ? 39.55400   107.56000 -20.84300 1.000 101.08296 ?  353  GLY   B N   1 
ATOM   16881 C  CA  . GLY   B 1 353  ? 40.51700   108.60000 -20.53800 1.000 108.43255 ?  353  GLY   B CA  1 
ATOM   16882 C  C   . GLY   B 1 353  ? 40.74500   108.78600 -19.05200 1.000 115.03754 ?  353  GLY   B C   1 
ATOM   16883 O  O   . GLY   B 1 353  ? 40.97200   109.90900 -18.59100 1.000 130.59939 ?  353  GLY   B O   1 
ATOM   16884 N  N   . SER   B 1 354  ? 40.67900   107.69000 -18.29200 1.000 108.04977 ?  354  SER   B N   1 
ATOM   16885 C  CA  . SER   B 1 354  ? 40.95300   107.76100 -16.85900 1.000 116.32631 ?  354  SER   B CA  1 
ATOM   16886 C  C   . SER   B 1 354  ? 42.37800   108.23400 -16.60300 1.000 122.32572 ?  354  SER   B C   1 
ATOM   16887 O  O   . SER   B 1 354  ? 42.60300   109.20300 -15.86900 1.000 117.71550 ?  354  SER   B O   1 
ATOM   16888 C  CB  . SER   B 1 354  ? 40.70800   106.39700 -16.21300 1.000 123.00999 ?  354  SER   B CB  1 
ATOM   16889 O  OG  . SER   B 1 354  ? 41.28000   105.35800 -16.98900 1.000 119.32821 ?  354  SER   B OG  1 
ATOM   16890 N  N   . THR   B 1 355  ? 43.35700   107.55800 -17.20400 1.000 124.35302 ?  355  THR   B N   1 
ATOM   16891 C  CA  . THR   B 1 355  ? 44.73300   108.03800 -17.21700 1.000 119.52879 ?  355  THR   B CA  1 
ATOM   16892 C  C   . THR   B 1 355  ? 44.96500   109.10300 -18.28100 1.000 124.29634 ?  355  THR   B C   1 
ATOM   16893 O  O   . THR   B 1 355  ? 46.09200   109.59500 -18.41000 1.000 102.17209 ?  355  THR   B O   1 
ATOM   16894 C  CB  . THR   B 1 355  ? 45.70300   106.86900 -17.43800 1.000 106.23320 ?  355  THR   B CB  1 
ATOM   16895 O  OG1 . THR   B 1 355  ? 45.37700   106.18900 -18.65700 1.000 103.17126 ?  355  THR   B OG1 1 
ATOM   16896 C  CG2 . THR   B 1 355  ? 45.61700   105.88400 -16.28500 1.000 94.84599  ?  355  THR   B CG2 1 
ATOM   16897 N  N   . GLY   B 1 356  ? 43.92600   109.47900 -19.02700 1.000 135.12415 ?  356  GLY   B N   1 
ATOM   16898 C  CA  . GLY   B 1 356  ? 44.06100   110.38200 -20.15300 1.000 117.07244 ?  356  GLY   B CA  1 
ATOM   16899 C  C   . GLY   B 1 356  ? 44.30000   109.62000 -21.43900 1.000 104.25568 ?  356  GLY   B C   1 
ATOM   16900 O  O   . GLY   B 1 356  ? 43.79300   108.50600 -21.60100 1.000 119.18356 ?  356  GLY   B O   1 
ATOM   16901 N  N   . LEU   B 1 357  ? 45.08500   110.21300 -22.34600 1.000 88.03008  ?  357  LEU   B N   1 
ATOM   16902 C  CA  . LEU   B 1 357  ? 45.56300   109.60300 -23.58900 1.000 107.97329 ?  357  LEU   B CA  1 
ATOM   16903 C  C   . LEU   B 1 357  ? 44.57600   108.62200 -24.22600 1.000 87.12622  ?  357  LEU   B C   1 
ATOM   16904 O  O   . LEU   B 1 357  ? 44.80700   107.40800 -24.23400 1.000 78.79215  ?  357  LEU   B O   1 
ATOM   16905 C  CB  . LEU   B 1 357  ? 46.92800   108.92700 -23.35100 1.000 126.88712 ?  357  LEU   B CB  1 
ATOM   16906 C  CG  . LEU   B 1 357  ? 47.21500   107.70900 -22.45100 1.000 124.96881 ?  357  LEU   B CG  1 
ATOM   16907 C  CD1 . LEU   B 1 357  ? 48.60100   107.16000 -22.76600 1.000 122.31544 ?  357  LEU   B CD1 1 
ATOM   16908 C  CD2 . LEU   B 1 357  ? 47.11200   108.01300 -20.96300 1.000 112.44781 ?  357  LEU   B CD2 1 
ATOM   16909 N  N   . ALA   B 1 358  ? 43.48000   109.14000 -24.77900 1.000 62.53674  ?  358  ALA   B N   1 
ATOM   16910 C  CA  . ALA   B 1 358  ? 42.46800   108.29500 -25.40300 1.000 57.59814  ?  358  ALA   B CA  1 
ATOM   16911 C  C   . ALA   B 1 358  ? 42.95500   107.84200 -26.77400 1.000 50.49769  ?  358  ALA   B C   1 
ATOM   16912 O  O   . ALA   B 1 358  ? 43.27800   108.67200 -27.63000 1.000 48.10710  ?  358  ALA   B O   1 
ATOM   16913 C  CB  . ALA   B 1 358  ? 41.14200   109.04300 -25.52200 1.000 47.81596  ?  358  ALA   B CB  1 
ATOM   16914 N  N   . LYS   B 1 359  ? 43.00200   106.52900 -26.98600 1.000 52.15834  ?  359  LYS   B N   1 
ATOM   16915 C  CA  . LYS   B 1 359  ? 43.53100   105.95200 -28.21200 1.000 43.78616  ?  359  LYS   B CA  1 
ATOM   16916 C  C   . LYS   B 1 359  ? 42.44200   105.18000 -28.94500 1.000 51.14016  ?  359  LYS   B C   1 
ATOM   16917 O  O   . LYS   B 1 359  ? 41.55200   104.59000 -28.32600 1.000 54.67484  ?  359  LYS   B O   1 
ATOM   16918 C  CB  . LYS   B 1 359  ? 44.72000   105.02900 -27.91500 1.000 48.00627  ?  359  LYS   B CB  1 
ATOM   16919 C  CG  . LYS   B 1 359  ? 44.58500   104.25600 -26.61000 1.000 63.58746  ?  359  LYS   B CG  1 
ATOM   16920 C  CD  . LYS   B 1 359  ? 45.92500   104.10900 -25.90300 1.000 68.94500  ?  359  LYS   B CD  1 
ATOM   16921 C  CE  . LYS   B 1 359  ? 45.76700   103.46000 -24.53300 1.000 73.75243  ?  359  LYS   B CE  1 
ATOM   16922 N  NZ  . LYS   B 1 359  ? 47.03700   103.48600 -23.75200 1.000 93.42681  ?  359  LYS   B NZ  1 
ATOM   16923 N  N   . GLY   B 1 360  ? 42.52500   105.18500 -30.27400 1.000 47.39252  ?  360  GLY   B N   1 
ATOM   16924 C  CA  . GLY   B 1 360  ? 41.53900   104.51100 -31.09800 1.000 33.95840  ?  360  GLY   B CA  1 
ATOM   16925 C  C   . GLY   B 1 360  ? 41.93000   103.10400 -31.50800 1.000 41.76350  ?  360  GLY   B C   1 
ATOM   16926 O  O   . GLY   B 1 360  ? 42.79400   102.91600 -32.37000 1.000 33.08623  ?  360  GLY   B O   1 
ATOM   16927 N  N   . VAL   B 1 361  ? 41.28800   102.10800 -30.90500 1.000 40.45060  ?  361  VAL   B N   1 
ATOM   16928 C  CA  . VAL   B 1 361  ? 41.57900   100.70900 -31.19600 1.000 24.33545  ?  361  VAL   B CA  1 
ATOM   16929 C  C   . VAL   B 1 361  ? 40.94800   100.32900 -32.53000 1.000 36.34989  ?  361  VAL   B C   1 
ATOM   16930 O  O   . VAL   B 1 361  ? 39.75200   100.55500 -32.75300 1.000 42.87766  ?  361  VAL   B O   1 
ATOM   16931 C  CB  . VAL   B 1 361  ? 41.06900   99.80800  -30.06100 1.000 27.19407  ?  361  VAL   B CB  1 
ATOM   16932 C  CG1 . VAL   B 1 361  ? 41.18900   98.33500  -30.43900 1.000 24.46150  ?  361  VAL   B CG1 1 
ATOM   16933 C  CG2 . VAL   B 1 361  ? 41.82800   100.10700 -28.77700 1.000 28.82890  ?  361  VAL   B CG2 1 
ATOM   16934 N  N   . MET   B 1 362  ? 41.74900   99.74600  -33.42000 1.000 27.94187  ?  362  MET   B N   1 
ATOM   16935 C  CA  . MET   B 1 362  ? 41.29800   99.33800  -34.74500 1.000 26.59899  ?  362  MET   B CA  1 
ATOM   16936 C  C   . MET   B 1 362  ? 41.02800   97.83900  -34.75700 1.000 34.94274  ?  362  MET   B C   1 
ATOM   16937 O  O   . MET   B 1 362  ? 41.88700   97.04500  -34.36100 1.000 39.40231  ?  362  MET   B O   1 
ATOM   16938 C  CB  . MET   B 1 362  ? 42.33600   99.69500  -35.81100 1.000 38.03159  ?  362  MET   B CB  1 
ATOM   16939 C  CG  . MET   B 1 362  ? 42.58300   101.19000 -35.96500 1.000 45.48018  ?  362  MET   B CG  1 
ATOM   16940 S  SD  . MET   B 1 362  ? 43.79000   101.59100 -37.23900 1.000 72.39255  ?  362  MET   B SD  1 
ATOM   16941 C  CE  . MET   B 1 362  ? 45.16100   100.58200 -36.70700 1.000 26.66831  ?  362  MET   B CE  1 
ATOM   16942 N  N   . ILE   B 1 363  ? 39.84000   97.45800  -35.22000 1.000 40.98493  ?  363  ILE   B N   1 
ATOM   16943 C  CA  . ILE   B 1 363  ? 39.41300   96.06500  -35.26400 1.000 38.51347  ?  363  ILE   B CA  1 
ATOM   16944 C  C   . ILE   B 1 363  ? 39.07300   95.70300  -36.70500 1.000 26.89795  ?  363  ILE   B C   1 
ATOM   16945 O  O   . ILE   B 1 363  ? 38.47300   96.50500  -37.43000 1.000 25.63913  ?  363  ILE   B O   1 
ATOM   16946 C  CB  . ILE   B 1 363  ? 38.21500   95.82300  -34.32000 1.000 24.50459  ?  363  ILE   B CB  1 
ATOM   16947 C  CG1 . ILE   B 1 363  ? 38.61700   96.15400  -32.88200 1.000 29.71701  ?  363  ILE   B CG1 1 
ATOM   16948 C  CG2 . ILE   B 1 363  ? 37.71400   94.39000  -34.41400 1.000 20.80907  ?  363  ILE   B CG2 1 
ATOM   16949 C  CD1 . ILE   B 1 363  ? 39.78600   95.34600  -32.37700 1.000 22.83463  ?  363  ILE   B CD1 1 
ATOM   16950 N  N   . GLU   B 1 364  ? 39.47000   94.50400  -37.12100 1.000 24.07712  ?  364  GLU   B N   1 
ATOM   16951 C  CA  . GLU   B 1 364  ? 39.26000   94.02500  -38.48000 1.000 31.48259  ?  364  GLU   B CA  1 
ATOM   16952 C  C   . GLU   B 1 364  ? 38.09400   93.04000  -38.53400 1.000 35.71703  ?  364  GLU   B C   1 
ATOM   16953 O  O   . GLU   B 1 364  ? 37.63900   92.52000  -37.51100 1.000 33.70606  ?  364  GLU   B O   1 
ATOM   16954 C  CB  . GLU   B 1 364  ? 40.53500   93.36800  -39.02100 1.000 33.65022  ?  364  GLU   B CB  1 
ATOM   16955 C  CG  . GLU   B 1 364  ? 41.74500   94.29600  -39.03600 1.000 40.75180  ?  364  GLU   B CG  1 
ATOM   16956 C  CD  . GLU   B 1 364  ? 43.05400   93.57700  -39.33200 1.000 58.79430  ?  364  GLU   B CD  1 
ATOM   16957 O  OE1 . GLU   B 1 364  ? 43.14800   92.35700  -39.07000 1.000 53.55501  ?  364  GLU   B OE1 1 
ATOM   16958 O  OE2 . GLU   B 1 364  ? 43.99600   94.24000  -39.81800 1.000 55.85078  -1 364  GLU   B OE2 1 
ATOM   16959 N  N   . HIS   B 1 365  ? 37.61900   92.78700  -39.75900 1.000 30.24002  ?  365  HIS   B N   1 
ATOM   16960 C  CA  . HIS   B 1 365  ? 36.44700   91.93500  -39.95300 1.000 31.30457  ?  365  HIS   B CA  1 
ATOM   16961 C  C   . HIS   B 1 365  ? 36.67000   90.53800  -39.38600 1.000 31.09833  ?  365  HIS   B C   1 
ATOM   16962 O  O   . HIS   B 1 365  ? 35.78300   89.97800  -38.73000 1.000 35.90250  ?  365  HIS   B O   1 
ATOM   16963 C  CB  . HIS   B 1 365  ? 36.09700   91.84900  -41.44100 1.000 35.16484  ?  365  HIS   B CB  1 
ATOM   16964 C  CG  . HIS   B 1 365  ? 35.14400   92.90700  -41.90900 1.000 39.67910  ?  365  HIS   B CG  1 
ATOM   16965 N  ND1 . HIS   B 1 365  ? 33.77800   92.79700  -41.76100 1.000 39.16470  ?  365  HIS   B ND1 1 
ATOM   16966 C  CD2 . HIS   B 1 365  ? 35.36000   94.08400  -42.54400 1.000 39.28788  ?  365  HIS   B CD2 1 
ATOM   16967 C  CE1 . HIS   B 1 365  ? 33.19400   93.86600  -42.27300 1.000 33.78852  ?  365  HIS   B CE1 1 
ATOM   16968 N  NE2 . HIS   B 1 365  ? 34.13100   94.66200  -42.75600 1.000 35.47268  ?  365  HIS   B NE2 1 
ATOM   16969 N  N   . HIS   B 1 366  ? 37.84700   89.95600  -39.63100 1.000 33.89298  ?  366  HIS   B N   1 
ATOM   16970 C  CA  . HIS   B 1 366  ? 38.11600   88.59900  -39.17000 1.000 35.41821  ?  366  HIS   B CA  1 
ATOM   16971 C  C   . HIS   B 1 366  ? 38.15700   88.50100  -37.65000 1.000 28.73302  ?  366  HIS   B C   1 
ATOM   16972 O  O   . HIS   B 1 366  ? 37.93800   87.41300  -37.10800 1.000 27.37626  ?  366  HIS   B O   1 
ATOM   16973 C  CB  . HIS   B 1 366  ? 39.42900   88.08500  -39.76800 1.000 38.17750  ?  366  HIS   B CB  1 
ATOM   16974 C  CG  . HIS   B 1 366  ? 40.65200   88.71000  -39.17300 1.000 33.15802  ?  366  HIS   B CG  1 
ATOM   16975 N  ND1 . HIS   B 1 366  ? 41.50700   88.02400  -38.33700 1.000 32.03790  ?  366  HIS   B ND1 1 
ATOM   16976 C  CD2 . HIS   B 1 366  ? 41.16400   89.95800  -39.29100 1.000 41.80692  ?  366  HIS   B CD2 1 
ATOM   16977 C  CE1 . HIS   B 1 366  ? 42.49200   88.82200  -37.96500 1.000 40.19526  ?  366  HIS   B CE1 1 
ATOM   16978 N  NE2 . HIS   B 1 366  ? 42.30800   90.00100  -38.53000 1.000 55.68765  ?  366  HIS   B NE2 1 
ATOM   16979 N  N   . ASN   B 1 367  ? 38.42500   89.60800  -36.95200 1.000 30.73545  ?  367  ASN   B N   1 
ATOM   16980 C  CA  . ASN   B 1 367  ? 38.36700   89.59500  -35.49400 1.000 27.73297  ?  367  ASN   B CA  1 
ATOM   16981 C  C   . ASN   B 1 367  ? 36.93900   89.41800  -35.00200 1.000 26.40195  ?  367  ASN   B C   1 
ATOM   16982 O  O   . ASN   B 1 367  ? 36.68300   88.62600  -34.08600 1.000 26.77792  ?  367  ASN   B O   1 
ATOM   16983 C  CB  . ASN   B 1 367  ? 38.95800   90.88600  -34.93600 1.000 23.34811  ?  367  ASN   B CB  1 
ATOM   16984 C  CG  . ASN   B 1 367  ? 40.40300   91.06600  -35.31400 1.000 28.85805  ?  367  ASN   B CG  1 
ATOM   16985 O  OD1 . ASN   B 1 367  ? 40.83600   92.16600  -35.65700 1.000 25.87903  ?  367  ASN   B OD1 1 
ATOM   16986 N  ND2 . ASN   B 1 367  ? 41.16600   89.98100  -35.25400 1.000 31.27463  ?  367  ASN   B ND2 1 
ATOM   16987 N  N   . LEU   B 1 368  ? 35.99700   90.15200  -35.60000 1.000 28.61046  ?  368  LEU   B N   1 
ATOM   16988 C  CA  . LEU   B 1 368  ? 34.60600   90.09400  -35.16400 1.000 27.08329  ?  368  LEU   B CA  1 
ATOM   16989 C  C   . LEU   B 1 368  ? 33.94800   88.78800  -35.58700 1.000 33.75896  ?  368  LEU   B C   1 
ATOM   16990 O  O   . LEU   B 1 368  ? 33.17300   88.20100  -34.82200 1.000 27.47854  ?  368  LEU   B O   1 
ATOM   16991 C  CB  . LEU   B 1 368  ? 33.83900   91.28800  -35.72800 1.000 30.59013  ?  368  LEU   B CB  1 
ATOM   16992 C  CG  . LEU   B 1 368  ? 32.38300   91.47300  -35.30000 1.000 30.47629  ?  368  LEU   B CG  1 
ATOM   16993 C  CD1 . LEU   B 1 368  ? 32.30800   91.79300  -33.81900 1.000 38.08075  ?  368  LEU   B CD1 1 
ATOM   16994 C  CD2 . LEU   B 1 368  ? 31.72600   92.57500  -36.12000 1.000 27.25446  ?  368  LEU   B CD2 1 
ATOM   16995 N  N   . VAL   B 1 369  ? 34.23900   88.32200  -36.80500 1.000 31.08939  ?  369  VAL   B N   1 
ATOM   16996 C  CA  . VAL   B 1 369  ? 33.66400   87.06500  -37.27900 1.000 34.23370  ?  369  VAL   B CA  1 
ATOM   16997 C  C   . VAL   B 1 369  ? 34.11100   85.90800  -36.39800 1.000 31.33636  ?  369  VAL   B C   1 
ATOM   16998 O  O   . VAL   B 1 369  ? 33.31600   85.02200  -36.06000 1.000 38.01180  ?  369  VAL   B O   1 
ATOM   16999 C  CB  . VAL   B 1 369  ? 34.03900   86.82800  -38.75300 1.000 35.65905  ?  369  VAL   B CB  1 
ATOM   17000 C  CG1 . VAL   B 1 369  ? 33.69000   85.40600  -39.16400 1.000 25.67701  ?  369  VAL   B CG1 1 
ATOM   17001 C  CG2 . VAL   B 1 369  ? 33.33400   87.83800  -39.64700 1.000 36.08547  ?  369  VAL   B CG2 1 
ATOM   17002 N  N   . ASN   B 1 370  ? 35.38800   85.90000  -36.01000 1.000 35.91471  ?  370  ASN   B N   1 
ATOM   17003 C  CA  . ASN   B 1 370  ? 35.89900   84.84700  -35.13800 1.000 33.18993  ?  370  ASN   B CA  1 
ATOM   17004 C  C   . ASN   B 1 370  ? 35.13100   84.79400  -33.82300 1.000 32.35298  ?  370  ASN   B C   1 
ATOM   17005 O  O   . ASN   B 1 370  ? 34.81300   83.70700  -33.32500 1.000 26.75746  ?  370  ASN   B O   1 
ATOM   17006 C  CB  . ASN   B 1 370  ? 37.39000   85.06600  -34.88200 1.000 35.74990  ?  370  ASN   B CB  1 
ATOM   17007 C  CG  . ASN   B 1 370  ? 37.89000   84.30700  -33.67400 1.000 32.79896  ?  370  ASN   B CG  1 
ATOM   17008 O  OD1 . ASN   B 1 370  ? 38.07700   83.09000  -33.72600 1.000 27.26953  ?  370  ASN   B OD1 1 
ATOM   17009 N  ND2 . ASN   B 1 370  ? 38.11000   85.02200  -32.57400 1.000 21.42669  ?  370  ASN   B ND2 1 
ATOM   17010 N  N   . PHE   B 1 371  ? 34.81600   85.95900  -33.25300 1.000 29.27303  ?  371  PHE   B N   1 
ATOM   17011 C  CA  . PHE   B 1 371  ? 34.08600   86.00300  -31.99000 1.000 26.02905  ?  371  PHE   B CA  1 
ATOM   17012 C  C   . PHE   B 1 371  ? 32.62600   85.60600  -32.18000 1.000 40.10182  ?  371  PHE   B C   1 
ATOM   17013 O  O   . PHE   B 1 371  ? 32.08000   84.81600  -31.40000 1.000 37.55124  ?  371  PHE   B O   1 
ATOM   17014 C  CB  . PHE   B 1 371  ? 34.18500   87.40100  -31.38000 1.000 29.45409  ?  371  PHE   B CB  1 
ATOM   17015 C  CG  . PHE   B 1 371  ? 33.58900   87.50900  -30.00700 1.000 36.00577  ?  371  PHE   B CG  1 
ATOM   17016 C  CD1 . PHE   B 1 371  ? 34.33300   87.17200  -28.88900 1.000 32.43726  ?  371  PHE   B CD1 1 
ATOM   17017 C  CD2 . PHE   B 1 371  ? 32.28800   87.95100  -29.83200 1.000 35.11006  ?  371  PHE   B CD2 1 
ATOM   17018 C  CE1 . PHE   B 1 371  ? 33.79100   87.27100  -27.62300 1.000 33.07749  ?  371  PHE   B CE1 1 
ATOM   17019 C  CE2 . PHE   B 1 371  ? 31.74000   88.05200  -28.56700 1.000 35.19904  ?  371  PHE   B CE2 1 
ATOM   17020 C  CZ  . PHE   B 1 371  ? 32.49400   87.71100  -27.46100 1.000 30.78606  ?  371  PHE   B CZ  1 
ATOM   17021 N  N   . CYS   B 1 372  ? 31.97400   86.15300  -33.20900 1.000 40.53556  ?  372  CYS   B N   1 
ATOM   17022 C  CA  . CYS   B 1 372  ? 30.56500   85.84800  -33.43200 1.000 31.69242  ?  372  CYS   B CA  1 
ATOM   17023 C  C   . CYS   B 1 372  ? 30.36700   84.37700  -33.77300 1.000 28.06755  ?  372  CYS   B C   1 
ATOM   17024 O  O   . CYS   B 1 372  ? 29.39100   83.75700  -33.33400 1.000 34.73713  ?  372  CYS   B O   1 
ATOM   17025 C  CB  . CYS   B 1 372  ? 30.00300   86.73700  -34.54100 1.000 29.03255  ?  372  CYS   B CB  1 
ATOM   17026 S  SG  . CYS   B 1 372  ? 29.79000   88.46600  -34.08300 1.000 58.06255  ?  372  CYS   B SG  1 
ATOM   17027 N  N   . GLU   B 1 373  ? 31.28400   83.79900  -34.55200 1.000 32.42242  ?  373  GLU   B N   1 
ATOM   17028 C  CA  . GLU   B 1 373  ? 31.16800   82.39000  -34.90600 1.000 30.81523  ?  373  GLU   B CA  1 
ATOM   17029 C  C   . GLU   B 1 373  ? 31.47400   81.47500  -33.73100 1.000 32.61621  ?  373  GLU   B C   1 
ATOM   17030 O  O   . GLU   B 1 373  ? 31.13300   80.28900  -33.78200 1.000 31.19416  ?  373  GLU   B O   1 
ATOM   17031 C  CB  . GLU   B 1 373  ? 32.08900   82.06100  -36.08000 1.000 31.62863  ?  373  GLU   B CB  1 
ATOM   17032 C  CG  . GLU   B 1 373  ? 31.59500   82.58200  -37.41900 1.000 33.11870  ?  373  GLU   B CG  1 
ATOM   17033 C  CD  . GLU   B 1 373  ? 30.25300   81.99500  -37.81900 1.000 46.89871  ?  373  GLU   B CD  1 
ATOM   17034 O  OE1 . GLU   B 1 373  ? 29.20900   82.55600  -37.42100 1.000 54.54459  ?  373  GLU   B OE1 1 
ATOM   17035 O  OE2 . GLU   B 1 373  ? 30.24300   80.97100  -38.53400 1.000 61.53517  -1 373  GLU   B OE2 1 
ATOM   17036 N  N   . TRP   B 1 374  ? 32.11900   81.99200  -32.68400 1.000 32.62999  ?  374  TRP   B N   1 
ATOM   17037 C  CA  . TRP   B 1 374  ? 32.28600   81.24100  -31.44700 1.000 31.04874  ?  374  TRP   B CA  1 
ATOM   17038 C  C   . TRP   B 1 374  ? 31.12300   81.46000  -30.48700 1.000 34.80620  ?  374  TRP   B C   1 
ATOM   17039 O  O   . TRP   B 1 374  ? 30.72100   80.53000  -29.78000 1.000 34.11137  ?  374  TRP   B O   1 
ATOM   17040 C  CB  . TRP   B 1 374  ? 33.59600   81.62900  -30.75400 1.000 26.77058  ?  374  TRP   B CB  1 
ATOM   17041 C  CG  . TRP   B 1 374  ? 33.60900   81.26300  -29.29300 1.000 28.51904  ?  374  TRP   B CG  1 
ATOM   17042 C  CD1 . TRP   B 1 374  ? 33.96100   80.05900  -28.75400 1.000 26.13195  ?  374  TRP   B CD1 1 
ATOM   17043 C  CD2 . TRP   B 1 374  ? 33.23600   82.10100  -28.18800 1.000 28.55453  ?  374  TRP   B CD2 1 
ATOM   17044 N  NE1 . TRP   B 1 374  ? 33.83600   80.09700  -27.38500 1.000 26.42967  ?  374  TRP   B NE1 1 
ATOM   17045 C  CE2 . TRP   B 1 374  ? 33.39200   81.33800  -27.01300 1.000 22.98635  ?  374  TRP   B CE2 1 
ATOM   17046 C  CE3 . TRP   B 1 374  ? 32.78500   83.42100  -28.08000 1.000 27.00255  ?  374  TRP   B CE3 1 
ATOM   17047 C  CZ2 . TRP   B 1 374  ? 33.11500   81.85100  -25.74600 1.000 27.20684  ?  374  TRP   B CZ2 1 
ATOM   17048 C  CZ3 . TRP   B 1 374  ? 32.51100   83.93000  -26.82000 1.000 25.16044  ?  374  TRP   B CZ3 1 
ATOM   17049 C  CH2 . TRP   B 1 374  ? 32.67900   83.14600  -25.67000 1.000 29.37821  ?  374  TRP   B CH2 1 
ATOM   17050 N  N   . TYR   B 1 375  ? 30.57400   82.67700  -30.45800 1.000 35.19850  ?  375  TYR   B N   1 
ATOM   17051 C  CA  . TYR   B 1 375  ? 29.54400   83.01900  -29.48000 1.000 27.25832  ?  375  TYR   B CA  1 
ATOM   17052 C  C   . TYR   B 1 375  ? 28.28500   82.18400  -29.67200 1.000 33.24655  ?  375  TYR   B C   1 
ATOM   17053 O  O   . TYR   B 1 375  ? 27.70500   81.69300  -28.69700 1.000 40.19036  ?  375  TYR   B O   1 
ATOM   17054 C  CB  . TYR   B 1 375  ? 29.22300   84.50800  -29.58600 1.000 27.92354  ?  375  TYR   B CB  1 
ATOM   17055 C  CG  . TYR   B 1 375  ? 28.20400   85.04400  -28.60600 1.000 33.98950  ?  375  TYR   B CG  1 
ATOM   17056 C  CD1 . TYR   B 1 375  ? 26.84100   84.93200  -28.85300 1.000 37.64315  ?  375  TYR   B CD1 1 
ATOM   17057 C  CD2 . TYR   B 1 375  ? 28.60800   85.70100  -27.45300 1.000 34.21910  ?  375  TYR   B CD2 1 
ATOM   17058 C  CE1 . TYR   B 1 375  ? 25.91300   85.44100  -27.97200 1.000 36.00806  ?  375  TYR   B CE1 1 
ATOM   17059 C  CE2 . TYR   B 1 375  ? 27.68600   86.21300  -26.56300 1.000 34.15079  ?  375  TYR   B CE2 1 
ATOM   17060 C  CZ  . TYR   B 1 375  ? 26.33900   86.08000  -26.82900 1.000 36.83928  ?  375  TYR   B CZ  1 
ATOM   17061 O  OH  . TYR   B 1 375  ? 25.41000   86.58800  -25.95200 1.000 32.40515  ?  375  TYR   B OH  1 
ATOM   17062 N  N   . ARG   B 1 376  ? 27.84200   82.02100  -30.91900 1.000 29.11883  ?  376  ARG   B N   1 
ATOM   17063 C  CA  . ARG   B 1 376  ? 26.57200   81.34100  -31.16600 1.000 38.99216  ?  376  ARG   B CA  1 
ATOM   17064 C  C   . ARG   B 1 376  ? 26.58000   79.88500  -30.71800 1.000 36.24169  ?  376  ARG   B C   1 
ATOM   17065 O  O   . ARG   B 1 376  ? 25.65600   79.48500  -29.98900 1.000 46.84270  ?  376  ARG   B O   1 
ATOM   17066 C  CB  . ARG   B 1 376  ? 26.19000   81.47100  -32.64400 1.000 34.71952  ?  376  ARG   B CB  1 
ATOM   17067 C  CG  . ARG   B 1 376  ? 25.08500   80.52000  -33.07400 1.000 36.09237  ?  376  ARG   B CG  1 
ATOM   17068 C  CD  . ARG   B 1 376  ? 24.55000   80.88500  -34.44300 1.000 45.77926  ?  376  ARG   B CD  1 
ATOM   17069 N  NE  . ARG   B 1 376  ? 25.62900   81.17600  -35.37800 1.000 51.93264  ?  376  ARG   B NE  1 
ATOM   17070 C  CZ  . ARG   B 1 376  ? 26.18900   80.27400  -36.17100 1.000 56.44783  ?  376  ARG   B CZ  1 
ATOM   17071 N  NH1 . ARG   B 1 376  ? 25.79600   79.01000  -36.16500 1.000 58.63111  ?  376  ARG   B NH1 1 
ATOM   17072 N  NH2 . ARG   B 1 376  ? 27.16900   80.64900  -36.98800 1.000 47.67625  ?  376  ARG   B NH2 1 
ATOM   17073 N  N   . PRO   B 1 377  ? 27.55000   79.04700  -31.09900 1.000 29.80550  ?  377  PRO   B N   1 
ATOM   17074 C  CA  . PRO   B 1 377  ? 27.50600   77.65300  -30.62800 1.000 31.14479  ?  377  PRO   B CA  1 
ATOM   17075 C  C   . PRO   B 1 377  ? 27.80200   77.51000  -29.14600 1.000 37.62837  ?  377  PRO   B C   1 
ATOM   17076 O  O   . PRO   B 1 377  ? 27.25100   76.61000  -28.50000 1.000 43.69475  ?  377  PRO   B O   1 
ATOM   17077 C  CB  . PRO   B 1 377  ? 28.57000   76.96000  -31.48800 1.000 17.66874  ?  377  PRO   B CB  1 
ATOM   17078 C  CG  . PRO   B 1 377  ? 29.52800   78.04500  -31.82500 1.000 31.77131  ?  377  PRO   B CG  1 
ATOM   17079 C  CD  . PRO   B 1 377  ? 28.69100   79.27500  -32.00600 1.000 26.70730  ?  377  PRO   B CD  1 
ATOM   17080 N  N   . TYR   B 1 378  ? 28.65400   78.37100  -28.58700 1.000 42.56861  ?  378  TYR   B N   1 
ATOM   17081 C  CA  . TYR   B 1 378  ? 29.01300   78.25100  -27.17800 1.000 33.63381  ?  378  TYR   B CA  1 
ATOM   17082 C  C   . TYR   B 1 378  ? 27.81200   78.50100  -26.27900 1.000 40.82871  ?  378  TYR   B C   1 
ATOM   17083 O  O   . TYR   B 1 378  ? 27.67500   77.87600  -25.22100 1.000 55.03848  ?  378  TYR   B O   1 
ATOM   17084 C  CB  . TYR   B 1 378  ? 30.14400   79.22100  -26.85000 1.000 27.20163  ?  378  TYR   B CB  1 
ATOM   17085 C  CG  . TYR   B 1 378  ? 30.64000   79.15800  -25.42600 1.000 30.79048  ?  378  TYR   B CG  1 
ATOM   17086 C  CD1 . TYR   B 1 378  ? 31.66100   78.29200  -25.06400 1.000 25.00237  ?  378  TYR   B CD1 1 
ATOM   17087 C  CD2 . TYR   B 1 378  ? 30.10600   79.98600  -24.44700 1.000 37.69049  ?  378  TYR   B CD2 1 
ATOM   17088 C  CE1 . TYR   B 1 378  ? 32.12600   78.24100  -23.76700 1.000 22.40830  ?  378  TYR   B CE1 1 
ATOM   17089 C  CE2 . TYR   B 1 378  ? 30.56400   79.94100  -23.14500 1.000 30.43758  ?  378  TYR   B CE2 1 
ATOM   17090 C  CZ  . TYR   B 1 378  ? 31.57400   79.06800  -22.81100 1.000 28.83389  ?  378  TYR   B CZ  1 
ATOM   17091 O  OH  . TYR   B 1 378  ? 32.03200   79.02500  -21.51500 1.000 40.00472  ?  378  TYR   B OH  1 
ATOM   17092 N  N   . PHE   B 1 379  ? 26.93000   79.41100  -26.67900 1.000 33.34683  ?  379  PHE   B N   1 
ATOM   17093 C  CA  . PHE   B 1 379  ? 25.74500   79.72200  -25.89800 1.000 35.94936  ?  379  PHE   B CA  1 
ATOM   17094 C  C   . PHE   B 1 379  ? 24.47200   79.14600  -26.49600 1.000 37.64126  ?  379  PHE   B C   1 
ATOM   17095 O  O   . PHE   B 1 379  ? 23.39000   79.37900  -25.94800 1.000 40.73835  ?  379  PHE   B O   1 
ATOM   17096 C  CB  . PHE   B 1 379  ? 25.60200   81.23700  -25.74300 1.000 34.76667  ?  379  PHE   B CB  1 
ATOM   17097 C  CG  . PHE   B 1 379  ? 26.69600   81.86900  -24.93800 1.000 41.09577  ?  379  PHE   B CG  1 
ATOM   17098 C  CD1 . PHE   B 1 379  ? 26.70600   81.76500  -23.55600 1.000 39.76684  ?  379  PHE   B CD1 1 
ATOM   17099 C  CD2 . PHE   B 1 379  ? 27.71300   82.57300  -25.56000 1.000 38.86934  ?  379  PHE   B CD2 1 
ATOM   17100 C  CE1 . PHE   B 1 379  ? 27.71000   82.35000  -22.81000 1.000 31.69230  ?  379  PHE   B CE1 1 
ATOM   17101 C  CE2 . PHE   B 1 379  ? 28.72000   83.16100  -24.82000 1.000 30.67791  ?  379  PHE   B CE2 1 
ATOM   17102 C  CZ  . PHE   B 1 379  ? 28.72000   83.04900  -23.44400 1.000 31.86213  ?  379  PHE   B CZ  1 
ATOM   17103 N  N   . GLY   B 1 380  ? 24.57000   78.40700  -27.59600 1.000 31.97557  ?  380  GLY   B N   1 
ATOM   17104 C  CA  . GLY   B 1 380  ? 23.38700   77.82000  -28.20700 1.000 36.02396  ?  380  GLY   B CA  1 
ATOM   17105 C  C   . GLY   B 1 380  ? 22.33600   78.82700  -28.62000 1.000 37.49287  ?  380  GLY   B C   1 
ATOM   17106 O  O   . GLY   B 1 380  ? 21.14000   78.60400  -28.39400 1.000 47.90722  ?  380  GLY   B O   1 
ATOM   17107 N  N   . VAL   B 1 381  ? 22.75300   79.93700  -29.22700 1.000 31.55405  ?  381  VAL   B N   1 
ATOM   17108 C  CA  . VAL   B 1 381  ? 21.79800   80.96400  -29.61600 1.000 34.87300  ?  381  VAL   B CA  1 
ATOM   17109 C  C   . VAL   B 1 381  ? 21.02700   80.49900  -30.84300 1.000 37.78213  ?  381  VAL   B C   1 
ATOM   17110 O  O   . VAL   B 1 381  ? 21.61400   80.08100  -31.85000 1.000 35.72300  ?  381  VAL   B O   1 
ATOM   17111 C  CB  . VAL   B 1 381  ? 22.51500   82.29600  -29.86800 1.000 31.28859  ?  381  VAL   B CB  1 
ATOM   17112 C  CG1 . VAL   B 1 381  ? 21.50800   83.43600  -29.91600 1.000 22.92528  ?  381  VAL   B CG1 1 
ATOM   17113 C  CG2 . VAL   B 1 381  ? 23.54200   82.53500  -28.77700 1.000 29.76225  ?  381  VAL   B CG2 1 
ATOM   17114 N  N   . THR   B 1 382  ? 19.70300   80.56100  -30.75800 1.000 44.01778  ?  382  THR   B N   1 
ATOM   17115 C  CA  . THR   B 1 382  ? 18.81200   80.19000  -31.84900 1.000 32.68984  ?  382  THR   B CA  1 
ATOM   17116 C  C   . THR   B 1 382  ? 17.97200   81.40000  -32.23500 1.000 32.46563  ?  382  THR   B C   1 
ATOM   17117 O  O   . THR   B 1 382  ? 17.99200   82.41000  -31.51900 1.000 35.24041  ?  382  THR   B O   1 
ATOM   17118 C  CB  . THR   B 1 382  ? 17.92600   79.02400  -31.42400 1.000 32.44919  ?  382  THR   B CB  1 
ATOM   17119 O  OG1 . THR   B 1 382  ? 17.02200   79.47000  -30.40600 1.000 44.82675  ?  382  THR   B OG1 1 
ATOM   17120 C  CG2 . THR   B 1 382  ? 18.78500   77.90100  -30.87400 1.000 36.59313  ?  382  THR   B CG2 1 
ATOM   17121 N  N   . PRO   B 1 383  ? 17.23600   81.36000  -33.35200 1.000 35.21850  ?  383  PRO   B N   1 
ATOM   17122 C  CA  . PRO   B 1 383  ? 16.35900   82.49600  -33.68600 1.000 29.49749  ?  383  PRO   B CA  1 
ATOM   17123 C  C   . PRO   B 1 383  ? 15.28100   82.76100  -32.65400 1.000 27.09370  ?  383  PRO   B C   1 
ATOM   17124 O  O   . PRO   B 1 383  ? 14.65000   83.82400  -32.70500 1.000 46.40179  ?  383  PRO   B O   1 
ATOM   17125 C  CB  . PRO   B 1 383  ? 15.75200   82.08900  -35.03400 1.000 40.41267  ?  383  PRO   B CB  1 
ATOM   17126 C  CG  . PRO   B 1 383  ? 16.76400   81.18400  -35.63100 1.000 38.04093  ?  383  PRO   B CG  1 
ATOM   17127 C  CD  . PRO   B 1 383  ? 17.34800   80.41500  -34.47800 1.000 38.38494  ?  383  PRO   B CD  1 
ATOM   17128 N  N   . ALA   B 1 384  ? 15.05700   81.84300  -31.71700 1.000 28.03740  ?  384  ALA   B N   1 
ATOM   17129 C  CA  . ALA   B 1 384  ? 14.05800   82.03000  -30.67500 1.000 29.06724  ?  384  ALA   B CA  1 
ATOM   17130 C  C   . ALA   B 1 384  ? 14.53100   82.92300  -29.53600 1.000 32.38636  ?  384  ALA   B C   1 
ATOM   17131 O  O   . ALA   B 1 384  ? 13.73600   83.21800  -28.63800 1.000 47.90612  ?  384  ALA   B O   1 
ATOM   17132 C  CB  . ALA   B 1 384  ? 13.63300   80.67200  -30.11400 1.000 31.82612  ?  384  ALA   B CB  1 
ATOM   17133 N  N   . ASP   B 1 385  ? 15.78600   83.35900  -29.53900 1.000 27.65363  ?  385  ASP   B N   1 
ATOM   17134 C  CA  . ASP   B 1 385  ? 16.31800   84.15000  -28.44000 1.000 23.01295  ?  385  ASP   B CA  1 
ATOM   17135 C  C   . ASP   B 1 385  ? 16.04300   85.63500  -28.65400 1.000 31.43314  ?  385  ASP   B C   1 
ATOM   17136 O  O   . ASP   B 1 385  ? 15.82600   86.09900  -29.77600 1.000 33.72557  ?  385  ASP   B O   1 
ATOM   17137 C  CB  . ASP   B 1 385  ? 17.82000   83.91500  -28.28500 1.000 24.02467  ?  385  ASP   B CB  1 
ATOM   17138 C  CG  . ASP   B 1 385  ? 18.13200   82.63800  -27.54100 1.000 31.31212  ?  385  ASP   B CG  1 
ATOM   17139 O  OD1 . ASP   B 1 385  ? 17.83300   82.56900  -26.33000 1.000 22.69993  ?  385  ASP   B OD1 1 
ATOM   17140 O  OD2 . ASP   B 1 385  ? 18.67200   81.70200  -28.16900 1.000 37.32055  -1 385  ASP   B OD2 1 
ATOM   17141 N  N   . LYS   B 1 386  ? 16.04800   86.38000  -27.54900 1.000 25.60798  ?  386  LYS   B N   1 
ATOM   17142 C  CA  . LYS   B 1 386  ? 15.91300   87.83000  -27.56200 1.000 28.71707  ?  386  LYS   B CA  1 
ATOM   17143 C  C   . LYS   B 1 386  ? 17.03900   88.41900  -26.73000 1.000 31.73029  ?  386  LYS   B C   1 
ATOM   17144 O  O   . LYS   B 1 386  ? 17.33000   87.92500  -25.63700 1.000 35.24754  ?  386  LYS   B O   1 
ATOM   17145 C  CB  . LYS   B 1 386  ? 14.55300   88.28200  -27.00500 1.000 35.01769  ?  386  LYS   B CB  1 
ATOM   17146 C  CG  . LYS   B 1 386  ? 13.36500   87.95100  -27.89400 1.000 28.24366  ?  386  LYS   B CG  1 
ATOM   17147 C  CD  . LYS   B 1 386  ? 12.19000   87.44600  -27.07400 1.000 35.42507  ?  386  LYS   B CD  1 
ATOM   17148 C  CE  . LYS   B 1 386  ? 10.87800   87.60700  -27.82200 1.000 41.43665  ?  386  LYS   B CE  1 
ATOM   17149 N  NZ  . LYS   B 1 386  ? 10.24800   88.92100  -27.53100 1.000 51.81633  ?  386  LYS   B NZ  1 
ATOM   17150 N  N   . ALA   B 1 387  ? 17.67200   89.47000  -27.24600 1.000 32.58085  ?  387  ALA   B N   1 
ATOM   17151 C  CA  . ALA   B 1 387  ? 18.86700   90.02400  -26.62600 1.000 25.89579  ?  387  ALA   B CA  1 
ATOM   17152 C  C   . ALA   B 1 387  ? 18.71000   91.51800  -26.39300 1.000 26.80022  ?  387  ALA   B C   1 
ATOM   17153 O  O   . ALA   B 1 387  ? 17.97500   92.20700  -27.10800 1.000 38.98060  ?  387  ALA   B O   1 
ATOM   17154 C  CB  . ALA   B 1 387  ? 20.11400   89.76000  -27.47900 1.000 25.33731  ?  387  ALA   B CB  1 
ATOM   17155 N  N   . LEU   B 1 388  ? 19.41900   92.00600  -25.38100 1.000 32.76800  ?  388  LEU   B N   1 
ATOM   17156 C  CA  . LEU   B 1 388  ? 19.41800   93.41100  -25.00000 1.000 37.19316  ?  388  LEU   B CA  1 
ATOM   17157 C  C   . LEU   B 1 388  ? 20.59500   94.12900  -25.65000 1.000 36.40702  ?  388  LEU   B C   1 
ATOM   17158 O  O   . LEU   B 1 388  ? 21.72200   93.62300  -25.63300 1.000 37.68763  ?  388  LEU   B O   1 
ATOM   17159 C  CB  . LEU   B 1 388  ? 19.49800   93.54500  -23.47700 1.000 21.72560  ?  388  LEU   B CB  1 
ATOM   17160 C  CG  . LEU   B 1 388  ? 18.31400   94.14400  -22.72500 1.000 33.79988  ?  388  LEU   B CG  1 
ATOM   17161 C  CD1 . LEU   B 1 388  ? 17.04000   93.39500  -23.03000 1.000 34.18220  ?  388  LEU   B CD1 1 
ATOM   17162 C  CD2 . LEU   B 1 388  ? 18.59700   94.13700  -21.22800 1.000 36.02866  ?  388  LEU   B CD2 1 
ATOM   17163 N  N   . VAL   B 1 389  ? 20.33400   95.29700  -26.22600 1.000 37.02396  ?  389  VAL   B N   1 
ATOM   17164 C  CA  . VAL   B 1 389  ? 21.39100   96.20200  -26.67900 1.000 38.55359  ?  389  VAL   B CA  1 
ATOM   17165 C  C   . VAL   B 1 389  ? 21.53500   97.24000  -25.56800 1.000 35.94049  ?  389  VAL   B C   1 
ATOM   17166 O  O   . VAL   B 1 389  ? 20.95600   98.32700  -25.61900 1.000 40.60045  ?  389  VAL   B O   1 
ATOM   17167 C  CB  . VAL   B 1 389  ? 21.07600   96.82900  -28.04000 1.000 36.75497  ?  389  VAL   B CB  1 
ATOM   17168 C  CG1 . VAL   B 1 389  ? 22.26700   97.63400  -28.55500 1.000 40.23133  ?  389  VAL   B CG1 1 
ATOM   17169 C  CG2 . VAL   B 1 389  ? 20.70800   95.75400  -29.05300 1.000 26.79748  ?  389  VAL   B CG2 1 
ATOM   17170 N  N   . TYR   B 1 390  ? 22.31900   96.89100  -24.54400 1.000 34.67303  ?  390  TYR   B N   1 
ATOM   17171 C  CA  . TYR   B 1 390  ? 22.42700   97.66100  -23.30800 1.000 39.04306  ?  390  TYR   B CA  1 
ATOM   17172 C  C   . TYR   B 1 390  ? 23.59700   98.64100  -23.30800 1.000 36.83740  ?  390  TYR   B C   1 
ATOM   17173 O  O   . TYR   B 1 390  ? 23.42600   99.80600  -22.93700 1.000 47.28816  ?  390  TYR   B O   1 
ATOM   17174 C  CB  . TYR   B 1 390  ? 22.54700   96.69700  -22.11700 1.000 34.14078  ?  390  TYR   B CB  1 
ATOM   17175 C  CG  . TYR   B 1 390  ? 22.64200   97.36400  -20.76300 1.000 46.58662  ?  390  TYR   B CG  1 
ATOM   17176 C  CD1 . TYR   B 1 390  ? 21.49900   97.74900  -20.07600 1.000 45.20495  ?  390  TYR   B CD1 1 
ATOM   17177 C  CD2 . TYR   B 1 390  ? 23.87400   97.59800  -20.16500 1.000 50.40381  ?  390  TYR   B CD2 1 
ATOM   17178 C  CE1 . TYR   B 1 390  ? 21.58000   98.35200  -18.83900 1.000 53.27903  ?  390  TYR   B CE1 1 
ATOM   17179 C  CE2 . TYR   B 1 390  ? 23.96500   98.20300  -18.92900 1.000 42.26237  ?  390  TYR   B CE2 1 
ATOM   17180 C  CZ  . TYR   B 1 390  ? 22.81500   98.57800  -18.27100 1.000 39.68566  ?  390  TYR   B CZ  1 
ATOM   17181 O  OH  . TYR   B 1 390  ? 22.89800   99.18200  -17.03900 1.000 73.40786  ?  390  TYR   B OH  1 
ATOM   17182 N  N   . SER   B 1 391  ? 24.78200   98.19800  -23.71800 1.000 41.93491  ?  391  SER   B N   1 
ATOM   17183 C  CA  . SER   B 1 391  ? 25.97900   99.02300  -23.63100 1.000 41.38848  ?  391  SER   B CA  1 
ATOM   17184 C  C   . SER   B 1 391  ? 25.98600   100.10300 -24.70900 1.000 36.05428  ?  391  SER   B C   1 
ATOM   17185 O  O   . SER   B 1 391  ? 25.36800   99.96800  -25.76800 1.000 37.54998  ?  391  SER   B O   1 
ATOM   17186 C  CB  . SER   B 1 391  ? 27.23300   98.16000  -23.75900 1.000 24.86413  ?  391  SER   B CB  1 
ATOM   17187 O  OG  . SER   B 1 391  ? 27.05100   96.90900  -23.11800 1.000 40.40695  ?  391  SER   B OG  1 
ATOM   17188 N  N   . SER   B 1 392  ? 26.71000   101.18600 -24.42100 1.000 31.34289  ?  392  SER   B N   1 
ATOM   17189 C  CA  . SER   B 1 392  ? 26.87300   102.26800 -25.38400 1.000 41.53118  ?  392  SER   B CA  1 
ATOM   17190 C  C   . SER   B 1 392  ? 27.53600   101.75400 -26.65500 1.000 42.43246  ?  392  SER   B C   1 
ATOM   17191 O  O   . SER   B 1 392  ? 28.47700   100.95700 -26.60400 1.000 41.24896  ?  392  SER   B O   1 
ATOM   17192 C  CB  . SER   B 1 392  ? 27.71200   103.39100 -24.77200 1.000 29.96476  ?  392  SER   B CB  1 
ATOM   17193 O  OG  . SER   B 1 392  ? 28.43800   104.08400 -25.77200 1.000 56.58472  ?  392  SER   B OG  1 
ATOM   17194 N  N   . PHE   B 1 393  ? 27.05000   102.22000 -27.80800 1.000 40.07183  ?  393  PHE   B N   1 
ATOM   17195 C  CA  . PHE   B 1 393  ? 27.58700   101.67500 -29.05000 1.000 43.42943  ?  393  PHE   B CA  1 
ATOM   17196 C  C   . PHE   B 1 393  ? 29.02100   102.11900 -29.31600 1.000 40.18921  ?  393  PHE   B C   1 
ATOM   17197 O  O   . PHE   B 1 393  ? 29.62300   101.64000 -30.28200 1.000 36.31633  ?  393  PHE   B O   1 
ATOM   17198 C  CB  . PHE   B 1 393  ? 26.64600   102.00500 -30.22300 1.000 29.12684  ?  393  PHE   B CB  1 
ATOM   17199 C  CG  . PHE   B 1 393  ? 26.89600   103.33400 -30.89200 1.000 29.63002  ?  393  PHE   B CG  1 
ATOM   17200 C  CD1 . PHE   B 1 393  ? 27.04800   104.49800 -30.15400 1.000 42.78280  ?  393  PHE   B CD1 1 
ATOM   17201 C  CD2 . PHE   B 1 393  ? 26.91100   103.42100 -32.27900 1.000 32.48289  ?  393  PHE   B CD2 1 
ATOM   17202 C  CE1 . PHE   B 1 393  ? 27.25600   105.71600 -30.78800 1.000 52.48018  ?  393  PHE   B CE1 1 
ATOM   17203 C  CE2 . PHE   B 1 393  ? 27.11200   104.63400 -32.91700 1.000 41.52975  ?  393  PHE   B CE2 1 
ATOM   17204 C  CZ  . PHE   B 1 393  ? 27.28600   105.78200 -32.17100 1.000 44.81645  ?  393  PHE   B CZ  1 
ATOM   17205 N  N   . SER   B 1 394  ? 29.58300   102.98000 -28.46600 1.000 35.56191  ?  394  SER   B N   1 
ATOM   17206 C  CA  . SER   B 1 394  ? 31.00400   103.30500 -28.46500 1.000 37.58497  ?  394  SER   B CA  1 
ATOM   17207 C  C   . SER   B 1 394  ? 31.83100   102.35400 -27.60400 1.000 33.03309  ?  394  SER   B C   1 
ATOM   17208 O  O   . SER   B 1 394  ? 32.99600   102.65100 -27.32100 1.000 31.94107  ?  394  SER   B O   1 
ATOM   17209 C  CB  . SER   B 1 394  ? 31.21900   104.74300 -27.98100 1.000 37.72350  ?  394  SER   B CB  1 
ATOM   17210 O  OG  . SER   B 1 394  ? 30.67500   105.68000 -28.89200 1.000 42.34029  ?  394  SER   B OG  1 
ATOM   17211 N  N   . PHE   B 1 395  ? 31.25900   101.22900 -27.17600 1.000 42.16608  ?  395  PHE   B N   1 
ATOM   17212 C  CA  . PHE   B 1 395  ? 31.95500   100.24000 -26.36500 1.000 42.15026  ?  395  PHE   B CA  1 
ATOM   17213 C  C   . PHE   B 1 395  ? 31.78000   98.86500  -26.99200 1.000 31.27230  ?  395  PHE   B C   1 
ATOM   17214 O  O   . PHE   B 1 395  ? 30.75400   98.57900  -27.61300 1.000 41.75411  ?  395  PHE   B O   1 
ATOM   17215 C  CB  . PHE   B 1 395  ? 31.43100   100.21800 -24.92100 1.000 35.91626  ?  395  PHE   B CB  1 
ATOM   17216 C  CG  . PHE   B 1 395  ? 32.19400   101.10700 -23.98400 1.000 54.38340  ?  395  PHE   B CG  1 
ATOM   17217 C  CD1 . PHE   B 1 395  ? 33.29200   100.62600 -23.28800 1.000 70.42104  ?  395  PHE   B CD1 1 
ATOM   17218 C  CD2 . PHE   B 1 395  ? 31.80500   102.42300 -23.78800 1.000 63.40709  ?  395  PHE   B CD2 1 
ATOM   17219 C  CE1 . PHE   B 1 395  ? 33.99400   101.44500 -22.42100 1.000 89.58589  ?  395  PHE   B CE1 1 
ATOM   17220 C  CE2 . PHE   B 1 395  ? 32.50200   103.24600 -22.92400 1.000 59.94515  ?  395  PHE   B CE2 1 
ATOM   17221 C  CZ  . PHE   B 1 395  ? 33.59700   102.75700 -22.23900 1.000 87.64614  ?  395  PHE   B CZ  1 
ATOM   17222 N  N   . ASP   B 1 396  ? 32.78700   98.00600  -26.81500 1.000 36.04812  ?  396  ASP   B N   1 
ATOM   17223 C  CA  . ASP   B 1 396  ? 32.73300   96.69200  -27.44700 1.000 31.70544  ?  396  ASP   B CA  1 
ATOM   17224 C  C   . ASP   B 1 396  ? 31.69800   95.77500  -26.81700 1.000 32.72927  ?  396  ASP   B C   1 
ATOM   17225 O  O   . ASP   B 1 396  ? 31.41500   94.71400  -27.38400 1.000 36.49252  ?  396  ASP   B O   1 
ATOM   17226 C  CB  . ASP   B 1 396  ? 34.11500   96.02800  -27.43500 1.000 35.94112  ?  396  ASP   B CB  1 
ATOM   17227 C  CG  . ASP   B 1 396  ? 34.71000   95.92700  -26.04800 1.000 57.85452  ?  396  ASP   B CG  1 
ATOM   17228 O  OD1 . ASP   B 1 396  ? 34.60000   96.90500  -25.27800 1.000 71.92844  ?  396  ASP   B OD1 1 
ATOM   17229 O  OD2 . ASP   B 1 396  ? 35.31400   94.87700  -25.73800 1.000 61.67574  -1 396  ASP   B OD2 1 
ATOM   17230 N  N   . GLY   B 1 397  ? 31.12300   96.15200  -25.67500 1.000 38.62839  ?  397  GLY   B N   1 
ATOM   17231 C  CA  . GLY   B 1 397  ? 29.97900   95.41500  -25.17100 1.000 25.17083  ?  397  GLY   B CA  1 
ATOM   17232 C  C   . GLY   B 1 397  ? 28.82100   95.44000  -26.14800 1.000 26.95874  ?  397  GLY   B C   1 
ATOM   17233 O  O   . GLY   B 1 397  ? 28.15200   94.42600  -26.36400 1.000 32.15691  ?  397  GLY   B O   1 
ATOM   17234 N  N   . SER   B 1 398  ? 28.58500   96.59500  -26.77500 1.000 21.88585  ?  398  SER   B N   1 
ATOM   17235 C  CA  . SER   B 1 398  ? 27.50300   96.68600  -27.74800 1.000 46.82099  ?  398  SER   B CA  1 
ATOM   17236 C  C   . SER   B 1 398  ? 27.78600   95.83400  -28.97800 1.000 36.16160  ?  398  SER   B C   1 
ATOM   17237 O  O   . SER   B 1 398  ? 26.84700   95.36200  -29.62800 1.000 48.71634  ?  398  SER   B O   1 
ATOM   17238 C  CB  . SER   B 1 398  ? 27.26900   98.14000  -28.15300 1.000 36.53442  ?  398  SER   B CB  1 
ATOM   17239 O  OG  . SER   B 1 398  ? 28.28900   98.59200  -29.02000 1.000 37.27324  ?  398  SER   B OG  1 
ATOM   17240 N  N   . ALA   B 1 399  ? 29.06300   95.62500  -29.31100 1.000 25.11884  ?  399  ALA   B N   1 
ATOM   17241 C  CA  . ALA   B 1 399  ? 29.39200   94.72200  -30.40900 1.000 23.87355  ?  399  ALA   B CA  1 
ATOM   17242 C  C   . ALA   B 1 399  ? 28.92000   93.30600  -30.11100 1.000 34.59505  ?  399  ALA   B C   1 
ATOM   17243 O  O   . ALA   B 1 399  ? 28.37100   92.62800  -30.98700 1.000 42.33133  ?  399  ALA   B O   1 
ATOM   17244 C  CB  . ALA   B 1 399  ? 30.89500   94.74300  -30.67900 1.000 31.00383  ?  399  ALA   B CB  1 
ATOM   17245 N  N   . LEU   B 1 400  ? 29.12800   92.84100  -28.87600 1.000 34.60567  ?  400  LEU   B N   1 
ATOM   17246 C  CA  . LEU   B 1 400  ? 28.55300   91.56500  -28.46300 1.000 42.36072  ?  400  LEU   B CA  1 
ATOM   17247 C  C   . LEU   B 1 400  ? 27.03100   91.61300  -28.52300 1.000 36.62553  ?  400  LEU   B C   1 
ATOM   17248 O  O   . LEU   B 1 400  ? 26.38600   90.63200  -28.91100 1.000 31.22544  ?  400  LEU   B O   1 
ATOM   17249 C  CB  . LEU   B 1 400  ? 29.03000   91.20900  -27.05200 1.000 30.70793  ?  400  LEU   B CB  1 
ATOM   17250 C  CG  . LEU   B 1 400  ? 28.71400   89.82600  -26.46900 1.000 28.92237  ?  400  LEU   B CG  1 
ATOM   17251 C  CD1 . LEU   B 1 400  ? 29.78300   89.43300  -25.46100 1.000 37.61425  ?  400  LEU   B CD1 1 
ATOM   17252 C  CD2 . LEU   B 1 400  ? 27.33500   89.76300  -25.82000 1.000 32.17372  ?  400  LEU   B CD2 1 
ATOM   17253 N  N   . ASP   B 1 401  ? 26.44100   92.75000  -28.14600 1.000 27.48365  ?  401  ASP   B N   1 
ATOM   17254 C  CA  . ASP   B 1 401  ? 24.98700   92.86300  -28.13300 1.000 26.35576  ?  401  ASP   B CA  1 
ATOM   17255 C  C   . ASP   B 1 401  ? 24.40900   92.66000  -29.52700 1.000 27.03055  ?  401  ASP   B C   1 
ATOM   17256 O  O   . ASP   B 1 401  ? 23.48700   91.86000  -29.72200 1.000 32.19693  ?  401  ASP   B O   1 
ATOM   17257 C  CB  . ASP   B 1 401  ? 24.57400   94.23000  -27.58300 1.000 29.22339  ?  401  ASP   B CB  1 
ATOM   17258 C  CG  . ASP   B 1 401  ? 24.93100   94.40700  -26.12200 1.000 31.57879  ?  401  ASP   B CG  1 
ATOM   17259 O  OD1 . ASP   B 1 401  ? 25.37900   93.42700  -25.49100 1.000 55.06253  ?  401  ASP   B OD1 1 
ATOM   17260 O  OD2 . ASP   B 1 401  ? 24.77400   95.53600  -25.61000 1.000 29.86209  -1 401  ASP   B OD2 1 
ATOM   17261 N  N   . ILE   B 1 402  ? 24.96000   93.36200  -30.51500 1.000 30.26542  ?  402  ILE   B N   1 
ATOM   17262 C  CA  . ILE   B 1 402  ? 24.35600   93.46900  -31.83800 1.000 20.53707  ?  402  ILE   B CA  1 
ATOM   17263 C  C   . ILE   B 1 402  ? 24.81100   92.34000  -32.75300 1.000 30.12356  ?  402  ILE   B C   1 
ATOM   17264 O  O   . ILE   B 1 402  ? 23.98800   91.57000  -33.26200 1.000 37.14963  ?  402  ILE   B O   1 
ATOM   17265 C  CB  . ILE   B 1 402  ? 24.68400   94.83400  -32.47000 1.000 23.28000  ?  402  ILE   B CB  1 
ATOM   17266 C  CG1 . ILE   B 1 402  ? 24.13100   95.97300  -31.61300 1.000 25.84522  ?  402  ILE   B CG1 1 
ATOM   17267 C  CG2 . ILE   B 1 402  ? 24.14300   94.91400  -33.88900 1.000 26.40377  ?  402  ILE   B CG2 1 
ATOM   17268 C  CD1 . ILE   B 1 402  ? 24.79900   97.30100  -31.88400 1.000 14.66860  ?  402  ILE   B CD1 1 
ATOM   17269 N  N   . PHE   B 1 403  ? 26.12600   92.23300  -32.96400 1.000 32.33074  ?  403  PHE   B N   1 
ATOM   17270 C  CA  . PHE   B 1 403  ? 26.64600   91.41300  -34.05700 1.000 21.87736  ?  403  PHE   B CA  1 
ATOM   17271 C  C   . PHE   B 1 403  ? 26.50300   89.92200  -33.77400 1.000 23.46391  ?  403  PHE   B C   1 
ATOM   17272 O  O   . PHE   B 1 403  ? 26.23700   89.13700  -34.69400 1.000 24.51813  ?  403  PHE   B O   1 
ATOM   17273 C  CB  . PHE   B 1 403  ? 28.10700   91.77500  -34.32500 1.000 21.49175  ?  403  PHE   B CB  1 
ATOM   17274 C  CG  . PHE   B 1 403  ? 28.31300   93.22700  -34.64100 1.000 23.33722  ?  403  PHE   B CG  1 
ATOM   17275 C  CD1 . PHE   B 1 403  ? 27.55400   93.84600  -35.62100 1.000 22.07068  ?  403  PHE   B CD1 1 
ATOM   17276 C  CD2 . PHE   B 1 403  ? 29.24400   93.97900  -33.94700 1.000 21.87721  ?  403  PHE   B CD2 1 
ATOM   17277 C  CE1 . PHE   B 1 403  ? 27.72700   95.18300  -35.91200 1.000 19.83439  ?  403  PHE   B CE1 1 
ATOM   17278 C  CE2 . PHE   B 1 403  ? 29.42300   95.32000  -34.23200 1.000 27.32437  ?  403  PHE   B CE2 1 
ATOM   17279 C  CZ  . PHE   B 1 403  ? 28.66300   95.92300  -35.21600 1.000 35.24722  ?  403  PHE   B CZ  1 
ATOM   17280 N  N   . THR   B 1 404  ? 26.68100   89.50600  -32.51800 1.000 23.62888  ?  404  THR   B N   1 
ATOM   17281 C  CA  . THR   B 1 404  ? 26.63300   88.07900  -32.21000 1.000 33.75637  ?  404  THR   B CA  1 
ATOM   17282 C  C   . THR   B 1 404  ? 25.23700   87.51700  -32.44100 1.000 32.17565  ?  404  THR   B C   1 
ATOM   17283 O  O   . THR   B 1 404  ? 25.07300   86.47700  -33.08900 1.000 39.80255  ?  404  THR   B O   1 
ATOM   17284 C  CB  . THR   B 1 404  ? 27.08500   87.82100  -30.76800 1.000 31.82548  ?  404  THR   B CB  1 
ATOM   17285 O  OG1 . THR   B 1 404  ? 26.13600   88.37800  -29.84900 1.000 27.72032  ?  404  THR   B OG1 1 
ATOM   17286 C  CG2 . THR   B 1 404  ? 28.45500   88.43100  -30.51500 1.000 37.03140  ?  404  THR   B CG2 1 
ATOM   17287 N  N   . HIS   B 1 405  ? 24.21600   88.20300  -31.93300 1.000 30.90412  ?  405  HIS   B N   1 
ATOM   17288 C  CA  . HIS   B 1 405  ? 22.85800   87.69200  -32.01800 1.000 32.20286  ?  405  HIS   B CA  1 
ATOM   17289 C  C   . HIS   B 1 405  ? 22.24200   87.88400  -33.39700 1.000 32.01657  ?  405  HIS   B C   1 
ATOM   17290 O  O   . HIS   B 1 405  ? 21.30100   87.16200  -33.74700 1.000 38.17339  ?  405  HIS   B O   1 
ATOM   17291 C  CB  . HIS   B 1 405  ? 21.99700   88.35700  -30.94500 1.000 29.72516  ?  405  HIS   B CB  1 
ATOM   17292 C  CG  . HIS   B 1 405  ? 22.55700   88.22000  -29.56300 1.000 25.06403  ?  405  HIS   B CG  1 
ATOM   17293 N  ND1 . HIS   B 1 405  ? 23.08100   89.28500  -28.86100 1.000 27.88696  ?  405  HIS   B ND1 1 
ATOM   17294 C  CD2 . HIS   B 1 405  ? 22.69000   87.13900  -28.75800 1.000 30.93979  ?  405  HIS   B CD2 1 
ATOM   17295 C  CE1 . HIS   B 1 405  ? 23.50300   88.86800  -27.68000 1.000 31.48326  ?  405  HIS   B CE1 1 
ATOM   17296 N  NE2 . HIS   B 1 405  ? 23.27800   87.56900  -27.59300 1.000 36.26003  ?  405  HIS   B NE2 1 
ATOM   17297 N  N   . LEU   B 1 406  ? 22.75300   88.82800  -34.19000 1.000 29.83886  ?  406  LEU   B N   1 
ATOM   17298 C  CA  . LEU   B 1 406  ? 22.22800   89.00400  -35.53900 1.000 31.35232  ?  406  LEU   B CA  1 
ATOM   17299 C  C   . LEU   B 1 406  ? 22.66000   87.86900  -36.45300 1.000 27.67954  ?  406  LEU   B C   1 
ATOM   17300 O  O   . LEU   B 1 406  ? 21.96900   87.56300  -37.43000 1.000 47.60798  ?  406  LEU   B O   1 
ATOM   17301 C  CB  . LEU   B 1 406  ? 22.66600   90.35000  -36.11300 1.000 24.49585  ?  406  LEU   B CB  1 
ATOM   17302 C  CG  . LEU   B 1 406  ? 21.74400   91.53200  -35.81000 1.000 35.38452  ?  406  LEU   B CG  1 
ATOM   17303 C  CD1 . LEU   B 1 406  ? 22.16800   92.77400  -36.58400 1.000 30.28170  ?  406  LEU   B CD1 1 
ATOM   17304 C  CD2 . LEU   B 1 406  ? 20.30000   91.17100  -36.11600 1.000 23.80338  ?  406  LEU   B CD2 1 
ATOM   17305 N  N   . LEU   B 1 407  ? 23.78200   87.22400  -36.14800 1.000 34.60449  ?  407  LEU   B N   1 
ATOM   17306 C  CA  . LEU   B 1 407  ? 24.21800   86.08800  -36.94400 1.000 39.37460  ?  407  LEU   B CA  1 
ATOM   17307 C  C   . LEU   B 1 407  ? 23.53000   84.79300  -36.54100 1.000 39.32506  ?  407  LEU   B C   1 
ATOM   17308 O  O   . LEU   B 1 407  ? 23.73200   83.77100  -37.20600 1.000 44.59647  ?  407  LEU   B O   1 
ATOM   17309 C  CB  . LEU   B 1 407  ? 25.73700   85.92600  -36.84200 1.000 32.32226  ?  407  LEU   B CB  1 
ATOM   17310 C  CG  . LEU   B 1 407  ? 26.58300   86.95000  -37.60100 1.000 31.02745  ?  407  LEU   B CG  1 
ATOM   17311 C  CD1 . LEU   B 1 407  ? 27.99600   86.42500  -37.80800 1.000 28.03344  ?  407  LEU   B CD1 1 
ATOM   17312 C  CD2 . LEU   B 1 407  ? 25.94200   87.30300  -38.93200 1.000 30.75876  ?  407  LEU   B CD2 1 
ATOM   17313 N  N   . ALA   B 1 408  ? 22.72300   84.81400  -35.48000 1.000 32.80940  ?  408  ALA   B N   1 
ATOM   17314 C  CA  . ALA   B 1 408  ? 22.00900   83.63600  -35.01300 1.000 36.85983  ?  408  ALA   B CA  1 
ATOM   17315 C  C   . ALA   B 1 408  ? 20.53300   83.64600  -35.38400 1.000 38.55072  ?  408  ALA   B C   1 
ATOM   17316 O  O   . ALA   B 1 408  ? 19.87000   82.61000  -35.25700 1.000 37.70698  ?  408  ALA   B O   1 
ATOM   17317 C  CB  . ALA   B 1 408  ? 22.15200   83.50200  -33.49200 1.000 31.87806  ?  408  ALA   B CB  1 
ATOM   17318 N  N   . GLY   B 1 409  ? 20.01000   84.77500  -35.84800 1.000 30.30229  ?  409  GLY   B N   1 
ATOM   17319 C  CA  . GLY   B 1 409  ? 18.60500   84.88600  -36.16400 1.000 39.28710  ?  409  GLY   B CA  1 
ATOM   17320 C  C   . GLY   B 1 409  ? 17.75400   85.42900  -35.04300 1.000 41.74629  ?  409  GLY   B C   1 
ATOM   17321 O  O   . GLY   B 1 409  ? 16.52200   85.38500  -35.14400 1.000 50.19700  ?  409  GLY   B O   1 
ATOM   17322 N  N   . ALA   B 1 410  ? 18.37100   85.94200  -33.98200 1.000 43.38674  ?  410  ALA   B N   1 
ATOM   17323 C  CA  . ALA   B 1 410  ? 17.65200   86.41400  -32.81200 1.000 19.31978  ?  410  ALA   B CA  1 
ATOM   17324 C  C   . ALA   B 1 410  ? 17.16300   87.84300  -33.03000 1.000 16.36470  ?  410  ALA   B C   1 
ATOM   17325 O  O   . ALA   B 1 410  ? 17.38200   88.45700  -34.07800 1.000 29.16894  ?  410  ALA   B O   1 
ATOM   17326 C  CB  . ALA   B 1 410  ? 18.54100   86.31800  -31.57600 1.000 26.11810  ?  410  ALA   B CB  1 
ATOM   17327 N  N   . ALA   B 1 411  ? 16.49000   88.38200  -32.02000 1.000 27.92910  ?  411  ALA   B N   1 
ATOM   17328 C  CA  . ALA   B 1 411  ? 15.90500   89.71200  -32.08000 1.000 29.18651  ?  411  ALA   B CA  1 
ATOM   17329 C  C   . ALA   B 1 411  ? 16.63400   90.62800  -31.11200 1.000 37.34562  ?  411  ALA   B C   1 
ATOM   17330 O  O   . ALA   B 1 411  ? 16.81100   90.28400  -29.93900 1.000 36.65948  ?  411  ALA   B O   1 
ATOM   17331 C  CB  . ALA   B 1 411  ? 14.41300   89.67100  -31.74200 1.000 32.31257  ?  411  ALA   B CB  1 
ATOM   17332 N  N   . LEU   B 1 412  ? 17.05300   91.78900  -31.60600 1.000 37.57610  ?  412  LEU   B N   1 
ATOM   17333 C  CA  . LEU   B 1 412  ? 17.70400   92.78900  -30.77500 1.000 32.60217  ?  412  LEU   B CA  1 
ATOM   17334 C  C   . LEU   B 1 412  ? 16.65500   93.73900  -30.21800 1.000 38.34354  ?  412  LEU   B C   1 
ATOM   17335 O  O   . LEU   B 1 412  ? 15.81000   94.24600  -30.96200 1.000 52.14296  ?  412  LEU   B O   1 
ATOM   17336 C  CB  . LEU   B 1 412  ? 18.74700   93.57000  -31.57500 1.000 35.27733  ?  412  LEU   B CB  1 
ATOM   17337 C  CG  . LEU   B 1 412  ? 19.75900   92.77500  -32.39800 1.000 35.30487  ?  412  LEU   B CG  1 
ATOM   17338 C  CD1 . LEU   B 1 412  ? 20.72100   93.72100  -33.09300 1.000 30.95532  ?  412  LEU   B CD1 1 
ATOM   17339 C  CD2 . LEU   B 1 412  ? 20.51400   91.80100  -31.51400 1.000 24.71227  ?  412  LEU   B CD2 1 
ATOM   17340 N  N   . HIS   B 1 413  ? 16.71100   93.97800  -28.91300 1.000 32.53940  ?  413  HIS   B N   1 
ATOM   17341 C  CA  . HIS   B 1 413  ? 15.79500   94.89200  -28.24200 1.000 29.72702  ?  413  HIS   B CA  1 
ATOM   17342 C  C   . HIS   B 1 413  ? 16.58700   96.10600  -27.76800 1.000 37.34143  ?  413  HIS   B C   1 
ATOM   17343 O  O   . HIS   B 1 413  ? 17.41200   96.00200  -26.85200 1.000 30.79803  ?  413  HIS   B O   1 
ATOM   17344 C  CB  . HIS   B 1 413  ? 15.07800   94.19500  -27.08800 1.000 32.18262  ?  413  HIS   B CB  1 
ATOM   17345 C  CG  . HIS   B 1 413  ? 13.93500   93.33600  -27.53100 1.000 41.75539  ?  413  HIS   B CG  1 
ATOM   17346 N  ND1 . HIS   B 1 413  ? 12.62300   93.62200  -27.21700 1.000 40.31455  ?  413  HIS   B ND1 1 
ATOM   17347 C  CD2 . HIS   B 1 413  ? 13.90500   92.20600  -28.27700 1.000 40.82252  ?  413  HIS   B CD2 1 
ATOM   17348 C  CE1 . HIS   B 1 413  ? 11.83600   92.70300  -27.74600 1.000 37.44303  ?  413  HIS   B CE1 1 
ATOM   17349 N  NE2 . HIS   B 1 413  ? 12.58800   91.83200  -28.39400 1.000 45.92604  ?  413  HIS   B NE2 1 
ATOM   17350 N  N   . ILE   B 1 414  ? 16.33400   97.25200  -28.40100 1.000 35.15037  ?  414  ILE   B N   1 
ATOM   17351 C  CA  . ILE   B 1 414  ? 17.04700   98.47900  -28.07000 1.000 31.47517  ?  414  ILE   B CA  1 
ATOM   17352 C  C   . ILE   B 1 414  ? 16.61300   98.97100  -26.69700 1.000 43.57718  ?  414  ILE   B C   1 
ATOM   17353 O  O   . ILE   B 1 414  ? 15.41700   99.15400  -26.43100 1.000 56.60496  ?  414  ILE   B O   1 
ATOM   17354 C  CB  . ILE   B 1 414  ? 16.79900   99.55000  -29.14200 1.000 27.90350  ?  414  ILE   B CB  1 
ATOM   17355 C  CG1 . ILE   B 1 414  ? 17.33200   99.08500  -30.49900 1.000 36.98139  ?  414  ILE   B CG1 1 
ATOM   17356 C  CG2 . ILE   B 1 414  ? 17.42400   100.87500 -28.72800 1.000 36.30249  ?  414  ILE   B CG2 1 
ATOM   17357 C  CD1 . ILE   B 1 414  ? 18.84500   99.13100  -30.61600 1.000 48.21206  ?  414  ILE   B CD1 1 
ATOM   17358 N  N   . VAL   B 1 415  ? 17.58700   99.19400  -25.82000 1.000 40.14013  ?  415  VAL   B N   1 
ATOM   17359 C  CA  . VAL   B 1 415  ? 17.34600   99.75300  -24.49400 1.000 51.27038  ?  415  VAL   B CA  1 
ATOM   17360 C  C   . VAL   B 1 415  ? 17.71400   101.23400 -24.54700 1.000 63.38024  ?  415  VAL   B C   1 
ATOM   17361 O  O   . VAL   B 1 415  ? 18.91100   101.55800 -24.63000 1.000 57.94409  ?  415  VAL   B O   1 
ATOM   17362 C  CB  . VAL   B 1 415  ? 18.15400   99.02100  -23.41700 1.000 44.84648  ?  415  VAL   B CB  1 
ATOM   17363 C  CG1 . VAL   B 1 415  ? 17.97500   99.69400  -22.07800 1.000 42.99330  ?  415  VAL   B CG1 1 
ATOM   17364 C  CG2 . VAL   B 1 415  ? 17.72300   97.57700  -23.33800 1.000 51.45103  ?  415  VAL   B CG2 1 
ATOM   17365 N  N   . PRO   B 1 416  ? 16.74700   102.14800 -24.52500 1.000 70.05532  ?  416  PRO   B N   1 
ATOM   17366 C  CA  . PRO   B 1 416  ? 17.08700   103.57600 -24.49900 1.000 63.91011  ?  416  PRO   B CA  1 
ATOM   17367 C  C   . PRO   B 1 416  ? 17.94800   103.90400 -23.28700 1.000 80.12032  ?  416  PRO   B C   1 
ATOM   17368 O  O   . PRO   B 1 416  ? 17.62000   103.53800 -22.15600 1.000 90.53833  ?  416  PRO   B O   1 
ATOM   17369 C  CB  . PRO   B 1 416  ? 15.71700   104.26500 -24.43200 1.000 74.63261  ?  416  PRO   B CB  1 
ATOM   17370 C  CG  . PRO   B 1 416  ? 14.76000   103.19100 -23.96100 1.000 80.78290  ?  416  PRO   B CG  1 
ATOM   17371 C  CD  . PRO   B 1 416  ? 15.29200   101.92600 -24.55000 1.000 67.04549  ?  416  PRO   B CD  1 
ATOM   17372 N  N   . SER   B 1 417  ? 19.07000   104.59100 -23.53500 1.000 90.76173  ?  417  SER   B N   1 
ATOM   17373 C  CA  . SER   B 1 417  ? 19.96700   104.98700 -22.45200 1.000 85.58125  ?  417  SER   B CA  1 
ATOM   17374 C  C   . SER   B 1 417  ? 19.25600   105.80500 -21.37900 1.000 104.01141 ?  417  SER   B C   1 
ATOM   17375 O  O   . SER   B 1 417  ? 19.77700   105.93300 -20.26600 1.000 107.40694 ?  417  SER   B O   1 
ATOM   17376 C  CB  . SER   B 1 417  ? 21.15300   105.77500 -23.01000 1.000 80.80422  ?  417  SER   B CB  1 
ATOM   17377 O  OG  . SER   B 1 417  ? 20.88400   107.16600 -23.00500 1.000 94.02339  ?  417  SER   B OG  1 
ATOM   17378 N  N   . GLU   B 1 418  ? 18.08700   106.37000 -21.69600 1.000 116.57738 ?  418  GLU   B N   1 
ATOM   17379 C  CA  . GLU   B 1 418  ? 17.23700   106.95800 -20.66800 1.000 114.19788 ?  418  GLU   B CA  1 
ATOM   17380 C  C   . GLU   B 1 418  ? 16.73200   105.89900 -19.69200 1.000 105.07148 ?  418  GLU   B C   1 
ATOM   17381 O  O   . GLU   B 1 418  ? 16.54400   106.19000 -18.50500 1.000 116.97077 ?  418  GLU   B O   1 
ATOM   17382 C  CB  . GLU   B 1 418  ? 16.05800   107.68200 -21.32500 1.000 111.34116 ?  418  GLU   B CB  1 
ATOM   17383 C  CG  . GLU   B 1 418  ? 16.45400   108.86600 -22.19700 1.000 125.69146 ?  418  GLU   B CG  1 
ATOM   17384 C  CD  . GLU   B 1 418  ? 15.94500   108.74400 -23.62400 1.000 126.51785 ?  418  GLU   B CD  1 
ATOM   17385 O  OE1 . GLU   B 1 418  ? 15.12300   107.84200 -23.89300 1.000 105.67644 ?  418  GLU   B OE1 1 
ATOM   17386 O  OE2 . GLU   B 1 418  ? 16.37300   109.54900 -24.48000 1.000 129.57655 -1 418  GLU   B OE2 1 
ATOM   17387 N  N   . ARG   B 1 419  ? 16.52300   104.66800 -20.17000 1.000 88.16044  ?  419  ARG   B N   1 
ATOM   17388 C  CA  . ARG   B 1 419  ? 15.96200   103.58100 -19.37000 1.000 90.23582  ?  419  ARG   B CA  1 
ATOM   17389 C  C   . ARG   B 1 419  ? 16.94000   102.40700 -19.29800 1.000 88.46168  ?  419  ARG   B C   1 
ATOM   17390 O  O   . ARG   B 1 419  ? 16.61400   101.28900 -19.69800 1.000 93.96588  ?  419  ARG   B O   1 
ATOM   17391 C  CB  . ARG   B 1 419  ? 14.60500   103.15500 -19.97000 1.000 96.07144  ?  419  ARG   B CB  1 
ATOM   17392 C  CG  . ARG   B 1 419  ? 13.77800   102.04100 -19.26700 1.000 105.01279 ?  419  ARG   B CG  1 
ATOM   17393 C  CD  . ARG   B 1 419  ? 13.87100   100.69400 -19.99300 1.000 94.16445  ?  419  ARG   B CD  1 
ATOM   17394 N  NE  . ARG   B 1 419  ? 12.89600   100.55000 -21.06400 1.000 108.83049 ?  419  ARG   B NE  1 
ATOM   17395 C  CZ  . ARG   B 1 419  ? 13.15400   99.99000  -22.23800 1.000 94.93841  ?  419  ARG   B CZ  1 
ATOM   17396 N  NH1 . ARG   B 1 419  ? 14.35800   99.52500  -22.53500 1.000 77.64346  ?  419  ARG   B NH1 1 
ATOM   17397 N  NH2 . ARG   B 1 419  ? 12.18000   99.89300  -23.13800 1.000 72.75828  ?  419  ARG   B NH2 1 
ATOM   17398 N  N   . LYS   B 1 420  ? 18.15800   102.62900 -18.81400 1.000 81.60882  ?  420  LYS   B N   1 
ATOM   17399 C  CA  . LYS   B 1 420  ? 19.04400   101.50100 -18.55900 1.000 65.41558  ?  420  LYS   B CA  1 
ATOM   17400 C  C   . LYS   B 1 420  ? 19.68400   101.58100 -17.18200 1.000 67.75742  ?  420  LYS   B C   1 
ATOM   17401 O  O   . LYS   B 1 420  ? 20.55400   100.76200 -16.86500 1.000 53.12417  ?  420  LYS   B O   1 
ATOM   17402 C  CB  . LYS   B 1 420  ? 20.12200   101.36500 -19.65300 1.000 65.19145  ?  420  LYS   B CB  1 
ATOM   17403 C  CG  . LYS   B 1 420  ? 21.02400   102.56900 -19.91000 1.000 77.79751  ?  420  LYS   B CG  1 
ATOM   17404 C  CD  . LYS   B 1 420  ? 22.18200   102.19600 -20.84900 1.000 57.73248  ?  420  LYS   B CD  1 
ATOM   17405 C  CE  . LYS   B 1 420  ? 23.44300   101.85600 -20.06300 1.000 59.66981  ?  420  LYS   B CE  1 
ATOM   17406 N  NZ  . LYS   B 1 420  ? 24.68900   102.05200 -20.85200 1.000 48.69977  ?  420  LYS   B NZ  1 
ATOM   17407 N  N   . TYR   B 1 421  ? 19.27100   102.53900 -16.35100 1.000 64.62931  ?  421  TYR   B N   1 
ATOM   17408 C  CA  . TYR   B 1 421  ? 19.81200   102.68300 -15.00900 1.000 53.40924  ?  421  TYR   B CA  1 
ATOM   17409 C  C   . TYR   B 1 421  ? 18.80800   102.31000 -13.92800 1.000 59.40677  ?  421  TYR   B C   1 
ATOM   17410 O  O   . TYR   B 1 421  ? 19.20300   102.15500 -12.76800 1.000 73.03496  ?  421  TYR   B O   1 
ATOM   17411 C  CB  . TYR   B 1 421  ? 20.31500   104.12200 -14.77700 1.000 65.64800  ?  421  TYR   B CB  1 
ATOM   17412 C  CG  . TYR   B 1 421  ? 21.34900   104.63900 -15.77800 1.000 79.86590  ?  421  TYR   B CG  1 
ATOM   17413 C  CD1 . TYR   B 1 421  ? 21.86200   103.82100 -16.77600 1.000 83.82440  ?  421  TYR   B CD1 1 
ATOM   17414 C  CD2 . TYR   B 1 421  ? 21.78500   105.96800 -15.73800 1.000 87.57307  ?  421  TYR   B CD2 1 
ATOM   17415 C  CE1 . TYR   B 1 421  ? 22.78800   104.28500 -17.68100 1.000 89.74972  ?  421  TYR   B CE1 1 
ATOM   17416 C  CE2 . TYR   B 1 421  ? 22.72200   106.44800 -16.65300 1.000 96.33863  ?  421  TYR   B CE2 1 
ATOM   17417 C  CZ  . TYR   B 1 421  ? 23.21700   105.58900 -17.62400 1.000 105.60967 ?  421  TYR   B CZ  1 
ATOM   17418 O  OH  . TYR   B 1 421  ? 24.14200   105.98900 -18.56200 1.000 105.02267 ?  421  TYR   B OH  1 
ATOM   17419 N  N   . ASP   B 1 422  ? 17.52700   102.17400 -14.26900 1.000 56.77953  ?  422  ASP   B N   1 
ATOM   17420 C  CA  . ASP   B 1 422  ? 16.53400   101.59700 -13.36500 1.000 55.45033  ?  422  ASP   B CA  1 
ATOM   17421 C  C   . ASP   B 1 422  ? 16.50600   100.09900 -13.62900 1.000 58.14920  ?  422  ASP   B C   1 
ATOM   17422 O  O   . ASP   B 1 422  ? 15.91200   99.63700  -14.60500 1.000 63.23658  ?  422  ASP   B O   1 
ATOM   17423 C  CB  . ASP   B 1 422  ? 15.16200   102.22900 -13.57000 1.000 45.17000  ?  422  ASP   B CB  1 
ATOM   17424 C  CG  . ASP   B 1 422  ? 14.13400   101.72500 -12.57100 1.000 67.60333  ?  422  ASP   B CG  1 
ATOM   17425 O  OD1 . ASP   B 1 422  ? 14.51000   100.98400 -11.63600 1.000 66.80703  ?  422  ASP   B OD1 1 
ATOM   17426 O  OD2 . ASP   B 1 422  ? 12.94200   102.06100 -12.72900 1.000 76.63100  -1 422  ASP   B OD2 1 
ATOM   17427 N  N   . LEU   B 1 423  ? 17.16100   99.33600  -12.75600 1.000 55.15930  ?  423  LEU   B N   1 
ATOM   17428 C  CA  . LEU   B 1 423  ? 17.25900   97.89800  -12.96900 1.000 60.51858  ?  423  LEU   B CA  1 
ATOM   17429 C  C   . LEU   B 1 423  ? 15.92900   97.20900  -12.70200 1.000 61.19060  ?  423  LEU   B C   1 
ATOM   17430 O  O   . LEU   B 1 423  ? 15.64900   96.15400  -13.28400 1.000 55.00367  ?  423  LEU   B O   1 
ATOM   17431 C  CB  . LEU   B 1 423  ? 18.36400   97.30500  -12.09100 1.000 55.92380  ?  423  LEU   B CB  1 
ATOM   17432 C  CG  . LEU   B 1 423  ? 19.85000   97.59000  -12.39200 1.000 72.01071  ?  423  LEU   B CG  1 
ATOM   17433 C  CD1 . LEU   B 1 423  ? 20.31500   96.80800  -13.61200 1.000 59.82896  ?  423  LEU   B CD1 1 
ATOM   17434 C  CD2 . LEU   B 1 423  ? 20.21500   99.07000  -12.54300 1.000 67.05752  ?  423  LEU   B CD2 1 
ATOM   17435 N  N   . ASP   B 1 424  ? 15.09900   97.78800  -11.83000 1.000 60.86063  ?  424  ASP   B N   1 
ATOM   17436 C  CA  . ASP   B 1 424  ? 13.75400   97.26400  -11.63000 1.000 65.93024  ?  424  ASP   B CA  1 
ATOM   17437 C  C   . ASP   B 1 424  ? 12.93800   97.36300  -12.91200 1.000 65.96470  ?  424  ASP   B C   1 
ATOM   17438 O  O   . ASP   B 1 424  ? 12.24700   96.41100  -13.29600 1.000 65.89256  ?  424  ASP   B O   1 
ATOM   17439 C  CB  . ASP   B 1 424  ? 13.06400   98.01700  -10.49100 1.000 65.61426  ?  424  ASP   B CB  1 
ATOM   17440 C  CG  . ASP   B 1 424  ? 12.33700   97.09200  -9.53200  1.000 90.76104  ?  424  ASP   B CG  1 
ATOM   17441 O  OD1 . ASP   B 1 424  ? 11.50700   96.28100  -9.99500  1.000 103.81494 ?  424  ASP   B OD1 1 
ATOM   17442 O  OD2 . ASP   B 1 424  ? 12.59100   97.17900  -8.31200  1.000 93.70416  -1 424  ASP   B OD2 1 
ATOM   17443 N  N   . ALA   B 1 425  ? 13.01800   98.50600  -13.59600 1.000 51.83057  ?  425  ALA   B N   1 
ATOM   17444 C  CA  . ALA   B 1 425  ? 12.29100   98.67100  -14.84900 1.000 43.15870  ?  425  ALA   B CA  1 
ATOM   17445 C  C   . ALA   B 1 425  ? 12.83800   97.74800  -15.92900 1.000 55.94445  ?  425  ALA   B C   1 
ATOM   17446 O  O   . ALA   B 1 425  ? 12.06800   97.14400  -16.68500 1.000 61.71576  ?  425  ALA   B O   1 
ATOM   17447 C  CB  . ALA   B 1 425  ? 12.35600   100.12800 -15.30300 1.000 40.41488  ?  425  ALA   B CB  1 
ATOM   17448 N  N   . LEU   B 1 426  ? 14.16500   97.62600  -16.01500 1.000 50.18264  ?  426  LEU   B N   1 
ATOM   17449 C  CA  . LEU   B 1 426  ? 14.76900   96.73700  -17.00100 1.000 43.40169  ?  426  LEU   B CA  1 
ATOM   17450 C  C   . LEU   B 1 426  ? 14.33900   95.29600  -16.76600 1.000 47.16534  ?  426  LEU   B C   1 
ATOM   17451 O  O   . LEU   B 1 426  ? 13.99100   94.57700  -17.70900 1.000 49.79108  ?  426  LEU   B O   1 
ATOM   17452 C  CB  . LEU   B 1 426  ? 16.29100   96.85700  -16.95400 1.000 61.88013  ?  426  LEU   B CB  1 
ATOM   17453 C  CG  . LEU   B 1 426  ? 17.05400   96.34600  -18.17900 1.000 55.04585  ?  426  LEU   B CG  1 
ATOM   17454 C  CD1 . LEU   B 1 426  ? 16.80900   97.24100  -19.38000 1.000 37.63063  ?  426  LEU   B CD1 1 
ATOM   17455 C  CD2 . LEU   B 1 426  ? 18.54000   96.24600  -17.88200 1.000 50.84850  ?  426  LEU   B CD2 1 
ATOM   17456 N  N   . ASN   B 1 427  ? 14.35600   94.85800  -15.50400 1.000 53.06005  ?  427  ASN   B N   1 
ATOM   17457 C  CA  . ASN   B 1 427  ? 13.94100   93.49500  -15.19000 1.000 50.28815  ?  427  ASN   B CA  1 
ATOM   17458 C  C   . ASN   B 1 427  ? 12.49000   93.25700  -15.58600 1.000 42.16686  ?  427  ASN   B C   1 
ATOM   17459 O  O   . ASN   B 1 427  ? 12.13000   92.15700  -16.02500 1.000 42.92259  ?  427  ASN   B O   1 
ATOM   17460 C  CB  . ASN   B 1 427  ? 14.14400   93.21700  -13.70300 1.000 47.24550  ?  427  ASN   B CB  1 
ATOM   17461 C  CG  . ASN   B 1 427  ? 13.65100   91.84600  -13.29900 1.000 53.76890  ?  427  ASN   B CG  1 
ATOM   17462 O  OD1 . ASN   B 1 427  ? 13.92500   90.85300  -13.97400 1.000 41.04034  ?  427  ASN   B OD1 1 
ATOM   17463 N  ND2 . ASN   B 1 427  ? 12.91400   91.78400  -12.19600 1.000 44.01658  ?  427  ASN   B ND2 1 
ATOM   17464 N  N   . ASP   B 1 428  ? 11.64400   94.27800  -15.43800 1.000 53.29806  ?  428  ASP   B N   1 
ATOM   17465 C  CA  . ASP   B 1 428  ? 10.25900   94.16600  -15.88200 1.000 41.55443  ?  428  ASP   B CA  1 
ATOM   17466 C  C   . ASP   B 1 428  ? 10.18700   94.01600  -17.39600 1.000 49.43425  ?  428  ASP   B C   1 
ATOM   17467 O  O   . ASP   B 1 428  ? 9.50200    93.12400  -17.91000 1.000 55.49359  ?  428  ASP   B O   1 
ATOM   17468 C  CB  . ASP   B 1 428  ? 9.45900    95.38500  -15.41900 1.000 34.52463  ?  428  ASP   B CB  1 
ATOM   17469 C  CG  . ASP   B 1 428  ? 9.24400    95.40800  -13.91600 1.000 57.63392  ?  428  ASP   B CG  1 
ATOM   17470 O  OD1 . ASP   B 1 428  ? 9.29200    94.32800  -13.28800 1.000 62.24432  ?  428  ASP   B OD1 1 
ATOM   17471 O  OD2 . ASP   B 1 428  ? 9.02100    96.50800  -13.36400 1.000 54.39542  -1 428  ASP   B OD2 1 
ATOM   17472 N  N   . TYR   B 1 429  ? 10.89500   94.88400  -18.12600 1.000 45.91896  ?  429  TYR   B N   1 
ATOM   17473 C  CA  . TYR   B 1 429  ? 10.95500   94.77000  -19.58100 1.000 37.96664  ?  429  TYR   B CA  1 
ATOM   17474 C  C   . TYR   B 1 429  ? 11.42900   93.38500  -20.00000 1.000 38.11841  ?  429  TYR   B C   1 
ATOM   17475 O  O   . TYR   B 1 429  ? 10.81200   92.73300  -20.84900 1.000 43.53781  ?  429  TYR   B O   1 
ATOM   17476 C  CB  . TYR   B 1 429  ? 11.87600   95.85100  -20.15300 1.000 34.16290  ?  429  TYR   B CB  1 
ATOM   17477 C  CG  . TYR   B 1 429  ? 11.93000   95.89500  -21.66800 1.000 45.43269  ?  429  TYR   B CG  1 
ATOM   17478 C  CD1 . TYR   B 1 429  ? 12.75500   95.03600  -22.38300 1.000 47.71470  ?  429  TYR   B CD1 1 
ATOM   17479 C  CD2 . TYR   B 1 429  ? 11.16100   96.80500  -22.38200 1.000 55.60164  ?  429  TYR   B CD2 1 
ATOM   17480 C  CE1 . TYR   B 1 429  ? 12.80500   95.07600  -23.76500 1.000 49.64289  ?  429  TYR   B CE1 1 
ATOM   17481 C  CE2 . TYR   B 1 429  ? 11.20500   96.85200  -23.76500 1.000 42.33494  ?  429  TYR   B CE2 1 
ATOM   17482 C  CZ  . TYR   B 1 429  ? 12.02700   95.98700  -24.45100 1.000 50.22577  ?  429  TYR   B CZ  1 
ATOM   17483 O  OH  . TYR   B 1 429  ? 12.07100   96.03500  -25.82600 1.000 47.92151  ?  429  TYR   B OH  1 
ATOM   17484 N  N   . CYS   B 1 430  ? 12.52700   92.91300  -19.40400 1.000 36.39772  ?  430  CYS   B N   1 
ATOM   17485 C  CA  . CYS   B 1 430  ? 13.05700   91.60600  -19.77600 1.000 38.16146  ?  430  CYS   B CA  1 
ATOM   17486 C  C   . CYS   B 1 430  ? 12.04700   90.50300  -19.49600 1.000 45.68628  ?  430  CYS   B C   1 
ATOM   17487 O  O   . CYS   B 1 430  ? 11.92000   89.55200  -20.27700 1.000 47.48789  ?  430  CYS   B O   1 
ATOM   17488 C  CB  . CYS   B 1 430  ? 14.36500   91.33900  -19.03400 1.000 32.41835  ?  430  CYS   B CB  1 
ATOM   17489 S  SG  . CYS   B 1 430  ? 15.64900   92.56300  -19.36400 1.000 45.06715  ?  430  CYS   B SG  1 
ATOM   17490 N  N   . ASN   B 1 431  ? 11.30900   90.61800  -18.39200 1.000 48.78047  ?  431  ASN   B N   1 
ATOM   17491 C  CA  . ASN   B 1 431  ? 10.31100   89.60400  -18.07700 1.000 48.71231  ?  431  ASN   B CA  1 
ATOM   17492 C  C   . ASN   B 1 431  ? 9.08300    89.73100  -18.97000 1.000 41.56218  ?  431  ASN   B C   1 
ATOM   17493 O  O   . ASN   B 1 431  ? 8.48000    88.71700  -19.34000 1.000 28.48196  ?  431  ASN   B O   1 
ATOM   17494 C  CB  . ASN   B 1 431  ? 9.92300    89.69900  -16.60100 1.000 29.31635  ?  431  ASN   B CB  1 
ATOM   17495 C  CG  . ASN   B 1 431  ? 10.92200   89.00300  -15.68900 1.000 47.13258  ?  431  ASN   B CG  1 
ATOM   17496 O  OD1 . ASN   B 1 431  ? 11.61700   88.07300  -16.10300 1.000 48.40710  ?  431  ASN   B OD1 1 
ATOM   17497 N  ND2 . ASN   B 1 431  ? 10.99100   89.44700  -14.43900 1.000 42.92339  ?  431  ASN   B ND2 1 
ATOM   17498 N  N   . GLN   B 1 432  ? 8.71000    90.95800  -19.33700 1.000 36.41195  ?  432  GLN   B N   1 
ATOM   17499 C  CA  . GLN   B 1 432  ? 7.52800    91.16700  -20.16500 1.000 36.53889  ?  432  GLN   B CA  1 
ATOM   17500 C  C   . GLN   B 1 432  ? 7.79300    90.85500  -21.62900 1.000 47.48828  ?  432  GLN   B C   1 
ATOM   17501 O  O   . GLN   B 1 432  ? 6.87400    90.44700  -22.34900 1.000 55.17425  ?  432  GLN   B O   1 
ATOM   17502 C  CB  . GLN   B 1 432  ? 7.03500    92.60900  -20.02700 1.000 43.47676  ?  432  GLN   B CB  1 
ATOM   17503 C  CG  . GLN   B 1 432  ? 6.41300    92.93900  -18.67700 1.000 43.56883  ?  432  GLN   B CG  1 
ATOM   17504 C  CD  . GLN   B 1 432  ? 6.45200    94.42500  -18.36700 1.000 55.42614  ?  432  GLN   B CD  1 
ATOM   17505 O  OE1 . GLN   B 1 432  ? 7.03900    95.21100  -19.11200 1.000 53.06217  ?  432  GLN   B OE1 1 
ATOM   17506 N  NE2 . GLN   B 1 432  ? 5.82100    94.81700  -17.26600 1.000 68.72485  ?  432  GLN   B NE2 1 
ATOM   17507 N  N   . GLU   B 1 433  ? 9.02900    91.03800  -22.08700 1.000 47.62290  ?  433  GLU   B N   1 
ATOM   17508 C  CA  . GLU   B 1 433  ? 9.36200    90.81400  -23.48500 1.000 41.13264  ?  433  GLU   B CA  1 
ATOM   17509 C  C   . GLU   B 1 433  ? 10.02100   89.46600  -23.74000 1.000 39.20145  ?  433  GLU   B C   1 
ATOM   17510 O  O   . GLU   B 1 433  ? 10.07100   89.03100  -24.89500 1.000 55.60266  ?  433  GLU   B O   1 
ATOM   17511 C  CB  . GLU   B 1 433  ? 10.28100   91.92800  -23.99100 1.000 45.03669  ?  433  GLU   B CB  1 
ATOM   17512 C  CG  . GLU   B 1 433  ? 9.74100    93.32900  -23.75300 1.000 55.16178  ?  433  GLU   B CG  1 
ATOM   17513 C  CD  . GLU   B 1 433  ? 8.65100    93.70100  -24.72700 1.000 71.11796  ?  433  GLU   B CD  1 
ATOM   17514 O  OE1 . GLU   B 1 433  ? 8.66500    93.16300  -25.85400 1.000 58.97022  ?  433  GLU   B OE1 1 
ATOM   17515 O  OE2 . GLU   B 1 433  ? 7.77000    94.51400  -24.36700 1.000 74.31956  -1 433  GLU   B OE2 1 
ATOM   17516 N  N   . GLY   B 1 434  ? 10.53000   88.80200  -22.70600 1.000 27.56221  ?  434  GLY   B N   1 
ATOM   17517 C  CA  . GLY   B 1 434  ? 11.09800   87.47900  -22.87400 1.000 38.00133  ?  434  GLY   B CA  1 
ATOM   17518 C  C   . GLY   B 1 434  ? 12.55600   87.46300  -23.28600 1.000 45.49528  ?  434  GLY   B C   1 
ATOM   17519 O  O   . GLY   B 1 434  ? 12.97600   86.60500  -24.06800 1.000 48.20396  ?  434  GLY   B O   1 
ATOM   17520 N  N   . ILE   B 1 435  ? 13.34100   88.40200  -22.75800 1.000 43.07439  ?  435  ILE   B N   1 
ATOM   17521 C  CA  . ILE   B 1 435  ? 14.76500   88.44900  -23.06100 1.000 30.12859  ?  435  ILE   B CA  1 
ATOM   17522 C  C   . ILE   B 1 435  ? 15.45500   87.23900  -22.44800 1.000 40.22496  ?  435  ILE   B C   1 
ATOM   17523 O  O   . ILE   B 1 435  ? 15.28700   86.94500  -21.25700 1.000 43.38620  ?  435  ILE   B O   1 
ATOM   17524 C  CB  . ILE   B 1 435  ? 15.37900   89.75800  -22.54800 1.000 35.49226  ?  435  ILE   B CB  1 
ATOM   17525 C  CG1 . ILE   B 1 435  ? 14.52600   90.95400  -22.99100 1.000 32.80217  ?  435  ILE   B CG1 1 
ATOM   17526 C  CG2 . ILE   B 1 435  ? 16.82600   89.87400  -23.00800 1.000 35.91876  ?  435  ILE   B CG2 1 
ATOM   17527 C  CD1 . ILE   B 1 435  ? 14.37200   91.09700  -24.49200 1.000 29.28783  ?  435  ILE   B CD1 1 
ATOM   17528 N  N   . THR   B 1 436  ? 16.24400   86.53700  -23.25900 1.000 35.53125  ?  436  THR   B N   1 
ATOM   17529 C  CA  . THR   B 1 436  ? 16.86500   85.27600  -22.86800 1.000 34.80394  ?  436  THR   B CA  1 
ATOM   17530 C  C   . THR   B 1 436  ? 18.36700   85.36800  -22.65400 1.000 34.67066  ?  436  THR   B C   1 
ATOM   17531 O  O   . THR   B 1 436  ? 18.88800   84.74600  -21.72700 1.000 37.23470  ?  436  THR   B O   1 
ATOM   17532 C  CB  . THR   B 1 436  ? 16.57500   84.20100  -23.92300 1.000 35.34182  ?  436  THR   B CB  1 
ATOM   17533 O  OG1 . THR   B 1 436  ? 16.96200   84.67400  -25.22000 1.000 31.61387  ?  436  THR   B OG1 1 
ATOM   17534 C  CG2 . THR   B 1 436  ? 15.09800   83.86700  -23.93900 1.000 27.68451  ?  436  THR   B CG2 1 
ATOM   17535 N  N   . ILE   B 1 437  ? 19.07800   86.12600  -23.48400 1.000 46.20834  ?  437  ILE   B N   1 
ATOM   17536 C  CA  . ILE   B 1 437  ? 20.53300   86.21000  -23.42900 1.000 35.79321  ?  437  ILE   B CA  1 
ATOM   17537 C  C   . ILE   B 1 437  ? 20.93400   87.67000  -23.57300 1.000 40.63898  ?  437  ILE   B C   1 
ATOM   17538 O  O   . ILE   B 1 437  ? 20.29400   88.42800  -24.31000 1.000 44.65226  ?  437  ILE   B O   1 
ATOM   17539 C  CB  . ILE   B 1 437  ? 21.18600   85.33500  -24.52200 1.000 27.74623  ?  437  ILE   B CB  1 
ATOM   17540 C  CG1 . ILE   B 1 437  ? 22.70100   85.24800  -24.32400 1.000 33.59075  ?  437  ILE   B CG1 1 
ATOM   17541 C  CG2 . ILE   B 1 437  ? 20.83700   85.84800  -25.91600 1.000 29.14827  ?  437  ILE   B CG2 1 
ATOM   17542 C  CD1 . ILE   B 1 437  ? 23.34200   84.07100  -25.03600 1.000 29.76790  ?  437  ILE   B CD1 1 
ATOM   17543 N  N   . SER   B 1 438  ? 21.98100   88.07200  -22.85400 1.000 30.74279  ?  438  SER   B N   1 
ATOM   17544 C  CA  . SER   B 1 438  ? 22.45300   89.45200  -22.89400 1.000 44.23360  ?  438  SER   B CA  1 
ATOM   17545 C  C   . SER   B 1 438  ? 23.75400   89.55900  -22.11600 1.000 44.62708  ?  438  SER   B C   1 
ATOM   17546 O  O   . SER   B 1 438  ? 24.09100   88.68700  -21.31000 1.000 41.35086  ?  438  SER   B O   1 
ATOM   17547 C  CB  . SER   B 1 438  ? 21.41700   90.42500  -22.32200 1.000 35.32979  ?  438  SER   B CB  1 
ATOM   17548 O  OG  . SER   B 1 438  ? 20.32000   90.56900  -23.20700 1.000 44.69546  ?  438  SER   B OG  1 
ATOM   17549 N  N   . TYR   B 1 439  ? 24.48100   90.64300  -22.37000 1.000 34.71529  ?  439  TYR   B N   1 
ATOM   17550 C  CA  . TYR   B 1 439  ? 25.68800   90.97100  -21.62700 1.000 30.11649  ?  439  TYR   B CA  1 
ATOM   17551 C  C   . TYR   B 1 439  ? 25.43600   92.21000  -20.78600 1.000 33.59860  ?  439  TYR   B C   1 
ATOM   17552 O  O   . TYR   B 1 439  ? 25.04000   93.25500  -21.31500 1.000 43.01443  ?  439  TYR   B O   1 
ATOM   17553 C  CB  . TYR   B 1 439  ? 26.87800   91.22100  -22.55600 1.000 35.08361  ?  439  TYR   B CB  1 
ATOM   17554 C  CG  . TYR   B 1 439  ? 28.01100   91.97100  -21.88400 1.000 35.54940  ?  439  TYR   B CG  1 
ATOM   17555 C  CD1 . TYR   B 1 439  ? 28.81200   91.35200  -20.93200 1.000 30.92839  ?  439  TYR   B CD1 1 
ATOM   17556 C  CD2 . TYR   B 1 439  ? 28.27000   93.30200  -22.18900 1.000 35.56320  ?  439  TYR   B CD2 1 
ATOM   17557 C  CE1 . TYR   B 1 439  ? 29.84400   92.02900  -20.31200 1.000 26.06221  ?  439  TYR   B CE1 1 
ATOM   17558 C  CE2 . TYR   B 1 439  ? 29.30100   93.99000  -21.57200 1.000 27.74900  ?  439  TYR   B CE2 1 
ATOM   17559 C  CZ  . TYR   B 1 439  ? 30.08500   93.34700  -20.63400 1.000 36.86423  ?  439  TYR   B CZ  1 
ATOM   17560 O  OH  . TYR   B 1 439  ? 31.11600   94.02000  -20.01300 1.000 36.56530  ?  439  TYR   B OH  1 
ATOM   17561 N  N   . LEU   B 1 440  ? 25.67300   92.09100  -19.48600 1.000 36.09042  ?  440  LEU   B N   1 
ATOM   17562 C  CA  . LEU   B 1 440  ? 25.62000   93.22200  -18.58500 1.000 39.96742  ?  440  LEU   B CA  1 
ATOM   17563 C  C   . LEU   B 1 440  ? 26.99300   93.45000  -17.96800 1.000 44.80532  ?  440  LEU   B C   1 
ATOM   17564 O  O   . LEU   B 1 440  ? 27.66000   92.48400  -17.57900 1.000 43.35156  ?  440  LEU   B O   1 
ATOM   17565 C  CB  . LEU   B 1 440  ? 24.58500   92.99600  -17.47200 1.000 32.77207  ?  440  LEU   B CB  1 
ATOM   17566 C  CG  . LEU   B 1 440  ? 23.14500   92.78000  -17.93500 1.000 26.37848  ?  440  LEU   B CG  1 
ATOM   17567 C  CD1 . LEU   B 1 440  ? 22.25000   92.39600  -16.76500 1.000 27.65680  ?  440  LEU   B CD1 1 
ATOM   17568 C  CD2 . LEU   B 1 440  ? 22.62400   94.02600  -18.63500 1.000 31.80814  ?  440  LEU   B CD2 1 
ATOM   17569 N  N   . PRO   B 1 441  ? 27.45200   94.69800  -17.88600 1.000 45.75312  ?  441  PRO   B N   1 
ATOM   17570 C  CA  . PRO   B 1 441  ? 28.71700   94.97500  -17.19700 1.000 30.51978  ?  441  PRO   B CA  1 
ATOM   17571 C  C   . PRO   B 1 441  ? 28.67800   94.49000  -15.75400 1.000 37.05819  ?  441  PRO   B C   1 
ATOM   17572 O  O   . PRO   B 1 441  ? 27.61300   94.28800  -15.16700 1.000 52.59809  ?  441  PRO   B O   1 
ATOM   17573 C  CB  . PRO   B 1 441  ? 28.83500   96.50200  -17.27100 1.000 37.14576  ?  441  PRO   B CB  1 
ATOM   17574 C  CG  . PRO   B 1 441  ? 28.02900   96.87900  -18.47100 1.000 54.34099  ?  441  PRO   B CG  1 
ATOM   17575 C  CD  . PRO   B 1 441  ? 26.88400   95.90300  -18.51500 1.000 44.92840  ?  441  PRO   B CD  1 
ATOM   17576 N  N   . THR   B 1 442  ? 29.87200   94.31000  -15.18200 1.000 46.39089  ?  442  THR   B N   1 
ATOM   17577 C  CA  . THR   B 1 442  ? 29.98300   93.69400  -13.86100 1.000 42.02061  ?  442  THR   B CA  1 
ATOM   17578 C  C   . THR   B 1 442  ? 29.19800   94.46800  -12.80800 1.000 43.90528  ?  442  THR   B C   1 
ATOM   17579 O  O   . THR   B 1 442  ? 28.51500   93.86800  -11.96900 1.000 46.29854  ?  442  THR   B O   1 
ATOM   17580 C  CB  . THR   B 1 442  ? 31.45200   93.58200  -13.45500 1.000 38.18624  ?  442  THR   B CB  1 
ATOM   17581 O  OG1 . THR   B 1 442  ? 32.16100   92.79900  -14.42400 1.000 38.45666  ?  442  THR   B OG1 1 
ATOM   17582 C  CG2 . THR   B 1 442  ? 31.57500   92.91800  -12.09200 1.000 35.23861  ?  442  THR   B CG2 1 
ATOM   17583 N  N   . GLY   B 1 443  ? 29.27600   95.79900  -12.83700 1.000 35.78349  ?  443  GLY   B N   1 
ATOM   17584 C  CA  . GLY   B 1 443  ? 28.55900   96.58900  -11.84900 1.000 38.87989  ?  443  GLY   B CA  1 
ATOM   17585 C  C   . GLY   B 1 443  ? 27.05300   96.49500  -12.00300 1.000 53.12180  ?  443  GLY   B C   1 
ATOM   17586 O  O   . GLY   B 1 443  ? 26.32700   96.34400  -11.01600 1.000 61.63588  ?  443  GLY   B O   1 
ATOM   17587 N  N   . ALA   B 1 444  ? 26.56300   96.58000  -13.24000 1.000 57.68953  ?  444  ALA   B N   1 
ATOM   17588 C  CA  . ALA   B 1 444  ? 25.12500   96.51100  -13.47100 1.000 44.53059  ?  444  ALA   B CA  1 
ATOM   17589 C  C   . ALA   B 1 444  ? 24.59000   95.10900  -13.21100 1.000 45.80978  ?  444  ALA   B C   1 
ATOM   17590 O  O   . ALA   B 1 444  ? 23.46100   94.94700  -12.73100 1.000 40.78482  ?  444  ALA   B O   1 
ATOM   17591 C  CB  . ALA   B 1 444  ? 24.80200   96.95600  -14.89700 1.000 32.58798  ?  444  ALA   B CB  1 
ATOM   17592 N  N   . ALA   B 1 445  ? 25.38900   94.08400  -13.51600 1.000 45.70604  ?  445  ALA   B N   1 
ATOM   17593 C  CA  . ALA   B 1 445  ? 24.94400   92.70800  -13.32000 1.000 41.24941  ?  445  ALA   B CA  1 
ATOM   17594 C  C   . ALA   B 1 445  ? 24.74900   92.40000  -11.84200 1.000 49.30636  ?  445  ALA   B C   1 
ATOM   17595 O  O   . ALA   B 1 445  ? 23.71700   91.85100  -11.44100 1.000 55.82126  ?  445  ALA   B O   1 
ATOM   17596 C  CB  . ALA   B 1 445  ? 25.94600   91.73700  -13.94500 1.000 29.40439  ?  445  ALA   B CB  1 
ATOM   17597 N  N   . GLU   B 1 446  ? 25.73300   92.75800  -11.01200 1.000 57.73861  ?  446  GLU   B N   1 
ATOM   17598 C  CA  . GLU   B 1 446  ? 25.65100   92.48300  -9.58200  1.000 49.75159  ?  446  GLU   B CA  1 
ATOM   17599 C  C   . GLU   B 1 446  ? 24.44700   93.15300  -8.93400  1.000 43.61276  ?  446  GLU   B C   1 
ATOM   17600 O  O   . GLU   B 1 446  ? 23.96300   92.67000  -7.90500  1.000 56.07855  ?  446  GLU   B O   1 
ATOM   17601 C  CB  . GLU   B 1 446  ? 26.94100   92.92900  -8.89000  1.000 52.83029  ?  446  GLU   B CB  1 
ATOM   17602 C  CG  . GLU   B 1 446  ? 28.12700   92.00400  -9.13400  1.000 50.85462  ?  446  GLU   B CG  1 
ATOM   17603 C  CD  . GLU   B 1 446  ? 29.19600   92.11200  -8.05900  1.000 61.02093  ?  446  GLU   B CD  1 
ATOM   17604 O  OE1 . GLU   B 1 446  ? 28.91300   92.68600  -6.98600  1.000 81.38041  ?  446  GLU   B OE1 1 
ATOM   17605 O  OE2 . GLU   B 1 446  ? 30.31700   91.61000  -8.28200  1.000 55.47429  -1 446  GLU   B OE2 1 
ATOM   17606 N  N   . GLN   B 1 447  ? 23.95500   94.24900  -9.50600  1.000 48.01257  ?  447  GLN   B N   1 
ATOM   17607 C  CA  . GLN   B 1 447  ? 22.73300   94.88000  -9.03000  1.000 44.66472  ?  447  GLN   B CA  1 
ATOM   17608 C  C   . GLN   B 1 447  ? 21.49100   94.38500  -9.75700  1.000 47.77271  ?  447  GLN   B C   1 
ATOM   17609 O  O   . GLN   B 1 447  ? 20.37900   94.76000  -9.37500  1.000 49.03689  ?  447  GLN   B O   1 
ATOM   17610 C  CB  . GLN   B 1 447  ? 22.83000   96.40200  -9.16800  1.000 38.93818  ?  447  GLN   B CB  1 
ATOM   17611 C  CG  . GLN   B 1 447  ? 23.83800   97.03800  -8.23100  1.000 53.73533  ?  447  GLN   B CG  1 
ATOM   17612 C  CD  . GLN   B 1 447  ? 23.63200   98.53100  -8.07900  1.000 65.32765  ?  447  GLN   B CD  1 
ATOM   17613 O  OE1 . GLN   B 1 447  ? 22.65700   99.09200  -8.58000  1.000 73.72795  ?  447  GLN   B OE1 1 
ATOM   17614 N  NE2 . GLN   B 1 447  ? 24.55400   99.18500  -7.38400  1.000 64.18800  ?  447  GLN   B NE2 1 
ATOM   17615 N  N   . PHE   B 1 448  ? 21.65200   93.57900  -10.80400 1.000 41.90236  ?  448  PHE   B N   1 
ATOM   17616 C  CA  . PHE   B 1 448  ? 20.52800   92.90500  -11.43500 1.000 39.51360  ?  448  PHE   B CA  1 
ATOM   17617 C  C   . PHE   B 1 448  ? 20.25200   91.54500  -10.81600 1.000 41.26950  ?  448  PHE   B C   1 
ATOM   17618 O  O   . PHE   B 1 448  ? 19.12700   91.04400  -10.92800 1.000 35.12741  ?  448  PHE   B O   1 
ATOM   17619 C  CB  . PHE   B 1 448  ? 20.78700   92.74600  -12.93900 1.000 47.11630  ?  448  PHE   B CB  1 
ATOM   17620 C  CG  . PHE   B 1 448  ? 19.58200   92.30300  -13.73200 1.000 38.96863  ?  448  PHE   B CG  1 
ATOM   17621 C  CD1 . PHE   B 1 448  ? 18.67000   93.23000  -14.21200 1.000 42.82560  ?  448  PHE   B CD1 1 
ATOM   17622 C  CD2 . PHE   B 1 448  ? 19.38000   90.96200  -14.02400 1.000 32.21524  ?  448  PHE   B CD2 1 
ATOM   17623 C  CE1 . PHE   B 1 448  ? 17.56900   92.82800  -14.95100 1.000 39.05725  ?  448  PHE   B CE1 1 
ATOM   17624 C  CE2 . PHE   B 1 448  ? 18.28300   90.55400  -14.76100 1.000 32.87965  ?  448  PHE   B CE2 1 
ATOM   17625 C  CZ  . PHE   B 1 448  ? 17.37600   91.48800  -15.22600 1.000 45.47380  ?  448  PHE   B CZ  1 
ATOM   17626 N  N   . MET   B 1 449  ? 21.25400   90.94300  -10.16400 1.000 44.23913  ?  449  MET   B N   1 
ATOM   17627 C  CA  . MET   B 1 449  ? 21.06600   89.64600  -9.52500  1.000 49.10768  ?  449  MET   B CA  1 
ATOM   17628 C  C   . MET   B 1 449  ? 20.09900   89.72400  -8.35500  1.000 50.18451  ?  449  MET   B C   1 
ATOM   17629 O  O   . MET   B 1 449  ? 19.53300   88.69800  -7.96200  1.000 55.43349  ?  449  MET   B O   1 
ATOM   17630 C  CB  . MET   B 1 449  ? 22.40700   89.08100  -9.04700  1.000 40.37854  ?  449  MET   B CB  1 
ATOM   17631 C  CG  . MET   B 1 449  ? 23.52700   89.13800  -10.07200 1.000 51.27826  ?  449  MET   B CG  1 
ATOM   17632 S  SD  . MET   B 1 449  ? 25.06800   88.38300  -9.50900  1.000 50.95167  ?  449  MET   B SD  1 
ATOM   17633 C  CE  . MET   B 1 449  ? 26.02000   88.42400  -11.02400 1.000 42.65306  ?  449  MET   B CE  1 
ATOM   17634 N  N   . GLN   B 1 450  ? 19.89800   90.91100  -7.78900  1.000 41.10864  ?  450  GLN   B N   1 
ATOM   17635 C  CA  . GLN   B 1 450  ? 18.96300   91.07000  -6.68700  1.000 54.83117  ?  450  GLN   B CA  1 
ATOM   17636 C  C   . GLN   B 1 450  ? 17.51600   91.17100  -7.15300  1.000 56.12125  ?  450  GLN   B C   1 
ATOM   17637 O  O   . GLN   B 1 450  ? 16.60800   91.01800  -6.33000  1.000 65.06412  ?  450  GLN   B O   1 
ATOM   17638 C  CB  . GLN   B 1 450  ? 19.33100   92.30900  -5.86600  1.000 59.04210  ?  450  GLN   B CB  1 
ATOM   17639 C  CG  . GLN   B 1 450  ? 19.42100   93.58000  -6.69000  1.000 67.75250  ?  450  GLN   B CG  1 
ATOM   17640 C  CD  . GLN   B 1 450  ? 20.05300   94.73500  -5.93500  1.000 85.53855  ?  450  GLN   B CD  1 
ATOM   17641 O  OE1 . GLN   B 1 450  ? 20.81100   94.53200  -4.98600  1.000 75.09212  ?  450  GLN   B OE1 1 
ATOM   17642 N  NE2 . GLN   B 1 450  ? 19.75700   95.95700  -6.36800  1.000 72.51616  ?  450  GLN   B NE2 1 
ATOM   17643 N  N   . MET   B 1 451  ? 17.28000   91.41400  -8.43900  1.000 46.98780  ?  451  MET   B N   1 
ATOM   17644 C  CA  . MET   B 1 451  ? 15.93200   91.55200  -8.96600  1.000 35.50022  ?  451  MET   B CA  1 
ATOM   17645 C  C   . MET   B 1 451  ? 15.35600   90.19000  -9.33700  1.000 41.86772  ?  451  MET   B C   1 
ATOM   17646 O  O   . MET   B 1 451  ? 16.08800   89.23400  -9.60700  1.000 46.53426  ?  451  MET   B O   1 
ATOM   17647 C  CB  . MET   B 1 451  ? 15.92400   92.46800  -10.18900 1.000 27.90282  ?  451  MET   B CB  1 
ATOM   17648 C  CG  . MET   B 1 451  ? 16.75900   93.72200  -10.02100 1.000 35.86854  ?  451  MET   B CG  1 
ATOM   17649 S  SD  . MET   B 1 451  ? 15.83600   95.04900  -9.23000  1.000 54.68434  ?  451  MET   B SD  1 
ATOM   17650 C  CE  . MET   B 1 451  ? 17.16300   96.08000  -8.60800  1.000 73.66604  ?  451  MET   B CE  1 
ATOM   17651 N  N   . ASP   B 1 452  ? 14.02700   90.11500  -9.35600  1.000 58.82782  ?  452  ASP   B N   1 
ATOM   17652 C  CA  . ASP   B 1 452  ? 13.31100   88.86800  -9.62300  1.000 49.39288  ?  452  ASP   B CA  1 
ATOM   17653 C  C   . ASP   B 1 452  ? 13.12400   88.72800  -11.12700 1.000 43.94108  ?  452  ASP   B C   1 
ATOM   17654 O  O   . ASP   B 1 452  ? 12.28900   89.40600  -11.72900 1.000 46.26995  ?  452  ASP   B O   1 
ATOM   17655 C  CB  . ASP   B 1 452  ? 11.97400   88.85400  -8.89300  1.000 46.86100  ?  452  ASP   B CB  1 
ATOM   17656 C  CG  . ASP   B 1 452  ? 11.33500   87.48300  -8.88000  1.000 75.25199  ?  452  ASP   B CG  1 
ATOM   17657 O  OD1 . ASP   B 1 452  ? 12.06400   86.48800  -9.08500  1.000 72.91004  ?  452  ASP   B OD1 1 
ATOM   17658 O  OD2 . ASP   B 1 452  ? 10.10600   87.39700  -8.66900  1.000 79.39289  -1 452  ASP   B OD2 1 
ATOM   17659 N  N   . ASN   B 1 453  ? 13.90100   87.83900  -11.74100 1.000 36.45988  ?  453  ASN   B N   1 
ATOM   17660 C  CA  . ASN   B 1 453  ? 13.87600   87.63000  -13.18100 1.000 33.82886  ?  453  ASN   B CA  1 
ATOM   17661 C  C   . ASN   B 1 453  ? 13.48800   86.19000  -13.47000 1.000 37.45519  ?  453  ASN   B C   1 
ATOM   17662 O  O   . ASN   B 1 453  ? 14.00200   85.26500  -12.83300 1.000 48.81197  ?  453  ASN   B O   1 
ATOM   17663 C  CB  . ASN   B 1 453  ? 15.23500   87.95300  -13.81200 1.000 36.02871  ?  453  ASN   B CB  1 
ATOM   17664 C  CG  . ASN   B 1 453  ? 15.31600   87.54500  -15.27400 1.000 39.68824  ?  453  ASN   B CG  1 
ATOM   17665 O  OD1 . ASN   B 1 453  ? 15.67700   86.41000  -15.59400 1.000 35.71882  ?  453  ASN   B OD1 1 
ATOM   17666 N  ND2 . ASN   B 1 453  ? 14.98600   88.47100  -16.16800 1.000 37.40745  ?  453  ASN   B ND2 1 
ATOM   17667 N  N   . GLN   B 1 454  ? 12.57900   86.00400  -14.42900 1.000 42.34953  ?  454  GLN   B N   1 
ATOM   17668 C  CA  . GLN   B 1 454  ? 12.16300   84.67300  -14.85400 1.000 48.79505  ?  454  GLN   B CA  1 
ATOM   17669 C  C   . GLN   B 1 454  ? 12.24500   84.51300  -16.36800 1.000 42.78905  ?  454  GLN   B C   1 
ATOM   17670 O  O   . GLN   B 1 454  ? 11.57600   83.64100  -16.93000 1.000 80.79340  ?  454  GLN   B O   1 
ATOM   17671 C  CB  . GLN   B 1 454  ? 10.74300   84.36700  -14.37100 1.000 51.42725  ?  454  GLN   B CB  1 
ATOM   17672 C  CG  . GLN   B 1 454  ? 10.60900   84.27000  -12.86400 1.000 56.90632  ?  454  GLN   B CG  1 
ATOM   17673 C  CD  . GLN   B 1 454  ? 10.02200   85.52600  -12.25400 1.000 61.07769  ?  454  GLN   B CD  1 
ATOM   17674 O  OE1 . GLN   B 1 454  ? 9.56600    86.42300  -12.96500 1.000 51.44218  ?  454  GLN   B OE1 1 
ATOM   17675 N  NE2 . GLN   B 1 454  ? 10.02900   85.59700  -10.92900 1.000 72.03081  ?  454  GLN   B NE2 1 
ATOM   17676 N  N   . SER   B 1 455  ? 13.04700   85.33300  -17.03500 1.000 29.45014  ?  455  SER   B N   1 
ATOM   17677 C  CA  . SER   B 1 455  ? 13.14300   85.32100  -18.48600 1.000 37.88443  ?  455  SER   B CA  1 
ATOM   17678 C  C   . SER   B 1 455  ? 14.52500   84.97600  -19.00900 1.000 47.03417  ?  455  SER   B C   1 
ATOM   17679 O  O   . SER   B 1 455  ? 14.62800   84.33900  -20.06000 1.000 46.07169  ?  455  SER   B O   1 
ATOM   17680 C  CB  . SER   B 1 455  ? 12.74800   86.68700  -19.05700 1.000 46.41048  ?  455  SER   B CB  1 
ATOM   17681 O  OG  . SER   B 1 455  ? 13.77400   87.62900  -18.80300 1.000 34.09623  ?  455  SER   B OG  1 
ATOM   17682 N  N   . PHE   B 1 456  ? 15.58400   85.38700  -18.31900 1.000 44.04662  ?  456  PHE   B N   1 
ATOM   17683 C  CA  . PHE   B 1 456  ? 16.93300   85.12500  -18.79600 1.000 33.69006  ?  456  PHE   B CA  1 
ATOM   17684 C  C   . PHE   B 1 456  ? 17.28600   83.65100  -18.64200 1.000 36.21129  ?  456  PHE   B C   1 
ATOM   17685 O  O   . PHE   B 1 456  ? 16.98800   83.02500  -17.62100 1.000 40.19218  ?  456  PHE   B O   1 
ATOM   17686 C  CB  . PHE   B 1 456  ? 17.94000   85.98400  -18.03100 1.000 28.33846  ?  456  PHE   B CB  1 
ATOM   17687 C  CG  . PHE   B 1 456  ? 18.17500   87.33100  -18.64600 1.000 24.18369  ?  456  PHE   B CG  1 
ATOM   17688 C  CD1 . PHE   B 1 456  ? 18.86200   87.44800  -19.84300 1.000 34.63403  ?  456  PHE   B CD1 1 
ATOM   17689 C  CD2 . PHE   B 1 456  ? 17.70100   88.48200  -18.03300 1.000 28.82099  ?  456  PHE   B CD2 1 
ATOM   17690 C  CE1 . PHE   B 1 456  ? 19.07600   88.68900  -20.41600 1.000 40.14129  ?  456  PHE   B CE1 1 
ATOM   17691 C  CE2 . PHE   B 1 456  ? 17.91000   89.72700  -18.60100 1.000 21.90837  ?  456  PHE   B CE2 1 
ATOM   17692 C  CZ  . PHE   B 1 456  ? 18.59900   89.83000  -19.79400 1.000 24.91622  ?  456  PHE   B CZ  1 
ATOM   17693 N  N   . ARG   B 1 457  ? 17.91600   83.09300  -19.67700 1.000 37.79585  ?  457  ARG   B N   1 
ATOM   17694 C  CA  . ARG   B 1 457  ? 18.53900   81.78100  -19.58700 1.000 33.76334  ?  457  ARG   B CA  1 
ATOM   17695 C  C   . ARG   B 1 457  ? 20.05500   81.86100  -19.45400 1.000 41.97870  ?  457  ARG   B C   1 
ATOM   17696 O  O   . ARG   B 1 457  ? 20.66400   80.93500  -18.90600 1.000 37.47792  ?  457  ARG   B O   1 
ATOM   17697 C  CB  . ARG   B 1 457  ? 18.17300   80.92800  -20.81500 1.000 26.33791  ?  457  ARG   B CB  1 
ATOM   17698 C  CG  . ARG   B 1 457  ? 19.08700   81.12100  -22.02000 1.000 42.95283  ?  457  ARG   B CG  1 
ATOM   17699 C  CD  . ARG   B 1 457  ? 18.63400   80.30800  -23.22900 1.000 22.07587  ?  457  ARG   B CD  1 
ATOM   17700 N  NE  . ARG   B 1 457  ? 19.21200   80.82500  -24.46400 1.000 32.03202  ?  457  ARG   B NE  1 
ATOM   17701 C  CZ  . ARG   B 1 457  ? 20.34400   80.38600  -25.00000 1.000 29.43361  ?  457  ARG   B CZ  1 
ATOM   17702 N  NH1 . ARG   B 1 457  ? 21.03900   79.41000  -24.44200 1.000 33.40863  ?  457  ARG   B NH1 1 
ATOM   17703 N  NH2 . ARG   B 1 457  ? 20.79100   80.94400  -26.12100 1.000 28.38149  ?  457  ARG   B NH2 1 
ATOM   17704 N  N   . VAL   B 1 458  ? 20.66500   82.95000  -19.92200 1.000 42.16380  ?  458  VAL   B N   1 
ATOM   17705 C  CA  . VAL   B 1 458  ? 22.11200   83.14500  -19.88400 1.000 37.42205  ?  458  VAL   B CA  1 
ATOM   17706 C  C   . VAL   B 1 458  ? 22.38400   84.62600  -19.66500 1.000 30.43003  ?  458  VAL   B C   1 
ATOM   17707 O  O   . VAL   B 1 458  ? 21.84800   85.47600  -20.38300 1.000 29.08284  ?  458  VAL   B O   1 
ATOM   17708 C  CB  . VAL   B 1 458  ? 22.79300   82.65500  -21.17900 1.000 26.97075  ?  458  VAL   B CB  1 
ATOM   17709 C  CG1 . VAL   B 1 458  ? 24.14900   83.33300  -21.37300 1.000 30.24355  ?  458  VAL   B CG1 1 
ATOM   17710 C  CG2 . VAL   B 1 458  ? 22.95100   81.14600  -21.16200 1.000 30.44891  ?  458  VAL   B CG2 1 
ATOM   17711 N  N   . VAL   B 1 459  ? 23.20700   84.94000  -18.66700 1.000 29.30585  ?  459  VAL   B N   1 
ATOM   17712 C  CA  . VAL   B 1 459  ? 23.66300   86.30300  -18.42400 1.000 32.31073  ?  459  VAL   B CA  1 
ATOM   17713 C  C   . VAL   B 1 459  ? 25.18400   86.29300  -18.43500 1.000 39.03801  ?  459  VAL   B C   1 
ATOM   17714 O  O   . VAL   B 1 459  ? 25.81100   85.53200  -17.68600 1.000 46.98977  ?  459  VAL   B O   1 
ATOM   17715 C  CB  . VAL   B 1 459  ? 23.12900   86.86700  -17.09900 1.000 30.75035  ?  459  VAL   B CB  1 
ATOM   17716 C  CG1 . VAL   B 1 459  ? 23.89000   88.12300  -16.73000 1.000 35.49754  ?  459  VAL   B CG1 1 
ATOM   17717 C  CG2 . VAL   B 1 459  ? 21.65100   87.17200  -17.21100 1.000 32.08865  ?  459  VAL   B CG2 1 
ATOM   17718 N  N   . ILE   B 1 460  ? 25.77500   87.12700  -19.28400 1.000 38.13953  ?  460  ILE   B N   1 
ATOM   17719 C  CA  . ILE   B 1 460  ? 27.22300   87.23300  -19.41300 1.000 34.61490  ?  460  ILE   B CA  1 
ATOM   17720 C  C   . ILE   B 1 460  ? 27.66800   88.54300  -18.78400 1.000 35.55418  ?  460  ILE   B C   1 
ATOM   17721 O  O   . ILE   B 1 460  ? 27.03200   89.58500  -18.98100 1.000 34.90789  ?  460  ILE   B O   1 
ATOM   17722 C  CB  . ILE   B 1 460  ? 27.66800   87.15300  -20.88600 1.000 37.40820  ?  460  ILE   B CB  1 
ATOM   17723 C  CG1 . ILE   B 1 460  ? 27.25100   85.81400  -21.49300 1.000 39.20991  ?  460  ILE   B CG1 1 
ATOM   17724 C  CG2 . ILE   B 1 460  ? 29.17000   87.34200  -20.99700 1.000 31.00231  ?  460  ILE   B CG2 1 
ATOM   17725 C  CD1 . ILE   B 1 460  ? 26.77000   85.92000  -22.91500 1.000 32.23580  ?  460  ILE   B CD1 1 
ATOM   17726 N  N   . THR   B 1 461  ? 28.76200   88.49100  -18.02700 1.000 42.73680  ?  461  THR   B N   1 
ATOM   17727 C  CA  . THR   B 1 461  ? 29.28900   89.67000  -17.35800 1.000 38.51948  ?  461  THR   B CA  1 
ATOM   17728 C  C   . THR   B 1 461  ? 30.80600   89.70400  -17.50200 1.000 36.03094  ?  461  THR   B C   1 
ATOM   17729 O  O   . THR   B 1 461  ? 31.43000   88.75600  -17.98600 1.000 33.07281  ?  461  THR   B O   1 
ATOM   17730 C  CB  . THR   B 1 461  ? 28.87400   89.70000  -15.88300 1.000 34.91083  ?  461  THR   B CB  1 
ATOM   17731 O  OG1 . THR   B 1 461  ? 29.10100   91.01000  -15.34800 1.000 37.39471  ?  461  THR   B OG1 1 
ATOM   17732 C  CG2 . THR   B 1 461  ? 29.66600   88.67800  -15.08600 1.000 35.85756  ?  461  THR   B CG2 1 
ATOM   17733 N  N   . GLY   B 1 462  ? 31.39400   90.81100  -17.08300 1.000 37.05114  ?  462  GLY   B N   1 
ATOM   17734 C  CA  . GLY   B 1 462  ? 32.82400   91.02000  -17.22100 1.000 35.61325  ?  462  GLY   B CA  1 
ATOM   17735 C  C   . GLY   B 1 462  ? 33.14400   92.49500  -17.33400 1.000 39.34421  ?  462  GLY   B C   1 
ATOM   17736 O  O   . GLY   B 1 462  ? 32.27300   93.33700  -17.53700 1.000 38.07172  ?  462  GLY   B O   1 
ATOM   17737 N  N   . GLY   B 1 463  ? 34.43200   92.80000  -17.19800 1.000 46.93915  ?  463  GLY   B N   1 
ATOM   17738 C  CA  . GLY   B 1 463  ? 34.88100   94.17800  -17.24100 1.000 32.05042  ?  463  GLY   B CA  1 
ATOM   17739 C  C   . GLY   B 1 463  ? 35.54500   94.59200  -15.94700 1.000 36.61614  ?  463  GLY   B C   1 
ATOM   17740 O  O   . GLY   B 1 463  ? 36.64200   95.15900  -15.95000 1.000 65.11985  ?  463  GLY   B O   1 
ATOM   17741 N  N   . ASP   B 1 464  ? 34.88200   94.31200  -14.83200 1.000 34.46185  ?  464  ASP   B N   1 
ATOM   17742 C  CA  . ASP   B 1 464  ? 35.43400   94.51300  -13.50500 1.000 45.41180  ?  464  ASP   B CA  1 
ATOM   17743 C  C   . ASP   B 1 464  ? 35.59600   93.15600  -12.82200 1.000 48.36642  ?  464  ASP   B C   1 
ATOM   17744 O  O   . ASP   B 1 464  ? 35.45900   92.09800  -13.45000 1.000 51.43535  ?  464  ASP   B O   1 
ATOM   17745 C  CB  . ASP   B 1 464  ? 34.54800   95.46600  -12.69700 1.000 35.29865  ?  464  ASP   B CB  1 
ATOM   17746 C  CG  . ASP   B 1 464  ? 35.17500   96.83900  -12.52200 1.000 61.63908  ?  464  ASP   B CG  1 
ATOM   17747 O  OD1 . ASP   B 1 464  ? 36.36400   96.99900  -12.86700 1.000 91.50176  ?  464  ASP   B OD1 1 
ATOM   17748 O  OD2 . ASP   B 1 464  ? 34.48200   97.75600  -12.03200 1.000 74.16667  -1 464  ASP   B OD2 1 
ATOM   17749 N  N   . VAL   B 1 465  ? 35.89600   93.18400  -11.52900 1.000 45.95826  ?  465  VAL   B N   1 
ATOM   17750 C  CA  . VAL   B 1 465  ? 36.09600   91.96500  -10.75600 1.000 45.60960  ?  465  VAL   B CA  1 
ATOM   17751 C  C   . VAL   B 1 465  ? 34.74500   91.50100  -10.22700 1.000 41.57219  ?  465  VAL   B C   1 
ATOM   17752 O  O   . VAL   B 1 465  ? 34.08400   92.21700  -9.46600  1.000 42.84750  ?  465  VAL   B O   1 
ATOM   17753 C  CB  . VAL   B 1 465  ? 37.09800   92.18700  -9.61400  1.000 35.55455  ?  465  VAL   B CB  1 
ATOM   17754 C  CG1 . VAL   B 1 465  ? 37.05400   91.02900  -8.62800  1.000 34.90070  ?  465  VAL   B CG1 1 
ATOM   17755 C  CG2 . VAL   B 1 465  ? 38.49200   92.34700  -10.18200 1.000 30.88397  ?  465  VAL   B CG2 1 
ATOM   17756 N  N   . LEU   B 1 466  ? 34.33200   90.30700  -10.64000 1.000 41.31637  ?  466  LEU   B N   1 
ATOM   17757 C  CA  . LEU   B 1 466  ? 33.06500   89.74200  -10.20100 1.000 46.07144  ?  466  LEU   B CA  1 
ATOM   17758 C  C   . LEU   B 1 466  ? 33.21700   89.11800  -8.81900  1.000 47.86618  ?  466  LEU   B C   1 
ATOM   17759 O  O   . LEU   B 1 466  ? 34.18100   88.39100  -8.55800  1.000 57.93378  ?  466  LEU   B O   1 
ATOM   17760 C  CB  . LEU   B 1 466  ? 32.57800   88.69900  -11.20700 1.000 46.65554  ?  466  LEU   B CB  1 
ATOM   17761 C  CG  . LEU   B 1 466  ? 31.28300   87.98000  -10.83900 1.000 38.06246  ?  466  LEU   B CG  1 
ATOM   17762 C  CD1 . LEU   B 1 466  ? 30.17000   88.99000  -10.62800 1.000 42.57202  ?  466  LEU   B CD1 1 
ATOM   17763 C  CD2 . LEU   B 1 466  ? 30.90600   86.96800  -11.90800 1.000 32.88630  ?  466  LEU   B CD2 1 
ATOM   17764 N  N   . LYS   B 1 467  ? 32.27100   89.40400  -7.93700  1.000 48.28220  ?  467  LYS   B N   1 
ATOM   17765 C  CA  . LYS   B 1 467  ? 32.26500   88.85100  -6.58700  1.000 44.45427  ?  467  LYS   B CA  1 
ATOM   17766 C  C   . LYS   B 1 467  ? 30.95300   88.16900  -6.23300  1.000 48.12624  ?  467  LYS   B C   1 
ATOM   17767 O  O   . LYS   B 1 467  ? 30.96900   87.09300  -5.63200  1.000 56.96955  ?  467  LYS   B O   1 
ATOM   17768 C  CB  . LYS   B 1 467  ? 32.55600   89.95400  -5.55800  1.000 39.78700  ?  467  LYS   B CB  1 
ATOM   17769 C  CG  . LYS   B 1 467  ? 33.85900   90.69600  -5.77500  1.000 39.48418  ?  467  LYS   B CG  1 
ATOM   17770 C  CD  . LYS   B 1 467  ? 33.82400   92.04300  -5.07600  1.000 53.18008  ?  467  LYS   B CD  1 
ATOM   17771 C  CE  . LYS   B 1 467  ? 32.89700   93.02000  -5.78500  1.000 62.13681  ?  467  LYS   B CE  1 
ATOM   17772 N  NZ  . LYS   B 1 467  ? 33.42400   93.41000  -7.12300  1.000 72.71611  ?  467  LYS   B NZ  1 
ATOM   17773 N  N   . LYS   B 1 468  ? 29.82100   88.76800  -6.59100  1.000 45.68151  ?  468  LYS   B N   1 
ATOM   17774 C  CA  . LYS   B 1 468  ? 28.51100   88.24200  -6.23400  1.000 53.39111  ?  468  LYS   B CA  1 
ATOM   17775 C  C   . LYS   B 1 468  ? 28.06500   87.20200  -7.25400  1.000 53.28733  ?  468  LYS   B C   1 
ATOM   17776 O  O   . LYS   B 1 468  ? 28.11100   87.44900  -8.46300  1.000 54.61463  ?  468  LYS   B O   1 
ATOM   17777 C  CB  . LYS   B 1 468  ? 27.49000   89.37700  -6.15400  1.000 43.56469  ?  468  LYS   B CB  1 
ATOM   17778 C  CG  . LYS   B 1 468  ? 26.08900   88.94400  -5.76200  1.000 54.71792  ?  468  LYS   B CG  1 
ATOM   17779 C  CD  . LYS   B 1 468  ? 25.13600   90.12800  -5.74900  1.000 49.61986  ?  468  LYS   B CD  1 
ATOM   17780 C  CE  . LYS   B 1 468  ? 23.85600   89.79500  -5.00100  1.000 70.92346  ?  468  LYS   B CE  1 
ATOM   17781 N  NZ  . LYS   B 1 468  ? 23.75300   90.56200  -3.72600  1.000 83.47760  ?  468  LYS   B NZ  1 
ATOM   17782 N  N   . ILE   B 1 469  ? 27.63700   86.04100  -6.76400  1.000 50.65960  ?  469  ILE   B N   1 
ATOM   17783 C  CA  . ILE   B 1 469  ? 27.05100   85.01200  -7.61700  1.000 51.04111  ?  469  ILE   B CA  1 
ATOM   17784 C  C   . ILE   B 1 469  ? 25.62500   84.66300  -7.22300  1.000 57.97187  ?  469  ILE   B C   1 
ATOM   17785 O  O   . ILE   B 1 469  ? 24.92400   84.01200  -8.01500  1.000 54.95095  ?  469  ILE   B O   1 
ATOM   17786 C  CB  . ILE   B 1 469  ? 27.91700   83.73500  -7.64600  1.000 42.97954  ?  469  ILE   B CB  1 
ATOM   17787 C  CG1 . ILE   B 1 469  ? 27.63900   82.87000  -6.41800  1.000 43.37707  ?  469  ILE   B CG1 1 
ATOM   17788 C  CG2 . ILE   B 1 469  ? 29.39300   84.08400  -7.72700  1.000 50.50706  ?  469  ILE   B CG2 1 
ATOM   17789 C  CD1 . ILE   B 1 469  ? 28.22200   81.48100  -6.52000  1.000 50.21570  ?  469  ILE   B CD1 1 
ATOM   17790 N  N   . GLU   B 1 470  ? 25.16500   85.07100  -6.04200  1.000 63.82793  ?  470  GLU   B N   1 
ATOM   17791 C  CA  . GLU   B 1 470  ? 23.79800   84.79300  -5.62000  1.000 60.23949  ?  470  GLU   B CA  1 
ATOM   17792 C  C   . GLU   B 1 470  ? 22.82600   85.65900  -6.41200  1.000 64.91531  ?  470  GLU   B C   1 
ATOM   17793 O  O   . GLU   B 1 470  ? 22.90600   86.89200  -6.37100  1.000 68.28419  ?  470  GLU   B O   1 
ATOM   17794 C  CB  . GLU   B 1 470  ? 23.64600   85.04800  -4.12300  1.000 73.07018  ?  470  GLU   B CB  1 
ATOM   17795 C  CG  . GLU   B 1 470  ? 23.29200   83.81200  -3.31500  1.000 85.38703  ?  470  GLU   B CG  1 
ATOM   17796 C  CD  . GLU   B 1 470  ? 23.26300   84.08200  -1.82500  1.000 105.14763 ?  470  GLU   B CD  1 
ATOM   17797 O  OE1 . GLU   B 1 470  ? 22.24600   84.62000  -1.33700  1.000 87.54440  ?  470  GLU   B OE1 1 
ATOM   17798 O  OE2 . GLU   B 1 470  ? 24.25900   83.76000  -1.14300  1.000 101.85398 -1 470  GLU   B OE2 1 
ATOM   17799 N  N   . ARG   B 1 471  ? 21.90200   85.01600  -7.12300  1.000 54.18090  ?  471  ARG   B N   1 
ATOM   17800 C  CA  . ARG   B 1 471  ? 20.98600   85.71200  -8.01200  1.000 43.99768  ?  471  ARG   B CA  1 
ATOM   17801 C  C   . ARG   B 1 471  ? 19.58200   85.14100  -7.86700  1.000 56.80326  ?  471  ARG   B C   1 
ATOM   17802 O  O   . ARG   B 1 471  ? 19.40000   83.96700  -7.53000  1.000 46.46247  ?  471  ARG   B O   1 
ATOM   17803 C  CB  . ARG   B 1 471  ? 21.45100   85.61100  -9.47200  1.000 43.26399  ?  471  ARG   B CB  1 
ATOM   17804 C  CG  . ARG   B 1 471  ? 21.75800   84.19200  -9.92500  1.000 43.29791  ?  471  ARG   B CG  1 
ATOM   17805 C  CD  . ARG   B 1 471  ? 22.99400   84.15300  -10.80800 1.000 38.35874  ?  471  ARG   B CD  1 
ATOM   17806 N  NE  . ARG   B 1 471  ? 23.09400   82.90300  -11.55200 1.000 40.38993  ?  471  ARG   B NE  1 
ATOM   17807 C  CZ  . ARG   B 1 471  ? 23.93700   81.92300  -11.26200 1.000 40.34488  ?  471  ARG   B CZ  1 
ATOM   17808 N  NH1 . ARG   B 1 471  ? 24.77700   82.01200  -10.24300 1.000 44.39182  ?  471  ARG   B NH1 1 
ATOM   17809 N  NH2 . ARG   B 1 471  ? 23.94000   80.82600  -12.01500 1.000 46.70251  ?  471  ARG   B NH2 1 
ATOM   17810 N  N   . ASN   B 1 472  ? 18.58800   85.99200  -8.12900  1.000 48.72222  ?  472  ASN   B N   1 
ATOM   17811 C  CA  . ASN   B 1 472  ? 17.18200   85.59700  -8.09700  1.000 43.79566  ?  472  ASN   B CA  1 
ATOM   17812 C  C   . ASN   B 1 472  ? 16.73700   85.29200  -9.52500  1.000 53.32861  ?  472  ASN   B C   1 
ATOM   17813 O  O   . ASN   B 1 472  ? 16.02900   86.06600  -10.17000 1.000 59.51427  ?  472  ASN   B O   1 
ATOM   17814 C  CB  . ASN   B 1 472  ? 16.33100   86.68900  -7.45800  1.000 45.09006  ?  472  ASN   B CB  1 
ATOM   17815 C  CG  . ASN   B 1 472  ? 16.37900   86.65100  -5.94700  1.000 60.92579  ?  472  ASN   B CG  1 
ATOM   17816 O  OD1 . ASN   B 1 472  ? 16.02300   85.64800  -5.32900  1.000 75.43708  ?  472  ASN   B OD1 1 
ATOM   17817 N  ND2 . ASN   B 1 472  ? 16.82500   87.74600  -5.34100  1.000 66.72210  ?  472  ASN   B ND2 1 
ATOM   17818 N  N   . GLY   B 1 473  ? 17.16500   84.13900  -10.02000 1.000 39.41610  ?  473  GLY   B N   1 
ATOM   17819 C  CA  . GLY   B 1 473  ? 16.79500   83.72000  -11.35800 1.000 33.64065  ?  473  GLY   B CA  1 
ATOM   17820 C  C   . GLY   B 1 473  ? 17.32900   82.33300  -11.64100 1.000 46.49238  ?  473  GLY   B C   1 
ATOM   17821 O  O   . GLY   B 1 473  ? 18.20800   81.82300  -10.93900 1.000 60.04751  ?  473  GLY   B O   1 
ATOM   17822 N  N   . THR   B 1 474  ? 16.77500   81.72800  -12.69000 1.000 43.19851  ?  474  THR   B N   1 
ATOM   17823 C  CA  . THR   B 1 474  ? 17.19000   80.40500  -13.13400 1.000 55.25734  ?  474  THR   B CA  1 
ATOM   17824 C  C   . THR   B 1 474  ? 18.18400   80.46300  -14.28600 1.000 58.47059  ?  474  THR   B C   1 
ATOM   17825 O  O   . THR   B 1 474  ? 18.30700   79.48900  -15.03600 1.000 59.22194  ?  474  THR   B O   1 
ATOM   17826 C  CB  . THR   B 1 474  ? 15.97500   79.57700  -13.54700 1.000 51.78297  ?  474  THR   B CB  1 
ATOM   17827 O  OG1 . THR   B 1 474  ? 15.08000   80.39900  -14.30700 1.000 51.75616  ?  474  THR   B OG1 1 
ATOM   17828 C  CG2 . THR   B 1 474  ? 15.25900   79.03800  -12.32000 1.000 40.79560  ?  474  THR   B CG2 1 
ATOM   17829 N  N   . TYR   B 1 475  ? 18.89100   81.57700  -14.44500 1.000 40.28097  ?  475  TYR   B N   1 
ATOM   17830 C  CA  . TYR   B 1 475  ? 19.79000   81.76000  -15.57300 1.000 37.58288  ?  475  TYR   B CA  1 
ATOM   17831 C  C   . TYR   B 1 475  ? 21.22300   81.40800  -15.19800 1.000 42.08749  ?  475  TYR   B C   1 
ATOM   17832 O  O   . TYR   B 1 475  ? 21.64100   81.55900  -14.04700 1.000 53.21038  ?  475  TYR   B O   1 
ATOM   17833 C  CB  . TYR   B 1 475  ? 19.73200   83.19800  -16.09500 1.000 38.47443  ?  475  TYR   B CB  1 
ATOM   17834 C  CG  . TYR   B 1 475  ? 20.00000   84.28200  -15.06800 1.000 32.06878  ?  475  TYR   B CG  1 
ATOM   17835 C  CD1 . TYR   B 1 475  ? 21.29900   84.64800  -14.72900 1.000 50.31466  ?  475  TYR   B CD1 1 
ATOM   17836 C  CD2 . TYR   B 1 475  ? 18.95400   84.96600  -14.46800 1.000 32.04143  ?  475  TYR   B CD2 1 
ATOM   17837 C  CE1 . TYR   B 1 475  ? 21.54400   85.65200  -13.80500 1.000 41.12576  ?  475  TYR   B CE1 1 
ATOM   17838 C  CE2 . TYR   B 1 475  ? 19.18800   85.97000  -13.54500 1.000 37.28223  ?  475  TYR   B CE2 1 
ATOM   17839 C  CZ  . TYR   B 1 475  ? 20.48300   86.30900  -13.21700 1.000 47.23229  ?  475  TYR   B CZ  1 
ATOM   17840 O  OH  . TYR   B 1 475  ? 20.71100   87.30800  -12.29700 1.000 43.47969  ?  475  TYR   B OH  1 
ATOM   17841 N  N   . LYS   B 1 476  ? 21.97600   80.94100  -16.19000 1.000 31.43598  ?  476  LYS   B N   1 
ATOM   17842 C  CA  . LYS   B 1 476  ? 23.39600   80.68800  -15.99000 1.000 37.20694  ?  476  LYS   B CA  1 
ATOM   17843 C  C   . LYS   B 1 476  ? 24.16200   82.00300  -15.94300 1.000 41.18309  ?  476  LYS   B C   1 
ATOM   17844 O  O   . LYS   B 1 476  ? 23.82400   82.96500  -16.64000 1.000 39.98001  ?  476  LYS   B O   1 
ATOM   17845 C  CB  . LYS   B 1 476  ? 23.94600   79.80600  -17.11000 1.000 36.42715  ?  476  LYS   B CB  1 
ATOM   17846 C  CG  . LYS   B 1 476  ? 23.36300   78.40500  -17.15500 1.000 32.57258  ?  476  LYS   B CG  1 
ATOM   17847 C  CD  . LYS   B 1 476  ? 23.65700   77.74400  -18.49100 1.000 21.86334  ?  476  LYS   B CD  1 
ATOM   17848 C  CE  . LYS   B 1 476  ? 23.72300   76.23400  -18.36000 1.000 31.57320  ?  476  LYS   B CE  1 
ATOM   17849 N  NZ  . LYS   B 1 476  ? 23.64500   75.56900  -19.69100 1.000 48.57878  ?  476  LYS   B NZ  1 
ATOM   17850 N  N   . LEU   B 1 477  ? 25.19900   82.04300  -15.11200 1.000 38.53481  ?  477  LEU   B N   1 
ATOM   17851 C  CA  . LEU   B 1 477  ? 26.05300   83.21300  -14.97500 1.000 33.62027  ?  477  LEU   B CA  1 
ATOM   17852 C  C   . LEU   B 1 477  ? 27.40100   82.92200  -15.61500 1.000 40.16500  ?  477  LEU   B C   1 
ATOM   17853 O  O   . LEU   B 1 477  ? 28.01400   81.88500  -15.33900 1.000 42.66622  ?  477  LEU   B O   1 
ATOM   17854 C  CB  . LEU   B 1 477  ? 26.23700   83.59700  -13.50500 1.000 28.76948  ?  477  LEU   B CB  1 
ATOM   17855 C  CG  . LEU   B 1 477  ? 27.00500   84.89500  -13.25900 1.000 39.48360  ?  477  LEU   B CG  1 
ATOM   17856 C  CD1 . LEU   B 1 477  ? 26.25000   86.07400  -13.85800 1.000 28.93972  ?  477  LEU   B CD1 1 
ATOM   17857 C  CD2 . LEU   B 1 477  ? 27.25300   85.10100  -11.77100 1.000 36.67189  ?  477  LEU   B CD2 1 
ATOM   17858 N  N   . TYR   B 1 478  ? 27.85800   83.83200  -16.46900 1.000 36.51938  ?  478  TYR   B N   1 
ATOM   17859 C  CA  . TYR   B 1 478  ? 29.12700   83.67700  -17.16100 1.000 36.13951  ?  478  TYR   B CA  1 
ATOM   17860 C  C   . TYR   B 1 478  ? 29.99400   84.90000  -16.91300 1.000 40.17466  ?  478  TYR   B C   1 
ATOM   17861 O  O   . TYR   B 1 478  ? 29.49000   86.02500  -16.84900 1.000 42.65035  ?  478  TYR   B O   1 
ATOM   17862 C  CB  . TYR   B 1 478  ? 28.92300   83.48500  -18.66200 1.000 32.26835  ?  478  TYR   B CB  1 
ATOM   17863 C  CG  . TYR   B 1 478  ? 28.47000   82.10200  -19.05800 1.000 35.02413  ?  478  TYR   B CG  1 
ATOM   17864 C  CD1 . TYR   B 1 478  ? 27.12900   81.75000  -19.01200 1.000 34.18352  ?  478  TYR   B CD1 1 
ATOM   17865 C  CD2 . TYR   B 1 478  ? 29.38100   81.15300  -19.49700 1.000 39.27964  ?  478  TYR   B CD2 1 
ATOM   17866 C  CE1 . TYR   B 1 478  ? 26.71100   80.49100  -19.38300 1.000 29.21781  ?  478  TYR   B CE1 1 
ATOM   17867 C  CE2 . TYR   B 1 478  ? 28.97200   79.89300  -19.87200 1.000 36.87143  ?  478  TYR   B CE2 1 
ATOM   17868 C  CZ  . TYR   B 1 478  ? 27.63500   79.56700  -19.81100 1.000 30.26978  ?  478  TYR   B CZ  1 
ATOM   17869 O  OH  . TYR   B 1 478  ? 27.22000   78.30900  -20.18100 1.000 38.60961  ?  478  TYR   B OH  1 
ATOM   17870 N  N   . ASN   B 1 479  ? 31.29900   84.67100  -16.77500 1.000 32.17393  ?  479  ASN   B N   1 
ATOM   17871 C  CA  . ASN   B 1 479  ? 32.27500   85.73000  -16.55700 1.000 27.11058  ?  479  ASN   B CA  1 
ATOM   17872 C  C   . ASN   B 1 479  ? 33.32500   85.67000  -17.65600 1.000 28.36081  ?  479  ASN   B C   1 
ATOM   17873 O  O   . ASN   B 1 479  ? 33.88900   84.60200  -17.92100 1.000 32.45613  ?  479  ASN   B O   1 
ATOM   17874 C  CB  . ASN   B 1 479  ? 32.93000   85.60000  -15.17800 1.000 23.56135  ?  479  ASN   B CB  1 
ATOM   17875 C  CG  . ASN   B 1 479  ? 33.74500   86.81900  -14.80400 1.000 34.41483  ?  479  ASN   B CG  1 
ATOM   17876 O  OD1 . ASN   B 1 479  ? 33.29400   87.95400  -14.95900 1.000 37.70913  ?  479  ASN   B OD1 1 
ATOM   17877 N  ND2 . ASN   B 1 479  ? 34.95300   86.59100  -14.29800 1.000 46.20385  ?  479  ASN   B ND2 1 
ATOM   17878 N  N   . GLY   B 1 480  ? 33.58300   86.81300  -18.29400 1.000 31.02159  ?  480  GLY   B N   1 
ATOM   17879 C  CA  . GLY   B 1 480  ? 34.51200   86.86800  -19.39900 1.000 30.43696  ?  480  GLY   B CA  1 
ATOM   17880 C  C   . GLY   B 1 480  ? 35.54400   87.96400  -19.20800 1.000 34.66227  ?  480  GLY   B C   1 
ATOM   17881 O  O   . GLY   B 1 480  ? 35.37000   88.89000  -18.41600 1.000 35.29394  ?  480  GLY   B O   1 
ATOM   17882 N  N   . TYR   B 1 481  ? 36.63400   87.83900  -19.96400 1.000 38.75896  ?  481  TYR   B N   1 
ATOM   17883 C  CA  . TYR   B 1 481  ? 37.74000   88.78100  -19.90500 1.000 31.19784  ?  481  TYR   B CA  1 
ATOM   17884 C  C   . TYR   B 1 481  ? 38.23900   89.05500  -21.31600 1.000 30.68737  ?  481  TYR   B C   1 
ATOM   17885 O  O   . TYR   B 1 481  ? 38.22000   88.17400  -22.18100 1.000 29.12337  ?  481  TYR   B O   1 
ATOM   17886 C  CB  . TYR   B 1 481  ? 38.89000   88.24800  -19.02800 1.000 29.53473  ?  481  TYR   B CB  1 
ATOM   17887 C  CG  . TYR   B 1 481  ? 40.21600   88.94000  -19.26200 1.000 34.83964  ?  481  TYR   B CG  1 
ATOM   17888 C  CD1 . TYR   B 1 481  ? 40.52900   90.12300  -18.60300 1.000 27.38299  ?  481  TYR   B CD1 1 
ATOM   17889 C  CD2 . TYR   B 1 481  ? 41.15300   88.41500  -20.14700 1.000 42.01617  ?  481  TYR   B CD2 1 
ATOM   17890 C  CE1 . TYR   B 1 481  ? 41.73800   90.76300  -18.81900 1.000 42.04460  ?  481  TYR   B CE1 1 
ATOM   17891 C  CE2 . TYR   B 1 481  ? 42.36500   89.05100  -20.37100 1.000 28.74624  ?  481  TYR   B CE2 1 
ATOM   17892 C  CZ  . TYR   B 1 481  ? 42.65200   90.22300  -19.70300 1.000 37.07190  ?  481  TYR   B CZ  1 
ATOM   17893 O  OH  . TYR   B 1 481  ? 43.85600   90.85900  -19.91800 1.000 50.37849  ?  481  TYR   B OH  1 
ATOM   17894 N  N   . GLY   B 1 482  ? 38.68900   90.28700  -21.54100 1.000 30.68628  ?  482  GLY   B N   1 
ATOM   17895 C  CA  . GLY   B 1 482  ? 39.29400   90.65400  -22.79900 1.000 38.58211  ?  482  GLY   B CA  1 
ATOM   17896 C  C   . GLY   B 1 482  ? 39.47300   92.15100  -22.94700 1.000 32.36473  ?  482  GLY   B C   1 
ATOM   17897 O  O   . GLY   B 1 482  ? 38.59400   92.94100  -22.59500 1.000 39.56613  ?  482  GLY   B O   1 
ATOM   17898 N  N   . PRO   B 1 483  ? 40.62500   92.56900  -23.45700 1.000 29.23583  ?  483  PRO   B N   1 
ATOM   17899 C  CA  . PRO   B 1 483  ? 40.82000   93.98200  -23.78800 1.000 23.18818  ?  483  PRO   B CA  1 
ATOM   17900 C  C   . PRO   B 1 483  ? 40.17500   94.32600  -25.12200 1.000 29.67695  ?  483  PRO   B C   1 
ATOM   17901 O  O   . PRO   B 1 483  ? 39.97100   93.47100  -25.98500 1.000 38.79700  ?  483  PRO   B O   1 
ATOM   17902 C  CB  . PRO   B 1 483  ? 42.34300   94.11700  -23.87100 1.000 28.35724  ?  483  PRO   B CB  1 
ATOM   17903 C  CG  . PRO   B 1 483  ? 42.79500   92.76000  -24.31400 1.000 26.21612  ?  483  PRO   B CG  1 
ATOM   17904 C  CD  . PRO   B 1 483  ? 41.84900   91.77700  -23.66900 1.000 37.18064  ?  483  PRO   B CD  1 
ATOM   17905 N  N   . THR   B 1 484  ? 39.85600   95.61500  -25.27500 1.000 22.86421  ?  484  THR   B N   1 
ATOM   17906 C  CA  . THR   B 1 484  ? 39.31700   96.10300  -26.54200 1.000 29.00410  ?  484  THR   B CA  1 
ATOM   17907 C  C   . THR   B 1 484  ? 40.26200   95.80500  -27.69900 1.000 35.46132  ?  484  THR   B C   1 
ATOM   17908 O  O   . THR   B 1 484  ? 39.81300   95.56000  -28.82600 1.000 41.34041  ?  484  THR   B O   1 
ATOM   17909 C  CB  . THR   B 1 484  ? 39.05000   97.60800  -26.45900 1.000 30.03116  ?  484  THR   B CB  1 
ATOM   17910 O  OG1 . THR   B 1 484  ? 38.44200   97.92300  -25.20000 1.000 38.44920  ?  484  THR   B OG1 1 
ATOM   17911 C  CG2 . THR   B 1 484  ? 38.12500   98.04800  -27.57900 1.000 17.58353  ?  484  THR   B CG2 1 
ATOM   17912 N  N   . GLU   B 1 485  ? 41.57200   95.80900  -27.43300 1.000 37.32593  ?  485  GLU   B N   1 
ATOM   17913 C  CA  . GLU   B 1 485  ? 42.56800   95.52800  -28.45900 1.000 32.65514  ?  485  GLU   B CA  1 
ATOM   17914 C  C   . GLU   B 1 485  ? 42.44200   94.12000  -29.02600 1.000 34.78123  ?  485  GLU   B C   1 
ATOM   17915 O  O   . GLU   B 1 485  ? 42.90500   93.87100  -30.14600 1.000 29.86421  ?  485  GLU   B O   1 
ATOM   17916 C  CB  . GLU   B 1 485  ? 43.97000   95.73800  -27.88300 1.000 24.49982  ?  485  GLU   B CB  1 
ATOM   17917 C  CG  . GLU   B 1 485  ? 44.31700   97.19400  -27.60100 1.000 30.18697  ?  485  GLU   B CG  1 
ATOM   17918 C  CD  . GLU   B 1 485  ? 43.77200   97.69400  -26.27500 1.000 36.78990  ?  485  GLU   B CD  1 
ATOM   17919 O  OE1 . GLU   B 1 485  ? 42.79700   97.10300  -25.75800 1.000 34.57847  ?  485  GLU   B OE1 1 
ATOM   17920 O  OE2 . GLU   B 1 485  ? 44.32400   98.68400  -25.75100 1.000 29.48797  -1 485  GLU   B OE2 1 
ATOM   17921 N  N   . CYS   B 1 486  ? 41.82500   93.20000  -28.28500 1.000 27.98914  ?  486  CYS   B N   1 
ATOM   17922 C  CA  . CYS   B 1 486  ? 41.64600   91.83300  -28.75900 1.000 37.90107  ?  486  CYS   B CA  1 
ATOM   17923 C  C   . CYS   B 1 486  ? 40.16700   91.48100  -28.86100 1.000 36.48130  ?  486  CYS   B C   1 
ATOM   17924 O  O   . CYS   B 1 486  ? 39.69300   90.54000  -28.21400 1.000 58.31197  ?  486  CYS   B O   1 
ATOM   17925 C  CB  . CYS   B 1 486  ? 42.38000   90.85200  -27.84000 1.000 37.29755  ?  486  CYS   B CB  1 
ATOM   17926 S  SG  . CYS   B 1 486  ? 44.17700   91.12100  -27.73800 1.000 39.47487  ?  486  CYS   B SG  1 
ATOM   17927 N  N   . THR   B 1 487  ? 39.44700   92.22900  -29.68600 1.000 36.47534  ?  487  THR   B N   1 
ATOM   17928 C  CA  . THR   B 1 487  ? 37.98800   92.10600  -29.90200 1.000 39.93964  ?  487  THR   B CA  1 
ATOM   17929 C  C   . THR   B 1 487  ? 37.30300   92.30900  -28.54600 1.000 48.30227  ?  487  THR   B C   1 
ATOM   17930 O  O   . THR   B 1 487  ? 37.75300   93.14600  -27.75100 1.000 78.37437  ?  487  THR   B O   1 
ATOM   17931 C  CB  . THR   B 1 487  ? 37.66900   90.80900  -30.60600 1.000 36.47280  ?  487  THR   B CB  1 
ATOM   17932 O  OG1 . THR   B 1 487  ? 38.71800   90.51100  -31.52700 1.000 65.10191  ?  487  THR   B OG1 1 
ATOM   17933 C  CG2 . THR   B 1 487  ? 36.36100   90.92800  -31.39200 1.000 31.47591  ?  487  THR   B CG2 1 
ATOM   17934 N  N   . ILE   B 1 488  ? 36.22700   91.58500  -28.25400 1.000 27.01398  ?  488  ILE   B N   1 
ATOM   17935 C  CA  . ILE   B 1 488  ? 35.38600   91.86400  -27.09500 1.000 33.79739  ?  488  ILE   B CA  1 
ATOM   17936 C  C   . ILE   B 1 488  ? 35.92000   91.12200  -25.87800 1.000 34.61391  ?  488  ILE   B C   1 
ATOM   17937 O  O   . ILE   B 1 488  ? 36.23500   91.73000  -24.84600 1.000 30.07998  ?  488  ILE   B O   1 
ATOM   17938 C  CB  . ILE   B 1 488  ? 33.92200   91.48300  -27.38700 1.000 32.83043  ?  488  ILE   B CB  1 
ATOM   17939 C  CG1 . ILE   B 1 488  ? 33.38000   92.31900  -28.55100 1.000 23.79090  ?  488  ILE   B CG1 1 
ATOM   17940 C  CG2 . ILE   B 1 488  ? 33.06200   91.64200  -26.14700 1.000 35.10363  ?  488  ILE   B CG2 1 
ATOM   17941 C  CD1 . ILE   B 1 488  ? 33.00600   91.48900  -29.76400 1.000 28.78696  ?  488  ILE   B CD1 1 
ATOM   17942 N  N   . MET   B 1 489  ? 36.02100   89.80100  -25.99000 1.000 36.23289  ?  489  MET   B N   1 
ATOM   17943 C  CA  . MET   B 1 489  ? 36.57300   88.97100  -24.93300 1.000 35.40208  ?  489  MET   B CA  1 
ATOM   17944 C  C   . MET   B 1 489  ? 37.45500   87.89400  -25.54700 1.000 35.89692  ?  489  MET   B C   1 
ATOM   17945 O  O   . MET   B 1 489  ? 37.32000   87.54100  -26.72300 1.000 38.23241  ?  489  MET   B O   1 
ATOM   17946 C  CB  . MET   B 1 489  ? 35.46700   88.33100  -24.08600 1.000 31.92007  ?  489  MET   B CB  1 
ATOM   17947 C  CG  . MET   B 1 489  ? 34.40300   89.30600  -23.61100 1.000 41.39744  ?  489  MET   B CG  1 
ATOM   17948 S  SD  . MET   B 1 489  ? 33.18000   88.54700  -22.53300 1.000 41.80553  ?  489  MET   B SD  1 
ATOM   17949 C  CE  . MET   B 1 489  ? 32.10600   89.94400  -22.21600 1.000 41.15441  ?  489  MET   B CE  1 
ATOM   17950 N  N   . VAL   B 1 490  ? 38.36700   87.37700  -24.73000 1.000 28.27569  ?  490  VAL   B N   1 
ATOM   17951 C  CA  . VAL   B 1 490  ? 39.22200   86.27100  -25.13900 1.000 25.11765  ?  490  VAL   B CA  1 
ATOM   17952 C  C   . VAL   B 1 490  ? 39.03800   85.03200  -24.27800 1.000 29.65499  ?  490  VAL   B C   1 
ATOM   17953 O  O   . VAL   B 1 490  ? 39.47600   83.94400  -24.68800 1.000 30.59323  ?  490  VAL   B O   1 
ATOM   17954 C  CB  . VAL   B 1 490  ? 40.70700   86.68800  -25.15300 1.000 27.10628  ?  490  VAL   B CB  1 
ATOM   17955 C  CG1 . VAL   B 1 490  ? 40.92400   87.85200  -26.11100 1.000 28.75405  ?  490  VAL   B CG1 1 
ATOM   17956 C  CG2 . VAL   B 1 490  ? 41.17400   87.03700  -23.74500 1.000 29.11392  ?  490  VAL   B CG2 1 
ATOM   17957 N  N   . THR   B 1 491  ? 38.41400   85.14200  -23.10700 1.000 30.10102  ?  491  THR   B N   1 
ATOM   17958 C  CA  . THR   B 1 491  ? 38.16200   84.00200  -22.24100 1.000 33.53070  ?  491  THR   B CA  1 
ATOM   17959 C  C   . THR   B 1 491  ? 36.71800   84.03100  -21.76400 1.000 32.85753  ?  491  THR   B C   1 
ATOM   17960 O  O   . THR   B 1 491  ? 36.09600   85.09300  -21.67400 1.000 34.18212  ?  491  THR   B O   1 
ATOM   17961 C  CB  . THR   B 1 491  ? 39.10000   83.98900  -21.02600 1.000 35.56989  ?  491  THR   B CB  1 
ATOM   17962 O  OG1 . THR   B 1 491  ? 39.14600   85.29700  -20.43800 1.000 42.99416  ?  491  THR   B OG1 1 
ATOM   17963 C  CG2 . THR   B 1 491  ? 40.50200   83.57000  -21.44300 1.000 36.83037  ?  491  THR   B CG2 1 
ATOM   17964 N  N   . MET   B 1 492  ? 36.19000   82.84800  -21.45800 1.000 27.91122  ?  492  MET   B N   1 
ATOM   17965 C  CA  . MET   B 1 492  ? 34.84600   82.71800  -20.91600 1.000 34.08226  ?  492  MET   B CA  1 
ATOM   17966 C  C   . MET   B 1 492  ? 34.85700   81.69500  -19.79200 1.000 41.04892  ?  492  MET   B C   1 
ATOM   17967 O  O   . MET   B 1 492  ? 35.59400   80.70600  -19.83800 1.000 37.97292  ?  492  MET   B O   1 
ATOM   17968 C  CB  . MET   B 1 492  ? 33.83300   82.29900  -21.99100 1.000 31.98683  ?  492  MET   B CB  1 
ATOM   17969 C  CG  . MET   B 1 492  ? 32.38300   82.54800  -21.60500 1.000 20.81461  ?  492  MET   B CG  1 
ATOM   17970 S  SD  . MET   B 1 492  ? 32.16600   84.14000  -20.78900 1.000 41.46769  ?  492  MET   B SD  1 
ATOM   17971 C  CE  . MET   B 1 492  ? 31.79200   85.19000  -22.18900 1.000 27.54133  ?  492  MET   B CE  1 
ATOM   17972 N  N   . PHE   B 1 493  ? 34.02700   81.94000  -18.78100 1.000 39.85427  ?  493  PHE   B N   1 
ATOM   17973 C  CA  . PHE   B 1 493  ? 33.91400   81.04300  -17.64000 1.000 37.37630  ?  493  PHE   B CA  1 
ATOM   17974 C  C   . PHE   B 1 493  ? 32.46500   80.97900  -17.18500 1.000 43.17293  ?  493  PHE   B C   1 
ATOM   17975 O  O   . PHE   B 1 493  ? 31.81100   82.01700  -17.04500 1.000 40.59813  ?  493  PHE   B O   1 
ATOM   17976 C  CB  . PHE   B 1 493  ? 34.80600   81.50500  -16.48400 1.000 32.92721  ?  493  PHE   B CB  1 
ATOM   17977 C  CG  . PHE   B 1 493  ? 34.77700   80.59000  -15.29600 1.000 37.47139  ?  493  PHE   B CG  1 
ATOM   17978 C  CD1 . PHE   B 1 493  ? 35.32000   79.31600  -15.37000 1.000 38.16905  ?  493  PHE   B CD1 1 
ATOM   17979 C  CD2 . PHE   B 1 493  ? 34.19900   80.99800  -14.10700 1.000 40.93851  ?  493  PHE   B CD2 1 
ATOM   17980 C  CE1 . PHE   B 1 493  ? 35.29200   78.46900  -14.27700 1.000 34.31510  ?  493  PHE   B CE1 1 
ATOM   17981 C  CE2 . PHE   B 1 493  ? 34.16400   80.15500  -13.01100 1.000 45.94088  ?  493  PHE   B CE2 1 
ATOM   17982 C  CZ  . PHE   B 1 493  ? 34.71300   78.88900  -13.09500 1.000 40.13869  ?  493  PHE   B CZ  1 
ATOM   17983 N  N   . GLU   B 1 494  ? 31.96900   79.76600  -16.95100 1.000 36.49848  ?  494  GLU   B N   1 
ATOM   17984 C  CA  . GLU   B 1 494  ? 30.64400   79.56800  -16.37900 1.000 41.74687  ?  494  GLU   B CA  1 
ATOM   17985 C  C   . GLU   B 1 494  ? 30.76900   79.47400  -14.86300 1.000 38.20017  ?  494  GLU   B C   1 
ATOM   17986 O  O   . GLU   B 1 494  ? 31.41100   78.55400  -14.34500 1.000 38.64292  ?  494  GLU   B O   1 
ATOM   17987 C  CB  . GLU   B 1 494  ? 29.98500   78.30900  -16.94200 1.000 44.27020  ?  494  GLU   B CB  1 
ATOM   17988 C  CG  . GLU   B 1 494  ? 28.59200   78.04100  -16.38900 1.000 48.25114  ?  494  GLU   B CG  1 
ATOM   17989 C  CD  . GLU   B 1 494  ? 27.89400   76.89500  -17.09600 1.000 50.78136  ?  494  GLU   B CD  1 
ATOM   17990 O  OE1 . GLU   B 1 494  ? 28.51500   76.28300  -17.99100 1.000 56.54272  ?  494  GLU   B OE1 1 
ATOM   17991 O  OE2 . GLU   B 1 494  ? 26.72400   76.61000  -16.76200 1.000 55.47182  -1 494  GLU   B OE2 1 
ATOM   17992 N  N   . VAL   B 1 495  ? 30.16300   80.42600  -14.15600 1.000 39.19485  ?  495  VAL   B N   1 
ATOM   17993 C  CA  . VAL   B 1 495  ? 30.21100   80.44000  -12.69700 1.000 34.52491  ?  495  VAL   B CA  1 
ATOM   17994 C  C   . VAL   B 1 495  ? 29.32300   79.31300  -12.18000 1.000 31.07106  ?  495  VAL   B C   1 
ATOM   17995 O  O   . VAL   B 1 495  ? 28.09300   79.40300  -12.23500 1.000 40.15047  ?  495  VAL   B O   1 
ATOM   17996 C  CB  . VAL   B 1 495  ? 29.77700   81.79500  -12.13100 1.000 33.05476  ?  495  VAL   B CB  1 
ATOM   17997 C  CG1 . VAL   B 1 495  ? 30.14300   81.89300  -10.66000 1.000 36.92729  ?  495  VAL   B CG1 1 
ATOM   17998 C  CG2 . VAL   B 1 495  ? 30.41800   82.92200  -12.91900 1.000 39.30718  ?  495  VAL   B CG2 1 
ATOM   17999 N  N   . ASP   B 1 496  ? 29.94600   78.25200  -11.66700 1.000 42.61417  ?  496  ASP   B N   1 
ATOM   18000 C  CA  . ASP   B 1 496  ? 29.22700   77.08100  -11.18700 1.000 47.20070  ?  496  ASP   B CA  1 
ATOM   18001 C  C   . ASP   B 1 496  ? 29.16000   76.97700  -9.67000  1.000 57.30212  ?  496  ASP   B C   1 
ATOM   18002 O  O   . ASP   B 1 496  ? 28.36000   76.18800  -9.15900  1.000 65.60603  ?  496  ASP   B O   1 
ATOM   18003 C  CB  . ASP   B 1 496  ? 29.87500   75.80100  -11.73600 1.000 44.24119  ?  496  ASP   B CB  1 
ATOM   18004 C  CG  . ASP   B 1 496  ? 31.29300   75.59400  -11.22000 1.000 60.25617  ?  496  ASP   B CG  1 
ATOM   18005 O  OD1 . ASP   B 1 496  ? 32.05700   76.58100  -11.13300 1.000 38.46399  ?  496  ASP   B OD1 1 
ATOM   18006 O  OD2 . ASP   B 1 496  ? 31.64300   74.43800  -10.89700 1.000 66.69525  -1 496  ASP   B OD2 1 
ATOM   18007 N  N   . LYS   B 1 497  ? 29.97300   77.74000  -8.94900  1.000 44.89816  ?  497  LYS   B N   1 
ATOM   18008 C  CA  . LYS   B 1 497  ? 30.07100   77.62400  -7.50000  1.000 42.55750  ?  497  LYS   B CA  1 
ATOM   18009 C  C   . LYS   B 1 497  ? 30.73200   78.89000  -6.97500  1.000 60.12589  ?  497  LYS   B C   1 
ATOM   18010 O  O   . LYS   B 1 497  ? 31.26800   79.68800  -7.75700  1.000 71.92151  ?  497  LYS   B O   1 
ATOM   18011 C  CB  . LYS   B 1 497  ? 30.86900   76.37100  -7.09500  1.000 55.85816  ?  497  LYS   B CB  1 
ATOM   18012 C  CG  . LYS   B 1 497  ? 32.36900   76.47200  -7.34700  1.000 61.55004  ?  497  LYS   B CG  1 
ATOM   18013 C  CD  . LYS   B 1 497  ? 32.97700   75.10500  -7.63200  1.000 48.13953  ?  497  LYS   B CD  1 
ATOM   18014 C  CE  . LYS   B 1 497  ? 34.35900   74.97100  -7.01200  1.000 58.06572  ?  497  LYS   B CE  1 
ATOM   18015 N  NZ  . LYS   B 1 497  ? 34.93600   73.61600  -7.23900  1.000 68.13415  ?  497  LYS   B NZ  1 
ATOM   18016 N  N   . PRO   B 1 498  ? 30.69000   79.12400  -5.66500  1.000 52.37996  ?  498  PRO   B N   1 
ATOM   18017 C  CA  . PRO   B 1 498  ? 31.39900   80.28400  -5.11400  1.000 48.18016  ?  498  PRO   B CA  1 
ATOM   18018 C  C   . PRO   B 1 498  ? 32.90500   80.13800  -5.25400  1.000 56.59803  ?  498  PRO   B C   1 
ATOM   18019 O  O   . PRO   B 1 498  ? 33.45200   79.03200  -5.26900  1.000 62.90607  ?  498  PRO   B O   1 
ATOM   18020 C  CB  . PRO   B 1 498  ? 30.97500   80.29500  -3.64100  1.000 42.17390  ?  498  PRO   B CB  1 
ATOM   18021 C  CG  . PRO   B 1 498  ? 29.67800   79.56300  -3.61900  1.000 49.13177  ?  498  PRO   B CG  1 
ATOM   18022 C  CD  . PRO   B 1 498  ? 29.80400   78.50100  -4.66700  1.000 46.20768  ?  498  PRO   B CD  1 
ATOM   18023 N  N   . TYR   B 1 499  ? 33.57400   81.28300  -5.36900  1.000 51.72098  ?  499  TYR   B N   1 
ATOM   18024 C  CA  . TYR   B 1 499  ? 35.02600   81.34500  -5.43900  1.000 36.38746  ?  499  TYR   B CA  1 
ATOM   18025 C  C   . TYR   B 1 499  ? 35.50600   82.55400  -4.65400  1.000 41.25765  ?  499  TYR   B C   1 
ATOM   18026 O  O   . TYR   B 1 499  ? 34.81500   83.57200  -4.57100  1.000 50.81341  ?  499  TYR   B O   1 
ATOM   18027 C  CB  . TYR   B 1 499  ? 35.54100   81.46100  -6.88300  1.000 43.31221  ?  499  TYR   B CB  1 
ATOM   18028 C  CG  . TYR   B 1 499  ? 35.27400   80.26100  -7.75800  1.000 34.61553  ?  499  TYR   B CG  1 
ATOM   18029 C  CD1 . TYR   B 1 499  ? 36.13900   79.17600  -7.76800  1.000 30.87883  ?  499  TYR   B CD1 1 
ATOM   18030 C  CD2 . TYR   B 1 499  ? 34.16600   80.22100  -8.59100  1.000 40.60098  ?  499  TYR   B CD2 1 
ATOM   18031 C  CE1 . TYR   B 1 499  ? 35.89800   78.07700  -8.57500  1.000 29.28027  ?  499  TYR   B CE1 1 
ATOM   18032 C  CE2 . TYR   B 1 499  ? 33.91600   79.12900  -9.39900  1.000 47.05857  ?  499  TYR   B CE2 1 
ATOM   18033 C  CZ  . TYR   B 1 499  ? 34.78400   78.06000  -9.38900  1.000 35.91446  ?  499  TYR   B CZ  1 
ATOM   18034 O  OH  . TYR   B 1 499  ? 34.52800   76.97600  -10.19900 1.000 49.02477  ?  499  TYR   B OH  1 
ATOM   18035 N  N   . ALA   B 1 500  ? 36.70200   82.43300  -4.07600  1.000 36.65702  ?  500  ALA   B N   1 
ATOM   18036 C  CA  . ALA   B 1 500  ? 37.38100   83.61800  -3.56500  1.000 45.40888  ?  500  ALA   B CA  1 
ATOM   18037 C  C   . ALA   B 1 500  ? 37.79100   84.53500  -4.71000  1.000 53.94858  ?  500  ALA   B C   1 
ATOM   18038 O  O   . ALA   B 1 500  ? 37.62100   85.75800  -4.63000  1.000 58.67502  ?  500  ALA   B O   1 
ATOM   18039 C  CB  . ALA   B 1 500  ? 38.59600   83.21500  -2.73200  1.000 58.86635  ?  500  ALA   B CB  1 
ATOM   18040 N  N   . ASN   B 1 501  ? 38.33500   83.96000  -5.78200  1.000 51.25299  ?  501  ASN   B N   1 
ATOM   18041 C  CA  . ASN   B 1 501  ? 38.59700   84.67100  -7.03000  1.000 41.60033  ?  501  ASN   B CA  1 
ATOM   18042 C  C   . ASN   B 1 501  ? 37.92100   83.88600  -8.14300  1.000 44.87418  ?  501  ASN   B C   1 
ATOM   18043 O  O   . ASN   B 1 501  ? 38.38900   82.80400  -8.51400  1.000 39.83973  ?  501  ASN   B O   1 
ATOM   18044 C  CB  . ASN   B 1 501  ? 40.09600   84.81700  -7.29600  1.000 36.03788  ?  501  ASN   B CB  1 
ATOM   18045 C  CG  . ASN   B 1 501  ? 40.39300   85.61600  -8.55700  1.000 51.36351  ?  501  ASN   B CG  1 
ATOM   18046 O  OD1 . ASN   B 1 501  ? 40.22700   85.12500  -9.67400  1.000 61.69213  ?  501  ASN   B OD1 1 
ATOM   18047 N  ND2 . ASN   B 1 501  ? 40.83600   86.85600  -8.38000  1.000 64.98551  ?  501  ASN   B ND2 1 
ATOM   18048 N  N   . ILE   B 1 502  ? 36.81600   84.41800  -8.65800  1.000 45.69318  ?  502  ILE   B N   1 
ATOM   18049 C  CA  . ILE   B 1 502  ? 36.07900   83.76800  -9.73800  1.000 39.92788  ?  502  ILE   B CA  1 
ATOM   18050 C  C   . ILE   B 1 502  ? 36.94000   83.80700  -10.99400 1.000 41.86041  ?  502  ILE   B C   1 
ATOM   18051 O  O   . ILE   B 1 502  ? 37.35900   84.89100  -11.42800 1.000 39.26807  ?  502  ILE   B O   1 
ATOM   18052 C  CB  . ILE   B 1 502  ? 34.71300   84.43200  -9.96600  1.000 37.36286  ?  502  ILE   B CB  1 
ATOM   18053 C  CG1 . ILE   B 1 502  ? 33.82800   84.25600  -8.73300  1.000 31.24090  ?  502  ILE   B CG1 1 
ATOM   18054 C  CG2 . ILE   B 1 502  ? 34.03300   83.84400  -11.19500 1.000 39.74230  ?  502  ILE   B CG2 1 
ATOM   18055 C  CD1 . ILE   B 1 502  ? 32.75300   85.30300  -8.60800  1.000 32.32464  ?  502  ILE   B CD1 1 
ATOM   18056 N  N   . PRO   B 1 503  ? 37.23500   82.65900  -11.59700 1.000 37.41447  ?  503  PRO   B N   1 
ATOM   18057 C  CA  . PRO   B 1 503  ? 38.12900   82.63500  -12.75800 1.000 32.79206  ?  503  PRO   B CA  1 
ATOM   18058 C  C   . PRO   B 1 503  ? 37.52100   83.33100  -13.96300 1.000 37.33084  ?  503  PRO   B C   1 
ATOM   18059 O  O   . PRO   B 1 503  ? 36.30300   83.46200  -14.10200 1.000 41.38913  ?  503  PRO   B O   1 
ATOM   18060 C  CB  . PRO   B 1 503  ? 38.31800   81.13900  -13.03300 1.000 32.75858  ?  503  PRO   B CB  1 
ATOM   18061 C  CG  . PRO   B 1 503  ? 37.88300   80.44900  -11.78600 1.000 27.27717  ?  503  PRO   B CG  1 
ATOM   18062 C  CD  . PRO   B 1 503  ? 36.82200   81.30900  -11.18800 1.000 35.41025  ?  503  PRO   B CD  1 
ATOM   18063 N  N   . ILE   B 1 504  ? 38.41200   83.77900  -14.85400 1.000 37.38024  ?  504  ILE   B N   1 
ATOM   18064 C  CA  . ILE   B 1 504  ? 37.98800   84.32900  -16.13700 1.000 34.39646  ?  504  ILE   B CA  1 
ATOM   18065 C  C   . ILE   B 1 504  ? 37.88600   83.26100  -17.21400 1.000 37.52217  ?  504  ILE   B C   1 
ATOM   18066 O  O   . ILE   B 1 504  ? 37.42200   83.55900  -18.32500 1.000 41.73005  ?  504  ILE   B O   1 
ATOM   18067 C  CB  . ILE   B 1 504  ? 38.93300   85.45200  -16.60400 1.000 41.17226  ?  504  ILE   B CB  1 
ATOM   18068 C  CG1 . ILE   B 1 504  ? 40.37800   84.95500  -16.65400 1.000 44.39824  ?  504  ILE   B CG1 1 
ATOM   18069 C  CG2 . ILE   B 1 504  ? 38.81300   86.66100  -15.68900 1.000 29.04972  ?  504  ILE   B CG2 1 
ATOM   18070 C  CD1 . ILE   B 1 504  ? 41.36300   86.01700  -17.08700 1.000 35.97853  ?  504  ILE   B CD1 1 
ATOM   18071 N  N   . GLY   B 1 505  ? 38.31500   82.03200  -16.92900 1.000 36.25121  ?  505  GLY   B N   1 
ATOM   18072 C  CA  . GLY   B 1 505  ? 38.00100   80.89800  -17.77700 1.000 33.92508  ?  505  GLY   B CA  1 
ATOM   18073 C  C   . GLY   B 1 505  ? 39.06300   80.46400  -18.76600 1.000 36.68275  ?  505  GLY   B C   1 
ATOM   18074 O  O   . GLY   B 1 505  ? 40.26400   80.64300  -18.53900 1.000 33.86304  ?  505  GLY   B O   1 
ATOM   18075 N  N   . LYS   B 1 506  ? 38.61200   79.88500  -19.87100 1.000 28.54022  ?  506  LYS   B N   1 
ATOM   18076 C  CA  . LYS   B 1 506  ? 39.45100   79.31900  -20.91000 1.000 26.89256  ?  506  LYS   B CA  1 
ATOM   18077 C  C   . LYS   B 1 506  ? 39.35100   80.13300  -22.19700 1.000 34.50109  ?  506  LYS   B C   1 
ATOM   18078 O  O   . LYS   B 1 506  ? 38.35100   80.82100  -22.43200 1.000 28.21256  ?  506  LYS   B O   1 
ATOM   18079 C  CB  . LYS   B 1 506  ? 39.04000   77.86400  -21.16900 1.000 18.80089  ?  506  LYS   B CB  1 
ATOM   18080 C  CG  . LYS   B 1 506  ? 39.08100   77.00400  -19.91700 1.000 24.51294  ?  506  LYS   B CG  1 
ATOM   18081 C  CD  . LYS   B 1 506  ? 39.08700   75.52500  -20.25100 1.000 33.99956  ?  506  LYS   B CD  1 
ATOM   18082 C  CE  . LYS   B 1 506  ? 39.32600   74.68100  -19.00900 1.000 44.00789  ?  506  LYS   B CE  1 
ATOM   18083 N  NZ  . LYS   B 1 506  ? 38.24600   73.67400  -18.81200 1.000 56.18711  ?  506  LYS   B NZ  1 
ATOM   18084 N  N   . PRO   B 1 507  ? 40.37800   80.09000  -23.04800 1.000 36.85953  ?  507  PRO   B N   1 
ATOM   18085 C  CA  . PRO   B 1 507  ? 40.35800   80.90000  -24.27400 1.000 27.88405  ?  507  PRO   B CA  1 
ATOM   18086 C  C   . PRO   B 1 507  ? 39.26000   80.47200  -25.23500 1.000 21.49802  ?  507  PRO   B C   1 
ATOM   18087 O  O   . PRO   B 1 507  ? 38.86500   79.30500  -25.29000 1.000 28.28616  ?  507  PRO   B O   1 
ATOM   18088 C  CB  . PRO   B 1 507  ? 41.74300   80.65400  -24.88600 1.000 28.16456  ?  507  PRO   B CB  1 
ATOM   18089 C  CG  . PRO   B 1 507  ? 42.58600   80.14500  -23.75900 1.000 29.35735  ?  507  PRO   B CG  1 
ATOM   18090 C  CD  . PRO   B 1 507  ? 41.65700   79.38100  -22.87400 1.000 24.47079  ?  507  PRO   B CD  1 
ATOM   18091 N  N   . ILE   B 1 508  ? 38.77900   81.43800  -26.01700 1.000 22.93548  ?  508  ILE   B N   1 
ATOM   18092 C  CA  . ILE   B 1 508  ? 37.76500   81.16300  -27.03100 1.000 32.33304  ?  508  ILE   B CA  1 
ATOM   18093 C  C   . ILE   B 1 508  ? 38.43900   80.59900  -28.27600 1.000 38.35030  ?  508  ILE   B C   1 
ATOM   18094 O  O   . ILE   B 1 508  ? 39.63100   80.26900  -28.25400 1.000 34.18742  ?  508  ILE   B O   1 
ATOM   18095 C  CB  . ILE   B 1 508  ? 36.94300   82.42200  -27.36700 1.000 22.97711  ?  508  ILE   B CB  1 
ATOM   18096 C  CG1 . ILE   B 1 508  ? 37.81100   83.45900  -28.08200 1.000 25.47784  ?  508  ILE   B CG1 1 
ATOM   18097 C  CG2 . ILE   B 1 508  ? 36.34400   83.02100  -26.11000 1.000 20.25946  ?  508  ILE   B CG2 1 
ATOM   18098 C  CD1 . ILE   B 1 508  ? 37.05000   84.69300  -28.50400 1.000 15.48942  ?  508  ILE   B CD1 1 
ATOM   18099 N  N   . ASP   B 1 509  ? 37.67700   80.48900  -29.36500 1.000 32.62787  ?  509  ASP   B N   1 
ATOM   18100 C  CA  . ASP   B 1 509  ? 38.18800   79.88800  -30.59100 1.000 28.24517  ?  509  ASP   B CA  1 
ATOM   18101 C  C   . ASP   B 1 509  ? 39.37800   80.67000  -31.13200 1.000 25.47958  ?  509  ASP   B C   1 
ATOM   18102 O  O   . ASP   B 1 509  ? 39.41700   81.90200  -31.06200 1.000 28.88594  ?  509  ASP   B O   1 
ATOM   18103 C  CB  . ASP   B 1 509  ? 37.08300   79.82800  -31.64700 1.000 33.95392  ?  509  ASP   B CB  1 
ATOM   18104 C  CG  . ASP   B 1 509  ? 36.03600   78.77500  -31.34000 1.000 45.85159  ?  509  ASP   B CG  1 
ATOM   18105 O  OD1 . ASP   B 1 509  ? 36.22000   78.02000  -30.36200 1.000 61.77766  ?  509  ASP   B OD1 1 
ATOM   18106 O  OD2 . ASP   B 1 509  ? 35.02900   78.70400  -32.07800 1.000 38.03111  -1 509  ASP   B OD2 1 
ATOM   18107 N  N   . ARG   B 1 510  ? 40.35500   79.93500  -31.67000 1.000 26.26332  ?  510  ARG   B N   1 
ATOM   18108 C  CA  . ARG   B 1 510  ? 41.52300   80.51600  -32.33700 1.000 21.68392  ?  510  ARG   B CA  1 
ATOM   18109 C  C   . ARG   B 1 510  ? 42.22700   81.53100  -31.44100 1.000 25.24636  ?  510  ARG   B C   1 
ATOM   18110 O  O   . ARG   B 1 510  ? 42.69600   82.57700  -31.89300 1.000 29.35813  ?  510  ARG   B O   1 
ATOM   18111 C  CB  . ARG   B 1 510  ? 41.13100   81.14400  -33.67600 1.000 23.93440  ?  510  ARG   B CB  1 
ATOM   18112 C  CG  . ARG   B 1 510  ? 40.60100   80.14100  -34.68800 1.000 26.38437  ?  510  ARG   B CG  1 
ATOM   18113 C  CD  . ARG   B 1 510  ? 40.35900   80.78400  -36.04300 1.000 44.75002  ?  510  ARG   B CD  1 
ATOM   18114 N  NE  . ARG   B 1 510  ? 39.55700   79.92700  -36.90700 1.000 60.12367  ?  510  ARG   B NE  1 
ATOM   18115 C  CZ  . ARG   B 1 510  ? 38.23100   79.89000  -36.90100 1.000 53.69432  ?  510  ARG   B CZ  1 
ATOM   18116 N  NH1 . ARG   B 1 510  ? 37.52200   80.67500  -36.10700 1.000 45.81563  ?  510  ARG   B NH1 1 
ATOM   18117 N  NH2 . ARG   B 1 510  ? 37.60200   79.04300  -37.71100 1.000 61.65798  ?  510  ARG   B NH2 1 
ATOM   18118 N  N   . THR   B 1 511  ? 42.29800   81.21400  -30.15200 1.000 25.63845  ?  511  THR   B N   1 
ATOM   18119 C  CA  . THR   B 1 511  ? 42.90300   82.09400  -29.16600 1.000 29.11852  ?  511  THR   B CA  1 
ATOM   18120 C  C   . THR   B 1 511  ? 43.76100   81.26800  -28.22100 1.000 32.34326  ?  511  THR   B C   1 
ATOM   18121 O  O   . THR   B 1 511  ? 43.35100   80.19000  -27.78000 1.000 34.72722  ?  511  THR   B O   1 
ATOM   18122 C  CB  . THR   B 1 511  ? 41.83200   82.86600  -28.37800 1.000 28.42046  ?  511  THR   B CB  1 
ATOM   18123 O  OG1 . THR   B 1 511  ? 40.94800   83.52700  -29.29100 1.000 33.02893  ?  511  THR   B OG1 1 
ATOM   18124 C  CG2 . THR   B 1 511  ? 42.47200   83.90000  -27.46700 1.000 32.11508  ?  511  THR   B CG2 1 
ATOM   18125 N  N   . ARG   B 1 512  ? 44.95800   81.76900  -27.92600 1.000 26.66425  ?  512  ARG   B N   1 
ATOM   18126 C  CA  . ARG   B 1 512  ? 45.84200   81.15900  -26.94500 1.000 21.20258  ?  512  ARG   B CA  1 
ATOM   18127 C  C   . ARG   B 1 512  ? 46.29900   82.22300  -25.96200 1.000 31.38490  ?  512  ARG   B C   1 
ATOM   18128 O  O   . ARG   B 1 512  ? 46.60600   83.35300  -26.35700 1.000 30.52700  ?  512  ARG   B O   1 
ATOM   18129 C  CB  . ARG   B 1 512  ? 47.05300   80.50300  -27.61000 1.000 24.64873  ?  512  ARG   B CB  1 
ATOM   18130 C  CG  . ARG   B 1 512  ? 46.89100   79.01300  -27.82100 1.000 34.25034  ?  512  ARG   B CG  1 
ATOM   18131 C  CD  . ARG   B 1 512  ? 47.87900   78.48200  -28.84400 1.000 47.52168  ?  512  ARG   B CD  1 
ATOM   18132 N  NE  . ARG   B 1 512  ? 49.26200   78.72900  -28.45400 1.000 60.96321  ?  512  ARG   B NE  1 
ATOM   18133 C  CZ  . ARG   B 1 512  ? 50.12700   79.43500  -29.16800 1.000 66.57725  ?  512  ARG   B CZ  1 
ATOM   18134 N  NH1 . ARG   B 1 512  ? 49.78400   79.98300  -30.32400 1.000 46.74424  ?  512  ARG   B NH1 1 
ATOM   18135 N  NH2 . ARG   B 1 512  ? 51.36700   79.59400  -28.71200 1.000 61.70336  ?  512  ARG   B NH2 1 
ATOM   18136 N  N   . ILE   B 1 513  ? 46.33700   81.86200  -24.68200 1.000 30.83866  ?  513  ILE   B N   1 
ATOM   18137 C  CA  . ILE   B 1 513  ? 46.79600   82.74800  -23.61800 1.000 37.17363  ?  513  ILE   B CA  1 
ATOM   18138 C  C   . ILE   B 1 513  ? 48.10600   82.19600  -23.07000 1.000 31.22146  ?  513  ILE   B C   1 
ATOM   18139 O  O   . ILE   B 1 513  ? 48.22700   80.98800  -22.82900 1.000 28.62981  ?  513  ILE   B O   1 
ATOM   18140 C  CB  . ILE   B 1 513  ? 45.73700   82.89300  -22.50900 1.000 37.32656  ?  513  ILE   B CB  1 
ATOM   18141 C  CG1 . ILE   B 1 513  ? 44.75600   84.01400  -22.85100 1.000 34.93916  ?  513  ILE   B CG1 1 
ATOM   18142 C  CG2 . ILE   B 1 513  ? 46.38500   83.19300  -21.17000 1.000 44.69814  ?  513  ILE   B CG2 1 
ATOM   18143 C  CD1 . ILE   B 1 513  ? 43.73000   83.63100  -23.88200 1.000 45.79741  ?  513  ILE   B CD1 1 
ATOM   18144 N  N   . LEU   B 1 514  ? 49.09200   83.07700  -22.89500 1.000 32.38085  ?  514  LEU   B N   1 
ATOM   18145 C  CA  . LEU   B 1 514  ? 50.39100   82.71400  -22.34100 1.000 31.51748  ?  514  LEU   B CA  1 
ATOM   18146 C  C   . LEU   B 1 514  ? 50.69400   83.60900  -21.15000 1.000 31.43789  ?  514  LEU   B C   1 
ATOM   18147 O  O   . LEU   B 1 514  ? 50.52800   84.83100  -21.23100 1.000 29.85686  ?  514  LEU   B O   1 
ATOM   18148 C  CB  . LEU   B 1 514  ? 51.50300   82.85000  -23.38600 1.000 32.81061  ?  514  LEU   B CB  1 
ATOM   18149 C  CG  . LEU   B 1 514  ? 51.31200   82.11500  -24.71100 1.000 33.55652  ?  514  LEU   B CG  1 
ATOM   18150 C  CD1 . LEU   B 1 514  ? 52.34800   82.57600  -25.71800 1.000 30.75218  ?  514  LEU   B CD1 1 
ATOM   18151 C  CD2 . LEU   B 1 514  ? 51.39700   80.61800  -24.50400 1.000 37.50366  ?  514  LEU   B CD2 1 
ATOM   18152 N  N   . ILE   B 1 515  ? 51.14000   83.00600  -20.05200 1.000 31.61307  ?  515  ILE   B N   1 
ATOM   18153 C  CA  . ILE   B 1 515  ? 51.54900   83.73900  -18.85800 1.000 35.41437  ?  515  ILE   B CA  1 
ATOM   18154 C  C   . ILE   B 1 515  ? 53.06900   83.84300  -18.88700 1.000 36.16812  ?  515  ILE   B C   1 
ATOM   18155 O  O   . ILE   B 1 515  ? 53.77300   82.83700  -18.75100 1.000 33.77689  ?  515  ILE   B O   1 
ATOM   18156 C  CB  . ILE   B 1 515  ? 51.05800   83.05500  -17.57400 1.000 33.59155  ?  515  ILE   B CB  1 
ATOM   18157 C  CG1 . ILE   B 1 515  ? 49.54200   82.84500  -17.62000 1.000 37.60618  ?  515  ILE   B CG1 1 
ATOM   18158 C  CG2 . ILE   B 1 515  ? 51.44400   83.87700  -16.35400 1.000 30.48233  ?  515  ILE   B CG2 1 
ATOM   18159 C  CD1 . ILE   B 1 515  ? 48.74600   84.12200  -17.78400 1.000 39.32030  ?  515  ILE   B CD1 1 
ATOM   18160 N  N   . LEU   B 1 516  ? 53.58500   85.05700  -19.06300 1.000 31.55577  ?  516  LEU   B N   1 
ATOM   18161 C  CA  . LEU   B 1 516  ? 55.01500   85.27500  -19.21100 1.000 34.61009  ?  516  LEU   B CA  1 
ATOM   18162 C  C   . LEU   B 1 516  ? 55.54100   86.18900  -18.11200 1.000 42.74627  ?  516  LEU   B C   1 
ATOM   18163 O  O   . LEU   B 1 516  ? 54.78700   86.92000  -17.46200 1.000 46.36210  ?  516  LEU   B O   1 
ATOM   18164 C  CB  . LEU   B 1 516  ? 55.34900   85.87600  -20.58100 1.000 38.84718  ?  516  LEU   B CB  1 
ATOM   18165 C  CG  . LEU   B 1 516  ? 54.79400   85.18700  -21.82900 1.000 31.99518  ?  516  LEU   B CG  1 
ATOM   18166 C  CD1 . LEU   B 1 516  ? 55.36500   85.87400  -23.04300 1.000 26.58524  ?  516  LEU   B CD1 1 
ATOM   18167 C  CD2 . LEU   B 1 516  ? 55.10700   83.69400  -21.85600 1.000 20.55930  ?  516  LEU   B CD2 1 
ATOM   18168 N  N   . ASP   B 1 517  ? 56.85800   86.14300  -17.92200 1.000 38.63738  ?  517  ASP   B N   1 
ATOM   18169 C  CA  . ASP   B 1 517  ? 57.53000   86.92500  -16.89500 1.000 44.23067  ?  517  ASP   B CA  1 
ATOM   18170 C  C   . ASP   B 1 517  ? 58.03800   88.23300  -17.50700 1.000 48.64259  ?  517  ASP   B C   1 
ATOM   18171 O  O   . ASP   B 1 517  ? 57.60900   88.63500  -18.59200 1.000 65.86923  ?  517  ASP   B O   1 
ATOM   18172 C  CB  . ASP   B 1 517  ? 58.64400   86.09000  -16.25600 1.000 40.15471  ?  517  ASP   B CB  1 
ATOM   18173 C  CG  . ASP   B 1 517  ? 59.72500   85.70300  -17.24900 1.000 55.62909  ?  517  ASP   B CG  1 
ATOM   18174 O  OD1 . ASP   B 1 517  ? 59.53900   85.94500  -18.46100 1.000 55.18583  ?  517  ASP   B OD1 1 
ATOM   18175 O  OD2 . ASP   B 1 517  ? 60.76400   85.15600  -16.81700 1.000 62.26372  -1 517  ASP   B OD2 1 
ATOM   18176 N  N   . GLU   B 1 518  ? 58.96800   88.90600  -16.82700 1.000 48.20441  ?  518  GLU   B N   1 
ATOM   18177 C  CA  . GLU   B 1 518  ? 59.48000   90.17900  -17.32100 1.000 36.20375  ?  518  GLU   B CA  1 
ATOM   18178 C  C   . GLU   B 1 518  ? 60.31700   90.01500  -18.58100 1.000 48.87947  ?  518  GLU   B C   1 
ATOM   18179 O  O   . GLU   B 1 518  ? 60.44000   90.96800  -19.35700 1.000 45.80696  ?  518  GLU   B O   1 
ATOM   18180 C  CB  . GLU   B 1 518  ? 60.30400   90.86900  -16.23600 1.000 49.83253  ?  518  GLU   B CB  1 
ATOM   18181 C  CG  . GLU   B 1 518  ? 59.53000   91.17600  -14.96500 1.000 67.53029  ?  518  GLU   B CG  1 
ATOM   18182 C  CD  . GLU   B 1 518  ? 59.27300   92.65700  -14.78800 1.000 112.01946 ?  518  GLU   B CD  1 
ATOM   18183 O  OE1 . GLU   B 1 518  ? 59.17000   93.36600  -15.81100 1.000 117.40332 ?  518  GLU   B OE1 1 
ATOM   18184 O  OE2 . GLU   B 1 518  ? 59.17500   93.11300  -13.62800 1.000 116.92326 -1 518  GLU   B OE2 1 
ATOM   18185 N  N   . ALA   B 1 519  ? 60.89800   88.83500  -18.79900 1.000 50.80250  ?  519  ALA   B N   1 
ATOM   18186 C  CA  . ALA   B 1 519  ? 61.70600   88.55600  -19.97800 1.000 40.13160  ?  519  ALA   B CA  1 
ATOM   18187 C  C   . ALA   B 1 519  ? 60.94300   87.75900  -21.02800 1.000 44.09189  ?  519  ALA   B C   1 
ATOM   18188 O  O   . ALA   B 1 519  ? 61.56500   87.12300  -21.88700 1.000 46.89120  ?  519  ALA   B O   1 
ATOM   18189 C  CB  . ALA   B 1 519  ? 62.98400   87.81700  -19.57900 1.000 37.75260  ?  519  ALA   B CB  1 
ATOM   18190 N  N   . LEU   B 1 520  ? 59.60900   87.77300  -20.96700 1.000 43.89730  ?  520  LEU   B N   1 
ATOM   18191 C  CA  . LEU   B 1 520  ? 58.74700   87.08100  -21.92800 1.000 31.71124  ?  520  LEU   B CA  1 
ATOM   18192 C  C   . LEU   B 1 520  ? 58.98700   85.57300  -21.93600 1.000 33.50176  ?  520  LEU   B C   1 
ATOM   18193 O  O   . LEU   B 1 520  ? 58.72300   84.89800  -22.93300 1.000 35.40077  ?  520  LEU   B O   1 
ATOM   18194 C  CB  . LEU   B 1 520  ? 58.90800   87.65600  -23.33800 1.000 24.18748  ?  520  LEU   B CB  1 
ATOM   18195 C  CG  . LEU   B 1 520  ? 58.95400   89.18300  -23.45600 1.000 29.15020  ?  520  LEU   B CG  1 
ATOM   18196 C  CD1 . LEU   B 1 520  ? 59.14500   89.60700  -24.90500 1.000 30.35232  ?  520  LEU   B CD1 1 
ATOM   18197 C  CD2 . LEU   B 1 520  ? 57.70600   89.82200  -22.86500 1.000 38.63420  ?  520  LEU   B CD2 1 
ATOM   18198 N  N   . ALA   B 1 521  ? 59.48200   85.02700  -20.82800 1.000 39.29230  ?  521  ALA   B N   1 
ATOM   18199 C  CA  . ALA   B 1 521  ? 59.68100   83.59100  -20.69900 1.000 41.29359  ?  521  ALA   B CA  1 
ATOM   18200 C  C   . ALA   B 1 521  ? 58.42200   82.92700  -20.15400 1.000 41.44525  ?  521  ALA   B C   1 
ATOM   18201 O  O   . ALA   B 1 521  ? 57.67700   83.51400  -19.36500 1.000 32.20756  ?  521  ALA   B O   1 
ATOM   18202 C  CB  . ALA   B 1 521  ? 60.86900   83.28400  -19.78500 1.000 27.01368  ?  521  ALA   B CB  1 
ATOM   18203 N  N   . LEU   B 1 522  ? 58.19200   81.69000  -20.58600 1.000 37.85493  ?  522  LEU   B N   1 
ATOM   18204 C  CA  . LEU   B 1 522  ? 57.00900   80.95500  -20.15900 1.000 26.98804  ?  522  LEU   B CA  1 
ATOM   18205 C  C   . LEU   B 1 522  ? 57.07600   80.65600  -18.66400 1.000 41.87371  ?  522  LEU   B C   1 
ATOM   18206 O  O   . LEU   B 1 522  ? 58.09700   80.17900  -18.16000 1.000 55.09060  ?  522  LEU   B O   1 
ATOM   18207 C  CB  . LEU   B 1 522  ? 56.88400   79.65900  -20.95700 1.000 33.77863  ?  522  LEU   B CB  1 
ATOM   18208 C  CG  . LEU   B 1 522  ? 55.55400   78.91500  -20.86700 1.000 46.99141  ?  522  LEU   B CG  1 
ATOM   18209 C  CD1 . LEU   B 1 522  ? 54.39700   79.86400  -21.13500 1.000 41.83342  ?  522  LEU   B CD1 1 
ATOM   18210 C  CD2 . LEU   B 1 522  ? 55.53700   77.74600  -21.84100 1.000 42.56410  ?  522  LEU   B CD2 1 
ATOM   18211 N  N   . GLN   B 1 523  ? 55.98500   80.94700  -17.95300 1.000 31.64059  ?  523  GLN   B N   1 
ATOM   18212 C  CA  . GLN   B 1 523  ? 55.85700   80.65500  -16.52900 1.000 25.63390  ?  523  GLN   B CA  1 
ATOM   18213 C  C   . GLN   B 1 523  ? 55.17700   79.30400  -16.32800 1.000 32.95750  ?  523  GLN   B C   1 
ATOM   18214 O  O   . GLN   B 1 523  ? 54.30000   78.92800  -17.11000 1.000 37.67713  ?  523  GLN   B O   1 
ATOM   18215 C  CB  . GLN   B 1 523  ? 55.04500   81.73700  -15.82200 1.000 23.51050  ?  523  GLN   B CB  1 
ATOM   18216 C  CG  . GLN   B 1 523  ? 55.66400   83.11800  -15.88200 1.000 35.78178  ?  523  GLN   B CG  1 
ATOM   18217 C  CD  . GLN   B 1 523  ? 56.73300   83.32900  -14.82900 1.000 32.02282  ?  523  GLN   B CD  1 
ATOM   18218 O  OE1 . GLN   B 1 523  ? 57.78900   82.69500  -14.85900 1.000 41.61843  ?  523  GLN   B OE1 1 
ATOM   18219 N  NE2 . GLN   B 1 523  ? 56.46400   84.22900  -13.89200 1.000 37.62576  ?  523  GLN   B NE2 1 
ATOM   18220 N  N   . PRO   B 1 524  ? 55.56100   78.55000  -15.30200 1.000 46.61577  ?  524  PRO   B N   1 
ATOM   18221 C  CA  . PRO   B 1 524  ? 54.89100   77.27400  -15.03900 1.000 34.38188  ?  524  PRO   B CA  1 
ATOM   18222 C  C   . PRO   B 1 524  ? 53.46000   77.49600  -14.57700 1.000 38.67357  ?  524  PRO   B C   1 
ATOM   18223 O  O   . PRO   B 1 524  ? 53.07100   78.59300  -14.16800 1.000 49.76741  ?  524  PRO   B O   1 
ATOM   18224 C  CB  . PRO   B 1 524  ? 55.73900   76.64000  -13.92800 1.000 33.98020  ?  524  PRO   B CB  1 
ATOM   18225 C  CG  . PRO   B 1 524  ? 57.01600   77.42700  -13.89900 1.000 25.34553  ?  524  PRO   B CG  1 
ATOM   18226 C  CD  . PRO   B 1 524  ? 56.66500   78.80100  -14.36300 1.000 36.33462  ?  524  PRO   B CD  1 
ATOM   18227 N  N   . ILE   B 1 525  ? 52.66700   76.42400  -14.65600 1.000 37.82479  ?  525  ILE   B N   1 
ATOM   18228 C  CA  . ILE   B 1 525  ? 51.28300   76.49000  -14.20200 1.000 31.64557  ?  525  ILE   B CA  1 
ATOM   18229 C  C   . ILE   B 1 525  ? 51.26000   76.81500  -12.71700 1.000 36.95256  ?  525  ILE   B C   1 
ATOM   18230 O  O   . ILE   B 1 525  ? 52.00900   76.23100  -11.92400 1.000 48.25878  ?  525  ILE   B O   1 
ATOM   18231 C  CB  . ILE   B 1 525  ? 50.55500   75.17000  -14.49600 1.000 31.81472  ?  525  ILE   B CB  1 
ATOM   18232 C  CG1 . ILE   B 1 525  ? 50.41500   74.95800  -16.00300 1.000 32.65802  ?  525  ILE   B CG1 1 
ATOM   18233 C  CG2 . ILE   B 1 525  ? 49.18800   75.14800  -13.82600 1.000 34.51021  ?  525  ILE   B CG2 1 
ATOM   18234 C  CD1 . ILE   B 1 525  ? 49.54300   73.77300  -16.36700 1.000 34.79116  ?  525  ILE   B CD1 1 
ATOM   18235 N  N   . GLY   B 1 526  ? 50.40300   77.75900  -12.33400 1.000 37.65155  ?  526  GLY   B N   1 
ATOM   18236 C  CA  . GLY   B 1 526  ? 50.30200   78.20900  -10.96800 1.000 35.75068  ?  526  GLY   B CA  1 
ATOM   18237 C  C   . GLY   B 1 526  ? 51.14200   79.42800  -10.64800 1.000 35.84052  ?  526  GLY   B C   1 
ATOM   18238 O  O   . GLY   B 1 526  ? 50.78400   80.19700  -9.75000  1.000 39.94753  ?  526  GLY   B O   1 
ATOM   18239 N  N   . VAL   B 1 527  ? 52.25300   79.62100  -11.36000 1.000 27.10282  ?  527  VAL   B N   1 
ATOM   18240 C  CA  . VAL   B 1 527  ? 53.09400   80.79800  -11.17100 1.000 26.21957  ?  527  VAL   B CA  1 
ATOM   18241 C  C   . VAL   B 1 527  ? 52.45800   81.97900  -11.88800 1.000 25.71277  ?  527  VAL   B C   1 
ATOM   18242 O  O   . VAL   B 1 527  ? 51.88800   81.83400  -12.97600 1.000 40.19675  ?  527  VAL   B O   1 
ATOM   18243 C  CB  . VAL   B 1 527  ? 54.52400   80.53200  -11.68000 1.000 38.84362  ?  527  VAL   B CB  1 
ATOM   18244 C  CG1 . VAL   B 1 527  ? 55.45200   81.68700  -11.31700 1.000 16.85852  ?  527  VAL   B CG1 1 
ATOM   18245 C  CG2 . VAL   B 1 527  ? 55.05600   79.21700  -11.12200 1.000 27.73456  ?  527  VAL   B CG2 1 
ATOM   18246 N  N   . ALA   B 1 528  ? 52.54200   83.15500  -11.27400 1.000 27.01704  ?  528  ALA   B N   1 
ATOM   18247 C  CA  . ALA   B 1 528  ? 51.91800   84.34400  -11.82900 1.000 28.08876  ?  528  ALA   B CA  1 
ATOM   18248 C  C   . ALA   B 1 528  ? 52.80800   84.97800  -12.89500 1.000 42.78374  ?  528  ALA   B C   1 
ATOM   18249 O  O   . ALA   B 1 528  ? 53.97600   84.62000  -13.07400 1.000 43.12603  ?  528  ALA   B O   1 
ATOM   18250 C  CB  . ALA   B 1 528  ? 51.61600   85.35900  -10.72900 1.000 31.97140  ?  528  ALA   B CB  1 
ATOM   18251 N  N   . GLY   B 1 529  ? 52.23200   85.94200  -13.60100 1.000 39.72357  ?  529  GLY   B N   1 
ATOM   18252 C  CA  . GLY   B 1 529  ? 52.94300   86.65100  -14.64400 1.000 41.17206  ?  529  GLY   B CA  1 
ATOM   18253 C  C   . GLY   B 1 529  ? 51.97900   87.48800  -15.45400 1.000 38.31180  ?  529  GLY   B C   1 
ATOM   18254 O  O   . GLY   B 1 529  ? 50.78100   87.56200  -15.16200 1.000 46.36162  ?  529  GLY   B O   1 
ATOM   18255 N  N   . GLU   B 1 530  ? 52.53000   88.12200  -16.48600 1.000 39.52301  ?  530  GLU   B N   1 
ATOM   18256 C  CA  . GLU   B 1 530  ? 51.73100   88.96000  -17.37000 1.000 36.38870  ?  530  GLU   B CA  1 
ATOM   18257 C  C   . GLU   B 1 530  ? 50.96800   88.10300  -18.37500 1.000 38.71403  ?  530  GLU   B C   1 
ATOM   18258 O  O   . GLU   B 1 530  ? 51.49600   87.12200  -18.90800 1.000 37.29943  ?  530  GLU   B O   1 
ATOM   18259 C  CB  . GLU   B 1 530  ? 52.61700   89.96600  -18.10600 1.000 38.32044  ?  530  GLU   B CB  1 
ATOM   18260 C  CG  . GLU   B 1 530  ? 51.83900   90.94400  -18.97200 1.000 40.96829  ?  530  GLU   B CG  1 
ATOM   18261 C  CD  . GLU   B 1 530  ? 52.68300   92.09500  -19.48100 1.000 38.59277  ?  530  GLU   B CD  1 
ATOM   18262 O  OE1 . GLU   B 1 530  ? 53.91100   91.92200  -19.61800 1.000 52.97599  ?  530  GLU   B OE1 1 
ATOM   18263 O  OE2 . GLU   B 1 530  ? 52.11300   93.17500  -19.75000 1.000 32.87502  -1 530  GLU   B OE2 1 
ATOM   18264 N  N   . LEU   B 1 531  ? 49.71500   88.48000  -18.62200 1.000 37.18380  ?  531  LEU   B N   1 
ATOM   18265 C  CA  . LEU   B 1 531  ? 48.87100   87.78100  -19.58200 1.000 34.25155  ?  531  LEU   B CA  1 
ATOM   18266 C  C   . LEU   B 1 531  ? 49.15200   88.28700  -20.99200 1.000 34.75589  ?  531  LEU   B C   1 
ATOM   18267 O  O   . LEU   B 1 531  ? 49.12100   89.49600  -21.24600 1.000 29.43099  ?  531  LEU   B O   1 
ATOM   18268 C  CB  . LEU   B 1 531  ? 47.39600   87.97700  -19.23100 1.000 28.41781  ?  531  LEU   B CB  1 
ATOM   18269 C  CG  . LEU   B 1 531  ? 46.38200   87.01500  -19.85900 1.000 34.64146  ?  531  LEU   B CG  1 
ATOM   18270 C  CD1 . LEU   B 1 531  ? 45.23900   86.74600  -18.89500 1.000 28.21009  ?  531  LEU   B CD1 1 
ATOM   18271 C  CD2 . LEU   B 1 531  ? 45.84300   87.55800  -21.17100 1.000 41.06024  ?  531  LEU   B CD2 1 
ATOM   18272 N  N   . PHE   B 1 532  ? 49.42000   87.35700  -21.90800 1.000 31.57066  ?  532  PHE   B N   1 
ATOM   18273 C  CA  . PHE   B 1 532  ? 49.69000   87.66200  -23.30700 1.000 29.37381  ?  532  PHE   B CA  1 
ATOM   18274 C  C   . PHE   B 1 532  ? 48.68600   86.91800  -24.17400 1.000 30.25588  ?  532  PHE   B C   1 
ATOM   18275 O  O   . PHE   B 1 532  ? 48.46200   85.71900  -23.97400 1.000 32.44820  ?  532  PHE   B O   1 
ATOM   18276 C  CB  . PHE   B 1 532  ? 51.11700   87.26200  -23.69800 1.000 33.52582  ?  532  PHE   B CB  1 
ATOM   18277 C  CG  . PHE   B 1 532  ? 52.16700   88.24800  -23.27100 1.000 24.76860  ?  532  PHE   B CG  1 
ATOM   18278 C  CD1 . PHE   B 1 532  ? 52.72700   88.18000  -22.00600 1.000 35.51870  ?  532  PHE   B CD1 1 
ATOM   18279 C  CD2 . PHE   B 1 532  ? 52.60100   89.23700  -24.13900 1.000 34.97239  ?  532  PHE   B CD2 1 
ATOM   18280 C  CE1 . PHE   B 1 532  ? 53.69600   89.08300  -21.61000 1.000 33.10492  ?  532  PHE   B CE1 1 
ATOM   18281 C  CE2 . PHE   B 1 532  ? 53.57200   90.14300  -23.75000 1.000 33.17968  ?  532  PHE   B CE2 1 
ATOM   18282 C  CZ  . PHE   B 1 532  ? 54.11900   90.06600  -22.48400 1.000 30.49034  ?  532  PHE   B CZ  1 
ATOM   18283 N  N   . ILE   B 1 533  ? 48.09800   87.61900  -25.14300 1.000 29.98959  ?  533  ILE   B N   1 
ATOM   18284 C  CA  . ILE   B 1 533  ? 47.04100   87.07300  -25.98900 1.000 39.01600  ?  533  ILE   B CA  1 
ATOM   18285 C  C   . ILE   B 1 533  ? 47.59400   86.81700  -27.38400 1.000 29.60914  ?  533  ILE   B C   1 
ATOM   18286 O  O   . ILE   B 1 533  ? 48.20500   87.70500  -27.99100 1.000 30.70836  ?  533  ILE   B O   1 
ATOM   18287 C  CB  . ILE   B 1 533  ? 45.82500   88.01300  -26.04700 1.000 30.13064  ?  533  ILE   B CB  1 
ATOM   18288 C  CG1 . ILE   B 1 533  ? 45.50700   88.55000  -24.65100 1.000 29.18783  ?  533  ILE   B CG1 1 
ATOM   18289 C  CG2 . ILE   B 1 533  ? 44.62800   87.29100  -26.63700 1.000 20.86922  ?  533  ILE   B CG2 1 
ATOM   18290 C  CD1 . ILE   B 1 533  ? 44.23200   89.34400  -24.57600 1.000 28.65379  ?  533  ILE   B CD1 1 
ATOM   18291 N  N   . VAL   B 1 534  ? 47.37100   85.60500  -27.89100 1.000 30.92292  ?  534  VAL   B N   1 
ATOM   18292 C  CA  . VAL   B 1 534  ? 47.77100   85.20500  -29.23700 1.000 32.00868  ?  534  VAL   B CA  1 
ATOM   18293 C  C   . VAL   B 1 534  ? 46.55200   84.62700  -29.93800 1.000 38.57397  ?  534  VAL   B C   1 
ATOM   18294 O  O   . VAL   B 1 534  ? 45.85300   83.78100  -29.36800 1.000 47.75636  ?  534  VAL   B O   1 
ATOM   18295 C  CB  . VAL   B 1 534  ? 48.91000   84.16400  -29.21900 1.000 25.22357  ?  534  VAL   B CB  1 
ATOM   18296 C  CG1 . VAL   B 1 534  ? 50.00300   84.55600  -30.18800 1.000 40.73990  ?  534  VAL   B CG1 1 
ATOM   18297 C  CG2 . VAL   B 1 534  ? 49.47000   83.99800  -27.81900 1.000 40.54548  ?  534  VAL   B CG2 1 
ATOM   18298 N  N   . GLY   B 1 535  ? 46.29700   85.06900  -31.16100 1.000 36.08470  ?  535  GLY   B N   1 
ATOM   18299 C  CA  . GLY   B 1 535  ? 45.26100   84.44200  -31.95800 1.000 41.26399  ?  535  GLY   B CA  1 
ATOM   18300 C  C   . GLY   B 1 535  ? 44.55300   85.44200  -32.85200 1.000 39.49339  ?  535  GLY   B C   1 
ATOM   18301 O  O   . GLY   B 1 535  ? 45.06800   86.52000  -33.13600 1.000 30.64549  ?  535  GLY   B O   1 
ATOM   18302 N  N   . GLU   B 1 536  ? 43.35400   85.04300  -33.28100 1.000 36.30618  ?  536  GLU   B N   1 
ATOM   18303 C  CA  . GLU   B 1 536  ? 42.56800   85.77400  -34.26700 1.000 34.19480  ?  536  GLU   B CA  1 
ATOM   18304 C  C   . GLU   B 1 536  ? 41.79600   86.95000  -33.68300 1.000 31.19180  ?  536  GLU   B C   1 
ATOM   18305 O  O   . GLU   B 1 536  ? 41.04900   87.60300  -34.42100 1.000 31.46500  ?  536  GLU   B O   1 
ATOM   18306 C  CB  . GLU   B 1 536  ? 41.59500   84.82000  -34.96400 1.000 24.45666  ?  536  GLU   B CB  1 
ATOM   18307 C  CG  . GLU   B 1 536  ? 42.24600   83.95500  -36.03200 1.000 35.28239  ?  536  GLU   B CG  1 
ATOM   18308 C  CD  . GLU   B 1 536  ? 41.91600   84.42300  -37.43800 1.000 42.74809  ?  536  GLU   B CD  1 
ATOM   18309 O  OE1 . GLU   B 1 536  ? 41.58100   85.61400  -37.60700 1.000 33.50919  ?  536  GLU   B OE1 1 
ATOM   18310 O  OE2 . GLU   B 1 536  ? 41.99000   83.59900  -38.37400 1.000 67.06972  -1 536  GLU   B OE2 1 
ATOM   18311 N  N   . GLY   B 1 537  ? 41.94800   87.24100  -32.39600 1.000 19.04595  ?  537  GLY   B N   1 
ATOM   18312 C  CA  . GLY   B 1 537  ? 41.24500   88.36500  -31.81400 1.000 16.48470  ?  537  GLY   B CA  1 
ATOM   18313 C  C   . GLY   B 1 537  ? 42.05200   89.64400  -31.85800 1.000 29.38547  ?  537  GLY   B C   1 
ATOM   18314 O  O   . GLY   B 1 537  ? 41.50700   90.73600  -31.67900 1.000 30.64296  ?  537  GLY   B O   1 
ATOM   18315 N  N   . LEU   B 1 538  ? 43.35100   89.52200  -32.11100 1.000 37.47873  ?  538  LEU   B N   1 
ATOM   18316 C  CA  . LEU   B 1 538  ? 44.23300   90.68100  -32.09100 1.000 37.52595  ?  538  LEU   B CA  1 
ATOM   18317 C  C   . LEU   B 1 538  ? 43.87100   91.64500  -33.21400 1.000 35.33869  ?  538  LEU   B C   1 
ATOM   18318 O  O   . LEU   B 1 538  ? 43.84100   91.26400  -34.39000 1.000 31.63557  ?  538  LEU   B O   1 
ATOM   18319 C  CB  . LEU   B 1 538  ? 45.68700   90.23600  -32.20800 1.000 41.66419  ?  538  LEU   B CB  1 
ATOM   18320 C  CG  . LEU   B 1 538  ? 46.39700   89.89300  -30.89600 1.000 41.00425  ?  538  LEU   B CG  1 
ATOM   18321 C  CD1 . LEU   B 1 538  ? 46.03100   88.48900  -30.44200 1.000 43.73417  ?  538  LEU   B CD1 1 
ATOM   18322 C  CD2 . LEU   B 1 538  ? 47.90700   90.04600  -31.03900 1.000 29.25272  ?  538  LEU   B CD2 1 
ATOM   18323 N  N   . GLY   B 1 539  ? 43.60200   92.89700  -32.85100 1.000 29.26663  ?  539  GLY   B N   1 
ATOM   18324 C  CA  . GLY   B 1 539  ? 43.27900   93.92500  -33.81600 1.000 32.44205  ?  539  GLY   B CA  1 
ATOM   18325 C  C   . GLY   B 1 539  ? 44.49700   94.39900  -34.58900 1.000 23.96701  ?  539  GLY   B C   1 
ATOM   18326 O  O   . GLY   B 1 539  ? 45.59800   93.85700  -34.48000 1.000 26.85671  ?  539  GLY   B O   1 
ATOM   18327 N  N   . ARG   B 1 540  ? 44.28000   95.44400  -35.39400 1.000 31.24646  ?  540  ARG   B N   1 
ATOM   18328 C  CA  . ARG   B 1 540  ? 45.35600   95.97100  -36.22700 1.000 29.26442  ?  540  ARG   B CA  1 
ATOM   18329 C  C   . ARG   B 1 540  ? 46.31100   96.86000  -35.44000 1.000 31.33036  ?  540  ARG   B C   1 
ATOM   18330 O  O   . ARG   B 1 540  ? 47.49300   96.95600  -35.78900 1.000 45.16037  ?  540  ARG   B O   1 
ATOM   18331 C  CB  . ARG   B 1 540  ? 44.77900   96.74400  -37.41600 1.000 24.62000  ?  540  ARG   B CB  1 
ATOM   18332 C  CG  . ARG   B 1 540  ? 45.81000   97.09800  -38.47700 1.000 18.14112  ?  540  ARG   B CG  1 
ATOM   18333 C  CD  . ARG   B 1 540  ? 45.19500   97.88700  -39.61500 1.000 16.59579  ?  540  ARG   B CD  1 
ATOM   18334 N  NE  . ARG   B 1 540  ? 44.35600   97.05700  -40.47100 1.000 27.04302  ?  540  ARG   B NE  1 
ATOM   18335 C  CZ  . ARG   B 1 540  ? 43.56300   97.53300  -41.42000 1.000 32.26461  ?  540  ARG   B CZ  1 
ATOM   18336 N  NH1 . ARG   B 1 540  ? 43.48200   98.83100  -41.66300 1.000 27.72281  ?  540  ARG   B NH1 1 
ATOM   18337 N  NH2 . ARG   B 1 540  ? 42.83000   96.68800  -42.13900 1.000 38.68094  ?  540  ARG   B NH2 1 
ATOM   18338 N  N   . GLY   B 1 541  ? 45.83200   97.50400  -34.38800 1.000 30.21310  ?  541  GLY   B N   1 
ATOM   18339 C  CA  . GLY   B 1 541  ? 46.65600   98.35700  -33.56600 1.000 23.75124  ?  541  GLY   B CA  1 
ATOM   18340 C  C   . GLY   B 1 541  ? 45.93400   99.64600  -33.25300 1.000 32.25795  ?  541  GLY   B C   1 
ATOM   18341 O  O   . GLY   B 1 541  ? 44.72200   99.76300  -33.42800 1.000 37.87946  ?  541  GLY   B O   1 
ATOM   18342 N  N   . TYR   B 1 542  ? 46.69500   100.63000 -32.78300 1.000 29.96072  ?  542  TYR   B N   1 
ATOM   18343 C  CA  . TYR   B 1 542  ? 46.13900   101.92000 -32.40400 1.000 29.83044  ?  542  TYR   B CA  1 
ATOM   18344 C  C   . TYR   B 1 542  ? 46.21800   102.88600 -33.57900 1.000 31.99449  ?  542  TYR   B C   1 
ATOM   18345 O  O   . TYR   B 1 542  ? 47.29300   103.09100 -34.15000 1.000 40.65131  ?  542  TYR   B O   1 
ATOM   18346 C  CB  . TYR   B 1 542  ? 46.88000   102.48900 -31.19500 1.000 31.97552  ?  542  TYR   B CB  1 
ATOM   18347 C  CG  . TYR   B 1 542  ? 46.78700   101.62400 -29.95800 1.000 37.92075  ?  542  TYR   B CG  1 
ATOM   18348 C  CD1 . TYR   B 1 542  ? 45.60700   101.54500 -29.23100 1.000 33.71160  ?  542  TYR   B CD1 1 
ATOM   18349 C  CD2 . TYR   B 1 542  ? 47.87900   100.88700 -29.51800 1.000 25.45168  ?  542  TYR   B CD2 1 
ATOM   18350 C  CE1 . TYR   B 1 542  ? 45.51600   100.75900 -28.10100 1.000 35.58068  ?  542  TYR   B CE1 1 
ATOM   18351 C  CE2 . TYR   B 1 542  ? 47.79700   100.09600 -28.38600 1.000 28.83016  ?  542  TYR   B CE2 1 
ATOM   18352 C  CZ  . TYR   B 1 542  ? 46.61100   100.03600 -27.68300 1.000 37.33125  ?  542  TYR   B CZ  1 
ATOM   18353 O  OH  . TYR   B 1 542  ? 46.51700   99.25200  -26.55600 1.000 35.04353  ?  542  TYR   B OH  1 
ATOM   18354 N  N   . LEU   B 1 543  ? 45.07700   103.47500 -33.93300 1.000 44.95082  ?  543  LEU   B N   1 
ATOM   18355 C  CA  . LEU   B 1 543  ? 45.02900   104.43300 -35.03100 1.000 36.00130  ?  543  LEU   B CA  1 
ATOM   18356 C  C   . LEU   B 1 543  ? 45.97600   105.59800 -34.77200 1.000 32.28564  ?  543  LEU   B C   1 
ATOM   18357 O  O   . LEU   B 1 543  ? 45.93400   106.22200 -33.70700 1.000 43.45966  ?  543  LEU   B O   1 
ATOM   18358 C  CB  . LEU   B 1 543  ? 43.60200   104.94900 -35.21600 1.000 37.48763  ?  543  LEU   B CB  1 
ATOM   18359 C  CG  . LEU   B 1 543  ? 43.40000   106.06900 -36.23800 1.000 38.95404  ?  543  LEU   B CG  1 
ATOM   18360 C  CD1 . LEU   B 1 543  ? 43.62200   105.54900 -37.64400 1.000 34.17568  ?  543  LEU   B CD1 1 
ATOM   18361 C  CD2 . LEU   B 1 543  ? 42.01100   106.66800 -36.10300 1.000 38.58495  ?  543  LEU   B CD2 1 
ATOM   18362 N  N   . ASN   B 1 544  ? 46.83800   105.87900 -35.74900 1.000 34.76767  ?  544  ASN   B N   1 
ATOM   18363 C  CA  . ASN   B 1 544  ? 47.77600   107.00400 -35.72000 1.000 38.15917  ?  544  ASN   B CA  1 
ATOM   18364 C  C   . ASN   B 1 544  ? 48.80000   106.90200 -34.58900 1.000 42.52873  ?  544  ASN   B C   1 
ATOM   18365 O  O   . ASN   B 1 544  ? 49.42100   107.90500 -34.22600 1.000 49.34531  ?  544  ASN   B O   1 
ATOM   18366 C  CB  . ASN   B 1 544  ? 47.03700   108.34600 -35.62600 1.000 36.26154  ?  544  ASN   B CB  1 
ATOM   18367 C  CG  . ASN   B 1 544  ? 46.06200   108.56000 -36.76700 1.000 42.31002  ?  544  ASN   B CG  1 
ATOM   18368 O  OD1 . ASN   B 1 544  ? 46.35200   108.23500 -37.92000 1.000 46.50609  ?  544  ASN   B OD1 1 
ATOM   18369 N  ND2 . ASN   B 1 544  ? 44.89700   109.11000 -36.45000 1.000 35.63743  ?  544  ASN   B ND2 1 
ATOM   18370 N  N   . ARG   B 1 545  ? 48.99800   105.71700 -34.01100 1.000 35.62909  ?  545  ARG   B N   1 
ATOM   18371 C  CA  . ARG   B 1 545  ? 50.00400   105.50000 -32.96800 1.000 35.22273  ?  545  ARG   B CA  1 
ATOM   18372 C  C   . ARG   B 1 545  ? 50.81200   104.25200 -33.30300 1.000 46.56271  ?  545  ARG   B C   1 
ATOM   18373 O  O   . ARG   B 1 545  ? 50.73600   103.23800 -32.59700 1.000 31.88061  ?  545  ARG   B O   1 
ATOM   18374 C  CB  . ARG   B 1 545  ? 49.36200   105.36800 -31.58600 1.000 36.65786  ?  545  ARG   B CB  1 
ATOM   18375 C  CG  . ARG   B 1 545  ? 48.30700   106.41100 -31.27000 1.000 44.19016  ?  545  ARG   B CG  1 
ATOM   18376 C  CD  . ARG   B 1 545  ? 48.75200   107.35700 -30.16900 1.000 35.76873  ?  545  ARG   B CD  1 
ATOM   18377 N  NE  . ARG   B 1 545  ? 48.24900   108.70600 -30.39700 1.000 83.68244  ?  545  ARG   B NE  1 
ATOM   18378 C  CZ  . ARG   B 1 545  ? 47.01600   109.10800 -30.11700 1.000 83.85536  ?  545  ARG   B CZ  1 
ATOM   18379 N  NH1 . ARG   B 1 545  ? 46.13300   108.29400 -29.56000 1.000 63.34817  ?  545  ARG   B NH1 1 
ATOM   18380 N  NH2 . ARG   B 1 545  ? 46.66000   110.35700 -30.40400 1.000 76.25010  ?  545  ARG   B NH2 1 
ATOM   18381 N  N   . PRO   B 1 546  ? 51.61000   104.29500 -34.37500 1.000 41.81360  ?  546  PRO   B N   1 
ATOM   18382 C  CA  . PRO   B 1 546  ? 52.37500   103.09800 -34.75200 1.000 29.56867  ?  546  PRO   B CA  1 
ATOM   18383 C  C   . PRO   B 1 546  ? 53.44100   102.71800 -33.74000 1.000 35.48514  ?  546  PRO   B C   1 
ATOM   18384 O  O   . PRO   B 1 546  ? 53.78600   101.53400 -33.64000 1.000 30.47475  ?  546  PRO   B O   1 
ATOM   18385 C  CB  . PRO   B 1 546  ? 52.99100   103.48900 -36.10200 1.000 19.49208  ?  546  PRO   B CB  1 
ATOM   18386 C  CG  . PRO   B 1 546  ? 53.07400   104.97100 -36.05200 1.000 41.99188  ?  546  PRO   B CG  1 
ATOM   18387 C  CD  . PRO   B 1 546  ? 51.87600   105.42900 -35.27600 1.000 42.19259  ?  546  PRO   B CD  1 
ATOM   18388 N  N   . GLU   B 1 547  ? 53.97300   103.67900 -32.98200 1.000 38.20102  ?  547  GLU   B N   1 
ATOM   18389 C  CA  . GLU   B 1 547  ? 54.98500   103.34600 -31.98500 1.000 39.24866  ?  547  GLU   B CA  1 
ATOM   18390 C  C   . GLU   B 1 547  ? 54.36500   102.68000 -30.76400 1.000 39.75709  ?  547  GLU   B C   1 
ATOM   18391 O  O   . GLU   B 1 547  ? 54.90600   101.69500 -30.25000 1.000 44.08089  ?  547  GLU   B O   1 
ATOM   18392 C  CB  . GLU   B 1 547  ? 55.76200   104.59800 -31.57900 1.000 43.48463  ?  547  GLU   B CB  1 
ATOM   18393 C  CG  . GLU   B 1 547  ? 56.92800   104.91600 -32.50400 1.000 43.41069  ?  547  GLU   B CG  1 
ATOM   18394 C  CD  . GLU   B 1 547  ? 57.00400   106.38800 -32.86000 1.000 58.14184  ?  547  GLU   B CD  1 
ATOM   18395 O  OE1 . GLU   B 1 547  ? 57.04300   107.22600 -31.93400 1.000 71.16577  ?  547  GLU   B OE1 1 
ATOM   18396 O  OE2 . GLU   B 1 547  ? 57.00500   106.71000 -34.06800 1.000 58.38426  -1 547  GLU   B OE2 1 
ATOM   18397 N  N   . LEU   B 1 548  ? 53.23100   103.19800 -30.28800 1.000 44.31909  ?  548  LEU   B N   1 
ATOM   18398 C  CA  . LEU   B 1 548  ? 52.52500   102.53700 -29.19600 1.000 38.02820  ?  548  LEU   B CA  1 
ATOM   18399 C  C   . LEU   B 1 548  ? 52.04800   101.15100 -29.61300 1.000 29.09865  ?  548  LEU   B C   1 
ATOM   18400 O  O   . LEU   B 1 548  ? 52.05700   100.21300 -28.80600 1.000 26.40501  ?  548  LEU   B O   1 
ATOM   18401 C  CB  . LEU   B 1 548  ? 51.34900   103.39700 -28.73700 1.000 37.47768  ?  548  LEU   B CB  1 
ATOM   18402 C  CG  . LEU   B 1 548  ? 50.44200   102.75000 -27.69200 1.000 36.60885  ?  548  LEU   B CG  1 
ATOM   18403 C  CD1 . LEU   B 1 548  ? 51.22100   102.47600 -26.41000 1.000 33.51411  ?  548  LEU   B CD1 1 
ATOM   18404 C  CD2 . LEU   B 1 548  ? 49.22200   103.62000 -27.42800 1.000 38.12027  ?  548  LEU   B CD2 1 
ATOM   18405 N  N   . THR   B 1 549  ? 51.63100   101.00300 -30.87400 1.000 26.40417  ?  549  THR   B N   1 
ATOM   18406 C  CA  . THR   B 1 549  ? 51.24900   99.68900  -31.37900 1.000 27.13350  ?  549  THR   B CA  1 
ATOM   18407 C  C   . THR   B 1 549  ? 52.39000   98.69300  -31.23600 1.000 32.28040  ?  549  THR   B C   1 
ATOM   18408 O  O   . THR   B 1 549  ? 52.17900   97.55000  -30.81200 1.000 35.04894  ?  549  THR   B O   1 
ATOM   18409 C  CB  . THR   B 1 549  ? 50.82100   99.79000  -32.84300 1.000 23.16620  ?  549  THR   B CB  1 
ATOM   18410 O  OG1 . THR   B 1 549  ? 49.80700   100.79500 -32.98100 1.000 30.30405  ?  549  THR   B OG1 1 
ATOM   18411 C  CG2 . THR   B 1 549  ? 50.28200   98.45200  -33.33100 1.000 18.02308  ?  549  THR   B CG2 1 
ATOM   18412 N  N   . ALA   B 1 550  ? 53.61100   99.11000  -31.57800 1.000 33.58019  ?  550  ALA   B N   1 
ATOM   18413 C  CA  . ALA   B 1 550  ? 54.75100   98.20900  -31.46600 1.000 25.87133  ?  550  ALA   B CA  1 
ATOM   18414 C  C   . ALA   B 1 550  ? 55.04400   97.84800  -30.01700 1.000 31.09128  ?  550  ALA   B C   1 
ATOM   18415 O  O   . ALA   B 1 550  ? 55.57000   96.76400  -29.74800 1.000 32.31381  ?  550  ALA   B O   1 
ATOM   18416 C  CB  . ALA   B 1 550  ? 55.98200   98.83400  -32.11600 1.000 22.40781  ?  550  ALA   B CB  1 
ATOM   18417 N  N   . GLU   B 1 551  ? 54.70800   98.73300  -29.07300 1.000 29.70455  ?  551  GLU   B N   1 
ATOM   18418 C  CA  . GLU   B 1 551  ? 54.95700   98.43300  -27.66600 1.000 31.49323  ?  551  GLU   B CA  1 
ATOM   18419 C  C   . GLU   B 1 551  ? 54.03900   97.32600  -27.16400 1.000 37.41249  ?  551  GLU   B C   1 
ATOM   18420 O  O   . GLU   B 1 551  ? 54.48500   96.42200  -26.44700 1.000 28.75710  ?  551  GLU   B O   1 
ATOM   18421 C  CB  . GLU   B 1 551  ? 54.78100   99.68800  -26.81300 1.000 38.77536  ?  551  GLU   B CB  1 
ATOM   18422 C  CG  . GLU   B 1 551  ? 55.70500   100.83900 -27.16900 1.000 58.71845  ?  551  GLU   B CG  1 
ATOM   18423 C  CD  . GLU   B 1 551  ? 55.68200   101.94400 -26.12900 1.000 82.67760  ?  551  GLU   B CD  1 
ATOM   18424 O  OE1 . GLU   B 1 551  ? 55.32500   101.66100 -24.96400 1.000 87.24948  ?  551  GLU   B OE1 1 
ATOM   18425 O  OE2 . GLU   B 1 551  ? 56.01300   103.09700 -26.47800 1.000 74.43370  -1 551  GLU   B OE2 1 
ATOM   18426 N  N   . LYS   B 1 552  ? 52.75500   97.38100  -27.52700 1.000 41.37251  ?  552  LYS   B N   1 
ATOM   18427 C  CA  . LYS   B 1 552  ? 51.76300   96.44300  -27.01400 1.000 33.87775  ?  552  LYS   B CA  1 
ATOM   18428 C  C   . LYS   B 1 552  ? 51.57400   95.23800  -27.92800 1.000 29.05294  ?  552  LYS   B C   1 
ATOM   18429 O  O   . LYS   B 1 552  ? 51.44200   94.10800  -27.44600 1.000 30.00949  ?  552  LYS   B O   1 
ATOM   18430 C  CB  . LYS   B 1 552  ? 50.42500   97.15800  -26.80700 1.000 33.18953  ?  552  LYS   B CB  1 
ATOM   18431 C  CG  . LYS   B 1 552  ? 50.54400   98.49000  -26.08000 1.000 35.38972  ?  552  LYS   B CG  1 
ATOM   18432 C  CD  . LYS   B 1 552  ? 50.80300   98.28300  -24.59600 1.000 54.18895  ?  552  LYS   B CD  1 
ATOM   18433 C  CE  . LYS   B 1 552  ? 49.55200   97.78200  -23.88800 1.000 57.47211  ?  552  LYS   B CE  1 
ATOM   18434 N  NZ  . LYS   B 1 552  ? 49.83200   97.28200  -22.50900 1.000 46.41535  ?  552  LYS   B NZ  1 
ATOM   18435 N  N   . PHE   B 1 553  ? 51.55400   95.45000  -29.23900 1.000 32.30074  ?  553  PHE   B N   1 
ATOM   18436 C  CA  . PHE   B 1 553  ? 51.47900   94.34700  -30.19300 1.000 36.38293  ?  553  PHE   B CA  1 
ATOM   18437 C  C   . PHE   B 1 553  ? 52.90900   93.97500  -30.56900 1.000 36.67087  ?  553  PHE   B C   1 
ATOM   18438 O  O   . PHE   B 1 553  ? 53.52100   94.60000  -31.43700 1.000 37.79768  ?  553  PHE   B O   1 
ATOM   18439 C  CB  . PHE   B 1 553  ? 50.64400   94.73600  -31.40700 1.000 27.37960  ?  553  PHE   B CB  1 
ATOM   18440 C  CG  . PHE   B 1 553  ? 49.21100   95.05100  -31.07800 1.000 28.92182  ?  553  PHE   B CG  1 
ATOM   18441 C  CD1 . PHE   B 1 553  ? 48.84000   96.32500  -30.67600 1.000 25.83336  ?  553  PHE   B CD1 1 
ATOM   18442 C  CD2 . PHE   B 1 553  ? 48.23400   94.06900  -31.16700 1.000 40.17003  ?  553  PHE   B CD2 1 
ATOM   18443 C  CE1 . PHE   B 1 553  ? 47.51800   96.61700  -30.37100 1.000 30.85010  ?  553  PHE   B CE1 1 
ATOM   18444 C  CE2 . PHE   B 1 553  ? 46.90900   94.35400  -30.86300 1.000 33.89628  ?  553  PHE   B CE2 1 
ATOM   18445 C  CZ  . PHE   B 1 553  ? 46.55200   95.63000  -30.46400 1.000 22.57099  ?  553  PHE   B CZ  1 
ATOM   18446 N  N   . ILE   B 1 554  ? 53.44700   92.96000  -29.90400 1.000 34.84574  ?  554  ILE   B N   1 
ATOM   18447 C  CA  . ILE   B 1 554  ? 54.84400   92.58700  -30.05600 1.000 29.27641  ?  554  ILE   B CA  1 
ATOM   18448 C  C   . ILE   B 1 554  ? 54.94500   91.29800  -30.85600 1.000 39.10351  ?  554  ILE   B C   1 
ATOM   18449 O  O   . ILE   B 1 554  ? 53.97600   90.55000  -31.02000 1.000 43.11615  ?  554  ILE   B O   1 
ATOM   18450 C  CB  . ILE   B 1 554  ? 55.54000   92.42800  -28.69200 1.000 21.62945  ?  554  ILE   B CB  1 
ATOM   18451 C  CG1 . ILE   B 1 554  ? 55.30600   91.02100  -28.14300 1.000 21.92221  ?  554  ILE   B CG1 1 
ATOM   18452 C  CG2 . ILE   B 1 554  ? 55.01900   93.45700  -27.71600 1.000 21.17511  ?  554  ILE   B CG2 1 
ATOM   18453 C  CD1 . ILE   B 1 554  ? 56.21900   90.65500  -27.00200 1.000 32.59345  ?  554  ILE   B CD1 1 
ATOM   18454 N  N   . VAL   B 1 555  ? 56.14800   91.04400  -31.36500 1.000 35.27662  ?  555  VAL   B N   1 
ATOM   18455 C  CA  . VAL   B 1 555  ? 56.52300   89.74800  -31.91600 1.000 39.52620  ?  555  VAL   B CA  1 
ATOM   18456 C  C   . VAL   B 1 555  ? 57.45400   89.09000  -30.91100 1.000 32.35811  ?  555  VAL   B C   1 
ATOM   18457 O  O   . VAL   B 1 555  ? 58.44300   89.69800  -30.48600 1.000 38.47517  ?  555  VAL   B O   1 
ATOM   18458 C  CB  . VAL   B 1 555  ? 57.19600   89.88100  -33.29300 1.000 27.26686  ?  555  VAL   B CB  1 
ATOM   18459 C  CG1 . VAL   B 1 555  ? 57.41100   88.51000  -33.90000 1.000 28.82152  ?  555  VAL   B CG1 1 
ATOM   18460 C  CG2 . VAL   B 1 555  ? 56.35900   90.73800  -34.22300 1.000 23.02353  ?  555  VAL   B CG2 1 
ATOM   18461 N  N   . HIS   B 1 556  ? 57.13600   87.86600  -30.51600 1.000 31.74678  ?  556  HIS   B N   1 
ATOM   18462 C  CA  . HIS   B 1 556  ? 57.92500   87.21600  -29.47700 1.000 49.44271  ?  556  HIS   B CA  1 
ATOM   18463 C  C   . HIS   B 1 556  ? 59.31900   86.88900  -30.00300 1.000 38.40080  ?  556  HIS   B C   1 
ATOM   18464 O  O   . HIS   B 1 556  ? 59.44900   86.33700  -31.10100 1.000 40.18414  ?  556  HIS   B O   1 
ATOM   18465 C  CB  . HIS   B 1 556  ? 57.24300   85.94900  -28.97700 1.000 48.11267  ?  556  HIS   B CB  1 
ATOM   18466 C  CG  . HIS   B 1 556  ? 57.83600   85.41700  -27.71100 1.000 46.36248  ?  556  HIS   B CG  1 
ATOM   18467 N  ND1 . HIS   B 1 556  ? 58.86700   84.50300  -27.70000 1.000 51.62569  ?  556  HIS   B ND1 1 
ATOM   18468 C  CD2 . HIS   B 1 556  ? 57.56200   85.69200  -26.41400 1.000 43.16625  ?  556  HIS   B CD2 1 
ATOM   18469 C  CE1 . HIS   B 1 556  ? 59.19300   84.22500  -26.45000 1.000 50.04082  ?  556  HIS   B CE1 1 
ATOM   18470 N  NE2 . HIS   B 1 556  ? 58.41600   84.93300  -25.65000 1.000 45.64873  ?  556  HIS   B NE2 1 
ATOM   18471 N  N   . PRO   B 1 557  ? 60.37900   87.20400  -29.25200 1.000 41.61221  ?  557  PRO   B N   1 
ATOM   18472 C  CA  . PRO   B 1 557  ? 61.74300   87.00700  -29.77100 1.000 37.72383  ?  557  PRO   B CA  1 
ATOM   18473 C  C   . PRO   B 1 557  ? 62.15500   85.55000  -29.92000 1.000 41.96178  ?  557  PRO   B C   1 
ATOM   18474 O  O   . PRO   B 1 557  ? 63.20500   85.29000  -30.52000 1.000 56.97586  ?  557  PRO   B O   1 
ATOM   18475 C  CB  . PRO   B 1 557  ? 62.61800   87.72200  -28.73500 1.000 43.44049  ?  557  PRO   B CB  1 
ATOM   18476 C  CG  . PRO   B 1 557  ? 61.80300   87.71700  -27.48300 1.000 56.60752  ?  557  PRO   B CG  1 
ATOM   18477 C  CD  . PRO   B 1 557  ? 60.37300   87.83700  -27.92200 1.000 46.77680  ?  557  PRO   B CD  1 
ATOM   18478 N  N   . GLN   B 1 558  ? 61.38300   84.59900  -29.39900 1.000 43.41763  ?  558  GLN   B N   1 
ATOM   18479 C  CA  . GLN   B 1 558  ? 61.68800   83.17900  -29.54600 1.000 36.81667  ?  558  GLN   B CA  1 
ATOM   18480 C  C   . GLN   B 1 558  ? 60.67700   82.42600  -30.39500 1.000 46.92520  ?  558  GLN   B C   1 
ATOM   18481 O  O   . GLN   B 1 558  ? 61.06800   81.58100  -31.20200 1.000 54.81087  ?  558  GLN   B O   1 
ATOM   18482 C  CB  . GLN   B 1 558  ? 61.78200   82.50800  -28.17000 1.000 41.80779  ?  558  GLN   B CB  1 
ATOM   18483 C  CG  . GLN   B 1 558  ? 63.09400   82.75000  -27.45200 1.000 50.12708  ?  558  GLN   B CG  1 
ATOM   18484 C  CD  . GLN   B 1 558  ? 62.99600   83.86200  -26.43100 1.000 56.50693  ?  558  GLN   B CD  1 
ATOM   18485 O  OE1 . GLN   B 1 558  ? 62.18900   83.79900  -25.50200 1.000 56.00470  ?  558  GLN   B OE1 1 
ATOM   18486 N  NE2 . GLN   B 1 558  ? 63.81600   84.89300  -26.59900 1.000 44.01177  ?  558  GLN   B NE2 1 
ATOM   18487 N  N   . THR   B 1 559  ? 59.38300   82.70600  -30.23000 1.000 47.55725  ?  559  THR   B N   1 
ATOM   18488 C  CA  . THR   B 1 559  ? 58.35200   82.02900  -31.00400 1.000 40.95821  ?  559  THR   B CA  1 
ATOM   18489 C  C   . THR   B 1 559  ? 57.97900   82.77500  -32.27700 1.000 42.53013  ?  559  THR   B C   1 
ATOM   18490 O  O   . THR   B 1 559  ? 57.39700   82.17200  -33.18500 1.000 46.90195  ?  559  THR   B O   1 
ATOM   18491 C  CB  . THR   B 1 559  ? 57.09300   81.82900  -30.15300 1.000 37.69938  ?  559  THR   B CB  1 
ATOM   18492 O  OG1 . THR   B 1 559  ? 56.35600   83.05700  -30.08600 1.000 43.70162  ?  559  THR   B OG1 1 
ATOM   18493 C  CG2 . THR   B 1 559  ? 57.47200   81.39700  -28.74800 1.000 26.86558  ?  559  THR   B CG2 1 
ATOM   18494 N  N   . GLY   B 1 560  ? 58.29500   84.06400  -32.36500 1.000 32.22650  ?  560  GLY   B N   1 
ATOM   18495 C  CA  . GLY   B 1 560  ? 57.96600   84.82600  -33.55000 1.000 35.66149  ?  560  GLY   B CA  1 
ATOM   18496 C  C   . GLY   B 1 560  ? 56.50100   85.14200  -33.72700 1.000 41.22448  ?  560  GLY   B C   1 
ATOM   18497 O  O   . GLY   B 1 560  ? 56.11800   85.65500  -34.78200 1.000 41.78435  ?  560  GLY   B O   1 
ATOM   18498 N  N   . GLU   B 1 561  ? 55.66900   84.85900  -32.72900 1.000 44.41507  ?  561  GLU   B N   1 
ATOM   18499 C  CA  . GLU   B 1 561  ? 54.23900   85.09800  -32.82400 1.000 35.41694  ?  561  GLU   B CA  1 
ATOM   18500 C  C   . GLU   B 1 561  ? 53.90600   86.52800  -32.42400 1.000 41.96601  ?  561  GLU   B C   1 
ATOM   18501 O  O   . GLU   B 1 561  ? 54.56500   87.12500  -31.56900 1.000 41.07885  ?  561  GLU   B O   1 
ATOM   18502 C  CB  . GLU   B 1 561  ? 53.46700   84.12600  -31.93400 1.000 34.93287  ?  561  GLU   B CB  1 
ATOM   18503 C  CG  . GLU   B 1 561  ? 53.73700   82.66900  -32.23000 1.000 38.04833  ?  561  GLU   B CG  1 
ATOM   18504 C  CD  . GLU   B 1 561  ? 53.02900   81.74400  -31.26300 1.000 60.29268  ?  561  GLU   B CD  1 
ATOM   18505 O  OE1 . GLU   B 1 561  ? 53.41900   81.71200  -30.07600 1.000 56.92699  ?  561  GLU   B OE1 1 
ATOM   18506 O  OE2 . GLU   B 1 561  ? 52.08200   81.05000  -31.69100 1.000 67.54985  -1 561  GLU   B OE2 1 
ATOM   18507 N  N   . ARG   B 1 562  ? 52.87100   87.07400  -33.05600 1.000 42.18411  ?  562  ARG   B N   1 
ATOM   18508 C  CA  . ARG   B 1 562  ? 52.36100   88.38500  -32.68300 1.000 33.20465  ?  562  ARG   B CA  1 
ATOM   18509 C  C   . ARG   B 1 562  ? 51.46500   88.22900  -31.46300 1.000 35.88679  ?  562  ARG   B C   1 
ATOM   18510 O  O   . ARG   B 1 562  ? 50.48100   87.48300  -31.50000 1.000 36.28982  ?  562  ARG   B O   1 
ATOM   18511 C  CB  . ARG   B 1 562  ? 51.60100   89.01800  -33.84500 1.000 22.72075  ?  562  ARG   B CB  1 
ATOM   18512 C  CG  . ARG   B 1 562  ? 51.22500   90.47200  -33.61400 1.000 30.66216  ?  562  ARG   B CG  1 
ATOM   18513 C  CD  . ARG   B 1 562  ? 50.71100   91.11100  -34.89100 1.000 36.06949  ?  562  ARG   B CD  1 
ATOM   18514 N  NE  . ARG   B 1 562  ? 50.34300   92.51000  -34.70600 1.000 39.11073  ?  562  ARG   B NE  1 
ATOM   18515 C  CZ  . ARG   B 1 562  ? 49.09400   92.95400  -34.67000 1.000 24.92146  ?  562  ARG   B CZ  1 
ATOM   18516 N  NH1 . ARG   B 1 562  ? 48.06600   92.12900  -34.77100 1.000 28.51705  ?  562  ARG   B NH1 1 
ATOM   18517 N  NH2 . ARG   B 1 562  ? 48.87200   94.25800  -34.53400 1.000 33.69351  ?  562  ARG   B NH2 1 
ATOM   18518 N  N   . MET   B 1 563  ? 51.81500   88.91200  -30.37800 1.000 28.19759  ?  563  MET   B N   1 
ATOM   18519 C  CA  . MET   B 1 563  ? 51.10300   88.78900  -29.11700 1.000 26.85891  ?  563  MET   B CA  1 
ATOM   18520 C  C   . MET   B 1 563  ? 50.75900   90.17200  -28.59000 1.000 36.59460  ?  563  MET   B C   1 
ATOM   18521 O  O   . MET   B 1 563  ? 51.43000   91.16000  -28.90700 1.000 29.83283  ?  563  MET   B O   1 
ATOM   18522 C  CB  . MET   B 1 563  ? 51.93900   88.03000  -28.07800 1.000 35.60452  ?  563  MET   B CB  1 
ATOM   18523 C  CG  . MET   B 1 563  ? 53.03800   87.17400  -28.68500 1.000 39.31272  ?  563  MET   B CG  1 
ATOM   18524 S  SD  . MET   B 1 563  ? 53.42900   85.72600  -27.69200 1.000 42.95452  ?  563  MET   B SD  1 
ATOM   18525 C  CE  . MET   B 1 563  ? 54.12700   86.53000  -26.26200 1.000 16.86535  ?  563  MET   B CE  1 
ATOM   18526 N  N   . TYR   B 1 564  ? 49.70600   90.23800  -27.78000 1.000 31.56635  ?  564  TYR   B N   1 
ATOM   18527 C  CA  . TYR   B 1 564  ? 49.29500   91.48400  -27.15200 1.000 27.48361  ?  564  TYR   B CA  1 
ATOM   18528 C  C   . TYR   B 1 564  ? 49.72000   91.49400  -25.68900 1.000 27.92107  ?  564  TYR   B C   1 
ATOM   18529 O  O   . TYR   B 1 564  ? 49.52400   90.50700  -24.97000 1.000 26.88524  ?  564  TYR   B O   1 
ATOM   18530 C  CB  . TYR   B 1 564  ? 47.78500   91.70200  -27.26400 1.000 27.04906  ?  564  TYR   B CB  1 
ATOM   18531 C  CG  . TYR   B 1 564  ? 47.35800   93.00300  -26.62900 1.000 25.80730  ?  564  TYR   B CG  1 
ATOM   18532 C  CD1 . TYR   B 1 564  ? 47.67400   94.21900  -27.22100 1.000 17.84804  ?  564  TYR   B CD1 1 
ATOM   18533 C  CD2 . TYR   B 1 564  ? 46.67000   93.02000  -25.42100 1.000 25.06927  ?  564  TYR   B CD2 1 
ATOM   18534 C  CE1 . TYR   B 1 564  ? 47.30300   95.41600  -26.63800 1.000 23.82627  ?  564  TYR   B CE1 1 
ATOM   18535 C  CE2 . TYR   B 1 564  ? 46.29400   94.21600  -24.82800 1.000 20.01241  ?  564  TYR   B CE2 1 
ATOM   18536 C  CZ  . TYR   B 1 564  ? 46.61400   95.41000  -25.44400 1.000 28.31777  ?  564  TYR   B CZ  1 
ATOM   18537 O  OH  . TYR   B 1 564  ? 46.24800   96.60600  -24.86800 1.000 36.22212  ?  564  TYR   B OH  1 
ATOM   18538 N  N   . ARG   B 1 565  ? 50.29900   92.61400  -25.26100 1.000 32.51716  ?  565  ARG   B N   1 
ATOM   18539 C  CA  . ARG   B 1 565  ? 50.76200   92.81800  -23.88800 1.000 37.06625  ?  565  ARG   B CA  1 
ATOM   18540 C  C   . ARG   B 1 565  ? 49.63300   93.47700  -23.10100 1.000 30.08950  ?  565  ARG   B C   1 
ATOM   18541 O  O   . ARG   B 1 565  ? 49.38200   94.67700  -23.24200 1.000 26.37098  ?  565  ARG   B O   1 
ATOM   18542 C  CB  . ARG   B 1 565  ? 52.02200   93.67700  -23.89100 1.000 36.59109  ?  565  ARG   B CB  1 
ATOM   18543 C  CG  . ARG   B 1 565  ? 52.94800   93.47800  -22.71500 1.000 48.56366  ?  565  ARG   B CG  1 
ATOM   18544 C  CD  . ARG   B 1 565  ? 54.29300   94.12800  -22.98900 1.000 52.07697  ?  565  ARG   B CD  1 
ATOM   18545 N  NE  . ARG   B 1 565  ? 55.38900   93.37800  -22.38900 1.000 57.21628  ?  565  ARG   B NE  1 
ATOM   18546 C  CZ  . ARG   B 1 565  ? 56.03500   93.74600  -21.29100 1.000 59.41279  ?  565  ARG   B CZ  1 
ATOM   18547 N  NH1 . ARG   B 1 565  ? 55.73700   94.86900  -20.65800 1.000 69.55725  ?  565  ARG   B NH1 1 
ATOM   18548 N  NH2 . ARG   B 1 565  ? 57.00200   92.96600  -20.81500 1.000 66.11353  ?  565  ARG   B NH2 1 
ATOM   18549 N  N   . THR   B 1 566  ? 48.95300   92.69400  -22.25700 1.000 32.70551  ?  566  THR   B N   1 
ATOM   18550 C  CA  . THR   B 1 566  ? 47.76500   93.19200  -21.56600 1.000 29.10177  ?  566  THR   B CA  1 
ATOM   18551 C  C   . THR   B 1 566  ? 48.10000   94.14700  -20.42600 1.000 31.83748  ?  566  THR   B C   1 
ATOM   18552 O  O   . THR   B 1 566  ? 47.33500   95.08100  -20.16200 1.000 35.54498  ?  566  THR   B O   1 
ATOM   18553 C  CB  . THR   B 1 566  ? 46.93400   92.02500  -21.01700 1.000 25.22268  ?  566  THR   B CB  1 
ATOM   18554 O  OG1 . THR   B 1 566  ? 47.73900   91.22000  -20.14800 1.000 29.75637  ?  566  THR   B OG1 1 
ATOM   18555 C  CG2 . THR   B 1 566  ? 46.41000   91.16100  -22.15300 1.000 35.16040  ?  566  THR   B CG2 1 
ATOM   18556 N  N   . GLY   B 1 567  ? 49.22600   93.94700  -19.74900 1.000 38.38472  ?  567  GLY   B N   1 
ATOM   18557 C  CA  . GLY   B 1 567  ? 49.46400   94.66700  -18.51600 1.000 35.52937  ?  567  GLY   B CA  1 
ATOM   18558 C  C   . GLY   B 1 567  ? 48.72100   94.10200  -17.33000 1.000 41.97669  ?  567  GLY   B C   1 
ATOM   18559 O  O   . GLY   B 1 567  ? 48.59200   94.78200  -16.30600 1.000 47.48488  ?  567  GLY   B O   1 
ATOM   18560 N  N   . ASP   B 1 568  ? 48.22900   92.87000  -17.43700 1.000 36.38257  ?  568  ASP   B N   1 
ATOM   18561 C  CA  . ASP   B 1 568  ? 47.43600   92.23000  -16.39900 1.000 34.76590  ?  568  ASP   B CA  1 
ATOM   18562 C  C   . ASP   B 1 568  ? 48.19000   91.03800  -15.82900 1.000 41.86769  ?  568  ASP   B C   1 
ATOM   18563 O  O   . ASP   B 1 568  ? 48.69800   90.20200  -16.58200 1.000 37.88250  ?  568  ASP   B O   1 
ATOM   18564 C  CB  . ASP   B 1 568  ? 46.08400   91.77400  -16.94900 1.000 37.82894  ?  568  ASP   B CB  1 
ATOM   18565 C  CG  . ASP   B 1 568  ? 45.27500   92.91400  -17.52000 1.000 49.51488  ?  568  ASP   B CG  1 
ATOM   18566 O  OD1 . ASP   B 1 568  ? 45.56900   94.07700  -17.17500 1.000 57.78120  ?  568  ASP   B OD1 1 
ATOM   18567 O  OD2 . ASP   B 1 568  ? 44.34500   92.64900  -18.30900 1.000 46.84181  -1 568  ASP   B OD2 1 
ATOM   18568 N  N   . ARG   B 1 569  ? 48.25500   90.96400  -14.50200 1.000 41.44509  ?  569  ARG   B N   1 
ATOM   18569 C  CA  . ARG   B 1 569  ? 48.80100   89.79600  -13.82900 1.000 29.84667  ?  569  ARG   B CA  1 
ATOM   18570 C  C   . ARG   B 1 569  ? 47.77400   88.67300  -13.84700 1.000 35.71923  ?  569  ARG   B C   1 
ATOM   18571 O  O   . ARG   B 1 569  ? 46.57800   88.90700  -13.65000 1.000 36.28412  ?  569  ARG   B O   1 
ATOM   18572 C  CB  . ARG   B 1 569  ? 49.17900   90.14100  -12.38800 1.000 42.45590  ?  569  ARG   B CB  1 
ATOM   18573 C  CG  . ARG   B 1 569  ? 50.26300   89.26300  -11.77800 1.000 54.96284  ?  569  ARG   B CG  1 
ATOM   18574 C  CD  . ARG   B 1 569  ? 50.41100   89.54700  -10.29000 1.000 44.96795  ?  569  ARG   B CD  1 
ATOM   18575 N  NE  . ARG   B 1 569  ? 49.88900   90.86500  -9.95000  1.000 67.68275  ?  569  ARG   B NE  1 
ATOM   18576 C  CZ  . ARG   B 1 569  ? 50.63700   91.94800  -9.78400  1.000 76.57503  ?  569  ARG   B CZ  1 
ATOM   18577 N  NH1 . ARG   B 1 569  ? 51.95600   91.90000  -9.88200  1.000 73.78258  ?  569  ARG   B NH1 1 
ATOM   18578 N  NH2 . ARG   B 1 569  ? 50.04600   93.11000  -9.51600  1.000 77.30183  ?  569  ARG   B NH2 1 
ATOM   18579 N  N   . ALA   B 1 570  ? 48.24000   87.45100  -14.08900 1.000 23.33456  ?  570  ALA   B N   1 
ATOM   18580 C  CA  . ALA   B 1 570  ? 47.32600   86.31900  -14.16000 1.000 31.15309  ?  570  ALA   B CA  1 
ATOM   18581 C  C   . ALA   B 1 570  ? 48.08800   85.03800  -13.85400 1.000 41.59698  ?  570  ALA   B C   1 
ATOM   18582 O  O   . ALA   B 1 570  ? 49.32000   85.02000  -13.78900 1.000 44.08510  ?  570  ALA   B O   1 
ATOM   18583 C  CB  . ALA   B 1 570  ? 46.64100   86.23600  -15.52600 1.000 40.92357  ?  570  ALA   B CB  1 
ATOM   18584 N  N   . ARG   B 1 571  ? 47.32900   83.95800  -13.67800 1.000 39.16233  ?  571  ARG   B N   1 
ATOM   18585 C  CA  . ARG   B 1 571  ? 47.89200   82.66800  -13.31100 1.000 48.69296  ?  571  ARG   B CA  1 
ATOM   18586 C  C   . ARG   B 1 571  ? 47.00000   81.56700  -13.86700 1.000 33.27498  ?  571  ARG   B C   1 
ATOM   18587 O  O   . ARG   B 1 571  ? 45.77400   81.69100  -13.85300 1.000 40.83268  ?  571  ARG   B O   1 
ATOM   18588 C  CB  . ARG   B 1 571  ? 48.02900   82.54900  -11.78600 1.000 46.39886  ?  571  ARG   B CB  1 
ATOM   18589 C  CG  . ARG   B 1 571  ? 47.87600   81.14100  -11.23000 1.000 51.49174  ?  571  ARG   B CG  1 
ATOM   18590 C  CD  . ARG   B 1 571  ? 47.39700   81.17300  -9.78500  1.000 55.33631  ?  571  ARG   B CD  1 
ATOM   18591 N  NE  . ARG   B 1 571  ? 48.24000   82.02200  -8.95200  1.000 66.28580  ?  571  ARG   B NE  1 
ATOM   18592 C  CZ  . ARG   B 1 571  ? 47.84200   82.60200  -7.82800  1.000 71.51117  ?  571  ARG   B CZ  1 
ATOM   18593 N  NH1 . ARG   B 1 571  ? 46.61300   82.44300  -7.36600  1.000 82.03551  ?  571  ARG   B NH1 1 
ATOM   18594 N  NH2 . ARG   B 1 571  ? 48.70000   83.36100  -7.15000  1.000 41.29976  ?  571  ARG   B NH2 1 
ATOM   18595 N  N   . PHE   B 1 572  ? 47.62200   80.50200  -14.36800 1.000 45.52966  ?  572  PHE   B N   1 
ATOM   18596 C  CA  . PHE   B 1 572  ? 46.88300   79.34400  -14.85400 1.000 36.39442  ?  572  PHE   B CA  1 
ATOM   18597 C  C   . PHE   B 1 572  ? 46.55700   78.40900  -13.69600 1.000 44.29400  ?  572  PHE   B C   1 
ATOM   18598 O  O   . PHE   B 1 572  ? 47.42200   78.10300  -12.86900 1.000 45.08550  ?  572  PHE   B O   1 
ATOM   18599 C  CB  . PHE   B 1 572  ? 47.69300   78.59400  -15.91300 1.000 40.10601  ?  572  PHE   B CB  1 
ATOM   18600 C  CG  . PHE   B 1 572  ? 47.24200   78.84900  -17.32300 1.000 37.50929  ?  572  PHE   B CG  1 
ATOM   18601 C  CD1 . PHE   B 1 572  ? 46.03700   78.34500  -17.78300 1.000 60.27411  ?  572  PHE   B CD1 1 
ATOM   18602 C  CD2 . PHE   B 1 572  ? 48.02700   79.58900  -18.19000 1.000 35.06795  ?  572  PHE   B CD2 1 
ATOM   18603 C  CE1 . PHE   B 1 572  ? 45.62400   78.57800  -19.08400 1.000 56.28643  ?  572  PHE   B CE1 1 
ATOM   18604 C  CE2 . PHE   B 1 572  ? 47.62100   79.82500  -19.48800 1.000 41.40170  ?  572  PHE   B CE2 1 
ATOM   18605 C  CZ  . PHE   B 1 572  ? 46.41700   79.32000  -19.93500 1.000 49.42563  ?  572  PHE   B CZ  1 
ATOM   18606 N  N   . LEU   B 1 573  ? 45.30200   77.95500  -13.63600 1.000 47.79631  ?  573  LEU   B N   1 
ATOM   18607 C  CA  . LEU   B 1 573  ? 44.91200   76.95600  -12.65400 1.000 36.89654  ?  573  LEU   B CA  1 
ATOM   18608 C  C   . LEU   B 1 573  ? 45.10600   75.55400  -13.22500 1.000 46.73773  ?  573  LEU   B C   1 
ATOM   18609 O  O   . LEU   B 1 573  ? 45.07900   75.36800  -14.44600 1.000 46.04772  ?  573  LEU   B O   1 
ATOM   18610 C  CB  . LEU   B 1 573  ? 43.45400   77.15000  -12.24800 1.000 36.76624  ?  573  LEU   B CB  1 
ATOM   18611 C  CG  . LEU   B 1 573  ? 43.11100   78.48600  -11.59100 1.000 35.57589  ?  573  LEU   B CG  1 
ATOM   18612 C  CD1 . LEU   B 1 573  ? 41.63700   78.54500  -11.23400 1.000 40.93891  ?  573  LEU   B CD1 1 
ATOM   18613 C  CD2 . LEU   B 1 573  ? 43.96800   78.70400  -10.35800 1.000 30.89284  ?  573  LEU   B CD2 1 
ATOM   18614 N  N   . PRO   B 1 574  ? 45.30600   74.54700  -12.36900 1.000 55.75838  ?  574  PRO   B N   1 
ATOM   18615 C  CA  . PRO   B 1 574  ? 45.58400   73.19300  -12.88200 1.000 53.79677  ?  574  PRO   B CA  1 
ATOM   18616 C  C   . PRO   B 1 574  ? 44.47500   72.60600  -13.74500 1.000 51.35668  ?  574  PRO   B C   1 
ATOM   18617 O  O   . PRO   B 1 574  ? 44.75000   71.68500  -14.52400 1.000 51.53506  ?  574  PRO   B O   1 
ATOM   18618 C  CB  . PRO   B 1 574  ? 45.79200   72.36700  -11.60300 1.000 36.91062  ?  574  PRO   B CB  1 
ATOM   18619 C  CG  . PRO   B 1 574  ? 45.19200   73.18600  -10.50100 1.000 45.62533  ?  574  PRO   B CG  1 
ATOM   18620 C  CD  . PRO   B 1 574  ? 45.40300   74.60900  -10.90200 1.000 43.65878  ?  574  PRO   B CD  1 
ATOM   18621 N  N   . ASP   B 1 575  ? 43.24100   73.10100  -13.64100 1.000 54.74625  ?  575  ASP   B N   1 
ATOM   18622 C  CA  . ASP   B 1 575  ? 42.13900   72.61400  -14.46400 1.000 60.59926  ?  575  ASP   B CA  1 
ATOM   18623 C  C   . ASP   B 1 575  ? 42.06200   73.29800  -15.82400 1.000 54.42267  ?  575  ASP   B C   1 
ATOM   18624 O  O   . ASP   B 1 575  ? 41.18800   72.95400  -16.62600 1.000 63.86936  ?  575  ASP   B O   1 
ATOM   18625 C  CB  . ASP   B 1 575  ? 40.80200   72.78000  -13.72700 1.000 44.92905  ?  575  ASP   B CB  1 
ATOM   18626 C  CG  . ASP   B 1 575  ? 40.50700   74.22400  -13.35500 1.000 50.89911  ?  575  ASP   B CG  1 
ATOM   18627 O  OD1 . ASP   B 1 575  ? 41.37600   75.09400  -13.57200 1.000 63.58535  ?  575  ASP   B OD1 1 
ATOM   18628 O  OD2 . ASP   B 1 575  ? 39.40000   74.48900  -12.83800 1.000 72.00944  -1 575  ASP   B OD2 1 
ATOM   18629 N  N   . GLY   B 1 576  ? 42.94600   74.25400  -16.10100 1.000 43.86626  ?  576  GLY   B N   1 
ATOM   18630 C  CA  . GLY   B 1 576  ? 42.96700   74.94700  -17.36900 1.000 44.51496  ?  576  GLY   B CA  1 
ATOM   18631 C  C   . GLY   B 1 576  ? 42.39300   76.34700  -17.34300 1.000 49.71029  ?  576  GLY   B C   1 
ATOM   18632 O  O   . GLY   B 1 576  ? 42.58000   77.09200  -18.31400 1.000 58.60501  ?  576  GLY   B O   1 
ATOM   18633 N  N   . ASN   B 1 577  ? 41.70500   76.72800  -16.27200 1.000 46.62159  ?  577  ASN   B N   1 
ATOM   18634 C  CA  . ASN   B 1 577  ? 41.10200   78.04900  -16.19200 1.000 41.92593  ?  577  ASN   B CA  1 
ATOM   18635 C  C   . ASN   B 1 577  ? 42.13000   79.09000  -15.77100 1.000 36.02215  ?  577  ASN   B C   1 
ATOM   18636 O  O   . ASN   B 1 577  ? 43.06300   78.80600  -15.01500 1.000 46.70054  ?  577  ASN   B O   1 
ATOM   18637 C  CB  . ASN   B 1 577  ? 39.93200   78.04700  -15.21000 1.000 47.36805  ?  577  ASN   B CB  1 
ATOM   18638 C  CG  . ASN   B 1 577  ? 38.76400   77.23000  -15.71000 1.000 36.49314  ?  577  ASN   B CG  1 
ATOM   18639 O  OD1 . ASN   B 1 577  ? 38.29300   77.42500  -16.82900 1.000 43.35489  ?  577  ASN   B OD1 1 
ATOM   18640 N  ND2 . ASN   B 1 577  ? 38.29400   76.30200  -14.88700 1.000 42.14521  ?  577  ASN   B ND2 1 
ATOM   18641 N  N   . ILE   B 1 578  ? 41.94800   80.30000  -16.26600 1.000 35.12000  ?  578  ILE   B N   1 
ATOM   18642 C  CA  . ILE   B 1 578  ? 42.85700   81.40200  -15.98000 1.000 36.65499  ?  578  ILE   B CA  1 
ATOM   18643 C  C   . ILE   B 1 578  ? 42.30200   82.20700  -14.81600 1.000 37.06612  ?  578  ILE   B C   1 
ATOM   18644 O  O   . ILE   B 1 578  ? 41.08900   82.41900  -14.71000 1.000 52.73982  ?  578  ILE   B O   1 
ATOM   18645 C  CB  . ILE   B 1 578  ? 43.05900   82.27900  -17.23000 1.000 36.94088  ?  578  ILE   B CB  1 
ATOM   18646 C  CG1 . ILE   B 1 578  ? 43.61400   81.44000  -18.38200 1.000 30.84209  ?  578  ILE   B CG1 1 
ATOM   18647 C  CG2 . ILE   B 1 578  ? 43.97900   83.45600  -16.92600 1.000 27.28651  ?  578  ILE   B CG2 1 
ATOM   18648 C  CD1 . ILE   B 1 578  ? 43.32200   82.01800  -19.74300 1.000 39.72826  ?  578  ILE   B CD1 1 
ATOM   18649 N  N   . GLU   B 1 579  ? 43.19200   82.64900  -13.93400 1.000 39.94232  ?  579  GLU   B N   1 
ATOM   18650 C  CA  . GLU   B 1 579  ? 42.83100   83.42100  -12.75600 1.000 37.08682  ?  579  GLU   B CA  1 
ATOM   18651 C  C   . GLU   B 1 579  ? 43.38700   84.83000  -12.89400 1.000 44.94392  ?  579  GLU   B C   1 
ATOM   18652 O  O   . GLU   B 1 579  ? 44.59000   85.00700  -13.11400 1.000 51.50750  ?  579  GLU   B O   1 
ATOM   18653 C  CB  . GLU   B 1 579  ? 43.37400   82.75900  -11.48600 1.000 37.80526  ?  579  GLU   B CB  1 
ATOM   18654 C  CG  . GLU   B 1 579  ? 42.43200   82.79700  -10.29700 1.000 54.14328  ?  579  GLU   B CG  1 
ATOM   18655 C  CD  . GLU   B 1 579  ? 42.94700   81.99000  -9.11600  1.000 68.22448  ?  579  GLU   B CD  1 
ATOM   18656 O  OE1 . GLU   B 1 579  ? 44.16800   82.02400  -8.84500  1.000 50.04682  ?  579  GLU   B OE1 1 
ATOM   18657 O  OE2 . GLU   B 1 579  ? 42.12500   81.31800  -8.45800  1.000 76.88380  -1 579  GLU   B OE2 1 
ATOM   18658 N  N   . PHE   B 1 580  ? 42.51400   85.82500  -12.77300 1.000 43.90876  ?  580  PHE   B N   1 
ATOM   18659 C  CA  . PHE   B 1 580  ? 42.94100   87.21600  -12.81400 1.000 33.09231  ?  580  PHE   B CA  1 
ATOM   18660 C  C   . PHE   B 1 580  ? 43.48400   87.63800  -11.45400 1.000 36.68336  ?  580  PHE   B C   1 
ATOM   18661 O  O   . PHE   B 1 580  ? 42.93000   87.28000  -10.41000 1.000 42.28817  ?  580  PHE   B O   1 
ATOM   18662 C  CB  . PHE   B 1 580  ? 41.77300   88.11200  -13.22000 1.000 29.26543  ?  580  PHE   B CB  1 
ATOM   18663 C  CG  . PHE   B 1 580  ? 42.14400   89.55100  -13.40300 1.000 24.08164  ?  580  PHE   B CG  1 
ATOM   18664 C  CD1 . PHE   B 1 580  ? 42.88400   89.95600  -14.50100 1.000 23.68536  ?  580  PHE   B CD1 1 
ATOM   18665 C  CD2 . PHE   B 1 580  ? 41.74200   90.50400  -12.48300 1.000 31.86405  ?  580  PHE   B CD2 1 
ATOM   18666 C  CE1 . PHE   B 1 580  ? 43.22300   91.28500  -14.67400 1.000 26.30206  ?  580  PHE   B CE1 1 
ATOM   18667 C  CE2 . PHE   B 1 580  ? 42.07500   91.83400  -12.65100 1.000 31.55387  ?  580  PHE   B CE2 1 
ATOM   18668 C  CZ  . PHE   B 1 580  ? 42.81800   92.22500  -13.74800 1.000 27.47453  ?  580  PHE   B CZ  1 
ATOM   18669 N  N   . LEU   B 1 581  ? 44.57800   88.40600  -11.47000 1.000 32.82038  ?  581  LEU   B N   1 
ATOM   18670 C  CA  . LEU   B 1 581  ? 45.25500   88.80200  -10.24100 1.000 34.51358  ?  581  LEU   B CA  1 
ATOM   18671 C  C   . LEU   B 1 581  ? 45.51700   90.30300  -10.14900 1.000 38.01421  ?  581  LEU   B C   1 
ATOM   18672 O  O   . LEU   B 1 581  ? 46.26300   90.73200  -9.26000  1.000 53.55040  ?  581  LEU   B O   1 
ATOM   18673 C  CB  . LEU   B 1 581  ? 46.57700   88.03800  -10.09000 1.000 31.46625  ?  581  LEU   B CB  1 
ATOM   18674 C  CG  . LEU   B 1 581  ? 46.47600   86.51900  -9.92800  1.000 37.14241  ?  581  LEU   B CG  1 
ATOM   18675 C  CD1 . LEU   B 1 581  ? 47.85600   85.89700  -9.80000  1.000 46.01953  ?  581  LEU   B CD1 1 
ATOM   18676 C  CD2 . LEU   B 1 581  ? 45.62100   86.16100  -8.72800  1.000 30.33691  ?  581  LEU   B CD2 1 
ATOM   18677 N  N   . GLY   B 1 582  ? 44.93800   91.10800  -11.02900 1.000 31.56896  ?  582  GLY   B N   1 
ATOM   18678 C  CA  . GLY   B 1 582  ? 45.06200   92.55200  -10.95500 1.000 41.07791  ?  582  GLY   B CA  1 
ATOM   18679 C  C   . GLY   B 1 582  ? 46.00600   93.10100  -12.01300 1.000 40.63788  ?  582  GLY   B C   1 
ATOM   18680 O  O   . GLY   B 1 582  ? 46.64100   92.36800  -12.77300 1.000 43.20611  ?  582  GLY   B O   1 
ATOM   18681 N  N   . ARG   B 1 583  ? 46.07900   94.43000  -12.04600 1.000 48.10326  ?  583  ARG   B N   1 
ATOM   18682 C  CA  . ARG   B 1 583  ? 46.97900   95.11900  -12.96100 1.000 47.31694  ?  583  ARG   B CA  1 
ATOM   18683 C  C   . ARG   B 1 583  ? 48.39800   95.11300  -12.41300 1.000 47.35670  ?  583  ARG   B C   1 
ATOM   18684 O  O   . ARG   B 1 583  ? 48.61600   95.26300  -11.20700 1.000 56.76709  ?  583  ARG   B O   1 
ATOM   18685 C  CB  . ARG   B 1 583  ? 46.52400   96.56100  -13.18700 1.000 41.94791  ?  583  ARG   B CB  1 
ATOM   18686 C  CG  . ARG   B 1 583  ? 45.13000   96.69900  -13.76000 1.000 39.80186  ?  583  ARG   B CG  1 
ATOM   18687 C  CD  . ARG   B 1 583  ? 45.13700   96.49800  -15.26200 1.000 32.28021  ?  583  ARG   B CD  1 
ATOM   18688 N  NE  . ARG   B 1 583  ? 45.96400   97.48200  -15.94900 1.000 59.42343  ?  583  ARG   B NE  1 
ATOM   18689 C  CZ  . ARG   B 1 583  ? 46.40000   97.35700  -17.19600 1.000 59.05275  ?  583  ARG   B CZ  1 
ATOM   18690 N  NH1 . ARG   B 1 583  ? 46.11600   96.28800  -17.92300 1.000 43.74815  ?  583  ARG   B NH1 1 
ATOM   18691 N  NH2 . ARG   B 1 583  ? 47.14100   98.32600  -17.72600 1.000 59.75215  ?  583  ARG   B NH2 1 
ATOM   18692 N  N   . LEU   B 1 584  ? 49.37000   94.94600  -13.31300 1.000 47.32991  ?  584  LEU   B N   1 
ATOM   18693 C  CA  . LEU   B 1 584  ? 50.76700   94.95100  -12.89800 1.000 39.67992  ?  584  LEU   B CA  1 
ATOM   18694 C  C   . LEU   B 1 584  ? 51.20900   96.31600  -12.39300 1.000 43.03504  ?  584  LEU   B C   1 
ATOM   18695 O  O   . LEU   B 1 584  ? 52.17500   96.39700  -11.62700 1.000 50.72284  ?  584  LEU   B O   1 
ATOM   18696 C  CB  . LEU   B 1 584  ? 51.66100   94.50400  -14.05400 1.000 37.01425  ?  584  LEU   B CB  1 
ATOM   18697 C  CG  . LEU   B 1 584  ? 51.60500   93.01600  -14.40400 1.000 40.11815  ?  584  LEU   B CG  1 
ATOM   18698 C  CD1 . LEU   B 1 584  ? 52.37900   92.73600  -15.68100 1.000 42.10889  ?  584  LEU   B CD1 1 
ATOM   18699 C  CD2 . LEU   B 1 584  ? 52.14000   92.17200  -13.25900 1.000 52.32842  ?  584  LEU   B CD2 1 
ATOM   18700 N  N   . ASP   B 1 585  ? 50.52300   97.38300  -12.79500 1.000 53.22085  ?  585  ASP   B N   1 
ATOM   18701 C  CA  . ASP   B 1 585  ? 50.84300   98.72300  -12.32600 1.000 57.79830  ?  585  ASP   B CA  1 
ATOM   18702 C  C   . ASP   B 1 585  ? 50.00500   99.16000  -11.13400 1.000 70.58928  ?  585  ASP   B C   1 
ATOM   18703 O  O   . ASP   B 1 585  ? 50.28800   100.21700 -10.56000 1.000 82.23419  ?  585  ASP   B O   1 
ATOM   18704 C  CB  . ASP   B 1 585  ? 50.67500   99.73900  -13.46300 1.000 55.50351  ?  585  ASP   B CB  1 
ATOM   18705 C  CG  . ASP   B 1 585  ? 49.21800   99.94100  -13.87200 1.000 82.24779  ?  585  ASP   B CG  1 
ATOM   18706 O  OD1 . ASP   B 1 585  ? 48.30500   99.83700  -13.02200 1.000 84.45775  ?  585  ASP   B OD1 1 
ATOM   18707 O  OD2 . ASP   B 1 585  ? 48.99100   100.22300 -15.06600 1.000 89.78979  -1 585  ASP   B OD2 1 
ATOM   18708 N  N   . ASN   B 1 586  ? 48.98500   98.38900  -10.75800 1.000 57.85508  ?  586  ASN   B N   1 
ATOM   18709 C  CA  . ASN   B 1 586  ? 48.05900   98.77400  -9.70300  1.000 78.13698  ?  586  ASN   B CA  1 
ATOM   18710 C  C   . ASN   B 1 586  ? 48.32200   98.04000  -8.39200  1.000 73.77405  ?  586  ASN   B C   1 
ATOM   18711 O  O   . ASN   B 1 586  ? 47.41700   97.92600  -7.55900  1.000 71.60347  ?  586  ASN   B O   1 
ATOM   18712 C  CB  . ASN   B 1 586  ? 46.61600   98.54400  -10.15600 1.000 57.63594  ?  586  ASN   B CB  1 
ATOM   18713 N  N   . LEU   B 1 587  ? 49.53700   97.53800  -8.19500  1.000 76.56092  ?  587  LEU   B N   1 
ATOM   18714 C  CA  . LEU   B 1 587  ? 49.91300   96.93000  -6.92700  1.000 79.55675  ?  587  LEU   B CA  1 
ATOM   18715 C  C   . LEU   B 1 587  ? 50.35500   98.02500  -5.96200  1.000 79.19592  ?  587  LEU   B C   1 
ATOM   18716 O  O   . LEU   B 1 587  ? 51.27500   98.79200  -6.26600  1.000 77.27444  ?  587  LEU   B O   1 
ATOM   18717 C  CB  . LEU   B 1 587  ? 51.02500   95.90300  -7.14100  1.000 79.63294  ?  587  LEU   B CB  1 
ATOM   18718 C  CG  . LEU   B 1 587  ? 51.08500   94.69100  -6.20800  1.000 73.65152  ?  587  LEU   B CG  1 
ATOM   18719 C  CD1 . LEU   B 1 587  ? 49.83800   93.83800  -6.33900  1.000 82.75456  ?  587  LEU   B CD1 1 
ATOM   18720 C  CD2 . LEU   B 1 587  ? 52.32200   93.86100  -6.51400  1.000 58.83878  ?  587  LEU   B CD2 1 
ATOM   18721 N  N   . VAL   B 1 588  ? 49.68900   98.11500  -4.81700  1.000 78.96723  ?  588  VAL   B N   1 
ATOM   18722 C  CA  . VAL   B 1 588  ? 50.04500   99.07700  -3.79200  1.000 65.59075  ?  588  VAL   B CA  1 
ATOM   18723 C  C   . VAL   B 1 588  ? 50.91300   98.38600  -2.74900  1.000 64.54635  ?  588  VAL   B C   1 
ATOM   18724 O  O   . VAL   B 1 588  ? 51.04500   97.16400  -2.72600  1.000 62.75313  ?  588  VAL   B O   1 
ATOM   18725 C  CB  . VAL   B 1 588  ? 48.79700   99.72500  -3.14000  1.000 53.16233  ?  588  VAL   B CB  1 
ATOM   18726 C  CG1 . VAL   B 1 588  ? 48.23400   100.83300 -4.02400  1.000 44.48247  ?  588  VAL   B CG1 1 
ATOM   18727 C  CG2 . VAL   B 1 588  ? 47.74700   98.67400  -2.84800  1.000 74.72167  ?  588  VAL   B CG2 1 
ATOM   18728 N  N   . LYS   B 1 589  ? 51.51600   99.17900  -1.86800  1.000 61.85629  ?  589  LYS   B N   1 
ATOM   18729 C  CA  . LYS   B 1 589  ? 52.38700   98.66000  -0.82500  1.000 62.37996  ?  589  LYS   B CA  1 
ATOM   18730 C  C   . LYS   B 1 589  ? 51.98400   99.26600  0.50900   1.000 65.76271  ?  589  LYS   B C   1 
ATOM   18731 O  O   . LYS   B 1 589  ? 51.84400   100.48800 0.62600   1.000 60.28208  ?  589  LYS   B O   1 
ATOM   18732 C  CB  . LYS   B 1 589  ? 53.86000   98.95800  -1.12900  1.000 65.84860  ?  589  LYS   B CB  1 
ATOM   18733 C  CG  . LYS   B 1 589  ? 54.68600   97.71100  -1.41200  1.000 76.30438  ?  589  LYS   B CG  1 
ATOM   18734 C  CD  . LYS   B 1 589  ? 55.82900   97.99700  -2.37200  1.000 86.47801  ?  589  LYS   B CD  1 
ATOM   18735 C  CE  . LYS   B 1 589  ? 56.54800   96.71600  -2.77100  1.000 62.61218  ?  589  LYS   B CE  1 
ATOM   18736 N  NZ  . LYS   B 1 589  ? 57.74700   96.99500  -3.60800  1.000 90.50198  ?  589  LYS   B NZ  1 
ATOM   18737 N  N   . ILE   B 1 590  ? 51.77900   98.40800  1.50300   1.000 54.33461  ?  590  ILE   B N   1 
ATOM   18738 C  CA  . ILE   B 1 590  ? 51.47700   98.82900  2.86400   1.000 44.22116  ?  590  ILE   B CA  1 
ATOM   18739 C  C   . ILE   B 1 590  ? 52.45900   98.12800  3.78800   1.000 46.72486  ?  590  ILE   B C   1 
ATOM   18740 O  O   . ILE   B 1 590  ? 52.48700   96.89300  3.84300   1.000 55.79674  ?  590  ILE   B O   1 
ATOM   18741 C  CB  . ILE   B 1 590  ? 50.03000   98.50800  3.26500   1.000 43.93750  ?  590  ILE   B CB  1 
ATOM   18742 C  CG1 . ILE   B 1 590  ? 49.05000   99.12900  2.26300   1.000 57.79028  ?  590  ILE   B CG1 1 
ATOM   18743 C  CG2 . ILE   B 1 590  ? 49.77100   98.97800  4.68500   1.000 52.32897  ?  590  ILE   B CG2 1 
ATOM   18744 C  CD1 . ILE   B 1 590  ? 47.81300   99.75100  2.88800   1.000 61.40300  ?  590  ILE   B CD1 1 
ATOM   18745 N  N   . ARG   B 1 591  ? 53.26700   98.91300  4.50100   1.000 49.72032  ?  591  ARG   B N   1 
ATOM   18746 C  CA  . ARG   B 1 591  ? 54.28900   98.38200  5.40400   1.000 59.94365  ?  591  ARG   B CA  1 
ATOM   18747 C  C   . ARG   B 1 591  ? 55.24600   97.44400  4.66800   1.000 62.17286  ?  591  ARG   B C   1 
ATOM   18748 O  O   . ARG   B 1 591  ? 55.65000   96.40300  5.19000   1.000 62.93149  ?  591  ARG   B O   1 
ATOM   18749 C  CB  . ARG   B 1 591  ? 53.65300   97.67800  6.60700   1.000 56.05064  ?  591  ARG   B CB  1 
ATOM   18750 C  CG  . ARG   B 1 591  ? 53.11700   98.61300  7.68700   1.000 54.23221  ?  591  ARG   B CG  1 
ATOM   18751 C  CD  . ARG   B 1 591  ? 52.42500   97.81700  8.77700   1.000 42.82104  ?  591  ARG   B CD  1 
ATOM   18752 N  NE  . ARG   B 1 591  ? 53.10400   96.54600  9.00000   1.000 51.76987  ?  591  ARG   B NE  1 
ATOM   18753 C  CZ  . ARG   B 1 591  ? 52.52300   95.46200  9.49500   1.000 59.94738  ?  591  ARG   B CZ  1 
ATOM   18754 N  NH1 . ARG   B 1 591  ? 51.24500   95.45900  9.83700   1.000 56.11492  ?  591  ARG   B NH1 1 
ATOM   18755 N  NH2 . ARG   B 1 591  ? 53.24300   94.35400  9.64900   1.000 70.34539  ?  591  ARG   B NH2 1 
ATOM   18756 N  N   . GLY   B 1 592  ? 55.61100   97.81300  3.44100   1.000 56.96291  ?  592  GLY   B N   1 
ATOM   18757 C  CA  . GLY   B 1 592  ? 56.51400   96.99700  2.65500   1.000 57.71611  ?  592  GLY   B CA  1 
ATOM   18758 C  C   . GLY   B 1 592  ? 55.92300   95.71700  2.11100   1.000 67.22195  ?  592  GLY   B C   1 
ATOM   18759 O  O   . GLY   B 1 592  ? 56.67400   94.84600  1.66300   1.000 52.32027  ?  592  GLY   B O   1 
ATOM   18760 N  N   . TYR   B 1 593  ? 54.60300   95.56800  2.14400   1.000 69.35534  ?  593  TYR   B N   1 
ATOM   18761 C  CA  . TYR   B 1 593  ? 53.92500   94.39900  1.60000   1.000 60.66145  ?  593  TYR   B CA  1 
ATOM   18762 C  C   . TYR   B 1 593  ? 53.17500   94.81600  0.34400   1.000 68.26441  ?  593  TYR   B C   1 
ATOM   18763 O  O   . TYR   B 1 593  ? 52.31800   95.70400  0.39600   1.000 61.60748  ?  593  TYR   B O   1 
ATOM   18764 C  CB  . TYR   B 1 593  ? 52.95700   93.79100  2.61400   1.000 45.70377  ?  593  TYR   B CB  1 
ATOM   18765 C  CG  . TYR   B 1 593  ? 53.60900   93.14800  3.81400   1.000 43.81997  ?  593  TYR   B CG  1 
ATOM   18766 C  CD1 . TYR   B 1 593  ? 54.00000   91.81600  3.78700   1.000 39.08489  ?  593  TYR   B CD1 1 
ATOM   18767 C  CD2 . TYR   B 1 593  ? 53.81400   93.86800  4.98300   1.000 50.15225  ?  593  TYR   B CD2 1 
ATOM   18768 C  CE1 . TYR   B 1 593  ? 54.58700   91.22200  4.88900   1.000 45.80473  ?  593  TYR   B CE1 1 
ATOM   18769 C  CE2 . TYR   B 1 593  ? 54.40100   93.28400  6.08800   1.000 45.56797  ?  593  TYR   B CE2 1 
ATOM   18770 C  CZ  . TYR   B 1 593  ? 54.78500   91.96200  6.03600   1.000 43.53621  ?  593  TYR   B CZ  1 
ATOM   18771 O  OH  . TYR   B 1 593  ? 55.36900   91.37800  7.13600   1.000 61.39129  ?  593  TYR   B OH  1 
ATOM   18772 N  N   . ARG   B 1 594  ? 53.49800   94.17700  -0.77600  1.000 69.19012  ?  594  ARG   B N   1 
ATOM   18773 C  CA  . ARG   B 1 594  ? 52.78200   94.41400  -2.02200  1.000 67.49306  ?  594  ARG   B CA  1 
ATOM   18774 C  C   . ARG   B 1 594  ? 51.43900   93.69600  -1.96600  1.000 63.65159  ?  594  ARG   B C   1 
ATOM   18775 O  O   . ARG   B 1 594  ? 51.39300   92.46500  -1.86100  1.000 83.05488  ?  594  ARG   B O   1 
ATOM   18776 C  CB  . ARG   B 1 594  ? 53.61300   93.93200  -3.20800  1.000 64.53248  ?  594  ARG   B CB  1 
ATOM   18777 N  N   . ILE   B 1 595  ? 50.34600   94.45800  -2.02600  1.000 50.74842  ?  595  ILE   B N   1 
ATOM   18778 C  CA  . ILE   B 1 595  ? 49.00800   93.91100  -1.84000  1.000 70.45283  ?  595  ILE   B CA  1 
ATOM   18779 C  C   . ILE   B 1 595  ? 48.09300   94.37800  -2.96400  1.000 81.08798  ?  595  ILE   B C   1 
ATOM   18780 O  O   . ILE   B 1 595  ? 48.28700   95.44800  -3.55000  1.000 81.25796  ?  595  ILE   B O   1 
ATOM   18781 C  CB  . ILE   B 1 595  ? 48.41400   94.30800  -0.46900  1.000 80.52192  ?  595  ILE   B CB  1 
ATOM   18782 C  CG1 . ILE   B 1 595  ? 48.25500   95.82700  -0.38100  1.000 77.02268  ?  595  ILE   B CG1 1 
ATOM   18783 C  CG2 . ILE   B 1 595  ? 49.29100   93.79300  0.66400   1.000 70.93507  ?  595  ILE   B CG2 1 
ATOM   18784 C  CD1 . ILE   B 1 595  ? 46.88300   96.27300  0.05800   1.000 56.23880  ?  595  ILE   B CD1 1 
ATOM   18785 N  N   . GLU   B 1 596  ? 47.08200   93.56300  -3.25900  1.000 78.00646  ?  596  GLU   B N   1 
ATOM   18786 C  CA  . GLU   B 1 596  ? 46.06200   93.91400  -4.24100  1.000 66.86640  ?  596  GLU   B CA  1 
ATOM   18787 C  C   . GLU   B 1 596  ? 44.72900   94.10900  -3.53500  1.000 58.45755  ?  596  GLU   B C   1 
ATOM   18788 O  O   . GLU   B 1 596  ? 44.14500   93.13000  -3.04500  1.000 67.34511  ?  596  GLU   B O   1 
ATOM   18789 C  CB  . GLU   B 1 596  ? 45.94300   92.83300  -5.31600  1.000 58.82004  ?  596  GLU   B CB  1 
ATOM   18790 C  CG  . GLU   B 1 596  ? 45.09000   93.24200  -6.50900  1.000 59.58679  ?  596  GLU   B CG  1 
ATOM   18791 C  CD  . GLU   B 1 596  ? 45.86600   94.04200  -7.53900  1.000 77.35475  ?  596  GLU   B CD  1 
ATOM   18792 O  OE1 . GLU   B 1 596  ? 47.01700   93.66500  -7.85000  1.000 78.43600  ?  596  GLU   B OE1 1 
ATOM   18793 O  OE2 . GLU   B 1 596  ? 45.32500   95.05000  -8.04100  1.000 72.59107  -1 596  GLU   B OE2 1 
ATOM   18794 N  N   . PRO   B 1 597  ? 44.21900   95.34200  -3.44600  1.000 58.60200  ?  597  PRO   B N   1 
ATOM   18795 C  CA  . PRO   B 1 597  ? 42.95300   95.59300  -2.73700  1.000 61.76102  ?  597  PRO   B CA  1 
ATOM   18796 C  C   . PRO   B 1 597  ? 41.78200   94.72500  -3.17900  1.000 60.09869  ?  597  PRO   B C   1 
ATOM   18797 O  O   . PRO   B 1 597  ? 40.81100   94.57100  -2.43100  1.000 63.38940  ?  597  PRO   B O   1 
ATOM   18798 C  CB  . PRO   B 1 597  ? 42.66900   97.07200  -3.04000  1.000 63.50689  ?  597  PRO   B CB  1 
ATOM   18799 C  CG  . PRO   B 1 597  ? 43.94800   97.64600  -3.61000  1.000 79.18418  ?  597  PRO   B CG  1 
ATOM   18800 C  CD  . PRO   B 1 597  ? 44.99000   96.57600  -3.66000  1.000 58.66432  ?  597  PRO   B CD  1 
ATOM   18801 N  N   . GLY   B 1 598  ? 41.84400   94.16800  -4.39000  1.000 65.84542  ?  598  GLY   B N   1 
ATOM   18802 C  CA  . GLY   B 1 598  ? 40.75300   93.33600  -4.86700  1.000 63.76414  ?  598  GLY   B CA  1 
ATOM   18803 C  C   . GLY   B 1 598  ? 40.61200   92.01900  -4.13400  1.000 53.53170  ?  598  GLY   B C   1 
ATOM   18804 O  O   . GLY   B 1 598  ? 39.52600   91.42900  -4.14300  1.000 57.88559  ?  598  GLY   B O   1 
ATOM   18805 N  N   . GLU   B 1 599  ? 41.68400   91.54300  -3.49800  1.000 42.86757  ?  599  GLU   B N   1 
ATOM   18806 C  CA  . GLU   B 1 599  ? 41.63100   90.26800  -2.79300  1.000 43.00519  ?  599  GLU   B CA  1 
ATOM   18807 C  C   . GLU   B 1 599  ? 40.84100   90.35700  -1.49400  1.000 57.03706  ?  599  GLU   B C   1 
ATOM   18808 O  O   . GLU   B 1 599  ? 40.46400   89.32000  -0.93900  1.000 56.02162  ?  599  GLU   B O   1 
ATOM   18809 C  CB  . GLU   B 1 599  ? 43.04900   89.77000  -2.50500  1.000 46.44664  ?  599  GLU   B CB  1 
ATOM   18810 C  CG  . GLU   B 1 599  ? 43.98900   89.82300  -3.70800  1.000 51.63394  ?  599  GLU   B CG  1 
ATOM   18811 C  CD  . GLU   B 1 599  ? 45.26500   89.02100  -3.50100  1.000 72.71165  ?  599  GLU   B CD  1 
ATOM   18812 O  OE1 . GLU   B 1 599  ? 45.55200   88.63900  -2.34600  1.000 82.48790  ?  599  GLU   B OE1 1 
ATOM   18813 O  OE2 . GLU   B 1 599  ? 45.97900   88.76500  -4.49500  1.000 76.56946  -1 599  GLU   B OE2 1 
ATOM   18814 N  N   . ILE   B 1 600  ? 40.59000   91.56800  -0.99900  1.000 57.47270  ?  600  ILE   B N   1 
ATOM   18815 C  CA  . ILE   B 1 600  ? 39.86900   91.72600  0.25800   1.000 53.82037  ?  600  ILE   B CA  1 
ATOM   18816 C  C   . ILE   B 1 600  ? 38.36600   91.71400  0.02500   1.000 58.80220  ?  600  ILE   B C   1 
ATOM   18817 O  O   . ILE   B 1 600  ? 37.59900   91.31800  0.91100   1.000 68.42190  ?  600  ILE   B O   1 
ATOM   18818 C  CB  . ILE   B 1 600  ? 40.31300   93.02500  0.94600   1.000 58.63348  ?  600  ILE   B CB  1 
ATOM   18819 C  CG1 . ILE   B 1 600  ? 41.79900   93.26900  0.67700   1.000 53.08836  ?  600  ILE   B CG1 1 
ATOM   18820 C  CG2 . ILE   B 1 600  ? 40.00200   92.97900  2.44600   1.000 58.05928  ?  600  ILE   B CG2 1 
ATOM   18821 C  CD1 . ILE   B 1 600  ? 42.33500   94.52000  1.32300   1.000 54.56886  ?  600  ILE   B CD1 1 
ATOM   18822 N  N   . GLU   B 1 601  ? 37.93000   92.13600  -1.16100  1.000 51.12289  ?  601  GLU   B N   1 
ATOM   18823 C  CA  . GLU   B 1 601  ? 36.50200   92.28400  -1.42400  1.000 45.23762  ?  601  GLU   B CA  1 
ATOM   18824 C  C   . GLU   B 1 601  ? 35.70500   90.99100  -1.27100  1.000 60.75599  ?  601  GLU   B C   1 
ATOM   18825 O  O   . GLU   B 1 601  ? 34.59900   91.05300  -0.70600  1.000 54.08575  ?  601  GLU   B O   1 
ATOM   18826 C  CB  . GLU   B 1 601  ? 36.30700   92.88600  -2.82100  1.000 56.60292  ?  601  GLU   B CB  1 
ATOM   18827 C  CG  . GLU   B 1 601  ? 37.24800   94.03900  -3.14100  1.000 65.60963  ?  601  GLU   B CG  1 
ATOM   18828 C  CD  . GLU   B 1 601  ? 36.63800   95.04400  -4.10200  1.000 70.00847  ?  601  GLU   B CD  1 
ATOM   18829 O  OE1 . GLU   B 1 601  ? 35.42100   94.95100  -4.37400  1.000 78.01306  ?  601  GLU   B OE1 1 
ATOM   18830 O  OE2 . GLU   B 1 601  ? 37.37300   95.93200  -4.58100  1.000 62.52287  -1 601  GLU   B OE2 1 
ATOM   18831 N  N   . PRO   B 1 602  ? 36.16700   89.82000  -1.73500  1.000 58.02746  ?  602  PRO   B N   1 
ATOM   18832 C  CA  . PRO   B 1 602  ? 35.36200   88.60400  -1.52400  1.000 48.21903  ?  602  PRO   B CA  1 
ATOM   18833 C  C   . PRO   B 1 602  ? 35.09300   88.29500  -0.06300  1.000 60.61226  ?  602  PRO   B C   1 
ATOM   18834 O  O   . PRO   B 1 602  ? 33.99500   87.83300  0.27300   1.000 67.06088  ?  602  PRO   B O   1 
ATOM   18835 C  CB  . PRO   B 1 602  ? 36.20600   87.50300  -2.18700  1.000 42.28944  ?  602  PRO   B CB  1 
ATOM   18836 C  CG  . PRO   B 1 602  ? 37.56600   88.08500  -2.33700  1.000 46.06449  ?  602  PRO   B CG  1 
ATOM   18837 C  CD  . PRO   B 1 602  ? 37.33900   89.53600  -2.58000  1.000 51.37157  ?  602  PRO   B CD  1 
ATOM   18838 N  N   . PHE   B 1 603  ? 36.06200   88.54000  0.82100   1.000 55.40255  ?  603  PHE   B N   1 
ATOM   18839 C  CA  . PHE   B 1 603  ? 35.86900   88.20300  2.22700   1.000 61.19110  ?  603  PHE   B CA  1 
ATOM   18840 C  C   . PHE   B 1 603  ? 34.88300   89.14300  2.90800   1.000 54.21213  ?  603  PHE   B C   1 
ATOM   18841 O  O   . PHE   B 1 603  ? 34.14500   88.71900  3.80300   1.000 63.29106  ?  603  PHE   B O   1 
ATOM   18842 C  CB  . PHE   B 1 603  ? 37.20900   88.21700  2.95500   1.000 52.17718  ?  603  PHE   B CB  1 
ATOM   18843 C  CG  . PHE   B 1 603  ? 38.20100   87.24200  2.40300   1.000 56.16983  ?  603  PHE   B CG  1 
ATOM   18844 C  CD1 . PHE   B 1 603  ? 38.11700   85.89600  2.71600   1.000 64.49479  ?  603  PHE   B CD1 1 
ATOM   18845 C  CD2 . PHE   B 1 603  ? 39.21600   87.66800  1.56600   1.000 67.65557  ?  603  PHE   B CD2 1 
ATOM   18846 C  CE1 . PHE   B 1 603  ? 39.02900   84.99400  2.20700   1.000 62.50342  ?  603  PHE   B CE1 1 
ATOM   18847 C  CE2 . PHE   B 1 603  ? 40.13200   86.77100  1.05400   1.000 62.56410  ?  603  PHE   B CE2 1 
ATOM   18848 C  CZ  . PHE   B 1 603  ? 40.03800   85.43200  1.37600   1.000 56.92699  ?  603  PHE   B CZ  1 
ATOM   18849 N  N   . LEU   B 1 604  ? 34.85700   90.41600  2.51000   1.000 52.61726  ?  604  LEU   B N   1 
ATOM   18850 C  CA  . LEU   B 1 604  ? 33.85800   91.32900  3.05200   1.000 55.84288  ?  604  LEU   B CA  1 
ATOM   18851 C  C   . LEU   B 1 604  ? 32.45200   90.93200  2.62200   1.000 61.18755  ?  604  LEU   B C   1 
ATOM   18852 O  O   . LEU   B 1 604  ? 31.50100   91.09100  3.39400   1.000 68.15506  ?  604  LEU   B O   1 
ATOM   18853 C  CB  . LEU   B 1 604  ? 34.16200   92.76400  2.62100   1.000 56.51490  ?  604  LEU   B CB  1 
ATOM   18854 C  CG  . LEU   B 1 604  ? 34.70100   93.69300  3.71000   1.000 54.48907  ?  604  LEU   B CG  1 
ATOM   18855 C  CD1 . LEU   B 1 604  ? 34.66100   95.14800  3.26100   1.000 40.92864  ?  604  LEU   B CD1 1 
ATOM   18856 C  CD2 . LEU   B 1 604  ? 33.92200   93.50900  5.00200   1.000 67.27905  ?  604  LEU   B CD2 1 
ATOM   18857 N  N   . MET   B 1 605  ? 32.30400   90.40500  1.40400   1.000 62.97724  ?  605  MET   B N   1 
ATOM   18858 C  CA  . MET   B 1 605  ? 30.99100   89.97900  0.93400   1.000 63.94504  ?  605  MET   B CA  1 
ATOM   18859 C  C   . MET   B 1 605  ? 30.50100   88.73900  1.67100   1.000 56.66325  ?  605  MET   B C   1 
ATOM   18860 O  O   . MET   B 1 605  ? 29.28900   88.56200  1.84100   1.000 56.24345  ?  605  MET   B O   1 
ATOM   18861 C  CB  . MET   B 1 605  ? 31.03400   89.70900  -0.56900  1.000 49.81541  ?  605  MET   B CB  1 
ATOM   18862 C  CG  . MET   B 1 605  ? 30.77600   90.92200  -1.43900  1.000 45.77093  ?  605  MET   B CG  1 
ATOM   18863 S  SD  . MET   B 1 605  ? 29.63000   90.53400  -2.77000  1.000 75.41027  ?  605  MET   B SD  1 
ATOM   18864 C  CE  . MET   B 1 605  ? 29.70400   92.03700  -3.74300  1.000 73.77593  ?  605  MET   B CE  1 
ATOM   18865 N  N   . ASN   B 1 606  ? 31.42000   87.87500  2.11500   1.000 46.62756  ?  606  ASN   B N   1 
ATOM   18866 C  CA  . ASN   B 1 606  ? 31.02600   86.66500  2.82800   1.000 56.82752  ?  606  ASN   B CA  1 
ATOM   18867 C  C   . ASN   B 1 606  ? 30.29700   86.97100  4.12900   1.000 73.32314  ?  606  ASN   B C   1 
ATOM   18868 O  O   . ASN   B 1 606  ? 29.64600   86.07900  4.68600   1.000 78.74299  ?  606  ASN   B O   1 
ATOM   18869 C  CB  . ASN   B 1 606  ? 32.25100   85.79700  3.11500   1.000 54.62794  ?  606  ASN   B CB  1 
ATOM   18870 C  CG  . ASN   B 1 606  ? 32.90400   85.27900  1.85100   1.000 83.81303  ?  606  ASN   B CG  1 
ATOM   18871 O  OD1 . ASN   B 1 606  ? 32.27200   85.21100  0.79600   1.000 81.47155  ?  606  ASN   B OD1 1 
ATOM   18872 N  ND2 . ASN   B 1 606  ? 34.17600   84.90800  1.95100   1.000 86.35306  ?  606  ASN   B ND2 1 
ATOM   18873 N  N   . HIS   B 1 607  ? 30.39800   88.20000  4.62200   1.000 66.08057  ?  607  HIS   B N   1 
ATOM   18874 C  CA  . HIS   B 1 607  ? 29.65300   88.59100  5.80600   1.000 63.79153  ?  607  HIS   B CA  1 
ATOM   18875 C  C   . HIS   B 1 607  ? 28.15500   88.45600  5.54200   1.000 75.00211  ?  607  HIS   B C   1 
ATOM   18876 O  O   . HIS   B 1 607  ? 27.67700   88.83300  4.46400   1.000 70.37988  ?  607  HIS   B O   1 
ATOM   18877 C  CB  . HIS   B 1 607  ? 29.99800   90.02700  6.19900   1.000 64.77329  ?  607  HIS   B CB  1 
ATOM   18878 C  CG  . HIS   B 1 607  ? 29.48000   90.43200  7.54400   1.000 74.87556  ?  607  HIS   B CG  1 
ATOM   18879 N  ND1 . HIS   B 1 607  ? 28.16600   90.78700  7.76000   1.000 70.25853  ?  607  HIS   B ND1 1 
ATOM   18880 C  CD2 . HIS   B 1 607  ? 30.10400   90.55300  8.74000   1.000 67.32095  ?  607  HIS   B CD2 1 
ATOM   18881 C  CE1 . HIS   B 1 607  ? 28.00000   91.10200  9.03200   1.000 69.07596  ?  607  HIS   B CE1 1 
ATOM   18882 N  NE2 . HIS   B 1 607  ? 29.16100   90.96900  9.64800   1.000 68.49752  ?  607  HIS   B NE2 1 
ATOM   18883 N  N   . PRO   B 1 608  ? 27.39200   87.91000  6.49100   1.000 72.08689  ?  608  PRO   B N   1 
ATOM   18884 C  CA  . PRO   B 1 608  ? 25.96800   87.65400  6.22800   1.000 67.82535  ?  608  PRO   B CA  1 
ATOM   18885 C  C   . PRO   B 1 608  ? 25.16700   88.90400  5.92100   1.000 63.35127  ?  608  PRO   B C   1 
ATOM   18886 O  O   . PRO   B 1 608  ? 24.16000   88.82000  5.20800   1.000 58.99773  ?  608  PRO   B O   1 
ATOM   18887 C  CB  . PRO   B 1 608  ? 25.49400   86.98200  7.52400   1.000 48.26657  ?  608  PRO   B CB  1 
ATOM   18888 C  CG  . PRO   B 1 608  ? 26.73100   86.38800  8.11000   1.000 47.95771  ?  608  PRO   B CG  1 
ATOM   18889 C  CD  . PRO   B 1 608  ? 27.82400   87.35800  7.78500   1.000 59.84850  ?  608  PRO   B CD  1 
ATOM   18890 N  N   . LEU   B 1 609  ? 25.58100   90.06300  6.42800   1.000 67.59549  ?  609  LEU   B N   1 
ATOM   18891 C  CA  . LEU   B 1 609  ? 24.84800   91.30100  6.20500   1.000 72.97317  ?  609  LEU   B CA  1 
ATOM   18892 C  C   . LEU   B 1 609  ? 25.39800   92.12900  5.05300   1.000 66.43926  ?  609  LEU   B C   1 
ATOM   18893 O  O   . LEU   B 1 609  ? 24.74000   93.08800  4.63400   1.000 60.97008  ?  609  LEU   B O   1 
ATOM   18894 C  CB  . LEU   B 1 609  ? 24.84500   92.15100  7.48000   1.000 72.11958  ?  609  LEU   B CB  1 
ATOM   18895 C  CG  . LEU   B 1 609  ? 23.65500   91.96600  8.42100   1.000 64.14364  ?  609  LEU   B CG  1 
ATOM   18896 C  CD1 . LEU   B 1 609  ? 23.82400   90.71100  9.26300   1.000 67.28748  ?  609  LEU   B CD1 1 
ATOM   18897 C  CD2 . LEU   B 1 609  ? 23.48800   93.19200  9.30300   1.000 69.23818  ?  609  LEU   B CD2 1 
ATOM   18898 N  N   . ILE   B 1 610  ? 26.57600   91.79400  4.53600   1.000 67.64883  ?  610  ILE   B N   1 
ATOM   18899 C  CA  . ILE   B 1 610  ? 27.19100   92.54800  3.45000   1.000 76.02570  ?  610  ILE   B CA  1 
ATOM   18900 C  C   . ILE   B 1 610  ? 26.78300   91.91400  2.12900   1.000 75.89783  ?  610  ILE   B C   1 
ATOM   18901 O  O   . ILE   B 1 610  ? 27.03900   90.72800  1.89300   1.000 72.10214  ?  610  ILE   B O   1 
ATOM   18902 C  CB  . ILE   B 1 610  ? 28.72000   92.58800  3.59000   1.000 84.89176  ?  610  ILE   B CB  1 
ATOM   18903 C  CG1 . ILE   B 1 610  ? 29.12600   93.12300  4.96400   1.000 69.29425  ?  610  ILE   B CG1 1 
ATOM   18904 C  CG2 . ILE   B 1 610  ? 29.33600   93.43000  2.47800   1.000 73.00558  ?  610  ILE   B CG2 1 
ATOM   18905 C  CD1 . ILE   B 1 610  ? 28.86400   94.58500  5.14800   1.000 66.81275  ?  610  ILE   B CD1 1 
ATOM   18906 N  N   . GLU   B 1 611  ? 26.14600   92.70500  1.26700   1.000 76.89916  ?  611  GLU   B N   1 
ATOM   18907 C  CA  . GLU   B 1 611  ? 25.72900   92.25000  -0.05300  1.000 89.32959  ?  611  GLU   B CA  1 
ATOM   18908 C  C   . GLU   B 1 611  ? 26.63500   92.75500  -1.16500  1.000 89.26719  ?  611  GLU   B C   1 
ATOM   18909 O  O   . GLU   B 1 611  ? 26.93900   92.00400  -2.09600  1.000 75.76133  ?  611  GLU   B O   1 
ATOM   18910 C  CB  . GLU   B 1 611  ? 24.28600   92.68800  -0.33100  1.000 82.90163  ?  611  GLU   B CB  1 
ATOM   18911 C  CG  . GLU   B 1 611  ? 23.93100   94.05400  0.23300   1.000 91.57011  ?  611  GLU   B CG  1 
ATOM   18912 C  CD  . GLU   B 1 611  ? 22.43800   94.32300  0.22000   1.000 109.97505 ?  611  GLU   B CD  1 
ATOM   18913 O  OE1 . GLU   B 1 611  ? 21.81500   94.18500  -0.85500  1.000 112.01111 ?  611  GLU   B OE1 1 
ATOM   18914 O  OE2 . GLU   B 1 611  ? 21.88600   94.67300  1.28500   1.000 101.82082 -1 611  GLU   B OE2 1 
ATOM   18915 N  N   . LEU   B 1 612  ? 27.07600   94.01000  -1.08600  1.000 90.07624  ?  612  LEU   B N   1 
ATOM   18916 C  CA  . LEU   B 1 612  ? 27.94400   94.62000  -2.08400  1.000 79.87060  ?  612  LEU   B CA  1 
ATOM   18917 C  C   . LEU   B 1 612  ? 29.13000   95.27400  -1.38900  1.000 83.99655  ?  612  LEU   B C   1 
ATOM   18918 O  O   . LEU   B 1 612  ? 28.98200   95.85400  -0.30900  1.000 81.83380  ?  612  LEU   B O   1 
ATOM   18919 C  CB  . LEU   B 1 612  ? 27.18200   95.65900  -2.92200  1.000 58.96568  ?  612  LEU   B CB  1 
ATOM   18920 C  CG  . LEU   B 1 612  ? 26.69900   95.27100  -4.32600  1.000 61.91714  ?  612  LEU   B CG  1 
ATOM   18921 C  CD1 . LEU   B 1 612  ? 25.99500   93.92300  -4.35300  1.000 56.32945  ?  612  LEU   B CD1 1 
ATOM   18922 C  CD2 . LEU   B 1 612  ? 25.78900   96.35200  -4.88800  1.000 63.86169  ?  612  LEU   B CD2 1 
ATOM   18923 N  N   . THR   B 1 613  ? 30.30700   95.18200  -2.00800  1.000 79.72027  ?  613  THR   B N   1 
ATOM   18924 C  CA  . THR   B 1 613  ? 31.50900   95.75100  -1.41300  1.000 75.95587  ?  613  THR   B CA  1 
ATOM   18925 C  C   . THR   B 1 613  ? 32.44400   96.26300  -2.50100  1.000 70.74040  ?  613  THR   B C   1 
ATOM   18926 O  O   . THR   B 1 613  ? 32.40100   95.81100  -3.64900  1.000 77.57772  ?  613  THR   B O   1 
ATOM   18927 C  CB  . THR   B 1 613  ? 32.24400   94.73300  -0.52900  1.000 69.57621  ?  613  THR   B CB  1 
ATOM   18928 O  OG1 . THR   B 1 613  ? 33.04400   95.42600  0.43600   1.000 79.26206  ?  613  THR   B OG1 1 
ATOM   18929 C  CG2 . THR   B 1 613  ? 33.13900   93.83000  -1.36400  1.000 58.02082  ?  613  THR   B CG2 1 
ATOM   18930 N  N   . THR   B 1 614  ? 33.28000   97.22800  -2.12100  1.000 69.41692  ?  614  THR   B N   1 
ATOM   18931 C  CA  . THR   B 1 614  ? 34.37000   97.70100  -2.96100  1.000 69.80792  ?  614  THR   B CA  1 
ATOM   18932 C  C   . THR   B 1 614  ? 35.44100   98.29700  -2.05400  1.000 69.11113  ?  614  THR   B C   1 
ATOM   18933 O  O   . THR   B 1 614  ? 35.13000   98.98100  -1.07300  1.000 63.15356  ?  614  THR   B O   1 
ATOM   18934 C  CB  . THR   B 1 614  ? 33.88200   98.70900  -4.02100  1.000 70.62085  ?  614  THR   B CB  1 
ATOM   18935 O  OG1 . THR   B 1 614  ? 34.77900   98.70800  -5.13900  1.000 75.50840  ?  614  THR   B OG1 1 
ATOM   18936 C  CG2 . THR   B 1 614  ? 33.76400   100.11900 -3.46300  1.000 67.32368  ?  614  THR   B CG2 1 
ATOM   18937 N  N   . VAL   B 1 615  ? 36.70000   97.99300  -2.36000  1.000 66.17084  ?  615  VAL   B N   1 
ATOM   18938 C  CA  . VAL   B 1 615  ? 37.83600   98.38900  -1.53500  1.000 56.41311  ?  615  VAL   B CA  1 
ATOM   18939 C  C   . VAL   B 1 615  ? 38.69100   99.36200  -2.33100  1.000 58.20560  ?  615  VAL   B C   1 
ATOM   18940 O  O   . VAL   B 1 615  ? 39.10800   99.05700  -3.45600  1.000 63.47488  ?  615  VAL   B O   1 
ATOM   18941 C  CB  . VAL   B 1 615  ? 38.66000   97.17000  -1.08500  1.000 58.69144  ?  615  VAL   B CB  1 
ATOM   18942 C  CG1 . VAL   B 1 615  ? 39.89200   97.61700  -0.31200  1.000 56.31105  ?  615  VAL   B CG1 1 
ATOM   18943 C  CG2 . VAL   B 1 615  ? 37.80600   96.24600  -0.23900  1.000 59.35160  ?  615  VAL   B CG2 1 
ATOM   18944 N  N   . LEU   B 1 616  ? 38.95600   100.52600 -1.74800  1.000 61.76417  ?  616  LEU   B N   1 
ATOM   18945 C  CA  . LEU   B 1 616  ? 39.70900   101.58400 -2.40500  1.000 57.52724  ?  616  LEU   B CA  1 
ATOM   18946 C  C   . LEU   B 1 616  ? 41.01500   101.82300 -1.66200  1.000 57.48375  ?  616  LEU   B C   1 
ATOM   18947 O  O   . LEU   B 1 616  ? 41.01400   102.01100 -0.44100  1.000 62.64959  ?  616  LEU   B O   1 
ATOM   18948 C  CB  . LEU   B 1 616  ? 38.89500   102.87900 -2.47000  1.000 65.19990  ?  616  LEU   B CB  1 
ATOM   18949 C  CG  . LEU   B 1 616  ? 37.72700   102.88600 -3.45400  1.000 67.40640  ?  616  LEU   B CG  1 
ATOM   18950 C  CD1 . LEU   B 1 616  ? 37.13900   104.28700 -3.57800  1.000 60.86421  ?  616  LEU   B CD1 1 
ATOM   18951 C  CD2 . LEU   B 1 616  ? 38.19300   102.36300 -4.80000  1.000 69.01478  ?  616  LEU   B CD2 1 
ATOM   18952 N  N   . ALA   B 1 617  ? 42.12300   101.81100 -2.39700  1.000 55.74804  ?  617  ALA   B N   1 
ATOM   18953 C  CA  . ALA   B 1 617  ? 43.42100   102.19000 -1.85100  1.000 44.50924  ?  617  ALA   B CA  1 
ATOM   18954 C  C   . ALA   B 1 617  ? 43.63000   103.67200 -2.12400  1.000 47.67997  ?  617  ALA   B C   1 
ATOM   18955 O  O   . ALA   B 1 617  ? 43.85100   104.07400 -3.27100  1.000 57.99168  ?  617  ALA   B O   1 
ATOM   18956 C  CB  . ALA   B 1 617  ? 44.54300   101.35500 -2.46200  1.000 38.59139  ?  617  ALA   B CB  1 
ATOM   18957 N  N   . LYS   B 1 618  ? 43.55000   104.48500 -1.07600  1.000 58.28016  ?  618  LYS   B N   1 
ATOM   18958 C  CA  . LYS   B 1 618  ? 43.75300   105.91800 -1.18600  1.000 59.51988  ?  618  LYS   B CA  1 
ATOM   18959 C  C   . LYS   B 1 618  ? 45.17800   106.27500 -0.76300  1.000 61.95461  ?  618  LYS   B C   1 
ATOM   18960 O  O   . LYS   B 1 618  ? 45.97200   105.41900 -0.36400  1.000 56.37959  ?  618  LYS   B O   1 
ATOM   18961 C  CB  . LYS   B 1 618  ? 42.70300   106.66400 -0.36200  1.000 51.51821  ?  618  LYS   B CB  1 
ATOM   18962 C  CG  . LYS   B 1 618  ? 41.29200   106.13300 -0.56300  1.000 53.63703  ?  618  LYS   B CG  1 
ATOM   18963 C  CD  . LYS   B 1 618  ? 40.24600   107.19100 -0.25200  1.000 64.53295  ?  618  LYS   B CD  1 
ATOM   18964 C  CE  . LYS   B 1 618  ? 39.94600   108.04400 -1.47700  1.000 83.48836  ?  618  LYS   B CE  1 
ATOM   18965 N  NZ  . LYS   B 1 618  ? 39.64200   107.21300 -2.67400  1.000 86.44851  ?  618  LYS   B NZ  1 
ATOM   18966 N  N   . GLU   B 1 619  ? 45.51100   107.56000 -0.86500  1.000 70.17806  ?  619  GLU   B N   1 
ATOM   18967 C  CA  . GLU   B 1 619  ? 46.86500   108.02800 -0.61600  1.000 63.65455  ?  619  GLU   B CA  1 
ATOM   18968 C  C   . GLU   B 1 619  ? 46.83900   109.27000 0.26200   1.000 66.15610  ?  619  GLU   B C   1 
ATOM   18969 O  O   . GLU   B 1 619  ? 45.91100   110.08100 0.19700   1.000 63.59588  ?  619  GLU   B O   1 
ATOM   18970 C  CB  . GLU   B 1 619  ? 47.59800   108.33500 -1.93000  1.000 59.70233  ?  619  GLU   B CB  1 
ATOM   18971 C  CG  . GLU   B 1 619  ? 49.11000   108.39800 -1.80700  1.000 82.99745  ?  619  GLU   B CG  1 
ATOM   18972 C  CD  . GLU   B 1 619  ? 49.75600   109.11800 -2.97400  1.000 105.56890 ?  619  GLU   B CD  1 
ATOM   18973 O  OE1 . GLU   B 1 619  ? 49.08200   109.96900 -3.59300  1.000 88.23779  ?  619  GLU   B OE1 1 
ATOM   18974 O  OE2 . GLU   B 1 619  ? 50.93700   108.83500 -3.27100  1.000 114.08459 -1 619  GLU   B OE2 1 
ATOM   18975 N  N   . GLN   B 1 620  ? 47.86700   109.39900 1.09400   1.000 77.77524  ?  620  GLN   B N   1 
ATOM   18976 C  CA  . GLN   B 1 620  ? 48.10800   110.59900 1.87700   1.000 83.25451  ?  620  GLN   B CA  1 
ATOM   18977 C  C   . GLN   B 1 620  ? 49.18400   111.44500 1.20200   1.000 89.22691  ?  620  GLN   B C   1 
ATOM   18978 O  O   . GLN   B 1 620  ? 49.95900   110.96000 0.37300   1.000 80.48906  ?  620  GLN   B O   1 
ATOM   18979 C  CB  . GLN   B 1 620  ? 48.52200   110.24700 3.30900   1.000 80.48682  ?  620  GLN   B CB  1 
ATOM   18980 C  CG  . GLN   B 1 620  ? 47.35000   109.97100 4.24400   1.000 77.08845  ?  620  GLN   B CG  1 
ATOM   18981 C  CD  . GLN   B 1 620  ? 46.93900   111.19300 5.04400   1.000 74.79674  ?  620  GLN   B CD  1 
ATOM   18982 O  OE1 . GLN   B 1 620  ? 47.67000   112.18200 5.10700   1.000 77.28032  ?  620  GLN   B OE1 1 
ATOM   18983 N  NE2 . GLN   B 1 620  ? 45.76200   111.13300 5.65800   1.000 72.02554  ?  620  GLN   B NE2 1 
ATOM   18984 N  N   . ALA   B 1 621  ? 49.21900   112.72800 1.57400   1.000 87.32312  ?  621  ALA   B N   1 
ATOM   18985 C  CA  . ALA   B 1 621  ? 50.09600   113.68100 0.89800   1.000 68.80003  ?  621  ALA   B CA  1 
ATOM   18986 C  C   . ALA   B 1 621  ? 51.55900   113.25800 0.95000   1.000 77.53312  ?  621  ALA   B C   1 
ATOM   18987 O  O   . ALA   B 1 621  ? 52.31500   113.53300 0.01400   1.000 96.11510  ?  621  ALA   B O   1 
ATOM   18988 C  CB  . ALA   B 1 621  ? 49.92600   115.07000 1.50900   1.000 65.29075  ?  621  ALA   B CB  1 
ATOM   18989 N  N   . ASP   B 1 622  ? 51.97600   112.59700 2.02300   1.000 72.61070  ?  622  ASP   B N   1 
ATOM   18990 C  CA  . ASP   B 1 622  ? 53.34100   112.10200 2.14900   1.000 67.38802  ?  622  ASP   B CA  1 
ATOM   18991 C  C   . ASP   B 1 622  ? 53.61400   110.86500 1.30700   1.000 84.29420  ?  622  ASP   B C   1 
ATOM   18992 O  O   . ASP   B 1 622  ? 54.74200   110.35800 1.33600   1.000 94.79827  ?  622  ASP   B O   1 
ATOM   18993 C  CB  . ASP   B 1 622  ? 53.62100   111.79400 3.61300   1.000 66.10117  ?  622  ASP   B CB  1 
ATOM   18994 C  CG  . ASP   B 1 622  ? 52.39000   111.32100 4.33100   1.000 93.94991  ?  622  ASP   B CG  1 
ATOM   18995 O  OD1 . ASP   B 1 622  ? 51.79600   110.33000 3.86100   1.000 104.09151 ?  622  ASP   B OD1 1 
ATOM   18996 O  OD2 . ASP   B 1 622  ? 52.01900   111.91500 5.36800   1.000 92.69064  -1 622  ASP   B OD2 1 
ATOM   18997 N  N   . GLY   B 1 623  ? 52.61600   110.35500 0.58700   1.000 86.92736  ?  623  GLY   B N   1 
ATOM   18998 C  CA  . GLY   B 1 623  ? 52.79100   109.19500 -0.25700  1.000 95.79655  ?  623  GLY   B CA  1 
ATOM   18999 C  C   . GLY   B 1 623  ? 52.43800   107.86500 0.37100   1.000 94.73969  ?  623  GLY   B C   1 
ATOM   19000 O  O   . GLY   B 1 623  ? 52.60400   106.83000 -0.28700  1.000 88.03480  ?  623  GLY   B O   1 
ATOM   19001 N  N   . ARG   B 1 624  ? 51.97000   107.84700 1.61800   1.000 82.03077  ?  624  ARG   B N   1 
ATOM   19002 C  CA  . ARG   B 1 624  ? 51.54500   106.60200 2.23900   1.000 67.73536  ?  624  ARG   B CA  1 
ATOM   19003 C  C   . ARG   B 1 624  ? 50.14200   106.23500 1.77000   1.000 72.14373  ?  624  ARG   B C   1 
ATOM   19004 O  O   . ARG   B 1 624  ? 49.31600   107.10100 1.46800   1.000 75.12078  ?  624  ARG   B O   1 
ATOM   19005 C  CB  . ARG   B 1 624  ? 51.58800   106.70500 3.76800   1.000 77.64789  ?  624  ARG   B CB  1 
ATOM   19006 C  CG  . ARG   B 1 624  ? 52.74100   107.55000 4.28600   1.000 85.66054  ?  624  ARG   B CG  1 
ATOM   19007 C  CD  . ARG   B 1 624  ? 52.98700   107.46900 5.80400   1.000 74.50772  ?  624  ARG   B CD  1 
ATOM   19008 N  NE  . ARG   B 1 624  ? 51.84300   107.56700 6.71200   1.000 78.01887  ?  624  ARG   B NE  1 
ATOM   19009 C  CZ  . ARG   B 1 624  ? 50.91200   108.51600 6.72200   1.000 87.32652  ?  624  ARG   B CZ  1 
ATOM   19010 N  NH1 . ARG   B 1 624  ? 50.81300   109.40900 5.75400   1.000 89.23134  ?  624  ARG   B NH1 1 
ATOM   19011 N  NH2 . ARG   B 1 624  ? 50.04700   108.56500 7.73100   1.000 70.31963  ?  624  ARG   B NH2 1 
ATOM   19012 N  N   . LYS   B 1 625  ? 49.88400   104.93300 1.70100   1.000 65.07699  ?  625  LYS   B N   1 
ATOM   19013 C  CA  . LYS   B 1 625  ? 48.62300   104.40600 1.20100   1.000 64.21149  ?  625  LYS   B CA  1 
ATOM   19014 C  C   . LYS   B 1 625  ? 47.81700   103.80200 2.34300   1.000 68.64781  ?  625  LYS   B C   1 
ATOM   19015 O  O   . LYS   B 1 625  ? 48.36900   103.11900 3.21200   1.000 67.12396  ?  625  LYS   B O   1 
ATOM   19016 C  CB  . LYS   B 1 625  ? 48.86800   103.35200 0.11800   1.000 61.81047  ?  625  LYS   B CB  1 
ATOM   19017 C  CG  . LYS   B 1 625  ? 49.40000   103.91300 -1.19600  1.000 73.64691  ?  625  LYS   B CG  1 
ATOM   19018 C  CD  . LYS   B 1 625  ? 50.83500   103.46500 -1.45200  1.000 80.98860  ?  625  LYS   B CD  1 
ATOM   19019 C  CE  . LYS   B 1 625  ? 51.35500   103.99000 -2.78200  1.000 72.19778  ?  625  LYS   B CE  1 
ATOM   19020 N  NZ  . LYS   B 1 625  ? 51.22200   105.47000 -2.88700  1.000 81.30469  ?  625  LYS   B NZ  1 
ATOM   19021 N  N   . TYR   B 1 626  ? 46.50900   104.05700 2.33900   1.000 54.29181  ?  626  TYR   B N   1 
ATOM   19022 C  CA  . TYR   B 1 626  ? 45.59700   103.45900 3.30300   1.000 47.47199  ?  626  TYR   B CA  1 
ATOM   19023 C  C   . TYR   B 1 626  ? 44.38300   102.89600 2.57800   1.000 54.48595  ?  626  TYR   B C   1 
ATOM   19024 O  O   . TYR   B 1 626  ? 43.85800   103.52000 1.65200   1.000 62.21584  ?  626  TYR   B O   1 
ATOM   19025 C  CB  . TYR   B 1 626  ? 45.16200   104.47100 4.37600   1.000 36.80257  ?  626  TYR   B CB  1 
ATOM   19026 C  CG  . TYR   B 1 626  ? 44.37000   105.66100 3.87400   1.000 46.81925  ?  626  TYR   B CG  1 
ATOM   19027 C  CD1 . TYR   B 1 626  ? 45.01000   106.78100 3.35800   1.000 53.80194  ?  626  TYR   B CD1 1 
ATOM   19028 C  CD2 . TYR   B 1 626  ? 42.98300   105.67600 3.94500   1.000 50.04165  ?  626  TYR   B CD2 1 
ATOM   19029 C  CE1 . TYR   B 1 626  ? 44.28900   107.87500 2.91200   1.000 54.18826  ?  626  TYR   B CE1 1 
ATOM   19030 C  CE2 . TYR   B 1 626  ? 42.25500   106.76500 3.50100   1.000 50.57822  ?  626  TYR   B CE2 1 
ATOM   19031 C  CZ  . TYR   B 1 626  ? 42.91300   107.86100 2.98700   1.000 48.20849  ?  626  TYR   B CZ  1 
ATOM   19032 O  OH  . TYR   B 1 626  ? 42.18900   108.94500 2.54500   1.000 72.51126  ?  626  TYR   B OH  1 
ATOM   19033 N  N   . LEU   B 1 627  ? 43.94500   101.71200 3.00100   1.000 52.25661  ?  627  LEU   B N   1 
ATOM   19034 C  CA  . LEU   B 1 627  ? 42.79200   101.05400 2.40100   1.000 51.38502  ?  627  LEU   B CA  1 
ATOM   19035 C  C   . LEU   B 1 627  ? 41.52400   101.43100 3.15500   1.000 50.49996  ?  627  LEU   B C   1 
ATOM   19036 O  O   . LEU   B 1 627  ? 41.49800   101.40800 4.38900   1.000 61.55207  ?  627  LEU   B O   1 
ATOM   19037 C  CB  . LEU   B 1 627  ? 42.96600   99.53500  2.41300   1.000 51.83319  ?  627  LEU   B CB  1 
ATOM   19038 C  CG  . LEU   B 1 627  ? 44.20300   98.94600  1.74000   1.000 54.70290  ?  627  LEU   B CG  1 
ATOM   19039 C  CD1 . LEU   B 1 627  ? 44.39100   97.51300  2.19900   1.000 50.68569  ?  627  LEU   B CD1 1 
ATOM   19040 C  CD2 . LEU   B 1 627  ? 44.07500   99.01100  0.23000   1.000 57.99258  ?  627  LEU   B CD2 1 
ATOM   19041 N  N   . VAL   B 1 628  ? 40.47400   101.76800 2.41100   1.000 49.32846  ?  628  VAL   B N   1 
ATOM   19042 C  CA  . VAL   B 1 628  ? 39.16400   102.06700 2.97600   1.000 47.47345  ?  628  VAL   B CA  1 
ATOM   19043 C  C   . VAL   B 1 628  ? 38.14500   101.15300 2.30700   1.000 59.13415  ?  628  VAL   B C   1 
ATOM   19044 O  O   . VAL   B 1 628  ? 38.14100   101.01400 1.07800   1.000 66.26246  ?  628  VAL   B O   1 
ATOM   19045 C  CB  . VAL   B 1 628  ? 38.79800   103.55400 2.80200   1.000 45.75813  ?  628  VAL   B CB  1 
ATOM   19046 C  CG1 . VAL   B 1 628  ? 39.07500   104.00700 1.38300   1.000 67.07091  ?  628  VAL   B CG1 1 
ATOM   19047 C  CG2 . VAL   B 1 628  ? 37.34300   103.81000 3.18200   1.000 56.41977  ?  628  VAL   B CG2 1 
ATOM   19048 N  N   . GLY   B 1 629  ? 37.30000   100.51400 3.11500   1.000 61.32202  ?  629  GLY   B N   1 
ATOM   19049 C  CA  . GLY   B 1 629  ? 36.33400   99.56000  2.60300   1.000 42.63961  ?  629  GLY   B CA  1 
ATOM   19050 C  C   . GLY   B 1 629  ? 34.90200   100.05700 2.60500   1.000 57.87845  ?  629  GLY   B C   1 
ATOM   19051 O  O   . GLY   B 1 629  ? 34.32900   100.32400 3.66600   1.000 62.99774  ?  629  GLY   B O   1 
ATOM   19052 N  N   . TYR   B 1 630  ? 34.31100   100.17700 1.41900   1.000 59.72887  ?  630  TYR   B N   1 
ATOM   19053 C  CA  . TYR   B 1 630  ? 32.93300   100.62600 1.26300   1.000 71.87565  ?  630  TYR   B CA  1 
ATOM   19054 C  C   . TYR   B 1 630  ? 32.01900   99.41300  1.14400   1.000 70.65068  ?  630  TYR   B C   1 
ATOM   19055 O  O   . TYR   B 1 630  ? 32.29400   98.50000  0.35900   1.000 69.33459  ?  630  TYR   B O   1 
ATOM   19056 C  CB  . TYR   B 1 630  ? 32.79200   101.52200 0.03000   1.000 72.03603  ?  630  TYR   B CB  1 
ATOM   19057 C  CG  . TYR   B 1 630  ? 33.67000   102.75700 0.05800   1.000 71.94668  ?  630  TYR   B CG  1 
ATOM   19058 C  CD1 . TYR   B 1 630  ? 34.99600   102.70100 -0.35600  1.000 65.72443  ?  630  TYR   B CD1 1 
ATOM   19059 C  CD2 . TYR   B 1 630  ? 33.17100   103.98000 0.49200   1.000 66.88722  ?  630  TYR   B CD2 1 
ATOM   19060 C  CE1 . TYR   B 1 630  ? 35.80300   103.82600 -0.33200  1.000 65.23793  ?  630  TYR   B CE1 1 
ATOM   19061 C  CE2 . TYR   B 1 630  ? 33.97100   105.11100 0.51800   1.000 64.14705  ?  630  TYR   B CE2 1 
ATOM   19062 C  CZ  . TYR   B 1 630  ? 35.28500   105.02900 0.10500   1.000 68.39483  ?  630  TYR   B CZ  1 
ATOM   19063 O  OH  . TYR   B 1 630  ? 36.08500   106.15000 0.12800   1.000 66.42941  ?  630  TYR   B OH  1 
ATOM   19064 N  N   . TYR   B 1 631  ? 30.93400   99.40400  1.91800   1.000 60.32381  ?  631  TYR   B N   1 
ATOM   19065 C  CA  . TYR   B 1 631  ? 30.03300   98.26100  1.93400   1.000 63.23054  ?  631  TYR   B CA  1 
ATOM   19066 C  C   . TYR   B 1 631  ? 28.58300   98.72000  1.88900   1.000 78.41942  ?  631  TYR   B C   1 
ATOM   19067 O  O   . TYR   B 1 631  ? 28.23700   99.80800  2.36000   1.000 72.07444  ?  631  TYR   B O   1 
ATOM   19068 C  CB  . TYR   B 1 631  ? 30.27100   97.36900  3.16700   1.000 56.83413  ?  631  TYR   B CB  1 
ATOM   19069 C  CG  . TYR   B 1 631  ? 29.96000   98.00100  4.51500   1.000 73.38461  ?  631  TYR   B CG  1 
ATOM   19070 C  CD1 . TYR   B 1 631  ? 28.67500   97.96200  5.04900   1.000 66.29243  ?  631  TYR   B CD1 1 
ATOM   19071 C  CD2 . TYR   B 1 631  ? 30.95800   98.61100  5.26600   1.000 70.72657  ?  631  TYR   B CD2 1 
ATOM   19072 C  CE1 . TYR   B 1 631  ? 28.39200   98.52100  6.28500   1.000 73.75369  ?  631  TYR   B CE1 1 
ATOM   19073 C  CE2 . TYR   B 1 631  ? 30.68300   99.17700  6.50400   1.000 71.69943  ?  631  TYR   B CE2 1 
ATOM   19074 C  CZ  . TYR   B 1 631  ? 29.39800   99.12700  7.00800   1.000 72.42750  ?  631  TYR   B CZ  1 
ATOM   19075 O  OH  . TYR   B 1 631  ? 29.11100   99.68500  8.23600   1.000 63.28028  ?  631  TYR   B OH  1 
ATOM   19076 N  N   . VAL   B 1 632  ? 27.73900   97.86800  1.31000   1.000 78.75438  ?  632  VAL   B N   1 
ATOM   19077 C  CA  . VAL   B 1 632  ? 26.29400   98.05800  1.28100   1.000 68.98044  ?  632  VAL   B CA  1 
ATOM   19078 C  C   . VAL   B 1 632  ? 25.67700   97.04300  2.23200   1.000 66.99228  ?  632  VAL   B C   1 
ATOM   19079 O  O   . VAL   B 1 632  ? 25.90300   95.83400  2.09500   1.000 59.40131  ?  632  VAL   B O   1 
ATOM   19080 C  CB  . VAL   B 1 632  ? 25.72400   97.90300  -0.13700  1.000 69.34160  ?  632  VAL   B CB  1 
ATOM   19081 C  CG1 . VAL   B 1 632  ? 24.22000   97.70800  -0.08000  1.000 65.06978  ?  632  VAL   B CG1 1 
ATOM   19082 C  CG2 . VAL   B 1 632  ? 26.06800   99.11600  -0.98400  1.000 73.98337  ?  632  VAL   B CG2 1 
ATOM   19083 N  N   . ALA   B 1 633  ? 24.90700   97.53300  3.19600   1.000 85.54581  ?  633  ALA   B N   1 
ATOM   19084 C  CA  . ALA   B 1 633  ? 24.26500   96.69500  4.19700   1.000 66.96423  ?  633  ALA   B CA  1 
ATOM   19085 C  C   . ALA   B 1 633  ? 22.95900   97.35600  4.60000   1.000 68.44976  ?  633  ALA   B C   1 
ATOM   19086 O  O   . ALA   B 1 633  ? 22.77600   98.55900  4.38200   1.000 62.08857  ?  633  ALA   B O   1 
ATOM   19087 C  CB  . ALA   B 1 633  ? 25.16900   96.49300  5.42200   1.000 67.87362  ?  633  ALA   B CB  1 
ATOM   19088 N  N   . PRO   B 1 634  ? 22.01900   96.59600  5.17400   1.000 77.56406  ?  634  PRO   B N   1 
ATOM   19089 C  CA  . PRO   B 1 634  ? 20.77700   97.22700  5.65400   1.000 57.43259  ?  634  PRO   B CA  1 
ATOM   19090 C  C   . PRO   B 1 634  ? 21.02100   98.33700  6.66300   1.000 68.93724  ?  634  PRO   B C   1 
ATOM   19091 O  O   . PRO   B 1 634  ? 20.34600   99.37200  6.61600   1.000 86.48287  ?  634  PRO   B O   1 
ATOM   19092 C  CB  . PRO   B 1 634  ? 20.00000   96.05000  6.26800   1.000 65.57302  ?  634  PRO   B CB  1 
ATOM   19093 C  CG  . PRO   B 1 634  ? 21.00400   94.93100  6.40900   1.000 75.30674  ?  634  PRO   B CG  1 
ATOM   19094 C  CD  . PRO   B 1 634  ? 21.97600   95.13000  5.29900   1.000 70.57875  ?  634  PRO   B CD  1 
ATOM   19095 N  N   . GLU   B 1 635  ? 21.97700   98.15500  7.57100   1.000 72.06261  ?  635  GLU   B N   1 
ATOM   19096 C  CA  . GLU   B 1 635  ? 22.34500   99.18300  8.53200   1.000 73.28375  ?  635  GLU   B CA  1 
ATOM   19097 C  C   . GLU   B 1 635  ? 23.85400   99.15700  8.72100   1.000 71.86926  ?  635  GLU   B C   1 
ATOM   19098 O  O   . GLU   B 1 635  ? 24.54600   98.25700  8.23700   1.000 69.66778  ?  635  GLU   B O   1 
ATOM   19099 C  CB  . GLU   B 1 635  ? 21.62300   98.98800  9.87200   1.000 76.55057  ?  635  GLU   B CB  1 
ATOM   19100 N  N   . GLU   B 1 636  ? 24.36300   100.16100 9.43200   1.000 75.66125  ?  636  GLU   B N   1 
ATOM   19101 C  CA  . GLU   B 1 636  ? 25.79100   100.24200 9.69700   1.000 73.42195  ?  636  GLU   B CA  1 
ATOM   19102 C  C   . GLU   B 1 636  ? 26.25700   99.03000  10.49900  1.000 65.86981  ?  636  GLU   B C   1 
ATOM   19103 O  O   . GLU   B 1 636  ? 25.48100   98.36700  11.19100  1.000 69.20875  ?  636  GLU   B O   1 
ATOM   19104 C  CB  . GLU   B 1 636  ? 26.12700   101.53000 10.45100  1.000 55.39895  ?  636  GLU   B CB  1 
ATOM   19105 N  N   . ILE   B 1 637  ? 27.54800   98.73800  10.38600  1.000 59.63128  ?  637  ILE   B N   1 
ATOM   19106 C  CA  . ILE   B 1 637  ? 28.15900   97.62600  11.10700  1.000 57.66925  ?  637  ILE   B CA  1 
ATOM   19107 C  C   . ILE   B 1 637  ? 29.33300   98.17800  11.90600  1.000 64.08236  ?  637  ILE   B C   1 
ATOM   19108 O  O   . ILE   B 1 637  ? 30.10100   98.99800  11.38100  1.000 70.76190  ?  637  ILE   B O   1 
ATOM   19109 C  CB  . ILE   B 1 637  ? 28.60400   96.51300  10.14500  1.000 62.05355  ?  637  ILE   B CB  1 
ATOM   19110 C  CG1 . ILE   B 1 637  ? 27.41100   96.00700  9.33000   1.000 62.24502  ?  637  ILE   B CG1 1 
ATOM   19111 C  CG2 . ILE   B 1 637  ? 29.26600   95.37000  10.90800  1.000 58.05438  ?  637  ILE   B CG2 1 
ATOM   19112 C  CD1 . ILE   B 1 637  ? 27.67100   94.70400  8.61100   1.000 56.81205  ?  637  ILE   B CD1 1 
ATOM   19113 N  N   . PRO   B 1 638  ? 29.50100   97.78300  13.16900  1.000 62.03193  ?  638  PRO   B N   1 
ATOM   19114 C  CA  . PRO   B 1 638  ? 30.60600   98.32700  13.96700  1.000 62.62565  ?  638  PRO   B CA  1 
ATOM   19115 C  C   . PRO   B 1 638  ? 31.95700   98.07400  13.31400  1.000 62.35997  ?  638  PRO   B C   1 
ATOM   19116 O  O   . PRO   B 1 638  ? 32.18400   97.03600  12.68700  1.000 67.50853  ?  638  PRO   B O   1 
ATOM   19117 C  CB  . PRO   B 1 638  ? 30.47700   97.59100  15.30800  1.000 60.42260  ?  638  PRO   B CB  1 
ATOM   19118 C  CG  . PRO   B 1 638  ? 29.52400   96.45400  15.05600  1.000 54.64678  ?  638  PRO   B CG  1 
ATOM   19119 C  CD  . PRO   B 1 638  ? 28.61600   96.92500  13.97200  1.000 56.94925  ?  638  PRO   B CD  1 
ATOM   19120 N  N   . HIS   B 1 639  ? 32.85100   99.05500  13.45900  1.000 66.06531  ?  639  HIS   B N   1 
ATOM   19121 C  CA  . HIS   B 1 639  ? 34.17100   98.97300  12.84000  1.000 65.83989  ?  639  HIS   B CA  1 
ATOM   19122 C  C   . HIS   B 1 639  ? 34.92900   97.74000  13.31300  1.000 57.60263  ?  639  HIS   B C   1 
ATOM   19123 O  O   . HIS   B 1 639  ? 35.58100   97.05800  12.51400  1.000 62.27295  ?  639  HIS   B O   1 
ATOM   19124 C  CB  . HIS   B 1 639  ? 34.96100   100.24900 13.14300  1.000 62.42320  ?  639  HIS   B CB  1 
ATOM   19125 C  CG  . HIS   B 1 639  ? 36.41600   100.16300 12.80000  1.000 66.62085  ?  639  HIS   B CG  1 
ATOM   19126 N  ND1 . HIS   B 1 639  ? 37.35200   99.61600  13.65200  1.000 74.46120  ?  639  HIS   B ND1 1 
ATOM   19127 C  CD2 . HIS   B 1 639  ? 37.09800   100.56800 11.70200  1.000 60.06752  ?  639  HIS   B CD2 1 
ATOM   19128 C  CE1 . HIS   B 1 639  ? 38.54600   99.67700  13.08900  1.000 67.81794  ?  639  HIS   B CE1 1 
ATOM   19129 N  NE2 . HIS   B 1 639  ? 38.42000   100.25100 11.90600  1.000 70.89697  ?  639  HIS   B NE2 1 
ATOM   19130 N  N   . GLY   B 1 640  ? 34.84900   97.43300  14.60800  1.000 59.92006  ?  640  GLY   B N   1 
ATOM   19131 C  CA  . GLY   B 1 640  ? 35.58400   96.29800  15.13600  1.000 67.20057  ?  640  GLY   B CA  1 
ATOM   19132 C  C   . GLY   B 1 640  ? 35.06200   94.96400  14.64700  1.000 66.53790  ?  640  GLY   B C   1 
ATOM   19133 O  O   . GLY   B 1 640  ? 35.82900   94.00400  14.52300  1.000 60.45574  ?  640  GLY   B O   1 
ATOM   19134 N  N   . GLU   B 1 641  ? 33.75800   94.88100  14.36300  1.000 57.29544  ?  641  GLU   B N   1 
ATOM   19135 C  CA  . GLU   B 1 641  ? 33.19000   93.62700  13.87700  1.000 56.34086  ?  641  GLU   B CA  1 
ATOM   19136 C  C   . GLU   B 1 641  ? 33.73900   93.27000  12.50300  1.000 62.69418  ?  641  GLU   B C   1 
ATOM   19137 O  O   . GLU   B 1 641  ? 34.10000   92.11300  12.25500  1.000 55.09142  ?  641  GLU   B O   1 
ATOM   19138 C  CB  . GLU   B 1 641  ? 31.66500   93.71500  13.83800  1.000 57.85874  ?  641  GLU   B CB  1 
ATOM   19139 C  CG  . GLU   B 1 641  ? 30.98800   92.38600  13.52900  1.000 77.86470  ?  641  GLU   B CG  1 
ATOM   19140 C  CD  . GLU   B 1 641  ? 29.48000   92.50300  13.43700  1.000 74.34779  ?  641  GLU   B CD  1 
ATOM   19141 O  OE1 . GLU   B 1 641  ? 28.93000   93.50900  13.92800  1.000 77.26299  ?  641  GLU   B OE1 1 
ATOM   19142 O  OE2 . GLU   B 1 641  ? 28.84400   91.58700  12.87300  1.000 77.82009  -1 641  GLU   B OE2 1 
ATOM   19143 N  N   . LEU   B 1 642  ? 33.80900   94.24800  11.59600  1.000 61.68033  ?  642  LEU   B N   1 
ATOM   19144 C  CA  . LEU   B 1 642  ? 34.42700   94.00500  10.29700  1.000 49.64418  ?  642  LEU   B CA  1 
ATOM   19145 C  C   . LEU   B 1 642  ? 35.90500   93.67100  10.45000  1.000 52.87007  ?  642  LEU   B C   1 
ATOM   19146 O  O   . LEU   B 1 642  ? 36.42200   92.78300  9.76300   1.000 59.60404  ?  642  LEU   B O   1 
ATOM   19147 C  CB  . LEU   B 1 642  ? 34.24300   95.22200  9.39200   1.000 50.42021  ?  642  LEU   B CB  1 
ATOM   19148 C  CG  . LEU   B 1 642  ? 32.80300   95.71700  9.26000   1.000 47.77646  ?  642  LEU   B CG  1 
ATOM   19149 C  CD1 . LEU   B 1 642  ? 32.75500   97.05600  8.55200   1.000 55.24451  ?  642  LEU   B CD1 1 
ATOM   19150 C  CD2 . LEU   B 1 642  ? 31.95700   94.69500  8.52000   1.000 52.55250  ?  642  LEU   B CD2 1 
ATOM   19151 N  N   . ARG   B 1 643  ? 36.60000   94.37400  11.34900  1.000 56.08810  ?  643  ARG   B N   1 
ATOM   19152 C  CA  . ARG   B 1 643  ? 38.00700   94.08000  11.59700  1.000 48.10717  ?  643  ARG   B CA  1 
ATOM   19153 C  C   . ARG   B 1 643  ? 38.19100   92.66900  12.14000  1.000 51.70887  ?  643  ARG   B C   1 
ATOM   19154 O  O   . ARG   B 1 643  ? 39.19100   92.01000  11.83500  1.000 48.87825  ?  643  ARG   B O   1 
ATOM   19155 C  CB  . ARG   B 1 643  ? 38.59300   95.11500  12.56100  1.000 44.35405  ?  643  ARG   B CB  1 
ATOM   19156 C  CG  . ARG   B 1 643  ? 40.02200   94.82900  13.00200  1.000 62.54938  ?  643  ARG   B CG  1 
ATOM   19157 C  CD  . ARG   B 1 643  ? 40.70500   96.07700  13.54400  1.000 59.44561  ?  643  ARG   B CD  1 
ATOM   19158 N  NE  . ARG   B 1 643  ? 41.48500   96.75500  12.51500  1.000 79.04054  ?  643  ARG   B NE  1 
ATOM   19159 C  CZ  . ARG   B 1 643  ? 42.69800   96.38500  12.12800  1.000 79.44462  ?  643  ARG   B CZ  1 
ATOM   19160 N  NH1 . ARG   B 1 643  ? 43.31000   95.34400  12.67100  1.000 69.47667  ?  643  ARG   B NH1 1 
ATOM   19161 N  NH2 . ARG   B 1 643  ? 43.31300   97.07500  11.17000  1.000 78.69993  ?  643  ARG   B NH2 1 
ATOM   19162 N  N   . GLU   B 1 644  ? 37.23600   92.18500  12.93600  1.000 63.98352  ?  644  GLU   B N   1 
ATOM   19163 C  CA  . GLU   B 1 644  ? 37.30200   90.80800  13.40800  1.000 63.21341  ?  644  GLU   B CA  1 
ATOM   19164 C  C   . GLU   B 1 644  ? 36.87700   89.82400  12.32900  1.000 62.54769  ?  644  GLU   B C   1 
ATOM   19165 O  O   . GLU   B 1 644  ? 37.39400   88.70200  12.28100  1.000 62.49429  ?  644  GLU   B O   1 
ATOM   19166 C  CB  . GLU   B 1 644  ? 36.43000   90.63500  14.65300  1.000 58.01666  ?  644  GLU   B CB  1 
ATOM   19167 C  CG  . GLU   B 1 644  ? 36.86400   89.49200  15.55800  1.000 95.42196  ?  644  GLU   B CG  1 
ATOM   19168 C  CD  . GLU   B 1 644  ? 35.78400   89.08300  16.54200  1.000 115.24533 ?  644  GLU   B CD  1 
ATOM   19169 O  OE1 . GLU   B 1 644  ? 35.34200   89.94200  17.33400  1.000 101.79835 ?  644  GLU   B OE1 1 
ATOM   19170 O  OE2 . GLU   B 1 644  ? 35.37400   87.90200  16.52100  1.000 116.80315 -1 644  GLU   B OE2 1 
ATOM   19171 N  N   . TRP   B 1 645  ? 35.94500   90.22300  11.46100  1.000 63.37739  ?  645  TRP   B N   1 
ATOM   19172 C  CA  . TRP   B 1 645  ? 35.51100   89.35100  10.37500  1.000 47.65594  ?  645  TRP   B CA  1 
ATOM   19173 C  C   . TRP   B 1 645  ? 36.64100   89.11700  9.38100   1.000 62.14932  ?  645  TRP   B C   1 
ATOM   19174 O  O   . TRP   B 1 645  ? 36.92600   87.97300  9.00600   1.000 58.26412  ?  645  TRP   B O   1 
ATOM   19175 C  CB  . TRP   B 1 645  ? 34.29200   89.95600  9.67800   1.000 58.05694  ?  645  TRP   B CB  1 
ATOM   19176 C  CG  . TRP   B 1 645  ? 33.75700   89.13000  8.54600   1.000 68.77953  ?  645  TRP   B CG  1 
ATOM   19177 C  CD1 . TRP   B 1 645  ? 33.88300   89.39000  7.21100   1.000 69.21135  ?  645  TRP   B CD1 1 
ATOM   19178 C  CD2 . TRP   B 1 645  ? 33.00300   87.91600  8.64900   1.000 66.98840  ?  645  TRP   B CD2 1 
ATOM   19179 N  NE1 . TRP   B 1 645  ? 33.25700   88.41000  6.47700   1.000 73.67244  ?  645  TRP   B NE1 1 
ATOM   19180 C  CE2 . TRP   B 1 645  ? 32.71000   87.49400  7.33600   1.000 73.66559  ?  645  TRP   B CE2 1 
ATOM   19181 C  CE3 . TRP   B 1 645  ? 32.55000   87.14300  9.72200   1.000 59.57481  ?  645  TRP   B CE3 1 
ATOM   19182 C  CZ2 . TRP   B 1 645  ? 31.98600   86.33400  7.06900   1.000 68.86752  ?  645  TRP   B CZ2 1 
ATOM   19183 C  CZ3 . TRP   B 1 645  ? 31.83100   85.99300  9.45400   1.000 69.51134  ?  645  TRP   B CZ3 1 
ATOM   19184 C  CH2 . TRP   B 1 645  ? 31.55500   85.60000  8.14000   1.000 70.92738  ?  645  TRP   B CH2 1 
ATOM   19185 N  N   . LEU   B 1 646  ? 37.30300   90.19200  8.95100   1.000 61.64108  ?  646  LEU   B N   1 
ATOM   19186 C  CA  . LEU   B 1 646  ? 38.38900   90.06400  7.98900   1.000 44.29981  ?  646  LEU   B CA  1 
ATOM   19187 C  C   . LEU   B 1 646  ? 39.62700   89.42100  8.59700   1.000 48.02181  ?  646  LEU   B C   1 
ATOM   19188 O  O   . LEU   B 1 646  ? 40.44500   88.86200  7.86100   1.000 58.65444  ?  646  LEU   B O   1 
ATOM   19189 C  CB  . LEU   B 1 646  ? 38.73000   91.43400  7.40700   1.000 39.40248  ?  646  LEU   B CB  1 
ATOM   19190 C  CG  . LEU   B 1 646  ? 37.57400   92.10500  6.66200   1.000 46.94135  ?  646  LEU   B CG  1 
ATOM   19191 C  CD1 . LEU   B 1 646  ? 37.95600   93.49600  6.18400   1.000 52.41004  ?  646  LEU   B CD1 1 
ATOM   19192 C  CD2 . LEU   B 1 646  ? 37.12600   91.24100  5.49600   1.000 55.74791  ?  646  LEU   B CD2 1 
ATOM   19193 N  N   . GLY   B 1 647  ? 39.78300   89.47600  9.91800   1.000 47.40152  ?  647  GLY   B N   1 
ATOM   19194 C  CA  . GLY   B 1 647  ? 40.87900   88.75800  10.53800  1.000 50.19502  ?  647  GLY   B CA  1 
ATOM   19195 C  C   . GLY   B 1 647  ? 40.75300   87.25300  10.46300  1.000 55.55540  ?  647  GLY   B C   1 
ATOM   19196 O  O   . GLY   B 1 647  ? 41.67700   86.54900  10.89000  1.000 53.95207  ?  647  GLY   B O   1 
ATOM   19197 N  N   . ASN   B 1 648  ? 39.63100   86.74800  9.94100   1.000 54.70628  ?  648  ASN   B N   1 
ATOM   19198 C  CA  . ASN   B 1 648  ? 39.45300   85.31100  9.78100   1.000 74.48049  ?  648  ASN   B CA  1 
ATOM   19199 C  C   . ASN   B 1 648  ? 40.38500   84.74500  8.71800   1.000 72.57969  ?  648  ASN   B C   1 
ATOM   19200 O  O   . ASN   B 1 648  ? 40.80600   83.58700  8.81900   1.000 70.27139  ?  648  ASN   B O   1 
ATOM   19201 C  CB  . ASN   B 1 648  ? 38.00400   84.99500  9.40400   1.000 79.51715  ?  648  ASN   B CB  1 
ATOM   19202 C  CG  . ASN   B 1 648  ? 37.07800   84.93100  10.60800  1.000 75.47193  ?  648  ASN   B CG  1 
ATOM   19203 O  OD1 . ASN   B 1 648  ? 37.52400   84.92300  11.75600  1.000 72.25255  ?  648  ASN   B OD1 1 
ATOM   19204 N  ND2 . ASN   B 1 648  ? 35.77300   84.87300  10.34300  1.000 78.82044  ?  648  ASN   B ND2 1 
ATOM   19205 N  N   . ASP   B 1 649  ? 40.71400   85.53800  7.69400   1.000 72.45240  ?  649  ASP   B N   1 
ATOM   19206 C  CA  . ASP   B 1 649  ? 41.44700   85.02700  6.54100   1.000 69.55607  ?  649  ASP   B CA  1 
ATOM   19207 C  C   . ASP   B 1 649  ? 42.58800   85.94600  6.11300   1.000 56.32127  ?  649  ASP   B C   1 
ATOM   19208 O  O   . ASP   B 1 649  ? 43.57800   85.47800  5.54300   1.000 75.23447  ?  649  ASP   B O   1 
ATOM   19209 C  CB  . ASP   B 1 649  ? 40.49200   84.80500  5.36400   1.000 82.67773  ?  649  ASP   B CB  1 
ATOM   19210 C  CG  . ASP   B 1 649  ? 39.14500   84.25400  5.79600   1.000 82.46598  ?  649  ASP   B CG  1 
ATOM   19211 O  OD1 . ASP   B 1 649  ? 38.30300   85.04600  6.26900   1.000 76.16238  ?  649  ASP   B OD1 1 
ATOM   19212 O  OD2 . ASP   B 1 649  ? 38.92900   83.02900  5.66700   1.000 83.10176  -1 649  ASP   B OD2 1 
ATOM   19213 N  N   . LEU   B 1 650  ? 42.46900   87.25800  6.38200   1.000 48.68703  ?  650  LEU   B N   1 
ATOM   19214 C  CA  . LEU   B 1 650  ? 43.47700   88.18800  5.88800   1.000 48.79511  ?  650  LEU   B CA  1 
ATOM   19215 C  C   . LEU   B 1 650  ? 44.47400   88.56300  6.98200   1.000 47.58550  ?  650  LEU   B C   1 
ATOM   19216 O  O   . LEU   B 1 650  ? 44.14300   88.53100  8.17100   1.000 56.25169  ?  650  LEU   B O   1 
ATOM   19217 C  CB  . LEU   B 1 650  ? 42.81200   89.45900  5.35300   1.000 34.12483  ?  650  LEU   B CB  1 
ATOM   19218 C  CG  . LEU   B 1 650  ? 41.93700   89.28700  4.11300   1.000 45.00389  ?  650  LEU   B CG  1 
ATOM   19219 C  CD1 . LEU   B 1 650  ? 40.57200   89.90800  4.33600   1.000 53.28548  ?  650  LEU   B CD1 1 
ATOM   19220 C  CD2 . LEU   B 1 650  ? 42.61300   89.90300  2.89900   1.000 53.18187  ?  650  LEU   B CD2 1 
ATOM   19221 N  N   . PRO   B 1 651  ? 45.70200   88.92200  6.61500   1.000 42.12656  ?  651  PRO   B N   1 
ATOM   19222 C  CA  . PRO   B 1 651  ? 46.67300   89.41100  7.59900   1.000 47.66113  ?  651  PRO   B CA  1 
ATOM   19223 C  C   . PRO   B 1 651  ? 46.34800   90.84000  8.02500   1.000 47.91493  ?  651  PRO   B C   1 
ATOM   19224 O  O   . PRO   B 1 651  ? 45.38800   91.45500  7.56400   1.000 48.52222  ?  651  PRO   B O   1 
ATOM   19225 C  CB  . PRO   B 1 651  ? 48.00400   89.34200  6.84600   1.000 42.36970  ?  651  PRO   B CB  1 
ATOM   19226 C  CG  . PRO   B 1 651  ? 47.62700   89.48700  5.42100   1.000 58.36529  ?  651  PRO   B CG  1 
ATOM   19227 C  CD  . PRO   B 1 651  ? 46.29600   88.80000  5.27200   1.000 59.64116  ?  651  PRO   B CD  1 
ATOM   19228 N  N   . ASP   B 1 652  ? 47.18800   91.37000  8.91700   1.000 45.87165  ?  652  ASP   B N   1 
ATOM   19229 C  CA  . ASP   B 1 652  ? 46.91300   92.67400  9.51300   1.000 45.22739  ?  652  ASP   B CA  1 
ATOM   19230 C  C   . ASP   B 1 652  ? 46.93000   93.78100  8.46600   1.000 44.12465  ?  652  ASP   B C   1 
ATOM   19231 O  O   . ASP   B 1 652  ? 46.00200   94.59600  8.39500   1.000 37.92301  ?  652  ASP   B O   1 
ATOM   19232 C  CB  . ASP   B 1 652  ? 47.92600   92.96800  10.61900  1.000 45.23623  ?  652  ASP   B CB  1 
ATOM   19233 C  CG  . ASP   B 1 652  ? 47.82800   94.39000  11.13200  1.000 69.14314  ?  652  ASP   B CG  1 
ATOM   19234 O  OD1 . ASP   B 1 652  ? 46.72800   94.79500  11.57000  1.000 79.09918  ?  652  ASP   B OD1 1 
ATOM   19235 O  OD2 . ASP   B 1 652  ? 48.85200   95.10500  11.09600  1.000 62.57374  -1 652  ASP   B OD2 1 
ATOM   19236 N  N   . TYR   B 1 653  ? 47.98100   93.82500  7.64100   1.000 47.62727  ?  653  TYR   B N   1 
ATOM   19237 C  CA  . TYR   B 1 653  ? 48.15600   94.91400  6.68600   1.000 39.94335  ?  653  TYR   B CA  1 
ATOM   19238 C  C   . TYR   B 1 653  ? 47.09800   94.92000  5.59000   1.000 51.05513  ?  653  TYR   B C   1 
ATOM   19239 O  O   . TYR   B 1 653  ? 46.95800   95.93300  4.89500   1.000 51.59813  ?  653  TYR   B O   1 
ATOM   19240 C  CB  . TYR   B 1 653  ? 49.55500   94.85100  6.06200   1.000 36.86719  ?  653  TYR   B CB  1 
ATOM   19241 C  CG  . TYR   B 1 653  ? 49.94600   93.48500  5.53900   1.000 50.46250  ?  653  TYR   B CG  1 
ATOM   19242 C  CD1 . TYR   B 1 653  ? 49.59000   93.08300  4.25700   1.000 47.49400  ?  653  TYR   B CD1 1 
ATOM   19243 C  CD2 . TYR   B 1 653  ? 50.67500   92.60000  6.32300   1.000 45.57840  ?  653  TYR   B CD2 1 
ATOM   19244 C  CE1 . TYR   B 1 653  ? 49.94300   91.83200  3.77400   1.000 44.15678  ?  653  TYR   B CE1 1 
ATOM   19245 C  CE2 . TYR   B 1 653  ? 51.03300   91.34800  5.84800   1.000 46.50827  ?  653  TYR   B CE2 1 
ATOM   19246 C  CZ  . TYR   B 1 653  ? 50.66500   90.97000  4.57400   1.000 51.75652  ?  653  TYR   B CZ  1 
ATOM   19247 O  OH  . TYR   B 1 653  ? 51.02200   89.72600  4.10300   1.000 70.46153  ?  653  TYR   B OH  1 
ATOM   19248 N  N   . MET   B 1 654  ? 46.34900   93.83300  5.42200   1.000 47.98329  ?  654  MET   B N   1 
ATOM   19249 C  CA  . MET   B 1 654  ? 45.27200   93.78600  4.44300   1.000 38.78788  ?  654  MET   B CA  1 
ATOM   19250 C  C   . MET   B 1 654  ? 43.91700   94.14900  5.03700   1.000 46.62289  ?  654  MET   B C   1 
ATOM   19251 O  O   . MET   B 1 654  ? 42.93000   94.20900  4.29900   1.000 52.60193  ?  654  MET   B O   1 
ATOM   19252 C  CB  . MET   B 1 654  ? 45.20000   92.39700  3.79900   1.000 47.38765  ?  654  MET   B CB  1 
ATOM   19253 C  CG  . MET   B 1 654  ? 46.48000   91.98200  3.08400   1.000 59.00322  ?  654  MET   B CG  1 
ATOM   19254 S  SD  . MET   B 1 654  ? 46.28400   90.56500  1.98500   1.000 60.59038  ?  654  MET   B SD  1 
ATOM   19255 C  CE  . MET   B 1 654  ? 45.42200   91.34300  0.62200   1.000 45.20277  ?  654  MET   B CE  1 
ATOM   19256 N  N   . ILE   B 1 655  ? 43.83300   94.39000  6.34000   1.000 45.01531  ?  655  ILE   B N   1 
ATOM   19257 C  CA  . ILE   B 1 655  ? 42.56900   94.82700  6.92000   1.000 41.54067  ?  655  ILE   B CA  1 
ATOM   19258 C  C   . ILE   B 1 655  ? 42.48200   96.33600  6.73600   1.000 45.18085  ?  655  ILE   B C   1 
ATOM   19259 O  O   . ILE   B 1 655  ? 43.38200   97.06400  7.17800   1.000 59.60590  ?  655  ILE   B O   1 
ATOM   19260 C  CB  . ILE   B 1 655  ? 42.44900   94.42200  8.39600   1.000 39.94253  ?  655  ILE   B CB  1 
ATOM   19261 C  CG1 . ILE   B 1 655  ? 42.60800   92.90800  8.54400   1.000 30.53293  ?  655  ILE   B CG1 1 
ATOM   19262 C  CG2 . ILE   B 1 655  ? 41.11600   94.88900  8.96800   1.000 47.92088  ?  655  ILE   B CG2 1 
ATOM   19263 C  CD1 . ILE   B 1 655  ? 42.51700   92.42900  9.96900   1.000 48.57288  ?  655  ILE   B CD1 1 
ATOM   19264 N  N   . PRO   B 1 656  ? 41.44900   96.84500  6.06600   1.000 50.44781  ?  656  PRO   B N   1 
ATOM   19265 C  CA  . PRO   B 1 656  ? 41.32800   98.29700  5.89400   1.000 53.70877  ?  656  PRO   B CA  1 
ATOM   19266 C  C   . PRO   B 1 656  ? 41.20900   99.01000  7.23400   1.000 57.05876  ?  656  PRO   B C   1 
ATOM   19267 O  O   . PRO   B 1 656  ? 40.63800   98.48800  8.19400   1.000 61.01264  ?  656  PRO   B O   1 
ATOM   19268 C  CB  . PRO   B 1 656  ? 40.04800   98.45300  5.06500   1.000 47.44718  ?  656  PRO   B CB  1 
ATOM   19269 C  CG  . PRO   B 1 656  ? 39.86400   97.12800  4.39100   1.000 59.66406  ?  656  PRO   B CG  1 
ATOM   19270 C  CD  . PRO   B 1 656  ? 40.39300   96.10800  5.35100   1.000 43.43901  ?  656  PRO   B CD  1 
ATOM   19271 N  N   . THR   B 1 657  ? 41.76200   100.22300 7.28700   1.000 58.31069  ?  657  THR   B N   1 
ATOM   19272 C  CA  . THR   B 1 657  ? 41.70800   101.02100 8.50600   1.000 55.56069  ?  657  THR   B CA  1 
ATOM   19273 C  C   . THR   B 1 657  ? 40.40500   101.79700 8.64700   1.000 59.23072  ?  657  THR   B C   1 
ATOM   19274 O  O   . THR   B 1 657  ? 40.07100   102.22100 9.76000   1.000 60.72676  ?  657  THR   B O   1 
ATOM   19275 C  CB  . THR   B 1 657  ? 42.89100   101.99000 8.55400   1.000 49.12895  ?  657  THR   B CB  1 
ATOM   19276 O  OG1 . THR   B 1 657  ? 42.64400   103.09300 7.67400   1.000 67.27273  ?  657  THR   B OG1 1 
ATOM   19277 C  CG2 . THR   B 1 657  ? 44.16600   101.28900 8.12100   1.000 43.67374  ?  657  THR   B CG2 1 
ATOM   19278 N  N   . TYR   B 1 658  ? 39.66300   101.99200 7.55700   1.000 54.26162  ?  658  TYR   B N   1 
ATOM   19279 C  CA  . TYR   B 1 658  ? 38.38700   102.69300 7.59000   1.000 62.85648  ?  658  TYR   B CA  1 
ATOM   19280 C  C   . TYR   B 1 658  ? 37.33800   101.88500 6.84200   1.000 60.18950  ?  658  TYR   B C   1 
ATOM   19281 O  O   . TYR   B 1 658  ? 37.64000   101.23500 5.83700   1.000 58.77143  ?  658  TYR   B O   1 
ATOM   19282 C  CB  . TYR   B 1 658  ? 38.49500   104.09700 6.97300   1.000 52.97106  ?  658  TYR   B CB  1 
ATOM   19283 C  CG  . TYR   B 1 658  ? 39.63100   104.92500 7.52600   1.000 57.63607  ?  658  TYR   B CG  1 
ATOM   19284 C  CD1 . TYR   B 1 658  ? 39.65700   105.29700 8.86300   1.000 66.20787  ?  658  TYR   B CD1 1 
ATOM   19285 C  CD2 . TYR   B 1 658  ? 40.67800   105.33600 6.71100   1.000 52.89465  ?  658  TYR   B CD2 1 
ATOM   19286 C  CE1 . TYR   B 1 658  ? 40.69500   106.05300 9.37600   1.000 49.40276  ?  658  TYR   B CE1 1 
ATOM   19287 C  CE2 . TYR   B 1 658  ? 41.72100   106.09300 7.21500   1.000 66.48203  ?  658  TYR   B CE2 1 
ATOM   19288 C  CZ  . TYR   B 1 658  ? 41.72300   106.44800 8.55000   1.000 54.49458  ?  658  TYR   B CZ  1 
ATOM   19289 O  OH  . TYR   B 1 658  ? 42.75400   107.20100 9.06400   1.000 66.85592  ?  658  TYR   B OH  1 
ATOM   19290 N  N   . PHE   B 1 659  ? 36.10600   101.92900 7.34100   1.000 55.40008  ?  659  PHE   B N   1 
ATOM   19291 C  CA  . PHE   B 1 659  ? 34.97100   101.28000 6.70300   1.000 49.87368  ?  659  PHE   B CA  1 
ATOM   19292 C  C   . PHE   B 1 659  ? 33.83000   102.28000 6.59500   1.000 63.43522  ?  659  PHE   B C   1 
ATOM   19293 O  O   . PHE   B 1 659  ? 33.58500   103.05300 7.52600   1.000 76.62033  ?  659  PHE   B O   1 
ATOM   19294 C  CB  . PHE   B 1 659  ? 34.51300   100.04700 7.48700   1.000 45.47921  ?  659  PHE   B CB  1 
ATOM   19295 C  CG  . PHE   B 1 659  ? 35.56900   98.98500  7.63100   1.000 43.11863  ?  659  PHE   B CG  1 
ATOM   19296 C  CD1 . PHE   B 1 659  ? 35.77600   98.05400  6.62800   1.000 53.63097  ?  659  PHE   B CD1 1 
ATOM   19297 C  CD2 . PHE   B 1 659  ? 36.33900   98.90400  8.78000   1.000 58.24229  ?  659  PHE   B CD2 1 
ATOM   19298 C  CE1 . PHE   B 1 659  ? 36.73900   97.06900  6.76200   1.000 53.95413  ?  659  PHE   B CE1 1 
ATOM   19299 C  CE2 . PHE   B 1 659  ? 37.30400   97.92100  8.92000   1.000 56.08916  ?  659  PHE   B CE2 1 
ATOM   19300 C  CZ  . PHE   B 1 659  ? 37.50400   97.00300  7.90900   1.000 56.91008  ?  659  PHE   B CZ  1 
ATOM   19301 N  N   . VAL   B 1 660  ? 33.13700   102.26600 5.45800   1.000 72.56861  ?  660  VAL   B N   1 
ATOM   19302 C  CA  . VAL   B 1 660  ? 32.05800   103.20800 5.17400   1.000 75.86718  ?  660  VAL   B CA  1 
ATOM   19303 C  C   . VAL   B 1 660  ? 30.79700   102.42300 4.84000   1.000 78.20734  ?  660  VAL   B C   1 
ATOM   19304 O  O   . VAL   B 1 660  ? 30.80200   101.59000 3.92500   1.000 81.52171  ?  660  VAL   B O   1 
ATOM   19305 C  CB  . VAL   B 1 660  ? 32.41300   104.15900 4.02200   1.000 64.19169  ?  660  VAL   B CB  1 
ATOM   19306 C  CG1 . VAL   B 1 660  ? 31.55600   105.41100 4.09500   1.000 63.95466  ?  660  VAL   B CG1 1 
ATOM   19307 C  CG2 . VAL   B 1 660  ? 33.89100   104.50300 4.04900   1.000 63.72905  ?  660  VAL   B CG2 1 
ATOM   19308 N  N   . HIS   B 1 661  ? 29.71700   102.70200 5.56700   1.000 78.28775  ?  661  HIS   B N   1 
ATOM   19309 C  CA  . HIS   B 1 661  ? 28.42200   102.09500 5.29400   1.000 77.63536  ?  661  HIS   B CA  1 
ATOM   19310 C  C   . HIS   B 1 661  ? 27.64900   102.93500 4.28800   1.000 81.63760  ?  661  HIS   B C   1 
ATOM   19311 O  O   . HIS   B 1 661  ? 27.61700   104.16500 4.38000   1.000 79.05973  ?  661  HIS   B O   1 
ATOM   19312 C  CB  . HIS   B 1 661  ? 27.60000   101.95100 6.57500   1.000 77.34421  ?  661  HIS   B CB  1 
ATOM   19313 C  CG  . HIS   B 1 661  ? 26.18600   101.52200 6.33400   1.000 67.88075  ?  661  HIS   B CG  1 
ATOM   19314 N  ND1 . HIS   B 1 661  ? 25.10200   102.20700 6.84100   1.000 80.17063  ?  661  HIS   B ND1 1 
ATOM   19315 C  CD2 . HIS   B 1 661  ? 25.67800   100.48400 5.62900   1.000 59.53136  ?  661  HIS   B CD2 1 
ATOM   19316 C  CE1 . HIS   B 1 661  ? 23.98800   101.60500 6.46300   1.000 75.91696  ?  661  HIS   B CE1 1 
ATOM   19317 N  NE2 . HIS   B 1 661  ? 24.31000   100.55700 5.72700   1.000 59.64390  ?  661  HIS   B NE2 1 
ATOM   19318 N  N   . MET   B 1 662  ? 27.01700   102.26000 3.33000   1.000 81.12240  ?  662  MET   B N   1 
ATOM   19319 C  CA  . MET   B 1 662  ? 26.21600   102.93500 2.32000   1.000 84.34793  ?  662  MET   B CA  1 
ATOM   19320 C  C   . MET   B 1 662  ? 24.98400   102.10200 2.00300   1.000 79.33489  ?  662  MET   B C   1 
ATOM   19321 O  O   . MET   B 1 662  ? 24.96300   100.88400 2.19400   1.000 73.52999  ?  662  MET   B O   1 
ATOM   19322 C  CB  . MET   B 1 662  ? 27.01900   103.19700 1.04200   1.000 69.37155  ?  662  MET   B CB  1 
ATOM   19323 C  CG  . MET   B 1 662  ? 28.04800   104.29400 1.19100   1.000 68.01451  ?  662  MET   B CG  1 
ATOM   19324 S  SD  . MET   B 1 662  ? 29.35600   104.13700 -0.02600  1.000 91.93494  ?  662  MET   B SD  1 
ATOM   19325 C  CE  . MET   B 1 662  ? 28.54000   104.88100 -1.43300  1.000 71.41466  ?  662  MET   B CE  1 
ATOM   19326 N  N   . LYS   B 1 663  ? 23.95000   102.78100 1.51000   1.000 80.47846  ?  663  LYS   B N   1 
ATOM   19327 C  CA  . LYS   B 1 663  ? 22.69300   102.12100 1.18500   1.000 74.19937  ?  663  LYS   B CA  1 
ATOM   19328 C  C   . LYS   B 1 663  ? 22.61600   101.68100 -0.27100  1.000 81.28407  ?  663  LYS   B C   1 
ATOM   19329 O  O   . LYS   B 1 663  ? 21.90700   100.71600 -0.57900  1.000 74.93441  ?  663  LYS   B O   1 
ATOM   19330 C  CB  . LYS   B 1 663  ? 21.51400   103.04600 1.50500   1.000 58.07411  ?  663  LYS   B CB  1 
ATOM   19331 N  N   . ALA   B 1 664  ? 23.33100   102.35900 -1.16900  1.000 84.83556  ?  664  ALA   B N   1 
ATOM   19332 C  CA  . ALA   B 1 664  ? 23.30600   102.01900 -2.58600  1.000 71.66981  ?  664  ALA   B CA  1 
ATOM   19333 C  C   . ALA   B 1 664  ? 24.58600   102.51700 -3.23800  1.000 83.67603  ?  664  ALA   B C   1 
ATOM   19334 O  O   . ALA   B 1 664  ? 24.96500   103.67800 -3.05400  1.000 79.76796  ?  664  ALA   B O   1 
ATOM   19335 C  CB  . ALA   B 1 664  ? 22.08000   102.62400 -3.28000  1.000 91.93997  ?  664  ALA   B CB  1 
ATOM   19336 N  N   . PHE   B 1 665  ? 25.24100   101.63700 -3.99500  1.000 90.80801  ?  665  PHE   B N   1 
ATOM   19337 C  CA  . PHE   B 1 665  ? 26.48700   101.97900 -4.67800  1.000 78.84417  ?  665  PHE   B CA  1 
ATOM   19338 C  C   . PHE   B 1 665  ? 26.19100   102.73100 -5.97000  1.000 76.70436  ?  665  PHE   B C   1 
ATOM   19339 O  O   . PHE   B 1 665  ? 25.45600   102.21400 -6.81900  1.000 71.02782  ?  665  PHE   B O   1 
ATOM   19340 C  CB  . PHE   B 1 665  ? 27.29100   100.72000 -4.99600  1.000 46.19245  ?  665  PHE   B CB  1 
ATOM   19341 C  CG  . PHE   B 1 665  ? 28.26500   100.32200 -3.92000  1.000 62.44916  ?  665  PHE   B CG  1 
ATOM   19342 C  CD1 . PHE   B 1 665  ? 28.36400   101.04900 -2.74500  1.000 68.65609  ?  665  PHE   B CD1 1 
ATOM   19343 C  CD2 . PHE   B 1 665  ? 29.08000   99.21200  -4.08500  1.000 64.98424  ?  665  PHE   B CD2 1 
ATOM   19344 C  CE1 . PHE   B 1 665  ? 29.25800   100.67600 -1.75600  1.000 72.13980  ?  665  PHE   B CE1 1 
ATOM   19345 C  CE2 . PHE   B 1 665  ? 29.97600   98.83400  -3.09900  1.000 61.18081  ?  665  PHE   B CE2 1 
ATOM   19346 C  CZ  . PHE   B 1 665  ? 30.06500   99.56700  -1.93400  1.000 62.86856  ?  665  PHE   B CZ  1 
ATOM   19347 N  N   . PRO   B 1 666  ? 26.71600   103.94300 -6.15200  1.000 83.68794  ?  666  PRO   B N   1 
ATOM   19348 C  CA  . PRO   B 1 666  ? 26.59800   104.61000 -7.45200  1.000 84.96308  ?  666  PRO   B CA  1 
ATOM   19349 C  C   . PRO   B 1 666  ? 27.17300   103.75900 -8.57500  1.000 78.82944  ?  666  PRO   B C   1 
ATOM   19350 O  O   . PRO   B 1 666  ? 28.13500   103.01000 -8.38900  1.000 70.72480  ?  666  PRO   B O   1 
ATOM   19351 C  CB  . PRO   B 1 666  ? 27.41200   105.89700 -7.27000  1.000 94.97007  ?  666  PRO   B CB  1 
ATOM   19352 C  CG  . PRO   B 1 666  ? 27.63200   106.05700 -5.78500  1.000 93.66888  ?  666  PRO   B CG  1 
ATOM   19353 C  CD  . PRO   B 1 666  ? 26.99900   104.89900 -5.07000  1.000 86.15190  ?  666  PRO   B CD  1 
ATOM   19354 N  N   . LEU   B 1 667  ? 26.57400   103.89700 -9.75700  1.000 75.95832  ?  667  LEU   B N   1 
ATOM   19355 C  CA  . LEU   B 1 667  ? 27.00500   103.20400 -10.96300 1.000 78.62743  ?  667  LEU   B CA  1 
ATOM   19356 C  C   . LEU   B 1 667  ? 27.27100   104.22100 -12.06400 1.000 72.76897  ?  667  LEU   B C   1 
ATOM   19357 O  O   . LEU   B 1 667  ? 26.49500   105.16400 -12.24800 1.000 71.25407  ?  667  LEU   B O   1 
ATOM   19358 C  CB  . LEU   B 1 667  ? 25.94800   102.19300 -11.43200 1.000 70.18549  ?  667  LEU   B CB  1 
ATOM   19359 C  CG  . LEU   B 1 667  ? 26.29800   100.70600 -11.32700 1.000 61.11159  ?  667  LEU   B CG  1 
ATOM   19360 C  CD1 . LEU   B 1 667  ? 26.49900   100.28800 -9.88200  1.000 65.06702  ?  667  LEU   B CD1 1 
ATOM   19361 C  CD2 . LEU   B 1 667  ? 25.21800   99.86200  -11.97300 1.000 51.26340  ?  667  LEU   B CD2 1 
ATOM   19362 N  N   . THR   B 1 668  ? 28.37000   104.02800 -12.79300 1.000 68.45117  ?  668  THR   B N   1 
ATOM   19363 C  CA  . THR   B 1 668  ? 28.71700   104.91900 -13.89000 1.000 63.76575  ?  668  THR   B CA  1 
ATOM   19364 C  C   . THR   B 1 668  ? 27.80800   104.66000 -15.09000 1.000 87.33297  ?  668  THR   B C   1 
ATOM   19365 O  O   . THR   B 1 668  ? 26.92600   103.79600 -15.07000 1.000 93.40724  ?  668  THR   B O   1 
ATOM   19366 C  CB  . THR   B 1 668  ? 30.18300   104.74700 -14.28500 1.000 72.07911  ?  668  THR   B CB  1 
ATOM   19367 O  OG1 . THR   B 1 668  ? 30.40000   103.41700 -14.77200 1.000 79.91070  ?  668  THR   B OG1 1 
ATOM   19368 C  CG2 . THR   B 1 668  ? 31.09000   105.00100 -13.09600 1.000 77.48185  ?  668  THR   B CG2 1 
ATOM   19369 N  N   . ALA   B 1 669  ? 28.03900   105.42200 -16.16000 1.000 90.70072  ?  669  ALA   B N   1 
ATOM   19370 C  CA  . ALA   B 1 669  ? 27.23000   105.29700 -17.36500 1.000 81.19333  ?  669  ALA   B CA  1 
ATOM   19371 C  C   . ALA   B 1 669  ? 27.51200   104.01700 -18.13700 1.000 82.34784  ?  669  ALA   B C   1 
ATOM   19372 O  O   . ALA   B 1 669  ? 26.77300   103.70800 -19.07700 1.000 91.04507  ?  669  ALA   B O   1 
ATOM   19373 C  CB  . ALA   B 1 669  ? 27.45200   106.50600 -18.27400 1.000 80.43534  ?  669  ALA   B CB  1 
ATOM   19374 N  N   . ASN   B 1 670  ? 28.54800   103.26500 -17.76500 1.000 65.70328  ?  670  ASN   B N   1 
ATOM   19375 C  CA  . ASN   B 1 670  ? 28.91300   102.04100 -18.46500 1.000 81.70513  ?  670  ASN   B CA  1 
ATOM   19376 C  C   . ASN   B 1 670  ? 28.90000   100.82900 -17.53800 1.000 77.57525  ?  670  ASN   B C   1 
ATOM   19377 O  O   . ASN   B 1 670  ? 29.59200   99.84000  -17.78700 1.000 63.50600  ?  670  ASN   B O   1 
ATOM   19378 C  CB  . ASN   B 1 670  ? 30.27500   102.20100 -19.13500 1.000 79.03206  ?  670  ASN   B CB  1 
ATOM   19379 C  CG  . ASN   B 1 670  ? 30.18100   102.93200 -20.45300 1.000 82.03967  ?  670  ASN   B CG  1 
ATOM   19380 O  OD1 . ASN   B 1 670  ? 30.64200   104.06500 -20.58300 1.000 82.46087  ?  670  ASN   B OD1 1 
ATOM   19381 N  ND2 . ASN   B 1 670  ? 29.56700   102.29000 -21.44100 1.000 77.91696  ?  670  ASN   B ND2 1 
ATOM   19382 N  N   . GLY   B 1 671  ? 28.11300   100.89400 -16.46900 1.000 70.87837  ?  671  GLY   B N   1 
ATOM   19383 C  CA  . GLY   B 1 671  ? 27.93300   99.75000  -15.58900 1.000 65.14623  ?  671  GLY   B CA  1 
ATOM   19384 C  C   . GLY   B 1 671  ? 29.10700   99.43100  -14.68900 1.000 71.62132  ?  671  GLY   B C   1 
ATOM   19385 O  O   . GLY   B 1 671  ? 29.44500   98.25300  -14.51300 1.000 79.43295  ?  671  GLY   B O   1 
ATOM   19386 N  N   . LYS   B 1 672  ? 29.73900   100.44900 -14.11200 1.000 69.91188  ?  672  LYS   B N   1 
ATOM   19387 C  CA  . LYS   B 1 672  ? 30.84400   100.25800 -13.18500 1.000 69.17046  ?  672  LYS   B CA  1 
ATOM   19388 C  C   . LYS   B 1 672  ? 30.62100   101.12200 -11.95400 1.000 74.62326  ?  672  LYS   B C   1 
ATOM   19389 O  O   . LYS   B 1 672  ? 29.94500   102.15200 -12.01300 1.000 75.59457  ?  672  LYS   B O   1 
ATOM   19390 C  CB  . LYS   B 1 672  ? 32.19500   100.60100 -13.83000 1.000 72.99293  ?  672  LYS   B CB  1 
ATOM   19391 C  CG  . LYS   B 1 672  ? 32.54900   99.74400  -15.03500 1.000 61.06581  ?  672  LYS   B CG  1 
ATOM   19392 C  CD  . LYS   B 1 672  ? 33.97400   100.00700 -15.49700 1.000 76.36973  ?  672  LYS   B CD  1 
ATOM   19393 C  CE  . LYS   B 1 672  ? 34.34000   99.14000  -16.69200 1.000 71.83699  ?  672  LYS   B CE  1 
ATOM   19394 N  NZ  . LYS   B 1 672  ? 35.68400   98.51200  -16.54200 1.000 56.87920  ?  672  LYS   B NZ  1 
ATOM   19395 N  N   . VAL   B 1 673  ? 31.18900   100.68500 -10.83100 1.000 67.18292  ?  673  VAL   B N   1 
ATOM   19396 C  CA  . VAL   B 1 673  ? 31.07100   101.44600 -9.59400  1.000 72.97454  ?  673  VAL   B CA  1 
ATOM   19397 C  C   . VAL   B 1 673  ? 31.84600   102.74900 -9.73000  1.000 77.41149  ?  673  VAL   B C   1 
ATOM   19398 O  O   . VAL   B 1 673  ? 33.04200   102.75000 -10.05000 1.000 84.52897  ?  673  VAL   B O   1 
ATOM   19399 C  CB  . VAL   B 1 673  ? 31.57300   100.61700 -8.40200  1.000 68.86203  ?  673  VAL   B CB  1 
ATOM   19400 C  CG1 . VAL   B 1 673  ? 31.79100   101.50800 -7.19300  1.000 64.62593  ?  673  VAL   B CG1 1 
ATOM   19401 C  CG2 . VAL   B 1 673  ? 30.58800   99.50200  -8.07400  1.000 57.81432  ?  673  VAL   B CG2 1 
ATOM   19402 N  N   . ASP   B 1 674  ? 31.16500   103.87100 -9.49400  1.000 70.26410  ?  674  ASP   B N   1 
ATOM   19403 C  CA  . ASP   B 1 674  ? 31.80000   105.18800 -9.54900  1.000 85.02493  ?  674  ASP   B CA  1 
ATOM   19404 C  C   . ASP   B 1 674  ? 32.75500   105.32100 -8.36400  1.000 95.42263  ?  674  ASP   B C   1 
ATOM   19405 O  O   . ASP   B 1 674  ? 32.44300   105.92000 -7.33200  1.000 90.88453  ?  674  ASP   B O   1 
ATOM   19406 C  CB  . ASP   B 1 674  ? 30.74900   106.29100 -9.54800  1.000 78.49158  ?  674  ASP   B CB  1 
ATOM   19407 C  CG  . ASP   B 1 674  ? 31.23200   107.55300 -10.23100 1.000 99.57890  ?  674  ASP   B CG  1 
ATOM   19408 O  OD1 . ASP   B 1 674  ? 32.45700   107.69000 -10.43800 1.000 96.46828  ?  674  ASP   B OD1 1 
ATOM   19409 O  OD2 . ASP   B 1 674  ? 30.38400   108.40900 -10.55700 1.000 105.29339 -1 674  ASP   B OD2 1 
ATOM   19410 N  N   . ARG   B 1 675  ? 33.95200   104.74900 -8.53100  1.000 86.52077  ?  675  ARG   B N   1 
ATOM   19411 C  CA  . ARG   B 1 675  ? 34.92700   104.71800 -7.44300  1.000 75.38327  ?  675  ARG   B CA  1 
ATOM   19412 C  C   . ARG   B 1 675  ? 35.32000   106.12300 -7.00600  1.000 73.15124  ?  675  ARG   B C   1 
ATOM   19413 O  O   . ARG   B 1 675  ? 35.52900   106.37600 -5.81300  1.000 86.60108  ?  675  ARG   B O   1 
ATOM   19414 C  CB  . ARG   B 1 675  ? 36.16300   103.92700 -7.87100  1.000 62.02096  ?  675  ARG   B CB  1 
ATOM   19415 C  CG  . ARG   B 1 675  ? 35.91300   102.44600 -8.11100  1.000 69.47136  ?  675  ARG   B CG  1 
ATOM   19416 C  CD  . ARG   B 1 675  ? 37.22200   101.66900 -8.16200  1.000 83.59796  ?  675  ARG   B CD  1 
ATOM   19417 N  NE  . ARG   B 1 675  ? 38.17700   102.26400 -9.09000  1.000 102.14738 ?  675  ARG   B NE  1 
ATOM   19418 C  CZ  . ARG   B 1 675  ? 38.65900   101.65600 -10.16700 1.000 115.87365 ?  675  ARG   B CZ  1 
ATOM   19419 N  NH1 . ARG   B 1 675  ? 38.30700   100.41900 -10.47900 1.000 112.78506 ?  675  ARG   B NH1 1 
ATOM   19420 N  NH2 . ARG   B 1 675  ? 39.51700   102.30600 -10.94900 1.000 102.75543 ?  675  ARG   B NH2 1 
ATOM   19421 N  N   . ARG   B 1 676  ? 35.42100   107.05400 -7.95600  1.000 73.18575  ?  676  ARG   B N   1 
ATOM   19422 C  CA  . ARG   B 1 676  ? 35.78300   108.42500 -7.62600  1.000 86.88338  ?  676  ARG   B CA  1 
ATOM   19423 C  C   . ARG   B 1 676  ? 34.64500   109.19900 -6.97200  1.000 90.75371  ?  676  ARG   B C   1 
ATOM   19424 O  O   . ARG   B 1 676  ? 34.87400   110.32000 -6.50500  1.000 107.71573 ?  676  ARG   B O   1 
ATOM   19425 C  CB  . ARG   B 1 676  ? 36.25300   109.15800 -8.88500  1.000 76.85008  ?  676  ARG   B CB  1 
ATOM   19426 N  N   . ALA   B 1 677  ? 33.43700   108.63600 -6.91900  1.000 74.37558  ?  677  ALA   B N   1 
ATOM   19427 C  CA  . ALA   B 1 677  ? 32.28700   109.31500 -6.33700  1.000 86.01070  ?  677  ALA   B CA  1 
ATOM   19428 C  C   . ALA   B 1 677  ? 31.91500   108.79200 -4.95700  1.000 90.80531  ?  677  ALA   B C   1 
ATOM   19429 O  O   . ALA   B 1 677  ? 30.90700   109.23300 -4.39400  1.000 88.79360  ?  677  ALA   B O   1 
ATOM   19430 C  CB  . ALA   B 1 677  ? 31.07700   109.20400 -7.27000  1.000 80.98362  ?  677  ALA   B CB  1 
ATOM   19431 N  N   . LEU   B 1 678  ? 32.69400   107.86800 -4.39900  1.000 90.03512  ?  678  LEU   B N   1 
ATOM   19432 C  CA  . LEU   B 1 678  ? 32.42200   107.37500 -3.05900  1.000 76.83637  ?  678  LEU   B CA  1 
ATOM   19433 C  C   . LEU   B 1 678  ? 32.91000   108.38200 -2.01900  1.000 82.26696  ?  678  LEU   B C   1 
ATOM   19434 O  O   . LEU   B 1 678  ? 33.90400   109.08100 -2.24000  1.000 85.72371  ?  678  LEU   B O   1 
ATOM   19435 C  CB  . LEU   B 1 678  ? 33.10200   106.02900 -2.84000  1.000 71.96625  ?  678  LEU   B CB  1 
ATOM   19436 C  CG  . LEU   B 1 678  ? 32.69200   104.92000 -3.81200  1.000 72.41884  ?  678  LEU   B CG  1 
ATOM   19437 C  CD1 . LEU   B 1 678  ? 33.53600   103.68200 -3.59400  1.000 65.58065  ?  678  LEU   B CD1 1 
ATOM   19438 C  CD2 . LEU   B 1 678  ? 31.21700   104.59200 -3.68700  1.000 67.47286  ?  678  LEU   B CD2 1 
ATOM   19439 N  N   . PRO   B 1 679  ? 32.22300   108.47900 -0.88000  1.000 69.26036  ?  679  PRO   B N   1 
ATOM   19440 C  CA  . PRO   B 1 679  ? 32.58700   109.49300 0.11900   1.000 72.92157  ?  679  PRO   B CA  1 
ATOM   19441 C  C   . PRO   B 1 679  ? 34.00500   109.29300 0.63000   1.000 92.08892  ?  679  PRO   B C   1 
ATOM   19442 O  O   . PRO   B 1 679  ? 34.42100   108.17700 0.94800   1.000 88.74127  ?  679  PRO   B O   1 
ATOM   19443 C  CB  . PRO   B 1 679  ? 31.54800   109.28900 1.22800   1.000 68.73704  ?  679  PRO   B CB  1 
ATOM   19444 C  CG  . PRO   B 1 679  ? 31.01800   107.90700 1.01400   1.000 66.07200  ?  679  PRO   B CG  1 
ATOM   19445 C  CD  . PRO   B 1 679  ? 31.05600   107.68600 -0.46200  1.000 72.59890  ?  679  PRO   B CD  1 
ATOM   19446 N  N   . ASP   B 1 680  ? 34.75100   110.39300 0.69600   1.000 102.50443 ?  680  ASP   B N   1 
ATOM   19447 C  CA  . ASP   B 1 680  ? 36.13500   110.38000 1.15100   1.000 86.87882  ?  680  ASP   B CA  1 
ATOM   19448 C  C   . ASP   B 1 680  ? 36.15200   110.64000 2.65300   1.000 95.12884  ?  680  ASP   B C   1 
ATOM   19449 O  O   . ASP   B 1 680  ? 35.88000   111.76000 3.09700   1.000 109.61971 ?  680  ASP   B O   1 
ATOM   19450 C  CB  . ASP   B 1 680  ? 36.95200   111.42600 0.39800   1.000 72.95678  ?  680  ASP   B CB  1 
ATOM   19451 C  CG  . ASP   B 1 680  ? 38.26200   110.87600 -0.12100  1.000 100.33143 ?  680  ASP   B CG  1 
ATOM   19452 O  OD1 . ASP   B 1 680  ? 38.96600   110.19100 0.65200   1.000 102.03887 ?  680  ASP   B OD1 1 
ATOM   19453 O  OD2 . ASP   B 1 680  ? 38.58400   111.12200 -1.30300  1.000 100.62295 -1 680  ASP   B OD2 1 
ATOM   19454 N  N   . VAL   B 1 681  ? 36.46300   109.60500 3.43600   1.000 89.82835  ?  681  VAL   B N   1 
ATOM   19455 C  CA  . VAL   B 1 681  ? 36.52100   109.76900 4.88300   1.000 95.17091  ?  681  VAL   B CA  1 
ATOM   19456 C  C   . VAL   B 1 681  ? 37.73700   110.60600 5.25600   1.000 92.43986  ?  681  VAL   B C   1 
ATOM   19457 O  O   . VAL   B 1 681  ? 38.74500   110.64700 4.53500   1.000 74.05035  ?  681  VAL   B O   1 
ATOM   19458 C  CB  . VAL   B 1 681  ? 36.54800   108.40600 5.59800   1.000 83.65003  ?  681  VAL   B CB  1 
ATOM   19459 C  CG1 . VAL   B 1 681  ? 35.47600   107.49600 5.03300   1.000 78.66112  ?  681  VAL   B CG1 1 
ATOM   19460 C  CG2 . VAL   B 1 681  ? 37.92500   107.76500 5.48000   1.000 71.29445  ?  681  VAL   B CG2 1 
ATOM   19461 N  N   . GLN   B 1 682  ? 37.64300   111.28800 6.39400   1.000 89.16174  ?  682  GLN   B N   1 
ATOM   19462 C  CA  . GLN   B 1 682  ? 38.70700   112.19100 6.82400   1.000 98.44951  ?  682  GLN   B CA  1 
ATOM   19463 C  C   . GLN   B 1 682  ? 39.76700   111.38100 7.55500   1.000 87.75353  ?  682  GLN   B C   1 
ATOM   19464 O  O   . GLN   B 1 682  ? 39.67800   111.12700 8.75800   1.000 78.63049  ?  682  GLN   B O   1 
ATOM   19465 C  CB  . GLN   B 1 682  ? 38.15100   113.31700 7.68800   1.000 85.55972  ?  682  GLN   B CB  1 
ATOM   19466 C  CG  . GLN   B 1 682  ? 38.97800   114.61100 7.66400   1.000 82.31993  ?  682  GLN   B CG  1 
ATOM   19467 C  CD  . GLN   B 1 682  ? 39.53200   114.98700 6.28700   1.000 101.14705 ?  682  GLN   B CD  1 
ATOM   19468 O  OE1 . GLN   B 1 682  ? 38.92800   114.71200 5.24700   1.000 101.93632 ?  682  GLN   B OE1 1 
ATOM   19469 N  NE2 . GLN   B 1 682  ? 40.70000   115.62200 6.28400   1.000 112.09797 ?  682  GLN   B NE2 1 
ATOM   19470 N  N   . ALA   B 1 683  ? 40.78200   110.96600 6.80500   1.000 81.06725  ?  683  ALA   B N   1 
ATOM   19471 C  CA  . ALA   B 1 683  ? 41.91400   110.27100 7.38700   1.000 67.52614  ?  683  ALA   B CA  1 
ATOM   19472 C  C   . ALA   B 1 683  ? 42.78400   111.26000 8.15500   1.000 72.45681  ?  683  ALA   B C   1 
ATOM   19473 O  O   . ALA   B 1 683  ? 42.51400   112.46200 8.21600   1.000 92.87345  ?  683  ALA   B O   1 
ATOM   19474 C  CB  . ALA   B 1 683  ? 42.72000   109.56300 6.30200   1.000 68.11490  ?  683  ALA   B CB  1 
ATOM   19475 N  N   . ASP   B 1 684  ? 43.85400   110.74000 8.74400   1.000 61.31051  ?  684  ASP   B N   1 
ATOM   19476 C  CA  . ASP   B 1 684  ? 44.76000   111.56000 9.52600   1.000 65.33536  ?  684  ASP   B CA  1 
ATOM   19477 C  C   . ASP   B 1 684  ? 46.16700   111.02300 9.35000   1.000 71.10155  ?  684  ASP   B C   1 
ATOM   19478 O  O   . ASP   B 1 684  ? 46.35800   109.81000 9.22400   1.000 77.06791  ?  684  ASP   B O   1 
ATOM   19479 C  CB  . ASP   B 1 684  ? 44.37700   111.55600 11.01100  1.000 57.03579  ?  684  ASP   B CB  1 
ATOM   19480 C  CG  . ASP   B 1 684  ? 44.26100   110.14900 11.57900  1.000 89.31485  ?  684  ASP   B CG  1 
ATOM   19481 O  OD1 . ASP   B 1 684  ? 43.72600   109.26100 10.88000  1.000 89.00896  ?  684  ASP   B OD1 1 
ATOM   19482 O  OD2 . ASP   B 1 684  ? 44.71100   109.92800 12.72300  1.000 90.26734  -1 684  ASP   B OD2 1 
ATOM   19483 N  N   . ALA   B 1 685  ? 47.14500   111.92500 9.32600   1.000 64.89829  ?  685  ALA   B N   1 
ATOM   19484 C  CA  . ALA   B 1 685  ? 48.52400   111.49100 9.47400   1.000 60.39852  ?  685  ALA   B CA  1 
ATOM   19485 C  C   . ALA   B 1 685  ? 48.63800   110.64900 10.73600  1.000 73.60961  ?  685  ALA   B C   1 
ATOM   19486 O  O   . ALA   B 1 685  ? 48.01100   110.95800 11.75300  1.000 80.69173  ?  685  ALA   B O   1 
ATOM   19487 C  CB  . ALA   B 1 685  ? 49.46700   112.69400 9.53800   1.000 65.82606  ?  685  ALA   B CB  1 
ATOM   19488 N  N   . GLU   B 1 686  ? 49.42400   109.57100 10.63900  1.000 65.83950  ?  686  GLU   B N   1 
ATOM   19489 C  CA  . GLU   B 1 686  ? 49.55600   108.48200 11.61000  1.000 60.08166  ?  686  GLU   B CA  1 
ATOM   19490 C  C   . GLU   B 1 686  ? 48.54600   107.37600 11.31400  1.000 59.75888  ?  686  GLU   B C   1 
ATOM   19491 O  O   . GLU   B 1 686  ? 48.74400   106.23700 11.74900  1.000 76.97632  ?  686  GLU   B O   1 
ATOM   19492 C  CB  . GLU   B 1 686  ? 49.41000   108.95700 13.06400  1.000 63.57494  ?  686  GLU   B CB  1 
ATOM   19493 C  CG  . GLU   B 1 686  ? 50.61700   108.66800 13.94600  1.000 84.02133  ?  686  GLU   B CG  1 
ATOM   19494 C  CD  . GLU   B 1 686  ? 51.04200   109.86400 14.77800  1.000 73.12844  ?  686  GLU   B CD  1 
ATOM   19495 O  OE1 . GLU   B 1 686  ? 51.71200   110.75900 14.22200  1.000 66.69644  ?  686  GLU   B OE1 1 
ATOM   19496 O  OE2 . GLU   B 1 686  ? 50.71400   109.90800 15.98400  1.000 71.28714  -1 686  GLU   B OE2 1 
ATOM   19497 N  N   . LEU   B 1 687  ? 47.47900   107.70400 10.58000  1.000 59.18681  ?  687  LEU   B N   1 
ATOM   19498 C  CA  . LEU   B 1 687  ? 46.49900   106.73500 10.06300  1.000 51.18315  ?  687  LEU   B CA  1 
ATOM   19499 C  C   . LEU   B 1 687  ? 46.19800   105.63200 11.07100  1.000 45.05866  ?  687  LEU   B C   1 
ATOM   19500 O  O   . LEU   B 1 687  ? 46.25500   104.43800 10.76800  1.000 48.12169  ?  687  LEU   B O   1 
ATOM   19501 C  CB  . LEU   B 1 687  ? 46.97200   106.13100 8.74000   1.000 41.62024  ?  687  LEU   B CB  1 
ATOM   19502 C  CG  . LEU   B 1 687  ? 46.93700   107.02000 7.49800   1.000 46.46702  ?  687  LEU   B CG  1 
ATOM   19503 C  CD1 . LEU   B 1 687  ? 47.65500   106.34300 6.34200   1.000 49.46864  ?  687  LEU   B CD1 1 
ATOM   19504 C  CD2 . LEU   B 1 687  ? 45.50200   107.35400 7.12100   1.000 57.20953  ?  687  LEU   B CD2 1 
ATOM   19505 N  N   . LEU   B 1 688  ? 45.87600   106.04500 12.29300  1.000 48.99945  ?  688  LEU   B N   1 
ATOM   19506 C  CA  . LEU   B 1 688  ? 45.77700   105.09200 13.39200  1.000 64.59531  ?  688  LEU   B CA  1 
ATOM   19507 C  C   . LEU   B 1 688  ? 44.45900   104.33100 13.35000  1.000 64.37142  ?  688  LEU   B C   1 
ATOM   19508 O  O   . LEU   B 1 688  ? 44.44000   103.09500 13.32900  1.000 63.44394  ?  688  LEU   B O   1 
ATOM   19509 C  CB  . LEU   B 1 688  ? 45.95200   105.82200 14.72400  1.000 54.28953  ?  688  LEU   B CB  1 
ATOM   19510 C  CG  . LEU   B 1 688  ? 47.35100   106.41900 14.88000  1.000 49.42714  ?  688  LEU   B CG  1 
ATOM   19511 C  CD1 . LEU   B 1 688  ? 47.41700   107.40000 16.04100  1.000 55.26411  ?  688  LEU   B CD1 1 
ATOM   19512 C  CD2 . LEU   B 1 688  ? 48.37600   105.31200 15.03600  1.000 47.84114  ?  688  LEU   B CD2 1 
ATOM   19513 N  N   . GLY   B 1 689  ? 43.34500   105.05400 13.33500  1.000 50.69395  ?  689  GLY   B N   1 
ATOM   19514 C  CA  . GLY   B 1 689  ? 42.04100   104.44000 13.24200  1.000 56.93967  ?  689  GLY   B CA  1 
ATOM   19515 C  C   . GLY   B 1 689  ? 41.52200   103.95900 14.58300  1.000 63.20713  ?  689  GLY   B C   1 
ATOM   19516 O  O   . GLY   B 1 689  ? 42.21500   103.95300 15.60300  1.000 61.08582  ?  689  GLY   B O   1 
ATOM   19517 N  N   . GLU   B 1 690  ? 40.26000   103.54100 14.56800  1.000 64.66076  ?  690  GLU   B N   1 
ATOM   19518 C  CA  . GLU   B 1 690  ? 39.59800   103.07800 15.77400  1.000 56.25157  ?  690  GLU   B CA  1 
ATOM   19519 C  C   . GLU   B 1 690  ? 40.30000   101.83500 16.32100  1.000 66.31660  ?  690  GLU   B C   1 
ATOM   19520 O  O   . GLU   B 1 690  ? 41.17500   101.24300 15.68200  1.000 69.20816  ?  690  GLU   B O   1 
ATOM   19521 C  CB  . GLU   B 1 690  ? 38.12500   102.78700 15.48600  1.000 70.96000  ?  690  GLU   B CB  1 
ATOM   19522 C  CG  . GLU   B 1 690  ? 37.49400   103.75900 14.49200  1.000 76.71665  ?  690  GLU   B CG  1 
ATOM   19523 C  CD  . GLU   B 1 690  ? 35.97800   103.67600 14.45400  1.000 77.91985  ?  690  GLU   B CD  1 
ATOM   19524 O  OE1 . GLU   B 1 690  ? 35.39200   102.98300 15.31200  1.000 69.12192  ?  690  GLU   B OE1 1 
ATOM   19525 O  OE2 . GLU   B 1 690  ? 35.37300   104.31000 13.56300  1.000 77.78085  -1 690  GLU   B OE2 1 
ATOM   19526 N  N   . ASP   B 1 691  ? 39.90000   101.44800 17.53300  1.000 62.21202  ?  691  ASP   B N   1 
ATOM   19527 C  CA  . ASP   B 1 691  ? 40.50100   100.34000 18.27500  1.000 61.66533  ?  691  ASP   B CA  1 
ATOM   19528 C  C   . ASP   B 1 691  ? 41.98000   100.57400 18.56800  1.000 49.32778  ?  691  ASP   B C   1 
ATOM   19529 O  O   . ASP   B 1 691  ? 42.70600   99.63200  18.89900  1.000 56.96733  ?  691  ASP   B O   1 
ATOM   19530 C  CB  . ASP   B 1 691  ? 40.30900   99.00200  17.54900  1.000 55.70213  ?  691  ASP   B CB  1 
ATOM   19531 N  N   . TYR   B 1 692  ? 42.43900   101.81700 18.44900  1.000 56.23469  ?  692  TYR   B N   1 
ATOM   19532 C  CA  . TYR   B 1 692  ? 43.78400   102.20700 18.84700  1.000 35.87390  ?  692  TYR   B CA  1 
ATOM   19533 C  C   . TYR   B 1 692  ? 43.70900   102.93900 20.17700  1.000 38.90213  ?  692  TYR   B C   1 
ATOM   19534 O  O   . TYR   B 1 692  ? 42.89000   103.84900 20.34600  1.000 44.17310  ?  692  TYR   B O   1 
ATOM   19535 C  CB  . TYR   B 1 692  ? 44.44200   103.10200 17.79300  1.000 38.52816  ?  692  TYR   B CB  1 
ATOM   19536 C  CG  . TYR   B 1 692  ? 45.72100   103.77000 18.26200  1.000 38.02361  ?  692  TYR   B CG  1 
ATOM   19537 C  CD1 . TYR   B 1 692  ? 46.93400   103.09400 18.22500  1.000 44.24221  ?  692  TYR   B CD1 1 
ATOM   19538 C  CD2 . TYR   B 1 692  ? 45.71600   105.07700 18.74100  1.000 37.82175  ?  692  TYR   B CD2 1 
ATOM   19539 C  CE1 . TYR   B 1 692  ? 48.10300   103.69600 18.65000  1.000 37.57801  ?  692  TYR   B CE1 1 
ATOM   19540 C  CE2 . TYR   B 1 692  ? 46.88100   105.68800 19.17100  1.000 32.72784  ?  692  TYR   B CE2 1 
ATOM   19541 C  CZ  . TYR   B 1 692  ? 48.07200   104.99100 19.12200  1.000 40.89387  ?  692  TYR   B CZ  1 
ATOM   19542 O  OH  . TYR   B 1 692  ? 49.24000   105.58400 19.54400  1.000 37.08762  ?  692  TYR   B OH  1 
ATOM   19543 N  N   . VAL   B 1 693  ? 44.55600   102.53600 21.11800  1.000 40.89525  ?  693  VAL   B N   1 
ATOM   19544 C  CA  . VAL   B 1 693  ? 44.63900   103.16600 22.42800  1.000 30.34044  ?  693  VAL   B CA  1 
ATOM   19545 C  C   . VAL   B 1 693  ? 46.08500   103.58800 22.64600  1.000 36.76387  ?  693  VAL   B C   1 
ATOM   19546 O  O   . VAL   B 1 693  ? 46.99600   102.75500 22.56500  1.000 35.07414  ?  693  VAL   B O   1 
ATOM   19547 C  CB  . VAL   B 1 693  ? 44.16700   102.22700 23.55200  1.000 25.12806  ?  693  VAL   B CB  1 
ATOM   19548 C  CG1 . VAL   B 1 693  ? 43.76200   103.02600 24.77300  1.000 41.19847  ?  693  VAL   B CG1 1 
ATOM   19549 C  CG2 . VAL   B 1 693  ? 43.01000   101.36300 23.07500  1.000 23.60355  ?  693  VAL   B CG2 1 
ATOM   19550 N  N   . ALA   B 1 694  ? 46.29500   104.88100 22.91700  1.000 38.94237  ?  694  ALA   B N   1 
ATOM   19551 C  CA  . ALA   B 1 694  ? 47.63200   105.42200 23.10200  1.000 34.71752  ?  694  ALA   B CA  1 
ATOM   19552 C  C   . ALA   B 1 694  ? 48.20900   105.00300 24.45500  1.000 33.07078  ?  694  ALA   B C   1 
ATOM   19553 O  O   . ALA   B 1 694  ? 47.46300   104.72100 25.39600  1.000 34.93840  ?  694  ALA   B O   1 
ATOM   19554 C  CB  . ALA   B 1 694  ? 47.60600   106.94400 23.00300  1.000 25.33447  ?  694  ALA   B CB  1 
ATOM   19555 N  N   . PRO   B 1 695  ? 49.53700   104.94300 24.56800  1.000 35.92708  ?  695  PRO   B N   1 
ATOM   19556 C  CA  . PRO   B 1 695  ? 50.16000   104.63000 25.86200  1.000 35.49612  ?  695  PRO   B CA  1 
ATOM   19557 C  C   . PRO   B 1 695  ? 49.72500   105.60600 26.94700  1.000 36.69077  ?  695  PRO   B C   1 
ATOM   19558 O  O   . PRO   B 1 695  ? 49.70000   106.82100 26.74100  1.000 45.98430  ?  695  PRO   B O   1 
ATOM   19559 C  CB  . PRO   B 1 695  ? 51.65900   104.74900 25.56700  1.000 32.40032  ?  695  PRO   B CB  1 
ATOM   19560 C  CG  . PRO   B 1 695  ? 51.77700   104.44300 24.12200  1.000 41.48751  ?  695  PRO   B CG  1 
ATOM   19561 C  CD  . PRO   B 1 695  ? 50.52600   104.98100 23.47500  1.000 34.00317  ?  695  PRO   B CD  1 
ATOM   19562 N  N   . THR   B 1 696  ? 49.38800   105.06000 28.11600  1.000 36.47915  ?  696  THR   B N   1 
ATOM   19563 C  CA  . THR   B 1 696  ? 48.94200   105.85100 29.25600  1.000 38.24714  ?  696  THR   B CA  1 
ATOM   19564 C  C   . THR   B 1 696  ? 49.99300   105.96900 30.35300  1.000 37.17292  ?  696  THR   B C   1 
ATOM   19565 O  O   . THR   B 1 696  ? 49.72300   106.59500 31.38300  1.000 46.34156  ?  696  THR   B O   1 
ATOM   19566 C  CB  . THR   B 1 696  ? 47.65200   105.25700 29.84100  1.000 32.11633  ?  696  THR   B CB  1 
ATOM   19567 O  OG1 . THR   B 1 696  ? 47.93700   104.00100 30.47000  1.000 34.96759  ?  696  THR   B OG1 1 
ATOM   19568 C  CG2 . THR   B 1 696  ? 46.62400   105.03700 28.74300  1.000 24.14808  ?  696  THR   B CG2 1 
ATOM   19569 N  N   . ASP   B 1 697  ? 51.17800   105.39200 30.16500  1.000 45.95789  ?  697  ASP   B N   1 
ATOM   19570 C  CA  . ASP   B 1 697  ? 52.23000   105.41600 31.17000  1.000 42.36977  ?  697  ASP   B CA  1 
ATOM   19571 C  C   . ASP   B 1 697  ? 53.57700   105.56600 30.48500  1.000 47.39140  ?  697  ASP   B C   1 
ATOM   19572 O  O   . ASP   B 1 697  ? 53.68700   105.52200 29.25700  1.000 43.84084  ?  697  ASP   B O   1 
ATOM   19573 C  CB  . ASP   B 1 697  ? 52.23800   104.14200 32.02200  1.000 37.99435  ?  697  ASP   B CB  1 
ATOM   19574 C  CG  . ASP   B 1 697  ? 51.10800   104.10300 33.01400  1.000 75.60505  ?  697  ASP   B CG  1 
ATOM   19575 O  OD1 . ASP   B 1 697  ? 51.23700   104.73900 34.08000  1.000 101.93461 ?  697  ASP   B OD1 1 
ATOM   19576 O  OD2 . ASP   B 1 697  ? 50.09400   103.42900 32.73300  1.000 90.28111  -1 697  ASP   B OD2 1 
ATOM   19577 N  N   . GLU   B 1 698  ? 54.61600   105.73200 31.30400  1.000 44.07007  ?  698  GLU   B N   1 
ATOM   19578 C  CA  . GLU   B 1 698  ? 55.97300   105.72000 30.77200  1.000 45.13048  ?  698  GLU   B CA  1 
ATOM   19579 C  C   . GLU   B 1 698  ? 56.36800   104.32000 30.32400  1.000 50.59418  ?  698  GLU   B C   1 
ATOM   19580 O  O   . GLU   B 1 698  ? 57.00100   104.15200 29.27600  1.000 49.37362  ?  698  GLU   B O   1 
ATOM   19581 C  CB  . GLU   B 1 698  ? 56.95000   106.24800 31.82000  1.000 49.49592  ?  698  GLU   B CB  1 
ATOM   19582 C  CG  . GLU   B 1 698  ? 58.39600   106.25800 31.36700  1.000 58.54831  ?  698  GLU   B CG  1 
ATOM   19583 C  CD  . GLU   B 1 698  ? 59.26200   107.15500 32.22300  1.000 83.52036  ?  698  GLU   B CD  1 
ATOM   19584 O  OE1 . GLU   B 1 698  ? 58.70600   108.01500 32.93900  1.000 80.80255  ?  698  GLU   B OE1 1 
ATOM   19585 O  OE2 . GLU   B 1 698  ? 60.50000   107.00000 32.17900  1.000 105.44129 -1 698  GLU   B OE2 1 
ATOM   19586 N  N   . LEU   B 1 699  ? 55.99700   103.30100 31.10400  1.000 45.37931  ?  699  LEU   B N   1 
ATOM   19587 C  CA  . LEU   B 1 699  ? 56.31600   101.93000 30.72600  1.000 49.51035  ?  699  LEU   B CA  1 
ATOM   19588 C  C   . LEU   B 1 699  ? 55.55300   101.51300 29.47600  1.000 43.54871  ?  699  LEU   B C   1 
ATOM   19589 O  O   . LEU   B 1 699  ? 56.12000   100.88100 28.57700  1.000 41.66862  ?  699  LEU   B O   1 
ATOM   19590 C  CB  . LEU   B 1 699  ? 56.01300   100.98100 31.88400  1.000 37.13119  ?  699  LEU   B CB  1 
ATOM   19591 C  CG  . LEU   B 1 699  ? 56.58600   99.56900  31.74300  1.000 36.76975  ?  699  LEU   B CG  1 
ATOM   19592 C  CD1 . LEU   B 1 699  ? 58.10600   99.58700  31.79800  1.000 29.78591  ?  699  LEU   B CD1 1 
ATOM   19593 C  CD2 . LEU   B 1 699  ? 56.01800   98.64900  32.80900  1.000 33.28931  ?  699  LEU   B CD2 1 
ATOM   19594 N  N   . GLU   B 1 700  ? 54.26600   101.85900 29.40000  1.000 40.40228  ?  700  GLU   B N   1 
ATOM   19595 C  CA  . GLU   B 1 700  ? 53.49500   101.55500 28.20000  1.000 36.71568  ?  700  GLU   B CA  1 
ATOM   19596 C  C   . GLU   B 1 700  ? 54.08500   102.25600 26.98300  1.000 38.28928  ?  700  GLU   B C   1 
ATOM   19597 O  O   . GLU   B 1 700  ? 54.10300   101.69500 25.88100  1.000 42.34105  ?  700  GLU   B O   1 
ATOM   19598 C  CB  . GLU   B 1 700  ? 52.03200   101.95000 28.40300  1.000 33.90782  ?  700  GLU   B CB  1 
ATOM   19599 C  CG  . GLU   B 1 700  ? 51.21800   100.91700 29.17000  1.000 40.45086  ?  700  GLU   B CG  1 
ATOM   19600 C  CD  . GLU   B 1 700  ? 49.80400   101.38400 29.44500  1.000 37.90224  ?  700  GLU   B CD  1 
ATOM   19601 O  OE1 . GLU   B 1 700  ? 49.50800   102.55900 29.15200  1.000 40.23544  ?  700  GLU   B OE1 1 
ATOM   19602 O  OE2 . GLU   B 1 700  ? 48.98900   100.58100 29.94800  1.000 43.34265  -1 700  GLU   B OE2 1 
ATOM   19603 N  N   . GLN   B 1 701  ? 54.58700   103.47800 27.16500  1.000 33.51659  ?  701  GLN   B N   1 
ATOM   19604 C  CA  . GLN   B 1 701  ? 55.25600   104.16500 26.06800  1.000 38.21436  ?  701  GLN   B CA  1 
ATOM   19605 C  C   . GLN   B 1 701  ? 56.52700   103.42800 25.65800  1.000 37.37840  ?  701  GLN   B C   1 
ATOM   19606 O  O   . GLN   B 1 701  ? 56.77800   103.21800 24.46600  1.000 42.00653  ?  701  GLN   B O   1 
ATOM   19607 C  CB  . GLN   B 1 701  ? 55.56300   105.61100 26.46700  1.000 41.23188  ?  701  GLN   B CB  1 
ATOM   19608 C  CG  . GLN   B 1 701  ? 56.69200   106.25800 25.68100  1.000 40.36544  ?  701  GLN   B CG  1 
ATOM   19609 C  CD  . GLN   B 1 701  ? 56.31700   106.57100 24.24400  1.000 48.55271  ?  701  GLN   B CD  1 
ATOM   19610 O  OE1 . GLN   B 1 701  ? 55.20300   106.28900 23.79900  1.000 60.62939  ?  701  GLN   B OE1 1 
ATOM   19611 N  NE2 . GLN   B 1 701  ? 57.25300   107.15500 23.50700  1.000 47.89466  ?  701  GLN   B NE2 1 
ATOM   19612 N  N   . GLN   B 1 702  ? 57.33300   103.01300 26.63900  1.000 34.40510  ?  702  GLN   B N   1 
ATOM   19613 C  CA  . GLN   B 1 702  ? 58.57300   102.30400 26.33300  1.000 37.66358  ?  702  GLN   B CA  1 
ATOM   19614 C  C   . GLN   B 1 702  ? 58.29000   100.98300 25.63100  1.000 35.60213  ?  702  GLN   B C   1 
ATOM   19615 O  O   . GLN   B 1 702  ? 58.92000   100.65600 24.61800  1.000 35.66170  ?  702  GLN   B O   1 
ATOM   19616 C  CB  . GLN   B 1 702  ? 59.37800   102.07400 27.61400  1.000 41.11152  ?  702  GLN   B CB  1 
ATOM   19617 C  CG  . GLN   B 1 702  ? 59.86100   103.35200 28.28600  1.000 77.83617  ?  702  GLN   B CG  1 
ATOM   19618 C  CD  . GLN   B 1 702  ? 60.63900   103.09500 29.56700  1.000 86.86701  ?  702  GLN   B CD  1 
ATOM   19619 O  OE1 . GLN   B 1 702  ? 60.61500   101.99200 30.11400  1.000 72.48264  ?  702  GLN   B OE1 1 
ATOM   19620 N  NE2 . GLN   B 1 702  ? 61.32500   104.12300 30.05700  1.000 73.64014  ?  702  GLN   B NE2 1 
ATOM   19621 N  N   . LEU   B 1 703  ? 57.34000   100.20800 26.15900  1.000 34.44837  ?  703  LEU   B N   1 
ATOM   19622 C  CA  . LEU   B 1 703  ? 56.99600   98.93300  25.53800  1.000 34.95354  ?  703  LEU   B CA  1 
ATOM   19623 C  C   . LEU   B 1 703  ? 56.49500   99.13500  24.11400  1.000 43.81551  ?  703  LEU   B C   1 
ATOM   19624 O  O   . LEU   B 1 703  ? 56.83700   98.36200  23.21100  1.000 36.58360  ?  703  LEU   B O   1 
ATOM   19625 C  CB  . LEU   B 1 703  ? 55.94800   98.20700  26.38000  1.000 33.76990  ?  703  LEU   B CB  1 
ATOM   19626 C  CG  . LEU   B 1 703  ? 56.38700   97.76400  27.77800  1.000 34.73807  ?  703  LEU   B CG  1 
ATOM   19627 C  CD1 . LEU   B 1 703  ? 55.19500   97.28400  28.58900  1.000 37.92743  ?  703  LEU   B CD1 1 
ATOM   19628 C  CD2 . LEU   B 1 703  ? 57.44800   96.68000  27.69200  1.000 39.27300  ?  703  LEU   B CD2 1 
ATOM   19629 N  N   . ALA   B 1 704  ? 55.69200   100.17800 23.89200  1.000 36.38290  ?  704  ALA   B N   1 
ATOM   19630 C  CA  . ALA   B 1 704  ? 55.20100   100.45000 22.54700  1.000 37.49463  ?  704  ALA   B CA  1 
ATOM   19631 C  C   . ALA   B 1 704  ? 56.34700   100.77000 21.59900  1.000 34.18845  ?  704  ALA   B C   1 
ATOM   19632 O  O   . ALA   B 1 704  ? 56.30400   100.41200 20.41700  1.000 51.91672  ?  704  ALA   B O   1 
ATOM   19633 C  CB  . ALA   B 1 704  ? 54.18800   101.59300 22.57400  1.000 35.64324  ?  704  ALA   B CB  1 
ATOM   19634 N  N   . GLN   B 1 705  ? 57.39100   101.42700 22.10300  1.000 39.17035  ?  705  GLN   B N   1 
ATOM   19635 C  CA  . GLN   B 1 705  ? 58.53100   101.75900 21.25600  1.000 37.03336  ?  705  GLN   B CA  1 
ATOM   19636 C  C   . GLN   B 1 705  ? 59.31200   100.50900 20.87900  1.000 36.15630  ?  705  GLN   B C   1 
ATOM   19637 O  O   . GLN   B 1 705  ? 59.67300   100.31800 19.71200  1.000 45.05434  ?  705  GLN   B O   1 
ATOM   19638 C  CB  . GLN   B 1 705  ? 59.43100   102.77000 21.96200  1.000 38.16198  ?  705  GLN   B CB  1 
ATOM   19639 C  CG  . GLN   B 1 705  ? 58.80200   104.14300 22.11400  1.000 58.46127  ?  705  GLN   B CG  1 
ATOM   19640 C  CD  . GLN   B 1 705  ? 59.67200   105.24500 21.54500  1.000 70.20392  ?  705  GLN   B CD  1 
ATOM   19641 O  OE1 . GLN   B 1 705  ? 60.71500   105.58100 22.10800  1.000 66.72783  ?  705  GLN   B OE1 1 
ATOM   19642 N  NE2 . GLN   B 1 705  ? 59.25100   105.81100 20.41800  1.000 75.28256  ?  705  GLN   B NE2 1 
ATOM   19643 N  N   . VAL   B 1 706  ? 59.58100   99.64100  21.85700  1.000 32.73669  ?  706  VAL   B N   1 
ATOM   19644 C  CA  . VAL   B 1 706  ? 60.27500   98.39000  21.56600  1.000 26.78101  ?  706  VAL   B CA  1 
ATOM   19645 C  C   . VAL   B 1 706  ? 59.43000   97.52300  20.64600  1.000 33.61470  ?  706  VAL   B C   1 
ATOM   19646 O  O   . VAL   B 1 706  ? 59.93100   96.94500  19.67400  1.000 43.60616  ?  706  VAL   B O   1 
ATOM   19647 C  CB  . VAL   B 1 706  ? 60.62300   97.65000  22.86800  1.000 27.59132  ?  706  VAL   B CB  1 
ATOM   19648 C  CG1 . VAL   B 1 706  ? 61.44400   96.41000  22.55900  1.000 25.80320  ?  706  VAL   B CG1 1 
ATOM   19649 C  CG2 . VAL   B 1 706  ? 61.37000   98.57500  23.81100  1.000 30.51538  ?  706  VAL   B CG2 1 
ATOM   19650 N  N   . TRP   B 1 707  ? 58.13200   97.42000  20.94000  1.000 29.80503  ?  707  TRP   B N   1 
ATOM   19651 C  CA  . TRP   B 1 707  ? 57.23800   96.67200  20.06500  1.000 35.83353  ?  707  TRP   B CA  1 
ATOM   19652 C  C   . TRP   B 1 707  ? 57.28500   97.21800  18.64500  1.000 44.45097  ?  707  TRP   B C   1 
ATOM   19653 O  O   . TRP   B 1 707  ? 57.30300   96.45000  17.67500  1.000 54.91861  ?  707  TRP   B O   1 
ATOM   19654 C  CB  . TRP   B 1 707  ? 55.80900   96.71900  20.60700  1.000 43.03761  ?  707  TRP   B CB  1 
ATOM   19655 C  CG  . TRP   B 1 707  ? 55.51600   95.70100  21.67100  1.000 35.36438  ?  707  TRP   B CG  1 
ATOM   19656 C  CD1 . TRP   B 1 707  ? 56.29200   95.39200  22.74900  1.000 32.61730  ?  707  TRP   B CD1 1 
ATOM   19657 C  CD2 . TRP   B 1 707  ? 54.35100   94.87400  21.76600  1.000 32.87724  ?  707  TRP   B CD2 1 
ATOM   19658 N  NE1 . TRP   B 1 707  ? 55.68800   94.41600  23.50500  1.000 25.42454  ?  707  TRP   B NE1 1 
ATOM   19659 C  CE2 . TRP   B 1 707  ? 54.49400   94.08200  22.92300  1.000 31.68195  ?  707  TRP   B CE2 1 
ATOM   19660 C  CE3 . TRP   B 1 707  ? 53.20300   94.72200  20.98200  1.000 41.08109  ?  707  TRP   B CE3 1 
ATOM   19661 C  CZ2 . TRP   B 1 707  ? 53.53200   93.15300  23.31600  1.000 33.67039  ?  707  TRP   B CZ2 1 
ATOM   19662 C  CZ3 . TRP   B 1 707  ? 52.24800   93.79900  21.37400  1.000 41.46049  ?  707  TRP   B CZ3 1 
ATOM   19663 C  CH2 . TRP   B 1 707  ? 52.41900   93.02700  22.53000  1.000 30.05520  ?  707  TRP   B CH2 1 
ATOM   19664 N  N   . SER   B 1 708  ? 57.32100   98.54700  18.50400  1.000 38.99867  ?  708  SER   B N   1 
ATOM   19665 C  CA  . SER   B 1 708  ? 57.35000   99.15600  17.17700  1.000 40.63246  ?  708  SER   B CA  1 
ATOM   19666 C  C   . SER   B 1 708  ? 58.60100   98.75400  16.40900  1.000 52.22363  ?  708  SER   B C   1 
ATOM   19667 O  O   . SER   B 1 708  ? 58.55000   98.54400  15.19100  1.000 46.52546  ?  708  SER   B O   1 
ATOM   19668 C  CB  . SER   B 1 708  ? 57.26400   100.67800 17.29100  1.000 32.96147  ?  708  SER   B CB  1 
ATOM   19669 O  OG  . SER   B 1 708  ? 55.95200   101.09400 17.62700  1.000 44.96452  ?  708  SER   B OG  1 
ATOM   19670 N  N   . HIS   B 1 709  ? 59.73500   98.64300  17.10400  1.000 39.41594  ?  709  HIS   B N   1 
ATOM   19671 C  CA  . HIS   B 1 709  ? 60.97500   98.27100  16.43300  1.000 41.69180  ?  709  HIS   B CA  1 
ATOM   19672 C  C   . HIS   B 1 709  ? 60.97100   96.79800  16.03900  1.000 48.54700  ?  709  HIS   B C   1 
ATOM   19673 O  O   . HIS   B 1 709  ? 61.36500   96.44700  14.92100  1.000 49.89116  ?  709  HIS   B O   1 
ATOM   19674 C  CB  . HIS   B 1 709  ? 62.17100   98.58800  17.33100  1.000 40.03648  ?  709  HIS   B CB  1 
ATOM   19675 C  CG  . HIS   B 1 709  ? 63.49600   98.36500  16.67100  1.000 53.17906  ?  709  HIS   B CG  1 
ATOM   19676 N  ND1 . HIS   B 1 709  ? 64.32200   97.31200  16.99700  1.000 53.91213  ?  709  HIS   B ND1 1 
ATOM   19677 C  CD2 . HIS   B 1 709  ? 64.13400   99.05800  15.69900  1.000 52.54180  ?  709  HIS   B CD2 1 
ATOM   19678 C  CE1 . HIS   B 1 709  ? 65.41400   97.36600  16.25600  1.000 60.70982  ?  709  HIS   B CE1 1 
ATOM   19679 N  NE2 . HIS   B 1 709  ? 65.32500   98.41700  15.45900  1.000 69.64204  ?  709  HIS   B NE2 1 
ATOM   19680 N  N   . VAL   B 1 710  ? 60.52000   95.92500  16.94000  1.000 45.12287  ?  710  VAL   B N   1 
ATOM   19681 C  CA  . VAL   B 1 710  ? 60.54600   94.49300  16.66500  1.000 42.23659  ?  710  VAL   B CA  1 
ATOM   19682 C  C   . VAL   B 1 710  ? 59.58000   94.14400  15.53900  1.000 42.19981  ?  710  VAL   B C   1 
ATOM   19683 O  O   . VAL   B 1 710  ? 59.92200   93.39900  14.61400  1.000 42.13745  ?  710  VAL   B O   1 
ATOM   19684 C  CB  . VAL   B 1 710  ? 60.23000   93.70100  17.94600  1.000 31.10929  ?  710  VAL   B CB  1 
ATOM   19685 C  CG1 . VAL   B 1 710  ? 60.13100   92.21600  17.64000  1.000 33.97063  ?  710  VAL   B CG1 1 
ATOM   19686 C  CG2 . VAL   B 1 710  ? 61.29000   93.97000  19.00300  1.000 38.63093  ?  710  VAL   B CG2 1 
ATOM   19687 N  N   . LEU   B 1 711  ? 58.36300   94.68200  15.59800  1.000 38.31989  ?  711  LEU   B N   1 
ATOM   19688 C  CA  . LEU   B 1 711  ? 57.33900   94.32100  14.62700  1.000 48.45057  ?  711  LEU   B CA  1 
ATOM   19689 C  C   . LEU   B 1 711  ? 57.40600   95.15900  13.36000  1.000 48.92044  ?  711  LEU   B C   1 
ATOM   19690 O  O   . LEU   B 1 711  ? 56.84400   94.75400  12.33600  1.000 61.00562  ?  711  LEU   B O   1 
ATOM   19691 C  CB  . LEU   B 1 711  ? 55.95500   94.44900  15.26100  1.000 44.82938  ?  711  LEU   B CB  1 
ATOM   19692 C  CG  . LEU   B 1 711  ? 55.66500   93.44500  16.37300  1.000 27.56091  ?  711  LEU   B CG  1 
ATOM   19693 C  CD1 . LEU   B 1 711  ? 54.31800   93.72900  17.01100  1.000 30.20084  ?  711  LEU   B CD1 1 
ATOM   19694 C  CD2 . LEU   B 1 711  ? 55.70900   92.04100  15.80600  1.000 41.84151  ?  711  LEU   B CD2 1 
ATOM   19695 N  N   . GLY   B 1 712  ? 58.07500   96.30600  13.40300  1.000 45.72220  ?  712  GLY   B N   1 
ATOM   19696 C  CA  . GLY   B 1 712  ? 58.18700   97.15200  12.23100  1.000 42.02174  ?  712  GLY   B CA  1 
ATOM   19697 C  C   . GLY   B 1 712  ? 56.94100   97.94300  11.89900  1.000 37.95090  ?  712  GLY   B C   1 
ATOM   19698 O  O   . GLY   B 1 712  ? 56.63500   98.14100  10.71800  1.000 57.05548  ?  712  GLY   B O   1 
ATOM   19699 N  N   . ILE   B 1 713  ? 56.21000   98.40100  12.91000  1.000 35.61637  ?  713  ILE   B N   1 
ATOM   19700 C  CA  . ILE   B 1 713  ? 55.00200   99.19400  12.72900  1.000 39.20858  ?  713  ILE   B CA  1 
ATOM   19701 C  C   . ILE   B 1 713  ? 55.22100   100.52800 13.42900  1.000 44.43822  ?  713  ILE   B C   1 
ATOM   19702 O  O   . ILE   B 1 713  ? 55.62000   100.54300 14.59500  1.000 46.70549  ?  713  ILE   B O   1 
ATOM   19703 C  CB  . ILE   B 1 713  ? 53.74800   98.49400  13.28500  1.000 47.21533  ?  713  ILE   B CB  1 
ATOM   19704 C  CG1 . ILE   B 1 713  ? 53.64100   97.07300  12.72100  1.000 48.31824  ?  713  ILE   B CG1 1 
ATOM   19705 C  CG2 . ILE   B 1 713  ? 52.48900   99.29700  12.96800  1.000 40.31400  ?  713  ILE   B CG2 1 
ATOM   19706 C  CD1 . ILE   B 1 713  ? 52.50500   96.25700  13.30600  1.000 43.74423  ?  713  ILE   B CD1 1 
ATOM   19707 N  N   . PRO   B 1 714  ? 54.98700   101.66500 12.76000  1.000 43.65315  ?  714  PRO   B N   1 
ATOM   19708 C  CA  . PRO   B 1 714  ? 55.32500   102.97100 13.34900  1.000 41.48580  ?  714  PRO   B CA  1 
ATOM   19709 C  C   . PRO   B 1 714  ? 54.72700   103.23000 14.72500  1.000 48.23799  ?  714  PRO   B C   1 
ATOM   19710 O  O   . PRO   B 1 714  ? 55.46500   103.47700 15.68400  1.000 68.22384  ?  714  PRO   B O   1 
ATOM   19711 C  CB  . PRO   B 1 714  ? 54.77300   103.96200 12.31800  1.000 29.71883  ?  714  PRO   B CB  1 
ATOM   19712 C  CG  . PRO   B 1 714  ? 54.84900   103.22600 11.02700  1.000 35.24796  ?  714  PRO   B CG  1 
ATOM   19713 C  CD  . PRO   B 1 714  ? 54.57300   101.78200 11.35100  1.000 40.50410  ?  714  PRO   B CD  1 
ATOM   19714 N  N   . GLN   B 1 715  ? 53.40400   103.19400 14.84500  1.000 34.75406  ?  715  GLN   B N   1 
ATOM   19715 C  CA  . GLN   B 1 715  ? 52.73200   103.48800 16.10600  1.000 44.48675  ?  715  GLN   B CA  1 
ATOM   19716 C  C   . GLN   B 1 715  ? 51.97700   102.25400 16.56900  1.000 51.46454  ?  715  GLN   B C   1 
ATOM   19717 O  O   . GLN   B 1 715  ? 51.07200   101.77700 15.87400  1.000 62.44668  ?  715  GLN   B O   1 
ATOM   19718 C  CB  . GLN   B 1 715  ? 51.77300   104.66900 15.96600  1.000 43.72802  ?  715  GLN   B CB  1 
ATOM   19719 C  CG  . GLN   B 1 715  ? 52.25400   105.75400 15.04200  1.000 56.47528  ?  715  GLN   B CG  1 
ATOM   19720 C  CD  . GLN   B 1 715  ? 52.92100   106.88200 15.79000  1.000 73.44024  ?  715  GLN   B CD  1 
ATOM   19721 O  OE1 . GLN   B 1 715  ? 52.75500   107.02000 17.00100  1.000 74.43698  ?  715  GLN   B OE1 1 
ATOM   19722 N  NE2 . GLN   B 1 715  ? 53.66400   107.71000 15.07100  1.000 86.27647  ?  715  GLN   B NE2 1 
ATOM   19723 N  N   . MET   B 1 716  ? 52.34000   101.74900 17.74100  1.000 31.93472  ?  716  MET   B N   1 
ATOM   19724 C  CA  . MET   B 1 716  ? 51.69200   100.58700 18.32600  1.000 39.46291  ?  716  MET   B CA  1 
ATOM   19725 C  C   . MET   B 1 716  ? 50.77600   101.01700 19.46400  1.000 41.48959  ?  716  MET   B C   1 
ATOM   19726 O  O   . MET   B 1 716  ? 51.14100   101.86600 20.28200  1.000 43.09642  ?  716  MET   B O   1 
ATOM   19727 C  CB  . MET   B 1 716  ? 52.73200   99.58600  18.83000  1.000 35.51622  ?  716  MET   B CB  1 
ATOM   19728 C  CG  . MET   B 1 716  ? 52.26400   98.14400  18.79100  1.000 48.73398  ?  716  MET   B CG  1 
ATOM   19729 S  SD  . MET   B 1 716  ? 52.51200   97.37300  17.18400  1.000 56.85334  ?  716  MET   B SD  1 
ATOM   19730 C  CE  . MET   B 1 716  ? 54.29200   97.36300  17.07300  1.000 48.36871  ?  716  MET   B CE  1 
ATOM   19731 N  N   . GLY   B 1 717  ? 49.57500   100.43200 19.50300  1.000 28.00002  ?  717  GLY   B N   1 
ATOM   19732 C  CA  . GLY   B 1 717  ? 48.62400   100.69100 20.56000  1.000 36.02674  ?  717  GLY   B CA  1 
ATOM   19733 C  C   . GLY   B 1 717  ? 48.71300   99.66800  21.68000  1.000 46.39814  ?  717  GLY   B C   1 
ATOM   19734 O  O   . GLY   B 1 717  ? 49.22300   98.56200  21.50400  1.000 47.40288  ?  717  GLY   B O   1 
ATOM   19735 N  N   . ILE   B 1 718  ? 48.20000   100.05000 22.85300  1.000 37.05105  ?  718  ILE   B N   1 
ATOM   19736 C  CA  . ILE   B 1 718  ? 48.31800   99.17900  24.01600  1.000 43.43571  ?  718  ILE   B CA  1 
ATOM   19737 C  C   . ILE   B 1 718  ? 47.41000   97.96100  23.91300  1.000 38.74212  ?  718  ILE   B C   1 
ATOM   19738 O  O   . ILE   B 1 718  ? 47.59800   96.99200  24.65600  1.000 37.91275  ?  718  ILE   B O   1 
ATOM   19739 C  CB  . ILE   B 1 718  ? 48.03800   99.96200  25.31000  1.000 35.27505  ?  718  ILE   B CB  1 
ATOM   19740 C  CG1 . ILE   B 1 718  ? 46.55000   100.27300 25.43500  1.000 38.58730  ?  718  ILE   B CG1 1 
ATOM   19741 C  CG2 . ILE   B 1 718  ? 48.85000   101.24800 25.34100  1.000 41.19724  ?  718  ILE   B CG2 1 
ATOM   19742 C  CD1 . ILE   B 1 718  ? 46.18800   100.94500 26.72900  1.000 44.28517  ?  718  ILE   B CD1 1 
ATOM   19743 N  N   . ASP   B 1 719  ? 46.43800   97.97000  23.00100  1.000 38.89842  ?  719  ASP   B N   1 
ATOM   19744 C  CA  . ASP   B 1 719  ? 45.54100   96.83700  22.81200  1.000 38.16680  ?  719  ASP   B CA  1 
ATOM   19745 C  C   . ASP   B 1 719  ? 45.80000   96.10300  21.50100  1.000 34.56128  ?  719  ASP   B C   1 
ATOM   19746 O  O   . ASP   B 1 719  ? 44.94500   95.33900  21.04600  1.000 48.10367  ?  719  ASP   B O   1 
ATOM   19747 C  CB  . ASP   B 1 719  ? 44.08400   97.29100  22.88500  1.000 43.01140  ?  719  ASP   B CB  1 
ATOM   19748 C  CG  . ASP   B 1 719  ? 43.56500   97.36500  24.30800  1.000 47.69013  ?  719  ASP   B CG  1 
ATOM   19749 O  OD1 . ASP   B 1 719  ? 44.00200   96.55500  25.15800  1.000 57.73442  ?  719  ASP   B OD1 1 
ATOM   19750 O  OD2 . ASP   B 1 719  ? 42.70200   98.22800  24.56700  1.000 40.68603  -1 719  ASP   B OD2 1 
ATOM   19751 N  N   . ASP   B 1 720  ? 46.96100   96.31800  20.88800  1.000 47.79557  ?  720  ASP   B N   1 
ATOM   19752 C  CA  . ASP   B 1 720  ? 47.33800   95.62100  19.66800  1.000 34.61450  ?  720  ASP   B CA  1 
ATOM   19753 C  C   . ASP   B 1 720  ? 47.96100   94.27500  20.00800  1.000 37.89680  ?  720  ASP   B C   1 
ATOM   19754 O  O   . ASP   B 1 720  ? 48.77500   94.17000  20.93100  1.000 39.28183  ?  720  ASP   B O   1 
ATOM   19755 C  CB  . ASP   B 1 720  ? 48.32300   96.45600  18.85200  1.000 37.54189  ?  720  ASP   B CB  1 
ATOM   19756 C  CG  . ASP   B 1 720  ? 47.73300   97.77100  18.40300  1.000 43.69916  ?  720  ASP   B CG  1 
ATOM   19757 O  OD1 . ASP   B 1 720  ? 46.59700   98.08500  18.82000  1.000 50.03981  ?  720  ASP   B OD1 1 
ATOM   19758 O  OD2 . ASP   B 1 720  ? 48.40700   98.49000  17.63600  1.000 42.59188  -1 720  ASP   B OD2 1 
ATOM   19759 N  N   . HIS   B 1 721  ? 47.57900   93.24800  19.25100  1.000 39.90521  ?  721  HIS   B N   1 
ATOM   19760 C  CA  . HIS   B 1 721  ? 48.01300   91.88400  19.51700  1.000 36.94743  ?  721  HIS   B CA  1 
ATOM   19761 C  C   . HIS   B 1 721  ? 49.31300   91.59500  18.78100  1.000 39.25100  ?  721  HIS   B C   1 
ATOM   19762 O  O   . HIS   B 1 721  ? 49.41200   91.82700  17.57200  1.000 54.55405  ?  721  HIS   B O   1 
ATOM   19763 C  CB  . HIS   B 1 721  ? 46.94200   90.88000  19.09700  1.000 41.94270  ?  721  HIS   B CB  1 
ATOM   19764 C  CG  . HIS   B 1 721  ? 47.18900   89.49200  19.60200  1.000 52.79781  ?  721  HIS   B CG  1 
ATOM   19765 N  ND1 . HIS   B 1 721  ? 48.13200   88.65400  19.04800  1.000 53.02147  ?  721  HIS   B ND1 1 
ATOM   19766 C  CD2 . HIS   B 1 721  ? 46.62100   88.80000  20.61800  1.000 43.95260  ?  721  HIS   B CD2 1 
ATOM   19767 C  CE1 . HIS   B 1 721  ? 48.13200   87.50400  19.69800  1.000 46.86188  ?  721  HIS   B CE1 1 
ATOM   19768 N  NE2 . HIS   B 1 721  ? 47.22400   87.56600  20.65500  1.000 36.24995  ?  721  HIS   B NE2 1 
ATOM   19769 N  N   . PHE   B 1 722  ? 50.29800   91.07400  19.51400  1.000 33.39802  ?  722  PHE   B N   1 
ATOM   19770 C  CA  . PHE   B 1 722  ? 51.61300   90.81500  18.93700  1.000 43.67204  ?  722  PHE   B CA  1 
ATOM   19771 C  C   . PHE   B 1 722  ? 51.51600   89.88800  17.73100  1.000 49.48212  ?  722  PHE   B C   1 
ATOM   19772 O  O   . PHE   B 1 722  ? 51.98400   90.21600  16.63600  1.000 51.88148  ?  722  PHE   B O   1 
ATOM   19773 C  CB  . PHE   B 1 722  ? 52.53400   90.22300  20.00500  1.000 31.05782  ?  722  PHE   B CB  1 
ATOM   19774 C  CG  . PHE   B 1 722  ? 53.99800   90.36500  19.69900  1.000 30.62708  ?  722  PHE   B CG  1 
ATOM   19775 C  CD1 . PHE   B 1 722  ? 54.68500   91.51900  20.04500  1.000 38.00823  ?  722  PHE   B CD1 1 
ATOM   19776 C  CD2 . PHE   B 1 722  ? 54.69400   89.33400  19.09000  1.000 32.23516  ?  722  PHE   B CD2 1 
ATOM   19777 C  CE1 . PHE   B 1 722  ? 56.03800   91.64700  19.77400  1.000 45.14572  ?  722  PHE   B CE1 1 
ATOM   19778 C  CE2 . PHE   B 1 722  ? 56.04700   89.45500  18.81700  1.000 34.69036  ?  722  PHE   B CE2 1 
ATOM   19779 C  CZ  . PHE   B 1 722  ? 56.72000   90.61400  19.15900  1.000 40.98579  ?  722  PHE   B CZ  1 
ATOM   19780 N  N   . LEU   B 1 723  ? 50.89700   88.72100  17.91500  1.000 45.13614  ?  723  LEU   B N   1 
ATOM   19781 C  CA  . LEU   B 1 723  ? 50.87300   87.73200  16.84400  1.000 45.02265  ?  723  LEU   B CA  1 
ATOM   19782 C  C   . LEU   B 1 723  ? 49.95300   88.15100  15.70700  1.000 44.74470  ?  723  LEU   B C   1 
ATOM   19783 O  O   . LEU   B 1 723  ? 50.14500   87.71900  14.56600  1.000 67.36824  ?  723  LEU   B O   1 
ATOM   19784 C  CB  . LEU   B 1 723  ? 50.45700   86.37200  17.39700  1.000 55.48124  ?  723  LEU   B CB  1 
ATOM   19785 C  CG  . LEU   B 1 723  ? 51.25300   85.86500  18.59800  1.000 47.03030  ?  723  LEU   B CG  1 
ATOM   19786 C  CD1 . LEU   B 1 723  ? 50.73900   84.50400  19.04500  1.000 39.48346  ?  723  LEU   B CD1 1 
ATOM   19787 C  CD2 . LEU   B 1 723  ? 52.73200   85.80000  18.25800  1.000 41.76966  ?  723  LEU   B CD2 1 
ATOM   19788 N  N   . GLU   B 1 724  ? 48.96000   88.99100  15.98800  1.000 48.88346  ?  724  GLU   B N   1 
ATOM   19789 C  CA  . GLU   B 1 724  ? 48.05800   89.44900  14.94200  1.000 49.41060  ?  724  GLU   B CA  1 
ATOM   19790 C  C   . GLU   B 1 724  ? 48.65700   90.54800  14.07800  1.000 52.19135  ?  724  GLU   B C   1 
ATOM   19791 O  O   . GLU   B 1 724  ? 48.05400   90.90200  13.05900  1.000 51.02564  ?  724  GLU   B O   1 
ATOM   19792 C  CB  . GLU   B 1 724  ? 46.74500   89.94900  15.54800  1.000 33.84886  ?  724  GLU   B CB  1 
ATOM   19793 C  CG  . GLU   B 1 724  ? 45.83600   88.84800  16.06000  1.000 53.31905  ?  724  GLU   B CG  1 
ATOM   19794 C  CD  . GLU   B 1 724  ? 44.54200   89.38800  16.64100  1.000 59.31356  ?  724  GLU   B CD  1 
ATOM   19795 O  OE1 . GLU   B 1 724  ? 44.24700   90.58700  16.44300  1.000 49.80814  ?  724  GLU   B OE1 1 
ATOM   19796 O  OE2 . GLU   B 1 724  ? 43.82100   88.61200  17.30100  1.000 83.79528  -1 724  GLU   B OE2 1 
ATOM   19797 N  N   . ARG   B 1 725  ? 49.81300   91.09300  14.45400  1.000 44.22532  ?  725  ARG   B N   1 
ATOM   19798 C  CA  . ARG   B 1 725  ? 50.45900   92.18500  13.73600  1.000 48.86567  ?  725  ARG   B CA  1 
ATOM   19799 C  C   . ARG   B 1 725  ? 51.83800   91.77100  13.24000  1.000 46.49425  ?  725  ARG   B C   1 
ATOM   19800 O  O   . ARG   B 1 725  ? 52.77500   92.57100  13.20300  1.000 51.22399  ?  725  ARG   B O   1 
ATOM   19801 C  CB  . ARG   B 1 725  ? 50.55400   93.43100  14.61200  1.000 29.82898  ?  725  ARG   B CB  1 
ATOM   19802 C  CG  . ARG   B 1 725  ? 49.21100   93.92600  15.12000  1.000 34.02965  ?  725  ARG   B CG  1 
ATOM   19803 C  CD  . ARG   B 1 725  ? 48.72500   95.12100  14.32700  1.000 44.74954  ?  725  ARG   B CD  1 
ATOM   19804 N  NE  . ARG   B 1 725  ? 49.20100   96.38100  14.88400  1.000 51.05806  ?  725  ARG   B NE  1 
ATOM   19805 C  CZ  . ARG   B 1 725  ? 49.31100   97.50600  14.19100  1.000 57.29431  ?  725  ARG   B CZ  1 
ATOM   19806 N  NH1 . ARG   B 1 725  ? 49.00100   97.55700  12.90600  1.000 70.81589  ?  725  ARG   B NH1 1 
ATOM   19807 N  NH2 . ARG   B 1 725  ? 49.74300   98.60600  14.80200  1.000 49.63973  ?  725  ARG   B NH2 1 
ATOM   19808 N  N   . GLY   B 1 726  ? 51.97500   90.50600  12.85500  1.000 43.60872  ?  726  GLY   B N   1 
ATOM   19809 C  CA  . GLY   B 1 726  ? 53.23000   89.99300  12.35400  1.000 47.44348  ?  726  GLY   B CA  1 
ATOM   19810 C  C   . GLY   B 1 726  ? 54.12000   89.35000  13.39000  1.000 41.71002  ?  726  GLY   B C   1 
ATOM   19811 O  O   . GLY   B 1 726  ? 55.28500   89.07100  13.08900  1.000 43.29954  ?  726  GLY   B O   1 
ATOM   19812 N  N   . GLY   B 1 727  ? 53.60800   89.10100  14.59300  1.000 59.12980  ?  727  GLY   B N   1 
ATOM   19813 C  CA  . GLY   B 1 727  ? 54.44300   88.54100  15.63900  1.000 48.71372  ?  727  GLY   B CA  1 
ATOM   19814 C  C   . GLY   B 1 727  ? 54.93200   87.14800  15.28400  1.000 51.18840  ?  727  GLY   B C   1 
ATOM   19815 O  O   . GLY   B 1 727  ? 54.19500   86.32400  14.73500  1.000 42.10635  ?  727  GLY   B O   1 
ATOM   19816 N  N   . ASP   B 1 728  ? 56.19100   86.88800  15.61500  1.000 50.34814  ?  728  ASP   B N   1 
ATOM   19817 C  CA  . ASP   B 1 728  ? 56.85200   85.63600  15.30000  1.000 58.53016  ?  728  ASP   B CA  1 
ATOM   19818 C  C   . ASP   B 1 728  ? 57.59000   85.13700  16.53100  1.000 61.10199  ?  728  ASP   B C   1 
ATOM   19819 O  O   . ASP   B 1 728  ? 57.86600   85.89400  17.46500  1.000 62.29776  ?  728  ASP   B O   1 
ATOM   19820 C  CB  . ASP   B 1 728  ? 57.83400   85.80800  14.13500  1.000 59.10315  ?  728  ASP   B CB  1 
ATOM   19821 C  CG  . ASP   B 1 728  ? 57.80000   84.64800  13.17500  1.000 84.37286  ?  728  ASP   B CG  1 
ATOM   19822 O  OD1 . ASP   B 1 728  ? 56.69100   84.28400  12.72800  1.000 98.18618  ?  728  ASP   B OD1 1 
ATOM   19823 O  OD2 . ASP   B 1 728  ? 58.88200   84.10600  12.86300  1.000 96.83628  -1 728  ASP   B OD2 1 
ATOM   19824 N  N   . SER   B 1 729  ? 57.90800   83.84200  16.51900  1.000 60.32340  ?  729  SER   B N   1 
ATOM   19825 C  CA  . SER   B 1 729  ? 58.72600   83.27500  17.58400  1.000 46.82601  ?  729  SER   B CA  1 
ATOM   19826 C  C   . SER   B 1 729  ? 60.07900   83.96500  17.66300  1.000 48.18871  ?  729  SER   B C   1 
ATOM   19827 O  O   . SER   B 1 729  ? 60.58000   84.24900  18.75700  1.000 47.04524  ?  729  SER   B O   1 
ATOM   19828 C  CB  . SER   B 1 729  ? 58.90600   81.77900  17.35700  1.000 54.57044  ?  729  SER   B CB  1 
ATOM   19829 O  OG  . SER   B 1 729  ? 57.78500   81.07800  17.84600  1.000 55.95488  ?  729  SER   B OG  1 
ATOM   19830 N  N   . ILE   B 1 730  ? 60.68900   84.23200  16.50800  1.000 54.13254  ?  730  ILE   B N   1 
ATOM   19831 C  CA  . ILE   B 1 730  ? 61.93900   84.98300  16.48400  1.000 57.77311  ?  730  ILE   B CA  1 
ATOM   19832 C  C   . ILE   B 1 730  ? 61.72600   86.37400  17.06400  1.000 51.34905  ?  730  ILE   B C   1 
ATOM   19833 O  O   . ILE   B 1 730  ? 62.56800   86.89100  17.80900  1.000 49.04529  ?  730  ILE   B O   1 
ATOM   19834 C  CB  . ILE   B 1 730  ? 62.49200   85.04200  15.04800  1.000 55.39542  ?  730  ILE   B CB  1 
ATOM   19835 C  CG1 . ILE   B 1 730  ? 62.81100   83.63400  14.53800  1.000 55.35895  ?  730  ILE   B CG1 1 
ATOM   19836 C  CG2 . ILE   B 1 730  ? 63.73000   85.91500  14.99000  1.000 52.18767  ?  730  ILE   B CG2 1 
ATOM   19837 C  CD1 . ILE   B 1 730  ? 63.54100   82.76300  15.54300  1.000 58.83024  ?  730  ILE   B CD1 1 
ATOM   19838 N  N   . LYS   B 1 731  ? 60.58500   86.99300  16.75000  1.000 50.26814  ?  731  LYS   B N   1 
ATOM   19839 C  CA  . LYS   B 1 731  ? 60.33100   88.35100  17.21300  1.000 42.29433  ?  731  LYS   B CA  1 
ATOM   19840 C  C   . LYS   B 1 731  ? 60.00600   88.39300  18.70000  1.000 42.54837  ?  731  LYS   B C   1 
ATOM   19841 O  O   . LYS   B 1 731  ? 60.25800   89.41000  19.35700  1.000 45.39553  ?  731  LYS   B O   1 
ATOM   19842 C  CB  . LYS   B 1 731  ? 59.20700   88.97600  16.39100  1.000 42.00993  ?  731  LYS   B CB  1 
ATOM   19843 C  CG  . LYS   B 1 731  ? 59.57900   89.18000  14.93200  1.000 37.26567  ?  731  LYS   B CG  1 
ATOM   19844 C  CD  . LYS   B 1 731  ? 58.50000   89.94000  14.18600  1.000 52.55735  ?  731  LYS   B CD  1 
ATOM   19845 C  CE  . LYS   B 1 731  ? 58.81200   90.02300  12.69900  1.000 56.23789  ?  731  LYS   B CE  1 
ATOM   19846 N  NZ  . LYS   B 1 731  ? 57.72700   90.70000  11.93200  1.000 71.09559  ?  731  LYS   B NZ  1 
ATOM   19847 N  N   . VAL   B 1 732  ? 59.45200   87.31200  19.25100  1.000 41.37111  ?  732  VAL   B N   1 
ATOM   19848 C  CA  . VAL   B 1 732  ? 59.29100   87.23700  20.69900  1.000 42.47062  ?  732  VAL   B CA  1 
ATOM   19849 C  C   . VAL   B 1 732  ? 60.65200   87.14900  21.37400  1.000 42.92862  ?  732  VAL   B C   1 
ATOM   19850 O  O   . VAL   B 1 732  ? 60.89400   87.78900  22.40600  1.000 43.59911  ?  732  VAL   B O   1 
ATOM   19851 C  CB  . VAL   B 1 732  ? 58.38800   86.05200  21.08000  1.000 40.41736  ?  732  VAL   B CB  1 
ATOM   19852 C  CG1 . VAL   B 1 732  ? 58.36600   85.86700  22.58800  1.000 30.38409  ?  732  VAL   B CG1 1 
ATOM   19853 C  CG2 . VAL   B 1 732  ? 56.98300   86.27500  20.55300  1.000 29.19166  ?  732  VAL   B CG2 1 
ATOM   19854 N  N   . MET   B 1 733  ? 61.56300   86.36000  20.80200  1.000 40.59588  ?  733  MET   B N   1 
ATOM   19855 C  CA  . MET   B 1 733  ? 62.93500   86.33800  21.29700  1.000 50.19725  ?  733  MET   B CA  1 
ATOM   19856 C  C   . MET   B 1 733  ? 63.59300   87.70100  21.13300  1.000 47.06895  ?  733  MET   B C   1 
ATOM   19857 O  O   . MET   B 1 733  ? 64.28700   88.17800  22.03900  1.000 54.66322  ?  733  MET   B O   1 
ATOM   19858 C  CB  . MET   B 1 733  ? 63.73700   85.26200  20.56700  1.000 52.31295  ?  733  MET   B CB  1 
ATOM   19859 C  CG  . MET   B 1 733  ? 65.24100   85.47800  20.60300  1.000 70.33676  ?  733  MET   B CG  1 
ATOM   19860 S  SD  . MET   B 1 733  ? 66.04600   84.97800  19.06800  1.000 88.96600  ?  733  MET   B SD  1 
ATOM   19861 C  CE  . MET   B 1 733  ? 66.38200   86.57200  18.32700  1.000 44.02373  ?  733  MET   B CE  1 
ATOM   19862 N  N   . GLN   B 1 734  ? 63.37800   88.34600  19.98200  1.000 44.14182  ?  734  GLN   B N   1 
ATOM   19863 C  CA  . GLN   B 1 734  ? 63.93100   89.67800  19.76200  1.000 46.75857  ?  734  GLN   B CA  1 
ATOM   19864 C  C   . GLN   B 1 734  ? 63.38700   90.67300  20.77800  1.000 44.96309  ?  734  GLN   B C   1 
ATOM   19865 O  O   . GLN   B 1 734  ? 64.13800   91.49600  21.31600  1.000 38.14901  ?  734  GLN   B O   1 
ATOM   19866 C  CB  . GLN   B 1 734  ? 63.62500   90.14200  18.33900  1.000 39.92315  ?  734  GLN   B CB  1 
ATOM   19867 C  CG  . GLN   B 1 734  ? 64.66200   91.08800  17.76500  1.000 59.98478  ?  734  GLN   B CG  1 
ATOM   19868 C  CD  . GLN   B 1 734  ? 65.66100   90.37200  16.88500  1.000 60.80960  ?  734  GLN   B CD  1 
ATOM   19869 O  OE1 . GLN   B 1 734  ? 65.34400   89.34800  16.28100  1.000 55.92964  ?  734  GLN   B OE1 1 
ATOM   19870 N  NE2 . GLN   B 1 734  ? 66.87500   90.90500  16.80700  1.000 59.55631  ?  734  GLN   B NE2 1 
ATOM   19871 N  N   . LEU   B 1 735  ? 62.08400   90.60900  21.05700  1.000 42.34898  ?  735  LEU   B N   1 
ATOM   19872 C  CA  . LEU   B 1 735  ? 61.49300   91.48800  22.06100  1.000 45.11227  ?  735  LEU   B CA  1 
ATOM   19873 C  C   . LEU   B 1 735  ? 62.11500   91.24900  23.43100  1.000 46.96437  ?  735  LEU   B C   1 
ATOM   19874 O  O   . LEU   B 1 735  ? 62.54800   92.19300  24.10200  1.000 42.57327  ?  735  LEU   B O   1 
ATOM   19875 C  CB  . LEU   B 1 735  ? 59.98100   91.27500  22.11700  1.000 42.49374  ?  735  LEU   B CB  1 
ATOM   19876 C  CG  . LEU   B 1 735  ? 59.22800   92.15600  23.11300  1.000 32.21357  ?  735  LEU   B CG  1 
ATOM   19877 C  CD1 . LEU   B 1 735  ? 59.15400   93.57900  22.60400  1.000 35.80988  ?  735  LEU   B CD1 1 
ATOM   19878 C  CD2 . LEU   B 1 735  ? 57.83700   91.60400  23.38300  1.000 33.36199  ?  735  LEU   B CD2 1 
ATOM   19879 N  N   . ILE   B 1 736  ? 62.16700   89.98400  23.85800  1.000 43.56113  ?  736  ILE   B N   1 
ATOM   19880 C  CA  . ILE   B 1 736  ? 62.74400   89.63700  25.15500  1.000 38.93228  ?  736  ILE   B CA  1 
ATOM   19881 C  C   . ILE   B 1 736  ? 64.15700   90.18900  25.28400  1.000 39.20238  ?  736  ILE   B C   1 
ATOM   19882 O  O   . ILE   B 1 736  ? 64.53400   90.74500  26.32400  1.000 36.46755  ?  736  ILE   B O   1 
ATOM   19883 C  CB  . ILE   B 1 736  ? 62.71200   88.11000  25.35000  1.000 38.53285  ?  736  ILE   B CB  1 
ATOM   19884 C  CG1 . ILE   B 1 736  ? 61.31300   87.66100  25.77100  1.000 41.26583  ?  736  ILE   B CG1 1 
ATOM   19885 C  CG2 . ILE   B 1 736  ? 63.75000   87.67300  26.36800  1.000 44.72621  ?  736  ILE   B CG2 1 
ATOM   19886 C  CD1 . ILE   B 1 736  ? 61.12800   86.16600  25.75800  1.000 31.41474  ?  736  ILE   B CD1 1 
ATOM   19887 N  N   . HIS   B 1 737  ? 64.95500   90.05800  24.22300  1.000 48.49858  ?  737  HIS   B N   1 
ATOM   19888 C  CA  . HIS   B 1 737  ? 66.32800   90.55300  24.25700  1.000 57.22648  ?  737  HIS   B CA  1 
ATOM   19889 C  C   . HIS   B 1 737  ? 66.36500   92.07700  24.25600  1.000 48.70985  ?  737  HIS   B C   1 
ATOM   19890 O  O   . HIS   B 1 737  ? 67.05500   92.69100  25.07800  1.000 39.76671  ?  737  HIS   B O   1 
ATOM   19891 C  CB  . HIS   B 1 737  ? 67.11300   89.98300  23.07500  1.000 49.45816  ?  737  HIS   B CB  1 
ATOM   19892 C  CG  . HIS   B 1 737  ? 67.47100   88.53800  23.23100  1.000 52.57167  ?  737  HIS   B CG  1 
ATOM   19893 N  ND1 . HIS   B 1 737  ? 67.95000   87.77100  22.19200  1.000 58.91151  ?  737  HIS   B ND1 1 
ATOM   19894 C  CD2 . HIS   B 1 737  ? 67.42200   87.72000  24.31000  1.000 54.46759  ?  737  HIS   B CD2 1 
ATOM   19895 C  CE1 . HIS   B 1 737  ? 68.17800   86.54200  22.62200  1.000 62.03558  ?  737  HIS   B CE1 1 
ATOM   19896 N  NE2 . HIS   B 1 737  ? 67.86700   86.48500  23.90400  1.000 55.27732  ?  737  HIS   B NE2 1 
ATOM   19897 N  N   . GLN   B 1 738  ? 65.62300   92.70800  23.34100  1.000 46.42637  ?  738  GLN   B N   1 
ATOM   19898 C  CA  . GLN   B 1 738  ? 65.55900   94.16500  23.31900  1.000 39.67060  ?  738  GLN   B CA  1 
ATOM   19899 C  C   . GLN   B 1 738  ? 64.94800   94.72800  24.59400  1.000 43.18853  ?  738  GLN   B C   1 
ATOM   19900 O  O   . GLN   B 1 738  ? 65.21700   95.88300  24.94100  1.000 48.54498  ?  738  GLN   B O   1 
ATOM   19901 C  CB  . GLN   B 1 738  ? 64.76500   94.64000  22.10000  1.000 42.61220  ?  738  GLN   B CB  1 
ATOM   19902 C  CG  . GLN   B 1 738  ? 65.50300   94.48600  20.77500  1.000 37.89589  ?  738  GLN   B CG  1 
ATOM   19903 C  CD  . GLN   B 1 738  ? 64.73600   95.08100  19.60900  1.000 57.57395  ?  738  GLN   B CD  1 
ATOM   19904 O  OE1 . GLN   B 1 738  ? 64.13300   96.14900  19.72900  1.000 46.42599  ?  738  GLN   B OE1 1 
ATOM   19905 N  NE2 . GLN   B 1 738  ? 64.75000   94.39000  18.47400  1.000 58.05725  ?  738  GLN   B NE2 1 
ATOM   19906 N  N   . LEU   B 1 739  ? 64.13400   93.94000  25.29900  1.000 56.48927  ?  739  LEU   B N   1 
ATOM   19907 C  CA  . LEU   B 1 739  ? 63.59900   94.36900  26.58500  1.000 44.93662  ?  739  LEU   B CA  1 
ATOM   19908 C  C   . LEU   B 1 739  ? 64.61100   94.19400  27.70600  1.000 45.51274  ?  739  LEU   B C   1 
ATOM   19909 O  O   . LEU   B 1 739  ? 64.60000   94.96600  28.67000  1.000 46.23384  ?  739  LEU   B O   1 
ATOM   19910 C  CB  . LEU   B 1 739  ? 62.32800   93.58600  26.91800  1.000 52.37035  ?  739  LEU   B CB  1 
ATOM   19911 C  CG  . LEU   B 1 739  ? 61.02900   94.06300  26.27300  1.000 46.40642  ?  739  LEU   B CG  1 
ATOM   19912 C  CD1 . LEU   B 1 739  ? 59.87500   93.14600  26.66100  1.000 26.40972  ?  739  LEU   B CD1 1 
ATOM   19913 C  CD2 . LEU   B 1 739  ? 60.75200   95.50200  26.67400  1.000 36.87231  ?  739  LEU   B CD2 1 
ATOM   19914 N  N   . LYS   B 1 740  ? 65.47500   93.18100  27.60900  1.000 48.05660  ?  740  LYS   B N   1 
ATOM   19915 C  CA  . LYS   B 1 740  ? 66.49700   92.98900  28.63200  1.000 46.46035  ?  740  LYS   B CA  1 
ATOM   19916 C  C   . LYS   B 1 740  ? 67.50600   94.12900  28.61000  1.000 54.02160  ?  740  LYS   B C   1 
ATOM   19917 O  O   . LYS   B 1 740  ? 67.97200   94.57500  29.66600  1.000 55.48272  ?  740  LYS   B O   1 
ATOM   19918 C  CB  . LYS   B 1 740  ? 67.19200   91.64200  28.43300  1.000 43.72407  ?  740  LYS   B CB  1 
ATOM   19919 C  CG  . LYS   B 1 740  ? 68.44200   91.44700  29.28000  1.000 67.08669  ?  740  LYS   B CG  1 
ATOM   19920 C  CD  . LYS   B 1 740  ? 68.17800   90.55000  30.48100  1.000 67.84699  ?  740  LYS   B CD  1 
ATOM   19921 C  CE  . LYS   B 1 740  ? 69.45200   89.85200  30.93900  1.000 97.90498  ?  740  LYS   B CE  1 
ATOM   19922 N  NZ  . LYS   B 1 740  ? 70.68100   90.57800  30.50900  1.000 76.30719  ?  740  LYS   B NZ  1 
ATOM   19923 N  N   . ASN   B 1 741  ? 67.83500   94.62900  27.41700  1.000 52.67191  ?  741  ASN   B N   1 
ATOM   19924 C  CA  . ASN   B 1 741  ? 68.79300   95.71900  27.27800  1.000 56.83197  ?  741  ASN   B CA  1 
ATOM   19925 C  C   . ASN   B 1 741  ? 68.28600   97.03400  27.85400  1.000 51.47165  ?  741  ASN   B C   1 
ATOM   19926 O  O   . ASN   B 1 741  ? 69.05200   98.00200  27.90000  1.000 63.74500  ?  741  ASN   B O   1 
ATOM   19927 C  CB  . ASN   B 1 741  ? 69.16400   95.91300  25.80500  1.000 62.01895  ?  741  ASN   B CB  1 
ATOM   19928 C  CG  . ASN   B 1 741  ? 69.81000   94.68000  25.19200  1.000 71.77864  ?  741  ASN   B CG  1 
ATOM   19929 O  OD1 . ASN   B 1 741  ? 70.37700   93.84000  25.89400  1.000 68.77631  ?  741  ASN   B OD1 1 
ATOM   19930 N  ND2 . ASN   B 1 741  ? 69.73500   94.57300  23.87000  1.000 63.99693  ?  741  ASN   B ND2 1 
ATOM   19931 N  N   . ILE   B 1 742  ? 67.02300   97.10400  28.27600  1.000 59.71626  ?  742  ILE   B N   1 
ATOM   19932 C  CA  . ILE   B 1 742  ? 66.49000   98.27000  28.96600  1.000 56.60645  ?  742  ILE   B CA  1 
ATOM   19933 C  C   . ILE   B 1 742  ? 66.02700   97.93300  30.37900  1.000 49.40742  ?  742  ILE   B C   1 
ATOM   19934 O  O   . ILE   B 1 742  ? 65.33300   98.73200  31.00700  1.000 44.00089  ?  742  ILE   B O   1 
ATOM   19935 C  CB  . ILE   B 1 742  ? 65.35700   98.93400  28.15700  1.000 49.58393  ?  742  ILE   B CB  1 
ATOM   19936 C  CG1 . ILE   B 1 742  ? 64.17800   97.97700  27.98700  1.000 49.56040  ?  742  ILE   B CG1 1 
ATOM   19937 C  CG2 . ILE   B 1 742  ? 65.86800   99.39200  26.79700  1.000 37.33744  ?  742  ILE   B CG2 1 
ATOM   19938 C  CD1 . ILE   B 1 742  ? 63.08000   98.52100  27.10500  1.000 39.94417  ?  742  ILE   B CD1 1 
ATOM   19939 N  N   . GLY   B 1 743  ? 66.39800   96.76100  30.88900  1.000 44.59476  ?  743  GLY   B N   1 
ATOM   19940 C  CA  . GLY   B 1 743  ? 66.11100   96.40400  32.26700  1.000 55.37492  ?  743  GLY   B CA  1 
ATOM   19941 C  C   . GLY   B 1 743  ? 64.73000   95.84500  32.52900  1.000 60.16172  ?  743  GLY   B C   1 
ATOM   19942 O  O   . GLY   B 1 743  ? 64.14800   96.11400  33.58700  1.000 59.53478  ?  743  GLY   B O   1 
ATOM   19943 N  N   . LEU   B 1 744  ? 64.18700   95.05900  31.60100  1.000 55.41893  ?  744  LEU   B N   1 
ATOM   19944 C  CA  . LEU   B 1 744  ? 62.85800   94.47900  31.74500  1.000 56.12005  ?  744  LEU   B CA  1 
ATOM   19945 C  C   . LEU   B 1 744  ? 62.92800   92.98600  31.45800  1.000 55.84569  ?  744  LEU   B C   1 
ATOM   19946 O  O   . LEU   B 1 744  ? 63.43500   92.57500  30.40900  1.000 43.92296  ?  744  LEU   B O   1 
ATOM   19947 C  CB  . LEU   B 1 744  ? 61.85400   95.15900  30.80600  1.000 51.29379  ?  744  LEU   B CB  1 
ATOM   19948 C  CG  . LEU   B 1 744  ? 61.60100   96.64600  31.06700  1.000 44.10288  ?  744  LEU   B CG  1 
ATOM   19949 C  CD1 . LEU   B 1 744  ? 61.02800   97.32700  29.83500  1.000 44.58839  ?  744  LEU   B CD1 1 
ATOM   19950 C  CD2 . LEU   B 1 744  ? 60.67800   96.83800  32.25900  1.000 40.63239  ?  744  LEU   B CD2 1 
ATOM   19951 N  N   . SER   B 1 745  ? 62.41700   92.18200  32.38700  1.000 50.93592  ?  745  SER   B N   1 
ATOM   19952 C  CA  . SER   B 1 745  ? 62.46600   90.72900  32.28600  1.000 39.03948  ?  745  SER   B CA  1 
ATOM   19953 C  C   . SER   B 1 745  ? 61.14400   90.19800  31.75000  1.000 46.89609  ?  745  SER   B C   1 
ATOM   19954 O  O   . SER   B 1 745  ? 60.07200   90.58200  32.23200  1.000 51.25398  ?  745  SER   B O   1 
ATOM   19955 C  CB  . SER   B 1 745  ? 62.76800   90.10000  33.64600  1.000 34.99364  ?  745  SER   B CB  1 
ATOM   19956 O  OG  . SER   B 1 745  ? 63.97300   90.61700  34.17800  1.000 62.66383  ?  745  SER   B OG  1 
ATOM   19957 N  N   . LEU   B 1 746  ? 61.22500   89.30600  30.76600  1.000 32.40103  ?  746  LEU   B N   1 
ATOM   19958 C  CA  . LEU   B 1 746  ? 60.03900   88.71000  30.16800  1.000 35.09652  ?  746  LEU   B CA  1 
ATOM   19959 C  C   . LEU   B 1 746  ? 60.35600   87.28200  29.75600  1.000 41.00480  ?  746  LEU   B C   1 
ATOM   19960 O  O   . LEU   B 1 746  ? 61.33600   87.04600  29.04400  1.000 40.64118  ?  746  LEU   B O   1 
ATOM   19961 C  CB  . LEU   B 1 746  ? 59.56500   89.52000  28.95700  1.000 36.52323  ?  746  LEU   B CB  1 
ATOM   19962 C  CG  . LEU   B 1 746  ? 58.35400   88.96700  28.20300  1.000 41.08940  ?  746  LEU   B CG  1 
ATOM   19963 C  CD1 . LEU   B 1 746  ? 57.11700   88.98500  29.08500  1.000 31.47499  ?  746  LEU   B CD1 1 
ATOM   19964 C  CD2 . LEU   B 1 746  ? 58.11300   89.75400  26.92500  1.000 45.13655  ?  746  LEU   B CD2 1 
ATOM   19965 N  N   . ARG   B 1 747  ? 59.53300   86.33800  30.20500  1.000 36.76524  ?  747  ARG   B N   1 
ATOM   19966 C  CA  . ARG   B 1 747  ? 59.68000   84.94600  29.81000  1.000 32.27716  ?  747  ARG   B CA  1 
ATOM   19967 C  C   . ARG   B 1 747  ? 58.93300   84.67900  28.50700  1.000 38.54286  ?  747  ARG   B C   1 
ATOM   19968 O  O   . ARG   B 1 747  ? 57.98900   85.38500  28.14300  1.000 40.83130  ?  747  ARG   B O   1 
ATOM   19969 C  CB  . ARG   B 1 747  ? 59.16700   84.00500  30.90100  1.000 42.59285  ?  747  ARG   B CB  1 
ATOM   19970 C  CG  . ARG   B 1 747  ? 60.01800   83.96300  32.15400  1.000 38.50432  ?  747  ARG   B CG  1 
ATOM   19971 C  CD  . ARG   B 1 747  ? 59.77900   82.67200  32.92500  1.000 42.44093  ?  747  ARG   B CD  1 
ATOM   19972 N  NE  . ARG   B 1 747  ? 58.36000   82.43800  33.16800  1.000 45.80410  ?  747  ARG   B NE  1 
ATOM   19973 C  CZ  . ARG   B 1 747  ? 57.69200   82.89900  34.21800  1.000 63.93485  ?  747  ARG   B CZ  1 
ATOM   19974 N  NH1 . ARG   B 1 747  ? 58.28600   83.62400  35.15200  1.000 57.85769  ?  747  ARG   B NH1 1 
ATOM   19975 N  NH2 . ARG   B 1 747  ? 56.39500   82.62600  34.33300  1.000 59.73323  ?  747  ARG   B NH2 1 
ATOM   19976 N  N   . TYR   B 1 748  ? 59.37300   83.63100  27.80900  1.000 39.82597  ?  748  TYR   B N   1 
ATOM   19977 C  CA  . TYR   B 1 748  ? 58.76500   83.27100  26.53200  1.000 42.64986  ?  748  TYR   B CA  1 
ATOM   19978 C  C   . TYR   B 1 748  ? 57.27400   82.98700  26.68600  1.000 46.70511  ?  748  TYR   B C   1 
ATOM   19979 O  O   . TYR   B 1 748  ? 56.45300   83.45800  25.88900  1.000 36.10036  ?  748  TYR   B O   1 
ATOM   19980 C  CB  . TYR   B 1 748  ? 59.49000   82.06200  25.94400  1.000 37.80478  ?  748  TYR   B CB  1 
ATOM   19981 C  CG  . TYR   B 1 748  ? 59.30300   81.89600  24.45900  1.000 40.99141  ?  748  TYR   B CG  1 
ATOM   19982 C  CD1 . TYR   B 1 748  ? 59.96900   82.71600  23.55600  1.000 42.03565  ?  748  TYR   B CD1 1 
ATOM   19983 C  CD2 . TYR   B 1 748  ? 58.45400   80.92300  23.95900  1.000 53.40518  ?  748  TYR   B CD2 1 
ATOM   19984 C  CE1 . TYR   B 1 748  ? 59.79600   82.56200  22.19700  1.000 45.87142  ?  748  TYR   B CE1 1 
ATOM   19985 C  CE2 . TYR   B 1 748  ? 58.27200   80.76400  22.60900  1.000 73.08650  ?  748  TYR   B CE2 1 
ATOM   19986 C  CZ  . TYR   B 1 748  ? 58.94500   81.58200  21.73100  1.000 71.43646  ?  748  TYR   B CZ  1 
ATOM   19987 O  OH  . TYR   B 1 748  ? 58.75700   81.41200  20.38200  1.000 77.36066  ?  748  TYR   B OH  1 
ATOM   19988 N  N   . ASP   B 1 749  ? 56.90300   82.21900  27.71300  1.000 49.31806  ?  749  ASP   B N   1 
ATOM   19989 C  CA  . ASP   B 1 749  ? 55.50000   81.88600  27.92900  1.000 47.87648  ?  749  ASP   B CA  1 
ATOM   19990 C  C   . ASP   B 1 749  ? 54.67200   83.09400  28.34500  1.000 49.54591  ?  749  ASP   B C   1 
ATOM   19991 O  O   . ASP   B 1 749  ? 53.45200   83.09400  28.14300  1.000 41.86098  ?  749  ASP   B O   1 
ATOM   19992 C  CB  . ASP   B 1 749  ? 55.38200   80.79100  28.98900  1.000 51.61579  ?  749  ASP   B CB  1 
ATOM   19993 C  CG  . ASP   B 1 749  ? 55.91400   81.23000  30.33700  1.000 45.86005  ?  749  ASP   B CG  1 
ATOM   19994 O  OD1 . ASP   B 1 749  ? 57.14600   81.38500  30.47400  1.000 46.85969  ?  749  ASP   B OD1 1 
ATOM   19995 O  OD2 . ASP   B 1 749  ? 55.09600   81.43400  31.25700  1.000 71.52116  -1 749  ASP   B OD2 1 
ATOM   19996 N  N   . GLN   B 1 750  ? 55.30400   84.12000  28.91500  1.000 40.94463  ?  750  GLN   B N   1 
ATOM   19997 C  CA  . GLN   B 1 750  ? 54.54900   85.26700  29.40400  1.000 40.43878  ?  750  GLN   B CA  1 
ATOM   19998 C  C   . GLN   B 1 750  ? 54.04700   86.14100  28.26100  1.000 49.18514  ?  750  GLN   B C   1 
ATOM   19999 O  O   . GLN   B 1 750  ? 53.01000   86.80200  28.39600  1.000 50.88580  ?  750  GLN   B O   1 
ATOM   20000 C  CB  . GLN   B 1 750  ? 55.41000   86.07500  30.37200  1.000 41.18968  ?  750  GLN   B CB  1 
ATOM   20001 C  CG  . GLN   B 1 750  ? 55.88000   85.27500  31.58100  1.000 44.52396  ?  750  GLN   B CG  1 
ATOM   20002 C  CD  . GLN   B 1 750  ? 56.45900   86.15100  32.67100  1.000 36.50779  ?  750  GLN   B CD  1 
ATOM   20003 O  OE1 . GLN   B 1 750  ? 57.33000   86.98200  32.41800  1.000 39.79743  ?  750  GLN   B OE1 1 
ATOM   20004 N  NE2 . GLN   B 1 750  ? 55.96900   85.97500  33.89300  1.000 49.97224  ?  750  GLN   B NE2 1 
ATOM   20005 N  N   . LEU   B 1 751  ? 54.75700   86.15600  27.13200  1.000 43.67121  ?  751  LEU   B N   1 
ATOM   20006 C  CA  . LEU   B 1 751  ? 54.27500   86.90600  25.97800  1.000 32.60909  ?  751  LEU   B CA  1 
ATOM   20007 C  C   . LEU   B 1 751  ? 53.00000   86.28700  25.42100  1.000 39.81869  ?  751  LEU   B C   1 
ATOM   20008 O  O   . LEU   B 1 751  ? 52.06400   87.00500  25.05000  1.000 39.79120  ?  751  LEU   B O   1 
ATOM   20009 C  CB  . LEU   B 1 751  ? 55.36200   86.96700  24.90500  1.000 26.17906  ?  751  LEU   B CB  1 
ATOM   20010 C  CG  . LEU   B 1 751  ? 55.25600   88.02700  23.80600  1.000 27.88354  ?  751  LEU   B CG  1 
ATOM   20011 C  CD1 . LEU   B 1 751  ? 54.30300   87.59000  22.69500  1.000 24.70741  ?  751  LEU   B CD1 1 
ATOM   20012 C  CD2 . LEU   B 1 751  ? 54.84300   89.37600  24.39000  1.000 24.65718  ?  751  LEU   B CD2 1 
ATOM   20013 N  N   . PHE   B 1 752  ? 52.94200   84.95600  25.35900  1.000 34.57225  ?  752  PHE   B N   1 
ATOM   20014 C  CA  . PHE   B 1 752  ? 51.78200   84.28400  24.79400  1.000 30.16615  ?  752  PHE   B CA  1 
ATOM   20015 C  C   . PHE   B 1 752  ? 50.58300   84.28900  25.73400  1.000 43.21864  ?  752  PHE   B C   1 
ATOM   20016 O  O   . PHE   B 1 752  ? 49.46200   84.02400  25.28600  1.000 43.39259  ?  752  PHE   B O   1 
ATOM   20017 C  CB  . PHE   B 1 752  ? 52.15000   82.85300  24.40600  1.000 23.37304  ?  752  PHE   B CB  1 
ATOM   20018 C  CG  . PHE   B 1 752  ? 53.11300   82.77200  23.25600  1.000 27.18821  ?  752  PHE   B CG  1 
ATOM   20019 C  CD1 . PHE   B 1 752  ? 52.66300   82.87500  21.95100  1.000 33.41776  ?  752  PHE   B CD1 1 
ATOM   20020 C  CD2 . PHE   B 1 752  ? 54.46900   82.59900  23.47900  1.000 40.34351  ?  752  PHE   B CD2 1 
ATOM   20021 C  CE1 . PHE   B 1 752  ? 53.54400   82.80400  20.88900  1.000 26.73490  ?  752  PHE   B CE1 1 
ATOM   20022 C  CE2 . PHE   B 1 752  ? 55.35600   82.52500  22.42000  1.000 25.28958  ?  752  PHE   B CE2 1 
ATOM   20023 C  CZ  . PHE   B 1 752  ? 54.89100   82.62700  21.12400  1.000 35.24052  ?  752  PHE   B CZ  1 
ATOM   20024 N  N   . THR   B 1 753  ? 50.79000   84.58000  27.01900  1.000 36.36433  ?  753  THR   B N   1 
ATOM   20025 C  CA  . THR   B 1 753  ? 49.69000   84.79000  27.94900  1.000 29.12868  ?  753  THR   B CA  1 
ATOM   20026 C  C   . THR   B 1 753  ? 49.38100   86.26400  28.16600  1.000 36.94951  ?  753  THR   B C   1 
ATOM   20027 O  O   . THR   B 1 753  ? 48.36300   86.58200  28.79100  1.000 42.78846  ?  753  THR   B O   1 
ATOM   20028 C  CB  . THR   B 1 753  ? 49.99000   84.13300  29.30400  1.000 31.94428  ?  753  THR   B CB  1 
ATOM   20029 O  OG1 . THR   B 1 753  ? 51.27600   84.55600  29.77500  1.000 46.30728  ?  753  THR   B OG1 1 
ATOM   20030 C  CG2 . THR   B 1 753  ? 49.97100   82.62000  29.17500  1.000 32.72680  ?  753  THR   B CG2 1 
ATOM   20031 N  N   . HIS   B 1 754  ? 50.23100   87.16100  27.67000  1.000 43.01970  ?  754  HIS   B N   1 
ATOM   20032 C  CA  . HIS   B 1 754  ? 50.00900   88.60600  27.74900  1.000 40.32444  ?  754  HIS   B CA  1 
ATOM   20033 C  C   . HIS   B 1 754  ? 50.40600   89.22200  26.41600  1.000 37.14147  ?  754  HIS   B C   1 
ATOM   20034 O  O   . HIS   B 1 754  ? 51.40500   89.94400  26.31400  1.000 45.96723  ?  754  HIS   B O   1 
ATOM   20035 C  CB  . HIS   B 1 754  ? 50.80100   89.21900  28.90500  1.000 38.61386  ?  754  HIS   B CB  1 
ATOM   20036 C  CG  . HIS   B 1 754  ? 50.39100   88.71200  30.25100  1.000 46.66993  ?  754  HIS   B CG  1 
ATOM   20037 N  ND1 . HIS   B 1 754  ? 50.81000   87.49700  30.74800  1.000 37.82879  ?  754  HIS   B ND1 1 
ATOM   20038 C  CD2 . HIS   B 1 754  ? 49.59100   89.25300  31.20100  1.000 45.67087  ?  754  HIS   B CD2 1 
ATOM   20039 C  CE1 . HIS   B 1 754  ? 50.29000   87.31300  31.94800  1.000 40.34031  ?  754  HIS   B CE1 1 
ATOM   20040 N  NE2 . HIS   B 1 754  ? 49.54600   88.36300  32.24700  1.000 44.61709  ?  754  HIS   B NE2 1 
ATOM   20041 N  N   . PRO   B 1 755  ? 49.63400   88.95800  25.36200  1.000 29.58037  ?  755  PRO   B N   1 
ATOM   20042 C  CA  . PRO   B 1 755  ? 50.05100   89.33300  24.00800  1.000 32.94618  ?  755  PRO   B CA  1 
ATOM   20043 C  C   . PRO   B 1 755  ? 49.78700   90.78200  23.63100  1.000 30.82449  ?  755  PRO   B C   1 
ATOM   20044 O  O   . PRO   B 1 755  ? 49.88500   91.11600  22.44700  1.000 41.53114  ?  755  PRO   B O   1 
ATOM   20045 C  CB  . PRO   B 1 755  ? 49.21200   88.38600  23.13900  1.000 32.68850  ?  755  PRO   B CB  1 
ATOM   20046 C  CG  . PRO   B 1 755  ? 47.94800   88.23500  23.90600  1.000 42.04070  ?  755  PRO   B CG  1 
ATOM   20047 C  CD  . PRO   B 1 755  ? 48.32300   88.28700  25.36900  1.000 30.47104  ?  755  PRO   B CD  1 
ATOM   20048 N  N   . THR   B 1 756  ? 49.44200   91.64700  24.58200  1.000 26.18095  ?  756  THR   B N   1 
ATOM   20049 C  CA  . THR   B 1 756  ? 49.24900   93.06400  24.31200  1.000 31.56502  ?  756  THR   B CA  1 
ATOM   20050 C  C   . THR   B 1 756  ? 50.03300   93.87600  25.33200  1.000 27.80877  ?  756  THR   B C   1 
ATOM   20051 O  O   . THR   B 1 756  ? 50.38600   93.38700  26.40700  1.000 32.98246  ?  756  THR   B O   1 
ATOM   20052 C  CB  . THR   B 1 756  ? 47.76400   93.47100  24.34700  1.000 37.80569  ?  756  THR   B CB  1 
ATOM   20053 O  OG1 . THR   B 1 756  ? 47.28500   93.47600  25.70000  1.000 29.15392  ?  756  THR   B OG1 1 
ATOM   20054 C  CG2 . THR   B 1 756  ? 46.92600   92.51400  23.51500  1.000 30.47116  ?  756  THR   B CG2 1 
ATOM   20055 N  N   . ILE   B 1 757  ? 50.30600   95.13300  24.97600  1.000 26.36988  ?  757  ILE   B N   1 
ATOM   20056 C  CA  . ILE   B 1 757  ? 51.06700   96.00000  25.87000  1.000 29.83595  ?  757  ILE   B CA  1 
ATOM   20057 C  C   . ILE   B 1 757  ? 50.26900   96.31600  27.12900  1.000 34.17780  ?  757  ILE   B C   1 
ATOM   20058 O  O   . ILE   B 1 757  ? 50.84000   96.42100  28.22400  1.000 36.32727  ?  757  ILE   B O   1 
ATOM   20059 C  CB  . ILE   B 1 757  ? 51.49700   97.27400  25.12000  1.000 37.59192  ?  757  ILE   B CB  1 
ATOM   20060 C  CG1 . ILE   B 1 757  ? 52.47800   96.91100  24.00400  1.000 36.80307  ?  757  ILE   B CG1 1 
ATOM   20061 C  CG2 . ILE   B 1 757  ? 52.13000   98.28000  26.06900  1.000 30.27096  ?  757  ILE   B CG2 1 
ATOM   20062 C  CD1 . ILE   B 1 757  ? 52.66300   97.99900  22.98200  1.000 32.85836  ?  757  ILE   B CD1 1 
ATOM   20063 N  N   . ARG   B 1 758  ? 48.94800   96.46200  27.00500  1.000 36.20122  ?  758  ARG   B N   1 
ATOM   20064 C  CA  . ARG   B 1 758  ? 48.10400   96.66300  28.17800  1.000 30.71018  ?  758  ARG   B CA  1 
ATOM   20065 C  C   . ARG   B 1 758  ? 48.30200   95.54200  29.19100  1.000 36.90689  ?  758  ARG   B C   1 
ATOM   20066 O  O   . ARG   B 1 758  ? 48.53400   95.79400  30.37900  1.000 41.53981  ?  758  ARG   B O   1 
ATOM   20067 C  CB  . ARG   B 1 758  ? 46.63700   96.75500  27.75200  1.000 38.53761  ?  758  ARG   B CB  1 
ATOM   20068 C  CG  . ARG   B 1 758  ? 45.68700   97.23400  28.83600  1.000 31.91981  ?  758  ARG   B CG  1 
ATOM   20069 C  CD  . ARG   B 1 758  ? 44.23300   97.03800  28.42100  1.000 53.12910  ?  758  ARG   B CD  1 
ATOM   20070 N  NE  . ARG   B 1 758  ? 43.75600   98.09800  27.54100  1.000 44.72500  ?  758  ARG   B NE  1 
ATOM   20071 C  CZ  . ARG   B 1 758  ? 43.20800   99.22900  27.96500  1.000 62.59209  ?  758  ARG   B CZ  1 
ATOM   20072 N  NH1 . ARG   B 1 758  ? 43.07200   99.48900  29.25400  1.000 64.72465  ?  758  ARG   B NH1 1 
ATOM   20073 N  NH2 . ARG   B 1 758  ? 42.79000   100.12200 27.07200  1.000 66.45450  ?  758  ARG   B NH2 1 
ATOM   20074 N  N   . GLN   B 1 759  ? 48.22900   94.29000  28.73300  1.000 28.24401  ?  759  GLN   B N   1 
ATOM   20075 C  CA  . GLN   B 1 759  ? 48.41600   93.16300  29.63900  1.000 32.70906  ?  759  GLN   B CA  1 
ATOM   20076 C  C   . GLN   B 1 759  ? 49.87000   93.01400  30.06100  1.000 31.61411  ?  759  GLN   B C   1 
ATOM   20077 O  O   . GLN   B 1 759  ? 50.14600   92.60200  31.19400  1.000 42.32452  ?  759  GLN   B O   1 
ATOM   20078 C  CB  . GLN   B 1 759  ? 47.92900   91.87300  28.98400  1.000 31.31162  ?  759  GLN   B CB  1 
ATOM   20079 C  CG  . GLN   B 1 759  ? 46.52600   91.95800  28.42300  1.000 34.13941  ?  759  GLN   B CG  1 
ATOM   20080 C  CD  . GLN   B 1 759  ? 46.15000   90.72400  27.63600  1.000 43.42281  ?  759  GLN   B CD  1 
ATOM   20081 O  OE1 . GLN   B 1 759  ? 46.14400   90.73600  26.40400  1.000 38.67970  ?  759  GLN   B OE1 1 
ATOM   20082 N  NE2 . GLN   B 1 759  ? 45.83700   89.64500  28.34400  1.000 62.83721  ?  759  GLN   B NE2 1 
ATOM   20083 N  N   . LEU   B 1 760  ? 50.80800   93.33500  29.16800  1.000 30.40331  ?  760  LEU   B N   1 
ATOM   20084 C  CA  . LEU   B 1 760  ? 52.21900   93.14800  29.48200  1.000 29.97637  ?  760  LEU   B CA  1 
ATOM   20085 C  C   . LEU   B 1 760  ? 52.67400   94.10600  30.57300  1.000 39.55083  ?  760  LEU   B C   1 
ATOM   20086 O  O   . LEU   B 1 760  ? 53.49400   93.74200  31.42400  1.000 38.36290  ?  760  LEU   B O   1 
ATOM   20087 C  CB  . LEU   B 1 760  ? 53.06300   93.33200  28.22300  1.000 35.66209  ?  760  LEU   B CB  1 
ATOM   20088 C  CG  . LEU   B 1 760  ? 54.42400   92.64300  28.23200  1.000 39.54860  ?  760  LEU   B CG  1 
ATOM   20089 C  CD1 . LEU   B 1 760  ? 54.25800   91.16900  28.55200  1.000 36.13963  ?  760  LEU   B CD1 1 
ATOM   20090 C  CD2 . LEU   B 1 760  ? 55.11000   92.83600  26.89000  1.000 43.26495  ?  760  LEU   B CD2 1 
ATOM   20091 N  N   . LYS   B 1 761  ? 52.14900   95.33400  30.56300  1.000 32.40360  ?  761  LYS   B N   1 
ATOM   20092 C  CA  . LYS   B 1 761  ? 52.53900   96.31900  31.56400  1.000 29.16584  ?  761  LYS   B CA  1 
ATOM   20093 C  C   . LYS   B 1 761  ? 52.18900   95.85500  32.97300  1.000 35.62128  ?  761  LYS   B C   1 
ATOM   20094 O  O   . LYS   B 1 761  ? 52.99600   96.00200  33.89900  1.000 41.79215  ?  761  LYS   B O   1 
ATOM   20095 C  CB  . LYS   B 1 761  ? 51.87000   97.65700  31.25800  1.000 35.76819  ?  761  LYS   B CB  1 
ATOM   20096 C  CG  . LYS   B 1 761  ? 52.10100   98.70600  32.31700  1.000 36.05839  ?  761  LYS   B CG  1 
ATOM   20097 C  CD  . LYS   B 1 761  ? 50.78400   99.15200  32.91700  1.000 52.24879  ?  761  LYS   B CD  1 
ATOM   20098 C  CE  . LYS   B 1 761  ? 51.01600   99.88900  34.21700  1.000 71.51217  ?  761  LYS   B CE  1 
ATOM   20099 N  NZ  . LYS   B 1 761  ? 51.17100   101.34000 33.96600  1.000 65.53333  ?  761  LYS   B NZ  1 
ATOM   20100 N  N   . ARG   B 1 762  ? 50.99400   95.28800  33.15500  1.000 34.93715  ?  762  ARG   B N   1 
ATOM   20101 C  CA  . ARG   B 1 762  ? 50.59000   94.82200  34.47900  1.000 35.39346  ?  762  ARG   B CA  1 
ATOM   20102 C  C   . ARG   B 1 762  ? 51.50700   93.71200  34.97500  1.000 46.91794  ?  762  ARG   B C   1 
ATOM   20103 O  O   . ARG   B 1 762  ? 51.93000   93.71500  36.13600  1.000 59.74966  ?  762  ARG   B O   1 
ATOM   20104 C  CB  . ARG   B 1 762  ? 49.14200   94.33800  34.45200  1.000 47.85175  ?  762  ARG   B CB  1 
ATOM   20105 C  CG  . ARG   B 1 762  ? 48.11800   95.40400  34.12200  1.000 55.24660  ?  762  ARG   B CG  1 
ATOM   20106 C  CD  . ARG   B 1 762  ? 46.75700   94.76800  33.90500  1.000 48.59420  ?  762  ARG   B CD  1 
ATOM   20107 N  NE  . ARG   B 1 762  ? 45.83300   95.64600  33.19700  1.000 44.49400  ?  762  ARG   B NE  1 
ATOM   20108 C  CZ  . ARG   B 1 762  ? 44.94700   95.22900  32.30300  1.000 51.47381  ?  762  ARG   B CZ  1 
ATOM   20109 N  NH1 . ARG   B 1 762  ? 44.85300   93.95300  31.96400  1.000 50.16301  ?  762  ARG   B NH1 1 
ATOM   20110 N  NH2 . ARG   B 1 762  ? 44.13400   96.11500  31.73300  1.000 49.74516  ?  762  ARG   B NH2 1 
ATOM   20111 N  N   . LEU   B 1 763  ? 51.82000   92.74700  34.10800  1.000 33.99202  ?  763  LEU   B N   1 
ATOM   20112 C  CA  . LEU   B 1 763  ? 52.66000   91.62800  34.52700  1.000 48.79119  ?  763  LEU   B CA  1 
ATOM   20113 C  C   . LEU   B 1 763  ? 54.04700   92.09800  34.95400  1.000 46.91611  ?  763  LEU   B C   1 
ATOM   20114 O  O   . LEU   B 1 763  ? 54.60400   91.60000  35.93900  1.000 43.83849  ?  763  LEU   B O   1 
ATOM   20115 C  CB  . LEU   B 1 763  ? 52.76500   90.60400  33.40000  1.000 43.67769  ?  763  LEU   B CB  1 
ATOM   20116 C  CG  . LEU   B 1 763  ? 53.73900   89.45600  33.65300  1.000 45.13046  ?  763  LEU   B CG  1 
ATOM   20117 C  CD1 . LEU   B 1 763  ? 53.06100   88.35500  34.45300  1.000 49.25318  ?  763  LEU   B CD1 1 
ATOM   20118 C  CD2 . LEU   B 1 763  ? 54.28600   88.92600  32.34100  1.000 45.08763  ?  763  LEU   B CD2 1 
ATOM   20119 N  N   . LEU   B 1 764  ? 54.62300   93.05600  34.22500  1.000 53.66097  ?  764  LEU   B N   1 
ATOM   20120 C  CA  . LEU   B 1 764  ? 55.94000   93.56500  34.59500  1.000 43.51585  ?  764  LEU   B CA  1 
ATOM   20121 C  C   . LEU   B 1 764  ? 55.86600   94.46300  35.82100  1.000 39.69848  ?  764  LEU   B C   1 
ATOM   20122 O  O   . LEU   B 1 764  ? 56.81700   94.52100  36.60700  1.000 46.87859  ?  764  LEU   B O   1 
ATOM   20123 C  CB  . LEU   B 1 764  ? 56.56700   94.31400  33.42000  1.000 34.55860  ?  764  LEU   B CB  1 
ATOM   20124 C  CG  . LEU   B 1 764  ? 56.59100   93.56300  32.08600  1.000 41.38923  ?  764  LEU   B CG  1 
ATOM   20125 C  CD1 . LEU   B 1 764  ? 57.40700   94.32400  31.05700  1.000 31.82110  ?  764  LEU   B CD1 1 
ATOM   20126 C  CD2 . LEU   B 1 764  ? 57.13300   92.15200  32.26400  1.000 45.88645  ?  764  LEU   B CD2 1 
ATOM   20127 N  N   . THR   B 1 765  ? 54.74800   95.16100  36.00700  1.000 42.14135  ?  765  THR   B N   1 
ATOM   20128 C  CA  . THR   B 1 765  ? 54.57200   95.97000  37.20600  1.000 49.31236  ?  765  THR   B CA  1 
ATOM   20129 C  C   . THR   B 1 765  ? 54.28500   95.10400  38.43000  1.000 53.74122  ?  765  THR   B C   1 
ATOM   20130 O  O   . THR   B 1 765  ? 54.86200   95.32900  39.50000  1.000 61.14713  ?  765  THR   B O   1 
ATOM   20131 C  CB  . THR   B 1 765  ? 53.44800   96.98200  36.98400  1.000 49.37490  ?  765  THR   B CB  1 
ATOM   20132 O  OG1 . THR   B 1 765  ? 53.96800   98.12200  36.28900  1.000 63.11228  ?  765  THR   B OG1 1 
ATOM   20133 C  CG2 . THR   B 1 765  ? 52.84800   97.42700  38.30500  1.000 59.02484  ?  765  THR   B CG2 1 
ATOM   20134 N  N   . GLU   B 1 766  ? 53.41400   94.10000  38.28300  1.000 56.34635  ?  766  GLU   B N   1 
ATOM   20135 C  CA  . GLU   B 1 766  ? 53.00200   93.27900  39.41900  1.000 49.75931  ?  766  GLU   B CA  1 
ATOM   20136 C  C   . GLU   B 1 766  ? 54.08300   92.28800  39.83500  1.000 55.29864  ?  766  GLU   B C   1 
ATOM   20137 O  O   . GLU   B 1 766  ? 54.27900   92.05200  41.03300  1.000 60.56262  ?  766  GLU   B O   1 
ATOM   20138 C  CB  . GLU   B 1 766  ? 51.70400   92.54300  39.09000  1.000 51.25817  ?  766  GLU   B CB  1 
ATOM   20139 C  CG  . GLU   B 1 766  ? 50.47300   93.42900  39.15400  1.000 40.36084  ?  766  GLU   B CG  1 
ATOM   20140 C  CD  . GLU   B 1 766  ? 49.27100   92.81900  38.46100  1.000 63.08292  ?  766  GLU   B CD  1 
ATOM   20141 O  OE1 . GLU   B 1 766  ? 49.31400   91.61200  38.13500  1.000 64.39488  ?  766  GLU   B OE1 1 
ATOM   20142 O  OE2 . GLU   B 1 766  ? 48.28600   93.55300  38.23400  1.000 52.53472  -1 766  GLU   B OE2 1 
ATOM   20143 N  N   . GLN   B 1 767  ? 54.78100   91.68800  38.87200  1.000 61.59443  ?  767  GLN   B N   1 
ATOM   20144 C  CA  . GLN   B 1 767  ? 55.89900   90.80100  39.16500  1.000 40.23510  ?  767  GLN   B CA  1 
ATOM   20145 C  C   . GLN   B 1 767  ? 57.21300   91.55300  39.33300  1.000 54.16087  ?  767  GLN   B C   1 
ATOM   20146 O  O   . GLN   B 1 767  ? 58.26300   90.91600  39.47600  1.000 59.11613  ?  767  GLN   B O   1 
ATOM   20147 C  CB  . GLN   B 1 767  ? 56.03500   89.73900  38.07000  1.000 40.44099  ?  767  GLN   B CB  1 
ATOM   20148 C  CG  . GLN   B 1 767  ? 55.56500   88.35100  38.49300  1.000 64.45709  ?  767  GLN   B CG  1 
ATOM   20149 C  CD  . GLN   B 1 767  ? 54.18700   88.36700  39.13400  1.000 70.97281  ?  767  GLN   B CD  1 
ATOM   20150 O  OE1 . GLN   B 1 767  ? 53.25800   88.99400  38.62400  1.000 62.15454  ?  767  GLN   B OE1 1 
ATOM   20151 N  NE2 . GLN   B 1 767  ? 54.04800   87.67200  40.25900  1.000 58.94227  ?  767  GLN   B NE2 1 
ATOM   20152 N  N   . LYS   B 1 768  ? 57.17100   92.88900  39.31900  1.000 51.34648  ?  768  LYS   B N   1 
ATOM   20153 C  CA  . LYS   B 1 768  ? 58.34000   93.73400  39.57600  1.000 54.25311  ?  768  LYS   B CA  1 
ATOM   20154 C  C   . LYS   B 1 768  ? 59.51600   93.36100  38.67500  1.000 47.38970  ?  768  LYS   B C   1 
ATOM   20155 O  O   . LYS   B 1 768  ? 60.67600   93.38100  39.09000  1.000 68.74223  ?  768  LYS   B O   1 
ATOM   20156 C  CB  . LYS   B 1 768  ? 58.73900   93.68400  41.05400  1.000 58.94845  ?  768  LYS   B CB  1 
ATOM   20157 C  CG  . LYS   B 1 768  ? 57.58900   93.98900  42.01100  1.000 58.08707  ?  768  LYS   B CG  1 
ATOM   20158 C  CD  . LYS   B 1 768  ? 58.06300   94.74900  43.24500  1.000 63.25986  ?  768  LYS   B CD  1 
ATOM   20159 C  CE  . LYS   B 1 768  ? 56.98700   94.79100  44.32300  1.000 56.74858  ?  768  LYS   B CE  1 
ATOM   20160 N  NZ  . LYS   B 1 768  ? 57.57500   94.96000  45.68200  1.000 42.89721  ?  768  LYS   B NZ  1 
ATOM   20161 N  N   . GLN   B 1 769  ? 59.21000   93.01600  37.42500  1.000 57.28596  ?  769  GLN   B N   1 
ATOM   20162 C  CA  . GLN   B 1 769  ? 60.23900   92.70100  36.43900  1.000 51.46055  ?  769  GLN   B CA  1 
ATOM   20163 C  C   . GLN   B 1 769  ? 60.64000   93.97900  35.71700  1.000 56.08982  ?  769  GLN   B C   1 
ATOM   20164 O  O   . GLN   B 1 769  ? 60.96100   93.95800  34.52400  1.000 58.32722  ?  769  GLN   B O   1 
ATOM   20165 C  CB  . GLN   B 1 769  ? 59.73500   91.65300  35.43800  1.000 39.24740  ?  769  GLN   B CB  1 
ATOM   20166 C  CG  . GLN   B 1 769  ? 59.31800   90.32100  36.06700  1.000 53.81824  ?  769  GLN   B CG  1 
ATOM   20167 C  CD  . GLN   B 1 769  ? 58.65600   89.37000  35.07800  1.000 60.62460  ?  769  GLN   B CD  1 
ATOM   20168 O  OE1 . GLN   B 1 769  ? 57.49200   88.99800  35.24200  1.000 61.73116  ?  769  GLN   B OE1 1 
ATOM   20169 N  NE2 . GLN   B 1 769  ? 59.39100   88.98500  34.04100  1.000 42.28258  ?  769  GLN   B NE2 1 
ATOM   20170 N  N   . VAL   B 1 770  ? 60.61200   95.09700  36.44100  1.000 62.00349  ?  770  VAL   B N   1 
ATOM   20171 C  CA  . VAL   B 1 770  ? 60.79400   96.40900  35.83200  1.000 57.73845  ?  770  VAL   B CA  1 
ATOM   20172 C  C   . VAL   B 1 770  ? 62.21100   96.95100  35.97600  1.000 67.58260  ?  770  VAL   B C   1 
ATOM   20173 O  O   . VAL   B 1 770  ? 62.62000   97.79300  35.16200  1.000 84.93515  ?  770  VAL   B O   1 
ATOM   20174 C  CB  . VAL   B 1 770  ? 59.78600   97.42600  36.40600  1.000 62.27277  ?  770  VAL   B CB  1 
ATOM   20175 C  CG1 . VAL   B 1 770  ? 58.41800   97.22000  35.77900  1.000 64.59188  ?  770  VAL   B CG1 1 
ATOM   20176 C  CG2 . VAL   B 1 770  ? 59.71200   97.30900  37.92400  1.000 63.86816  ?  770  VAL   B CG2 1 
ATOM   20177 N  N   . ASN   B 1 771  A 62.96400   96.51400  36.98000  1.000 63.51660  ?  770  ASN   B N   1 
ATOM   20178 C  CA  . ASN   B 1 771  A 64.33600   96.96100  37.17800  1.000 90.77329  ?  770  ASN   B CA  1 
ATOM   20179 C  C   . ASN   B 1 771  A 65.24700   95.74600  37.24300  1.000 89.70100  ?  770  ASN   B C   1 
ATOM   20180 O  O   . ASN   B 1 771  A 64.99100   94.81200  38.01000  1.000 108.36441 ?  770  ASN   B O   1 
ATOM   20181 C  CB  . ASN   B 1 771  A 64.47600   97.80600  38.45100  1.000 92.97893  ?  770  ASN   B CB  1 
ATOM   20182 C  CG  . ASN   B 1 771  A 63.84700   99.18600  38.31400  1.000 91.07942  ?  770  ASN   B CG  1 
ATOM   20183 O  OD1 . ASN   B 1 771  A 64.27700   100.00000 37.49700  1.000 89.86730  ?  770  ASN   B OD1 1 
ATOM   20184 N  ND2 . ASN   B 1 771  A 62.82500   99.45400  39.12200  1.000 83.10642  ?  770  ASN   B ND2 1 
ATOM   20185 N  N   . GLY   B 1 772  B 66.30100   95.75900  36.43400  1.000 70.91661  ?  770  GLY   B N   1 
ATOM   20186 C  CA  . GLY   B 1 772  B 67.22000   94.63900  36.39200  1.000 91.48393  ?  770  GLY   B CA  1 
ATOM   20187 C  C   . GLY   B 1 772  B 68.54300   95.05400  35.79700  1.000 99.01015  ?  770  GLY   B C   1 
ATOM   20188 O  O   . GLY   B 1 772  B 68.64400   96.05800  35.08500  1.000 85.52459  ?  770  GLY   B O   1 
ATOM   20189 N  N   . LEU   B 1 773  ? 69.56400   94.25700  36.09600  1.000 103.81816 ?  771  LEU   B N   1 
ATOM   20190 C  CA  . LEU   B 1 773  ? 70.91200   94.56800  35.64600  1.000 102.76330 ?  771  LEU   B CA  1 
ATOM   20191 C  C   . LEU   B 1 773  ? 71.06300   94.26900  34.15700  1.000 95.47060  ?  771  LEU   B C   1 
ATOM   20192 O  O   . LEU   B 1 773  ? 70.59200   93.24200  33.66000  1.000 90.51095  ?  771  LEU   B O   1 
ATOM   20193 C  CB  . LEU   B 1 773  ? 71.93400   93.77600  36.46300  1.000 93.08920  ?  771  LEU   B CB  1 
ATOM   20194 C  CG  . LEU   B 1 773  ? 71.72500   93.81700  37.98200  1.000 97.03088  ?  771  LEU   B CG  1 
ATOM   20195 C  CD1 . LEU   B 1 773  ? 70.98200   92.57900  38.47600  1.000 93.97104  ?  771  LEU   B CD1 1 
ATOM   20196 C  CD2 . LEU   B 1 773  ? 73.04000   93.97800  38.72500  1.000 106.51443 ?  771  LEU   B CD2 1 
ATOM   20197 N  N   . LEU   B 1 774  ? 71.71600   95.18800  33.44400  1.000 84.53710  ?  772  LEU   B N   1 
ATOM   20198 C  CA  . LEU   B 1 774  ? 71.96300   95.05600  32.00800  1.000 80.21555  ?  772  LEU   B CA  1 
ATOM   20199 C  C   . LEU   B 1 774  ? 73.27100   94.29000  31.82900  1.000 86.92227  ?  772  LEU   B C   1 
ATOM   20200 O  O   . LEU   B 1 774  ? 74.33700   94.86700  31.71300  1.000 84.37010  ?  772  LEU   B O   1 
ATOM   20201 C  CB  . LEU   B 1 774  ? 72.05000   96.42500  31.34300  1.000 77.94775  ?  772  LEU   B CB  1 
ATOM   20202 C  CG  . LEU   B 1 774  ? 70.88800   97.42300  31.32100  1.000 84.68033  ?  772  LEU   B CG  1 
ATOM   20203 C  CD1 . LEU   B 1 774  ? 70.74800   98.15300  32.64700  1.000 82.43924  ?  772  LEU   B CD1 1 
ATOM   20204 C  CD2 . LEU   B 1 774  ? 71.13500   98.42000  30.20400  1.000 73.57778  ?  772  LEU   B CD2 1 
ATOM   20205 N  N   . GLU   B 1 775  ? 73.19600   92.96800  31.80500  1.000 87.08043  ?  773  GLU   B N   1 
ATOM   20206 C  CA  . GLU   B 1 775  ? 74.39200   92.13300  31.80400  1.000 75.68104  ?  773  GLU   B CA  1 
ATOM   20207 C  C   . GLU   B 1 775  ? 74.85100   91.85700  30.37500  1.000 70.16351  ?  773  GLU   B C   1 
ATOM   20208 O  O   . GLU   B 1 775  ? 74.19400   91.07800  29.66600  1.000 79.02894  ?  773  GLU   B O   1 
ATOM   20209 C  CB  . GLU   B 1 775  ? 74.11600   90.83400  32.51900  1.000 70.55518  ?  773  GLU   B CB  1 
ATOM   20210 C  CG  . GLU   B 1 775  ? 73.59000   90.98300  33.93900  1.000 71.59680  ?  773  GLU   B CG  1 
ATOM   20211 C  CD  . GLU   B 1 775  ? 72.68200   89.86700  34.35200  1.000 101.91592 ?  773  GLU   B CD  1 
ATOM   20212 O  OE1 . GLU   B 1 775  ? 71.66800   89.66200  33.66200  1.000 106.39333 ?  773  GLU   B OE1 1 
ATOM   20213 O  OE2 . GLU   B 1 775  ? 72.98000   89.20400  35.36600  1.000 108.04950 -1 773  GLU   B OE2 1 
ATOM   20214 N  N   . PRO   B 1 776  ? 75.98200   92.40000  29.92400  1.000 71.67605  ?  774  PRO   B N   1 
ATOM   20215 C  CA  . PRO   B 1 776  ? 76.43200   92.10600  28.55600  1.000 73.07915  ?  774  PRO   B CA  1 
ATOM   20216 C  C   . PRO   B 1 776  ? 77.40100   90.92600  28.54100  1.000 61.40955  ?  774  PRO   B C   1 
ATOM   20217 O  O   . PRO   B 1 776  ? 77.78300   90.39500  29.58300  1.000 62.90190  ?  774  PRO   B O   1 
ATOM   20218 C  CB  . PRO   B 1 776  ? 77.17700   93.41300  28.11400  1.000 59.97981  ?  774  PRO   B CB  1 
ATOM   20219 C  CG  . PRO   B 1 776  ? 77.46200   94.15400  29.38000  1.000 73.95196  ?  774  PRO   B CG  1 
ATOM   20220 C  CD  . PRO   B 1 776  ? 76.72200   93.53200  30.54100  1.000 81.27691  ?  774  PRO   B CD  1 
ATOM   20221 N  N   . LEU   B 1 777  ? 77.76200   90.51500  27.32800  1.000 58.73562  ?  775  LEU   B N   1 
ATOM   20222 C  CA  . LEU   B 1 777  ? 78.65000   89.38300  27.10600  1.000 64.63540  ?  775  LEU   B CA  1 
ATOM   20223 C  C   . LEU   B 1 777  ? 80.09900   89.84400  27.19300  1.000 60.87463  ?  775  LEU   B C   1 
ATOM   20224 O  O   . LEU   B 1 777  ? 80.55900   90.63100  26.35800  1.000 64.12039  ?  775  LEU   B O   1 
ATOM   20225 C  CB  . LEU   B 1 777  ? 78.37700   88.73200  25.74400  1.000 70.30891  ?  775  LEU   B CB  1 
ATOM   20226 C  CG  . LEU   B 1 777  ? 78.90100   87.31700  25.47000  1.000 64.82193  ?  775  LEU   B CG  1 
ATOM   20227 C  CD1 . LEU   B 1 777  ? 78.03800   86.27000  26.14800  1.000 61.75682  ?  775  LEU   B CD1 1 
ATOM   20228 C  CD2 . LEU   B 1 777  ? 78.95900   87.06800  23.95700  1.000 54.75305  ?  775  LEU   B CD2 1 
ATOM   20229 N  N   . ARG   B 1 778  ? 80.82400   89.31900  28.17800  1.000 58.16866  ?  776  ARG   B N   1 
ATOM   20230 C  CA  . ARG   B 1 778  ? 82.20800   89.72400  28.37700  1.000 58.17470  ?  776  ARG   B CA  1 
ATOM   20231 C  C   . ARG   B 1 778  ? 83.10600   89.08800  27.32200  1.000 64.28953  ?  776  ARG   B C   1 
ATOM   20232 O  O   . ARG   B 1 778  ? 83.07800   87.87100  27.11600  1.000 63.38149  ?  776  ARG   B O   1 
ATOM   20233 C  CB  . ARG   B 1 778  ? 82.68400   89.33800  29.77900  1.000 60.48802  ?  776  ARG   B CB  1 
ATOM   20234 N  N   . GLU   B 1 779  ? 83.90500   89.91500  26.64700  1.000 55.80522  ?  777  GLU   B N   1 
ATOM   20235 C  CA  . GLU   B 1 779  ? 84.78300   89.42800  25.59100  1.000 63.75696  ?  777  GLU   B CA  1 
ATOM   20236 C  C   . GLU   B 1 779  ? 85.98200   88.69600  26.18000  1.000 58.40686  ?  777  GLU   B C   1 
ATOM   20237 O  O   . GLU   B 1 779  ? 86.59900   89.15600  27.14500  1.000 72.29329  ?  777  GLU   B O   1 
ATOM   20238 C  CB  . GLU   B 1 779  ? 85.25600   90.58500  24.70900  1.000 69.24631  ?  777  GLU   B CB  1 
ATOM   20239 C  CG  . GLU   B 1 779  ? 84.43800   90.76300  23.43700  1.000 77.71468  ?  777  GLU   B CG  1 
ATOM   20240 C  CD  . GLU   B 1 779  ? 84.51000   89.55700  22.51700  1.000 83.63134  ?  777  GLU   B CD  1 
ATOM   20241 O  OE1 . GLU   B 1 779  ? 85.63200   89.14300  22.15000  1.000 72.67517  ?  777  GLU   B OE1 1 
ATOM   20242 O  OE2 . GLU   B 1 779  ? 83.43900   89.02000  22.16200  1.000 74.10764  -1 777  GLU   B OE2 1 
ATOM   20243 N  N   . LEU   B 1 780  ? 86.31000   87.55000  25.58900  1.000 57.81339  ?  778  LEU   B N   1 
ATOM   20244 C  CA  . LEU   B 1 780  ? 87.41900   86.74100  26.07100  1.000 70.19915  ?  778  LEU   B CA  1 
ATOM   20245 C  C   . LEU   B 1 780  ? 88.74900   87.32900  25.61700  1.000 76.78843  ?  778  LEU   B C   1 
ATOM   20246 O  O   . LEU   B 1 780  ? 88.87200   87.83700  24.49800  1.000 76.09036  ?  778  LEU   B O   1 
ATOM   20247 C  CB  . LEU   B 1 780  ? 87.28900   85.29900  25.57500  1.000 48.95874  ?  778  LEU   B CB  1 
ATOM   20248 C  CG  . LEU   B 1 780  ? 86.56300   84.28700  26.47200  1.000 66.33768  ?  778  LEU   B CG  1 
ATOM   20249 C  CD1 . LEU   B 1 780  ? 87.52100   83.67800  27.48900  1.000 78.27415  ?  778  LEU   B CD1 1 
ATOM   20250 C  CD2 . LEU   B 1 780  ? 85.34800   84.89200  27.17100  1.000 61.95817  ?  778  LEU   B CD2 1 
ATOM   20251 N  N   . ASP   B 1 781  ? 89.74500   87.26200  26.49600  1.000 77.55494  ?  779  ASP   B N   1 
ATOM   20252 C  CA  . ASP   B 1 781  ? 91.07700   87.73000  26.15300  1.000 88.30986  ?  779  ASP   B CA  1 
ATOM   20253 C  C   . ASP   B 1 781  ? 91.74100   86.75900  25.17800  1.000 81.17446  ?  779  ASP   B C   1 
ATOM   20254 O  O   . ASP   B 1 781  ? 91.26700   85.64400  24.94600  1.000 93.42567  ?  779  ASP   B O   1 
ATOM   20255 C  CB  . ASP   B 1 781  ? 91.92900   87.89400  27.41000  1.000 97.06328  ?  779  ASP   B CB  1 
ATOM   20256 C  CG  . ASP   B 1 781  ? 91.54000   89.11200  28.22300  1.000 99.23146  ?  779  ASP   B CG  1 
ATOM   20257 O  OD1 . ASP   B 1 781  ? 91.63400   90.23900  27.69100  1.000 95.71573  ?  779  ASP   B OD1 1 
ATOM   20258 O  OD2 . ASP   B 1 781  ? 91.13600   88.94200  29.39300  1.000 105.30153 -1 779  ASP   B OD2 1 
ATOM   20259 N  N   . GLU   B 1 782  ? 92.85900   87.19600  24.60400  1.000 60.01625  ?  780  GLU   B N   1 
ATOM   20260 C  CA  . GLU   B 1 782  ? 93.55200   86.38200  23.61200  1.000 67.79107  ?  780  GLU   B CA  1 
ATOM   20261 C  C   . GLU   B 1 782  ? 94.23600   85.19900  24.28600  1.000 62.46394  ?  780  GLU   B C   1 
ATOM   20262 O  O   . GLU   B 1 782  ? 95.02600   85.37500  25.21900  1.000 77.38282  ?  780  GLU   B O   1 
ATOM   20263 C  CB  . GLU   B 1 782  ? 94.57300   87.22100  22.84500  1.000 73.63048  ?  780  GLU   B CB  1 
ATOM   20264 C  CG  . GLU   B 1 782  ? 95.65200   86.39000  22.15100  1.000 81.08690  ?  780  GLU   B CG  1 
ATOM   20265 C  CD  . GLU   B 1 782  ? 96.15400   87.02100  20.86300  1.000 111.44534 ?  780  GLU   B CD  1 
ATOM   20266 O  OE1 . GLU   B 1 782  ? 95.91300   88.22900  20.65600  1.000 118.76210 ?  780  GLU   B OE1 1 
ATOM   20267 O  OE2 . GLU   B 1 782  ? 96.78900   86.30700  20.05700  1.000 107.35864 -1 780  GLU   B OE2 1 
ATOM   20268 N  N   . GLN   B 1 783  ? 93.92600   83.99600  23.81600  1.000 73.67103  ?  781  GLN   B N   1 
ATOM   20269 C  CA  . GLN   B 1 783  ? 94.58900   82.76600  24.22600  1.000 77.52463  ?  781  GLN   B CA  1 
ATOM   20270 C  C   . GLN   B 1 783  ? 95.13100   82.05700  22.98900  1.000 87.94253  ?  781  GLN   B C   1 
ATOM   20271 O  O   . GLN   B 1 783  ? 95.03000   82.55400  21.86400  1.000 92.79316  ?  781  GLN   B O   1 
ATOM   20272 C  CB  . GLN   B 1 783  ? 93.63100   81.85400  24.99900  1.000 52.85572  ?  781  GLN   B CB  1 
ATOM   20273 C  CG  . GLN   B 1 783  ? 92.66700   82.58700  25.91700  1.000 65.22334  ?  781  GLN   B CG  1 
ATOM   20274 C  CD  . GLN   B 1 783  ? 91.87200   81.64400  26.80100  1.000 84.11363  ?  781  GLN   B CD  1 
ATOM   20275 O  OE1 . GLN   B 1 783  ? 92.21900   80.47200  26.94600  1.000 88.19622  ?  781  GLN   B OE1 1 
ATOM   20276 N  NE2 . GLN   B 1 783  ? 90.79600   82.15200  27.39500  1.000 74.61019  ?  781  GLN   B NE2 1 
ATOM   20277 N  N   . ALA   B 1 784  ? 95.71800   80.88200  23.20400  1.000 91.47158  ?  782  ALA   B N   1 
ATOM   20278 C  CA  . ALA   B 1 784  ? 96.12700   80.04300  22.08500  1.000 83.17945  ?  782  ALA   B CA  1 
ATOM   20279 C  C   . ALA   B 1 784  ? 95.00000   79.12500  21.62900  1.000 75.67896  ?  782  ALA   B C   1 
ATOM   20280 O  O   . ALA   B 1 784  ? 94.83400   78.89600  20.42600  1.000 71.76728  ?  782  ALA   B O   1 
ATOM   20281 C  CB  . ALA   B 1 784  ? 97.36000   79.21800  22.46100  1.000 80.17760  ?  782  ALA   B CB  1 
ATOM   20282 N  N   . GLU   B 1 785  ? 94.22200   78.60000  22.57300  1.000 64.43965  ?  783  GLU   B N   1 
ATOM   20283 C  CA  . GLU   B 1 785  ? 93.05800   77.78000  22.27800  1.000 56.20842  ?  783  GLU   B CA  1 
ATOM   20284 C  C   . GLU   B 1 785  ? 91.91900   78.20100  23.19500  1.000 64.67078  ?  783  GLU   B C   1 
ATOM   20285 O  O   . GLU   B 1 785  ? 92.14300   78.62700  24.33100  1.000 77.76105  ?  783  GLU   B O   1 
ATOM   20286 C  CB  . GLU   B 1 785  ? 93.35200   76.28400  22.45500  1.000 56.25786  ?  783  GLU   B CB  1 
ATOM   20287 C  CG  . GLU   B 1 785  ? 94.52500   75.77500  21.63200  1.000 67.63662  ?  783  GLU   B CG  1 
ATOM   20288 C  CD  . GLU   B 1 785  ? 95.08600   74.47000  22.16200  1.000 86.15730  ?  783  GLU   B CD  1 
ATOM   20289 O  OE1 . GLU   B 1 785  ? 94.71000   74.07100  23.28500  1.000 74.28281  ?  783  GLU   B OE1 1 
ATOM   20290 O  OE2 . GLU   B 1 785  ? 95.90400   73.84400  21.45500  1.000 82.72618  -1 783  GLU   B OE2 1 
ATOM   20291 N  N   . TYR   B 1 786  ? 90.69500   78.08200  22.69200  1.000 65.06166  ?  784  TYR   B N   1 
ATOM   20292 C  CA  . TYR   B 1 786  ? 89.50800   78.48200  23.42900  1.000 58.76597  ?  784  TYR   B CA  1 
ATOM   20293 C  C   . TYR   B 1 786  ? 88.58700   77.28600  23.62100  1.000 56.37873  ?  784  TYR   B C   1 
ATOM   20294 O  O   . TYR   B 1 786  ? 88.75500   76.23100  23.00500  1.000 63.77032  ?  784  TYR   B O   1 
ATOM   20295 C  CB  . TYR   B 1 786  ? 88.75800   79.61100  22.71100  1.000 56.13778  ?  784  TYR   B CB  1 
ATOM   20296 C  CG  . TYR   B 1 786  ? 89.61300   80.80700  22.35900  1.000 64.21543  ?  784  TYR   B CG  1 
ATOM   20297 C  CD1 . TYR   B 1 786  ? 90.40500   80.80800  21.21700  1.000 52.71762  ?  784  TYR   B CD1 1 
ATOM   20298 C  CD2 . TYR   B 1 786  ? 89.62000   81.94200  23.16100  1.000 62.81091  ?  784  TYR   B CD2 1 
ATOM   20299 C  CE1 . TYR   B 1 786  ? 91.18300   81.89900  20.88700  1.000 60.07461  ?  784  TYR   B CE1 1 
ATOM   20300 C  CE2 . TYR   B 1 786  ? 90.39500   83.04000  22.83800  1.000 54.10227  ?  784  TYR   B CE2 1 
ATOM   20301 C  CZ  . TYR   B 1 786  ? 91.17500   83.01300  21.69900  1.000 60.43546  ?  784  TYR   B CZ  1 
ATOM   20302 O  OH  . TYR   B 1 786  ? 91.95100   84.10000  21.36800  1.000 65.19073  ?  784  TYR   B OH  1 
ATOM   20303 N  N   . GLU   B 1 787  ? 87.60000   77.46700  24.49100  1.000 66.37010  ?  785  GLU   B N   1 
ATOM   20304 C  CA  . GLU   B 1 787  ? 86.63600   76.41400  24.76500  1.000 77.18754  ?  785  GLU   B CA  1 
ATOM   20305 C  C   . GLU   B 1 787  ? 85.58100   76.36600  23.67000  1.000 75.07079  ?  785  GLU   B C   1 
ATOM   20306 O  O   . GLU   B 1 787  ? 85.15700   77.40000  23.14700  1.000 92.14725  ?  785  GLU   B O   1 
ATOM   20307 C  CB  . GLU   B 1 787  ? 85.96300   76.63900  26.11900  1.000 81.95462  ?  785  GLU   B CB  1 
ATOM   20308 C  CG  . GLU   B 1 787  ? 86.90700   77.05300  27.23400  1.000 90.09258  ?  785  GLU   B CG  1 
ATOM   20309 C  CD  . GLU   B 1 787  ? 86.19400   77.22300  28.56300  1.000 106.05389 ?  785  GLU   B CD  1 
ATOM   20310 O  OE1 . GLU   B 1 787  ? 84.99600   76.87700  28.64500  1.000 90.55292  ?  785  GLU   B OE1 1 
ATOM   20311 O  OE2 . GLU   B 1 787  ? 86.83100   77.70200  29.52500  1.000 115.03123 -1 785  GLU   B OE2 1 
ATOM   20312 N  N   . THR   B 1 788  ? 85.16200   75.15700  23.32400  1.000 71.76133  ?  786  THR   B N   1 
ATOM   20313 C  CA  . THR   B 1 788  ? 84.05800   74.97100  22.40100  1.000 54.15187  ?  786  THR   B CA  1 
ATOM   20314 C  C   . THR   B 1 788  ? 82.76400   74.80500  23.17900  1.000 65.96096  ?  786  THR   B C   1 
ATOM   20315 O  O   . THR   B 1 788  ? 82.76100   74.37100  24.33400  1.000 84.19590  ?  786  THR   B O   1 
ATOM   20316 C  CB  . THR   B 1 788  ? 84.28500   73.74800  21.51500  1.000 63.03089  ?  786  THR   B CB  1 
ATOM   20317 O  OG1 . THR   B 1 788  ? 84.50300   72.60200  22.34500  1.000 61.08764  ?  786  THR   B OG1 1 
ATOM   20318 C  CG2 . THR   B 1 788  ? 85.49200   73.96200  20.61300  1.000 61.35905  ?  786  THR   B CG2 1 
ATOM   20319 N  N   . SER   B 1 789  ? 81.65900   75.15900  22.53600  1.000 65.97595  ?  787  SER   B N   1 
ATOM   20320 C  CA  . SER   B 1 789  ? 80.36400   75.00800  23.17500  1.000 69.38122  ?  787  SER   B CA  1 
ATOM   20321 C  C   . SER   B 1 789  ? 79.92700   73.54700  23.15700  1.000 65.87201  ?  787  SER   B C   1 
ATOM   20322 O  O   . SER   B 1 789  ? 80.46400   72.71600  22.41800  1.000 62.57790  ?  787  SER   B O   1 
ATOM   20323 C  CB  . SER   B 1 789  ? 79.32000   75.87800  22.48000  1.000 69.68166  ?  787  SER   B CB  1 
ATOM   20324 O  OG  . SER   B 1 789  ? 78.54200   75.10300  21.58800  1.000 78.63321  ?  787  SER   B OG  1 
ATOM   20325 N  N   . ALA   B 1 790  ? 78.93300   73.23800  23.99400  1.000 65.79715  ?  788  ALA   B N   1 
ATOM   20326 C  CA  . ALA   B 1 790  ? 78.40100   71.88100  24.03500  1.000 69.19610  ?  788  ALA   B CA  1 
ATOM   20327 C  C   . ALA   B 1 790  ? 77.78000   71.48300  22.70300  1.000 76.26090  ?  788  ALA   B C   1 
ATOM   20328 O  O   . ALA   B 1 790  ? 77.81600   70.30500  22.32900  1.000 77.39036  ?  788  ALA   B O   1 
ATOM   20329 C  CB  . ALA   B 1 790  ? 77.37500   71.75000  25.16100  1.000 54.19605  ?  788  ALA   B CB  1 
ATOM   20330 N  N   . VAL   B 1 791  ? 77.21500   72.44600  21.97100  1.000 78.38826  ?  789  VAL   B N   1 
ATOM   20331 C  CA  . VAL   B 1 791  ? 76.65000   72.13600  20.66200  1.000 65.36196  ?  789  VAL   B CA  1 
ATOM   20332 C  C   . VAL   B 1 791  ? 77.75100   72.01800  19.61000  1.000 65.77959  ?  789  VAL   B C   1 
ATOM   20333 O  O   . VAL   B 1 791  ? 77.62200   71.23700  18.66100  1.000 68.57866  ?  789  VAL   B O   1 
ATOM   20334 C  CB  . VAL   B 1 791  ? 75.58100   73.17800  20.27300  1.000 76.39610  ?  789  VAL   B CB  1 
ATOM   20335 C  CG1 . VAL   B 1 791  ? 76.19500   74.40800  19.59800  1.000 70.74051  ?  789  VAL   B CG1 1 
ATOM   20336 C  CG2 . VAL   B 1 791  ? 74.51700   72.54600  19.38600  1.000 73.85606  ?  789  VAL   B CG2 1 
ATOM   20337 N  N   . GLU   B 1 792  ? 78.85300   72.76000  19.76300  1.000 62.17840  ?  790  GLU   B N   1 
ATOM   20338 C  CA  . GLU   B 1 792  ? 79.97600   72.59900  18.84400  1.000 60.64906  ?  790  GLU   B CA  1 
ATOM   20339 C  C   . GLU   B 1 792  ? 80.69700   71.28400  19.08300  1.000 68.25261  ?  790  GLU   B C   1 
ATOM   20340 O  O   . GLU   B 1 792  ? 81.34200   70.75500  18.17200  1.000 65.99416  ?  790  GLU   B O   1 
ATOM   20341 C  CB  . GLU   B 1 792  ? 80.96200   73.75700  18.98300  1.000 57.26822  ?  790  GLU   B CB  1 
ATOM   20342 C  CG  . GLU   B 1 792  ? 80.49400   75.07400  18.39300  1.000 65.20842  ?  790  GLU   B CG  1 
ATOM   20343 C  CD  . GLU   B 1 792  ? 81.55800   76.15100  18.48600  1.000 67.09089  ?  790  GLU   B CD  1 
ATOM   20344 O  OE1 . GLU   B 1 792  ? 82.46300   76.01900  19.33600  1.000 79.43878  ?  790  GLU   B OE1 1 
ATOM   20345 O  OE2 . GLU   B 1 792  ? 81.49200   77.12700  17.70900  1.000 69.76927  -1 790  GLU   B OE2 1 
ATOM   20346 N  N   . LYS   B 1 793  ? 80.60800   70.75200  20.30200  1.000 74.65769  ?  791  LYS   B N   1 
ATOM   20347 C  CA  . LYS   B 1 793  ? 81.24800   69.47900  20.60400  1.000 83.93153  ?  791  LYS   B CA  1 
ATOM   20348 C  C   . LYS   B 1 793  ? 80.54100   68.33200  19.89300  1.000 75.19042  ?  791  LYS   B C   1 
ATOM   20349 O  O   . LYS   B 1 793  ? 81.18400   67.51700  19.22000  1.000 61.40988  ?  791  LYS   B O   1 
ATOM   20350 C  CB  . LYS   B 1 793  ? 81.27100   69.25500  22.11600  1.000 77.46725  ?  791  LYS   B CB  1 
ATOM   20351 C  CG  . LYS   B 1 793  ? 82.31200   70.09400  22.84400  1.000 75.49941  ?  791  LYS   B CG  1 
ATOM   20352 C  CD  . LYS   B 1 793  ? 82.16400   69.97900  24.35300  1.000 71.19194  ?  791  LYS   B CD  1 
ATOM   20353 C  CE  . LYS   B 1 793  ? 83.16700   70.86700  25.07300  1.000 66.38654  ?  791  LYS   B CE  1 
ATOM   20354 N  NZ  . LYS   B 1 793  ? 82.49400   71.96000  25.82900  1.000 70.04770  ?  791  LYS   B NZ  1 
ATOM   20355 N  N   . ARG   B 1 794  ? 79.21000   68.27200  20.01400  1.000 67.78013  ?  792  ARG   B N   1 
ATOM   20356 C  CA  . ARG   B 1 794  ? 78.43700   67.21100  19.37500  1.000 69.55578  ?  792  ARG   B CA  1 
ATOM   20357 C  C   . ARG   B 1 794  ? 78.72200   67.13400  17.88100  1.000 69.50738  ?  792  ARG   B C   1 
ATOM   20358 O  O   . ARG   B 1 794  ? 78.85800   66.03900  17.32400  1.000 69.54118  ?  792  ARG   B O   1 
ATOM   20359 C  CB  . ARG   B 1 794  ? 76.94300   67.42900  19.62100  1.000 52.50679  ?  792  ARG   B CB  1 
ATOM   20360 C  CG  . ARG   B 1 794  ? 76.09900   66.18300  19.42700  1.000 67.12999  ?  792  ARG   B CG  1 
ATOM   20361 C  CD  . ARG   B 1 794  ? 74.61900   66.52000  19.35300  1.000 79.03623  ?  792  ARG   B CD  1 
ATOM   20362 N  NE  . ARG   B 1 794  ? 73.83600   65.41700  18.80600  1.000 81.45553  ?  792  ARG   B NE  1 
ATOM   20363 C  CZ  . ARG   B 1 794  ? 72.72000   65.56600  18.10600  1.000 76.70171  ?  792  ARG   B CZ  1 
ATOM   20364 N  NH1 . ARG   B 1 794  ? 72.22200   66.76300  17.84400  1.000 77.35392  ?  792  ARG   B NH1 1 
ATOM   20365 N  NH2 . ARG   B 1 794  ? 72.08600   64.48500  17.65800  1.000 77.37769  ?  792  ARG   B NH2 1 
ATOM   20366 N  N   . MET   B 1 795  ? 78.81900   68.28900  17.21700  1.000 64.77554  ?  793  MET   B N   1 
ATOM   20367 C  CA  . MET   B 1 795  ? 79.14900   68.29900  15.79600  1.000 59.90837  ?  793  MET   B CA  1 
ATOM   20368 C  C   . MET   B 1 795  ? 80.50200   67.65100  15.54200  1.000 51.44740  ?  793  MET   B C   1 
ATOM   20369 O  O   . MET   B 1 795  ? 80.64900   66.84500  14.61600  1.000 57.34545  ?  793  MET   B O   1 
ATOM   20370 C  CB  . MET   B 1 795  ? 79.13500   69.73200  15.26500  1.000 60.98705  ?  793  MET   B CB  1 
ATOM   20371 C  CG  . MET   B 1 795  ? 77.76100   70.22300  14.85500  1.000 63.11393  ?  793  MET   B CG  1 
ATOM   20372 S  SD  . MET   B 1 795  ? 77.00400   69.14000  13.63200  1.000 60.54754  ?  793  MET   B SD  1 
ATOM   20373 C  CE  . MET   B 1 795  ? 75.62500   68.49600  14.57100  1.000 39.16547  ?  793  MET   B CE  1 
ATOM   20374 N  N   . TYR   B 1 796  ? 81.50200   67.98700  16.36100  1.000 56.49943  ?  794  TYR   B N   1 
ATOM   20375 C  CA  . TYR   B 1 796  ? 82.82200   67.38500  16.21100  1.000 59.17293  ?  794  TYR   B CA  1 
ATOM   20376 C  C   . TYR   B 1 796  ? 82.77500   65.87300  16.40400  1.000 62.64386  ?  794  TYR   B C   1 
ATOM   20377 O  O   . TYR   B 1 796  ? 83.51400   65.14200  15.73600  1.000 50.64777  ?  794  TYR   B O   1 
ATOM   20378 C  CB  . TYR   B 1 796  ? 83.80100   68.01400  17.20600  1.000 51.42932  ?  794  TYR   B CB  1 
ATOM   20379 C  CG  . TYR   B 1 796  ? 85.26000   67.76300  16.88100  1.000 53.32369  ?  794  TYR   B CG  1 
ATOM   20380 C  CD1 . TYR   B 1 796  ? 85.87400   66.56300  17.22300  1.000 55.84572  ?  794  TYR   B CD1 1 
ATOM   20381 C  CD2 . TYR   B 1 796  ? 86.02800   68.73300  16.24800  1.000 59.77538  ?  794  TYR   B CD2 1 
ATOM   20382 C  CE1 . TYR   B 1 796  ? 87.20800   66.33200  16.93200  1.000 54.66256  ?  794  TYR   B CE1 1 
ATOM   20383 C  CE2 . TYR   B 1 796  ? 87.36200   68.51100  15.95100  1.000 57.73254  ?  794  TYR   B CE2 1 
ATOM   20384 C  CZ  . TYR   B 1 796  ? 87.94700   67.31100  16.29500  1.000 52.15451  ?  794  TYR   B CZ  1 
ATOM   20385 O  OH  . TYR   B 1 796  ? 89.27300   67.09500  15.99400  1.000 40.28998  ?  794  TYR   B OH  1 
ATOM   20386 N  N   . ILE   B 1 797  ? 81.92100   65.38800  17.30600  1.000 65.43608  ?  795  ILE   B N   1 
ATOM   20387 C  CA  . ILE   B 1 797  ? 81.85600   63.95300  17.57300  1.000 65.81568  ?  795  ILE   B CA  1 
ATOM   20388 C  C   . ILE   B 1 797  ? 81.22400   63.21700  16.39700  1.000 63.90472  ?  795  ILE   B C   1 
ATOM   20389 O  O   . ILE   B 1 797  ? 81.73300   62.18200  15.95100  1.000 62.15101  ?  795  ILE   B O   1 
ATOM   20390 C  CB  . ILE   B 1 797  ? 81.09400   63.68200  18.88300  1.000 71.17526  ?  795  ILE   B CB  1 
ATOM   20391 C  CG1 . ILE   B 1 797  ? 81.60200   64.60300  19.99400  1.000 65.13012  ?  795  ILE   B CG1 1 
ATOM   20392 C  CG2 . ILE   B 1 797  ? 81.24400   62.22600  19.30000  1.000 73.91681  ?  795  ILE   B CG2 1 
ATOM   20393 C  CD1 . ILE   B 1 797  ? 80.94700   64.36600  21.33600  1.000 61.39579  ?  795  ILE   B CD1 1 
ATOM   20394 N  N   . ILE   B 1 798  ? 80.10300   63.73200  15.88200  1.000 55.15906  ?  796  ILE   B N   1 
ATOM   20395 C  CA  . ILE   B 1 798  ? 79.42300   63.06300  14.77400  1.000 44.92226  ?  796  ILE   B CA  1 
ATOM   20396 C  C   . ILE   B 1 798  ? 80.33100   62.99100  13.55300  1.000 48.30838  ?  796  ILE   B C   1 
ATOM   20397 O  O   . ILE   B 1 798  ? 80.34900   61.98700  12.83200  1.000 56.86148  ?  796  ILE   B O   1 
ATOM   20398 C  CB  . ILE   B 1 798  ? 78.09200   63.76700  14.45100  1.000 43.05046  ?  796  ILE   B CB  1 
ATOM   20399 C  CG1 . ILE   B 1 798  ? 77.23000   63.88800  15.70500  1.000 47.62725  ?  796  ILE   B CG1 1 
ATOM   20400 C  CG2 . ILE   B 1 798  ? 77.32400   62.99900  13.39000  1.000 46.71860  ?  796  ILE   B CG2 1 
ATOM   20401 C  CD1 . ILE   B 1 798  ? 75.98400   64.71900  15.50300  1.000 48.33179  ?  796  ILE   B CD1 1 
ATOM   20402 N  N   . GLN   B 1 799  ? 81.10800   64.04700  13.30900  1.000 46.25955  ?  797  GLN   B N   1 
ATOM   20403 C  CA  . GLN   B 1 799  ? 82.02800   64.03600  12.17800  1.000 52.83115  ?  797  GLN   B CA  1 
ATOM   20404 C  C   . GLN   B 1 799  ? 83.18100   63.06400  12.39900  1.000 54.82156  ?  797  GLN   B C   1 
ATOM   20405 O  O   . GLN   B 1 799  ? 83.75700   62.56000  11.42900  1.000 59.97761  ?  797  GLN   B O   1 
ATOM   20406 C  CB  . GLN   B 1 799  ? 82.55600   65.44700  11.91900  1.000 51.05034  ?  797  GLN   B CB  1 
ATOM   20407 C  CG  . GLN   B 1 799  ? 83.36300   65.61000  10.63700  1.000 51.96169  ?  797  GLN   B CG  1 
ATOM   20408 C  CD  . GLN   B 1 799  ? 82.56000   65.32000  9.38500   1.000 50.66041  ?  797  GLN   B CD  1 
ATOM   20409 O  OE1 . GLN   B 1 799  ? 81.47000   65.85800  9.18800   1.000 65.64325  ?  797  GLN   B OE1 1 
ATOM   20410 N  NE2 . GLN   B 1 799  ? 83.09700   64.45900  8.52900   1.000 59.55964  ?  797  GLN   B NE2 1 
ATOM   20411 N  N   . GLN   B 1 800  ? 83.52400   62.77600  13.65900  1.000 53.73578  ?  798  GLN   B N   1 
ATOM   20412 C  CA  . GLN   B 1 800  ? 84.66400   61.90100  13.92200  1.000 65.40403  ?  798  GLN   B CA  1 
ATOM   20413 C  C   . GLN   B 1 800  ? 84.35300   60.45600  13.55400  1.000 64.41226  ?  798  GLN   B C   1 
ATOM   20414 O  O   . GLN   B 1 800  ? 85.20500   59.75900  12.99000  1.000 67.76147  ?  798  GLN   B O   1 
ATOM   20415 C  CB  . GLN   B 1 800  ? 85.09600   62.00900  15.38200  1.000 63.25807  ?  798  GLN   B CB  1 
ATOM   20416 C  CG  . GLN   B 1 800  ? 85.94200   63.24100  15.69200  1.000 58.69574  ?  798  GLN   B CG  1 
ATOM   20417 C  CD  . GLN   B 1 800  ? 86.48200   63.93000  14.44500  1.000 54.97059  ?  798  GLN   B CD  1 
ATOM   20418 O  OE1 . GLN   B 1 800  ? 87.41100   63.44300  13.79500  1.000 42.54114  ?  798  GLN   B OE1 1 
ATOM   20419 N  NE2 . GLN   B 1 800  ? 85.89800   65.07400  14.10900  1.000 52.02427  ?  798  GLN   B NE2 1 
ATOM   20420 N  N   . GLN   B 1 801  ? 83.15100   59.98300  13.86800  1.000 56.44474  ?  799  GLN   B N   1 
ATOM   20421 C  CA  . GLN   B 1 801  ? 82.67200   58.74700  13.26700  1.000 61.61290  ?  799  GLN   B CA  1 
ATOM   20422 C  C   . GLN   B 1 801  ? 82.40400   59.00500  11.79100  1.000 74.01762  ?  799  GLN   B C   1 
ATOM   20423 O  O   . GLN   B 1 801  ? 81.60300   59.88200  11.45000  1.000 91.84380  ?  799  GLN   B O   1 
ATOM   20424 C  CB  . GLN   B 1 801  ? 81.40700   58.25900  13.96500  1.000 59.77440  ?  799  GLN   B CB  1 
ATOM   20425 C  CG  . GLN   B 1 801  ? 80.87500   56.95000  13.40400  1.000 99.02983  ?  799  GLN   B CG  1 
ATOM   20426 C  CD  . GLN   B 1 801  ? 79.81800   57.14100  12.33000  1.000 105.60281 ?  799  GLN   B CD  1 
ATOM   20427 O  OE1 . GLN   B 1 801  ? 79.19500   58.19800  12.23100  1.000 120.60152 ?  799  GLN   B OE1 1 
ATOM   20428 N  NE2 . GLN   B 1 801  ? 79.61000   56.10800  11.51900  1.000 91.78360  ?  799  GLN   B NE2 1 
ATOM   20429 N  N   . ASP   B 1 802  ? 83.07600   58.25100  10.91900  1.000 73.65666  ?  800  ASP   B N   1 
ATOM   20430 C  CA  . ASP   B 1 802  ? 83.02400   58.50100  9.48200   1.000 73.17183  ?  800  ASP   B CA  1 
ATOM   20431 C  C   . ASP   B 1 802  ? 83.52900   59.90600  9.17200   1.000 58.61007  ?  800  ASP   B C   1 
ATOM   20432 O  O   . ASP   B 1 802  ? 82.73500   60.82600  8.95000   1.000 61.91918  ?  800  ASP   B O   1 
ATOM   20433 C  CB  . ASP   B 1 802  ? 81.60300   58.30200  8.94200   1.000 68.02973  ?  800  ASP   B CB  1 
ATOM   20434 C  CG  . ASP   B 1 802  ? 81.58700   57.77900  7.52500   1.000 76.33665  ?  800  ASP   B CG  1 
ATOM   20435 O  OD1 . ASP   B 1 802  ? 82.65400   57.79200  6.87600   1.000 75.91072  ?  800  ASP   B OD1 1 
ATOM   20436 O  OD2 . ASP   B 1 802  ? 80.50900   57.34900  7.06500   1.000 84.26959  -1 800  ASP   B OD2 1 
ATOM   20437 N  N   . VAL   B 1 803  ? 84.85400   60.07700  9.16500   1.000 57.38477  ?  801  VAL   B N   1 
ATOM   20438 C  CA  . VAL   B 1 803  ? 85.46100   61.37200  8.88000   1.000 57.59953  ?  801  VAL   B CA  1 
ATOM   20439 C  C   . VAL   B 1 803  ? 85.14800   61.83000  7.46000   1.000 68.60305  ?  801  VAL   B C   1 
ATOM   20440 O  O   . VAL   B 1 803  ? 85.19500   63.03100  7.16700   1.000 67.75774  ?  801  VAL   B O   1 
ATOM   20441 C  CB  . VAL   B 1 803  ? 86.98400   61.28400  9.14500   1.000 42.76378  ?  801  VAL   B CB  1 
ATOM   20442 C  CG1 . VAL   B 1 803  ? 87.56500   60.03600  8.50100   1.000 62.45932  ?  801  VAL   B CG1 1 
ATOM   20443 C  CG2 . VAL   B 1 803  ? 87.72200   62.53700  8.67500   1.000 68.86889  ?  801  VAL   B CG2 1 
ATOM   20444 N  N   . GLU   B 1 804  ? 84.78900   60.90000  6.57300   1.000 59.73700  ?  802  GLU   B N   1 
ATOM   20445 C  CA  . GLU   B 1 804  ? 84.49500   61.20300  5.18000   1.000 61.08998  ?  802  GLU   B CA  1 
ATOM   20446 C  C   . GLU   B 1 804  ? 83.00400   61.38000  4.91300   1.000 55.05042  ?  802  GLU   B C   1 
ATOM   20447 O  O   . GLU   B 1 804  ? 82.57100   61.27400  3.76100   1.000 54.20640  ?  802  GLU   B O   1 
ATOM   20448 C  CB  . GLU   B 1 804  ? 85.06600   60.11200  4.27700   1.000 50.95693  ?  802  GLU   B CB  1 
ATOM   20449 C  CG  . GLU   B 1 804  ? 86.57900   60.07500  4.27000   1.000 59.97296  ?  802  GLU   B CG  1 
ATOM   20450 C  CD  . GLU   B 1 804  ? 87.15000   59.96700  2.87400   1.000 79.74517  ?  802  GLU   B CD  1 
ATOM   20451 O  OE1 . GLU   B 1 804  ? 87.23100   58.83500  2.35300   1.000 80.53261  ?  802  GLU   B OE1 1 
ATOM   20452 O  OE2 . GLU   B 1 804  ? 87.51900   61.01300  2.29800   1.000 96.21797  -1 802  GLU   B OE2 1 
ATOM   20453 N  N   . SER   B 1 805  ? 82.21000   61.64500  5.94600   1.000 61.86017  ?  803  SER   B N   1 
ATOM   20454 C  CA  . SER   B 1 805  ? 80.78800   61.88400  5.75300   1.000 44.34344  ?  803  SER   B CA  1 
ATOM   20455 C  C   . SER   B 1 805  ? 80.53800   63.32000  5.31300   1.000 54.77253  ?  803  SER   B C   1 
ATOM   20456 O  O   . SER   B 1 805  ? 81.29700   64.23700  5.64200   1.000 59.45680  ?  803  SER   B O   1 
ATOM   20457 C  CB  . SER   B 1 805  ? 80.01300   61.59800  7.03900   1.000 47.58106  ?  803  SER   B CB  1 
ATOM   20458 O  OG  . SER   B 1 805  ? 78.65300   61.98000  6.91000   1.000 40.87749  ?  803  SER   B OG  1 
ATOM   20459 N  N   . ILE   B 1 806  ? 79.45800   63.50800  4.56200   1.000 64.03407  ?  804  ILE   B N   1 
ATOM   20460 C  CA  . ILE   B 1 806  ? 79.00200   64.82300  4.13500   1.000 51.51951  ?  804  ILE   B CA  1 
ATOM   20461 C  C   . ILE   B 1 806  ? 77.58600   65.10300  4.63400   1.000 46.12968  ?  804  ILE   B C   1 
ATOM   20462 O  O   . ILE   B 1 806  ? 76.91900   66.00400  4.13800   1.000 53.95123  ?  804  ILE   B O   1 
ATOM   20463 C  CB  . ILE   B 1 806  ? 79.10200   64.97700  2.60400   1.000 45.85827  ?  804  ILE   B CB  1 
ATOM   20464 C  CG1 . ILE   B 1 806  ? 78.53600   63.73900  1.91100   1.000 44.82856  ?  804  ILE   B CG1 1 
ATOM   20465 C  CG2 . ILE   B 1 806  ? 80.53900   65.19200  2.18200   1.000 46.03085  ?  804  ILE   B CG2 1 
ATOM   20466 C  CD1 . ILE   B 1 806  ? 78.09600   63.99300  0.49200   1.000 45.34239  ?  804  ILE   B CD1 1 
ATOM   20467 N  N   . ALA   B 1 807  ? 77.12900   64.33500  5.62900   1.000 38.58191  ?  805  ALA   B N   1 
ATOM   20468 C  CA  . ALA   B 1 807  ? 75.76200   64.47700  6.12600   1.000 38.10616  ?  805  ALA   B CA  1 
ATOM   20469 C  C   . ALA   B 1 807  ? 75.52000   65.83600  6.76900   1.000 43.14511  ?  805  ALA   B C   1 
ATOM   20470 O  O   . ALA   B 1 807  ? 74.38100   66.31800  6.78900   1.000 50.06265  ?  805  ALA   B O   1 
ATOM   20471 C  CB  . ALA   B 1 807  ? 75.44200   63.36400  7.12600   1.000 46.70079  ?  805  ALA   B CB  1 
ATOM   20472 N  N   . TYR   B 1 808  ? 76.56300   66.46000  7.30500   1.000 55.62704  ?  806  TYR   B N   1 
ATOM   20473 C  CA  . TYR   B 1 808  ? 76.44100   67.75700  7.95000   1.000 54.32971  ?  806  TYR   B CA  1 
ATOM   20474 C  C   . TYR   B 1 808  ? 77.15200   68.84900  7.15700   1.000 52.24653  ?  806  TYR   B C   1 
ATOM   20475 O  O   . TYR   B 1 808  ? 77.58300   69.85800  7.71900   1.000 52.34197  ?  806  TYR   B O   1 
ATOM   20476 C  CB  . TYR   B 1 808  ? 76.95200   67.67600  9.38500   1.000 59.96272  ?  806  TYR   B CB  1 
ATOM   20477 C  CG  . TYR   B 1 808  ? 76.02400   66.87100  10.26400  1.000 50.44983  ?  806  TYR   B CG  1 
ATOM   20478 C  CD1 . TYR   B 1 808  ? 76.12800   65.48800  10.33300  1.000 54.68783  ?  806  TYR   B CD1 1 
ATOM   20479 C  CD2 . TYR   B 1 808  ? 75.01900   67.49000  10.99600  1.000 54.67133  ?  806  TYR   B CD2 1 
ATOM   20480 C  CE1 . TYR   B 1 808  ? 75.27300   64.74600  11.12200  1.000 52.95169  ?  806  TYR   B CE1 1 
ATOM   20481 C  CE2 . TYR   B 1 808  ? 74.15700   66.75600  11.79000  1.000 53.78858  ?  806  TYR   B CE2 1 
ATOM   20482 C  CZ  . TYR   B 1 808  ? 74.29000   65.38500  11.84800  1.000 58.54819  ?  806  TYR   B CZ  1 
ATOM   20483 O  OH  . TYR   B 1 808  ? 73.43600   64.64800  12.63600  1.000 73.53900  ?  806  TYR   B OH  1 
ATOM   20484 N  N   . ASN   B 1 809  ? 77.27500   68.65300  5.84600   1.000 52.78518  ?  807  ASN   B N   1 
ATOM   20485 C  CA  . ASN   B 1 809  ? 77.67400   69.71400  4.93400   1.000 49.98960  ?  807  ASN   B CA  1 
ATOM   20486 C  C   . ASN   B 1 809  ? 76.44300   70.50100  4.51000   1.000 57.44592  ?  807  ASN   B C   1 
ATOM   20487 O  O   . ASN   B 1 809  ? 75.37900   69.92800  4.25900   1.000 63.88800  ?  807  ASN   B O   1 
ATOM   20488 C  CB  . ASN   B 1 809  ? 78.37900   69.14400  3.70300   1.000 40.99862  ?  807  ASN   B CB  1 
ATOM   20489 C  CG  . ASN   B 1 809  ? 79.70300   68.49700  4.03900   1.000 56.44641  ?  807  ASN   B CG  1 
ATOM   20490 O  OD1 . ASN   B 1 809  ? 79.87800   67.94300  5.12500   1.000 71.02304  ?  807  ASN   B OD1 1 
ATOM   20491 N  ND2 . ASN   B 1 809  ? 80.64800   68.56500  3.10900   1.000 53.12741  ?  807  ASN   B ND2 1 
ATOM   20492 N  N   . VAL   B 1 810  ? 76.58900   71.81700  4.43400   1.000 45.68607  ?  808  VAL   B N   1 
ATOM   20493 C  CA  . VAL   B 1 810  ? 75.49400   72.71100  4.08700   1.000 38.60987  ?  808  VAL   B CA  1 
ATOM   20494 C  C   . VAL   B 1 810  ? 75.82700   73.34100  2.74300   1.000 52.37226  ?  808  VAL   B C   1 
ATOM   20495 O  O   . VAL   B 1 810  ? 76.72000   74.19200  2.64800   1.000 59.26137  ?  808  VAL   B O   1 
ATOM   20496 C  CB  . VAL   B 1 810  ? 75.26500   73.77200  5.16800   1.000 45.16368  ?  808  VAL   B CB  1 
ATOM   20497 C  CG1 . VAL   B 1 810  ? 74.04600   74.61300  4.83800   1.000 42.21929  ?  808  VAL   B CG1 1 
ATOM   20498 C  CG2 . VAL   B 1 810  ? 75.10300   73.10300  6.52300   1.000 44.67877  ?  808  VAL   B CG2 1 
ATOM   20499 N  N   . VAL   B 1 811  ? 75.11400   72.92400  1.70000   1.000 55.74845  ?  809  VAL   B N   1 
ATOM   20500 C  CA  . VAL   B 1 811  ? 75.33600   73.40400  0.34200   1.000 41.54834  ?  809  VAL   B CA  1 
ATOM   20501 C  C   . VAL   B 1 811  ? 74.15800   74.27700  -0.06300  1.000 40.20875  ?  809  VAL   B C   1 
ATOM   20502 O  O   . VAL   B 1 811  ? 72.99900   73.87400  0.09100   1.000 45.11171  ?  809  VAL   B O   1 
ATOM   20503 C  CB  . VAL   B 1 811  ? 75.51500   72.23900  -0.64500  1.000 37.67200  ?  809  VAL   B CB  1 
ATOM   20504 C  CG1 . VAL   B 1 811  ? 76.15300   72.73600  -1.92300  1.000 41.00586  ?  809  VAL   B CG1 1 
ATOM   20505 C  CG2 . VAL   B 1 811  ? 76.35200   71.13700  -0.01900  1.000 37.71988  ?  809  VAL   B CG2 1 
ATOM   20506 N  N   . TYR   B 1 812  ? 74.45200   75.46900  -0.58000  1.000 35.98497  ?  810  TYR   B N   1 
ATOM   20507 C  CA  . TYR   B 1 812  ? 73.43000   76.38000  -1.07500  1.000 34.31018  ?  810  TYR   B CA  1 
ATOM   20508 C  C   . TYR   B 1 812  ? 73.80000   76.85100  -2.47500  1.000 32.26909  ?  810  TYR   B C   1 
ATOM   20509 O  O   . TYR   B 1 812  ? 74.95400   76.76100  -2.90100  1.000 27.48505  ?  810  TYR   B O   1 
ATOM   20510 C  CB  . TYR   B 1 812  ? 73.24100   77.58800  -0.14800  1.000 33.55191  ?  810  TYR   B CB  1 
ATOM   20511 C  CG  . TYR   B 1 812  ? 72.26800   77.35500  0.99000   1.000 42.67711  ?  810  TYR   B CG  1 
ATOM   20512 C  CD1 . TYR   B 1 812  ? 70.90800   77.57900  0.82300   1.000 45.81607  ?  810  TYR   B CD1 1 
ATOM   20513 C  CD2 . TYR   B 1 812  ? 72.71200   76.92700  2.23400   1.000 41.14580  ?  810  TYR   B CD2 1 
ATOM   20514 C  CE1 . TYR   B 1 812  ? 70.01500   77.37100  1.86200   1.000 40.44198  ?  810  TYR   B CE1 1 
ATOM   20515 C  CE2 . TYR   B 1 812  ? 71.82600   76.71900  3.27700   1.000 29.60713  ?  810  TYR   B CE2 1 
ATOM   20516 C  CZ  . TYR   B 1 812  ? 70.48200   76.94100  3.08600   1.000 26.88919  ?  810  TYR   B CZ  1 
ATOM   20517 O  OH  . TYR   B 1 812  ? 69.60400   76.73200  4.12500   1.000 60.84402  ?  810  TYR   B OH  1 
ATOM   20518 N  N   . THR   B 1 813  ? 72.80000   77.36000  -3.19200  1.000 37.09321  ?  811  THR   B N   1 
ATOM   20519 C  CA  . THR   B 1 813  ? 72.97700   77.78200  -4.57600  1.000 30.40741  ?  811  THR   B CA  1 
ATOM   20520 C  C   . THR   B 1 813  ? 72.22800   79.08600  -4.79300  1.000 32.92550  ?  811  THR   B C   1 
ATOM   20521 O  O   . THR   B 1 813  ? 71.09700   79.24000  -4.32100  1.000 36.40364  ?  811  THR   B O   1 
ATOM   20522 C  CB  . THR   B 1 813  ? 72.48600   76.69500  -5.54700  1.000 36.11200  ?  811  THR   B CB  1 
ATOM   20523 O  OG1 . THR   B 1 813  ? 73.61200   75.97400  -6.06300  1.000 41.03258  ?  811  THR   B OG1 1 
ATOM   20524 C  CG2 . THR   B 1 813  ? 71.68300   77.28700  -6.71400  1.000 37.70829  ?  811  THR   B CG2 1 
ATOM   20525 N  N   . ILE   B 1 814  ? 72.87100   80.03200  -5.47500  1.000 29.25500  ?  812  ILE   B N   1 
ATOM   20526 C  CA  . ILE   B 1 814  ? 72.25100   81.29200  -5.86700  1.000 31.56470  ?  812  ILE   B CA  1 
ATOM   20527 C  C   . ILE   B 1 814  ? 72.53000   81.50900  -7.34500  1.000 38.95139  ?  812  ILE   B C   1 
ATOM   20528 O  O   . ILE   B 1 814  ? 73.68600   81.43900  -7.77700  1.000 49.93347  ?  812  ILE   B O   1 
ATOM   20529 C  CB  . ILE   B 1 814  ? 72.77400   82.48900  -5.05000  1.000 43.32840  ?  812  ILE   B CB  1 
ATOM   20530 C  CG1 . ILE   B 1 814  ? 72.93900   82.12000  -3.57800  1.000 54.71866  ?  812  ILE   B CG1 1 
ATOM   20531 C  CG2 . ILE   B 1 814  ? 71.83800   83.67800  -5.19300  1.000 33.88645  ?  812  ILE   B CG2 1 
ATOM   20532 C  CD1 . ILE   B 1 814  ? 73.64500   83.18000  -2.76900  1.000 57.96140  ?  812  ILE   B CD1 1 
ATOM   20533 N  N   . ASN   B 1 815  ? 71.48100   81.77100  -8.11600  1.000 41.37388  ?  813  ASN   B N   1 
ATOM   20534 C  CA  . ASN   B 1 815  ? 71.62300   82.04200  -9.54000  1.000 31.22532  ?  813  ASN   B CA  1 
ATOM   20535 C  C   . ASN   B 1 815  ? 71.66700   83.55100  -9.75400  1.000 40.19459  ?  813  ASN   B C   1 
ATOM   20536 O  O   . ASN   B 1 815  ? 70.69900   84.25600  -9.44400  1.000 53.72346  ?  813  ASN   B O   1 
ATOM   20537 C  CB  . ASN   B 1 815  ? 70.48000   81.41000  -10.33500 1.000 33.34140  ?  813  ASN   B CB  1 
ATOM   20538 C  CG  . ASN   B 1 815  ? 70.42800   79.89600  -10.19400 1.000 44.67447  ?  813  ASN   B CG  1 
ATOM   20539 O  OD1 . ASN   B 1 815  ? 71.44400   79.24100  -9.95200  1.000 60.34723  ?  813  ASN   B OD1 1 
ATOM   20540 N  ND2 . ASN   B 1 815  ? 69.23600   79.33300  -10.34900 1.000 51.87191  ?  813  ASN   B ND2 1 
ATOM   20541 N  N   . PHE   B 1 816  ? 72.79100   84.04300  -10.27200 1.000 51.56987  ?  814  PHE   B N   1 
ATOM   20542 C  CA  . PHE   B 1 816  ? 73.00600   85.45600  -10.54000 1.000 49.12745  ?  814  PHE   B CA  1 
ATOM   20543 C  C   . PHE   B 1 816  ? 72.90300   85.74000  -12.03500 1.000 47.54244  ?  814  PHE   B C   1 
ATOM   20544 O  O   . PHE   B 1 816  ? 73.18900   84.86500  -12.85900 1.000 47.00783  ?  814  PHE   B O   1 
ATOM   20545 C  CB  . PHE   B 1 816  ? 74.38600   85.91400  -10.05200 1.000 54.56563  ?  814  PHE   B CB  1 
ATOM   20546 C  CG  . PHE   B 1 816  ? 74.49100   86.07500  -8.56300  1.000 54.90653  ?  814  PHE   B CG  1 
ATOM   20547 C  CD1 . PHE   B 1 816  ? 73.95800   87.18700  -7.93400  1.000 41.83241  ?  814  PHE   B CD1 1 
ATOM   20548 C  CD2 . PHE   B 1 816  ? 75.14600   85.12500  -7.79600  1.000 47.93226  ?  814  PHE   B CD2 1 
ATOM   20549 C  CE1 . PHE   B 1 816  ? 74.06200   87.34000  -6.56600  1.000 46.74041  ?  814  PHE   B CE1 1 
ATOM   20550 C  CE2 . PHE   B 1 816  ? 75.25500   85.27300  -6.42600  1.000 40.40948  ?  814  PHE   B CE2 1 
ATOM   20551 C  CZ  . PHE   B 1 816  ? 74.71200   86.38100  -5.81100  1.000 45.27146  ?  814  PHE   B CZ  1 
ATOM   20552 N  N   . PRO   B 1 817  ? 72.50300   86.95100  -12.42000 1.000 45.62554  ?  815  PRO   B N   1 
ATOM   20553 C  CA  . PRO   B 1 817  ? 72.59100   87.33400  -13.83300 1.000 39.07369  ?  815  PRO   B CA  1 
ATOM   20554 C  C   . PRO   B 1 817  ? 74.04300   87.38200  -14.28500 1.000 54.96516  ?  815  PRO   B C   1 
ATOM   20555 O  O   . PRO   B 1 817  ? 74.95200   87.63800  -13.49300 1.000 64.79012  ?  815  PRO   B O   1 
ATOM   20556 C  CB  . PRO   B 1 817  ? 71.94400   88.72400  -13.86900 1.000 36.44082  ?  815  PRO   B CB  1 
ATOM   20557 C  CG  . PRO   B 1 817  ? 72.05900   89.23200  -12.46600 1.000 43.36818  ?  815  PRO   B CG  1 
ATOM   20558 C  CD  . PRO   B 1 817  ? 71.92700   88.02300  -11.59000 1.000 51.57045  ?  815  PRO   B CD  1 
ATOM   20559 N  N   . LEU   B 1 818  ? 74.25600   87.13000  -15.58200 1.000 57.00145  ?  816  LEU   B N   1 
ATOM   20560 C  CA  . LEU   B 1 818  ? 75.61200   87.14800  -16.12900 1.000 48.24601  ?  816  LEU   B CA  1 
ATOM   20561 C  C   . LEU   B 1 818  ? 76.26800   88.51600  -16.00100 1.000 53.53090  ?  816  LEU   B C   1 
ATOM   20562 O  O   . LEU   B 1 818  ? 77.49400   88.61700  -16.11800 1.000 55.45502  ?  816  LEU   B O   1 
ATOM   20563 C  CB  . LEU   B 1 818  ? 75.60600   86.72500  -17.59900 1.000 34.19716  ?  816  LEU   B CB  1 
ATOM   20564 C  CG  . LEU   B 1 818  ? 75.10400   85.32000  -17.92800 1.000 44.76882  ?  816  LEU   B CG  1 
ATOM   20565 C  CD1 . LEU   B 1 818  ? 74.47300   85.28900  -19.30700 1.000 41.38543  ?  816  LEU   B CD1 1 
ATOM   20566 C  CD2 . LEU   B 1 818  ? 76.23200   84.31500  -17.84100 1.000 56.03226  ?  816  LEU   B CD2 1 
ATOM   20567 N  N   . THR   B 1 819  ? 75.48200   89.56600  -15.76200 1.000 55.10355  ?  817  THR   B N   1 
ATOM   20568 C  CA  . THR   B 1 819  ? 75.98700   90.92500  -15.61700 1.000 40.67957  ?  817  THR   B CA  1 
ATOM   20569 C  C   . THR   B 1 819  ? 76.73100   91.15200  -14.30700 1.000 48.32181  ?  817  THR   B C   1 
ATOM   20570 O  O   . THR   B 1 819  ? 77.16100   92.28300  -14.05500 1.000 54.43547  ?  817  THR   B O   1 
ATOM   20571 C  CB  . THR   B 1 819  ? 74.82900   91.92200  -15.72100 1.000 50.04509  ?  817  THR   B CB  1 
ATOM   20572 O  OG1 . THR   B 1 819  ? 74.25200   92.12400  -14.42500 1.000 61.96401  ?  817  THR   B OG1 1 
ATOM   20573 C  CG2 . THR   B 1 819  ? 73.75400   91.39600  -16.66100 1.000 33.76084  ?  817  THR   B CG2 1 
ATOM   20574 N  N   . VAL   B 1 820  ? 76.88600   90.12900  -13.46900 1.000 49.89416  ?  818  VAL   B N   1 
ATOM   20575 C  CA  . VAL   B 1 820  ? 77.55000   90.25600  -12.17700 1.000 45.20372  ?  818  VAL   B CA  1 
ATOM   20576 C  C   . VAL   B 1 820  ? 78.99400   89.80100  -12.32600 1.000 50.35111  ?  818  VAL   B C   1 
ATOM   20577 O  O   . VAL   B 1 820  ? 79.26800   88.76500  -12.94800 1.000 48.10773  ?  818  VAL   B O   1 
ATOM   20578 C  CB  . VAL   B 1 820  ? 76.82500   89.44000  -11.09200 1.000 52.38698  ?  818  VAL   B CB  1 
ATOM   20579 C  CG1 . VAL   B 1 820  ? 77.58600   89.50000  -9.77600  1.000 40.41246  ?  818  VAL   B CG1 1 
ATOM   20580 C  CG2 . VAL   B 1 820  ? 75.40200   89.94200  -10.90800 1.000 48.30525  ?  818  VAL   B CG2 1 
ATOM   20581 N  N   . ASP   B 1 821  ? 79.91800   90.57400  -11.76100 1.000 54.08044  ?  819  ASP   B N   1 
ATOM   20582 C  CA  . ASP   B 1 821  ? 81.32500   90.20300  -11.79500 1.000 58.84139  ?  819  ASP   B CA  1 
ATOM   20583 C  C   . ASP   B 1 821  ? 81.57400   89.02200  -10.86700 1.000 59.65250  ?  819  ASP   B C   1 
ATOM   20584 O  O   . ASP   B 1 821  ? 81.22700   89.06400  -9.68300  1.000 56.92115  ?  819  ASP   B O   1 
ATOM   20585 C  CB  . ASP   B 1 821  ? 82.19800   91.39000  -11.39100 1.000 62.69111  ?  819  ASP   B CB  1 
ATOM   20586 C  CG  . ASP   B 1 821  ? 83.63600   91.24300  -11.85600 1.000 71.30106  ?  819  ASP   B CG  1 
ATOM   20587 O  OD1 . ASP   B 1 821  ? 84.18400   90.12100  -11.78000 1.000 72.61266  ?  819  ASP   B OD1 1 
ATOM   20588 O  OD2 . ASP   B 1 821  ? 84.21800   92.25500  -12.29900 1.000 83.99310  -1 819  ASP   B OD2 1 
ATOM   20589 N  N   . THR   B 1 822  ? 82.17800   87.96500  -11.41200 1.000 52.28068  ?  820  THR   B N   1 
ATOM   20590 C  CA  . THR   B 1 822  ? 82.45800   86.78300  -10.60700 1.000 57.81631  ?  820  THR   B CA  1 
ATOM   20591 C  C   . THR   B 1 822  ? 83.48400   87.08700  -9.52200  1.000 61.52625  ?  820  THR   B C   1 
ATOM   20592 O  O   . THR   B 1 822  ? 83.37300   86.58800  -8.39500  1.000 60.46686  ?  820  THR   B O   1 
ATOM   20593 C  CB  . THR   B 1 822  ? 82.93600   85.64600  -11.50800 1.000 46.67863  ?  820  THR   B CB  1 
ATOM   20594 O  OG1 . THR   B 1 822  ? 81.86800   85.25600  -12.37900 1.000 42.72836  ?  820  THR   B OG1 1 
ATOM   20595 C  CG2 . THR   B 1 822  ? 83.37100   84.44300  -10.68000 1.000 58.66347  ?  820  THR   B CG2 1 
ATOM   20596 N  N   . GLU   B 1 823  ? 84.48100   87.91500  -9.83600  1.000 59.85943  ?  821  GLU   B N   1 
ATOM   20597 C  CA  . GLU   B 1 823  ? 85.47600   88.27200  -8.83000  1.000 71.95890  ?  821  GLU   B CA  1 
ATOM   20598 C  C   . GLU   B 1 823  ? 84.84700   89.06800  -7.69700  1.000 60.98516  ?  821  GLU   B C   1 
ATOM   20599 O  O   . GLU   B 1 823  ? 85.15500   88.83200  -6.52300  1.000 57.70400  ?  821  GLU   B O   1 
ATOM   20600 C  CB  . GLU   B 1 823  ? 86.62100   89.05300  -9.47200  1.000 56.92564  ?  821  GLU   B CB  1 
ATOM   20601 C  CG  . GLU   B 1 823  ? 87.35100   88.27100  -10.54800 1.000 62.96522  ?  821  GLU   B CG  1 
ATOM   20602 C  CD  . GLU   B 1 823  ? 87.47600   86.79700  -10.20400 1.000 81.24710  ?  821  GLU   B CD  1 
ATOM   20603 O  OE1 . GLU   B 1 823  ? 88.18800   86.46800  -9.23000  1.000 84.81368  ?  821  GLU   B OE1 1 
ATOM   20604 O  OE2 . GLU   B 1 823  ? 86.85300   85.96900  -10.90200 1.000 66.56200  -1 821  GLU   B OE2 1 
ATOM   20605 N  N   . GLN   B 1 824  ? 83.95000   90.00200  -8.03000  1.000 52.72575  ?  822  GLN   B N   1 
ATOM   20606 C  CA  . GLN   B 1 824  ? 83.26300   90.79200  -7.01100  1.000 52.61454  ?  822  GLN   B CA  1 
ATOM   20607 C  C   . GLN   B 1 824  ? 82.62100   89.90200  -5.95500  1.000 61.73949  ?  822  GLN   B C   1 
ATOM   20608 O  O   . GLN   B 1 824  ? 82.61100   90.24100  -4.76500  1.000 66.35830  ?  822  GLN   B O   1 
ATOM   20609 C  CB  . GLN   B 1 824  ? 82.20900   91.68500  -7.66600  1.000 46.01031  ?  822  GLN   B CB  1 
ATOM   20610 C  CG  . GLN   B 1 824  ? 81.77500   92.86600  -6.81400  1.000 71.73884  ?  822  GLN   B CG  1 
ATOM   20611 C  CD  . GLN   B 1 824  ? 80.80900   93.78800  -7.53700  1.000 78.45838  ?  822  GLN   B CD  1 
ATOM   20612 O  OE1 . GLN   B 1 824  ? 79.65300   93.43500  -7.77700  1.000 59.63035  ?  822  GLN   B OE1 1 
ATOM   20613 N  NE2 . GLN   B 1 824  ? 81.28100   94.97900  -7.88800  1.000 67.88761  ?  822  GLN   B NE2 1 
ATOM   20614 N  N   . ILE   B 1 825  ? 82.08400   88.75400  -6.37100  1.000 60.44862  ?  823  ILE   B N   1 
ATOM   20615 C  CA  . ILE   B 1 825  ? 81.54800   87.79500  -5.41200  1.000 51.79040  ?  823  ILE   B CA  1 
ATOM   20616 C  C   . ILE   B 1 825  ? 82.66800   87.19600  -4.57200  1.000 51.47057  ?  823  ILE   B C   1 
ATOM   20617 O  O   . ILE   B 1 825  ? 82.52100   87.01800  -3.35600  1.000 53.14200  ?  823  ILE   B O   1 
ATOM   20618 C  CB  . ILE   B 1 825  ? 80.74600   86.70500  -6.14300  1.000 46.24313  ?  823  ILE   B CB  1 
ATOM   20619 C  CG1 . ILE   B 1 825  ? 79.75600   87.33800  -7.11900  1.000 50.42623  ?  823  ILE   B CG1 1 
ATOM   20620 C  CG2 . ILE   B 1 825  ? 80.02500   85.81800  -5.14600  1.000 48.18052  ?  823  ILE   B CG2 1 
ATOM   20621 C  CD1 . ILE   B 1 825  ? 79.09100   86.33900  -8.03100  1.000 45.57766  ?  823  ILE   B CD1 1 
ATOM   20622 N  N   . ARG   B 1 826  ? 83.80500   86.87800  -5.20000  1.000 55.33421  ?  824  ARG   B N   1 
ATOM   20623 C  CA  . ARG   B 1 826  ? 84.91000   86.26900  -4.46500  1.000 59.96409  ?  824  ARG   B CA  1 
ATOM   20624 C  C   . ARG   B 1 826  ? 85.45900   87.21200  -3.40200  1.000 54.45048  ?  824  ARG   B C   1 
ATOM   20625 O  O   . ARG   B 1 826  ? 85.72700   86.79000  -2.27000  1.000 54.58553  ?  824  ARG   B O   1 
ATOM   20626 C  CB  . ARG   B 1 826  ? 86.02300   85.84800  -5.42700  1.000 46.18495  ?  824  ARG   B CB  1 
ATOM   20627 C  CG  . ARG   B 1 826  ? 87.30300   85.41900  -4.72000  1.000 39.54592  ?  824  ARG   B CG  1 
ATOM   20628 C  CD  . ARG   B 1 826  ? 88.47100   85.29500  -5.68700  1.000 60.89355  ?  824  ARG   B CD  1 
ATOM   20629 N  NE  . ARG   B 1 826  ? 88.72800   86.53600  -6.41000  1.000 84.83207  ?  824  ARG   B NE  1 
ATOM   20630 C  CZ  . ARG   B 1 826  ? 89.30200   87.61100  -5.88600  1.000 77.06121  ?  824  ARG   B CZ  1 
ATOM   20631 N  NH1 . ARG   B 1 826  ? 89.68800   87.64300  -4.62000  1.000 65.29908  ?  824  ARG   B NH1 1 
ATOM   20632 N  NH2 . ARG   B 1 826  ? 89.49400   88.68200  -6.65100  1.000 75.84226  ?  824  ARG   B NH2 1 
ATOM   20633 N  N   . VAL   B 1 827  ? 85.63800   88.49000  -3.74500  1.000 50.12791  ?  825  VAL   B N   1 
ATOM   20634 C  CA  . VAL   B 1 827  ? 86.14700   89.45500  -2.77200  1.000 52.65344  ?  825  VAL   B CA  1 
ATOM   20635 C  C   . VAL   B 1 827  ? 85.20700   89.55200  -1.57800  1.000 53.96999  ?  825  VAL   B C   1 
ATOM   20636 O  O   . VAL   B 1 827  ? 85.64100   89.51700  -0.42000  1.000 57.04572  ?  825  VAL   B O   1 
ATOM   20637 C  CB  . VAL   B 1 827  ? 86.36400   90.83000  -3.43100  1.000 47.32241  ?  825  VAL   B CB  1 
ATOM   20638 C  CG1 . VAL   B 1 827  ? 87.33400   91.66200  -2.60400  1.000 58.77888  ?  825  VAL   B CG1 1 
ATOM   20639 C  CG2 . VAL   B 1 827  ? 86.89800   90.66500  -4.83800  1.000 50.72776  ?  825  VAL   B CG2 1 
ATOM   20640 N  N   . ALA   B 1 828  ? 83.90200   89.66600  -1.84300  1.000 49.94621  ?  826  ALA   B N   1 
ATOM   20641 C  CA  . ALA   B 1 828  ? 82.93100   89.79800  -0.76100  1.000 42.32530  ?  826  ALA   B CA  1 
ATOM   20642 C  C   . ALA   B 1 828  ? 82.95100   88.58100  0.15300   1.000 50.22882  ?  826  ALA   B C   1 
ATOM   20643 O  O   . ALA   B 1 828  ? 82.75700   88.70300  1.36800   1.000 53.87521  ?  826  ALA   B O   1 
ATOM   20644 C  CB  . ALA   B 1 828  ? 81.53300   90.00900  -1.33500  1.000 39.20938  ?  826  ALA   B CB  1 
ATOM   20645 N  N   . LEU   B 1 829  ? 83.17900   87.39500  -0.41400  1.000 48.79750  ?  827  LEU   B N   1 
ATOM   20646 C  CA  . LEU   B 1 829  ? 83.27100   86.19700  0.41000   1.000 45.66577  ?  827  LEU   B CA  1 
ATOM   20647 C  C   . LEU   B 1 829  ? 84.58900   86.15300  1.17300   1.000 52.07704  ?  827  LEU   B C   1 
ATOM   20648 O  O   . LEU   B 1 829  ? 84.62800   85.72200  2.33100   1.000 51.06304  ?  827  LEU   B O   1 
ATOM   20649 C  CB  . LEU   B 1 829  ? 83.10400   84.95100  -0.45600  1.000 41.18852  ?  827  LEU   B CB  1 
ATOM   20650 C  CG  . LEU   B 1 829  ? 81.71000   84.76300  -1.05300  1.000 51.20013  ?  827  LEU   B CG  1 
ATOM   20651 C  CD1 . LEU   B 1 829  ? 81.67600   83.52000  -1.92500  1.000 34.65900  ?  827  LEU   B CD1 1 
ATOM   20652 C  CD2 . LEU   B 1 829  ? 80.65900   84.69500  0.04800   1.000 29.14551  ?  827  LEU   B CD2 1 
ATOM   20653 N  N   . GLU   B 1 830  ? 85.67900   86.60100  0.54600   1.000 52.44885  ?  828  GLU   B N   1 
ATOM   20654 C  CA  . GLU   B 1 830  ? 86.95300   86.65400  1.25400   1.000 55.75668  ?  828  GLU   B CA  1 
ATOM   20655 C  C   . GLU   B 1 830  ? 86.93000   87.69400  2.36700   1.000 57.35001  ?  828  GLU   B C   1 
ATOM   20656 O  O   . GLU   B 1 830  ? 87.63700   87.54300  3.37100   1.000 58.10083  ?  828  GLU   B O   1 
ATOM   20657 C  CB  . GLU   B 1 830  ? 88.08700   86.93100  0.26700   1.000 25.94578  ?  828  GLU   B CB  1 
ATOM   20658 C  CG  . GLU   B 1 830  ? 88.43200   85.72600  -0.59800  1.000 48.63923  ?  828  GLU   B CG  1 
ATOM   20659 C  CD  . GLU   B 1 830  ? 89.36000   86.07000  -1.74500  1.000 65.41745  ?  828  GLU   B CD  1 
ATOM   20660 O  OE1 . GLU   B 1 830  ? 89.49800   87.27100  -2.06000  1.000 64.42069  ?  828  GLU   B OE1 1 
ATOM   20661 O  OE2 . GLU   B 1 830  ? 89.94500   85.13700  -2.33800  1.000 52.84065  -1 828  GLU   B OE2 1 
ATOM   20662 N  N   . GLN   B 1 831  ? 86.12400   88.74800  2.21200   1.000 44.46435  ?  829  GLN   B N   1 
ATOM   20663 C  CA  . GLN   B 1 831  ? 85.95900   89.71300  3.29300   1.000 49.13758  ?  829  GLN   B CA  1 
ATOM   20664 C  C   . GLN   B 1 831  ? 85.12500   89.13700  4.42700   1.000 60.85601  ?  829  GLN   B C   1 
ATOM   20665 O  O   . GLN   B 1 831  ? 85.36500   89.45800  5.59700   1.000 66.42870  ?  829  GLN   B O   1 
ATOM   20666 C  CB  . GLN   B 1 831  ? 85.31600   90.99800  2.76700   1.000 40.89823  ?  829  GLN   B CB  1 
ATOM   20667 C  CG  . GLN   B 1 831  ? 86.19400   91.79700  1.81700   1.000 62.42378  ?  829  GLN   B CG  1 
ATOM   20668 C  CD  . GLN   B 1 831  ? 85.43800   92.91300  1.11600   1.000 71.14587  ?  829  GLN   B CD  1 
ATOM   20669 O  OE1 . GLN   B 1 831  ? 84.23800   92.80200  0.86100   1.000 64.56920  ?  829  GLN   B OE1 1 
ATOM   20670 N  NE2 . GLN   B 1 831  ? 86.14200   93.99300  0.79500   1.000 70.11095  ?  829  GLN   B NE2 1 
ATOM   20671 N  N   . LEU   B 1 832  ? 84.14200   88.29300  4.10500   1.000 55.99695  ?  830  LEU   B N   1 
ATOM   20672 C  CA  . LEU   B 1 832  ? 83.32900   87.68100  5.15000   1.000 47.67126  ?  830  LEU   B CA  1 
ATOM   20673 C  C   . LEU   B 1 832  ? 84.12900   86.66400  5.95100   1.000 56.76193  ?  830  LEU   B C   1 
ATOM   20674 O  O   . LEU   B 1 832  ? 83.84000   86.44500  7.13400   1.000 58.72081  ?  830  LEU   B O   1 
ATOM   20675 C  CB  . LEU   B 1 832  ? 82.08800   87.03000  4.54200   1.000 38.30435  ?  830  LEU   B CB  1 
ATOM   20676 C  CG  . LEU   B 1 832  ? 80.97200   87.98900  4.12100   1.000 47.44976  ?  830  LEU   B CG  1 
ATOM   20677 C  CD1 . LEU   B 1 832  ? 80.07100   87.35100  3.07700   1.000 50.74253  ?  830  LEU   B CD1 1 
ATOM   20678 C  CD2 . LEU   B 1 832  ? 80.15900   88.43100  5.32400   1.000 40.05957  ?  830  LEU   B CD2 1 
ATOM   20679 N  N   . VAL   B 1 833  ? 85.13200   86.03700  5.33100   1.000 51.98738  ?  831  VAL   B N   1 
ATOM   20680 C  CA  . VAL   B 1 833  ? 86.01800   85.14800  6.07500   1.000 57.95796  ?  831  VAL   B CA  1 
ATOM   20681 C  C   . VAL   B 1 833  ? 86.76100   85.92600  7.15200   1.000 63.55003  ?  831  VAL   B C   1 
ATOM   20682 O  O   . VAL   B 1 833  ? 86.88200   85.47400  8.29800   1.000 64.59891  ?  831  VAL   B O   1 
ATOM   20683 C  CB  . VAL   B 1 833  ? 86.98600   84.43300  5.11300   1.000 54.43399  ?  831  VAL   B CB  1 
ATOM   20684 C  CG1 . VAL   B 1 833  ? 88.28100   84.07600  5.82000   1.000 46.67120  ?  831  VAL   B CG1 1 
ATOM   20685 C  CG2 . VAL   B 1 833  ? 86.33300   83.18400  4.54800   1.000 52.72271  ?  831  VAL   B CG2 1 
ATOM   20686 N  N   . LEU   B 1 834  ? 87.24700   87.12100  6.80900   1.000 58.51641  ?  832  LEU   B N   1 
ATOM   20687 C  CA  . LEU   B 1 834  ? 87.93500   87.95200  7.78900   1.000 51.74377  ?  832  LEU   B CA  1 
ATOM   20688 C  C   . LEU   B 1 834  ? 86.97300   88.53800  8.81600   1.000 51.83113  ?  832  LEU   B C   1 
ATOM   20689 O  O   . LEU   B 1 834  ? 87.34600   88.71100  9.98100   1.000 71.27942  ?  832  LEU   B O   1 
ATOM   20690 C  CB  . LEU   B 1 834  ? 88.69200   89.07400  7.08300   1.000 54.31522  ?  832  LEU   B CB  1 
ATOM   20691 C  CG  . LEU   B 1 834  ? 89.94800   88.66100  6.31800   1.000 72.23237  ?  832  LEU   B CG  1 
ATOM   20692 C  CD1 . LEU   B 1 834  ? 90.28300   89.70400  5.26400   1.000 54.84398  ?  832  LEU   B CD1 1 
ATOM   20693 C  CD2 . LEU   B 1 834  ? 91.11600   88.44700  7.27400   1.000 65.52096  ?  832  LEU   B CD2 1 
ATOM   20694 N  N   . ARG   B 1 835  ? 85.73900   88.84200  8.41000   1.000 45.46906  ?  833  ARG   B N   1 
ATOM   20695 C  CA  . ARG   B 1 835  ? 84.81700   89.54100  9.30100   1.000 48.32633  ?  833  ARG   B CA  1 
ATOM   20696 C  C   . ARG   B 1 835  ? 84.34900   88.64600  10.44300  1.000 56.12725  ?  833  ARG   B C   1 
ATOM   20697 O  O   . ARG   B 1 835  ? 84.20500   89.10900  11.58200  1.000 49.80048  ?  833  ARG   B O   1 
ATOM   20698 C  CB  . ARG   B 1 835  ? 83.62300   90.06700  8.50500   1.000 49.09044  ?  833  ARG   B CB  1 
ATOM   20699 C  CG  . ARG   B 1 835  ? 82.51000   90.65300  9.35400   1.000 43.76466  ?  833  ARG   B CG  1 
ATOM   20700 C  CD  . ARG   B 1 835  ? 81.48600   91.36400  8.48900   1.000 45.24402  ?  833  ARG   B CD  1 
ATOM   20701 N  NE  . ARG   B 1 835  ? 80.27500   91.67600  9.23700   1.000 58.48529  ?  833  ARG   B NE  1 
ATOM   20702 C  CZ  . ARG   B 1 835  ? 80.07700   92.80800  9.89800   1.000 57.02469  ?  833  ARG   B CZ  1 
ATOM   20703 N  NH1 . ARG   B 1 835  ? 80.99200   93.76200  9.92000   1.000 75.26969  ?  833  ARG   B NH1 1 
ATOM   20704 N  NH2 . ARG   B 1 835  ? 78.93500   92.98400  10.55600  1.000 53.92412  ?  833  ARG   B NH2 1 
ATOM   20705 N  N   . HIS   B 1 836  ? 84.11100   87.36800  10.16500  1.000 61.37666  ?  834  HIS   B N   1 
ATOM   20706 C  CA  . HIS   B 1 836  ? 83.57200   86.43700  11.14700  1.000 59.15949  ?  834  HIS   B CA  1 
ATOM   20707 C  C   . HIS   B 1 836  ? 84.62200   85.39700  11.50900  1.000 65.10036  ?  834  HIS   B C   1 
ATOM   20708 O  O   . HIS   B 1 836  ? 85.18600   84.74000  10.62500  1.000 52.09783  ?  834  HIS   B O   1 
ATOM   20709 C  CB  . HIS   B 1 836  ? 82.31000   85.76200  10.61400  1.000 47.53768  ?  834  HIS   B CB  1 
ATOM   20710 C  CG  . HIS   B 1 836  ? 81.25600   86.73000  10.17900  1.000 53.25820  ?  834  HIS   B CG  1 
ATOM   20711 N  ND1 . HIS   B 1 836  ? 80.43500   87.38500  11.07200  1.000 59.60808  ?  834  HIS   B ND1 1 
ATOM   20712 C  CD2 . HIS   B 1 836  ? 80.89800   87.16600  8.94800   1.000 47.21164  ?  834  HIS   B CD2 1 
ATOM   20713 C  CE1 . HIS   B 1 836  ? 79.61100   88.17700  10.40900  1.000 59.56248  ?  834  HIS   B CE1 1 
ATOM   20714 N  NE2 . HIS   B 1 836  ? 79.87000   88.06200  9.11900   1.000 53.03463  ?  834  HIS   B NE2 1 
ATOM   20715 N  N   . GLU   B 1 837  ? 84.87300   85.24900  12.81400  1.000 62.67137  ?  835  GLU   B N   1 
ATOM   20716 C  CA  . GLU   B 1 837  ? 85.90100   84.32400  13.27900  1.000 73.28205  ?  835  GLU   B CA  1 
ATOM   20717 C  C   . GLU   B 1 837  ? 85.54700   82.87900  12.96100  1.000 57.52871  ?  835  GLU   B C   1 
ATOM   20718 O  O   . GLU   B 1 837  ? 86.44700   82.05100  12.77500  1.000 59.77010  ?  835  GLU   B O   1 
ATOM   20719 C  CB  . GLU   B 1 837  ? 86.11800   84.49100  14.78300  1.000 71.76834  ?  835  GLU   B CB  1 
ATOM   20720 C  CG  . GLU   B 1 837  ? 87.08700   85.60000  15.15800  1.000 71.79498  ?  835  GLU   B CG  1 
ATOM   20721 C  CD  . GLU   B 1 837  ? 87.38400   85.63100  16.64500  1.000 68.14723  ?  835  GLU   B CD  1 
ATOM   20722 O  OE1 . GLU   B 1 837  ? 86.67100   84.94500  17.40700  1.000 60.94057  ?  835  GLU   B OE1 1 
ATOM   20723 O  OE2 . GLU   B 1 837  ? 88.32800   86.34000  17.05100  1.000 88.92692  -1 835  GLU   B OE2 1 
ATOM   20724 N  N   . GLY   B 1 838  ? 84.25400   82.55400  12.90700  1.000 50.80614  ?  836  GLY   B N   1 
ATOM   20725 C  CA  . GLY   B 1 838  ? 83.85700   81.19200  12.58800  1.000 42.89865  ?  836  GLY   B CA  1 
ATOM   20726 C  C   . GLY   B 1 838  ? 84.40700   80.72500  11.25600  1.000 47.77324  ?  836  GLY   B C   1 
ATOM   20727 O  O   . GLY   B 1 838  ? 84.86000   79.58500  11.12300  1.000 49.49755  ?  836  GLY   B O   1 
ATOM   20728 N  N   . LEU   B 1 839  ? 84.39200   81.60600  10.25400  1.000 47.71150  ?  837  LEU   B N   1 
ATOM   20729 C  CA  . LEU   B 1 839  ? 84.96600   81.27300  8.95900   1.000 56.82733  ?  837  LEU   B CA  1 
ATOM   20730 C  C   . LEU   B 1 839  ? 86.48200   81.14600  9.01000   1.000 59.69938  ?  837  LEU   B C   1 
ATOM   20731 O  O   . LEU   B 1 839  ? 87.08500   80.70200  8.02800   1.000 57.02356  ?  837  LEU   B O   1 
ATOM   20732 C  CB  . LEU   B 1 839  ? 84.55600   82.32200  7.92600   1.000 59.22272  ?  837  LEU   B CB  1 
ATOM   20733 C  CG  . LEU   B 1 839  ? 83.13100   82.16500  7.39200   1.000 46.58584  ?  837  LEU   B CG  1 
ATOM   20734 C  CD1 . LEU   B 1 839  ? 82.59300   83.49500  6.89200   1.000 44.34898  ?  837  LEU   B CD1 1 
ATOM   20735 C  CD2 . LEU   B 1 839  ? 83.09100   81.11200  6.29500   1.000 34.58369  ?  837  LEU   B CD2 1 
ATOM   20736 N  N   . ARG   B 1 840  ? 87.10500   81.52100  10.12500  1.000 63.93091  ?  838  ARG   B N   1 
ATOM   20737 C  CA  . ARG   B 1 840  ? 88.52900   81.32300  10.32800  1.000 62.81540  ?  838  ARG   B CA  1 
ATOM   20738 C  C   . ARG   B 1 840  ? 88.82800   80.43000  11.52500  1.000 66.06501  ?  838  ARG   B C   1 
ATOM   20739 O  O   . ARG   B 1 840  ? 90.00300   80.23700  11.85700  1.000 70.16923  ?  838  ARG   B O   1 
ATOM   20740 C  CB  . ARG   B 1 840  ? 89.23000   82.67700  10.49700  1.000 63.85923  ?  838  ARG   B CB  1 
ATOM   20741 C  CG  . ARG   B 1 840  ? 89.64000   83.32900  9.18200   1.000 69.75234  ?  838  ARG   B CG  1 
ATOM   20742 C  CD  . ARG   B 1 840  ? 89.94500   84.81700  9.34700   1.000 57.79685  ?  838  ARG   B CD  1 
ATOM   20743 N  NE  . ARG   B 1 840  ? 90.18000   85.19000  10.73800  1.000 74.48296  ?  838  ARG   B NE  1 
ATOM   20744 C  CZ  . ARG   B 1 840  ? 89.36800   85.95400  11.45900  1.000 70.30681  ?  838  ARG   B CZ  1 
ATOM   20745 N  NH1 . ARG   B 1 840  ? 88.25800   86.45800  10.94700  1.000 60.74469  ?  838  ARG   B NH1 1 
ATOM   20746 N  NH2 . ARG   B 1 840  ? 89.68100   86.21800  12.72400  1.000 77.17164  ?  838  ARG   B NH2 1 
ATOM   20747 N  N   . SER   B 1 841  ? 87.80400   79.87500  12.17400  1.000 48.83266  ?  839  SER   B N   1 
ATOM   20748 C  CA  . SER   B 1 841  ? 87.98500   79.01700  13.33700  1.000 40.98271  ?  839  SER   B CA  1 
ATOM   20749 C  C   . SER   B 1 841  ? 88.18500   77.57200  12.89800  1.000 49.39796  ?  839  SER   B C   1 
ATOM   20750 O  O   . SER   B 1 841  ? 87.43100   77.06200  12.06400  1.000 71.46645  ?  839  SER   B O   1 
ATOM   20751 C  CB  . SER   B 1 841  ? 86.77600   79.10900  14.27100  1.000 53.36074  ?  839  SER   B CB  1 
ATOM   20752 O  OG  . SER   B 1 841  ? 86.43100   80.45400  14.55300  1.000 64.14785  ?  839  SER   B OG  1 
ATOM   20753 N  N   . THR   B 1 842  ? 89.19800   76.92000  13.45900  1.000 59.37734  ?  840  THR   B N   1 
ATOM   20754 C  CA  . THR   B 1 842  ? 89.40200   75.48800  13.29900  1.000 64.09921  ?  840  THR   B CA  1 
ATOM   20755 C  C   . THR   B 1 842  ? 89.23100   74.79500  14.64700  1.000 57.98022  ?  840  THR   B C   1 
ATOM   20756 O  O   . THR   B 1 842  ? 89.38400   75.40600  15.70800  1.000 62.19003  ?  840  THR   B O   1 
ATOM   20757 C  CB  . THR   B 1 842  ? 90.78400   75.17600  12.70500  1.000 56.78883  ?  840  THR   B CB  1 
ATOM   20758 O  OG1 . THR   B 1 842  ? 91.33300   74.01700  13.34300  1.000 67.93467  ?  840  THR   B OG1 1 
ATOM   20759 C  CG2 . THR   B 1 842  ? 91.73400   76.34700  12.88100  1.000 62.31201  ?  840  THR   B CG2 1 
ATOM   20760 N  N   . TYR   B 1 843  ? 88.89600   73.50800  14.59600  1.000 55.35871  ?  841  TYR   B N   1 
ATOM   20761 C  CA  . TYR   B 1 843  ? 88.55600   72.73700  15.78500  1.000 55.23907  ?  841  TYR   B CA  1 
ATOM   20762 C  C   . TYR   B 1 843  ? 89.55000   71.59700  15.96000  1.000 70.36929  ?  841  TYR   B C   1 
ATOM   20763 O  O   . TYR   B 1 843  ? 89.85600   70.88200  15.00000  1.000 64.78621  ?  841  TYR   B O   1 
ATOM   20764 C  CB  . TYR   B 1 843  ? 87.12700   72.19200  15.69300  1.000 51.77222  ?  841  TYR   B CB  1 
ATOM   20765 C  CG  . TYR   B 1 843  ? 86.06000   73.26700  15.71300  1.000 54.14321  ?  841  TYR   B CG  1 
ATOM   20766 C  CD1 . TYR   B 1 843  ? 85.79400   74.03200  14.58400  1.000 48.64660  ?  841  TYR   B CD1 1 
ATOM   20767 C  CD2 . TYR   B 1 843  ? 85.31700   73.51400  16.86100  1.000 60.76764  ?  841  TYR   B CD2 1 
ATOM   20768 C  CE1 . TYR   B 1 843  ? 84.82200   75.01600  14.59900  1.000 44.86207  ?  841  TYR   B CE1 1 
ATOM   20769 C  CE2 . TYR   B 1 843  ? 84.34200   74.49400  16.88500  1.000 64.79468  ?  841  TYR   B CE2 1 
ATOM   20770 C  CZ  . TYR   B 1 843  ? 84.09800   75.24100  15.75300  1.000 63.77623  ?  841  TYR   B CZ  1 
ATOM   20771 O  OH  . TYR   B 1 843  ? 83.12600   76.21500  15.78100  1.000 63.07152  ?  841  TYR   B OH  1 
ATOM   20772 N  N   . HIS   B 1 844  ? 90.04900   71.43200  17.18600  1.000 79.70215  ?  842  HIS   B N   1 
ATOM   20773 C  CA  . HIS   B 1 844  ? 91.00900   70.37900  17.49600  1.000 70.69523  ?  842  HIS   B CA  1 
ATOM   20774 C  C   . HIS   B 1 844  ? 90.64100   69.66400  18.79000  1.000 69.60992  ?  842  HIS   B C   1 
ATOM   20775 O  O   . HIS   B 1 844  ? 89.55400   69.87400  19.33900  1.000 69.28948  ?  842  HIS   B O   1 
ATOM   20776 C  CB  . HIS   B 1 844  ? 92.42200   70.95500  17.60000  1.000 60.25705  ?  842  HIS   B CB  1 
ATOM   20777 C  CG  . HIS   B 1 844  ? 92.82700   71.77900  16.41900  1.000 67.07155  ?  842  HIS   B CG  1 
ATOM   20778 N  ND1 . HIS   B 1 844  ? 93.49100   71.24900  15.33300  1.000 83.26546  ?  842  HIS   B ND1 1 
ATOM   20779 C  CD2 . HIS   B 1 844  ? 92.65800   73.09600  16.15000  1.000 62.33328  ?  842  HIS   B CD2 1 
ATOM   20780 C  CE1 . HIS   B 1 844  ? 93.71900   72.20400  14.44900  1.000 64.19503  ?  842  HIS   B CE1 1 
ATOM   20781 N  NE2 . HIS   B 1 844  ? 93.22200   73.33400  14.92000  1.000 76.94189  ?  842  HIS   B NE2 1 
ATOM   20782 N  N   . MET   B 1 845  ? 91.54300   68.82100  19.28800  1.000 67.37742  ?  843  MET   B N   1 
ATOM   20783 C  CA  . MET   B 1 845  ? 91.29800   68.05400  20.50200  1.000 81.74929  ?  843  MET   B CA  1 
ATOM   20784 C  C   . MET   B 1 845  ? 92.52900   68.09800  21.39400  1.000 83.78529  ?  843  MET   B C   1 
ATOM   20785 O  O   . MET   B 1 845  ? 93.64500   67.84400  20.92900  1.000 70.38285  ?  843  MET   B O   1 
ATOM   20786 C  CB  . MET   B 1 845  ? 90.93700   66.60000  20.17700  1.000 68.16419  ?  843  MET   B CB  1 
ATOM   20787 C  CG  . MET   B 1 845  ? 90.26800   65.86300  21.32500  1.000 74.05920  ?  843  MET   B CG  1 
ATOM   20788 S  SD  . MET   B 1 845  ? 88.88400   64.83900  20.79100  1.000 82.85160  ?  843  MET   B SD  1 
ATOM   20789 C  CE  . MET   B 1 845  ? 88.33600   64.15600  22.35400  1.000 70.75832  ?  843  MET   B CE  1 
ATOM   20790 N  N   . ARG   B 1 846  ? 92.32000   68.42400  22.66900  1.000 81.51336  ?  844  ARG   B N   1 
ATOM   20791 C  CA  . ARG   B 1 846  ? 93.37000   68.41400  23.68600  1.000 84.85713  ?  844  ARG   B CA  1 
ATOM   20792 C  C   . ARG   B 1 846  ? 93.09300   67.24700  24.62800  1.000 86.96142  ?  844  ARG   B C   1 
ATOM   20793 O  O   . ARG   B 1 846  ? 92.20100   67.32700  25.47800  1.000 80.17661  ?  844  ARG   B O   1 
ATOM   20794 C  CB  . ARG   B 1 846  ? 93.42100   69.73400  24.45000  1.000 71.42540  ?  844  ARG   B CB  1 
ATOM   20795 C  CG  . ARG   B 1 846  ? 94.67000   69.86400  25.29900  1.000 74.97437  ?  844  ARG   B CG  1 
ATOM   20796 C  CD  . ARG   B 1 846  ? 95.59800   70.94500  24.78900  1.000 71.40442  ?  844  ARG   B CD  1 
ATOM   20797 N  NE  . ARG   B 1 846  ? 96.50100   70.42700  23.77100  1.000 88.71255  ?  844  ARG   B NE  1 
ATOM   20798 C  CZ  . ARG   B 1 846  ? 97.33100   71.17300  23.05600  1.000 86.43918  ?  844  ARG   B CZ  1 
ATOM   20799 N  NH1 . ARG   B 1 846  ? 97.45300   72.47200  23.27300  1.000 87.71907  ?  844  ARG   B NH1 1 
ATOM   20800 N  NH2 . ARG   B 1 846  ? 98.07800   70.59600  22.11800  1.000 108.32255 ?  844  ARG   B NH2 1 
ATOM   20801 N  N   . GLY   B 1 847  ? 93.86400   66.17100  24.48300  1.000 79.61112  ?  845  GLY   B N   1 
ATOM   20802 C  CA  . GLY   B 1 847  ? 93.63700   64.97000  25.26300  1.000 71.32956  ?  845  GLY   B CA  1 
ATOM   20803 C  C   . GLY   B 1 847  ? 92.23900   64.42100  25.07100  1.000 76.66967  ?  845  GLY   B C   1 
ATOM   20804 O  O   . GLY   B 1 847  ? 91.97900   63.68200  24.11700  1.000 80.97700  ?  845  GLY   B O   1 
ATOM   20805 N  N   . ASP   B 1 848  ? 91.32300   64.79400  25.96800  1.000 70.48028  ?  846  ASP   B N   1 
ATOM   20806 C  CA  . ASP   B 1 848  ? 89.92600   64.38100  25.90000  1.000 80.25393  ?  846  ASP   B CA  1 
ATOM   20807 C  C   . ASP   B 1 848  ? 88.98700   65.58400  25.89400  1.000 85.75029  ?  846  ASP   B C   1 
ATOM   20808 O  O   . ASP   B 1 848  ? 87.83700   65.48100  26.32500  1.000 79.26253  ?  846  ASP   B O   1 
ATOM   20809 C  CB  . ASP   B 1 848  ? 89.57400   63.44700  27.05800  1.000 85.17814  ?  846  ASP   B CB  1 
ATOM   20810 C  CG  . ASP   B 1 848  ? 90.36300   62.15700  27.02800  1.000 89.15153  ?  846  ASP   B CG  1 
ATOM   20811 O  OD1 . ASP   B 1 848  ? 90.36000   61.48400  25.97600  1.000 93.45407  ?  846  ASP   B OD1 1 
ATOM   20812 O  OD2 . ASP   B 1 848  ? 90.98200   61.81500  28.05800  1.000 89.37738  -1 846  ASP   B OD2 1 
ATOM   20813 N  N   . GLU   B 1 849  ? 89.46000   66.73000  25.40800  1.000 87.92814  ?  847  GLU   B N   1 
ATOM   20814 C  CA  . GLU   B 1 849  ? 88.67200   67.95700  25.40200  1.000 82.37415  ?  847  GLU   B CA  1 
ATOM   20815 C  C   . GLU   B 1 849  ? 88.65000   68.55100  24.00200  1.000 73.85405  ?  847  GLU   B C   1 
ATOM   20816 O  O   . GLU   B 1 849  ? 89.69000   68.63100  23.34000  1.000 63.30633  ?  847  GLU   B O   1 
ATOM   20817 C  CB  . GLU   B 1 849  ? 89.22900   68.97900  26.40100  1.000 75.36285  ?  847  GLU   B CB  1 
ATOM   20818 C  CG  . GLU   B 1 849  ? 88.16100   69.83400  27.08600  1.000 86.63468  ?  847  GLU   B CG  1 
ATOM   20819 C  CD  . GLU   B 1 849  ? 87.09500   69.00500  27.77800  1.000 98.15993  ?  847  GLU   B CD  1 
ATOM   20820 O  OE1 . GLU   B 1 849  ? 87.46400   68.10000  28.55500  1.000 95.95710  ?  847  GLU   B OE1 1 
ATOM   20821 O  OE2 . GLU   B 1 849  ? 85.89100   69.25700  27.55000  1.000 101.32415 -1 847  GLU   B OE2 1 
ATOM   20822 N  N   . ILE   B 1 850  ? 87.46300   68.96900  23.56200  1.000 71.61318  ?  848  ILE   B N   1 
ATOM   20823 C  CA  . ILE   B 1 850  ? 87.30000   69.61300  22.26200  1.000 84.28022  ?  848  ILE   B CA  1 
ATOM   20824 C  C   . ILE   B 1 850  ? 87.62800   71.09200  22.40800  1.000 74.46567  ?  848  ILE   B C   1 
ATOM   20825 O  O   . ILE   B 1 850  ? 87.05300   71.78600  23.25500  1.000 70.02141  ?  848  ILE   B O   1 
ATOM   20826 C  CB  . ILE   B 1 850  ? 85.87300   69.41100  21.72500  1.000 81.30249  ?  848  ILE   B CB  1 
ATOM   20827 C  CG1 . ILE   B 1 850  ? 85.51600   67.92200  21.70700  1.000 62.20259  ?  848  ILE   B CG1 1 
ATOM   20828 C  CG2 . ILE   B 1 850  ? 85.73100   70.02900  20.34000  1.000 71.98000  ?  848  ILE   B CG2 1 
ATOM   20829 C  CD1 . ILE   B 1 850  ? 85.96000   67.18900  20.46400  1.000 61.48200  ?  848  ILE   B CD1 1 
ATOM   20830 N  N   . VAL   B 1 851  ? 88.55800   71.58000  21.58500  1.000 64.91385  ?  849  VAL   B N   1 
ATOM   20831 C  CA  . VAL   B 1 851  ? 89.05200   72.94500  21.69700  1.000 76.88211  ?  849  VAL   B CA  1 
ATOM   20832 C  C   . VAL   B 1 851  ? 88.91700   73.65000  20.35400  1.000 82.76551  ?  849  VAL   B C   1 
ATOM   20833 O  O   . VAL   B 1 851  ? 88.78700   73.02100  19.30200  1.000 96.96887  ?  849  VAL   B O   1 
ATOM   20834 C  CB  . VAL   B 1 851  ? 90.51700   72.99900  22.18700  1.000 80.07274  ?  849  VAL   B CB  1 
ATOM   20835 C  CG1 . VAL   B 1 851  ? 90.57400   72.76800  23.68700  1.000 84.44477  ?  849  VAL   B CG1 1 
ATOM   20836 C  CG2 . VAL   B 1 851  ? 91.37000   71.97300  21.44900  1.000 63.40231  ?  849  VAL   B CG2 1 
ATOM   20837 N  N   . LYS   B 1 852  ? 88.94200   74.97800  20.41000  1.000 77.20596  ?  850  LYS   B N   1 
ATOM   20838 C  CA  . LYS   B 1 852  ? 88.81300   75.82900  19.23900  1.000 64.09069  ?  850  LYS   B CA  1 
ATOM   20839 C  C   . LYS   B 1 852  ? 90.09600   76.62500  19.04600  1.000 59.35371  ?  850  LYS   B C   1 
ATOM   20840 O  O   . LYS   B 1 852  ? 90.75800   77.01200  20.01400  1.000 62.82318  ?  850  LYS   B O   1 
ATOM   20841 C  CB  . LYS   B 1 852  ? 87.61400   76.78100  19.37800  1.000 79.71013  ?  850  LYS   B CB  1 
ATOM   20842 C  CG  . LYS   B 1 852  ? 87.41700   77.74100  18.21400  1.000 66.82298  ?  850  LYS   B CG  1 
ATOM   20843 C  CD  . LYS   B 1 852  ? 85.94300   78.03100  17.98100  1.000 63.15341  ?  850  LYS   B CD  1 
ATOM   20844 C  CE  . LYS   B 1 852  ? 85.23300   78.38700  19.27700  1.000 58.88241  ?  850  LYS   B CE  1 
ATOM   20845 N  NZ  . LYS   B 1 852  ? 83.76700   78.54900  19.07800  1.000 71.86658  ?  850  LYS   B NZ  1 
ATOM   20846 N  N   . ARG   B 1 853  ? 90.44400   76.86100  17.78400  1.000 71.56464  ?  851  ARG   B N   1 
ATOM   20847 C  CA  . ARG   B 1 853  ? 91.64900   77.59400  17.41700  1.000 73.27223  ?  851  ARG   B CA  1 
ATOM   20848 C  C   . ARG   B 1 853  ? 91.28900   78.60700  16.34100  1.000 65.13898  ?  851  ARG   B C   1 
ATOM   20849 O  O   . ARG   B 1 853  ? 90.82300   78.22700  15.26200  1.000 68.77899  ?  851  ARG   B O   1 
ATOM   20850 C  CB  . ARG   B 1 853  ? 92.74000   76.63700  16.92300  1.000 67.92868  ?  851  ARG   B CB  1 
ATOM   20851 C  CG  . ARG   B 1 853  ? 94.15500   77.17800  17.04100  1.000 70.47458  ?  851  ARG   B CG  1 
ATOM   20852 C  CD  . ARG   B 1 853  ? 95.18200   76.07400  16.83300  1.000 72.17411  ?  851  ARG   B CD  1 
ATOM   20853 N  NE  . ARG   B 1 853  ? 95.07600   75.03300  17.84900  1.000 71.21324  ?  851  ARG   B NE  1 
ATOM   20854 C  CZ  . ARG   B 1 853  ? 95.72000   73.87500  17.80300  1.000 64.34978  ?  851  ARG   B CZ  1 
ATOM   20855 N  NH1 . ARG   B 1 853  ? 96.53400   73.57500  16.80400  1.000 58.89769  ?  851  ARG   B NH1 1 
ATOM   20856 N  NH2 . ARG   B 1 853  ? 95.53800   72.99300  18.78300  1.000 47.17590  ?  851  ARG   B NH2 1 
ATOM   20857 N  N   . ILE   B 1 854  ? 91.49500   79.88500  16.63000  1.000 57.16888  ?  852  ILE   B N   1 
ATOM   20858 C  CA  . ILE   B 1 854  ? 91.18600   80.94900  15.68200  1.000 55.26972  ?  852  ILE   B CA  1 
ATOM   20859 C  C   . ILE   B 1 854  ? 92.44500   81.30300  14.90300  1.000 53.93839  ?  852  ILE   B C   1 
ATOM   20860 O  O   . ILE   B 1 854  ? 93.55500   81.29700  15.44700  1.000 51.74468  ?  852  ILE   B O   1 
ATOM   20861 C  CB  . ILE   B 1 854  ? 90.60400   82.17900  16.40600  1.000 59.16900  ?  852  ILE   B CB  1 
ATOM   20862 C  CG1 . ILE   B 1 854  ? 89.71300   81.74000  17.57100  1.000 58.18806  ?  852  ILE   B CG1 1 
ATOM   20863 C  CG2 . ILE   B 1 854  ? 89.82100   83.05700  15.43400  1.000 59.42543  ?  852  ILE   B CG2 1 
ATOM   20864 C  CD1 . ILE   B 1 854  ? 88.34900   81.22900  17.15200  1.000 59.09053  ?  852  ILE   B CD1 1 
ATOM   20865 N  N   . VAL   B 1 855  ? 92.27100   81.60700  13.62100  1.000 57.38726  ?  853  VAL   B N   1 
ATOM   20866 C  CA  . VAL   B 1 855  ? 93.37700   81.89200  12.70900  1.000 52.51403  ?  853  VAL   B CA  1 
ATOM   20867 C  C   . VAL   B 1 855  ? 93.20600   83.31500  12.18500  1.000 76.34776  ?  853  VAL   B C   1 
ATOM   20868 O  O   . VAL   B 1 855  ? 92.07700   83.72800  11.88600  1.000 71.40893  ?  853  VAL   B O   1 
ATOM   20869 C  CB  . VAL   B 1 855  ? 93.42000   80.86100  11.56800  1.000 58.02286  ?  853  VAL   B CB  1 
ATOM   20870 C  CG1 . VAL   B 1 855  ? 94.51900   81.18400  10.57000  1.000 58.43011  ?  853  VAL   B CG1 1 
ATOM   20871 C  CG2 . VAL   B 1 855  ? 93.60700   79.46300  12.13100  1.000 56.50656  ?  853  VAL   B CG2 1 
ATOM   20872 N  N   . PRO   B 1 856  ? 94.28000   84.10500  12.07500  1.000 73.50598  ?  854  PRO   B N   1 
ATOM   20873 C  CA  . PRO   B 1 856  ? 94.11900   85.49200  11.61000  1.000 55.78625  ?  854  PRO   B CA  1 
ATOM   20874 C  C   . PRO   B 1 856  ? 93.82700   85.62100  10.12400  1.000 64.04685  ?  854  PRO   B C   1 
ATOM   20875 O  O   . PRO   B 1 856  ? 93.34600   86.68000  9.70100   1.000 59.29629  ?  854  PRO   B O   1 
ATOM   20876 C  CB  . PRO   B 1 856  ? 95.46400   86.13700  11.96600  1.000 51.87438  ?  854  PRO   B CB  1 
ATOM   20877 C  CG  . PRO   B 1 856  ? 96.42600   85.00000  11.94300  1.000 64.32850  ?  854  PRO   B CG  1 
ATOM   20878 C  CD  . PRO   B 1 856  ? 95.66500   83.82800  12.49500  1.000 58.89328  ?  854  PRO   B CD  1 
ATOM   20879 N  N   . ARG   B 1 857  ? 94.09900   84.59700  9.31800   1.000 66.06454  ?  855  ARG   B N   1 
ATOM   20880 C  CA  . ARG   B 1 857  ? 93.86700   84.69800  7.88400   1.000 78.54846  ?  855  ARG   B CA  1 
ATOM   20881 C  C   . ARG   B 1 857  ? 93.66700   83.30300  7.30600   1.000 79.96147  ?  855  ARG   B C   1 
ATOM   20882 O  O   . ARG   B 1 857  ? 94.38300   82.36800  7.67000   1.000 77.04437  ?  855  ARG   B O   1 
ATOM   20883 C  CB  . ARG   B 1 857  ? 95.03300   85.41300  7.18800   1.000 50.04276  ?  855  ARG   B CB  1 
ATOM   20884 N  N   . ALA   B 1 858  ? 92.68900   83.17200  6.40600   1.000 61.52117  ?  856  ALA   B N   1 
ATOM   20885 C  CA  . ALA   B 1 858  ? 92.37400   81.90200  5.76300   1.000 57.52379  ?  856  ALA   B CA  1 
ATOM   20886 C  C   . ALA   B 1 858  ? 92.08700   82.13200  4.28600   1.000 63.78505  ?  856  ALA   B C   1 
ATOM   20887 O  O   . ALA   B 1 858  ? 91.47500   83.13700  3.91500   1.000 78.68545  ?  856  ALA   B O   1 
ATOM   20888 C  CB  . ALA   B 1 858  ? 91.17400   81.21900  6.43000   1.000 57.38958  ?  856  ALA   B CB  1 
ATOM   20889 N  N   . GLU   B 1 859  ? 92.52100   81.19200  3.44700   1.000 54.61174  ?  857  GLU   B N   1 
ATOM   20890 C  CA  . GLU   B 1 859  ? 92.41500   81.32100  1.99700   1.000 59.84307  ?  857  GLU   B CA  1 
ATOM   20891 C  C   . GLU   B 1 859  ? 91.22000   80.51800  1.49300   1.000 64.49796  ?  857  GLU   B C   1 
ATOM   20892 O  O   . GLU   B 1 859  ? 91.15900   79.29900  1.68400   1.000 65.97382  ?  857  GLU   B O   1 
ATOM   20893 C  CB  . GLU   B 1 859  ? 93.70000   80.85600  1.31400   1.000 55.71539  ?  857  GLU   B CB  1 
ATOM   20894 C  CG  . GLU   B 1 859  ? 93.86700   81.37900  -0.10200  1.000 77.04699  ?  857  GLU   B CG  1 
ATOM   20895 C  CD  . GLU   B 1 859  ? 95.04800   80.75700  -0.82100  1.000 101.46855 ?  857  GLU   B CD  1 
ATOM   20896 O  OE1 . GLU   B 1 859  ? 95.72200   79.89100  -0.22400  1.000 97.23255  ?  857  GLU   B OE1 1 
ATOM   20897 O  OE2 . GLU   B 1 859  ? 95.30400   81.13600  -1.98300  1.000 117.18763 -1 857  GLU   B OE2 1 
ATOM   20898 N  N   . LEU   B 1 860  ? 90.28900   81.20100  0.83400   1.000 55.51985  ?  858  LEU   B N   1 
ATOM   20899 C  CA  . LEU   B 1 860  ? 89.05500   80.58500  0.37200   1.000 49.11706  ?  858  LEU   B CA  1 
ATOM   20900 C  C   . LEU   B 1 860  ? 89.26800   79.85100  -0.94700  1.000 48.73133  ?  858  LEU   B C   1 
ATOM   20901 O  O   . LEU   B 1 860  ? 90.04700   80.27900  -1.80300  1.000 57.97854  ?  858  LEU   B O   1 
ATOM   20902 C  CB  . LEU   B 1 860  ? 87.97200   81.65300  0.20800   1.000 48.94795  ?  858  LEU   B CB  1 
ATOM   20903 C  CG  . LEU   B 1 860  ? 86.56800   81.23800  -0.22600  1.000 40.57315  ?  858  LEU   B CG  1 
ATOM   20904 C  CD1 . LEU   B 1 860  ? 86.02200   80.13500  0.66400   1.000 45.25869  ?  858  LEU   B CD1 1 
ATOM   20905 C  CD2 . LEU   B 1 860  ? 85.66000   82.45100  -0.19200  1.000 38.98026  ?  858  LEU   B CD2 1 
ATOM   20906 N  N   . SER   B 1 861  ? 88.56300   78.73300  -1.10800  1.000 38.17245  ?  859  SER   B N   1 
ATOM   20907 C  CA  . SER   B 1 861  ? 88.60800   77.95600  -2.34300  1.000 47.41132  ?  859  SER   B CA  1 
ATOM   20908 C  C   . SER   B 1 861  ? 87.48800   78.43600  -3.26300  1.000 54.86918  ?  859  SER   B C   1 
ATOM   20909 O  O   . SER   B 1 861  ? 86.30500   78.22800  -2.97400  1.000 63.90307  ?  859  SER   B O   1 
ATOM   20910 C  CB  . SER   B 1 861  ? 88.48400   76.46400  -2.04900  1.000 44.27564  ?  859  SER   B CB  1 
ATOM   20911 O  OG  . SER   B 1 861  ? 88.59000   75.70000  -3.23900  1.000 50.43020  ?  859  SER   B OG  1 
ATOM   20912 N  N   . PHE   B 1 862  ? 87.85900   79.07600  -4.36900  1.000 41.50455  ?  860  PHE   B N   1 
ATOM   20913 C  CA  . PHE   B 1 862  ? 86.90500   79.64800  -5.31700  1.000 37.71959  ?  860  PHE   B CA  1 
ATOM   20914 C  C   . PHE   B 1 862  ? 87.18800   79.05700  -6.69400  1.000 44.26326  ?  860  PHE   B C   1 
ATOM   20915 O  O   . PHE   B 1 862  ? 88.05600   79.54700  -7.42300  1.000 56.79380  ?  860  PHE   B O   1 
ATOM   20916 C  CB  . PHE   B 1 862  ? 87.00000   81.16900  -5.33200  1.000 35.26095  ?  860  PHE   B CB  1 
ATOM   20917 C  CG  . PHE   B 1 862  ? 85.80300   81.84900  -5.92700  1.000 49.92032  ?  860  PHE   B CG  1 
ATOM   20918 C  CD1 . PHE   B 1 862  ? 84.61000   81.92100  -5.22600  1.000 48.20898  ?  860  PHE   B CD1 1 
ATOM   20919 C  CD2 . PHE   B 1 862  ? 85.87100   82.42100  -7.18500  1.000 45.57684  ?  860  PHE   B CD2 1 
ATOM   20920 C  CE1 . PHE   B 1 862  ? 83.51000   82.55100  -5.77000  1.000 40.14195  ?  860  PHE   B CE1 1 
ATOM   20921 C  CE2 . PHE   B 1 862  ? 84.77500   83.05100  -7.73400  1.000 47.49909  ?  860  PHE   B CE2 1 
ATOM   20922 C  CZ  . PHE   B 1 862  ? 83.59300   83.11600  -7.02600  1.000 57.52581  ?  860  PHE   B CZ  1 
ATOM   20923 N  N   . VAL   B 1 863  ? 86.45000   78.01300  -7.04900  1.000 42.66815  ?  861  VAL   B N   1 
ATOM   20924 C  CA  . VAL   B 1 863  ? 86.64400   77.30900  -8.30900  1.000 34.87183  ?  861  VAL   B CA  1 
ATOM   20925 C  C   . VAL   B 1 863  ? 85.70000   77.88000  -9.35700  1.000 49.26956  ?  861  VAL   B C   1 
ATOM   20926 O  O   . VAL   B 1 863  ? 84.48600   77.96000  -9.13500  1.000 61.62932  ?  861  VAL   B O   1 
ATOM   20927 C  CB  . VAL   B 1 863  ? 86.41400   75.80100  -8.12900  1.000 33.28322  ?  861  VAL   B CB  1 
ATOM   20928 C  CG1 . VAL   B 1 863  ? 86.59200   75.07400  -9.45100  1.000 42.31486  ?  861  VAL   B CG1 1 
ATOM   20929 C  CG2 . VAL   B 1 863  ? 87.36100   75.25800  -7.07800  1.000 56.48157  ?  861  VAL   B CG2 1 
ATOM   20930 N  N   . ARG   B 1 864  ? 86.25300   78.27100  -10.50100 1.000 50.76517  ?  862  ARG   B N   1 
ATOM   20931 C  CA  . ARG   B 1 864  ? 85.46800   78.75300  -11.63000 1.000 46.46779  ?  862  ARG   B CA  1 
ATOM   20932 C  C   . ARG   B 1 864  ? 85.30600   77.63100  -12.64800 1.000 50.20600  ?  862  ARG   B C   1 
ATOM   20933 O  O   . ARG   B 1 864  ? 86.28000   76.95100  -12.98900 1.000 61.28124  ?  862  ARG   B O   1 
ATOM   20934 C  CB  . ARG   B 1 864  ? 86.13000   79.97100  -12.27800 1.000 43.13894  ?  862  ARG   B CB  1 
ATOM   20935 C  CG  . ARG   B 1 864  ? 85.96500   81.25700  -11.48400 1.000 50.05484  ?  862  ARG   B CG  1 
ATOM   20936 C  CD  . ARG   B 1 864  ? 86.82700   82.37400  -12.04800 1.000 54.10005  ?  862  ARG   B CD  1 
ATOM   20937 N  NE  . ARG   B 1 864  ? 87.40900   83.19200  -10.99100 1.000 65.27820  ?  862  ARG   B NE  1 
ATOM   20938 C  CZ  . ARG   B 1 864  ? 88.48200   82.85400  -10.28800 1.000 66.20368  ?  862  ARG   B CZ  1 
ATOM   20939 N  NH1 . ARG   B 1 864  ? 89.12800   81.72100  -10.51400 1.000 66.85181  ?  862  ARG   B NH1 1 
ATOM   20940 N  NH2 . ARG   B 1 864  ? 88.91700   83.67200  -9.33400  1.000 64.60081  ?  862  ARG   B NH2 1 
ATOM   20941 N  N   . GLN   B 1 865  ? 84.07700   77.43700  -13.12500 1.000 43.16086  ?  863  GLN   B N   1 
ATOM   20942 C  CA  . GLN   B 1 865  ? 83.77100   76.36800  -14.06400 1.000 31.76082  ?  863  GLN   B CA  1 
ATOM   20943 C  C   . GLN   B 1 865  ? 82.76300   76.85600  -15.09300 1.000 44.47809  ?  863  GLN   B C   1 
ATOM   20944 O  O   . GLN   B 1 865  ? 81.90300   77.69000  -14.80000 1.000 45.02941  ?  863  GLN   B O   1 
ATOM   20945 C  CB  . GLN   B 1 865  ? 83.21100   75.12800  -13.35700 1.000 27.04428  ?  863  GLN   B CB  1 
ATOM   20946 C  CG  . GLN   B 1 865  ? 84.23700   74.32200  -12.58600 1.000 25.13747  ?  863  GLN   B CG  1 
ATOM   20947 C  CD  . GLN   B 1 865  ? 83.60100   73.22000  -11.76500 1.000 31.96557  ?  863  GLN   B CD  1 
ATOM   20948 O  OE1 . GLN   B 1 865  ? 82.91100   73.48500  -10.77900 1.000 35.35188  ?  863  GLN   B OE1 1 
ATOM   20949 N  NE2 . GLN   B 1 865  ? 83.82500   71.97400  -12.16800 1.000 28.52349  ?  863  GLN   B NE2 1 
ATOM   20950 N  N   . THR   B 1 866  ? 82.88100   76.32100  -16.30200 1.000 47.03182  ?  864  THR   B N   1 
ATOM   20951 C  CA  . THR   B 1 866  ? 81.94000   76.58500  -17.38000 1.000 39.54737  ?  864  THR   B CA  1 
ATOM   20952 C  C   . THR   B 1 866  ? 81.05500   75.35900  -17.55700 1.000 47.58833  ?  864  THR   B C   1 
ATOM   20953 O  O   . THR   B 1 866  ? 81.56200   74.24100  -17.69900 1.000 60.32422  ?  864  THR   B O   1 
ATOM   20954 C  CB  . THR   B 1 866  ? 82.67700   76.91000  -18.68200 1.000 41.52037  ?  864  THR   B CB  1 
ATOM   20955 O  OG1 . THR   B 1 866  ? 83.07700   78.28700  -18.67900 1.000 53.80623  ?  864  THR   B OG1 1 
ATOM   20956 C  CG2 . THR   B 1 866  ? 81.78700   76.64400  -19.89000 1.000 46.01306  ?  864  THR   B CG2 1 
ATOM   20957 N  N   . GLY   B 1 867  ? 79.73700   75.56500  -17.53100 1.000 44.85508  ?  865  GLY   B N   1 
ATOM   20958 C  CA  . GLY   B 1 867  ? 78.79900   74.46700  -17.62800 1.000 42.69790  ?  865  GLY   B CA  1 
ATOM   20959 C  C   . GLY   B 1 867  ? 77.60200   74.82900  -18.48500 1.000 37.90934  ?  865  GLY   B C   1 
ATOM   20960 O  O   . GLY   B 1 867  ? 77.50900   75.93400  -19.02100 1.000 52.78688  ?  865  GLY   B O   1 
ATOM   20961 N  N   . GLU   B 1 868  ? 76.69300   73.86300  -18.61100 1.000 47.53914  ?  866  GLU   B N   1 
ATOM   20962 C  CA  . GLU   B 1 868  ? 75.42000   74.03700  -19.29600 1.000 37.70340  ?  866  GLU   B CA  1 
ATOM   20963 C  C   . GLU   B 1 868  ? 74.29900   73.57500  -18.37600 1.000 40.05876  ?  866  GLU   B C   1 
ATOM   20964 O  O   . GLU   B 1 868  ? 74.53900   73.02300  -17.29800 1.000 39.63598  ?  866  GLU   B O   1 
ATOM   20965 C  CB  . GLU   B 1 868  ? 75.37700   73.26600  -20.62200 1.000 32.62857  ?  866  GLU   B CB  1 
ATOM   20966 C  CG  . GLU   B 1 868  ? 75.27400   71.75700  -20.47600 1.000 33.20504  ?  866  GLU   B CG  1 
ATOM   20967 C  CD  . GLU   B 1 868  ? 75.25600   71.05000  -21.81800 1.000 55.70482  ?  866  GLU   B CD  1 
ATOM   20968 O  OE1 . GLU   B 1 868  ? 74.66100   71.59900  -22.77000 1.000 59.68866  ?  866  GLU   B OE1 1 
ATOM   20969 O  OE2 . GLU   B 1 868  ? 75.84700   69.95400  -21.92700 1.000 62.17760  -1 866  GLU   B OE2 1 
ATOM   20970 N  N   . GLU   B 1 869  ? 73.06000   73.79000  -18.82600 1.000 50.14087  ?  867  GLU   B N   1 
ATOM   20971 C  CA  . GLU   B 1 869  ? 71.90000   73.57000  -17.96500 1.000 34.04918  ?  867  GLU   B CA  1 
ATOM   20972 C  C   . GLU   B 1 869  ? 71.84900   72.13900  -17.44600 1.000 30.97428  ?  867  GLU   B C   1 
ATOM   20973 O  O   . GLU   B 1 869  ? 71.65400   71.90800  -16.24700 1.000 49.95605  ?  867  GLU   B O   1 
ATOM   20974 C  CB  . GLU   B 1 869  ? 70.61800   73.91100  -18.72000 1.000 33.58488  ?  867  GLU   B CB  1 
ATOM   20975 C  CG  . GLU   B 1 869  ? 69.50600   74.40800  -17.82200 1.000 34.90994  ?  867  GLU   B CG  1 
ATOM   20976 C  CD  . GLU   B 1 869  ? 69.91900   75.61500  -17.00400 1.000 58.76112  ?  867  GLU   B CD  1 
ATOM   20977 O  OE1 . GLU   B 1 869  ? 70.58900   76.51700  -17.55600 1.000 50.89639  ?  867  GLU   B OE1 1 
ATOM   20978 O  OE2 . GLU   B 1 869  ? 69.57500   75.65900  -15.80500 1.000 76.03279  -1 867  GLU   B OE2 1 
ATOM   20979 N  N   . GLU   B 1 870  ? 72.02700   71.16300  -18.33100 1.000 30.90997  ?  868  GLU   B N   1 
ATOM   20980 C  CA  . GLU   B 1 870  ? 71.91700   69.76000  -17.96300 1.000 33.53960  ?  868  GLU   B CA  1 
ATOM   20981 C  C   . GLU   B 1 870  ? 73.21400   69.19400  -17.40000 1.000 44.61730  ?  868  GLU   B C   1 
ATOM   20982 O  O   . GLU   B 1 870  ? 73.41400   67.97300  -17.43400 1.000 43.52903  ?  868  GLU   B O   1 
ATOM   20983 C  CB  . GLU   B 1 870  ? 71.46000   68.94200  -19.16900 1.000 38.46036  ?  868  GLU   B CB  1 
ATOM   20984 C  CG  . GLU   B 1 870  ? 70.32700   69.59000  -19.93300 1.000 54.24170  ?  868  GLU   B CG  1 
ATOM   20985 C  CD  . GLU   B 1 870  ? 69.61900   68.61400  -20.84000 1.000 55.47658  ?  868  GLU   B CD  1 
ATOM   20986 O  OE1 . GLU   B 1 870  ? 70.09900   67.46600  -20.96200 1.000 56.56219  ?  868  GLU   B OE1 1 
ATOM   20987 O  OE2 . GLU   B 1 870  ? 68.58700   68.99500  -21.43100 1.000 47.43858  -1 868  GLU   B OE2 1 
ATOM   20988 N  N   . SER   B 1 871  ? 74.09800   70.05200  -16.88500 1.000 40.16449  ?  869  SER   B N   1 
ATOM   20989 C  CA  . SER   B 1 871  ? 75.34200   69.60100  -16.27100 1.000 37.71582  ?  869  SER   B CA  1 
ATOM   20990 C  C   . SER   B 1 871  ? 75.68300   70.29900  -14.96300 1.000 33.72932  ?  869  SER   B C   1 
ATOM   20991 O  O   . SER   B 1 871  ? 76.64700   69.88300  -14.31100 1.000 37.11812  ?  869  SER   B O   1 
ATOM   20992 C  CB  . SER   B 1 871  ? 76.51500   69.78600  -17.24400 1.000 32.39188  ?  869  SER   B CB  1 
ATOM   20993 O  OG  . SER   B 1 871  ? 76.95800   71.13300  -17.24600 1.000 31.45922  ?  869  SER   B OG  1 
ATOM   20994 N  N   . VAL   B 1 872  ? 74.94100   71.33200  -14.55100 1.000 28.05390  ?  870  VAL   B N   1 
ATOM   20995 C  CA  . VAL   B 1 872  ? 75.29300   72.09100  -13.35300 1.000 32.86713  ?  870  VAL   B CA  1 
ATOM   20996 C  C   . VAL   B 1 872  ? 75.28100   71.19500  -12.12000 1.000 36.60021  ?  870  VAL   B C   1 
ATOM   20997 O  O   . VAL   B 1 872  ? 76.13800   71.31800  -11.23600 1.000 37.08749  ?  870  VAL   B O   1 
ATOM   20998 C  CB  . VAL   B 1 872  ? 74.34300   73.29300  -13.19300 1.000 26.66371  ?  870  VAL   B CB  1 
ATOM   20999 C  CG1 . VAL   B 1 872  ? 74.58400   74.00800  -11.86700 1.000 27.30189  ?  870  VAL   B CG1 1 
ATOM   21000 C  CG2 . VAL   B 1 872  ? 74.51300   74.25300  -14.35400 1.000 23.18947  ?  870  VAL   B CG2 1 
ATOM   21001 N  N   . GLN   B 1 873  ? 74.31700   70.27700  -12.04200 1.000 34.06743  ?  871  GLN   B N   1 
ATOM   21002 C  CA  . GLN   B 1 873  ? 74.23500   69.39900  -10.88000 1.000 33.99536  ?  871  GLN   B CA  1 
ATOM   21003 C  C   . GLN   B 1 873  ? 75.40400   68.42500  -10.83600 1.000 34.18701  ?  871  GLN   B C   1 
ATOM   21004 O  O   . GLN   B 1 873  ? 75.94900   68.15200  -9.76000  1.000 39.41351  ?  871  GLN   B O   1 
ATOM   21005 C  CB  . GLN   B 1 873  ? 72.90700   68.64600  -10.88600 1.000 50.41146  ?  871  GLN   B CB  1 
ATOM   21006 C  CG  . GLN   B 1 873  ? 71.69700   69.54400  -11.06100 1.000 51.72628  ?  871  GLN   B CG  1 
ATOM   21007 C  CD  . GLN   B 1 873  ? 70.39600   68.81800  -10.79900 1.000 52.85812  ?  871  GLN   B CD  1 
ATOM   21008 O  OE1 . GLN   B 1 873  ? 69.71000   68.40400  -11.73100 1.000 53.75424  ?  871  GLN   B OE1 1 
ATOM   21009 N  NE2 . GLN   B 1 873  ? 70.05000   68.65800  -9.52700  1.000 56.34968  ?  871  GLN   B NE2 1 
ATOM   21010 N  N   . SER   B 1 874  ? 75.80500   67.88900  -11.99200 1.000 33.23339  ?  872  SER   B N   1 
ATOM   21011 C  CA  . SER   B 1 874  ? 76.92100   66.95000  -12.01700 1.000 26.97279  ?  872  SER   B CA  1 
ATOM   21012 C  C   . SER   B 1 874  ? 78.21000   67.62000  -11.56300 1.000 42.48535  ?  872  SER   B C   1 
ATOM   21013 O  O   . SER   B 1 874  ? 79.01100   67.01800  -10.84000 1.000 41.76315  ?  872  SER   B O   1 
ATOM   21014 C  CB  . SER   B 1 874  ? 77.08600   66.36200  -13.41700 1.000 27.51676  ?  872  SER   B CB  1 
ATOM   21015 O  OG  . SER   B 1 874  ? 77.73200   65.10000  -13.36200 1.000 54.84517  ?  872  SER   B OG  1 
ATOM   21016 N  N   . LEU   B 1 875  ? 78.42100   68.87200  -11.97300 1.000 38.37154  ?  873  LEU   B N   1 
ATOM   21017 C  CA  . LEU   B 1 875  ? 79.59700   69.61000  -11.52600 1.000 30.02609  ?  873  LEU   B CA  1 
ATOM   21018 C  C   . LEU   B 1 875  ? 79.54600   69.87900  -10.02800 1.000 42.07903  ?  873  LEU   B C   1 
ATOM   21019 O  O   . LEU   B 1 875  ? 80.55000   69.71200  -9.32700  1.000 59.90435  ?  873  LEU   B O   1 
ATOM   21020 C  CB  . LEU   B 1 875  ? 79.71300   70.92700  -12.29400 1.000 36.67963  ?  873  LEU   B CB  1 
ATOM   21021 C  CG  . LEU   B 1 875  ? 79.95700   70.84700  -13.80200 1.000 40.82433  ?  873  LEU   B CG  1 
ATOM   21022 C  CD1 . LEU   B 1 875  ? 79.80900   72.22300  -14.43100 1.000 28.43470  ?  873  LEU   B CD1 1 
ATOM   21023 C  CD2 . LEU   B 1 875  ? 81.32600   70.25700  -14.10400 1.000 38.98512  ?  873  LEU   B CD2 1 
ATOM   21024 N  N   . LEU   B 1 876  ? 78.38100   70.28900  -9.52100  1.000 42.37770  ?  874  LEU   B N   1 
ATOM   21025 C  CA  . LEU   B 1 876  ? 78.27500   70.68200  -8.11900  1.000 43.60146  ?  874  LEU   B CA  1 
ATOM   21026 C  C   . LEU   B 1 876  ? 78.44400   69.48900  -7.18300  1.000 41.20279  ?  874  LEU   B C   1 
ATOM   21027 O  O   . LEU   B 1 876  ? 79.04700   69.61700  -6.11200  1.000 41.76073  ?  874  LEU   B O   1 
ATOM   21028 C  CB  . LEU   B 1 876  ? 76.93500   71.37600  -7.87600  1.000 25.37405  ?  874  LEU   B CB  1 
ATOM   21029 C  CG  . LEU   B 1 876  ? 76.68200   71.89300  -6.45900  1.000 42.84271  ?  874  LEU   B CG  1 
ATOM   21030 C  CD1 . LEU   B 1 876  ? 77.87900   72.69000  -5.94100  1.000 46.63660  ?  874  LEU   B CD1 1 
ATOM   21031 C  CD2 . LEU   B 1 876  ? 75.40400   72.71900  -6.41100  1.000 46.47380  ?  874  LEU   B CD2 1 
ATOM   21032 N  N   . ALA   B 1 877  ? 77.91700   68.32200  -7.56600  1.000 41.68308  ?  875  ALA   B N   1 
ATOM   21033 C  CA  . ALA   B 1 877  ? 78.00500   67.15000  -6.69900  1.000 41.03878  ?  875  ALA   B CA  1 
ATOM   21034 C  C   . ALA   B 1 877  ? 79.45200   66.73200  -6.48000  1.000 41.20291  ?  875  ALA   B C   1 
ATOM   21035 O  O   . ALA   B 1 877  ? 79.82400   66.30000  -5.38200  1.000 46.76481  ?  875  ALA   B O   1 
ATOM   21036 C  CB  . ALA   B 1 877  ? 77.20100   65.99300  -7.29200  1.000 35.74490  ?  875  ALA   B CB  1 
ATOM   21037 N  N   . GLU   B 1 878  ? 80.28400   66.85700  -7.51100  1.000 40.37791  ?  876  GLU   B N   1 
ATOM   21038 C  CA  . GLU   B 1 878  ? 81.68500   66.48300  -7.39100  1.000 51.87809  ?  876  GLU   B CA  1 
ATOM   21039 C  C   . GLU   B 1 878  ? 82.48100   67.44200  -6.51600  1.000 45.67360  ?  876  GLU   B C   1 
ATOM   21040 O  O   . GLU   B 1 878  ? 83.62800   67.13600  -6.17800  1.000 65.61505  ?  876  GLU   B O   1 
ATOM   21041 C  CB  . GLU   B 1 878  ? 82.30700   66.38900  -8.78400  1.000 39.53690  ?  876  GLU   B CB  1 
ATOM   21042 C  CG  . GLU   B 1 878  ? 81.50400   65.50400  -9.72300  1.000 62.38515  ?  876  GLU   B CG  1 
ATOM   21043 C  CD  . GLU   B 1 878  ? 82.31700   64.98600  -10.88700 1.000 84.80307  ?  876  GLU   B CD  1 
ATOM   21044 O  OE1 . GLU   B 1 878  ? 82.36300   65.67000  -11.93100 1.000 90.64313  ?  876  GLU   B OE1 1 
ATOM   21045 O  OE2 . GLU   B 1 878  ? 82.90200   63.88900  -10.76100 1.000 94.63094  -1 876  GLU   B OE2 1 
ATOM   21046 N  N   . GLN   B 1 879  ? 81.90600   68.58100  -6.13500  1.000 33.50796  ?  877  GLN   B N   1 
ATOM   21047 C  CA  . GLN   B 1 879  ? 82.58500   69.53400  -5.27000  1.000 40.59349  ?  877  GLN   B CA  1 
ATOM   21048 C  C   . GLN   B 1 879  ? 82.13000   69.45000  -3.81900  1.000 47.41557  ?  877  GLN   B C   1 
ATOM   21049 O  O   . GLN   B 1 879  ? 82.73900   70.09200  -2.95600  1.000 60.18408  ?  877  GLN   B O   1 
ATOM   21050 C  CB  . GLN   B 1 879  ? 82.38000   70.96000  -5.79400  1.000 40.98090  ?  877  GLN   B CB  1 
ATOM   21051 C  CG  . GLN   B 1 879  ? 82.76500   71.13700  -7.25400  1.000 40.44566  ?  877  GLN   B CG  1 
ATOM   21052 C  CD  . GLN   B 1 879  ? 83.96600   72.04000  -7.43500  1.000 53.95921  ?  877  GLN   B CD  1 
ATOM   21053 O  OE1 . GLN   B 1 879  ? 85.09800   71.64500  -7.16100  1.000 67.70211  ?  877  GLN   B OE1 1 
ATOM   21054 N  NE2 . GLN   B 1 879  ? 83.72600   73.25900  -7.90400  1.000 48.24064  ?  877  GLN   B NE2 1 
ATOM   21055 N  N   . ILE   B 1 880  ? 81.08100   68.68100  -3.53100  1.000 39.92861  ?  878  ILE   B N   1 
ATOM   21056 C  CA  . ILE   B 1 880  ? 80.63800   68.46100  -2.16100  1.000 40.74059  ?  878  ILE   B CA  1 
ATOM   21057 C  C   . ILE   B 1 880  ? 81.49100   67.35200  -1.56200  1.000 40.58834  ?  878  ILE   B C   1 
ATOM   21058 O  O   . ILE   B 1 880  ? 81.20400   66.16300  -1.73700  1.000 49.05212  ?  878  ILE   B O   1 
ATOM   21059 C  CB  . ILE   B 1 880  ? 79.13900   68.11700  -2.10100  1.000 47.43449  ?  878  ILE   B CB  1 
ATOM   21060 C  CG1 . ILE   B 1 880  ? 78.31500   69.22700  -2.75900  1.000 48.69949  ?  878  ILE   B CG1 1 
ATOM   21061 C  CG2 . ILE   B 1 880  ? 78.69800   67.90600  -0.66300  1.000 44.83847  ?  878  ILE   B CG2 1 
ATOM   21062 C  CD1 . ILE   B 1 880  ? 76.88800   68.83300  -3.07100  1.000 33.23017  ?  878  ILE   B CD1 1 
ATOM   21063 N  N   . LYS   B 1 881  ? 82.55100   67.73600  -0.86600  1.000 56.37205  ?  879  LYS   B N   1 
ATOM   21064 C  CA  . LYS   B 1 881  ? 83.54700   66.82100  -0.33800  1.000 45.41436  ?  879  LYS   B CA  1 
ATOM   21065 C  C   . LYS   B 1 881  ? 83.59100   66.90900  1.18300   1.000 45.17005  ?  879  LYS   B C   1 
ATOM   21066 O  O   . LYS   B 1 881  ? 83.09600   67.87900  1.77000   1.000 47.04907  ?  879  LYS   B O   1 
ATOM   21067 C  CB  . LYS   B 1 881  ? 84.92800   67.14300  -0.92900  1.000 49.82443  ?  879  LYS   B CB  1 
ATOM   21068 C  CG  . LYS   B 1 881  ? 85.07500   66.75300  -2.39300  1.000 41.89946  ?  879  LYS   B CG  1 
ATOM   21069 C  CD  . LYS   B 1 881  ? 85.76900   67.84600  -3.18900  1.000 54.38237  ?  879  LYS   B CD  1 
ATOM   21070 C  CE  . LYS   B 1 881  ? 86.45600   67.28500  -4.42500  1.000 66.52481  ?  879  LYS   B CE  1 
ATOM   21071 N  NZ  . LYS   B 1 881  ? 86.94800   68.36300  -5.33100  1.000 77.01803  ?  879  LYS   B NZ  1 
ATOM   21072 N  N   . PRO   B 1 882  ? 84.16200   65.90700  1.85500   1.000 55.29425  ?  880  PRO   B N   1 
ATOM   21073 C  CA  . PRO   B 1 882  ? 84.24600   65.96000  3.31900   1.000 51.31755  ?  880  PRO   B CA  1 
ATOM   21074 C  C   . PRO   B 1 882  ? 85.13600   67.09600  3.79700   1.000 58.45782  ?  880  PRO   B C   1 
ATOM   21075 O  O   . PRO   B 1 882  ? 86.08000   67.51100  3.12000   1.000 58.20044  ?  880  PRO   B O   1 
ATOM   21076 C  CB  . PRO   B 1 882  ? 84.84900   64.60100  3.69400   1.000 40.05831  ?  880  PRO   B CB  1 
ATOM   21077 C  CG  . PRO   B 1 882  ? 84.60100   63.72900  2.52300   1.000 47.42582  ?  880  PRO   B CG  1 
ATOM   21078 C  CD  . PRO   B 1 882  ? 84.65400   64.62300  1.32800   1.000 49.76532  ?  880  PRO   B CD  1 
ATOM   21079 N  N   . PHE   B 1 883  ? 84.83400   67.58200  4.99600   1.000 56.14337  ?  881  PHE   B N   1 
ATOM   21080 C  CA  . PHE   B 1 883  ? 85.54600   68.69900  5.59700   1.000 48.42558  ?  881  PHE   B CA  1 
ATOM   21081 C  C   . PHE   B 1 883  ? 86.50000   68.20600  6.67600   1.000 58.02486  ?  881  PHE   B C   1 
ATOM   21082 O  O   . PHE   B 1 883  ? 86.13800   67.37000  7.50900   1.000 62.58105  ?  881  PHE   B O   1 
ATOM   21083 C  CB  . PHE   B 1 883  ? 84.56500   69.70500  6.20300   1.000 60.18164  ?  881  PHE   B CB  1 
ATOM   21084 C  CG  . PHE   B 1 883  ? 84.27700   70.88300  5.31600   1.000 59.72444  ?  881  PHE   B CG  1 
ATOM   21085 C  CD1 . PHE   B 1 883  ? 85.30200   71.71200  4.88800   1.000 61.80050  ?  881  PHE   B CD1 1 
ATOM   21086 C  CD2 . PHE   B 1 883  ? 82.98100   71.16200  4.91300   1.000 50.68062  ?  881  PHE   B CD2 1 
ATOM   21087 C  CE1 . PHE   B 1 883  ? 85.03900   72.79900  4.07100   1.000 59.91118  ?  881  PHE   B CE1 1 
ATOM   21088 C  CE2 . PHE   B 1 883  ? 82.71100   72.24600  4.09700   1.000 47.39541  ?  881  PHE   B CE2 1 
ATOM   21089 C  CZ  . PHE   B 1 883  ? 83.74100   73.06600  3.67500   1.000 59.95740  ?  881  PHE   B CZ  1 
ATOM   21090 N  N   . ASP   B 1 884  ? 87.72200   68.73000  6.65600   1.000 74.67168  ?  882  ASP   B N   1 
ATOM   21091 C  CA  . ASP   B 1 884  ? 88.67200   68.52800  7.74400   1.000 63.17851  ?  882  ASP   B CA  1 
ATOM   21092 C  C   . ASP   B 1 884  ? 88.41400   69.61100  8.78400   1.000 60.98514  ?  882  ASP   B C   1 
ATOM   21093 O  O   . ASP   B 1 884  ? 88.76000   70.77800  8.57200   1.000 62.54501  ?  882  ASP   B O   1 
ATOM   21094 C  CB  . ASP   B 1 884  ? 90.10700   68.58000  7.22800   1.000 68.45664  ?  882  ASP   B CB  1 
ATOM   21095 C  CG  . ASP   B 1 884  ? 91.10700   68.02600  8.22400   1.000 73.89566  ?  882  ASP   B CG  1 
ATOM   21096 O  OD1 . ASP   B 1 884  ? 90.77300   67.93800  9.42600   1.000 58.90205  ?  882  ASP   B OD1 1 
ATOM   21097 O  OD2 . ASP   B 1 884  ? 92.23100   67.67900  7.80300   1.000 59.01750  -1 882  ASP   B OD2 1 
ATOM   21098 N  N   . LEU   B 1 885  ? 87.80300   69.22600  9.90900   1.000 54.61648  ?  883  LEU   B N   1 
ATOM   21099 C  CA  . LEU   B 1 885  ? 87.40600   70.19600  10.92400  1.000 48.16235  ?  883  LEU   B CA  1 
ATOM   21100 C  C   . LEU   B 1 885  ? 88.59000   70.91700  11.55400  1.000 57.30867  ?  883  LEU   B C   1 
ATOM   21101 O  O   . LEU   B 1 885  ? 88.38100   71.88900  12.28800  1.000 62.89556  ?  883  LEU   B O   1 
ATOM   21102 C  CB  . LEU   B 1 885  ? 86.57800   69.51000  12.01500  1.000 40.42107  ?  883  LEU   B CB  1 
ATOM   21103 C  CG  . LEU   B 1 885  ? 85.14000   69.12800  11.64200  1.000 47.31850  ?  883  LEU   B CG  1 
ATOM   21104 C  CD1 . LEU   B 1 885  ? 84.26100   69.01400  12.87800  1.000 51.77017  ?  883  LEU   B CD1 1 
ATOM   21105 C  CD2 . LEU   B 1 885  ? 84.54000   70.12500  10.66000  1.000 63.86840  ?  883  LEU   B CD2 1 
ATOM   21106 N  N   . ALA   B 1 886  ? 89.81800   70.47500  11.28600  1.000 62.06738  ?  884  ALA   B N   1 
ATOM   21107 C  CA  . ALA   B 1 886  ? 91.00700   71.12600  11.81300  1.000 50.39923  ?  884  ALA   B CA  1 
ATOM   21108 C  C   . ALA   B 1 886  ? 91.60200   72.14800  10.85400  1.000 59.70747  ?  884  ALA   B C   1 
ATOM   21109 O  O   . ALA   B 1 886  ? 92.51900   72.87900  11.24400  1.000 73.13671  ?  884  ALA   B O   1 
ATOM   21110 C  CB  . ALA   B 1 886  ? 92.06800   70.07900  12.16500  1.000 62.72421  ?  884  ALA   B CB  1 
ATOM   21111 N  N   . LYS   B 1 887  ? 91.10800   72.22200  9.62200   1.000 62.85083  ?  885  LYS   B N   1 
ATOM   21112 C  CA  . LYS   B 1 887  ? 91.60500   73.16200  8.63100   1.000 64.28337  ?  885  LYS   B CA  1 
ATOM   21113 C  C   . LYS   B 1 887  ? 90.54300   74.21000  8.32100   1.000 58.73548  ?  885  LYS   B C   1 
ATOM   21114 O  O   . LYS   B 1 887  ? 89.34000   73.94400  8.39600   1.000 60.98226  ?  885  LYS   B O   1 
ATOM   21115 C  CB  . LYS   B 1 887  ? 92.02200   72.43600  7.34800   1.000 50.94835  ?  885  LYS   B CB  1 
ATOM   21116 C  CG  . LYS   B 1 887  ? 93.13800   71.42500  7.56200   1.000 50.62031  ?  885  LYS   B CG  1 
ATOM   21117 C  CD  . LYS   B 1 887  ? 94.00700   71.27700  6.32600   1.000 59.55654  ?  885  LYS   B CD  1 
ATOM   21118 C  CE  . LYS   B 1 887  ? 93.82300   69.91000  5.68700   1.000 75.93956  ?  885  LYS   B CE  1 
ATOM   21119 N  NZ  . LYS   B 1 887  ? 95.08200   69.11400  5.71200   1.000 78.17180  ?  885  LYS   B NZ  1 
ATOM   21120 N  N   . ALA   B 1 888  ? 91.00000   75.40500  7.97600   1.000 56.91251  ?  886  ALA   B N   1 
ATOM   21121 C  CA  . ALA   B 1 888  ? 90.14400   76.55100  7.72300   1.000 48.65841  ?  886  ALA   B CA  1 
ATOM   21122 C  C   . ALA   B 1 888  ? 90.48800   77.15500  6.37100   1.000 54.70407  ?  886  ALA   B C   1 
ATOM   21123 O  O   . ALA   B 1 888  ? 91.60600   76.98400  5.87300   1.000 60.33162  ?  886  ALA   B O   1 
ATOM   21124 C  CB  . ALA   B 1 888  ? 90.29900   77.60600  8.83000   1.000 53.64131  ?  886  ALA   B CB  1 
ATOM   21125 N  N   . PRO   B 1 889  ? 89.54000   77.86600  5.73900   1.000 59.95790  ?  887  PRO   B N   1 
ATOM   21126 C  CA  . PRO   B 1 889  ? 88.16500   78.14300  6.18000   1.000 52.72154  ?  887  PRO   B CA  1 
ATOM   21127 C  C   . PRO   B 1 889  ? 87.26300   76.92300  6.03500   1.000 52.65957  ?  887  PRO   B C   1 
ATOM   21128 O  O   . PRO   B 1 889  ? 87.41100   76.13400  5.10300   1.000 56.02837  ?  887  PRO   B O   1 
ATOM   21129 C  CB  . PRO   B 1 889  ? 87.74100   79.29700  5.26200   1.000 28.50029  ?  887  PRO   B CB  1 
ATOM   21130 C  CG  . PRO   B 1 889  ? 88.50700   79.05800  4.00100   1.000 49.40244  ?  887  PRO   B CG  1 
ATOM   21131 C  CD  . PRO   B 1 889  ? 89.83900   78.51400  4.44900   1.000 46.19328  ?  887  PRO   B CD  1 
ATOM   21132 N  N   . LEU   B 1 890  ? 86.32700   76.73500  6.96400   1.000 42.25135  ?  888  LEU   B N   1 
ATOM   21133 C  CA  . LEU   B 1 890  ? 85.33800   75.66200  6.86400   1.000 46.45507  ?  888  LEU   B CA  1 
ATOM   21134 C  C   . LEU   B 1 890  ? 84.22300   75.99200  5.88300   1.000 49.47377  ?  888  LEU   B C   1 
ATOM   21135 O  O   . LEU   B 1 890  ? 83.04400   75.76200  6.16600   1.000 45.58865  ?  888  LEU   B O   1 
ATOM   21136 C  CB  . LEU   B 1 890  ? 84.77400   75.35900  8.24900   1.000 44.29923  ?  888  LEU   B CB  1 
ATOM   21137 C  CG  . LEU   B 1 890  ? 85.70300   74.52200  9.12700   1.000 47.84239  ?  888  LEU   B CG  1 
ATOM   21138 C  CD1 . LEU   B 1 890  ? 85.16700   74.42700  10.54400  1.000 48.76834  ?  888  LEU   B CD1 1 
ATOM   21139 C  CD2 . LEU   B 1 890  ? 85.90200   73.13800  8.52500   1.000 39.40639  ?  888  LEU   B CD2 1 
ATOM   21140 N  N   . LEU   B 1 891  ? 84.58200   76.54300  4.72700   1.000 41.31074  ?  889  LEU   B N   1 
ATOM   21141 C  CA  . LEU   B 1 891  ? 83.63200   76.89700  3.68600   1.000 48.00865  ?  889  LEU   B CA  1 
ATOM   21142 C  C   . LEU   B 1 891  ? 84.37100   76.90900  2.35700   1.000 44.03281  ?  889  LEU   B C   1 
ATOM   21143 O  O   . LEU   B 1 891  ? 85.51800   77.35300  2.28900   1.000 47.81918  ?  889  LEU   B O   1 
ATOM   21144 C  CB  . LEU   B 1 891  ? 82.98800   78.26200  3.95400   1.000 46.07165  ?  889  LEU   B CB  1 
ATOM   21145 C  CG  . LEU   B 1 891  ? 82.00500   78.75600  2.89200   1.000 43.34656  ?  889  LEU   B CG  1 
ATOM   21146 C  CD1 . LEU   B 1 891  ? 80.69200   79.17300  3.53100   1.000 48.58035  ?  889  LEU   B CD1 1 
ATOM   21147 C  CD2 . LEU   B 1 891  ? 82.61000   79.90200  2.09600   1.000 32.16731  ?  889  LEU   B CD2 1 
ATOM   21148 N  N   . ARG   B 1 892  ? 83.71600   76.40300  1.31500   1.000 54.09641  ?  890  ARG   B N   1 
ATOM   21149 C  CA  . ARG   B 1 892  ? 84.23400   76.45200  -0.04400  1.000 46.88740  ?  890  ARG   B CA  1 
ATOM   21150 C  C   . ARG   B 1 892  ? 83.16900   77.05100  -0.94900  1.000 47.57888  ?  890  ARG   B C   1 
ATOM   21151 O  O   . ARG   B 1 892  ? 81.97200   76.95800  -0.66500  1.000 49.48250  ?  890  ARG   B O   1 
ATOM   21152 C  CB  . ARG   B 1 892  ? 84.64100   75.05900  -0.54900  1.000 42.37146  ?  890  ARG   B CB  1 
ATOM   21153 C  CG  . ARG   B 1 892  ? 85.38000   74.22000  0.48300   1.000 39.79875  ?  890  ARG   B CG  1 
ATOM   21154 C  CD  . ARG   B 1 892  ? 85.89200   72.91900  -0.11000  1.000 47.89739  ?  890  ARG   B CD  1 
ATOM   21155 N  NE  . ARG   B 1 892  ? 86.21800   71.93200  0.91400   1.000 45.34293  ?  890  ARG   B NE  1 
ATOM   21156 C  CZ  . ARG   B 1 892  ? 85.42700   70.92900  1.27100   1.000 62.42489  ?  890  ARG   B CZ  1 
ATOM   21157 N  NH1 . ARG   B 1 892  ? 84.23000   70.76200  0.72700   1.000 56.25983  ?  890  ARG   B NH1 1 
ATOM   21158 N  NH2 . ARG   B 1 892  ? 85.84800   70.07000  2.19500   1.000 52.49869  ?  890  ARG   B NH2 1 
ATOM   21159 N  N   . ALA   B 1 893  ? 83.60800   77.67300  -2.04000  1.000 47.46253  ?  891  ALA   B N   1 
ATOM   21160 C  CA  . ALA   B 1 893  ? 82.70300   78.39100  -2.92500  1.000 40.76591  ?  891  ALA   B CA  1 
ATOM   21161 C  C   . ALA   B 1 893  ? 83.11000   78.14900  -4.37200  1.000 39.60751  ?  891  ALA   B C   1 
ATOM   21162 O  O   . ALA   B 1 893  ? 84.03300   77.38300  -4.66500  1.000 49.98346  ?  891  ALA   B O   1 
ATOM   21163 C  CB  . ALA   B 1 893  ? 82.68600   79.89000  -2.60100  1.000 40.55894  ?  891  ALA   B CB  1 
ATOM   21164 N  N   . GLY   B 1 894  ? 82.41000   78.81500  -5.27700  1.000 48.04524  ?  892  GLY   B N   1 
ATOM   21165 C  CA  . GLY   B 1 894  ? 82.65700   78.66800  -6.69700  1.000 52.04491  ?  892  GLY   B CA  1 
ATOM   21166 C  C   . GLY   B 1 894  ? 81.48500   79.18400  -7.49700  1.000 48.96178  ?  892  GLY   B C   1 
ATOM   21167 O  O   . GLY   B 1 894  ? 80.38700   79.39200  -6.98100  1.000 42.56856  ?  892  GLY   B O   1 
ATOM   21168 N  N   . VAL   B 1 895  ? 81.73800   79.39200  -8.78700  1.000 46.60638  ?  893  VAL   B N   1 
ATOM   21169 C  CA  . VAL   B 1 895  ? 80.74000   79.92700  -9.70600  1.000 42.06510  ?  893  VAL   B CA  1 
ATOM   21170 C  C   . VAL   B 1 895  ? 80.73200   79.07100  -10.96300 1.000 42.33606  ?  893  VAL   B C   1 
ATOM   21171 O  O   . VAL   B 1 895  ? 81.74700   78.98200  -11.66400 1.000 50.42983  ?  893  VAL   B O   1 
ATOM   21172 C  CB  . VAL   B 1 895  ? 81.00900   81.40000  -10.06400 1.000 39.19657  ?  893  VAL   B CB  1 
ATOM   21173 C  CG1 . VAL   B 1 895  ? 80.17100   81.81300  -11.26100 1.000 29.40064  ?  893  VAL   B CG1 1 
ATOM   21174 C  CG2 . VAL   B 1 895  ? 80.71400   82.30100  -8.87400  1.000 50.38091  ?  893  VAL   B CG2 1 
ATOM   21175 N  N   . ILE   B 1 896  ? 79.59400   78.44300  -11.24600 1.000 40.47502  ?  894  ILE   B N   1 
ATOM   21176 C  CA  . ILE   B 1 896  ? 79.38800   77.73000  -12.50100 1.000 39.03474  ?  894  ILE   B CA  1 
ATOM   21177 C  C   . ILE   B 1 896  ? 78.69300   78.68000  -13.46500 1.000 37.97961  ?  894  ILE   B C   1 
ATOM   21178 O  O   . ILE   B 1 896  ? 77.58100   79.15000  -13.19500 1.000 38.57022  ?  894  ILE   B O   1 
ATOM   21179 C  CB  . ILE   B 1 896  ? 78.56400   76.45100  -12.29600 1.000 33.99808  ?  894  ILE   B CB  1 
ATOM   21180 C  CG1 . ILE   B 1 896  ? 79.18200   75.58100  -11.20100 1.000 27.34588  ?  894  ILE   B CG1 1 
ATOM   21181 C  CG2 . ILE   B 1 896  ? 78.45700   75.67600  -13.60300 1.000 26.46027  ?  894  ILE   B CG2 1 
ATOM   21182 C  CD1 . ILE   B 1 896  ? 78.41400   74.30600  -10.92800 1.000 30.41546  ?  894  ILE   B CD1 1 
ATOM   21183 N  N   . GLU   B 1 897  ? 79.34900   78.97000  -14.58400 1.000 47.97237  ?  895  GLU   B N   1 
ATOM   21184 C  CA  . GLU   B 1 897  ? 78.83600   79.89900  -15.58100 1.000 42.65545  ?  895  GLU   B CA  1 
ATOM   21185 C  C   . GLU   B 1 897  ? 78.21900   79.11500  -16.73100 1.000 39.62117  ?  895  GLU   B C   1 
ATOM   21186 O  O   . GLU   B 1 897  ? 78.87800   78.25600  -17.32800 1.000 37.14250  ?  895  GLU   B O   1 
ATOM   21187 C  CB  . GLU   B 1 897  ? 79.94700   80.81600  -16.09000 1.000 44.14669  ?  895  GLU   B CB  1 
ATOM   21188 C  CG  . GLU   B 1 897  ? 79.44000   82.05000  -16.80900 1.000 53.05869  ?  895  GLU   B CG  1 
ATOM   21189 C  CD  . GLU   B 1 897  ? 80.55500   82.99900  -17.18900 1.000 63.91260  ?  895  GLU   B CD  1 
ATOM   21190 O  OE1 . GLU   B 1 897  ? 81.49500   83.17000  -16.38200 1.000 69.10923  ?  895  GLU   B OE1 1 
ATOM   21191 O  OE2 . GLU   B 1 897  ? 80.48700   83.57700  -18.29300 1.000 66.10842  -1 895  GLU   B OE2 1 
ATOM   21192 N  N   . THR   B 1 898  ? 76.95700   79.40500  -17.03000 1.000 45.03459  ?  896  THR   B N   1 
ATOM   21193 C  CA  . THR   B 1 898  ? 76.25400   78.83300  -18.16400 1.000 44.76778  ?  896  THR   B CA  1 
ATOM   21194 C  C   . THR   B 1 898  ? 76.03900   79.91600  -19.21500 1.000 52.94313  ?  896  THR   B C   1 
ATOM   21195 O  O   . THR   B 1 898  ? 76.51900   81.04800  -19.08400 1.000 60.58141  ?  896  THR   B O   1 
ATOM   21196 C  CB  . THR   B 1 898  ? 74.92700   78.20800  -17.72100 1.000 43.70975  ?  896  THR   B CB  1 
ATOM   21197 O  OG1 . THR   B 1 898  ? 73.99900   79.24300  -17.37000 1.000 51.51622  ?  896  THR   B OG1 1 
ATOM   21198 C  CG2 . THR   B 1 898  ? 75.14000   77.29500  -16.52700 1.000 46.34966  ?  896  THR   B CG2 1 
ATOM   21199 N  N   . ALA   B 1 899  ? 75.30400   79.56700  -20.26900 1.000 60.13779  ?  897  ALA   B N   1 
ATOM   21200 C  CA  . ALA   B 1 899  ? 75.02200   80.53100  -21.32200 1.000 48.42413  ?  897  ALA   B CA  1 
ATOM   21201 C  C   . ALA   B 1 899  ? 73.99600   81.57900  -20.90600 1.000 57.90237  ?  897  ALA   B C   1 
ATOM   21202 O  O   . ALA   B 1 899  ? 73.82500   82.56800  -21.62700 1.000 74.49705  ?  897  ALA   B O   1 
ATOM   21203 C  CB  . ALA   B 1 899  ? 74.54500   79.80200  -22.57900 1.000 58.00933  ?  897  ALA   B CB  1 
ATOM   21204 N  N   . ASP   B 1 900  ? 73.31800   81.39700  -19.76900 1.000 59.15931  ?  898  ASP   B N   1 
ATOM   21205 C  CA  . ASP   B 1 900  ? 72.26000   82.30800  -19.35700 1.000 56.03341  ?  898  ASP   B CA  1 
ATOM   21206 C  C   . ASP   B 1 900  ? 72.30300   82.71600  -17.89200 1.000 50.82806  ?  898  ASP   B C   1 
ATOM   21207 O  O   . ASP   B 1 900  ? 71.55500   83.62200  -17.51000 1.000 52.35225  ?  898  ASP   B O   1 
ATOM   21208 C  CB  . ASP   B 1 900  ? 70.87900   81.70100  -19.65400 1.000 55.71078  ?  898  ASP   B CB  1 
ATOM   21209 C  CG  . ASP   B 1 900  ? 70.80100   80.22000  -19.31600 1.000 80.78018  ?  898  ASP   B CG  1 
ATOM   21210 O  OD1 . ASP   B 1 900  ? 71.85500   79.60200  -19.04800 1.000 76.62378  ?  898  ASP   B OD1 1 
ATOM   21211 O  OD2 . ASP   B 1 900  ? 69.67700   79.67100  -19.32600 1.000 90.87872  -1 898  ASP   B OD2 1 
ATOM   21212 N  N   . LYS   B 1 901  ? 73.14100   82.09700  -17.06400 1.000 45.75645  ?  899  LYS   B N   1 
ATOM   21213 C  CA  . LYS   B 1 901  ? 73.17100   82.44400  -15.65000 1.000 40.30319  ?  899  LYS   B CA  1 
ATOM   21214 C  C   . LYS   B 1 901  ? 74.52600   82.08200  -15.06800 1.000 44.09020  ?  899  LYS   B C   1 
ATOM   21215 O  O   . LYS   B 1 901  ? 75.28500   81.29900  -15.64500 1.000 47.35992  ?  899  LYS   B O   1 
ATOM   21216 C  CB  . LYS   B 1 901  ? 72.05600   81.73500  -14.87300 1.000 39.87258  ?  899  LYS   B CB  1 
ATOM   21217 C  CG  . LYS   B 1 901  ? 72.22300   80.22600  -14.79300 1.000 39.16221  ?  899  LYS   B CG  1 
ATOM   21218 C  CD  . LYS   B 1 901  ? 71.07700   79.57500  -14.03400 1.000 35.07094  ?  899  LYS   B CD  1 
ATOM   21219 C  CE  . LYS   B 1 901  ? 71.11800   78.06000  -14.16900 1.000 47.21380  ?  899  LYS   B CE  1 
ATOM   21220 N  NZ  . LYS   B 1 901  ? 70.00600   77.39400  -13.43400 1.000 56.34850  ?  899  LYS   B NZ  1 
ATOM   21221 N  N   . LYS   B 1 902  ? 74.81500   82.66900  -13.90800 1.000 46.61801  ?  900  LYS   B N   1 
ATOM   21222 C  CA  . LYS   B 1 902  ? 76.00100   82.35400  -13.11900 1.000 46.81261  ?  900  LYS   B CA  1 
ATOM   21223 C  C   . LYS   B 1 902  ? 75.52800   81.75500  -11.80100 1.000 42.18257  ?  900  LYS   B C   1 
ATOM   21224 O  O   . LYS   B 1 902  ? 74.90100   82.44500  -10.99100 1.000 40.58683  ?  900  LYS   B O   1 
ATOM   21225 C  CB  . LYS   B 1 902  ? 76.85600   83.59900  -12.88100 1.000 42.93424  ?  900  LYS   B CB  1 
ATOM   21226 C  CG  . LYS   B 1 902  ? 77.57900   84.12600  -14.11500 1.000 57.55998  ?  900  LYS   B CG  1 
ATOM   21227 C  CD  . LYS   B 1 902  ? 78.40300   85.36400  -13.77400 1.000 56.47918  ?  900  LYS   B CD  1 
ATOM   21228 C  CE  . LYS   B 1 902  ? 79.34800   85.74700  -14.90000 1.000 52.14217  ?  900  LYS   B CE  1 
ATOM   21229 N  NZ  . LYS   B 1 902  ? 80.35900   86.73900  -14.44300 1.000 47.03131  ?  900  LYS   B NZ  1 
ATOM   21230 N  N   . VAL   B 1 903  ? 75.82400   80.47700  -11.58800 1.000 41.49091  ?  901  VAL   B N   1 
ATOM   21231 C  CA  . VAL   B 1 903  ? 75.37600   79.76100  -10.39900 1.000 35.61589  ?  901  VAL   B CA  1 
ATOM   21232 C  C   . VAL   B 1 903  ? 76.46700   79.85600  -9.33800  1.000 38.46638  ?  901  VAL   B C   1 
ATOM   21233 O  O   . VAL   B 1 903  ? 77.50000   79.18700  -9.43100  1.000 41.79715  ?  901  VAL   B O   1 
ATOM   21234 C  CB  . VAL   B 1 903  ? 75.03900   78.30000  -10.71500 1.000 27.75739  ?  901  VAL   B CB  1 
ATOM   21235 C  CG1 . VAL   B 1 903  ? 74.44500   77.62600  -9.49400  1.000 31.89495  ?  901  VAL   B CG1 1 
ATOM   21236 C  CG2 . VAL   B 1 903  ? 74.07800   78.22400  -11.88400 1.000 36.27621  ?  901  VAL   B CG2 1 
ATOM   21237 N  N   . LEU   B 1 904  ? 76.23600   80.68600  -8.32400  1.000 32.60526  ?  902  LEU   B N   1 
ATOM   21238 C  CA  . LEU   B 1 904  ? 77.11800   80.74100  -7.16700  1.000 31.43732  ?  902  LEU   B CA  1 
ATOM   21239 C  C   . LEU   B 1 904  ? 76.73300   79.63500  -6.19100  1.000 39.09342  ?  902  LEU   B C   1 
ATOM   21240 O  O   . LEU   B 1 904  ? 75.55600   79.47600  -5.85200  1.000 47.86979  ?  902  LEU   B O   1 
ATOM   21241 C  CB  . LEU   B 1 904  ? 77.02900   82.11500  -6.49900  1.000 34.72419  ?  902  LEU   B CB  1 
ATOM   21242 C  CG  . LEU   B 1 904  ? 77.88800   82.46600  -5.27300  1.000 39.40145  ?  902  LEU   B CG  1 
ATOM   21243 C  CD1 . LEU   B 1 904  ? 77.21900   82.06100  -3.96900  1.000 42.71228  ?  902  LEU   B CD1 1 
ATOM   21244 C  CD2 . LEU   B 1 904  ? 79.27500   81.85300  -5.37000  1.000 36.48497  ?  902  LEU   B CD2 1 
ATOM   21245 N  N   . TRP   B 1 905  ? 77.72400   78.86500  -5.74800  1.000 36.75482  ?  903  TRP   B N   1 
ATOM   21246 C  CA  . TRP   B 1 905  ? 77.50900   77.77900  -4.80300  1.000 37.48939  ?  903  TRP   B CA  1 
ATOM   21247 C  C   . TRP   B 1 905  ? 78.50200   77.89800  -3.65900  1.000 44.01869  ?  903  TRP   B C   1 
ATOM   21248 O  O   . TRP   B 1 905  ? 79.65000   78.30300  -3.86500  1.000 50.89163  ?  903  TRP   B O   1 
ATOM   21249 C  CB  . TRP   B 1 905  ? 77.65600   76.40500  -5.47900  1.000 35.58795  ?  903  TRP   B CB  1 
ATOM   21250 C  CG  . TRP   B 1 905  ? 79.06600   76.06300  -5.88100  1.000 40.58202  ?  903  TRP   B CG  1 
ATOM   21251 C  CD1 . TRP   B 1 905  ? 79.64500   76.27500  -7.09900  1.000 39.33695  ?  903  TRP   B CD1 1 
ATOM   21252 C  CD2 . TRP   B 1 905  ? 80.07100   75.44500  -5.06400  1.000 47.22252  ?  903  TRP   B CD2 1 
ATOM   21253 N  NE1 . TRP   B 1 905  ? 80.94500   75.83100  -7.09100  1.000 43.04237  ?  903  TRP   B NE1 1 
ATOM   21254 C  CE2 . TRP   B 1 905  ? 81.23200   75.31800  -5.85300  1.000 47.71651  ?  903  TRP   B CE2 1 
ATOM   21255 C  CE3 . TRP   B 1 905  ? 80.10200   74.99000  -3.74100  1.000 43.40454  ?  903  TRP   B CE3 1 
ATOM   21256 C  CZ2 . TRP   B 1 905  ? 82.40900   74.75400  -5.36500  1.000 32.00950  ?  903  TRP   B CZ2 1 
ATOM   21257 C  CZ3 . TRP   B 1 905  ? 81.27400   74.43200  -3.25800  1.000 49.29046  ?  903  TRP   B CZ3 1 
ATOM   21258 C  CH2 . TRP   B 1 905  ? 82.41000   74.31900  -4.06900  1.000 34.44676  ?  903  TRP   B CH2 1 
ATOM   21259 N  N   . PHE   B 1 906  ? 78.06100   77.54900  -2.45100  1.000 36.28326  ?  904  PHE   B N   1 
ATOM   21260 C  CA  . PHE   B 1 906  ? 78.98000   77.41200  -1.33200  1.000 40.64976  ?  904  PHE   B CA  1 
ATOM   21261 C  C   . PHE   B 1 906  ? 78.63400   76.15800  -0.54300  1.000 46.57647  ?  904  PHE   B C   1 
ATOM   21262 O  O   . PHE   B 1 906  ? 77.47300   75.74800  -0.47200  1.000 46.73760  ?  904  PHE   B O   1 
ATOM   21263 C  CB  . PHE   B 1 906  ? 79.00500   78.67200  -0.42800  1.000 39.12132  ?  904  PHE   B CB  1 
ATOM   21264 C  CG  . PHE   B 1 906  ? 77.71200   78.97000  0.30100   1.000 36.33999  ?  904  PHE   B CG  1 
ATOM   21265 C  CD1 . PHE   B 1 906  ? 77.25800   78.16500  1.33900   1.000 42.45852  ?  904  PHE   B CD1 1 
ATOM   21266 C  CD2 . PHE   B 1 906  ? 76.97400   80.09500  -0.03200  1.000 31.78325  ?  904  PHE   B CD2 1 
ATOM   21267 C  CE1 . PHE   B 1 906  ? 76.08000   78.46300  2.00600   1.000 67.23481  ?  904  PHE   B CE1 1 
ATOM   21268 C  CE2 . PHE   B 1 906  ? 75.79900   80.39800  0.63200   1.000 40.60528  ?  904  PHE   B CE2 1 
ATOM   21269 C  CZ  . PHE   B 1 906  ? 75.35300   79.58400  1.65200   1.000 60.84603  ?  904  PHE   B CZ  1 
ATOM   21270 N  N   . ASP   B 1 907  ? 79.66500   75.53800  0.02400   1.000 51.04032  ?  905  ASP   B N   1 
ATOM   21271 C  CA  . ASP   B 1 907  ? 79.52100   74.36200  0.87300   1.000 43.09236  ?  905  ASP   B CA  1 
ATOM   21272 C  C   . ASP   B 1 907  ? 80.14100   74.67500  2.22400   1.000 48.56456  ?  905  ASP   B C   1 
ATOM   21273 O  O   . ASP   B 1 907  ? 81.31500   75.05400  2.29800   1.000 50.19433  ?  905  ASP   B O   1 
ATOM   21274 C  CB  . ASP   B 1 907  ? 80.18300   73.13500  0.24000   1.000 44.55104  ?  905  ASP   B CB  1 
ATOM   21275 C  CG  . ASP   B 1 907  ? 79.95700   71.86500  1.04700   1.000 59.79079  ?  905  ASP   B CG  1 
ATOM   21276 O  OD1 . ASP   B 1 907  ? 79.05700   71.86000  1.91400   1.000 65.34544  ?  905  ASP   B OD1 1 
ATOM   21277 O  OD2 . ASP   B 1 907  ? 80.67900   70.87000  0.81400   1.000 61.97226  -1 905  ASP   B OD2 1 
ATOM   21278 N  N   . SER   B 1 908  ? 79.35200   74.52300  3.28600   1.000 48.10515  ?  906  SER   B N   1 
ATOM   21279 C  CA  . SER   B 1 908  ? 79.82300   74.82900  4.62900   1.000 41.40284  ?  906  SER   B CA  1 
ATOM   21280 C  C   . SER   B 1 908  ? 79.64200   73.62600  5.54600   1.000 54.35256  ?  906  SER   B C   1 
ATOM   21281 O  O   . SER   B 1 908  ? 79.31600   72.52700  5.08600   1.000 52.82704  ?  906  SER   B O   1 
ATOM   21282 C  CB  . SER   B 1 908  ? 79.08300   76.05100  5.18700   1.000 41.50049  ?  906  SER   B CB  1 
ATOM   21283 O  OG  . SER   B 1 908  ? 79.60000   76.40700  6.45500   1.000 57.78383  ?  906  SER   B OG  1 
ATOM   21284 N  N   . HIS   B 1 909  ? 79.84900   73.82600  6.84400   1.000 61.12942  ?  907  HIS   B N   1 
ATOM   21285 C  CA  . HIS   B 1 909  ? 79.63900   72.79400  7.84600   1.000 49.28481  ?  907  HIS   B CA  1 
ATOM   21286 C  C   . HIS   B 1 909  ? 78.66300   73.30900  8.89500   1.000 58.09127  ?  907  HIS   B C   1 
ATOM   21287 O  O   . HIS   B 1 909  ? 78.63600   74.50400  9.20400   1.000 61.41695  ?  907  HIS   B O   1 
ATOM   21288 C  CB  . HIS   B 1 909  ? 80.96600   72.38200  8.51000   1.000 48.18062  ?  907  HIS   B CB  1 
ATOM   21289 C  CG  . HIS   B 1 909  ? 81.02900   70.94000  8.91600   1.000 50.71157  ?  907  HIS   B CG  1 
ATOM   21290 N  ND1 . HIS   B 1 909  ? 80.33800   70.43600  9.99800   1.000 55.32114  ?  907  HIS   B ND1 1 
ATOM   21291 C  CD2 . HIS   B 1 909  ? 81.71800   69.89800  8.39200   1.000 52.31500  ?  907  HIS   B CD2 1 
ATOM   21292 C  CE1 . HIS   B 1 909  ? 80.59400   69.14500  10.11900  1.000 50.36268  ?  907  HIS   B CE1 1 
ATOM   21293 N  NE2 . HIS   B 1 909  ? 81.42900   68.79300  9.15700   1.000 54.15791  ?  907  HIS   B NE2 1 
ATOM   21294 N  N   . HIS   B 1 910  ? 77.85700   72.39600  9.44400   1.000 56.71135  ?  908  HIS   B N   1 
ATOM   21295 C  CA  . HIS   B 1 910  ? 76.90900   72.77800  10.48500  1.000 52.78885  ?  908  HIS   B CA  1 
ATOM   21296 C  C   . HIS   B 1 910  ? 77.59500   73.30700  11.73700  1.000 59.14673  ?  908  HIS   B C   1 
ATOM   21297 O  O   . HIS   B 1 910  ? 76.92900   73.92100  12.57800  1.000 65.83042  ?  908  HIS   B O   1 
ATOM   21298 C  CB  . HIS   B 1 910  ? 76.01600   71.59200  10.85200  1.000 54.14117  ?  908  HIS   B CB  1 
ATOM   21299 C  CG  . HIS   B 1 910  ? 74.56000   71.93200  10.89900  1.000 57.80456  ?  908  HIS   B CG  1 
ATOM   21300 N  ND1 . HIS   B 1 910  ? 74.06700   72.98900  11.63400  1.000 66.90611  ?  908  HIS   B ND1 1 
ATOM   21301 C  CD2 . HIS   B 1 910  ? 73.49000   71.35600  10.30400  1.000 72.91017  ?  908  HIS   B CD2 1 
ATOM   21302 C  CE1 . HIS   B 1 910  ? 72.75600   73.05000  11.48800  1.000 68.06231  ?  908  HIS   B CE1 1 
ATOM   21303 N  NE2 . HIS   B 1 910  ? 72.38000   72.06900  10.68800  1.000 89.15987  ?  908  HIS   B NE2 1 
ATOM   21304 N  N   . ILE   B 1 911  ? 78.90300   73.09600  11.87500  1.000 60.77691  ?  909  ILE   B N   1 
ATOM   21305 C  CA  . ILE   B 1 911  ? 79.67600   73.62800  12.99200  1.000 59.79979  ?  909  ILE   B CA  1 
ATOM   21306 C  C   . ILE   B 1 911  ? 79.88900   75.12600  12.81000  1.000 53.89907  ?  909  ILE   B C   1 
ATOM   21307 O  O   . ILE   B 1 911  ? 80.44000   75.79800  13.69000  1.000 66.62504  ?  909  ILE   B O   1 
ATOM   21308 C  CB  . ILE   B 1 911  ? 81.01900   72.88200  13.11800  1.000 59.84183  ?  909  ILE   B CB  1 
ATOM   21309 C  CG1 . ILE   B 1 911  ? 81.57000   72.97600  14.54200  1.000 48.68981  ?  909  ILE   B CG1 1 
ATOM   21310 C  CG2 . ILE   B 1 911  ? 82.02000   73.39600  12.09600  1.000 44.67292  ?  909  ILE   B CG2 1 
ATOM   21311 C  CD1 . ILE   B 1 911  ? 82.55700   71.88200  14.87000  1.000 54.25879  ?  909  ILE   B CD1 1 
ATOM   21312 N  N   . LEU   B 1 912  ? 79.44500   75.66300  11.67400  1.000 55.99778  ?  910  LEU   B N   1 
ATOM   21313 C  CA  . LEU   B 1 912  ? 79.67700   77.06400  11.35000  1.000 54.61541  ?  910  LEU   B CA  1 
ATOM   21314 C  C   . LEU   B 1 912  ? 78.39500   77.74900  10.89000  1.000 59.78697  ?  910  LEU   B C   1 
ATOM   21315 O  O   . LEU   B 1 912  ? 78.18500   78.93400  11.17000  1.000 69.12777  ?  910  LEU   B O   1 
ATOM   21316 C  CB  . LEU   B 1 912  ? 80.77000   77.17300  10.28100  1.000 42.54161  ?  910  LEU   B CB  1 
ATOM   21317 C  CG  . LEU   B 1 912  ? 80.97100   78.49400  9.53700   1.000 49.41898  ?  910  LEU   B CG  1 
ATOM   21318 C  CD1 . LEU   B 1 912  ? 81.21400   79.64400  10.50600  1.000 46.88869  ?  910  LEU   B CD1 1 
ATOM   21319 C  CD2 . LEU   B 1 912  ? 82.12000   78.37100  8.54100   1.000 49.88458  ?  910  LEU   B CD2 1 
ATOM   21320 N  N   . LEU   B 1 913  ? 77.52400   77.01600  10.19900  1.000 56.08825  ?  911  LEU   B N   1 
ATOM   21321 C  CA  . LEU   B 1 913  ? 76.34500   77.59300  9.56300   1.000 57.80155  ?  911  LEU   B CA  1 
ATOM   21322 C  C   . LEU   B 1 913  ? 75.08600   76.93800  10.11100  1.000 54.01109  ?  911  LEU   B C   1 
ATOM   21323 O  O   . LEU   B 1 913  ? 74.87800   75.73500  9.92400   1.000 68.94041  ?  911  LEU   B O   1 
ATOM   21324 C  CB  . LEU   B 1 913  ? 76.41100   77.42600  8.04400   1.000 54.64638  ?  911  LEU   B CB  1 
ATOM   21325 C  CG  . LEU   B 1 913  ? 75.80100   78.55600  7.21400   1.000 56.13903  ?  911  LEU   B CG  1 
ATOM   21326 C  CD1 . LEU   B 1 913  ? 76.51500   79.86800  7.49500   1.000 52.05630  ?  911  LEU   B CD1 1 
ATOM   21327 C  CD2 . LEU   B 1 913  ? 75.85400   78.21800  5.73200   1.000 57.37706  ?  911  LEU   B CD2 1 
ATOM   21328 N  N   . ASP   B 1 914  ? 74.24900   77.72700  10.77200  1.000 44.68356  ?  912  ASP   B N   1 
ATOM   21329 C  CA  . ASP   B 1 914  ? 72.92000   77.29600  11.18000  1.000 48.34011  ?  912  ASP   B CA  1 
ATOM   21330 C  C   . ASP   B 1 914  ? 71.88400   78.18000  10.48800  1.000 45.64171  ?  912  ASP   B C   1 
ATOM   21331 O  O   . ASP   B 1 914  ? 72.21900   79.03000  9.65800   1.000 41.54810  ?  912  ASP   B O   1 
ATOM   21332 C  CB  . ASP   B 1 914  ? 72.78300   77.30200  12.71100  1.000 59.29040  ?  912  ASP   B CB  1 
ATOM   21333 C  CG  . ASP   B 1 914  ? 72.53100   78.68800  13.29200  1.000 56.92118  ?  912  ASP   B CG  1 
ATOM   21334 O  OD1 . ASP   B 1 914  ? 72.93800   79.69400  12.68000  1.000 67.56537  ?  912  ASP   B OD1 1 
ATOM   21335 O  OD2 . ASP   B 1 914  ? 71.93200   78.76900  14.38600  1.000 43.95055  -1 912  ASP   B OD2 1 
ATOM   21336 N  N   . GLY   B 1 915  ? 70.61300   77.96600  10.83700  1.000 43.75635  ?  913  GLY   B N   1 
ATOM   21337 C  CA  . GLY   B 1 915  ? 69.53600   78.65200  10.13700  1.000 48.43620  ?  913  GLY   B CA  1 
ATOM   21338 C  C   . GLY   B 1 915  ? 69.66800   80.16200  10.17700  1.000 50.27855  ?  913  GLY   B C   1 
ATOM   21339 O  O   . GLY   B 1 915  ? 69.61300   80.83100  9.14200   1.000 40.35365  ?  913  GLY   B O   1 
ATOM   21340 N  N   . LEU   B 1 916  ? 69.85200   80.72200  11.37400  1.000 55.43994  ?  914  LEU   B N   1 
ATOM   21341 C  CA  . LEU   B 1 916  ? 69.93100   82.17300  11.50100  1.000 47.63291  ?  914  LEU   B CA  1 
ATOM   21342 C  C   . LEU   B 1 916  ? 71.26700   82.72200  11.01600  1.000 46.43684  ?  914  LEU   B C   1 
ATOM   21343 O  O   . LEU   B 1 916  ? 71.31100   83.83700  10.48600  1.000 47.47680  ?  914  LEU   B O   1 
ATOM   21344 C  CB  . LEU   B 1 916  ? 69.67900   82.59700  12.95000  1.000 63.19998  ?  914  LEU   B CB  1 
ATOM   21345 C  CG  . LEU   B 1 916  ? 68.23400   82.56200  13.47000  1.000 52.65437  ?  914  LEU   B CG  1 
ATOM   21346 C  CD1 . LEU   B 1 916  ? 67.27900   83.20000  12.47300  1.000 45.30491  ?  914  LEU   B CD1 1 
ATOM   21347 C  CD2 . LEU   B 1 916  ? 67.78700   81.14600  13.81500  1.000 57.91814  ?  914  LEU   B CD2 1 
ATOM   21348 N  N   . SER   B 1 917  ? 72.36000   81.96800  11.18600  1.000 40.05069  ?  915  SER   B N   1 
ATOM   21349 C  CA  . SER   B 1 917  ? 73.63700   82.39800  10.62200  1.000 41.84084  ?  915  SER   B CA  1 
ATOM   21350 C  C   . SER   B 1 917  ? 73.58000   82.44700  9.10300   1.000 45.86854  ?  915  SER   B C   1 
ATOM   21351 O  O   . SER   B 1 917  ? 74.25400   83.27800  8.48200   1.000 48.90061  ?  915  SER   B O   1 
ATOM   21352 C  CB  . SER   B 1 917  ? 74.77000   81.47100  11.06700  1.000 49.32330  ?  915  SER   B CB  1 
ATOM   21353 O  OG  . SER   B 1 917  ? 74.82200   81.35700  12.47900  1.000 54.59776  ?  915  SER   B OG  1 
ATOM   21354 N  N   . LYS   B 1 918  ? 72.79300   81.56000  8.49200   1.000 52.94402  ?  916  LYS   B N   1 
ATOM   21355 C  CA  . LYS   B 1 918  ? 72.58400   81.62600  7.05000   1.000 46.99280  ?  916  LYS   B CA  1 
ATOM   21356 C  C   . LYS   B 1 918  ? 71.96400   82.95900  6.64600   1.000 46.32730  ?  916  LYS   B C   1 
ATOM   21357 O  O   . LYS   B 1 918  ? 72.40900   83.58900  5.67900   1.000 38.74655  ?  916  LYS   B O   1 
ATOM   21358 C  CB  . LYS   B 1 918  ? 71.70200   80.46000  6.60500   1.000 41.62935  ?  916  LYS   B CB  1 
ATOM   21359 C  CG  . LYS   B 1 918  ? 71.30300   80.49600  5.14500   1.000 36.25967  ?  916  LYS   B CG  1 
ATOM   21360 C  CD  . LYS   B 1 918  ? 69.94500   79.84200  4.93800   1.000 42.42468  ?  916  LYS   B CD  1 
ATOM   21361 C  CE  . LYS   B 1 918  ? 68.80600   80.81800  5.18500   1.000 43.21011  ?  916  LYS   B CE  1 
ATOM   21362 N  NZ  . LYS   B 1 918  ? 67.51300   80.31000  4.64200   1.000 52.29586  ?  916  LYS   B NZ  1 
ATOM   21363 N  N   . SER   B 1 919  ? 70.94500   83.41100  7.38300   1.000 47.86138  ?  917  SER   B N   1 
ATOM   21364 C  CA  . SER   B 1 919  ? 70.29900   84.68000  7.05700   1.000 53.80110  ?  917  SER   B CA  1 
ATOM   21365 C  C   . SER   B 1 919  ? 71.25400   85.85300  7.24300   1.000 54.05091  ?  917  SER   B C   1 
ATOM   21366 O  O   . SER   B 1 919  ? 71.21400   86.82000  6.47400   1.000 62.68938  ?  917  SER   B O   1 
ATOM   21367 C  CB  . SER   B 1 919  ? 69.05000   84.87000  7.91400   1.000 45.78004  ?  917  SER   B CB  1 
ATOM   21368 O  OG  . SER   B 1 919  ? 68.14700   83.79400  7.73800   1.000 67.44389  ?  917  SER   B OG  1 
ATOM   21369 N  N   . ILE   B 1 920  ? 72.10800   85.79000  8.26700   1.000 47.76249  ?  918  ILE   B N   1 
ATOM   21370 C  CA  . ILE   B 1 920  ? 73.11500   86.82900  8.46800   1.000 44.40405  ?  918  ILE   B CA  1 
ATOM   21371 C  C   . ILE   B 1 920  ? 74.08400   86.85400  7.29400   1.000 39.87505  ?  918  ILE   B C   1 
ATOM   21372 O  O   . ILE   B 1 920  ? 74.38300   87.91400  6.73200   1.000 52.63611  ?  918  ILE   B O   1 
ATOM   21373 C  CB  . ILE   B 1 920  ? 73.85100   86.61100  9.80300   1.000 50.31180  ?  918  ILE   B CB  1 
ATOM   21374 C  CG1 . ILE   B 1 920  ? 72.90100   86.82300  10.98100  1.000 43.28456  ?  918  ILE   B CG1 1 
ATOM   21375 C  CG2 . ILE   B 1 920  ? 75.05600   87.53200  9.91800   1.000 41.12319  ?  918  ILE   B CG2 1 
ATOM   21376 C  CD1 . ILE   B 1 920  ? 73.42300   86.25000  12.27700  1.000 40.31457  ?  918  ILE   B CD1 1 
ATOM   21377 N  N   . LEU   B 1 921  ? 74.58100   85.68000  6.90100   1.000 37.29570  ?  919  LEU   B N   1 
ATOM   21378 C  CA  . LEU   B 1 921  ? 75.51800   85.60400  5.78400   1.000 38.39233  ?  919  LEU   B CA  1 
ATOM   21379 C  C   . LEU   B 1 921  ? 74.89300   86.12700  4.49700   1.000 46.80849  ?  919  LEU   B C   1 
ATOM   21380 O  O   . LEU   B 1 921  ? 75.55400   86.82200  3.71600   1.000 49.93467  ?  919  LEU   B O   1 
ATOM   21381 C  CB  . LEU   B 1 921  ? 75.99400   84.16400  5.60200   1.000 30.92947  ?  919  LEU   B CB  1 
ATOM   21382 C  CG  . LEU   B 1 921  ? 77.15200   83.95300  4.63100   1.000 32.25030  ?  919  LEU   B CG  1 
ATOM   21383 C  CD1 . LEU   B 1 921  ? 78.37900   84.71600  5.09700   1.000 53.89260  ?  919  LEU   B CD1 1 
ATOM   21384 C  CD2 . LEU   B 1 921  ? 77.45700   82.47200  4.50100   1.000 45.09555  ?  919  LEU   B CD2 1 
ATOM   21385 N  N   . ALA   B 1 922  ? 73.61800   85.80700  4.25900   1.000 45.77936  ?  920  ALA   B N   1 
ATOM   21386 C  CA  . ALA   B 1 922  ? 72.95000   86.28200  3.05100   1.000 42.54666  ?  920  ALA   B CA  1 
ATOM   21387 C  C   . ALA   B 1 922  ? 72.77900   87.79400  3.07100   1.000 45.27601  ?  920  ALA   B C   1 
ATOM   21388 O  O   . ALA   B 1 922  ? 72.99000   88.46300  2.05200   1.000 36.05244  ?  920  ALA   B O   1 
ATOM   21389 C  CB  . ALA   B 1 922  ? 71.59300   85.59400  2.89500   1.000 49.30315  ?  920  ALA   B CB  1 
ATOM   21390 N  N   . ARG   B 1 923  ? 72.39500   88.34800  4.22300   1.000 51.74476  ?  921  ARG   B N   1 
ATOM   21391 C  CA  . ARG   B 1 923  ? 72.21600   89.79100  4.33900   1.000 42.40535  ?  921  ARG   B CA  1 
ATOM   21392 C  C   . ARG   B 1 923  ? 73.54000   90.53100  4.17800   1.000 50.99961  ?  921  ARG   B C   1 
ATOM   21393 O  O   . ARG   B 1 923  ? 73.59300   91.58400  3.53200   1.000 47.88544  ?  921  ARG   B O   1 
ATOM   21394 C  CB  . ARG   B 1 923  ? 71.57200   90.12400  5.68400   1.000 35.40929  ?  921  ARG   B CB  1 
ATOM   21395 C  CG  . ARG   B 1 923  ? 71.39000   91.60700  5.94700   1.000 56.18966  ?  921  ARG   B CG  1 
ATOM   21396 C  CD  . ARG   B 1 923  ? 71.58500   91.92100  7.42300   1.000 62.04968  ?  921  ARG   B CD  1 
ATOM   21397 N  NE  . ARG   B 1 923  ? 70.78800   91.04800  8.27600   1.000 49.23446  ?  921  ARG   B NE  1 
ATOM   21398 C  CZ  . ARG   B 1 923  ? 71.14700   90.65900  9.49200   1.000 66.15587  ?  921  ARG   B CZ  1 
ATOM   21399 N  NH1 . ARG   B 1 923  ? 72.28500   91.05600  10.03700  1.000 74.87453  ?  921  ARG   B NH1 1 
ATOM   21400 N  NH2 . ARG   B 1 923  ? 70.34500   89.84700  10.17700  1.000 64.24762  ?  921  ARG   B NH2 1 
ATOM   21401 N  N   . GLU   B 1 924  ? 74.62100   89.99400  4.74800   1.000 42.94965  ?  922  GLU   B N   1 
ATOM   21402 C  CA  . GLU   B 1 924  ? 75.91100   90.67200  4.67600   1.000 42.78201  ?  922  GLU   B CA  1 
ATOM   21403 C  C   . GLU   B 1 924  ? 76.54000   90.54700  3.29300   1.000 53.33355  ?  922  GLU   B C   1 
ATOM   21404 O  O   . GLU   B 1 924  ? 77.19600   91.48400  2.82300   1.000 57.39258  ?  922  GLU   B O   1 
ATOM   21405 C  CB  . GLU   B 1 924  ? 76.85200   90.12300  5.75000   1.000 40.08561  ?  922  GLU   B CB  1 
ATOM   21406 C  CG  . GLU   B 1 924  ? 76.39700   90.43100  7.16900   1.000 41.99225  ?  922  GLU   B CG  1 
ATOM   21407 C  CD  . GLU   B 1 924  ? 77.51300   90.30900  8.18500   1.000 49.08724  ?  922  GLU   B CD  1 
ATOM   21408 O  OE1 . GLU   B 1 924  ? 78.65800   90.02000  7.78100   1.000 59.88619  ?  922  GLU   B OE1 1 
ATOM   21409 O  OE2 . GLU   B 1 924  ? 77.24200   90.49500  9.39000   1.000 59.08917  -1 922  GLU   B OE2 1 
ATOM   21410 N  N   . LEU   B 1 925  ? 76.35800   89.40400  2.62700   1.000 52.40246  ?  923  LEU   B N   1 
ATOM   21411 C  CA  . LEU   B 1 925  ? 76.85500   89.26400  1.26100   1.000 47.39051  ?  923  LEU   B CA  1 
ATOM   21412 C  C   . LEU   B 1 925  ? 76.11300   90.19400  0.31000   1.000 49.01357  ?  923  LEU   B C   1 
ATOM   21413 O  O   . LEU   B 1 925  ? 76.71800   90.77600  -0.59900  1.000 47.18501  ?  923  LEU   B O   1 
ATOM   21414 C  CB  . LEU   B 1 925  ? 76.72500   87.81500  0.79700   1.000 46.95834  ?  923  LEU   B CB  1 
ATOM   21415 C  CG  . LEU   B 1 925  ? 77.08000   87.57200  -0.66900  1.000 44.04514  ?  923  LEU   B CG  1 
ATOM   21416 C  CD1 . LEU   B 1 925  ? 78.55500   87.84700  -0.90500  1.000 33.36832  ?  923  LEU   B CD1 1 
ATOM   21417 C  CD2 . LEU   B 1 925  ? 76.70400   86.15800  -1.09000  1.000 38.55008  ?  923  LEU   B CD2 1 
ATOM   21418 N  N   . GLN   B 1 926  ? 74.80100   90.34200  0.50300   1.000 45.63834  ?  924  GLN   B N   1 
ATOM   21419 C  CA  . GLN   B 1 926  ? 74.03700   91.28000  -0.31100  1.000 46.52374  ?  924  GLN   B CA  1 
ATOM   21420 C  C   . GLN   B 1 926  ? 74.52000   92.70900  -0.10000  1.000 46.58258  ?  924  GLN   B C   1 
ATOM   21421 O  O   . GLN   B 1 926  ? 74.57400   93.49900  -1.04900  1.000 63.58501  ?  924  GLN   B O   1 
ATOM   21422 C  CB  . GLN   B 1 926  ? 72.54700   91.16100  0.01100   1.000 40.32279  ?  924  GLN   B CB  1 
ATOM   21423 C  CG  . GLN   B 1 926  ? 71.63400   91.68400  -1.08300  1.000 31.72247  ?  924  GLN   B CG  1 
ATOM   21424 C  CD  . GLN   B 1 926  ? 70.17500   91.70200  -0.67000  1.000 46.06847  ?  924  GLN   B CD  1 
ATOM   21425 O  OE1 . GLN   B 1 926  ? 69.33500   91.05300  -1.29400  1.000 51.34226  ?  924  GLN   B OE1 1 
ATOM   21426 N  NE2 . GLN   B 1 926  ? 69.86700   92.44800  0.38400   1.000 37.88881  ?  924  GLN   B NE2 1 
ATOM   21427 N  N   . ALA   B 1 927  ? 74.88000   93.05800  1.13700   1.000 48.83751  ?  925  ALA   B N   1 
ATOM   21428 C  CA  . ALA   B 1 927  ? 75.38000   94.40300  1.40300   1.000 47.91727  ?  925  ALA   B CA  1 
ATOM   21429 C  C   . ALA   B 1 927  ? 76.73400   94.62900  0.74400   1.000 55.53966  ?  925  ALA   B C   1 
ATOM   21430 O  O   . ALA   B 1 927  ? 76.96800   95.68200  0.14100   1.000 54.56993  ?  925  ALA   B O   1 
ATOM   21431 C  CB  . ALA   B 1 927  ? 75.47100   94.64300  2.90900   1.000 50.42634  ?  925  ALA   B CB  1 
ATOM   21432 N  N   . LEU   B 1 928  ? 77.63700   93.65200  0.84600   1.000 45.86247  ?  926  LEU   B N   1 
ATOM   21433 C  CA  . LEU   B 1 928  ? 78.95300   93.80300  0.23600   1.000 43.97341  ?  926  LEU   B CA  1 
ATOM   21434 C  C   . LEU   B 1 928  ? 78.86300   93.88500  -1.28100  1.000 46.12413  ?  926  LEU   B C   1 
ATOM   21435 O  O   . LEU   B 1 928  ? 79.65800   94.59200  -1.91100  1.000 61.22359  ?  926  LEU   B O   1 
ATOM   21436 C  CB  . LEU   B 1 928  ? 79.85900   92.64600  0.65300   1.000 42.49403  ?  926  LEU   B CB  1 
ATOM   21437 C  CG  . LEU   B 1 928  ? 80.35900   92.67700  2.09600   1.000 40.80552  ?  926  LEU   B CG  1 
ATOM   21438 C  CD1 . LEU   B 1 928  ? 80.92500   91.32600  2.49200   1.000 46.07815  ?  926  LEU   B CD1 1 
ATOM   21439 C  CD2 . LEU   B 1 928  ? 81.39700   93.77000  2.27300   1.000 42.40866  ?  926  LEU   B CD2 1 
ATOM   21440 N  N   . LEU   B 1 929  ? 77.90500   93.18000  -1.88600  1.000 49.00320  ?  927  LEU   B N   1 
ATOM   21441 C  CA  . LEU   B 1 929  ? 77.78300   93.20400  -3.33900  1.000 58.77176  ?  927  LEU   B CA  1 
ATOM   21442 C  C   . LEU   B 1 929  ? 77.24400   94.53900  -3.83600  1.000 55.05017  ?  927  LEU   B C   1 
ATOM   21443 O  O   . LEU   B 1 929  ? 77.51200   94.92700  -4.97900  1.000 67.74637  ?  927  LEU   B O   1 
ATOM   21444 C  CB  . LEU   B 1 929  ? 76.88700   92.05800  -3.80700  1.000 63.60220  ?  927  LEU   B CB  1 
ATOM   21445 C  CG  . LEU   B 1 929  ? 77.51900   90.66600  -3.78900  1.000 46.65212  ?  927  LEU   B CG  1 
ATOM   21446 C  CD1 . LEU   B 1 929  ? 76.49100   89.60900  -4.15400  1.000 48.76982  ?  927  LEU   B CD1 1 
ATOM   21447 C  CD2 . LEU   B 1 929  ? 78.70500   90.61000  -4.73200  1.000 48.38295  ?  927  LEU   B CD2 1 
ATOM   21448 N  N   . GLY   B 1 930  ? 76.49000   95.24900  -3.00100  1.000 41.30932  ?  928  GLY   B N   1 
ATOM   21449 C  CA  . GLY   B 1 930  ? 75.97100   96.55400  -3.35900  1.000 53.44623  ?  928  GLY   B CA  1 
ATOM   21450 C  C   . GLY   B 1 930  ? 76.88400   97.68200  -2.92600  1.000 65.18361  ?  928  GLY   B C   1 
ATOM   21451 O  O   . GLY   B 1 930  ? 76.44800   98.83100  -2.79700  1.000 51.77772  ?  928  GLY   B O   1 
ATOM   21452 N  N   . GLN   B 1 931  ? 78.15700   97.35400  -2.69600  1.000 56.90606  ?  929  GLN   B N   1 
ATOM   21453 C  CA  . GLN   B 1 931  ? 79.17200   98.32800  -2.29200  1.000 57.15541  ?  929  GLN   B CA  1 
ATOM   21454 C  C   . GLN   B 1 931  ? 78.73300   99.11700  -1.06000  1.000 56.77643  ?  929  GLN   B C   1 
ATOM   21455 O  O   . GLN   B 1 931  ? 78.89100   100.33700 -0.98200  1.000 74.78459  ?  929  GLN   B O   1 
ATOM   21456 C  CB  . GLN   B 1 931  ? 79.52700   99.26300  -3.45100  1.000 72.67905  ?  929  GLN   B CB  1 
ATOM   21457 C  CG  . GLN   B 1 931  ? 80.02000   98.54700  -4.70700  1.000 70.48388  ?  929  GLN   B CG  1 
ATOM   21458 C  CD  . GLN   B 1 931  ? 81.35100   97.84300  -4.50100  1.000 90.42282  ?  929  GLN   B CD  1 
ATOM   21459 O  OE1 . GLN   B 1 931  ? 81.60900   96.79400  -5.09200  1.000 92.23180  ?  929  GLN   B OE1 1 
ATOM   21460 N  NE2 . GLN   B 1 931  ? 82.20200   98.41800  -3.65900  1.000 102.89930 ?  929  GLN   B NE2 1 
ATOM   21461 N  N   . GLN   B 1 932  ? 78.17300   98.40800  -0.08800  1.000 59.98877  ?  930  GLN   B N   1 
ATOM   21462 C  CA  . GLN   B 1 932  ? 77.80500   98.97300  1.19900   1.000 62.14096  ?  930  GLN   B CA  1 
ATOM   21463 C  C   . GLN   B 1 932  ? 78.93600   98.76200  2.20100   1.000 75.17165  ?  930  GLN   B C   1 
ATOM   21464 O  O   . GLN   B 1 932  ? 79.79400   97.89400  2.03100   1.000 69.33349  ?  930  GLN   B O   1 
ATOM   21465 C  CB  . GLN   B 1 932  ? 76.51900   98.32500  1.70300   1.000 55.81208  ?  930  GLN   B CB  1 
ATOM   21466 C  CG  . GLN   B 1 932  ? 75.45500   99.28300  2.17800   1.000 58.84313  ?  930  GLN   B CG  1 
ATOM   21467 C  CD  . GLN   B 1 932  ? 74.06500   98.67900  2.04300   1.000 87.23925  ?  930  GLN   B CD  1 
ATOM   21468 O  OE1 . GLN   B 1 932  ? 73.64800   98.30900  0.94800   1.000 98.02258  ?  930  GLN   B OE1 1 
ATOM   21469 N  NE2 . GLN   B 1 932  ? 73.36000   98.54100  3.15700   1.000 94.70491  ?  930  GLN   B NE2 1 
ATOM   21470 N  N   . VAL   B 1 933  ? 78.93400   99.57800  3.25000   1.000 75.15032  ?  931  VAL   B N   1 
ATOM   21471 C  CA  . VAL   B 1 933  ? 79.91100   99.46800  4.32700   1.000 81.22063  ?  931  VAL   B CA  1 
ATOM   21472 C  C   . VAL   B 1 933  ? 79.27200   98.70500  5.47800   1.000 85.58097  ?  931  VAL   B C   1 
ATOM   21473 O  O   . VAL   B 1 933  ? 78.12800   98.98500  5.85900   1.000 91.72715  ?  931  VAL   B O   1 
ATOM   21474 C  CB  . VAL   B 1 933  ? 80.40400   100.85200 4.78200   1.000 80.68015  ?  931  VAL   B CB  1 
ATOM   21475 C  CG1 . VAL   B 1 933  ? 81.75200   100.72700 5.47600   1.000 72.18734  ?  931  VAL   B CG1 1 
ATOM   21476 C  CG2 . VAL   B 1 933  ? 80.49400   101.79700 3.59100   1.000 90.43317  ?  931  VAL   B CG2 1 
ATOM   21477 N  N   . LEU   B 1 934  ? 80.00200   97.74100  6.02800   1.000 75.02533  ?  932  LEU   B N   1 
ATOM   21478 C  CA  . LEU   B 1 934  ? 79.49100   96.87100  7.07800   1.000 67.36971  ?  932  LEU   B CA  1 
ATOM   21479 C  C   . LEU   B 1 934  ? 80.09500   97.26700  8.41800   1.000 77.66330  ?  932  LEU   B C   1 
ATOM   21480 O  O   . LEU   B 1 934  ? 81.31600   97.42400  8.53400   1.000 75.75276  ?  932  LEU   B O   1 
ATOM   21481 C  CB  . LEU   B 1 934  ? 79.80000   95.40500  6.77000   1.000 54.94047  ?  932  LEU   B CB  1 
ATOM   21482 C  CG  . LEU   B 1 934  ? 78.81000   94.72000  5.82900   1.000 52.34692  ?  932  LEU   B CG  1 
ATOM   21483 C  CD1 . LEU   B 1 934  ? 79.28700   93.32300  5.48400   1.000 53.27460  ?  932  LEU   B CD1 1 
ATOM   21484 C  CD2 . LEU   B 1 934  ? 77.42700   94.67900  6.45400   1.000 55.74592  ?  932  LEU   B CD2 1 
ATOM   21485 N  N   . SER   B 1 935  ? 79.24000   97.42600  9.41900   1.000 70.21483  ?  933  SER   B N   1 
ATOM   21486 C  CA  . SER   B 1 935  ? 79.71000   97.74300  10.76100  1.000 69.42229  ?  933  SER   B CA  1 
ATOM   21487 C  C   . SER   B 1 935  ? 80.41800   96.53200  11.36000  1.000 74.90407  ?  933  SER   B C   1 
ATOM   21488 O  O   . SER   B 1 935  ? 79.83800   95.44100  11.39700  1.000 74.85303  ?  933  SER   B O   1 
ATOM   21489 C  CB  . SER   B 1 935  ? 78.53900   98.16300  11.64400  1.000 87.36125  ?  933  SER   B CB  1 
ATOM   21490 O  OG  . SER   B 1 935  ? 77.45400   97.25900  11.50800  1.000 83.77602  ?  933  SER   B OG  1 
ATOM   21491 N  N   . PRO   B 1 936  ? 81.65600   96.67900  11.83700  1.000 81.48053  ?  934  PRO   B N   1 
ATOM   21492 C  CA  . PRO   B 1 936  ? 82.39800   95.52400  12.36000  1.000 76.68044  ?  934  PRO   B CA  1 
ATOM   21493 C  C   . PRO   B 1 936  ? 81.67900   94.84100  13.51600  1.000 72.21620  ?  934  PRO   B C   1 
ATOM   21494 O  O   . PRO   B 1 936  ? 80.86900   95.43800  14.23000  1.000 56.49962  ?  934  PRO   B O   1 
ATOM   21495 C  CB  . PRO   B 1 936  ? 83.72800   96.13400  12.81800  1.000 60.02216  ?  934  PRO   B CB  1 
ATOM   21496 C  CG  . PRO   B 1 936  ? 83.87900   97.36400  11.98200  1.000 69.05327  ?  934  PRO   B CG  1 
ATOM   21497 C  CD  . PRO   B 1 936  ? 82.48600   97.89600  11.79200  1.000 63.46360  ?  934  PRO   B CD  1 
ATOM   21498 N  N   . VAL   B 1 937  ? 81.99600   93.55900  13.69400  1.000 68.24453  ?  935  VAL   B N   1 
ATOM   21499 C  CA  . VAL   B 1 937  ? 81.36200   92.74000  14.72100  1.000 60.31944  ?  935  VAL   B CA  1 
ATOM   21500 C  C   . VAL   B 1 937  ? 82.05900   92.96900  16.05300  1.000 61.81947  ?  935  VAL   B C   1 
ATOM   21501 O  O   . VAL   B 1 937  ? 83.28700   93.10300  16.12000  1.000 70.02639  ?  935  VAL   B O   1 
ATOM   21502 C  CB  . VAL   B 1 937  ? 81.39200   91.25400  14.32200  1.000 54.75044  ?  935  VAL   B CB  1 
ATOM   21503 C  CG1 . VAL   B 1 937  ? 80.57200   90.42000  15.29900  1.000 59.72898  ?  935  VAL   B CG1 1 
ATOM   21504 C  CG2 . VAL   B 1 937  ? 80.87900   91.08200  12.90200  1.000 55.12271  ?  935  VAL   B CG2 1 
ATOM   21505 N  N   . GLU   B 1 938  ? 81.26900   93.00600  17.12400  1.000 68.26388  ?  936  GLU   B N   1 
ATOM   21506 C  CA  . GLU   B 1 938  ? 81.76600   93.31400  18.45800  1.000 70.08784  ?  936  GLU   B CA  1 
ATOM   21507 C  C   . GLU   B 1 938  ? 81.93600   92.08700  19.34300  1.000 76.55958  ?  936  GLU   B C   1 
ATOM   21508 O  O   . GLU   B 1 938  ? 82.77700   92.10700  20.24800  1.000 90.16609  ?  936  GLU   B O   1 
ATOM   21509 C  CB  . GLU   B 1 938  ? 80.82400   94.31400  19.14600  1.000 62.50559  ?  936  GLU   B CB  1 
ATOM   21510 C  CG  . GLU   B 1 938  ? 79.54200   93.71800  19.74500  1.000 91.89036  ?  936  GLU   B CG  1 
ATOM   21511 C  CD  . GLU   B 1 938  ? 78.70400   92.90900  18.75500  1.000 101.41569 ?  936  GLU   B CD  1 
ATOM   21512 O  OE1 . GLU   B 1 938  ? 78.87200   93.07700  17.52800  1.000 100.52784 ?  936  GLU   B OE1 1 
ATOM   21513 O  OE2 . GLU   B 1 938  ? 77.87200   92.09600  19.21300  1.000 95.47729  -1 936  GLU   B OE2 1 
ATOM   21514 N  N   . LYS   B 1 939  ? 81.17800   91.02100  19.10400  1.000 63.88251  ?  937  LYS   B N   1 
ATOM   21515 C  CA  . LYS   B 1 939  ? 81.23000   89.81500  19.91700  1.000 57.21582  ?  937  LYS   B CA  1 
ATOM   21516 C  C   . LYS   B 1 939  ? 81.78900   88.65100  19.10700  1.000 60.66913  ?  937  LYS   B C   1 
ATOM   21517 O  O   . LYS   B 1 939  ? 81.95300   88.72600  17.88600  1.000 62.27894  ?  937  LYS   B O   1 
ATOM   21518 C  CB  . LYS   B 1 939  ? 79.84000   89.46400  20.46300  1.000 71.61697  ?  937  LYS   B CB  1 
ATOM   21519 C  CG  . LYS   B 1 939  ? 79.22600   90.52800  21.35900  1.000 72.30135  ?  937  LYS   B CG  1 
ATOM   21520 C  CD  . LYS   B 1 939  ? 80.24100   91.12000  22.32400  1.000 64.57520  ?  937  LYS   B CD  1 
ATOM   21521 C  CE  . LYS   B 1 939  ? 79.54900   91.70700  23.54300  1.000 63.56558  ?  937  LYS   B CE  1 
ATOM   21522 N  NZ  . LYS   B 1 939  ? 80.36200   92.77000  24.19500  1.000 65.47264  ?  937  LYS   B NZ  1 
ATOM   21523 N  N   . THR   B 1 940  ? 82.08700   87.56200  19.81300  1.000 65.08993  ?  938  THR   B N   1 
ATOM   21524 C  CA  . THR   B 1 940  ? 82.64100   86.36200  19.20400  1.000 61.61740  ?  938  THR   B CA  1 
ATOM   21525 C  C   . THR   B 1 940  ? 81.96100   85.14000  19.80500  1.000 60.15826  ?  938  THR   B C   1 
ATOM   21526 O  O   . THR   B 1 940  ? 81.41900   85.19000  20.91100  1.000 54.90329  ?  938  THR   B O   1 
ATOM   21527 C  CB  . THR   B 1 940  ? 84.15900   86.27000  19.41100  1.000 61.22607  ?  938  THR   B CB  1 
ATOM   21528 O  OG1 . THR   B 1 940  ? 84.46400   86.46300  20.79800  1.000 78.33735  ?  938  THR   B OG1 1 
ATOM   21529 C  CG2 . THR   B 1 940  ? 84.87600   87.33100  18.59000  1.000 57.70991  ?  938  THR   B CG2 1 
ATOM   21530 N  N   . TYR   B 1 941  ? 81.99600   84.03300  19.05900  1.000 67.01557  ?  939  TYR   B N   1 
ATOM   21531 C  CA  . TYR   B 1 941  ? 81.40600   82.79500  19.55900  1.000 54.97577  ?  939  TYR   B CA  1 
ATOM   21532 C  C   . TYR   B 1 941  ? 82.16300   82.27700  20.77600  1.000 68.87625  ?  939  TYR   B C   1 
ATOM   21533 O  O   . TYR   B 1 941  ? 81.54500   81.81500  21.74400  1.000 62.39871  ?  939  TYR   B O   1 
ATOM   21534 C  CB  . TYR   B 1 941  ? 81.37500   81.73700  18.45300  1.000 67.03143  ?  939  TYR   B CB  1 
ATOM   21535 C  CG  . TYR   B 1 941  ? 80.45400   80.56200  18.73400  1.000 53.60740  ?  939  TYR   B CG  1 
ATOM   21536 C  CD1 . TYR   B 1 941  ? 80.77900   79.60900  19.69200  1.000 72.92673  ?  939  TYR   B CD1 1 
ATOM   21537 C  CD2 . TYR   B 1 941  ? 79.26300   80.40700  18.03900  1.000 59.02172  ?  939  TYR   B CD2 1 
ATOM   21538 C  CE1 . TYR   B 1 941  ? 79.94200   78.54100  19.95400  1.000 74.27797  ?  939  TYR   B CE1 1 
ATOM   21539 C  CE2 . TYR   B 1 941  ? 78.42000   79.33700  18.29300  1.000 73.13481  ?  939  TYR   B CE2 1 
ATOM   21540 C  CZ  . TYR   B 1 941  ? 78.76600   78.40700  19.25100  1.000 78.26664  ?  939  TYR   B CZ  1 
ATOM   21541 O  OH  . TYR   B 1 941  ? 77.93500   77.34000  19.50900  1.000 70.67085  ?  939  TYR   B OH  1 
ATOM   21542 N  N   . LYS   B 1 942  ? 83.49900   82.34600  20.74500  1.000 61.46644  ?  940  LYS   B N   1 
ATOM   21543 C  CA  . LYS   B 1 942  ? 84.30400   81.88400  21.87300  1.000 64.36934  ?  940  LYS   B CA  1 
ATOM   21544 C  C   . LYS   B 1 942  ? 83.84800   82.52000  23.18200  1.000 61.35694  ?  940  LYS   B C   1 
ATOM   21545 O  O   . LYS   B 1 942  ? 83.85700   81.87000  24.23500  1.000 70.23436  ?  940  LYS   B O   1 
ATOM   21546 C  CB  . LYS   B 1 942  ? 85.78100   82.18900  21.61300  1.000 46.10553  ?  940  LYS   B CB  1 
ATOM   21547 C  CG  . LYS   B 1 942  ? 86.05100   83.66100  21.34900  1.000 61.78673  ?  940  LYS   B CG  1 
ATOM   21548 C  CD  . LYS   B 1 942  ? 87.43300   83.91700  20.77500  1.000 50.07310  ?  940  LYS   B CD  1 
ATOM   21549 C  CE  . LYS   B 1 942  ? 87.66500   85.41400  20.60700  1.000 56.54229  ?  940  LYS   B CE  1 
ATOM   21550 N  NZ  . LYS   B 1 942  ? 88.97200   85.72400  19.96800  1.000 61.11976  ?  940  LYS   B NZ  1 
ATOM   21551 N  N   . SER   B 1 943  ? 83.42500   83.78500  23.13200  1.000 53.77894  ?  941  SER   B N   1 
ATOM   21552 C  CA  . SER   B 1 943  ? 82.94800   84.45900  24.33400  1.000 54.38722  ?  941  SER   B CA  1 
ATOM   21553 C  C   . SER   B 1 943  ? 81.60400   83.90200  24.78600  1.000 67.86616  ?  941  SER   B C   1 
ATOM   21554 O  O   . SER   B 1 943  ? 81.35200   83.77900  25.99100  1.000 84.53006  ?  941  SER   B O   1 
ATOM   21555 C  CB  . SER   B 1 943  ? 82.85200   85.96100  24.08200  1.000 56.38168  ?  941  SER   B CB  1 
ATOM   21556 O  OG  . SER   B 1 943  ? 84.02200   86.42900  23.43600  1.000 63.32592  ?  941  SER   B OG  1 
ATOM   21557 N  N   . PHE   B 1 944  ? 80.72100   83.56900  23.83800  1.000 67.02645  ?  942  PHE   B N   1 
ATOM   21558 C  CA  . PHE   B 1 944  ? 79.46500   82.92700  24.20800  1.000 58.75771  ?  942  PHE   B CA  1 
ATOM   21559 C  C   . PHE   B 1 944  ? 79.69600   81.52100  24.73900  1.000 62.45975  ?  942  PHE   B C   1 
ATOM   21560 O  O   . PHE   B 1 944  ? 78.96500   81.07000  25.62900  1.000 53.59868  ?  942  PHE   B O   1 
ATOM   21561 C  CB  . PHE   B 1 944  ? 78.51000   82.88200  23.01200  1.000 51.36774  ?  942  PHE   B CB  1 
ATOM   21562 C  CG  . PHE   B 1 944  ? 77.21800   82.15500  23.29400  1.000 52.58109  ?  942  PHE   B CG  1 
ATOM   21563 C  CD1 . PHE   B 1 944  ? 76.18800   82.78200  23.97900  1.000 62.74655  ?  942  PHE   B CD1 1 
ATOM   21564 C  CD2 . PHE   B 1 944  ? 77.03800   80.84200  22.88300  1.000 46.49803  ?  942  PHE   B CD2 1 
ATOM   21565 C  CE1 . PHE   B 1 944  ? 74.99900   82.11800  24.24200  1.000 62.26259  ?  942  PHE   B CE1 1 
ATOM   21566 C  CE2 . PHE   B 1 944  ? 75.85400   80.17200  23.14500  1.000 45.54094  ?  942  PHE   B CE2 1 
ATOM   21567 C  CZ  . PHE   B 1 944  ? 74.83200   80.81200  23.82500  1.000 53.78152  ?  942  PHE   B CZ  1 
ATOM   21568 N  N   . ALA   B 1 945  ? 80.69700   80.81800  24.20000  1.000 59.97933  ?  943  ALA   B N   1 
ATOM   21569 C  CA  . ALA   B 1 945  ? 80.99100   79.46200  24.65500  1.000 64.55355  ?  943  ALA   B CA  1 
ATOM   21570 C  C   . ALA   B 1 945  ? 81.24500   79.43100  26.15600  1.000 71.95085  ?  943  ALA   B C   1 
ATOM   21571 O  O   . ALA   B 1 945  ? 80.60000   78.67400  26.89000  1.000 59.90575  ?  943  ALA   B O   1 
ATOM   21572 C  CB  . ALA   B 1 945  ? 82.19100   78.90300  23.89000  1.000 66.82227  ?  943  ALA   B CB  1 
ATOM   21573 N  N   . ARG   B 1 946  ? 82.17700   80.26100  26.63100  1.000 71.46208  ?  944  ARG   B N   1 
ATOM   21574 C  CA  . ARG   B 1 946  ? 82.46900   80.30700  28.06100  1.000 70.08771  ?  944  ARG   B CA  1 
ATOM   21575 C  C   . ARG   B 1 946  ? 81.23000   80.68800  28.86200  1.000 70.17808  ?  944  ARG   B C   1 
ATOM   21576 O  O   . ARG   B 1 946  ? 80.93700   80.07900  29.89800  1.000 70.18650  ?  944  ARG   B O   1 
ATOM   21577 C  CB  . ARG   B 1 946  ? 83.61100   81.28600  28.33200  1.000 64.44307  ?  944  ARG   B CB  1 
ATOM   21578 N  N   . TRP   B 1 947  ? 80.48000   81.69000  28.38700  1.000 60.41735  ?  945  TRP   B N   1 
ATOM   21579 C  CA  . TRP   B 1 947  ? 79.29700   82.15000  29.11100  1.000 63.70710  ?  945  TRP   B CA  1 
ATOM   21580 C  C   . TRP   B 1 947  ? 78.30700   81.01400  29.33700  1.000 69.24658  ?  945  TRP   B C   1 
ATOM   21581 O  O   . TRP   B 1 947  ? 77.75600   80.86900  30.43500  1.000 70.26471  ?  945  TRP   B O   1 
ATOM   21582 C  CB  . TRP   B 1 947  ? 78.62600   83.29900  28.35500  1.000 52.40518  ?  945  TRP   B CB  1 
ATOM   21583 C  CG  . TRP   B 1 947  ? 77.36200   83.80200  29.00800  1.000 58.83752  ?  945  TRP   B CG  1 
ATOM   21584 C  CD1 . TRP   B 1 947  ? 77.25500   84.81400  29.91800  1.000 66.02252  ?  945  TRP   B CD1 1 
ATOM   21585 C  CD2 . TRP   B 1 947  ? 76.03100   83.31100  28.79800  1.000 62.53055  ?  945  TRP   B CD2 1 
ATOM   21586 N  NE1 . TRP   B 1 947  ? 75.94200   84.98300  30.28800  1.000 62.59456  ?  945  TRP   B NE1 1 
ATOM   21587 C  CE2 . TRP   B 1 947  ? 75.17100   84.07200  29.61500  1.000 64.27077  ?  945  TRP   B CE2 1 
ATOM   21588 C  CE3 . TRP   B 1 947  ? 75.48400   82.30100  28.00000  1.000 59.87192  ?  945  TRP   B CE3 1 
ATOM   21589 C  CZ2 . TRP   B 1 947  ? 73.79400   83.85600  29.65600  1.000 68.01186  ?  945  TRP   B CZ2 1 
ATOM   21590 C  CZ3 . TRP   B 1 947  ? 74.11800   82.08900  28.04300  1.000 69.05055  ?  945  TRP   B CZ3 1 
ATOM   21591 C  CH2 . TRP   B 1 947  ? 73.28900   82.86200  28.86500  1.000 60.34193  ?  945  TRP   B CH2 1 
ATOM   21592 N  N   . GLN   B 1 948  ? 78.07200   80.19300  28.31200  1.000 69.71377  ?  946  GLN   B N   1 
ATOM   21593 C  CA  . GLN   B 1 948  ? 77.13900   79.08300  28.46700  1.000 72.90107  ?  946  GLN   B CA  1 
ATOM   21594 C  C   . GLN   B 1 948  ? 77.71000   78.00800  29.38400  1.000 79.24138  ?  946  GLN   B C   1 
ATOM   21595 O  O   . GLN   B 1 948  ? 76.98000   77.42800  30.19700  1.000 88.41411  ?  946  GLN   B O   1 
ATOM   21596 C  CB  . GLN   B 1 948  ? 76.78400   78.50000  27.10200  1.000 65.79560  ?  946  GLN   B CB  1 
ATOM   21597 C  CG  . GLN   B 1 948  ? 75.31000   78.17800  26.94600  1.000 53.12786  ?  946  GLN   B CG  1 
ATOM   21598 C  CD  . GLN   B 1 948  ? 75.04600   77.23900  25.79400  1.000 49.69113  ?  946  GLN   B CD  1 
ATOM   21599 O  OE1 . GLN   B 1 948  ? 75.97500   76.69200  25.19900  1.000 57.97420  ?  946  GLN   B OE1 1 
ATOM   21600 N  NE2 . GLN   B 1 948  ? 73.77500   77.03900  25.47600  1.000 46.64216  ?  946  GLN   B NE2 1 
ATOM   21601 N  N   . ASN   B 1 949  ? 79.01100   77.72700  29.26800  1.000 61.91061  ?  947  ASN   B N   1 
ATOM   21602 C  CA  . ASN   B 1 949  ? 79.64600   76.80000  30.19800  1.000 67.09614  ?  947  ASN   B CA  1 
ATOM   21603 C  C   . ASN   B 1 949  ? 79.49800   77.28300  31.63600  1.000 73.20314  ?  947  ASN   B C   1 
ATOM   21604 O  O   . ASN   B 1 949  ? 79.23700   76.48700  32.54500  1.000 71.53685  ?  947  ASN   B O   1 
ATOM   21605 C  CB  . ASN   B 1 949  ? 81.12100   76.61800  29.83500  1.000 76.01186  ?  947  ASN   B CB  1 
ATOM   21606 C  CG  . ASN   B 1 949  ? 81.32100   76.22000  28.38200  1.000 73.43856  ?  947  ASN   B CG  1 
ATOM   21607 O  OD1 . ASN   B 1 949  ? 80.36800   75.87600  27.68400  1.000 72.57091  ?  947  ASN   B OD1 1 
ATOM   21608 N  ND2 . ASN   B 1 949  ? 82.56500   76.27200  27.91900  1.000 77.87380  ?  947  ASN   B ND2 1 
ATOM   21609 N  N   . GLU   B 1 950  ? 79.64600   78.59100  31.85900  1.000 75.38196  ?  948  GLU   B N   1 
ATOM   21610 C  CA  . GLU   B 1 950  ? 79.44000   79.13700  33.19600  1.000 74.55417  ?  948  GLU   B CA  1 
ATOM   21611 C  C   . GLU   B 1 950  ? 77.96700   79.09900  33.58500  1.000 76.55400  ?  948  GLU   B C   1 
ATOM   21612 O  O   . GLU   B 1 950  ? 77.63600   78.83000  34.74500  1.000 85.96425  ?  948  GLU   B O   1 
ATOM   21613 C  CB  . GLU   B 1 950  ? 79.98300   80.56500  33.27100  1.000 85.53667  ?  948  GLU   B CB  1 
ATOM   21614 C  CG  . GLU   B 1 950  ? 81.46900   80.68100  32.96400  1.000 95.69568  ?  948  GLU   B CG  1 
ATOM   21615 C  CD  . GLU   B 1 950  ? 81.90800   82.11400  32.71900  1.000 113.50948 ?  948  GLU   B CD  1 
ATOM   21616 O  OE1 . GLU   B 1 950  ? 81.09800   83.03600  32.95700  1.000 103.78926 ?  948  GLU   B OE1 1 
ATOM   21617 O  OE2 . GLU   B 1 950  ? 83.06300   82.31800  32.28500  1.000 119.83842 -1 948  GLU   B OE2 1 
ATOM   21618 N  N   . TRP   B 1 951  ? 77.06800   79.35400  32.62700  1.000 75.06092  ?  949  TRP   B N   1 
ATOM   21619 C  CA  . TRP   B 1 951  ? 75.63600   79.24200  32.88900  1.000 74.01368  ?  949  TRP   B CA  1 
ATOM   21620 C  C   . TRP   B 1 951  ? 75.24500   77.85400  33.36500  1.000 77.34645  ?  949  TRP   B C   1 
ATOM   21621 O  O   . TRP   B 1 951  ? 74.13000   77.67200  33.86700  1.000 73.26226  ?  949  TRP   B O   1 
ATOM   21622 C  CB  . TRP   B 1 951  ? 74.83100   79.59400  31.63200  1.000 63.65633  ?  949  TRP   B CB  1 
ATOM   21623 C  CG  . TRP   B 1 951  ? 73.33700   79.44700  31.79900  1.000 62.12791  ?  949  TRP   B CG  1 
ATOM   21624 C  CD1 . TRP   B 1 951  ? 72.49200   80.31500  32.42800  1.000 54.45279  ?  949  TRP   B CD1 1 
ATOM   21625 C  CD2 . TRP   B 1 951  ? 72.52300   78.36000  31.33800  1.000 69.91921  ?  949  TRP   B CD2 1 
ATOM   21626 N  NE1 . TRP   B 1 951  ? 71.20300   79.83900  32.38500  1.000 64.95848  ?  949  TRP   B NE1 1 
ATOM   21627 C  CE2 . TRP   B 1 951  ? 71.19400   78.64100  31.72000  1.000 69.39767  ?  949  TRP   B CE2 1 
ATOM   21628 C  CE3 . TRP   B 1 951  ? 72.78800   77.17800  30.63900  1.000 70.04437  ?  949  TRP   B CE3 1 
ATOM   21629 C  CZ2 . TRP   B 1 951  ? 70.13400   77.78400  31.42500  1.000 55.31833  ?  949  TRP   B CZ2 1 
ATOM   21630 C  CZ3 . TRP   B 1 951  ? 71.73400   76.32900  30.34600  1.000 72.77806  ?  949  TRP   B CZ3 1 
ATOM   21631 C  CH2 . TRP   B 1 951  ? 70.42400   76.63700  30.73900  1.000 69.45387  ?  949  TRP   B CH2 1 
ATOM   21632 N  N   . PHE   B 1 952  ? 76.14000   76.87700  33.24400  1.000 79.22323  ?  950  PHE   B N   1 
ATOM   21633 C  CA  . PHE   B 1 952  ? 75.76100   75.50900  33.55900  1.000 95.44356  ?  950  PHE   B CA  1 
ATOM   21634 C  C   . PHE   B 1 952  ? 75.66300   75.28600  35.06600  1.000 108.72358 ?  950  PHE   B C   1 
ATOM   21635 O  O   . PHE   B 1 952  ? 74.69100   74.69100  35.54600  1.000 97.33614  ?  950  PHE   B O   1 
ATOM   21636 C  CB  . PHE   B 1 952  ? 76.74200   74.54300  32.89900  1.000 89.87938  ?  950  PHE   B CB  1 
ATOM   21637 C  CG  . PHE   B 1 952  ? 76.51400   74.37900  31.42000  1.000 94.84431  ?  950  PHE   B CG  1 
ATOM   21638 C  CD1 . PHE   B 1 952  ? 75.26400   74.62700  30.86800  1.000 83.71768  ?  950  PHE   B CD1 1 
ATOM   21639 C  CD2 . PHE   B 1 952  ? 77.54200   73.98300  30.58100  1.000 91.30800  ?  950  PHE   B CD2 1 
ATOM   21640 C  CE1 . PHE   B 1 952  ? 75.04300   74.47900  29.50800  1.000 63.65456  ?  950  PHE   B CE1 1 
ATOM   21641 C  CE2 . PHE   B 1 952  ? 77.32900   73.83300  29.22000  1.000 75.62731  ?  950  PHE   B CE2 1 
ATOM   21642 C  CZ  . PHE   B 1 952  ? 76.07700   74.08100  28.68300  1.000 60.44773  ?  950  PHE   B CZ  1 
ATOM   21643 N  N   . ALA   B 1 953  ? 76.61700   75.80000  35.83900  1.000 97.06853  ?  951  ALA   B N   1 
ATOM   21644 C  CA  . ALA   B 1 953  ? 76.59400   75.59200  37.28500  1.000 66.35527  ?  951  ALA   B CA  1 
ATOM   21645 C  C   . ALA   B 1 953  ? 75.34700   76.18500  37.94300  1.000 72.33142  ?  951  ALA   B C   1 
ATOM   21646 O  O   . ALA   B 1 953  ? 75.13700   76.02100  39.15000  1.000 85.03219  ?  951  ALA   B O   1 
ATOM   21647 C  CB  . ALA   B 1 953  ? 77.85800   76.17500  37.92100  1.000 78.29861  ?  951  ALA   B CB  1 
ATOM   21648 N  N   . SER   B 1 954  ? 74.50300   76.85200  37.16000  1.000 67.41786  ?  952  SER   B N   1 
ATOM   21649 C  CA  . SER   B 1 954  ? 73.32000   77.50700  37.69300  1.000 75.16438  ?  952  SER   B CA  1 
ATOM   21650 C  C   . SER   B 1 954  ? 72.25200   76.49400  38.09600  1.000 71.28729  ?  952  SER   B C   1 
ATOM   21651 O  O   . SER   B 1 954  ? 72.26900   75.32600  37.69600  1.000 65.18181  ?  952  SER   B O   1 
ATOM   21652 C  CB  . SER   B 1 954  ? 72.73400   78.47200  36.66300  1.000 74.21044  ?  952  SER   B CB  1 
ATOM   21653 O  OG  . SER   B 1 954  ? 71.76500   77.82000  35.85800  1.000 69.77164  ?  952  SER   B OG  1 
ATOM   21654 N  N   . ASP   B 1 955  ? 71.30300   76.97000  38.90400  1.000 87.51897  ?  953  ASP   B N   1 
ATOM   21655 C  CA  . ASP   B 1 955  ? 70.13200   76.17300  39.24600  1.000 91.62161  ?  953  ASP   B CA  1 
ATOM   21656 C  C   . ASP   B 1 955  ? 69.11700   76.15300  38.11500  1.000 95.87955  ?  953  ASP   B C   1 
ATOM   21657 O  O   . ASP   B 1 955  ? 68.33000   75.20500  38.00800  1.000 94.70329  ?  953  ASP   B O   1 
ATOM   21658 C  CB  . ASP   B 1 955  ? 69.48000   76.70900  40.52200  1.000 94.33699  ?  953  ASP   B CB  1 
ATOM   21659 N  N   . GLU   B 1 956  ? 69.11700   77.18800  37.27100  1.000 102.68128 ?  954  GLU   B N   1 
ATOM   21660 C  CA  . GLU   B 1 956  ? 68.19900   77.21800  36.13900  1.000 92.51145  ?  954  GLU   B CA  1 
ATOM   21661 C  C   . GLU   B 1 956  ? 68.52500   76.11900  35.13500  1.000 88.77764  ?  954  GLU   B C   1 
ATOM   21662 O  O   . GLU   B 1 956  ? 67.61400   75.49800  34.57600  1.000 94.11830  ?  954  GLU   B O   1 
ATOM   21663 C  CB  . GLU   B 1 956  ? 68.22900   78.59300  35.47200  1.000 76.93940  ?  954  GLU   B CB  1 
ATOM   21664 C  CG  . GLU   B 1 956  ? 67.27400   78.72500  34.29800  1.000 97.88857  ?  954  GLU   B CG  1 
ATOM   21665 C  CD  . GLU   B 1 956  ? 67.14200   80.15400  33.81200  1.000 111.69294 ?  954  GLU   B CD  1 
ATOM   21666 O  OE1 . GLU   B 1 956  ? 68.06000   80.95900  34.07300  1.000 92.65561  ?  954  GLU   B OE1 1 
ATOM   21667 O  OE2 . GLU   B 1 956  ? 66.12000   80.47100  33.16700  1.000 124.68060 -1 954  GLU   B OE2 1 
ATOM   21668 N  N   . TYR   B 1 957  ? 69.81600   75.86700  34.89100  1.000 73.99576  ?  955  TYR   B N   1 
ATOM   21669 C  CA  . TYR   B 1 957  ? 70.22000   74.73600  34.06000  1.000 74.82509  ?  955  TYR   B CA  1 
ATOM   21670 C  C   . TYR   B 1 957  ? 69.60300   73.44700  34.59000  1.000 85.64961  ?  955  TYR   B C   1 
ATOM   21671 O  O   . TYR   B 1 957  ? 68.87700   72.74700  33.87700  1.000 79.06568  ?  955  TYR   B O   1 
ATOM   21672 C  CB  . TYR   B 1 957  ? 71.75000   74.63000  34.03100  1.000 69.27320  ?  955  TYR   B CB  1 
ATOM   21673 C  CG  . TYR   B 1 957  ? 72.34600   73.43000  33.28900  1.000 86.41678  ?  955  TYR   B CG  1 
ATOM   21674 C  CD1 . TYR   B 1 957  ? 71.60700   72.67700  32.37200  1.000 90.04677  ?  955  TYR   B CD1 1 
ATOM   21675 C  CD2 . TYR   B 1 957  ? 73.64500   73.01800  33.56400  1.000 91.82077  ?  955  TYR   B CD2 1 
ATOM   21676 C  CE1 . TYR   B 1 957  ? 72.17800   71.58600  31.72100  1.000 99.31350  ?  955  TYR   B CE1 1 
ATOM   21677 C  CE2 . TYR   B 1 957  ? 74.22100   71.94400  32.93100  1.000 94.57768  ?  955  TYR   B CE2 1 
ATOM   21678 C  CZ  . TYR   B 1 957  ? 73.48800   71.22700  32.01100  1.000 102.88661 ?  955  TYR   B CZ  1 
ATOM   21679 O  OH  . TYR   B 1 957  ? 74.07200   70.14800  31.38700  1.000 96.31729  ?  955  TYR   B OH  1 
ATOM   21680 N  N   . GLU   B 1 958  ? 69.87500   73.13000  35.85900  1.000 96.90684  ?  956  GLU   B N   1 
ATOM   21681 C  CA  . GLU   B 1 958  ? 69.35500   71.89700  36.43900  1.000 88.25112  ?  956  GLU   B CA  1 
ATOM   21682 C  C   . GLU   B 1 958  ? 67.83200   71.88500  36.43900  1.000 79.32516  ?  956  GLU   B C   1 
ATOM   21683 O  O   . GLU   B 1 958  ? 67.21400   70.82900  36.26100  1.000 87.93852  ?  956  GLU   B O   1 
ATOM   21684 C  CB  . GLU   B 1 958  ? 69.90000   71.71100  37.85400  1.000 81.92956  ?  956  GLU   B CB  1 
ATOM   21685 C  CG  . GLU   B 1 958  ? 71.02000   70.68700  37.94400  1.000 81.17614  ?  956  GLU   B CG  1 
ATOM   21686 C  CD  . GLU   B 1 958  ? 72.33200   71.19800  37.37800  1.000 90.06187  ?  956  GLU   B CD  1 
ATOM   21687 O  OE1 . GLU   B 1 958  ? 72.47300   72.42700  37.19100  1.000 75.71249  ?  956  GLU   B OE1 1 
ATOM   21688 O  OE2 . GLU   B 1 958  ? 73.22500   70.36300  37.12200  1.000 100.20892 -1 956  GLU   B OE2 1 
ATOM   21689 N  N   . GLN   B 1 959  ? 67.20900   73.05000  36.63100  1.000 69.81007  ?  957  GLN   B N   1 
ATOM   21690 C  CA  . GLN   B 1 959  ? 65.76300   73.14700  36.45200  1.000 88.62060  ?  957  GLN   B CA  1 
ATOM   21691 C  C   . GLN   B 1 959  ? 65.37800   72.80800  35.01800  1.000 102.95688 ?  957  GLN   B C   1 
ATOM   21692 O  O   . GLN   B 1 959  ? 64.43700   72.04200  34.77900  1.000 113.40221 ?  957  GLN   B O   1 
ATOM   21693 C  CB  . GLN   B 1 959  ? 65.27200   74.54700  36.82600  1.000 86.71528  ?  957  GLN   B CB  1 
ATOM   21694 C  CG  . GLN   B 1 959  ? 63.77000   74.63400  37.11300  1.000 103.59861 ?  957  GLN   B CG  1 
ATOM   21695 C  CD  . GLN   B 1 959  ? 62.90700   74.48000  35.86700  1.000 119.30809 ?  957  GLN   B CD  1 
ATOM   21696 O  OE1 . GLN   B 1 959  ? 63.26500   74.95500  34.78700  1.000 121.22824 ?  957  GLN   B OE1 1 
ATOM   21697 N  NE2 . GLN   B 1 959  ? 61.77200   73.80300  36.01000  1.000 93.15217  ?  957  GLN   B NE2 1 
ATOM   21698 N  N   . GLN   B 1 960  ? 66.09700   73.37600  34.04700  1.000 104.09672 ?  958  GLN   B N   1 
ATOM   21699 C  CA  . GLN   B 1 960  ? 65.81200   73.08000  32.64800  1.000 92.86967  ?  958  GLN   B CA  1 
ATOM   21700 C  C   . GLN   B 1 960  ? 65.96800   71.59000  32.35500  1.000 93.57786  ?  958  GLN   B C   1 
ATOM   21701 O  O   . GLN   B 1 960  ? 65.15500   71.01200  31.62200  1.000 96.56065  ?  958  GLN   B O   1 
ATOM   21702 C  CB  . GLN   B 1 960  ? 66.71200   73.92100  31.74300  1.000 99.08463  ?  958  GLN   B CB  1 
ATOM   21703 C  CG  . GLN   B 1 960  ? 66.31800   75.39200  31.67000  1.000 84.48583  ?  958  GLN   B CG  1 
ATOM   21704 C  CD  . GLN   B 1 960  ? 66.77100   76.05700  30.38600  1.000 86.45961  ?  958  GLN   B CD  1 
ATOM   21705 O  OE1 . GLN   B 1 960  ? 67.45600   75.44700  29.56500  1.000 99.84279  ?  958  GLN   B OE1 1 
ATOM   21706 N  NE2 . GLN   B 1 960  ? 66.39200   77.31800  30.20800  1.000 67.43136  ?  958  GLN   B NE2 1 
ATOM   21707 N  N   . ILE   B 1 961  ? 66.99400   70.94400  32.92700  1.000 79.77417  ?  959  ILE   B N   1 
ATOM   21708 C  CA  . ILE   B 1 961  ? 67.10100   69.48600  32.82600  1.000 86.54035  ?  959  ILE   B CA  1 
ATOM   21709 C  C   . ILE   B 1 961  ? 65.90800   68.82500  33.49300  1.000 77.71933  ?  959  ILE   B C   1 
ATOM   21710 O  O   . ILE   B 1 961  ? 65.31900   67.87600  32.96000  1.000 71.85393  ?  959  ILE   B O   1 
ATOM   21711 C  CB  . ILE   B 1 961  ? 68.40200   68.96600  33.46300  1.000 56.29744  ?  959  ILE   B CB  1 
ATOM   21712 C  CG1 . ILE   B 1 961  ? 69.62900   69.75900  33.05100  1.000 68.11612  ?  959  ILE   B CG1 1 
ATOM   21713 C  CG2 . ILE   B 1 961  ? 68.61100   67.50400  33.10800  1.000 55.38738  ?  959  ILE   B CG2 1 
ATOM   21714 C  CD1 . ILE   B 1 961  ? 70.87300   69.21600  33.71000  1.000 67.60571  ?  959  ILE   B CD1 1 
ATOM   21715 N  N   . ALA   B 1 962  ? 65.57700   69.28500  34.70200  1.000 74.52893  ?  960  ALA   B N   1 
ATOM   21716 C  CA  . ALA   B 1 962  ? 64.52900   68.65300  35.49200  1.000 85.35788  ?  960  ALA   B CA  1 
ATOM   21717 C  C   . ALA   B 1 962  ? 63.25300   68.49000  34.68400  1.000 98.47271  ?  960  ALA   B C   1 
ATOM   21718 O  O   . ALA   B 1 962  ? 62.60900   67.43800  34.74100  1.000 106.18314 ?  960  ALA   B O   1 
ATOM   21719 C  CB  . ALA   B 1 962  ? 64.26800   69.46800  36.76000  1.000 72.20891  ?  960  ALA   B CB  1 
ATOM   21720 N  N   . TYR   B 1 963  ? 62.89400   69.51100  33.89800  1.000 92.47862  ?  961  TYR   B N   1 
ATOM   21721 C  CA  . TYR   B 1 963  ? 61.71800   69.42100  33.03600  1.000 85.93278  ?  961  TYR   B CA  1 
ATOM   21722 C  C   . TYR   B 1 963  ? 61.75300   68.16900  32.17000  1.000 84.99059  ?  961  TYR   B C   1 
ATOM   21723 O  O   . TYR   B 1 963  ? 60.74200   67.47000  32.03900  1.000 91.71522  ?  961  TYR   B O   1 
ATOM   21724 C  CB  . TYR   B 1 963  ? 61.61600   70.66900  32.15800  1.000 75.93531  ?  961  TYR   B CB  1 
ATOM   21725 C  CG  . TYR   B 1 963  ? 60.59400   70.55000  31.04800  1.000 73.21829  ?  961  TYR   B CG  1 
ATOM   21726 C  CD1 . TYR   B 1 963  ? 59.23200   70.62300  31.32100  1.000 77.73715  ?  961  TYR   B CD1 1 
ATOM   21727 C  CD2 . TYR   B 1 963  ? 60.98800   70.36200  29.73000  1.000 75.21635  ?  961  TYR   B CD2 1 
ATOM   21728 C  CE1 . TYR   B 1 963  ? 58.29200   70.51300  30.31000  1.000 67.83881  ?  961  TYR   B CE1 1 
ATOM   21729 C  CE2 . TYR   B 1 963  ? 60.05500   70.25300  28.71100  1.000 84.04991  ?  961  TYR   B CE2 1 
ATOM   21730 C  CZ  . TYR   B 1 963  ? 58.70900   70.32900  29.00800  1.000 78.77144  ?  961  TYR   B CZ  1 
ATOM   21731 O  OH  . TYR   B 1 963  ? 57.77500   70.22000  27.99900  1.000 71.58963  ?  961  TYR   B OH  1 
ATOM   21732 N  N   . TRP   B 1 964  ? 62.90900   67.86900  31.57100  1.000 89.61981  ?  962  TRP   B N   1 
ATOM   21733 C  CA  . TRP   B 1 964  ? 63.03300   66.65600  30.76800  1.000 89.10271  ?  962  TRP   B CA  1 
ATOM   21734 C  C   . TRP   B 1 964  ? 62.95600   65.40800  31.63900  1.000 86.49728  ?  962  TRP   B C   1 
ATOM   21735 O  O   . TRP   B 1 964  ? 62.32100   64.41700  31.25700  1.000 84.23113  ?  962  TRP   B O   1 
ATOM   21736 C  CB  . TRP   B 1 964  ? 64.34200   66.67700  29.97400  1.000 87.36988  ?  962  TRP   B CB  1 
ATOM   21737 C  CG  . TRP   B 1 964  ? 64.55600   67.95000  29.21200  1.000 82.43975  ?  962  TRP   B CG  1 
ATOM   21738 C  CD1 . TRP   B 1 964  ? 65.51400   68.89300  29.44400  1.000 87.16441  ?  962  TRP   B CD1 1 
ATOM   21739 C  CD2 . TRP   B 1 964  ? 63.78300   68.42700  28.10300  1.000 84.32683  ?  962  TRP   B CD2 1 
ATOM   21740 N  NE1 . TRP   B 1 964  ? 65.38800   69.92600  28.54700  1.000 90.35068  ?  962  TRP   B NE1 1 
ATOM   21741 C  CE2 . TRP   B 1 964  ? 64.33200   69.66400  27.71300  1.000 82.39229  ?  962  TRP   B CE2 1 
ATOM   21742 C  CE3 . TRP   B 1 964  ? 62.68200   67.92700  27.40200  1.000 80.94329  ?  962  TRP   B CE3 1 
ATOM   21743 C  CZ2 . TRP   B 1 964  ? 63.81800   70.40900  26.65300  1.000 73.80113  ?  962  TRP   B CZ2 1 
ATOM   21744 C  CZ3 . TRP   B 1 964  ? 62.17300   68.66700  26.35000  1.000 76.18309  ?  962  TRP   B CZ3 1 
ATOM   21745 C  CH2 . TRP   B 1 964  ? 62.74000   69.89400  25.98600  1.000 73.41695  ?  962  TRP   B CH2 1 
ATOM   21746 N  N   . LYS   B 1 965  ? 63.59100   65.44000  32.81400  1.000 88.31066  ?  963  LYS   B N   1 
ATOM   21747 C  CA  . LYS   B 1 965  ? 63.59800   64.26900  33.68400  1.000 77.17970  ?  963  LYS   B CA  1 
ATOM   21748 C  C   . LYS   B 1 965  ? 62.18800   63.90000  34.13400  1.000 65.82393  ?  963  LYS   B C   1 
ATOM   21749 O  O   . LYS   B 1 965  ? 61.85800   62.71400  34.24300  1.000 80.09518  ?  963  LYS   B O   1 
ATOM   21750 C  CB  . LYS   B 1 965  ? 64.50700   64.51400  34.88900  1.000 62.63257  ?  963  LYS   B CB  1 
ATOM   21751 C  CG  . LYS   B 1 965  ? 65.82500   63.75200  34.83000  1.000 60.48743  ?  963  LYS   B CG  1 
ATOM   21752 C  CD  . LYS   B 1 965  ? 66.80700   64.25300  35.88000  1.000 78.51994  ?  963  LYS   B CD  1 
ATOM   21753 C  CE  . LYS   B 1 965  ? 67.92500   63.24600  36.13000  1.000 78.93217  ?  963  LYS   B CE  1 
ATOM   21754 N  NZ  . LYS   B 1 965  ? 69.20300   63.90200  36.54000  1.000 63.93384  ?  963  LYS   B NZ  1 
ATOM   21755 N  N   . THR   B 1 966  ? 61.33700   64.89700  34.39100  1.000 67.73146  ?  964  THR   B N   1 
ATOM   21756 C  CA  . THR   B 1 966  ? 59.95400   64.61200  34.75700  1.000 79.31643  ?  964  THR   B CA  1 
ATOM   21757 C  C   . THR   B 1 966  ? 59.05200   64.41200  33.54600  1.000 80.73893  ?  964  THR   B C   1 
ATOM   21758 O  O   . THR   B 1 966  ? 57.89900   63.99800  33.71500  1.000 70.64573  ?  964  THR   B O   1 
ATOM   21759 C  CB  . THR   B 1 966  ? 59.37200   65.72700  35.63700  1.000 79.23897  ?  964  THR   B CB  1 
ATOM   21760 O  OG1 . THR   B 1 966  ? 57.95100   65.57000  35.72400  1.000 98.38240  ?  964  THR   B OG1 1 
ATOM   21761 C  CG2 . THR   B 1 966  ? 59.65500   67.09200  35.04400  1.000 87.37210  ?  964  THR   B CG2 1 
ATOM   21762 N  N   . LEU   B 1 967  ? 59.53900   64.69500  32.34000  1.000 85.05792  ?  965  LEU   B N   1 
ATOM   21763 C  CA  . LEU   B 1 967  ? 58.77900   64.47800  31.11500  1.000 76.39303  ?  965  LEU   B CA  1 
ATOM   21764 C  C   . LEU   B 1 967  ? 59.16100   63.18500  30.40600  1.000 84.07304  ?  965  LEU   B C   1 
ATOM   21765 O  O   . LEU   B 1 967  ? 58.28100   62.47400  29.91100  1.000 79.93094  ?  965  LEU   B O   1 
ATOM   21766 C  CB  . LEU   B 1 967  ? 58.96600   65.66400  30.16200  1.000 68.76327  ?  965  LEU   B CB  1 
ATOM   21767 C  CG  . LEU   B 1 967  ? 58.02800   65.78900  28.95900  1.000 75.64436  ?  965  LEU   B CG  1 
ATOM   21768 C  CD1 . LEU   B 1 967  ? 56.62700   66.19300  29.39600  1.000 62.65511  ?  965  LEU   B CD1 1 
ATOM   21769 C  CD2 . LEU   B 1 967  ? 58.59100   66.78500  27.95200  1.000 56.53000  ?  965  LEU   B CD2 1 
ATOM   21770 N  N   . LEU   B 1 968  ? 60.45000   62.85700  30.36100  1.000 72.27981  ?  966  LEU   B N   1 
ATOM   21771 C  CA  . LEU   B 1 968  ? 60.94200   61.65400  29.69500  1.000 83.89528  ?  966  LEU   B CA  1 
ATOM   21772 C  C   . LEU   B 1 968  ? 61.46400   60.67200  30.74000  1.000 92.98964  ?  966  LEU   B C   1 
ATOM   21773 O  O   . LEU   B 1 968  ? 62.65500   60.35600  30.79500  1.000 94.12689  ?  966  LEU   B O   1 
ATOM   21774 C  CB  . LEU   B 1 968  ? 62.03300   62.01400  28.67700  1.000 82.64207  ?  966  LEU   B CB  1 
ATOM   21775 C  CG  . LEU   B 1 968  ? 61.91300   63.35300  27.94900  1.000 82.31898  ?  966  LEU   B CG  1 
ATOM   21776 C  CD1 . LEU   B 1 968  ? 63.20200   63.66600  27.20300  1.000 68.52190  ?  966  LEU   B CD1 1 
ATOM   21777 C  CD2 . LEU   B 1 968  ? 60.72600   63.34700  26.99800  1.000 84.11530  ?  966  LEU   B CD2 1 
ATOM   21778 N  N   . GLN   B 1 969  ? 60.55300   60.18300  31.57700  1.000 94.66329  ?  967  GLN   B N   1 
ATOM   21779 C  CA  . GLN   B 1 969  ? 60.87800   59.22300  32.63300  1.000 99.21609  ?  967  GLN   B CA  1 
ATOM   21780 C  C   . GLN   B 1 969  ? 60.11000   57.93800  32.34700  1.000 99.43833  ?  967  GLN   B C   1 
ATOM   21781 O  O   . GLN   B 1 969  ? 59.04000   57.69700  32.91000  1.000 102.92702 ?  967  GLN   B O   1 
ATOM   21782 C  CB  . GLN   B 1 969  ? 60.54200   59.78500  34.00900  1.000 96.41083  ?  967  GLN   B CB  1 
ATOM   21783 C  CG  . GLN   B 1 969  ? 61.42200   59.24600  35.12300  1.000 86.20383  ?  967  GLN   B CG  1 
ATOM   21784 C  CD  . GLN   B 1 969  ? 60.86600   59.54800  36.49900  1.000 85.97901  ?  967  GLN   B CD  1 
ATOM   21785 O  OE1 . GLN   B 1 969  ? 60.47800   58.64200  37.23700  1.000 90.25475  ?  967  GLN   B OE1 1 
ATOM   21786 N  NE2 . GLN   B 1 969  ? 60.82300   60.82700  36.85200  1.000 71.22995  ?  967  GLN   B NE2 1 
ATOM   21787 N  N   . GLY   B 1 970  ? 60.66200   57.11300  31.46100  1.000 89.37034  ?  968  GLY   B N   1 
ATOM   21788 C  CA  . GLY   B 1 970  ? 60.00400   55.88600  31.06000  1.000 77.79408  ?  968  GLY   B CA  1 
ATOM   21789 C  C   . GLY   B 1 970  ? 58.69200   56.13400  30.34500  1.000 88.92412  ?  968  GLY   B C   1 
ATOM   21790 O  O   . GLY   B 1 970  ? 58.23700   57.27900  30.25100  1.000 98.41663  ?  968  GLY   B O   1 
ATOM   21791 N  N   . GLU   B 1 971  ? 58.07800   55.06800  29.83500  1.000 77.93407  ?  969  GLU   B N   1 
ATOM   21792 C  CA  . GLU   B 1 971  ? 56.78800   55.15100  29.15200  1.000 85.41228  ?  969  GLU   B CA  1 
ATOM   21793 C  C   . GLU   B 1 971  ? 56.82200   56.19100  28.03300  1.000 91.16855  ?  969  GLU   B C   1 
ATOM   21794 O  O   . GLU   B 1 971  ? 55.91300   57.01100  27.88000  1.000 88.24229  ?  969  GLU   B O   1 
ATOM   21795 C  CB  . GLU   B 1 971  ? 55.66300   55.44700  30.14600  1.000 78.87080  ?  969  GLU   B CB  1 
ATOM   21796 N  N   . LEU   B 1 972  ? 57.90200   56.16200  27.25000  1.000 93.25521  ?  970  LEU   B N   1 
ATOM   21797 C  CA  . LEU   B 1 972  ? 58.01000   57.05700  26.10500  1.000 82.07549  ?  970  LEU   B CA  1 
ATOM   21798 C  C   . LEU   B 1 972  ? 57.18500   56.51200  24.94100  1.000 74.45671  ?  970  LEU   B C   1 
ATOM   21799 O  O   . LEU   B 1 972  ? 57.22400   55.31000  24.66500  1.000 85.34960  ?  970  LEU   B O   1 
ATOM   21800 C  CB  . LEU   B 1 972  ? 59.46900   57.21700  25.67800  1.000 81.97730  ?  970  LEU   B CB  1 
ATOM   21801 C  CG  . LEU   B 1 972  ? 60.35800   58.17700  26.47400  1.000 84.30806  ?  970  LEU   B CG  1 
ATOM   21802 C  CD1 . LEU   B 1 972  ? 59.62900   59.47900  26.76800  1.000 75.74617  ?  970  LEU   B CD1 1 
ATOM   21803 C  CD2 . LEU   B 1 972  ? 60.85600   57.52800  27.75900  1.000 102.42146 ?  970  LEU   B CD2 1 
ATOM   21804 N  N   . PRO   B 1 973  ? 56.43000   57.36600  24.24900  1.000 71.23407  ?  971  PRO   B N   1 
ATOM   21805 C  CA  . PRO   B 1 973  ? 55.58100   56.88100  23.15400  1.000 66.72492  ?  971  PRO   B CA  1 
ATOM   21806 C  C   . PRO   B 1 973  ? 56.39600   56.25100  22.03400  1.000 79.41837  ?  971  PRO   B C   1 
ATOM   21807 O  O   . PRO   B 1 973  ? 57.58000   56.53900  21.84500  1.000 94.99420  ?  971  PRO   B O   1 
ATOM   21808 C  CB  . PRO   B 1 973  ? 54.86000   58.14800  22.67300  1.000 63.62188  ?  971  PRO   B CB  1 
ATOM   21809 C  CG  . PRO   B 1 973  ? 54.92200   59.08900  23.83700  1.000 75.06345  ?  971  PRO   B CG  1 
ATOM   21810 C  CD  . PRO   B 1 973  ? 56.23600   58.80200  24.50700  1.000 77.89662  ?  971  PRO   B CD  1 
ATOM   21811 N  N   . ALA   B 1 974  ? 55.73900   55.36900  21.28500  1.000 70.78701  ?  972  ALA   B N   1 
ATOM   21812 C  CA  . ALA   B 1 974  ? 56.34900   54.67200  20.16000  1.000 64.91350  ?  972  ALA   B CA  1 
ATOM   21813 C  C   . ALA   B 1 974  ? 55.66200   55.12100  18.87900  1.000 70.19394  ?  972  ALA   B C   1 
ATOM   21814 O  O   . ALA   B 1 974  ? 54.43800   55.00400  18.75200  1.000 66.44536  ?  972  ALA   B O   1 
ATOM   21815 C  CB  . ALA   B 1 974  ? 56.24600   53.15600  20.32700  1.000 68.60758  ?  972  ALA   B CB  1 
ATOM   21816 N  N   . VAL   B 1 975  ? 56.44300   55.64200  17.94100  1.000 71.64895  ?  973  VAL   B N   1 
ATOM   21817 C  CA  . VAL   B 1 975  ? 55.93200   56.09500  16.65400  1.000 67.47568  ?  973  VAL   B CA  1 
ATOM   21818 C  C   . VAL   B 1 975  ? 56.35900   55.06200  15.61900  1.000 69.64538  ?  973  VAL   B C   1 
ATOM   21819 O  O   . VAL   B 1 975  ? 57.49100   55.08300  15.12100  1.000 77.53318  ?  973  VAL   B O   1 
ATOM   21820 C  CB  . VAL   B 1 975  ? 56.42700   57.50300  16.30100  1.000 62.42786  ?  973  VAL   B CB  1 
ATOM   21821 C  CG1 . VAL   B 1 975  ? 55.56900   58.54600  17.00000  1.000 54.74670  ?  973  VAL   B CG1 1 
ATOM   21822 C  CG2 . VAL   B 1 975  ? 57.88800   57.67500  16.70300  1.000 54.75536  ?  973  VAL   B CG2 1 
ATOM   21823 N  N   . GLN   B 1 976  ? 55.45600   54.14200  15.29900  1.000 66.42574  ?  974  GLN   B N   1 
ATOM   21824 C  CA  . GLN   B 1 976  ? 55.72300   53.08800  14.32400  1.000 68.34710  ?  974  GLN   B CA  1 
ATOM   21825 C  C   . GLN   B 1 976  ? 55.18600   53.55600  12.97700  1.000 67.05479  ?  974  GLN   B C   1 
ATOM   21826 O  O   . GLN   B 1 976  ? 53.98600   53.46700  12.70800  1.000 75.67274  ?  974  GLN   B O   1 
ATOM   21827 C  CB  . GLN   B 1 976  ? 55.09400   51.76800  14.75400  1.000 59.15905  ?  974  GLN   B CB  1 
ATOM   21828 C  CG  . GLN   B 1 976  ? 55.55900   50.57600  13.93100  1.000 81.05437  ?  974  GLN   B CG  1 
ATOM   21829 C  CD  . GLN   B 1 976  ? 56.77100   49.88700  14.53100  1.000 94.15753  ?  974  GLN   B CD  1 
ATOM   21830 O  OE1 . GLN   B 1 976  ? 56.67200   49.21100  15.55600  1.000 92.07656  ?  974  GLN   B OE1 1 
ATOM   21831 N  NE2 . GLN   B 1 976  ? 57.92400   50.05400  13.89300  1.000 84.34916  ?  974  GLN   B NE2 1 
ATOM   21832 N  N   . LEU   B 1 977  ? 56.07800   54.05700  12.13700  1.000 56.31218  ?  975  LEU   B N   1 
ATOM   21833 C  CA  . LEU   B 1 977  ? 55.67000   54.52200  10.82500  1.000 52.90519  ?  975  LEU   B CA  1 
ATOM   21834 C  C   . LEU   B 1 977  ? 55.53700   53.34600  9.85900   1.000 51.52536  ?  975  LEU   B C   1 
ATOM   21835 O  O   . LEU   B 1 977  ? 56.26300   52.35500  9.97300   1.000 49.40739  ?  975  LEU   B O   1 
ATOM   21836 C  CB  . LEU   B 1 977  ? 56.68100   55.52500  10.28200  1.000 53.64091  ?  975  LEU   B CB  1 
ATOM   21837 C  CG  . LEU   B 1 977  ? 56.81700   56.82000  11.08000  1.000 62.58141  ?  975  LEU   B CG  1 
ATOM   21838 C  CD1 . LEU   B 1 977  ? 58.00000   57.63700  10.57900  1.000 48.25061  ?  975  LEU   B CD1 1 
ATOM   21839 C  CD2 . LEU   B 1 977  ? 55.52800   57.61600  11.00400  1.000 44.64994  ?  975  LEU   B CD2 1 
ATOM   21840 N  N   . PRO   B 1 978  ? 54.60700   53.42800  8.89800   1.000 54.74803  ?  976  PRO   B N   1 
ATOM   21841 C  CA  . PRO   B 1 978  ? 54.45100   52.33000  7.93400   1.000 48.59747  ?  976  PRO   B CA  1 
ATOM   21842 C  C   . PRO   B 1 978  ? 55.60600   52.26000  6.94800   1.000 45.75039  ?  976  PRO   B C   1 
ATOM   21843 O  O   . PRO   B 1 978  ? 55.42900   52.58100  5.77100   1.000 53.81500  ?  976  PRO   B O   1 
ATOM   21844 C  CB  . PRO   B 1 978  ? 53.13300   52.67100  7.22700   1.000 51.37310  ?  976  PRO   B CB  1 
ATOM   21845 C  CG  . PRO   B 1 978  ? 53.03100   54.15700  7.33400   1.000 53.95610  ?  976  PRO   B CG  1 
ATOM   21846 C  CD  . PRO   B 1 978  ? 53.62600   54.50500  8.67400   1.000 55.43972  ?  976  PRO   B CD  1 
ATOM   21847 N  N   . THR   B 1 979  ? 56.78400   51.84000  7.40900   1.000 37.39914  ?  977  THR   B N   1 
ATOM   21848 C  CA  . THR   B 1 979  ? 57.97900   51.79300  6.58300   1.000 43.00876  ?  977  THR   B CA  1 
ATOM   21849 C  C   . THR   B 1 979  ? 58.24900   50.36900  6.10600   1.000 48.58405  ?  977  THR   B C   1 
ATOM   21850 O  O   . THR   B 1 979  ? 57.52700   49.42300  6.42800   1.000 59.85503  ?  977  THR   B O   1 
ATOM   21851 C  CB  . THR   B 1 979  ? 59.19300   52.32800  7.34800   1.000 52.32701  ?  977  THR   B CB  1 
ATOM   21852 O  OG1 . THR   B 1 979  ? 59.77200   51.27400  8.13000   1.000 44.09014  ?  977  THR   B OG1 1 
ATOM   21853 C  CG2 . THR   B 1 979  ? 58.78900   53.46400  8.26200   1.000 38.50949  ?  977  THR   B CG2 1 
ATOM   21854 N  N   . LYS   B 1 980  ? 59.31700   50.22200  5.32500   1.000 45.27700  ?  978  LYS   B N   1 
ATOM   21855 C  CA  . LYS   B 1 980  ? 59.78300   48.91100  4.90900   1.000 45.41423  ?  978  LYS   B CA  1 
ATOM   21856 C  C   . LYS   B 1 980  ? 60.50300   48.23200  6.07000   1.000 53.40077  ?  978  LYS   B C   1 
ATOM   21857 O  O   . LYS   B 1 980  ? 60.56500   48.75200  7.18800   1.000 58.44170  ?  978  LYS   B O   1 
ATOM   21858 C  CB  . LYS   B 1 980  ? 60.69700   49.03200  3.69100   1.000 38.38532  ?  978  LYS   B CB  1 
ATOM   21859 C  CG  . LYS   B 1 980  ? 60.15200   49.92200  2.58800   1.000 43.53073  ?  978  LYS   B CG  1 
ATOM   21860 C  CD  . LYS   B 1 980  ? 61.06700   49.92200  1.37200   1.000 50.04907  ?  978  LYS   B CD  1 
ATOM   21861 C  CE  . LYS   B 1 980  ? 60.27300   49.93700  0.07400   1.000 49.50803  ?  978  LYS   B CE  1 
ATOM   21862 N  NZ  . LYS   B 1 980  ? 60.65700   48.81100  -0.82200  1.000 75.61259  ?  978  LYS   B NZ  1 
ATOM   21863 N  N   . LYS   B 1 981  ? 61.05500   47.05100  5.80600   1.000 55.11486  ?  979  LYS   B N   1 
ATOM   21864 C  CA  . LYS   B 1 981  ? 61.84800   46.36200  6.81500   1.000 67.73532  ?  979  LYS   B CA  1 
ATOM   21865 C  C   . LYS   B 1 981  ? 63.07200   47.19900  7.16700   1.000 67.04241  ?  979  LYS   B C   1 
ATOM   21866 O  O   . LYS   B 1 981  ? 63.86800   47.55000  6.29000   1.000 57.79342  ?  979  LYS   B O   1 
ATOM   21867 C  CB  . LYS   B 1 981  ? 62.26200   44.98200  6.30800   1.000 71.98488  ?  979  LYS   B CB  1 
ATOM   21868 N  N   . ARG   B 1 982  ? 63.20900   47.53000  8.44500   1.000 64.69611  ?  980  ARG   B N   1 
ATOM   21869 C  CA  . ARG   B 1 982  ? 64.29700   48.40200  8.87800   1.000 65.41982  ?  980  ARG   B CA  1 
ATOM   21870 C  C   . ARG   B 1 982  ? 65.63700   47.70700  8.67000   1.000 59.24292  ?  980  ARG   B C   1 
ATOM   21871 O  O   . ARG   B 1 982  ? 65.79100   46.54200  9.05500   1.000 66.46254  ?  980  ARG   B O   1 
ATOM   21872 C  CB  . ARG   B 1 982  ? 64.12600   48.78500  10.34600  1.000 62.77614  ?  980  ARG   B CB  1 
ATOM   21873 C  CG  . ARG   B 1 982  ? 62.91900   49.66600  10.62200  1.000 65.22810  ?  980  ARG   B CG  1 
ATOM   21874 C  CD  . ARG   B 1 982  ? 62.99600   50.27700  12.00900  1.000 73.21222  ?  980  ARG   B CD  1 
ATOM   21875 N  NE  . ARG   B 1 982  ? 64.11600   51.20100  12.12900  1.000 70.70088  ?  980  ARG   B NE  1 
ATOM   21876 C  CZ  . ARG   B 1 982  ? 64.03400   52.50700  11.91500  1.000 67.57566  ?  980  ARG   B CZ  1 
ATOM   21877 N  NH1 . ARG   B 1 982  ? 62.89300   53.08200  11.56900  1.000 49.23483  ?  980  ARG   B NH1 1 
ATOM   21878 N  NH2 . ARG   B 1 982  ? 65.12600   53.25600  12.05200  1.000 62.69137  ?  980  ARG   B NH2 1 
ATOM   21879 N  N   . PRO   B 1 983  ? 66.61700   48.37400  8.06200   1.000 56.31447  ?  981  PRO   B N   1 
ATOM   21880 C  CA  . PRO   B 1 983  ? 67.92200   47.74500  7.88800   1.000 64.91196  ?  981  PRO   B CA  1 
ATOM   21881 C  C   . PRO   B 1 983  ? 68.54000   47.41700  9.22300   1.000 76.26205  ?  981  PRO   B C   1 
ATOM   21882 O  O   . PRO   B 1 983  ? 68.22400   48.04800  10.25300  1.000 78.17483  ?  981  PRO   B O   1 
ATOM   21883 C  CB  . PRO   B 1 983  ? 68.72900   48.81600  7.13800   1.000 70.69828  ?  981  PRO   B CB  1 
ATOM   21884 C  CG  . PRO   B 1 983  ? 67.70800   49.68300  6.48600   1.000 65.76880  ?  981  PRO   B CG  1 
ATOM   21885 C  CD  . PRO   B 1 983  ? 66.54100   49.69600  7.42200   1.000 71.25866  ?  981  PRO   B CD  1 
ATOM   21886 N  N   . PRO   B 1 984  ? 69.43000   46.41700  9.27400   1.000 79.69556  ?  982  PRO   B N   1 
ATOM   21887 C  CA  . PRO   B 1 984  ? 70.06100   46.06100  10.55600  1.000 78.70242  ?  982  PRO   B CA  1 
ATOM   21888 C  C   . PRO   B 1 984  ? 70.82600   47.20800  11.19100  1.000 87.06858  ?  982  PRO   B C   1 
ATOM   21889 O  O   . PRO   B 1 984  ? 70.82700   47.34000  12.42100  1.000 87.32628  ?  982  PRO   B O   1 
ATOM   21890 C  CB  . PRO   B 1 984  ? 70.99200   44.90100  10.17500  1.000 84.39378  ?  982  PRO   B CB  1 
ATOM   21891 C  CG  . PRO   B 1 984  ? 70.41000   44.33600  8.92400   1.000 91.32071  ?  982  PRO   B CG  1 
ATOM   21892 C  CD  . PRO   B 1 984  ? 69.81100   45.49700  8.18800   1.000 83.15487  ?  982  PRO   B CD  1 
ATOM   21893 N  N   . GLN   B 1 985  ? 71.47500   48.04400  10.38800  1.000 94.09939  ?  983  GLN   B N   1 
ATOM   21894 C  CA  . GLN   B 1 985  ? 72.22700   49.18800  10.88000  1.000 90.40201  ?  983  GLN   B CA  1 
ATOM   21895 C  C   . GLN   B 1 985  ? 71.49600   50.48300  10.54800  1.000 84.51822  ?  983  GLN   B C   1 
ATOM   21896 O  O   . GLN   B 1 985  ? 70.49100   50.49800  9.83200   1.000 89.64794  ?  983  GLN   B O   1 
ATOM   21897 C  CB  . GLN   B 1 985  ? 73.63900   49.20700  10.28500  1.000 96.83996  ?  983  GLN   B CB  1 
ATOM   21898 N  N   . LEU   B 1 986  ? 72.01900   51.58200  11.08600  1.000 79.29932  ?  984  LEU   B N   1 
ATOM   21899 C  CA  . LEU   B 1 986  ? 71.48300   52.90500  10.79300  1.000 78.26088  ?  984  LEU   B CA  1 
ATOM   21900 C  C   . LEU   B 1 986  ? 72.03800   53.38900  9.45900   1.000 76.25723  ?  984  LEU   B C   1 
ATOM   21901 O  O   . LEU   B 1 986  ? 73.25100   53.56800  9.31100   1.000 83.16976  ?  984  LEU   B O   1 
ATOM   21902 C  CB  . LEU   B 1 986  ? 71.82900   53.88700  11.91200  1.000 66.09885  ?  984  LEU   B CB  1 
ATOM   21903 C  CG  . LEU   B 1 986  ? 70.70300   54.22300  12.89700  1.000 80.72137  ?  984  LEU   B CG  1 
ATOM   21904 C  CD1 . LEU   B 1 986  ? 70.99000   55.52100  13.63400  1.000 78.19720  ?  984  LEU   B CD1 1 
ATOM   21905 C  CD2 . LEU   B 1 986  ? 69.36000   54.30400  12.18800  1.000 77.50025  ?  984  LEU   B CD2 1 
ATOM   21906 N  N   . THR   B 1 987  ? 71.15300   53.59000  8.48900   1.000 78.30096  ?  985  THR   B N   1 
ATOM   21907 C  CA  . THR   B 1 987  ? 71.52600   54.07100  7.16900   1.000 73.85884  ?  985  THR   B CA  1 
ATOM   21908 C  C   . THR   B 1 987  ? 71.05800   55.50900  6.99100   1.000 69.53724  ?  985  THR   B C   1 
ATOM   21909 O  O   . THR   B 1 987  ? 70.07200   55.93800  7.59700   1.000 72.92172  ?  985  THR   B O   1 
ATOM   21910 C  CB  . THR   B 1 987  ? 70.93000   53.18900  6.07000   1.000 71.62276  ?  985  THR   B CB  1 
ATOM   21911 O  OG1 . THR   B 1 987  ? 69.53100   52.99500  6.31800   1.000 75.10784  ?  985  THR   B OG1 1 
ATOM   21912 C  CG2 . THR   B 1 987  ? 71.62600   51.84100  6.05100   1.000 61.40042  ?  985  THR   B CG2 1 
ATOM   21913 N  N   . PHE   B 1 988  ? 71.77800   56.25500  6.14900   1.000 55.54291  ?  986  PHE   B N   1 
ATOM   21914 C  CA  . PHE   B 1 988  ? 71.50400   57.67600  5.97300   1.000 48.91899  ?  986  PHE   B CA  1 
ATOM   21915 C  C   . PHE   B 1 988  ? 71.35000   58.06400  4.50600   1.000 49.36566  ?  986  PHE   B C   1 
ATOM   21916 O  O   . PHE   B 1 988  ? 71.38700   59.25500  4.18300   1.000 48.03770  ?  986  PHE   B O   1 
ATOM   21917 C  CB  . PHE   B 1 988  ? 72.59500   58.52100  6.63600   1.000 47.92907  ?  986  PHE   B CB  1 
ATOM   21918 C  CG  . PHE   B 1 988  ? 72.94200   58.07200  8.02800   1.000 72.77380  ?  986  PHE   B CG  1 
ATOM   21919 C  CD1 . PHE   B 1 988  ? 72.18000   58.48000  9.11200   1.000 66.19954  ?  986  PHE   B CD1 1 
ATOM   21920 C  CD2 . PHE   B 1 988  ? 74.02300   57.23500  8.25200   1.000 70.90104  ?  986  PHE   B CD2 1 
ATOM   21921 C  CE1 . PHE   B 1 988  ? 72.49400   58.06700  10.39300  1.000 79.73351  ?  986  PHE   B CE1 1 
ATOM   21922 C  CE2 . PHE   B 1 988  ? 74.34300   56.81800  9.53100   1.000 74.36076  ?  986  PHE   B CE2 1 
ATOM   21923 C  CZ  . PHE   B 1 988  ? 73.57800   57.23400  10.60300  1.000 80.96926  ?  986  PHE   B CZ  1 
ATOM   21924 N  N   . ASP   B 1 989  ? 71.17400   57.09300  3.61200   1.000 50.02859  ?  987  ASP   B N   1 
ATOM   21925 C  CA  . ASP   B 1 989  ? 70.85400   57.40800  2.22600   1.000 46.28873  ?  987  ASP   B CA  1 
ATOM   21926 C  C   . ASP   B 1 989  ? 69.43500   57.95700  2.14400   1.000 36.05528  ?  987  ASP   B C   1 
ATOM   21927 O  O   . ASP   B 1 989  ? 68.50600   57.38500  2.72200   1.000 50.61000  ?  987  ASP   B O   1 
ATOM   21928 C  CB  . ASP   B 1 989  ? 70.99500   56.16400  1.34800   1.000 50.01861  ?  987  ASP   B CB  1 
ATOM   21929 C  CG  . ASP   B 1 989  ? 72.23600   55.35200  1.67400   1.000 70.75082  ?  987  ASP   B CG  1 
ATOM   21930 O  OD1 . ASP   B 1 989  ? 72.19700   54.56100  2.64200   1.000 76.47444  ?  987  ASP   B OD1 1 
ATOM   21931 O  OD2 . ASP   B 1 989  ? 73.25000   55.50100  0.95900   1.000 74.88101  -1 987  ASP   B OD2 1 
ATOM   21932 N  N   . GLY   B 1 990  ? 69.25900   59.06900  1.43100   1.000 35.17562  ?  988  GLY   B N   1 
ATOM   21933 C  CA  . GLY   B 1 990  ? 67.97400   59.73500  1.43600   1.000 38.98719  ?  988  GLY   B CA  1 
ATOM   21934 C  C   . GLY   B 1 990  ? 67.64700   60.43900  0.13600   1.000 32.32287  ?  988  GLY   B C   1 
ATOM   21935 O  O   . GLY   B 1 990  ? 68.45000   60.48800  -0.79800  1.000 37.20313  ?  988  GLY   B O   1 
ATOM   21936 N  N   . ALA   B 1 991  ? 66.43500   60.98500  0.09300   1.000 32.26112  ?  989  ALA   B N   1 
ATOM   21937 C  CA  . ALA   B 1 991  ? 65.93300   61.75000  -1.04000  1.000 29.68725  ?  989  ALA   B CA  1 
ATOM   21938 C  C   . ALA   B 1 991  ? 64.96200   62.79600  -0.49800  1.000 31.86681  ?  989  ALA   B C   1 
ATOM   21939 O  O   . ALA   B 1 991  ? 64.79300   62.93500  0.71700   1.000 35.07026  ?  989  ALA   B O   1 
ATOM   21940 C  CB  . ALA   B 1 991  ? 65.28700   60.82400  -2.07700  1.000 33.21708  ?  989  ALA   B CB  1 
ATOM   21941 N  N   . ILE   B 1 992  ? 64.30800   63.52700  -1.39800  1.000 34.35304  ?  990  ILE   B N   1 
ATOM   21942 C  CA  . ILE   B 1 992  ? 63.48900   64.66800  -0.99400  1.000 34.31859  ?  990  ILE   B CA  1 
ATOM   21943 C  C   . ILE   B 1 992  ? 62.26500   64.77400  -1.89700  1.000 33.32247  ?  990  ILE   B C   1 
ATOM   21944 O  O   . ILE   B 1 992  ? 62.37500   64.71100  -3.12500  1.000 45.12738  ?  990  ILE   B O   1 
ATOM   21945 C  CB  . ILE   B 1 992  ? 64.30700   65.97600  -1.02100  1.000 30.74938  ?  990  ILE   B CB  1 
ATOM   21946 C  CG1 . ILE   B 1 992  ? 65.02500   66.17200  0.31400   1.000 46.76162  ?  990  ILE   B CG1 1 
ATOM   21947 C  CG2 . ILE   B 1 992  ? 63.42200   67.17000  -1.34100  1.000 30.57316  ?  990  ILE   B CG2 1 
ATOM   21948 C  CD1 . ILE   B 1 992  ? 65.73300   67.49800  0.44200   1.000 61.22127  ?  990  ILE   B CD1 1 
ATOM   21949 N  N   . GLN   B 1 993  ? 61.09500   64.93400  -1.28300  1.000 31.42733  ?  991  GLN   B N   1 
ATOM   21950 C  CA  . GLN   B 1 993  ? 59.87900   65.32300  -1.97700  1.000 34.43039  ?  991  GLN   B CA  1 
ATOM   21951 C  C   . GLN   B 1 993  ? 59.40300   66.65300  -1.40800  1.000 37.46896  ?  991  GLN   B C   1 
ATOM   21952 O  O   . GLN   B 1 993  ? 59.71000   66.99700  -0.26300  1.000 42.60777  ?  991  GLN   B O   1 
ATOM   21953 C  CB  . GLN   B 1 993  ? 58.77900   64.26300  -1.83800  1.000 37.03990  ?  991  GLN   B CB  1 
ATOM   21954 C  CG  . GLN   B 1 993  ? 58.85400   63.14600  -2.86600  1.000 38.82744  ?  991  GLN   B CG  1 
ATOM   21955 C  CD  . GLN   B 1 993  ? 58.17900   63.51300  -4.17000  1.000 52.23245  ?  991  GLN   B CD  1 
ATOM   21956 O  OE1 . GLN   B 1 993  ? 57.69000   64.63100  -4.33700  1.000 53.59853  ?  991  GLN   B OE1 1 
ATOM   21957 N  NE2 . GLN   B 1 993  ? 58.14700   62.57000  -5.10500  1.000 64.91563  ?  991  GLN   B NE2 1 
ATOM   21958 N  N   . MET   B 1 994  ? 58.65300   67.40300  -2.20900  1.000 38.36601  ?  992  MET   B N   1 
ATOM   21959 C  CA  . MET   B 1 994  ? 58.25100   68.75100  -1.83800  1.000 36.25287  ?  992  MET   B CA  1 
ATOM   21960 C  C   . MET   B 1 994  ? 56.75100   68.92600  -2.02400  1.000 37.67468  ?  992  MET   B C   1 
ATOM   21961 O  O   . MET   B 1 994  ? 56.18500   68.49800  -3.03400  1.000 50.37248  ?  992  MET   B O   1 
ATOM   21962 C  CB  . MET   B 1 994  ? 59.01100   69.79600  -2.66700  1.000 48.33974  ?  992  MET   B CB  1 
ATOM   21963 C  CG  . MET   B 1 994  ? 59.41800   71.04000  -1.89500  1.000 66.03899  ?  992  MET   B CG  1 
ATOM   21964 S  SD  . MET   B 1 994  ? 58.23300   72.38800  -2.09400  1.000 93.72354  ?  992  MET   B SD  1 
ATOM   21965 C  CE  . MET   B 1 994  ? 58.42500   72.76600  -3.83600  1.000 90.41623  ?  992  MET   B CE  1 
ATOM   21966 N  N   . TYR   B 1 995  ? 56.11200   69.55100  -1.03800  1.000 36.06102  ?  993  TYR   B N   1 
ATOM   21967 C  CA  . TYR   B 1 995  ? 54.69700   69.88800  -1.09400  1.000 38.60573  ?  993  TYR   B CA  1 
ATOM   21968 C  C   . TYR   B 1 995  ? 54.55300   71.39100  -0.91600  1.000 39.79358  ?  993  TYR   B C   1 
ATOM   21969 O  O   . TYR   B 1 995  ? 55.18700   71.97900  -0.03300  1.000 35.19613  ?  993  TYR   B O   1 
ATOM   21970 C  CB  . TYR   B 1 995  ? 53.90000   69.13300  -0.02500  1.000 34.87256  ?  993  TYR   B CB  1 
ATOM   21971 C  CG  . TYR   B 1 995  ? 52.52200   69.70400  0.25900   1.000 36.30879  ?  993  TYR   B CG  1 
ATOM   21972 C  CD1 . TYR   B 1 995  ? 51.61400   69.93600  -0.76700  1.000 36.69394  ?  993  TYR   B CD1 1 
ATOM   21973 C  CD2 . TYR   B 1 995  ? 52.12700   69.99700  1.56000   1.000 37.75584  ?  993  TYR   B CD2 1 
ATOM   21974 C  CE1 . TYR   B 1 995  ? 50.35600   70.45600  -0.50900  1.000 39.48842  ?  993  TYR   B CE1 1 
ATOM   21975 C  CE2 . TYR   B 1 995  ? 50.86900   70.51600  1.82900   1.000 36.02649  ?  993  TYR   B CE2 1 
ATOM   21976 C  CZ  . TYR   B 1 995  ? 49.98800   70.74300  0.79200   1.000 43.90601  ?  993  TYR   B CZ  1 
ATOM   21977 O  OH  . TYR   B 1 995  ? 48.73900   71.25800  1.05600   1.000 42.10674  ?  993  TYR   B OH  1 
ATOM   21978 N  N   . ARG   B 1 996  ? 53.72800   72.00800  -1.75400  1.000 40.22102  ?  994  ARG   B N   1 
ATOM   21979 C  CA  . ARG   B 1 996  ? 53.54800   73.45200  -1.76800  1.000 42.59073  ?  994  ARG   B CA  1 
ATOM   21980 C  C   . ARG   B 1 996  ? 52.13300   73.79400  -1.31900  1.000 46.81760  ?  994  ARG   B C   1 
ATOM   21981 O  O   . ARG   B 1 996  ? 51.15800   73.34500  -1.93200  1.000 54.84709  ?  994  ARG   B O   1 
ATOM   21982 C  CB  . ARG   B 1 996  ? 53.81900   74.01300  -3.16400  1.000 33.47090  ?  994  ARG   B CB  1 
ATOM   21983 C  CG  . ARG   B 1 996  ? 53.23900   75.39600  -3.41600  1.000 46.82959  ?  994  ARG   B CG  1 
ATOM   21984 C  CD  . ARG   B 1 996  ? 54.21200   76.49100  -3.02700  1.000 37.65860  ?  994  ARG   B CD  1 
ATOM   21985 N  NE  . ARG   B 1 996  ? 53.69700   77.81100  -3.36600  1.000 48.28009  ?  994  ARG   B NE  1 
ATOM   21986 C  CZ  . ARG   B 1 996  ? 54.31200   78.94900  -3.07700  1.000 55.58156  ?  994  ARG   B CZ  1 
ATOM   21987 N  NH1 . ARG   B 1 996  ? 55.47700   78.96300  -2.45000  1.000 43.15891  ?  994  ARG   B NH1 1 
ATOM   21988 N  NH2 . ARG   B 1 996  ? 53.74200   80.10200  -3.42200  1.000 49.03236  ?  994  ARG   B NH2 1 
ATOM   21989 N  N   . VAL   B 1 997  ? 52.02600   74.58700  -0.25800  1.000 40.57893  ?  995  VAL   B N   1 
ATOM   21990 C  CA  . VAL   B 1 997  ? 50.75300   75.16100  0.16400   1.000 46.24606  ?  995  VAL   B CA  1 
ATOM   21991 C  C   . VAL   B 1 997  ? 50.60400   76.51200  -0.52400  1.000 42.90121  ?  995  VAL   B C   1 
ATOM   21992 O  O   . VAL   B 1 997  ? 51.43800   77.40500  -0.33500  1.000 39.34471  ?  995  VAL   B O   1 
ATOM   21993 C  CB  . VAL   B 1 997  ? 50.68700   75.30700  1.69100   1.000 38.35439  ?  995  VAL   B CB  1 
ATOM   21994 C  CG1 . VAL   B 1 997  ? 49.25500   75.52700  2.13600   1.000 39.06427  ?  995  VAL   B CG1 1 
ATOM   21995 C  CG2 . VAL   B 1 997  ? 51.28500   74.08200  2.36800   1.000 28.12041  ?  995  VAL   B CG2 1 
ATOM   21996 N  N   . ASN   B 1 998  ? 49.54500   76.66500  -1.32600  1.000 47.14351  ?  996  ASN   B N   1 
ATOM   21997 C  CA  . ASN   B 1 998  ? 49.41200   77.85400  -2.15700  1.000 50.78727  ?  996  ASN   B CA  1 
ATOM   21998 C  C   . ASN   B 1 998  ? 49.23700   79.10400  -1.29000  1.000 51.58719  ?  996  ASN   B C   1 
ATOM   21999 O  O   . ASN   B 1 998  ? 48.92600   79.00800  -0.10000  1.000 50.72962  ?  996  ASN   B O   1 
ATOM   22000 C  CB  . ASN   B 1 998  ? 48.24400   77.69300  -3.14200  1.000 46.92847  ?  996  ASN   B CB  1 
ATOM   22001 C  CG  . ASN   B 1 998  ? 46.89300   77.56600  -2.45900  1.000 48.10162  ?  996  ASN   B CG  1 
ATOM   22002 O  OD1 . ASN   B 1 998  ? 46.55400   78.33400  -1.56000  1.000 55.28862  ?  996  ASN   B OD1 1 
ATOM   22003 N  ND2 . ASN   B 1 998  ? 46.10600   76.59200  -2.89900  1.000 55.03285  ?  996  ASN   B ND2 1 
ATOM   22004 N  N   . PRO   B 1 999  ? 49.46400   80.29200  -1.86500  1.000 58.97156  ?  997  PRO   B N   1 
ATOM   22005 C  CA  . PRO   B 1 999  ? 49.29500   81.52300  -1.07300  1.000 54.44546  ?  997  PRO   B CA  1 
ATOM   22006 C  C   . PRO   B 1 999  ? 47.91800   81.66500  -0.44700  1.000 58.11827  ?  997  PRO   B C   1 
ATOM   22007 O  O   . PRO   B 1 999  ? 47.80200   82.19500  0.66600   1.000 47.56441  ?  997  PRO   B O   1 
ATOM   22008 C  CB  . PRO   B 1 999  ? 49.56900   82.63000  -2.09900  1.000 47.70531  ?  997  PRO   B CB  1 
ATOM   22009 C  CG  . PRO   B 1 999  ? 50.48700   82.00000  -3.08400  1.000 51.21082  ?  997  PRO   B CG  1 
ATOM   22010 C  CD  . PRO   B 1 999  ? 50.05900   80.56500  -3.18700  1.000 57.31018  ?  997  PRO   B CD  1 
ATOM   22011 N  N   . GLU   B 1 1000 ? 46.86900   81.20600  -1.13500  1.000 59.12735  ?  998  GLU   B N   1 
ATOM   22012 C  CA  . GLU   B 1 1000 ? 45.51600   81.31800  -0.59900  1.000 45.23195  ?  998  GLU   B CA  1 
ATOM   22013 C  C   . GLU   B 1 1000 ? 45.38000   80.55800  0.71700   1.000 54.41541  ?  998  GLU   B C   1 
ATOM   22014 O  O   . GLU   B 1 1000 ? 44.91200   81.10900  1.72100   1.000 46.11069  ?  998  GLU   B O   1 
ATOM   22015 C  CB  . GLU   B 1 1000 ? 44.50500   80.81100  -1.63000  1.000 57.31789  ?  998  GLU   B CB  1 
ATOM   22016 C  CG  . GLU   B 1 1000 ? 43.10700   80.56600  -1.07800  1.000 82.94863  ?  998  GLU   B CG  1 
ATOM   22017 C  CD  . GLU   B 1 1000 ? 42.03300   80.59000  -2.15300  1.000 76.74211  ?  998  GLU   B CD  1 
ATOM   22018 O  OE1 . GLU   B 1 1000 ? 42.04000   81.51800  -2.99100  1.000 68.75416  ?  998  GLU   B OE1 1 
ATOM   22019 O  OE2 . GLU   B 1 1000 ? 41.17700   79.68000  -2.15600  1.000 70.12369  -1 998  GLU   B OE2 1 
ATOM   22020 N  N   . ILE   B 1 1001 ? 45.79700   79.28900  0.73600   1.000 59.05203  ?  999  ILE   B N   1 
ATOM   22021 C  CA  . ILE   B 1 1001 ? 45.69500   78.49300  1.95600   1.000 45.09975  ?  999  ILE   B CA  1 
ATOM   22022 C  C   . ILE   B 1 1001 ? 46.65000   79.02100  3.02100   1.000 47.74823  ?  999  ILE   B C   1 
ATOM   22023 O  O   . ILE   B 1 1001 ? 46.32400   79.03000  4.21500   1.000 56.12914  ?  999  ILE   B O   1 
ATOM   22024 C  CB  . ILE   B 1 1001 ? 45.94900   77.00400  1.65100   1.000 46.03019  ?  999  ILE   B CB  1 
ATOM   22025 C  CG1 . ILE   B 1 1001 ? 45.02500   76.51400  0.53100   1.000 51.09992  ?  999  ILE   B CG1 1 
ATOM   22026 C  CG2 . ILE   B 1 1001 ? 45.75800   76.15400  2.90100   1.000 35.78377  ?  999  ILE   B CG2 1 
ATOM   22027 C  CD1 . ILE   B 1 1001 ? 43.55000   76.72200  0.80900   1.000 48.47848  ?  999  ILE   B CD1 1 
ATOM   22028 N  N   . THR   B 1 1002 ? 47.83600   79.48000  2.61000   1.000 52.89260  ?  1000 THR   B N   1 
ATOM   22029 C  CA  . THR   B 1 1002 ? 48.82600   79.95200  3.57500   1.000 53.96985  ?  1000 THR   B CA  1 
ATOM   22030 C  C   . THR   B 1 1002 ? 48.31700   81.16700  4.34300   1.000 59.78032  ?  1000 THR   B C   1 
ATOM   22031 O  O   . THR   B 1 1002 ? 48.57300   81.30300  5.54700   1.000 44.78988  ?  1000 THR   B O   1 
ATOM   22032 C  CB  . THR   B 1 1002 ? 50.13900   80.27400  2.86000   1.000 45.60401  ?  1000 THR   B CB  1 
ATOM   22033 O  OG1 . THR   B 1 1002 ? 50.62100   79.09900  2.19800   1.000 49.20475  ?  1000 THR   B OG1 1 
ATOM   22034 C  CG2 . THR   B 1 1002 ? 51.18500   80.73900  3.85700   1.000 46.83420  ?  1000 THR   B CG2 1 
ATOM   22035 N  N   . ARG   B 1 1003 ? 47.58900   82.06000  3.66400   1.000 52.28857  ?  1001 ARG   B N   1 
ATOM   22036 C  CA  . ARG   B 1 1003 ? 46.96200   83.18000  4.35600   1.000 52.20733  ?  1001 ARG   B CA  1 
ATOM   22037 C  C   . ARG   B 1 1003 ? 45.95100   82.69800  5.38100   1.000 64.98542  ?  1001 ARG   B C   1 
ATOM   22038 O  O   . ARG   B 1 1003 ? 45.91000   83.19900  6.51200   1.000 65.49138  ?  1001 ARG   B O   1 
ATOM   22039 C  CB  . ARG   B 1 1003 ? 46.28900   84.11400  3.35400   1.000 54.06999  ?  1001 ARG   B CB  1 
ATOM   22040 C  CG  . ARG   B 1 1003 ? 47.31800   84.96700  2.63900   1.000 74.44843  ?  1001 ARG   B CG  1 
ATOM   22041 C  CD  . ARG   B 1 1003 ? 46.70400   85.92300  1.65100   1.000 76.72801  ?  1001 ARG   B CD  1 
ATOM   22042 N  NE  . ARG   B 1 1003 ? 47.64500   86.59800  0.75800   1.000 93.17282  ?  1001 ARG   B NE  1 
ATOM   22043 C  CZ  . ARG   B 1 1003 ? 48.81900   87.13400  1.08200   1.000 95.67841  ?  1001 ARG   B CZ  1 
ATOM   22044 N  NH1 . ARG   B 1 1003 ? 49.24200   87.20200  2.33400   1.000 94.95325  ?  1001 ARG   B NH1 1 
ATOM   22045 N  NH2 . ARG   B 1 1003 ? 49.57900   87.64700  0.11900   1.000 83.30726  ?  1001 ARG   B NH2 1 
ATOM   22046 N  N   . LYS   B 1 1004 ? 45.10900   81.74500  4.98800   1.000 54.40119  ?  1002 LYS   B N   1 
ATOM   22047 C  CA  . LYS   B 1 1004 ? 44.10200   81.22300  5.89700   1.000 56.91782  ?  1002 LYS   B CA  1 
ATOM   22048 C  C   . LYS   B 1 1004 ? 44.73800   80.52500  7.08700   1.000 58.82859  ?  1002 LYS   B C   1 
ATOM   22049 O  O   . LYS   B 1 1004 ? 44.20100   80.58400  8.19700   1.000 56.91948  ?  1002 LYS   B O   1 
ATOM   22050 C  CB  . LYS   B 1 1004 ? 43.17400   80.27200  5.14500   1.000 49.03276  ?  1002 LYS   B CB  1 
ATOM   22051 N  N   . LEU   B 1 1005 ? 45.88200   79.86800  6.88400   1.000 50.26441  ?  1003 LEU   B N   1 
ATOM   22052 C  CA  . LEU   B 1 1005 ? 46.55100   79.20000  7.99500   1.000 54.69844  ?  1003 LEU   B CA  1 
ATOM   22053 C  C   . LEU   B 1 1005 ? 47.05800   80.21300  9.01100   1.000 52.53475  ?  1003 LEU   B C   1 
ATOM   22054 O  O   . LEU   B 1 1005 ? 46.80100   80.08400  10.21500  1.000 54.19456  ?  1003 LEU   B O   1 
ATOM   22055 C  CB  . LEU   B 1 1005 ? 47.70200   78.33400  7.47800   1.000 53.35666  ?  1003 LEU   B CB  1 
ATOM   22056 C  CG  . LEU   B 1 1005 ? 47.35000   77.13900  6.58900   1.000 54.54339  ?  1003 LEU   B CG  1 
ATOM   22057 C  CD1 . LEU   B 1 1005 ? 48.56000   76.69200  5.79000   1.000 53.61424  ?  1003 LEU   B CD1 1 
ATOM   22058 C  CD2 . LEU   B 1 1005 ? 46.81200   75.98300  7.40900   1.000 55.24831  ?  1003 LEU   B CD2 1 
ATOM   22059 N  N   . LYS   B 1 1006 ? 47.77700   81.23500  8.54100   1.000 65.22756  ?  1004 LYS   B N   1 
ATOM   22060 C  CA  . LYS   B 1 1006 ? 48.34900   82.22200  9.45100   1.000 72.33522  ?  1004 LYS   B CA  1 
ATOM   22061 C  C   . LYS   B 1 1006 ? 47.26300   83.04000  10.13500  1.000 57.45971  ?  1004 LYS   B C   1 
ATOM   22062 O  O   . LYS   B 1 1006 ? 47.35100   83.31800  11.33600  1.000 53.46104  ?  1004 LYS   B O   1 
ATOM   22063 C  CB  . LYS   B 1 1006 ? 49.30900   83.14000  8.69600   1.000 66.60843  ?  1004 LYS   B CB  1 
ATOM   22064 C  CG  . LYS   B 1 1006 ? 50.72400   82.60500  8.58300   1.000 64.00596  ?  1004 LYS   B CG  1 
ATOM   22065 C  CD  . LYS   B 1 1006 ? 51.52800   83.39400  7.56600   1.000 62.94046  ?  1004 LYS   B CD  1 
ATOM   22066 C  CE  . LYS   B 1 1006 ? 52.71200   84.08100  8.21900   1.000 57.79945  ?  1004 LYS   B CE  1 
ATOM   22067 N  NZ  . LYS   B 1 1006 ? 53.74000   84.44300  7.20800   1.000 72.16220  ?  1004 LYS   B NZ  1 
ATOM   22068 N  N   . ALA   B 1 1007 ? 46.23500   83.43700  9.38400   1.000 43.65209  ?  1005 ALA   B N   1 
ATOM   22069 C  CA  . ALA   B 1 1007 ? 45.13100   84.18600  9.97200   1.000 67.44385  ?  1005 ALA   B CA  1 
ATOM   22070 C  C   . ALA   B 1 1007 ? 44.43900   83.37500  11.05800  1.000 66.73579  ?  1005 ALA   B C   1 
ATOM   22071 O  O   . ALA   B 1 1007 ? 44.17400   83.88100  12.15500  1.000 79.44617  ?  1005 ALA   B O   1 
ATOM   22072 C  CB  . ALA   B 1 1007 ? 44.13400   84.58900  8.88700   1.000 54.51337  ?  1005 ALA   B CB  1 
ATOM   22073 N  N   . THR   B 1 1008 ? 44.14400   82.10600  10.76900  1.000 60.21177  ?  1006 THR   B N   1 
ATOM   22074 C  CA  . THR   B 1 1008 ? 43.45400   81.26700  11.74200  1.000 53.53342  ?  1006 THR   B CA  1 
ATOM   22075 C  C   . THR   B 1 1008 ? 44.28600   81.08000  13.00300  1.000 58.70745  ?  1006 THR   B C   1 
ATOM   22076 O  O   . THR   B 1 1008 ? 43.76000   81.15800  14.12000  1.000 78.41555  ?  1006 THR   B O   1 
ATOM   22077 C  CB  . THR   B 1 1008 ? 43.11800   79.91300  11.12600  1.000 55.93472  ?  1006 THR   B CB  1 
ATOM   22078 O  OG1 . THR   B 1 1008 ? 42.17000   80.08500  10.06400  1.000 70.97640  ?  1006 THR   B OG1 1 
ATOM   22079 C  CG2 . THR   B 1 1008 ? 42.53500   79.01200  12.17400  1.000 56.66540  ?  1006 THR   B CG2 1 
ATOM   22080 N  N   . ALA   B 1 1009 ? 45.58700   80.82800  12.84600  1.000 51.78969  ?  1007 ALA   B N   1 
ATOM   22081 C  CA  . ALA   B 1 1009 ? 46.45400   80.69400  14.01100  1.000 50.81782  ?  1007 ALA   B CA  1 
ATOM   22082 C  C   . ALA   B 1 1009 ? 46.48400   81.98200  14.82300  1.000 61.78305  ?  1007 ALA   B C   1 
ATOM   22083 O  O   . ALA   B 1 1009 ? 46.49900   81.94600  16.05900  1.000 64.29516  ?  1007 ALA   B O   1 
ATOM   22084 C  CB  . ALA   B 1 1009 ? 47.86300   80.29900  13.57200  1.000 65.75442  ?  1007 ALA   B CB  1 
ATOM   22085 N  N   . ALA   B 1 1010 ? 46.47400   83.13100  14.14100  1.000 63.79497  ?  1008 ALA   B N   1 
ATOM   22086 C  CA  . ALA   B 1 1010 ? 46.55200   84.41800  14.82500  1.000 64.42470  ?  1008 ALA   B CA  1 
ATOM   22087 C  C   . ALA   B 1 1010 ? 45.32600   84.65900  15.69800  1.000 62.44933  ?  1008 ALA   B C   1 
ATOM   22088 O  O   . ALA   B 1 1010 ? 45.44900   84.92200  16.90100  1.000 65.12069  ?  1008 ALA   B O   1 
ATOM   22089 C  CB  . ALA   B 1 1010 ? 46.71000   85.54200  13.80000  1.000 61.81854  ?  1008 ALA   B CB  1 
ATOM   22090 N  N   . LYS   B 1 1011 ? 44.13300   84.56300  15.11100  1.000 52.25055  ?  1009 LYS   B N   1 
ATOM   22091 C  CA  . LYS   B 1 1011 ? 42.89500   84.81700  15.83800  1.000 49.57536  ?  1009 LYS   B CA  1 
ATOM   22092 C  C   . LYS   B 1 1011 ? 42.71100   83.88800  17.03500  1.000 64.08414  ?  1009 LYS   B C   1 
ATOM   22093 O  O   . LYS   B 1 1011 ? 41.81400   84.12400  17.85300  1.000 77.85172  ?  1009 LYS   B O   1 
ATOM   22094 C  CB  . LYS   B 1 1011 ? 41.72800   84.68500  14.86300  1.000 46.87953  ?  1009 LYS   B CB  1 
ATOM   22095 C  CG  . LYS   B 1 1011 ? 40.34300   84.91200  15.41700  1.000 69.00520  ?  1009 LYS   B CG  1 
ATOM   22096 C  CD  . LYS   B 1 1011 ? 39.37000   84.83200  14.27000  1.000 71.33037  ?  1009 LYS   B CD  1 
ATOM   22097 C  CE  . LYS   B 1 1011 ? 39.55400   83.51000  13.52400  1.000 82.12946  ?  1009 LYS   B CE  1 
ATOM   22098 N  NZ  . LYS   B 1 1011 ? 38.28600   83.01400  12.94300  1.000 78.53588  ?  1009 LYS   B NZ  1 
ATOM   22099 N  N   . HIS   B 1 1012 ? 43.54200   82.85500  17.17500  1.000 56.28503  ?  1010 HIS   B N   1 
ATOM   22100 C  CA  . HIS   B 1 1012 ? 43.44500   81.93000  18.29700  1.000 63.68910  ?  1010 HIS   B CA  1 
ATOM   22101 C  C   . HIS   B 1 1012 ? 44.74200   81.87600  19.09900  1.000 59.37303  ?  1010 HIS   B C   1 
ATOM   22102 O  O   . HIS   B 1 1012 ? 45.09800   80.82700  19.64100  1.000 53.41794  ?  1010 HIS   B O   1 
ATOM   22103 C  CB  . HIS   B 1 1012 ? 43.04500   80.53900  17.81100  1.000 47.89980  ?  1010 HIS   B CB  1 
ATOM   22104 C  CG  . HIS   B 1 1012 ? 41.67100   80.48800  17.21900  1.000 55.69122  ?  1010 HIS   B CG  1 
ATOM   22105 N  ND1 . HIS   B 1 1012 ? 41.41400   80.82200  15.90700  1.000 62.95262  ?  1010 HIS   B ND1 1 
ATOM   22106 C  CD2 . HIS   B 1 1012 ? 40.47700   80.15800  17.76500  1.000 65.37039  ?  1010 HIS   B CD2 1 
ATOM   22107 C  CE1 . HIS   B 1 1012 ? 40.12100   80.69200  15.66700  1.000 68.63004  ?  1010 HIS   B CE1 1 
ATOM   22108 N  NE2 . HIS   B 1 1012 ? 39.53000   80.29100  16.77800  1.000 80.41930  ?  1010 HIS   B NE2 1 
ATOM   22109 N  N   . ASP   B 1 1013 ? 45.44700   83.00700  19.18200  1.000 58.01698  ?  1011 ASP   B N   1 
ATOM   22110 C  CA  . ASP   B 1 1013 ? 46.64000   83.14500  20.02200  1.000 63.64011  ?  1011 ASP   B CA  1 
ATOM   22111 C  C   . ASP   B 1 1013 ? 47.65900   82.05000  19.72900  1.000 61.40096  ?  1011 ASP   B C   1 
ATOM   22112 O  O   . ASP   B 1 1013 ? 48.27200   81.48200  20.63600  1.000 57.03930  ?  1011 ASP   B O   1 
ATOM   22113 C  CB  . ASP   B 1 1013 ? 46.27000   83.15100  21.50500  1.000 68.21405  ?  1011 ASP   B CB  1 
ATOM   22114 C  CG  . ASP   B 1 1013 ? 46.11000   84.54900  22.06100  1.000 59.09924  ?  1011 ASP   B CG  1 
ATOM   22115 O  OD1 . ASP   B 1 1013 ? 45.50600   85.40000  21.37400  1.000 77.04672  ?  1011 ASP   B OD1 1 
ATOM   22116 O  OD2 . ASP   B 1 1013 ? 46.58100   84.79100  23.19100  1.000 63.20232  -1 1011 ASP   B OD2 1 
ATOM   22117 N  N   . LEU   B 1 1014 ? 47.83400   81.74500  18.44600  1.000 58.84673  ?  1012 LEU   B N   1 
ATOM   22118 C  CA  . LEU   B 1 1014 ? 48.75500   80.70800  18.01000  1.000 69.43631  ?  1012 LEU   B CA  1 
ATOM   22119 C  C   . LEU   B 1 1014 ? 49.65200   81.24000  16.90500  1.000 59.36269  ?  1012 LEU   B C   1 
ATOM   22120 O  O   . LEU   B 1 1014 ? 49.25600   82.10400  16.11800  1.000 55.16183  ?  1012 LEU   B O   1 
ATOM   22121 C  CB  . LEU   B 1 1014 ? 48.01000   79.46600  17.50300  1.000 65.47697  ?  1012 LEU   B CB  1 
ATOM   22122 C  CG  . LEU   B 1 1014 ? 47.25700   78.63900  18.54100  1.000 50.14320  ?  1012 LEU   B CG  1 
ATOM   22123 C  CD1 . LEU   B 1 1014 ? 46.16100   77.84100  17.86100  1.000 40.41523  ?  1012 LEU   B CD1 1 
ATOM   22124 C  CD2 . LEU   B 1 1014 ? 48.21300   77.72800  19.30600  1.000 51.01667  ?  1012 LEU   B CD2 1 
ATOM   22125 N  N   . THR   B 1 1015 ? 50.87000   80.71100  16.85500  1.000 56.61519  ?  1013 THR   B N   1 
ATOM   22126 C  CA  . THR   B 1 1015 ? 51.76700   80.96500  15.74300  1.000 51.07276  ?  1013 THR   B CA  1 
ATOM   22127 C  C   . THR   B 1 1015 ? 51.48700   79.96400  14.62500  1.000 58.19461  ?  1013 THR   B C   1 
ATOM   22128 O  O   . THR   B 1 1015 ? 50.64900   79.06800  14.75300  1.000 66.01842  ?  1013 THR   B O   1 
ATOM   22129 C  CB  . THR   B 1 1015 ? 53.21900   80.87900  16.19900  1.000 47.60155  ?  1013 THR   B CB  1 
ATOM   22130 O  OG1 . THR   B 1 1015 ? 53.59300   79.50200  16.33100  1.000 46.73648  ?  1013 THR   B OG1 1 
ATOM   22131 C  CG2 . THR   B 1 1015 ? 53.39300   81.57400  17.53700  1.000 54.46939  ?  1013 THR   B CG2 1 
ATOM   22132 N  N   . LEU   B 1 1016 ? 52.19900   80.11000  13.50700  1.000 51.10909  ?  1014 LEU   B N   1 
ATOM   22133 C  CA  . LEU   B 1 1016 ? 52.04800   79.13900  12.43000  1.000 47.39320  ?  1014 LEU   B CA  1 
ATOM   22134 C  C   . LEU   B 1 1016 ? 52.74700   77.82900  12.76400  1.000 52.04360  ?  1014 LEU   B C   1 
ATOM   22135 O  O   . LEU   B 1 1016 ? 52.25200   76.75300  12.41500  1.000 66.59177  ?  1014 LEU   B O   1 
ATOM   22136 C  CB  . LEU   B 1 1016 ? 52.58500   79.70400  11.11800  1.000 40.45535  ?  1014 LEU   B CB  1 
ATOM   22137 C  CG  . LEU   B 1 1016 ? 52.21700   78.89100  9.87900   1.000 42.77090  ?  1014 LEU   B CG  1 
ATOM   22138 C  CD1 . LEU   B 1 1016 ? 50.70800   78.71200  9.78900   1.000 64.05638  ?  1014 LEU   B CD1 1 
ATOM   22139 C  CD2 . LEU   B 1 1016 ? 52.75500   79.57100  8.63700   1.000 46.00036  ?  1014 LEU   B CD2 1 
ATOM   22140 N  N   . TYR   B 1 1017 ? 53.89900   77.90500  13.43500  1.000 32.91445  ?  1015 TYR   B N   1 
ATOM   22141 C  CA  . TYR   B 1 1017 ? 54.59400   76.69300  13.85500  1.000 36.60048  ?  1015 TYR   B CA  1 
ATOM   22142 C  C   . TYR   B 1 1017 ? 53.70000   75.82300  14.72800  1.000 61.10083  ?  1015 TYR   B C   1 
ATOM   22143 O  O   . TYR   B 1 1017 ? 53.64200   74.60100  14.54700  1.000 64.30345  ?  1015 TYR   B O   1 
ATOM   22144 C  CB  . TYR   B 1 1017 ? 55.87400   77.06800  14.60000  1.000 37.86941  ?  1015 TYR   B CB  1 
ATOM   22145 C  CG  . TYR   B 1 1017 ? 56.62200   75.90900  15.21700  1.000 41.78608  ?  1015 TYR   B CG  1 
ATOM   22146 C  CD1 . TYR   B 1 1017 ? 57.52900   75.16800  14.47100  1.000 49.57094  ?  1015 TYR   B CD1 1 
ATOM   22147 C  CD2 . TYR   B 1 1017 ? 56.43900   75.57000  16.55000  1.000 53.26801  ?  1015 TYR   B CD2 1 
ATOM   22148 C  CE1 . TYR   B 1 1017 ? 58.22500   74.11600  15.03400  1.000 47.63423  ?  1015 TYR   B CE1 1 
ATOM   22149 C  CE2 . TYR   B 1 1017 ? 57.13000   74.51900  17.12100  1.000 56.18248  ?  1015 TYR   B CE2 1 
ATOM   22150 C  CZ  . TYR   B 1 1017 ? 58.02200   73.79600  16.35800  1.000 54.02357  ?  1015 TYR   B CZ  1 
ATOM   22151 O  OH  . TYR   B 1 1017 ? 58.71400   72.75000  16.91900  1.000 48.05661  ?  1015 TYR   B OH  1 
ATOM   22152 N  N   . MET   B 1 1018 ? 52.99100   76.43700  15.67700  1.000 64.81292  ?  1016 MET   B N   1 
ATOM   22153 C  CA  . MET   B 1 1018 ? 52.08300   75.68500  16.53500  1.000 58.85372  ?  1016 MET   B CA  1 
ATOM   22154 C  C   . MET   B 1 1018 ? 50.99200   75.00900  15.71400  1.000 51.63781  ?  1016 MET   B C   1 
ATOM   22155 O  O   . MET   B 1 1018 ? 50.69000   73.82600  15.91300  1.000 67.92518  ?  1016 MET   B O   1 
ATOM   22156 C  CB  . MET   B 1 1018 ? 51.47200   76.61600  17.58200  1.000 58.26650  ?  1016 MET   B CB  1 
ATOM   22157 C  CG  . MET   B 1 1018 ? 52.39200   76.93200  18.74600  1.000 73.39741  ?  1016 MET   B CG  1 
ATOM   22158 S  SD  . MET   B 1 1018 ? 51.98600   78.49300  19.55200  1.000 70.82220  ?  1016 MET   B SD  1 
ATOM   22159 C  CE  . MET   B 1 1018 ? 53.34600   78.59600  20.71200  1.000 28.51374  ?  1016 MET   B CE  1 
ATOM   22160 N  N   . LEU   B 1 1019 ? 50.39000   75.75000  14.78200  1.000 49.18355  ?  1017 LEU   B N   1 
ATOM   22161 C  CA  . LEU   B 1 1019 ? 49.36500   75.17700  13.91500  1.000 40.12238  ?  1017 LEU   B CA  1 
ATOM   22162 C  C   . LEU   B 1 1019 ? 49.91500   73.99900  13.11800  1.000 56.44990  ?  1017 LEU   B C   1 
ATOM   22163 O  O   . LEU   B 1 1019 ? 49.26800   72.95100  13.01100  1.000 62.19828  ?  1017 LEU   B O   1 
ATOM   22164 C  CB  . LEU   B 1 1019 ? 48.81800   76.25200  12.97800  1.000 38.99908  ?  1017 LEU   B CB  1 
ATOM   22165 C  CG  . LEU   B 1 1019 ? 47.57600   75.91900  12.15300  1.000 50.13214  ?  1017 LEU   B CG  1 
ATOM   22166 C  CD1 . LEU   B 1 1019 ? 46.31600   76.30100  12.90300  1.000 47.78680  ?  1017 LEU   B CD1 1 
ATOM   22167 C  CD2 . LEU   B 1 1019 ? 47.63600   76.63500  10.81900  1.000 54.67819  ?  1017 LEU   B CD2 1 
ATOM   22168 N  N   . MET   B 1 1020 ? 51.11600   74.15400  12.55500  1.000 57.59964  ?  1018 MET   B N   1 
ATOM   22169 C  CA  . MET   B 1 1020 ? 51.73100   73.06100  11.80900  1.000 53.75391  ?  1018 MET   B CA  1 
ATOM   22170 C  C   . MET   B 1 1020 ? 52.09300   71.90100  12.72900  1.000 55.43269  ?  1018 MET   B C   1 
ATOM   22171 O  O   . MET   B 1 1020 ? 51.80200   70.73900  12.42000  1.000 56.98065  ?  1018 MET   B O   1 
ATOM   22172 C  CB  . MET   B 1 1020 ? 52.97100   73.56000  11.06700  1.000 58.00254  ?  1018 MET   B CB  1 
ATOM   22173 C  CG  . MET   B 1 1020 ? 52.71300   74.69200  10.09200  1.000 45.01381  ?  1018 MET   B CG  1 
ATOM   22174 S  SD  . MET   B 1 1020 ? 51.96100   74.11700  8.56000   1.000 53.17052  ?  1018 MET   B SD  1 
ATOM   22175 C  CE  . MET   B 1 1020 ? 50.34100   74.86800  8.67600   1.000 45.20773  ?  1018 MET   B CE  1 
ATOM   22176 N  N   . LEU   B 1 1021 ? 52.73600   72.20100  13.86300  1.000 50.47964  ?  1019 LEU   B N   1 
ATOM   22177 C  CA  . LEU   B 1 1021 ? 53.12900   71.16000  14.81100  1.000 51.92570  ?  1019 LEU   B CA  1 
ATOM   22178 C  C   . LEU   B 1 1021 ? 51.94500   70.28900  15.21000  1.000 65.09684  ?  1019 LEU   B C   1 
ATOM   22179 O  O   . LEU   B 1 1021 ? 52.08600   69.07200  15.37900  1.000 61.53430  ?  1019 LEU   B O   1 
ATOM   22180 C  CB  . LEU   B 1 1021 ? 53.75900   71.80000  16.04900  1.000 36.56736  ?  1019 LEU   B CB  1 
ATOM   22181 C  CG  . LEU   B 1 1021 ? 54.47300   70.88300  17.04100  1.000 52.77843  ?  1019 LEU   B CG  1 
ATOM   22182 C  CD1 . LEU   B 1 1021 ? 55.64700   70.19100  16.37800  1.000 55.67124  ?  1019 LEU   B CD1 1 
ATOM   22183 C  CD2 . LEU   B 1 1021 ? 54.93200   71.67400  18.25600  1.000 54.96106  ?  1019 LEU   B CD2 1 
ATOM   22184 N  N   . THR   B 1 1022 ? 50.76800   70.89600  15.36400  1.000 53.86415  ?  1020 THR   B N   1 
ATOM   22185 C  CA  . THR   B 1 1022 ? 49.56900   70.12700  15.67700  1.000 59.31964  ?  1020 THR   B CA  1 
ATOM   22186 C  C   . THR   B 1 1022 ? 49.19800   69.20100  14.52500  1.000 68.85470  ?  1020 THR   B C   1 
ATOM   22187 O  O   . THR   B 1 1022 ? 48.98000   68.00000  14.72300  1.000 73.53349  ?  1020 THR   B O   1 
ATOM   22188 C  CB  . THR   B 1 1022 ? 48.41500   71.07600  15.99900  1.000 72.39693  ?  1020 THR   B CB  1 
ATOM   22189 O  OG1 . THR   B 1 1022 ? 48.82400   71.99100  17.02300  1.000 62.16050  ?  1020 THR   B OG1 1 
ATOM   22190 C  CG2 . THR   B 1 1022 ? 47.19100   70.29600  16.46700  1.000 59.82212  ?  1020 THR   B CG2 1 
ATOM   22191 N  N   . ILE   B 1 1023 ? 49.12800   69.74700  13.30800  1.000 59.82696  ?  1021 ILE   B N   1 
ATOM   22192 C  CA  . ILE   B 1 1023 ? 48.75500   68.94300  12.14600  1.000 47.64092  ?  1021 ILE   B CA  1 
ATOM   22193 C  C   . ILE   B 1 1023 ? 49.75700   67.81700  11.92700  1.000 53.99655  ?  1021 ILE   B C   1 
ATOM   22194 O  O   . ILE   B 1 1023 ? 49.37800   66.68400  11.60800  1.000 59.19251  ?  1021 ILE   B O   1 
ATOM   22195 C  CB  . ILE   B 1 1023 ? 48.62700   69.83800  10.90000  1.000 35.06623  ?  1021 ILE   B CB  1 
ATOM   22196 C  CG1 . ILE   B 1 1023 ? 47.60300   70.94700  11.14700  1.000 47.67622  ?  1021 ILE   B CG1 1 
ATOM   22197 C  CG2 . ILE   B 1 1023 ? 48.23200   69.01500  9.68900   1.000 44.57168  ?  1021 ILE   B CG2 1 
ATOM   22198 C  CD1 . ILE   B 1 1023 ? 47.43500   71.89000  9.97700   1.000 45.18979  ?  1021 ILE   B CD1 1 
ATOM   22199 N  N   . VAL   B 1 1024 ? 51.04900   68.10800  12.09800  1.000 46.00579  ?  1022 VAL   B N   1 
ATOM   22200 C  CA  . VAL   B 1 1024 ? 52.07200   67.07600  11.94800  1.000 49.58491  ?  1022 VAL   B CA  1 
ATOM   22201 C  C   . VAL   B 1 1024 ? 51.83300   65.94200  12.93800  1.000 63.87860  ?  1022 VAL   B C   1 
ATOM   22202 O  O   . VAL   B 1 1024 ? 51.97700   64.76000  12.60100  1.000 72.51365  ?  1022 VAL   B O   1 
ATOM   22203 C  CB  . VAL   B 1 1024 ? 53.47600   67.69200  12.11200  1.000 48.15505  ?  1022 VAL   B CB  1 
ATOM   22204 C  CG1 . VAL   B 1 1024 ? 54.52700   66.60800  12.28700  1.000 35.44985  ?  1022 VAL   B CG1 1 
ATOM   22205 C  CG2 . VAL   B 1 1024 ? 53.81300   68.56500  10.91500  1.000 39.27879  ?  1022 VAL   B CG2 1 
ATOM   22206 N  N   . SER   B 1 1025 ? 51.43600   66.28000  14.16400  1.000 69.38012  ?  1023 SER   B N   1 
ATOM   22207 C  CA  . SER   B 1 1025 ? 51.25800   65.26200  15.19300  1.000 73.70349  ?  1023 SER   B CA  1 
ATOM   22208 C  C   . SER   B 1 1025 ? 49.99900   64.44100  14.95300  1.000 64.38799  ?  1023 SER   B C   1 
ATOM   22209 O  O   . SER   B 1 1025 ? 50.01600   63.21300  15.09700  1.000 73.64620  ?  1023 SER   B O   1 
ATOM   22210 C  CB  . SER   B 1 1025 ? 51.21900   65.92300  16.56400  1.000 68.68914  ?  1023 SER   B CB  1 
ATOM   22211 O  OG  . SER   B 1 1025 ? 52.26600   66.86500  16.66200  1.000 68.71624  ?  1023 SER   B OG  1 
ATOM   22212 N  N   . ILE   B 1 1026 ? 48.89200   65.10300  14.60600  1.000 54.86644  ?  1024 ILE   B N   1 
ATOM   22213 C  CA  . ILE   B 1 1026 ? 47.68800   64.38000  14.20700  1.000 56.63782  ?  1024 ILE   B CA  1 
ATOM   22214 C  C   . ILE   B 1 1026 ? 48.00400   63.42800  13.06500  1.000 63.80180  ?  1024 ILE   B C   1 
ATOM   22215 O  O   . ILE   B 1 1026 ? 47.54500   62.27900  13.04000  1.000 68.21299  ?  1024 ILE   B O   1 
ATOM   22216 C  CB  . ILE   B 1 1026 ? 46.57900   65.37100  13.81300  1.000 48.25159  ?  1024 ILE   B CB  1 
ATOM   22217 C  CG1 . ILE   B 1 1026 ? 46.26900   66.31900  14.97000  1.000 51.86371  ?  1024 ILE   B CG1 1 
ATOM   22218 C  CG2 . ILE   B 1 1026 ? 45.34000   64.62400  13.36100  1.000 52.22973  ?  1024 ILE   B CG2 1 
ATOM   22219 C  CD1 . ILE   B 1 1026 ? 45.49500   67.53900  14.54700  1.000 51.32088  ?  1024 ILE   B CD1 1 
ATOM   22220 N  N   . TRP   B 1 1027 ? 48.80000   63.89900  12.10500  1.000 77.32439  ?  1025 TRP   B N   1 
ATOM   22221 C  CA  . TRP   B 1 1027 ? 49.21000   63.07900  10.97200  1.000 72.55790  ?  1025 TRP   B CA  1 
ATOM   22222 C  C   . TRP   B 1 1027 ? 50.02300   61.87200  11.43200  1.000 66.79766  ?  1025 TRP   B C   1 
ATOM   22223 O  O   . TRP   B 1 1027 ? 49.76700   60.73800  11.00900  1.000 62.38358  ?  1025 TRP   B O   1 
ATOM   22224 C  CB  . TRP   B 1 1027 ? 50.00100   63.95400  9.99700   1.000 54.47044  ?  1025 TRP   B CB  1 
ATOM   22225 C  CG  . TRP   B 1 1027 ? 50.54000   63.27000  8.78900   1.000 55.61773  ?  1025 TRP   B CG  1 
ATOM   22226 C  CD1 . TRP   B 1 1027 ? 49.82600   62.67400  7.79000   1.000 62.47904  ?  1025 TRP   B CD1 1 
ATOM   22227 C  CD2 . TRP   B 1 1027 ? 51.92000   63.14000  8.43000   1.000 49.74068  ?  1025 TRP   B CD2 1 
ATOM   22228 N  NE1 . TRP   B 1 1027 ? 50.67800   62.16700  6.83800   1.000 63.36764  ?  1025 TRP   B NE1 1 
ATOM   22229 C  CE2 . TRP   B 1 1027 ? 51.96900   62.44100  7.20800   1.000 53.75458  ?  1025 TRP   B CE2 1 
ATOM   22230 C  CE3 . TRP   B 1 1027 ? 53.11900   63.54100  9.02800   1.000 45.23321  ?  1025 TRP   B CE3 1 
ATOM   22231 C  CZ2 . TRP   B 1 1027 ? 53.17100   62.13400  6.57300   1.000 47.34796  ?  1025 TRP   B CZ2 1 
ATOM   22232 C  CZ3 . TRP   B 1 1027 ? 54.31100   63.23400  8.39700   1.000 52.50080  ?  1025 TRP   B CZ3 1 
ATOM   22233 C  CH2 . TRP   B 1 1027 ? 54.32900   62.53800  7.18200   1.000 49.91608  ?  1025 TRP   B CH2 1 
ATOM   22234 N  N   . LEU   B 1 1028 ? 51.00200   62.09700  12.31200  1.000 46.72068  ?  1026 LEU   B N   1 
ATOM   22235 C  CA  . LEU   B 1 1028 ? 51.79800   60.98600  12.82700  1.000 60.29085  ?  1026 LEU   B CA  1 
ATOM   22236 C  C   . LEU   B 1 1028 ? 50.93900   60.01600  13.63000  1.000 62.91581  ?  1026 LEU   B C   1 
ATOM   22237 O  O   . LEU   B 1 1028 ? 51.13100   58.79600  13.55200  1.000 65.53375  ?  1026 LEU   B O   1 
ATOM   22238 C  CB  . LEU   B 1 1028 ? 52.94600   61.51700  13.68500  1.000 53.98039  ?  1026 LEU   B CB  1 
ATOM   22239 C  CG  . LEU   B 1 1028 ? 54.06900   62.23300  12.93700  1.000 60.94727  ?  1026 LEU   B CG  1 
ATOM   22240 C  CD1 . LEU   B 1 1028 ? 55.11500   62.75000  13.91300  1.000 59.09344  ?  1026 LEU   B CD1 1 
ATOM   22241 C  CD2 . LEU   B 1 1028 ? 54.69800   61.30900  11.90500  1.000 64.53229  ?  1026 LEU   B CD2 1 
ATOM   22242 N  N   . SER   B 1 1029 ? 49.99100   60.54000  14.41000  1.000 61.85180  ?  1027 SER   B N   1 
ATOM   22243 C  CA  . SER   B 1 1029 ? 49.11200   59.67900  15.19700  1.000 65.19784  ?  1027 SER   B CA  1 
ATOM   22244 C  C   . SER   B 1 1029 ? 48.29200   58.76500  14.29900  1.000 70.25167  ?  1027 SER   B C   1 
ATOM   22245 O  O   . SER   B 1 1029 ? 48.24500   57.54800  14.51100  1.000 64.44078  ?  1027 SER   B O   1 
ATOM   22246 C  CB  . SER   B 1 1029 ? 48.19000   60.52600  16.07300  1.000 61.45688  ?  1027 SER   B CB  1 
ATOM   22247 O  OG  . SER   B 1 1029 ? 48.73800   60.70100  17.36500  1.000 87.16093  ?  1027 SER   B OG  1 
ATOM   22248 N  N   . LYS   B 1 1030 ? 47.64200   59.34000  13.28300  1.000 65.22501  ?  1028 LYS   B N   1 
ATOM   22249 C  CA  . LYS   B 1 1030 ? 46.79700   58.55700  12.38700  1.000 63.16117  ?  1028 LYS   B CA  1 
ATOM   22250 C  C   . LYS   B 1 1030 ? 47.57300   57.43700  11.70300  1.000 70.26133  ?  1028 LYS   B C   1 
ATOM   22251 O  O   . LYS   B 1 1030 ? 46.98200   56.42100  11.31900  1.000 76.22086  ?  1028 LYS   B O   1 
ATOM   22252 C  CB  . LYS   B 1 1030 ? 46.15600   59.47400  11.34400  1.000 67.19460  ?  1028 LYS   B CB  1 
ATOM   22253 C  CG  . LYS   B 1 1030 ? 44.70800   59.83200  11.63500  1.000 70.22944  ?  1028 LYS   B CG  1 
ATOM   22254 C  CD  . LYS   B 1 1030 ? 44.60100   60.95800  12.64700  1.000 52.59344  ?  1028 LYS   B CD  1 
ATOM   22255 C  CE  . LYS   B 1 1030 ? 43.15000   61.36800  12.85600  1.000 74.13595  ?  1028 LYS   B CE  1 
ATOM   22256 N  NZ  . LYS   B 1 1030 ? 42.47600   61.74000  11.58200  1.000 68.12571  ?  1028 LYS   B NZ  1 
ATOM   22257 N  N   . MET   B 1 1031 ? 48.88500   57.60000  11.53400  1.000 63.89380  ?  1029 MET   B N   1 
ATOM   22258 C  CA  . MET   B 1 1031 ? 49.71600   56.53700  10.98500  1.000 57.58126  ?  1029 MET   B CA  1 
ATOM   22259 C  C   . MET   B 1 1031 ? 50.23900   55.59300  12.05600  1.000 64.93538  ?  1029 MET   B C   1 
ATOM   22260 O  O   . MET   B 1 1031 ? 50.64300   54.47000  11.73300  1.000 69.31405  ?  1029 MET   B O   1 
ATOM   22261 C  CB  . MET   B 1 1031 ? 50.89500   57.13100  10.20700  1.000 54.95470  ?  1029 MET   B CB  1 
ATOM   22262 C  CG  . MET   B 1 1031 ? 50.52900   57.62300  8.81300   1.000 67.00711  ?  1029 MET   B CG  1 
ATOM   22263 S  SD  . MET   B 1 1031 ? 51.87200   58.48800  7.96900   1.000 59.60025  ?  1029 MET   B SD  1 
ATOM   22264 C  CE  . MET   B 1 1031 ? 52.74500   59.20900  9.35400   1.000 42.90390  ?  1029 MET   B CE  1 
ATOM   22265 N  N   . ASN   B 1 1032 ? 50.24500   56.02300  13.31400  1.000 66.28797  ?  1030 ASN   B N   1 
ATOM   22266 C  CA  . ASN   B 1 1032 ? 50.61700   55.16300  14.43400  1.000 66.21065  ?  1030 ASN   B CA  1 
ATOM   22267 C  C   . ASN   B 1 1032 ? 49.34900   54.75200  15.17800  1.000 63.39365  ?  1030 ASN   B C   1 
ATOM   22268 O  O   . ASN   B 1 1032 ? 49.05100   55.21900  16.27900  1.000 73.73019  ?  1030 ASN   B O   1 
ATOM   22269 C  CB  . ASN   B 1 1032 ? 51.60900   55.88300  15.34400  1.000 59.05089  ?  1030 ASN   B CB  1 
ATOM   22270 C  CG  . ASN   B 1 1032 ? 52.29200   54.94900  16.31900  1.000 60.95135  ?  1030 ASN   B CG  1 
ATOM   22271 O  OD1 . ASN   B 1 1032 ? 52.97300   54.00500  15.92000  1.000 74.61724  ?  1030 ASN   B OD1 1 
ATOM   22272 N  ND2 . ASN   B 1 1032 ? 52.12400   55.21500  17.60900  1.000 71.06969  ?  1030 ASN   B ND2 1 
ATOM   22273 N  N   . SER   B 1 1033 ? 48.59800   53.85500  14.53800  1.000 76.42730  ?  1031 SER   B N   1 
ATOM   22274 C  CA  . SER   B 1 1033 ? 47.22700   53.50300  14.94200  1.000 73.28135  ?  1031 SER   B CA  1 
ATOM   22275 C  C   . SER   B 1 1033 ? 46.44900   54.81800  14.94600  1.000 74.13528  ?  1031 SER   B C   1 
ATOM   22276 O  O   . SER   B 1 1033 ? 46.47900   55.53800  13.93600  1.000 97.41338  ?  1031 SER   B O   1 
ATOM   22277 C  CB  . SER   B 1 1033 ? 47.23800   52.73400  16.25800  1.000 83.83750  ?  1031 SER   B CB  1 
ATOM   22278 O  OG  . SER   B 1 1033 ? 47.48100   53.60400  17.35100  1.000 91.86472  ?  1031 SER   B OG  1 
ATOM   22279 N  N   . ASP   B 1 1034 ? 45.74400   55.16500  16.02200  1.000 62.51735  ?  1032 ASP   B N   1 
ATOM   22280 C  CA  . ASP   B 1 1034 ? 45.26900   56.52800  16.25100  1.000 52.48243  ?  1032 ASP   B CA  1 
ATOM   22281 C  C   . ASP   B 1 1034 ? 45.70700   56.94300  17.65500  1.000 59.77324  ?  1032 ASP   B C   1 
ATOM   22282 O  O   . ASP   B 1 1034 ? 44.90000   57.20600  18.54600  1.000 71.69075  ?  1032 ASP   B O   1 
ATOM   22283 C  CB  . ASP   B 1 1034 ? 43.75500   56.65900  16.06600  1.000 61.88005  ?  1032 ASP   B CB  1 
ATOM   22284 C  CG  . ASP   B 1 1034 ? 43.36400   56.99500  14.62800  1.000 73.29738  ?  1032 ASP   B CG  1 
ATOM   22285 O  OD1 . ASP   B 1 1034 ? 43.85200   56.32200  13.69500  1.000 58.22610  ?  1032 ASP   B OD1 1 
ATOM   22286 O  OD2 . ASP   B 1 1034 ? 42.57300   57.94200  14.42900  1.000 81.08295  -1 1032 ASP   B OD2 1 
ATOM   22287 N  N   . SER   B 1 1035 ? 47.02700   56.98600  17.84000  1.000 58.18692  ?  1033 SER   B N   1 
ATOM   22288 C  CA  . SER   B 1 1035 ? 47.61800   57.17600  19.15600  1.000 59.38981  ?  1033 SER   B CA  1 
ATOM   22289 C  C   . SER   B 1 1035 ? 47.18600   58.50200  19.77200  1.000 83.75782  ?  1033 SER   B C   1 
ATOM   22290 O  O   . SER   B 1 1035 ? 46.89400   59.47600  19.07300  1.000 86.19412  ?  1033 SER   B O   1 
ATOM   22291 C  CB  . SER   B 1 1035 ? 49.14200   57.11900  19.06200  1.000 53.41119  ?  1033 SER   B CB  1 
ATOM   22292 O  OG  . SER   B 1 1035 ? 49.74000   57.67200  20.22000  1.000 68.36353  ?  1033 SER   B OG  1 
ATOM   22293 N  N   . ASN   B 1 1036 ? 47.14300   58.52400  21.10300  1.000 90.09351  ?  1034 ASN   B N   1 
ATOM   22294 C  CA  . ASN   B 1 1036 ? 46.82000   59.72500  21.85900  1.000 85.59006  ?  1034 ASN   B CA  1 
ATOM   22295 C  C   . ASN   B 1 1036 ? 48.06000   60.46900  22.33300  1.000 78.07078  ?  1034 ASN   B C   1 
ATOM   22296 O  O   . ASN   B 1 1036 ? 47.93200   61.55000  22.91500  1.000 83.52714  ?  1034 ASN   B O   1 
ATOM   22297 C  CB  . ASN   B 1 1036 ? 45.93500   59.37500  23.06200  1.000 95.57010  ?  1034 ASN   B CB  1 
ATOM   22298 C  CG  . ASN   B 1 1036 ? 44.68400   58.61000  22.66600  1.000 95.80134  ?  1034 ASN   B CG  1 
ATOM   22299 O  OD1 . ASN   B 1 1036 ? 44.76200   57.49800  22.14300  1.000 107.25871 ?  1034 ASN   B OD1 1 
ATOM   22300 N  ND2 . ASN   B 1 1036 ? 43.52200   59.20500  22.91400  1.000 80.25722  ?  1034 ASN   B ND2 1 
ATOM   22301 N  N   . GLN   B 1 1037 ? 49.25100   59.92000  22.09600  1.000 63.14289  ?  1035 GLN   B N   1 
ATOM   22302 C  CA  . GLN   B 1 1037 ? 50.50300   60.54800  22.50300  1.000 66.45284  ?  1035 GLN   B CA  1 
ATOM   22303 C  C   . GLN   B 1 1037 ? 51.55500   60.28100  21.43800  1.000 80.81712  ?  1035 GLN   B C   1 
ATOM   22304 O  O   . GLN   B 1 1037 ? 51.83400   59.12100  21.11900  1.000 82.82392  ?  1035 GLN   B O   1 
ATOM   22305 C  CB  . GLN   B 1 1037 ? 50.97000   60.01700  23.86100  1.000 70.29017  ?  1035 GLN   B CB  1 
ATOM   22306 C  CG  . GLN   B 1 1037 ? 50.29300   60.66700  25.05000  1.000 68.59487  ?  1035 GLN   B CG  1 
ATOM   22307 C  CD  . GLN   B 1 1037 ? 51.28600   61.11400  26.10100  1.000 86.67162  ?  1035 GLN   B CD  1 
ATOM   22308 O  OE1 . GLN   B 1 1037 ? 51.28500   62.27100  26.52200  1.000 87.62297  ?  1035 GLN   B OE1 1 
ATOM   22309 N  NE2 . GLN   B 1 1037 ? 52.14700   60.19700  26.52700  1.000 81.17029  ?  1035 GLN   B NE2 1 
ATOM   22310 N  N   . VAL   B 1 1038 ? 52.13800   61.34600  20.89600  1.000 88.05994  ?  1036 VAL   B N   1 
ATOM   22311 C  CA  . VAL   B 1 1038 ? 53.16000   61.24100  19.86500  1.000 56.53795  ?  1036 VAL   B CA  1 
ATOM   22312 C  C   . VAL   B 1 1038 ? 54.49400   61.72000  20.43200  1.000 55.22088  ?  1036 VAL   B C   1 
ATOM   22313 O  O   . VAL   B 1 1038 ? 54.58100   62.21100  21.55700  1.000 61.26087  ?  1036 VAL   B O   1 
ATOM   22314 C  CB  . VAL   B 1 1038 ? 52.78900   62.03100  18.59400  1.000 68.10831  ?  1036 VAL   B CB  1 
ATOM   22315 C  CG1 . VAL   B 1 1038 ? 51.81900   61.23800  17.73400  1.000 67.45450  ?  1036 VAL   B CG1 1 
ATOM   22316 C  CG2 . VAL   B 1 1038 ? 52.20400   63.38600  18.96200  1.000 62.10276  ?  1036 VAL   B CG2 1 
ATOM   22317 N  N   . ILE   B 1 1039 ? 55.54400   61.57400  19.62600  1.000 55.94994  ?  1037 ILE   B N   1 
ATOM   22318 C  CA  . ILE   B 1 1039 ? 56.87700   62.03800  19.99200  1.000 56.49417  ?  1037 ILE   B CA  1 
ATOM   22319 C  C   . ILE   B 1 1039 ? 57.66000   62.34500  18.72100  1.000 71.79999  ?  1037 ILE   B C   1 
ATOM   22320 O  O   . ILE   B 1 1039 ? 57.84500   61.47500  17.86200  1.000 77.02794  ?  1037 ILE   B O   1 
ATOM   22321 C  CB  . ILE   B 1 1039 ? 57.61300   61.00800  20.86800  1.000 46.19770  ?  1037 ILE   B CB  1 
ATOM   22322 C  CG1 . ILE   B 1 1039 ? 59.10500   61.34200  20.94800  1.000 65.63782  ?  1037 ILE   B CG1 1 
ATOM   22323 C  CG2 . ILE   B 1 1039 ? 57.39700   59.59800  20.33800  1.000 67.18834  ?  1037 ILE   B CG2 1 
ATOM   22324 C  CD1 . ILE   B 1 1039 ? 59.79300   60.78200  22.17500  1.000 65.10204  ?  1037 ILE   B CD1 1 
ATOM   22325 N  N   . LEU   B 1 1040 ? 58.11800   63.58600  18.58800  1.000 60.90831  ?  1038 LEU   B N   1 
ATOM   22326 C  CA  . LEU   B 1 1040 ? 58.84700   64.01500  17.40500  1.000 52.06793  ?  1038 LEU   B CA  1 
ATOM   22327 C  C   . LEU   B 1 1040 ? 60.01800   64.87700  17.85800  1.000 53.94222  ?  1038 LEU   B C   1 
ATOM   22328 O  O   . LEU   B 1 1040 ? 60.35600   64.92600  19.04400  1.000 73.56030  ?  1038 LEU   B O   1 
ATOM   22329 C  CB  . LEU   B 1 1040 ? 57.91200   64.74400  16.43100  1.000 44.81280  ?  1038 LEU   B CB  1 
ATOM   22330 C  CG  . LEU   B 1 1040 ? 57.15700   65.94900  16.99000  1.000 59.65066  ?  1038 LEU   B CG  1 
ATOM   22331 C  CD1 . LEU   B 1 1040 ? 57.76600   67.23800  16.48100  1.000 71.43036  ?  1038 LEU   B CD1 1 
ATOM   22332 C  CD2 . LEU   B 1 1040 ? 55.68400   65.87300  16.62700  1.000 49.51493  ?  1038 LEU   B CD2 1 
ATOM   22333 N  N   . GLY   B 1 1041 ? 60.65000   65.55900  16.90100  1.000 55.76011  ?  1039 GLY   B N   1 
ATOM   22334 C  CA  . GLY   B 1 1041 ? 61.78200   66.40700  17.19300  1.000 57.14034  ?  1039 GLY   B CA  1 
ATOM   22335 C  C   . GLY   B 1 1041 ? 61.61200   67.78000  16.56700  1.000 58.94259  ?  1039 GLY   B C   1 
ATOM   22336 O  O   . GLY   B 1 1041 ? 60.75300   67.99700  15.70900  1.000 57.80499  ?  1039 GLY   B O   1 
ATOM   22337 N  N   . THR   B 1 1042 ? 62.45700   68.70500  17.01400  1.000 63.06164  ?  1040 THR   B N   1 
ATOM   22338 C  CA  . THR   B 1 1042 ? 62.42800   70.07300  16.51600  1.000 45.75419  ?  1040 THR   B CA  1 
ATOM   22339 C  C   . THR   B 1 1042 ? 63.76700   70.72500  16.82300  1.000 42.77379  ?  1040 THR   B C   1 
ATOM   22340 O  O   . THR   B 1 1042 ? 64.51500   70.27000  17.69300  1.000 53.15004  ?  1040 THR   B O   1 
ATOM   22341 C  CB  . THR   B 1 1042 ? 61.27400   70.87100  17.13500  1.000 44.94037  ?  1040 THR   B CB  1 
ATOM   22342 O  OG1 . THR   B 1 1042 ? 60.98000   72.01100  16.31900  1.000 52.91209  ?  1040 THR   B OG1 1 
ATOM   22343 C  CG2 . THR   B 1 1042 ? 61.63600   71.33600  18.53700  1.000 53.87716  ?  1040 THR   B CG2 1 
ATOM   22344 N  N   . VAL   B 1 1043 ? 64.06800   71.79000  16.08500  1.000 46.27316  ?  1041 VAL   B N   1 
ATOM   22345 C  CA  . VAL   B 1 1043 ? 65.28400   72.56900  16.28600  1.000 54.60753  ?  1041 VAL   B CA  1 
ATOM   22346 C  C   . VAL   B 1 1043 ? 64.88500   73.96300  16.74500  1.000 55.51153  ?  1041 VAL   B C   1 
ATOM   22347 O  O   . VAL   B 1 1043 ? 63.86600   74.50900  16.30500  1.000 57.13192  ?  1041 VAL   B O   1 
ATOM   22348 C  CB  . VAL   B 1 1043 ? 66.16000   72.62200  15.01800  1.000 37.44204  ?  1041 VAL   B CB  1 
ATOM   22349 C  CG1 . VAL   B 1 1043 ? 66.47900   71.21300  14.54200  1.000 35.30978  ?  1041 VAL   B CG1 1 
ATOM   22350 C  CG2 . VAL   B 1 1043 ? 65.47800   73.41500  13.91500  1.000 49.53755  ?  1041 VAL   B CG2 1 
ATOM   22351 N  N   . THR   B 1 1044 ? 65.67400   74.52400  17.65500  1.000 57.25362  ?  1042 THR   B N   1 
ATOM   22352 C  CA  . THR   B 1 1044 ? 65.37800   75.81100  18.26300  1.000 62.77795  ?  1042 THR   B CA  1 
ATOM   22353 C  C   . THR   B 1 1044 ? 66.60700   76.70100  18.17400  1.000 66.60404  ?  1042 THR   B C   1 
ATOM   22354 O  O   . THR   B 1 1044 ? 67.73700   76.21600  18.27400  1.000 58.90086  ?  1042 THR   B O   1 
ATOM   22355 C  CB  . THR   B 1 1044 ? 64.95500   75.65900  19.73400  1.000 62.20565  ?  1042 THR   B CB  1 
ATOM   22356 O  OG1 . THR   B 1 1044 ? 66.03900   75.10600  20.49000  1.000 62.91416  ?  1042 THR   B OG1 1 
ATOM   22357 C  CG2 . THR   B 1 1044 ? 63.74800   74.74200  19.85400  1.000 38.24051  ?  1042 THR   B CG2 1 
ATOM   22358 N  N   . ASP   B 1 1045 ? 66.37900   78.00000  17.98400  1.000 62.82867  ?  1043 ASP   B N   1 
ATOM   22359 C  CA  . ASP   B 1 1045 ? 67.47500   78.96000  17.98100  1.000 62.72894  ?  1043 ASP   B CA  1 
ATOM   22360 C  C   . ASP   B 1 1045 ? 68.19200   78.94500  19.32500  1.000 69.95591  ?  1043 ASP   B C   1 
ATOM   22361 O  O   . ASP   B 1 1045 ? 67.56900   79.09100  20.38100  1.000 78.32730  ?  1043 ASP   B O   1 
ATOM   22362 C  CB  . ASP   B 1 1045 ? 66.94900   80.36500  17.67500  1.000 67.45981  ?  1043 ASP   B CB  1 
ATOM   22363 C  CG  . ASP   B 1 1045 ? 65.97500   80.87200  18.73100  1.000 79.35521  ?  1043 ASP   B CG  1 
ATOM   22364 O  OD1 . ASP   B 1 1045 ? 64.80000   80.44400  18.72100  1.000 80.50971  ?  1043 ASP   B OD1 1 
ATOM   22365 O  OD2 . ASP   B 1 1045 ? 66.39000   81.69100  19.58100  1.000 62.26003  -1 1043 ASP   B OD2 1 
ATOM   22366 N  N   . GLY   B 1 1046 ? 69.50700   78.76100  19.28900  1.000 67.17997  ?  1044 GLY   B N   1 
ATOM   22367 C  CA  . GLY   B 1 1046 ? 70.27500   78.76100  20.51800  1.000 69.49821  ?  1044 GLY   B CA  1 
ATOM   22368 C  C   . GLY   B 1 1046 ? 70.66000   80.16300  20.93400  1.000 79.67150  ?  1044 GLY   B C   1 
ATOM   22369 O  O   . GLY   B 1 1046 ? 71.63700   80.36400  21.66100  1.000 92.18958  ?  1044 GLY   B O   1 
ATOM   22370 N  N   . ARG   B 1 1047 ? 69.88900   81.14400  20.46700  1.000 76.10657  ?  1045 ARG   B N   1 
ATOM   22371 C  CA  . ARG   B 1 1047 ? 70.16300   82.55600  20.72100  1.000 78.49878  ?  1045 ARG   B CA  1 
ATOM   22372 C  C   . ARG   B 1 1047 ? 69.75700   82.88000  22.15700  1.000 82.24237  ?  1045 ARG   B C   1 
ATOM   22373 O  O   . ARG   B 1 1047 ? 68.70400   83.46100  22.43100  1.000 79.62091  ?  1045 ARG   B O   1 
ATOM   22374 C  CB  . ARG   B 1 1047 ? 69.42900   83.42600  19.70900  1.000 64.06961  ?  1045 ARG   B CB  1 
ATOM   22375 C  CG  . ARG   B 1 1047 ? 70.31400   83.96200  18.59300  1.000 72.07423  ?  1045 ARG   B CG  1 
ATOM   22376 C  CD  . ARG   B 1 1047 ? 70.89900   82.84300  17.73900  1.000 52.97307  ?  1045 ARG   B CD  1 
ATOM   22377 N  NE  . ARG   B 1 1047 ? 71.97800   83.32700  16.88300  1.000 58.54155  ?  1045 ARG   B NE  1 
ATOM   22378 C  CZ  . ARG   B 1 1047 ? 72.40800   82.71100  15.79100  1.000 44.98773  ?  1045 ARG   B CZ  1 
ATOM   22379 N  NH1 . ARG   B 1 1047 ? 71.87000   81.57600  15.38000  1.000 60.84282  ?  1045 ARG   B NH1 1 
ATOM   22380 N  NH2 . ARG   B 1 1047 ? 73.41000   83.24400  15.09700  1.000 48.10760  ?  1045 ARG   B NH2 1 
ATOM   22381 N  N   . GLN   B 1 1048 ? 70.62700   82.49500  23.09500  1.000 76.51279  ?  1046 GLN   B N   1 
ATOM   22382 C  CA  . GLN   B 1 1048 ? 70.34100   82.69300  24.51400  1.000 71.43566  ?  1046 GLN   B CA  1 
ATOM   22383 C  C   . GLN   B 1 1048 ? 70.59200   84.13900  24.93400  1.000 63.28536  ?  1046 GLN   B C   1 
ATOM   22384 O  O   . GLN   B 1 1048 ? 69.67600   84.83200  25.38800  1.000 61.83367  ?  1046 GLN   B O   1 
ATOM   22385 C  CB  . GLN   B 1 1048 ? 71.18100   81.72900  25.35900  1.000 73.05263  ?  1046 GLN   B CB  1 
ATOM   22386 C  CG  . GLN   B 1 1048 ? 70.60500   81.46200  26.74300  1.000 71.67286  ?  1046 GLN   B CG  1 
ATOM   22387 C  CD  . GLN   B 1 1048 ? 71.26000   80.28100  27.43600  1.000 71.15904  ?  1046 GLN   B CD  1 
ATOM   22388 O  OE1 . GLN   B 1 1048 ? 72.12000   79.60900  26.86700  1.000 68.39200  ?  1046 GLN   B OE1 1 
ATOM   22389 N  NE2 . GLN   B 1 1048 ? 70.85600   80.02800  28.67600  1.000 60.63930  ?  1046 GLN   B NE2 1 
ATOM   22390 N  N   . HIS   B 1 1049 ? 71.82900   84.61100  24.78600  1.000 61.33603  ?  1047 HIS   B N   1 
ATOM   22391 C  CA  . HIS   B 1 1049 ? 72.15800   85.97600  25.15800  1.000 66.48418  ?  1047 HIS   B CA  1 
ATOM   22392 C  C   . HIS   B 1 1049 ? 71.69000   86.95000  24.07600  1.000 68.10437  ?  1047 HIS   B C   1 
ATOM   22393 O  O   . HIS   B 1 1049 ? 71.69400   86.61700  22.89000  1.000 69.64693  ?  1047 HIS   B O   1 
ATOM   22394 C  CB  . HIS   B 1 1049 ? 73.66400   86.12200  25.36100  1.000 63.57855  ?  1047 HIS   B CB  1 
ATOM   22395 C  CG  . HIS   B 1 1049 ? 74.04200   87.13100  26.40200  1.000 71.05103  ?  1047 HIS   B CG  1 
ATOM   22396 N  ND1 . HIS   B 1 1049 ? 75.29400   87.70200  26.46600  1.000 80.13586  ?  1047 HIS   B ND1 1 
ATOM   22397 C  CD2 . HIS   B 1 1049 ? 73.34400   87.64200  27.44300  1.000 70.82865  ?  1047 HIS   B CD2 1 
ATOM   22398 C  CE1 . HIS   B 1 1049 ? 75.34000   88.54500  27.48200  1.000 87.54785  ?  1047 HIS   B CE1 1 
ATOM   22399 N  NE2 . HIS   B 1 1049 ? 74.17000   88.52400  28.09400  1.000 81.53296  ?  1047 HIS   B NE2 1 
ATOM   22400 N  N   . PRO   B 1 1050 ? 71.24800   88.15300  24.45800  1.000 57.35976  ?  1048 PRO   B N   1 
ATOM   22401 C  CA  . PRO   B 1 1050 ? 70.97300   89.17500  23.43400  1.000 51.99158  ?  1048 PRO   B CA  1 
ATOM   22402 C  C   . PRO   B 1 1050 ? 72.15000   89.44100  22.51400  1.000 57.07657  ?  1048 PRO   B C   1 
ATOM   22403 O  O   . PRO   B 1 1050 ? 71.95400   89.68700  21.31600  1.000 46.80420  ?  1048 PRO   B O   1 
ATOM   22404 C  CB  . PRO   B 1 1050 ? 70.61300   90.40700  24.27300  1.000 53.98909  ?  1048 PRO   B CB  1 
ATOM   22405 C  CG  . PRO   B 1 1050 ? 69.98600   89.82900  25.48800  1.000 56.33336  ?  1048 PRO   B CG  1 
ATOM   22406 C  CD  . PRO   B 1 1050 ? 70.75300   88.56400  25.78300  1.000 59.08084  ?  1048 PRO   B CD  1 
ATOM   22407 N  N   . ASP   B 1 1051 ? 73.37600   89.38500  23.04100  1.000 60.12487  ?  1049 ASP   B N   1 
ATOM   22408 C  CA  . ASP   B 1 1051 ? 74.53900   89.72300  22.23100  1.000 58.85956  ?  1049 ASP   B CA  1 
ATOM   22409 C  C   . ASP   B 1 1051 ? 74.77900   88.70700  21.12800  1.000 47.77730  ?  1049 ASP   B C   1 
ATOM   22410 O  O   . ASP   B 1 1051 ? 75.27700   89.07000  20.05800  1.000 65.92015  ?  1049 ASP   B O   1 
ATOM   22411 C  CB  . ASP   B 1 1051 ? 75.78500   89.84400  23.10800  1.000 59.11339  ?  1049 ASP   B CB  1 
ATOM   22412 C  CG  . ASP   B 1 1051 ? 75.68900   90.98200  24.10000  1.000 54.68370  ?  1049 ASP   B CG  1 
ATOM   22413 O  OD1 . ASP   B 1 1051 ? 74.55800   91.36200  24.46300  1.000 61.63916  ?  1049 ASP   B OD1 1 
ATOM   22414 O  OD2 . ASP   B 1 1051 ? 76.74800   91.49400  24.51900  1.000 63.64031  -1 1049 ASP   B OD2 1 
ATOM   22415 N  N   . THR   B 1 1052 ? 74.42100   87.44400  21.35200  1.000 49.37668  ?  1050 THR   B N   1 
ATOM   22416 C  CA  . THR   B 1 1052 ? 74.76600   86.41100  20.38500  1.000 65.77476  ?  1050 THR   B CA  1 
ATOM   22417 C  C   . THR   B 1 1052 ? 73.73300   86.30600  19.26800  1.000 61.46456  ?  1050 THR   B C   1 
ATOM   22418 O  O   . THR   B 1 1052 ? 73.55900   85.23500  18.67900  1.000 72.74877  ?  1050 THR   B O   1 
ATOM   22419 C  CB  . THR   B 1 1052 ? 74.93600   85.05600  21.07300  1.000 69.16893  ?  1050 THR   B CB  1 
ATOM   22420 O  OG1 . THR   B 1 1052 ? 75.13600   84.05800  20.07200  1.000 91.55802  ?  1050 THR   B OG1 1 
ATOM   22421 C  CG2 . THR   B 1 1052 ? 73.70700   84.68600  21.88400  1.000 57.16388  ?  1050 THR   B CG2 1 
ATOM   22422 N  N   . ARG   B 1 1053 ? 73.06300   87.41300  18.95000  1.000 58.46764  ?  1051 ARG   B N   1 
ATOM   22423 C  CA  . ARG   B 1 1053 ? 72.01100   87.39900  17.94100  1.000 58.70888  ?  1051 ARG   B CA  1 
ATOM   22424 C  C   . ARG   B 1 1053 ? 72.53500   87.58800  16.52500  1.000 56.80774  ?  1051 ARG   B C   1 
ATOM   22425 O  O   . ARG   B 1 1053 ? 71.93300   87.06900  15.57900  1.000 66.14858  ?  1051 ARG   B O   1 
ATOM   22426 C  CB  . ARG   B 1 1053 ? 70.97700   88.48500  18.24000  1.000 64.20000  ?  1051 ARG   B CB  1 
ATOM   22427 C  CG  . ARG   B 1 1053 ? 69.78600   88.00900  19.05300  1.000 57.94365  ?  1051 ARG   B CG  1 
ATOM   22428 C  CD  . ARG   B 1 1053 ? 68.80500   89.14800  19.27300  1.000 57.76052  ?  1051 ARG   B CD  1 
ATOM   22429 N  NE  . ARG   B 1 1053 ? 69.42200   90.26000  19.98700  1.000 57.54727  ?  1051 ARG   B NE  1 
ATOM   22430 C  CZ  . ARG   B 1 1053 ? 68.86300   91.45000  20.15500  1.000 58.37008  ?  1051 ARG   B CZ  1 
ATOM   22431 N  NH1 . ARG   B 1 1053 ? 67.66000   91.72300  19.67500  1.000 59.41482  ?  1051 ARG   B NH1 1 
ATOM   22432 N  NH2 . ARG   B 1 1053 ? 69.53000   92.39300  20.81500  1.000 46.14580  ?  1051 ARG   B NH2 1 
ATOM   22433 N  N   . GLU   B 1 1054 ? 73.63000   88.32500  16.34800  1.000 58.59533  ?  1052 GLU   B N   1 
ATOM   22434 C  CA  . GLU   B 1 1054 ? 74.19200   88.57100  15.02600  1.000 52.43051  ?  1052 GLU   B CA  1 
ATOM   22435 C  C   . GLU   B 1 1054 ? 75.49500   87.81400  14.80600  1.000 41.91204  ?  1052 GLU   B C   1 
ATOM   22436 O  O   . GLU   B 1 1054 ? 76.28600   88.18500  13.93100  1.000 36.11587  ?  1052 GLU   B O   1 
ATOM   22437 C  CB  . GLU   B 1 1054 ? 74.40400   90.07000  14.80800  1.000 46.69816  ?  1052 GLU   B CB  1 
ATOM   22438 C  CG  . GLU   B 1 1054 ? 73.11700   90.87900  14.79300  1.000 75.08174  ?  1052 GLU   B CG  1 
ATOM   22439 C  CD  . GLU   B 1 1054 ? 72.15800   90.42600  13.70800  1.000 89.31759  ?  1052 GLU   B CD  1 
ATOM   22440 O  OE1 . GLU   B 1 1054 ? 72.58200   90.33400  12.53600  1.000 82.65884  ?  1052 GLU   B OE1 1 
ATOM   22441 O  OE2 . GLU   B 1 1054 ? 70.98000   90.15600  14.02700  1.000 96.38825  -1 1052 GLU   B OE2 1 
ATOM   22442 N  N   . LEU   B 1 1055 ? 75.72900   86.75600  15.57500  1.000 52.86358  ?  1053 LEU   B N   1 
ATOM   22443 C  CA  . LEU   B 1 1055 ? 76.97800   86.01300  15.51500  1.000 57.11652  ?  1053 LEU   B CA  1 
ATOM   22444 C  C   . LEU   B 1 1055 ? 76.86800   84.85900  14.52900  1.000 55.90839  ?  1053 LEU   B C   1 
ATOM   22445 O  O   . LEU   B 1 1055 ? 75.83200   84.19200  14.44500  1.000 56.58994  ?  1053 LEU   B O   1 
ATOM   22446 C  CB  . LEU   B 1 1055 ? 77.35600   85.48800  16.90200  1.000 52.83945  ?  1053 LEU   B CB  1 
ATOM   22447 C  CG  . LEU   B 1 1055 ? 78.14000   86.44400  17.80400  1.000 56.57869  ?  1053 LEU   B CG  1 
ATOM   22448 C  CD1 . LEU   B 1 1055 ? 79.39400   86.92200  17.09400  1.000 67.09105  ?  1053 LEU   B CD1 1 
ATOM   22449 C  CD2 . LEU   B 1 1055 ? 77.29400   87.62600  18.22500  1.000 52.44119  ?  1053 LEU   B CD2 1 
ATOM   22450 N  N   . LEU   B 1 1056 ? 77.94300   84.63000  13.78100  1.000 44.11295  ?  1054 LEU   B N   1 
ATOM   22451 C  CA  . LEU   B 1 1056 ? 77.99800   83.54300  12.81200  1.000 43.45280  ?  1054 LEU   B CA  1 
ATOM   22452 C  C   . LEU   B 1 1056 ? 78.49500   82.28100  13.50700  1.000 46.68372  ?  1054 LEU   B C   1 
ATOM   22453 O  O   . LEU   B 1 1056 ? 79.61800   82.25400  14.02100  1.000 70.50540  ?  1054 LEU   B O   1 
ATOM   22454 C  CB  . LEU   B 1 1056 ? 78.90900   83.90900  11.64200  1.000 47.59982  ?  1054 LEU   B CB  1 
ATOM   22455 C  CG  . LEU   B 1 1056 ? 78.43400   83.48200  10.25400  1.000 44.10870  ?  1054 LEU   B CG  1 
ATOM   22456 C  CD1 . LEU   B 1 1056 ? 77.21500   84.29200  9.84500   1.000 47.61348  ?  1054 LEU   B CD1 1 
ATOM   22457 C  CD2 . LEU   B 1 1056 ? 79.55400   83.63500  9.23400   1.000 31.95550  ?  1054 LEU   B CD2 1 
ATOM   22458 N  N   . GLY   B 1 1057 ? 77.66500   81.24400  13.52600  1.000 56.75982  ?  1055 GLY   B N   1 
ATOM   22459 C  CA  . GLY   B 1 1057 ? 78.04900   80.00900  14.17700  1.000 60.63314  ?  1055 GLY   B CA  1 
ATOM   22460 C  C   . GLY   B 1 1057 ? 76.87300   79.06100  14.30400  1.000 59.08632  ?  1055 GLY   B C   1 
ATOM   22461 O  O   . GLY   B 1 1057 ? 75.80900   79.27100  13.71600  1.000 58.13271  ?  1055 GLY   B O   1 
ATOM   22462 N  N   . MET   B 1 1058 ? 77.09400   78.01300  15.09500  1.000 63.68750  ?  1056 MET   B N   1 
ATOM   22463 C  CA  . MET   B 1 1058 ? 76.13500   76.93200  15.28800  1.000 62.25284  ?  1056 MET   B CA  1 
ATOM   22464 C  C   . MET   B 1 1058 ? 75.38500   77.15100  16.59700  1.000 58.67490  ?  1056 MET   B C   1 
ATOM   22465 O  O   . MET   B 1 1058 ? 75.99900   77.18900  17.66800  1.000 59.01639  ?  1056 MET   B O   1 
ATOM   22466 C  CB  . MET   B 1 1058 ? 76.85700   75.58400  15.29600  1.000 62.03042  ?  1056 MET   B CB  1 
ATOM   22467 C  CG  . MET   B 1 1058 ? 76.05300   74.42500  15.85300  1.000 80.01684  ?  1056 MET   B CG  1 
ATOM   22468 S  SD  . MET   B 1 1058 ? 74.47600   74.17600  15.02000  1.000 76.58639  ?  1056 MET   B SD  1 
ATOM   22469 C  CE  . MET   B 1 1058 ? 74.36900   72.39000  15.05300  1.000 62.05752  ?  1056 MET   B CE  1 
ATOM   22470 N  N   . PHE   B 1 1059 ? 74.06100   77.27900  16.51300  1.000 59.74232  ?  1057 PHE   B N   1 
ATOM   22471 C  CA  . PHE   B 1 1059 ? 73.27400   77.61000  17.69500  1.000 60.62928  ?  1057 PHE   B CA  1 
ATOM   22472 C  C   . PHE   B 1 1059 ? 72.06000   76.70700  17.85200  1.000 71.47192  ?  1057 PHE   B C   1 
ATOM   22473 O  O   . PHE   B 1 1059 ? 71.63500   76.42900  18.97800  1.000 68.08658  ?  1057 PHE   B O   1 
ATOM   22474 C  CB  . PHE   B 1 1059 ? 72.83400   79.07300  17.64500  1.000 59.69913  ?  1057 PHE   B CB  1 
ATOM   22475 C  CG  . PHE   B 1 1059 ? 73.96000   80.03700  17.84000  1.000 69.84828  ?  1057 PHE   B CG  1 
ATOM   22476 C  CD1 . PHE   B 1 1059 ? 74.33300   80.42700  19.11100  1.000 61.42973  ?  1057 PHE   B CD1 1 
ATOM   22477 C  CD2 . PHE   B 1 1059 ? 74.67000   80.52500  16.75600  1.000 75.52061  ?  1057 PHE   B CD2 1 
ATOM   22478 C  CE1 . PHE   B 1 1059 ? 75.38100   81.29400  19.29800  1.000 63.91990  ?  1057 PHE   B CE1 1 
ATOM   22479 C  CE2 . PHE   B 1 1059 ? 75.71700   81.40400  16.93800  1.000 71.80609  ?  1057 PHE   B CE2 1 
ATOM   22480 C  CZ  . PHE   B 1 1059 ? 76.07300   81.79000  18.21100  1.000 56.68954  ?  1057 PHE   B CZ  1 
ATOM   22481 N  N   . VAL   B 1 1060 ? 71.49400   76.25000  16.73200  1.000 79.31198  ?  1058 VAL   B N   1 
ATOM   22482 C  CA  . VAL   B 1 1060 ? 70.28800   75.43800  16.79600  1.000 68.05805  ?  1058 VAL   B CA  1 
ATOM   22483 C  C   . VAL   B 1 1060 ? 70.54100   74.19300  17.64500  1.000 74.65456  ?  1058 VAL   B C   1 
ATOM   22484 O  O   . VAL   B 1 1060 ? 71.65000   73.64300  17.67900  1.000 74.27965  ?  1058 VAL   B O   1 
ATOM   22485 C  CB  . VAL   B 1 1060 ? 69.79900   75.06600  15.38500  1.000 54.78386  ?  1058 VAL   B CB  1 
ATOM   22486 C  CG1 . VAL   B 1 1060 ? 69.27600   76.30200  14.66200  1.000 69.15814  ?  1058 VAL   B CG1 1 
ATOM   22487 C  CG2 . VAL   B 1 1060 ? 70.91600   74.42000  14.58500  1.000 59.61844  ?  1058 VAL   B CG2 1 
ATOM   22488 N  N   . ASN   B 1 1061 ? 69.50600   73.76300  18.36200  1.000 62.46913  ?  1059 ASN   B N   1 
ATOM   22489 C  CA  . ASN   B 1 1061 ? 69.61100   72.62900  19.26700  1.000 65.63886  ?  1059 ASN   B CA  1 
ATOM   22490 C  C   . ASN   B 1 1061 ? 68.40800   71.71700  19.08100  1.000 71.73120  ?  1059 ASN   B C   1 
ATOM   22491 O  O   . ASN   B 1 1061 ? 67.27200   72.18800  18.98100  1.000 68.40418  ?  1059 ASN   B O   1 
ATOM   22492 C  CB  . ASN   B 1 1061 ? 69.70800   73.09800  20.72400  1.000 78.76846  ?  1059 ASN   B CB  1 
ATOM   22493 C  CG  . ASN   B 1 1061 ? 69.79900   71.94900  21.70400  1.000 78.45726  ?  1059 ASN   B CG  1 
ATOM   22494 O  OD1 . ASN   B 1 1061 ? 70.43100   70.92800  21.43100  1.000 81.31387  ?  1059 ASN   B OD1 1 
ATOM   22495 N  ND2 . ASN   B 1 1061 ? 69.15900   72.10800  22.85700  1.000 60.59346  ?  1059 ASN   B ND2 1 
ATOM   22496 N  N   . THR   B 1 1062 ? 68.66800   70.41100  19.02900  1.000 72.93125  ?  1060 THR   B N   1 
ATOM   22497 C  CA  . THR   B 1 1062 ? 67.59900   69.43100  18.87800  1.000 61.17804  ?  1060 THR   B CA  1 
ATOM   22498 C  C   . THR   B 1 1062 ? 66.81200   69.30900  20.17800  1.000 56.45976  ?  1060 THR   B C   1 
ATOM   22499 O  O   . THR   B 1 1062 ? 67.39500   69.21300  21.26200  1.000 58.76810  ?  1060 THR   B O   1 
ATOM   22500 C  CB  . THR   B 1 1062 ? 68.18200   68.07500  18.48600  1.000 67.69613  ?  1060 THR   B CB  1 
ATOM   22501 O  OG1 . THR   B 1 1062 ? 69.43100   67.88400  19.16100  1.000 96.06738  ?  1060 THR   B OG1 1 
ATOM   22502 C  CG2 . THR   B 1 1062 ? 68.43000   68.01900  16.99200  1.000 71.14387  ?  1060 THR   B CG2 1 
ATOM   22503 N  N   . LEU   B 1 1063 ? 65.48500   69.30600  20.07000  1.000 62.96024  ?  1061 LEU   B N   1 
ATOM   22504 C  CA  . LEU   B 1 1063 ? 64.61400   69.31000  21.24200  1.000 59.02841  ?  1061 LEU   B CA  1 
ATOM   22505 C  C   . LEU   B 1 1063 ? 63.58000   68.20100  21.11500  1.000 56.81273  ?  1061 LEU   B C   1 
ATOM   22506 O  O   . LEU   B 1 1063 ? 62.78700   68.20200  20.14900  1.000 53.06804  ?  1061 LEU   B O   1 
ATOM   22507 C  CB  . LEU   B 1 1063 ? 63.92800   70.66600  21.41800  1.000 58.91832  ?  1061 LEU   B CB  1 
ATOM   22508 C  CG  . LEU   B 1 1063 ? 64.07200   71.29500  22.80500  1.000 49.68987  ?  1061 LEU   B CG  1 
ATOM   22509 C  CD1 . LEU   B 1 1063 ? 65.53400   71.33700  23.21800  1.000 45.67036  ?  1061 LEU   B CD1 1 
ATOM   22510 C  CD2 . LEU   B 1 1063 ? 63.46700   72.68300  22.83100  1.000 64.20675  ?  1061 LEU   B CD2 1 
ATOM   22511 N  N   . PRO   B 1 1064 ? 63.54500   67.24800  22.04200  1.000 62.98398  ?  1062 PRO   B N   1 
ATOM   22512 C  CA  . PRO   B 1 1064 ? 62.46700   66.25500  22.03700  1.000 49.31806  ?  1062 PRO   B CA  1 
ATOM   22513 C  C   . PRO   B 1 1064 ? 61.14100   66.90800  22.37300  1.000 52.23866  ?  1062 PRO   B C   1 
ATOM   22514 O  O   . PRO   B 1 1064 ? 61.05200   67.76300  23.25700  1.000 65.91730  ?  1062 PRO   B O   1 
ATOM   22515 C  CB  . PRO   B 1 1064 ? 62.88800   65.25900  23.12300  1.000 47.96880  ?  1062 PRO   B CB  1 
ATOM   22516 C  CG  . PRO   B 1 1064 ? 64.33400   65.55400  23.38900  1.000 76.24681  ?  1062 PRO   B CG  1 
ATOM   22517 C  CD  . PRO   B 1 1064 ? 64.51300   67.00600  23.11900  1.000 74.23974  ?  1062 PRO   B CD  1 
ATOM   22518 N  N   . LEU   B 1 1065 ? 60.10400   66.49700  21.65600  1.000 44.11666  ?  1063 LEU   B N   1 
ATOM   22519 C  CA  . LEU   B 1 1065 ? 58.77400   67.07900  21.79500  1.000 46.93477  ?  1063 LEU   B CA  1 
ATOM   22520 C  C   . LEU   B 1 1065 ? 57.80000   65.93900  22.07400  1.000 73.62962  ?  1063 LEU   B C   1 
ATOM   22521 O  O   . LEU   B 1 1065 ? 57.44100   65.18400  21.16500  1.000 80.82275  ?  1063 LEU   B O   1 
ATOM   22522 C  CB  . LEU   B 1 1065 ? 58.39400   67.86000  20.54200  1.000 54.36555  ?  1063 LEU   B CB  1 
ATOM   22523 C  CG  . LEU   B 1 1065 ? 58.86100   69.30900  20.40700  1.000 57.40843  ?  1063 LEU   B CG  1 
ATOM   22524 C  CD1 . LEU   B 1 1065 ? 58.29600   69.92700  19.13600  1.000 58.10876  ?  1063 LEU   B CD1 1 
ATOM   22525 C  CD2 . LEU   B 1 1065 ? 58.44800   70.11600  21.62300  1.000 53.96637  ?  1063 LEU   B CD2 1 
ATOM   22526 N  N   . LEU   B 1 1066 ? 57.38700   65.81000  23.33500  1.000 67.51213  ?  1064 LEU   B N   1 
ATOM   22527 C  CA  . LEU   B 1 1066 ? 56.40000   64.81500  23.74300  1.000 49.54106  ?  1064 LEU   B CA  1 
ATOM   22528 C  C   . LEU   B 1 1066 ? 55.02600   65.47500  23.72200  1.000 51.38321  ?  1064 LEU   B C   1 
ATOM   22529 O  O   . LEU   B 1 1066 ? 54.70300   66.28200  24.60100  1.000 68.19441  ?  1064 LEU   B O   1 
ATOM   22530 C  CB  . LEU   B 1 1066 ? 56.73100   64.25900  25.12700  1.000 53.14457  ?  1064 LEU   B CB  1 
ATOM   22531 C  CG  . LEU   B 1 1066 ? 56.26300   62.83600  25.43600  1.000 57.28385  ?  1064 LEU   B CG  1 
ATOM   22532 C  CD1 . LEU   B 1 1066 ? 57.20400   62.19600  26.44100  1.000 59.26660  ?  1064 LEU   B CD1 1 
ATOM   22533 C  CD2 . LEU   B 1 1066 ? 54.83200   62.83500  25.95900  1.000 62.19669  ?  1064 LEU   B CD2 1 
ATOM   22534 N  N   . LEU   B 1 1067 ? 54.22200   65.14200  22.71900  1.000 51.01683  ?  1065 LEU   B N   1 
ATOM   22535 C  CA  . LEU   B 1 1067 ? 52.92500   65.77100  22.50900  1.000 51.79698  ?  1065 LEU   B CA  1 
ATOM   22536 C  C   . LEU   B 1 1067 ? 51.79800   64.78500  22.81300  1.000 64.03039  ?  1065 LEU   B C   1 
ATOM   22537 O  O   . LEU   B 1 1067 ? 52.01900   63.61800  23.14700  1.000 68.70134  ?  1065 LEU   B O   1 
ATOM   22538 C  CB  . LEU   B 1 1067 ? 52.80100   66.32300  21.07900  1.000 70.12576  ?  1065 LEU   B CB  1 
ATOM   22539 C  CG  . LEU   B 1 1067 ? 53.61400   67.54900  20.62400  1.000 70.86115  ?  1065 LEU   B CG  1 
ATOM   22540 C  CD1 . LEU   B 1 1067 ? 55.09300   67.29900  20.69100  1.000 66.18163  ?  1065 LEU   B CD1 1 
ATOM   22541 C  CD2 . LEU   B 1 1067 ? 53.26400   67.98800  19.22500  1.000 49.79975  ?  1065 LEU   B CD2 1 
ATOM   22542 N  N   . SER   B 1 1068 ? 50.56600   65.27600  22.69600  1.000 63.21257  ?  1066 SER   B N   1 
ATOM   22543 C  CA  . SER   B 1 1068 ? 49.39600   64.47500  23.01900  1.000 58.01978  ?  1066 SER   B CA  1 
ATOM   22544 C  C   . SER   B 1 1068 ? 48.21900   64.95000  22.18400  1.000 64.15689  ?  1066 SER   B C   1 
ATOM   22545 O  O   . SER   B 1 1068 ? 48.02600   66.15500  22.00000  1.000 73.01069  ?  1066 SER   B O   1 
ATOM   22546 C  CB  . SER   B 1 1068 ? 49.05600   64.55900  24.51100  1.000 59.86187  ?  1066 SER   B CB  1 
ATOM   22547 O  OG  . SER   B 1 1068 ? 50.12200   64.06800  25.30700  1.000 75.67048  ?  1066 SER   B OG  1 
ATOM   22548 N  N   . ILE   B 1 1069 ? 47.43700   63.99700  21.68300  1.000 63.47611  ?  1067 ILE   B N   1 
ATOM   22549 C  CA  . ILE   B 1 1069 ? 46.29300   64.28100  20.82600  1.000 59.76691  ?  1067 ILE   B CA  1 
ATOM   22550 C  C   . ILE   B 1 1069 ? 45.06500   63.60500  21.41500  1.000 78.32180  ?  1067 ILE   B C   1 
ATOM   22551 O  O   . ILE   B 1 1069 ? 45.10200   62.41300  21.73700  1.000 86.82461  ?  1067 ILE   B O   1 
ATOM   22552 C  CB  . ILE   B 1 1069 ? 46.52500   63.80100  19.38000  1.000 60.63426  ?  1067 ILE   B CB  1 
ATOM   22553 C  CG1 . ILE   B 1 1069 ? 47.92000   64.19900  18.89400  1.000 71.65183  ?  1067 ILE   B CG1 1 
ATOM   22554 C  CG2 . ILE   B 1 1069 ? 45.44700   64.35100  18.45700  1.000 59.73788  ?  1067 ILE   B CG2 1 
ATOM   22555 C  CD1 . ILE   B 1 1069 ? 48.07400   65.68200  18.62400  1.000 77.31692  ?  1067 ILE   B CD1 1 
ATOM   22556 N  N   . ASP   B 1 1070 ? 43.98200   64.36300  21.55600  1.000 65.41528  ?  1068 ASP   B N   1 
ATOM   22557 C  CA  . ASP   B 1 1070 ? 42.68400   63.82700  21.94800  1.000 58.40943  ?  1068 ASP   B CA  1 
ATOM   22558 C  C   . ASP   B 1 1070 ? 41.79700   63.83100  20.71100  1.000 80.26369  ?  1068 ASP   B C   1 
ATOM   22559 O  O   . ASP   B 1 1070 ? 41.35000   64.89300  20.26400  1.000 81.11271  ?  1068 ASP   B O   1 
ATOM   22560 C  CB  . ASP   B 1 1070 ? 42.05700   64.64100  23.07700  1.000 81.66811  ?  1068 ASP   B CB  1 
ATOM   22561 C  CG  . ASP   B 1 1070 ? 40.62000   64.23400  23.36300  1.000 88.19479  ?  1068 ASP   B CG  1 
ATOM   22562 O  OD1 . ASP   B 1 1070 ? 40.26700   63.05400  23.14000  1.000 91.55552  ?  1068 ASP   B OD1 1 
ATOM   22563 O  OD2 . ASP   B 1 1070 ? 39.83800   65.10100  23.80400  1.000 83.27437  -1 1068 ASP   B OD2 1 
ATOM   22564 N  N   . HIS   B 1 1071 ? 41.54300   62.64300  20.16200  1.000 76.90002  ?  1069 HIS   B N   1 
ATOM   22565 C  CA  . HIS   B 1 1071 ? 40.76000   62.55300  18.93800  1.000 66.84411  ?  1069 HIS   B CA  1 
ATOM   22566 C  C   . HIS   B 1 1071 ? 39.28100   62.82300  19.17500  1.000 72.27169  ?  1069 HIS   B C   1 
ATOM   22567 O  O   . HIS   B 1 1071 ? 38.55600   63.10200  18.21400  1.000 90.40702  ?  1069 HIS   B O   1 
ATOM   22568 C  CB  . HIS   B 1 1071 ? 40.95400   61.17900  18.29800  1.000 70.45828  ?  1069 HIS   B CB  1 
ATOM   22569 C  CG  . HIS   B 1 1071 ? 42.38600   60.84700  18.01300  1.000 73.88392  ?  1069 HIS   B CG  1 
ATOM   22570 N  ND1 . HIS   B 1 1071 ? 42.89000   60.76200  16.73200  1.000 67.12617  ?  1069 HIS   B ND1 1 
ATOM   22571 C  CD2 . HIS   B 1 1071 ? 43.42400   60.58900  18.84400  1.000 66.58778  ?  1069 HIS   B CD2 1 
ATOM   22572 C  CE1 . HIS   B 1 1071 ? 44.17600   60.46200  16.78700  1.000 68.26424  ?  1069 HIS   B CE1 1 
ATOM   22573 N  NE2 . HIS   B 1 1071 ? 44.52500   60.35200  18.05700  1.000 63.42600  ?  1069 HIS   B NE2 1 
ATOM   22574 N  N   . GLU   B 1 1072 ? 38.81900   62.76000  20.42500  1.000 82.10641  ?  1070 GLU   B N   1 
ATOM   22575 C  CA  . GLU   B 1 1072 ? 37.41400   63.00800  20.72500  1.000 87.71218  ?  1070 GLU   B CA  1 
ATOM   22576 C  C   . GLU   B 1 1072 ? 37.08200   64.48800  20.85300  1.000 85.72540  ?  1070 GLU   B C   1 
ATOM   22577 O  O   . GLU   B 1 1072 ? 35.89700   64.83500  20.91000  1.000 67.46043  ?  1070 GLU   B O   1 
ATOM   22578 C  CB  . GLU   B 1 1072 ? 37.00500   62.28000  22.01000  1.000 81.69198  ?  1070 GLU   B CB  1 
ATOM   22579 C  CG  . GLU   B 1 1072 ? 37.12700   60.76700  21.93000  1.000 77.77829  ?  1070 GLU   B CG  1 
ATOM   22580 C  CD  . GLU   B 1 1072 ? 36.29300   60.17500  20.80700  1.000 85.94408  ?  1070 GLU   B CD  1 
ATOM   22581 O  OE1 . GLU   B 1 1072 ? 35.14900   60.63500  20.59900  1.000 72.49122  ?  1070 GLU   B OE1 1 
ATOM   22582 O  OE2 . GLU   B 1 1072 ? 36.78500   59.25000  20.12700  1.000 84.85401  -1 1070 GLU   B OE2 1 
ATOM   22583 N  N   . GLU   B 1 1073 ? 38.08400   65.36200  20.89800  1.000 92.02236  ?  1071 GLU   B N   1 
ATOM   22584 C  CA  . GLU   B 1 1073 ? 37.87300   66.80000  20.94500  1.000 87.00897  ?  1071 GLU   B CA  1 
ATOM   22585 C  C   . GLU   B 1 1073 ? 38.22200   67.42100  19.59600  1.000 89.22240  ?  1071 GLU   B C   1 
ATOM   22586 O  O   . GLU   B 1 1073 ? 38.55200   66.73000  18.62700  1.000 80.21636  ?  1071 GLU   B O   1 
ATOM   22587 C  CB  . GLU   B 1 1073 ? 38.68700   67.43300  22.07300  1.000 82.69578  ?  1071 GLU   B CB  1 
ATOM   22588 C  CG  . GLU   B 1 1073 ? 37.89000   68.43400  22.89200  1.000 80.38656  ?  1071 GLU   B CG  1 
ATOM   22589 C  CD  . GLU   B 1 1073 ? 36.95500   67.77000  23.88400  1.000 96.58259  ?  1071 GLU   B CD  1 
ATOM   22590 O  OE1 . GLU   B 1 1073 ? 37.43800   66.95700  24.70000  1.000 82.86632  ?  1071 GLU   B OE1 1 
ATOM   22591 O  OE2 . GLU   B 1 1073 ? 35.74000   68.06300  23.85300  1.000 108.21350 -1 1071 GLU   B OE2 1 
ATOM   22592 N  N   . SER   B 1 1074 ? 38.15200   68.74500  19.54200  1.000 93.22820  ?  1072 SER   B N   1 
ATOM   22593 C  CA  . SER   B 1 1074 ? 38.29600   69.46200  18.28700  1.000 82.72317  ?  1072 SER   B CA  1 
ATOM   22594 C  C   . SER   B 1 1074 ? 39.75600   69.80300  18.00600  1.000 83.79471  ?  1072 SER   B C   1 
ATOM   22595 O  O   . SER   B 1 1074 ? 40.62500   69.73200  18.88000  1.000 71.73793  ?  1072 SER   B O   1 
ATOM   22596 C  CB  . SER   B 1 1074 ? 37.45300   70.73900  18.29900  1.000 73.98212  ?  1072 SER   B CB  1 
ATOM   22597 O  OG  . SER   B 1 1074 ? 37.54800   71.42900  17.06400  1.000 86.87820  ?  1072 SER   B OG  1 
ATOM   22598 N  N   . PHE   B 1 1075 ? 40.01000   70.16300  16.74600  1.000 84.99935  ?  1073 PHE   B N   1 
ATOM   22599 C  CA  . PHE   B 1 1075 ? 41.32300   70.64800  16.33600  1.000 88.43150  ?  1073 PHE   B CA  1 
ATOM   22600 C  C   . PHE   B 1 1075 ? 41.77100   71.81900  17.20300  1.000 85.01507  ?  1073 PHE   B C   1 
ATOM   22601 O  O   . PHE   B 1 1075 ? 42.95200   71.93000  17.55200  1.000 68.25407  ?  1073 PHE   B O   1 
ATOM   22602 C  CB  . PHE   B 1 1075 ? 41.26600   71.03900  14.85600  1.000 83.24231  ?  1073 PHE   B CB  1 
ATOM   22603 C  CG  . PHE   B 1 1075 ? 42.56800   71.53300  14.29100  1.000 75.55242  ?  1073 PHE   B CG  1 
ATOM   22604 C  CD1 . PHE   B 1 1075 ? 43.75000   70.84900  14.52100  1.000 52.18653  ?  1073 PHE   B CD1 1 
ATOM   22605 C  CD2 . PHE   B 1 1075 ? 42.59900   72.66900  13.49800  1.000 73.04374  ?  1073 PHE   B CD2 1 
ATOM   22606 C  CE1 . PHE   B 1 1075 ? 44.94300   71.30300  13.98700  1.000 73.74012  ?  1073 PHE   B CE1 1 
ATOM   22607 C  CE2 . PHE   B 1 1075 ? 43.78800   73.12700  12.96100  1.000 72.75933  ?  1073 PHE   B CE2 1 
ATOM   22608 C  CZ  . PHE   B 1 1075 ? 44.96100   72.44300  13.20600  1.000 73.93818  ?  1073 PHE   B CZ  1 
ATOM   22609 N  N   . LEU   B 1 1076 ? 40.82800   72.68500  17.58900  1.000 82.94893  ?  1074 LEU   B N   1 
ATOM   22610 C  CA  . LEU   B 1 1076 ? 41.16100   73.85900  18.39200  1.000 71.07794  ?  1074 LEU   B CA  1 
ATOM   22611 C  C   . LEU   B 1 1076 ? 41.70500   73.46700  19.76100  1.000 69.90011  ?  1074 LEU   B C   1 
ATOM   22612 O  O   . LEU   B 1 1076 ? 42.74400   73.97800  20.19400  1.000 83.11242  ?  1074 LEU   B O   1 
ATOM   22613 C  CB  . LEU   B 1 1076 ? 39.93400   74.75400  18.54500  1.000 63.58387  ?  1074 LEU   B CB  1 
ATOM   22614 C  CG  . LEU   B 1 1076 ? 39.96800   76.02800  17.70800  1.000 77.39537  ?  1074 LEU   B CG  1 
ATOM   22615 C  CD1 . LEU   B 1 1076 ? 39.76400   75.67300  16.26200  1.000 70.21443  ?  1074 LEU   B CD1 1 
ATOM   22616 C  CD2 . LEU   B 1 1076 ? 38.89900   77.00100  18.17400  1.000 66.66368  ?  1074 LEU   B CD2 1 
ATOM   22617 N  N   . HIS   B 1 1077 ? 40.99600   72.58100  20.46800  1.000 65.79747  ?  1075 HIS   B N   1 
ATOM   22618 C  CA  . HIS   B 1 1077 ? 41.45600   72.12600  21.77700  1.000 69.40872  ?  1075 HIS   B CA  1 
ATOM   22619 C  C   . HIS   B 1 1077 ? 42.89600   71.63900  21.70100  1.000 67.91440  ?  1075 HIS   B C   1 
ATOM   22620 O  O   . HIS   B 1 1077 ? 43.75000   72.05800  22.49100  1.000 73.46323  ?  1075 HIS   B O   1 
ATOM   22621 C  CB  . HIS   B 1 1077 ? 40.52900   71.02100  22.30100  1.000 76.99651  ?  1075 HIS   B CB  1 
ATOM   22622 C  CG  . HIS   B 1 1077 ? 40.96800   70.39500  23.59700  1.000 82.61552  ?  1075 HIS   B CG  1 
ATOM   22623 N  ND1 . HIS   B 1 1077 ? 40.06800   69.96500  24.54700  1.000 82.06925  ?  1075 HIS   B ND1 1 
ATOM   22624 C  CD2 . HIS   B 1 1077 ? 42.19600   70.09300  24.08500  1.000 92.35074  ?  1075 HIS   B CD2 1 
ATOM   22625 C  CE1 . HIS   B 1 1077 ? 40.72100   69.44600  25.57100  1.000 93.49949  ?  1075 HIS   B CE1 1 
ATOM   22626 N  NE2 . HIS   B 1 1077 ? 42.01500   69.51300  25.31600  1.000 89.09210  ?  1075 HIS   B NE2 1 
ATOM   22627 N  N   . ASN   B 1 1078 ? 43.18200   70.75200  20.74900  1.000 74.88978  ?  1076 ASN   B N   1 
ATOM   22628 C  CA  . ASN   B 1 1078 ? 44.53300   70.21700  20.63800  1.000 79.68686  ?  1076 ASN   B CA  1 
ATOM   22629 C  C   . ASN   B 1 1078 ? 45.53200   71.31300  20.29600  1.000 72.21860  ?  1076 ASN   B C   1 
ATOM   22630 O  O   . ASN   B 1 1078 ? 46.62500   71.35800  20.87000  1.000 64.44681  ?  1076 ASN   B O   1 
ATOM   22631 C  CB  . ASN   B 1 1078 ? 44.56900   69.10100  19.59800  1.000 89.55188  ?  1076 ASN   B CB  1 
ATOM   22632 C  CG  . ASN   B 1 1078 ? 43.87700   67.84800  20.08000  1.000 74.48509  ?  1076 ASN   B CG  1 
ATOM   22633 O  OD1 . ASN   B 1 1078 ? 44.45400   67.05400  20.82500  1.000 53.90777  ?  1076 ASN   B OD1 1 
ATOM   22634 N  ND2 . ASN   B 1 1078 ? 42.62600   67.66900  19.67000  1.000 55.19062  ?  1076 ASN   B ND2 1 
ATOM   22635 N  N   . LEU   B 1 1079 ? 45.16500   72.21200  19.37500  1.000 66.42853  ?  1077 LEU   B N   1 
ATOM   22636 C  CA  . LEU   B 1 1079 ? 46.01600   73.35200  19.04100  1.000 58.58318  ?  1077 LEU   B CA  1 
ATOM   22637 C  C   . LEU   B 1 1079 ? 46.52700   74.04500  20.29800  1.000 65.75238  ?  1077 LEU   B C   1 
ATOM   22638 O  O   . LEU   B 1 1079 ? 47.73700   74.23500  20.47400  1.000 58.55017  ?  1077 LEU   B O   1 
ATOM   22639 C  CB  . LEU   B 1 1079 ? 45.24700   74.34300  18.16500  1.000 48.50065  ?  1077 LEU   B CB  1 
ATOM   22640 C  CG  . LEU   B 1 1079 ? 45.13300   74.07500  16.66000  1.000 66.23183  ?  1077 LEU   B CG  1 
ATOM   22641 C  CD1 . LEU   B 1 1079 ? 44.12500   75.02300  16.02900  1.000 52.86489  ?  1077 LEU   B CD1 1 
ATOM   22642 C  CD2 . LEU   B 1 1079 ? 46.48400   74.19500  15.96900  1.000 50.23963  ?  1077 LEU   B CD2 1 
ATOM   22643 N  N   . GLN   B 1 1080 ? 45.61000   74.41100  21.19700  1.000 66.68183  ?  1078 GLN   B N   1 
ATOM   22644 C  CA  . GLN   B 1 1080 ? 46.00800   75.03000  22.45600  1.000 75.18390  ?  1078 GLN   B CA  1 
ATOM   22645 C  C   . GLN   B 1 1080 ? 46.76300   74.05300  23.34900  1.000 69.37580  ?  1078 GLN   B C   1 
ATOM   22646 O  O   . GLN   B 1 1080 ? 47.63100   74.46900  24.12600  1.000 74.65966  ?  1078 GLN   B O   1 
ATOM   22647 C  CB  . GLN   B 1 1080 ? 44.77800   75.57700  23.17900  1.000 42.01710  ?  1078 GLN   B CB  1 
ATOM   22648 N  N   . GLN   B 1 1081 ? 46.45600   72.75700  23.24800  1.000 66.57989  ?  1079 GLN   B N   1 
ATOM   22649 C  CA  . GLN   B 1 1081 ? 47.16300   71.76400  24.05000  1.000 64.82770  ?  1079 GLN   B CA  1 
ATOM   22650 C  C   . GLN   B 1 1081 ? 48.60700   71.60500  23.58800  1.000 70.91290  ?  1079 GLN   B C   1 
ATOM   22651 O  O   . GLN   B 1 1081 ? 49.50900   71.41400  24.41400  1.000 72.69862  ?  1079 GLN   B O   1 
ATOM   22652 C  CB  . GLN   B 1 1081 ? 46.42500   70.42500  23.99800  1.000 72.43587  ?  1079 GLN   B CB  1 
ATOM   22653 C  CG  . GLN   B 1 1081 ? 45.52000   70.16600  25.19900  1.000 80.65020  ?  1079 GLN   B CG  1 
ATOM   22654 C  CD  . GLN   B 1 1081 ? 46.29800   69.98200  26.49100  1.000 89.33268  ?  1079 GLN   B CD  1 
ATOM   22655 O  OE1 . GLN   B 1 1081 ? 46.24100   70.82300  27.39000  1.000 79.75321  ?  1079 GLN   B OE1 1 
ATOM   22656 N  NE2 . GLN   B 1 1081 ? 47.02600   68.87600  26.59300  1.000 88.17499  ?  1079 GLN   B NE2 1 
ATOM   22657 N  N   . VAL   B 1 1082 ? 48.84900   71.67900  22.27400  1.000 68.74686  ?  1080 VAL   B N   1 
ATOM   22658 C  CA  . VAL   B 1 1082 ? 50.22100   71.63700  21.76600  1.000 68.00500  ?  1080 VAL   B CA  1 
ATOM   22659 C  C   . VAL   B 1 1082 ? 51.00200   72.84900  22.26000  1.000 66.21031  ?  1080 VAL   B C   1 
ATOM   22660 O  O   . VAL   B 1 1082 ? 52.15800   72.73600  22.68800  1.000 53.13651  ?  1080 VAL   B O   1 
ATOM   22661 C  CB  . VAL   B 1 1082 ? 50.22900   71.54700  20.22800  1.000 64.48883  ?  1080 VAL   B CB  1 
ATOM   22662 C  CG1 . VAL   B 1 1082 ? 51.62600   71.22600  19.72700  1.000 62.62137  ?  1080 VAL   B CG1 1 
ATOM   22663 C  CG2 . VAL   B 1 1082 ? 49.27300   70.47100  19.75600  1.000 62.43471  ?  1080 VAL   B CG2 1 
ATOM   22664 N  N   . LYS   B 1 1083 ? 50.37900   74.02900  22.20600  1.000 60.39653  ?  1081 LYS   B N   1 
ATOM   22665 C  CA  . LYS   B 1 1083 ? 51.02100   75.23900  22.70900  1.000 67.09075  ?  1081 LYS   B CA  1 
ATOM   22666 C  C   . LYS   B 1 1083 ? 51.39900   75.08600  24.17500  1.000 71.66621  ?  1081 LYS   B C   1 
ATOM   22667 O  O   . LYS   B 1 1083 ? 52.53000   75.38900  24.57400  1.000 62.88294  ?  1081 LYS   B O   1 
ATOM   22668 C  CB  . LYS   B 1 1083 ? 50.09200   76.43600  22.51400  1.000 62.25773  ?  1081 LYS   B CB  1 
ATOM   22669 C  CG  . LYS   B 1 1083 ? 50.51800   77.69200  23.25500  1.000 58.07479  ?  1081 LYS   B CG  1 
ATOM   22670 C  CD  . LYS   B 1 1083 ? 49.37800   78.69800  23.29000  1.000 65.58268  ?  1081 LYS   B CD  1 
ATOM   22671 C  CE  . LYS   B 1 1083 ? 49.88900   80.12000  23.16600  1.000 61.47643  ?  1081 LYS   B CE  1 
ATOM   22672 N  NZ  . LYS   B 1 1083 ? 48.76800   81.09100  23.04900  1.000 61.76719  ?  1081 LYS   B NZ  1 
ATOM   22673 N  N   . ALA   B 1 1084 ? 50.46000   74.59700  24.99000  1.000 62.40571  ?  1082 ALA   B N   1 
ATOM   22674 C  CA  . ALA   B 1 1084 ? 50.71200   74.42100  26.41500  1.000 58.38362  ?  1082 ALA   B CA  1 
ATOM   22675 C  C   . ALA   B 1 1084 ? 51.83700   73.43200  26.68500  1.000 60.73828  ?  1082 ALA   B C   1 
ATOM   22676 O  O   . ALA   B 1 1084 ? 52.39200   73.42700  27.78800  1.000 58.01486  ?  1082 ALA   B O   1 
ATOM   22677 C  CB  . ALA   B 1 1084 ? 49.43300   73.96600  27.11700  1.000 60.05201  ?  1082 ALA   B CB  1 
ATOM   22678 N  N   . LYS   B 1 1085 ? 52.18400   72.59600  25.70900  1.000 62.82284  ?  1083 LYS   B N   1 
ATOM   22679 C  CA  . LYS   B 1 1085 ? 53.30700   71.68400  25.85400  1.000 62.43183  ?  1083 LYS   B CA  1 
ATOM   22680 C  C   . LYS   B 1 1085 ? 54.57400   72.19200  25.18400  1.000 70.16102  ?  1083 LYS   B C   1 
ATOM   22681 O  O   . LYS   B 1 1085 ? 55.67200   71.78800  25.58400  1.000 69.53962  ?  1083 LYS   B O   1 
ATOM   22682 C  CB  . LYS   B 1 1085 ? 52.94600   70.30700  25.28500  1.000 61.65623  ?  1083 LYS   B CB  1 
ATOM   22683 N  N   . LEU   B 1 1086 ? 54.44700   73.07600  24.19000  1.000 63.33466  ?  1084 LEU   B N   1 
ATOM   22684 C  CA  . LEU   B 1 1086 ? 55.61500   73.59000  23.48300  1.000 78.95201  ?  1084 LEU   B CA  1 
ATOM   22685 C  C   . LEU   B 1 1086 ? 56.32700   74.66800  24.29200  1.000 77.09582  ?  1084 LEU   B C   1 
ATOM   22686 O  O   . LEU   B 1 1086 ? 57.55200   74.61700  24.46300  1.000 68.03662  ?  1084 LEU   B O   1 
ATOM   22687 C  CB  . LEU   B 1 1086 ? 55.20000   74.13400  22.11500  1.000 74.16972  ?  1084 LEU   B CB  1 
ATOM   22688 C  CG  . LEU   B 1 1086 ? 56.25300   74.93200  21.34400  1.000 59.52129  ?  1084 LEU   B CG  1 
ATOM   22689 C  CD1 . LEU   B 1 1086 ? 57.40200   74.04100  20.88900  1.000 52.69710  ?  1084 LEU   B CD1 1 
ATOM   22690 C  CD2 . LEU   B 1 1086 ? 55.61300   75.64300  20.16100  1.000 63.07780  ?  1084 LEU   B CD2 1 
ATOM   22691 N  N   . LEU   B 1 1087 ? 55.57400   75.65100  24.78700  1.000 68.55415  ?  1085 LEU   B N   1 
ATOM   22692 C  CA  . LEU   B 1 1087 ? 56.15800   76.72800  25.58500  1.000 56.42172  ?  1085 LEU   B CA  1 
ATOM   22693 C  C   . LEU   B 1 1087 ? 57.01000   76.23400  26.74900  1.000 56.52034  ?  1085 LEU   B C   1 
ATOM   22694 O  O   . LEU   B 1 1087 ? 58.05400   76.85500  27.01400  1.000 62.03241  ?  1085 LEU   B O   1 
ATOM   22695 C  CB  . LEU   B 1 1087 ? 55.04500   77.65900  26.09000  1.000 40.78680  ?  1085 LEU   B CB  1 
ATOM   22696 C  CG  . LEU   B 1 1087 ? 54.13600   78.26400  25.01700  1.000 55.43951  ?  1085 LEU   B CG  1 
ATOM   22697 C  CD1 . LEU   B 1 1087 ? 53.08900   79.18700  25.63200  1.000 53.74393  ?  1085 LEU   B CD1 1 
ATOM   22698 C  CD2 . LEU   B 1 1087 ? 54.97000   79.00200  23.98000  1.000 47.85891  ?  1085 LEU   B CD2 1 
ATOM   22699 N  N   . PRO   B 1 1088 ? 56.64400   75.17400  27.48000  1.000 57.94739  ?  1086 PRO   B N   1 
ATOM   22700 C  CA  . PRO   B 1 1088 ? 57.59900   74.61100  28.44800  1.000 50.15872  ?  1086 PRO   B CA  1 
ATOM   22701 C  C   . PRO   B 1 1088 ? 58.93000   74.24200  27.81700  1.000 58.67160  ?  1086 PRO   B C   1 
ATOM   22702 O  O   . PRO   B 1 1088 ? 59.98000   74.69000  28.29000  1.000 73.54359  ?  1086 PRO   B O   1 
ATOM   22703 C  CB  . PRO   B 1 1088 ? 56.85200   73.39000  28.99300  1.000 50.08175  ?  1086 PRO   B CB  1 
ATOM   22704 C  CG  . PRO   B 1 1088 ? 55.42200   73.75800  28.88200  1.000 53.38166  ?  1086 PRO   B CG  1 
ATOM   22705 C  CD  . PRO   B 1 1088 ? 55.30700   74.56700  27.62300  1.000 59.48528  ?  1086 PRO   B CD  1 
ATOM   22706 N  N   . ALA   B 1 1089 ? 58.91200   73.45500  26.73800  1.000 70.02098  ?  1087 ALA   B N   1 
ATOM   22707 C  CA  . ALA   B 1 1089 ? 60.15900   73.03900  26.10300  1.000 76.58011  ?  1087 ALA   B CA  1 
ATOM   22708 C  C   . ALA   B 1 1089 ? 60.97600   74.24100  25.64900  1.000 79.76767  ?  1087 ALA   B C   1 
ATOM   22709 O  O   . ALA   B 1 1089 ? 62.19800   74.28100  25.83900  1.000 72.30166  ?  1087 ALA   B O   1 
ATOM   22710 C  CB  . ALA   B 1 1089 ? 59.86400   72.11300  24.92400  1.000 69.33132  ?  1087 ALA   B CB  1 
ATOM   22711 N  N   . LEU   B 1 1090 ? 60.31600   75.23900  25.05900  1.000 64.53794  ?  1088 LEU   B N   1 
ATOM   22712 C  CA  . LEU   B 1 1090 ? 61.01200   76.44800  24.64100  1.000 58.75629  ?  1088 LEU   B CA  1 
ATOM   22713 C  C   . LEU   B 1 1090 ? 61.52400   77.25700  25.82400  1.000 72.51032  ?  1088 LEU   B C   1 
ATOM   22714 O  O   . LEU   B 1 1090 ? 62.41400   78.09600  25.64800  1.000 82.07936  ?  1088 LEU   B O   1 
ATOM   22715 C  CB  . LEU   B 1 1090 ? 60.08600   77.29600  23.77100  1.000 65.63434  ?  1088 LEU   B CB  1 
ATOM   22716 C  CG  . LEU   B 1 1090 ? 59.87600   76.71200  22.37500  1.000 63.97511  ?  1088 LEU   B CG  1 
ATOM   22717 C  CD1 . LEU   B 1 1090 ? 59.15000   77.69600  21.48300  1.000 58.74675  ?  1088 LEU   B CD1 1 
ATOM   22718 C  CD2 . LEU   B 1 1090 ? 61.21500   76.31600  21.76700  1.000 73.24676  ?  1088 LEU   B CD2 1 
ATOM   22719 N  N   . GLN   B 1 1091 ? 60.98300   77.02700  27.02200  1.000 66.17932  ?  1089 GLN   B N   1 
ATOM   22720 C  CA  . GLN   B 1 1091 ? 61.53000   77.64300  28.22300  1.000 73.75070  ?  1089 GLN   B CA  1 
ATOM   22721 C  C   . GLN   B 1 1091 ? 62.75600   76.90500  28.74400  1.000 60.77717  ?  1089 GLN   B C   1 
ATOM   22722 O  O   . GLN   B 1 1091 ? 63.56700   77.50600  29.45700  1.000 66.55428  ?  1089 GLN   B O   1 
ATOM   22723 C  CB  . GLN   B 1 1091 ? 60.46000   77.71200  29.31600  1.000 75.36041  ?  1089 GLN   B CB  1 
ATOM   22724 C  CG  . GLN   B 1 1091 ? 59.75900   79.06000  29.42200  1.000 64.03576  ?  1089 GLN   B CG  1 
ATOM   22725 C  CD  . GLN   B 1 1091 ? 60.66400   80.14600  29.97300  1.000 78.76342  ?  1089 GLN   B CD  1 
ATOM   22726 O  OE1 . GLN   B 1 1091 ? 60.73800   81.24700  29.42600  1.000 80.81026  ?  1089 GLN   B OE1 1 
ATOM   22727 N  NE2 . GLN   B 1 1091 ? 61.36200   79.83800  31.06200  1.000 77.00931  ?  1089 GLN   B NE2 1 
ATOM   22728 N  N   . ASN   B 1 1092 ? 62.90900   75.62600  28.40800  1.000 60.64998  ?  1090 ASN   B N   1 
ATOM   22729 C  CA  . ASN   B 1 1092 ? 64.07500   74.83600  28.78800  1.000 79.07788  ?  1090 ASN   B CA  1 
ATOM   22730 C  C   . ASN   B 1 1092 ? 64.83500   74.36600  27.55500  1.000 81.73344  ?  1090 ASN   B C   1 
ATOM   22731 O  O   . ASN   B 1 1092 ? 65.37500   73.25800  27.51900  1.000 78.42217  ?  1090 ASN   B O   1 
ATOM   22732 C  CB  . ASN   B 1 1092 ? 63.68400   73.63900  29.65500  1.000 83.60466  ?  1090 ASN   B CB  1 
ATOM   22733 C  CG  . ASN   B 1 1092 ? 62.42000   73.87900  30.46200  1.000 86.28261  ?  1090 ASN   B CG  1 
ATOM   22734 O  OD1 . ASN   B 1 1092 ? 61.34700   73.38800  30.11800  1.000 73.67282  ?  1090 ASN   B OD1 1 
ATOM   22735 N  ND2 . ASN   B 1 1092 ? 62.54600   74.63000  31.54900  1.000 88.01433  ?  1090 ASN   B ND2 1 
ATOM   22736 N  N   . GLN   B 1 1093 ? 64.89600   75.21200  26.53000  1.000 77.29662  ?  1091 GLN   B N   1 
ATOM   22737 C  CA  . GLN   B 1 1093 ? 65.48400   74.82900  25.25300  1.000 60.40671  ?  1091 GLN   B CA  1 
ATOM   22738 C  C   . GLN   B 1 1093 ? 67.00400   74.92300  25.22900  1.000 56.72052  ?  1091 GLN   B C   1 
ATOM   22739 O  O   . GLN   B 1 1093 ? 67.60700   74.58300  24.20600  1.000 71.01333  ?  1091 GLN   B O   1 
ATOM   22740 C  CB  . GLN   B 1 1093 ? 64.90400   75.69600  24.13200  1.000 63.30654  ?  1091 GLN   B CB  1 
ATOM   22741 C  CG  . GLN   B 1 1093 ? 65.15300   77.18200  24.29900  1.000 63.32950  ?  1091 GLN   B CG  1 
ATOM   22742 C  CD  . GLN   B 1 1093 ? 65.42900   77.87300  22.97900  1.000 62.45003  ?  1091 GLN   B CD  1 
ATOM   22743 O  OE1 . GLN   B 1 1093 ? 64.65600   78.72400  22.53500  1.000 55.97431  ?  1091 GLN   B OE1 1 
ATOM   22744 N  NE2 . GLN   B 1 1093 ? 66.53700   77.50800  22.34300  1.000 55.91215  ?  1091 GLN   B NE2 1 
ATOM   22745 N  N   . TYR   B 1 1094 ? 67.64300   75.36400  26.31400  1.000 61.47800  ?  1092 TYR   B N   1 
ATOM   22746 C  CA  . TYR   B 1 1094 ? 69.08400   75.59000  26.32600  1.000 79.03970  ?  1092 TYR   B CA  1 
ATOM   22747 C  C   . TYR   B 1 1094 ? 69.84800   74.46000  27.00900  1.000 69.65261  ?  1092 TYR   B C   1 
ATOM   22748 O  O   . TYR   B 1 1094 ? 70.94600   74.67800  27.53200  1.000 59.83046  ?  1092 TYR   B O   1 
ATOM   22749 C  CB  . TYR   B 1 1094 ? 69.40300   76.93600  26.98000  1.000 60.60389  ?  1092 TYR   B CB  1 
ATOM   22750 C  CG  . TYR   B 1 1094 ? 68.70800   78.09300  26.29700  1.000 59.97941  ?  1092 TYR   B CG  1 
ATOM   22751 C  CD1 . TYR   B 1 1094 ? 69.14300   78.56000  25.06100  1.000 61.21249  ?  1092 TYR   B CD1 1 
ATOM   22752 C  CD2 . TYR   B 1 1094 ? 67.60200   78.70200  26.87400  1.000 65.45947  ?  1092 TYR   B CD2 1 
ATOM   22753 C  CE1 . TYR   B 1 1094 ? 68.49900   79.61100  24.42600  1.000 59.36776  ?  1092 TYR   B CE1 1 
ATOM   22754 C  CE2 . TYR   B 1 1094 ? 66.95400   79.75300  26.24800  1.000 72.23600  ?  1092 TYR   B CE2 1 
ATOM   22755 C  CZ  . TYR   B 1 1094 ? 67.40600   80.20400  25.02600  1.000 68.90391  ?  1092 TYR   B CZ  1 
ATOM   22756 O  OH  . TYR   B 1 1094 ? 66.75700   81.24900  24.40700  1.000 71.76724  ?  1092 TYR   B OH  1 
ATOM   22757 N  N   . VAL   B 1 1095 ? 69.29600   73.25600  27.00100  1.000 74.70490  ?  1093 VAL   B N   1 
ATOM   22758 C  CA  . VAL   B 1 1095 ? 69.95900   72.07300  27.54300  1.000 74.76724  ?  1093 VAL   B CA  1 
ATOM   22759 C  C   . VAL   B 1 1095 ? 70.56100   71.29500  26.38000  1.000 68.94486  ?  1093 VAL   B C   1 
ATOM   22760 O  O   . VAL   B 1 1095 ? 69.84500   71.01400  25.40800  1.000 81.32104  ?  1093 VAL   B O   1 
ATOM   22761 C  CB  . VAL   B 1 1095 ? 68.98500   71.18800  28.34000  1.000 93.06289  ?  1093 VAL   B CB  1 
ATOM   22762 C  CG1 . VAL   B 1 1095 ? 69.75000   70.30100  29.31600  1.000 75.81382  ?  1093 VAL   B CG1 1 
ATOM   22763 C  CG2 . VAL   B 1 1095 ? 67.96200   72.04300  29.05900  1.000 76.72433  ?  1093 VAL   B CG2 1 
ATOM   22764 N  N   . PRO   B 1 1096 ? 71.84400   70.94300  26.42900  1.000 50.98747  ?  1094 PRO   B N   1 
ATOM   22765 C  CA  . PRO   B 1 1096 ? 72.44000   70.17700  25.33000  1.000 67.45646  ?  1094 PRO   B CA  1 
ATOM   22766 C  C   . PRO   B 1 1096 ? 71.73400   68.84400  25.14300  1.000 80.23256  ?  1094 PRO   B C   1 
ATOM   22767 O  O   . PRO   B 1 1096 ? 71.21000   68.25400  26.09000  1.000 90.72980  ?  1094 PRO   B O   1 
ATOM   22768 C  CB  . PRO   B 1 1096 ? 73.89400   69.98500  25.77500  1.000 63.14208  ?  1094 PRO   B CB  1 
ATOM   22769 C  CG  . PRO   B 1 1096 ? 74.13900   71.09300  26.74700  1.000 80.79410  ?  1094 PRO   B CG  1 
ATOM   22770 C  CD  . PRO   B 1 1096 ? 72.83500   71.31000  27.45300  1.000 69.19489  ?  1094 PRO   B CD  1 
ATOM   22771 N  N   . PHE   B 1 1097 ? 71.71800   68.37500  23.89200  1.000 88.83358  ?  1095 PHE   B N   1 
ATOM   22772 C  CA  . PHE   B 1 1097 ? 71.01900   67.13200  23.58500  1.000 84.56516  ?  1095 PHE   B CA  1 
ATOM   22773 C  C   . PHE   B 1 1097 ? 71.67400   65.93400  24.25700  1.000 78.76911  ?  1095 PHE   B C   1 
ATOM   22774 O  O   . PHE   B 1 1097 ? 70.98400   64.96700  24.59900  1.000 77.76354  ?  1095 PHE   B O   1 
ATOM   22775 C  CB  . PHE   B 1 1097 ? 70.94700   66.91400  22.07400  1.000 79.50729  ?  1095 PHE   B CB  1 
ATOM   22776 C  CG  . PHE   B 1 1097 ? 69.91200   65.90700  21.66200  1.000 64.86247  ?  1095 PHE   B CG  1 
ATOM   22777 C  CD1 . PHE   B 1 1097 ? 68.56200   66.18000  21.82100  1.000 52.13351  ?  1095 PHE   B CD1 1 
ATOM   22778 C  CD2 . PHE   B 1 1097 ? 70.28600   64.68100  21.13400  1.000 56.34505  ?  1095 PHE   B CD2 1 
ATOM   22779 C  CE1 . PHE   B 1 1097 ? 67.60200   65.25400  21.45200  1.000 49.24837  ?  1095 PHE   B CE1 1 
ATOM   22780 C  CE2 . PHE   B 1 1097 ? 69.33000   63.74800  20.76300  1.000 58.75913  ?  1095 PHE   B CE2 1 
ATOM   22781 C  CZ  . PHE   B 1 1097 ? 67.98600   64.03500  20.92300  1.000 47.04728  ?  1095 PHE   B CZ  1 
ATOM   22782 N  N   . ASP   B 1 1098 ? 72.99500   65.97300  24.45000  1.000 68.29891  ?  1096 ASP   B N   1 
ATOM   22783 C  CA  . ASP   B 1 1098 ? 73.65100   64.91500  25.21000  1.000 85.66673  ?  1096 ASP   B CA  1 
ATOM   22784 C  C   . ASP   B 1 1098 ? 73.10300   64.84500  26.62900  1.000 96.35068  ?  1096 ASP   B C   1 
ATOM   22785 O  O   . ASP   B 1 1098 ? 72.85900   63.75300  27.15400  1.000 94.88376  ?  1096 ASP   B O   1 
ATOM   22786 C  CB  . ASP   B 1 1098 ? 75.16300   65.13700  25.23000  1.000 92.59441  ?  1096 ASP   B CB  1 
ATOM   22787 C  CG  . ASP   B 1 1098 ? 75.75300   65.23100  23.84100  1.000 112.69014 ?  1096 ASP   B CG  1 
ATOM   22788 O  OD1 . ASP   B 1 1098 ? 75.01700   64.96600  22.86800  1.000 109.75738 ?  1096 ASP   B OD1 1 
ATOM   22789 O  OD2 . ASP   B 1 1098 ? 76.95100   65.56800  23.72400  1.000 116.11358 -1 1096 ASP   B OD2 1 
ATOM   22790 N  N   . LYS   B 1 1099 ? 72.88500   66.00300  27.25800  1.000 84.43195  ?  1097 LYS   B N   1 
ATOM   22791 C  CA  . LYS   B 1 1099 ? 72.38200   66.02100  28.62800  1.000 84.87672  ?  1097 LYS   B CA  1 
ATOM   22792 C  C   . LYS   B 1 1099 ? 70.94300   65.52400  28.70400  1.000 85.50253  ?  1097 LYS   B C   1 
ATOM   22793 O  O   . LYS   B 1 1099 ? 70.56200   64.86300  29.67700  1.000 94.62691  ?  1097 LYS   B O   1 
ATOM   22794 C  CB  . LYS   B 1 1099 ? 72.49600   67.43100  29.21000  1.000 82.01414  ?  1097 LYS   B CB  1 
ATOM   22795 N  N   . ILE   B 1 1100 ? 70.12600   65.83500  27.69300  1.000 73.23444  ?  1098 ILE   B N   1 
ATOM   22796 C  CA  . ILE   B 1 1100 ? 68.74200   65.36600  27.69600  1.000 74.03659  ?  1098 ILE   B CA  1 
ATOM   22797 C  C   . ILE   B 1 1100 ? 68.69100   63.84900  27.59200  1.000 82.83370  ?  1098 ILE   B C   1 
ATOM   22798 O  O   . ILE   B 1 1100 ? 67.77800   63.21100  28.13200  1.000 97.70816  ?  1098 ILE   B O   1 
ATOM   22799 C  CB  . ILE   B 1 1100 ? 67.94300   66.03500  26.56000  1.000 79.19049  ?  1098 ILE   B CB  1 
ATOM   22800 C  CG1 . ILE   B 1 1100 ? 68.04800   67.55700  26.65800  1.000 86.36753  ?  1098 ILE   B CG1 1 
ATOM   22801 C  CG2 . ILE   B 1 1100 ? 66.47900   65.60000  26.59700  1.000 72.04328  ?  1098 ILE   B CG2 1 
ATOM   22802 C  CD1 . ILE   B 1 1100 ? 67.08800   68.29600  25.75200  1.000 83.00843  ?  1098 ILE   B CD1 1 
ATOM   22803 N  N   . LEU   B 1 1101 ? 69.66800   63.24500  26.91500  1.000 73.38891  ?  1099 LEU   B N   1 
ATOM   22804 C  CA  . LEU   B 1 1101 ? 69.66600   61.79400  26.76100  1.000 79.41042  ?  1099 LEU   B CA  1 
ATOM   22805 C  C   . LEU   B 1 1101 ? 70.03600   61.10200  28.06700  1.000 78.93067  ?  1099 LEU   B C   1 
ATOM   22806 O  O   . LEU   B 1 1101 ? 69.39400   60.12200  28.46300  1.000 95.93731  ?  1099 LEU   B O   1 
ATOM   22807 C  CB  . LEU   B 1 1101 ? 70.61600   61.38600  25.63500  1.000 79.68092  ?  1099 LEU   B CB  1 
ATOM   22808 C  CG  . LEU   B 1 1101 ? 70.14300   61.74700  24.22400  1.000 62.44781  ?  1099 LEU   B CG  1 
ATOM   22809 C  CD1 . LEU   B 1 1101 ? 71.02200   61.08600  23.17500  1.000 57.65618  ?  1099 LEU   B CD1 1 
ATOM   22810 C  CD2 . LEU   B 1 1101 ? 68.68000   61.36500  24.02200  1.000 55.63655  ?  1099 LEU   B CD2 1 
ATOM   22811 N  N   . GLU   B 1 1102 ? 71.06900   61.59700  28.75200  1.000 79.45053  ?  1100 GLU   B N   1 
ATOM   22812 C  CA  . GLU   B 1 1102 ? 71.43500   61.02000  30.04200  1.000 80.88540  ?  1100 GLU   B CA  1 
ATOM   22813 C  C   . GLU   B 1 1102 ? 70.31200   61.19200  31.05700  1.000 77.01969  ?  1100 GLU   B C   1 
ATOM   22814 O  O   . GLU   B 1 1102 ? 70.08000   60.31200  31.89300  1.000 77.97951  ?  1100 GLU   B O   1 
ATOM   22815 C  CB  . GLU   B 1 1102 ? 72.72900   61.65100  30.55500  1.000 76.75358  ?  1100 GLU   B CB  1 
ATOM   22816 C  CG  . GLU   B 1 1102 ? 73.75500   61.92800  29.47000  1.000 91.86611  ?  1100 GLU   B CG  1 
ATOM   22817 C  CD  . GLU   B 1 1102 ? 75.13800   61.40900  29.81700  1.000 124.26019 ?  1100 GLU   B CD  1 
ATOM   22818 O  OE1 . GLU   B 1 1102 ? 75.40200   61.16600  31.01300  1.000 124.67968 ?  1100 GLU   B OE1 1 
ATOM   22819 O  OE2 . GLU   B 1 1102 ? 75.96300   61.25000  28.89200  1.000 120.44101 -1 1100 GLU   B OE2 1 
ATOM   22820 N  N   . ALA   B 1 1103 ? 69.59900   62.31800  30.99400  1.000 87.76441  ?  1101 ALA   B N   1 
ATOM   22821 C  CA  . ALA   B 1 1103 ? 68.45600   62.52800  31.87400  1.000 95.46392  ?  1101 ALA   B CA  1 
ATOM   22822 C  C   . ALA   B 1 1103 ? 67.26900   61.65300  31.49300  1.000 99.52980  ?  1101 ALA   B C   1 
ATOM   22823 O  O   . ALA   B 1 1103 ? 66.42800   61.36200  32.35000  1.000 99.34608  ?  1101 ALA   B O   1 
ATOM   22824 C  CB  . ALA   B 1 1103 ? 68.04600   64.00100  31.86400  1.000 89.07057  ?  1101 ALA   B CB  1 
ATOM   22825 N  N   . ALA   B 1 1104 ? 67.18300   61.23000  30.23300  1.000 99.23508  ?  1102 ALA   B N   1 
ATOM   22826 C  CA  . ALA   B 1 1104 ? 66.12100   60.33400  29.80100  1.000 92.93484  ?  1102 ALA   B CA  1 
ATOM   22827 C  C   . ALA   B 1 1104 ? 66.49800   58.86400  29.92700  1.000 97.74639  ?  1102 ALA   B C   1 
ATOM   22828 O  O   . ALA   B 1 1104 ? 65.60200   58.01300  29.93300  1.000 93.46062  ?  1102 ALA   B O   1 
ATOM   22829 C  CB  . ALA   B 1 1104 ? 65.72500   60.64000  28.35200  1.000 88.08034  ?  1102 ALA   B CB  1 
ATOM   22830 N  N   . ARG   B 1 1105 ? 67.79400   58.55600  30.04200  1.000 93.02290  ?  1103 ARG   B N   1 
ATOM   22831 C  CA  . ARG   B 1 1105 ? 68.28200   57.18000  30.16700  1.000 97.30950  ?  1103 ARG   B CA  1 
ATOM   22832 C  C   . ARG   B 1 1105 ? 67.64500   56.27400  29.11600  1.000 108.23784 ?  1103 ARG   B C   1 
ATOM   22833 O  O   . ARG   B 1 1105 ? 67.08100   55.22000  29.42100  1.000 96.91945  ?  1103 ARG   B O   1 
ATOM   22834 C  CB  . ARG   B 1 1105 ? 68.03300   56.63200  31.57300  1.000 102.81541 ?  1103 ARG   B CB  1 
ATOM   22835 C  CG  . ARG   B 1 1105 ? 69.09800   56.96000  32.61000  1.000 99.71828  ?  1103 ARG   B CG  1 
ATOM   22836 C  CD  . ARG   B 1 1105 ? 68.67500   56.39400  33.95900  1.000 99.93662  ?  1103 ARG   B CD  1 
ATOM   22837 N  NE  . ARG   B 1 1105 ? 69.67300   56.56700  35.00600  1.000 97.97425  ?  1103 ARG   B NE  1 
ATOM   22838 C  CZ  . ARG   B 1 1105 ? 70.23100   55.56700  35.67400  1.000 122.15458 ?  1103 ARG   B CZ  1 
ATOM   22839 N  NH1 . ARG   B 1 1105 ? 69.95400   54.30500  35.38700  1.000 124.71729 ?  1103 ARG   B NH1 1 
ATOM   22840 N  NH2 . ARG   B 1 1105 ? 71.08800   55.83800  36.65500  1.000 125.74205 ?  1103 ARG   B NH2 1 
ATOM   22841 N  N   . VAL   B 1 1106 ? 67.73000   56.69800  27.86500  1.000 101.90360 ?  1104 VAL   B N   1 
ATOM   22842 C  CA  . VAL   B 1 1106 ? 67.06300   56.01300  26.76600  1.000 89.34057  ?  1104 VAL   B CA  1 
ATOM   22843 C  C   . VAL   B 1 1106 ? 67.96200   54.89900  26.24800  1.000 87.12726  ?  1104 VAL   B C   1 
ATOM   22844 O  O   . VAL   B 1 1106 ? 69.18000   55.07200  26.11200  1.000 68.74235  ?  1104 VAL   B O   1 
ATOM   22845 C  CB  . VAL   B 1 1106 ? 66.69400   57.01100  25.65000  1.000 89.09749  ?  1104 VAL   B CB  1 
ATOM   22846 C  CG1 . VAL   B 1 1106 ? 67.88400   57.89700  25.30600  1.000 90.26587  ?  1104 VAL   B CG1 1 
ATOM   22847 C  CG2 . VAL   B 1 1106 ? 66.16800   56.28100  24.41700  1.000 86.83378  ?  1104 VAL   B CG2 1 
ATOM   22848 N  N   . LYS   B 1 1107 ? 67.36100   53.74200  25.97400  1.000 88.06387  ?  1105 LYS   B N   1 
ATOM   22849 C  CA  . LYS   B 1 1107 ? 68.10500   52.61000  25.44000  1.000 85.37462  ?  1105 LYS   B CA  1 
ATOM   22850 C  C   . LYS   B 1 1107 ? 68.51600   52.86900  23.99500  1.000 94.60541  ?  1105 LYS   B C   1 
ATOM   22851 O  O   . LYS   B 1 1107 ? 67.87700   53.63700  23.27000  1.000 88.75253  ?  1105 LYS   B O   1 
ATOM   22852 C  CB  . LYS   B 1 1107 ? 67.26800   51.33300  25.52400  1.000 90.15122  ?  1105 LYS   B CB  1 
ATOM   22853 N  N   . ARG   B 1 1108 ? 69.59900   52.21500  23.57700  1.000 89.48956  ?  1106 ARG   B N   1 
ATOM   22854 C  CA  . ARG   B 1 1108 ? 70.15900   52.38400  22.23700  1.000 88.03113  ?  1106 ARG   B CA  1 
ATOM   22855 C  C   . ARG   B 1 1108 ? 69.74900   51.18200  21.39200  1.000 87.18037  ?  1106 ARG   B C   1 
ATOM   22856 O  O   . ARG   B 1 1108 ? 70.35100   50.10900  21.48600  1.000 105.43304 ?  1106 ARG   B O   1 
ATOM   22857 C  CB  . ARG   B 1 1108 ? 71.67500   52.53600  22.30000  1.000 70.95490  ?  1106 ARG   B CB  1 
ATOM   22858 N  N   . GLU   B 1 1109 ? 68.72200   51.36700  20.55900  1.000 90.74744  ?  1107 GLU   B N   1 
ATOM   22859 C  CA  . GLU   B 1 1109 ? 68.23500   50.26700  19.73200  1.000 104.02696 ?  1107 GLU   B CA  1 
ATOM   22860 C  C   . GLU   B 1 1109 ? 69.20500   49.93000  18.60600  1.000 100.49281 ?  1107 GLU   B C   1 
ATOM   22861 O  O   . GLU   B 1 1109 ? 69.28200   48.76900  18.18600  1.000 99.57291  ?  1107 GLU   B O   1 
ATOM   22862 C  CB  . GLU   B 1 1109 ? 66.85900   50.60700  19.15700  1.000 87.96761  ?  1107 GLU   B CB  1 
ATOM   22863 C  CG  . GLU   B 1 1109 ? 65.81200   50.94800  20.20400  1.000 83.54201  ?  1107 GLU   B CG  1 
ATOM   22864 C  CD  . GLU   B 1 1109 ? 65.25300   49.71900  20.89100  1.000 100.51730 ?  1107 GLU   B CD  1 
ATOM   22865 O  OE1 . GLU   B 1 1109 ? 65.36800   48.61300  20.32200  1.000 110.48936 ?  1107 GLU   B OE1 1 
ATOM   22866 O  OE2 . GLU   B 1 1109 ? 64.69800   49.85900  22.00200  1.000 92.18484  -1 1107 GLU   B OE2 1 
ATOM   22867 N  N   . GLY   B 1 1110 ? 69.94200   50.90900  18.11200  1.000 79.95200  ?  1108 GLY   B N   1 
ATOM   22868 C  CA  . GLY   B 1 1110 ? 70.87300   50.68600  17.01100  1.000 83.37294  ?  1108 GLY   B CA  1 
ATOM   22869 C  C   . GLY   B 1 1110 ? 70.28700   50.88000  15.62700  1.000 88.71705  ?  1108 GLY   B C   1 
ATOM   22870 O  O   . GLY   B 1 1110 ? 70.87500   51.56700  14.79400  1.000 91.83107  ?  1108 GLY   B O   1 
ATOM   22871 N  N   . ASN   B 1 1111 ? 69.13300   50.26700  15.36300  1.000 89.91066  ?  1109 ASN   B N   1 
ATOM   22872 C  CA  . ASN   B 1 1111 ? 68.42700   50.49700  14.11000  1.000 82.56756  ?  1109 ASN   B CA  1 
ATOM   22873 C  C   . ASN   B 1 1111 ? 67.58200   51.76800  14.10800  1.000 80.57646  ?  1109 ASN   B C   1 
ATOM   22874 O  O   . ASN   B 1 1111 ? 67.07300   52.14300  13.04600  1.000 81.89803  ?  1109 ASN   B O   1 
ATOM   22875 C  CB  . ASN   B 1 1111 ? 67.54400   49.29000  13.76400  1.000 67.09162  ?  1109 ASN   B CB  1 
ATOM   22876 C  CG  . ASN   B 1 1111 ? 66.38400   49.09600  14.74000  1.000 88.51083  ?  1109 ASN   B CG  1 
ATOM   22877 O  OD1 . ASN   B 1 1111 ? 66.35900   49.67700  15.82900  1.000 99.02046  ?  1109 ASN   B OD1 1 
ATOM   22878 N  ND2 . ASN   B 1 1111 ? 65.39700   48.29700  14.33000  1.000 97.12279  ?  1109 ASN   B ND2 1 
ATOM   22879 N  N   . ARG   B 1 1112 ? 67.43400   52.44100  15.25000  1.000 66.65995  ?  1110 ARG   B N   1 
ATOM   22880 C  CA  . ARG   B 1 1112 ? 66.64200   53.65700  15.35600  1.000 64.50321  ?  1110 ARG   B CA  1 
ATOM   22881 C  C   . ARG   B 1 1112 ? 67.47600   54.76100  15.98600  1.000 62.40782  ?  1110 ARG   B C   1 
ATOM   22882 O  O   . ARG   B 1 1112 ? 68.53000   54.51900  16.57900  1.000 67.31057  ?  1110 ARG   B O   1 
ATOM   22883 C  CB  . ARG   B 1 1112 ? 65.37100   53.42200  16.18300  1.000 57.31994  ?  1110 ARG   B CB  1 
ATOM   22884 C  CG  . ARG   B 1 1112 ? 64.64800   52.15100  15.77700  1.000 71.80226  ?  1110 ARG   B CG  1 
ATOM   22885 C  CD  . ARG   B 1 1112 ? 63.37200   51.88000  16.56000  1.000 70.08290  ?  1110 ARG   B CD  1 
ATOM   22886 N  NE  . ARG   B 1 1112 ? 62.38600   52.94900  16.48000  1.000 72.28528  ?  1110 ARG   B NE  1 
ATOM   22887 C  CZ  . ARG   B 1 1112 ? 61.26200   52.84600  15.78800  1.000 80.87111  ?  1110 ARG   B CZ  1 
ATOM   22888 N  NH1 . ARG   B 1 1112 ? 60.98200   51.75400  15.09900  1.000 71.97273  ?  1110 ARG   B NH1 1 
ATOM   22889 N  NH2 . ARG   B 1 1112 ? 60.40600   53.86600  15.77300  1.000 89.85895  ?  1110 ARG   B NH2 1 
ATOM   22890 N  N   . HIS   B 1 1113 ? 66.99100   55.95900  15.85100  1.000 67.36479  ?  1111 HIS   B N   1 
ATOM   22891 C  CA  . HIS   B 1 1113 ? 67.67000   57.09900  16.43500  1.000 66.08914  ?  1111 HIS   B CA  1 
ATOM   22892 C  C   . HIS   B 1 1113 ? 67.18300   57.32600  17.86100  1.000 76.43661  ?  1111 HIS   B C   1 
ATOM   22893 O  O   . HIS   B 1 1113 ? 66.05200   56.96000  18.20300  1.000 71.24676  ?  1111 HIS   B O   1 
ATOM   22894 C  CB  . HIS   B 1 1113 ? 67.42500   58.35300  15.59800  1.000 67.52779  ?  1111 HIS   B CB  1 
ATOM   22895 C  CG  . HIS   B 1 1113 ? 68.04100   58.29900  14.23300  1.000 80.32688  ?  1111 HIS   B CG  1 
ATOM   22896 N  ND1 . HIS   B 1 1113 ? 67.41200   57.71600  13.15300  1.000 83.96024  ?  1111 HIS   B ND1 1 
ATOM   22897 C  CD2 . HIS   B 1 1113 ? 69.23000   58.75700  13.77300  1.000 82.19649  ?  1111 HIS   B CD2 1 
ATOM   22898 C  CE1 . HIS   B 1 1113 ? 68.18700   57.81600  12.08800  1.000 80.65966  ?  1111 HIS   B CE1 1 
ATOM   22899 N  NE2 . HIS   B 1 1113 ? 69.29600   58.44300  12.43700  1.000 75.68171  ?  1111 HIS   B NE2 1 
ATOM   22900 N  N   . PRO   B 1 1114 ? 68.02500   57.90800  18.71200  1.000 80.86258  ?  1112 PRO   B N   1 
ATOM   22901 C  CA  . PRO   B 1 1114 ? 67.61800   58.15300  20.10000  1.000 64.36849  ?  1112 PRO   B CA  1 
ATOM   22902 C  C   . PRO   B 1 1114 ? 66.38100   59.03900  20.18300  1.000 65.87249  ?  1112 PRO   B C   1 
ATOM   22903 O  O   . PRO   B 1 1114 ? 66.27800   60.06400  19.50300  1.000 75.29162  ?  1112 PRO   B O   1 
ATOM   22904 C  CB  . PRO   B 1 1114 ? 68.85300   58.83100  20.71100  1.000 63.87821  ?  1112 PRO   B CB  1 
ATOM   22905 C  CG  . PRO   B 1 1114 ? 69.63700   59.33600  19.52700  1.000 69.37189  ?  1112 PRO   B CG  1 
ATOM   22906 C  CD  . PRO   B 1 1114 ? 69.43400   58.27400  18.49600  1.000 69.04556  ?  1112 PRO   B CD  1 
ATOM   22907 N  N   . LEU   B 1 1115 ? 65.42100   58.59900  20.99900  1.000 67.97556  ?  1113 LEU   B N   1 
ATOM   22908 C  CA  . LEU   B 1 1115 ? 64.21000   59.34200  21.33900  1.000 66.46846  ?  1113 LEU   B CA  1 
ATOM   22909 C  C   . LEU   B 1 1115 ? 63.24500   59.50000  20.16700  1.000 67.77753  ?  1113 LEU   B C   1 
ATOM   22910 O  O   . LEU   B 1 1115 ? 62.14700   58.93300  20.19700  1.000 80.97081  ?  1113 LEU   B O   1 
ATOM   22911 C  CB  . LEU   B 1 1115 ? 64.57200   60.70800  21.92500  1.000 67.29740  ?  1113 LEU   B CB  1 
ATOM   22912 C  CG  . LEU   B 1 1115 ? 64.68700   60.70000  23.45200  1.000 63.47823  ?  1113 LEU   B CG  1 
ATOM   22913 C  CD1 . LEU   B 1 1115 ? 64.73800   62.11100  24.00100  1.000 63.99231  ?  1113 LEU   B CD1 1 
ATOM   22914 C  CD2 . LEU   B 1 1115 ? 63.53400   59.92200  24.07300  1.000 54.04401  ?  1113 LEU   B CD2 1 
ATOM   22915 N  N   . PHE   B 1 1116 ? 63.61000   60.26900  19.14300  1.000 69.56818  ?  1114 PHE   B N   1 
ATOM   22916 C  CA  . PHE   B 1 1116 ? 62.71200   60.48000  18.01600  1.000 70.39828  ?  1114 PHE   B CA  1 
ATOM   22917 C  C   . PHE   B 1 1116 ? 63.37200   60.06600  16.70700  1.000 60.25760  ?  1114 PHE   B C   1 
ATOM   22918 O  O   . PHE   B 1 1116 ? 64.60000   60.02200  16.58400  1.000 71.12618  ?  1114 PHE   B O   1 
ATOM   22919 C  CB  . PHE   B 1 1116 ? 62.23400   61.94300  17.91900  1.000 66.18058  ?  1114 PHE   B CB  1 
ATOM   22920 C  CG  . PHE   B 1 1116 ? 63.33300   62.96400  18.03000  1.000 66.95097  ?  1114 PHE   B CG  1 
ATOM   22921 C  CD1 . PHE   B 1 1116 ? 64.14800   63.25100  16.94500  1.000 77.19703  ?  1114 PHE   B CD1 1 
ATOM   22922 C  CD2 . PHE   B 1 1116 ? 63.53400   63.65600  19.21300  1.000 65.92657  ?  1114 PHE   B CD2 1 
ATOM   22923 C  CE1 . PHE   B 1 1116 ? 65.15500   64.19400  17.04400  1.000 75.20534  ?  1114 PHE   B CE1 1 
ATOM   22924 C  CE2 . PHE   B 1 1116 ? 64.53900   64.60200  19.31900  1.000 76.31087  ?  1114 PHE   B CE2 1 
ATOM   22925 C  CZ  . PHE   B 1 1116 ? 65.35000   64.87100  18.23200  1.000 80.62528  ?  1114 PHE   B CZ  1 
ATOM   22926 N  N   . ASP   B 1 1117 ? 62.52100   59.75200  15.72700  1.000 60.33511  ?  1115 ASP   B N   1 
ATOM   22927 C  CA  . ASP   B 1 1117 ? 62.94800   59.45000  14.37000  1.000 63.14214  ?  1115 ASP   B CA  1 
ATOM   22928 C  C   . ASP   B 1 1117 ? 62.31800   60.36100  13.32700  1.000 59.98500  ?  1115 ASP   B C   1 
ATOM   22929 O  O   . ASP   B 1 1117 ? 62.80500   60.39900  12.19100  1.000 60.68143  ?  1115 ASP   B O   1 
ATOM   22930 C  CB  . ASP   B 1 1117 ? 62.62700   57.98900  14.01600  1.000 79.96453  ?  1115 ASP   B CB  1 
ATOM   22931 C  CG  . ASP   B 1 1117 ? 63.62500   57.01200  14.61000  1.000 73.42822  ?  1115 ASP   B CG  1 
ATOM   22932 O  OD1 . ASP   B 1 1117 ? 64.77400   56.95700  14.12000  1.000 64.47658  ?  1115 ASP   B OD1 1 
ATOM   22933 O  OD2 . ASP   B 1 1117 ? 63.25900   56.30100  15.57000  1.000 61.26361  -1 1115 ASP   B OD2 1 
ATOM   22934 N  N   . VAL   B 1 1118 ? 61.25800   61.08700  13.67400  1.000 51.20794  ?  1116 VAL   B N   1 
ATOM   22935 C  CA  . VAL   B 1 1118 ? 60.66800   62.10800  12.81600  1.000 43.32426  ?  1116 VAL   B CA  1 
ATOM   22936 C  C   . VAL   B 1 1118 ? 61.09200   63.47300  13.34000  1.000 54.65195  ?  1116 VAL   B C   1 
ATOM   22937 O  O   . VAL   B 1 1118 ? 60.95700   63.75200  14.53800  1.000 66.52323  ?  1116 VAL   B O   1 
ATOM   22938 C  CB  . VAL   B 1 1118 ? 59.13600   61.98900  12.78300  1.000 35.05109  ?  1116 VAL   B CB  1 
ATOM   22939 C  CG1 . VAL   B 1 1118 ? 58.57700   62.67700  11.55000  1.000 48.53868  ?  1116 VAL   B CG1 1 
ATOM   22940 C  CG2 . VAL   B 1 1118 ? 58.72400   60.53100  12.82400  1.000 55.67433  ?  1116 VAL   B CG2 1 
ATOM   22941 N  N   . MET   B 1 1119 ? 61.60200   64.32400  12.45000  1.000 43.48107  ?  1117 MET   B N   1 
ATOM   22942 C  CA  . MET   B 1 1119 ? 62.07100   65.65500  12.81400  1.000 40.89851  ?  1117 MET   B CA  1 
ATOM   22943 C  C   . MET   B 1 1119 ? 61.26500   66.71900  12.08100  1.000 41.37719  ?  1117 MET   B C   1 
ATOM   22944 O  O   . MET   B 1 1119 ? 60.98600   66.58700  10.88500  1.000 57.50797  ?  1117 MET   B O   1 
ATOM   22945 C  CB  . MET   B 1 1119 ? 63.56500   65.82300  12.50800  1.000 49.51489  ?  1117 MET   B CB  1 
ATOM   22946 C  CG  . MET   B 1 1119 ? 64.06400   67.25800  12.61000  1.000 56.49396  ?  1117 MET   B CG  1 
ATOM   22947 S  SD  . MET   B 1 1119 ? 64.31200   67.81200  14.30300  1.000 57.77148  ?  1117 MET   B SD  1 
ATOM   22948 C  CE  . MET   B 1 1119 ? 65.90700   67.09000  14.66600  1.000 47.26886  ?  1117 MET   B CE  1 
ATOM   22949 N  N   . PHE   B 1 1120 ? 60.90000   67.77600  12.80300  1.000 45.71963  ?  1118 PHE   B N   1 
ATOM   22950 C  CA  . PHE   B 1 1120 ? 60.10800   68.87400  12.26300  1.000 48.68606  ?  1118 PHE   B CA  1 
ATOM   22951 C  C   . PHE   B 1 1120 ? 60.87000   70.17800  12.44900  1.000 54.47241  ?  1118 PHE   B C   1 
ATOM   22952 O  O   . PHE   B 1 1120 ? 61.12400   70.59300  13.58500  1.000 60.34860  ?  1118 PHE   B O   1 
ATOM   22953 C  CB  . PHE   B 1 1120 ? 58.74300   68.94600  12.94900  1.000 41.55415  ?  1118 PHE   B CB  1 
ATOM   22954 C  CG  . PHE   B 1 1120 ? 57.84600   70.01700  12.40600  1.000 45.77331  ?  1118 PHE   B CG  1 
ATOM   22955 C  CD1 . PHE   B 1 1120 ? 57.58900   70.10100  11.04800  1.000 50.41143  ?  1118 PHE   B CD1 1 
ATOM   22956 C  CD2 . PHE   B 1 1120 ? 57.25300   70.93600  13.25500  1.000 52.45197  ?  1118 PHE   B CD2 1 
ATOM   22957 C  CE1 . PHE   B 1 1120 ? 56.75900   71.08500  10.54500  1.000 50.30612  ?  1118 PHE   B CE1 1 
ATOM   22958 C  CE2 . PHE   B 1 1120 ? 56.42200   71.92300  12.75900  1.000 57.80501  ?  1118 PHE   B CE2 1 
ATOM   22959 C  CZ  . PHE   B 1 1120 ? 56.17500   71.99800  11.40200  1.000 46.13127  ?  1118 PHE   B CZ  1 
ATOM   22960 N  N   . MET   B 1 1121 ? 61.23300   70.82000  11.34200  1.000 52.36911  ?  1119 MET   B N   1 
ATOM   22961 C  CA  . MET   B 1 1121 ? 61.90600   72.11200  11.36200  1.000 48.33652  ?  1119 MET   B CA  1 
ATOM   22962 C  C   . MET   B 1 1121 ? 61.03000   73.16100  10.68800  1.000 43.86915  ?  1119 MET   B C   1 
ATOM   22963 O  O   . MET   B 1 1121 ? 60.06900   72.84600  9.98100   1.000 46.25488  ?  1119 MET   B O   1 
ATOM   22964 C  CB  . MET   B 1 1121 ? 63.27200   72.04500  10.66900  1.000 46.24223  ?  1119 MET   B CB  1 
ATOM   22965 C  CG  . MET   B 1 1121 ? 63.99500   70.72300  10.82500  1.000 50.45215  ?  1119 MET   B CG  1 
ATOM   22966 S  SD  . MET   B 1 1121 ? 65.63000   70.79600  10.07300  1.000 58.40641  ?  1119 MET   B SD  1 
ATOM   22967 C  CE  . MET   B 1 1121 ? 66.43200   69.38400  10.82900  1.000 50.44483  ?  1119 MET   B CE  1 
ATOM   22968 N  N   . MET   B 1 1122 ? 61.37400   74.42700  10.91500  1.000 37.74411  ?  1120 MET   B N   1 
ATOM   22969 C  CA  . MET   B 1 1122 ? 60.63200   75.52400  10.31300  1.000 41.96889  ?  1120 MET   B CA  1 
ATOM   22970 C  C   . MET   B 1 1122 ? 61.51300   76.76400  10.26000  1.000 52.61355  ?  1120 MET   B C   1 
ATOM   22971 O  O   . MET   B 1 1122 ? 62.20000   77.08500  11.23200  1.000 52.34810  ?  1120 MET   B O   1 
ATOM   22972 C  CB  . MET   B 1 1122 ? 59.34700   75.82100  11.09000  1.000 27.53713  ?  1120 MET   B CB  1 
ATOM   22973 C  CG  . MET   B 1 1122 ? 58.40200   76.75200  10.35900  1.000 35.63774  ?  1120 MET   B CG  1 
ATOM   22974 S  SD  . MET   B 1 1122 ? 56.68100   76.41400  10.75500  1.000 52.90663  ?  1120 MET   B SD  1 
ATOM   22975 C  CE  . MET   B 1 1122 ? 55.86900   77.83000  10.01900  1.000 37.12688  ?  1120 MET   B CE  1 
ATOM   22976 N  N   . GLN   B 1 1123 ? 61.49000   77.44900  9.11700   1.000 48.22315  ?  1121 GLN   B N   1 
ATOM   22977 C  CA  . GLN   B 1 1123 ? 62.20000   78.70400  8.92600   1.000 44.99752  ?  1121 GLN   B CA  1 
ATOM   22978 C  C   . GLN   B 1 1123 ? 61.20700   79.79900  8.56300   1.000 54.34862  ?  1121 GLN   B C   1 
ATOM   22979 O  O   . GLN   B 1 1123 ? 60.21000   79.55200  7.87800   1.000 38.98814  ?  1121 GLN   B O   1 
ATOM   22980 C  CB  . GLN   B 1 1123 ? 63.26300   78.59400  7.82500   1.000 52.17491  ?  1121 GLN   B CB  1 
ATOM   22981 C  CG  . GLN   B 1 1123 ? 64.59900   78.05700  8.30000   1.000 62.52424  ?  1121 GLN   B CG  1 
ATOM   22982 C  CD  . GLN   B 1 1123 ? 65.68200   78.18200  7.24800   1.000 64.81852  ?  1121 GLN   B CD  1 
ATOM   22983 O  OE1 . GLN   B 1 1123 ? 66.41200   79.17400  7.20600   1.000 74.68823  ?  1121 GLN   B OE1 1 
ATOM   22984 N  NE2 . GLN   B 1 1123 ? 65.79400   77.17400  6.39000   1.000 50.20559  ?  1121 GLN   B NE2 1 
ATOM   22985 N  N   . GLY   B 1 1124 ? 61.48400   81.01100  9.02400   1.000 62.46190  ?  1122 GLY   B N   1 
ATOM   22986 C  CA  . GLY   B 1 1124 ? 60.62400   82.13000  8.71900   1.000 43.88678  ?  1122 GLY   B CA  1 
ATOM   22987 C  C   . GLY   B 1 1124 ? 60.83400   82.62700  7.30200   1.000 57.09124  ?  1122 GLY   B C   1 
ATOM   22988 O  O   . GLY   B 1 1124 ? 61.55800   82.04700  6.49200   1.000 77.39319  ?  1122 GLY   B O   1 
ATOM   22989 N  N   . ALA   B 1 1125 ? 60.17400   83.74100  7.00400   1.000 50.73683  ?  1123 ALA   B N   1 
ATOM   22990 C  CA  . ALA   B 1 1125 ? 60.33800   84.37100  5.70800   1.000 52.47622  ?  1123 ALA   B CA  1 
ATOM   22991 C  C   . ALA   B 1 1125 ? 61.76100   84.91200  5.56600   1.000 56.28014  ?  1123 ALA   B C   1 
ATOM   22992 O  O   . ALA   B 1 1125 ? 62.39500   85.28000  6.55800   1.000 52.54213  ?  1123 ALA   B O   1 
ATOM   22993 C  CB  . ALA   B 1 1125 ? 59.32400   85.49800  5.53500   1.000 42.00904  ?  1123 ALA   B CB  1 
ATOM   22994 N  N   . PRO   B 1 1126 ? 62.29500   84.95400  4.34500   1.000 54.43491  ?  1124 PRO   B N   1 
ATOM   22995 C  CA  . PRO   B 1 1126 ? 63.66300   85.45600  4.16500   1.000 54.07469  ?  1124 PRO   B CA  1 
ATOM   22996 C  C   . PRO   B 1 1126 ? 63.76000   86.93200  4.51900   1.000 57.85837  ?  1124 PRO   B C   1 
ATOM   22997 O  O   . PRO   B 1 1126 ? 62.86300   87.72300  4.21700   1.000 61.88556  ?  1124 PRO   B O   1 
ATOM   22998 C  CB  . PRO   B 1 1126 ? 63.94100   85.21700  2.67400   1.000 50.44734  ?  1124 PRO   B CB  1 
ATOM   22999 C  CG  . PRO   B 1 1126 ? 62.91300   84.22700  2.23400   1.000 52.75323  ?  1124 PRO   B CG  1 
ATOM   23000 C  CD  . PRO   B 1 1126 ? 61.70600   84.49800  3.07500   1.000 52.63649  ?  1124 PRO   B CD  1 
ATOM   23001 N  N   . GLU   B 1 1127 ? 64.86400   87.29700  5.17400   1.000 52.53131  ?  1125 GLU   B N   1 
ATOM   23002 C  CA  . GLU   B 1 1127 ? 65.06100   88.68700  5.57200   1.000 61.70839  ?  1125 GLU   B CA  1 
ATOM   23003 C  C   . GLU   B 1 1127 ? 65.48200   89.55200  4.39000   1.000 59.96029  ?  1125 GLU   B C   1 
ATOM   23004 O  O   . GLU   B 1 1127 ? 65.02500   90.69300  4.25600   1.000 65.02016  ?  1125 GLU   B O   1 
ATOM   23005 C  CB  . GLU   B 1 1127 ? 66.10000   88.77700  6.69400   1.000 67.79999  ?  1125 GLU   B CB  1 
ATOM   23006 C  CG  . GLU   B 1 1127 ? 65.68200   88.11600  8.00700   1.000 72.71256  ?  1125 GLU   B CG  1 
ATOM   23007 C  CD  . GLU   B 1 1127 ? 64.62500   88.90300  8.76800   1.000 94.24716  ?  1125 GLU   B CD  1 
ATOM   23008 O  OE1 . GLU   B 1 1127 ? 64.25200   90.00800  8.32000   1.000 104.13207 ?  1125 GLU   B OE1 1 
ATOM   23009 O  OE2 . GLU   B 1 1127 ? 64.16000   88.41000  9.81800   1.000 95.52857  -1 1125 GLU   B OE2 1 
ATOM   23010 N  N   . THR   B 1 1128 ? 66.34300   89.02700  3.52600   1.000 58.01823  ?  1126 THR   B N   1 
ATOM   23011 C  CA  . THR   B 1 1128 ? 66.84300   89.75300  2.37200   1.000 39.64615  ?  1126 THR   B CA  1 
ATOM   23012 C  C   . THR   B 1 1128 ? 66.41500   89.05700  1.09000   1.000 44.26378  ?  1126 THR   B C   1 
ATOM   23013 O  O   . THR   B 1 1128 ? 66.03900   87.88200  1.08800   1.000 44.79364  ?  1126 THR   B O   1 
ATOM   23014 C  CB  . THR   B 1 1128 ? 68.36600   89.86300  2.40200   1.000 37.92286  ?  1126 THR   B CB  1 
ATOM   23015 O  OG1 . THR   B 1 1128 ? 68.92100   88.61400  2.83600   1.000 51.38183  ?  1126 THR   B OG1 1 
ATOM   23016 C  CG2 . THR   B 1 1128 ? 68.79100   90.96400  3.35400   1.000 67.01516  ?  1126 THR   B CG2 1 
ATOM   23017 N  N   . GLU   B 1 1129 ? 66.48600   89.80200  -0.01400  1.000 46.19115  ?  1127 GLU   B N   1 
ATOM   23018 C  CA  . GLU   B 1 1129 ? 66.14500   89.21900  -1.30400  1.000 40.44259  ?  1127 GLU   B CA  1 
ATOM   23019 C  C   . GLU   B 1 1129 ? 67.15100   88.15400  -1.71500  1.000 44.46516  ?  1127 GLU   B C   1 
ATOM   23020 O  O   . GLU   B 1 1129 ? 66.77600   87.16400  -2.35200  1.000 50.31747  ?  1127 GLU   B O   1 
ATOM   23021 C  CB  . GLU   B 1 1129 ? 66.05600   90.30800  -2.37200  1.000 50.17910  ?  1127 GLU   B CB  1 
ATOM   23022 C  CG  . GLU   B 1 1129 ? 65.58100   89.80800  -3.72900  1.000 55.82253  ?  1127 GLU   B CG  1 
ATOM   23023 C  CD  . GLU   B 1 1129 ? 65.58800   90.89000  -4.79200  1.000 82.22432  ?  1127 GLU   B CD  1 
ATOM   23024 O  OE1 . GLU   B 1 1129 ? 65.57000   92.08600  -4.43100  1.000 95.82082  ?  1127 GLU   B OE1 1 
ATOM   23025 O  OE2 . GLU   B 1 1129 ? 65.62000   90.54300  -5.99100  1.000 95.32688  -1 1127 GLU   B OE2 1 
ATOM   23026 N  N   . LEU   B 1 1130 ? 68.42600   88.33600  -1.36200  1.000 43.01286  ?  1128 LEU   B N   1 
ATOM   23027 C  CA  . LEU   B 1 1130 ? 69.42600   87.32500  -1.68700  1.000 49.58952  ?  1128 LEU   B CA  1 
ATOM   23028 C  C   . LEU   B 1 1130 ? 69.12900   86.01800  -0.96800  1.000 43.94741  ?  1128 LEU   B C   1 
ATOM   23029 O  O   . LEU   B 1 1130 ? 69.32600   84.93300  -1.52600  1.000 54.13907  ?  1128 LEU   B O   1 
ATOM   23030 C  CB  . LEU   B 1 1130 ? 70.82500   87.82700  -1.33300  1.000 51.78327  ?  1128 LEU   B CB  1 
ATOM   23031 C  CG  . LEU   B 1 1130 ? 71.98900   86.98900  -1.87000  1.000 38.02784  ?  1128 LEU   B CG  1 
ATOM   23032 C  CD1 . LEU   B 1 1130 ? 73.01800   87.87000  -2.55600  1.000 47.97514  ?  1128 LEU   B CD1 1 
ATOM   23033 C  CD2 . LEU   B 1 1130 ? 72.63400   86.18600  -0.75400  1.000 47.13194  ?  1128 LEU   B CD2 1 
ATOM   23034 N  N   . GLU   B 1 1131 ? 68.64300   86.10300  0.27200   1.000 46.44420  ?  1129 GLU   B N   1 
ATOM   23035 C  CA  . GLU   B 1 1131 ? 68.29400   84.89600  1.01100   1.000 47.71332  ?  1129 GLU   B CA  1 
ATOM   23036 C  C   . GLU   B 1 1131 ? 67.12100   84.16700  0.36900   1.000 37.39878  ?  1129 GLU   B C   1 
ATOM   23037 O  O   . GLU   B 1 1131 ? 67.06200   82.93300  0.41200   1.000 49.46001  ?  1129 GLU   B O   1 
ATOM   23038 C  CB  . GLU   B 1 1131 ? 67.97400   85.24800  2.46300   1.000 46.88715  ?  1129 GLU   B CB  1 
ATOM   23039 C  CG  . GLU   B 1 1131 ? 67.80200   84.04300  3.36600   1.000 54.34868  ?  1129 GLU   B CG  1 
ATOM   23040 C  CD  . GLU   B 1 1131 ? 67.39000   84.42500  4.77000   1.000 56.67847  ?  1129 GLU   B CD  1 
ATOM   23041 O  OE1 . GLU   B 1 1131 ? 67.43300   85.63000  5.09800   1.000 63.24860  ?  1129 GLU   B OE1 1 
ATOM   23042 O  OE2 . GLU   B 1 1131 ? 67.02300   83.51700  5.54500   1.000 66.59766  -1 1129 GLU   B OE2 1 
ATOM   23043 N  N   . SER   B 1 1132 ? 66.18800   84.90400  -0.23400  1.000 43.75983  ?  1130 SER   B N   1 
ATOM   23044 C  CA  . SER   B 1 1132 ? 65.03200   84.26400  -0.84900  1.000 39.59463  ?  1130 SER   B CA  1 
ATOM   23045 C  C   . SER   B 1 1132 ? 65.41500   83.50100  -2.11000  1.000 39.09093  ?  1130 SER   B C   1 
ATOM   23046 O  O   . SER   B 1 1132 ? 64.75800   82.51400  -2.45700  1.000 43.57168  ?  1130 SER   B O   1 
ATOM   23047 C  CB  . SER   B 1 1132 ? 63.96700   85.30800  -1.16800  1.000 43.42419  ?  1130 SER   B CB  1 
ATOM   23048 O  OG  . SER   B 1 1132 ? 64.42400   86.18400  -2.18200  1.000 54.29832  ?  1130 SER   B OG  1 
ATOM   23049 N  N   . ASN   B 1 1133 ? 66.46700   83.93700  -2.80500  1.000 43.59269  ?  1131 ASN   B N   1 
ATOM   23050 C  CA  . ASN   B 1 1133 ? 66.91100   83.30600  -4.04000  1.000 34.97354  ?  1131 ASN   B CA  1 
ATOM   23051 C  C   . ASN   B 1 1133 ? 67.98100   82.24100  -3.81100  1.000 45.83416  ?  1131 ASN   B C   1 
ATOM   23052 O  O   . ASN   B 1 1133 ? 68.64800   81.83000  -4.76900  1.000 46.56640  ?  1131 ASN   B O   1 
ATOM   23053 C  CB  . ASN   B 1 1133 ? 67.42100   84.36600  -5.02000  1.000 38.27132  ?  1131 ASN   B CB  1 
ATOM   23054 C  CG  . ASN   B 1 1133 ? 66.37900   85.42300  -5.32500  1.000 41.39652  ?  1131 ASN   B CG  1 
ATOM   23055 O  OD1 . ASN   B 1 1133 ? 66.68600   86.61400  -5.39300  1.000 55.91494  ?  1131 ASN   B OD1 1 
ATOM   23056 N  ND2 . ASN   B 1 1133 ? 65.13400   84.99400  -5.50300  1.000 47.01491  ?  1131 ASN   B ND2 1 
ATOM   23057 N  N   . MET   B 1 1134 ? 68.15400   81.78700  -2.57300  1.000 41.65881  ?  1132 MET   B N   1 
ATOM   23058 C  CA  . MET   B 1 1134 ? 69.04500   80.67800  -2.26800  1.000 36.07650  ?  1132 MET   B CA  1 
ATOM   23059 C  C   . MET   B 1 1134 ? 68.27700   79.36300  -2.28000  1.000 38.76642  ?  1132 MET   B C   1 
ATOM   23060 O  O   . MET   B 1 1134 ? 67.08000   79.31700  -1.98600  1.000 60.76932  ?  1132 MET   B O   1 
ATOM   23061 C  CB  . MET   B 1 1134 ? 69.70700   80.87300  -0.90600  1.000 39.58263  ?  1132 MET   B CB  1 
ATOM   23062 C  CG  . MET   B 1 1134 ? 70.72100   81.99500  -0.87400  1.000 48.47256  ?  1132 MET   B CG  1 
ATOM   23063 S  SD  . MET   B 1 1134 ? 71.61700   82.06600  0.68300   1.000 50.08018  ?  1132 MET   B SD  1 
ATOM   23064 C  CE  . MET   B 1 1134 ? 70.39500   81.35400  1.77700   1.000 60.69587  ?  1132 MET   B CE  1 
ATOM   23065 N  N   . HIS   B 1 1135 ? 68.98300   78.28500  -2.61200  1.000 36.03254  ?  1133 HIS   B N   1 
ATOM   23066 C  CA  . HIS   B 1 1135 ? 68.38700   76.95500  -2.68300  1.000 33.45794  ?  1133 HIS   B CA  1 
ATOM   23067 C  C   . HIS   B 1 1135 ? 69.25100   75.97800  -1.90300  1.000 34.79000  ?  1133 HIS   B C   1 
ATOM   23068 O  O   . HIS   B 1 1135 ? 70.42900   75.79700  -2.22500  1.000 43.32205  ?  1133 HIS   B O   1 
ATOM   23069 C  CB  . HIS   B 1 1135 ? 68.24000   76.49400  -4.13400  1.000 45.00011  ?  1133 HIS   B CB  1 
ATOM   23070 C  CG  . HIS   B 1 1135 ? 67.33100   77.35600  -4.95200  1.000 51.74563  ?  1133 HIS   B CG  1 
ATOM   23071 N  ND1 . HIS   B 1 1135 ? 67.79700   78.23200  -5.90900  1.000 49.60505  ?  1133 HIS   B ND1 1 
ATOM   23072 C  CD2 . HIS   B 1 1135 ? 65.98200   77.47500  -4.95700  1.000 55.78902  ?  1133 HIS   B CD2 1 
ATOM   23073 C  CE1 . HIS   B 1 1135 ? 66.77400   78.85400  -6.46700  1.000 74.73254  ?  1133 HIS   B CE1 1 
ATOM   23074 N  NE2 . HIS   B 1 1135 ? 65.66200   78.41400  -5.90800  1.000 66.10427  ?  1133 HIS   B NE2 1 
ATOM   23075 N  N   . HIS   B 1 1136 ? 68.66800   75.34500  -0.88900  1.000 38.27441  ?  1134 HIS   B N   1 
ATOM   23076 C  CA  . HIS   B 1 1136 ? 69.40000   74.33800  -0.13400  1.000 37.84017  ?  1134 HIS   B CA  1 
ATOM   23077 C  C   . HIS   B 1 1136 ? 69.50600   73.05900  -0.95100  1.000 40.49000  ?  1134 HIS   B C   1 
ATOM   23078 O  O   . HIS   B 1 1136 ? 68.50900   72.56200  -1.48400  1.000 38.97240  ?  1134 HIS   B O   1 
ATOM   23079 C  CB  . HIS   B 1 1136 ? 68.71700   74.06200  1.20300   1.000 33.13203  ?  1134 HIS   B CB  1 
ATOM   23080 C  CG  . HIS   B 1 1136 ? 69.52000   73.19200  2.12200   1.000 48.27188  ?  1134 HIS   B CG  1 
ATOM   23081 N  ND1 . HIS   B 1 1136 ? 68.95200   72.19100  2.88100   1.000 49.02560  ?  1134 HIS   B ND1 1 
ATOM   23082 C  CD2 . HIS   B 1 1136 ? 70.84400   73.17300  2.40500   1.000 47.96976  ?  1134 HIS   B CD2 1 
ATOM   23083 C  CE1 . HIS   B 1 1136 ? 69.89200   71.59200  3.59100   1.000 43.98208  ?  1134 HIS   B CE1 1 
ATOM   23084 N  NE2 . HIS   B 1 1136 ? 71.04900   72.16800  3.32000   1.000 47.12494  ?  1134 HIS   B NE2 1 
ATOM   23085 N  N   . ILE   B 1 1137 ? 70.71800   72.52900  -1.05200  1.000 39.53373  ?  1135 ILE   B N   1 
ATOM   23086 C  CA  . ILE   B 1 1137 ? 71.00000   71.34700  -1.85400  1.000 35.34949  ?  1135 ILE   B CA  1 
ATOM   23087 C  C   . ILE   B 1 1137 ? 71.12100   70.14000  -0.93900  1.000 35.75875  ?  1135 ILE   B C   1 
ATOM   23088 O  O   . ILE   B 1 1137 ? 71.75600   70.20600  0.12200   1.000 46.24567  ?  1135 ILE   B O   1 
ATOM   23089 C  CB  . ILE   B 1 1137 ? 72.28000   71.53400  -2.68800  1.000 47.07547  ?  1135 ILE   B CB  1 
ATOM   23090 C  CG1 . ILE   B 1 1137 ? 72.29700   72.92500  -3.32200  1.000 49.70460  ?  1135 ILE   B CG1 1 
ATOM   23091 C  CG2 . ILE   B 1 1137 ? 72.37500   70.46200  -3.75100  1.000 34.03773  ?  1135 ILE   B CG2 1 
ATOM   23092 C  CD1 . ILE   B 1 1137 ? 71.13900   73.17400  -4.26000  1.000 37.45586  ?  1135 ILE   B CD1 1 
ATOM   23093 N  N   . ASN   B 1 1138 ? 70.51000   69.03400  -1.34900  1.000 36.41633  ?  1136 ASN   B N   1 
ATOM   23094 C  CA  . ASN   B 1 1138 ? 70.58500   67.76900  -0.63400  1.000 39.05075  ?  1136 ASN   B CA  1 
ATOM   23095 C  C   . ASN   B 1 1138 ? 71.47500   66.82100  -1.42400  1.000 37.34348  ?  1136 ASN   B C   1 
ATOM   23096 O  O   . ASN   B 1 1138 ? 71.21800   66.56400  -2.60600  1.000 34.42701  ?  1136 ASN   B O   1 
ATOM   23097 C  CB  . ASN   B 1 1138 ? 69.19500   67.16400  -0.43900  1.000 37.90977  ?  1136 ASN   B CB  1 
ATOM   23098 C  CG  . ASN   B 1 1138 ? 69.19800   65.98800  0.52100   1.000 41.52336  ?  1136 ASN   B CG  1 
ATOM   23099 O  OD1 . ASN   B 1 1138 ? 69.35200   64.83800  0.11100   1.000 40.25537  ?  1136 ASN   B OD1 1 
ATOM   23100 N  ND2 . ASN   B 1 1138 ? 69.01200   66.27100  1.80500   1.000 46.79283  ?  1136 ASN   B ND2 1 
ATOM   23101 N  N   . ALA   B 1 1139 ? 72.51800   66.31000  -0.77600  1.000 40.23489  ?  1137 ALA   B N   1 
ATOM   23102 C  CA  . ALA   B 1 1139 ? 73.42900   65.36300  -1.40200  1.000 34.77600  ?  1137 ALA   B CA  1 
ATOM   23103 C  C   . ALA   B 1 1139 ? 72.91600   63.92500  -1.34500  1.000 39.04394  ?  1137 ALA   B C   1 
ATOM   23104 O  O   . ALA   B 1 1139 ? 73.70200   62.98500  -1.52500  1.000 44.74469  ?  1137 ALA   B O   1 
ATOM   23105 C  CB  . ALA   B 1 1139 ? 74.81200   65.46300  -0.75500  1.000 30.22814  ?  1137 ALA   B CB  1 
ATOM   23106 N  N   . GLY   B 1 1140 ? 71.61800   63.73700  -1.11300  1.000 36.27748  ?  1138 GLY   B N   1 
ATOM   23107 C  CA  . GLY   B 1 1140 ? 71.04500   62.41000  -1.02300  1.000 31.54538  ?  1138 GLY   B CA  1 
ATOM   23108 C  C   . GLY   B 1 1140 ? 71.30600   61.77400  0.32400   1.000 34.01372  ?  1138 GLY   B C   1 
ATOM   23109 O  O   . GLY   B 1 1140 ? 71.74900   60.62500  0.40400   1.000 40.12445  ?  1138 GLY   B O   1 
ATOM   23110 N  N   . ILE   B 1 1141 ? 71.05300   62.52700  1.39200   1.000 38.57816  ?  1139 ILE   B N   1 
ATOM   23111 C  CA  . ILE   B 1 1141 ? 71.30600   62.08600  2.75800   1.000 38.77154  ?  1139 ILE   B CA  1 
ATOM   23112 C  C   . ILE   B 1 1141 ? 70.09000   62.42300  3.60800   1.000 43.29041  ?  1139 ILE   B C   1 
ATOM   23113 O  O   . ILE   B 1 1141 ? 69.59700   63.55600  3.57200   1.000 43.46857  ?  1139 ILE   B O   1 
ATOM   23114 C  CB  . ILE   B 1 1141 ? 72.57200   62.73800  3.35100   1.000 38.54796  ?  1139 ILE   B CB  1 
ATOM   23115 C  CG1 . ILE   B 1 1141 ? 73.70600   62.75200  2.32400   1.000 39.18258  ?  1139 ILE   B CG1 1 
ATOM   23116 C  CG2 . ILE   B 1 1141 ? 73.00400   62.02000  4.61900   1.000 50.75459  ?  1139 ILE   B CG2 1 
ATOM   23117 C  CD1 . ILE   B 1 1141 ? 74.99800   63.31200  2.85100   1.000 51.51784  ?  1139 ILE   B CD1 1 
ATOM   23118 N  N   . SER   B 1 1142 ? 69.60700   61.44100  4.36400   1.000 42.71708  ?  1140 SER   B N   1 
ATOM   23119 C  CA  . SER   B 1 1142 ? 68.53300   61.63700  5.33300   1.000 37.92830  ?  1140 SER   B CA  1 
ATOM   23120 C  C   . SER   B 1 1142 ? 69.10800   61.35500  6.71400   1.000 49.30514  ?  1140 SER   B C   1 
ATOM   23121 O  O   . SER   B 1 1142 ? 69.38200   60.19800  7.05200   1.000 58.81738  ?  1140 SER   B O   1 
ATOM   23122 C  CB  . SER   B 1 1142 ? 67.34100   60.73000  5.03200   1.000 39.30350  ?  1140 SER   B CB  1 
ATOM   23123 O  OG  . SER   B 1 1142 ? 66.22900   61.05400  5.85100   1.000 48.90285  ?  1140 SER   B OG  1 
ATOM   23124 N  N   . LYS   B 1 1143 ? 69.30500   62.41200  7.50500   1.000 48.48576  ?  1141 LYS   B N   1 
ATOM   23125 C  CA  . LYS   B 1 1143 ? 69.87200   62.24300  8.83700   1.000 48.77062  ?  1141 LYS   B CA  1 
ATOM   23126 C  C   . LYS   B 1 1143 ? 68.93300   61.49000  9.77000   1.000 48.30653  ?  1141 LYS   B C   1 
ATOM   23127 O  O   . LYS   B 1 1143 ? 69.39100   60.94600  10.78000  1.000 56.00559  ?  1141 LYS   B O   1 
ATOM   23128 C  CB  . LYS   B 1 1143 ? 70.23800   63.60700  9.42800   1.000 60.87336  ?  1141 LYS   B CB  1 
ATOM   23129 C  CG  . LYS   B 1 1143 ? 71.22800   64.39700  8.57700   1.000 65.54250  ?  1141 LYS   B CG  1 
ATOM   23130 C  CD  . LYS   B 1 1143 ? 71.76400   65.61600  9.31100   1.000 53.39861  ?  1141 LYS   B CD  1 
ATOM   23131 C  CE  . LYS   B 1 1143 ? 70.77700   66.76800  9.26300   1.000 65.96319  ?  1141 LYS   B CE  1 
ATOM   23132 N  NZ  . LYS   B 1 1143 ? 70.75700   67.53900  10.53600  1.000 79.07839  ?  1141 LYS   B NZ  1 
ATOM   23133 N  N   . PHE   B 1 1144 ? 67.64000   61.43700  9.45000   1.000 51.38878  ?  1142 PHE   B N   1 
ATOM   23134 C  CA  . PHE   B 1 1144 ? 66.68400   60.65200  10.22000  1.000 55.76157  ?  1142 PHE   B CA  1 
ATOM   23135 C  C   . PHE   B 1 1144 ? 65.83700   59.78800  9.29800   1.000 57.59786  ?  1142 PHE   B C   1 
ATOM   23136 O  O   . PHE   B 1 1144 ? 66.12900   59.66300  8.10400   1.000 59.92869  ?  1142 PHE   B O   1 
ATOM   23137 C  CB  . PHE   B 1 1144 ? 65.78100   61.55900  11.05500  1.000 53.27456  ?  1142 PHE   B CB  1 
ATOM   23138 C  CG  . PHE   B 1 1144 ? 66.52700   62.48800  11.96000  1.000 71.84662  ?  1142 PHE   B CG  1 
ATOM   23139 C  CD1 . PHE   B 1 1144 ? 67.32100   61.99500  12.98200  1.000 80.48615  ?  1142 PHE   B CD1 1 
ATOM   23140 C  CD2 . PHE   B 1 1144 ? 66.43800   63.85600  11.78700  1.000 65.80255  ?  1142 PHE   B CD2 1 
ATOM   23141 C  CE1 . PHE   B 1 1144 ? 68.00600   62.85200  13.82000  1.000 66.87273  ?  1142 PHE   B CE1 1 
ATOM   23142 C  CE2 . PHE   B 1 1144 ? 67.12300   64.71600  12.61600  1.000 65.85276  ?  1142 PHE   B CE2 1 
ATOM   23143 C  CZ  . PHE   B 1 1144 ? 67.90900   64.21500  13.63500  1.000 63.89012  ?  1142 PHE   B CZ  1 
ATOM   23144 N  N   . ASP   B 1 1145 ? 64.78700   59.17900  9.84800   1.000 47.59429  ?  1143 ASP   B N   1 
ATOM   23145 C  CA  . ASP   B 1 1145 ? 63.87300   58.41000  9.01400   1.000 46.00375  ?  1143 ASP   B CA  1 
ATOM   23146 C  C   . ASP   B 1 1145 ? 63.00200   59.33000  8.17400   1.000 40.43731  ?  1143 ASP   B C   1 
ATOM   23147 O  O   . ASP   B 1 1145 ? 62.67500   59.01100  7.02500   1.000 47.21131  ?  1143 ASP   B O   1 
ATOM   23148 C  CB  . ASP   B 1 1145 ? 63.00400   57.50000  9.87600   1.000 56.49175  ?  1143 ASP   B CB  1 
ATOM   23149 C  CG  . ASP   B 1 1145 ? 63.81800   56.54200  10.72000  1.000 54.91614  ?  1143 ASP   B CG  1 
ATOM   23150 O  OD1 . ASP   B 1 1145 ? 65.06400   56.54400  10.61100  1.000 59.84357  ?  1143 ASP   B OD1 1 
ATOM   23151 O  OD2 . ASP   B 1 1145 ? 63.20000   55.78100  11.49300  1.000 53.49432  -1 1143 ASP   B OD2 1 
ATOM   23152 N  N   . LEU   B 1 1146 ? 62.61800   60.47700  8.72900   1.000 36.32561  ?  1144 LEU   B N   1 
ATOM   23153 C  CA  . LEU   B 1 1146 ? 61.75400   61.41500  8.02200   1.000 38.28618  ?  1144 LEU   B CA  1 
ATOM   23154 C  C   . LEU   B 1 1146 ? 61.92400   62.78600  8.65100   1.000 36.68149  ?  1144 LEU   B C   1 
ATOM   23155 O  O   . LEU   B 1 1146 ? 61.67700   62.95200  9.84900   1.000 37.77744  ?  1144 LEU   B O   1 
ATOM   23156 C  CB  . LEU   B 1 1146 ? 60.29600   60.96800  8.08500   1.000 33.92734  ?  1144 LEU   B CB  1 
ATOM   23157 C  CG  . LEU   B 1 1146 ? 59.31700   61.89800  7.37400   1.000 28.73483  ?  1144 LEU   B CG  1 
ATOM   23158 C  CD1 . LEU   B 1 1146 ? 59.68300   62.01000  5.90600   1.000 36.72889  ?  1144 LEU   B CD1 1 
ATOM   23159 C  CD2 . LEU   B 1 1146 ? 57.88100   61.42600  7.54500   1.000 41.07737  ?  1144 LEU   B CD2 1 
ATOM   23160 N  N   . THR   B 1 1147 ? 62.34500   63.76000  7.85300   1.000 41.56858  ?  1145 THR   B N   1 
ATOM   23161 C  CA  . THR   B 1 1147 ? 62.47900   65.13800  8.29900   1.000 34.74462  ?  1145 THR   B CA  1 
ATOM   23162 C  C   . THR   B 1 1147 ? 61.52700   66.01200  7.50000   1.000 40.51700  ?  1145 THR   B C   1 
ATOM   23163 O  O   . THR   B 1 1147 ? 61.52600   65.96900  6.26500   1.000 51.32987  ?  1145 THR   B O   1 
ATOM   23164 C  CB  . THR   B 1 1147 ? 63.91600   65.63600  8.13700   1.000 33.28760  ?  1145 THR   B CB  1 
ATOM   23165 O  OG1 . THR   B 1 1147 ? 64.82800   64.62300  8.58100   1.000 50.97147  ?  1145 THR   B OG1 1 
ATOM   23166 C  CG2 . THR   B 1 1147 ? 64.12700   66.89300  8.95500   1.000 34.78211  ?  1145 THR   B CG2 1 
ATOM   23167 N  N   . LEU   B 1 1148 ? 60.71300   66.79400  8.20200   1.000 31.21578  ?  1146 LEU   B N   1 
ATOM   23168 C  CA  . LEU   B 1 1148 ? 59.81400   67.75800  7.58200   1.000 37.21260  ?  1146 LEU   B CA  1 
ATOM   23169 C  C   . LEU   B 1 1148 ? 60.31100   69.16000  7.90500   1.000 45.33271  ?  1146 LEU   B C   1 
ATOM   23170 O  O   . LEU   B 1 1148 ? 60.44300   69.51500  9.08100   1.000 44.04714  ?  1146 LEU   B O   1 
ATOM   23171 C  CB  . LEU   B 1 1148 ? 58.38000   67.57400  8.07600   1.000 40.82904  ?  1146 LEU   B CB  1 
ATOM   23172 C  CG  . LEU   B 1 1148 ? 57.49700   66.56200  7.34500   1.000 47.35107  ?  1146 LEU   B CG  1 
ATOM   23173 C  CD1 . LEU   B 1 1148 ? 57.70800   65.16700  7.90400   1.000 48.01524  ?  1146 LEU   B CD1 1 
ATOM   23174 C  CD2 . LEU   B 1 1148 ? 56.03700   66.96900  7.44500   1.000 30.35700  ?  1146 LEU   B CD2 1 
ATOM   23175 N  N   . GLU   B 1 1149 ? 60.59100   69.95000  6.87000   1.000 35.03070  ?  1147 GLU   B N   1 
ATOM   23176 C  CA  . GLU   B 1 1149 ? 60.94700   71.35400  7.03200   1.000 35.97135  ?  1147 GLU   B CA  1 
ATOM   23177 C  C   . GLU   B 1 1149 ? 59.93400   72.21200  6.29300   1.000 32.55839  ?  1147 GLU   B C   1 
ATOM   23178 O  O   . GLU   B 1 1149 ? 59.64700   71.96600  5.11700   1.000 40.74891  ?  1147 GLU   B O   1 
ATOM   23179 C  CB  . GLU   B 1 1149 ? 62.36200   71.65400  6.52100   1.000 44.23401  ?  1147 GLU   B CB  1 
ATOM   23180 C  CG  . GLU   B 1 1149 ? 62.74300   73.13300  6.63600   1.000 55.43803  ?  1147 GLU   B CG  1 
ATOM   23181 C  CD  . GLU   B 1 1149 ? 64.23900   73.36300  6.79200   1.000 69.77157  ?  1147 GLU   B CD  1 
ATOM   23182 O  OE1 . GLU   B 1 1149 ? 65.02900   72.59700  6.20100   1.000 61.09901  ?  1147 GLU   B OE1 1 
ATOM   23183 O  OE2 . GLU   B 1 1149 ? 64.62500   74.31500  7.50700   1.000 64.51862  -1 1147 GLU   B OE2 1 
ATOM   23184 N  N   . VAL   B 1 1150 ? 59.39400   73.21300  6.98500   1.000 30.18835  ?  1148 VAL   B N   1 
ATOM   23185 C  CA  . VAL   B 1 1150 ? 58.45200   74.16300  6.40300   1.000 37.35532  ?  1148 VAL   B CA  1 
ATOM   23186 C  C   . VAL   B 1 1150 ? 59.18700   75.47200  6.15400   1.000 43.15323  ?  1148 VAL   B C   1 
ATOM   23187 O  O   . VAL   B 1 1150 ? 59.81800   76.02200  7.06600   1.000 50.99247  ?  1148 VAL   B O   1 
ATOM   23188 C  CB  . VAL   B 1 1150 ? 57.23400   74.37500  7.32000   1.000 40.34523  ?  1148 VAL   B CB  1 
ATOM   23189 C  CG1 . VAL   B 1 1150 ? 56.34000   75.48500  6.78200   1.000 38.33214  ?  1148 VAL   B CG1 1 
ATOM   23190 C  CG2 . VAL   B 1 1150 ? 56.44400   73.08300  7.46200   1.000 35.33660  ?  1148 VAL   B CG2 1 
ATOM   23191 N  N   . LEU   B 1 1151 ? 59.12100   75.96600  4.91900   1.000 42.53522  ?  1149 LEU   B N   1 
ATOM   23192 C  CA  . LEU   B 1 1151 ? 59.78800   77.20000  4.52700   1.000 47.71671  ?  1149 LEU   B CA  1 
ATOM   23193 C  C   . LEU   B 1 1151 ? 58.76500   78.16700  3.94900   1.000 51.08279  ?  1149 LEU   B C   1 
ATOM   23194 O  O   . LEU   B 1 1151 ? 58.03600   77.82000  3.01400   1.000 51.44385  ?  1149 LEU   B O   1 
ATOM   23195 C  CB  . LEU   B 1 1151 ? 60.89900   76.92800  3.50800   1.000 40.15500  ?  1149 LEU   B CB  1 
ATOM   23196 C  CG  . LEU   B 1 1151 ? 61.98200   75.92900  3.92500   1.000 42.05715  ?  1149 LEU   B CG  1 
ATOM   23197 C  CD1 . LEU   B 1 1151 ? 62.21100   74.90200  2.83200   1.000 52.07205  ?  1149 LEU   B CD1 1 
ATOM   23198 C  CD2 . LEU   B 1 1151 ? 63.28100   76.64200  4.26400   1.000 56.66963  ?  1149 LEU   B CD2 1 
ATOM   23199 N  N   . GLU   B 1 1152 ? 58.70900   79.37400  4.51000   1.000 60.40696  ?  1150 GLU   B N   1 
ATOM   23200 C  CA  . GLU   B 1 1152 ? 57.82300   80.42200  4.00800   1.000 58.38006  ?  1150 GLU   B CA  1 
ATOM   23201 C  C   . GLU   B 1 1152 ? 58.52200   81.10700  2.84200   1.000 61.77660  ?  1150 GLU   B C   1 
ATOM   23202 O  O   . GLU   B 1 1152 ? 59.43100   81.91700  3.03500   1.000 76.67088  ?  1150 GLU   B O   1 
ATOM   23203 C  CB  . GLU   B 1 1152 ? 57.47500   81.41900  5.10900   1.000 62.86977  ?  1150 GLU   B CB  1 
ATOM   23204 C  CG  . GLU   B 1 1152 ? 57.03300   80.78800  6.42200   1.000 70.33566  ?  1150 GLU   B CG  1 
ATOM   23205 C  CD  . GLU   B 1 1152 ? 56.34000   81.77800  7.34500   1.000 86.48895  ?  1150 GLU   B CD  1 
ATOM   23206 O  OE1 . GLU   B 1 1152 ? 55.69800   82.72300  6.83600   1.000 61.09281  ?  1150 GLU   B OE1 1 
ATOM   23207 O  OE2 . GLU   B 1 1152 ? 56.43400   81.61100  8.58100   1.000 77.97041  -1 1150 GLU   B OE2 1 
ATOM   23208 N  N   . ARG   B 1 1153 ? 58.10900   80.77100  1.62300   1.000 52.13558  ?  1151 ARG   B N   1 
ATOM   23209 C  CA  . ARG   B 1 1153 ? 58.72100   81.31100  0.41900   1.000 53.69968  ?  1151 ARG   B CA  1 
ATOM   23210 C  C   . ARG   B 1 1153 ? 57.63400   81.67000  -0.58100  1.000 56.71141  ?  1151 ARG   B C   1 
ATOM   23211 O  O   . ARG   B 1 1153 ? 56.68200   80.90800  -0.77000  1.000 57.19492  ?  1151 ARG   B O   1 
ATOM   23212 C  CB  . ARG   B 1 1153 ? 59.69500   80.31000  -0.22000  1.000 44.58931  ?  1151 ARG   B CB  1 
ATOM   23213 C  CG  . ARG   B 1 1153 ? 60.79400   79.80400  0.70200   1.000 53.31562  ?  1151 ARG   B CG  1 
ATOM   23214 C  CD  . ARG   B 1 1153 ? 61.85700   80.86000  0.93300   1.000 49.24900  ?  1151 ARG   B CD  1 
ATOM   23215 N  NE  . ARG   B 1 1153 ? 62.28200   80.91000  2.32700   1.000 63.64806  ?  1151 ARG   B NE  1 
ATOM   23216 C  CZ  . ARG   B 1 1153 ? 63.49500   80.58800  2.75400   1.000 70.19483  ?  1151 ARG   B CZ  1 
ATOM   23217 N  NH1 . ARG   B 1 1153 ? 64.43500   80.17600  1.91800   1.000 55.57935  ?  1151 ARG   B NH1 1 
ATOM   23218 N  NH2 . ARG   B 1 1153 ? 63.77300   80.68200  4.05100   1.000 77.46813  ?  1151 ARG   B NH2 1 
ATOM   23219 N  N   . GLU   B 1 1154 ? 57.78600   82.83700  -1.21200  1.000 58.03267  ?  1152 GLU   B N   1 
ATOM   23220 C  CA  . GLU   B 1 1154 ? 56.93000   83.26500  -2.32100  1.000 62.77588  ?  1152 GLU   B CA  1 
ATOM   23221 C  C   . GLU   B 1 1154 ? 55.46100   83.32500  -1.90800  1.000 64.00591  ?  1152 GLU   B C   1 
ATOM   23222 O  O   . GLU   B 1 1154 ? 54.57400   82.80600  -2.59000  1.000 57.14959  ?  1152 GLU   B O   1 
ATOM   23223 C  CB  . GLU   B 1 1154 ? 57.11900   82.35700  -3.54000  1.000 57.76118  ?  1152 GLU   B CB  1 
ATOM   23224 C  CG  . GLU   B 1 1154 ? 58.52600   82.37800  -4.12600  1.000 70.87296  ?  1152 GLU   B CG  1 
ATOM   23225 C  CD  . GLU   B 1 1154 ? 58.63300   83.24900  -5.36700  1.000 97.60146  ?  1152 GLU   B CD  1 
ATOM   23226 O  OE1 . GLU   B 1 1154 ? 57.61800   83.40100  -6.07800  1.000 94.08701  ?  1152 GLU   B OE1 1 
ATOM   23227 O  OE2 . GLU   B 1 1154 ? 59.73400   83.77800  -5.63400  1.000 105.12053 -1 1152 GLU   B OE2 1 
ATOM   23228 N  N   . ASN   B 1 1155 ? 55.20600   83.96800  -0.77100  1.000 58.67323  ?  1153 ASN   B N   1 
ATOM   23229 C  CA  . ASN   B 1 1155 ? 53.86700   84.14100  -0.21700  1.000 52.23573  ?  1153 ASN   B CA  1 
ATOM   23230 C  C   . ASN   B 1 1155 ? 53.15200   82.82000  0.04700   1.000 46.88354  ?  1153 ASN   B C   1 
ATOM   23231 O  O   . ASN   B 1 1155 ? 51.93900   82.81700  0.27000   1.000 56.55382  ?  1153 ASN   B O   1 
ATOM   23232 C  CB  . ASN   B 1 1155 ? 52.99800   85.02400  -1.12300  1.000 44.91566  ?  1153 ASN   B CB  1 
ATOM   23233 C  CG  . ASN   B 1 1155 ? 53.42500   86.47300  -1.09900  1.000 62.41745  ?  1153 ASN   B CG  1 
ATOM   23234 O  OD1 . ASN   B 1 1155 ? 53.84200   86.98700  -0.06200  1.000 85.93255  ?  1153 ASN   B OD1 1 
ATOM   23235 N  ND2 . ASN   B 1 1155 ? 53.32600   87.14100  -2.24200  1.000 52.93947  ?  1153 ASN   B ND2 1 
ATOM   23236 N  N   . GLY   B 1 1156 ? 53.86600   81.69700  0.02800   1.000 57.88954  ?  1154 GLY   B N   1 
ATOM   23237 C  CA  . GLY   B 1 1156 ? 53.25800   80.41400  0.31900   1.000 49.17319  ?  1154 GLY   B CA  1 
ATOM   23238 C  C   . GLY   B 1 1156 ? 54.08600   79.60700  1.29600   1.000 45.46842  ?  1154 GLY   B C   1 
ATOM   23239 O  O   . GLY   B 1 1156 ? 54.84100   80.17100  2.09400   1.000 51.57129  ?  1154 GLY   B O   1 
ATOM   23240 N  N   . LEU   B 1 1157 ? 53.96300   78.28300  1.24700   1.000 36.25652  ?  1155 LEU   B N   1 
ATOM   23241 C  CA  . LEU   B 1 1157 ? 54.72400   77.40600  2.12600   1.000 36.92370  ?  1155 LEU   B CA  1 
ATOM   23242 C  C   . LEU   B 1 1157 ? 55.31400   76.27100  1.30600   1.000 38.15820  ?  1155 LEU   B C   1 
ATOM   23243 O  O   . LEU   B 1 1157 ? 54.59800   75.62000  0.53800   1.000 39.54291  ?  1155 LEU   B O   1 
ATOM   23244 C  CB  . LEU   B 1 1157 ? 53.84800   76.84200  3.24900   1.000 43.53670  ?  1155 LEU   B CB  1 
ATOM   23245 C  CG  . LEU   B 1 1157 ? 53.37200   77.81400  4.32700   1.000 41.04368  ?  1155 LEU   B CG  1 
ATOM   23246 C  CD1 . LEU   B 1 1157 ? 52.39600   77.12100  5.25200   1.000 42.30958  ?  1155 LEU   B CD1 1 
ATOM   23247 C  CD2 . LEU   B 1 1157 ? 54.55300   78.34700  5.10600   1.000 45.49640  ?  1155 LEU   B CD2 1 
ATOM   23248 N  N   . ASN   B 1 1158 ? 56.61300   76.03700  1.46300   1.000 41.30989  ?  1156 ASN   B N   1 
ATOM   23249 C  CA  . ASN   B 1 1158 ? 57.30900   74.94700  0.78200   1.000 41.45846  ?  1156 ASN   B CA  1 
ATOM   23250 C  C   . ASN   B 1 1158 ? 57.62200   73.89000  1.83500   1.000 40.26233  ?  1156 ASN   B C   1 
ATOM   23251 O  O   . ASN   B 1 1158 ? 58.63400   73.96900  2.53200   1.000 38.64966  ?  1156 ASN   B O   1 
ATOM   23252 C  CB  . ASN   B 1 1158 ? 58.57700   75.43000  0.08400   1.000 33.66302  ?  1156 ASN   B CB  1 
ATOM   23253 C  CG  . ASN   B 1 1158 ? 58.30200   76.49700  -0.95100  1.000 39.79274  ?  1156 ASN   B CG  1 
ATOM   23254 O  OD1 . ASN   B 1 1158 ? 57.15400   76.88300  -1.17300  1.000 56.89981  ?  1156 ASN   B OD1 1 
ATOM   23255 N  ND2 . ASN   B 1 1158 ? 59.35800   76.99200  -1.58400  1.000 58.45974  ?  1156 ASN   B ND2 1 
ATOM   23256 N  N   . ILE   B 1 1159 ? 56.73100   72.91200  1.96000   1.000 41.40696  ?  1157 ILE   B N   1 
ATOM   23257 C  CA  . ILE   B 1 1159 ? 56.93500   71.80400  2.88600   1.000 36.90730  ?  1157 ILE   B CA  1 
ATOM   23258 C  C   . ILE   B 1 1159 ? 57.86000   70.79200  2.22100   1.000 38.06619  ?  1157 ILE   B C   1 
ATOM   23259 O  O   . ILE   B 1 1159 ? 57.56600   70.29200  1.13000   1.000 40.40240  ?  1157 ILE   B O   1 
ATOM   23260 C  CB  . ILE   B 1 1159 ? 55.60000   71.15900  3.28500   1.000 39.48123  ?  1157 ILE   B CB  1 
ATOM   23261 C  CG1 . ILE   B 1 1159 ? 54.47900   72.20700  3.32300   1.000 36.10911  ?  1157 ILE   B CG1 1 
ATOM   23262 C  CG2 . ILE   B 1 1159 ? 55.74400   70.42800  4.61300   1.000 35.44700  ?  1157 ILE   B CG2 1 
ATOM   23263 C  CD1 . ILE   B 1 1159 ? 53.93700   72.50700  4.70600   1.000 46.62230  ?  1157 ILE   B CD1 1 
ATOM   23264 N  N   . VAL   B 1 1160 ? 58.98000   70.49200  2.87500   1.000 29.35441  ?  1158 VAL   B N   1 
ATOM   23265 C  CA  . VAL   B 1 1160 ? 60.01000   69.61000  2.33800   1.000 30.93690  ?  1158 VAL   B CA  1 
ATOM   23266 C  C   . VAL   B 1 1160 ? 60.00700   68.31700  3.14000   1.000 41.12021  ?  1158 VAL   B C   1 
ATOM   23267 O  O   . VAL   B 1 1160 ? 60.08700   68.34400  4.37400   1.000 46.09991  ?  1158 VAL   B O   1 
ATOM   23268 C  CB  . VAL   B 1 1160 ? 61.39800   70.27800  2.37700   1.000 45.53274  ?  1158 VAL   B CB  1 
ATOM   23269 C  CG1 . VAL   B 1 1160 ? 62.49600   69.27600  2.02600   1.000 16.48705  ?  1158 VAL   B CG1 1 
ATOM   23270 C  CG2 . VAL   B 1 1160 ? 61.43900   71.46800  1.43600   1.000 39.46515  ?  1158 VAL   B CG2 1 
ATOM   23271 N  N   . PHE   B 1 1161 ? 59.91700   67.18900  2.43900   1.000 45.33426  ?  1159 PHE   B N   1 
ATOM   23272 C  CA  . PHE   B 1 1161 ? 59.93700   65.86300  3.05000   1.000 33.79914  ?  1159 PHE   B CA  1 
ATOM   23273 C  C   . PHE   B 1 1161 ? 61.26800   65.20100  2.71500   1.000 37.53619  ?  1159 PHE   B C   1 
ATOM   23274 O  O   . PHE   B 1 1161 ? 61.49800   64.80300  1.56800   1.000 39.87056  ?  1159 PHE   B O   1 
ATOM   23275 C  CB  . PHE   B 1 1161 ? 58.76900   65.01200  2.55800   1.000 23.83593  ?  1159 PHE   B CB  1 
ATOM   23276 C  CG  . PHE   B 1 1161 ? 57.42300   65.49700  3.01400   1.000 31.61924  ?  1159 PHE   B CG  1 
ATOM   23277 C  CD1 . PHE   B 1 1161 ? 56.85300   66.63300  2.46100   1.000 35.07943  ?  1159 PHE   B CD1 1 
ATOM   23278 C  CD2 . PHE   B 1 1161 ? 56.71900   64.80500  3.98500   1.000 28.04421  ?  1159 PHE   B CD2 1 
ATOM   23279 C  CE1 . PHE   B 1 1161 ? 55.61100   67.07600  2.87600   1.000 39.82809  ?  1159 PHE   B CE1 1 
ATOM   23280 C  CE2 . PHE   B 1 1161 ? 55.47600   65.24100  4.40300   1.000 32.09456  ?  1159 PHE   B CE2 1 
ATOM   23281 C  CZ  . PHE   B 1 1161 ? 54.92100   66.37800  3.84800   1.000 38.59722  ?  1159 PHE   B CZ  1 
ATOM   23282 N  N   . GLU   B 1 1162 ? 62.14000   65.08900  3.71000   1.000 34.41256  ?  1160 GLU   B N   1 
ATOM   23283 C  CA  . GLU   B 1 1162 ? 63.41400   64.39400  3.57700   1.000 36.83820  ?  1160 GLU   B CA  1 
ATOM   23284 C  C   . GLU   B 1 1162 ? 63.27100   63.01900  4.21700   1.000 39.18237  ?  1160 GLU   B C   1 
ATOM   23285 O  O   . GLU   B 1 1162 ? 62.92400   62.92000  5.39900   1.000 41.99441  ?  1160 GLU   B O   1 
ATOM   23286 C  CB  . GLU   B 1 1162 ? 64.53300   65.19300  4.24300   1.000 33.94945  ?  1160 GLU   B CB  1 
ATOM   23287 C  CG  . GLU   B 1 1162 ? 65.92100   64.63100  4.04000   1.000 40.27811  ?  1160 GLU   B CG  1 
ATOM   23288 C  CD  . GLU   B 1 1162 ? 66.96700   65.39600  4.82600   1.000 53.90891  ?  1160 GLU   B CD  1 
ATOM   23289 O  OE1 . GLU   B 1 1162 ? 67.11400   65.13900  6.04200   1.000 53.06119  ?  1160 GLU   B OE1 1 
ATOM   23290 O  OE2 . GLU   B 1 1162 ? 67.63100   66.26800  4.22900   1.000 68.38875  -1 1160 GLU   B OE2 1 
ATOM   23291 N  N   . TYR   B 1 1163 ? 63.52700   61.96300  3.44400   1.000 31.42724  ?  1161 TYR   B N   1 
ATOM   23292 C  CA  . TYR   B 1 1163 ? 63.21600   60.61500  3.90100   1.000 39.80404  ?  1161 TYR   B CA  1 
ATOM   23293 C  C   . TYR   B 1 1163 ? 64.35500   59.65700  3.58800   1.000 41.18243  ?  1161 TYR   B C   1 
ATOM   23294 O  O   . TYR   B 1 1163 ? 65.03900   59.78700  2.57000   1.000 40.39962  ?  1161 TYR   B O   1 
ATOM   23295 C  CB  . TYR   B 1 1163 ? 61.91500   60.09300  3.27100   1.000 33.62348  ?  1161 TYR   B CB  1 
ATOM   23296 C  CG  . TYR   B 1 1163 ? 61.92500   60.03200  1.75800   1.000 44.70833  ?  1161 TYR   B CG  1 
ATOM   23297 C  CD1 . TYR   B 1 1163 ? 61.64600   61.16000  0.99700   1.000 43.54131  ?  1161 TYR   B CD1 1 
ATOM   23298 C  CD2 . TYR   B 1 1163 ? 62.19700   58.84300  1.09100   1.000 36.74718  ?  1161 TYR   B CD2 1 
ATOM   23299 C  CE1 . TYR   B 1 1163 ? 61.64700   61.10900  -0.38400  1.000 32.19496  ?  1161 TYR   B CE1 1 
ATOM   23300 C  CE2 . TYR   B 1 1163 ? 62.20000   58.78300  -0.29000  1.000 35.83582  ?  1161 TYR   B CE2 1 
ATOM   23301 C  CZ  . TYR   B 1 1163 ? 61.92500   59.92100  -1.02300  1.000 32.09336  ?  1161 TYR   B CZ  1 
ATOM   23302 O  OH  . TYR   B 1 1163 ? 61.92600   59.87200  -2.39900  1.000 38.78729  ?  1161 TYR   B OH  1 
ATOM   23303 N  N   . ASN   B 1 1164 ? 64.54100   58.68800  4.48400   1.000 41.43743  ?  1162 ASN   B N   1 
ATOM   23304 C  CA  . ASN   B 1 1164 ? 65.50900   57.61800  4.27500   1.000 45.39775  ?  1162 ASN   B CA  1 
ATOM   23305 C  C   . ASN   B 1 1164 ? 64.99900   56.67000  3.19700   1.000 47.88584  ?  1162 ASN   B C   1 
ATOM   23306 O  O   . ASN   B 1 1164 ? 63.90600   56.10900  3.32200   1.000 53.03158  ?  1162 ASN   B O   1 
ATOM   23307 C  CB  . ASN   B 1 1164 ? 65.74600   56.86600  5.58100   1.000 48.87282  ?  1162 ASN   B CB  1 
ATOM   23308 C  CG  . ASN   B 1 1164 ? 66.74700   55.74300  5.43400   1.000 50.53026  ?  1162 ASN   B CG  1 
ATOM   23309 O  OD1 . ASN   B 1 1164 ? 66.37200   54.57900  5.30300   1.000 53.41815  ?  1162 ASN   B OD1 1 
ATOM   23310 N  ND2 . ASN   B 1 1164 ? 68.03000   56.08400  5.46400   1.000 58.22403  ?  1162 ASN   B ND2 1 
ATOM   23311 N  N   . THR   B 1 1165 ? 65.79100   56.48500  2.13800   1.000 40.52091  ?  1163 THR   B N   1 
ATOM   23312 C  CA  . THR   B 1 1165 ? 65.31800   55.70700  0.99900   1.000 43.53037  ?  1163 THR   B CA  1 
ATOM   23313 C  C   . THR   B 1 1165 ? 65.25200   54.21600  1.28900   1.000 40.55491  ?  1163 THR   B C   1 
ATOM   23314 O  O   . THR   B 1 1165 ? 64.60900   53.48200  0.53200   1.000 42.37467  ?  1163 THR   B O   1 
ATOM   23315 C  CB  . THR   B 1 1165 ? 66.20900   55.94800  -0.21500  1.000 39.48224  ?  1163 THR   B CB  1 
ATOM   23316 O  OG1 . THR   B 1 1165 ? 67.57600   55.71700  0.14600   1.000 43.53946  ?  1163 THR   B OG1 1 
ATOM   23317 C  CG2 . THR   B 1 1165 ? 66.03800   57.37200  -0.71300  1.000 25.30346  ?  1163 THR   B CG2 1 
ATOM   23318 N  N   . HIS   B 1 1166 ? 65.90800   53.74900  2.35000   1.000 39.44799  ?  1164 HIS   B N   1 
ATOM   23319 C  CA  . HIS   B 1 1166 ? 65.80300   52.34600  2.72200   1.000 39.52324  ?  1164 HIS   B CA  1 
ATOM   23320 C  C   . HIS   B 1 1166 ? 64.50300   52.04100  3.45100   1.000 45.11642  ?  1164 HIS   B C   1 
ATOM   23321 O  O   . HIS   B 1 1166 ? 64.13500   50.86800  3.57300   1.000 47.26982  ?  1164 HIS   B O   1 
ATOM   23322 C  CB  . HIS   B 1 1166 ? 66.99600   51.93300  3.58800   1.000 36.82886  ?  1164 HIS   B CB  1 
ATOM   23323 C  CG  . HIS   B 1 1166 ? 68.31700   52.03900  2.89100   1.000 50.05207  ?  1164 HIS   B CG  1 
ATOM   23324 N  ND1 . HIS   B 1 1166 ? 69.49900   51.62700  3.46900   1.000 59.10877  ?  1164 HIS   B ND1 1 
ATOM   23325 C  CD2 . HIS   B 1 1166 ? 68.64400   52.51200  1.66500   1.000 58.74018  ?  1164 HIS   B CD2 1 
ATOM   23326 C  CE1 . HIS   B 1 1166 ? 70.49600   51.84300  2.63000   1.000 57.24237  ?  1164 HIS   B CE1 1 
ATOM   23327 N  NE2 . HIS   B 1 1166 ? 70.00500   52.37900  1.52800   1.000 60.64513  ?  1164 HIS   B NE2 1 
ATOM   23328 N  N   . LEU   B 1 1167 ? 63.79700   53.06900  3.92600   1.000 45.58710  ?  1165 LEU   B N   1 
ATOM   23329 C  CA  . LEU   B 1 1167 ? 62.53800   52.88800  4.63100   1.000 39.87517  ?  1165 LEU   B CA  1 
ATOM   23330 C  C   . LEU   B 1 1167 ? 61.32100   53.32400  3.83000   1.000 42.28331  ?  1165 LEU   B C   1 
ATOM   23331 O  O   . LEU   B 1 1167 ? 60.21700   52.84700  4.11000   1.000 51.56905  ?  1165 LEU   B O   1 
ATOM   23332 C  CB  . LEU   B 1 1167 ? 62.55700   53.65900  5.96000   1.000 42.17903  ?  1165 LEU   B CB  1 
ATOM   23333 C  CG  . LEU   B 1 1167 ? 63.66400   53.28700  6.94900   1.000 44.67285  ?  1165 LEU   B CG  1 
ATOM   23334 C  CD1 . LEU   B 1 1167 ? 63.86600   54.39800  7.96800   1.000 45.81305  ?  1165 LEU   B CD1 1 
ATOM   23335 C  CD2 . LEU   B 1 1167 ? 63.34800   51.97100  7.64200   1.000 50.08418  ?  1165 LEU   B CD2 1 
ATOM   23336 N  N   . PHE   B 1 1168 ? 61.49100   54.21100  2.85300   1.000 48.13609  ?  1166 PHE   B N   1 
ATOM   23337 C  CA  . PHE   B 1 1168 ? 60.38800   54.67800  2.02300   1.000 51.38958  ?  1166 PHE   B CA  1 
ATOM   23338 C  C   . PHE   B 1 1168 ? 60.84200   54.73000  0.57400   1.000 44.54708  ?  1166 PHE   B C   1 
ATOM   23339 O  O   . PHE   B 1 1168 ? 61.94100   55.21400  0.28600   1.000 47.94197  ?  1166 PHE   B O   1 
ATOM   23340 C  CB  . PHE   B 1 1168 ? 59.90300   56.07100  2.44700   1.000 40.88754  ?  1166 PHE   B CB  1 
ATOM   23341 C  CG  . PHE   B 1 1168 ? 59.67100   56.22100  3.92000   1.000 37.00387  ?  1166 PHE   B CG  1 
ATOM   23342 C  CD1 . PHE   B 1 1168 ? 60.71100   56.56000  4.77200   1.000 36.20881  ?  1166 PHE   B CD1 1 
ATOM   23343 C  CD2 . PHE   B 1 1168 ? 58.40500   56.05200  4.44900   1.000 46.24684  ?  1166 PHE   B CD2 1 
ATOM   23344 C  CE1 . PHE   B 1 1168 ? 60.49100   56.70800  6.12800   1.000 40.07099  ?  1166 PHE   B CE1 1 
ATOM   23345 C  CE2 . PHE   B 1 1168 ? 58.18000   56.20000  5.80100   1.000 41.85602  ?  1166 PHE   B CE2 1 
ATOM   23346 C  CZ  . PHE   B 1 1168 ? 59.22200   56.52900  6.64200   1.000 38.28955  ?  1166 PHE   B CZ  1 
ATOM   23347 N  N   . ASP   B 1 1169 ? 60.00000   54.24300  -0.33200  1.000 41.54628  ?  1167 ASP   B N   1 
ATOM   23348 C  CA  . ASP   B 1 1169 ? 60.21200   54.44000  -1.75500  1.000 48.81462  ?  1167 ASP   B CA  1 
ATOM   23349 C  C   . ASP   B 1 1169 ? 59.35800   55.61200  -2.23100  1.000 48.08209  ?  1167 ASP   B C   1 
ATOM   23350 O  O   . ASP   B 1 1169 ? 58.60100   56.21400  -1.46500  1.000 48.38989  ?  1167 ASP   B O   1 
ATOM   23351 C  CB  . ASP   B 1 1169 ? 59.90800   53.16200  -2.54100  1.000 61.15784  ?  1167 ASP   B CB  1 
ATOM   23352 C  CG  . ASP   B 1 1169 ? 58.46600   52.72000  -2.41000  1.000 60.66618  ?  1167 ASP   B CG  1 
ATOM   23353 O  OD1 . ASP   B 1 1169 ? 57.57000   53.40300  -2.95400  1.000 71.04493  ?  1167 ASP   B OD1 1 
ATOM   23354 O  OD2 . ASP   B 1 1169 ? 58.23100   51.68000  -1.76200  1.000 61.79331  -1 1167 ASP   B OD2 1 
ATOM   23355 N  N   . GLU   B 1 1170 ? 59.48200   55.93300  -3.52100  1.000 50.78685  ?  1168 GLU   B N   1 
ATOM   23356 C  CA  . GLU   B 1 1170 ? 58.83800   57.13200  -4.04800  1.000 52.65847  ?  1168 GLU   B CA  1 
ATOM   23357 C  C   . GLU   B 1 1170 ? 57.32300   57.06000  -3.90300  1.000 52.55716  ?  1168 GLU   B C   1 
ATOM   23358 O  O   . GLU   B 1 1170 ? 56.67200   58.06900  -3.60500  1.000 50.30880  ?  1168 GLU   B O   1 
ATOM   23359 C  CB  . GLU   B 1 1170 ? 59.23500   57.33900  -5.51000  1.000 52.36277  ?  1168 GLU   B CB  1 
ATOM   23360 N  N   . GLY   B 1 1171 ? 56.74500   55.87300  -4.09100  1.000 50.71307  ?  1169 GLY   B N   1 
ATOM   23361 C  CA  . GLY   B 1 1171 ? 55.30200   55.74300  -3.98500  1.000 44.26501  ?  1169 GLY   B CA  1 
ATOM   23362 C  C   . GLY   B 1 1171 ? 54.80200   55.88200  -2.56100  1.000 42.86429  ?  1169 GLY   B C   1 
ATOM   23363 O  O   . GLY   B 1 1171 ? 53.73300   56.45100  -2.32200  1.000 47.82336  ?  1169 GLY   B O   1 
ATOM   23364 N  N   . MET   B 1 1172 ? 55.56300   55.36500  -1.59700  1.000 45.62716  ?  1170 MET   B N   1 
ATOM   23365 C  CA  . MET   B 1 1172 ? 55.17600   55.48900  -0.19700  1.000 39.71377  ?  1170 MET   B CA  1 
ATOM   23366 C  C   . MET   B 1 1172 ? 55.17100   56.94800  0.23500   1.000 44.49693  ?  1170 MET   B C   1 
ATOM   23367 O  O   . MET   B 1 1172 ? 54.16100   57.46200  0.73100   1.000 51.50001  ?  1170 MET   B O   1 
ATOM   23368 C  CB  . MET   B 1 1172 ? 56.12300   54.67200  0.67800   1.000 36.46009  ?  1170 MET   B CB  1 
ATOM   23369 C  CG  . MET   B 1 1172 ? 56.34300   53.26300  0.17800   1.000 40.43163  ?  1170 MET   B CG  1 
ATOM   23370 S  SD  . MET   B 1 1172 ? 57.12900   52.21600  1.40800   1.000 48.49984  ?  1170 MET   B SD  1 
ATOM   23371 C  CE  . MET   B 1 1172 ? 56.32300   52.80500  2.88400   1.000 59.26346  ?  1170 MET   B CE  1 
ATOM   23372 N  N   . ILE   B 1 1173 ? 56.29800   57.63800  0.03900   1.000 41.65048  ?  1171 ILE   B N   1 
ATOM   23373 C  CA  . ILE   B 1 1173 ? 56.40900   59.02300  0.48400   1.000 46.09917  ?  1171 ILE   B CA  1 
ATOM   23374 C  C   . ILE   B 1 1173 ? 55.39100   59.90400  -0.23000  1.000 43.98543  ?  1171 ILE   B C   1 
ATOM   23375 O  O   . ILE   B 1 1173 ? 54.93300   60.91100  0.32600   1.000 51.66334  ?  1171 ILE   B O   1 
ATOM   23376 C  CB  . ILE   B 1 1173 ? 57.85600   59.52800  0.29200   1.000 34.03808  ?  1171 ILE   B CB  1 
ATOM   23377 C  CG1 . ILE   B 1 1173 ? 58.23200   60.51900  1.39500   1.000 43.14677  ?  1171 ILE   B CG1 1 
ATOM   23378 C  CG2 . ILE   B 1 1173 ? 58.04700   60.15600  -1.07600  1.000 49.42214  ?  1171 ILE   B CG2 1 
ATOM   23379 C  CD1 . ILE   B 1 1173 ? 58.39400   59.88400  2.75400   1.000 46.66576  ?  1171 ILE   B CD1 1 
ATOM   23380 N  N   . LEU   B 1 1174 ? 54.99400   59.53100  -1.44900  1.000 32.73202  ?  1172 LEU   B N   1 
ATOM   23381 C  CA  . LEU   B 1 1174 ? 53.98900   60.31300  -2.16300  1.000 37.67038  ?  1172 LEU   B CA  1 
ATOM   23382 C  C   . LEU   B 1 1174 ? 52.61000   60.12600  -1.54500  1.000 43.86221  ?  1172 LEU   B C   1 
ATOM   23383 O  O   . LEU   B 1 1174 ? 51.82500   61.07800  -1.46500  1.000 43.90233  ?  1172 LEU   B O   1 
ATOM   23384 C  CB  . LEU   B 1 1174 ? 53.97500   59.92600  -3.63900  1.000 34.59921  ?  1172 LEU   B CB  1 
ATOM   23385 C  CG  . LEU   B 1 1174 ? 54.98000   60.66600  -4.52300  1.000 47.65431  ?  1172 LEU   B CG  1 
ATOM   23386 C  CD1 . LEU   B 1 1174 ? 55.02200   60.05500  -5.91000  1.000 49.37636  ?  1172 LEU   B CD1 1 
ATOM   23387 C  CD2 . LEU   B 1 1174 ? 54.63400   62.14200  -4.60000  1.000 52.05460  ?  1172 LEU   B CD2 1 
ATOM   23388 N  N   . ARG   B 1 1175 ? 52.29500   58.90100  -1.11600  1.000 33.79775  ?  1173 ARG   B N   1 
ATOM   23389 C  CA  . ARG   B 1 1175 ? 51.06200   58.67100  -0.37300  1.000 38.07739  ?  1173 ARG   B CA  1 
ATOM   23390 C  C   . ARG   B 1 1175 ? 51.03500   59.51200  0.89500   1.000 48.30425  ?  1173 ARG   B C   1 
ATOM   23391 O  O   . ARG   B 1 1175 ? 50.03500   60.17500  1.19600   1.000 50.90514  ?  1173 ARG   B O   1 
ATOM   23392 C  CB  . ARG   B 1 1175 ? 50.92600   57.18800  -0.03000  1.000 46.62579  ?  1173 ARG   B CB  1 
ATOM   23393 C  CG  . ARG   B 1 1175 ? 50.09700   56.37900  -1.00600  1.000 43.74320  ?  1173 ARG   B CG  1 
ATOM   23394 C  CD  . ARG   B 1 1175 ? 49.61000   55.10100  -0.34500  1.000 55.05704  ?  1173 ARG   B CD  1 
ATOM   23395 N  NE  . ARG   B 1 1175 ? 50.69800   54.35700  0.27900   1.000 52.76965  ?  1173 ARG   B NE  1 
ATOM   23396 C  CZ  . ARG   B 1 1175 ? 51.53300   53.56200  -0.37700  1.000 56.07452  ?  1173 ARG   B CZ  1 
ATOM   23397 N  NH1 . ARG   B 1 1175 ? 51.44100   53.39200  -1.68600  1.000 51.94734  ?  1173 ARG   B NH1 1 
ATOM   23398 N  NH2 . ARG   B 1 1175 ? 52.48100   52.91900  0.29900   1.000 66.60204  ?  1173 ARG   B NH2 1 
ATOM   23399 N  N   . MET   B 1 1176 ? 52.14100   59.51100  1.64400   1.000 41.31406  ?  1174 MET   B N   1 
ATOM   23400 C  CA  . MET   B 1 1176 ? 52.18300   60.23600  2.90900   1.000 44.03292  ?  1174 MET   B CA  1 
ATOM   23401 C  C   . MET   B 1 1176 ? 52.03300   61.73600  2.70000   1.000 45.74600  ?  1174 MET   B C   1 
ATOM   23402 O  O   . MET   B 1 1176 ? 51.36000   62.41400  3.48600   1.000 55.41361  ?  1174 MET   B O   1 
ATOM   23403 C  CB  . MET   B 1 1176 ? 53.48300   59.92200  3.64400   1.000 40.91186  ?  1174 MET   B CB  1 
ATOM   23404 C  CG  . MET   B 1 1176 ? 53.83400   58.45400  3.62400   1.000 43.13898  ?  1174 MET   B CG  1 
ATOM   23405 S  SD  . MET   B 1 1176 ? 55.44200   58.10900  4.34800   1.000 40.96948  ?  1174 MET   B SD  1 
ATOM   23406 C  CE  . MET   B 1 1176 ? 55.56900   59.43500  5.54500   1.000 43.22879  ?  1174 MET   B CE  1 
ATOM   23407 N  N   . VAL   B 1 1177 ? 52.65400   62.27600  1.65000   1.000 35.21509  ?  1175 VAL   B N   1 
ATOM   23408 C  CA  . VAL   B 1 1177 ? 52.52300   63.70400  1.36800   1.000 42.87620  ?  1175 VAL   B CA  1 
ATOM   23409 C  C   . VAL   B 1 1177 ? 51.07400   64.04800  1.04800   1.000 39.68227  ?  1175 VAL   B C   1 
ATOM   23410 O  O   . VAL   B 1 1177 ? 50.52500   65.03500  1.55300   1.000 48.59257  ?  1175 VAL   B O   1 
ATOM   23411 C  CB  . VAL   B 1 1177 ? 53.47000   64.11800  0.22700   1.000 36.86860  ?  1175 VAL   B CB  1 
ATOM   23412 C  CG1 . VAL   B 1 1177 ? 53.10500   65.50500  -0.29100  1.000 24.97440  ?  1175 VAL   B CG1 1 
ATOM   23413 C  CG2 . VAL   B 1 1177 ? 54.91800   64.08300  0.70500   1.000 28.39198  ?  1175 VAL   B CG2 1 
ATOM   23414 N  N   . ALA   B 1 1178 ? 50.43000   63.23000  0.21100   1.000 48.39080  ?  1176 ALA   B N   1 
ATOM   23415 C  CA  . ALA   B 1 1178 ? 49.03200   63.46700  -0.13000  1.000 47.79774  ?  1176 ALA   B CA  1 
ATOM   23416 C  C   . ALA   B 1 1178 ? 48.14200   63.38000  1.10300   1.000 48.44520  ?  1176 ALA   B C   1 
ATOM   23417 O  O   . ALA   B 1 1178 ? 47.17200   64.13600  1.23300   1.000 56.49248  ?  1176 ALA   B O   1 
ATOM   23418 C  CB  . ALA   B 1 1178 ? 48.57500   62.47200  -1.19500  1.000 35.28632  ?  1176 ALA   B CB  1 
ATOM   23419 N  N   . GLN   B 1 1179 ? 48.45400   62.46100  2.01900   1.000 44.08498  ?  1177 GLN   B N   1 
ATOM   23420 C  CA  . GLN   B 1 1179 ? 47.69000   62.37200  3.25800   1.000 47.46615  ?  1177 GLN   B CA  1 
ATOM   23421 C  C   . GLN   B 1 1179 ? 47.88900   63.61800  4.11200   1.000 47.95677  ?  1177 GLN   B C   1 
ATOM   23422 O  O   . GLN   B 1 1179 ? 46.94000   64.11000  4.73200   1.000 52.57278  ?  1177 GLN   B O   1 
ATOM   23423 C  CB  . GLN   B 1 1179 ? 48.08900   61.11300  4.03100   1.000 52.03315  ?  1177 GLN   B CB  1 
ATOM   23424 C  CG  . GLN   B 1 1179 ? 47.76000   59.80500  3.31300   1.000 43.95436  ?  1177 GLN   B CG  1 
ATOM   23425 C  CD  . GLN   B 1 1179 ? 48.52200   58.61200  3.87000   1.000 49.94452  ?  1177 GLN   B CD  1 
ATOM   23426 O  OE1 . GLN   B 1 1179 ? 49.19900   58.71100  4.89400   1.000 52.44608  ?  1177 GLN   B OE1 1 
ATOM   23427 N  NE2 . GLN   B 1 1179 ? 48.41500   57.47600  3.19100   1.000 53.02738  ?  1177 GLN   B NE2 1 
ATOM   23428 N  N   . PHE   B 1 1180 ? 49.11500   64.14500  4.14800   1.000 55.30825  ?  1178 PHE   B N   1 
ATOM   23429 C  CA  . PHE   B 1 1180 ? 49.38400   65.36100  4.90800   1.000 48.29768  ?  1178 PHE   B CA  1 
ATOM   23430 C  C   . PHE   B 1 1180 ? 48.56200   66.53100  4.38200   1.000 47.87811  ?  1178 PHE   B C   1 
ATOM   23431 O  O   . PHE   B 1 1180 ? 47.96000   67.28100  5.15800   1.000 54.05109  ?  1178 PHE   B O   1 
ATOM   23432 C  CB  . PHE   B 1 1180 ? 50.87500   65.68700  4.85800   1.000 33.99080  ?  1178 PHE   B CB  1 
ATOM   23433 C  CG  . PHE   B 1 1180 ? 51.27500   66.83600  5.73500   1.000 48.42773  ?  1178 PHE   B CG  1 
ATOM   23434 C  CD1 . PHE   B 1 1180 ? 51.48500   66.64800  7.09200   1.000 47.15384  ?  1178 PHE   B CD1 1 
ATOM   23435 C  CD2 . PHE   B 1 1180 ? 51.44900   68.10400  5.20300   1.000 47.41060  ?  1178 PHE   B CD2 1 
ATOM   23436 C  CE1 . PHE   B 1 1180 ? 51.85900   67.70400  7.90200   1.000 49.36071  ?  1178 PHE   B CE1 1 
ATOM   23437 C  CE2 . PHE   B 1 1180 ? 51.82300   69.16400  6.00600   1.000 47.12273  ?  1178 PHE   B CE2 1 
ATOM   23438 C  CZ  . PHE   B 1 1180 ? 52.02800   68.96400  7.35800   1.000 51.30277  ?  1178 PHE   B CZ  1 
ATOM   23439 N  N   . GLU   B 1 1181 ? 48.53400   66.70700  3.05800   1.000 44.16515  ?  1179 GLU   B N   1 
ATOM   23440 C  CA  . GLU   B 1 1181 ? 47.72700   67.77300  2.47300   1.000 40.02415  ?  1179 GLU   B CA  1 
ATOM   23441 C  C   . GLU   B 1 1181 ? 46.25200   67.57800  2.79000   1.000 54.50064  ?  1179 GLU   B C   1 
ATOM   23442 O  O   . GLU   B 1 1181 ? 45.55200   68.53600  3.13900   1.000 59.31481  ?  1179 GLU   B O   1 
ATOM   23443 C  CB  . GLU   B 1 1181 ? 47.94200   67.83000  0.96100   1.000 35.01302  ?  1179 GLU   B CB  1 
ATOM   23444 C  CG  . GLU   B 1 1181 ? 46.90800   68.67400  0.22700   1.000 50.85471  ?  1179 GLU   B CG  1 
ATOM   23445 C  CD  . GLU   B 1 1181 ? 47.18600   68.79200  -1.26100  1.000 61.60639  ?  1179 GLU   B CD  1 
ATOM   23446 O  OE1 . GLU   B 1 1181 ? 47.34800   67.74700  -1.92800  1.000 37.73012  ?  1179 GLU   B OE1 1 
ATOM   23447 O  OE2 . GLU   B 1 1181 ? 47.24600   69.93500  -1.76300  1.000 67.02639  -1 1179 GLU   B OE2 1 
ATOM   23448 N  N   . HIS   B 1 1182 ? 45.76600   66.33800  2.67800   1.000 60.39621  ?  1180 HIS   B N   1 
ATOM   23449 C  CA  . HIS   B 1 1182 ? 44.37000   66.04800  2.98300   1.000 42.15008  ?  1180 HIS   B CA  1 
ATOM   23450 C  C   . HIS   B 1 1182 ? 44.02900   66.42000  4.42000   1.000 51.36393  ?  1180 HIS   B C   1 
ATOM   23451 O  O   . HIS   B 1 1182 ? 42.96900   66.99900  4.68400   1.000 53.86459  ?  1180 HIS   B O   1 
ATOM   23452 C  CB  . HIS   B 1 1182 ? 44.08000   64.56900  2.72500   1.000 52.22667  ?  1180 HIS   B CB  1 
ATOM   23453 C  CG  . HIS   B 1 1182 ? 42.62400   64.25200  2.58000   1.000 63.00584  ?  1180 HIS   B CG  1 
ATOM   23454 N  ND1 . HIS   B 1 1182 ? 41.78600   64.96400  1.75000   1.000 69.79653  ?  1180 HIS   B ND1 1 
ATOM   23455 C  CD2 . HIS   B 1 1182 ? 41.85800   63.29800  3.16000   1.000 44.98894  ?  1180 HIS   B CD2 1 
ATOM   23456 C  CE1 . HIS   B 1 1182 ? 40.56600   64.46300  1.82400   1.000 59.31232  ?  1180 HIS   B CE1 1 
ATOM   23457 N  NE2 . HIS   B 1 1182 ? 40.58300   63.45100  2.67300   1.000 60.57916  ?  1180 HIS   B NE2 1 
ATOM   23458 N  N   . LEU   B 1 1183 ? 44.92200   66.10600  5.36400   1.000 48.48251  ?  1181 LEU   B N   1 
ATOM   23459 C  CA  . LEU   B 1 1183 ? 44.69000   66.48400  6.75500   1.000 53.02324  ?  1181 LEU   B CA  1 
ATOM   23460 C  C   . LEU   B 1 1183 ? 44.74600   67.99500  6.93900   1.000 64.91828  ?  1181 LEU   B C   1 
ATOM   23461 O  O   . LEU   B 1 1183 ? 43.92400   68.56700  7.66400   1.000 77.97348  ?  1181 LEU   B O   1 
ATOM   23462 C  CB  . LEU   B 1 1183 ? 45.71100   65.80200  7.66400   1.000 30.32174  ?  1181 LEU   B CB  1 
ATOM   23463 C  CG  . LEU   B 1 1183 ? 45.40500   64.35400  8.04400   1.000 51.99243  ?  1181 LEU   B CG  1 
ATOM   23464 C  CD1 . LEU   B 1 1183 ? 46.19300   63.96600  9.27800   1.000 57.48392  ?  1181 LEU   B CD1 1 
ATOM   23465 C  CD2 . LEU   B 1 1183 ? 43.90800   64.13800  8.26200   1.000 72.51269  ?  1181 LEU   B CD2 1 
ATOM   23466 N  N   . LEU   B 1 1184 ? 45.71100   68.65600  6.29300   1.000 50.51869  ?  1182 LEU   B N   1 
ATOM   23467 C  CA  . LEU   B 1 1184 ? 45.84800   70.10300  6.43100   1.000 48.58049  ?  1182 LEU   B CA  1 
ATOM   23468 C  C   . LEU   B 1 1184 ? 44.61000   70.82500  5.90900   1.000 48.06722  ?  1182 LEU   B C   1 
ATOM   23469 O  O   . LEU   B 1 1184 ? 44.02400   71.66100  6.60700   1.000 53.11295  ?  1182 LEU   B O   1 
ATOM   23470 C  CB  . LEU   B 1 1184 ? 47.10300   70.57800  5.69800   1.000 49.61060  ?  1182 LEU   B CB  1 
ATOM   23471 C  CG  . LEU   B 1 1184 ? 47.56000   72.02100  5.92500   1.000 39.32153  ?  1182 LEU   B CG  1 
ATOM   23472 C  CD1 . LEU   B 1 1184 ? 49.07300   72.08200  6.03400   1.000 38.88016  ?  1182 LEU   B CD1 1 
ATOM   23473 C  CD2 . LEU   B 1 1184 ? 47.07500   72.93200  4.80700   1.000 46.12825  ?  1182 LEU   B CD2 1 
ATOM   23474 N  N   . LEU   B 1 1185 ? 44.19600   70.51200  4.67900   1.000 44.87277  ?  1183 LEU   B N   1 
ATOM   23475 C  CA  . LEU   B 1 1185 ? 43.00600   71.14500  4.11800   1.000 58.54837  ?  1183 LEU   B CA  1 
ATOM   23476 C  C   . LEU   B 1 1185 ? 41.76200   70.81900  4.93400   1.000 72.15756  ?  1183 LEU   B C   1 
ATOM   23477 O  O   . LEU   B 1 1185 ? 40.84000   71.64000  5.01700   1.000 72.03840  ?  1183 LEU   B O   1 
ATOM   23478 C  CB  . LEU   B 1 1185 ? 42.81700   70.71700  2.66200   1.000 45.49902  ?  1183 LEU   B CB  1 
ATOM   23479 C  CG  . LEU   B 1 1185 ? 43.99100   70.98700  1.71800   1.000 49.52493  ?  1183 LEU   B CG  1 
ATOM   23480 C  CD1 . LEU   B 1 1185 ? 43.63000   70.60900  0.28800   1.000 35.34784  ?  1183 LEU   B CD1 1 
ATOM   23481 C  CD2 . LEU   B 1 1185 ? 44.43500   72.44200  1.80100   1.000 56.21119  ?  1183 LEU   B CD2 1 
ATOM   23482 N  N   . GLN   B 1 1186 ? 41.71600   69.63100  5.54200   1.000 68.77231  ?  1184 GLN   B N   1 
ATOM   23483 C  CA  . GLN   B 1 1186 ? 40.60700   69.29300  6.42500   1.000 63.62118  ?  1184 GLN   B CA  1 
ATOM   23484 C  C   . GLN   B 1 1186 ? 40.61700   70.16800  7.67100   1.000 68.30765  ?  1184 GLN   B C   1 
ATOM   23485 O  O   . GLN   B 1 1186 ? 39.58600   70.72800  8.06000   1.000 78.54491  ?  1184 GLN   B O   1 
ATOM   23486 C  CB  . GLN   B 1 1186 ? 40.67400   67.81600  6.81600   1.000 60.94644  ?  1184 GLN   B CB  1 
ATOM   23487 C  CG  . GLN   B 1 1186 ? 40.03800   66.86300  5.82200   1.000 63.67336  ?  1184 GLN   B CG  1 
ATOM   23488 C  CD  . GLN   B 1 1186 ? 40.19000   65.41400  6.24200   1.000 71.40425  ?  1184 GLN   B CD  1 
ATOM   23489 O  OE1 . GLN   B 1 1186 ? 39.32300   64.85700  6.91600   1.000 79.95238  ?  1184 GLN   B OE1 1 
ATOM   23490 N  NE2 . GLN   B 1 1186 ? 41.30200   64.79900  5.85500   1.000 62.87106  ?  1184 GLN   B NE2 1 
ATOM   23491 N  N   . ALA   B 1 1187 ? 41.78300   70.30200  8.30600   1.000 64.99734  ?  1185 ALA   B N   1 
ATOM   23492 C  CA  . ALA   B 1 1187 ? 41.85800   71.00400  9.58200   1.000 70.74605  ?  1185 ALA   B CA  1 
ATOM   23493 C  C   . ALA   B 1 1187 ? 41.56100   72.49100  9.42600   1.000 80.48992  ?  1185 ALA   B C   1 
ATOM   23494 O  O   . ALA   B 1 1187 ? 40.93800   73.09700  10.30600  1.000 90.27843  ?  1185 ALA   B O   1 
ATOM   23495 C  CB  . ALA   B 1 1187 ? 43.23400   70.79200  10.21300  1.000 50.18899  ?  1185 ALA   B CB  1 
ATOM   23496 N  N   . VAL   B 1 1188 ? 41.98600   73.09700  8.31700   1.000 70.42280  ?  1186 VAL   B N   1 
ATOM   23497 C  CA  . VAL   B 1 1188 ? 41.87100   74.54700  8.19400   1.000 74.23790  ?  1186 VAL   B CA  1 
ATOM   23498 C  C   . VAL   B 1 1188 ? 40.43600   74.96400  7.88600   1.000 70.44351  ?  1186 VAL   B C   1 
ATOM   23499 O  O   . VAL   B 1 1188 ? 39.97400   76.01300  8.34900   1.000 80.62730  ?  1186 VAL   B O   1 
ATOM   23500 C  CB  . VAL   B 1 1188 ? 42.87100   75.08200  7.14900   1.000 75.98799  ?  1186 VAL   B CB  1 
ATOM   23501 C  CG1 . VAL   B 1 1188 ? 42.30300   75.01000  5.73600   1.000 61.58785  ?  1186 VAL   B CG1 1 
ATOM   23502 C  CG2 . VAL   B 1 1188 ? 43.26600   76.51200  7.48800   1.000 71.95135  ?  1186 VAL   B CG2 1 
ATOM   23503 N  N   . HIS   B 1 1189 ? 39.70200   74.15900  7.12300   1.000 72.74143  ?  1187 HIS   B N   1 
ATOM   23504 C  CA  . HIS   B 1 1189 ? 38.31300   74.46100  6.81200   1.000 81.27835  ?  1187 HIS   B CA  1 
ATOM   23505 C  C   . HIS   B 1 1189 ? 37.34200   73.79100  7.77200   1.000 78.76910  ?  1187 HIS   B C   1 
ATOM   23506 O  O   . HIS   B 1 1189 ? 36.12900   73.99300  7.64800   1.000 78.67667  ?  1187 HIS   B O   1 
ATOM   23507 C  CB  . HIS   B 1 1189 ? 37.98800   74.04400  5.37400   1.000 87.21086  ?  1187 HIS   B CB  1 
ATOM   23508 C  CG  . HIS   B 1 1189 ? 38.49100   75.00100  4.34000   1.000 90.18597  ?  1187 HIS   B CG  1 
ATOM   23509 N  ND1 . HIS   B 1 1189 ? 39.45200   74.65800  3.41400   1.000 76.81059  ?  1187 HIS   B ND1 1 
ATOM   23510 C  CD2 . HIS   B 1 1189 ? 38.16500   76.29100  4.08500   1.000 88.64948  ?  1187 HIS   B CD2 1 
ATOM   23511 C  CE1 . HIS   B 1 1189 ? 39.69600   75.69500  2.63100   1.000 94.92986  ?  1187 HIS   B CE1 1 
ATOM   23512 N  NE2 . HIS   B 1 1189 ? 38.92900   76.69800  3.01800   1.000 90.20586  ?  1187 HIS   B NE2 1 
ATOM   23513 N  N   . GLY   B 1 1190 ? 37.84800   73.00200  8.71500   1.000 73.22813  ?  1188 GLY   B N   1 
ATOM   23514 C  CA  . GLY   B 1 1190 ? 37.02500   72.32400  9.69500   1.000 79.68587  ?  1188 GLY   B CA  1 
ATOM   23515 C  C   . GLY   B 1 1190 ? 37.68200   72.34400  11.05700  1.000 71.73742  ?  1188 GLY   B C   1 
ATOM   23516 O  O   . GLY   B 1 1190 ? 38.26700   71.35000  11.50000  1.000 78.80287  ?  1188 GLY   B O   1 
ATOM   23517 N  N   . LEU   B 1 1191 ? 37.58800   73.48500  11.73000  1.000 71.10206  ?  1189 LEU   B N   1 
ATOM   23518 C  CA  . LEU   B 1 1191 ? 38.30400   73.69800  12.97700  1.000 81.69517  ?  1189 LEU   B CA  1 
ATOM   23519 C  C   . LEU   B 1 1191 ? 37.49000   73.32400  14.20300  1.000 77.26446  ?  1189 LEU   B C   1 
ATOM   23520 O  O   . LEU   B 1 1191 ? 38.07600   73.01000  15.24700  1.000 70.66688  ?  1189 LEU   B O   1 
ATOM   23521 C  CB  . LEU   B 1 1191 ? 38.73700   75.15800  13.06900  1.000 78.04881  ?  1189 LEU   B CB  1 
ATOM   23522 C  CG  . LEU   B 1 1191 ? 39.29800   75.66600  11.74600  1.000 87.36701  ?  1189 LEU   B CG  1 
ATOM   23523 C  CD1 . LEU   B 1 1191 ? 38.37100   76.69400  11.09800  1.000 63.80725  ?  1189 LEU   B CD1 1 
ATOM   23524 C  CD2 . LEU   B 1 1191 ? 40.68200   76.20300  11.97200  1.000 61.75367  ?  1189 LEU   B CD2 1 
ATOM   23525 N  N   . ASP   B 1 1192 ? 36.16400   73.35000  14.10000  1.000 77.92066  ?  1190 ASP   B N   1 
ATOM   23526 C  CA  . ASP   B 1 1192 ? 35.28700   72.91600  15.17600  1.000 90.63386  ?  1190 ASP   B CA  1 
ATOM   23527 C  C   . ASP   B 1 1192 ? 34.93900   71.43600  15.08600  1.000 90.89402  ?  1190 ASP   B C   1 
ATOM   23528 O  O   . ASP   B 1 1192 ? 34.24300   70.92200  15.96800  1.000 98.40029  ?  1190 ASP   B O   1 
ATOM   23529 C  CB  . ASP   B 1 1192 ? 34.00700   73.75900  15.17900  1.000 88.98215  ?  1190 ASP   B CB  1 
ATOM   23530 C  CG  . ASP   B 1 1192 ? 33.99700   74.80000  16.28300  1.000 113.01479 ?  1190 ASP   B CG  1 
ATOM   23531 O  OD1 . ASP   B 1 1192 ? 34.99500   74.88300  17.03100  1.000 95.31889  ?  1190 ASP   B OD1 1 
ATOM   23532 O  OD2 . ASP   B 1 1192 ? 32.99400   75.53500  16.40600  1.000 127.81289 -1 1190 ASP   B OD2 1 
ATOM   23533 N  N   . GLN   B 1 1193 ? 35.40300   70.74300  14.04900  1.000 80.99106  ?  1191 GLN   B N   1 
ATOM   23534 C  CA  . GLN   B 1 1193 ? 35.18900   69.30900  13.93400  1.000 78.36709  ?  1191 GLN   B CA  1 
ATOM   23535 C  C   . GLN   B 1 1193 ? 36.15000   68.55100  14.84200  1.000 79.64987  ?  1191 GLN   B C   1 
ATOM   23536 O  O   . GLN   B 1 1193 ? 37.23100   69.03900  15.18700  1.000 81.71178  ?  1191 GLN   B O   1 
ATOM   23537 C  CB  . GLN   B 1 1193 ? 35.37300   68.84800  12.48800  1.000 82.09065  ?  1191 GLN   B CB  1 
ATOM   23538 C  CG  . GLN   B 1 1193 ? 34.25400   69.26600  11.55400  1.000 92.99034  ?  1191 GLN   B CG  1 
ATOM   23539 C  CD  . GLN   B 1 1193 ? 33.74600   68.11600  10.71000  1.000 105.79908 ?  1191 GLN   B CD  1 
ATOM   23540 O  OE1 . GLN   B 1 1193 ? 32.55800   67.79300  10.73300  1.000 112.26168 ?  1191 GLN   B OE1 1 
ATOM   23541 N  NE2 . GLN   B 1 1193 ? 34.64600   67.48700  9.96200   1.000 92.74326  ?  1191 GLN   B NE2 1 
ATOM   23542 N  N   . GLN   B 1 1194 ? 35.74500   67.34600  15.23000  1.000 76.80648  ?  1192 GLN   B N   1 
ATOM   23543 C  CA  . GLN   B 1 1194 ? 36.58300   66.52200  16.08700  1.000 77.18575  ?  1192 GLN   B CA  1 
ATOM   23544 C  C   . GLN   B 1 1194 ? 37.75300   65.94600  15.29700  1.000 76.22861  ?  1192 GLN   B C   1 
ATOM   23545 O  O   . GLN   B 1 1194 ? 37.64900   65.67700  14.09700  1.000 91.65321  ?  1192 GLN   B O   1 
ATOM   23546 C  CB  . GLN   B 1 1194 ? 35.76200   65.39400  16.71300  1.000 94.14177  ?  1192 GLN   B CB  1 
ATOM   23547 C  CG  . GLN   B 1 1194 ? 34.95300   65.81900  17.92800  1.000 95.49436  ?  1192 GLN   B CG  1 
ATOM   23548 C  CD  . GLN   B 1 1194 ? 33.83500   64.84900  18.25200  1.000 85.04847  ?  1192 GLN   B CD  1 
ATOM   23549 O  OE1 . GLN   B 1 1194 ? 34.00100   63.94300  19.06700  1.000 88.22847  ?  1192 GLN   B OE1 1 
ATOM   23550 N  NE2 . GLN   B 1 1194 ? 32.68500   65.03700  17.61400  1.000 75.32735  ?  1192 GLN   B NE2 1 
ATOM   23551 N  N   . VAL   B 1 1195 ? 38.88100   65.76300  15.98800  1.000 63.80071  ?  1193 VAL   B N   1 
ATOM   23552 C  CA  . VAL   B 1 1195 ? 40.08300   65.24800  15.33500  1.000 69.23995  ?  1193 VAL   B CA  1 
ATOM   23553 C  C   . VAL   B 1 1195 ? 39.82700   63.85900  14.75900  1.000 73.91352  ?  1193 VAL   B C   1 
ATOM   23554 O  O   . VAL   B 1 1195 ? 40.31600   63.52000  13.67300  1.000 77.97394  ?  1193 VAL   B O   1 
ATOM   23555 C  CB  . VAL   B 1 1195 ? 41.26700   65.25300  16.32100  1.000 69.75441  ?  1193 VAL   B CB  1 
ATOM   23556 C  CG1 . VAL   B 1 1195 ? 42.33800   64.26100  15.89400  1.000 54.25589  ?  1193 VAL   B CG1 1 
ATOM   23557 C  CG2 . VAL   B 1 1195 ? 41.85300   66.65300  16.43400  1.000 70.64773  ?  1193 VAL   B CG2 1 
ATOM   23558 N  N   . LYS   B 1 1196 ? 39.04200   63.04000  15.46700  1.000 74.54125  ?  1194 LYS   B N   1 
ATOM   23559 C  CA  . LYS   B 1 1196 ? 38.71400   61.70700  14.97000  1.000 65.09587  ?  1194 LYS   B CA  1 
ATOM   23560 C  C   . LYS   B 1 1196 ? 37.98500   61.76400  13.63300  1.000 68.78915  ?  1194 LYS   B C   1 
ATOM   23561 O  O   . LYS   B 1 1196 ? 38.09400   60.83200  12.82800  1.000 81.34001  ?  1194 LYS   B O   1 
ATOM   23562 C  CB  . LYS   B 1 1196 ? 37.87200   60.95200  16.00100  1.000 70.92857  ?  1194 LYS   B CB  1 
ATOM   23563 C  CG  . LYS   B 1 1196 ? 36.40500   61.37700  16.04300  1.000 78.10676  ?  1194 LYS   B CG  1 
ATOM   23564 C  CD  . LYS   B 1 1196 ? 35.59700   60.54900  17.03200  1.000 82.75584  ?  1194 LYS   B CD  1 
ATOM   23565 C  CE  . LYS   B 1 1196 ? 34.10800   60.63400  16.73100  1.000 77.51793  ?  1194 LYS   B CE  1 
ATOM   23566 N  NZ  . LYS   B 1 1196 ? 33.78500   60.05900  15.39400  1.000 88.11180  ?  1194 LYS   B NZ  1 
ATOM   23567 N  N   . ARG   B 1 1197 ? 37.24700   62.84700  13.37300  1.000 51.71353  ?  1195 ARG   B N   1 
ATOM   23568 C  CA  . ARG   B 1 1197 ? 36.49600   62.99400  12.13200  1.000 64.44802  ?  1195 ARG   B CA  1 
ATOM   23569 C  C   . ARG   B 1 1197 ? 37.38100   63.31300  10.93600  1.000 67.16634  ?  1195 ARG   B C   1 
ATOM   23570 O  O   . ARG   B 1 1197 ? 36.86400   63.39500  9.81500   1.000 62.68022  ?  1195 ARG   B O   1 
ATOM   23571 C  CB  . ARG   B 1 1197 ? 35.43300   64.08300  12.28900  1.000 80.57183  ?  1195 ARG   B CB  1 
ATOM   23572 C  CG  . ARG   B 1 1197 ? 33.99700   63.58200  12.38400  1.000 89.55659  ?  1195 ARG   B CG  1 
ATOM   23573 C  CD  . ARG   B 1 1197 ? 33.03000   64.73700  12.16000  1.000 105.26464 ?  1195 ARG   B CD  1 
ATOM   23574 N  NE  . ARG   B 1 1197 ? 31.63100   64.36800  12.34600  1.000 111.08166 ?  1195 ARG   B NE  1 
ATOM   23575 C  CZ  . ARG   B 1 1197 ? 30.77300   64.15000  11.35800  1.000 115.01616 ?  1195 ARG   B CZ  1 
ATOM   23576 N  NH1 . ARG   B 1 1197 ? 31.14900   64.20800  10.09100  1.000 103.93747 ?  1195 ARG   B NH1 1 
ATOM   23577 N  NH2 . ARG   B 1 1197 ? 29.50500   63.87100  11.64900  1.000 125.45456 ?  1195 ARG   B NH2 1 
ATOM   23578 N  N   . PHE   B 1 1198 ? 38.68200   63.50500  11.14500  1.000 70.71053  ?  1196 PHE   B N   1 
ATOM   23579 C  CA  . PHE   B 1 1198 ? 39.62000   63.75800  10.06000  1.000 67.52817  ?  1196 PHE   B CA  1 
ATOM   23580 C  C   . PHE   B 1 1198 ? 40.08300   62.43200  9.46900   1.000 71.73569  ?  1196 PHE   B C   1 
ATOM   23581 O  O   . PHE   B 1 1198 ? 40.43900   61.50600  10.20600  1.000 67.32836  ?  1196 PHE   B O   1 
ATOM   23582 C  CB  . PHE   B 1 1198 ? 40.82400   64.56100  10.56000  1.000 70.53807  ?  1196 PHE   B CB  1 
ATOM   23583 C  CG  . PHE   B 1 1198 ? 40.48600   65.95900  11.00400  1.000 78.81681  ?  1196 PHE   B CG  1 
ATOM   23584 C  CD1 . PHE   B 1 1198 ? 39.38100   66.61900  10.49200  1.000 73.94450  ?  1196 PHE   B CD1 1 
ATOM   23585 C  CD2 . PHE   B 1 1198 ? 41.28200   66.61600  11.93000  1.000 70.64563  ?  1196 PHE   B CD2 1 
ATOM   23586 C  CE1 . PHE   B 1 1198 ? 39.07300   67.90500  10.89900  1.000 73.48763  ?  1196 PHE   B CE1 1 
ATOM   23587 C  CE2 . PHE   B 1 1198 ? 40.98000   67.90200  12.34000  1.000 55.08579  ?  1196 PHE   B CE2 1 
ATOM   23588 C  CZ  . PHE   B 1 1198 ? 39.87400   68.54700  11.82400  1.000 67.86860  ?  1196 PHE   B CZ  1 
ATOM   23589 N  N   . GLU   B 1 1199 ? 40.08200   62.34400  8.14100   1.000 70.08481  ?  1197 GLU   B N   1 
ATOM   23590 C  CA  . GLU   B 1 1199 ? 40.45200   61.12300  7.43900   1.000 72.23308  ?  1197 GLU   B CA  1 
ATOM   23591 C  C   . GLU   B 1 1199 ? 41.85500   61.25200  6.86100   1.000 68.01433  ?  1197 GLU   B C   1 
ATOM   23592 O  O   . GLU   B 1 1199 ? 42.17700   62.25100  6.20800   1.000 60.97756  ?  1197 GLU   B O   1 
ATOM   23593 C  CB  . GLU   B 1 1199 ? 39.45300   60.80300  6.32500   1.000 62.19536  ?  1197 GLU   B CB  1 
ATOM   23594 C  CG  . GLU   B 1 1199 ? 39.02400   62.00000  5.49400   1.000 78.40059  ?  1197 GLU   B CG  1 
ATOM   23595 C  CD  . GLU   B 1 1199 ? 38.03700   61.62500  4.40400   1.000 89.92488  ?  1197 GLU   B CD  1 
ATOM   23596 O  OE1 . GLU   B 1 1199 ? 37.77700   60.41400  4.23300   1.000 82.00094  ?  1197 GLU   B OE1 1 
ATOM   23597 O  OE2 . GLU   B 1 1199 ? 37.51900   62.53800  3.72400   1.000 81.87446  -1 1197 GLU   B OE2 1 
ATOM   23598 N  N   . LEU   B 1 1200 ? 42.68200   60.23400  7.10600   1.000 69.74525  ?  1198 LEU   B N   1 
ATOM   23599 C  CA  . LEU   B 1 1200 ? 44.02300   60.18500  6.53700   1.000 53.25762  ?  1198 LEU   B CA  1 
ATOM   23600 C  C   . LEU   B 1 1200 ? 44.01000   59.74500  5.07800   1.000 62.49186  ?  1198 LEU   B C   1 
ATOM   23601 O  O   . LEU   B 1 1200 ? 44.83400   60.21300  4.28600   1.000 69.27355  ?  1198 LEU   B O   1 
ATOM   23602 C  CB  . LEU   B 1 1200 ? 44.89900   59.24000  7.36000   1.000 36.48098  ?  1198 LEU   B CB  1 
ATOM   23603 C  CG  . LEU   B 1 1200 ? 46.41200   59.34300  7.18500   1.000 47.62304  ?  1198 LEU   B CG  1 
ATOM   23604 C  CD1 . LEU   B 1 1200 ? 46.94800   60.58100  7.88000   1.000 60.89677  ?  1198 LEU   B CD1 1 
ATOM   23605 C  CD2 . LEU   B 1 1200 ? 47.08700   58.09700  7.72500   1.000 58.92956  ?  1198 LEU   B CD2 1 
ATOM   23606 N  N   . VAL   B 1 1201 ? 43.09100   58.86400  4.70400   1.000 59.32389  ?  1199 VAL   B N   1 
ATOM   23607 C  CA  . VAL   B 1 1201 ? 43.04300   58.33100  3.34800   1.000 60.19554  ?  1199 VAL   B CA  1 
ATOM   23608 C  C   . VAL   B 1 1201 ? 42.42800   59.35300  2.40600   1.000 60.17907  ?  1199 VAL   B C   1 
ATOM   23609 O  O   . VAL   B 1 1201 ? 41.50400   60.08900  2.77000   1.000 75.90148  ?  1199 VAL   B O   1 
ATOM   23610 C  CB  . VAL   B 1 1201 ? 42.25800   57.01100  3.32500   1.000 61.45392  ?  1199 VAL   B CB  1 
ATOM   23611 C  CG1 . VAL   B 1 1201 ? 42.60900   56.20300  2.09500   1.000 64.13048  ?  1199 VAL   B CG1 1 
ATOM   23612 C  CG2 . VAL   B 1 1201 ? 42.58700   56.22600  4.55500   1.000 69.23958  ?  1199 VAL   B CG2 1 
ATOM   23613 N  N   . THR   B 1 1202 ? 42.93800   59.38800  1.18200   1.000 62.71329  ?  1200 THR   B N   1 
ATOM   23614 C  CA  . THR   B 1 1202 ? 42.40400   60.22500  0.12200   1.000 58.65033  ?  1200 THR   B CA  1 
ATOM   23615 C  C   . THR   B 1 1202 ? 41.41700   59.42900  -0.72400  1.000 67.94347  ?  1200 THR   B C   1 
ATOM   23616 O  O   . THR   B 1 1202 ? 41.43800   58.19600  -0.74900  1.000 69.58036  ?  1200 THR   B O   1 
ATOM   23617 C  CB  . THR   B 1 1202 ? 43.53500   60.76900  -0.75300  1.000 53.59976  ?  1200 THR   B CB  1 
ATOM   23618 O  OG1 . THR   B 1 1202 ? 43.89600   59.78800  -1.73100  1.000 68.79693  ?  1200 THR   B OG1 1 
ATOM   23619 C  CG2 . THR   B 1 1202 ? 44.75100   61.08900  0.10100   1.000 48.12133  ?  1200 THR   B CG2 1 
ATOM   23620 N  N   . GLU   B 1 1203 ? 40.53900   60.15500  -1.42100  1.000 61.14353  ?  1201 GLU   B N   1 
ATOM   23621 C  CA  . GLU   B 1 1203 ? 39.54300   59.49100  -2.25700  1.000 66.95174  ?  1201 GLU   B CA  1 
ATOM   23622 C  C   . GLU   B 1 1203 ? 40.20600   58.68100  -3.36400  1.000 64.71619  ?  1201 GLU   B C   1 
ATOM   23623 O  O   . GLU   B 1 1203 ? 39.75100   57.57900  -3.69400  1.000 77.97771  ?  1201 GLU   B O   1 
ATOM   23624 C  CB  . GLU   B 1 1203 ? 38.57500   60.52000  -2.84000  1.000 64.74332  ?  1201 GLU   B CB  1 
ATOM   23625 C  CG  . GLU   B 1 1203 ? 37.25500   60.62400  -2.08400  1.000 71.89689  ?  1201 GLU   B CG  1 
ATOM   23626 C  CD  . GLU   B 1 1203 ? 37.44800   60.83300  -0.58900  1.000 91.96590  ?  1201 GLU   B CD  1 
ATOM   23627 O  OE1 . GLU   B 1 1203 ? 38.26400   61.69900  -0.20300  1.000 89.92624  ?  1201 GLU   B OE1 1 
ATOM   23628 O  OE2 . GLU   B 1 1203 ? 36.78300   60.13100  0.20300   1.000 85.28741  -1 1201 GLU   B OE2 1 
ATOM   23629 N  N   . ASP   B 1 1204 ? 41.28500   59.20700  -3.94700  1.000 66.06152  ?  1202 ASP   B N   1 
ATOM   23630 C  CA  . ASP   B 1 1204 ? 42.03500   58.43800  -4.93500  1.000 76.31375  ?  1202 ASP   B CA  1 
ATOM   23631 C  C   . ASP   B 1 1204 ? 42.67000   57.21100  -4.29700  1.000 70.29198  ?  1202 ASP   B C   1 
ATOM   23632 O  O   . ASP   B 1 1204 ? 42.78500   56.15700  -4.93300  1.000 75.32559  ?  1202 ASP   B O   1 
ATOM   23633 C  CB  . ASP   B 1 1204 ? 43.10300   59.31200  -5.59100  1.000 63.34305  ?  1202 ASP   B CB  1 
ATOM   23634 C  CG  . ASP   B 1 1204 ? 42.53400   60.22100  -6.66400  1.000 77.30000  ?  1202 ASP   B CG  1 
ATOM   23635 O  OD1 . ASP   B 1 1204 ? 41.30000   60.21500  -6.86500  1.000 80.28688  ?  1202 ASP   B OD1 1 
ATOM   23636 O  OD2 . ASP   B 1 1204 ? 43.32200   60.94700  -7.30600  1.000 86.97144  -1 1202 ASP   B OD2 1 
ATOM   23637 N  N   . GLU   B 1 1205 ? 43.08800   57.33000  -3.03600  1.000 56.89709  ?  1203 GLU   B N   1 
ATOM   23638 C  CA  . GLU   B 1 1205 ? 43.64000   56.18000  -2.33100  1.000 58.95908  ?  1203 GLU   B CA  1 
ATOM   23639 C  C   . GLU   B 1 1205 ? 42.58100   55.11100  -2.10300  1.000 66.71782  ?  1203 GLU   B C   1 
ATOM   23640 O  O   . GLU   B 1 1205 ? 42.90800   53.92200  -2.02300  1.000 76.44887  ?  1203 GLU   B O   1 
ATOM   23641 C  CB  . GLU   B 1 1205 ? 44.24100   56.62100  -0.99700  1.000 61.28078  ?  1203 GLU   B CB  1 
ATOM   23642 C  CG  . GLU   B 1 1205 ? 45.74900   56.80500  -0.99200  1.000 58.17105  ?  1203 GLU   B CG  1 
ATOM   23643 C  CD  . GLU   B 1 1205 ? 46.27700   57.14500  0.39200   1.000 73.47717  ?  1203 GLU   B CD  1 
ATOM   23644 O  OE1 . GLU   B 1 1205 ? 45.68000   58.01700  1.05800   1.000 72.87476  ?  1203 GLU   B OE1 1 
ATOM   23645 O  OE2 . GLU   B 1 1205 ? 47.28100   56.53700  0.82000   1.000 79.49271  -1 1203 GLU   B OE2 1 
ATOM   23646 N  N   . LYS   B 1 1206 ? 41.31300   55.51100  -2.00000  1.000 65.77945  ?  1204 LYS   B N   1 
ATOM   23647 C  CA  . LYS   B 1 1206 ? 40.25000   54.54800  -1.74800  1.000 69.95831  ?  1204 LYS   B CA  1 
ATOM   23648 C  C   . LYS   B 1 1206 ? 39.77800   53.87100  -3.02700  1.000 68.15770  ?  1204 LYS   B C   1 
ATOM   23649 O  O   . LYS   B 1 1206 ? 39.32900   52.72000  -2.98100  1.000 73.88010  ?  1204 LYS   B O   1 
ATOM   23650 C  CB  . LYS   B 1 1206 ? 39.08300   55.23700  -1.03800  1.000 63.68783  ?  1204 LYS   B CB  1 
ATOM   23651 C  CG  . LYS   B 1 1206 ? 39.44300   55.75700  0.34800   1.000 68.79889  ?  1204 LYS   B CG  1 
ATOM   23652 C  CD  . LYS   B 1 1206 ? 38.22000   55.90500  1.23800   1.000 63.06046  ?  1204 LYS   B CD  1 
ATOM   23653 C  CE  . LYS   B 1 1206 ? 37.50700   57.22500  0.99000   1.000 68.08111  ?  1204 LYS   B CE  1 
ATOM   23654 N  NZ  . LYS   B 1 1206 ? 37.64200   58.14800  2.15400   1.000 60.58595  ?  1204 LYS   B NZ  1 
ATOM   23655 N  N   . ARG   B 1 1207 ? 39.87100   54.55700  -4.16900  1.000 63.09808  ?  1205 ARG   B N   1 
ATOM   23656 C  CA  . ARG   B 1 1207 ? 39.53400   53.91900  -5.43700  1.000 68.09078  ?  1205 ARG   B CA  1 
ATOM   23657 C  C   . ARG   B 1 1207 ? 40.62200   52.94600  -5.86300  1.000 73.77997  ?  1205 ARG   B C   1 
ATOM   23658 O  O   . ARG   B 1 1207 ? 40.32600   51.85600  -6.36800  1.000 75.41236  ?  1205 ARG   B O   1 
ATOM   23659 C  CB  . ARG   B 1 1207 ? 39.30300   54.97600  -6.51800  1.000 71.72510  ?  1205 ARG   B CB  1 
ATOM   23660 C  CG  . ARG   B 1 1207 ? 38.35700   54.54000  -7.63900  1.000 80.49245  ?  1205 ARG   B CG  1 
ATOM   23661 C  CD  . ARG   B 1 1207 ? 36.95400   54.21000  -7.11800  1.000 92.72376  ?  1205 ARG   B CD  1 
ATOM   23662 N  NE  . ARG   B 1 1207 ? 36.64000   54.91900  -5.88200  1.000 111.28142 ?  1205 ARG   B NE  1 
ATOM   23663 C  CZ  . ARG   B 1 1207 ? 35.47800   54.85500  -5.24600  1.000 118.56018 ?  1205 ARG   B CZ  1 
ATOM   23664 N  NH1 . ARG   B 1 1207 ? 34.47000   54.13700  -5.71500  1.000 119.44182 ?  1205 ARG   B NH1 1 
ATOM   23665 N  NH2 . ARG   B 1 1207 ? 35.32800   55.52000  -4.10300  1.000 108.56957 ?  1205 ARG   B NH2 1 
ATOM   23666 N  N   . ASP   B 1 1208 ? 41.88700   53.32700  -5.67200  1.000 73.07926  ?  1206 ASP   B N   1 
ATOM   23667 C  CA  . ASP   B 1 1208 ? 42.98600   52.39700  -5.89700  1.000 66.01828  ?  1206 ASP   B CA  1 
ATOM   23668 C  C   . ASP   B 1 1208 ? 42.83200   51.14400  -5.04600  1.000 71.05892  ?  1206 ASP   B C   1 
ATOM   23669 O  O   . ASP   B 1 1208 ? 43.20300   50.04800  -5.48000  1.000 66.89530  ?  1206 ASP   B O   1 
ATOM   23670 C  CB  . ASP   B 1 1208 ? 44.31600   53.08800  -5.59900  1.000 78.33472  ?  1206 ASP   B CB  1 
ATOM   23671 C  CG  . ASP   B 1 1208 ? 45.46500   52.51300  -6.39600  1.000 99.63153  ?  1206 ASP   B CG  1 
ATOM   23672 O  OD1 . ASP   B 1 1208 ? 45.43000   52.61000  -7.64100  1.000 114.02293 ?  1206 ASP   B OD1 1 
ATOM   23673 O  OD2 . ASP   B 1 1208 ? 46.40400   51.96900  -5.77700  1.000 85.23035  -1 1206 ASP   B OD2 1 
ATOM   23674 N  N   . LEU   B 1 1209 ? 42.27700   51.28600  -3.84000  1.000 73.99919  ?  1207 LEU   B N   1 
ATOM   23675 C  CA  . LEU   B 1 1209 ? 42.02800   50.12700  -2.98900  1.000 70.37415  ?  1207 LEU   B CA  1 
ATOM   23676 C  C   . LEU   B 1 1209 ? 40.91200   49.25800  -3.55600  1.000 73.83935  ?  1207 LEU   B C   1 
ATOM   23677 O  O   . LEU   B 1 1209 ? 41.03300   48.02900  -3.60400  1.000 75.27317  ?  1207 LEU   B O   1 
ATOM   23678 C  CB  . LEU   B 1 1209 ? 41.68500   50.58600  -1.57100  1.000 55.01040  ?  1207 LEU   B CB  1 
ATOM   23679 C  CG  . LEU   B 1 1209 ? 42.46500   49.93300  -0.42700  1.000 71.07161  ?  1207 LEU   B CG  1 
ATOM   23680 C  CD1 . LEU   B 1 1209 ? 43.95700   49.89900  -0.72800  1.000 51.90779  ?  1207 LEU   B CD1 1 
ATOM   23681 C  CD2 . LEU   B 1 1209 ? 42.19900   50.65700  0.88400   1.000 74.12344  ?  1207 LEU   B CD2 1 
ATOM   23682 N  N   . PHE   B 1 1210 ? 39.81600   49.88400  -3.99300  1.000 70.65764  ?  1208 PHE   B N   1 
ATOM   23683 C  CA  . PHE   B 1 1210 ? 38.68700   49.12500  -4.52300  1.000 69.87346  ?  1208 PHE   B CA  1 
ATOM   23684 C  C   . PHE   B 1 1210 ? 39.08600   48.32300  -5.75500  1.000 72.45671  ?  1208 PHE   B C   1 
ATOM   23685 O  O   . PHE   B 1 1210 ? 38.69300   47.15900  -5.90300  1.000 89.47049  ?  1208 PHE   B O   1 
ATOM   23686 C  CB  . PHE   B 1 1210 ? 37.53100   50.07200  -4.85000  1.000 73.56098  ?  1208 PHE   B CB  1 
ATOM   23687 C  CG  . PHE   B 1 1210 ? 36.46000   49.45100  -5.70200  1.000 85.19735  ?  1208 PHE   B CG  1 
ATOM   23688 C  CD1 . PHE   B 1 1210 ? 35.50500   48.61900  -5.14300  1.000 89.95295  ?  1208 PHE   B CD1 1 
ATOM   23689 C  CD2 . PHE   B 1 1210 ? 36.41000   49.70100  -7.06500  1.000 84.47451  ?  1208 PHE   B CD2 1 
ATOM   23690 C  CE1 . PHE   B 1 1210 ? 34.51800   48.04600  -5.92700  1.000 81.11811  ?  1208 PHE   B CE1 1 
ATOM   23691 C  CE2 . PHE   B 1 1210 ? 35.42800   49.13000  -7.85400  1.000 93.07406  ?  1208 PHE   B CE2 1 
ATOM   23692 C  CZ  . PHE   B 1 1210 ? 34.48000   48.30200  -7.28400  1.000 81.19875  ?  1208 PHE   B CZ  1 
ATOM   23693 N  N   . LEU   B 1 1211 ? 39.87300   48.92500  -6.64800  1.000 67.62905  ?  1209 LEU   B N   1 
ATOM   23694 C  CA  . LEU   B 1 1211 ? 40.24600   48.24300  -7.88200  1.000 73.57074  ?  1209 LEU   B CA  1 
ATOM   23695 C  C   . LEU   B 1 1211 ? 41.29100   47.16100  -7.64000  1.000 76.94791  ?  1209 LEU   B C   1 
ATOM   23696 O  O   . LEU   B 1 1211 ? 41.36300   46.19000  -8.40300  1.000 91.34635  ?  1209 LEU   B O   1 
ATOM   23697 C  CB  . LEU   B 1 1211 ? 40.75700   49.25800  -8.90400  1.000 81.40186  ?  1209 LEU   B CB  1 
ATOM   23698 C  CG  . LEU   B 1 1211 ? 39.78100   50.37600  -9.28500  1.000 87.96155  ?  1209 LEU   B CG  1 
ATOM   23699 C  CD1 . LEU   B 1 1211 ? 40.48400   51.46900  -10.07900 1.000 71.85382  ?  1209 LEU   B CD1 1 
ATOM   23700 C  CD2 . LEU   B 1 1211 ? 38.59500   49.82000  -10.06100 1.000 76.42461  ?  1209 LEU   B CD2 1 
ATOM   23701 N  N   . ARG   B 1 1212 ? 42.10300   47.30200  -6.59400  1.000 72.78024  ?  1210 ARG   B N   1 
ATOM   23702 C  CA  . ARG   B 1 1212 ? 43.16300   46.34600  -6.30300  1.000 77.61450  ?  1210 ARG   B CA  1 
ATOM   23703 C  C   . ARG   B 1 1212 ? 42.75200   45.27300  -5.30100  1.000 83.54841  ?  1210 ARG   B C   1 
ATOM   23704 O  O   . ARG   B 1 1212 ? 43.50900   44.31500  -5.10300  1.000 82.36418  ?  1210 ARG   B O   1 
ATOM   23705 C  CB  . ARG   B 1 1212 ? 44.40400   47.08300  -5.78100  1.000 71.39051  ?  1210 ARG   B CB  1 
ATOM   23706 C  CG  . ARG   B 1 1212 ? 45.46800   47.32800  -6.84200  1.000 63.95350  ?  1210 ARG   B CG  1 
ATOM   23707 C  CD  . ARG   B 1 1212 ? 45.86900   48.79700  -6.91500  1.000 63.60789  ?  1210 ARG   B CD  1 
ATOM   23708 N  NE  . ARG   B 1 1212 ? 46.71200   49.21500  -5.80200  1.000 69.68461  ?  1210 ARG   B NE  1 
ATOM   23709 C  CZ  . ARG   B 1 1212 ? 48.01700   48.99800  -5.73600  1.000 87.14696  ?  1210 ARG   B CZ  1 
ATOM   23710 N  NH1 . ARG   B 1 1212 ? 48.65600   48.33700  -6.68700  1.000 91.09909  ?  1210 ARG   B NH1 1 
ATOM   23711 N  NH2 . ARG   B 1 1212 ? 48.69900   49.44700  -4.68400  1.000 94.20312  ?  1210 ARG   B NH2 1 
ATOM   23712 N  N   . VAL   B 1 1213 ? 41.58500   45.40200  -4.66900  1.000 76.38099  ?  1211 VAL   B N   1 
ATOM   23713 C  CA  . VAL   B 1 1213 ? 41.20000   44.50400  -3.58500  1.000 77.17800  ?  1211 VAL   B CA  1 
ATOM   23714 C  C   . VAL   B 1 1213 ? 39.75200   44.05100  -3.73700  1.000 76.84963  ?  1211 VAL   B C   1 
ATOM   23715 O  O   . VAL   B 1 1213 ? 39.48000   42.86200  -3.94300  1.000 80.39536  ?  1211 VAL   B O   1 
ATOM   23716 C  CB  . VAL   B 1 1213 ? 41.41400   45.17100  -2.21000  1.000 74.00154  ?  1211 VAL   B CB  1 
ATOM   23717 C  CG1 . VAL   B 1 1213 ? 41.02500   44.22400  -1.09100  1.000 62.37163  ?  1211 VAL   B CG1 1 
ATOM   23718 C  CG2 . VAL   B 1 1213 ? 42.86200   45.62400  -2.03700  1.000 67.93769  ?  1211 VAL   B CG2 1 
ATOM   23719 N  N   . ASN   B 1 1214 ? 38.81300   44.99400  -3.63700  1.000 71.77122  ?  1212 ASN   B N   1 
ATOM   23720 C  CA  . ASN   B 1 1214 ? 37.40200   44.67500  -3.46000  1.000 65.75505  ?  1212 ASN   B CA  1 
ATOM   23721 C  C   . ASN   B 1 1214 ? 36.59900   44.73400  -4.75400  1.000 65.02547  ?  1212 ASN   B C   1 
ATOM   23722 O  O   . ASN   B 1 1214 ? 35.36900   44.83600  -4.70200  1.000 69.28073  ?  1212 ASN   B O   1 
ATOM   23723 C  CB  . ASN   B 1 1214 ? 36.78200   45.60500  -2.42000  1.000 59.59753  ?  1212 ASN   B CB  1 
ATOM   23724 C  CG  . ASN   B 1 1214 ? 37.38800   45.42000  -1.05200  1.000 63.95790  ?  1212 ASN   B CG  1 
ATOM   23725 O  OD1 . ASN   B 1 1214 ? 37.73300   44.30600  -0.66200  1.000 67.46784  ?  1212 ASN   B OD1 1 
ATOM   23726 N  ND2 . ASN   B 1 1214 ? 37.52200   46.51200  -0.31000  1.000 66.60525  ?  1212 ASN   B ND2 1 
ATOM   23727 N  N   . ASP   B 1 1215 ? 37.25800   44.67200  -5.91000  1.000 64.80486  ?  1213 ASP   B N   1 
ATOM   23728 C  CA  . ASP   B 1 1215 ? 36.55700   44.54100  -7.18800  1.000 78.51489  ?  1213 ASP   B CA  1 
ATOM   23729 C  C   . ASP   B 1 1215 ? 36.39700   43.05000  -7.45400  1.000 86.56932  ?  1213 ASP   B C   1 
ATOM   23730 O  O   . ASP   B 1 1215 ? 37.22400   42.42000  -8.11600  1.000 87.11627  ?  1213 ASP   B O   1 
ATOM   23731 C  CB  . ASP   B 1 1215 ? 37.31300   45.24500  -8.30700  1.000 78.24712  ?  1213 ASP   B CB  1 
ATOM   23732 C  CG  . ASP   B 1 1215 ? 36.42000   45.58700  -9.49000  1.000 89.44734  ?  1213 ASP   B CG  1 
ATOM   23733 O  OD1 . ASP   B 1 1215 ? 35.19200   45.37800  -9.39000  1.000 85.85688  ?  1213 ASP   B OD1 1 
ATOM   23734 O  OD2 . ASP   B 1 1215 ? 36.94600   46.06800  -10.51800 1.000 71.28378  -1 1213 ASP   B OD2 1 
ATOM   23735 N  N   . THR   B 1 1216 ? 35.31300   42.47300  -6.92400  1.000 77.22790  ?  1214 THR   B N   1 
ATOM   23736 C  CA  . THR   B 1 1216 ? 35.16200   41.02300  -6.87400  1.000 68.50247  ?  1214 THR   B CA  1 
ATOM   23737 C  C   . THR   B 1 1216 ? 33.78000   40.55400  -7.32300  1.000 72.92146  ?  1214 THR   B C   1 
ATOM   23738 O  O   . THR   B 1 1216 ? 33.40600   39.40900  -7.04700  1.000 73.68463  ?  1214 THR   B O   1 
ATOM   23739 C  CB  . THR   B 1 1216 ? 35.44600   40.50800  -5.45900  1.000 70.70448  ?  1214 THR   B CB  1 
ATOM   23740 O  OG1 . THR   B 1 1216 ? 34.70500   41.28700  -4.51100  1.000 69.50361  ?  1214 THR   B OG1 1 
ATOM   23741 C  CG2 . THR   B 1 1216 ? 36.93400   40.59900  -5.13100  1.000 70.78660  ?  1214 THR   B CG2 1 
ATOM   23742 N  N   . ALA   B 1 1217 ? 33.01400   41.39700  -8.01100  1.000 76.96951  ?  1215 ALA   B N   1 
ATOM   23743 C  CA  . ALA   B 1 1217 ? 31.66700   41.01300  -8.42100  1.000 77.46427  ?  1215 ALA   B CA  1 
ATOM   23744 C  C   . ALA   B 1 1217 ? 31.71500   39.98600  -9.54900  1.000 74.57824  ?  1215 ALA   B C   1 
ATOM   23745 O  O   . ALA   B 1 1217 ? 32.44300   40.15700  -10.53200 1.000 64.94221  ?  1215 ALA   B O   1 
ATOM   23746 C  CB  . ALA   B 1 1217 ? 30.87300   42.24300  -8.86000  1.000 54.25941  ?  1215 ALA   B CB  1 
ATOM   23747 N  N   . LYS   B 1 1218 ? 30.93100   38.91700  -9.40200  1.000 76.83952  ?  1216 LYS   B N   1 
ATOM   23748 C  CA  . LYS   B 1 1218 ? 30.83000   37.87600  -10.42500 1.000 76.30203  ?  1216 LYS   B CA  1 
ATOM   23749 C  C   . LYS   B 1 1218 ? 29.51500   37.13900  -10.22900 1.000 81.86634  ?  1216 LYS   B C   1 
ATOM   23750 O  O   . LYS   B 1 1218 ? 29.25100   36.62800  -9.13500  1.000 68.70150  ?  1216 LYS   B O   1 
ATOM   23751 C  CB  . LYS   B 1 1218 ? 32.01300   36.90800  -10.34600 1.000 66.72446  ?  1216 LYS   B CB  1 
ATOM   23752 C  CG  . LYS   B 1 1218 ? 31.90900   35.71000  -11.28100 1.000 66.67897  ?  1216 LYS   B CG  1 
ATOM   23753 C  CD  . LYS   B 1 1218 ? 33.27800   35.30000  -11.80700 1.000 86.26114  ?  1216 LYS   B CD  1 
ATOM   23754 C  CE  . LYS   B 1 1218 ? 33.21000   33.99100  -12.58000 1.000 74.12007  ?  1216 LYS   B CE  1 
ATOM   23755 N  NZ  . LYS   B 1 1218 ? 34.53300   33.60900  -13.14900 1.000 74.69770  ?  1216 LYS   B NZ  1 
ATOM   23756 N  N   . ALA   B 1 1219 ? 28.69400   37.08200  -11.27500 1.000 85.80688  ?  1217 ALA   B N   1 
ATOM   23757 C  CA  . ALA   B 1 1219 ? 27.40800   36.40500  -11.18000 1.000 76.92204  ?  1217 ALA   B CA  1 
ATOM   23758 C  C   . ALA   B 1 1219 ? 27.61300   34.89900  -11.07100 1.000 78.52018  ?  1217 ALA   B C   1 
ATOM   23759 O  O   . ALA   B 1 1219 ? 28.39800   34.31100  -11.82200 1.000 74.49461  ?  1217 ALA   B O   1 
ATOM   23760 C  CB  . ALA   B 1 1219 ? 26.53800   36.73800  -12.39100 1.000 58.83776  ?  1217 ALA   B CB  1 
ATOM   23761 N  N   . TYR   B 1 1220 ? 26.90800   34.27700  -10.13100 1.000 75.60879  ?  1218 TYR   B N   1 
ATOM   23762 C  CA  . TYR   B 1 1220 ? 27.03300   32.85400  -9.87100  1.000 69.81587  ?  1218 TYR   B CA  1 
ATOM   23763 C  C   . TYR   B 1 1220 ? 25.66000   32.20100  -9.86900  1.000 78.96266  ?  1218 TYR   B C   1 
ATOM   23764 O  O   . TYR   B 1 1220 ? 24.67000   32.82500  -9.46800  1.000 65.20091  ?  1218 TYR   B O   1 
ATOM   23765 C  CB  . TYR   B 1 1220 ? 27.73500   32.59800  -8.52800  1.000 63.03179  ?  1218 TYR   B CB  1 
ATOM   23766 C  CG  . TYR   B 1 1220 ? 29.24500   32.63100  -8.61900  1.000 67.33076  ?  1218 TYR   B CG  1 
ATOM   23767 C  CD1 . TYR   B 1 1220 ? 29.89500   32.25000  -9.78600  1.000 74.49363  ?  1218 TYR   B CD1 1 
ATOM   23768 C  CD2 . TYR   B 1 1220 ? 30.02200   33.04300  -7.54200  1.000 71.50683  ?  1218 TYR   B CD2 1 
ATOM   23769 C  CE1 . TYR   B 1 1220 ? 31.27600   32.27800  -9.88000  1.000 76.38687  ?  1218 TYR   B CE1 1 
ATOM   23770 C  CE2 . TYR   B 1 1220 ? 31.40700   33.07300  -7.62700  1.000 55.51550  ?  1218 TYR   B CE2 1 
ATOM   23771 C  CZ  . TYR   B 1 1220 ? 32.02600   32.68900  -8.80000  1.000 63.18537  ?  1218 TYR   B CZ  1 
ATOM   23772 O  OH  . TYR   B 1 1220 ? 33.39900   32.71300  -8.90300  1.000 74.98266  ?  1218 TYR   B OH  1 
ATOM   23773 N  N   . PRO   B 1 1221 ? 25.56900   30.95000  -10.31800 1.000 80.97379  ?  1219 PRO   B N   1 
ATOM   23774 C  CA  . PRO   B 1 1221 ? 24.26300   30.28500  -10.40100 1.000 66.44008  ?  1219 PRO   B CA  1 
ATOM   23775 C  C   . PRO   B 1 1221 ? 23.63400   30.08800  -9.03100  1.000 75.86869  ?  1219 PRO   B C   1 
ATOM   23776 O  O   . PRO   B 1 1221 ? 24.31700   29.87900  -8.02600  1.000 78.13392  ?  1219 PRO   B O   1 
ATOM   23777 C  CB  . PRO   B 1 1221 ? 24.59100   28.93900  -11.05900 1.000 75.44693  ?  1219 PRO   B CB  1 
ATOM   23778 C  CG  . PRO   B 1 1221 ? 25.90100   29.16400  -11.75900 1.000 71.60216  ?  1219 PRO   B CG  1 
ATOM   23779 C  CD  . PRO   B 1 1221 ? 26.64700   30.12500  -10.88900 1.000 58.87728  ?  1219 PRO   B CD  1 
ATOM   23780 N  N   . ASN   B 1 1222 ? 22.30100   30.14100  -9.00800  1.000 77.02579  ?  1220 ASN   B N   1 
ATOM   23781 C  CA  . ASN   B 1 1222 ? 21.52700   30.09400  -7.77500  1.000 85.42864  ?  1220 ASN   B CA  1 
ATOM   23782 C  C   . ASN   B 1 1222 ? 20.92200   28.71600  -7.51100  1.000 86.52156  ?  1220 ASN   B C   1 
ATOM   23783 O  O   . ASN   B 1 1222 ? 19.84600   28.61600  -6.91300  1.000 74.03159  ?  1220 ASN   B O   1 
ATOM   23784 C  CB  . ASN   B 1 1222 ? 20.43200   31.15900  -7.80800  1.000 72.80170  ?  1220 ASN   B CB  1 
ATOM   23785 C  CG  . ASN   B 1 1222 ? 20.23000   31.82400  -6.46700  1.000 91.12935  ?  1220 ASN   B CG  1 
ATOM   23786 O  OD1 . ASN   B 1 1222 ? 20.08700   31.15100  -5.44800  1.000 97.43242  ?  1220 ASN   B OD1 1 
ATOM   23787 N  ND2 . ASN   B 1 1222 ? 20.21900   33.15200  -6.45700  1.000 103.30780 ?  1220 ASN   B ND2 1 
ATOM   23788 N  N   . LYS   B 1 1223 ? 21.59500   27.65000  -7.93800  1.000 84.43689  ?  1221 LYS   B N   1 
ATOM   23789 C  CA  . LYS   B 1 1223 ? 21.09600   26.29000  -7.75700  1.000 80.82389  ?  1221 LYS   B CA  1 
ATOM   23790 C  C   . LYS   B 1 1223 ? 21.60300   25.75000  -6.42400  1.000 94.50952  ?  1221 LYS   B C   1 
ATOM   23791 O  O   . LYS   B 1 1223 ? 22.81000   25.55600  -6.24500  1.000 103.40197 ?  1221 LYS   B O   1 
ATOM   23792 C  CB  . LYS   B 1 1223 ? 21.53500   25.39500  -8.91300  1.000 78.82840  ?  1221 LYS   B CB  1 
ATOM   23793 N  N   . LEU   B 1 1224 ? 20.68200   25.50400  -5.49300  1.000 77.66324  ?  1222 LEU   B N   1 
ATOM   23794 C  CA  . LEU   B 1 1224 ? 21.05700   24.96700  -4.19200  1.000 61.42650  ?  1222 LEU   B CA  1 
ATOM   23795 C  C   . LEU   B 1 1224 ? 21.74900   23.61600  -4.35200  1.000 77.14056  ?  1222 LEU   B C   1 
ATOM   23796 O  O   . LEU   B 1 1224 ? 21.52000   22.88600  -5.32000  1.000 84.06967  ?  1222 LEU   B O   1 
ATOM   23797 C  CB  . LEU   B 1 1224 ? 19.82400   24.83600  -3.29700  1.000 73.30214  ?  1222 LEU   B CB  1 
ATOM   23798 C  CG  . LEU   B 1 1224 ? 18.94100   26.08500  -3.22000  1.000 75.32597  ?  1222 LEU   B CG  1 
ATOM   23799 C  CD1 . LEU   B 1 1224 ? 17.59100   25.82400  -3.87100  1.000 91.19824  ?  1222 LEU   B CD1 1 
ATOM   23800 C  CD2 . LEU   B 1 1224 ? 18.76900   26.55700  -1.78000  1.000 56.28566  ?  1222 LEU   B CD2 1 
ATOM   23801 N  N   . ILE   B 1 1225 ? 22.61400   23.29400  -3.38600  1.000 87.95939  ?  1223 ILE   B N   1 
ATOM   23802 C  CA  . ILE   B 1 1225 ? 23.45100   22.09700  -3.48200  1.000 86.64655  ?  1223 ILE   B CA  1 
ATOM   23803 C  C   . ILE   B 1 1225 ? 22.59400   20.84100  -3.56800  1.000 78.47171  ?  1223 ILE   B C   1 
ATOM   23804 O  O   . ILE   B 1 1225 ? 22.88900   19.92100  -4.34200  1.000 80.70704  ?  1223 ILE   B O   1 
ATOM   23805 C  CB  . ILE   B 1 1225 ? 24.42000   22.03200  -2.28800  1.000 71.98823  ?  1223 ILE   B CB  1 
ATOM   23806 C  CG1 . ILE   B 1 1225 ? 23.74100   22.59500  -1.03800  1.000 62.60474  ?  1223 ILE   B CG1 1 
ATOM   23807 C  CG2 . ILE   B 1 1225 ? 25.71200   22.77000  -2.60100  1.000 44.89064  ?  1223 ILE   B CG2 1 
ATOM   23808 C  CD1 . ILE   B 1 1225 ? 24.57800   22.49400  0.20400   1.000 70.85414  ?  1223 ILE   B CD1 1 
ATOM   23809 N  N   . MET   B 1 1226 ? 21.52700   20.77900  -2.76800  1.000 74.63667  ?  1224 MET   B N   1 
ATOM   23810 C  CA  . MET   B 1 1226 ? 20.66300   19.60400  -2.75600  1.000 69.92158  ?  1224 MET   B CA  1 
ATOM   23811 C  C   . MET   B 1 1226 ? 20.05000   19.34900  -4.12700  1.000 74.51288  ?  1224 MET   B C   1 
ATOM   23812 O  O   . MET   B 1 1226 ? 19.93700   18.19700  -4.56200  1.000 78.26104  ?  1224 MET   B O   1 
ATOM   23813 C  CB  . MET   B 1 1226 ? 19.57400   19.79000  -1.70700  1.000 61.11382  ?  1224 MET   B CB  1 
ATOM   23814 C  CG  . MET   B 1 1226 ? 19.30200   21.24900  -1.40700  1.000 59.04824  ?  1224 MET   B CG  1 
ATOM   23815 S  SD  . MET   B 1 1226 ? 18.18900   21.46100  -0.01900  1.000 88.85680  ?  1224 MET   B SD  1 
ATOM   23816 C  CE  . MET   B 1 1226 ? 17.97200   23.23300  -0.03500  1.000 84.22454  ?  1224 MET   B CE  1 
ATOM   23817 N  N   . SER   B 1 1227 ? 19.65000   20.41400  -4.82600  1.000 78.68281  ?  1225 SER   B N   1 
ATOM   23818 C  CA  . SER   B 1 1227 ? 19.10800   20.25600  -6.17200  1.000 85.13570  ?  1225 SER   B CA  1 
ATOM   23819 C  C   . SER   B 1 1227 ? 20.18700   19.81700  -7.15500  1.000 86.19885  ?  1225 SER   B C   1 
ATOM   23820 O  O   . SER   B 1 1227 ? 19.90800   19.05800  -8.09100  1.000 91.06785  ?  1225 SER   B O   1 
ATOM   23821 C  CB  . SER   B 1 1227 ? 18.46300   21.56200  -6.63200  1.000 85.48839  ?  1225 SER   B CB  1 
ATOM   23822 O  OG  . SER   B 1 1227 ? 17.52200   22.02300  -5.68100  1.000 94.37882  ?  1225 SER   B OG  1 
ATOM   23823 N  N   . MET   B 1 1228 ? 21.42300   20.28900  -6.96100  1.000 85.12386  ?  1226 MET   B N   1 
ATOM   23824 C  CA  . MET   B 1 1228 ? 22.52200   19.89100  -7.83700  1.000 76.33153  ?  1226 MET   B CA  1 
ATOM   23825 C  C   . MET   B 1 1228 ? 22.71600   18.38000  -7.82800  1.000 86.24624  ?  1226 MET   B C   1 
ATOM   23826 O  O   . MET   B 1 1228 ? 22.99800   17.77500  -8.86900  1.000 90.44598  ?  1226 MET   B O   1 
ATOM   23827 C  CB  . MET   B 1 1228 ? 23.81400   20.59000  -7.41200  1.000 80.06378  ?  1226 MET   B CB  1 
ATOM   23828 C  CG  . MET   B 1 1228 ? 23.84500   22.08600  -7.67200  1.000 98.17494  ?  1226 MET   B CG  1 
ATOM   23829 S  SD  . MET   B 1 1228 ? 25.40400   22.83200  -7.15300  1.000 90.91478  ?  1226 MET   B SD  1 
ATOM   23830 C  CE  . MET   B 1 1228 ? 25.96100   23.55900  -8.69200  1.000 75.26030  ?  1226 MET   B CE  1 
ATOM   23831 N  N   . LEU   B 1 1229 ? 22.57300   17.75400  -6.65900  1.000 87.75997  ?  1227 LEU   B N   1 
ATOM   23832 C  CA  . LEU   B 1 1229 ? 22.72200   16.30600  -6.57700  1.000 93.86719  ?  1227 LEU   B CA  1 
ATOM   23833 C  C   . LEU   B 1 1229 ? 21.54900   15.59400  -7.23700  1.000 93.02867  ?  1227 LEU   B C   1 
ATOM   23834 O  O   . LEU   B 1 1229 ? 21.74000   14.57900  -7.91800  1.000 94.19452  ?  1227 LEU   B O   1 
ATOM   23835 C  CB  . LEU   B 1 1229 ? 22.86700   15.87600  -5.11800  1.000 81.62120  ?  1227 LEU   B CB  1 
ATOM   23836 C  CG  . LEU   B 1 1229 ? 23.11100   14.38500  -4.88700  1.000 70.38972  ?  1227 LEU   B CG  1 
ATOM   23837 C  CD1 . LEU   B 1 1229 ? 24.50300   13.99600  -5.35800  1.000 65.08823  ?  1227 LEU   B CD1 1 
ATOM   23838 C  CD2 . LEU   B 1 1229 ? 22.91700   14.03800  -3.42000  1.000 68.64124  ?  1227 LEU   B CD2 1 
ATOM   23839 N  N   . GLU   B 1 1230 ? 20.32900   16.10700  -7.04600  1.000 84.03405  ?  1228 GLU   B N   1 
ATOM   23840 C  CA  . GLU   B 1 1230 ? 19.16600   15.54700  -7.73000  1.000 75.50042  ?  1228 GLU   B CA  1 
ATOM   23841 C  C   . GLU   B 1 1230 ? 19.38300   15.51600  -9.23600  1.000 86.69875  ?  1228 GLU   B C   1 
ATOM   23842 O  O   . GLU   B 1 1230 ? 19.09200   14.51500  -9.90100  1.000 102.30384 ?  1228 GLU   B O   1 
ATOM   23843 C  CB  . GLU   B 1 1230 ? 17.91300   16.35800  -7.39400  1.000 65.81796  ?  1228 GLU   B CB  1 
ATOM   23844 C  CG  . GLU   B 1 1230 ? 17.44100   16.23200  -5.96200  1.000 58.32883  ?  1228 GLU   B CG  1 
ATOM   23845 C  CD  . GLU   B 1 1230 ? 16.23200   17.10500  -5.67300  1.000 68.45972  ?  1228 GLU   B CD  1 
ATOM   23846 O  OE1 . GLU   B 1 1230 ? 15.81600   17.85900  -6.57700  1.000 71.86763  ?  1228 GLU   B OE1 1 
ATOM   23847 O  OE2 . GLU   B 1 1230 ? 15.70200   17.04000  -4.54200  1.000 59.81928  -1 1228 GLU   B OE2 1 
ATOM   23848 N  N   . ASP   B 1 1231 ? 19.89900   16.61600  -9.78800  1.000 88.87373  ?  1229 ASP   B N   1 
ATOM   23849 C  CA  . ASP   B 1 1231 ? 20.21500   16.66800  -11.21100 1.000 99.02749  ?  1229 ASP   B CA  1 
ATOM   23850 C  C   . ASP   B 1 1231 ? 21.30800   15.66500  -11.56100 1.000 84.44530  ?  1229 ASP   B C   1 
ATOM   23851 O  O   . ASP   B 1 1231 ? 21.12200   14.79200  -12.41700 1.000 92.86653  ?  1229 ASP   B O   1 
ATOM   23852 C  CB  . ASP   B 1 1231 ? 20.64400   18.08700  -11.59800 1.000 90.97185  ?  1229 ASP   B CB  1 
ATOM   23853 C  CG  . ASP   B 1 1231 ? 19.53900   19.11300  -11.39900 1.000 94.32435  ?  1229 ASP   B CG  1 
ATOM   23854 O  OD1 . ASP   B 1 1231 ? 18.71800   18.94400  -10.47200 1.000 105.85416 ?  1229 ASP   B OD1 1 
ATOM   23855 O  OD2 . ASP   B 1 1231 ? 19.49500   20.09600  -12.16900 1.000 92.55255  -1 1229 ASP   B OD2 1 
ATOM   23856 N  N   . TRP   B 1 1232 ? 22.46100   15.77500  -10.89500 1.000 90.31663  ?  1230 TRP   B N   1 
ATOM   23857 C  CA  . TRP   B 1 1232 ? 23.57000   14.86600  -11.16400 1.000 101.75436 ?  1230 TRP   B CA  1 
ATOM   23858 C  C   . TRP   B 1 1232 ? 23.16700   13.40900  -10.97700 1.000 91.66288  ?  1230 TRP   B C   1 
ATOM   23859 O  O   . TRP   B 1 1232 ? 23.70900   12.52600  -11.65100 1.000 85.31733  ?  1230 TRP   B O   1 
ATOM   23860 C  CB  . TRP   B 1 1232 ? 24.75700   15.20600  -10.26200 1.000 98.55290  ?  1230 TRP   B CB  1 
ATOM   23861 C  CG  . TRP   B 1 1232 ? 25.58700   16.36400  -10.73700 1.000 94.15072  ?  1230 TRP   B CG  1 
ATOM   23862 C  CD1 . TRP   B 1 1232 ? 25.92000   17.47500  -10.01900 1.000 87.19616  ?  1230 TRP   B CD1 1 
ATOM   23863 C  CD2 . TRP   B 1 1232 ? 26.19700   16.52200  -12.02700 1.000 109.34652 ?  1230 TRP   B CD2 1 
ATOM   23864 N  NE1 . TRP   B 1 1232 ? 26.69600   18.31600  -10.78000 1.000 98.05668  ?  1230 TRP   B NE1 1 
ATOM   23865 C  CE2 . TRP   B 1 1232 ? 26.88000   17.75400  -12.01600 1.000 115.76421 ?  1230 TRP   B CE2 1 
ATOM   23866 C  CE3 . TRP   B 1 1232 ? 26.23000   15.74200  -13.18900 1.000 112.14027 ?  1230 TRP   B CE3 1 
ATOM   23867 C  CZ2 . TRP   B 1 1232 ? 27.58800   18.22600  -13.12100 1.000 120.76047 ?  1230 TRP   B CZ2 1 
ATOM   23868 C  CZ3 . TRP   B 1 1232 ? 26.93500   16.21300  -14.28600 1.000 107.59926 ?  1230 TRP   B CZ3 1 
ATOM   23869 C  CH2 . TRP   B 1 1232 ? 27.60300   17.44300  -14.24300 1.000 115.46688 ?  1230 TRP   B CH2 1 
ATOM   23870 N  N   . ALA   B 1 1233 ? 22.22200   13.13800  -10.07300 1.000 89.38497  ?  1231 ALA   B N   1 
ATOM   23871 C  CA  . ALA   B 1 1233 ? 21.72400   11.77500  -9.91200  1.000 93.22369  ?  1231 ALA   B CA  1 
ATOM   23872 C  C   . ALA   B 1 1233 ? 21.01600   11.30300  -11.17400 1.000 107.48674 ?  1231 ALA   B C   1 
ATOM   23873 O  O   . ALA   B 1 1233 ? 21.27900   10.20400  -11.67300 1.000 112.65050 ?  1231 ALA   B O   1 
ATOM   23874 C  CB  . ALA   B 1 1233 ? 20.78600   11.69200  -8.70700  1.000 75.85511  ?  1231 ALA   B CB  1 
ATOM   23875 N  N   . ALA   B 1 1234 ? 20.11600   12.13000  -11.71100 1.000 92.52798  ?  1232 ALA   B N   1 
ATOM   23876 C  CA  . ALA   B 1 1234 ? 19.38400   11.74300  -12.91300 1.000 89.02824  ?  1232 ALA   B CA  1 
ATOM   23877 C  C   . ALA   B 1 1234 ? 20.32200   11.55500  -14.10000 1.000 90.93501  ?  1232 ALA   B C   1 
ATOM   23878 O  O   . ALA   B 1 1234 ? 20.15700   10.61600  -14.88800 1.000 93.53947  ?  1232 ALA   B O   1 
ATOM   23879 C  CB  . ALA   B 1 1234 ? 18.31300   12.78700  -13.23000 1.000 74.61230  ?  1232 ALA   B CB  1 
ATOM   23880 N  N   . ALA   B 1 1235 ? 21.32200   12.42900  -14.23700 1.000 93.73957  ?  1233 ALA   B N   1 
ATOM   23881 C  CA  . ALA   B 1 1235 ? 22.23500   12.34800  -15.37300 1.000 94.60642  ?  1233 ALA   B CA  1 
ATOM   23882 C  C   . ALA   B 1 1235 ? 23.18500   11.16300  -15.23800 1.000 93.99855  ?  1233 ALA   B C   1 
ATOM   23883 O  O   . ALA   B 1 1235 ? 23.23800   10.28900  -16.11000 1.000 94.08583  ?  1233 ALA   B O   1 
ATOM   23884 C  CB  . ALA   B 1 1235 ? 23.01600   13.65600  -15.51100 1.000 96.25381  ?  1233 ALA   B CB  1 
ATOM   23885 N  N   . THR   B 1 1236 ? 23.95400   11.12200  -14.15200 1.000 100.06245 ?  1234 THR   B N   1 
ATOM   23886 C  CA  . THR   B 1 1236 ? 24.88700   10.02700  -13.91500 1.000 101.75063 ?  1234 THR   B CA  1 
ATOM   23887 C  C   . THR   B 1 1236 ? 24.47000   9.25300   -12.67000 1.000 106.11502 ?  1234 THR   B C   1 
ATOM   23888 O  O   . THR   B 1 1236 ? 25.04700   9.45000   -11.59400 1.000 111.36928 ?  1234 THR   B O   1 
ATOM   23889 C  CB  . THR   B 1 1236 ? 26.31600   10.55000  -13.75900 1.000 95.25478  ?  1234 THR   B CB  1 
ATOM   23890 O  OG1 . THR   B 1 1236 ? 26.31200   11.71100  -12.92000 1.000 112.43915 ?  1234 THR   B OG1 1 
ATOM   23891 C  CG2 . THR   B 1 1236 ? 26.90700   10.91000  -15.11500 1.000 95.81315  ?  1234 THR   B CG2 1 
ATOM   23892 N  N   . PRO   B 1 1237 ? 23.47800   8.36400   -12.77500 1.000 104.78422 ?  1235 PRO   B N   1 
ATOM   23893 C  CA  . PRO   B 1 1237 ? 23.00100   7.65800   -11.57600 1.000 99.84390  ?  1235 PRO   B CA  1 
ATOM   23894 C  C   . PRO   B 1 1237 ? 23.94400   6.57700   -11.08800 1.000 97.12402  ?  1235 PRO   B C   1 
ATOM   23895 O  O   . PRO   B 1 1237 ? 23.82300   6.15400   -9.93100  1.000 95.60394  ?  1235 PRO   B O   1 
ATOM   23896 C  CB  . PRO   B 1 1237 ? 21.66300   7.06500   -12.03200 1.000 104.97543 ?  1235 PRO   B CB  1 
ATOM   23897 C  CG  . PRO   B 1 1237 ? 21.84800   6.84500   -13.49500 1.000 109.99707 ?  1235 PRO   B CG  1 
ATOM   23898 C  CD  . PRO   B 1 1237 ? 22.74300   7.95700   -13.98600 1.000 107.75014 ?  1235 PRO   B CD  1 
ATOM   23899 N  N   . ASP   B 1 1238 ? 24.87600   6.11800   -11.91900 1.000 94.20545  ?  1236 ASP   B N   1 
ATOM   23900 C  CA  . ASP   B 1 1238 ? 25.77100   5.03100   -11.55000 1.000 102.65672 ?  1236 ASP   B CA  1 
ATOM   23901 C  C   . ASP   B 1 1238 ? 27.21400   5.49000   -11.38600 1.000 99.05135  ?  1236 ASP   B C   1 
ATOM   23902 O  O   . ASP   B 1 1238 ? 28.11900   4.65100   -11.33100 1.000 87.04599  ?  1236 ASP   B O   1 
ATOM   23903 C  CB  . ASP   B 1 1238 ? 25.67700   3.90500   -12.58100 1.000 104.84019 ?  1236 ASP   B CB  1 
ATOM   23904 C  CG  . ASP   B 1 1238 ? 24.30200   3.25700   -12.60700 1.000 109.62096 ?  1236 ASP   B CG  1 
ATOM   23905 O  OD1 . ASP   B 1 1238 ? 23.82100   2.83600   -11.53300 1.000 101.31881 ?  1236 ASP   B OD1 1 
ATOM   23906 O  OD2 . ASP   B 1 1238 ? 23.69900   3.17800   -13.69800 1.000 105.04538 -1 1236 ASP   B OD2 1 
ATOM   23907 N  N   . LYS   B 1 1239 ? 27.44900   6.79700   -11.30700 1.000 103.78321 ?  1237 LYS   B N   1 
ATOM   23908 C  CA  . LYS   B 1 1239 ? 28.77100   7.32600   -11.00500 1.000 100.42568 ?  1237 LYS   B CA  1 
ATOM   23909 C  C   . LYS   B 1 1239 ? 28.97100   7.35700   -9.49600  1.000 97.70989  ?  1237 LYS   B C   1 
ATOM   23910 O  O   . LYS   B 1 1239 ? 28.05400   7.69700   -8.74400  1.000 87.77641  ?  1237 LYS   B O   1 
ATOM   23911 C  CB  . LYS   B 1 1239 ? 28.94100   8.72900   -11.59100 1.000 87.04261  ?  1237 LYS   B CB  1 
ATOM   23912 C  CG  . LYS   B 1 1239 ? 30.29100   8.96600   -12.24400 1.000 89.83376  ?  1237 LYS   B CG  1 
ATOM   23913 C  CD  . LYS   B 1 1239 ? 30.33700   10.31700  -12.93300 1.000 91.05724  ?  1237 LYS   B CD  1 
ATOM   23914 C  CE  . LYS   B 1 1239 ? 30.88700   11.38600  -12.00700 1.000 75.07853  ?  1237 LYS   B CE  1 
ATOM   23915 N  NZ  . LYS   B 1 1239 ? 32.28200   11.08700  -11.57500 1.000 81.26863  ?  1237 LYS   B NZ  1 
ATOM   23916 N  N   . THR   B 1 1240 ? 30.17200   6.99000   -9.05800  1.000 84.53021  ?  1238 THR   B N   1 
ATOM   23917 C  CA  . THR   B 1 1240 ? 30.44500   6.90200   -7.62900  1.000 89.68332  ?  1238 THR   B CA  1 
ATOM   23918 C  C   . THR   B 1 1240 ? 30.54800   8.29000   -7.00800  1.000 90.85144  ?  1238 THR   B C   1 
ATOM   23919 O  O   . THR   B 1 1240 ? 31.16600   9.19900   -7.57000  1.000 82.29741  ?  1238 THR   B O   1 
ATOM   23920 C  CB  . THR   B 1 1240 ? 31.73200   6.11600   -7.38000  1.000 85.22004  ?  1238 THR   B CB  1 
ATOM   23921 O  OG1 . THR   B 1 1240 ? 32.68300   6.41000   -8.41100  1.000 98.03222  ?  1238 THR   B OG1 1 
ATOM   23922 C  CG2 . THR   B 1 1240 ? 31.44400   4.62100   -7.37100  1.000 96.35345  ?  1238 THR   B CG2 1 
ATOM   23923 N  N   . ALA   B 1 1241 ? 29.93100   8.44800   -5.83700  1.000 84.86770  ?  1239 ALA   B N   1 
ATOM   23924 C  CA  . ALA   B 1 1241 ? 29.90300   9.71300   -5.11000  1.000 81.40847  ?  1239 ALA   B CA  1 
ATOM   23925 C  C   . ALA   B 1 1241 ? 30.66600   9.67600   -3.79700  1.000 74.69753  ?  1239 ALA   B C   1 
ATOM   23926 O  O   . ALA   B 1 1241 ? 31.31100   10.66300  -3.43800  1.000 82.80828  ?  1239 ALA   B O   1 
ATOM   23927 C  CB  . ALA   B 1 1241 ? 28.45500   10.13200  -4.82800  1.000 74.13363  ?  1239 ALA   B CB  1 
ATOM   23928 N  N   . LEU   B 1 1242 ? 30.60300   8.56400   -3.06600  1.000 61.77900  ?  1240 LEU   B N   1 
ATOM   23929 C  CA  . LEU   B 1 1242 ? 31.24100   8.43700   -1.76400  1.000 56.30698  ?  1240 LEU   B CA  1 
ATOM   23930 C  C   . LEU   B 1 1242 ? 32.08200   7.17100   -1.72800  1.000 58.13457  ?  1240 LEU   B C   1 
ATOM   23931 O  O   . LEU   B 1 1242 ? 31.70700   6.14800   -2.30900  1.000 58.81327  ?  1240 LEU   B O   1 
ATOM   23932 C  CB  . LEU   B 1 1242 ? 30.19900   8.40900   -0.63900  1.000 54.90143  ?  1240 LEU   B CB  1 
ATOM   23933 C  CG  . LEU   B 1 1242 ? 29.08500   9.45600   -0.70300  1.000 61.98637  ?  1240 LEU   B CG  1 
ATOM   23934 C  CD1 . LEU   B 1 1242 ? 28.09000   9.23700   0.42400   1.000 59.98463  ?  1240 LEU   B CD1 1 
ATOM   23935 C  CD2 . LEU   B 1 1242 ? 29.66100   10.86200  -0.64500  1.000 71.35910  ?  1240 LEU   B CD2 1 
ATOM   23936 N  N   . VAL   B 1 1243 ? 33.22500   7.24600   -1.05000  1.000 64.65228  ?  1241 VAL   B N   1 
ATOM   23937 C  CA  . VAL   B 1 1243 ? 34.13500   6.11600   -0.88500  1.000 57.69347  ?  1241 VAL   B CA  1 
ATOM   23938 C  C   . VAL   B 1 1243 ? 34.49200   6.05100   0.59400   1.000 64.05924  ?  1241 VAL   B C   1 
ATOM   23939 O  O   . VAL   B 1 1243 ? 35.29300   6.85600   1.08200   1.000 72.82558  ?  1241 VAL   B O   1 
ATOM   23940 C  CB  . VAL   B 1 1243 ? 35.39600   6.23700   -1.75000  1.000 59.04940  ?  1241 VAL   B CB  1 
ATOM   23941 C  CG1 . VAL   B 1 1243 ? 36.29000   5.02200   -1.55400  1.000 59.31913  ?  1241 VAL   B CG1 1 
ATOM   23942 C  CG2 . VAL   B 1 1243 ? 35.02900   6.39000   -3.22100  1.000 67.96599  ?  1241 VAL   B CG2 1 
ATOM   23943 N  N   . PHE   B 1 1244 ? 33.89800   5.10300   1.31300   1.000 67.49822  ?  1242 PHE   B N   1 
ATOM   23944 C  CA  . PHE   B 1 1244 ? 34.21300   4.86000   2.71500   1.000 67.41271  ?  1242 PHE   B CA  1 
ATOM   23945 C  C   . PHE   B 1 1244 ? 34.67800   3.41900   2.85800   1.000 83.17223  ?  1242 PHE   B C   1 
ATOM   23946 O  O   . PHE   B 1 1244 ? 33.95200   2.49200   2.48200   1.000 84.96450  ?  1242 PHE   B O   1 
ATOM   23947 C  CB  . PHE   B 1 1244 ? 33.00600   5.12700   3.61600   1.000 53.58946  ?  1242 PHE   B CB  1 
ATOM   23948 C  CG  . PHE   B 1 1244 ? 33.33700   5.14000   5.08100   1.000 56.93940  ?  1242 PHE   B CG  1 
ATOM   23949 C  CD1 . PHE   B 1 1244 ? 34.57100   5.59200   5.51800   1.000 65.73051  ?  1242 PHE   B CD1 1 
ATOM   23950 C  CD2 . PHE   B 1 1244 ? 32.42300   4.69200   6.01900   1.000 65.66908  ?  1242 PHE   B CD2 1 
ATOM   23951 C  CE1 . PHE   B 1 1244 ? 34.88500   5.60500   6.86400   1.000 61.02155  ?  1242 PHE   B CE1 1 
ATOM   23952 C  CE2 . PHE   B 1 1244 ? 32.73200   4.70200   7.36700   1.000 68.51143  ?  1242 PHE   B CE2 1 
ATOM   23953 C  CZ  . PHE   B 1 1244 ? 33.96500   5.15900   7.78900   1.000 54.31430  ?  1242 PHE   B CZ  1 
ATOM   23954 N  N   . ARG   B 1 1245 ? 35.88300   3.23600   3.40200   1.000 80.23181  ?  1243 ARG   B N   1 
ATOM   23955 C  CA  . ARG   B 1 1245 ? 36.48500   1.91500   3.54600   1.000 70.85731  ?  1243 ARG   B CA  1 
ATOM   23956 C  C   . ARG   B 1 1245 ? 36.51700   1.20000   2.20100   1.000 81.89901  ?  1243 ARG   B C   1 
ATOM   23957 O  O   . ARG   B 1 1245 ? 37.19700   1.65100   1.27300   1.000 79.66755  ?  1243 ARG   B O   1 
ATOM   23958 C  CB  . ARG   B 1 1245 ? 35.73500   1.09500   4.60300   1.000 61.95241  ?  1243 ARG   B CB  1 
ATOM   23959 C  CG  . ARG   B 1 1245 ? 36.11700   1.47300   6.03100   1.000 59.78020  ?  1243 ARG   B CG  1 
ATOM   23960 C  CD  . ARG   B 1 1245 ? 34.99600   1.23300   7.03500   1.000 75.79138  ?  1243 ARG   B CD  1 
ATOM   23961 N  NE  . ARG   B 1 1245 ? 35.29400   1.86500   8.31600   1.000 84.76462  ?  1243 ARG   B NE  1 
ATOM   23962 C  CZ  . ARG   B 1 1245 ? 34.43100   1.99200   9.31600   1.000 94.53871  ?  1243 ARG   B CZ  1 
ATOM   23963 N  NH1 . ARG   B 1 1245 ? 33.19900   1.51500   9.23200   1.000 81.51829  ?  1243 ARG   B NH1 1 
ATOM   23964 N  NH2 . ARG   B 1 1245 ? 34.81300   2.61500   10.42800  1.000 79.08205  ?  1243 ARG   B NH2 1 
ATOM   23965 N  N   . GLU   B 1 1246 ? 35.78200   0.09600   2.07400   1.000 88.84503  ?  1244 GLU   B N   1 
ATOM   23966 C  CA  . GLU   B 1 1246 ? 35.73800   -0.66300  0.83000   1.000 77.25347  ?  1244 GLU   B CA  1 
ATOM   23967 C  C   . GLU   B 1 1246 ? 34.40800   -0.50800  0.10100   1.000 67.40718  ?  1244 GLU   B C   1 
ATOM   23968 O  O   . GLU   B 1 1246 ? 34.10200   -1.29900  -0.79700  1.000 65.40715  ?  1244 GLU   B O   1 
ATOM   23969 C  CB  . GLU   B 1 1246 ? 36.03300   -2.13900  1.10100   1.000 64.51231  ?  1244 GLU   B CB  1 
ATOM   23970 C  CG  . GLU   B 1 1246 ? 37.45100   -2.40100  1.59100   1.000 73.19924  ?  1244 GLU   B CG  1 
ATOM   23971 C  CD  . GLU   B 1 1246 ? 38.50400   -2.03000  0.55900   1.000 86.84863  ?  1244 GLU   B CD  1 
ATOM   23972 O  OE1 . GLU   B 1 1246 ? 38.46200   -2.58000  -0.56100  1.000 86.90912  ?  1244 GLU   B OE1 1 
ATOM   23973 O  OE2 . GLU   B 1 1246 ? 39.37600   -1.18900  0.86900   1.000 86.56343  -1 1244 GLU   B OE2 1 
ATOM   23974 N  N   . GLN   B 1 1247 ? 33.62000   0.50000   0.45900   1.000 78.26457  ?  1245 GLN   B N   1 
ATOM   23975 C  CA  . GLN   B 1 1247 ? 32.30600   0.72300   -0.12600  1.000 77.64068  ?  1245 GLN   B CA  1 
ATOM   23976 C  C   . GLN   B 1 1247 ? 32.34800   1.87800   -1.12100  1.000 60.39259  ?  1245 GLN   B C   1 
ATOM   23977 O  O   . GLN   B 1 1247 ? 33.20700   2.76000   -1.05400  1.000 70.66288  ?  1245 GLN   B O   1 
ATOM   23978 C  CB  . GLN   B 1 1247 ? 31.27200   1.00300   0.96900   1.000 68.42147  ?  1245 GLN   B CB  1 
ATOM   23979 C  CG  . GLN   B 1 1247 ? 31.48200   0.18400   2.23800   1.000 83.51365  ?  1245 GLN   B CG  1 
ATOM   23980 C  CD  . GLN   B 1 1247 ? 30.99200   0.89500   3.48600   1.000 94.04708  ?  1245 GLN   B CD  1 
ATOM   23981 O  OE1 . GLN   B 1 1247 ? 29.97100   1.58200   3.46300   1.000 78.75223  ?  1245 GLN   B OE1 1 
ATOM   23982 N  NE2 . GLN   B 1 1247 ? 31.72400   0.73600   4.58500   1.000 83.20675  ?  1245 GLN   B NE2 1 
ATOM   23983 N  N   . ARG   B 1 1248 ? 31.39800   1.86000   -2.05700  1.000 57.18267  ?  1246 ARG   B N   1 
ATOM   23984 C  CA  . ARG   B 1 1248 ? 31.30300   2.88400   -3.10000  1.000 54.82017  ?  1246 ARG   B CA  1 
ATOM   23985 C  C   . ARG   B 1 1248 ? 29.82700   3.19800   -3.33000  1.000 65.31011  ?  1246 ARG   B C   1 
ATOM   23986 O  O   . ARG   B 1 1248 ? 29.11700   2.42800   -3.98300  1.000 77.42254  ?  1246 ARG   B O   1 
ATOM   23987 C  CB  . ARG   B 1 1248 ? 31.97900   2.42600   -4.38700  1.000 57.41230  ?  1246 ARG   B CB  1 
ATOM   23988 C  CG  . ARG   B 1 1248 ? 33.49500   2.53500   -4.36300  1.000 67.68313  ?  1246 ARG   B CG  1 
ATOM   23989 C  CD  . ARG   B 1 1248 ? 34.10200   2.19300   -5.71500  1.000 68.52713  ?  1246 ARG   B CD  1 
ATOM   23990 N  NE  . ARG   B 1 1248 ? 35.37600   2.87100   -5.92600  1.000 90.89355  ?  1246 ARG   B NE  1 
ATOM   23991 C  CZ  . ARG   B 1 1248 ? 35.59100   3.80400   -6.84400  1.000 92.24598  ?  1246 ARG   B CZ  1 
ATOM   23992 N  NH1 . ARG   B 1 1248 ? 34.63500   4.19100   -7.67300  1.000 88.70064  ?  1246 ARG   B NH1 1 
ATOM   23993 N  NH2 . ARG   B 1 1248 ? 36.79600   4.35800   -6.93700  1.000 74.66249  ?  1246 ARG   B NH2 1 
ATOM   23994 N  N   . VAL   B 1 1249 ? 29.37400   4.33300   -2.80100  1.000 60.55395  ?  1247 VAL   B N   1 
ATOM   23995 C  CA  . VAL   B 1 1249 ? 27.99200   4.77400   -2.95200  1.000 52.07496  ?  1247 VAL   B CA  1 
ATOM   23996 C  C   . VAL   B 1 1249 ? 27.88200   5.64200   -4.19800  1.000 59.82871  ?  1247 VAL   B C   1 
ATOM   23997 O  O   . VAL   B 1 1249 ? 28.64900   6.59600   -4.37300  1.000 72.16938  ?  1247 VAL   B O   1 
ATOM   23998 C  CB  . VAL   B 1 1249 ? 27.52300   5.54100   -1.70500  1.000 53.01456  ?  1247 VAL   B CB  1 
ATOM   23999 C  CG1 . VAL   B 1 1249 ? 26.00700   5.69600   -1.71100  1.000 57.52809  ?  1247 VAL   B CG1 1 
ATOM   24000 C  CG2 . VAL   B 1 1249 ? 27.99800   4.83800   -0.44200  1.000 53.89524  ?  1247 VAL   B CG2 1 
ATOM   24001 N  N   . THR   B 1 1250 ? 26.92500   5.31700   -5.06400  1.000 65.54420  ?  1248 THR   B N   1 
ATOM   24002 C  CA  . THR   B 1 1250 ? 26.73200   6.07300   -6.29000  1.000 73.80143  ?  1248 THR   B CA  1 
ATOM   24003 C  C   . THR   B 1 1250 ? 25.83700   7.28600   -6.03900  1.000 76.45136  ?  1248 THR   B C   1 
ATOM   24004 O  O   . THR   B 1 1250 ? 25.29600   7.48200   -4.94700  1.000 74.74817  ?  1248 THR   B O   1 
ATOM   24005 C  CB  . THR   B 1 1250 ? 26.13200   5.18700   -7.38200  1.000 82.87901  ?  1248 THR   B CB  1 
ATOM   24006 O  OG1 . THR   B 1 1250 ? 24.71000   5.11000   -7.21300  1.000 80.67017  ?  1248 THR   B OG1 1 
ATOM   24007 C  CG2 . THR   B 1 1250 ? 26.72500   3.78600   -7.31700  1.000 75.77631  ?  1248 THR   B CG2 1 
ATOM   24008 N  N   . TYR   B 1 1251 ? 25.68900   8.11300   -7.07700  1.000 72.45715  ?  1249 TYR   B N   1 
ATOM   24009 C  CA  . TYR   B 1 1251 ? 24.84800   9.30100   -6.96600  1.000 69.00026  ?  1249 TYR   B CA  1 
ATOM   24010 C  C   . TYR   B 1 1251 ? 23.39600   8.92100   -6.70300  1.000 75.84546  ?  1249 TYR   B C   1 
ATOM   24011 O  O   . TYR   B 1 1251 ? 22.73300   9.50700   -5.83900  1.000 71.31070  ?  1249 TYR   B O   1 
ATOM   24012 C  CB  . TYR   B 1 1251 ? 24.96000   10.14700  -8.23500  1.000 76.03809  ?  1249 TYR   B CB  1 
ATOM   24013 C  CG  . TYR   B 1 1251 ? 26.15100   11.08300  -8.26100  1.000 89.19070  ?  1249 TYR   B CG  1 
ATOM   24014 C  CD1 . TYR   B 1 1251 ? 27.44400   10.60200  -8.10500  1.000 78.84997  ?  1249 TYR   B CD1 1 
ATOM   24015 C  CD2 . TYR   B 1 1251 ? 25.98000   12.44800  -8.44600  1.000 83.62400  ?  1249 TYR   B CD2 1 
ATOM   24016 C  CE1 . TYR   B 1 1251 ? 28.53500   11.45500  -8.13100  1.000 81.00505  ?  1249 TYR   B CE1 1 
ATOM   24017 C  CE2 . TYR   B 1 1251 ? 27.06400   13.30800  -8.47300  1.000 90.98133  ?  1249 TYR   B CE2 1 
ATOM   24018 C  CZ  . TYR   B 1 1251 ? 28.33800   12.80700  -8.31500  1.000 87.57747  ?  1249 TYR   B CZ  1 
ATOM   24019 O  OH  . TYR   B 1 1251 ? 29.41700   13.66300  -8.34100  1.000 82.73170  ?  1249 TYR   B OH  1 
ATOM   24020 N  N   . ARG   B 1 1252 ? 22.88400   7.93400   -7.44300  1.000 84.91490  ?  1250 ARG   B N   1 
ATOM   24021 C  CA  . ARG   B 1 1252 ? 21.50000   7.51200   -7.25200  1.000 81.94237  ?  1250 ARG   B CA  1 
ATOM   24022 C  C   . ARG   B 1 1252 ? 21.31400   6.83200   -5.90300  1.000 71.15814  ?  1250 ARG   B C   1 
ATOM   24023 O  O   . ARG   B 1 1252 ? 20.32500   7.08800   -5.20400  1.000 66.87862  ?  1250 ARG   B O   1 
ATOM   24024 C  CB  . ARG   B 1 1252 ? 21.07400   6.57900   -8.38500  1.000 86.76534  ?  1250 ARG   B CB  1 
ATOM   24025 C  CG  . ARG   B 1 1252 ? 19.58200   6.59200   -8.67800  1.000 89.45472  ?  1250 ARG   B CG  1 
ATOM   24026 C  CD  . ARG   B 1 1252 ? 19.11700   5.25000   -9.23100  1.000 74.87114  ?  1250 ARG   B CD  1 
ATOM   24027 N  NE  . ARG   B 1 1252 ? 18.66300   4.35000   -8.17600  1.000 84.88017  ?  1250 ARG   B NE  1 
ATOM   24028 C  CZ  . ARG   B 1 1252 ? 19.31400   3.26100   -7.78800  1.000 91.86085  ?  1250 ARG   B CZ  1 
ATOM   24029 N  NH1 . ARG   B 1 1252 ? 20.45900   2.90300   -8.34600  1.000 90.19691  ?  1250 ARG   B NH1 1 
ATOM   24030 N  NH2 . ARG   B 1 1252 ? 18.80400   2.51400   -6.81200  1.000 74.94054  ?  1250 ARG   B NH2 1 
ATOM   24031 N  N   . GLU   B 1 1253 ? 22.24900   5.95600   -5.52400  1.000 67.37832  ?  1251 GLU   B N   1 
ATOM   24032 C  CA  . GLU   B 1 1253 ? 22.18300   5.33100   -4.20800  1.000 65.88106  ?  1251 GLU   B CA  1 
ATOM   24033 C  C   . GLU   B 1 1253 ? 22.23600   6.37800   -3.11000  1.000 72.65794  ?  1251 GLU   B C   1 
ATOM   24034 O  O   . GLU   B 1 1253 ? 21.47400   6.30900   -2.13900  1.000 75.43092  ?  1251 GLU   B O   1 
ATOM   24035 C  CB  . GLU   B 1 1253 ? 23.32400   4.33300   -4.02600  1.000 67.74565  ?  1251 GLU   B CB  1 
ATOM   24036 C  CG  . GLU   B 1 1253 ? 23.30700   3.16400   -4.98200  1.000 73.10745  ?  1251 GLU   B CG  1 
ATOM   24037 C  CD  . GLU   B 1 1253 ? 24.50700   2.25700   -4.79500  1.000 88.91157  ?  1251 GLU   B CD  1 
ATOM   24038 O  OE1 . GLU   B 1 1253 ? 25.41200   2.62000   -4.01200  1.000 78.37990  ?  1251 GLU   B OE1 1 
ATOM   24039 O  OE2 . GLU   B 1 1253 ? 24.54600   1.18100   -5.42700  1.000 96.56331  -1 1251 GLU   B OE2 1 
ATOM   24040 N  N   . LEU   B 1 1254 ? 23.13700   7.35000   -3.23900  1.000 69.08681  ?  1252 LEU   B N   1 
ATOM   24041 C  CA  . LEU   B 1 1254 ? 23.16000   8.43800   -2.27400  1.000 67.73318  ?  1252 LEU   B CA  1 
ATOM   24042 C  C   . LEU   B 1 1254 ? 21.81000   9.14600   -2.24600  1.000 70.46521  ?  1252 LEU   B C   1 
ATOM   24043 O  O   . LEU   B 1 1254 ? 21.07700   9.06600   -1.25200  1.000 70.93300  ?  1252 LEU   B O   1 
ATOM   24044 C  CB  . LEU   B 1 1254 ? 24.30400   9.40200   -2.60200  1.000 66.06132  ?  1252 LEU   B CB  1 
ATOM   24045 C  CG  . LEU   B 1 1254 ? 24.45000   10.66100  -1.74100  1.000 61.62731  ?  1252 LEU   B CG  1 
ATOM   24046 C  CD1 . LEU   B 1 1254 ? 24.57900   10.31200  -0.25300  1.000 53.31922  ?  1252 LEU   B CD1 1 
ATOM   24047 C  CD2 . LEU   B 1 1254 ? 25.65100   11.48400  -2.19000  1.000 57.23419  ?  1252 LEU   B CD2 1 
ATOM   24048 N  N   . ASN   B 1 1255 ? 21.43600   9.77900   -3.36800  1.000 58.14038  ?  1253 ASN   B N   1 
ATOM   24049 C  CA  . ASN   B 1 1255 ? 20.19700   10.55300  -3.44200  1.000 68.49228  ?  1253 ASN   B CA  1 
ATOM   24050 C  C   . ASN   B 1 1255 ? 19.01100   9.80700   -2.83700  1.000 70.77335  ?  1253 ASN   B C   1 
ATOM   24051 O  O   . ASN   B 1 1255 ? 18.22000   10.39500  -2.09100  1.000 65.10165  ?  1253 ASN   B O   1 
ATOM   24052 C  CB  . ASN   B 1 1255 ? 19.89900   10.92700  -4.89600  1.000 67.83206  ?  1253 ASN   B CB  1 
ATOM   24053 C  CG  . ASN   B 1 1255 ? 18.86100   12.03200  -5.01200  1.000 83.63010  ?  1253 ASN   B CG  1 
ATOM   24054 O  OD1 . ASN   B 1 1255 ? 18.74600   12.88500  -4.13200  1.000 84.97180  ?  1253 ASN   B OD1 1 
ATOM   24055 N  ND2 . ASN   B 1 1255 ? 18.09900   12.02000  -6.10000  1.000 81.73013  ?  1253 ASN   B ND2 1 
ATOM   24056 N  N   . GLU   B 1 1256 ? 18.88700   8.50700   -3.11800  1.000 64.94575  ?  1254 GLU   B N   1 
ATOM   24057 C  CA  . GLU   B 1 1256 ? 17.75900   7.74000   -2.59300  1.000 66.44289  ?  1254 GLU   B CA  1 
ATOM   24058 C  C   . GLU   B 1 1256 ? 17.81300   7.64200   -1.07100  1.000 61.82741  ?  1254 GLU   B C   1 
ATOM   24059 O  O   . GLU   B 1 1256 ? 16.83800   7.96700   -0.38300  1.000 66.73771  ?  1254 GLU   B O   1 
ATOM   24060 C  CB  . GLU   B 1 1256 ? 17.73400   6.34500   -3.22000  1.000 64.70270  ?  1254 GLU   B CB  1 
ATOM   24061 N  N   . ARG   B 1 1257 ? 18.94600   7.18300   -0.52900  1.000 56.83299  ?  1255 ARG   B N   1 
ATOM   24062 C  CA  . ARG   B 1 1257 ? 19.08000   7.06500   0.92000   1.000 66.84900  ?  1255 ARG   B CA  1 
ATOM   24063 C  C   . ARG   B 1 1257 ? 18.87100   8.40900   1.60200   1.000 68.98721  ?  1255 ARG   B C   1 
ATOM   24064 O  O   . ARG   B 1 1257 ? 18.29000   8.47700   2.69200   1.000 66.29334  ?  1255 ARG   B O   1 
ATOM   24065 C  CB  . ARG   B 1 1257 ? 20.45200   6.49400   1.28300   1.000 61.12469  ?  1255 ARG   B CB  1 
ATOM   24066 C  CG  . ARG   B 1 1257 ? 20.51400   4.97400   1.28800   1.000 75.55356  ?  1255 ARG   B CG  1 
ATOM   24067 C  CD  . ARG   B 1 1257 ? 21.88300   4.47100   0.84400   1.000 73.24815  ?  1255 ARG   B CD  1 
ATOM   24068 N  NE  . ARG   B 1 1257 ? 22.73200   4.11700   1.97700   1.000 90.65029  ?  1255 ARG   B NE  1 
ATOM   24069 C  CZ  . ARG   B 1 1257 ? 23.88600   3.47000   1.87800   1.000 77.78206  ?  1255 ARG   B CZ  1 
ATOM   24070 N  NH1 . ARG   B 1 1257 ? 24.36900   3.09000   0.70600   1.000 66.78968  ?  1255 ARG   B NH1 1 
ATOM   24071 N  NH2 . ARG   B 1 1257 ? 24.57500   3.20000   2.98400   1.000 66.78128  ?  1255 ARG   B NH2 1 
ATOM   24072 N  N   . VAL   B 1 1258 ? 19.34400   9.49000   0.97700   1.000 70.38494  ?  1256 VAL   B N   1 
ATOM   24073 C  CA  . VAL   B 1 1258 ? 19.05400   10.82100  1.49800   1.000 67.61432  ?  1256 VAL   B CA  1 
ATOM   24074 C  C   . VAL   B 1 1258 ? 17.55700   11.08400  1.51500   1.000 63.28847  ?  1256 VAL   B C   1 
ATOM   24075 O  O   . VAL   B 1 1258 ? 17.02400   11.64200  2.48300   1.000 61.79271  ?  1256 VAL   B O   1 
ATOM   24076 C  CB  . VAL   B 1 1258 ? 19.80200   11.90100  0.70100   1.000 70.44084  ?  1256 VAL   B CB  1 
ATOM   24077 C  CG1 . VAL   B 1 1258 ? 19.72900   13.15000  1.47700   1.000 71.98555  ?  1256 VAL   B CG1 1 
ATOM   24078 C  CG2 . VAL   B 1 1258 ? 21.27500   11.53900  0.57500   1.000 56.49935  ?  1256 VAL   B CG2 1 
ATOM   24079 N  N   . ASN   B 1 1259 ? 16.86100   10.70000  0.44300   1.000 60.57686  ?  1257 ASN   B N   1 
ATOM   24080 C  CA  . ASN   B 1 1259 ? 15.42300   10.93300  0.36900   1.000 64.39817  ?  1257 ASN   B CA  1 
ATOM   24081 C  C   . ASN   B 1 1259 ? 14.68800   10.20400  1.48500   1.000 59.93552  ?  1257 ASN   B C   1 
ATOM   24082 O  O   . ASN   B 1 1259 ? 13.76800   10.76100  2.09600   1.000 68.68926  ?  1257 ASN   B O   1 
ATOM   24083 C  CB  . ASN   B 1 1259 ? 14.88900   10.49400  -0.99400  1.000 57.72059  ?  1257 ASN   B CB  1 
ATOM   24084 C  CG  . ASN   B 1 1259 ? 15.45500   11.31300  -2.13900  1.000 71.23796  ?  1257 ASN   B CG  1 
ATOM   24085 O  OD1 . ASN   B 1 1259 ? 15.79600   12.48300  -1.97500  1.000 75.04333  ?  1257 ASN   B OD1 1 
ATOM   24086 N  ND2 . ASN   B 1 1259 ? 15.56000   10.69600  -3.30900  1.000 73.89338  ?  1257 ASN   B ND2 1 
ATOM   24087 N  N   . GLN   B 1 1260 ? 15.08200   8.95900   1.76700   1.000 61.79706  ?  1258 GLN   B N   1 
ATOM   24088 C  CA  . GLN   B 1 1260 ? 14.41200   8.17900   2.80600   1.000 62.16105  ?  1258 GLN   B CA  1 
ATOM   24089 C  C   . GLN   B 1 1260 ? 14.49400   8.87800   4.15700   1.000 64.44706  ?  1258 GLN   B C   1 
ATOM   24090 O  O   . GLN   B 1 1260 ? 13.49100   9.00400   4.86800   1.000 58.46613  ?  1258 GLN   B O   1 
ATOM   24091 C  CB  . GLN   B 1 1260 ? 15.02300   6.78100   2.88800   1.000 65.97505  ?  1258 GLN   B CB  1 
ATOM   24092 C  CG  . GLN   B 1 1260 ? 15.07200   6.03800   1.56500   1.000 66.97844  ?  1258 GLN   B CG  1 
ATOM   24093 C  CD  . GLN   B 1 1260 ? 15.72100   4.67500   1.69700   1.000 63.57458  ?  1258 GLN   B CD  1 
ATOM   24094 O  OE1 . GLN   B 1 1260 ? 15.54200   3.98800   2.70200   1.000 68.69866  ?  1258 GLN   B OE1 1 
ATOM   24095 N  NE2 . GLN   B 1 1260 ? 16.48400   4.27900   0.68400   1.000 65.18978  ?  1258 GLN   B NE2 1 
ATOM   24096 N  N   . LEU   B 1 1261 ? 15.68900   9.33800   4.53100   1.000 69.88859  ?  1259 LEU   B N   1 
ATOM   24097 C  CA  . LEU   B 1 1261 ? 15.82600   10.09900  5.76600   1.000 66.45186  ?  1259 LEU   B CA  1 
ATOM   24098 C  C   . LEU   B 1 1261 ? 15.17500   11.47200  5.65000   1.000 70.51874  ?  1259 LEU   B C   1 
ATOM   24099 O  O   . LEU   B 1 1261 ? 14.68200   12.01000  6.64900   1.000 61.22971  ?  1259 LEU   B O   1 
ATOM   24100 C  CB  . LEU   B 1 1261 ? 17.30200   10.23200  6.13400   1.000 59.36914  ?  1259 LEU   B CB  1 
ATOM   24101 C  CG  . LEU   B 1 1261 ? 17.61500   10.77300  7.52900   1.000 72.27903  ?  1259 LEU   B CG  1 
ATOM   24102 C  CD1 . LEU   B 1 1261 ? 16.88000   9.98600   8.60700   1.000 59.07967  ?  1259 LEU   B CD1 1 
ATOM   24103 C  CD2 . LEU   B 1 1261 ? 19.11400   10.76100  7.77000   1.000 63.80428  ?  1259 LEU   B CD2 1 
ATOM   24104 N  N   . ALA   B 1 1262 ? 15.15800   12.04800  4.44400   1.000 63.29350  ?  1260 ALA   B N   1 
ATOM   24105 C  CA  . ALA   B 1 1262 ? 14.53400   13.35300  4.24700   1.000 63.70132  ?  1260 ALA   B CA  1 
ATOM   24106 C  C   . ALA   B 1 1262 ? 13.03800   13.29300  4.52100   1.000 76.74149  ?  1260 ALA   B C   1 
ATOM   24107 O  O   . ALA   B 1 1262 ? 12.50400   14.10300  5.28900   1.000 76.23697  ?  1260 ALA   B O   1 
ATOM   24108 C  CB  . ALA   B 1 1262 ? 14.80000   13.85500  2.82800   1.000 66.58045  ?  1260 ALA   B CB  1 
ATOM   24109 N  N   . HIS   B 1 1263 ? 12.34100   12.34500  3.88500   1.000 75.04255  ?  1261 HIS   B N   1 
ATOM   24110 C  CA  . HIS   B 1 1263 ? 10.91800   12.16200  4.15200   1.000 64.71363  ?  1261 HIS   B CA  1 
ATOM   24111 C  C   . HIS   B 1 1263 ? 10.66100   11.95600  5.63900   1.000 61.67627  ?  1261 HIS   B C   1 
ATOM   24112 O  O   . HIS   B 1 1263 ? 9.71100    12.51700  6.19500   1.000 56.82861  ?  1261 HIS   B O   1 
ATOM   24113 C  CB  . HIS   B 1 1263 ? 10.37000   10.98000  3.34800   1.000 58.01163  ?  1261 HIS   B CB  1 
ATOM   24114 C  CG  . HIS   B 1 1263 ? 10.45100   11.16600  1.86400   1.000 68.62725  ?  1261 HIS   B CG  1 
ATOM   24115 N  ND1 . HIS   B 1 1263 ? 9.90300    12.25500  1.22000   1.000 75.86238  ?  1261 HIS   B ND1 1 
ATOM   24116 C  CD2 . HIS   B 1 1263 ? 11.01000   10.39900  0.89800   1.000 67.49279  ?  1261 HIS   B CD2 1 
ATOM   24117 C  CE1 . HIS   B 1 1263 ? 10.12700   12.15300  -0.07900  1.000 79.75353  ?  1261 HIS   B CE1 1 
ATOM   24118 N  NE2 . HIS   B 1 1263 ? 10.79700   11.03700  -0.30000  1.000 60.25183  ?  1261 HIS   B NE2 1 
ATOM   24119 N  N   . THR   B 1 1264 ? 11.50900   11.16600  6.30400   1.000 60.31046  ?  1262 THR   B N   1 
ATOM   24120 C  CA  . THR   B 1 1264 ? 11.35000   10.95500  7.74000   1.000 63.92931  ?  1262 THR   B CA  1 
ATOM   24121 C  C   . THR   B 1 1264 ? 11.40500   12.27800  8.49600   1.000 67.81996  ?  1262 THR   B C   1 
ATOM   24122 O  O   . THR   B 1 1264 ? 10.52100   12.57900  9.30400   1.000 57.30018  ?  1262 THR   B O   1 
ATOM   24123 C  CB  . THR   B 1 1264 ? 12.42000   9.99500   8.26200   1.000 65.90957  ?  1262 THR   B CB  1 
ATOM   24124 O  OG1 . THR   B 1 1264 ? 12.40000   8.78400   7.49600   1.000 68.85324  ?  1262 THR   B OG1 1 
ATOM   24125 C  CG2 . THR   B 1 1264 ? 12.16900   9.66500   9.73200   1.000 49.37593  ?  1262 THR   B CG2 1 
ATOM   24126 N  N   . LEU   B 1 1265 ? 12.42800   13.09300  8.22000   1.000 78.35416  ?  1263 LEU   B N   1 
ATOM   24127 C  CA  . LEU   B 1 1265 ? 12.60800   14.35400  8.93800   1.000 69.42827  ?  1263 LEU   B CA  1 
ATOM   24128 C  C   . LEU   B 1 1265 ? 11.40500   15.27600  8.76700   1.000 73.58935  ?  1263 LEU   B C   1 
ATOM   24129 O  O   . LEU   B 1 1265 ? 10.93600   15.88300  9.73800   1.000 68.14742  ?  1263 LEU   B O   1 
ATOM   24130 C  CB  . LEU   B 1 1265 ? 13.88300   15.04300  8.45300   1.000 57.01313  ?  1263 LEU   B CB  1 
ATOM   24131 C  CG  . LEU   B 1 1265 ? 15.19500   14.50300  9.02500   1.000 80.05500  ?  1263 LEU   B CG  1 
ATOM   24132 C  CD1 . LEU   B 1 1265 ? 16.37800   14.96000  8.18200   1.000 68.03954  ?  1263 LEU   B CD1 1 
ATOM   24133 C  CD2 . LEU   B 1 1265 ? 15.36400   14.93100  10.46900  1.000 74.61203  ?  1263 LEU   B CD2 1 
ATOM   24134 N  N   . ARG   B 1 1266 ? 10.89700   15.39700  7.53800   1.000 71.18224  ?  1264 ARG   B N   1 
ATOM   24135 C  CA  . ARG   B 1 1266 ? 9.71500    16.21700  7.28600   1.000 69.93165  ?  1264 ARG   B CA  1 
ATOM   24136 C  C   . ARG   B 1 1266 ? 8.52800    15.74700  8.11400   1.000 77.22249  ?  1264 ARG   B C   1 
ATOM   24137 O  O   . ARG   B 1 1266 ? 7.85600    16.55000  8.77300   1.000 67.46619  ?  1264 ARG   B O   1 
ATOM   24138 C  CB  . ARG   B 1 1266 ? 9.36200    16.17500  5.80400   1.000 48.47712  ?  1264 ARG   B CB  1 
ATOM   24139 C  CG  . ARG   B 1 1266 ? 10.29000   16.94300  4.91000   1.000 64.50083  ?  1264 ARG   B CG  1 
ATOM   24140 C  CD  . ARG   B 1 1266 ? 9.64100    17.09900  3.56500   1.000 69.07238  ?  1264 ARG   B CD  1 
ATOM   24141 N  NE  . ARG   B 1 1266 ? 10.29900   18.10700  2.75000   1.000 82.69268  ?  1264 ARG   B NE  1 
ATOM   24142 C  CZ  . ARG   B 1 1266 ? 9.72300    18.71200  1.72400   1.000 83.92583  ?  1264 ARG   B CZ  1 
ATOM   24143 N  NH1 . ARG   B 1 1266 ? 8.46300    18.47000  1.39900   1.000 85.01387  ?  1264 ARG   B NH1 1 
ATOM   24144 N  NH2 . ARG   B 1 1266 ? 10.42200   19.58900  1.01500   1.000 73.52974  ?  1264 ARG   B NH2 1 
ATOM   24145 N  N   . GLU   B 1 1267 ? 8.24500    14.44200  8.07900   1.000 67.72011  ?  1265 GLU   B N   1 
ATOM   24146 C  CA  . GLU   B 1 1267 ? 7.15700    13.86700  8.86000   1.000 62.50873  ?  1265 GLU   B CA  1 
ATOM   24147 C  C   . GLU   B 1 1267 ? 7.31400    14.10900  10.35800  1.000 69.27519  ?  1265 GLU   B C   1 
ATOM   24148 O  O   . GLU   B 1 1267 ? 6.36100    13.86900  11.10900  1.000 70.37839  ?  1265 GLU   B O   1 
ATOM   24149 C  CB  . GLU   B 1 1267 ? 7.05400    12.36800  8.55800   1.000 71.68368  ?  1265 GLU   B CB  1 
ATOM   24150 C  CG  . GLU   B 1 1267 ? 5.96500    11.97800  7.54000   1.000 85.87685  ?  1265 GLU   B CG  1 
ATOM   24151 C  CD  . GLU   B 1 1267 ? 6.35400    12.22200  6.08000   1.000 103.58987 ?  1265 GLU   B CD  1 
ATOM   24152 O  OE1 . GLU   B 1 1267 ? 7.21300    13.08900  5.80700   1.000 83.35553  ?  1265 GLU   B OE1 1 
ATOM   24153 O  OE2 . GLU   B 1 1267 ? 5.79800    11.52900  5.19800   1.000 94.58266  -1 1265 GLU   B OE2 1 
ATOM   24154 N  N   . LYS   B 1 1268 ? 8.48000    14.57500  10.80600  1.000 69.62016  ?  1266 LYS   B N   1 
ATOM   24155 C  CA  . LYS   B 1 1268 ? 8.68500    15.01500  12.17900  1.000 70.55348  ?  1266 LYS   B CA  1 
ATOM   24156 C  C   . LYS   B 1 1268 ? 8.61100    16.53200  12.32200  1.000 72.52896  ?  1266 LYS   B C   1 
ATOM   24157 O  O   . LYS   B 1 1268 ? 8.95700    17.06000  13.38500  1.000 68.47240  ?  1266 LYS   B O   1 
ATOM   24158 C  CB  . LYS   B 1 1268 ? 10.03100   14.51300  12.70900  1.000 79.80850  ?  1266 LYS   B CB  1 
ATOM   24159 C  CG  . LYS   B 1 1268 ? 10.41600   13.11900  12.24800  1.000 67.16637  ?  1266 LYS   B CG  1 
ATOM   24160 C  CD  . LYS   B 1 1268 ? 9.55200    12.05400  12.89300  1.000 75.43365  ?  1266 LYS   B CD  1 
ATOM   24161 C  CE  . LYS   B 1 1268 ? 10.28700   11.37900  14.03700  1.000 72.51416  ?  1266 LYS   B CE  1 
ATOM   24162 N  NZ  . LYS   B 1 1268 ? 9.36100    11.00900  15.14000  1.000 77.27915  ?  1266 LYS   B NZ  1 
ATOM   24163 N  N   . GLY   B 1 1269 ? 8.18500    17.24100  11.27900  1.000 67.90559  ?  1267 GLY   B N   1 
ATOM   24164 C  CA  . GLY   B 1 1269 ? 8.01200    18.68000  11.35300  1.000 77.65659  ?  1267 GLY   B CA  1 
ATOM   24165 C  C   . GLY   B 1 1269 ? 9.27000    19.47800  11.07200  1.000 90.61996  ?  1267 GLY   B C   1 
ATOM   24166 O  O   . GLY   B 1 1269 ? 9.80900    20.13300  11.97000  1.000 99.42375  ?  1267 GLY   B O   1 
ATOM   24167 N  N   . VAL   B 1 1270 ? 9.74900    19.43400  9.83100   1.000 79.65328  ?  1268 VAL   B N   1 
ATOM   24168 C  CA  . VAL   B 1 1270 ? 10.91900   20.19500  9.40800   1.000 79.98403  ?  1268 VAL   B CA  1 
ATOM   24169 C  C   . VAL   B 1 1270 ? 10.46100   21.18200  8.34300   1.000 84.19222  ?  1268 VAL   B C   1 
ATOM   24170 O  O   . VAL   B 1 1270 ? 10.09100   20.78500  7.23000   1.000 68.52567  ?  1268 VAL   B O   1 
ATOM   24171 C  CB  . VAL   B 1 1270 ? 12.04900   19.29500  8.88700   1.000 76.52832  ?  1268 VAL   B CB  1 
ATOM   24172 C  CG1 . VAL   B 1 1270 ? 13.08400   20.12200  8.13500   1.000 56.13863  ?  1268 VAL   B CG1 1 
ATOM   24173 C  CG2 . VAL   B 1 1270 ? 12.71400   18.55700  10.04100  1.000 61.39542  ?  1268 VAL   B CG2 1 
ATOM   24174 N  N   . GLN   B 1 1271 ? 10.46500   22.46300  8.69400   1.000 94.00547  ?  1269 GLN   B N   1 
ATOM   24175 C  CA  . GLN   B 1 1271 ? 10.18000   23.55800  7.77900   1.000 91.43375  ?  1269 GLN   B CA  1 
ATOM   24176 C  C   . GLN   B 1 1271 ? 11.43700   24.41700  7.68600   1.000 86.37345  ?  1269 GLN   B C   1 
ATOM   24177 O  O   . GLN   B 1 1271 ? 12.36200   24.22700  8.48700   1.000 84.33805  ?  1269 GLN   B O   1 
ATOM   24178 C  CB  . GLN   B 1 1271 ? 8.96800    24.36000  8.26300   1.000 89.18395  ?  1269 GLN   B CB  1 
ATOM   24179 C  CG  . GLN   B 1 1271 ? 7.69200    23.53500  8.40200   1.000 74.02902  ?  1269 GLN   B CG  1 
ATOM   24180 C  CD  . GLN   B 1 1271 ? 7.37800    23.17200  9.84200   1.000 93.81888  ?  1269 GLN   B CD  1 
ATOM   24181 O  OE1 . GLN   B 1 1271 ? 7.99500    23.68900  10.77400  1.000 84.66162  ?  1269 GLN   B OE1 1 
ATOM   24182 N  NE2 . GLN   B 1 1271 ? 6.41600    22.27400  10.03100  1.000 76.15506  ?  1269 GLN   B NE2 1 
ATOM   24183 N  N   . PRO   B 1 1272 ? 11.53300   25.33400  6.71900   1.000 72.39191  ?  1270 PRO   B N   1 
ATOM   24184 C  CA  . PRO   B 1 1272 ? 12.73700   26.16600  6.60600   1.000 73.44781  ?  1270 PRO   B CA  1 
ATOM   24185 C  C   . PRO   B 1 1272 ? 13.13300   26.82300  7.92500   1.000 76.05278  ?  1270 PRO   B C   1 
ATOM   24186 O  O   . PRO   B 1 1272 ? 12.28300   27.20200  8.73500   1.000 69.02026  ?  1270 PRO   B O   1 
ATOM   24187 C  CB  . PRO   B 1 1272 ? 12.33800   27.20500  5.55600   1.000 68.84842  ?  1270 PRO   B CB  1 
ATOM   24188 C  CG  . PRO   B 1 1272 ? 11.41500   26.45400  4.65300   1.000 83.59387  ?  1270 PRO   B CG  1 
ATOM   24189 C  CD  . PRO   B 1 1272 ? 10.67400   25.45900  5.52500   1.000 80.24757  ?  1270 PRO   B CD  1 
ATOM   24190 N  N   . ASP   B 1 1273 ? 14.44900   26.93000  8.13300   1.000 72.41833  ?  1271 ASP   B N   1 
ATOM   24191 C  CA  . ASP   B 1 1273 ? 15.11000   27.56100  9.27600   1.000 72.07890  ?  1271 ASP   B CA  1 
ATOM   24192 C  C   . ASP   B 1 1273 ? 14.99200   26.75400  10.56300  1.000 65.23033  ?  1271 ASP   B C   1 
ATOM   24193 O  O   . ASP   B 1 1273 ? 15.32000   27.27100  11.64200  1.000 62.02563  ?  1271 ASP   B O   1 
ATOM   24194 C  CB  . ASP   B 1 1273 ? 14.60400   28.98900  9.52300   1.000 89.62687  ?  1271 ASP   B CB  1 
ATOM   24195 C  CG  . ASP   B 1 1273 ? 15.20300   30.00100  8.55600   1.000 76.18487  ?  1271 ASP   B CG  1 
ATOM   24196 O  OD1 . ASP   B 1 1273 ? 15.82100   29.58600  7.55200   1.000 77.76509  ?  1271 ASP   B OD1 1 
ATOM   24197 O  OD2 . ASP   B 1 1273 ? 15.05700   31.21500  8.80500   1.000 71.71536  -1 1271 ASP   B OD2 1 
ATOM   24198 N  N   . ASP   B 1 1274 ? 14.54500   25.50300  10.48900  1.000 67.82679  ?  1272 ASP   B N   1 
ATOM   24199 C  CA  . ASP   B 1 1274 ? 14.51500   24.62300  11.64900  1.000 58.22749  ?  1272 ASP   B CA  1 
ATOM   24200 C  C   . ASP   B 1 1274 ? 15.86600   23.93200  11.79400  1.000 63.10844  ?  1272 ASP   B C   1 
ATOM   24201 O  O   . ASP   B 1 1274 ? 16.42400   23.43100  10.81200  1.000 61.20278  ?  1272 ASP   B O   1 
ATOM   24202 C  CB  . ASP   B 1 1274 ? 13.39600   23.58900  11.51900  1.000 64.72627  ?  1272 ASP   B CB  1 
ATOM   24203 C  CG  . ASP   B 1 1274 ? 12.04200   24.14000  11.92700  1.000 80.83800  ?  1272 ASP   B CG  1 
ATOM   24204 O  OD1 . ASP   B 1 1274 ? 11.98100   24.90800  12.91300  1.000 65.54466  ?  1272 ASP   B OD1 1 
ATOM   24205 O  OD2 . ASP   B 1 1274 ? 11.03800   23.80000  11.26600  1.000 85.25545  -1 1272 ASP   B OD2 1 
ATOM   24206 N  N   . LEU   B 1 1275 ? 16.38700   23.91000  13.01700  1.000 61.38440  ?  1273 LEU   B N   1 
ATOM   24207 C  CA  . LEU   B 1 1275 ? 17.70600   23.36000  13.30000  1.000 52.26192  ?  1273 LEU   B CA  1 
ATOM   24208 C  C   . LEU   B 1 1275 ? 17.58300   21.93600  13.82300  1.000 67.18136  ?  1273 LEU   B C   1 
ATOM   24209 O  O   . LEU   B 1 1275 ? 16.85200   21.68300  14.78700  1.000 72.70689  ?  1273 LEU   B O   1 
ATOM   24210 C  CB  . LEU   B 1 1275 ? 18.45000   24.22000  14.32100  1.000 54.43366  ?  1273 LEU   B CB  1 
ATOM   24211 C  CG  . LEU   B 1 1275 ? 18.20600   25.72600  14.26900  1.000 70.21825  ?  1273 LEU   B CG  1 
ATOM   24212 C  CD1 . LEU   B 1 1275 ? 18.80300   26.39000  15.50200  1.000 67.69485  ?  1273 LEU   B CD1 1 
ATOM   24213 C  CD2 . LEU   B 1 1275 ? 18.77600   26.32100  12.98600  1.000 69.81519  ?  1273 LEU   B CD2 1 
ATOM   24214 N  N   . VAL   B 1 1276 ? 18.31000   21.01600  13.19500  1.000 77.15973  ?  1274 VAL   B N   1 
ATOM   24215 C  CA  . VAL   B 1 1276 ? 18.40000   19.62900  13.63800  1.000 69.75109  ?  1274 VAL   B CA  1 
ATOM   24216 C  C   . VAL   B 1 1276 ? 19.85400   19.34100  13.98900  1.000 59.49238  ?  1274 VAL   B C   1 
ATOM   24217 O  O   . VAL   B 1 1276 ? 20.75600   19.56800  13.17300  1.000 59.15223  ?  1274 VAL   B O   1 
ATOM   24218 C  CB  . VAL   B 1 1276 ? 17.86600   18.65400  12.56900  1.000 66.60765  ?  1274 VAL   B CB  1 
ATOM   24219 C  CG1 . VAL   B 1 1276 ? 17.74900   19.35000  11.22300  1.000 40.11713  ?  1274 VAL   B CG1 1 
ATOM   24220 C  CG2 . VAL   B 1 1276 ? 18.72600   17.38900  12.47600  1.000 64.39049  ?  1274 VAL   B CG2 1 
ATOM   24221 N  N   . MET   B 1 1277 ? 20.07900   18.86800  15.21000  1.000 56.92605  ?  1275 MET   B N   1 
ATOM   24222 C  CA  . MET   B 1 1277 ? 21.42400   18.60000  15.69100  1.000 50.91152  ?  1275 MET   B CA  1 
ATOM   24223 C  C   . MET   B 1 1277 ? 21.93500   17.26400  15.16300  1.000 68.98280  ?  1275 MET   B C   1 
ATOM   24224 O  O   . MET   B 1 1277 ? 21.16000   16.35100  14.86500  1.000 67.06016  ?  1275 MET   B O   1 
ATOM   24225 C  CB  . MET   B 1 1277 ? 21.44400   18.60400  17.21800  1.000 47.21649  ?  1275 MET   B CB  1 
ATOM   24226 C  CG  . MET   B 1 1277 ? 20.94100   19.89700  17.82900  1.000 46.36677  ?  1275 MET   B CG  1 
ATOM   24227 S  SD  . MET   B 1 1277 ? 20.86500   19.81800  19.62700  1.000 97.15436  ?  1275 MET   B SD  1 
ATOM   24228 C  CE  . MET   B 1 1277 ? 22.51700   19.25400  20.02800  1.000 58.33672  ?  1275 MET   B CE  1 
ATOM   24229 N  N   . LEU   B 1 1278 ? 23.25900   17.15600  15.05100  1.000 58.16707  ?  1276 LEU   B N   1 
ATOM   24230 C  CA  . LEU   B 1 1278 ? 23.91900   15.95600  14.55700  1.000 49.14848  ?  1276 LEU   B CA  1 
ATOM   24231 C  C   . LEU   B 1 1278 ? 24.98400   15.51100  15.54800  1.000 57.56458  ?  1276 LEU   B C   1 
ATOM   24232 O  O   . LEU   B 1 1278 ? 25.76000   16.32800  16.04700  1.000 60.53442  ?  1276 LEU   B O   1 
ATOM   24233 C  CB  . LEU   B 1 1278 ? 24.55900   16.19400  13.18200  1.000 38.94730  ?  1276 LEU   B CB  1 
ATOM   24234 C  CG  . LEU   B 1 1278 ? 23.62200   16.53700  12.02000  1.000 45.87025  ?  1276 LEU   B CG  1 
ATOM   24235 C  CD1 . LEU   B 1 1278 ? 24.36800   16.46900  10.69900  1.000 55.07365  ?  1276 LEU   B CD1 1 
ATOM   24236 C  CD2 . LEU   B 1 1278 ? 22.40200   15.62600  11.98500  1.000 50.56262  ?  1276 LEU   B CD2 1 
ATOM   24237 N  N   . MET   B 1 1279 ? 25.02200   14.20500  15.82500  1.000 66.03037  ?  1277 MET   B N   1 
ATOM   24238 C  CA  . MET   B 1 1279 ? 26.02200   13.61900  16.72100  1.000 74.11946  ?  1277 MET   B CA  1 
ATOM   24239 C  C   . MET   B 1 1279 ? 26.50200   12.31600  16.08100  1.000 76.41958  ?  1277 MET   B C   1 
ATOM   24240 O  O   . MET   B 1 1279 ? 26.04200   11.22400  16.41900  1.000 76.35041  ?  1277 MET   B O   1 
ATOM   24241 C  CB  . MET   B 1 1279 ? 25.45800   13.39100  18.12100  1.000 61.05129  ?  1277 MET   B CB  1 
ATOM   24242 C  CG  . MET   B 1 1279 ? 25.27600   14.66000  18.93000  1.000 73.53277  ?  1277 MET   B CG  1 
ATOM   24243 S  SD  . MET   B 1 1279 ? 24.54000   14.32900  20.54000  1.000 90.86474  ?  1277 MET   B SD  1 
ATOM   24244 C  CE  . MET   B 1 1279 ? 25.90200   13.50600  21.36500  1.000 81.33869  ?  1277 MET   B CE  1 
ATOM   24245 N  N   . ALA   B 1 1280 ? 27.44400   12.43800  15.14800  1.000 66.96341  ?  1278 ALA   B N   1 
ATOM   24246 C  CA  . ALA   B 1 1280 ? 27.93700   11.28600  14.41100  1.000 51.30439  ?  1278 ALA   B CA  1 
ATOM   24247 C  C   . ALA   B 1 1280 ? 29.41600   11.46800  14.10800  1.000 67.82842  ?  1278 ALA   B C   1 
ATOM   24248 O  O   . ALA   B 1 1280 ? 29.91100   12.59400  14.00600  1.000 71.01074  ?  1278 ALA   B O   1 
ATOM   24249 C  CB  . ALA   B 1 1280 ? 27.15600   11.07800  13.10900  1.000 34.46537  ?  1278 ALA   B CB  1 
ATOM   24250 N  N   . GLU   B 1 1281 ? 30.11700   10.34700  13.97000  1.000 59.31596  ?  1279 GLU   B N   1 
ATOM   24251 C  CA  . GLU   B 1 1281 ? 31.49700   10.35300  13.51500  1.000 50.34269  ?  1279 GLU   B CA  1 
ATOM   24252 C  C   . GLU   B 1 1281 ? 31.54100   10.25200  11.99300  1.000 53.90764  ?  1279 GLU   B C   1 
ATOM   24253 O  O   . GLU   B 1 1281 ? 30.52800   10.01400  11.33200  1.000 59.03367  ?  1279 GLU   B O   1 
ATOM   24254 C  CB  . GLU   B 1 1281 ? 32.28000   9.21200   14.16000  1.000 51.65252  ?  1279 GLU   B CB  1 
ATOM   24255 C  CG  . GLU   B 1 1281 ? 32.20500   9.20700   15.67700  1.000 66.03363  ?  1279 GLU   B CG  1 
ATOM   24256 C  CD  . GLU   B 1 1281 ? 33.07200   8.13400   16.30300  1.000 73.85861  ?  1279 GLU   B CD  1 
ATOM   24257 O  OE1 . GLU   B 1 1281 ? 34.28300   8.37700   16.48600  1.000 83.27669  ?  1279 GLU   B OE1 1 
ATOM   24258 O  OE2 . GLU   B 1 1281 ? 32.54100   7.04800   16.61500  1.000 93.47501  -1 1279 GLU   B OE2 1 
ATOM   24259 N  N   . ARG   B 1 1282 ? 32.73500   10.44700  11.43400  1.000 42.70108  ?  1280 ARG   B N   1 
ATOM   24260 C  CA  . ARG   B 1 1282 ? 32.89100   10.43800  9.98400   1.000 40.06945  ?  1280 ARG   B CA  1 
ATOM   24261 C  C   . ARG   B 1 1282 ? 32.44400   9.09600   9.41700   1.000 51.20423  ?  1280 ARG   B C   1 
ATOM   24262 O  O   . ARG   B 1 1282 ? 33.01900   8.05200   9.73900   1.000 58.09540  ?  1280 ARG   B O   1 
ATOM   24263 C  CB  . ARG   B 1 1282 ? 34.34300   10.72800  9.61100   1.000 39.11692  ?  1280 ARG   B CB  1 
ATOM   24264 C  CG  . ARG   B 1 1282 ? 34.51700   11.31900  8.22200   1.000 49.18272  ?  1280 ARG   B CG  1 
ATOM   24265 C  CD  . ARG   B 1 1282 ? 35.72600   12.23700  8.15800   1.000 58.18520  ?  1280 ARG   B CD  1 
ATOM   24266 N  NE  . ARG   B 1 1282 ? 36.95500   11.55000  8.53900   1.000 48.27665  ?  1280 ARG   B NE  1 
ATOM   24267 C  CZ  . ARG   B 1 1282 ? 37.80100   11.98800  9.46000   1.000 55.43811  ?  1280 ARG   B CZ  1 
ATOM   24268 N  NH1 . ARG   B 1 1282 ? 37.58100   13.11200  10.12400  1.000 71.71253  ?  1280 ARG   B NH1 1 
ATOM   24269 N  NH2 . ARG   B 1 1282 ? 38.89800   11.28200  9.72200   1.000 67.37696  ?  1280 ARG   B NH2 1 
ATOM   24270 N  N   . SER   B 1 1283 ? 31.40700   9.12200   8.58500   1.000 51.42645  ?  1281 SER   B N   1 
ATOM   24271 C  CA  . SER   B 1 1283 ? 30.80200   7.89700   8.07600   1.000 49.87165  ?  1281 SER   B CA  1 
ATOM   24272 C  C   . SER   B 1 1283 ? 29.98100   8.23300   6.83500   1.000 60.21567  ?  1281 SER   B C   1 
ATOM   24273 O  O   . SER   B 1 1283 ? 30.03900   9.35100   6.31200   1.000 68.70669  ?  1281 SER   B O   1 
ATOM   24274 C  CB  . SER   B 1 1283 ? 29.94000   7.23400   9.15400   1.000 57.13196  ?  1281 SER   B CB  1 
ATOM   24275 O  OG  . SER   B 1 1283 ? 28.94700   8.13100   9.62200   1.000 49.44372  ?  1281 SER   B OG  1 
ATOM   24276 N  N   . VAL   B 1 1284 ? 29.21700   7.25100   6.35800   1.000 61.01073  ?  1282 VAL   B N   1 
ATOM   24277 C  CA  . VAL   B 1 1284 ? 28.23000   7.52500   5.32200   1.000 65.60024  ?  1282 VAL   B CA  1 
ATOM   24278 C  C   . VAL   B 1 1284 ? 26.93700   8.03300   5.94700   1.000 58.23655  ?  1282 VAL   B C   1 
ATOM   24279 O  O   . VAL   B 1 1284 ? 26.23100   8.85100   5.34600   1.000 60.51448  ?  1282 VAL   B O   1 
ATOM   24280 C  CB  . VAL   B 1 1284 ? 27.98900   6.27000   4.46700   1.000 61.62520  ?  1282 VAL   B CB  1 
ATOM   24281 C  CG1 . VAL   B 1 1284 ? 27.08000   6.58900   3.28700   1.000 59.79089  ?  1282 VAL   B CG1 1 
ATOM   24282 C  CG2 . VAL   B 1 1284 ? 29.31500   5.70200   3.99100   1.000 64.76504  ?  1282 VAL   B CG2 1 
ATOM   24283 N  N   . GLU   B 1 1285 ? 26.61400   7.56900   7.15700   1.000 65.28795  ?  1283 GLU   B N   1 
ATOM   24284 C  CA  . GLU   B 1 1285 ? 25.44200   8.07700   7.86200   1.000 62.10191  ?  1283 GLU   B CA  1 
ATOM   24285 C  C   . GLU   B 1 1285 ? 25.57600   9.56900   8.14200   1.000 66.99342  ?  1283 GLU   B C   1 
ATOM   24286 O  O   . GLU   B 1 1285 ? 24.58700   10.31000  8.08700   1.000 77.09837  ?  1283 GLU   B O   1 
ATOM   24287 C  CB  . GLU   B 1 1285 ? 25.24000   7.30300   9.16500   1.000 52.39372  ?  1283 GLU   B CB  1 
ATOM   24288 C  CG  . GLU   B 1 1285 ? 25.33800   5.79100   9.01700   1.000 69.38957  ?  1283 GLU   B CG  1 
ATOM   24289 C  CD  . GLU   B 1 1285 ? 26.73200   5.26200   9.30600   1.000 70.11078  ?  1283 GLU   B CD  1 
ATOM   24290 O  OE1 . GLU   B 1 1285 ? 27.07700   5.10500   10.49600  1.000 63.20557  ?  1283 GLU   B OE1 1 
ATOM   24291 O  OE2 . GLU   B 1 1285 ? 27.48300   5.00300   8.34200   1.000 82.89471  -1 1283 GLU   B OE2 1 
ATOM   24292 N  N   . MET   B 1 1286 ? 26.79400   10.02300  8.45100   1.000 64.93344  ?  1284 MET   B N   1 
ATOM   24293 C  CA  . MET   B 1 1286 ? 27.03400   11.44900  8.64300   1.000 58.78257  ?  1284 MET   B CA  1 
ATOM   24294 C  C   . MET   B 1 1286 ? 26.72000   12.23100  7.37500   1.000 60.52497  ?  1284 MET   B C   1 
ATOM   24295 O  O   . MET   B 1 1286 ? 26.10600   13.30300  7.43100   1.000 54.33556  ?  1284 MET   B O   1 
ATOM   24296 C  CB  . MET   B 1 1286 ? 28.48500   11.68000  9.06700   1.000 51.97290  ?  1284 MET   B CB  1 
ATOM   24297 C  CG  . MET   B 1 1286 ? 28.69100   12.82700  10.04200  1.000 66.89262  ?  1284 MET   B CG  1 
ATOM   24298 S  SD  . MET   B 1 1286 ? 30.33800   13.54500  9.89400   1.000 55.19413  ?  1284 MET   B SD  1 
ATOM   24299 C  CE  . MET   B 1 1286 ? 30.37500   13.89500  8.13900   1.000 35.30916  ?  1284 MET   B CE  1 
ATOM   24300 N  N   . MET   B 1 1287 ? 27.12600   11.70000  6.21900   1.000 56.36368  ?  1285 MET   B N   1 
ATOM   24301 C  CA  . MET   B 1 1287 ? 26.85800   12.37900  4.95800   1.000 50.82345  ?  1285 MET   B CA  1 
ATOM   24302 C  C   . MET   B 1 1287 ? 25.37400   12.37000  4.62000   1.000 61.73003  ?  1285 MET   B C   1 
ATOM   24303 O  O   . MET   B 1 1287 ? 24.82500   13.39600  4.20300   1.000 70.91366  ?  1285 MET   B O   1 
ATOM   24304 C  CB  . MET   B 1 1287 ? 27.66800   11.73900  3.83300   1.000 67.67892  ?  1285 MET   B CB  1 
ATOM   24305 C  CG  . MET   B 1 1287 ? 29.03200   12.36100  3.69900   1.000 66.37110  ?  1285 MET   B CG  1 
ATOM   24306 S  SD  . MET   B 1 1287 ? 28.81800   14.14800  3.66500   1.000 66.91098  ?  1285 MET   B SD  1 
ATOM   24307 C  CE  . MET   B 1 1287 ? 30.34200   14.65700  2.90100   1.000 49.06168  ?  1285 MET   B CE  1 
ATOM   24308 N  N   . VAL   B 1 1288 ? 24.71000   11.22500  4.78300   1.000 70.59117  ?  1286 VAL   B N   1 
ATOM   24309 C  CA  . VAL   B 1 1288 ? 23.28800   11.14400  4.46300   1.000 69.09545  ?  1286 VAL   B CA  1 
ATOM   24310 C  C   . VAL   B 1 1288 ? 22.48600   12.07300  5.36500   1.000 61.20018  ?  1286 VAL   B C   1 
ATOM   24311 O  O   . VAL   B 1 1288 ? 21.51300   12.69900  4.92800   1.000 67.77494  ?  1286 VAL   B O   1 
ATOM   24312 C  CB  . VAL   B 1 1288 ? 22.80200   9.68600   4.56300   1.000 67.45608  ?  1286 VAL   B CB  1 
ATOM   24313 C  CG1 . VAL   B 1 1288 ? 21.30100   9.59300   4.31400   1.000 67.30418  ?  1286 VAL   B CG1 1 
ATOM   24314 C  CG2 . VAL   B 1 1288 ? 23.56100   8.81600   3.57400   1.000 56.60921  ?  1286 VAL   B CG2 1 
ATOM   24315 N  N   . ALA   B 1 1289 ? 22.89300   12.19600  6.63100   1.000 50.00285  ?  1287 ALA   B N   1 
ATOM   24316 C  CA  . ALA   B 1 1289 ? 22.15300   13.03900  7.56400   1.000 58.74292  ?  1287 ALA   B CA  1 
ATOM   24317 C  C   . ALA   B 1 1289 ? 22.18500   14.50100  7.13700   1.000 67.61879  ?  1287 ALA   B C   1 
ATOM   24318 O  O   . ALA   B 1 1289 ? 21.15700   15.18700  7.16900   1.000 69.74298  ?  1287 ALA   B O   1 
ATOM   24319 C  CB  . ALA   B 1 1289 ? 22.71400   12.88000  8.97600   1.000 48.21937  ?  1287 ALA   B CB  1 
ATOM   24320 N  N   . ILE   B 1 1290 ? 23.35600   14.99300  6.72600   1.000 64.36319  ?  1288 ILE   B N   1 
ATOM   24321 C  CA  . ILE   B 1 1290 ? 23.48600   16.39500  6.33100   1.000 60.63961  ?  1288 ILE   B CA  1 
ATOM   24322 C  C   . ILE   B 1 1290 ? 22.59300   16.69000  5.13200   1.000 59.41435  ?  1288 ILE   B C   1 
ATOM   24323 O  O   . ILE   B 1 1290 ? 21.72800   17.57200  5.17700   1.000 56.13364  ?  1288 ILE   B O   1 
ATOM   24324 C  CB  . ILE   B 1 1290 ? 24.95600   16.73700  6.03100   1.000 54.20309  ?  1288 ILE   B CB  1 
ATOM   24325 C  CG1 . ILE   B 1 1290 ? 25.73800   16.92800  7.33100   1.000 55.76488  ?  1288 ILE   B CG1 1 
ATOM   24326 C  CG2 . ILE   B 1 1290 ? 25.05200   17.98100  5.15900   1.000 45.72598  ?  1288 ILE   B CG2 1 
ATOM   24327 C  CD1 . ILE   B 1 1290 ? 27.22800   17.08800  7.12000   1.000 43.91124  ?  1288 ILE   B CD1 1 
ATOM   24328 N  N   . PHE   B 1 1291 ? 22.79100   15.94600  4.04200   1.000 51.08548  ?  1289 PHE   B N   1 
ATOM   24329 C  CA  . PHE   B 1 1291 ? 22.01100   16.17700  2.83300   1.000 52.64257  ?  1289 PHE   B CA  1 
ATOM   24330 C  C   . PHE   B 1 1291 ? 20.51800   15.98000  3.07500   1.000 71.52843  ?  1289 PHE   B C   1 
ATOM   24331 O  O   . PHE   B 1 1291 ? 19.69600   16.64400  2.43300   1.000 72.95490  ?  1289 PHE   B O   1 
ATOM   24332 C  CB  . PHE   B 1 1291 ? 22.49300   15.24900  1.71900   1.000 60.74798  ?  1289 PHE   B CB  1 
ATOM   24333 C  CG  . PHE   B 1 1291 ? 23.59900   15.81800  0.87500   1.000 73.00763  ?  1289 PHE   B CG  1 
ATOM   24334 C  CD1 . PHE   B 1 1291 ? 23.32800   16.75200  -0.11200  1.000 71.74083  ?  1289 PHE   B CD1 1 
ATOM   24335 C  CD2 . PHE   B 1 1291 ? 24.91000   15.40200  1.05400   1.000 60.45272  ?  1289 PHE   B CD2 1 
ATOM   24336 C  CE1 . PHE   B 1 1291 ? 24.34200   17.26300  -0.89900  1.000 67.92838  ?  1289 PHE   B CE1 1 
ATOM   24337 C  CE2 . PHE   B 1 1291 ? 25.92700   15.91000  0.26800   1.000 52.47084  ?  1289 PHE   B CE2 1 
ATOM   24338 C  CZ  . PHE   B 1 1291 ? 25.64200   16.84100  -0.70800  1.000 70.60606  ?  1289 PHE   B CZ  1 
ATOM   24339 N  N   . ALA   B 1 1292 ? 20.14300   15.07500  3.98600   1.000 67.71433  ?  1290 ALA   B N   1 
ATOM   24340 C  CA  . ALA   B 1 1292 ? 18.72500   14.84800  4.25200   1.000 63.88296  ?  1290 ALA   B CA  1 
ATOM   24341 C  C   . ALA   B 1 1292 ? 18.12000   16.00600  5.02900   1.000 65.43062  ?  1290 ALA   B C   1 
ATOM   24342 O  O   . ALA   B 1 1292 ? 16.95800   16.36800  4.81200   1.000 68.24937  ?  1290 ALA   B O   1 
ATOM   24343 C  CB  . ALA   B 1 1292 ? 18.52600   13.53500  5.00700   1.000 60.84631  ?  1290 ALA   B CB  1 
ATOM   24344 N  N   . VAL   B 1 1293 ? 18.89300   16.58800  5.94600   1.000 58.57860  ?  1291 VAL   B N   1 
ATOM   24345 C  CA  . VAL   B 1 1293 ? 18.45000   17.78700  6.64700   1.000 58.38560  ?  1291 VAL   B CA  1 
ATOM   24346 C  C   . VAL   B 1 1293 ? 18.16100   18.90600  5.65400   1.000 64.56722  ?  1291 VAL   B C   1 
ATOM   24347 O  O   . VAL   B 1 1293 ? 17.17700   19.64600  5.79200   1.000 63.33231  ?  1291 VAL   B O   1 
ATOM   24348 C  CB  . VAL   B 1 1293 ? 19.50500   18.20500  7.68600   1.000 52.71746  ?  1291 VAL   B CB  1 
ATOM   24349 C  CG1 . VAL   B 1 1293 ? 19.30700   19.65000  8.08600   1.000 50.39095  ?  1291 VAL   B CG1 1 
ATOM   24350 C  CG2 . VAL   B 1 1293 ? 19.45000   17.28000  8.89700   1.000 54.38000  ?  1291 VAL   B CG2 1 
ATOM   24351 N  N   . LEU   B 1 1294 ? 19.00300   19.03700  4.62700   1.000 50.56287  ?  1292 LEU   B N   1 
ATOM   24352 C  CA  . LEU   B 1 1294 ? 18.79300   20.07400  3.62200   1.000 59.17928  ?  1292 LEU   B CA  1 
ATOM   24353 C  C   . LEU   B 1 1294 ? 17.57400   19.76600  2.76100   1.000 62.46286  ?  1292 LEU   B C   1 
ATOM   24354 O  O   . LEU   B 1 1294 ? 16.71200   20.63000  2.55800   1.000 67.75826  ?  1292 LEU   B O   1 
ATOM   24355 C  CB  . LEU   B 1 1294 ? 20.04600   20.22300  2.76000   1.000 59.51824  ?  1292 LEU   B CB  1 
ATOM   24356 C  CG  . LEU   B 1 1294 ? 21.33900   20.49500  3.53100   1.000 46.14217  ?  1292 LEU   B CG  1 
ATOM   24357 C  CD1 . LEU   B 1 1294 ? 22.42200   20.94600  2.58000   1.000 43.03180  ?  1292 LEU   B CD1 1 
ATOM   24358 C  CD2 . LEU   B 1 1294 ? 21.12600   21.52700  4.63000   1.000 42.91691  ?  1292 LEU   B CD2 1 
ATOM   24359 N  N   . LYS   B 1 1295 ? 17.48900   18.53600  2.24600   1.000 69.02072  ?  1293 LYS   B N   1 
ATOM   24360 C  CA  . LYS   B 1 1295 ? 16.34200   18.13300  1.43700   1.000 71.69541  ?  1293 LYS   B CA  1 
ATOM   24361 C  C   . LYS   B 1 1295 ? 15.03400   18.31400  2.19600   1.000 65.53687  ?  1293 LYS   B C   1 
ATOM   24362 O  O   . LYS   B 1 1295 ? 14.01900   18.72000  1.61600   1.000 64.22675  ?  1293 LYS   B O   1 
ATOM   24363 C  CB  . LYS   B 1 1295 ? 16.50000   16.67900  0.99800   1.000 62.24723  ?  1293 LYS   B CB  1 
ATOM   24364 C  CG  . LYS   B 1 1295 ? 17.39300   16.49200  -0.20500  1.000 56.22845  ?  1293 LYS   B CG  1 
ATOM   24365 C  CD  . LYS   B 1 1295 ? 17.10800   15.17400  -0.89400  1.000 68.70348  ?  1293 LYS   B CD  1 
ATOM   24366 C  CE  . LYS   B 1 1295 ? 17.52300   15.25300  -2.34300  1.000 57.56651  ?  1293 LYS   B CE  1 
ATOM   24367 N  NZ  . LYS   B 1 1295 ? 17.22500   16.61900  -2.84500  1.000 72.99267  ?  1293 LYS   B NZ  1 
ATOM   24368 N  N   . ALA   B 1 1296 ? 15.03900   18.01000  3.49600   1.000 52.71223  ?  1294 ALA   B N   1 
ATOM   24369 C  CA  . ALA   B 1 1296 ? 13.85100   18.22700  4.31300   1.000 70.42350  ?  1294 ALA   B CA  1 
ATOM   24370 C  C   . ALA   B 1 1296 ? 13.48900   19.70500  4.37700   1.000 71.17155  ?  1294 ALA   B C   1 
ATOM   24371 O  O   . ALA   B 1 1296 ? 12.30700   20.06500  4.32800   1.000 74.71798  ?  1294 ALA   B O   1 
ATOM   24372 C  CB  . ALA   B 1 1296 ? 14.07400   17.66400  5.71600   1.000 64.73624  ?  1294 ALA   B CB  1 
ATOM   24373 N  N   . GLY   B 1 1297 ? 14.49200   20.57400  4.48300   1.000 75.99560  ?  1295 GLY   B N   1 
ATOM   24374 C  CA  . GLY   B 1 1297 ? 14.25300   22.00400  4.48500   1.000 73.85732  ?  1295 GLY   B CA  1 
ATOM   24375 C  C   . GLY   B 1 1297 ? 14.90300   22.74000  5.63900   1.000 73.12610  ?  1295 GLY   B C   1 
ATOM   24376 O  O   . GLY   B 1 1297 ? 14.82200   23.96900  5.72000   1.000 77.49794  ?  1295 GLY   B O   1 
ATOM   24377 N  N   . GLY   B 1 1298 ? 15.55600   22.00500  6.53300   1.000 65.27437  ?  1296 GLY   B N   1 
ATOM   24378 C  CA  . GLY   B 1 1298 ? 16.14000   22.56600  7.72900   1.000 59.06516  ?  1296 GLY   B CA  1 
ATOM   24379 C  C   . GLY   B 1 1298 ? 17.61600   22.87300  7.58100   1.000 66.22747  ?  1296 GLY   B C   1 
ATOM   24380 O  O   . GLY   B 1 1298 ? 18.16600   22.92700  6.47500   1.000 56.95840  ?  1296 GLY   B O   1 
ATOM   24381 N  N   . ALA   B 1 1299 ? 18.26600   23.08600  8.72200   1.000 57.70517  ?  1297 ALA   B N   1 
ATOM   24382 C  CA  . ALA   B 1 1299 ? 19.69400   23.35700  8.78400   1.000 67.21421  ?  1297 ALA   B CA  1 
ATOM   24383 C  C   . ALA   B 1 1299 ? 20.33000   22.41000  9.78900   1.000 66.64655  ?  1297 ALA   B C   1 
ATOM   24384 O  O   . ALA   B 1 1299 ? 19.75800   22.14900  10.85200  1.000 54.38244  ?  1297 ALA   B O   1 
ATOM   24385 C  CB  . ALA   B 1 1299 ? 19.96900   24.81400  9.17700   1.000 66.44305  ?  1297 ALA   B CB  1 
ATOM   24386 N  N   . TYR   B 1 1300 ? 21.50600   21.88700  9.45200   1.000 58.39302  ?  1298 TYR   B N   1 
ATOM   24387 C  CA  . TYR   B 1 1300 ? 22.14900   20.90500  10.31200  1.000 60.24106  ?  1298 TYR   B CA  1 
ATOM   24388 C  C   . TYR   B 1 1300 ? 23.08000   21.58200  11.31100  1.000 56.83322  ?  1298 TYR   B C   1 
ATOM   24389 O  O   . TYR   B 1 1300 ? 23.72100   22.59300  11.01200  1.000 59.48502  ?  1298 TYR   B O   1 
ATOM   24390 C  CB  . TYR   B 1 1300 ? 22.90500   19.85300  9.48700   1.000 54.01763  ?  1298 TYR   B CB  1 
ATOM   24391 C  CG  . TYR   B 1 1300 ? 24.24400   20.26200  8.89900   1.000 54.26868  ?  1298 TYR   B CG  1 
ATOM   24392 C  CD1 . TYR   B 1 1300 ? 25.42700   20.08900  9.61300   1.000 50.66355  ?  1298 TYR   B CD1 1 
ATOM   24393 C  CD2 . TYR   B 1 1300 ? 24.33100   20.76800  7.60700   1.000 49.77167  ?  1298 TYR   B CD2 1 
ATOM   24394 C  CE1 . TYR   B 1 1300 ? 26.65100   20.44300  9.07100   1.000 46.15755  ?  1298 TYR   B CE1 1 
ATOM   24395 C  CE2 . TYR   B 1 1300 ? 25.55100   21.12200  7.05700   1.000 52.00790  ?  1298 TYR   B CE2 1 
ATOM   24396 C  CZ  . TYR   B 1 1300 ? 26.70600   20.95800  7.79200   1.000 48.54593  ?  1298 TYR   B CZ  1 
ATOM   24397 O  OH  . TYR   B 1 1300 ? 27.91600   21.31200  7.24000   1.000 48.10461  ?  1298 TYR   B OH  1 
ATOM   24398 N  N   . LEU   B 1 1301 ? 23.13200   21.01400  12.51600  1.000 53.42357  ?  1299 LEU   B N   1 
ATOM   24399 C  CA  . LEU   B 1 1301 ? 23.97400   21.51200  13.59600  1.000 48.41962  ?  1299 LEU   B CA  1 
ATOM   24400 C  C   . LEU   B 1 1301 ? 24.98400   20.42300  13.93800  1.000 67.01108  ?  1299 LEU   B C   1 
ATOM   24401 O  O   . LEU   B 1 1301 ? 24.58200   19.33400  14.38100  1.000 82.22653  ?  1299 LEU   B O   1 
ATOM   24402 C  CB  . LEU   B 1 1301 ? 23.13100   21.87700  14.82500  1.000 49.54531  ?  1299 LEU   B CB  1 
ATOM   24403 C  CG  . LEU   B 1 1301 ? 23.65700   22.94700  15.78800  1.000 46.18199  ?  1299 LEU   B CG  1 
ATOM   24404 C  CD1 . LEU   B 1 1301 ? 22.49700   23.62000  16.49200  1.000 58.54327  ?  1299 LEU   B CD1 1 
ATOM   24405 C  CD2 . LEU   B 1 1301 ? 24.62900   22.38200  16.79800  1.000 44.76175  ?  1299 LEU   B CD2 1 
ATOM   24406 N  N   . PRO   B 1 1302 ? 26.28700   20.63700  13.72500  1.000 65.42508  ?  1300 PRO   B N   1 
ATOM   24407 C  CA  . PRO   B 1 1302 ? 27.26700   19.59100  14.05700  1.000 52.43650  ?  1300 PRO   B CA  1 
ATOM   24408 C  C   . PRO   B 1 1302 ? 27.73800   19.64600  15.50300  1.000 49.63238  ?  1300 PRO   B C   1 
ATOM   24409 O  O   . PRO   B 1 1302 ? 28.10200   20.71300  16.00600  1.000 56.91216  ?  1300 PRO   B O   1 
ATOM   24410 C  CB  . PRO   B 1 1302 ? 28.41400   19.87300  13.08000  1.000 44.60361  ?  1300 PRO   B CB  1 
ATOM   24411 C  CG  . PRO   B 1 1302 ? 28.33600   21.34200  12.83700  1.000 63.78545  ?  1300 PRO   B CG  1 
ATOM   24412 C  CD  . PRO   B 1 1302 ? 26.88100   21.72500  12.92900  1.000 64.46134  ?  1300 PRO   B CD  1 
ATOM   24413 N  N   . ILE   B 1 1303 ? 27.73300   18.50000  16.18200  1.000 58.86878  ?  1301 ILE   B N   1 
ATOM   24414 C  CA  . ILE   B 1 1303 ? 28.22700   18.39000  17.55000  1.000 60.95821  ?  1301 ILE   B CA  1 
ATOM   24415 C  C   . ILE   B 1 1303 ? 29.20700   17.22900  17.61200  1.000 65.71790  ?  1301 ILE   B C   1 
ATOM   24416 O  O   . ILE   B 1 1303 ? 28.90500   16.12700  17.13600  1.000 61.76711  ?  1301 ILE   B O   1 
ATOM   24417 C  CB  . ILE   B 1 1303 ? 27.10500   18.16000  18.58500  1.000 63.45404  ?  1301 ILE   B CB  1 
ATOM   24418 C  CG1 . ILE   B 1 1303 ? 26.00000   19.21500  18.51900  1.000 60.85383  ?  1301 ILE   B CG1 1 
ATOM   24419 C  CG2 . ILE   B 1 1303 ? 27.66800   18.06000  19.99300  1.000 43.20288  ?  1301 ILE   B CG2 1 
ATOM   24420 C  CD1 . ILE   B 1 1303 ? 24.96400   18.91000  17.48900  1.000 77.51681  ?  1301 ILE   B CD1 1 
ATOM   24421 N  N   . ASP   B 1 1304 ? 30.35100   17.46400  18.23000  1.000 65.85028  ?  1302 ASP   B N   1 
ATOM   24422 C  CA  . ASP   B 1 1304 ? 31.31800   16.40100  18.42600  1.000 67.63162  ?  1302 ASP   B CA  1 
ATOM   24423 C  C   . ASP   B 1 1304 ? 30.70600   15.31500  19.30700  1.000 73.90927  ?  1302 ASP   B C   1 
ATOM   24424 O  O   . ASP   B 1 1304 ? 30.17200   15.62400  20.38200  1.000 80.51451  ?  1302 ASP   B O   1 
ATOM   24425 C  CB  . ASP   B 1 1304 ? 32.58600   16.97000  19.05900  1.000 78.56334  ?  1302 ASP   B CB  1 
ATOM   24426 C  CG  . ASP   B 1 1304 ? 33.56800   15.89600  19.46500  1.000 86.50527  ?  1302 ASP   B CG  1 
ATOM   24427 O  OD1 . ASP   B 1 1304 ? 33.37600   15.29500  20.53800  1.000 87.25852  ?  1302 ASP   B OD1 1 
ATOM   24428 O  OD2 . ASP   B 1 1304 ? 34.53400   15.65000  18.71300  1.000 86.68982  -1 1302 ASP   B OD2 1 
ATOM   24429 N  N   . PRO   B 1 1305 ? 30.73100   14.04900  18.88000  1.000 84.08406  ?  1303 PRO   B N   1 
ATOM   24430 C  CA  . PRO   B 1 1305 ? 30.10500   12.99400  19.69700  1.000 74.59692  ?  1303 PRO   B CA  1 
ATOM   24431 C  C   . PRO   B 1 1305 ? 30.76000   12.80300  21.05600  1.000 79.07587  ?  1303 PRO   B C   1 
ATOM   24432 O  O   . PRO   B 1 1305 ? 30.06500   12.50600  22.03600  1.000 74.22555  ?  1303 PRO   B O   1 
ATOM   24433 C  CB  . PRO   B 1 1305 ? 30.24800   11.74500  18.81500  1.000 66.94239  ?  1303 PRO   B CB  1 
ATOM   24434 C  CG  . PRO   B 1 1305 ? 30.39900   12.26900  17.42000  1.000 68.91306  ?  1303 PRO   B CG  1 
ATOM   24435 C  CD  . PRO   B 1 1305 ? 31.16000   13.55400  17.56100  1.000 73.62230  ?  1303 PRO   B CD  1 
ATOM   24436 N  N   . HIS   B 1 1306 ? 32.08200   12.96400  21.14500  1.000 75.73872  ?  1304 HIS   B N   1 
ATOM   24437 C  CA  . HIS   B 1 1306 ? 32.82100   12.77400  22.38800  1.000 78.50020  ?  1304 HIS   B CA  1 
ATOM   24438 C  C   . HIS   B 1 1306 ? 33.03700   14.08400  23.14200  1.000 87.87364  ?  1304 HIS   B C   1 
ATOM   24439 O  O   . HIS   B 1 1306 ? 34.05300   14.24900  23.82600  1.000 94.94673  ?  1304 HIS   B O   1 
ATOM   24440 C  CB  . HIS   B 1 1306 ? 34.16100   12.09700  22.10100  1.000 79.50025  ?  1304 HIS   B CB  1 
ATOM   24441 C  CG  . HIS   B 1 1306 ? 34.11600   11.13600  20.95500  1.000 82.91730  ?  1304 HIS   B CG  1 
ATOM   24442 N  ND1 . HIS   B 1 1306 ? 33.57100   9.87500   21.06300  1.000 69.13613  ?  1304 HIS   B ND1 1 
ATOM   24443 C  CD2 . HIS   B 1 1306 ? 34.54100   11.25400  19.67400  1.000 81.76656  ?  1304 HIS   B CD2 1 
ATOM   24444 C  CE1 . HIS   B 1 1306 ? 33.66600   9.25500   19.90000  1.000 67.30715  ?  1304 HIS   B CE1 1 
ATOM   24445 N  NE2 . HIS   B 1 1306 ? 34.25100   10.07000  19.04000  1.000 77.63885  ?  1304 HIS   B NE2 1 
ATOM   24446 N  N   . SER   B 1 1307 ? 32.10200   15.02600  23.01700  1.000 77.14425  ?  1305 SER   B N   1 
ATOM   24447 C  CA  . SER   B 1 1307 ? 32.22400   16.30300  23.69700  1.000 82.39421  ?  1305 SER   B CA  1 
ATOM   24448 C  C   . SER   B 1 1307 ? 31.72200   16.19500  25.13600  1.000 90.22564  ?  1305 SER   B C   1 
ATOM   24449 O  O   . SER   B 1 1307 ? 30.83400   15.39000  25.43100  1.000 98.55335  ?  1305 SER   B O   1 
ATOM   24450 C  CB  . SER   B 1 1307 ? 31.43600   17.38100  22.95800  1.000 86.99170  ?  1305 SER   B CB  1 
ATOM   24451 O  OG  . SER   B 1 1307 ? 30.22700   16.86400  22.43100  1.000 90.21564  ?  1305 SER   B OG  1 
ATOM   24452 N  N   . PRO   B 1 1308 ? 32.29300   16.98200  26.04900  1.000 92.30844  ?  1306 PRO   B N   1 
ATOM   24453 C  CA  . PRO   B 1 1308 ? 31.80400   16.97800  27.43400  1.000 83.83230  ?  1306 PRO   B CA  1 
ATOM   24454 C  C   . PRO   B 1 1308 ? 30.31700   17.29100  27.50100  1.000 88.65158  ?  1306 PRO   B C   1 
ATOM   24455 O  O   . PRO   B 1 1308 ? 29.75000   17.93800  26.61700  1.000 92.31011  ?  1306 PRO   B O   1 
ATOM   24456 C  CB  . PRO   B 1 1308 ? 32.63400   18.07100  28.12000  1.000 92.67297  ?  1306 PRO   B CB  1 
ATOM   24457 C  CG  . PRO   B 1 1308 ? 33.76800   18.37300  27.21300  1.000 98.13951  ?  1306 PRO   B CG  1 
ATOM   24458 C  CD  . PRO   B 1 1308 ? 33.54900   17.73200  25.88100  1.000 93.40449  ?  1306 PRO   B CD  1 
ATOM   24459 N  N   . ALA   B 1 1309 ? 29.68600   16.81600  28.57600  1.000 85.23025  ?  1307 ALA   B N   1 
ATOM   24460 C  CA  . ALA   B 1 1309 ? 28.23600   16.90600  28.69100  1.000 90.25924  ?  1307 ALA   B CA  1 
ATOM   24461 C  C   . ALA   B 1 1309 ? 27.74300   18.34100  28.79400  1.000 99.78009  ?  1307 ALA   B C   1 
ATOM   24462 O  O   . ALA   B 1 1309 ? 26.56500   18.59700  28.52300  1.000 95.07856  ?  1307 ALA   B O   1 
ATOM   24463 C  CB  . ALA   B 1 1309 ? 27.75600   16.10600  29.90200  1.000 70.80116  ?  1307 ALA   B CB  1 
ATOM   24464 N  N   . GLU   B 1 1310 ? 28.60900   19.28300  29.17400  1.000 92.07054  ?  1308 GLU   B N   1 
ATOM   24465 C  CA  . GLU   B 1 1310 ? 28.16000   20.66300  29.30800  1.000 87.95774  ?  1308 GLU   B CA  1 
ATOM   24466 C  C   . GLU   B 1 1310 ? 27.79400   21.27000  27.95900  1.000 102.81205 ?  1308 GLU   B C   1 
ATOM   24467 O  O   . GLU   B 1 1310 ? 26.91800   22.14000  27.89000  1.000 100.65021 ?  1308 GLU   B O   1 
ATOM   24468 C  CB  . GLU   B 1 1310 ? 29.22900   21.50300  30.01700  1.000 86.85358  ?  1308 GLU   B CB  1 
ATOM   24469 C  CG  . GLU   B 1 1310 ? 30.63300   21.47700  29.40100  1.000 107.34493 ?  1308 GLU   B CG  1 
ATOM   24470 C  CD  . GLU   B 1 1310 ? 30.74600   22.23900  28.09000  1.000 118.40855 ?  1308 GLU   B CD  1 
ATOM   24471 O  OE1 . GLU   B 1 1310 ? 30.67100   23.48700  28.11300  1.000 103.26988 ?  1308 GLU   B OE1 1 
ATOM   24472 O  OE2 . GLU   B 1 1310 ? 30.92100   21.58700  27.03900  1.000 116.35861 -1 1308 GLU   B OE2 1 
ATOM   24473 N  N   . ARG   B 1 1311 ? 28.43500   20.82000  26.87900  1.000 88.24962  ?  1309 ARG   B N   1 
ATOM   24474 C  CA  . ARG   B 1 1311 ? 28.16500   21.41200  25.57500  1.000 83.14664  ?  1309 ARG   B CA  1 
ATOM   24475 C  C   . ARG   B 1 1311 ? 26.86700   20.88300  24.98300  1.000 97.27457  ?  1309 ARG   B C   1 
ATOM   24476 O  O   . ARG   B 1 1311 ? 26.08300   21.65600  24.42000  1.000 98.80675  ?  1309 ARG   B O   1 
ATOM   24477 C  CB  . ARG   B 1 1311 ? 29.33400   21.16000  24.62500  1.000 86.31480  ?  1309 ARG   B CB  1 
ATOM   24478 C  CG  . ARG   B 1 1311 ? 30.11400   22.41800  24.27200  1.000 87.04527  ?  1309 ARG   B CG  1 
ATOM   24479 C  CD  . ARG   B 1 1311 ? 31.31300   22.10200  23.39500  1.000 103.52957 ?  1309 ARG   B CD  1 
ATOM   24480 N  NE  . ARG   B 1 1311 ? 30.91400   21.58600  22.09000  1.000 119.57631 ?  1309 ARG   B NE  1 
ATOM   24481 C  CZ  . ARG   B 1 1311 ? 31.76000   21.17900  21.15300  1.000 100.14685 ?  1309 ARG   B CZ  1 
ATOM   24482 N  NH1 . ARG   B 1 1311 ? 33.06900   21.21500  21.34000  1.000 93.71297  ?  1309 ARG   B NH1 1 
ATOM   24483 N  NH2 . ARG   B 1 1311 ? 31.27900   20.71800  20.00100  1.000 69.96487  ?  1309 ARG   B NH2 1 
ATOM   24484 N  N   . ILE   B 1 1312 ? 26.62200   19.57400  25.10600  1.000 96.61159  ?  1310 ILE   B N   1 
ATOM   24485 C  CA  . ILE   B 1 1312 ? 25.35000   19.00500  24.66100  1.000 106.88344 ?  1310 ILE   B CA  1 
ATOM   24486 C  C   . ILE   B 1 1312 ? 24.18800   19.75600  25.29200  1.000 104.02749 ?  1310 ILE   B C   1 
ATOM   24487 O  O   . ILE   B 1 1312 ? 23.17400   20.03200  24.63800  1.000 95.85667  ?  1310 ILE   B O   1 
ATOM   24488 C  CB  . ILE   B 1 1312 ? 25.28900   17.50100  24.98900  1.000 99.00338  ?  1310 ILE   B CB  1 
ATOM   24489 C  CG1 . ILE   B 1 1312 ? 26.55700   16.79600  24.51000  1.000 82.33815  ?  1310 ILE   B CG1 1 
ATOM   24490 C  CG2 . ILE   B 1 1312 ? 24.05100   16.86700  24.36200  1.000 91.21173  ?  1310 ILE   B CG2 1 
ATOM   24491 C  CD1 . ILE   B 1 1312 ? 26.60700   16.60000  23.02700  1.000 87.39356  ?  1310 ILE   B CD1 1 
ATOM   24492 N  N   . ALA   B 1 1313 ? 24.32300   20.10900  26.57200  1.000 92.99584  ?  1311 ALA   B N   1 
ATOM   24493 C  CA  . ALA   B 1 1313 ? 23.27800   20.86700  27.25100  1.000 94.37761  ?  1311 ALA   B CA  1 
ATOM   24494 C  C   . ALA   B 1 1313 ? 23.24800   22.31500  26.77600  1.000 96.09854  ?  1311 ALA   B C   1 
ATOM   24495 O  O   . ALA   B 1 1313 ? 22.17600   22.85900  26.48600  1.000 88.78464  ?  1311 ALA   B O   1 
ATOM   24496 C  CB  . ALA   B 1 1313 ? 23.48600   20.80100  28.76400  1.000 91.47519  ?  1311 ALA   B CB  1 
ATOM   24497 N  N   . TYR   B 1 1314 ? 24.41900   22.95700  26.69500  1.000 89.38398  ?  1312 TYR   B N   1 
ATOM   24498 C  CA  . TYR   B 1 1314 ? 24.47500   24.35400  26.27300  1.000 94.23326  ?  1312 TYR   B CA  1 
ATOM   24499 C  C   . TYR   B 1 1314 ? 23.91600   24.52900  24.86700  1.000 88.77892  ?  1312 TYR   B C   1 
ATOM   24500 O  O   . TYR   B 1 1314 ? 23.03600   25.36700  24.63800  1.000 81.01205  ?  1312 TYR   B O   1 
ATOM   24501 C  CB  . TYR   B 1 1314 ? 25.91000   24.88300  26.34100  1.000 90.80879  ?  1312 TYR   B CB  1 
ATOM   24502 C  CG  . TYR   B 1 1314 ? 26.04700   26.28800  25.78600  1.000 98.30270  ?  1312 TYR   B CG  1 
ATOM   24503 C  CD1 . TYR   B 1 1314 ? 25.59200   27.38700  26.50400  1.000 90.43663  ?  1312 TYR   B CD1 1 
ATOM   24504 C  CD2 . TYR   B 1 1314 ? 26.62200   26.51300  24.54000  1.000 98.34358  ?  1312 TYR   B CD2 1 
ATOM   24505 C  CE1 . TYR   B 1 1314 ? 25.70600   28.67200  25.99600  1.000 98.58238  ?  1312 TYR   B CE1 1 
ATOM   24506 C  CE2 . TYR   B 1 1314 ? 26.73900   27.79400  24.02400  1.000 91.60386  ?  1312 TYR   B CE2 1 
ATOM   24507 C  CZ  . TYR   B 1 1314 ? 26.28000   28.86800  24.75700  1.000 101.03526 ?  1312 TYR   B CZ  1 
ATOM   24508 O  OH  . TYR   B 1 1314 ? 26.39400   30.14300  24.24900  1.000 102.12730 ?  1312 TYR   B OH  1 
ATOM   24509 N  N   . ILE   B 1 1315 ? 24.41500   23.74000  23.91000  1.000 75.11090  ?  1313 ILE   B N   1 
ATOM   24510 C  CA  . ILE   B 1 1315 ? 23.99000   23.89500  22.52000  1.000 85.68864  ?  1313 ILE   B CA  1 
ATOM   24511 C  C   . ILE   B 1 1315 ? 22.50000   23.60600  22.38000  1.000 87.10105  ?  1313 ILE   B C   1 
ATOM   24512 O  O   . ILE   B 1 1315 ? 21.77000   24.33600  21.69900  1.000 82.38616  ?  1313 ILE   B O   1 
ATOM   24513 C  CB  . ILE   B 1 1315 ? 24.82900   22.99900  21.59200  1.000 72.65355  ?  1313 ILE   B CB  1 
ATOM   24514 C  CG1 . ILE   B 1 1315 ? 26.32500   23.21700  21.83800  1.000 81.10430  ?  1313 ILE   B CG1 1 
ATOM   24515 C  CG2 . ILE   B 1 1315 ? 24.48900   23.29000  20.15000  1.000 66.13930  ?  1313 ILE   B CG2 1 
ATOM   24516 C  CD1 . ILE   B 1 1315 ? 27.21000   22.76500  20.69000  1.000 70.94528  ?  1313 ILE   B CD1 1 
ATOM   24517 N  N   . PHE   B 1 1316 ? 22.02400   22.53900  23.02800  1.000 86.50562  ?  1314 PHE   B N   1 
ATOM   24518 C  CA  . PHE   B 1 1316 ? 20.59700   22.22900  22.98700  1.000 94.81052  ?  1314 PHE   B CA  1 
ATOM   24519 C  C   . PHE   B 1 1316 ? 19.77100   23.37200  23.56100  1.000 90.44859  ?  1314 PHE   B C   1 
ATOM   24520 O  O   . PHE   B 1 1316 ? 18.68200   23.67700  23.05900  1.000 84.95004  ?  1314 PHE   B O   1 
ATOM   24521 C  CB  . PHE   B 1 1316 ? 20.31700   20.93300  23.74700  1.000 91.20056  ?  1314 PHE   B CB  1 
ATOM   24522 N  N   . ALA   B 1 1317 ? 20.27800   24.02000  24.61000  1.000 89.06069  ?  1315 ALA   B N   1 
ATOM   24523 C  CA  . ALA   B 1 1317 ? 19.59400   25.17800  25.17400  1.000 86.84587  ?  1315 ALA   B CA  1 
ATOM   24524 C  C   . ALA   B 1 1317 ? 19.70300   26.38000  24.24500  1.000 83.89095  ?  1315 ALA   B C   1 
ATOM   24525 O  O   . ALA   B 1 1317 ? 18.68900   26.93900  23.80900  1.000 89.46863  ?  1315 ALA   B O   1 
ATOM   24526 C  CB  . ALA   B 1 1317 ? 20.17100   25.50500  26.55300  1.000 59.48191  ?  1315 ALA   B CB  1 
ATOM   24527 N  N   . ASP   B 1 1318 ? 20.93400   26.78500  23.92200  1.000 74.84430  ?  1316 ASP   B N   1 
ATOM   24528 C  CA  . ASP   B 1 1318 ? 21.15300   27.99500  23.13700  1.000 80.50703  ?  1316 ASP   B CA  1 
ATOM   24529 C  C   . ASP   B 1 1318 ? 20.51500   27.92100  21.75500  1.000 83.01430  ?  1316 ASP   B C   1 
ATOM   24530 O  O   . ASP   B 1 1318 ? 20.22200   28.96500  21.16300  1.000 91.50026  ?  1316 ASP   B O   1 
ATOM   24531 C  CB  . ASP   B 1 1318 ? 22.65600   28.26700  23.01200  1.000 76.27676  ?  1316 ASP   B CB  1 
ATOM   24532 C  CG  . ASP   B 1 1318 ? 22.96300   29.64800  22.45300  1.000 91.98418  ?  1316 ASP   B CG  1 
ATOM   24533 O  OD1 . ASP   B 1 1318 ? 22.77600   30.64800  23.17900  1.000 92.70110  ?  1316 ASP   B OD1 1 
ATOM   24534 O  OD2 . ASP   B 1 1318 ? 23.40200   29.73100  21.28600  1.000 97.40121  -1 1316 ASP   B OD2 1 
ATOM   24535 N  N   . SER   B 1 1319 ? 20.28000   26.71900  21.23100  1.000 77.69996  ?  1317 SER   B N   1 
ATOM   24536 C  CA  . SER   B 1 1319 ? 19.71600   26.59700  19.89400  1.000 83.19737  ?  1317 SER   B CA  1 
ATOM   24537 C  C   . SER   B 1 1319 ? 18.20700   26.41900  19.90500  1.000 75.96075  ?  1317 SER   B C   1 
ATOM   24538 O  O   . SER   B 1 1319 ? 17.53700   26.82500  18.94800  1.000 64.87453  ?  1317 SER   B O   1 
ATOM   24539 C  CB  . SER   B 1 1319 ? 20.36100   25.42500  19.14900  1.000 73.51234  ?  1317 SER   B CB  1 
ATOM   24540 O  OG  . SER   B 1 1319 ? 20.04300   24.18800  19.76400  1.000 88.17276  ?  1317 SER   B OG  1 
ATOM   24541 N  N   . GLY   B 1 1320 ? 17.65700   25.84100  20.96900  1.000 87.61725  ?  1318 GLY   B N   1 
ATOM   24542 C  CA  . GLY   B 1 1320 ? 16.25100   25.50600  20.96800  1.000 90.23964  ?  1318 GLY   B CA  1 
ATOM   24543 C  C   . GLY   B 1 1320 ? 15.87900   24.45000  19.95600  1.000 96.97777  ?  1318 GLY   B C   1 
ATOM   24544 O  O   . GLY   B 1 1320 ? 14.70700   24.34600  19.58400  1.000 103.85461 ?  1318 GLY   B O   1 
ATOM   24545 N  N   . ALA   B 1 1321 ? 16.84900   23.66900  19.48800  1.000 90.68517  ?  1319 ALA   B N   1 
ATOM   24546 C  CA  . ALA   B 1 1321 ? 16.56900   22.60000  18.54300  1.000 92.10248  ?  1319 ALA   B CA  1 
ATOM   24547 C  C   . ALA   B 1 1321 ? 15.89800   21.42800  19.25100  1.000 86.91282  ?  1319 ALA   B C   1 
ATOM   24548 O  O   . ALA   B 1 1321 ? 16.16800   21.14300  20.42200  1.000 76.36123  ?  1319 ALA   B O   1 
ATOM   24549 C  CB  . ALA   B 1 1321 ? 17.85900   22.14200  17.86100  1.000 75.21836  ?  1319 ALA   B CB  1 
ATOM   24550 N  N   . LYS   B 1 1322 ? 15.00500   20.75000  18.52900  1.000 63.24417  ?  1320 LYS   B N   1 
ATOM   24551 C  CA  . LYS   B 1 1322 ? 14.24500   19.63300  19.07800  1.000 85.84893  ?  1320 LYS   B CA  1 
ATOM   24552 C  C   . LYS   B 1 1322 ? 14.63800   18.27900  18.50700  1.000 76.23709  ?  1320 LYS   B C   1 
ATOM   24553 O  O   . LYS   B 1 1322 ? 14.47900   17.26700  19.19400  1.000 83.18930  ?  1320 LYS   B O   1 
ATOM   24554 C  CB  . LYS   B 1 1322 ? 12.74200   19.85000  18.85100  1.000 68.14642  ?  1320 LYS   B CB  1 
ATOM   24555 N  N   . LEU   B 1 1323 ? 15.15600   18.23600  17.28300  1.000 70.93261  ?  1321 LEU   B N   1 
ATOM   24556 C  CA  . LEU   B 1 1323 ? 15.50600   16.99500  16.60300  1.000 69.85256  ?  1321 LEU   B CA  1 
ATOM   24557 C  C   . LEU   B 1 1323 ? 17.02100   16.83100  16.57600  1.000 76.28851  ?  1321 LEU   B C   1 
ATOM   24558 O  O   . LEU   B 1 1323 ? 17.74400   17.77300  16.23400  1.000 67.85742  ?  1321 LEU   B O   1 
ATOM   24559 C  CB  . LEU   B 1 1323 ? 14.94600   16.99000  15.17800  1.000 65.01856  ?  1321 LEU   B CB  1 
ATOM   24560 C  CG  . LEU   B 1 1323 ? 14.63000   15.63800  14.53900  1.000 72.87417  ?  1321 LEU   B CG  1 
ATOM   24561 C  CD1 . LEU   B 1 1323 ? 13.59300   15.81100  13.44200  1.000 72.64366  ?  1321 LEU   B CD1 1 
ATOM   24562 C  CD2 . LEU   B 1 1323 ? 15.88500   14.96800  13.99500  1.000 82.17727  ?  1321 LEU   B CD2 1 
ATOM   24563 N  N   . VAL   B 1 1324 ? 17.49700   15.63800  16.93300  1.000 82.00638  ?  1322 VAL   B N   1 
ATOM   24564 C  CA  . VAL   B 1 1324 ? 18.91800   15.30300  16.87000  1.000 72.92825  ?  1322 VAL   B CA  1 
ATOM   24565 C  C   . VAL   B 1 1324 ? 19.06700   13.95600  16.17400  1.000 67.26758  ?  1322 VAL   B C   1 
ATOM   24566 O  O   . VAL   B 1 1324 ? 18.59000   12.93200  16.67800  1.000 70.95717  ?  1322 VAL   B O   1 
ATOM   24567 C  CB  . VAL   B 1 1324 ? 19.57900   15.28000  18.26200  1.000 61.95447  ?  1322 VAL   B CB  1 
ATOM   24568 C  CG1 . VAL   B 1 1324 ? 18.73600   14.50400  19.25700  1.000 73.77670  ?  1322 VAL   B CG1 1 
ATOM   24569 C  CG2 . VAL   B 1 1324 ? 20.98300   14.68500  18.17900  1.000 54.55553  ?  1322 VAL   B CG2 1 
ATOM   24570 N  N   . LEU   B 1 1325 ? 19.70400   13.95900  15.00700  1.000 60.32690  ?  1323 LEU   B N   1 
ATOM   24571 C  CA  . LEU   B 1 1325 ? 20.06300   12.72000  14.33200  1.000 57.79829  ?  1323 LEU   B CA  1 
ATOM   24572 C  C   . LEU   B 1 1325 ? 21.38900   12.23000  14.89900  1.000 56.21340  ?  1323 LEU   B C   1 
ATOM   24573 O  O   . LEU   B 1 1325 ? 22.40700   12.92200  14.78800  1.000 68.62450  ?  1323 LEU   B O   1 
ATOM   24574 C  CB  . LEU   B 1 1325 ? 20.16100   12.94100  12.82400  1.000 56.85747  ?  1323 LEU   B CB  1 
ATOM   24575 C  CG  . LEU   B 1 1325 ? 18.87000   12.84700  12.00900  1.000 65.43185  ?  1323 LEU   B CG  1 
ATOM   24576 C  CD1 . LEU   B 1 1325 ? 19.02200   13.57700  10.68100  1.000 57.38617  ?  1323 LEU   B CD1 1 
ATOM   24577 C  CD2 . LEU   B 1 1325 ? 18.48200   11.39500  11.78500  1.000 74.67362  ?  1323 LEU   B CD2 1 
ATOM   24578 N  N   . ALA   B 1 1326 ? 21.38200   11.05200  15.51900  1.000 64.29915  ?  1324 ALA   B N   1 
ATOM   24579 C  CA  . ALA   B 1 1326 ? 22.55200   10.54700  16.22200  1.000 64.05662  ?  1324 ALA   B CA  1 
ATOM   24580 C  C   . ALA   B 1 1326 ? 22.81400   9.09300   15.85800  1.000 64.85253  ?  1324 ALA   B C   1 
ATOM   24581 O  O   . ALA   B 1 1326 ? 21.90900   8.36000   15.44900  1.000 57.93321  ?  1324 ALA   B O   1 
ATOM   24582 C  CB  . ALA   B 1 1326 ? 22.39000   10.67300  17.74500  1.000 59.42170  ?  1324 ALA   B CB  1 
ATOM   24583 N  N   . GLN   B 1 1327 ? 24.07200   8.68900   16.00800  1.000 71.16463  ?  1325 GLN   B N   1 
ATOM   24584 C  CA  . GLN   B 1 1327 ? 24.45900   7.29900   15.84200  1.000 63.95537  ?  1325 GLN   B CA  1 
ATOM   24585 C  C   . GLN   B 1 1327 ? 24.16800   6.51900   17.12000  1.000 72.60368  ?  1325 GLN   B C   1 
ATOM   24586 O  O   . GLN   B 1 1327 ? 23.95900   7.09100   18.19300  1.000 78.76466  ?  1325 GLN   B O   1 
ATOM   24587 C  CB  . GLN   B 1 1327 ? 25.94200   7.18700   15.48700  1.000 54.77535  ?  1325 GLN   B CB  1 
ATOM   24588 C  CG  . GLN   B 1 1327 ? 26.26400   7.47300   14.03000  1.000 43.78149  ?  1325 GLN   B CG  1 
ATOM   24589 C  CD  . GLN   B 1 1327 ? 27.75600   7.43700   13.75300  1.000 55.10730  ?  1325 GLN   B CD  1 
ATOM   24590 O  OE1 . GLN   B 1 1327 ? 28.57000   7.59000   14.66300  1.000 54.38531  ?  1325 GLN   B OE1 1 
ATOM   24591 N  NE2 . GLN   B 1 1327 ? 28.12100   7.23200   12.49100  1.000 53.11872  ?  1325 GLN   B NE2 1 
ATOM   24592 N  N   . SER   B 1 1328 ? 24.16600   5.19200   16.98900  1.000 70.27635  ?  1326 SER   B N   1 
ATOM   24593 C  CA  . SER   B 1 1328 ? 23.81000   4.31200   18.10200  1.000 64.37395  ?  1326 SER   B CA  1 
ATOM   24594 C  C   . SER   B 1 1328 ? 24.61400   4.56400   19.37300  1.000 62.81517  ?  1326 SER   B C   1 
ATOM   24595 O  O   . SER   B 1 1328 ? 24.00000   4.67200   20.44700  1.000 66.22401  ?  1326 SER   B O   1 
ATOM   24596 C  CB  . SER   B 1 1328 ? 23.93700   2.85000   17.65100  1.000 76.18168  ?  1326 SER   B CB  1 
ATOM   24597 O  OG  . SER   B 1 1328 ? 23.07000   2.57600   16.56500  1.000 90.27949  ?  1326 SER   B OG  1 
ATOM   24598 N  N   . PRO   B 1 1329 ? 25.94900   4.67400   19.34600  1.000 63.01161  ?  1327 PRO   B N   1 
ATOM   24599 C  CA  . PRO   B 1 1329 ? 26.68200   4.88800   20.60600  1.000 60.09776  ?  1327 PRO   B CA  1 
ATOM   24600 C  C   . PRO   B 1 1329 ? 26.45400   6.25600   21.23000  1.000 66.95763  ?  1327 PRO   B C   1 
ATOM   24601 O  O   . PRO   B 1 1329 ? 26.88500   6.47100   22.37100  1.000 69.70539  ?  1327 PRO   B O   1 
ATOM   24602 C  CB  . PRO   B 1 1329 ? 28.15300   4.70600   20.19700  1.000 48.08236  ?  1327 PRO   B CB  1 
ATOM   24603 C  CG  . PRO   B 1 1329 ? 28.11500   4.03000   18.86100  1.000 59.47796  ?  1327 PRO   B CG  1 
ATOM   24604 C  CD  . PRO   B 1 1329 ? 26.87800   4.54000   18.21000  1.000 61.57289  ?  1327 PRO   B CD  1 
ATOM   24605 N  N   . PHE   B 1 1330 ? 25.79100   7.18200   20.53300  1.000 70.57628  ?  1328 PHE   B N   1 
ATOM   24606 C  CA  . PHE   B 1 1330 ? 25.57900   8.53200   21.04000  1.000 80.17824  ?  1328 PHE   B CA  1 
ATOM   24607 C  C   . PHE   B 1 1330 ? 24.10300   8.89900   21.15400  1.000 74.03704  ?  1328 PHE   B C   1 
ATOM   24608 O  O   . PHE   B 1 1330 ? 23.78300   10.07800  21.34400  1.000 72.27263  ?  1328 PHE   B O   1 
ATOM   24609 C  CB  . PHE   B 1 1330 ? 26.30700   9.55000   20.15400  1.000 75.00010  ?  1328 PHE   B CB  1 
ATOM   24610 C  CG  . PHE   B 1 1330 ? 27.65300   9.08100   19.67200  1.000 66.36859  ?  1328 PHE   B CG  1 
ATOM   24611 C  CD1 . PHE   B 1 1330 ? 28.69000   8.86900   20.56800  1.000 61.34139  ?  1328 PHE   B CD1 1 
ATOM   24612 C  CD2 . PHE   B 1 1330 ? 27.88200   8.85200   18.32400  1.000 67.22055  ?  1328 PHE   B CD2 1 
ATOM   24613 C  CE1 . PHE   B 1 1330 ? 29.93000   8.43600   20.12900  1.000 61.96492  ?  1328 PHE   B CE1 1 
ATOM   24614 C  CE2 . PHE   B 1 1330 ? 29.11900   8.42000   17.87700  1.000 65.29535  ?  1328 PHE   B CE2 1 
ATOM   24615 C  CZ  . PHE   B 1 1330 ? 30.14500   8.21100   18.78200  1.000 63.77062  ?  1328 PHE   B CZ  1 
ATOM   24616 N  N   . VAL   B 1 1331 ? 23.19600   7.92600   21.04000  1.000 80.09616  ?  1329 VAL   B N   1 
ATOM   24617 C  CA  . VAL   B 1 1331 ? 21.77800   8.21900   21.22700  1.000 79.83255  ?  1329 VAL   B CA  1 
ATOM   24618 C  C   . VAL   B 1 1331 ? 21.47800   8.46900   22.70100  1.000 76.71551  ?  1329 VAL   B C   1 
ATOM   24619 O  O   . VAL   B 1 1331 ? 20.57200   9.24200   23.04000  1.000 68.19425  ?  1329 VAL   B O   1 
ATOM   24620 C  CB  . VAL   B 1 1331 ? 20.92100   7.07700   20.64100  1.000 65.86348  ?  1329 VAL   B CB  1 
ATOM   24621 C  CG1 . VAL   B 1 1331 ? 19.49400   7.13800   21.15400  1.000 66.02490  ?  1329 VAL   B CG1 1 
ATOM   24622 C  CG2 . VAL   B 1 1331 ? 20.92300   7.13800   19.11800  1.000 59.21240  ?  1329 VAL   B CG2 1 
ATOM   24623 N  N   . GLU   B 1 1332 ? 22.25200   7.85100   23.59800  1.000 89.05145  ?  1330 GLU   B N   1 
ATOM   24624 C  CA  . GLU   B 1 1332 ? 22.04500   8.04900   25.03000  1.000 88.35450  ?  1330 GLU   B CA  1 
ATOM   24625 C  C   . GLU   B 1 1332 ? 22.33700   9.48700   25.44400  1.000 94.06125  ?  1330 GLU   B C   1 
ATOM   24626 O  O   . GLU   B 1 1332 ? 21.60900   10.06200  26.26200  1.000 102.03741 ?  1330 GLU   B O   1 
ATOM   24627 C  CB  . GLU   B 1 1332 ? 22.92000   7.07700   25.82500  1.000 85.68225  ?  1330 GLU   B CB  1 
ATOM   24628 C  CG  . GLU   B 1 1332 ? 24.41200   7.20700   25.53500  1.000 88.04488  ?  1330 GLU   B CG  1 
ATOM   24629 C  CD  . GLU   B 1 1332 ? 25.27000   6.33600   26.43000  1.000 101.94769 ?  1330 GLU   B CD  1 
ATOM   24630 O  OE1 . GLU   B 1 1332 ? 24.72700   5.40500   27.06200  1.000 103.36512 ?  1330 GLU   B OE1 1 
ATOM   24631 O  OE2 . GLU   B 1 1332 ? 26.49100   6.59000   26.50500  1.000 95.28114  -1 1330 GLU   B OE2 1 
ATOM   24632 N  N   . LYS   B 1 1333 ? 23.39700   10.08600  24.89300  1.000 86.95655  ?  1331 LYS   B N   1 
ATOM   24633 C  CA  . LYS   B 1 1333 ? 23.77400   11.43700  25.29000  1.000 75.17301  ?  1331 LYS   B CA  1 
ATOM   24634 C  C   . LYS   B 1 1333 ? 22.72700   12.46000  24.87000  1.000 69.81463  ?  1331 LYS   B C   1 
ATOM   24635 O  O   . LYS   B 1 1333 ? 22.50200   13.44500  25.58300  1.000 69.09083  ?  1331 LYS   B O   1 
ATOM   24636 C  CB  . LYS   B 1 1333 ? 25.13700   11.79300  24.69700  1.000 73.66512  ?  1331 LYS   B CB  1 
ATOM   24637 C  CG  . LYS   B 1 1333 ? 26.25000   10.82700  25.08000  1.000 81.23572  ?  1331 LYS   B CG  1 
ATOM   24638 C  CD  . LYS   B 1 1333 ? 27.53700   11.14500  24.33400  1.000 87.30139  ?  1331 LYS   B CD  1 
ATOM   24639 C  CE  . LYS   B 1 1333 ? 28.73700   10.48700  24.99600  1.000 78.16196  ?  1331 LYS   B CE  1 
ATOM   24640 N  NZ  . LYS   B 1 1333 ? 29.59400   11.47800  25.70600  1.000 82.14916  ?  1331 LYS   B NZ  1 
ATOM   24641 N  N   . ALA   B 1 1334 ? 22.07500   12.24300  23.72800  1.000 72.22508  ?  1332 ALA   B N   1 
ATOM   24642 C  CA  . ALA   B 1 1334 ? 21.02500   13.12500  23.24200  1.000 83.89589  ?  1332 ALA   B CA  1 
ATOM   24643 C  C   . ALA   B 1 1334 ? 19.65900   12.77800  23.81500  1.000 94.66120  ?  1332 ALA   B C   1 
ATOM   24644 O  O   . ALA   B 1 1334 ? 18.64000   13.21400  23.26800  1.000 90.67232  ?  1332 ALA   B O   1 
ATOM   24645 C  CB  . ALA   B 1 1334 ? 20.97700   13.09600  21.71300  1.000 52.85523  ?  1332 ALA   B CB  1 
ATOM   24646 N  N   . SER   B 1 1335 ? 19.61800   12.00500  24.90600  1.000 92.54050  ?  1333 SER   B N   1 
ATOM   24647 C  CA  . SER   B 1 1335 ? 18.34500   11.68600  25.54500  1.000 96.23285  ?  1333 SER   B CA  1 
ATOM   24648 C  C   . SER   B 1 1335 ? 17.58500   12.94500  25.94300  1.000 96.31358  ?  1333 SER   B C   1 
ATOM   24649 O  O   . SER   B 1 1335 ? 16.35200   12.92600  26.01500  1.000 88.87466  ?  1333 SER   B O   1 
ATOM   24650 C  CB  . SER   B 1 1335 ? 18.57600   10.80600  26.77500  1.000 96.44981  ?  1333 SER   B CB  1 
ATOM   24651 O  OG  . SER   B 1 1335 ? 19.75900   11.18300  27.45800  1.000 90.31293  ?  1333 SER   B OG  1 
ATOM   24652 N  N   . MET   B 1 1336 ? 18.29500   14.05200  26.18800  1.000 86.27415  ?  1334 MET   B N   1 
ATOM   24653 C  CA  . MET   B 1 1336 ? 17.66200   15.28800  26.61700  1.000 84.90661  ?  1334 MET   B CA  1 
ATOM   24654 C  C   . MET   B 1 1336 ? 16.96500   16.01200  25.48800  1.000 86.74852  ?  1334 MET   B C   1 
ATOM   24655 O  O   . MET   B 1 1336 ? 16.63600   17.19700  25.62600  1.000 78.96977  ?  1334 MET   B O   1 
ATOM   24656 C  CB  . MET   B 1 1336 ? 18.68400   16.19200  27.29600  1.000 89.92480  ?  1334 MET   B CB  1 
ATOM   24657 C  CG  . MET   B 1 1336 ? 19.14200   15.64200  28.63100  1.000 100.72728 ?  1334 MET   B CG  1 
ATOM   24658 S  SD  . MET   B 1 1336 ? 18.00600   15.01100  29.93200  1.000 118.90318 ?  1334 MET   B SD  1 
ATOM   24659 C  CE  . MET   B 1 1336 ? 16.39100   15.80300  29.75400  1.000 81.23283  ?  1334 MET   B CE  1 
ATOM   24660 N  N   . ALA   B 1 1337 ? 16.75800   15.34700  24.35800  1.000 87.20831  ?  1335 ALA   B N   1 
ATOM   24661 C  CA  . ALA   B 1 1337 ? 15.96700   15.88300  23.26000  1.000 79.74610  ?  1335 ALA   B CA  1 
ATOM   24662 C  C   . ALA   B 1 1337 ? 14.75600   14.99300  23.03200  1.000 91.74286  ?  1335 ALA   B C   1 
ATOM   24663 O  O   . ALA   B 1 1337 ? 14.77600   13.79700  23.33700  1.000 82.54275  ?  1335 ALA   B O   1 
ATOM   24664 C  CB  . ALA   B 1 1337 ? 16.77900   15.99700  21.96300  1.000 79.30584  ?  1335 ALA   B CB  1 
ATOM   24665 N  N   . GLU   B 1 1338 ? 13.69600   15.58900  22.49100  1.000 92.98271  ?  1336 GLU   B N   1 
ATOM   24666 C  CA  . GLU   B 1 1338 ? 12.45500   14.84700  22.29800  1.000 92.78609  ?  1336 GLU   B CA  1 
ATOM   24667 C  C   . GLU   B 1 1338 ? 12.55000   13.90600  21.10100  1.000 94.94191  ?  1336 GLU   B C   1 
ATOM   24668 O  O   . GLU   B 1 1338 ? 12.09100   12.75800  21.16200  1.000 110.82496 ?  1336 GLU   B O   1 
ATOM   24669 C  CB  . GLU   B 1 1338 ? 11.29700   15.82800  22.14000  1.000 104.17790 ?  1336 GLU   B CB  1 
ATOM   24670 C  CG  . GLU   B 1 1338 ? 11.71800   17.14300  21.50600  1.000 100.94886 ?  1336 GLU   B CG  1 
ATOM   24671 C  CD  . GLU   B 1 1338 ? 10.55700   18.09400  21.29600  1.000 112.88551 ?  1336 GLU   B CD  1 
ATOM   24672 O  OE1 . GLU   B 1 1338 ? 9.86100    17.97500  20.26700  1.000 104.82494 ?  1336 GLU   B OE1 1 
ATOM   24673 O  OE2 . GLU   B 1 1338 ? 10.35400   18.97900  22.15400  1.000 95.25499  -1 1336 GLU   B OE2 1 
ATOM   24674 N  N   . VAL   B 1 1339 ? 13.15500   14.36500  20.00900  1.000 82.30292  ?  1337 VAL   B N   1 
ATOM   24675 C  CA  . VAL   B 1 1339 ? 13.30500   13.57000  18.79500  1.000 79.19201  ?  1337 VAL   B CA  1 
ATOM   24676 C  C   . VAL   B 1 1339 ? 14.77500   13.20300  18.66600  1.000 78.99243  ?  1337 VAL   B C   1 
ATOM   24677 O  O   . VAL   B 1 1339 ? 15.61100   14.05000  18.32400  1.000 81.26874  ?  1337 VAL   B O   1 
ATOM   24678 C  CB  . VAL   B 1 1339 ? 12.80100   14.31800  17.55400  1.000 69.85250  ?  1337 VAL   B CB  1 
ATOM   24679 C  CG1 . VAL   B 1 1339 ? 12.53800   13.34400  16.41200  1.000 68.31964  ?  1337 VAL   B CG1 1 
ATOM   24680 C  CG2 . VAL   B 1 1339 ? 11.53900   15.10300  17.88600  1.000 61.87510  ?  1337 VAL   B CG2 1 
ATOM   24681 N  N   . VAL   B 1 1340 ? 15.09400   11.94300  18.95300  1.000 76.34449  ?  1338 VAL   B N   1 
ATOM   24682 C  CA  . VAL   B 1 1340 ? 16.45200   11.43200  18.81700  1.000 73.06476  ?  1338 VAL   B CA  1 
ATOM   24683 C  C   . VAL   B 1 1340 ? 16.45200   10.27900  17.82300  1.000 64.37785  ?  1338 VAL   B C   1 
ATOM   24684 O  O   . VAL   B 1 1340 ? 16.53800   9.11000   18.21500  1.000 84.17743  ?  1338 VAL   B O   1 
ATOM   24685 C  CB  . VAL   B 1 1340 ? 17.02400   10.98500  20.17600  1.000 76.72973  ?  1338 VAL   B CB  1 
ATOM   24686 C  CG1 . VAL   B 1 1340 ? 18.54300   10.89700  20.11400  1.000 63.44274  ?  1338 VAL   B CG1 1 
ATOM   24687 C  CG2 . VAL   B 1 1340 ? 16.58400   11.93600  21.27600  1.000 75.88624  ?  1338 VAL   B CG2 1 
ATOM   24688 N  N   . LEU   B 1 1341 ? 16.35400   10.59700  16.53500  1.000 61.43184  ?  1339 LEU   B N   1 
ATOM   24689 C  CA  . LEU   B 1 1341 ? 16.37700   9.56800   15.50400  1.000 70.44512  ?  1339 LEU   B CA  1 
ATOM   24690 C  C   . LEU   B 1 1341 ? 17.74300   8.89200   15.45000  1.000 86.08372  ?  1339 LEU   B C   1 
ATOM   24691 O  O   . LEU   B 1 1341 ? 18.77900   9.56300   15.40200  1.000 79.26705  ?  1339 LEU   B O   1 
ATOM   24692 C  CB  . LEU   B 1 1341 ? 16.03700   10.17300  14.14400  1.000 54.27239  ?  1339 LEU   B CB  1 
ATOM   24693 C  CG  . LEU   B 1 1341 ? 14.57700   10.54900  13.90400  1.000 67.95311  ?  1339 LEU   B CG  1 
ATOM   24694 C  CD1 . LEU   B 1 1341 ? 14.42100   11.21200  12.54400  1.000 68.96215  ?  1339 LEU   B CD1 1 
ATOM   24695 C  CD2 . LEU   B 1 1341 ? 13.68400   9.32200   14.01600  1.000 69.80489  ?  1339 LEU   B CD2 1 
ATOM   24696 N  N   . ASP   B 1 1342 ? 17.74400   7.55900   15.45400  1.000 77.37919  ?  1340 ASP   B N   1 
ATOM   24697 C  CA  . ASP   B 1 1342 ? 18.97200   6.78100   15.33300  1.000 67.66281  ?  1340 ASP   B CA  1 
ATOM   24698 C  C   . ASP   B 1 1342 ? 19.31100   6.61700   13.85600  1.000 71.87080  ?  1340 ASP   B C   1 
ATOM   24699 O  O   . ASP   B 1 1342 ? 18.52200   6.05000   13.09300  1.000 73.74698  ?  1340 ASP   B O   1 
ATOM   24700 C  CB  . ASP   B 1 1342 ? 18.82100   5.41800   16.01000  1.000 66.69988  ?  1340 ASP   B CB  1 
ATOM   24701 C  CG  . ASP   B 1 1342 ? 20.13600   4.65600   16.10300  1.000 67.94212  ?  1340 ASP   B CG  1 
ATOM   24702 O  OD1 . ASP   B 1 1342 ? 21.15300   5.12900   15.55200  1.000 73.14801  ?  1340 ASP   B OD1 1 
ATOM   24703 O  OD2 . ASP   B 1 1342 ? 20.15300   3.57700   16.73300  1.000 72.80465  -1 1340 ASP   B OD2 1 
ATOM   24704 N  N   . LEU   B 1 1343 ? 20.48400   7.11400   13.45700  1.000 68.88735  ?  1341 LEU   B N   1 
ATOM   24705 C  CA  . LEU   B 1 1343 ? 20.92900   6.97800   12.07600  1.000 66.62578  ?  1341 LEU   B CA  1 
ATOM   24706 C  C   . LEU   B 1 1343 ? 21.27600   5.54200   11.70800  1.000 75.46921  ?  1341 LEU   B C   1 
ATOM   24707 O  O   . LEU   B 1 1343 ? 21.41100   5.24200   10.51700  1.000 66.97984  ?  1341 LEU   B O   1 
ATOM   24708 C  CB  . LEU   B 1 1343 ? 22.13700   7.88200   11.82100  1.000 68.30990  ?  1341 LEU   B CB  1 
ATOM   24709 C  CG  . LEU   B 1 1343 ? 21.85000   9.38100   11.73100  1.000 60.17650  ?  1341 LEU   B CG  1 
ATOM   24710 C  CD1 . LEU   B 1 1343 ? 23.07100   10.18100  12.14000  1.000 60.27197  ?  1341 LEU   B CD1 1 
ATOM   24711 C  CD2 . LEU   B 1 1343 ? 21.42200   9.74900   10.32500  1.000 55.14869  ?  1341 LEU   B CD2 1 
ATOM   24712 N  N   . ASN   B 1 1344 ? 21.41900   4.65600   12.69400  1.000 68.64703  ?  1342 ASN   B N   1 
ATOM   24713 C  CA  . ASN   B 1 1344 ? 21.76400   3.26300   12.45000  1.000 71.71704  ?  1342 ASN   B CA  1 
ATOM   24714 C  C   . ASN   B 1 1344 ? 20.56800   2.32400   12.52900  1.000 75.70893  ?  1342 ASN   B C   1 
ATOM   24715 O  O   . ASN   B 1 1344 ? 20.72100   1.13200   12.24500  1.000 77.58251  ?  1342 ASN   B O   1 
ATOM   24716 C  CB  . ASN   B 1 1344 ? 22.83300   2.80000   13.44500  1.000 70.89475  ?  1342 ASN   B CB  1 
ATOM   24717 C  CG  . ASN   B 1 1344 ? 24.13100   3.56800   13.30400  1.000 65.45678  ?  1342 ASN   B CG  1 
ATOM   24718 O  OD1 . ASN   B 1 1344 ? 24.70400   4.02500   14.29300  1.000 62.09091  ?  1342 ASN   B OD1 1 
ATOM   24719 N  ND2 . ASN   B 1 1344 ? 24.60400   3.71100   12.07100  1.000 42.74964  ?  1342 ASN   B ND2 1 
ATOM   24720 N  N   . SER   B 1 1345 ? 19.39800   2.81700   12.91800  1.000 73.95604  ?  1343 SER   B N   1 
ATOM   24721 C  CA  . SER   B 1 1345 ? 18.17900   2.02000   12.92800  1.000 59.92022  ?  1343 SER   B CA  1 
ATOM   24722 C  C   . SER   B 1 1345 ? 17.41300   2.26600   11.63600  1.000 63.21518  ?  1343 SER   B C   1 
ATOM   24723 O  O   . SER   B 1 1345 ? 17.20300   3.41900   11.24400  1.000 63.78929  ?  1343 SER   B O   1 
ATOM   24724 C  CB  . SER   B 1 1345 ? 17.30500   2.35900   14.13600  1.000 48.64643  ?  1343 SER   B CB  1 
ATOM   24725 O  OG  . SER   B 1 1345 ? 16.01100   1.79700   13.99700  1.000 66.54468  ?  1343 SER   B OG  1 
ATOM   24726 N  N   . ALA   B 1 1346 ? 17.00400   1.18300   10.97500  1.000 62.49008  ?  1344 ALA   B N   1 
ATOM   24727 C  CA  . ALA   B 1 1346 ? 16.25100   1.31100   9.73500   1.000 56.83989  ?  1344 ALA   B CA  1 
ATOM   24728 C  C   . ALA   B 1 1346 ? 14.86500   1.90500   9.95200   1.000 65.12702  ?  1344 ALA   B C   1 
ATOM   24729 O  O   . ALA   B 1 1346 ? 14.22100   2.30000   8.97300   1.000 55.26354  ?  1344 ALA   B O   1 
ATOM   24730 C  CB  . ALA   B 1 1346 ? 16.14200   -0.05100  9.04900   1.000 46.96122  ?  1344 ALA   B CB  1 
ATOM   24731 N  N   . SER   B 1 1347 ? 14.40000   1.98400   11.20400  1.000 59.88798  ?  1345 SER   B N   1 
ATOM   24732 C  CA  . SER   B 1 1347 ? 13.11400   2.61300   11.48700  1.000 61.85351  ?  1345 SER   B CA  1 
ATOM   24733 C  C   . SER   B 1 1347 ? 13.12900   4.09900   11.15000  1.000 73.08188  ?  1345 SER   B C   1 
ATOM   24734 O  O   . SER   B 1 1347 ? 12.07700   4.68000   10.85900  1.000 80.73162  ?  1345 SER   B O   1 
ATOM   24735 C  CB  . SER   B 1 1347 ? 12.74200   2.40500   12.95700  1.000 61.63688  ?  1345 SER   B CB  1 
ATOM   24736 O  OG  . SER   B 1 1347 ? 13.69100   3.00800   13.82200  1.000 56.38478  ?  1345 SER   B OG  1 
ATOM   24737 N  N   . SER   B 1 1348 ? 14.30300   4.72500   11.18000  1.000 68.30877  ?  1346 SER   B N   1 
ATOM   24738 C  CA  . SER   B 1 1348 ? 14.45100   6.13900   10.86900  1.000 60.08821  ?  1346 SER   B CA  1 
ATOM   24739 C  C   . SER   B 1 1348 ? 14.54400   6.41600   9.37200   1.000 62.36679  ?  1346 SER   B C   1 
ATOM   24740 O  O   . SER   B 1 1348 ? 14.78900   7.56300   8.98400   1.000 67.88677  ?  1346 SER   B O   1 
ATOM   24741 C  CB  . SER   B 1 1348 ? 15.68400   6.69900   11.58400  1.000 62.40133  ?  1346 SER   B CB  1 
ATOM   24742 O  OG  . SER   B 1 1348 ? 15.64800   6.38200   12.96500  1.000 67.74366  ?  1346 SER   B OG  1 
ATOM   24743 N  N   . TYR   B 1 1349 ? 14.35200   5.40700   8.52700   1.000 62.81627  ?  1347 TYR   B N   1 
ATOM   24744 C  CA  . TYR   B 1 1349 ? 14.38500   5.57000   7.07900   1.000 66.56997  ?  1347 TYR   B CA  1 
ATOM   24745 C  C   . TYR   B 1 1349 ? 13.05600   5.11100   6.49700   1.000 77.82016  ?  1347 TYR   B C   1 
ATOM   24746 O  O   . TYR   B 1 1349 ? 12.56700   4.02800   6.83600   1.000 89.40403  ?  1347 TYR   B O   1 
ATOM   24747 C  CB  . TYR   B 1 1349 ? 15.54300   4.78000   6.45900   1.000 62.74838  ?  1347 TYR   B CB  1 
ATOM   24748 C  CG  . TYR   B 1 1349 ? 16.91600   5.27300   6.86500   1.000 63.11299  ?  1347 TYR   B CG  1 
ATOM   24749 C  CD1 . TYR   B 1 1349 ? 17.45700   4.94200   8.10200   1.000 62.56326  ?  1347 TYR   B CD1 1 
ATOM   24750 C  CD2 . TYR   B 1 1349 ? 17.67300   6.06600   6.01100   1.000 65.72318  ?  1347 TYR   B CD2 1 
ATOM   24751 C  CE1 . TYR   B 1 1349 ? 18.71000   5.38900   8.47800   1.000 66.81568  ?  1347 TYR   B CE1 1 
ATOM   24752 C  CE2 . TYR   B 1 1349 ? 18.92900   6.51700   6.37700   1.000 57.24235  ?  1347 TYR   B CE2 1 
ATOM   24753 C  CZ  . TYR   B 1 1349 ? 19.44200   6.17500   7.61200   1.000 68.73650  ?  1347 TYR   B CZ  1 
ATOM   24754 O  OH  . TYR   B 1 1349 ? 20.69000   6.62000   7.98500   1.000 63.58855  ?  1347 TYR   B OH  1 
ATOM   24755 N  N   . ALA   B 1 1350 ? 12.47500   5.93500   5.62700   1.000 75.26128  ?  1348 ALA   B N   1 
ATOM   24756 C  CA  . ALA   B 1 1350 ? 11.18300   5.62900   5.03200   1.000 71.99242  ?  1348 ALA   B CA  1 
ATOM   24757 C  C   . ALA   B 1 1350 ? 11.35800   4.73000   3.81100   1.000 87.24210  ?  1348 ALA   B C   1 
ATOM   24758 O  O   . ALA   B 1 1350 ? 12.46800   4.33500   3.44300   1.000 87.19743  ?  1348 ALA   B O   1 
ATOM   24759 C  CB  . ALA   B 1 1350 ? 10.44800   6.91500   4.66400   1.000 63.96127  ?  1348 ALA   B CB  1 
ATOM   24760 N  N   . ALA   B 1 1351 ? 10.23700   4.40600   3.16600   1.000 82.74041  ?  1349 ALA   B N   1 
ATOM   24761 C  CA  . ALA   B 1 1351 ? 10.25200   3.51700   2.01300   1.000 78.29818  ?  1349 ALA   B CA  1 
ATOM   24762 C  C   . ALA   B 1 1351 ? 10.38000   4.25300   0.68700   1.000 86.06275  ?  1349 ALA   B C   1 
ATOM   24763 O  O   . ALA   B 1 1351 ? 10.73200   3.62700   -0.32000  1.000 77.12487  ?  1349 ALA   B O   1 
ATOM   24764 C  CB  . ALA   B 1 1351 ? 8.98300    2.66000   1.99300   1.000 76.01420  ?  1349 ALA   B CB  1 
ATOM   24765 N  N   . ASP   B 1 1352 ? 10.11000   5.55500   0.66100   1.000 89.34745  ?  1350 ASP   B N   1 
ATOM   24766 C  CA  . ASP   B 1 1352 ? 10.12500   6.31000   -0.58400  1.000 77.05216  ?  1350 ASP   B CA  1 
ATOM   24767 C  C   . ASP   B 1 1352 ? 11.54100   6.75900   -0.92100  1.000 75.54601  ?  1350 ASP   B C   1 
ATOM   24768 O  O   . ASP   B 1 1352 ? 12.23600   7.34100   -0.08200  1.000 81.58262  ?  1350 ASP   B O   1 
ATOM   24769 C  CB  . ASP   B 1 1352 ? 9.19500    7.51700   -0.48100  1.000 72.08917  ?  1350 ASP   B CB  1 
ATOM   24770 C  CG  . ASP   B 1 1352 ? 8.76600    8.03400   -1.83600  1.000 86.91138  ?  1350 ASP   B CG  1 
ATOM   24771 O  OD1 . ASP   B 1 1352 ? 7.75600    7.53100   -2.36900  1.000 104.15630 ?  1350 ASP   B OD1 1 
ATOM   24772 O  OD2 . ASP   B 1 1352 ? 9.44500    8.93500   -2.37200  1.000 88.85865  -1 1350 ASP   B OD2 1 
ATOM   24773 N  N   . THR   B 1 1353 ? 11.96700   6.48900   -2.15700  1.000 62.85590  ?  1351 THR   B N   1 
ATOM   24774 C  CA  . THR   B 1 1353 ? 13.28600   6.87400   -2.64300  1.000 75.78880  ?  1351 THR   B CA  1 
ATOM   24775 C  C   . THR   B 1 1353 ? 13.20300   7.94000   -3.73300  1.000 70.57085  ?  1351 THR   B C   1 
ATOM   24776 O  O   . THR   B 1 1353 ? 14.10300   8.05300   -4.57000  1.000 79.39506  ?  1351 THR   B O   1 
ATOM   24777 C  CB  . THR   B 1 1353 ? 14.05400   5.65400   -3.15200  1.000 84.41484  ?  1351 THR   B CB  1 
ATOM   24778 O  OG1 . THR   B 1 1353 ? 13.21500   4.88100   -4.02100  1.000 59.53416  ?  1351 THR   B OG1 1 
ATOM   24779 C  CG2 . THR   B 1 1353 ? 14.51200   4.78600   -1.98800  1.000 60.88028  ?  1351 THR   B CG2 1 
ATOM   24780 N  N   . SER   B 1 1354 ? 12.13100   8.72600   -3.73800  1.000 77.60229  ?  1352 SER   B N   1 
ATOM   24781 C  CA  . SER   B 1 1354 ? 11.97900   9.83600   -4.66500  1.000 89.71357  ?  1352 SER   B CA  1 
ATOM   24782 C  C   . SER   B 1 1354 ? 12.34500   11.14600  -3.97600  1.000 94.27856  ?  1352 SER   B C   1 
ATOM   24783 O  O   . SER   B 1 1354 ? 12.24100   11.27800  -2.75300  1.000 81.82549  ?  1352 SER   B O   1 
ATOM   24784 C  CB  . SER   B 1 1354 ? 10.55000   9.91300   -5.20900  1.000 94.00217  ?  1352 SER   B CB  1 
ATOM   24785 O  OG  . SER   B 1 1354 ? 9.65800    10.42300  -4.23200  1.000 97.78884  ?  1352 SER   B OG  1 
ATOM   24786 N  N   . ASN   B 1 1355 ? 12.77400   12.11300  -4.77900  1.000 91.06322  ?  1353 ASN   B N   1 
ATOM   24787 C  CA  . ASN   B 1 1355 ? 13.21900   13.39400  -4.24300  1.000 75.26111  ?  1353 ASN   B CA  1 
ATOM   24788 C  C   . ASN   B 1 1355 ? 12.04600   14.12800  -3.60000  1.000 70.52683  ?  1353 ASN   B C   1 
ATOM   24789 O  O   . ASN   B 1 1355 ? 11.00600   14.30900  -4.24500  1.000 84.06379  ?  1353 ASN   B O   1 
ATOM   24790 C  CB  . ASN   B 1 1355 ? 13.83900   14.24800  -5.34900  1.000 62.75213  ?  1353 ASN   B CB  1 
ATOM   24791 C  CG  . ASN   B 1 1355 ? 14.95700   13.52900  -6.08900  1.000 65.19867  ?  1353 ASN   B CG  1 
ATOM   24792 O  OD1 . ASN   B 1 1355 ? 15.60200   12.63200  -5.54500  1.000 76.17552  ?  1353 ASN   B OD1 1 
ATOM   24793 N  ND2 . ASN   B 1 1355 ? 15.18800   13.92100  -7.33700  1.000 53.27264  ?  1353 ASN   B ND2 1 
ATOM   24794 N  N   . PRO   B 1 1356 ? 12.16400   14.54900  -2.34400  1.000 70.80525  ?  1354 PRO   B N   1 
ATOM   24795 C  CA  . PRO   B 1 1356 ? 11.08900   15.31400  -1.70800  1.000 64.83415  ?  1354 PRO   B CA  1 
ATOM   24796 C  C   . PRO   B 1 1356 ? 10.89300   16.64300  -2.41300  1.000 80.72404  ?  1354 PRO   B C   1 
ATOM   24797 O  O   . PRO   B 1 1356 ? 11.80300   17.12600  -3.10400  1.000 85.97717  ?  1354 PRO   B O   1 
ATOM   24798 C  CB  . PRO   B 1 1356 ? 11.59500   15.51200  -0.26900  1.000 56.97138  ?  1354 PRO   B CB  1 
ATOM   24799 C  CG  . PRO   B 1 1356 ? 12.68000   14.50000  -0.08900  1.000 75.86514  ?  1354 PRO   B CG  1 
ATOM   24800 C  CD  . PRO   B 1 1356 ? 13.30000   14.33200  -1.43600  1.000 79.75218  ?  1354 PRO   B CD  1 
ATOM   24801 N  N   . PRO   B 1 1357 ? 9.72400    17.26200  -2.27700  1.000 94.01224  ?  1355 PRO   B N   1 
ATOM   24802 C  CA  . PRO   B 1 1357 ? 9.50800    18.56200  -2.92100  1.000 87.86065  ?  1355 PRO   B CA  1 
ATOM   24803 C  C   . PRO   B 1 1357 ? 10.36500   19.64600  -2.28500  1.000 84.06332  ?  1355 PRO   B C   1 
ATOM   24804 O  O   . PRO   B 1 1357 ? 10.63700   19.63200  -1.08300  1.000 85.26979  ?  1355 PRO   B O   1 
ATOM   24805 C  CB  . PRO   B 1 1357 ? 8.01200    18.83400  -2.70800  1.000 86.31077  ?  1355 PRO   B CB  1 
ATOM   24806 C  CG  . PRO   B 1 1357 ? 7.49000    17.74400  -1.82500  1.000 87.74024  ?  1355 PRO   B CG  1 
ATOM   24807 C  CD  . PRO   B 1 1357 ? 8.61300    16.86900  -1.39300  1.000 90.97774  ?  1355 PRO   B CD  1 
ATOM   24808 N  N   . LEU   B 1 1358 ? 10.80400   20.59100  -3.11200  1.000 85.53680  ?  1356 LEU   B N   1 
ATOM   24809 C  CA  . LEU   B 1 1358 ? 11.66700   21.66400  -2.63500  1.000 82.25217  ?  1356 LEU   B CA  1 
ATOM   24810 C  C   . LEU   B 1 1358 ? 10.85200   22.71800  -1.89400  1.000 78.80327  ?  1356 LEU   B C   1 
ATOM   24811 O  O   . LEU   B 1 1358 ? 9.70800    23.01000  -2.25500  1.000 84.02902  ?  1356 LEU   B O   1 
ATOM   24812 C  CB  . LEU   B 1 1358 ? 12.42400   22.30100  -3.79900  1.000 63.70775  ?  1356 LEU   B CB  1 
ATOM   24813 C  CG  . LEU   B 1 1358 ? 13.79500   22.89500  -3.46800  1.000 91.80218  ?  1356 LEU   B CG  1 
ATOM   24814 C  CD1 . LEU   B 1 1358 ? 14.46000   22.16800  -2.30000  1.000 89.62200  ?  1356 LEU   B CD1 1 
ATOM   24815 C  CD2 . LEU   B 1 1358 ? 14.68000   22.85900  -4.69900  1.000 94.93439  ?  1356 LEU   B CD2 1 
ATOM   24816 N  N   . VAL   B 1 1359 ? 11.45600   23.29700  -0.85800  1.000 79.78095  ?  1357 VAL   B N   1 
ATOM   24817 C  CA  . VAL   B 1 1359 ? 10.73400   24.14000  0.08500   1.000 82.20934  ?  1357 VAL   B CA  1 
ATOM   24818 C  C   . VAL   B 1 1359 ? 11.65300   25.28700  0.50200   1.000 90.59278  ?  1357 VAL   B C   1 
ATOM   24819 O  O   . VAL   B 1 1359 ? 11.23700   26.21700  1.20400   1.000 88.19125  ?  1357 VAL   B O   1 
ATOM   24820 C  CB  . VAL   B 1 1359 ? 10.26100   23.29300  1.28800   1.000 81.96453  ?  1357 VAL   B CB  1 
ATOM   24821 C  CG1 . VAL   B 1 1359 ? 11.41400   22.48500  1.85300   1.000 87.00613  ?  1357 VAL   B CG1 1 
ATOM   24822 C  CG2 . VAL   B 1 1359 ? 9.56100    24.11300  2.36800   1.000 93.02348  ?  1357 VAL   B CG2 1 
ATOM   24823 N  N   . ASN   B 1 1360 ? 12.90300   25.24700  0.04400   1.000 101.21915 ?  1358 ASN   B N   1 
ATOM   24824 C  CA  . ASN   B 1 1360 ? 13.92900   26.17600  0.49700   1.000 95.60896  ?  1358 ASN   B CA  1 
ATOM   24825 C  C   . ASN   B 1 1360 ? 14.15800   27.30300  -0.50400  1.000 76.38566  ?  1358 ASN   B C   1 
ATOM   24826 O  O   . ASN   B 1 1360 ? 13.92700   27.15500  -1.70800  1.000 72.02192  ?  1358 ASN   B O   1 
ATOM   24827 C  CB  . ASN   B 1 1360 ? 15.25000   25.44700  0.74700   1.000 81.00827  ?  1358 ASN   B CB  1 
ATOM   24828 C  CG  . ASN   B 1 1360 ? 15.16200   24.45900  1.89000   1.000 85.46775  ?  1358 ASN   B CG  1 
ATOM   24829 O  OD1 . ASN   B 1 1360 ? 14.99600   23.25900  1.67500   1.000 91.43600  ?  1358 ASN   B OD1 1 
ATOM   24830 N  ND2 . ASN   B 1 1360 ? 15.26400   24.96000  3.11600   1.000 66.57687  ?  1358 ASN   B ND2 1 
ATOM   24831 N  N   . GLN   B 1 1361 ? 14.63300   28.43100  0.01400   1.000 79.56879  ?  1359 GLN   B N   1 
ATOM   24832 C  CA  . GLN   B 1 1361 ? 14.99600   29.59700  -0.77200  1.000 89.43714  ?  1359 GLN   B CA  1 
ATOM   24833 C  C   . GLN   B 1 1361 ? 16.37700   30.08100  -0.35500  1.000 85.60025  ?  1359 GLN   B C   1 
ATOM   24834 O  O   . GLN   B 1 1361 ? 16.81600   29.81600  0.77000   1.000 77.13526  ?  1359 GLN   B O   1 
ATOM   24835 C  CB  . GLN   B 1 1361 ? 13.96500   30.72600  -0.60300  1.000 85.63963  ?  1359 GLN   B CB  1 
ATOM   24836 C  CG  . GLN   B 1 1361 ? 12.78100   30.64600  -1.57200  1.000 95.27944  ?  1359 GLN   B CG  1 
ATOM   24837 C  CD  . GLN   B 1 1361 ? 13.19900   30.65000  -3.04000  1.000 111.83825 ?  1359 GLN   B CD  1 
ATOM   24838 O  OE1 . GLN   B 1 1361 ? 13.68700   29.64800  -3.57000  1.000 96.85024  ?  1359 GLN   B OE1 1 
ATOM   24839 N  NE2 . GLN   B 1 1361 ? 13.00100   31.78300  -3.70400  1.000 111.10817 ?  1359 GLN   B NE2 1 
ATOM   24840 N  N   . PRO   B 1 1362 ? 17.08800   30.78300  -1.24600  1.000 79.83654  ?  1360 PRO   B N   1 
ATOM   24841 C  CA  . PRO   B 1 1362 ? 18.48500   31.16000  -0.95600  1.000 69.86401  ?  1360 PRO   B CA  1 
ATOM   24842 C  C   . PRO   B 1 1362 ? 18.70100   31.85200  0.38200   1.000 65.24071  ?  1360 PRO   B C   1 
ATOM   24843 O  O   . PRO   B 1 1362 ? 19.80900   31.77900  0.92900   1.000 68.73079  ?  1360 PRO   B O   1 
ATOM   24844 C  CB  . PRO   B 1 1362 ? 18.84000   32.09100  -2.12200  1.000 60.51269  ?  1360 PRO   B CB  1 
ATOM   24845 C  CG  . PRO   B 1 1362 ? 17.94900   31.67700  -3.23100  1.000 68.73921  ?  1360 PRO   B CG  1 
ATOM   24846 C  CD  . PRO   B 1 1362 ? 16.71100   31.06800  -2.64300  1.000 83.43981  ?  1360 PRO   B CD  1 
ATOM   24847 N  N   . GLY   B 1 1363 ? 17.68900   32.52400  0.92700   1.000 68.09001  ?  1361 GLY   B N   1 
ATOM   24848 C  CA  . GLY   B 1 1363 ? 17.84300   33.18900  2.20500   1.000 60.95351  ?  1361 GLY   B CA  1 
ATOM   24849 C  C   . GLY   B 1 1363 ? 17.64000   32.32000  3.42300   1.000 56.59244  ?  1361 GLY   B C   1 
ATOM   24850 O  O   . GLY   B 1 1363 ? 17.74900   32.80800  4.55100   1.000 46.68080  ?  1361 GLY   B O   1 
ATOM   24851 N  N   . ASP   B 1 1364 ? 17.34700   31.03800  3.23100   1.000 69.79772  ?  1362 ASP   B N   1 
ATOM   24852 C  CA  . ASP   B 1 1364 ? 17.08000   30.13200  4.33600   1.000 62.61563  ?  1362 ASP   B CA  1 
ATOM   24853 C  C   . ASP   B 1 1364 ? 18.37700   29.55500  4.88800   1.000 71.12286  ?  1362 ASP   B C   1 
ATOM   24854 O  O   . ASP   B 1 1364 ? 19.37500   29.41700  4.17400   1.000 67.85345  ?  1362 ASP   B O   1 
ATOM   24855 C  CB  . ASP   B 1 1364 ? 16.15300   28.99900  3.89400   1.000 73.39372  ?  1362 ASP   B CB  1 
ATOM   24856 C  CG  . ASP   B 1 1364 ? 14.76200   29.48700  3.54300   1.000 76.31888  ?  1362 ASP   B CG  1 
ATOM   24857 O  OD1 . ASP   B 1 1364 ? 14.29800   30.47200  4.15800   1.000 77.62371  ?  1362 ASP   B OD1 1 
ATOM   24858 O  OD2 . ASP   B 1 1364 ? 14.13200   28.88300  2.65000   1.000 75.58557  -1 1362 ASP   B OD2 1 
ATOM   24859 N  N   . LEU   B 1 1365 ? 18.34800   29.21600  6.17400   1.000 62.34470  ?  1363 LEU   B N   1 
ATOM   24860 C  CA  . LEU   B 1 1365 ? 19.51900   28.66700  6.84100   1.000 54.83121  ?  1363 LEU   B CA  1 
ATOM   24861 C  C   . LEU   B 1 1365 ? 19.89900   27.31000  6.26400   1.000 64.26260  ?  1363 LEU   B C   1 
ATOM   24862 O  O   . LEU   B 1 1365 ? 19.03900   26.47800  5.96100   1.000 52.25888  ?  1363 LEU   B O   1 
ATOM   24863 C  CB  . LEU   B 1 1365 ? 19.26100   28.54400  8.34300   1.000 44.74237  ?  1363 LEU   B CB  1 
ATOM   24864 C  CG  . LEU   B 1 1365 ? 18.83200   29.83400  9.03500   1.000 59.45074  ?  1363 LEU   B CG  1 
ATOM   24865 C  CD1 . LEU   B 1 1365 ? 18.78800   29.65600  10.54100  1.000 51.43990  ?  1363 LEU   B CD1 1 
ATOM   24866 C  CD2 . LEU   B 1 1365 ? 19.83600   30.90900  8.66300   1.000 63.97423  ?  1363 LEU   B CD2 1 
ATOM   24867 N  N   . VAL   B 1 1366 ? 21.20300   27.08900  6.11800   1.000 74.56236  ?  1364 VAL   B N   1 
ATOM   24868 C  CA  . VAL   B 1 1366 ? 21.71200   25.81000  5.66000   1.000 69.70466  ?  1364 VAL   B CA  1 
ATOM   24869 C  C   . VAL   B 1 1366 ? 22.49300   25.06600  6.74200   1.000 59.72764  ?  1364 VAL   B C   1 
ATOM   24870 O  O   . VAL   B 1 1366 ? 22.47700   23.82900  6.75400   1.000 66.72250  ?  1364 VAL   B O   1 
ATOM   24871 C  CB  . VAL   B 1 1366 ? 22.55900   25.97800  4.37900   1.000 70.11171  ?  1364 VAL   B CB  1 
ATOM   24872 C  CG1 . VAL   B 1 1366 ? 23.94700   26.50100  4.69400   1.000 58.66577  ?  1364 VAL   B CG1 1 
ATOM   24873 C  CG2 . VAL   B 1 1366 ? 22.64500   24.65700  3.62900   1.000 72.03205  ?  1364 VAL   B CG2 1 
ATOM   24874 N  N   . TYR   B 1 1367 ? 23.14600   25.77200  7.66600   1.000 56.37305  ?  1365 TYR   B N   1 
ATOM   24875 C  CA  . TYR   B 1 1367 ? 23.76400   25.13600  8.82400   1.000 58.11325  ?  1365 TYR   B CA  1 
ATOM   24876 C  C   . TYR   B 1 1367 ? 24.08500   26.20100  9.85800   1.000 58.65742  ?  1365 TYR   B C   1 
ATOM   24877 O  O   . TYR   B 1 1367 ? 24.11200   27.39800  9.56100   1.000 66.76777  ?  1365 TYR   B O   1 
ATOM   24878 C  CB  . TYR   B 1 1367 ? 25.03100   24.34900  8.45500   1.000 57.85471  ?  1365 TYR   B CB  1 
ATOM   24879 C  CG  . TYR   B 1 1367 ? 26.22000   25.18200  8.01400   1.000 55.27294  ?  1365 TYR   B CG  1 
ATOM   24880 C  CD1 . TYR   B 1 1367 ? 27.11700   25.70800  8.94000   1.000 51.94424  ?  1365 TYR   B CD1 1 
ATOM   24881 C  CD2 . TYR   B 1 1367 ? 26.46500   25.41100  6.66700   1.000 62.58243  ?  1365 TYR   B CD2 1 
ATOM   24882 C  CE1 . TYR   B 1 1367 ? 28.20700   26.46000  8.53300   1.000 55.89218  ?  1365 TYR   B CE1 1 
ATOM   24883 C  CE2 . TYR   B 1 1367 ? 27.54900   26.16000  6.25100   1.000 56.90159  ?  1365 TYR   B CE2 1 
ATOM   24884 C  CZ  . TYR   B 1 1367 ? 28.41800   26.68000  7.18500   1.000 64.91299  ?  1365 TYR   B CZ  1 
ATOM   24885 O  OH  . TYR   B 1 1367 ? 29.49800   27.42300  6.76300   1.000 64.54693  ?  1365 TYR   B OH  1 
ATOM   24886 N  N   . VAL   B 1 1368 ? 24.33400   25.74100  11.08100  1.000 40.91162  ?  1366 VAL   B N   1 
ATOM   24887 C  CA  . VAL   B 1 1368 ? 24.70500   26.59900  12.19700  1.000 44.09580  ?  1366 VAL   B CA  1 
ATOM   24888 C  C   . VAL   B 1 1368 ? 25.96900   26.01800  12.80900  1.000 48.33012  ?  1366 VAL   B C   1 
ATOM   24889 O  O   . VAL   B 1 1368 ? 25.91500   24.98500  13.48800  1.000 58.06515  ?  1366 VAL   B O   1 
ATOM   24890 C  CB  . VAL   B 1 1368 ? 23.59100   26.70700  13.24500  1.000 47.43975  ?  1366 VAL   B CB  1 
ATOM   24891 C  CG1 . VAL   B 1 1368 ? 24.06500   27.52300  14.43700  1.000 48.83006  ?  1366 VAL   B CG1 1 
ATOM   24892 C  CG2 . VAL   B 1 1368 ? 22.34300   27.32300  12.62700  1.000 49.78644  ?  1366 VAL   B CG2 1 
ATOM   24893 N  N   . MET   B 1 1369 ? 27.10300   26.67400  12.57400  1.000 58.35400  ?  1367 MET   B N   1 
ATOM   24894 C  CA  . MET   B 1 1369 ? 28.39200   26.22500  13.08400  1.000 62.06032  ?  1367 MET   B CA  1 
ATOM   24895 C  C   . MET   B 1 1369 ? 28.72600   26.96300  14.37600  1.000 64.98784  ?  1367 MET   B C   1 
ATOM   24896 O  O   . MET   B 1 1369 ? 28.61400   28.19200  14.44300  1.000 67.21674  ?  1367 MET   B O   1 
ATOM   24897 C  CB  . MET   B 1 1369 ? 29.49500   26.44800  12.04900  1.000 49.42494  ?  1367 MET   B CB  1 
ATOM   24898 C  CG  . MET   B 1 1369 ? 30.84700   25.93700  12.49900  1.000 57.80661  ?  1367 MET   B CG  1 
ATOM   24899 S  SD  . MET   B 1 1369 ? 30.98500   24.15700  12.25000  1.000 52.00245  ?  1367 MET   B SD  1 
ATOM   24900 C  CE  . MET   B 1 1369 ? 30.23900   23.98300  10.63000  1.000 39.72791  ?  1367 MET   B CE  1 
ATOM   24901 N  N   . TYR   B 1 1370 ? 29.13300   26.21300  15.39600  1.000 59.00043  ?  1368 TYR   B N   1 
ATOM   24902 C  CA  . TYR   B 1 1370 ? 29.50100   26.77900  16.68400  1.000 48.12253  ?  1368 TYR   B CA  1 
ATOM   24903 C  C   . TYR   B 1 1370 ? 31.00700   26.99900  16.75700  1.000 60.31738  ?  1368 TYR   B C   1 
ATOM   24904 O  O   . TYR   B 1 1370 ? 31.79400   26.24600  16.17800  1.000 71.31612  ?  1368 TYR   B O   1 
ATOM   24905 C  CB  . TYR   B 1 1370 ? 29.04600   25.87700  17.83100  1.000 55.69404  ?  1368 TYR   B CB  1 
ATOM   24906 C  CG  . TYR   B 1 1370 ? 27.65500   26.20000  18.31900  1.000 62.44386  ?  1368 TYR   B CG  1 
ATOM   24907 C  CD1 . TYR   B 1 1370 ? 26.55900   26.07700  17.47600  1.000 61.99002  ?  1368 TYR   B CD1 1 
ATOM   24908 C  CD2 . TYR   B 1 1370 ? 27.43700   26.64400  19.61800  1.000 67.31135  ?  1368 TYR   B CD2 1 
ATOM   24909 C  CE1 . TYR   B 1 1370 ? 25.28200   26.37800  17.91300  1.000 68.59549  ?  1368 TYR   B CE1 1 
ATOM   24910 C  CE2 . TYR   B 1 1370 ? 26.16400   26.94900  20.06500  1.000 68.58757  ?  1368 TYR   B CE2 1 
ATOM   24911 C  CZ  . TYR   B 1 1370 ? 25.09100   26.81400  19.20900  1.000 71.18747  ?  1368 TYR   B CZ  1 
ATOM   24912 O  OH  . TYR   B 1 1370 ? 23.82400   27.11800  19.65500  1.000 67.84728  ?  1368 TYR   B OH  1 
ATOM   24913 N  N   . THR   B 1 1371 ? 31.39700   28.04400  17.48200  1.000 68.62637  ?  1369 THR   B N   1 
ATOM   24914 C  CA  . THR   B 1 1371 ? 32.78300   28.46300  17.59300  1.000 82.65815  ?  1369 THR   B CA  1 
ATOM   24915 C  C   . THR   B 1 1371 ? 33.41400   27.87000  18.85200  1.000 86.58556  ?  1369 THR   B C   1 
ATOM   24916 O  O   . THR   B 1 1371 ? 32.86400   26.96600  19.48700  1.000 90.75246  ?  1369 THR   B O   1 
ATOM   24917 C  CB  . THR   B 1 1371 ? 32.87100   29.99000  17.59400  1.000 75.90245  ?  1369 THR   B CB  1 
ATOM   24918 O  OG1 . THR   B 1 1371 ? 32.50900   30.48700  18.88800  1.000 75.47367  ?  1369 THR   B OG1 1 
ATOM   24919 C  CG2 . THR   B 1 1371 ? 31.93900   30.58400  16.54800  1.000 52.67385  ?  1369 THR   B CG2 1 
ATOM   24920 N  N   . SER   B 1 1372 ? 34.58200   28.38800  19.22000  1.000 95.86098  ?  1370 SER   B N   1 
ATOM   24921 C  CA  . SER   B 1 1372 ? 35.28700   27.92900  20.41000  1.000 107.28045 ?  1370 SER   B CA  1 
ATOM   24922 C  C   . SER   B 1 1372 ? 34.76600   28.63700  21.65800  1.000 108.08492 ?  1370 SER   B C   1 
ATOM   24923 O  O   . SER   B 1 1372 ? 34.96000   28.16600  22.78000  1.000 113.72492 ?  1370 SER   B O   1 
ATOM   24924 C  CB  . SER   B 1 1372 ? 36.79100   28.15900  20.26200  1.000 105.48737 ?  1370 SER   B CB  1 
ATOM   24925 O  OG  . SER   B 1 1372 ? 37.08400   29.54300  20.17800  1.000 105.86521 ?  1370 SER   B OG  1 
ATOM   24926 N  N   . THR   B 1 1375 ? 38.49600   31.80700  24.82500  1.000 110.80639 ?  1373 THR   B N   1 
ATOM   24927 C  CA  . THR   B 1 1375 ? 37.52300   32.88800  24.71800  1.000 117.06534 ?  1373 THR   B CA  1 
ATOM   24928 C  C   . THR   B 1 1375 ? 36.48600   32.80700  25.83700  1.000 108.50588 ?  1373 THR   B C   1 
ATOM   24929 O  O   . THR   B 1 1375 ? 36.45600   33.65200  26.73300  1.000 91.23862  ?  1373 THR   B O   1 
ATOM   24930 C  CB  . THR   B 1 1375 ? 36.80400   32.86600  23.35400  1.000 114.96966 ?  1373 THR   B CB  1 
ATOM   24931 O  OG1 . THR   B 1 1375 ? 36.51700   31.51200  22.98000  1.000 111.97491 ?  1373 THR   B OG1 1 
ATOM   24932 C  CG2 . THR   B 1 1375 ? 37.67300   33.50900  22.28100  1.000 84.98674  ?  1373 THR   B CG2 1 
ATOM   24933 N  N   . GLY   B 1 1376 ? 35.63700   31.78400  25.78000  1.000 112.09126 ?  1374 GLY   B N   1 
ATOM   24934 C  CA  . GLY   B 1 1376 ? 34.61300   31.59600  26.78800  1.000 92.47388  ?  1374 GLY   B CA  1 
ATOM   24935 C  C   . GLY   B 1 1376 ? 33.49500   30.67800  26.33800  1.000 99.14591  ?  1374 GLY   B C   1 
ATOM   24936 O  O   . GLY   B 1 1376 ? 33.70400   29.47500  26.15500  1.000 98.84049  ?  1374 GLY   B O   1 
ATOM   24937 N  N   . LYS   B 1 1377 ? 32.30100   31.23900  26.15600  1.000 102.75492 ?  1375 LYS   B N   1 
ATOM   24938 C  CA  . LYS   B 1 1377 ? 31.14200   30.45800  25.73700  1.000 101.23145 ?  1375 LYS   B CA  1 
ATOM   24939 C  C   . LYS   B 1 1377 ? 31.04700   30.44300  24.21600  1.000 95.96525  ?  1375 LYS   B C   1 
ATOM   24940 O  O   . LYS   B 1 1377 ? 31.21900   31.49100  23.58200  1.000 96.67445  ?  1375 LYS   B O   1 
ATOM   24941 C  CB  . LYS   B 1 1377 ? 29.86000   31.03000  26.32800  1.000 79.19625  ?  1375 LYS   B CB  1 
ATOM   24942 N  N   . PRO   B 1 1378 ? 30.79400   29.29100  23.60200  1.000 86.06285  ?  1376 PRO   B N   1 
ATOM   24943 C  CA  . PRO   B 1 1378 ? 30.66800   29.24300  22.14200  1.000 81.70941  ?  1376 PRO   B CA  1 
ATOM   24944 C  C   . PRO   B 1 1378 ? 29.39900   29.93400  21.66800  1.000 77.42269  ?  1376 PRO   B C   1 
ATOM   24945 O  O   . PRO   B 1 1378 ? 28.42400   30.08900  22.40600  1.000 86.37074  ?  1376 PRO   B O   1 
ATOM   24946 C  CB  . PRO   B 1 1378 ? 30.63000   27.74100  21.83300  1.000 89.61056  ?  1376 PRO   B CB  1 
ATOM   24947 C  CG  . PRO   B 1 1378 ? 31.16900   27.07100  23.06700  1.000 92.16938  ?  1376 PRO   B CG  1 
ATOM   24948 C  CD  . PRO   B 1 1378 ? 30.75500   27.94900  24.20400  1.000 83.73276  ?  1376 PRO   B CD  1 
ATOM   24949 N  N   . LYS   B 1 1379 ? 29.42700   30.35200  20.40400  1.000 61.75339  ?  1377 LYS   B N   1 
ATOM   24950 C  CA  . LYS   B 1 1379 ? 28.30000   31.02700  19.77700  1.000 61.28711  ?  1377 LYS   B CA  1 
ATOM   24951 C  C   . LYS   B 1 1379 ? 28.00600   30.38200  18.43200  1.000 50.90444  ?  1377 LYS   B C   1 
ATOM   24952 O  O   . LYS   B 1 1379 ? 28.92600   29.99700  17.70500  1.000 64.17498  ?  1377 LYS   B O   1 
ATOM   24953 C  CB  . LYS   B 1 1379 ? 28.57700   32.52500  19.59200  1.000 62.01547  ?  1377 LYS   B CB  1 
ATOM   24954 N  N   . GLY   B 1 1380 ? 26.72300   30.27000  18.10100  1.000 51.44545  ?  1378 GLY   B N   1 
ATOM   24955 C  CA  . GLY   B 1 1380 ? 26.32200   29.62300  16.86800  1.000 54.41070  ?  1378 GLY   B CA  1 
ATOM   24956 C  C   . GLY   B 1 1380 ? 26.18300   30.56800  15.69300  1.000 59.74844  ?  1378 GLY   B C   1 
ATOM   24957 O  O   . GLY   B 1 1380 ? 25.33300   31.46200  15.70200  1.000 69.29631  ?  1378 GLY   B O   1 
ATOM   24958 N  N   . VAL   B 1 1381 ? 27.00100   30.36800  14.66600  1.000 47.97639  ?  1379 VAL   B N   1 
ATOM   24959 C  CA  . VAL   B 1 1381 ? 27.01300   31.24200  13.49800  1.000 57.94192  ?  1379 VAL   B CA  1 
ATOM   24960 C  C   . VAL   B 1 1381 ? 25.99600   30.71600  12.49000  1.000 56.68911  ?  1379 VAL   B C   1 
ATOM   24961 O  O   . VAL   B 1 1381 ? 26.17900   29.64300  11.91000  1.000 61.12783  ?  1379 VAL   B O   1 
ATOM   24962 C  CB  . VAL   B 1 1381 ? 28.41400   31.33100  12.88300  1.000 51.39966  ?  1379 VAL   B CB  1 
ATOM   24963 C  CG1 . VAL   B 1 1381 ? 28.50600   32.53300  11.97100  1.000 54.21357  ?  1379 VAL   B CG1 1 
ATOM   24964 C  CG2 . VAL   B 1 1381 ? 29.47100   31.41200  13.97900  1.000 45.35331  ?  1379 VAL   B CG2 1 
ATOM   24965 N  N   . MET   B 1 1382 ? 24.92400   31.47400  12.27600  1.000 52.74496  ?  1380 MET   B N   1 
ATOM   24966 C  CA  . MET   B 1 1382 ? 23.89200   31.07800  11.32600  1.000 54.23149  ?  1380 MET   B CA  1 
ATOM   24967 C  C   . MET   B 1 1382 ? 24.30000   31.46800  9.91100   1.000 52.17815  ?  1380 MET   B C   1 
ATOM   24968 O  O   . MET   B 1 1382 ? 24.61600   32.63100  9.64400   1.000 61.92821  ?  1380 MET   B O   1 
ATOM   24969 C  CB  . MET   B 1 1382 ? 22.55800   31.72100  11.69700  1.000 61.50862  ?  1380 MET   B CB  1 
ATOM   24970 C  CG  . MET   B 1 1382 ? 22.19500   31.55400  13.16300  1.000 67.12153  ?  1380 MET   B CG  1 
ATOM   24971 S  SD  . MET   B 1 1382 ? 20.92900   32.70300  13.72800  1.000 61.03354  ?  1380 MET   B SD  1 
ATOM   24972 C  CE  . MET   B 1 1382 ? 20.34800   33.37100  12.17300  1.000 68.55080  ?  1380 MET   B CE  1 
ATOM   24973 N  N   . ILE   B 1 1383 ? 24.29200   30.49200  9.00500   1.000 54.80935  ?  1381 ILE   B N   1 
ATOM   24974 C  CA  . ILE   B 1 1383 ? 24.71800   30.67900  7.62200   1.000 63.78717  ?  1381 ILE   B CA  1 
ATOM   24975 C  C   . ILE   B 1 1383 ? 23.56700   30.29600  6.70100   1.000 65.55937  ?  1381 ILE   B C   1 
ATOM   24976 O  O   . ILE   B 1 1383 ? 22.86200   29.31200  6.95000   1.000 74.63278  ?  1381 ILE   B O   1 
ATOM   24977 C  CB  . ILE   B 1 1383 ? 25.98600   29.85200  7.30700   1.000 51.44951  ?  1381 ILE   B CB  1 
ATOM   24978 C  CG1 . ILE   B 1 1383 ? 27.24900   30.63000  7.69000   1.000 59.42566  ?  1381 ILE   B CG1 1 
ATOM   24979 C  CG2 . ILE   B 1 1383 ? 26.04600   29.44600  5.83700   1.000 52.36767  ?  1381 ILE   B CG2 1 
ATOM   24980 C  CD1 . ILE   B 1 1383 ? 27.54300   30.64000  9.16500   1.000 60.50124  ?  1381 ILE   B CD1 1 
ATOM   24981 N  N   . GLU   B 1 1384 ? 23.37300   31.07800  5.64300   1.000 60.44709  ?  1382 GLU   B N   1 
ATOM   24982 C  CA  . GLU   B 1 1384 ? 22.30200   30.84900  4.68500   1.000 60.01017  ?  1382 GLU   B CA  1 
ATOM   24983 C  C   . GLU   B 1 1384 ? 22.80800   30.07100  3.47500   1.000 63.24137  ?  1382 GLU   B C   1 
ATOM   24984 O  O   . GLU   B 1 1384 ? 24.00700   29.84000  3.30100   1.000 80.67509  ?  1382 GLU   B O   1 
ATOM   24985 C  CB  . GLU   B 1 1384 ? 21.68800   32.17900  4.24000   1.000 64.95044  ?  1382 GLU   B CB  1 
ATOM   24986 C  CG  . GLU   B 1 1384 ? 21.14800   33.01300  5.38100   1.000 66.75789  ?  1382 GLU   B CG  1 
ATOM   24987 C  CD  . GLU   B 1 1384 ? 20.69300   34.38400  4.93400   1.000 66.56912  ?  1382 GLU   B CD  1 
ATOM   24988 O  OE1 . GLU   B 1 1384 ? 21.01900   34.78200  3.79500   1.000 66.69785  ?  1382 GLU   B OE1 1 
ATOM   24989 O  OE2 . GLU   B 1 1384 ? 20.01300   35.06700  5.72800   1.000 66.00526  -1 1382 GLU   B OE2 1 
ATOM   24990 N  N   . HIS   B 1 1385 ? 21.86000   29.67000  2.62600   1.000 65.33759  ?  1383 HIS   B N   1 
ATOM   24991 C  CA  . HIS   B 1 1385 ? 22.20100   28.90800  1.42900   1.000 55.32554  ?  1383 HIS   B CA  1 
ATOM   24992 C  C   . HIS   B 1 1385 ? 23.01400   29.75000  0.45400   1.000 56.62212  ?  1383 HIS   B C   1 
ATOM   24993 O  O   . HIS   B 1 1385 ? 24.06200   29.31500  -0.03700  1.000 49.79386  ?  1383 HIS   B O   1 
ATOM   24994 C  CB  . HIS   B 1 1385 ? 20.92900   28.39300  0.75500   1.000 69.08412  ?  1383 HIS   B CB  1 
ATOM   24995 C  CG  . HIS   B 1 1385 ? 20.52800   27.01900  1.18900   1.000 69.32141  ?  1383 HIS   B CG  1 
ATOM   24996 N  ND1 . HIS   B 1 1385 ? 19.58000   26.79400  2.16300   1.000 71.73462  ?  1383 HIS   B ND1 1 
ATOM   24997 C  CD2 . HIS   B 1 1385 ? 20.94500   25.79800  0.78000   1.000 60.74574  ?  1383 HIS   B CD2 1 
ATOM   24998 C  CE1 . HIS   B 1 1385 ? 19.43100   25.49300  2.33700   1.000 73.49163  ?  1383 HIS   B CE1 1 
ATOM   24999 N  NE2 . HIS   B 1 1385 ? 20.24700   24.86600  1.50800   1.000 76.77550  ?  1383 HIS   B NE2 1 
ATOM   25000 N  N   . GLY   B 1 1386 ? 22.53600   30.96200  0.15600   1.000 59.67571  ?  1384 GLY   B N   1 
ATOM   25001 C  CA  . GLY   B 1 1386 ? 23.23600   31.81200  -0.79400  1.000 61.33623  ?  1384 GLY   B CA  1 
ATOM   25002 C  C   . GLY   B 1 1386 ? 24.66900   32.08700  -0.38300  1.000 70.68986  ?  1384 GLY   B C   1 
ATOM   25003 O  O   . GLY   B 1 1386 ? 25.56100   32.18200  -1.23000  1.000 79.57046  ?  1384 GLY   B O   1 
ATOM   25004 N  N   . ALA   B 1 1387 ? 24.90800   32.21200  0.92300   1.000 71.42423  ?  1385 ALA   B N   1 
ATOM   25005 C  CA  . ALA   B 1 1387 ? 26.27000   32.36300  1.42100   1.000 53.24219  ?  1385 ALA   B CA  1 
ATOM   25006 C  C   . ALA   B 1 1387 ? 27.13200   31.16900  1.02800   1.000 70.31860  ?  1385 ALA   B C   1 
ATOM   25007 O  O   . ALA   B 1 1387 ? 28.25100   31.33300  0.52800   1.000 74.65192  ?  1385 ALA   B O   1 
ATOM   25008 C  CB  . ALA   B 1 1387 ? 26.25000   32.54000  2.94000   1.000 53.20681  ?  1385 ALA   B CB  1 
ATOM   25009 N  N   . LEU   B 1 1388 ? 26.61700   29.95500  1.24100   1.000 58.13433  ?  1386 LEU   B N   1 
ATOM   25010 C  CA  . LEU   B 1 1388 ? 27.37500   28.75400  0.90800   1.000 50.46325  ?  1386 LEU   B CA  1 
ATOM   25011 C  C   . LEU   B 1 1388 ? 27.59700   28.63400  -0.59500  1.000 61.91707  ?  1386 LEU   B C   1 
ATOM   25012 O  O   . LEU   B 1 1388 ? 28.66600   28.19700  -1.03600  1.000 57.01462  ?  1386 LEU   B O   1 
ATOM   25013 C  CB  . LEU   B 1 1388 ? 26.65300   27.51800  1.44100   1.000 55.40449  ?  1386 LEU   B CB  1 
ATOM   25014 C  CG  . LEU   B 1 1388 ? 27.44000   26.20800  1.49000   1.000 51.82164  ?  1386 LEU   B CG  1 
ATOM   25015 C  CD1 . LEU   B 1 1388 ? 28.83600   26.43600  2.04400   1.000 42.73588  ?  1386 LEU   B CD1 1 
ATOM   25016 C  CD2 . LEU   B 1 1388 ? 26.69600   25.18000  2.32300   1.000 57.61071  ?  1386 LEU   B CD2 1 
ATOM   25017 N  N   . LEU   B 1 1389 ? 26.60000   29.01600  -1.39700  1.000 56.69418  ?  1387 LEU   B N   1 
ATOM   25018 C  CA  . LEU   B 1 1389 ? 26.73100   28.89200  -2.84500  1.000 53.45474  ?  1387 LEU   B CA  1 
ATOM   25019 C  C   . LEU   B 1 1389 ? 27.86600   29.75700  -3.37500  1.000 64.17168  ?  1387 LEU   B C   1 
ATOM   25020 O  O   . LEU   B 1 1389 ? 28.64000   29.31900  -4.23400  1.000 66.09913  ?  1387 LEU   B O   1 
ATOM   25021 C  CB  . LEU   B 1 1389 ? 25.41500   29.26500  -3.52600  1.000 66.24456  ?  1387 LEU   B CB  1 
ATOM   25022 C  CG  . LEU   B 1 1389 ? 24.34000   28.18000  -3.59300  1.000 63.97626  ?  1387 LEU   B CG  1 
ATOM   25023 C  CD1 . LEU   B 1 1389 ? 23.10000   28.69100  -4.31300  1.000 66.80089  ?  1387 LEU   B CD1 1 
ATOM   25024 C  CD2 . LEU   B 1 1389 ? 24.89000   26.94600  -4.28200  1.000 59.85844  ?  1387 LEU   B CD2 1 
ATOM   25025 N  N   . ASN   B 1 1390 ? 27.98600   30.98700  -2.86800  1.000 61.54756  ?  1388 ASN   B N   1 
ATOM   25026 C  CA  . ASN   B 1 1390 ? 28.97900   31.91700  -3.39800  1.000 68.94691  ?  1388 ASN   B CA  1 
ATOM   25027 C  C   . ASN   B 1 1390 ? 30.39600   31.42700  -3.12700  1.000 66.40734  ?  1388 ASN   B C   1 
ATOM   25028 O  O   . ASN   B 1 1390 ? 31.24100   31.40400  -4.03000  1.000 60.45576  ?  1388 ASN   B O   1 
ATOM   25029 C  CB  . ASN   B 1 1390 ? 28.76300   33.30900  -2.80300  1.000 67.33671  ?  1388 ASN   B CB  1 
ATOM   25030 C  CG  . ASN   B 1 1390 ? 29.58500   34.37800  -3.50000  1.000 71.65951  ?  1388 ASN   B CG  1 
ATOM   25031 O  OD1 . ASN   B 1 1390 ? 29.29400   34.76200  -4.63300  1.000 62.34878  ?  1388 ASN   B OD1 1 
ATOM   25032 N  ND2 . ASN   B 1 1390 ? 30.61600   34.86800  -2.82000  1.000 70.92362  ?  1388 ASN   B ND2 1 
ATOM   25033 N  N   . VAL   B 1 1391 ? 30.67600   31.02700  -1.88500  1.000 57.14141  ?  1389 VAL   B N   1 
ATOM   25034 C  CA  . VAL   B 1 1391 ? 32.00900   30.52700  -1.57400  1.000 52.39401  ?  1389 VAL   B CA  1 
ATOM   25035 C  C   . VAL   B 1 1391 ? 32.27800   29.22000  -2.31300  1.000 68.62227  ?  1389 VAL   B C   1 
ATOM   25036 O  O   . VAL   B 1 1391 ? 33.41100   28.96100  -2.73600  1.000 61.46097  ?  1389 VAL   B O   1 
ATOM   25037 C  CB  . VAL   B 1 1391 ? 32.18300   30.38000  -0.05000  1.000 55.17500  ?  1389 VAL   B CB  1 
ATOM   25038 C  CG1 . VAL   B 1 1391 ? 31.17800   29.39400  0.51700   1.000 63.77388  ?  1389 VAL   B CG1 1 
ATOM   25039 C  CG2 . VAL   B 1 1391 ? 33.60300   29.96100  0.28800   1.000 45.72855  ?  1389 VAL   B CG2 1 
ATOM   25040 N  N   . LEU   B 1 1392 ? 31.25000   28.39000  -2.51100  1.000 61.88840  ?  1390 LEU   B N   1 
ATOM   25041 C  CA  . LEU   B 1 1392 ? 31.45500   27.14100  -3.23600  1.000 64.24690  ?  1390 LEU   B CA  1 
ATOM   25042 C  C   . LEU   B 1 1392 ? 31.68500   27.40000  -4.71900  1.000 63.49718  ?  1390 LEU   B C   1 
ATOM   25043 O  O   . LEU   B 1 1392 ? 32.57100   26.79200  -5.33200  1.000 63.72881  ?  1390 LEU   B O   1 
ATOM   25044 C  CB  . LEU   B 1 1392 ? 30.26300   26.20700  -3.03000  1.000 62.06424  ?  1390 LEU   B CB  1 
ATOM   25045 C  CG  . LEU   B 1 1392 ? 30.17600   25.49600  -1.67600  1.000 59.68556  ?  1390 LEU   B CG  1 
ATOM   25046 C  CD1 . LEU   B 1 1392 ? 28.87500   24.71200  -1.56800  1.000 44.36628  ?  1390 LEU   B CD1 1 
ATOM   25047 C  CD2 . LEU   B 1 1392 ? 31.38100   24.59200  -1.45100  1.000 45.62140  ?  1390 LEU   B CD2 1 
ATOM   25048 N  N   . HIS   B 1 1393 ? 30.90200   28.30200  -5.31000  1.000 62.10483  ?  1391 HIS   B N   1 
ATOM   25049 C  CA  . HIS   B 1 1393 ? 31.09300   28.63400  -6.71800  1.000 70.93430  ?  1391 HIS   B CA  1 
ATOM   25050 C  C   . HIS   B 1 1393 ? 32.42400   29.34400  -6.93500  1.000 68.75812  ?  1391 HIS   B C   1 
ATOM   25051 O  O   . HIS   B 1 1393 ? 33.16800   29.01700  -7.86800  1.000 64.85410  ?  1391 HIS   B O   1 
ATOM   25052 C  CB  . HIS   B 1 1393 ? 29.93100   29.49600  -7.21400  1.000 57.21599  ?  1391 HIS   B CB  1 
ATOM   25053 C  CG  . HIS   B 1 1393 ? 28.74500   28.70800  -7.67500  1.000 69.20362  ?  1391 HIS   B CG  1 
ATOM   25054 N  ND1 . HIS   B 1 1393 ? 28.85100   27.63000  -8.52800  1.000 78.32266  ?  1391 HIS   B ND1 1 
ATOM   25055 C  CD2 . HIS   B 1 1393 ? 27.42500   28.84600  -7.40700  1.000 70.16792  ?  1391 HIS   B CD2 1 
ATOM   25056 C  CE1 . HIS   B 1 1393 ? 27.64800   27.13800  -8.76400  1.000 77.23492  ?  1391 HIS   B CE1 1 
ATOM   25057 N  NE2 . HIS   B 1 1393 ? 26.76500   27.85800  -8.09600  1.000 75.02440  ?  1391 HIS   B NE2 1 
ATOM   25058 N  N   . GLY   B 1 1394 ? 32.74200   30.31800  -6.08000  1.000 60.85847  ?  1392 GLY   B N   1 
ATOM   25059 C  CA  . GLY   B 1 1394 ? 34.00000   31.03200  -6.22500  1.000 74.28171  ?  1392 GLY   B CA  1 
ATOM   25060 C  C   . GLY   B 1 1394 ? 35.20200   30.12000  -6.08800  1.000 68.14798  ?  1392 GLY   B C   1 
ATOM   25061 O  O   . GLY   B 1 1394 ? 36.19300   30.26700  -6.81000  1.000 60.41249  ?  1392 GLY   B O   1 
ATOM   25062 N  N   . MET   B 1 1395 ? 35.12800   29.15700  -5.16900  1.000 59.03974  ?  1393 MET   B N   1 
ATOM   25063 C  CA  . MET   B 1 1395 ? 36.21500   28.19800  -5.03000  1.000 65.51710  ?  1393 MET   B CA  1 
ATOM   25064 C  C   . MET   B 1 1395 ? 36.25700   27.22500  -6.19800  1.000 69.97261  ?  1393 MET   B C   1 
ATOM   25065 O  O   . MET   B 1 1395 ? 37.33500   26.74000  -6.55900  1.000 71.75454  ?  1393 MET   B O   1 
ATOM   25066 C  CB  . MET   B 1 1395 ? 36.08200   27.44200  -3.71300  1.000 62.31401  ?  1393 MET   B CB  1 
ATOM   25067 C  CG  . MET   B 1 1395 ? 36.44100   28.27200  -2.50200  1.000 68.78118  ?  1393 MET   B CG  1 
ATOM   25068 S  SD  . MET   B 1 1395 ? 38.20600   28.60900  -2.47700  1.000 71.26022  ?  1393 MET   B SD  1 
ATOM   25069 C  CE  . MET   B 1 1395 ? 38.67200   27.65300  -1.05000  1.000 55.26828  ?  1393 MET   B CE  1 
ATOM   25070 N  N   . GLN   B 1 1396 ? 35.10300   26.92900  -6.79900  1.000 70.45315  ?  1394 GLN   B N   1 
ATOM   25071 C  CA  . GLN   B 1 1396 ? 35.09300   26.08100  -7.98300  1.000 71.37188  ?  1394 GLN   B CA  1 
ATOM   25072 C  C   . GLN   B 1 1396 ? 35.68100   26.80500  -9.18600  1.000 71.05494  ?  1394 GLN   B C   1 
ATOM   25073 O  O   . GLN   B 1 1396 ? 36.24900   26.16500  -10.07800 1.000 75.60803  ?  1394 GLN   B O   1 
ATOM   25074 C  CB  . GLN   B 1 1396 ? 33.66700   25.60900  -8.27400  1.000 76.33557  ?  1394 GLN   B CB  1 
ATOM   25075 C  CG  . GLN   B 1 1396 ? 33.56300   24.58900  -9.39200  1.000 71.39127  ?  1394 GLN   B CG  1 
ATOM   25076 C  CD  . GLN   B 1 1396 ? 34.21400   23.26200  -9.04500  1.000 78.64859  ?  1394 GLN   B CD  1 
ATOM   25077 O  OE1 . GLN   B 1 1396 ? 34.62600   22.51400  -9.93200  1.000 89.99579  ?  1394 GLN   B OE1 1 
ATOM   25078 N  NE2 . GLN   B 1 1396 ? 34.30100   22.95900  -7.75400  1.000 76.57383  ?  1394 GLN   B NE2 1 
ATOM   25079 N  N   . ASP   B 1 1397 ? 35.56200   28.13300  -9.22600  1.000 73.23524  ?  1395 ASP   B N   1 
ATOM   25080 C  CA  . ASP   B 1 1397 ? 36.20600   28.89200  -10.29100 1.000 76.86524  ?  1395 ASP   B CA  1 
ATOM   25081 C  C   . ASP   B 1 1397 ? 37.71400   28.94500  -10.09900 1.000 69.11428  ?  1395 ASP   B C   1 
ATOM   25082 O  O   . ASP   B 1 1397 ? 38.46500   28.96300  -11.08100 1.000 73.66623  ?  1395 ASP   B O   1 
ATOM   25083 C  CB  . ASP   B 1 1397 ? 35.62900   30.30500  -10.35300 1.000 69.70113  ?  1395 ASP   B CB  1 
ATOM   25084 C  CG  . ASP   B 1 1397 ? 35.34400   30.75500  -11.77200 1.000 97.03829  ?  1395 ASP   B CG  1 
ATOM   25085 O  OD1 . ASP   B 1 1397 ? 36.29800   30.82800  -12.57700 1.000 94.73878  ?  1395 ASP   B OD1 1 
ATOM   25086 O  OD2 . ASP   B 1 1397 ? 34.16800   31.03500  -12.08400 1.000 101.75112 -1 1395 ASP   B OD2 1 
ATOM   25087 N  N   . GLU   B 1 1398 ? 38.17100   28.95600  -8.85000  1.000 59.20996  ?  1396 GLU   B N   1 
ATOM   25088 C  CA  . GLU   B 1 1398 ? 39.59800   29.04600  -8.57500  1.000 73.83711  ?  1396 GLU   B CA  1 
ATOM   25089 C  C   . GLU   B 1 1398 ? 40.26300   27.67500  -8.63700  1.000 78.87566  ?  1396 GLU   B C   1 
ATOM   25090 O  O   . GLU   B 1 1398 ? 41.23500   27.47500  -9.37200  1.000 82.70691  ?  1396 GLU   B O   1 
ATOM   25091 C  CB  . GLU   B 1 1398 ? 39.81600   29.69400  -7.20800  1.000 82.29012  ?  1396 GLU   B CB  1 
ATOM   25092 C  CG  . GLU   B 1 1398 ? 39.39800   31.14900  -7.13000  1.000 88.75572  ?  1396 GLU   B CG  1 
ATOM   25093 C  CD  . GLU   B 1 1398 ? 40.41200   32.04400  -7.79000  1.000 92.50574  ?  1396 GLU   B CD  1 
ATOM   25094 O  OE1 . GLU   B 1 1398 ? 41.61300   31.82100  -7.54200  1.000 84.52681  ?  1396 GLU   B OE1 1 
ATOM   25095 O  OE2 . GLU   B 1 1398 ? 40.01600   32.96600  -8.53700  1.000 101.58222 -1 1396 GLU   B OE2 1 
ATOM   25096 N  N   . TYR   B 1 1399 ? 39.74300   26.71600  -7.86500  1.000 81.39928  ?  1397 TYR   B N   1 
ATOM   25097 C  CA  . TYR   B 1 1399 ? 40.29200   25.36500  -7.76300  1.000 84.12586  ?  1397 TYR   B CA  1 
ATOM   25098 C  C   . TYR   B 1 1399 ? 39.19600   24.38800  -8.17100  1.000 81.39123  ?  1397 TYR   B C   1 
ATOM   25099 O  O   . TYR   B 1 1399 ? 38.52300   23.79600  -7.31300  1.000 84.21106  ?  1397 TYR   B O   1 
ATOM   25100 C  CB  . TYR   B 1 1399 ? 40.80700   25.07100  -6.35400  1.000 79.07055  ?  1397 TYR   B CB  1 
ATOM   25101 C  CG  . TYR   B 1 1399 ? 41.43400   26.26400  -5.66200  1.000 87.27579  ?  1397 TYR   B CG  1 
ATOM   25102 C  CD1 . TYR   B 1 1399 ? 40.65000   27.22500  -5.03000  1.000 84.84415  ?  1397 TYR   B CD1 1 
ATOM   25103 C  CD2 . TYR   B 1 1399 ? 42.81000   26.44100  -5.66200  1.000 88.77565  ?  1397 TYR   B CD2 1 
ATOM   25104 C  CE1 . TYR   B 1 1399 ? 41.22300   28.31700  -4.40700  1.000 76.22364  ?  1397 TYR   B CE1 1 
ATOM   25105 C  CE2 . TYR   B 1 1399 ? 43.38800   27.52800  -5.04600  1.000 75.72954  ?  1397 TYR   B CE2 1 
ATOM   25106 C  CZ  . TYR   B 1 1399 ? 42.59300   28.46200  -4.41900  1.000 72.53154  ?  1397 TYR   B CZ  1 
ATOM   25107 O  OH  . TYR   B 1 1399 ? 43.16900   29.54600  -3.80200  1.000 81.15430  ?  1397 TYR   B OH  1 
ATOM   25108 N  N   . PRO   B 1 1400 ? 38.98900   24.19300  -9.47300  1.000 76.45006  ?  1398 PRO   B N   1 
ATOM   25109 C  CA  . PRO   B 1 1400 ? 37.84200   23.39600  -9.92900  1.000 81.06095  ?  1398 PRO   B CA  1 
ATOM   25110 C  C   . PRO   B 1 1400 ? 38.01700   21.91800  -9.60900  1.000 91.63091  ?  1398 PRO   B C   1 
ATOM   25111 O  O   . PRO   B 1 1400 ? 39.04700   21.31500  -9.92100  1.000 89.39065  ?  1398 PRO   B O   1 
ATOM   25112 C  CB  . PRO   B 1 1400 ? 37.81100   23.64700  -11.44300 1.000 76.87838  ?  1398 PRO   B CB  1 
ATOM   25113 C  CG  . PRO   B 1 1400 ? 38.71200   24.84000  -11.67300 1.000 72.56797  ?  1398 PRO   B CG  1 
ATOM   25114 C  CD  . PRO   B 1 1400 ? 39.74000   24.77700  -10.59500 1.000 63.70754  ?  1398 PRO   B CD  1 
ATOM   25115 N  N   . LEU   B 1 1401 ? 36.99700   21.34300  -8.97200  1.000 103.74237 ?  1399 LEU   B N   1 
ATOM   25116 C  CA  . LEU   B 1 1401 ? 36.88100   19.90100  -8.76300  1.000 95.35750  ?  1399 LEU   B CA  1 
ATOM   25117 C  C   . LEU   B 1 1401 ? 35.72400   19.42500  -9.63600  1.000 101.03977 ?  1399 LEU   B C   1 
ATOM   25118 O  O   . LEU   B 1 1401 ? 34.55600   19.54500  -9.25600  1.000 90.01540  ?  1399 LEU   B O   1 
ATOM   25119 C  CB  . LEU   B 1 1401 ? 36.65100   19.56500  -7.29000  1.000 79.89715  ?  1399 LEU   B CB  1 
ATOM   25120 C  CG  . LEU   B 1 1401 ? 36.84300   18.10300  -6.87100  1.000 73.20698  ?  1399 LEU   B CG  1 
ATOM   25121 C  CD1 . LEU   B 1 1401 ? 37.27300   18.01900  -5.41900  1.000 74.54833  ?  1399 LEU   B CD1 1 
ATOM   25122 C  CD2 . LEU   B 1 1401 ? 35.58000   17.28300  -7.09000  1.000 86.98086  ?  1399 LEU   B CD2 1 
ATOM   25123 N  N   . LEU   B 1 1402 ? 36.05300   18.89600  -10.80600 1.000 92.66897  ?  1400 LEU   B N   1 
ATOM   25124 C  CA  . LEU   B 1 1402 ? 35.06500   18.40600  -11.75000 1.000 95.03962  ?  1400 LEU   B CA  1 
ATOM   25125 C  C   . LEU   B 1 1402 ? 34.95000   16.88700  -11.61200 1.000 101.56406 ?  1400 LEU   B C   1 
ATOM   25126 O  O   . LEU   B 1 1402 ? 35.30600   16.31600  -10.57500 1.000 99.78995  ?  1400 LEU   B O   1 
ATOM   25127 C  CB  . LEU   B 1 1402 ? 35.46500   18.84500  -13.16100 1.000 91.28593  ?  1400 LEU   B CB  1 
ATOM   25128 C  CG  . LEU   B 1 1402 ? 36.09900   20.23300  -13.25100 1.000 90.81227  ?  1400 LEU   B CG  1 
ATOM   25129 C  CD1 . LEU   B 1 1402 ? 36.94700   20.35700  -14.50900 1.000 56.05751  ?  1400 LEU   B CD1 1 
ATOM   25130 C  CD2 . LEU   B 1 1402 ? 35.02500   21.31000  -13.20900 1.000 92.12648  ?  1400 LEU   B CD2 1 
ATOM   25131 N  N   . GLN   B 1 1403 ? 34.45500   16.22300  -12.65400 1.000 103.72147 ?  1401 GLN   B N   1 
ATOM   25132 C  CA  . GLN   B 1 1403 ? 34.55300   14.77500  -12.70700 1.000 91.65024  ?  1401 GLN   B CA  1 
ATOM   25133 C  C   . GLN   B 1 1403 ? 36.02100   14.36100  -12.69300 1.000 99.67067  ?  1401 GLN   B C   1 
ATOM   25134 O  O   . GLN   B 1 1403 ? 36.92300   15.16800  -12.93500 1.000 110.76350 ?  1401 GLN   B O   1 
ATOM   25135 C  CB  . GLN   B 1 1403 ? 33.86100   14.23000  -13.95700 1.000 79.77618  ?  1401 GLN   B CB  1 
ATOM   25136 C  CG  . GLN   B 1 1403 ? 32.55400   14.92600  -14.30000 1.000 95.44494  ?  1401 GLN   B CG  1 
ATOM   25137 C  CD  . GLN   B 1 1403 ? 32.27700   14.95800  -15.79500 1.000 112.15378 ?  1401 GLN   B CD  1 
ATOM   25138 O  OE1 . GLN   B 1 1403 ? 33.20000   14.94200  -16.61100 1.000 110.98335 ?  1401 GLN   B OE1 1 
ATOM   25139 N  NE2 . GLN   B 1 1403 ? 30.99900   15.00200  -16.16000 1.000 115.23859 ?  1401 GLN   B NE2 1 
ATOM   25140 N  N   . ASP   B 1 1404 ? 36.25600   13.08400  -12.38700 1.000 102.95608 ?  1402 ASP   B N   1 
ATOM   25141 C  CA  . ASP   B 1 1404 ? 37.59600   12.50200  -12.32800 1.000 103.18154 ?  1402 ASP   B CA  1 
ATOM   25142 C  C   . ASP   B 1 1404 ? 38.44500   13.10700  -11.20800 1.000 96.24491  ?  1402 ASP   B C   1 
ATOM   25143 O  O   . ASP   B 1 1404 ? 39.56300   12.64400  -10.95600 1.000 83.68145  ?  1402 ASP   B O   1 
ATOM   25144 C  CB  . ASP   B 1 1404 ? 38.34200   12.64200  -13.67200 1.000 90.07287  ?  1402 ASP   B CB  1 
ATOM   25145 C  CG  . ASP   B 1 1404 ? 37.44400   12.42500  -14.90200 1.000 119.62605 ?  1402 ASP   B CG  1 
ATOM   25146 O  OD1 . ASP   B 1 1404 ? 36.63400   13.31600  -15.25100 1.000 122.46133 ?  1402 ASP   B OD1 1 
ATOM   25147 O  OD2 . ASP   B 1 1404 ? 37.56300   11.34900  -15.53100 1.000 132.45190 -1 1402 ASP   B OD2 1 
ATOM   25148 N  N   . ASP   B 1 1405 ? 37.93500   14.13600  -10.53700 1.000 104.64208 ?  1403 ASP   B N   1 
ATOM   25149 C  CA  . ASP   B 1 1405 ? 38.60800   14.78400  -9.42100  1.000 92.97113  ?  1403 ASP   B CA  1 
ATOM   25150 C  C   . ASP   B 1 1405 ? 37.95900   14.35900  -8.10700  1.000 86.95706  ?  1403 ASP   B C   1 
ATOM   25151 O  O   . ASP   B 1 1405 ? 36.79000   13.96500  -8.06500  1.000 81.54415  ?  1403 ASP   B O   1 
ATOM   25152 C  CB  . ASP   B 1 1405 ? 38.56300   16.30800  -9.57300  1.000 86.48207  ?  1403 ASP   B CB  1 
ATOM   25153 C  CG  . ASP   B 1 1405 ? 39.12500   16.77800  -10.90500 1.000 101.02125 ?  1403 ASP   B CG  1 
ATOM   25154 O  OD1 . ASP   B 1 1405 ? 40.09500   16.16100  -11.39500 1.000 95.20981  ?  1403 ASP   B OD1 1 
ATOM   25155 O  OD2 . ASP   B 1 1405 ? 38.59700   17.76600  -11.46300 1.000 94.03674  -1 1403 ASP   B OD2 1 
ATOM   25156 N  N   . ALA   B 1 1406 ? 38.73300   14.44300  -7.02500  1.000 80.23006  ?  1404 ALA   B N   1 
ATOM   25157 C  CA  . ALA   B 1 1406 ? 38.31000   13.88800  -5.74800  1.000 71.29586  ?  1404 ALA   B CA  1 
ATOM   25158 C  C   . ALA   B 1 1406 ? 38.76600   14.76200  -4.59100  1.000 80.46209  ?  1404 ALA   B C   1 
ATOM   25159 O  O   . ALA   B 1 1406 ? 39.89100   15.26800  -4.58600  1.000 80.94632  ?  1404 ALA   B O   1 
ATOM   25160 C  CB  . ALA   B 1 1406 ? 38.85500   12.46700  -5.55800  1.000 72.12922  ?  1404 ALA   B CB  1 
ATOM   25161 N  N   . PHE   B 1 1407 ? 37.88300   14.91800  -3.60600  1.000 86.50294  ?  1405 PHE   B N   1 
ATOM   25162 C  CA  . PHE   B 1 1407 ? 38.17500   15.57100  -2.33900  1.000 79.06111  ?  1405 PHE   B CA  1 
ATOM   25163 C  C   . PHE   B 1 1407 ? 38.27800   14.52000  -1.23900  1.000 69.40943  ?  1405 PHE   B C   1 
ATOM   25164 O  O   . PHE   B 1 1407 ? 37.75600   13.40800  -1.36400  1.000 77.31160  ?  1405 PHE   B O   1 
ATOM   25165 C  CB  . PHE   B 1 1407 ? 37.09200   16.60000  -1.99000  1.000 72.08335  ?  1405 PHE   B CB  1 
ATOM   25166 C  CG  . PHE   B 1 1407 ? 37.63200   17.90100  -1.46100  1.000 66.05983  ?  1405 PHE   B CG  1 
ATOM   25167 C  CD1 . PHE   B 1 1407 ? 38.63900   17.91700  -0.50900  1.000 76.09339  ?  1405 PHE   B CD1 1 
ATOM   25168 C  CD2 . PHE   B 1 1407 ? 37.12800   19.10900  -1.91400  1.000 67.68362  ?  1405 PHE   B CD2 1 
ATOM   25169 C  CE1 . PHE   B 1 1407 ? 39.13500   19.11000  -0.01900  1.000 69.89452  ?  1405 PHE   B CE1 1 
ATOM   25170 C  CE2 . PHE   B 1 1407 ? 37.62000   20.30600  -1.42900  1.000 73.78544  ?  1405 PHE   B CE2 1 
ATOM   25171 C  CZ  . PHE   B 1 1407 ? 38.62500   20.30600  -0.48000  1.000 79.61256  ?  1405 PHE   B CZ  1 
ATOM   25172 N  N   . LEU   B 1 1408 ? 38.95700   14.88200  -0.15200  1.000 65.46757  ?  1406 LEU   B N   1 
ATOM   25173 C  CA  . LEU   B 1 1408 ? 39.19600   13.98100  0.97200   1.000 70.97690  ?  1406 LEU   B CA  1 
ATOM   25174 C  C   . LEU   B 1 1408 ? 38.60800   14.59700  2.23600   1.000 65.27716  ?  1406 LEU   B C   1 
ATOM   25175 O  O   . LEU   B 1 1408 ? 39.13100   15.59200  2.74900   1.000 79.28544  ?  1406 LEU   B O   1 
ATOM   25176 C  CB  . LEU   B 1 1408 ? 40.69000   13.70800  1.14600   1.000 64.75609  ?  1406 LEU   B CB  1 
ATOM   25177 C  CG  . LEU   B 1 1408 ? 41.07000   12.62300  2.15600   1.000 53.56872  ?  1406 LEU   B CG  1 
ATOM   25178 C  CD1 . LEU   B 1 1408 ? 40.14800   11.43500  2.01900   1.000 56.88881  ?  1406 LEU   B CD1 1 
ATOM   25179 C  CD2 . LEU   B 1 1408 ? 42.50700   12.19000  1.96600   1.000 71.84525  ?  1406 LEU   B CD2 1 
ATOM   25180 N  N   . LEU   B 1 1409 ? 37.53300   14.00100  2.74300   1.000 50.18900  ?  1407 LEU   B N   1 
ATOM   25181 C  CA  . LEU   B 1 1409 ? 36.90500   14.46500  3.97700   1.000 54.66570  ?  1407 LEU   B CA  1 
ATOM   25182 C  C   . LEU   B 1 1409 ? 37.77800   14.06100  5.15600   1.000 54.26299  ?  1407 LEU   B C   1 
ATOM   25183 O  O   . LEU   B 1 1409 ? 37.79400   12.89800  5.56300   1.000 52.64145  ?  1407 LEU   B O   1 
ATOM   25184 C  CB  . LEU   B 1 1409 ? 35.50100   13.88700  4.11300   1.000 55.27930  ?  1407 LEU   B CB  1 
ATOM   25185 C  CG  . LEU   B 1 1409 ? 34.62900   14.48100  5.22000   1.000 42.79940  ?  1407 LEU   B CG  1 
ATOM   25186 C  CD1 . LEU   B 1 1409 ? 34.29000   15.93500  4.92400   1.000 43.65629  ?  1407 LEU   B CD1 1 
ATOM   25187 C  CD2 . LEU   B 1 1409 ? 33.36900   13.64900  5.40300   1.000 49.28400  ?  1407 LEU   B CD2 1 
ATOM   25188 N  N   . LYS   B 1 1410 ? 38.51300   15.02400  5.71200   1.000 52.69285  ?  1408 LYS   B N   1 
ATOM   25189 C  CA  . LYS   B 1 1410 ? 39.36400   14.77400  6.86800   1.000 54.58747  ?  1408 LYS   B CA  1 
ATOM   25190 C  C   . LYS   B 1 1410 ? 39.18500   15.77700  7.99500   1.000 57.15562  ?  1408 LYS   B C   1 
ATOM   25191 O  O   . LYS   B 1 1410 ? 39.54500   15.45800  9.13500   1.000 61.67411  ?  1408 LYS   B O   1 
ATOM   25192 C  CB  . LYS   B 1 1410 ? 40.84500   14.76000  6.45600   1.000 61.09434  ?  1408 LYS   B CB  1 
ATOM   25193 C  CG  . LYS   B 1 1410 ? 41.31000   16.02700  5.75900   1.000 63.28954  ?  1408 LYS   B CG  1 
ATOM   25194 C  CD  . LYS   B 1 1410 ? 42.82500   16.15300  5.79200   1.000 65.34748  ?  1408 LYS   B CD  1 
ATOM   25195 C  CE  . LYS   B 1 1410 ? 43.32400   16.62200  7.14600   1.000 69.48358  ?  1408 LYS   B CE  1 
ATOM   25196 N  NZ  . LYS   B 1 1410 ? 44.79800   16.46100  7.26300   1.000 50.83184  ?  1408 LYS   B NZ  1 
ATOM   25197 N  N   . THR   B 1 1411 ? 38.65000   16.96500  7.72600   1.000 65.14967  ?  1409 THR   B N   1 
ATOM   25198 C  CA  . THR   B 1 1411 ? 38.41700   17.95200  8.77000   1.000 61.84266  ?  1409 THR   B CA  1 
ATOM   25199 C  C   . THR   B 1 1411 ? 37.19600   17.56800  9.59400   1.000 48.69573  ?  1409 THR   B C   1 
ATOM   25200 O  O   . THR   B 1 1411 ? 36.16800   17.15600  9.04900   1.000 57.57783  ?  1409 THR   B O   1 
ATOM   25201 C  CB  . THR   B 1 1411 ? 38.21400   19.34000  8.16200   1.000 54.75154  ?  1409 THR   B CB  1 
ATOM   25202 O  OG1 . THR   B 1 1411 ? 39.16000   19.55000  7.10400   1.000 45.76133  ?  1409 THR   B OG1 1 
ATOM   25203 C  CG2 . THR   B 1 1411 ? 38.39300   20.41400  9.22600   1.000 49.51569  ?  1409 THR   B CG2 1 
ATOM   25204 N  N   . THR   B 1 1412 ? 37.31600   17.69700  10.91500  1.000 47.34891  ?  1410 THR   B N   1 
ATOM   25205 C  CA  . THR   B 1 1412 ? 36.19800   17.39200  11.79900  1.000 47.00922  ?  1410 THR   B CA  1 
ATOM   25206 C  C   . THR   B 1 1412 ? 35.00600   18.27200  11.45200  1.000 55.98758  ?  1410 THR   B C   1 
ATOM   25207 O  O   . THR   B 1 1412 ? 35.15000   19.48100  11.24800  1.000 61.92568  ?  1410 THR   B O   1 
ATOM   25208 C  CB  . THR   B 1 1412 ? 36.59900   17.59400  13.25800  1.000 34.50440  ?  1410 THR   B CB  1 
ATOM   25209 O  OG1 . THR   B 1 1412 ? 37.90500   17.04500  13.47400  1.000 72.57517  ?  1410 THR   B OG1 1 
ATOM   25210 C  CG2 . THR   B 1 1412 ? 35.60600   16.90400  14.18100  1.000 57.60834  ?  1410 THR   B CG2 1 
ATOM   25211 N  N   . TYR   B 1 1413 ? 33.82300   17.66100  11.38400  1.000 61.84586  ?  1411 TYR   B N   1 
ATOM   25212 C  CA  . TYR   B 1 1413 ? 32.65200   18.38000  10.89600  1.000 49.97629  ?  1411 TYR   B CA  1 
ATOM   25213 C  C   . TYR   B 1 1413 ? 32.16600   19.45800  11.85900  1.000 52.10032  ?  1411 TYR   B C   1 
ATOM   25214 O  O   . TYR   B 1 1413 ? 31.17800   20.13400  11.55100  1.000 41.66945  ?  1411 TYR   B O   1 
ATOM   25215 C  CB  . TYR   B 1 1413 ? 31.53200   17.38700  10.56100  1.000 42.09949  ?  1411 TYR   B CB  1 
ATOM   25216 C  CG  . TYR   B 1 1413 ? 30.66200   16.93200  11.71500  1.000 48.14265  ?  1411 TYR   B CG  1 
ATOM   25217 C  CD1 . TYR   B 1 1413 ? 31.21400   16.56700  12.93600  1.000 45.79994  ?  1411 TYR   B CD1 1 
ATOM   25218 C  CD2 . TYR   B 1 1413 ? 29.28400   16.82700  11.56200  1.000 39.11782  ?  1411 TYR   B CD2 1 
ATOM   25219 C  CE1 . TYR   B 1 1413 ? 30.41400   16.14100  13.98200  1.000 48.58333  ?  1411 TYR   B CE1 1 
ATOM   25220 C  CE2 . TYR   B 1 1413 ? 28.48000   16.40000  12.59700  1.000 46.49789  ?  1411 TYR   B CE2 1 
ATOM   25221 C  CZ  . TYR   B 1 1413 ? 29.04800   16.05800  13.80500  1.000 52.75301  ?  1411 TYR   B CZ  1 
ATOM   25222 O  OH  . TYR   B 1 1413 ? 28.24500   15.63200  14.83700  1.000 52.06222  ?  1411 TYR   B OH  1 
ATOM   25223 N  N   . ILE   B 1 1414 ? 32.84200   19.64400  12.99900  1.000 52.10735  ?  1412 ILE   B N   1 
ATOM   25224 C  CA  . ILE   B 1 1414 ? 32.58300   20.78800  13.86700  1.000 61.84347  ?  1412 ILE   B CA  1 
ATOM   25225 C  C   . ILE   B 1 1414 ? 33.38100   22.01900  13.45900  1.000 66.36983  ?  1412 ILE   B C   1 
ATOM   25226 O  O   . ILE   B 1 1414 ? 33.29800   23.05300  14.13700  1.000 55.25458  ?  1412 ILE   B O   1 
ATOM   25227 C  CB  . ILE   B 1 1414 ? 32.88700   20.44700  15.34000  1.000 51.29579  ?  1412 ILE   B CB  1 
ATOM   25228 C  CG1 . ILE   B 1 1414 ? 34.35600   20.06100  15.50500  1.000 44.92482  ?  1412 ILE   B CG1 1 
ATOM   25229 C  CG2 . ILE   B 1 1414 ? 31.98300   19.32900  15.82800  1.000 62.51387  ?  1412 ILE   B CG2 1 
ATOM   25230 C  CD1 . ILE   B 1 1414 ? 34.77200   19.89800  16.94400  1.000 53.56615  ?  1412 ILE   B CD1 1 
ATOM   25231 N  N   . PHE   B 1 1415 ? 34.15700   21.94100  12.38000  1.000 57.65925  ?  1413 PHE   B N   1 
ATOM   25232 C  CA  . PHE   B 1 1415 ? 34.89700   23.07500  11.84700  1.000 46.29522  ?  1413 PHE   B CA  1 
ATOM   25233 C  C   . PHE   B 1 1415 ? 34.30900   23.47900  10.50200  1.000 53.94765  ?  1413 PHE   B C   1 
ATOM   25234 O  O   . PHE   B 1 1415 ? 33.95400   22.62000  9.68900   1.000 61.62171  ?  1413 PHE   B O   1 
ATOM   25235 C  CB  . PHE   B 1 1415 ? 36.38200   22.73900  11.68500  1.000 53.24326  ?  1413 PHE   B CB  1 
ATOM   25236 C  CG  . PHE   B 1 1415 ? 37.06100   22.35600  12.96800  1.000 63.79835  ?  1413 PHE   B CG  1 
ATOM   25237 C  CD1 . PHE   B 1 1415 ? 36.89800   23.12300  14.10900  1.000 64.65968  ?  1413 PHE   B CD1 1 
ATOM   25238 C  CD2 . PHE   B 1 1415 ? 37.86300   21.22600  13.03400  1.000 71.79283  ?  1413 PHE   B CD2 1 
ATOM   25239 C  CE1 . PHE   B 1 1415 ? 37.52100   22.77300  15.29300  1.000 70.25445  ?  1413 PHE   B CE1 1 
ATOM   25240 C  CE2 . PHE   B 1 1415 ? 38.48800   20.87000  14.21600  1.000 69.19463  ?  1413 PHE   B CE2 1 
ATOM   25241 C  CZ  . PHE   B 1 1415 ? 38.31700   21.64500  15.34600  1.000 61.68241  ?  1413 PHE   B CZ  1 
ATOM   25242 N  N   . ASP   B 1 1416 ? 34.21400   24.79200  10.27000  1.000 58.53646  ?  1414 ASP   B N   1 
ATOM   25243 C  CA  . ASP   B 1 1416 ? 33.62600   25.28600  9.02700   1.000 56.65961  ?  1414 ASP   B CA  1 
ATOM   25244 C  C   . ASP   B 1 1416 ? 34.37500   24.77700  7.80000   1.000 53.83567  ?  1414 ASP   B C   1 
ATOM   25245 O  O   . ASP   B 1 1416 ? 33.78800   24.67400  6.71700   1.000 53.75509  ?  1414 ASP   B O   1 
ATOM   25246 C  CB  . ASP   B 1 1416 ? 33.59200   26.81800  9.03000   1.000 59.02146  ?  1414 ASP   B CB  1 
ATOM   25247 C  CG  . ASP   B 1 1416 ? 34.97700   27.43700  9.12100   1.000 81.60893  ?  1414 ASP   B CG  1 
ATOM   25248 O  OD1 . ASP   B 1 1416 ? 35.89600   26.78200  9.66000   1.000 84.03370  ?  1414 ASP   B OD1 1 
ATOM   25249 O  OD2 . ASP   B 1 1416 ? 35.14500   28.58600  8.65500   1.000 73.51880  -1 1414 ASP   B OD2 1 
ATOM   25250 N  N   . ILE   B 1 1417 ? 35.66200   24.45100  7.95000   1.000 49.61107  ?  1415 ILE   B N   1 
ATOM   25251 C  CA  . ILE   B 1 1417 ? 36.44800   23.94800  6.82500   1.000 60.43997  ?  1415 ILE   B CA  1 
ATOM   25252 C  C   . ILE   B 1 1417 ? 35.82100   22.68300  6.25500   1.000 54.48625  ?  1415 ILE   B C   1 
ATOM   25253 O  O   . ILE   B 1 1417 ? 35.80900   22.47200  5.03500   1.000 53.79629  ?  1415 ILE   B O   1 
ATOM   25254 C  CB  . ILE   B 1 1417 ? 37.90700   23.71000  7.26000   1.000 57.84666  ?  1415 ILE   B CB  1 
ATOM   25255 C  CG1 . ILE   B 1 1417 ? 38.61200   25.04100  7.52800   1.000 60.03944  ?  1415 ILE   B CG1 1 
ATOM   25256 C  CG2 . ILE   B 1 1417 ? 38.65800   22.89900  6.21400   1.000 46.97018  ?  1415 ILE   B CG2 1 
ATOM   25257 C  CD1 . ILE   B 1 1417 ? 39.67400   24.96400  8.60900   1.000 52.41073  ?  1415 ILE   B CD1 1 
ATOM   25258 N  N   . SER   B 1 1418 ? 35.27800   21.82700  7.12700   1.000 57.69752  ?  1416 SER   B N   1 
ATOM   25259 C  CA  . SER   B 1 1418 ? 34.67100   20.57800  6.67600   1.000 49.59977  ?  1416 SER   B CA  1 
ATOM   25260 C  C   . SER   B 1 1418 ? 33.55600   20.82200  5.66800   1.000 51.52265  ?  1416 SER   B C   1 
ATOM   25261 O  O   . SER   B 1 1418 ? 33.33500   19.99400  4.77600   1.000 45.91061  ?  1416 SER   B O   1 
ATOM   25262 C  CB  . SER   B 1 1418 ? 34.14100   19.79400  7.87800   1.000 32.88000  ?  1416 SER   B CB  1 
ATOM   25263 O  OG  . SER   B 1 1418 ? 33.12400   20.51800  8.54600   1.000 42.68382  ?  1416 SER   B OG  1 
ATOM   25264 N  N   . VAL   B 1 1419 ? 32.85600   21.95200  5.78400   1.000 56.83413  ?  1417 VAL   B N   1 
ATOM   25265 C  CA  . VAL   B 1 1419 ? 31.79300   22.27100  4.83800   1.000 47.97180  ?  1417 VAL   B CA  1 
ATOM   25266 C  C   . VAL   B 1 1419 ? 32.35100   22.43100  3.43100   1.000 49.70760  ?  1417 VAL   B C   1 
ATOM   25267 O  O   . VAL   B 1 1419 ? 31.68400   22.08800  2.44700   1.000 64.85163  ?  1417 VAL   B O   1 
ATOM   25268 C  CB  . VAL   B 1 1419 ? 31.03900   23.53500  5.29500   1.000 45.42508  ?  1417 VAL   B CB  1 
ATOM   25269 C  CG1 . VAL   B 1 1419 ? 29.83600   23.78300  4.40400   1.000 44.62114  ?  1417 VAL   B CG1 1 
ATOM   25270 C  CG2 . VAL   B 1 1419 ? 30.62000   23.40400  6.75100   1.000 38.54997  ?  1417 VAL   B CG2 1 
ATOM   25271 N  N   . ALA   B 1 1420 ? 33.57900   22.94400  3.30500   1.000 46.84708  ?  1418 ALA   B N   1 
ATOM   25272 C  CA  . ALA   B 1 1420 ? 34.18700   23.07300  1.98400   1.000 64.59402  ?  1418 ALA   B CA  1 
ATOM   25273 C  C   . ALA   B 1 1420 ? 34.42000   21.71300  1.33900   1.000 61.96597  ?  1418 ALA   B C   1 
ATOM   25274 O  O   . ALA   B 1 1420 ? 34.48800   21.61300  0.10900   1.000 53.19013  ?  1418 ALA   B O   1 
ATOM   25275 C  CB  . ALA   B 1 1420 ? 35.50200   23.84700  2.07800   1.000 49.13275  ?  1418 ALA   B CB  1 
ATOM   25276 N  N   . GLU   B 1 1421 ? 34.54500   20.66200  2.14800   1.000 53.82825  ?  1419 GLU   B N   1 
ATOM   25277 C  CA  . GLU   B 1 1421 ? 34.72500   19.31100  1.63300   1.000 58.37009  ?  1419 GLU   B CA  1 
ATOM   25278 C  C   . GLU   B 1 1421 ? 33.41400   18.54600  1.54000   1.000 55.40199  ?  1419 GLU   B C   1 
ATOM   25279 O  O   . GLU   B 1 1421 ? 33.24300   17.72800  0.62700   1.000 62.75155  ?  1419 GLU   B O   1 
ATOM   25280 C  CB  . GLU   B 1 1421 ? 35.70700   18.53600  2.52100   1.000 58.43937  ?  1419 GLU   B CB  1 
ATOM   25281 C  CG  . GLU   B 1 1421 ? 36.85200   19.38100  3.07200   1.000 53.34067  ?  1419 GLU   B CG  1 
ATOM   25282 C  CD  . GLU   B 1 1421 ? 37.56500   18.73300  4.25400   1.000 49.93868  ?  1419 GLU   B CD  1 
ATOM   25283 O  OE1 . GLU   B 1 1421 ? 36.97900   17.84000  4.90200   1.000 47.36658  ?  1419 GLU   B OE1 1 
ATOM   25284 O  OE2 . GLU   B 1 1421 ? 38.71400   19.12900  4.54500   1.000 61.68884  -1 1419 GLU   B OE2 1 
ATOM   25285 N  N   . ILE   B 1 1422 ? 32.48400   18.80300  2.46200   1.000 53.52979  ?  1420 ILE   B N   1 
ATOM   25286 C  CA  . ILE   B 1 1422 ? 31.20400   18.10200  2.46700   1.000 41.80012  ?  1420 ILE   B CA  1 
ATOM   25287 C  C   . ILE   B 1 1422 ? 30.41800   18.39100  1.19500   1.000 55.80814  ?  1420 ILE   B C   1 
ATOM   25288 O  O   . ILE   B 1 1422 ? 29.70600   17.51700  0.68200   1.000 63.13975  ?  1420 ILE   B O   1 
ATOM   25289 C  CB  . ILE   B 1 1422 ? 30.41500   18.47800  3.73800   1.000 43.48175  ?  1420 ILE   B CB  1 
ATOM   25290 C  CG1 . ILE   B 1 1422 ? 31.00500   17.76300  4.95700   1.000 30.03279  ?  1420 ILE   B CG1 1 
ATOM   25291 C  CG2 . ILE   B 1 1422 ? 28.93100   18.16100  3.59000   1.000 45.28543  ?  1420 ILE   B CG2 1 
ATOM   25292 C  CD1 . ILE   B 1 1422 ? 30.55200   18.33900  6.28200   1.000 36.70347  ?  1420 ILE   B CD1 1 
ATOM   25293 N  N   . PHE   B 1 1423 ? 30.55200   19.59900  0.64400   1.000 57.17524  ?  1421 PHE   B N   1 
ATOM   25294 C  CA  . PHE   B 1 1423 ? 29.81500   19.99000  -0.54800  1.000 52.57849  ?  1421 PHE   B CA  1 
ATOM   25295 C  C   . PHE   B 1 1423 ? 30.69100   20.34000  -1.74100  1.000 63.11464  ?  1421 PHE   B C   1 
ATOM   25296 O  O   . PHE   B 1 1423 ? 30.15800   20.48500  -2.84600  1.000 59.34900  ?  1421 PHE   B O   1 
ATOM   25297 C  CB  . PHE   B 1 1423 ? 28.90500   21.19200  -0.24600  1.000 52.30282  ?  1421 PHE   B CB  1 
ATOM   25298 C  CG  . PHE   B 1 1423 ? 27.94500   20.95800  0.88100   1.000 52.96404  ?  1421 PHE   B CG  1 
ATOM   25299 C  CD1 . PHE   B 1 1423 ? 26.96000   19.99200  0.77900   1.000 58.09158  ?  1421 PHE   B CD1 1 
ATOM   25300 C  CD2 . PHE   B 1 1423 ? 28.02700   21.70600  2.04200   1.000 52.92490  ?  1421 PHE   B CD2 1 
ATOM   25301 C  CE1 . PHE   B 1 1423 ? 26.07400   19.77500  1.81700   1.000 63.03456  ?  1421 PHE   B CE1 1 
ATOM   25302 C  CE2 . PHE   B 1 1423 ? 27.14500   21.49500  3.08300   1.000 58.82566  ?  1421 PHE   B CE2 1 
ATOM   25303 C  CZ  . PHE   B 1 1423 ? 26.16700   20.52900  2.97000   1.000 65.92917  ?  1421 PHE   B CZ  1 
ATOM   25304 N  N   . GLY   B 1 1424 ? 32.00800   20.47200  -1.56000  1.000 69.08875  ?  1422 GLY   B N   1 
ATOM   25305 C  CA  . GLY   B 1 1424 ? 32.87800   20.93600  -2.63100  1.000 75.52214  ?  1422 GLY   B CA  1 
ATOM   25306 C  C   . GLY   B 1 1424 ? 32.94200   20.02400  -3.84100  1.000 74.46550  ?  1422 GLY   B C   1 
ATOM   25307 O  O   . GLY   B 1 1424 ? 33.32500   20.47500  -4.92600  1.000 70.33204  ?  1422 GLY   B O   1 
ATOM   25308 N  N   . TRP   B 1 1425 ? 32.58200   18.75200  -3.68300  1.000 85.64925  ?  1423 TRP   B N   1 
ATOM   25309 C  CA  . TRP   B 1 1425 ? 32.60600   17.81300  -4.79800  1.000 82.05582  ?  1423 TRP   B CA  1 
ATOM   25310 C  C   . TRP   B 1 1425 ? 31.31700   17.82600  -5.61100  1.000 79.99026  ?  1423 TRP   B C   1 
ATOM   25311 O  O   . TRP   B 1 1425 ? 31.34000   17.45900  -6.79300  1.000 72.41127  ?  1423 TRP   B O   1 
ATOM   25312 C  CB  . TRP   B 1 1425 ? 32.87100   16.39400  -4.28300  1.000 73.30355  ?  1423 TRP   B CB  1 
ATOM   25313 C  CG  . TRP   B 1 1425 ? 31.78500   15.88300  -3.38000  1.000 81.85238  ?  1423 TRP   B CG  1 
ATOM   25314 C  CD1 . TRP   B 1 1425 ? 31.74200   15.97100  -2.01900  1.000 77.59520  ?  1423 TRP   B CD1 1 
ATOM   25315 C  CD2 . TRP   B 1 1425 ? 30.58200   15.21000  -3.77700  1.000 84.46151  ?  1423 TRP   B CD2 1 
ATOM   25316 N  NE1 . TRP   B 1 1425 ? 30.58800   15.39500  -1.54400  1.000 81.64898  ?  1423 TRP   B NE1 1 
ATOM   25317 C  CE2 . TRP   B 1 1425 ? 29.85900   14.92100  -2.60200  1.000 81.56487  ?  1423 TRP   B CE2 1 
ATOM   25318 C  CE3 . TRP   B 1 1425 ? 30.04700   14.82400  -5.01000  1.000 67.64978  ?  1423 TRP   B CE3 1 
ATOM   25319 C  CZ2 . TRP   B 1 1425 ? 28.63000   14.26500  -2.62500  1.000 79.06400  ?  1423 TRP   B CZ2 1 
ATOM   25320 C  CZ3 . TRP   B 1 1425 ? 28.82700   14.17500  -5.03000  1.000 74.79369  ?  1423 TRP   B CZ3 1 
ATOM   25321 C  CH2 . TRP   B 1 1425 ? 28.13200   13.90100  -3.84500  1.000 89.74032  ?  1423 TRP   B CH2 1 
ATOM   25322 N  N   . VAL   B 1 1426 ? 30.19700   18.24100  -5.00400  1.000 76.05348  ?  1424 VAL   B N   1 
ATOM   25323 C  CA  . VAL   B 1 1426 ? 28.90900   18.20200  -5.70500  1.000 64.30648  ?  1424 VAL   B CA  1 
ATOM   25324 C  C   . VAL   B 1 1426 ? 28.91800   19.04300  -6.97800  1.000 85.71636  ?  1424 VAL   B C   1 
ATOM   25325 O  O   . VAL   B 1 1426 ? 28.48200   18.53800  -8.02600  1.000 90.48185  ?  1424 VAL   B O   1 
ATOM   25326 C  CB  . VAL   B 1 1426 ? 27.77000   18.58600  -4.74200  1.000 59.17826  ?  1424 VAL   B CB  1 
ATOM   25327 C  CG1 . VAL   B 1 1426 ? 26.42600   18.51400  -5.44900  1.000 68.48793  ?  1424 VAL   B CG1 1 
ATOM   25328 C  CG2 . VAL   B 1 1426 ? 27.77700   17.68300  -3.51400  1.000 57.12818  ?  1424 VAL   B CG2 1 
ATOM   25329 N  N   . PRO   B 1 1427 ? 29.38000   20.29800  -6.97500  1.000 93.45516  ?  1425 PRO   B N   1 
ATOM   25330 C  CA  . PRO   B 1 1427 ? 29.51600   21.01900  -8.24800  1.000 81.79529  ?  1425 PRO   B CA  1 
ATOM   25331 C  C   . PRO   B 1 1427 ? 30.65800   20.44200  -9.07200  1.000 80.92849  ?  1425 PRO   B C   1 
ATOM   25332 O  O   . PRO   B 1 1427 ? 31.79200   20.33200  -8.59800  1.000 82.71206  ?  1425 PRO   B O   1 
ATOM   25333 C  CB  . PRO   B 1 1427 ? 29.80000   22.46100  -7.81400  1.000 70.65470  ?  1425 PRO   B CB  1 
ATOM   25334 C  CG  . PRO   B 1 1427 ? 30.41400   22.32800  -6.47200  1.000 74.24124  ?  1425 PRO   B CG  1 
ATOM   25335 C  CD  . PRO   B 1 1427 ? 29.71700   21.16700  -5.83200  1.000 77.74445  ?  1425 PRO   B CD  1 
ATOM   25336 N  N   . GLY   B 1 1428 ? 30.34900   20.06400  -10.30900 1.000 71.93221  ?  1426 GLY   B N   1 
ATOM   25337 C  CA  . GLY   B 1 1428 ? 31.32100   19.44800  -11.18700 1.000 83.28013  ?  1426 GLY   B CA  1 
ATOM   25338 C  C   . GLY   B 1 1428 ? 31.19500   17.94800  -11.33900 1.000 91.49382  ?  1426 GLY   B C   1 
ATOM   25339 O  O   . GLY   B 1 1428 ? 31.93400   17.36500  -12.14100 1.000 97.09219  ?  1426 GLY   B O   1 
ATOM   25340 N  N   . ARG   B 1 1429 ? 30.28600   17.30800  -10.60100 1.000 92.78058  ?  1427 ARG   B N   1 
ATOM   25341 C  CA  . ARG   B 1 1429 ? 30.06800   15.86000  -10.66400 1.000 93.12947  ?  1427 ARG   B CA  1 
ATOM   25342 C  C   . ARG   B 1 1429 ? 31.36000   15.09400  -10.37500 1.000 90.23650  ?  1427 ARG   B C   1 
ATOM   25343 O  O   . ARG   B 1 1429 ? 31.84100   14.29700  -11.18200 1.000 90.27257  ?  1427 ARG   B O   1 
ATOM   25344 C  CB  . ARG   B 1 1429 ? 29.47800   15.44700  -12.01700 1.000 89.22873  ?  1427 ARG   B CB  1 
ATOM   25345 N  N   . GLY   B 1 1430 ? 31.91500   15.35200  -9.20200  1.000 80.94500  ?  1428 GLY   B N   1 
ATOM   25346 C  CA  . GLY   B 1 1430 ? 33.12400   14.69500  -8.74200  1.000 79.36266  ?  1428 GLY   B CA  1 
ATOM   25347 C  C   . GLY   B 1 1430 ? 32.82300   13.55500  -7.79500  1.000 79.73949  ?  1428 GLY   B C   1 
ATOM   25348 O  O   . GLY   B 1 1430 ? 31.86200   12.80000  -7.98200  1.000 80.14251  ?  1428 GLY   B O   1 
ATOM   25349 N  N   . LYS   B 1 1431 ? 33.65300   13.42800  -6.76400  1.000 74.47377  ?  1429 LYS   B N   1 
ATOM   25350 C  CA  . LYS   B 1 1431 ? 33.46700   12.39900  -5.75200  1.000 67.57585  ?  1429 LYS   B CA  1 
ATOM   25351 C  C   . LYS   B 1 1431 ? 34.20000   12.82700  -4.49200  1.000 76.16033  ?  1429 LYS   B C   1 
ATOM   25352 O  O   . LYS   B 1 1431 ? 35.07000   13.70200  -4.52400  1.000 80.94014  ?  1429 LYS   B O   1 
ATOM   25353 C  CB  . LYS   B 1 1431 ? 33.96900   11.03300  -6.23500  1.000 71.91680  ?  1429 LYS   B CB  1 
ATOM   25354 N  N   . LEU   B 1 1432 ? 33.83500   12.19900  -3.37800  1.000 68.46981  ?  1430 LEU   B N   1 
ATOM   25355 C  CA  . LEU   B 1 1432 ? 34.48300   12.45000  -2.10100  1.000 74.11980  ?  1430 LEU   B CA  1 
ATOM   25356 C  C   . LEU   B 1 1432 ? 34.84500   11.12600  -1.44600  1.000 69.79014  ?  1430 LEU   B C   1 
ATOM   25357 O  O   . LEU   B 1 1432 ? 34.03500   10.19400  -1.42100  1.000 69.69190  ?  1430 LEU   B O   1 
ATOM   25358 C  CB  . LEU   B 1 1432 ? 33.58800   13.25300  -1.16100  1.000 68.49886  ?  1430 LEU   B CB  1 
ATOM   25359 C  CG  . LEU   B 1 1432 ? 34.13300   13.27000  0.26600   1.000 72.51195  ?  1430 LEU   B CG  1 
ATOM   25360 C  CD1 . LEU   B 1 1432 ? 35.16600   14.37400  0.44800   1.000 71.34143  ?  1430 LEU   B CD1 1 
ATOM   25361 C  CD2 . LEU   B 1 1432 ? 33.02100   13.39500  1.26300   1.000 43.60619  ?  1430 LEU   B CD2 1 
ATOM   25362 N  N   . VAL   B 1 1433 ? 36.06000   11.05100  -0.91600  1.000 60.86645  ?  1431 VAL   B N   1 
ATOM   25363 C  CA  . VAL   B 1 1433 ? 36.53100   9.88800   -0.17600  1.000 67.77022  ?  1431 VAL   B CA  1 
ATOM   25364 C  C   . VAL   B 1 1433 ? 36.38300   10.20400  1.30700   1.000 66.76121  ?  1431 VAL   B C   1 
ATOM   25365 O  O   . VAL   B 1 1433 ? 37.05800   11.09600  1.83100   1.000 55.65408  ?  1431 VAL   B O   1 
ATOM   25366 C  CB  . VAL   B 1 1433 ? 37.98200   9.54400   -0.53600  1.000 71.36140  ?  1431 VAL   B CB  1 
ATOM   25367 C  CG1 . VAL   B 1 1433 ? 38.47400   8.35300   0.27800   1.000 65.40679  ?  1431 VAL   B CG1 1 
ATOM   25368 C  CG2 . VAL   B 1 1433 ? 38.09800   9.27700   -2.02300  1.000 56.21514  ?  1431 VAL   B CG2 1 
ATOM   25369 N  N   . ILE   B 1 1434 ? 35.48900   9.49000   1.98500   1.000 67.51989  ?  1432 ILE   B N   1 
ATOM   25370 C  CA  . ILE   B 1 1434 ? 35.32700   9.65300   3.42600   1.000 59.54029  ?  1432 ILE   B CA  1 
ATOM   25371 C  C   . ILE   B 1 1434 ? 36.47100   8.92700   4.12100   1.000 59.07818  ?  1432 ILE   B C   1 
ATOM   25372 O  O   . ILE   B 1 1434 ? 36.62400   7.70800   3.98500   1.000 70.01889  ?  1432 ILE   B O   1 
ATOM   25373 C  CB  . ILE   B 1 1434 ? 33.96400   9.13000   3.90200   1.000 50.28548  ?  1432 ILE   B CB  1 
ATOM   25374 C  CG1 . ILE   B 1 1434 ? 32.83300   10.02200  3.38200   1.000 55.01624  ?  1432 ILE   B CG1 1 
ATOM   25375 C  CG2 . ILE   B 1 1434 ? 33.92700   9.05600   5.42700   1.000 45.76484  ?  1432 ILE   B CG2 1 
ATOM   25376 C  CD1 . ILE   B 1 1434 ? 31.81900   9.29700   2.51900   1.000 62.13187  ?  1432 ILE   B CD1 1 
ATOM   25377 N  N   . LEU   B 1 1435 ? 37.28900   9.67700   4.84900   1.000 55.24062  ?  1433 LEU   B N   1 
ATOM   25378 C  CA  . LEU   B 1 1435 ? 38.39200   9.08400   5.58700   1.000 53.80430  ?  1433 LEU   B CA  1 
ATOM   25379 C  C   . LEU   B 1 1435 ? 37.87700   8.35300   6.82200   1.000 55.02213  ?  1433 LEU   B C   1 
ATOM   25380 O  O   . LEU   B 1 1435 ? 36.81100   8.66400   7.36000   1.000 56.76557  ?  1433 LEU   B O   1 
ATOM   25381 C  CB  . LEU   B 1 1435 ? 39.39700   10.16000  5.99500   1.000 55.09217  ?  1433 LEU   B CB  1 
ATOM   25382 C  CG  . LEU   B 1 1435 ? 40.86800   9.77000   6.13100   1.000 61.90944  ?  1433 LEU   B CG  1 
ATOM   25383 C  CD1 . LEU   B 1 1435 ? 41.53900   9.69800   4.77200   1.000 54.16177  ?  1433 LEU   B CD1 1 
ATOM   25384 C  CD2 . LEU   B 1 1435 ? 41.58900   10.76100  7.03600   1.000 65.22174  ?  1433 LEU   B CD2 1 
ATOM   25385 N  N   . GLU   B 1 1436 ? 38.64600   7.36900   7.26400   1.000 54.83534  ?  1434 GLU   B N   1 
ATOM   25386 C  CA  . GLU   B 1 1436 ? 38.29000   6.63800   8.46800   1.000 56.48568  ?  1434 GLU   B CA  1 
ATOM   25387 C  C   . GLU   B 1 1436 ? 38.34800   7.57300   9.67500   1.000 53.85978  ?  1434 GLU   B C   1 
ATOM   25388 O  O   . GLU   B 1 1436 ? 39.19600   8.46800   9.72200   1.000 60.42448  ?  1434 GLU   B O   1 
ATOM   25389 C  CB  . GLU   B 1 1436 ? 39.23600   5.45300   8.66400   1.000 71.83734  ?  1434 GLU   B CB  1 
ATOM   25390 C  CG  . GLU   B 1 1436 ? 38.98100   4.62900   9.91300   1.000 88.87764  ?  1434 GLU   B CG  1 
ATOM   25391 C  CD  . GLU   B 1 1436 ? 38.21000   3.35700   9.62200   1.000 94.07690  ?  1434 GLU   B CD  1 
ATOM   25392 O  OE1 . GLU   B 1 1436 ? 38.28900   2.85900   8.47900   1.000 88.00475  ?  1434 GLU   B OE1 1 
ATOM   25393 O  OE2 . GLU   B 1 1436 ? 37.52200   2.85600   10.53700  1.000 97.58046  -1 1434 GLU   B OE2 1 
ATOM   25394 N  N   . PRO   B 1 1437 ? 37.44000   7.42200   10.63900  1.000 61.99153  ?  1435 PRO   B N   1 
ATOM   25395 C  CA  . PRO   B 1 1437 ? 37.51900   8.23200   11.86100  1.000 65.85289  ?  1435 PRO   B CA  1 
ATOM   25396 C  C   . PRO   B 1 1437 ? 38.88200   8.11700   12.52900  1.000 67.60513  ?  1435 PRO   B C   1 
ATOM   25397 O  O   . PRO   B 1 1437 ? 39.43000   7.02200   12.68000  1.000 77.38153  ?  1435 PRO   B O   1 
ATOM   25398 C  CB  . PRO   B 1 1437 ? 36.40800   7.64700   12.73800  1.000 48.41880  ?  1435 PRO   B CB  1 
ATOM   25399 C  CG  . PRO   B 1 1437 ? 35.40700   7.13900   11.76300  1.000 47.83615  ?  1435 PRO   B CG  1 
ATOM   25400 C  CD  . PRO   B 1 1437 ? 36.18800   6.64600   10.57200  1.000 55.49521  ?  1435 PRO   B CD  1 
ATOM   25401 N  N   . GLU   B 1 1438 ? 39.43200   9.26900   12.91800  1.000 62.79221  ?  1436 GLU   B N   1 
ATOM   25402 C  CA  . GLU   B 1 1438 ? 40.73500   9.45200   13.55500  1.000 63.89721  ?  1436 GLU   B CA  1 
ATOM   25403 C  C   . GLU   B 1 1438 ? 41.90600   9.19500   12.61100  1.000 68.88238  ?  1436 GLU   B C   1 
ATOM   25404 O  O   . GLU   B 1 1438 ? 43.06200   9.33800   13.03300  1.000 63.48518  ?  1436 GLU   B O   1 
ATOM   25405 C  CB  . GLU   B 1 1438 ? 40.90300   8.58400   14.81200  1.000 62.53925  ?  1436 GLU   B CB  1 
ATOM   25406 C  CG  . GLU   B 1 1438 ? 39.80500   8.78200   15.84500  1.000 81.35670  ?  1436 GLU   B CG  1 
ATOM   25407 C  CD  . GLU   B 1 1438 ? 40.30600   8.61900   17.26500  1.000 99.52450  ?  1436 GLU   B CD  1 
ATOM   25408 O  OE1 . GLU   B 1 1438 ? 41.27500   7.85800   17.46900  1.000 103.95070 ?  1436 GLU   B OE1 1 
ATOM   25409 O  OE2 . GLU   B 1 1438 ? 39.73200   9.25200   18.17700  1.000 106.01333 ?  1436 GLU   B OE2 1 
ATOM   25410 N  N   . ALA   B 1 1439 ? 41.65800   8.83900   11.34900  1.000 56.86719  ?  1437 ALA   B N   1 
ATOM   25411 C  CA  . ALA   B 1 1439 ? 42.75000   8.66000   10.39900  1.000 58.66103  ?  1437 ALA   B CA  1 
ATOM   25412 C  C   . ALA   B 1 1439 ? 43.37700   9.97800   9.97000   1.000 82.29150  ?  1437 ALA   B C   1 
ATOM   25413 O  O   . ALA   B 1 1439 ? 44.43300   9.96100   9.32900   1.000 87.14350  ?  1437 ALA   B O   1 
ATOM   25414 C  CB  . ALA   B 1 1439 ? 42.26600   7.89800   9.16400   1.000 60.94489  ?  1437 ALA   B CB  1 
ATOM   25415 N  N   . GLU   B 1 1440 ? 42.75600   11.11200  10.30100  1.000 89.25872  ?  1438 GLU   B N   1 
ATOM   25416 C  CA  . GLU   B 1 1440 ? 43.35400   12.41200  10.02400  1.000 85.40218  ?  1438 GLU   B CA  1 
ATOM   25417 C  C   . GLU   B 1 1440 ? 44.62800   12.65000  10.82200  1.000 80.34907  ?  1438 GLU   B C   1 
ATOM   25418 O  O   . GLU   B 1 1440 ? 45.34400   13.61900  10.54300  1.000 75.82421  ?  1438 GLU   B O   1 
ATOM   25419 C  CB  . GLU   B 1 1440 ? 42.34100   13.52400  10.32100  1.000 69.36021  ?  1438 GLU   B CB  1 
ATOM   25420 C  CG  . GLU   B 1 1440 ? 42.40400   14.07300  11.74400  1.000 77.56426  ?  1438 GLU   B CG  1 
ATOM   25421 C  CD  . GLU   B 1 1440 ? 41.28200   13.55900  12.62700  1.000 83.73659  ?  1438 GLU   B CD  1 
ATOM   25422 O  OE1 . GLU   B 1 1440 ? 40.53500   12.66500  12.17900  1.000 89.62937  ?  1438 GLU   B OE1 1 
ATOM   25423 O  OE2 . GLU   B 1 1440 ? 41.14800   14.04900  13.76900  1.000 74.72216  -1 1438 GLU   B OE2 1 
ATOM   25424 N  N   . LYS   B 1 1441 ? 44.92500   11.79600  11.79900  1.000 79.58488  ?  1439 LYS   B N   1 
ATOM   25425 C  CA  . LYS   B 1 1441 ? 46.04600   11.99000  12.70000  1.000 82.86438  ?  1439 LYS   B CA  1 
ATOM   25426 C  C   . LYS   B 1 1441 ? 47.23700   11.10000  12.37600  1.000 92.55869  ?  1439 LYS   B C   1 
ATOM   25427 O  O   . LYS   B 1 1441 ? 48.23500   11.15100  13.09600  1.000 102.22701 ?  1439 LYS   B O   1 
ATOM   25428 C  CB  . LYS   B 1 1441 ? 45.59900   11.76200  14.14800  1.000 65.05515  ?  1439 LYS   B CB  1 
ATOM   25429 C  CG  . LYS   B 1 1441 ? 44.52100   12.72600  14.59100  1.000 74.20156  ?  1439 LYS   B CG  1 
ATOM   25430 C  CD  . LYS   B 1 1441 ? 43.44600   12.03100  15.40700  1.000 88.21474  ?  1439 LYS   B CD  1 
ATOM   25431 C  CE  . LYS   B 1 1441 ? 43.85100   11.90800  16.86600  1.000 68.19923  ?  1439 LYS   B CE  1 
ATOM   25432 N  NZ  . LYS   B 1 1441 ? 42.66500   11.82000  17.76500  1.000 89.10485  ?  1439 LYS   B NZ  1 
ATOM   25433 N  N   . ASN   B 1 1442 ? 47.17000   10.28200  11.32300  1.000 80.88903  ?  1440 ASN   B N   1 
ATOM   25434 C  CA  . ASN   B 1 1442 ? 48.43600   9.76300   10.82700  1.000 82.79472  ?  1440 ASN   B CA  1 
ATOM   25435 C  C   . ASN   B 1 1442 ? 48.60000   10.12500  9.35300   1.000 89.85883  ?  1440 ASN   B C   1 
ATOM   25436 O  O   . ASN   B 1 1442 ? 47.62200   10.15000  8.60800   1.000 86.17879  ?  1440 ASN   B O   1 
ATOM   25437 C  CB  . ASN   B 1 1442 ? 48.56500   8.22700   11.09800  1.000 86.04125  ?  1440 ASN   B CB  1 
ATOM   25438 C  CG  . ASN   B 1 1442 ? 48.01000   7.30300   9.97000   1.000 92.11955  ?  1440 ASN   B CG  1 
ATOM   25439 O  OD1 . ASN   B 1 1442 ? 47.58700   7.69300   8.89100   1.000 80.78528  ?  1440 ASN   B OD1 1 
ATOM   25440 N  ND2 . ASN   B 1 1442 ? 48.04700   6.00700   10.27700  1.000 95.75672  ?  1440 ASN   B ND2 1 
ATOM   25441 N  N   . PRO   B 1 1443 ? 49.79500   10.48200  8.92900   1.000 83.37757  ?  1441 PRO   B N   1 
ATOM   25442 C  CA  . PRO   B 1 1443 ? 49.96800   10.87700  7.51400   1.000 76.03233  ?  1441 PRO   B CA  1 
ATOM   25443 C  C   . PRO   B 1 1443 ? 50.01100   9.70000   6.57900   1.000 74.67330  ?  1441 PRO   B C   1 
ATOM   25444 O  O   . PRO   B 1 1443 ? 49.79000   9.89100   5.38300   1.000 70.54691  ?  1441 PRO   B O   1 
ATOM   25445 C  CB  . PRO   B 1 1443 ? 51.31100   11.66300  7.50800   1.000 74.66278  ?  1441 PRO   B CB  1 
ATOM   25446 C  CG  . PRO   B 1 1443 ? 51.87000   11.55500  8.88000   1.000 80.65319  ?  1441 PRO   B CG  1 
ATOM   25447 C  CD  . PRO   B 1 1443 ? 51.04100   10.64100  9.72600   1.000 78.17018  ?  1441 PRO   B CD  1 
ATOM   25448 N  N   . LYS   B 1 1444 ? 50.24200   8.49100   7.09700   1.000 69.35620  ?  1442 LYS   B N   1 
ATOM   25449 C  CA  . LYS   B 1 1444 ? 50.19000   7.27800   6.28900   1.000 79.44246  ?  1442 LYS   B CA  1 
ATOM   25450 C  C   . LYS   B 1 1444 ? 48.83000   7.16000   5.61200   1.000 88.68445  ?  1442 LYS   B C   1 
ATOM   25451 O  O   . LYS   B 1 1444 ? 48.72900   7.33800   4.39400   1.000 80.99954  ?  1442 LYS   B O   1 
ATOM   25452 C  CB  . LYS   B 1 1444 ? 50.47800   6.04900   7.16200   1.000 63.94486  ?  1442 LYS   B CB  1 
ATOM   25453 N  N   . ALA   B 1 1445 ? 47.77900   6.92100   6.40700   1.000 81.78236  ?  1443 ALA   B N   1 
ATOM   25454 C  CA  . ALA   B 1 1445 ? 46.44400   6.69900   5.85200   1.000 83.01353  ?  1443 ALA   B CA  1 
ATOM   25455 C  C   . ALA   B 1 1445 ? 45.99600   7.83700   4.94400   1.000 86.53674  ?  1443 ALA   B C   1 
ATOM   25456 O  O   . ALA   B 1 1445 ? 45.28700   7.59900   3.96000   1.000 74.35872  ?  1443 ALA   B O   1 
ATOM   25457 C  CB  . ALA   B 1 1445 ? 45.42900   6.50100   6.98000   1.000 72.70020  ?  1443 ALA   B CB  1 
ATOM   25458 N  N   . ILE   B 1 1446 ? 46.38200   9.07600   5.25800   1.000 78.86644  ?  1444 ILE   B N   1 
ATOM   25459 C  CA  . ILE   B 1 1446 ? 46.09300   10.18500  4.35300   1.000 74.12559  ?  1444 ILE   B CA  1 
ATOM   25460 C  C   . ILE   B 1 1446 ? 46.79100   9.96500   3.02000   1.000 78.03572  ?  1444 ILE   B C   1 
ATOM   25461 O  O   . ILE   B 1 1446 ? 46.17200   10.04700  1.95200   1.000 77.26964  ?  1444 ILE   B O   1 
ATOM   25462 C  CB  . ILE   B 1 1446 ? 46.50300   11.52700  4.98600   1.000 82.08235  ?  1444 ILE   B CB  1 
ATOM   25463 C  CG1 . ILE   B 1 1446 ? 45.93200   11.65400  6.39700   1.000 77.24521  ?  1444 ILE   B CG1 1 
ATOM   25464 C  CG2 . ILE   B 1 1446 ? 46.03900   12.69000  4.11900   1.000 65.94446  ?  1444 ILE   B CG2 1 
ATOM   25465 C  CD1 . ILE   B 1 1446 ? 46.47700   12.83500  7.16600   1.000 55.37782  ?  1444 ILE   B CD1 1 
ATOM   25466 N  N   . TRP   B 1 1447 ? 48.09400   9.67300   3.06400   1.000 83.81360  ?  1445 TRP   B N   1 
ATOM   25467 C  CA  . TRP   B 1 1447 ? 48.84100   9.42600   1.83500   1.000 80.29322  ?  1445 TRP   B CA  1 
ATOM   25468 C  C   . TRP   B 1 1447 ? 48.30400   8.20500   1.10000   1.000 81.94315  ?  1445 TRP   B C   1 
ATOM   25469 O  O   . TRP   B 1 1447 ? 48.13800   8.23600   -0.12500  1.000 81.92190  ?  1445 TRP   B O   1 
ATOM   25470 C  CB  . TRP   B 1 1447 ? 50.32900   9.25500   2.15000   1.000 81.48336  ?  1445 TRP   B CB  1 
ATOM   25471 C  CG  . TRP   B 1 1447 ? 51.22500   9.23400   0.93200   1.000 85.24384  ?  1445 TRP   B CG  1 
ATOM   25472 C  CD1 . TRP   B 1 1447 ? 52.14800   8.27900   0.61300   1.000 71.72770  ?  1445 TRP   B CD1 1 
ATOM   25473 C  CD2 . TRP   B 1 1447 ? 51.28800   10.21500  -0.11500  1.000 79.29388  ?  1445 TRP   B CD2 1 
ATOM   25474 N  NE1 . TRP   B 1 1447 ? 52.77400   8.60000   -0.56700  1.000 86.43310  ?  1445 TRP   B NE1 1 
ATOM   25475 C  CE2 . TRP   B 1 1447 ? 52.26500   9.78300   -1.03400  1.000 86.21340  ?  1445 TRP   B CE2 1 
ATOM   25476 C  CE3 . TRP   B 1 1447 ? 50.61200   11.41400  -0.36600  1.000 70.96782  ?  1445 TRP   B CE3 1 
ATOM   25477 C  CZ2 . TRP   B 1 1447 ? 52.58200   10.50600  -2.18300  1.000 99.86701  ?  1445 TRP   B CZ2 1 
ATOM   25478 C  CZ3 . TRP   B 1 1447 ? 50.92800   12.12900  -1.50800  1.000 75.21119  ?  1445 TRP   B CZ3 1 
ATOM   25479 C  CH2 . TRP   B 1 1447 ? 51.90400   11.67300  -2.40100  1.000 88.89799  ?  1445 TRP   B CH2 1 
ATOM   25480 N  N   . GLN   B 1 1448 ? 48.01700   7.12300   1.83400   1.000 77.58803  ?  1446 GLN   B N   1 
ATOM   25481 C  CA  . GLN   B 1 1448 ? 47.45500   5.92600   1.20800   1.000 86.31662  ?  1446 GLN   B CA  1 
ATOM   25482 C  C   . GLN   B 1 1448 ? 46.18500   6.24400   0.43200   1.000 80.55399  ?  1446 GLN   B C   1 
ATOM   25483 O  O   . GLN   B 1 1448 ? 45.97900   5.71900   -0.66700  1.000 85.24570  ?  1446 GLN   B O   1 
ATOM   25484 C  CB  . GLN   B 1 1448 ? 47.16900   4.84900   2.25100   1.000 88.83766  ?  1446 GLN   B CB  1 
ATOM   25485 C  CG  . GLN   B 1 1448 ? 48.27600   4.63700   3.23300   1.000 95.12667  ?  1446 GLN   B CG  1 
ATOM   25486 C  CD  . GLN   B 1 1448 ? 48.16200   3.32400   3.96400   1.000 97.81083  ?  1446 GLN   B CD  1 
ATOM   25487 O  OE1 . GLN   B 1 1448 ? 47.06300   2.85800   4.26900   1.000 91.58536  ?  1446 GLN   B OE1 1 
ATOM   25488 N  NE2 . GLN   B 1 1448 ? 49.30400   2.72100   4.26200   1.000 83.09554  ?  1446 GLN   B NE2 1 
ATOM   25489 N  N   . ALA   B 1 1449 ? 45.31500   7.09200   0.98300   1.000 86.13384  ?  1447 ALA   B N   1 
ATOM   25490 C  CA  . ALA   B 1 1449 ? 44.20000   7.58600   0.19200   1.000 81.13151  ?  1447 ALA   B CA  1 
ATOM   25491 C  C   . ALA   B 1 1449 ? 44.71100   8.28700   -1.06000  1.000 85.49842  ?  1447 ALA   B C   1 
ATOM   25492 O  O   . ALA   B 1 1449 ? 44.37000   7.90000   -2.18700  1.000 92.79763  ?  1447 ALA   B O   1 
ATOM   25493 C  CB  . ALA   B 1 1449 ? 43.33900   8.52500   1.03800   1.000 62.39166  ?  1447 ALA   B CB  1 
ATOM   25494 N  N   . VAL   B 1 1450 ? 45.55000   9.31000   -0.88800  1.000 79.29714  ?  1448 VAL   B N   1 
ATOM   25495 C  CA  . VAL   B 1 1450 ? 45.84600   10.20100  -2.00900  1.000 91.57480  ?  1448 VAL   B CA  1 
ATOM   25496 C  C   . VAL   B 1 1450 ? 46.35000   9.42400   -3.22200  1.000 105.52459 ?  1448 VAL   B C   1 
ATOM   25497 O  O   . VAL   B 1 1450 ? 46.00700   9.74300   -4.36700  1.000 113.03452 ?  1448 VAL   B O   1 
ATOM   25498 C  CB  . VAL   B 1 1450 ? 46.84100   11.29400  -1.57400  1.000 83.39693  ?  1448 VAL   B CB  1 
ATOM   25499 C  CG1 . VAL   B 1 1450 ? 47.16700   12.22700  -2.71700  1.000 71.59694  ?  1448 VAL   B CG1 1 
ATOM   25500 C  CG2 . VAL   B 1 1450 ? 46.30700   12.08500  -0.41300  1.000 73.47099  ?  1448 VAL   B CG2 1 
ATOM   25501 N  N   . VAL   B 1 1451 ? 47.20300   8.42800   -2.99700  1.000 94.16032  ?  1449 VAL   B N   1 
ATOM   25502 C  CA  . VAL   B 1 1451 ? 47.68800   7.59100   -4.08900  1.000 93.65739  ?  1449 VAL   B CA  1 
ATOM   25503 C  C   . VAL   B 1 1451 ? 46.56100   6.71600   -4.63700  1.000 94.89010  ?  1449 VAL   B C   1 
ATOM   25504 O  O   . VAL   B 1 1451 ? 46.33200   6.65500   -5.85300  1.000 95.67909  ?  1449 VAL   B O   1 
ATOM   25505 C  CB  . VAL   B 1 1451 ? 48.88700   6.75100   -3.61200  1.000 96.15159  ?  1449 VAL   B CB  1 
ATOM   25506 C  CG1 . VAL   B 1 1451 ? 49.70600   6.28100   -4.78400  1.000 89.89312  ?  1449 VAL   B CG1 1 
ATOM   25507 C  CG2 . VAL   B 1 1451 ? 49.74700   7.58900   -2.68600  1.000 93.39163  ?  1449 VAL   B CG2 1 
ATOM   25508 N  N   . GLY   B 1 1452 ? 45.82800   6.04300   -3.75100  1.000 93.23094  ?  1450 GLY   B N   1 
ATOM   25509 C  CA  . GLY   B 1 1452 ? 44.80400   5.09900   -4.16000  1.000 91.59995  ?  1450 GLY   B CA  1 
ATOM   25510 C  C   . GLY   B 1 1452 ? 43.62800   5.70400   -4.89900  1.000 101.66417 ?  1450 GLY   B C   1 
ATOM   25511 O  O   . GLY   B 1 1452 ? 43.47300   5.50000   -6.10700  1.000 113.10777 ?  1450 GLY   B O   1 
ATOM   25512 N  N   . ALA   B 1 1453 ? 42.78900   6.45000   -4.18400  1.000 91.60876  ?  1451 ALA   B N   1 
ATOM   25513 C  CA  . ALA   B 1 1453 ? 41.57600   7.00800   -4.76400  1.000 77.40547  ?  1451 ALA   B CA  1 
ATOM   25514 C  C   . ALA   B 1 1453 ? 41.83400   8.20300   -5.67300  1.000 93.43633  ?  1451 ALA   B C   1 
ATOM   25515 O  O   . ALA   B 1 1453 ? 40.87500   8.74600   -6.23300  1.000 85.22637  ?  1451 ALA   B O   1 
ATOM   25516 C  CB  . ALA   B 1 1453 ? 40.60400   7.40600   -3.65300  1.000 79.83423  ?  1451 ALA   B CB  1 
ATOM   25517 N  N   . GLY   B 1 1454 ? 43.08800   8.62500   -5.83300  1.000 94.57298  ?  1452 GLY   B N   1 
ATOM   25518 C  CA  . GLY   B 1 1454 ? 43.41300   9.72300   -6.72300  1.000 91.02265  ?  1452 GLY   B CA  1 
ATOM   25519 C  C   . GLY   B 1 1454 ? 42.85300   11.05400  -6.25900  1.000 91.31782  ?  1452 GLY   B C   1 
ATOM   25520 O  O   . GLY   B 1 1454 ? 42.23100   11.77000  -7.05300  1.000 86.68122  ?  1452 GLY   B O   1 
ATOM   25521 N  N   . ILE   B 1 1455 ? 43.04400   11.38600  -4.97500  1.000 89.50781  ?  1453 ILE   B N   1 
ATOM   25522 C  CA  . ILE   B 1 1455 ? 42.59700   12.68100  -4.45600  1.000 87.04785  ?  1453 ILE   B CA  1 
ATOM   25523 C  C   . ILE   B 1 1455 ? 43.33000   13.83000  -5.12500  1.000 92.28318  ?  1453 ILE   B C   1 
ATOM   25524 O  O   . ILE   B 1 1455 ? 44.55900   13.82800  -5.29300  1.000 99.22205  ?  1453 ILE   B O   1 
ATOM   25525 C  CB  . ILE   B 1 1455 ? 42.67700   12.74600  -2.91800  1.000 75.77171  ?  1453 ILE   B CB  1 
ATOM   25526 C  CG1 . ILE   B 1 1455 ? 41.60600   11.85700  -2.31400  1.000 79.95999  ?  1453 ILE   B CG1 1 
ATOM   25527 C  CG2 . ILE   B 1 1455 ? 42.27600   14.02300  -2.39100  1.000 92.77920  ?  1453 ILE   B CG2 1 
ATOM   25528 C  CD1 . ILE   B 1 1455 ? 42.10100   10.31300  -2.15400  1.000 92.99192  ?  1453 ILE   B CD1 1 
ATOM   25529 N  N   . THR   B 1 1456 ? 42.55100   14.82400  -5.52100  1.000 88.74932  ?  1454 THR   B N   1 
ATOM   25530 C  CA  . THR   B 1 1456 ? 43.06100   16.00700  -6.17700  1.000 76.72358  ?  1454 THR   B CA  1 
ATOM   25531 C  C   . THR   B 1 1456 ? 42.92100   17.26300  -5.33900  1.000 79.66078  ?  1454 THR   B C   1 
ATOM   25532 O  O   . THR   B 1 1456 ? 43.71600   18.18600  -5.51400  1.000 83.97997  ?  1454 THR   B O   1 
ATOM   25533 C  CB  . THR   B 1 1456 ? 42.35100   16.21500  -7.52100  1.000 84.18409  ?  1454 THR   B CB  1 
ATOM   25534 O  OG1 . THR   B 1 1456 ? 40.97900   16.56500  -7.29800  1.000 84.04736  ?  1454 THR   B OG1 1 
ATOM   25535 C  CG2 . THR   B 1 1456 ? 42.41700   14.94600  -8.36800  1.000 78.80133  ?  1454 THR   B CG2 1 
ATOM   25536 N  N   . HIS   B 1 1457 ? 41.94100   17.32200  -4.43700  1.000 79.44408  ?  1455 HIS   B N   1 
ATOM   25537 C  CA  . HIS   B 1 1457 ? 41.74700   18.44900  -3.53200  1.000 71.44812  ?  1455 HIS   B CA  1 
ATOM   25538 C  C   . HIS   B 1 1457 ? 41.94300   17.97100  -2.10200  1.000 61.24949  ?  1455 HIS   B C   1 
ATOM   25539 O  O   . HIS   B 1 1457 ? 41.39700   16.93500  -1.71300  1.000 80.39062  ?  1455 HIS   B O   1 
ATOM   25540 C  CB  . HIS   B 1 1457 ? 40.35100   19.05700  -3.69000  1.000 66.08804  ?  1455 HIS   B CB  1 
ATOM   25541 C  CG  . HIS   B 1 1457 ? 40.17800   19.86700  -4.93600  1.000 71.74108  ?  1455 HIS   B CG  1 
ATOM   25542 N  ND1 . HIS   B 1 1457 ? 40.24100   19.31600  -6.19700  1.000 67.53269  ?  1455 HIS   B ND1 1 
ATOM   25543 C  CD2 . HIS   B 1 1457 ? 39.93100   21.18600  -5.11400  1.000 84.34766  ?  1455 HIS   B CD2 1 
ATOM   25544 C  CE1 . HIS   B 1 1457 ? 40.04500   20.26100  -7.09900  1.000 79.31925  ?  1455 HIS   B CE1 1 
ATOM   25545 N  NE2 . HIS   B 1 1457 ? 39.85300   21.40500  -6.46800  1.000 85.57397  ?  1455 HIS   B NE2 1 
ATOM   25546 N  N   . ILE   B 1 1458 ? 42.70700   18.72700  -1.32000  1.000 53.55845  ?  1456 ILE   B N   1 
ATOM   25547 C  CA  . ILE   B 1 1458 ? 42.97800   18.36200  0.06800   1.000 62.59934  ?  1456 ILE   B CA  1 
ATOM   25548 C  C   . ILE   B 1 1458 ? 43.08400   19.63700  0.89600   1.000 68.91752  ?  1456 ILE   B C   1 
ATOM   25549 O  O   . ILE   B 1 1458 ? 43.73400   20.60500  0.48800   1.000 53.80928  ?  1456 ILE   B O   1 
ATOM   25550 C  CB  . ILE   B 1 1458 ? 44.25800   17.50300  0.19000   1.000 64.48944  ?  1456 ILE   B CB  1 
ATOM   25551 C  CG1 . ILE   B 1 1458 ? 44.54000   17.11000  1.64600   1.000 67.35023  ?  1456 ILE   B CG1 1 
ATOM   25552 C  CG2 . ILE   B 1 1458 ? 45.45800   18.19800  -0.44200  1.000 72.09010  ?  1456 ILE   B CG2 1 
ATOM   25553 C  CD1 . ILE   B 1 1458 ? 43.33600   16.57600  2.38100   1.000 70.49735  ?  1456 ILE   B CD1 1 
ATOM   25554 N  N   . ASN   B 1 1459 ? 42.43200   19.63900  2.05400   1.000 61.14550  ?  1457 ASN   B N   1 
ATOM   25555 C  CA  . ASN   B 1 1459 ? 42.52500   20.73100  3.01000   1.000 39.62703  ?  1457 ASN   B CA  1 
ATOM   25556 C  C   . ASN   B 1 1459 ? 43.46600   20.33700  4.14200   1.000 51.37712  ?  1457 ASN   B C   1 
ATOM   25557 O  O   . ASN   B 1 1459 ? 43.49700   19.17600  4.56200   1.000 61.86103  ?  1457 ASN   B O   1 
ATOM   25558 C  CB  . ASN   B 1 1459 ? 41.14700   21.09000  3.56800   1.000 43.08590  ?  1457 ASN   B CB  1 
ATOM   25559 C  CG  . ASN   B 1 1459 ? 40.27000   21.79200  2.54900   1.000 49.85148  ?  1457 ASN   B CG  1 
ATOM   25560 O  OD1 . ASN   B 1 1459 ? 40.73700   22.19700  1.48500   1.000 57.47305  ?  1457 ASN   B OD1 1 
ATOM   25561 N  ND2 . ASN   B 1 1459 ? 38.98900   21.93600  2.86800   1.000 54.58094  ?  1457 ASN   B ND2 1 
ATOM   25562 N  N   . PHE   B 1 1460 ? 44.23300   21.30700  4.63100   1.000 50.63446  ?  1458 PHE   B N   1 
ATOM   25563 C  CA  . PHE   B 1 1460 ? 45.24500   21.04100  5.64100   1.000 55.34656  ?  1458 PHE   B CA  1 
ATOM   25564 C  C   . PHE   B 1 1460 ? 45.39400   22.25700  6.54200   1.000 62.69479  ?  1458 PHE   B C   1 
ATOM   25565 O  O   . PHE   B 1 1460 ? 45.36600   23.39700  6.07000   1.000 50.49126  ?  1458 PHE   B O   1 
ATOM   25566 C  CB  . PHE   B 1 1460 ? 46.59800   20.70500  5.00000   1.000 57.12072  ?  1458 PHE   B CB  1 
ATOM   25567 C  CG  . PHE   B 1 1460 ? 46.98900   19.25700  5.11200   1.000 61.50387  ?  1458 PHE   B CG  1 
ATOM   25568 C  CD1 . PHE   B 1 1460 ? 47.39600   18.72600  6.32600   1.000 59.52211  ?  1458 PHE   B CD1 1 
ATOM   25569 C  CD2 . PHE   B 1 1460 ? 46.96100   18.43100  3.99800   1.000 52.85405  ?  1458 PHE   B CD2 1 
ATOM   25570 C  CE1 . PHE   B 1 1460 ? 47.76300   17.39400  6.42900   1.000 64.37133  ?  1458 PHE   B CE1 1 
ATOM   25571 C  CE2 . PHE   B 1 1460 ? 47.32600   17.09800  4.09300   1.000 42.99989  ?  1458 PHE   B CE2 1 
ATOM   25572 C  CZ  . PHE   B 1 1460 ? 47.72700   16.58000  5.31100   1.000 63.40571  ?  1458 PHE   B CZ  1 
ATOM   25573 N  N   . VAL   B 1 1461 ? 45.54600   22.00500  7.83700   1.000 58.91746  ?  1459 VAL   B N   1 
ATOM   25574 C  CA  . VAL   B 1 1461 ? 45.94600   23.04000  8.78500   1.000 56.10380  ?  1459 VAL   B CA  1 
ATOM   25575 C  C   . VAL   B 1 1461 ? 47.46700   23.12100  8.72300   1.000 81.48248  ?  1459 VAL   B C   1 
ATOM   25576 O  O   . VAL   B 1 1461 ? 48.12800   22.07700  8.61100   1.000 83.42482  ?  1459 VAL   B O   1 
ATOM   25577 C  CB  . VAL   B 1 1461 ? 45.43400   22.73000  10.20200  1.000 56.80884  ?  1459 VAL   B CB  1 
ATOM   25578 C  CG1 . VAL   B 1 1461 ? 46.21100   23.51100  11.25500  1.000 76.51719  ?  1459 VAL   B CG1 1 
ATOM   25579 C  CG2 . VAL   B 1 1461 ? 43.95200   23.03700  10.30000  1.000 70.30959  ?  1459 VAL   B CG2 1 
ATOM   25580 N  N   . PRO   B 1 1462 ? 48.06200   24.32000  8.75100   1.000 80.53870  ?  1460 PRO   B N   1 
ATOM   25581 C  CA  . PRO   B 1 1462 ? 49.53300   24.41100  8.69700   1.000 69.70188  ?  1460 PRO   B CA  1 
ATOM   25582 C  C   . PRO   B 1 1462 ? 50.24600   23.54300  9.72200   1.000 76.71089  ?  1460 PRO   B C   1 
ATOM   25583 O  O   . PRO   B 1 1462 ? 51.28500   22.95000  9.40600   1.000 65.58135  ?  1460 PRO   B O   1 
ATOM   25584 C  CB  . PRO   B 1 1462 ? 49.78700   25.90400  8.94000   1.000 73.58016  ?  1460 PRO   B CB  1 
ATOM   25585 C  CG  . PRO   B 1 1462 ? 48.57200   26.57100  8.39500   1.000 82.43654  ?  1460 PRO   B CG  1 
ATOM   25586 C  CD  . PRO   B 1 1462 ? 47.42200   25.64600  8.69100   1.000 74.45594  ?  1460 PRO   B CD  1 
ATOM   25587 N  N   . SER   B 1 1463 ? 49.70900   23.43600  10.93900  1.000 73.94170  ?  1461 SER   B N   1 
ATOM   25588 C  CA  . SER   B 1 1463 ? 50.32700   22.60600  11.96600  1.000 64.25233  ?  1461 SER   B CA  1 
ATOM   25589 C  C   . SER   B 1 1463 ? 50.25700   21.11500  11.65200  1.000 74.03544  ?  1461 SER   B C   1 
ATOM   25590 O  O   . SER   B 1 1463 ? 50.92100   20.32700  12.33400  1.000 61.01269  ?  1461 SER   B O   1 
ATOM   25591 C  CB  . SER   B 1 1463 ? 49.67200   22.88000  13.32000  1.000 60.65336  ?  1461 SER   B CB  1 
ATOM   25592 O  OG  . SER   B 1 1463 ? 48.41800   22.23000  13.41900  1.000 75.72468  ?  1461 SER   B OG  1 
ATOM   25593 N  N   . MET   B 1 1464 ? 49.47700   20.71200  10.64600  1.000 82.83751  ?  1462 MET   B N   1 
ATOM   25594 C  CA  . MET   B 1 1464 ? 49.34900   19.31200  10.26600  1.000 68.20982  ?  1462 MET   B CA  1 
ATOM   25595 C  C   . MET   B 1 1464 ? 49.94800   18.99400  8.90400   1.000 71.85107  ?  1462 MET   B C   1 
ATOM   25596 O  O   . MET   B 1 1464 ? 50.13600   17.81300  8.59100   1.000 80.19338  ?  1462 MET   B O   1 
ATOM   25597 C  CB  . MET   B 1 1464 ? 47.87200   18.89100  10.27400  1.000 57.67706  ?  1462 MET   B CB  1 
ATOM   25598 C  CG  . MET   B 1 1464 ? 47.25300   18.81800  11.65800  1.000 64.72527  ?  1462 MET   B CG  1 
ATOM   25599 S  SD  . MET   B 1 1464 ? 47.65200   17.28500  12.51800  1.000 93.61597  ?  1462 MET   B SD  1 
ATOM   25600 C  CE  . MET   B 1 1464 ? 46.24500   17.13300  13.61700  1.000 78.65768  ?  1462 MET   B CE  1 
ATOM   25601 N  N   . LEU   B 1 1465 ? 50.24600   20.00600  8.08700   1.000 72.43668  ?  1463 LEU   B N   1 
ATOM   25602 C  CA  . LEU   B 1 1465 ? 50.85600   19.74900  6.78800   1.000 69.67629  ?  1463 LEU   B CA  1 
ATOM   25603 C  C   . LEU   B 1 1465 ? 52.31000   19.31400  6.93500   1.000 76.15758  ?  1463 LEU   B C   1 
ATOM   25604 O  O   . LEU   B 1 1465 ? 52.80500   18.52100  6.12500   1.000 77.14852  ?  1463 LEU   B O   1 
ATOM   25605 C  CB  . LEU   B 1 1465 ? 50.75000   21.00000  5.91300   1.000 61.79151  ?  1463 LEU   B CB  1 
ATOM   25606 C  CG  . LEU   B 1 1465 ? 50.50400   20.86900  4.40500   1.000 54.49471  ?  1463 LEU   B CG  1 
ATOM   25607 C  CD1 . LEU   B 1 1465 ? 50.34300   22.24300  3.77900   1.000 56.05432  ?  1463 LEU   B CD1 1 
ATOM   25608 C  CD2 . LEU   B 1 1465 ? 51.60500   20.11200  3.70200   1.000 70.02795  ?  1463 LEU   B CD2 1 
ATOM   25609 N  N   . ILE   B 1 1466 ? 53.00200   19.80100  7.96100   1.000 77.63543  ?  1464 ILE   B N   1 
ATOM   25610 C  CA  . ILE   B 1 1466 ? 54.42600   19.51000  8.13000   1.000 82.83019  ?  1464 ILE   B CA  1 
ATOM   25611 C  C   . ILE   B 1 1466 ? 54.64800   18.02900  8.43700   1.000 81.15323  ?  1464 ILE   B C   1 
ATOM   25612 O  O   . ILE   B 1 1466 ? 55.52500   17.42100  7.80600   1.000 88.72532  ?  1464 ILE   B O   1 
ATOM   25613 C  CB  . ILE   B 1 1466 ? 55.06700   20.43200  9.18900   1.000 86.86544  ?  1464 ILE   B CB  1 
ATOM   25614 C  CG1 . ILE   B 1 1466 ? 56.05300   19.66300  10.08000  1.000 99.10147  ?  1464 ILE   B CG1 1 
ATOM   25615 C  CG2 . ILE   B 1 1466 ? 54.00600   21.17100  9.99900   1.000 64.78674  ?  1464 ILE   B CG2 1 
ATOM   25616 C  CD1 . ILE   B 1 1466 ? 57.30500   20.44400  10.43400  1.000 94.66678  ?  1464 ILE   B CD1 1 
ATOM   25617 N  N   . PRO   B 1 1467 ? 53.90500   17.38900  9.35400   1.000 76.64854  ?  1465 PRO   B N   1 
ATOM   25618 C  CA  . PRO   B 1 1467 ? 54.08800   15.93600  9.51900   1.000 74.08219  ?  1465 PRO   B CA  1 
ATOM   25619 C  C   . PRO   B 1 1467 ? 53.78700   15.15700  8.25400   1.000 74.19509  ?  1465 PRO   B C   1 
ATOM   25620 O  O   . PRO   B 1 1467 ? 54.40500   14.11100  8.01500   1.000 83.12983  ?  1465 PRO   B O   1 
ATOM   25621 C  CB  . PRO   B 1 1467 ? 53.11000   15.58000  10.64700  1.000 67.82152  ?  1465 PRO   B CB  1 
ATOM   25622 C  CG  . PRO   B 1 1467 ? 52.89800   16.84900  11.38100  1.000 76.02909  ?  1465 PRO   B CG  1 
ATOM   25623 C  CD  . PRO   B 1 1467 ? 52.93300   17.91200  10.33300  1.000 82.56034  ?  1465 PRO   B CD  1 
ATOM   25624 N  N   . PHE   B 1 1468 ? 52.85700   15.64800  7.43200   1.000 63.93680  ?  1466 PHE   B N   1 
ATOM   25625 C  CA  . PHE   B 1 1468 ? 52.54500   14.99400  6.16500   1.000 66.49785  ?  1466 PHE   B CA  1 
ATOM   25626 C  C   . PHE   B 1 1468 ? 53.75800   14.97900  5.24100   1.000 76.48582  ?  1466 PHE   B C   1 
ATOM   25627 O  O   . PHE   B 1 1468 ? 54.13400   13.92700  4.71000   1.000 82.38606  ?  1466 PHE   B O   1 
ATOM   25628 C  CB  . PHE   B 1 1468 ? 51.35600   15.69800  5.50500   1.000 57.88631  ?  1466 PHE   B CB  1 
ATOM   25629 C  CG  . PHE   B 1 1468 ? 50.76400   14.94900  4.34400   1.000 69.67354  ?  1466 PHE   B CG  1 
ATOM   25630 C  CD1 . PHE   B 1 1468 ? 50.38600   13.62200  4.47500   1.000 77.02668  ?  1466 PHE   B CD1 1 
ATOM   25631 C  CD2 . PHE   B 1 1468 ? 50.56700   15.57900  3.12400   1.000 63.40538  ?  1466 PHE   B CD2 1 
ATOM   25632 C  CE1 . PHE   B 1 1468 ? 49.83700   12.93300  3.40700   1.000 69.26628  ?  1466 PHE   B CE1 1 
ATOM   25633 C  CE2 . PHE   B 1 1468 ? 50.01400   14.89700  2.05200   1.000 50.83320  ?  1466 PHE   B CE2 1 
ATOM   25634 C  CZ  . PHE   B 1 1468 ? 49.65000   13.57100  2.19400   1.000 66.32058  ?  1466 PHE   B CZ  1 
ATOM   25635 N  N   . VAL   B 1 1469 ? 54.39700   16.13600  5.04700   1.000 82.93193  ?  1467 VAL   B N   1 
ATOM   25636 C  CA  . VAL   B 1 1469 ? 55.55200   16.19100  4.15300   1.000 97.99660  ?  1467 VAL   B CA  1 
ATOM   25637 C  C   . VAL   B 1 1469 ? 56.80800   15.63600  4.81900   1.000 97.47356  ?  1467 VAL   B C   1 
ATOM   25638 O  O   . VAL   B 1 1469 ? 57.69800   15.12300  4.13000   1.000 92.78569  ?  1467 VAL   B O   1 
ATOM   25639 C  CB  . VAL   B 1 1469 ? 55.77800   17.62500  3.64100   1.000 88.52072  ?  1467 VAL   B CB  1 
ATOM   25640 C  CG1 . VAL   B 1 1469 ? 54.46500   18.24300  3.22600   1.000 78.15752  ?  1467 VAL   B CG1 1 
ATOM   25641 C  CG2 . VAL   B 1 1469 ? 56.45700   18.48400  4.70200   1.000 80.93372  ?  1467 VAL   B CG2 1 
ATOM   25642 N  N   . GLU   B 1 1470 ? 56.91100   15.72300  6.14900   1.000 88.40069  ?  1468 GLU   B N   1 
ATOM   25643 C  CA  . GLU   B 1 1470 ? 58.03800   15.10600  6.83800   1.000 89.72002  ?  1468 GLU   B CA  1 
ATOM   25644 C  C   . GLU   B 1 1470 ? 58.03400   13.59400  6.68100   1.000 92.62511  ?  1468 GLU   B C   1 
ATOM   25645 O  O   . GLU   B 1 1470 ? 59.08500   12.96000  6.82700   1.000 88.82454  ?  1468 GLU   B O   1 
ATOM   25646 C  CB  . GLU   B 1 1470 ? 58.02500   15.47700  8.32300   1.000 78.17649  ?  1468 GLU   B CB  1 
ATOM   25647 C  CG  . GLU   B 1 1470 ? 58.54100   16.87800  8.61300   1.000 93.82961  ?  1468 GLU   B CG  1 
ATOM   25648 C  CD  . GLU   B 1 1470 ? 59.06300   17.03400  10.02700  1.000 93.32542  ?  1468 GLU   B CD  1 
ATOM   25649 O  OE1 . GLU   B 1 1470 ? 58.25700   16.93500  10.97700  1.000 88.74788  ?  1468 GLU   B OE1 1 
ATOM   25650 O  OE2 . GLU   B 1 1470 ? 60.28100   17.26100  10.18800  1.000 99.24240  -1 1468 GLU   B OE2 1 
ATOM   25651 N  N   . TYR   B 1 1471 ? 56.87600   13.00500  6.38300   1.000 95.81128  ?  1469 TYR   B N   1 
ATOM   25652 C  CA  . TYR   B 1 1471 ? 56.77900   11.57400  6.13800   1.000 104.90604 ?  1469 TYR   B CA  1 
ATOM   25653 C  C   . TYR   B 1 1471 ? 56.68300   11.23900  4.65900   1.000 99.43086  ?  1469 TYR   B C   1 
ATOM   25654 O  O   . TYR   B 1 1471 ? 56.87100   10.07500  4.28900   1.000 116.30900 ?  1469 TYR   B O   1 
ATOM   25655 C  CB  . TYR   B 1 1471 ? 55.56000   10.98100  6.85800   1.000 111.70985 ?  1469 TYR   B CB  1 
ATOM   25656 C  CG  . TYR   B 1 1471 ? 55.64800   10.95900  8.37200   1.000 114.11129 ?  1469 TYR   B CG  1 
ATOM   25657 C  CD1 . TYR   B 1 1471 ? 56.54900   11.76800  9.05900   1.000 108.63420 ?  1469 TYR   B CD1 1 
ATOM   25658 C  CD2 . TYR   B 1 1471 ? 54.82900   10.12000  9.11300   1.000 103.63450 ?  1469 TYR   B CD2 1 
ATOM   25659 C  CE1 . TYR   B 1 1471 ? 56.62400   11.74900  10.43700  1.000 111.82341 ?  1469 TYR   B CE1 1 
ATOM   25660 C  CE2 . TYR   B 1 1471 ? 54.89800   10.08800  10.49000  1.000 112.58848 ?  1469 TYR   B CE2 1 
ATOM   25661 C  CZ  . TYR   B 1 1471 ? 55.79600   10.90500  11.14700  1.000 119.16703 ?  1469 TYR   B CZ  1 
ATOM   25662 O  OH  . TYR   B 1 1471 ? 55.86300   10.87400  12.52000  1.000 107.77296 ?  1469 TYR   B OH  1 
ATOM   25663 N  N   . LEU   B 1 1472 ? 56.38900   12.22500  3.81200   1.000 81.81853  ?  1470 LEU   B N   1 
ATOM   25664 C  CA  . LEU   B 1 1472 ? 56.34300   12.03700  2.37000   1.000 90.12368  ?  1470 LEU   B CA  1 
ATOM   25665 C  C   . LEU   B 1 1472 ? 57.71500   12.14500  1.71300   1.000 100.24375 ?  1470 LEU   B C   1 
ATOM   25666 O  O   . LEU   B 1 1472 ? 57.79300   12.40100  0.50500   1.000 95.85348  ?  1470 LEU   B O   1 
ATOM   25667 C  CB  . LEU   B 1 1472 ? 55.38300   13.04600  1.73900   1.000 83.53838  ?  1470 LEU   B CB  1 
ATOM   25668 C  CG  . LEU   B 1 1472 ? 53.98000   12.57500  1.35900   1.000 87.20336  ?  1470 LEU   B CG  1 
ATOM   25669 C  CD1 . LEU   B 1 1472 ? 53.34500   11.76000  2.47800   1.000 84.95332  ?  1470 LEU   B CD1 1 
ATOM   25670 C  CD2 . LEU   B 1 1472 ? 53.12400   13.77600  0.99700   1.000 77.00919  ?  1470 LEU   B CD2 1 
ATOM   25671 N  N   . GLU   B 1 1473 ? 58.79200   11.96400  2.48300   1.000 109.21690 ?  1471 GLU   B N   1 
ATOM   25672 C  CA  . GLU   B 1 1473 ? 60.13200   11.92100  1.91100   1.000 103.78222 ?  1471 GLU   B CA  1 
ATOM   25673 C  C   . GLU   B 1 1473 ? 60.38400   10.63500  1.13600   1.000 112.72349 ?  1471 GLU   B C   1 
ATOM   25674 O  O   . GLU   B 1 1473 ? 61.32700   10.58000  0.34000   1.000 92.48636  ?  1471 GLU   B O   1 
ATOM   25675 C  CB  . GLU   B 1 1473 ? 61.17900   12.07100  3.01600   1.000 89.13559  ?  1471 GLU   B CB  1 
ATOM   25676 C  CG  . GLU   B 1 1473 ? 60.90500   13.21400  3.97900   1.000 97.50128  ?  1471 GLU   B CG  1 
ATOM   25677 C  CD  . GLU   B 1 1473 ? 61.60600   14.49300  3.57300   1.000 104.73841 ?  1471 GLU   B CD  1 
ATOM   25678 O  OE1 . GLU   B 1 1473 ? 62.39300   14.45800  2.60400   1.000 113.01694 ?  1471 GLU   B OE1 1 
ATOM   25679 O  OE2 . GLU   B 1 1473 ? 61.37000   15.53300  4.22400   1.000 107.32503 -1 1471 GLU   B OE2 1 
ATOM   25680 N  N   . GLY   B 1 1474 ? 59.56800   9.60600   1.35500   1.000 113.86049 ?  1472 GLY   B N   1 
ATOM   25681 C  CA  . GLY   B 1 1474 ? 59.71400   8.35000   0.64600   1.000 103.31383 ?  1472 GLY   B CA  1 
ATOM   25682 C  C   . GLY   B 1 1474 ? 58.92000   8.30000   -0.64200  1.000 108.73502 ?  1472 GLY   B C   1 
ATOM   25683 O  O   . GLY   B 1 1474 ? 57.76800   7.85200   -0.65200  1.000 113.23386 ?  1472 GLY   B O   1 
ATOM   25684 N  N   . ARG   B 1 1475 ? 59.53200   8.77300   -1.73300  1.000 102.75609 ?  1473 ARG   B N   1 
ATOM   25685 C  CA  . ARG   B 1 1475 ? 58.94100   8.79300   -3.06900  1.000 92.59139  ?  1473 ARG   B CA  1 
ATOM   25686 C  C   . ARG   B 1 1475 ? 57.70600   9.68500   -3.14200  1.000 124.43126 ?  1473 ARG   B C   1 
ATOM   25687 O  O   . ARG   B 1 1475 ? 57.15600   10.09000  -2.11400  1.000 136.64866 ?  1473 ARG   B O   1 
ATOM   25688 C  CB  . ARG   B 1 1475 ? 58.58300   7.37600   -3.52900  1.000 78.71256  ?  1473 ARG   B CB  1 
ATOM   25689 N  N   . THR   B 1 1476 ? 57.27000   10.00500  -4.35900  1.000 134.95738 ?  1474 THR   B N   1 
ATOM   25690 C  CA  . THR   B 1 1476 ? 56.01100   10.70600  -4.56400  1.000 130.46862 ?  1474 THR   B CA  1 
ATOM   25691 C  C   . THR   B 1 1476 ? 54.91700   9.79100   -5.09500  1.000 121.13870 ?  1474 THR   B C   1 
ATOM   25692 O  O   . THR   B 1 1476 ? 53.75000   10.19900  -5.11900  1.000 123.07620 ?  1474 THR   B O   1 
ATOM   25693 C  CB  . THR   B 1 1476 ? 56.20700   11.90000  -5.51200  1.000 118.37013 ?  1474 THR   B CB  1 
ATOM   25694 O  OG1 . THR   B 1 1476 ? 55.14000   12.83900  -5.32900  1.000 105.78782 ?  1474 THR   B OG1 1 
ATOM   25695 C  CG2 . THR   B 1 1476 ? 56.23700   11.44100  -6.96000  1.000 111.84608 ?  1474 THR   B CG2 1 
ATOM   25696 N  N   . GLU   B 1 1477 ? 55.27300   8.57000   -5.50300  1.000 109.21951 ?  1475 GLU   B N   1 
ATOM   25697 C  CA  . GLU   B 1 1477 ? 54.33200   7.50200   -5.89500  1.000 88.62274  ?  1475 GLU   B CA  1 
ATOM   25698 C  C   . GLU   B 1 1477 ? 53.39000   8.06500   -6.96100  1.000 101.89241 ?  1475 GLU   B C   1 
ATOM   25699 O  O   . GLU   B 1 1477 ? 53.86600   8.74300   -7.88400  1.000 102.25767 ?  1475 GLU   B O   1 
ATOM   25700 C  CB  . GLU   B 1 1477 ? 53.67100   6.96000   -4.64700  1.000 72.65721  ?  1475 GLU   B CB  1 
ATOM   25701 C  CG  . GLU   B 1 1477 ? 54.61000   6.86000   -3.44100  1.000 77.98046  ?  1475 GLU   B CG  1 
ATOM   25702 C  CD  . GLU   B 1 1477 ? 54.06400   5.97200   -2.35300  1.000 78.59206  ?  1475 GLU   B CD  1 
ATOM   25703 O  OE1 . GLU   B 1 1477 ? 53.04200   5.31500   -2.62600  1.000 71.93658  ?  1475 GLU   B OE1 1 
ATOM   25704 O  OE2 . GLU   B 1 1477 ? 54.63000   5.94800   -1.23400  1.000 73.06351  -1 1475 GLU   B OE2 1 
ATOM   25705 N  N   . ALA   B 1 1478 ? 52.07800   7.81800   -6.87700  1.000 101.80378 ?  1476 ALA   B N   1 
ATOM   25706 C  CA  . ALA   B 1 1478 ? 51.10300   8.50000   -7.72100  1.000 104.19141 ?  1476 ALA   B CA  1 
ATOM   25707 C  C   . ALA   B 1 1478 ? 50.60900   9.75000   -7.00400  1.000 119.35031 ?  1476 ALA   B C   1 
ATOM   25708 O  O   . ALA   B 1 1478 ? 50.20900   9.68900   -5.83800  1.000 115.35614 ?  1476 ALA   B O   1 
ATOM   25709 C  CB  . ALA   B 1 1478 ? 49.91800   7.59700   -8.07500  1.000 71.80293  ?  1476 ALA   B CB  1 
ATOM   25710 N  N   . ASN   B 1 1479 ? 50.63500   10.88600  -7.70500  1.000 121.65288 ?  1477 ASN   B N   1 
ATOM   25711 C  CA  . ASN   B 1 1479 ? 50.32400   12.18400  -7.10900  1.000 106.06884 ?  1477 ASN   B CA  1 
ATOM   25712 C  C   . ASN   B 1 1479 ? 49.34200   12.91800  -8.02100  1.000 102.89714 ?  1477 ASN   B C   1 
ATOM   25713 O  O   . ASN   B 1 1479 ? 49.70200   13.85600  -8.73600  1.000 111.82569 ?  1477 ASN   B O   1 
ATOM   25714 C  CB  . ASN   B 1 1479 ? 51.59500   13.00400  -6.87400  1.000 118.54841 ?  1477 ASN   B CB  1 
ATOM   25715 C  CG  . ASN   B 1 1479 ? 52.55400   12.94300  -8.05000  1.000 122.39717 ?  1477 ASN   B CG  1 
ATOM   25716 O  OD1 . ASN   B 1 1479 ? 52.99900   11.86500  -8.44700  1.000 114.13419 ?  1477 ASN   B OD1 1 
ATOM   25717 N  ND2 . ASN   B 1 1479 ? 52.86200   14.10100  -8.62300  1.000 107.16189 ?  1477 ASN   B ND2 1 
ATOM   25718 N  N   . ARG   B 1 1480 ? 48.09200   12.46200  -8.01300  1.000 88.64568  ?  1478 ARG   B N   1 
ATOM   25719 C  CA  . ARG   B 1 1480 ? 47.03400   13.18100  -8.70600  1.000 88.44205  ?  1478 ARG   B CA  1 
ATOM   25720 C  C   . ARG   B 1 1480 ? 46.66200   14.47700  -7.99900  1.000 95.19775  ?  1478 ARG   B C   1 
ATOM   25721 O  O   . ARG   B 1 1480 ? 45.83100   15.23100  -8.51800  1.000 93.24414  ?  1478 ARG   B O   1 
ATOM   25722 C  CB  . ARG   B 1 1480 ? 45.80600   12.28200  -8.85000  1.000 72.72612  ?  1478 ARG   B CB  1 
ATOM   25723 C  CG  . ARG   B 1 1480 ? 45.87700   11.33900  -10.03300 1.000 90.36104  ?  1478 ARG   B CG  1 
ATOM   25724 C  CD  . ARG   B 1 1480 ? 45.72100   12.09900  -11.34000 1.000 98.66650  ?  1478 ARG   B CD  1 
ATOM   25725 N  NE  . ARG   B 1 1480 ? 44.43600   12.78500  -11.43400 1.000 90.52383  ?  1478 ARG   B NE  1 
ATOM   25726 C  CZ  . ARG   B 1 1480 ? 43.24800   12.19200  -11.40700 1.000 97.16178  ?  1478 ARG   B CZ  1 
ATOM   25727 N  NH1 . ARG   B 1 1480 ? 43.12800   10.87500  -11.33900 1.000 107.36724 ?  1478 ARG   B NH1 1 
ATOM   25728 N  NH2 . ARG   B 1 1480 ? 42.15000   12.94100  -11.45700 1.000 86.33306  ?  1478 ARG   B NH2 1 
ATOM   25729 N  N   . LEU   B 1 1481 ? 47.25600   14.73400  -6.83300  1.000 84.12294  ?  1479 LEU   B N   1 
ATOM   25730 C  CA  . LEU   B 1 1481 ? 47.02300   15.96300  -6.08700  1.000 81.72537  ?  1479 LEU   B CA  1 
ATOM   25731 C  C   . LEU   B 1 1481 ? 47.29200   17.18700  -6.95200  1.000 89.71356  ?  1479 LEU   B C   1 
ATOM   25732 O  O   . LEU   B 1 1481 ? 48.31300   17.26600  -7.64000  1.000 94.18744  ?  1479 LEU   B O   1 
ATOM   25733 C  CB  . LEU   B 1 1481 ? 47.92400   15.98200  -4.85100  1.000 78.31985  ?  1479 LEU   B CB  1 
ATOM   25734 C  CG  . LEU   B 1 1481 ? 47.34000   16.41100  -3.50600  1.000 69.14472  ?  1479 LEU   B CG  1 
ATOM   25735 C  CD1 . LEU   B 1 1481 ? 46.01500   15.71800  -3.23400  1.000 86.86413  ?  1479 LEU   B CD1 1 
ATOM   25736 C  CD2 . LEU   B 1 1481 ? 48.34200   16.12000  -2.39700  1.000 57.69623  ?  1479 LEU   B CD2 1 
ATOM   25737 N  N   . ARG   B 1 1482 ? 46.36800   18.14200  -6.91100  1.000 87.33981  ?  1480 ARG   B N   1 
ATOM   25738 C  CA  . ARG   B 1 1482 ? 46.48500   19.38100  -7.66900  1.000 81.08882  ?  1480 ARG   B CA  1 
ATOM   25739 C  C   . ARG   B 1 1482 ? 46.57500   20.61500  -6.78900  1.000 84.44692  ?  1480 ARG   B C   1 
ATOM   25740 O  O   . ARG   B 1 1482 ? 47.32600   21.54100  -7.11000  1.000 81.01715  ?  1480 ARG   B O   1 
ATOM   25741 C  CB  . ARG   B 1 1482 ? 45.29500   19.52600  -8.62600  1.000 68.50703  ?  1480 ARG   B CB  1 
ATOM   25742 C  CG  . ARG   B 1 1482 ? 45.46700   20.60100  -9.68300  1.000 64.34639  ?  1480 ARG   B CG  1 
ATOM   25743 C  CD  . ARG   B 1 1482 ? 44.65100   20.26200  -10.91300 1.000 60.77194  ?  1480 ARG   B CD  1 
ATOM   25744 N  NE  . ARG   B 1 1482 ? 43.61200   19.28900  -10.60400 1.000 77.74609  ?  1480 ARG   B NE  1 
ATOM   25745 C  CZ  . ARG   B 1 1482 ? 43.01100   18.52200  -11.50300 1.000 90.05425  ?  1480 ARG   B CZ  1 
ATOM   25746 N  NH1 . ARG   B 1 1482 ? 43.30800   18.60400  -12.78900 1.000 95.92870  ?  1480 ARG   B NH1 1 
ATOM   25747 N  NH2 . ARG   B 1 1482 ? 42.09200   17.64900  -11.10000 1.000 84.69509  ?  1480 ARG   B NH2 1 
ATOM   25748 N  N   . TYR   B 1 1483 ? 45.83200   20.65400  -5.68400  1.000 88.55562  ?  1481 TYR   B N   1 
ATOM   25749 C  CA  . TYR   B 1 1483 ? 45.81400   21.79600  -4.78200  1.000 76.92204  ?  1481 TYR   B CA  1 
ATOM   25750 C  C   . TYR   B 1 1483 ? 45.92900   21.32300  -3.34000  1.000 64.65375  ?  1481 TYR   B C   1 
ATOM   25751 O  O   . TYR   B 1 1483 ? 45.35500   20.29700  -2.96600  1.000 68.25400  ?  1481 TYR   B O   1 
ATOM   25752 C  CB  . TYR   B 1 1483 ? 44.52800   22.62300  -4.94000  1.000 63.07119  ?  1481 TYR   B CB  1 
ATOM   25753 C  CG  . TYR   B 1 1483 ? 44.04600   22.77900  -6.36700  1.000 73.29618  ?  1481 TYR   B CG  1 
ATOM   25754 C  CD1 . TYR   B 1 1483 ? 44.71800   23.59800  -7.26500  1.000 61.67708  ?  1481 TYR   B CD1 1 
ATOM   25755 C  CD2 . TYR   B 1 1483 ? 42.91400   22.11300  -6.81100  1.000 73.94985  ?  1481 TYR   B CD2 1 
ATOM   25756 C  CE1 . TYR   B 1 1483 ? 44.27300   23.74500  -8.56900  1.000 69.33961  ?  1481 TYR   B CE1 1 
ATOM   25757 C  CE2 . TYR   B 1 1483 ? 42.46400   22.25200  -8.10900  1.000 76.75644  ?  1481 TYR   B CE2 1 
ATOM   25758 C  CZ  . TYR   B 1 1483 ? 43.14400   23.06700  -8.98400  1.000 78.49405  ?  1481 TYR   B CZ  1 
ATOM   25759 O  OH  . TYR   B 1 1483 ? 42.68700   23.19900  -10.27600 1.000 90.61201  ?  1481 TYR   B OH  1 
ATOM   25760 N  N   . ILE   B 1 1484 ? 46.67500   22.07600  -2.53900  1.000 65.73729  ?  1482 ILE   B N   1 
ATOM   25761 C  CA  . ILE   B 1 1484 ? 46.71300   21.91100  -1.08900  1.000 56.47949  ?  1482 ILE   B CA  1 
ATOM   25762 C  C   . ILE   B 1 1484 ? 46.21000   23.22300  -0.50400  1.000 70.01232  ?  1482 ILE   B C   1 
ATOM   25763 O  O   . ILE   B 1 1484 ? 46.95800   24.20500  -0.42900  1.000 71.71937  ?  1482 ILE   B O   1 
ATOM   25764 C  CB  . ILE   B 1 1484 ? 48.11300   21.57000  -0.57000  1.000 61.50166  ?  1482 ILE   B CB  1 
ATOM   25765 C  CG1 . ILE   B 1 1484 ? 48.66900   20.34000  -1.28600  1.000 76.27996  ?  1482 ILE   B CG1 1 
ATOM   25766 C  CG2 . ILE   B 1 1484 ? 48.08400   21.34900  0.93700   1.000 56.09205  ?  1482 ILE   B CG2 1 
ATOM   25767 C  CD1 . ILE   B 1 1484 ? 50.02600   19.90500  -0.77700  1.000 68.84184  ?  1482 ILE   B CD1 1 
ATOM   25768 N  N   . LEU   B 1 1485 ? 44.94200   23.25300  -0.09900  1.000 74.04422  ?  1483 LEU   B N   1 
ATOM   25769 C  CA  . LEU   B 1 1485 ? 44.31600   24.46200  0.42900   1.000 57.26154  ?  1483 LEU   B CA  1 
ATOM   25770 C  C   . LEU   B 1 1485 ? 44.55200   24.52100  1.93500   1.000 60.53554  ?  1483 LEU   B C   1 
ATOM   25771 O  O   . LEU   B 1 1485 ? 44.02100   23.69800  2.68800   1.000 47.25710  ?  1483 LEU   B O   1 
ATOM   25772 C  CB  . LEU   B 1 1485 ? 42.82600   24.48100  0.09800   1.000 43.45157  ?  1483 LEU   B CB  1 
ATOM   25773 C  CG  . LEU   B 1 1485 ? 42.45400   24.00500  -1.30800  1.000 54.41026  ?  1483 LEU   B CG  1 
ATOM   25774 C  CD1 . LEU   B 1 1485 ? 40.94600   23.99500  -1.50000  1.000 54.99313  ?  1483 LEU   B CD1 1 
ATOM   25775 C  CD2 . LEU   B 1 1485 ? 43.12400   24.87400  -2.36100  1.000 69.13518  ?  1483 LEU   B CD2 1 
ATOM   25776 N  N   . ALA   B 1 1486 ? 45.34500   25.49600  2.37200   1.000 65.98019  ?  1484 ALA   B N   1 
ATOM   25777 C  CA  . ALA   B 1 1486 ? 45.72200   25.63400  3.77100   1.000 59.73655  ?  1484 ALA   B CA  1 
ATOM   25778 C  C   . ALA   B 1 1486 ? 44.90500   26.73400  4.43500   1.000 63.77529  ?  1484 ALA   B C   1 
ATOM   25779 O  O   . ALA   B 1 1486 ? 44.68200   27.79900  3.85000   1.000 61.14233  ?  1484 ALA   B O   1 
ATOM   25780 C  CB  . ALA   B 1 1486 ? 47.21600   25.93600  3.90400   1.000 57.94922  ?  1484 ALA   B CB  1 
ATOM   25781 N  N   . CYS   B 1 1487 ? 44.46300   26.46800  5.66100   1.000 61.50985  ?  1485 CYS   B N   1 
ATOM   25782 C  CA  . CYS   B 1 1487 ? 43.64000   27.39600  6.42300   1.000 57.12273  ?  1485 CYS   B CA  1 
ATOM   25783 C  C   . CYS   B 1 1487 ? 43.63100   26.94700  7.87500   1.000 60.00877  ?  1485 CYS   B C   1 
ATOM   25784 O  O   . CYS   B 1 1487 ? 43.80600   25.76100  8.16800   1.000 72.09028  ?  1485 CYS   B O   1 
ATOM   25785 C  CB  . CYS   B 1 1487 ? 42.20900   27.46200  5.87100   1.000 48.34292  ?  1485 CYS   B CB  1 
ATOM   25786 S  SG  . CYS   B 1 1487 ? 41.11400   28.59800  6.74900   1.000 65.38293  ?  1485 CYS   B SG  1 
ATOM   25787 N  N   . GLY   B 1 1488 ? 43.43000   27.90500  8.77800   1.000 54.37807  ?  1486 GLY   B N   1 
ATOM   25788 C  CA  . GLY   B 1 1488 ? 43.38600   27.60600  10.19600  1.000 55.69269  ?  1486 GLY   B CA  1 
ATOM   25789 C  C   . GLY   B 1 1488 ? 44.49000   28.28000  10.98400  1.000 66.87972  ?  1486 GLY   B C   1 
ATOM   25790 O  O   . GLY   B 1 1488 ? 44.23900   28.89600  12.02300  1.000 69.21435  ?  1486 GLY   B O   1 
ATOM   25791 N  N   . GLU   B 1 1489 ? 45.72200   28.16400  10.49800  1.000 73.73384  ?  1487 GLU   B N   1 
ATOM   25792 C  CA  . GLU   B 1 1489 ? 46.88200   28.80300  11.10100  1.000 56.81204  ?  1487 GLU   B CA  1 
ATOM   25793 C  C   . GLU   B 1 1489 ? 47.62700   29.57600  10.01900  1.000 65.00995  ?  1487 GLU   B C   1 
ATOM   25794 O  O   . GLU   B 1 1489 ? 47.25100   29.56000  8.84400   1.000 71.70153  ?  1487 GLU   B O   1 
ATOM   25795 C  CB  . GLU   B 1 1489 ? 47.79200   27.77000  11.77900  1.000 68.12535  ?  1487 GLU   B CB  1 
ATOM   25796 N  N   . ALA   B 1 1490 ? 48.69300   30.26300  10.42000  1.000 60.08022  ?  1488 ALA   B N   1 
ATOM   25797 C  CA  . ALA   B 1 1490 ? 49.50600   31.02900  9.48700   1.000 54.10500  ?  1488 ALA   B CA  1 
ATOM   25798 C  C   . ALA   B 1 1490 ? 50.54200   30.13000  8.82700   1.000 59.26884  ?  1488 ALA   B C   1 
ATOM   25799 O  O   . ALA   B 1 1490 ? 51.14500   29.27300  9.47800   1.000 65.06677  ?  1488 ALA   B O   1 
ATOM   25800 C  CB  . ALA   B 1 1490 ? 50.20000   32.19100  10.19600  1.000 41.03063  ?  1488 ALA   B CB  1 
ATOM   25801 N  N   . MET   B 1 1491 ? 50.74100   30.33100  7.53500   1.000 65.29952  ?  1489 MET   B N   1 
ATOM   25802 C  CA  . MET   B 1 1491 ? 51.72500   29.55100  6.80000   1.000 62.41857  ?  1489 MET   B CA  1 
ATOM   25803 C  C   . MET   B 1 1491 ? 53.12700   29.97400  7.21300   1.000 73.31049  ?  1489 MET   B C   1 
ATOM   25804 O  O   . MET   B 1 1491 ? 53.45300   31.16300  7.12300   1.000 88.97335  ?  1489 MET   B O   1 
ATOM   25805 C  CB  . MET   B 1 1491 ? 51.54500   29.74200  5.29600   1.000 48.04774  ?  1489 MET   B CB  1 
ATOM   25806 C  CG  . MET   B 1 1491 ? 50.72900   28.66200  4.60600   1.000 70.95109  ?  1489 MET   B CG  1 
ATOM   25807 S  SD  . MET   B 1 1491 ? 51.68200   27.17300  4.24500   1.000 108.21105 ?  1489 MET   B SD  1 
ATOM   25808 C  CE  . MET   B 1 1491 ? 51.36300   26.17500  5.70200   1.000 114.86406 ?  1489 MET   B CE  1 
ATOM   25809 N  N   . PRO   B 1 1492 ? 53.97100   29.06400  7.69000   1.000 87.62011  ?  1490 PRO   B N   1 
ATOM   25810 C  CA  . PRO   B 1 1492 ? 55.39400   29.39600  7.81300   1.000 88.78367  ?  1490 PRO   B CA  1 
ATOM   25811 C  C   . PRO   B 1 1492 ? 55.99000   29.60900  6.43000   1.000 94.94456  ?  1490 PRO   B C   1 
ATOM   25812 O  O   . PRO   B 1 1492 ? 55.85300   28.76500  5.54200   1.000 94.58668  ?  1490 PRO   B O   1 
ATOM   25813 C  CB  . PRO   B 1 1492 ? 55.99000   28.16700  8.51200   1.000 84.25193  ?  1490 PRO   B CB  1 
ATOM   25814 C  CG  . PRO   B 1 1492 ? 54.82400   27.48100  9.15500   1.000 78.44590  ?  1490 PRO   B CG  1 
ATOM   25815 C  CD  . PRO   B 1 1492 ? 53.66200   27.73800  8.24800   1.000 89.40848  ?  1490 PRO   B CD  1 
ATOM   25816 N  N   . ASP   B 1 1493 ? 56.64200   30.75900  6.24200   1.000 101.13149 ?  1491 ASP   B N   1 
ATOM   25817 C  CA  . ASP   B 1 1493 ? 57.20400   31.07100  4.93300   1.000 97.93115  ?  1491 ASP   B CA  1 
ATOM   25818 C  C   . ASP   B 1 1493 ? 58.31200   30.10800  4.52700   1.000 84.00302  ?  1491 ASP   B C   1 
ATOM   25819 O  O   . ASP   B 1 1493 ? 58.70900   30.10500  3.35600   1.000 85.91748  ?  1491 ASP   B O   1 
ATOM   25820 C  CB  . ASP   B 1 1493 ? 57.71800   32.51400  4.90200   1.000 93.06701  ?  1491 ASP   B CB  1 
ATOM   25821 C  CG  . ASP   B 1 1493 ? 58.28400   32.96300  6.23400   1.000 96.21000  ?  1491 ASP   B CG  1 
ATOM   25822 O  OD1 . ASP   B 1 1493 ? 58.39900   32.11900  7.14800   1.000 102.80781 ?  1491 ASP   B OD1 1 
ATOM   25823 O  OD2 . ASP   B 1 1493 ? 58.60800   34.16200  6.36600   1.000 85.40960  -1 1491 ASP   B OD2 1 
ATOM   25824 N  N   . GLU   B 1 1494 ? 58.80800   29.29000  5.45400   1.000 79.73123  ?  1492 GLU   B N   1 
ATOM   25825 C  CA  . GLU   B 1 1494 ? 59.76400   28.23900  5.13800   1.000 89.38200  ?  1492 GLU   B CA  1 
ATOM   25826 C  C   . GLU   B 1 1494 ? 59.09700   26.91200  4.80500   1.000 96.98667  ?  1492 GLU   B C   1 
ATOM   25827 O  O   . GLU   B 1 1494 ? 59.77400   26.00200  4.31300   1.000 93.08318  ?  1492 GLU   B O   1 
ATOM   25828 C  CB  . GLU   B 1 1494 ? 60.73200   28.03900  6.30800   1.000 71.47808  ?  1492 GLU   B CB  1 
ATOM   25829 N  N   . LEU   B 1 1495 ? 57.79400   26.77600  5.06000   1.000 109.21626 ?  1493 LEU   B N   1 
ATOM   25830 C  CA  . LEU   B 1 1495 ? 57.10400   25.52300  4.78000   1.000 97.82579  ?  1493 LEU   B CA  1 
ATOM   25831 C  C   . LEU   B 1 1495 ? 56.67400   25.41700  3.32400   1.000 90.55015  ?  1493 LEU   B C   1 
ATOM   25832 O  O   . LEU   B 1 1495 ? 56.55500   24.30400  2.80000   1.000 95.01999  ?  1493 LEU   B O   1 
ATOM   25833 C  CB  . LEU   B 1 1495 ? 55.88500   25.37600  5.69200   1.000 96.31116  ?  1493 LEU   B CB  1 
ATOM   25834 N  N   . VAL   B 1 1496 ? 56.43300   26.55300  2.66200   1.000 85.51810  ?  1494 VAL   B N   1 
ATOM   25835 C  CA  . VAL   B 1 1496 ? 55.99800   26.51500  1.26200   1.000 96.66634  ?  1494 VAL   B CA  1 
ATOM   25836 C  C   . VAL   B 1 1496 ? 57.02100   25.83300  0.36500   1.000 96.93489  ?  1494 VAL   B C   1 
ATOM   25837 O  O   . VAL   B 1 1496 ? 56.61600   25.05600  -0.51400  1.000 96.54975  ?  1494 VAL   B O   1 
ATOM   25838 C  CB  . VAL   B 1 1496 ? 55.61000   27.92300  0.78800   1.000 89.66459  ?  1494 VAL   B CB  1 
ATOM   25839 C  CG1 . VAL   B 1 1496 ? 56.10100   28.98400  1.76900   1.000 78.54962  ?  1494 VAL   B CG1 1 
ATOM   25840 C  CG2 . VAL   B 1 1496 ? 56.12500   28.19500  -0.62500  1.000 84.06032  ?  1494 VAL   B CG2 1 
ATOM   25841 N  N   . PRO   B 1 1497 ? 58.33500   26.04900  0.51300   1.000 104.02734 ?  1495 PRO   B N   1 
ATOM   25842 C  CA  . PRO   B 1 1497 ? 59.27100   25.26700  -0.31300  1.000 104.40399 ?  1495 PRO   B CA  1 
ATOM   25843 C  C   . PRO   B 1 1497 ? 59.27700   23.78700  0.03000   1.000 105.53948 ?  1495 PRO   B C   1 
ATOM   25844 O  O   . PRO   B 1 1497 ? 59.35600   22.95200  -0.88000  1.000 100.44708 ?  1495 PRO   B O   1 
ATOM   25845 C  CB  . PRO   B 1 1497 ? 60.62800   25.92800  -0.03000  1.000 91.12420  ?  1495 PRO   B CB  1 
ATOM   25846 C  CG  . PRO   B 1 1497 ? 60.45100   26.62200  1.27000   1.000 91.17424  ?  1495 PRO   B CG  1 
ATOM   25847 C  CD  . PRO   B 1 1497 ? 59.04000   27.10000  1.26900   1.000 94.81273  ?  1495 PRO   B CD  1 
ATOM   25848 N  N   . LYS   B 1 1498 ? 59.19300   23.43500  1.31800   1.000 97.33275  ?  1496 LYS   B N   1 
ATOM   25849 C  CA  . LYS   B 1 1498 ? 59.18200   22.02500  1.70200   1.000 91.71257  ?  1496 LYS   B CA  1 
ATOM   25850 C  C   . LYS   B 1 1498 ? 58.02300   21.28300  1.04700   1.000 97.66047  ?  1496 LYS   B C   1 
ATOM   25851 O  O   . LYS   B 1 1498 ? 58.16400   20.12000  0.65100   1.000 99.66256  ?  1496 LYS   B O   1 
ATOM   25852 C  CB  . LYS   B 1 1498 ? 59.11600   21.89300  3.22400   1.000 62.85837  ?  1496 LYS   B CB  1 
ATOM   25853 N  N   . VAL   B 1 1499 ? 56.86900   21.94200  0.92300   1.000 91.35122  ?  1497 VAL   B N   1 
ATOM   25854 C  CA  . VAL   B 1 1499 ? 55.75100   21.35900  0.18700   1.000 88.45206  ?  1497 VAL   B CA  1 
ATOM   25855 C  C   . VAL   B 1 1499 ? 56.09200   21.25200  -1.29400  1.000 102.21584 ?  1497 VAL   B C   1 
ATOM   25856 O  O   . VAL   B 1 1499 ? 55.97900   20.18000  -1.90000  1.000 95.95916  ?  1497 VAL   B O   1 
ATOM   25857 C  CB  . VAL   B 1 1499 ? 54.47300   22.18900  0.41000   1.000 86.64371  ?  1497 VAL   B CB  1 
ATOM   25858 C  CG1 . VAL   B 1 1499 ? 53.36100   21.72500  -0.52700  1.000 66.05067  ?  1497 VAL   B CG1 1 
ATOM   25859 C  CG2 . VAL   B 1 1499 ? 54.03500   22.11000  1.86400   1.000 78.13111  ?  1497 VAL   B CG2 1 
ATOM   25860 N  N   . TYR   B 1 1500 ? 56.52500   22.36200  -1.89400  1.000 102.92353 ?  1498 TYR   B N   1 
ATOM   25861 C  CA  . TYR   B 1 1500 ? 56.88200   22.39000  -3.30700  1.000 94.63453  ?  1498 TYR   B CA  1 
ATOM   25862 C  C   . TYR   B 1 1500 ? 58.10700   21.54300  -3.62900  1.000 109.42983 ?  1498 TYR   B C   1 
ATOM   25863 O  O   . TYR   B 1 1500 ? 58.43100   21.38200  -4.81000  1.000 108.60175 ?  1498 TYR   B O   1 
ATOM   25864 C  CB  . TYR   B 1 1500 ? 57.12100   23.83200  -3.74900  1.000 89.76975  ?  1498 TYR   B CB  1 
ATOM   25865 C  CG  . TYR   B 1 1500 ? 55.87000   24.56000  -4.18200  1.000 96.75480  ?  1498 TYR   B CG  1 
ATOM   25866 C  CD1 . TYR   B 1 1500 ? 55.13200   24.12300  -5.27200  1.000 92.78374  ?  1498 TYR   B CD1 1 
ATOM   25867 C  CD2 . TYR   B 1 1500 ? 55.42700   25.68600  -3.49900  1.000 89.11582  ?  1498 TYR   B CD2 1 
ATOM   25868 C  CE1 . TYR   B 1 1500 ? 53.99100   24.78800  -5.67400  1.000 93.74156  ?  1498 TYR   B CE1 1 
ATOM   25869 C  CE2 . TYR   B 1 1500 ? 54.28500   26.35700  -3.89300  1.000 91.77566  ?  1498 TYR   B CE2 1 
ATOM   25870 C  CZ  . TYR   B 1 1500 ? 53.57000   25.90200  -4.98200  1.000 97.33745  ?  1498 TYR   B CZ  1 
ATOM   25871 O  OH  . TYR   B 1 1500 ? 52.43100   26.56100  -5.38500  1.000 83.79168  ?  1498 TYR   B OH  1 
ATOM   25872 N  N   . GLU   B 1 1501 ? 58.79900   21.01700  -2.61900  1.000 109.14811 ?  1499 GLU   B N   1 
ATOM   25873 C  CA  . GLU   B 1 1501 ? 59.90300   20.08500  -2.81800  1.000 100.99545 ?  1499 GLU   B CA  1 
ATOM   25874 C  C   . GLU   B 1 1501 ? 59.45300   18.63400  -2.69900  1.000 101.59189 ?  1499 GLU   B C   1 
ATOM   25875 O  O   . GLU   B 1 1501 ? 59.72600   17.82300  -3.59000  1.000 107.45170 ?  1499 GLU   B O   1 
ATOM   25876 C  CB  . GLU   B 1 1501 ? 61.02300   20.36800  -1.81000  1.000 107.14952 ?  1499 GLU   B CB  1 
ATOM   25877 N  N   . VAL   B 1 1502 ? 58.76000   18.29700  -1.60900  1.000 106.01159 ?  1500 VAL   B N   1 
ATOM   25878 C  CA  . VAL   B 1 1502 ? 58.23900   16.94400  -1.43500  1.000 101.75932 ?  1500 VAL   B CA  1 
ATOM   25879 C  C   . VAL   B 1 1502 ? 57.18200   16.63800  -2.49100  1.000 100.22564 ?  1500 VAL   B C   1 
ATOM   25880 O  O   . VAL   B 1 1502 ? 57.15000   15.54100  -3.06200  1.000 108.47521 ?  1500 VAL   B O   1 
ATOM   25881 C  CB  . VAL   B 1 1502 ? 57.69000   16.77200  -0.00600  1.000 93.54620  ?  1500 VAL   B CB  1 
ATOM   25882 C  CG1 . VAL   B 1 1502 ? 56.58800   15.74100  0.01800   1.000 95.64811  ?  1500 VAL   B CG1 1 
ATOM   25883 C  CG2 . VAL   B 1 1502 ? 58.81100   16.38500  0.95500   1.000 91.18273  ?  1500 VAL   B CG2 1 
ATOM   25884 N  N   . LEU   B 1 1503 ? 56.30400   17.60300  -2.77100  1.000 94.47662  ?  1501 LEU   B N   1 
ATOM   25885 C  CA  . LEU   B 1 1503 ? 55.28500   17.48600  -3.81200  1.000 97.26326  ?  1501 LEU   B CA  1 
ATOM   25886 C  C   . LEU   B 1 1503 ? 55.57200   18.55900  -4.85500  1.000 96.75509  ?  1501 LEU   B C   1 
ATOM   25887 O  O   . LEU   B 1 1503 ? 54.94600   19.63000  -4.85100  1.000 104.02674 ?  1501 LEU   B O   1 
ATOM   25888 C  CB  . LEU   B 1 1503 ? 53.87800   17.62500  -3.23500  1.000 96.49977  ?  1501 LEU   B CB  1 
ATOM   25889 C  CG  . LEU   B 1 1503 ? 53.33200   16.37700  -2.54200  1.000 79.40013  ?  1501 LEU   B CG  1 
ATOM   25890 C  CD1 . LEU   B 1 1503 ? 52.59800   16.74800  -1.26100  1.000 86.14609  ?  1501 LEU   B CD1 1 
ATOM   25891 C  CD2 . LEU   B 1 1503 ? 52.42300   15.60900  -3.48800  1.000 81.38352  ?  1501 LEU   B CD2 1 
ATOM   25892 N  N   . PRO   B 1 1504 ? 56.51600   18.30700  -5.76700  1.000 99.34539  ?  1502 PRO   B N   1 
ATOM   25893 C  CA  . PRO   B 1 1504 ? 56.92900   19.36300  -6.70400  1.000 95.84672  ?  1502 PRO   B CA  1 
ATOM   25894 C  C   . PRO   B 1 1504 ? 55.86500   19.74100  -7.71900  1.000 85.50760  ?  1502 PRO   B C   1 
ATOM   25895 O  O   . PRO   B 1 1504 ? 55.95300   20.83100  -8.29700  1.000 92.09003  ?  1502 PRO   B O   1 
ATOM   25896 C  CB  . PRO   B 1 1504 ? 58.16400   18.76200  -7.38800  1.000 93.92323  ?  1502 PRO   B CB  1 
ATOM   25897 C  CG  . PRO   B 1 1504 ? 57.97800   17.28700  -7.27000  1.000 94.13299  ?  1502 PRO   B CG  1 
ATOM   25898 C  CD  . PRO   B 1 1504 ? 57.27600   17.06000  -5.96200  1.000 104.14112 ?  1502 PRO   B CD  1 
ATOM   25899 N  N   . GLU   B 1 1505 ? 54.86500   18.89400  -7.95000  1.000 72.97455  ?  1503 GLU   B N   1 
ATOM   25900 C  CA  . GLU   B 1 1505 ? 53.85200   19.15800  -8.96200  1.000 90.86604  ?  1503 GLU   B CA  1 
ATOM   25901 C  C   . GLU   B 1 1505 ? 52.54500   19.68300  -8.38400  1.000 96.66444  ?  1503 GLU   B C   1 
ATOM   25902 O  O   . GLU   B 1 1505 ? 51.59100   19.89500  -9.13900  1.000 84.09273  ?  1503 GLU   B O   1 
ATOM   25903 C  CB  . GLU   B 1 1505 ? 53.58400   17.89000  -9.78000  1.000 102.73383 ?  1503 GLU   B CB  1 
ATOM   25904 C  CG  . GLU   B 1 1505 ? 54.32000   17.85000  -11.11200 1.000 89.52563  ?  1503 GLU   B CG  1 
ATOM   25905 C  CD  . GLU   B 1 1505 ? 53.52800   18.49200  -12.23700 1.000 117.45232 ?  1503 GLU   B CD  1 
ATOM   25906 O  OE1 . GLU   B 1 1505 ? 52.36800   18.89400  -12.00000 1.000 117.14137 ?  1503 GLU   B OE1 1 
ATOM   25907 O  OE2 . GLU   B 1 1505 ? 54.06500   18.59600  -13.36000 1.000 121.25739 -1 1503 GLU   B OE2 1 
ATOM   25908 N  N   . VAL   B 1 1506 ? 52.47700   19.90800  -7.07300  1.000 101.34690 ?  1504 VAL   B N   1 
ATOM   25909 C  CA  . VAL   B 1 1506 ? 51.26200   20.41000  -6.44100  1.000 92.64791  ?  1504 VAL   B CA  1 
ATOM   25910 C  C   . VAL   B 1 1506 ? 51.30300   21.93400  -6.42100  1.000 98.73249  ?  1504 VAL   B C   1 
ATOM   25911 O  O   . VAL   B 1 1506 ? 52.33200   22.53800  -6.73800  1.000 105.06030 ?  1504 VAL   B O   1 
ATOM   25912 C  CB  . VAL   B 1 1506 ? 51.10100   19.82900  -5.02400  1.000 84.49661  ?  1504 VAL   B CB  1 
ATOM   25913 C  CG1 . VAL   B 1 1506 ? 51.85300   20.67600  -4.00200  1.000 64.73564  ?  1504 VAL   B CG1 1 
ATOM   25914 C  CG2 . VAL   B 1 1506 ? 49.62800   19.69700  -4.67000  1.000 83.05905  ?  1504 VAL   B CG2 1 
ATOM   25915 N  N   . LYS   B 1 1507 ? 50.18500   22.56500  -6.06100  1.000 104.68950 ?  1505 LYS   B N   1 
ATOM   25916 C  CA  . LYS   B 1 1507 ? 50.07600   24.02400  -6.01000  1.000 86.79454  ?  1505 LYS   B CA  1 
ATOM   25917 C  C   . LYS   B 1 1507 ? 49.55700   24.42900  -4.63200  1.000 75.84678  ?  1505 LYS   B C   1 
ATOM   25918 O  O   . LYS   B 1 1507 ? 48.35100   24.36300  -4.37300  1.000 80.03070  ?  1505 LYS   B O   1 
ATOM   25919 C  CB  . LYS   B 1 1507 ? 49.16700   24.54300  -7.12100  1.000 66.78987  ?  1505 LYS   B CB  1 
ATOM   25920 N  N   . LEU   B 1 1508 ? 50.46400   24.85600  -3.75400  1.000 68.76251  ?  1506 LEU   B N   1 
ATOM   25921 C  CA  . LEU   B 1 1508 ? 50.09500   25.25800  -2.40200  1.000 62.16333  ?  1506 LEU   B CA  1 
ATOM   25922 C  C   . LEU   B 1 1508 ? 49.42400   26.62700  -2.40800  1.000 67.57570  ?  1506 LEU   B C   1 
ATOM   25923 O  O   . LEU   B 1 1508 ? 49.80800   27.52100  -3.16800  1.000 73.61475  ?  1506 LEU   B O   1 
ATOM   25924 C  CB  . LEU   B 1 1508 ? 51.33100   25.28300  -1.50000  1.000 66.71293  ?  1506 LEU   B CB  1 
ATOM   25925 C  CG  . LEU   B 1 1508 ? 51.13200   25.67300  -0.03400  1.000 73.82202  ?  1506 LEU   B CG  1 
ATOM   25926 C  CD1 . LEU   B 1 1508 ? 50.14100   24.74600  0.64800   1.000 66.57363  ?  1506 LEU   B CD1 1 
ATOM   25927 C  CD2 . LEU   B 1 1508 ? 52.45900   25.66500  0.70400   1.000 85.21740  ?  1506 LEU   B CD2 1 
ATOM   25928 N  N   . GLU   B 1 1509 ? 48.41100   26.78600  -1.55700  1.000 72.55847  ?  1507 GLU   B N   1 
ATOM   25929 C  CA  . GLU   B 1 1509 ? 47.63700   28.01800  -1.48300  1.000 65.97291  ?  1507 GLU   B CA  1 
ATOM   25930 C  C   . GLU   B 1 1509 ? 47.29900   28.32800  -0.03100  1.000 73.14268  ?  1507 GLU   B C   1 
ATOM   25931 O  O   . GLU   B 1 1509 ? 47.03500   27.41800  0.75900   1.000 77.64521  ?  1507 GLU   B O   1 
ATOM   25932 C  CB  . GLU   B 1 1509 ? 46.34700   27.91400  -2.30900  1.000 56.51232  ?  1507 GLU   B CB  1 
ATOM   25933 C  CG  . GLU   B 1 1509 ? 46.57400   27.63400  -3.78600  1.000 53.46187  ?  1507 GLU   B CG  1 
ATOM   25934 C  CD  . GLU   B 1 1509 ? 46.34900   28.85500  -4.65100  1.000 77.91712  ?  1507 GLU   B CD  1 
ATOM   25935 O  OE1 . GLU   B 1 1509 ? 45.51300   29.70300  -4.27400  1.000 88.61003  ?  1507 GLU   B OE1 1 
ATOM   25936 O  OE2 . GLU   B 1 1509 ? 47.00400   28.96700  -5.70800  1.000 82.01845  -1 1507 GLU   B OE2 1 
ATOM   25937 N  N   . ASN   B 1 1510 ? 47.30800   29.61400  0.31500   1.000 67.27377  ?  1508 ASN   B N   1 
ATOM   25938 C  CA  . ASN   B 1 1510 ? 46.95600   30.08000  1.65000   1.000 60.94847  ?  1508 ASN   B CA  1 
ATOM   25939 C  C   . ASN   B 1 1510 ? 45.57700   30.72000  1.60600   1.000 66.57585  ?  1508 ASN   B C   1 
ATOM   25940 O  O   . ASN   B 1 1510 ? 45.29000   31.52300  0.71100   1.000 67.85710  ?  1508 ASN   B O   1 
ATOM   25941 C  CB  . ASN   B 1 1510 ? 47.98900   31.07800  2.17900   1.000 64.11327  ?  1508 ASN   B CB  1 
ATOM   25942 C  CG  . ASN   B 1 1510 ? 47.94400   31.22000  3.68800   1.000 61.05149  ?  1508 ASN   B CG  1 
ATOM   25943 O  OD1 . ASN   B 1 1510 ? 47.84800   30.23100  4.41400   1.000 61.73845  ?  1508 ASN   B OD1 1 
ATOM   25944 N  ND2 . ASN   B 1 1510 ? 48.01200   32.45600  4.16900   1.000 54.96277  ?  1508 ASN   B ND2 1 
ATOM   25945 N  N   . ILE   B 1 1511 ? 44.72400   30.36100  2.56300   1.000 58.52704  ?  1509 ILE   B N   1 
ATOM   25946 C  CA  . ILE   B 1 1511 ? 43.33000   30.78700  2.57300   1.000 58.07278  ?  1509 ILE   B CA  1 
ATOM   25947 C  C   . ILE   B 1 1511 ? 42.95500   31.22300  3.98200   1.000 53.65722  ?  1509 ILE   B C   1 
ATOM   25948 O  O   . ILE   B 1 1511 ? 43.40100   30.62600  4.96900   1.000 51.59683  ?  1509 ILE   B O   1 
ATOM   25949 C  CB  . ILE   B 1 1511 ? 42.39900   29.66200  2.07100   1.000 55.29361  ?  1509 ILE   B CB  1 
ATOM   25950 C  CG1 . ILE   B 1 1511 ? 42.79200   29.26700  0.64600   1.000 59.48884  ?  1509 ILE   B CG1 1 
ATOM   25951 C  CG2 . ILE   B 1 1511 ? 40.94000   30.09600  2.11900   1.000 48.92347  ?  1509 ILE   B CG2 1 
ATOM   25952 C  CD1 . ILE   B 1 1511 ? 41.86100   28.30600  -0.00400  1.000 63.61061  ?  1509 ILE   B CD1 1 
ATOM   25953 N  N   . TYR   B 1 1512 ? 42.14400   32.27500  4.07100   1.000 32.75750  ?  1510 TYR   B N   1 
ATOM   25954 C  CA  . TYR   B 1 1512 ? 41.72400   32.85500  5.33700   1.000 43.60031  ?  1510 TYR   B CA  1 
ATOM   25955 C  C   . TYR   B 1 1512 ? 40.21600   33.06400  5.31200   1.000 53.42148  ?  1510 TYR   B C   1 
ATOM   25956 O  O   . TYR   B 1 1512 ? 39.64600   33.41000  4.27200   1.000 37.22922  ?  1510 TYR   B O   1 
ATOM   25957 C  CB  . TYR   B 1 1512 ? 42.45400   34.18700  5.60000   1.000 42.48987  ?  1510 TYR   B CB  1 
ATOM   25958 C  CG  . TYR   B 1 1512 ? 41.85200   35.03500  6.70200   1.000 48.33096  ?  1510 TYR   B CG  1 
ATOM   25959 C  CD1 . TYR   B 1 1512 ? 42.21200   34.84400  8.03100   1.000 42.66585  ?  1510 TYR   B CD1 1 
ATOM   25960 C  CD2 . TYR   B 1 1512 ? 40.92600   36.03200  6.41200   1.000 45.48345  ?  1510 TYR   B CD2 1 
ATOM   25961 C  CE1 . TYR   B 1 1512 ? 41.66300   35.61800  9.04100   1.000 38.84017  ?  1510 TYR   B CE1 1 
ATOM   25962 C  CE2 . TYR   B 1 1512 ? 40.37000   36.80800  7.41500   1.000 49.34290  ?  1510 TYR   B CE2 1 
ATOM   25963 C  CZ  . TYR   B 1 1512 ? 40.74300   36.59700  8.72700   1.000 45.51020  ?  1510 TYR   B CZ  1 
ATOM   25964 O  OH  . TYR   B 1 1512 ? 40.19500   37.36700  9.72900   1.000 49.17057  ?  1510 TYR   B OH  1 
ATOM   25965 N  N   . GLY   B 1 1513 ? 39.57400   32.85100  6.45800   1.000 46.31898  ?  1511 GLY   B N   1 
ATOM   25966 C  CA  . GLY   B 1 1513 ? 38.14900   33.04300  6.56700   1.000 51.49851  ?  1511 GLY   B CA  1 
ATOM   25967 C  C   . GLY   B 1 1513 ? 37.60800   32.75900  7.95300   1.000 55.16464  ?  1511 GLY   B C   1 
ATOM   25968 O  O   . GLY   B 1 1513 ? 37.84300   31.69500  8.53500   1.000 63.61823  ?  1511 GLY   B O   1 
ATOM   25969 N  N   . PRO   B 1 1514 ? 36.86900   33.71300  8.50800   1.000 59.15036  ?  1512 PRO   B N   1 
ATOM   25970 C  CA  . PRO   B 1 1514 ? 36.18400   33.48000  9.78100   1.000 68.07495  ?  1512 PRO   B CA  1 
ATOM   25971 C  C   . PRO   B 1 1514 ? 34.91900   32.66200  9.57900   1.000 50.53570  ?  1512 PRO   B C   1 
ATOM   25972 O  O   . PRO   B 1 1514 ? 34.33300   32.62500  8.49500   1.000 49.65757  ?  1512 PRO   B O   1 
ATOM   25973 C  CB  . PRO   B 1 1514 ? 35.84200   34.89400  10.27400  1.000 50.03457  ?  1512 PRO   B CB  1 
ATOM   25974 C  CG  . PRO   B 1 1514 ? 36.49600   35.84700  9.29000   1.000 53.82264  ?  1512 PRO   B CG  1 
ATOM   25975 C  CD  . PRO   B 1 1514 ? 36.65300   35.08200  8.02000   1.000 58.26071  ?  1512 PRO   B CD  1 
ATOM   25976 N  N   . THR   B 1 1515 ? 34.49700   32.00100  10.65900  1.000 37.31239  ?  1513 THR   B N   1 
ATOM   25977 C  CA  . THR   B 1 1515 ? 33.23700   31.26700  10.61100  1.000 53.95243  ?  1513 THR   B CA  1 
ATOM   25978 C  C   . THR   B 1 1515 ? 32.06600   32.20200  10.34700  1.000 58.53353  ?  1513 THR   B C   1 
ATOM   25979 O  O   . THR   B 1 1515 ? 31.08400   31.80500  9.70800   1.000 57.39709  ?  1513 THR   B O   1 
ATOM   25980 C  CB  . THR   B 1 1515 ? 33.01600   30.49800  11.91200  1.000 49.73543  ?  1513 THR   B CB  1 
ATOM   25981 O  OG1 . THR   B 1 1515 ? 34.27300   30.02400  12.41100  1.000 57.01955  ?  1513 THR   B OG1 1 
ATOM   25982 C  CG2 . THR   B 1 1515 ? 32.09300   29.31600  11.67100  1.000 48.71521  ?  1513 THR   B CG2 1 
ATOM   25983 N  N   . GLU   B 1 1516 ? 32.15900   33.44800  10.81700  1.000 58.82768  ?  1514 GLU   B N   1 
ATOM   25984 C  CA  . GLU   B 1 1516 ? 31.14500   34.46600  10.57200  1.000 44.72490  ?  1514 GLU   B CA  1 
ATOM   25985 C  C   . GLU   B 1 1516 ? 31.09800   34.91400  9.11800   1.000 48.94385  ?  1514 GLU   B C   1 
ATOM   25986 O  O   . GLU   B 1 1516 ? 30.23700   35.72700  8.76300   1.000 41.10357  ?  1514 GLU   B O   1 
ATOM   25987 C  CB  . GLU   B 1 1516 ? 31.38400   35.65900  11.49600  1.000 32.27751  ?  1514 GLU   B CB  1 
ATOM   25988 C  CG  . GLU   B 1 1516 ? 31.11200   35.35800  12.96700  1.000 38.69731  ?  1514 GLU   B CG  1 
ATOM   25989 C  CD  . GLU   B 1 1516 ? 32.30000   34.72800  13.67600  1.000 49.01698  ?  1514 GLU   B CD  1 
ATOM   25990 O  OE1 . GLU   B 1 1516 ? 33.17800   34.16100  12.99000  1.000 55.39710  ?  1514 GLU   B OE1 1 
ATOM   25991 O  OE2 . GLU   B 1 1516 ? 32.36000   34.80700  14.92200  1.000 48.61936  -1 1514 GLU   B OE2 1 
ATOM   25992 N  N   . ALA   B 1 1517 ? 32.00600   34.42100  8.27900   1.000 52.88419  ?  1515 ALA   B N   1 
ATOM   25993 C  CA  . ALA   B 1 1517 ? 31.81200   34.46800  6.83700   1.000 62.00093  ?  1515 ALA   B CA  1 
ATOM   25994 C  C   . ALA   B 1 1517 ? 31.11800   33.18200  6.41800   1.000 75.79643  ?  1515 ALA   B C   1 
ATOM   25995 O  O   . ALA   B 1 1517 ? 30.09200   32.80400  6.99300   1.000 99.42552  ?  1515 ALA   B O   1 
ATOM   25996 C  CB  . ALA   B 1 1517 ? 33.14300   34.63400  6.10200   1.000 58.25758  ?  1515 ALA   B CB  1 
ATOM   25997 N  N   . THR   B 1 1518 ? 31.67100   32.49200  5.42800   1.000 61.94913  ?  1516 THR   B N   1 
ATOM   25998 C  CA  . THR   B 1 1518 ? 31.21500   31.14700  5.07700   1.000 62.26388  ?  1516 THR   B CA  1 
ATOM   25999 C  C   . THR   B 1 1518 ? 32.47600   30.35600  4.74500   1.000 65.73094  ?  1516 THR   B C   1 
ATOM   26000 O  O   . THR   B 1 1518 ? 32.93500   30.35900  3.59800   1.000 52.54692  ?  1516 THR   B O   1 
ATOM   26001 C  CB  . THR   B 1 1518 ? 30.21700   31.15000  3.92600   1.000 68.95970  ?  1516 THR   B CB  1 
ATOM   26002 O  OG1 . THR   B 1 1518 ? 29.16100   32.07800  4.20800   1.000 61.55967  ?  1516 THR   B OG1 1 
ATOM   26003 C  CG2 . THR   B 1 1518 ? 29.62200   29.76100  3.74900   1.000 62.28000  ?  1516 THR   B CG2 1 
ATOM   26004 N  N   . ILE   B 1 1519 ? 33.03200   29.70000  5.76800   1.000 61.90777  ?  1517 ILE   B N   1 
ATOM   26005 C  CA  . ILE   B 1 1519 ? 34.25100   28.90200  5.67500   1.000 53.06669  ?  1517 ILE   B CA  1 
ATOM   26006 C  C   . ILE   B 1 1519 ? 35.45300   29.79800  5.39200   1.000 58.28640  ?  1517 ILE   B C   1 
ATOM   26007 O  O   . ILE   B 1 1519 ? 36.35000   29.93100  6.23400   1.000 62.86600  ?  1517 ILE   B O   1 
ATOM   26008 C  CB  . ILE   B 1 1519 ? 34.13000   27.79200  4.61200   1.000 57.84936  ?  1517 ILE   B CB  1 
ATOM   26009 C  CG1 . ILE   B 1 1519 ? 32.76600   27.09400  4.70100   1.000 57.12424  ?  1517 ILE   B CG1 1 
ATOM   26010 C  CG2 . ILE   B 1 1519 ? 35.25600   26.78900  4.77400   1.000 50.96516  ?  1517 ILE   B CG2 1 
ATOM   26011 C  CD1 . ILE   B 1 1519 ? 32.35300   26.38900  3.42100   1.000 54.76189  ?  1517 ILE   B CD1 1 
ATOM   26012 N  N   . TYR   B 1 1520 ? 35.48100   30.42200  4.21400   1.000 49.43388  ?  1518 TYR   B N   1 
ATOM   26013 C  CA  . TYR   B 1 1520 ? 36.64400   31.16100  3.74100   1.000 59.34490  ?  1518 TYR   B CA  1 
ATOM   26014 C  C   . TYR   B 1 1520 ? 36.23700   32.56300  3.30000   1.000 63.20930  ?  1518 TYR   B C   1 
ATOM   26015 O  O   . TYR   B 1 1520 ? 35.05200   32.88600  3.19100   1.000 68.69126  ?  1518 TYR   B O   1 
ATOM   26016 C  CB  . TYR   B 1 1520 ? 37.33200   30.41500  2.59100   1.000 47.83905  ?  1518 TYR   B CB  1 
ATOM   26017 C  CG  . TYR   B 1 1520 ? 37.74500   29.00000  2.94000   1.000 57.22020  ?  1518 TYR   B CG  1 
ATOM   26018 C  CD1 . TYR   B 1 1520 ? 38.31400   28.69800  4.17500   1.000 61.12235  ?  1518 TYR   B CD1 1 
ATOM   26019 C  CD2 . TYR   B 1 1520 ? 37.53700   27.96100  2.04500   1.000 50.27806  ?  1518 TYR   B CD2 1 
ATOM   26020 C  CE1 . TYR   B 1 1520 ? 38.68700   27.40000  4.49400   1.000 68.66092  ?  1518 TYR   B CE1 1 
ATOM   26021 C  CE2 . TYR   B 1 1520 ? 37.90200   26.66500  2.35000   1.000 50.49144  ?  1518 TYR   B CE2 1 
ATOM   26022 C  CZ  . TYR   B 1 1520 ? 38.47500   26.38700  3.57500   1.000 67.69338  ?  1518 TYR   B CZ  1 
ATOM   26023 O  OH  . TYR   B 1 1520 ? 38.83600   25.09200  3.87200   1.000 63.93309  ?  1518 TYR   B OH  1 
ATOM   26024 N  N   . ALA   B 1 1521 ? 37.24400   33.40000  3.03300   1.000 66.40428  ?  1519 ALA   B N   1 
ATOM   26025 C  CA  . ALA   B 1 1521 ? 37.00000   34.79000  2.66000   1.000 56.23104  ?  1519 ALA   B CA  1 
ATOM   26026 C  C   . ALA   B 1 1521 ? 38.06900   35.33900  1.71700   1.000 58.48054  ?  1519 ALA   B C   1 
ATOM   26027 O  O   . ALA   B 1 1521 ? 37.74900   36.08200  0.78400   1.000 69.14255  ?  1519 ALA   B O   1 
ATOM   26028 C  CB  . ALA   B 1 1521 ? 36.90500   35.66300  3.91300   1.000 50.25478  ?  1519 ALA   B CB  1 
ATOM   26029 N  N   . SER   B 1 1522 ? 39.33500   34.98800  1.94700   1.000 54.30301  ?  1520 SER   B N   1 
ATOM   26030 C  CA  . SER   B 1 1522 ? 40.44100   35.48200  1.13600   1.000 54.86461  ?  1520 SER   B CA  1 
ATOM   26031 C  C   . SER   B 1 1522 ? 41.37100   34.33600  0.75800   1.000 55.04692  ?  1520 SER   B C   1 
ATOM   26032 O  O   . SER   B 1 1522 ? 41.33600   33.25400  1.35000   1.000 59.33693  ?  1520 SER   B O   1 
ATOM   26033 C  CB  . SER   B 1 1522 ? 41.23200   36.57800  1.86700   1.000 57.03178  ?  1520 SER   B CB  1 
ATOM   26034 O  OG  . SER   B 1 1522 ? 41.97300   36.04500  2.95100   1.000 62.73677  ?  1520 SER   B OG  1 
ATOM   26035 N  N   . ARG   B 1 1523 ? 42.21800   34.59000  -0.23800  1.000 54.36217  ?  1521 ARG   B N   1 
ATOM   26036 C  CA  . ARG   B 1 1523 ? 43.10900   33.56600  -0.76300  1.000 57.01754  ?  1521 ARG   B CA  1 
ATOM   26037 C  C   . ARG   B 1 1523 ? 44.36600   34.21500  -1.32500  1.000 61.15635  ?  1521 ARG   B C   1 
ATOM   26038 O  O   . ARG   B 1 1523 ? 44.33100   35.34400  -1.82100  1.000 66.49548  ?  1521 ARG   B O   1 
ATOM   26039 C  CB  . ARG   B 1 1523 ? 42.41900   32.73300  -1.85100  1.000 61.20801  ?  1521 ARG   B CB  1 
ATOM   26040 C  CG  . ARG   B 1 1523 ? 41.87800   33.56800  -3.00600  1.000 79.12080  ?  1521 ARG   B CG  1 
ATOM   26041 C  CD  . ARG   B 1 1523 ? 41.84400   32.76900  -4.28800  1.000 82.12755  ?  1521 ARG   B CD  1 
ATOM   26042 N  NE  . ARG   B 1 1523 ? 43.16100   32.68300  -4.90800  1.000 88.27518  ?  1521 ARG   B NE  1 
ATOM   26043 C  CZ  . ARG   B 1 1523 ? 43.50900   33.29600  -6.03200  1.000 87.49839  ?  1521 ARG   B CZ  1 
ATOM   26044 N  NH1 . ARG   B 1 1523 ? 42.65900   34.06900  -6.69000  1.000 102.96079 ?  1521 ARG   B NH1 1 
ATOM   26045 N  NH2 . ARG   B 1 1523 ? 44.73600   33.12100  -6.51400  1.000 82.59471  ?  1521 ARG   B NH2 1 
ATOM   26046 N  N   . TYR   B 1 1524 ? 45.47800   33.48500  -1.24700  1.000 68.71438  ?  1522 TYR   B N   1 
ATOM   26047 C  CA  . TYR   B 1 1524 ? 46.74800   33.93100  -1.80700  1.000 65.52952  ?  1522 TYR   B CA  1 
ATOM   26048 C  C   . TYR   B 1 1524 ? 47.46800   32.74300  -2.42500  1.000 78.02583  ?  1522 TYR   B C   1 
ATOM   26049 O  O   . TYR   B 1 1524 ? 47.66400   31.71900  -1.76200  1.000 66.49627  ?  1522 TYR   B O   1 
ATOM   26050 C  CB  . TYR   B 1 1524 ? 47.63600   34.58300  -0.74200  1.000 70.71572  ?  1522 TYR   B CB  1 
ATOM   26051 C  CG  . TYR   B 1 1524 ? 48.96000   35.07600  -1.28400  1.000 75.14399  ?  1522 TYR   B CG  1 
ATOM   26052 C  CD1 . TYR   B 1 1524 ? 49.00700   35.99000  -2.33000  1.000 73.84881  ?  1522 TYR   B CD1 1 
ATOM   26053 C  CD2 . TYR   B 1 1524 ? 50.16200   34.61600  -0.76200  1.000 71.42877  ?  1522 TYR   B CD2 1 
ATOM   26054 C  CE1 . TYR   B 1 1524 ? 50.21400   36.44100  -2.83400  1.000 61.92808  ?  1522 TYR   B CE1 1 
ATOM   26055 C  CE2 . TYR   B 1 1524 ? 51.37500   35.05900  -1.26300  1.000 82.18613  ?  1522 TYR   B CE2 1 
ATOM   26056 C  CZ  . TYR   B 1 1524 ? 51.39400   35.97300  -2.29700  1.000 80.72373  ?  1522 TYR   B CZ  1 
ATOM   26057 O  OH  . TYR   B 1 1524 ? 52.59600   36.41900  -2.79700  1.000 80.60238  ?  1522 TYR   B OH  1 
ATOM   26058 N  N   . SER   B 1 1525 ? 47.87000   32.88600  -3.68500  1.000 82.74426  ?  1523 SER   B N   1 
ATOM   26059 C  CA  . SER   B 1 1525 ? 48.53700   31.80700  -4.40500  1.000 69.16606  ?  1523 SER   B CA  1 
ATOM   26060 C  C   . SER   B 1 1525 ? 50.02300   31.80200  -4.06900  1.000 67.43406  ?  1523 SER   B C   1 
ATOM   26061 O  O   . SER   B 1 1525 ? 50.73400   32.77000  -4.36000  1.000 88.39979  ?  1523 SER   B O   1 
ATOM   26062 C  CB  . SER   B 1 1525 ? 48.32700   31.96500  -5.90800  1.000 73.74463  ?  1523 SER   B CB  1 
ATOM   26063 O  OG  . SER   B 1 1525 ? 46.95000   31.91700  -6.24000  1.000 68.67938  ?  1523 SER   B OG  1 
ATOM   26064 N  N   . LEU   B 1 1526 ? 50.49200   30.71700  -3.46000  1.000 68.61241  ?  1524 LEU   B N   1 
ATOM   26065 C  CA  . LEU   B 1 1526 ? 51.91100   30.54500  -3.17500  1.000 78.27900  ?  1524 LEU   B CA  1 
ATOM   26066 C  C   . LEU   B 1 1526 ? 52.59200   29.88900  -4.37000  1.000 87.87607  ?  1524 LEU   B C   1 
ATOM   26067 O  O   . LEU   B 1 1526 ? 52.01700   29.01400  -5.02400  1.000 100.31779 ?  1524 LEU   B O   1 
ATOM   26068 C  CB  . LEU   B 1 1526 ? 52.11700   29.69900  -1.91400  1.000 69.57689  ?  1524 LEU   B CB  1 
ATOM   26069 C  CG  . LEU   B 1 1526 ? 52.00300   30.40200  -0.55500  1.000 79.82310  ?  1524 LEU   B CG  1 
ATOM   26070 C  CD1 . LEU   B 1 1526 ? 50.59900   30.93200  -0.31400  1.000 89.79376  ?  1524 LEU   B CD1 1 
ATOM   26071 C  CD2 . LEU   B 1 1526 ? 52.40700   29.47200  0.57700   1.000 76.70887  ?  1524 LEU   B CD2 1 
ATOM   26072 N  N   . ALA   B 1 1527 ? 53.81400   30.32500  -4.66000  1.000 92.72030  ?  1525 ALA   B N   1 
ATOM   26073 C  CA  . ALA   B 1 1527 ? 54.55100   29.85600  -5.82200  1.000 93.46118  ?  1525 ALA   B CA  1 
ATOM   26074 C  C   . ALA   B 1 1527 ? 55.88000   29.24400  -5.39900  1.000 108.23856 ?  1525 ALA   B C   1 
ATOM   26075 O  O   . ALA   B 1 1527 ? 56.42400   29.55500  -4.33400  1.000 111.55556 ?  1525 ALA   B O   1 
ATOM   26076 C  CB  . ALA   B 1 1527 ? 54.79400   30.99100  -6.82500  1.000 76.34497  ?  1525 ALA   B CB  1 
ATOM   26077 N  N   . LYS   B 1 1528 ? 56.40300   28.36900  -6.26400  1.000 103.24456 ?  1526 LYS   B N   1 
ATOM   26078 C  CA  . LYS   B 1 1528 ? 57.63100   27.64600  -5.95000  1.000 98.38224  ?  1526 LYS   B CA  1 
ATOM   26079 C  C   . LYS   B 1 1528 ? 58.81200   28.58900  -5.76100  1.000 97.44007  ?  1526 LYS   B C   1 
ATOM   26080 O  O   . LYS   B 1 1528 ? 59.74500   28.27200  -5.01400  1.000 99.16636  ?  1526 LYS   B O   1 
ATOM   26081 C  CB  . LYS   B 1 1528 ? 57.93600   26.62600  -7.04700  1.000 85.26809  ?  1526 LYS   B CB  1 
ATOM   26082 N  N   . GLY   B 1 1529 ? 58.79100   29.75100  -6.41900  1.000 97.83272  ?  1527 GLY   B N   1 
ATOM   26083 C  CA  . GLY   B 1 1529 ? 59.83300   30.73800  -6.20700  1.000 104.58338 ?  1527 GLY   B CA  1 
ATOM   26084 C  C   . GLY   B 1 1529 ? 59.92900   31.23100  -4.77800  1.000 119.40625 ?  1527 GLY   B C   1 
ATOM   26085 O  O   . GLY   B 1 1529 ? 60.93300   31.85400  -4.41400  1.000 128.53595 ?  1527 GLY   B O   1 
ATOM   26086 N  N   . SER   B 1 1530 ? 58.90700   30.96400  -3.95900  1.000 121.58094 ?  1528 SER   B N   1 
ATOM   26087 C  CA  . SER   B 1 1530 ? 58.88400   31.32900  -2.54600  1.000 112.99170 ?  1528 SER   B CA  1 
ATOM   26088 C  C   . SER   B 1 1530 ? 59.18000   32.81100  -2.35300  1.000 113.82578 ?  1528 SER   B C   1 
ATOM   26089 O  O   . SER   B 1 1530 ? 58.75200   33.64400  -3.15900  1.000 118.22732 ?  1528 SER   B O   1 
ATOM   26090 C  CB  . SER   B 1 1530 ? 59.88300   30.47700  -1.75700  1.000 105.66653 ?  1528 SER   B CB  1 
ATOM   26091 O  OG  . SER   B 1 1530 ? 61.19800   30.99300  -1.86900  1.000 126.35233 ?  1528 SER   B OG  1 
ATOM   26092 N  N   . GLN   B 1 1531 ? 59.89800   33.14100  -1.27800  1.000 106.21951 ?  1529 GLN   B N   1 
ATOM   26093 C  CA  . GLN   B 1 1531 ? 60.36700   34.49900  -0.99900  1.000 110.76591 ?  1529 GLN   B CA  1 
ATOM   26094 C  C   . GLN   B 1 1531 ? 59.19200   35.47200  -0.84500  1.000 110.06477 ?  1529 GLN   B C   1 
ATOM   26095 O  O   . GLN   B 1 1531 ? 58.95300   36.35300  -1.67300  1.000 116.72840 ?  1529 GLN   B O   1 
ATOM   26096 C  CB  . GLN   B 1 1531 ? 61.34000   34.97000  -2.08600  1.000 109.82979 ?  1529 GLN   B CB  1 
ATOM   26097 N  N   . GLU   B 1 1532 ? 58.45900   35.28000  0.25100   1.000 92.01654  ?  1530 GLU   B N   1 
ATOM   26098 C  CA  . GLU   B 1 1532 ? 57.40300   36.19500  0.68100   1.000 89.81868  ?  1530 GLU   B CA  1 
ATOM   26099 C  C   . GLU   B 1 1532 ? 57.64600   36.48000  2.15700   1.000 92.54807  ?  1530 GLU   B C   1 
ATOM   26100 O  O   . GLU   B 1 1532 ? 57.53500   35.57000  2.98600   1.000 82.30659  ?  1530 GLU   B O   1 
ATOM   26101 C  CB  . GLU   B 1 1532 ? 56.01200   35.59600  0.45800   1.000 70.54720  ?  1530 GLU   B CB  1 
ATOM   26102 C  CG  . GLU   B 1 1532 ? 55.88700   34.71300  -0.77300  1.000 93.16467  ?  1530 GLU   B CG  1 
ATOM   26103 C  CD  . GLU   B 1 1532 ? 55.43500   35.48500  -1.99400  1.000 108.21513 ?  1530 GLU   B CD  1 
ATOM   26104 O  OE1 . GLU   B 1 1532 ? 55.07900   36.67400  -1.84200  1.000 96.09776  ?  1530 GLU   B OE1 1 
ATOM   26105 O  OE2 . GLU   B 1 1532 ? 55.43300   34.90600  -3.10100  1.000 108.65379 -1 1530 GLU   B OE2 1 
ATOM   26106 N  N   . SER   B 1 1533 ? 57.98600   37.73800  2.48600   1.000 100.19278 ?  1531 SER   B N   1 
ATOM   26107 C  CA  . SER   B 1 1533 ? 58.46600   38.07000  3.82700   1.000 98.63747  ?  1531 SER   B CA  1 
ATOM   26108 C  C   . SER   B 1 1533 ? 57.45700   37.65200  4.90200   1.000 101.41450 ?  1531 SER   B C   1 
ATOM   26109 O  O   . SER   B 1 1533 ? 57.83600   36.90200  5.81100   1.000 91.94511  ?  1531 SER   B O   1 
ATOM   26110 C  CB  . SER   B 1 1533 ? 58.87000   39.55300  3.90500   1.000 103.06312 ?  1531 SER   B CB  1 
ATOM   26111 O  OG  . SER   B 1 1533 ? 57.95700   40.40200  3.23500   1.000 99.19306  ?  1531 SER   B OG  1 
ATOM   26112 N  N   . PRO   B 1 1534 ? 56.17100   38.05700  4.84300   1.000 103.34860 ?  1532 PRO   B N   1 
ATOM   26113 C  CA  . PRO   B 1 1534 ? 55.14300   37.21800  5.46200   1.000 75.80335  ?  1532 PRO   B CA  1 
ATOM   26114 C  C   . PRO   B 1 1534 ? 54.40500   36.46400  4.37200   1.000 71.36269  ?  1532 PRO   B C   1 
ATOM   26115 O  O   . PRO   B 1 1534 ? 54.58500   36.75700  3.18600   1.000 79.77304  ?  1532 PRO   B O   1 
ATOM   26116 C  CB  . PRO   B 1 1534 ? 54.22900   38.23000  6.17200   1.000 55.07248  ?  1532 PRO   B CB  1 
ATOM   26117 C  CG  . PRO   B 1 1534 ? 54.77300   39.61200  5.78900   1.000 78.90164  ?  1532 PRO   B CG  1 
ATOM   26118 C  CD  . PRO   B 1 1534 ? 55.59600   39.37800  4.56400   1.000 88.29902  ?  1532 PRO   B CD  1 
ATOM   26119 N  N   . VAL   B 1 1535 ? 53.57400   35.49500  4.73700   1.000 69.86352  ?  1533 VAL   B N   1 
ATOM   26120 C  CA  . VAL   B 1 1535 ? 52.68200   34.84000  3.78700   1.000 66.40012  ?  1533 VAL   B CA  1 
ATOM   26121 C  C   . VAL   B 1 1535 ? 51.33700   35.56000  3.85500   1.000 54.08662  ?  1533 VAL   B C   1 
ATOM   26122 O  O   . VAL   B 1 1535 ? 50.61800   35.40600  4.85600   1.000 59.11491  ?  1533 VAL   B O   1 
ATOM   26123 C  CB  . VAL   B 1 1535 ? 52.54000   33.34300  4.07700   1.000 76.67791  ?  1533 VAL   B CB  1 
ATOM   26124 C  CG1 . VAL   B 1 1535 ? 52.06300   32.61100  2.82500   1.000 66.12717  ?  1533 VAL   B CG1 1 
ATOM   26125 C  CG2 . VAL   B 1 1535 ? 53.87400   32.78900  4.53100   1.000 73.92532  ?  1533 VAL   B CG2 1 
ATOM   26126 N  N   . PRO   B 1 1536 ? 50.98400   36.36600  2.85800   1.000 57.00689  ?  1534 PRO   B N   1 
ATOM   26127 C  CA  . PRO   B 1 1536 ? 49.73900   37.13500  2.93300   1.000 60.84782  ?  1534 PRO   B CA  1 
ATOM   26128 C  C   . PRO   B 1 1536 ? 48.51800   36.23200  2.93400   1.000 65.82897  ?  1534 PRO   B C   1 
ATOM   26129 O  O   . PRO   B 1 1536 ? 48.50400   35.16100  2.32200   1.000 65.95677  ?  1534 PRO   B O   1 
ATOM   26130 C  CB  . PRO   B 1 1536 ? 49.77800   38.00100  1.66700   1.000 61.53066  ?  1534 PRO   B CB  1 
ATOM   26131 C  CG  . PRO   B 1 1536 ? 51.21000   38.01900  1.24500   1.000 66.00633  ?  1534 PRO   B CG  1 
ATOM   26132 C  CD  . PRO   B 1 1536 ? 51.78300   36.70700  1.67100   1.000 68.36108  ?  1534 PRO   B CD  1 
ATOM   26133 N  N   . ILE   B 1 1537 ? 47.47900   36.68100  3.64600   1.000 56.08713  ?  1535 ILE   B N   1 
ATOM   26134 C  CA  . ILE   B 1 1537 ? 46.18100   36.01800  3.55300   1.000 47.62620  ?  1535 ILE   B CA  1 
ATOM   26135 C  C   . ILE   B 1 1537 ? 45.46900   36.35800  2.25500   1.000 50.43940  ?  1535 ILE   B C   1 
ATOM   26136 O  O   . ILE   B 1 1537 ? 44.45200   35.73100  1.93500   1.000 62.73054  ?  1535 ILE   B O   1 
ATOM   26137 C  CB  . ILE   B 1 1537 ? 45.28300   36.36000  4.75800   1.000 40.77468  ?  1535 ILE   B CB  1 
ATOM   26138 C  CG1 . ILE   B 1 1537 ? 45.03300   37.86200  4.85500   1.000 51.09590  ?  1535 ILE   B CG1 1 
ATOM   26139 C  CG2 . ILE   B 1 1537 ? 45.91100   35.86000  6.04500   1.000 43.53372  ?  1535 ILE   B CG2 1 
ATOM   26140 C  CD1 . ILE   B 1 1537 ? 44.24800   38.25500  6.08800   1.000 45.04001  ?  1535 ILE   B CD1 1 
ATOM   26141 N  N   . GLY   B 1 1538 ? 45.96800   37.33100  1.50400   1.000 48.58302  ?  1536 GLY   B N   1 
ATOM   26142 C  CA  . GLY   B 1 1538 ? 45.55400   37.53800  0.13300   1.000 56.50351  ?  1536 GLY   B CA  1 
ATOM   26143 C  C   . GLY   B 1 1538 ? 44.48700   38.60000  -0.04100  1.000 55.25027  ?  1536 GLY   B C   1 
ATOM   26144 O  O   . GLY   B 1 1538 ? 44.24000   39.44300  0.82400   1.000 57.97802  ?  1536 GLY   B O   1 
ATOM   26145 N  N   . LYS   B 1 1539 ? 43.85200   38.55200  -1.21500  1.000 58.07960  ?  1537 LYS   B N   1 
ATOM   26146 C  CA  . LYS   B 1 1539 ? 42.74900   39.40000  -1.63700  1.000 59.56232  ?  1537 LYS   B CA  1 
ATOM   26147 C  C   . LYS   B 1 1539 ? 41.43200   38.64000  -1.53600  1.000 60.44902  ?  1537 LYS   B C   1 
ATOM   26148 O  O   . LYS   B 1 1539 ? 41.41700   37.40600  -1.52500  1.000 57.85788  ?  1537 LYS   B O   1 
ATOM   26149 C  CB  . LYS   B 1 1539 ? 42.97600   39.88200  -3.07600  1.000 55.62161  ?  1537 LYS   B CB  1 
ATOM   26150 C  CG  . LYS   B 1 1539 ? 44.34800   40.49800  -3.31600  1.000 63.59682  ?  1537 LYS   B CG  1 
ATOM   26151 C  CD  . LYS   B 1 1539 ? 44.41700   41.16900  -4.67800  1.000 75.58574  ?  1537 LYS   B CD  1 
ATOM   26152 C  CE  . LYS   B 1 1539 ? 45.82000   41.11300  -5.26500  1.000 82.73086  ?  1537 LYS   B CE  1 
ATOM   26153 N  NZ  . LYS   B 1 1539 ? 46.85900   41.55200  -4.29600  1.000 78.75730  ?  1537 LYS   B NZ  1 
ATOM   26154 N  N   . PRO   B 1 1540 ? 40.30100   39.34500  -1.45000  1.000 67.03767  ?  1538 PRO   B N   1 
ATOM   26155 C  CA  . PRO   B 1 1540 ? 39.02300   38.66300  -1.20600  1.000 67.89938  ?  1538 PRO   B CA  1 
ATOM   26156 C  C   . PRO   B 1 1540 ? 38.63700   37.70900  -2.32800  1.000 67.48971  ?  1538 PRO   B C   1 
ATOM   26157 O  O   . PRO   B 1 1540 ? 39.06000   37.84000  -3.47900  1.000 68.40155  ?  1538 PRO   B O   1 
ATOM   26158 C  CB  . PRO   B 1 1540 ? 38.01700   39.81700  -1.09700  1.000 59.38240  ?  1538 PRO   B CB  1 
ATOM   26159 C  CG  . PRO   B 1 1540 ? 38.83000   41.00200  -0.73800  1.000 57.60671  ?  1538 PRO   B CG  1 
ATOM   26160 C  CD  . PRO   B 1 1540 ? 40.14900   40.81000  -1.42000  1.000 68.44281  ?  1538 PRO   B CD  1 
ATOM   26161 N  N   . LEU   B 1 1541 ? 37.80900   36.73200  -1.96100  1.000 73.30468  ?  1539 LEU   B N   1 
ATOM   26162 C  CA  . LEU   B 1 1541 ? 37.24800   35.78100  -2.90300  1.000 64.79649  ?  1539 LEU   B CA  1 
ATOM   26163 C  C   . LEU   B 1 1541 ? 36.16000   36.47100  -3.72500  1.000 70.52652  ?  1539 LEU   B C   1 
ATOM   26164 O  O   . LEU   B 1 1541 ? 35.80900   37.62200  -3.45600  1.000 68.53256  ?  1539 LEU   B O   1 
ATOM   26165 C  CB  . LEU   B 1 1541 ? 36.70800   34.56700  -2.14600  1.000 49.62621  ?  1539 LEU   B CB  1 
ATOM   26166 C  CG  . LEU   B 1 1541 ? 37.76300   33.55900  -1.68700  1.000 57.36119  ?  1539 LEU   B CG  1 
ATOM   26167 C  CD1 . LEU   B 1 1541 ? 37.18300   32.59900  -0.65800  1.000 56.82995  ?  1539 LEU   B CD1 1 
ATOM   26168 C  CD2 . LEU   B 1 1541 ? 38.33200   32.80300  -2.87800  1.000 49.16083  ?  1539 LEU   B CD2 1 
ATOM   26169 N  N   . PRO   B 1 1542 ? 35.63100   35.80900  -4.75700  1.000 74.87774  ?  1540 PRO   B N   1 
ATOM   26170 C  CA  . PRO   B 1 1542 ? 34.54600   36.41700  -5.54000  1.000 58.29586  ?  1540 PRO   B CA  1 
ATOM   26171 C  C   . PRO   B 1 1542 ? 33.37600   36.86200  -4.67000  1.000 66.53935  ?  1540 PRO   B C   1 
ATOM   26172 O  O   . PRO   B 1 1542 ? 32.96900   36.16800  -3.73600  1.000 69.57001  ?  1540 PRO   B O   1 
ATOM   26173 C  CB  . PRO   B 1 1542 ? 34.14000   35.29500  -6.49800  1.000 59.10028  ?  1540 PRO   B CB  1 
ATOM   26174 C  CG  . PRO   B 1 1542 ? 35.40000   34.54600  -6.72000  1.000 58.25796  ?  1540 PRO   B CG  1 
ATOM   26175 C  CD  . PRO   B 1 1542 ? 36.16600   34.60400  -5.42300  1.000 63.72834  ?  1540 PRO   B CD  1 
ATOM   26176 N  N   . ASN   B 1 1543 ? 32.84400   38.04700  -4.99200  1.000 69.64207  ?  1541 ASN   B N   1 
ATOM   26177 C  CA  . ASN   B 1 1543 ? 31.70500   38.65300  -4.29000  1.000 57.08429  ?  1541 ASN   B CA  1 
ATOM   26178 C  C   . ASN   B 1 1543 ? 31.96900   38.79700  -2.79300  1.000 61.19681  ?  1541 ASN   B C   1 
ATOM   26179 O  O   . ASN   B 1 1543 ? 31.04200   38.84300  -1.98000  1.000 55.26598  ?  1541 ASN   B O   1 
ATOM   26180 C  CB  . ASN   B 1 1543 ? 30.41100   37.87600  -4.54900  1.000 68.67650  ?  1541 ASN   B CB  1 
ATOM   26181 C  CG  . ASN   B 1 1543 ? 29.60100   38.46400  -5.69400  1.000 81.90930  ?  1541 ASN   B CG  1 
ATOM   26182 O  OD1 . ASN   B 1 1543 ? 29.14800   37.74600  -6.58500  1.000 73.26904  ?  1541 ASN   B OD1 1 
ATOM   26183 N  ND2 . ASN   B 1 1543 ? 29.42600   39.78200  -5.67900  1.000 86.62831  ?  1541 ASN   B ND2 1 
ATOM   26184 N  N   . TYR   B 1 1544 ? 33.24400   38.87400  -2.42800  1.000 66.34762  ?  1542 TYR   B N   1 
ATOM   26185 C  CA  . TYR   B 1 1544 ? 33.68300   39.19900  -1.08200  1.000 64.85769  ?  1542 TYR   B CA  1 
ATOM   26186 C  C   . TYR   B 1 1544 ? 34.32800   40.58100  -1.09000  1.000 72.70792  ?  1542 TYR   B C   1 
ATOM   26187 O  O   . TYR   B 1 1544 ? 34.97200   40.97600  -2.06700  1.000 62.59742  ?  1542 TYR   B O   1 
ATOM   26188 C  CB  . TYR   B 1 1544 ? 34.68800   38.16500  -0.56400  1.000 71.71034  ?  1542 TYR   B CB  1 
ATOM   26189 C  CG  . TYR   B 1 1544 ? 34.11600   37.04900  0.28700   1.000 74.10382  ?  1542 TYR   B CG  1 
ATOM   26190 C  CD1 . TYR   B 1 1544 ? 33.67100   37.28900  1.58100   1.000 76.36117  ?  1542 TYR   B CD1 1 
ATOM   26191 C  CD2 . TYR   B 1 1544 ? 34.05600   35.74600  -0.19300  1.000 69.42947  ?  1542 TYR   B CD2 1 
ATOM   26192 C  CE1 . TYR   B 1 1544 ? 33.16600   36.26600  2.36700   1.000 70.41182  ?  1542 TYR   B CE1 1 
ATOM   26193 C  CE2 . TYR   B 1 1544 ? 33.55300   34.71600  0.58500   1.000 67.70726  ?  1542 TYR   B CE2 1 
ATOM   26194 C  CZ  . TYR   B 1 1544 ? 33.11000   34.98200  1.86400   1.000 74.14322  ?  1542 TYR   B CZ  1 
ATOM   26195 O  OH  . TYR   B 1 1544 ? 32.61200   33.96000  2.64100   1.000 60.95819  ?  1542 TYR   B OH  1 
ATOM   26196 N  N   . ARG   B 1 1545 ? 34.15000   41.31800  0.00600   1.000 71.02786  ?  1543 ARG   B N   1 
ATOM   26197 C  CA  . ARG   B 1 1545 ? 34.74700   42.64300  0.15300   1.000 55.33469  ?  1543 ARG   B CA  1 
ATOM   26198 C  C   . ARG   B 1 1545 ? 35.31500   42.77300  1.55700   1.000 57.98152  ?  1543 ARG   B C   1 
ATOM   26199 O  O   . ARG   B 1 1545 ? 34.58900   42.59900  2.54100   1.000 61.02868  ?  1543 ARG   B O   1 
ATOM   26200 C  CB  . ARG   B 1 1545 ? 33.72300   43.75000  -0.12100  1.000 65.08609  ?  1543 ARG   B CB  1 
ATOM   26201 C  CG  . ARG   B 1 1545 ? 33.43400   43.97500  -1.59800  1.000 75.12492  ?  1543 ARG   B CG  1 
ATOM   26202 C  CD  . ARG   B 1 1545 ? 32.33600   45.00700  -1.80000  1.000 66.67940  ?  1543 ARG   B CD  1 
ATOM   26203 N  NE  . ARG   B 1 1545 ? 31.13800   44.68700  -1.03300  1.000 57.98413  ?  1543 ARG   B NE  1 
ATOM   26204 C  CZ  . ARG   B 1 1545 ? 30.21900   43.80800  -1.40800  1.000 55.00945  ?  1543 ARG   B CZ  1 
ATOM   26205 N  NH1 . ARG   B 1 1545 ? 30.32600   43.13800  -2.54400  1.000 60.53618  ?  1543 ARG   B NH1 1 
ATOM   26206 N  NH2 . ARG   B 1 1545 ? 29.16600   43.59400  -0.62300  1.000 56.13533  ?  1543 ARG   B NH2 1 
ATOM   26207 N  N   . MET   B 1 1546 ? 36.60600   43.08500  1.64800   1.000 60.10078  ?  1544 MET   B N   1 
ATOM   26208 C  CA  . MET   B 1 1546 ? 37.30300   43.19800  2.92100   1.000 66.72297  ?  1544 MET   B CA  1 
ATOM   26209 C  C   . MET   B 1 1546 ? 37.78100   44.62900  3.13500   1.000 67.46484  ?  1544 MET   B C   1 
ATOM   26210 O  O   . MET   B 1 1546 ? 38.25200   45.28500  2.20000   1.000 53.59695  ?  1544 MET   B O   1 
ATOM   26211 C  CB  . MET   B 1 1546 ? 38.49100   42.23300  2.98200   1.000 58.81696  ?  1544 MET   B CB  1 
ATOM   26212 C  CG  . MET   B 1 1546 ? 38.09600   40.77300  2.85600   1.000 58.48930  ?  1544 MET   B CG  1 
ATOM   26213 S  SD  . MET   B 1 1546 ? 39.52200   39.67400  2.84800   1.000 61.26601  ?  1544 MET   B SD  1 
ATOM   26214 C  CE  . MET   B 1 1546 ? 39.59900   39.19100  4.57000   1.000 42.97169  ?  1544 MET   B CE  1 
ATOM   26215 N  N   . TYR   B 1 1547 ? 37.65400   45.10600  4.37400   1.000 59.02927  ?  1545 TYR   B N   1 
ATOM   26216 C  CA  . TYR   B 1 1547 ? 38.05800   46.45300  4.75200   1.000 48.88153  ?  1545 TYR   B CA  1 
ATOM   26217 C  C   . TYR   B 1 1547 ? 38.88800   46.40200  6.02400   1.000 57.26384  ?  1545 TYR   B C   1 
ATOM   26218 O  O   . TYR   B 1 1547 ? 38.58600   45.63600  6.94400   1.000 63.63863  ?  1545 TYR   B O   1 
ATOM   26219 C  CB  . TYR   B 1 1547 ? 36.84800   47.37500  4.97300   1.000 45.20338  ?  1545 TYR   B CB  1 
ATOM   26220 C  CG  . TYR   B 1 1547 ? 35.89500   47.44200  3.80400   1.000 62.51778  ?  1545 TYR   B CG  1 
ATOM   26221 C  CD1 . TYR   B 1 1547 ? 36.23600   48.12100  2.64300   1.000 62.86037  ?  1545 TYR   B CD1 1 
ATOM   26222 C  CD2 . TYR   B 1 1547 ? 34.64800   46.83300  3.86600   1.000 58.03949  ?  1545 TYR   B CD2 1 
ATOM   26223 C  CE1 . TYR   B 1 1547 ? 35.36400   48.18500  1.57100   1.000 68.49641  ?  1545 TYR   B CE1 1 
ATOM   26224 C  CE2 . TYR   B 1 1547 ? 33.77100   46.89200  2.80100   1.000 58.84991  ?  1545 TYR   B CE2 1 
ATOM   26225 C  CZ  . TYR   B 1 1547 ? 34.13300   47.56900  1.65700   1.000 63.56787  ?  1545 TYR   B CZ  1 
ATOM   26226 O  OH  . TYR   B 1 1547 ? 33.25800   47.62600  0.59700   1.000 73.01547  ?  1545 TYR   B OH  1 
ATOM   26227 N  N   . ILE   B 1 1548 ? 39.93000   47.22500  6.07100   1.000 55.81878  ?  1546 ILE   B N   1 
ATOM   26228 C  CA  . ILE   B 1 1548 ? 40.76600   47.38500  7.25400   1.000 55.45159  ?  1546 ILE   B CA  1 
ATOM   26229 C  C   . ILE   B 1 1548 ? 40.53500   48.79500  7.77900   1.000 61.63565  ?  1546 ILE   B C   1 
ATOM   26230 O  O   . ILE   B 1 1548 ? 40.95000   49.77900  7.15300   1.000 62.56369  ?  1546 ILE   B O   1 
ATOM   26231 C  CB  . ILE   B 1 1548 ? 42.24800   47.13200  6.94700   1.000 47.62667  ?  1546 ILE   B CB  1 
ATOM   26232 C  CG1 . ILE   B 1 1548 ? 42.47300   45.65500  6.61900   1.000 54.94699  ?  1546 ILE   B CG1 1 
ATOM   26233 C  CG2 . ILE   B 1 1548 ? 43.10500   47.53700  8.12500   1.000 46.50080  ?  1546 ILE   B CG2 1 
ATOM   26234 C  CD1 . ILE   B 1 1548 ? 43.81900   45.35700  6.00800   1.000 40.91417  ?  1546 ILE   B CD1 1 
ATOM   26235 N  N   . ILE   B 1 1549 ? 39.86600   48.89700  8.92300   1.000 63.26158  ?  1547 ILE   B N   1 
ATOM   26236 C  CA  . ILE   B 1 1549 ? 39.46200   50.18100  9.47600   1.000 61.01434  ?  1547 ILE   B CA  1 
ATOM   26237 C  C   . ILE   B 1 1549 ? 40.19900   50.43000  10.78600  1.000 61.04379  ?  1547 ILE   B C   1 
ATOM   26238 O  O   . ILE   B 1 1549 ? 40.65800   49.50600  11.46500  1.000 52.47847  ?  1547 ILE   B O   1 
ATOM   26239 C  CB  . ILE   B 1 1549 ? 37.93500   50.26000  9.68700   1.000 56.39011  ?  1547 ILE   B CB  1 
ATOM   26240 C  CG1 . ILE   B 1 1549 ? 37.48400   49.20700  10.69900  1.000 52.86723  ?  1547 ILE   B CG1 1 
ATOM   26241 C  CG2 . ILE   B 1 1549 ? 37.20200   50.08200  8.36600   1.000 63.05895  ?  1547 ILE   B CG2 1 
ATOM   26242 C  CD1 . ILE   B 1 1549 ? 36.00300   49.24200  10.99300  1.000 51.22336  ?  1547 ILE   B CD1 1 
ATOM   26243 N  N   . ASN   B 1 1550 ? 40.31000   51.71000  11.13600  1.000 70.91209  ?  1548 ASN   B N   1 
ATOM   26244 C  CA  . ASN   B 1 1550 ? 40.89000   52.12300  12.40200  1.000 75.81343  ?  1548 ASN   B CA  1 
ATOM   26245 C  C   . ASN   B 1 1550 ? 39.81500   52.11200  13.48700  1.000 73.94348  ?  1548 ASN   B C   1 
ATOM   26246 O  O   . ASN   B 1 1550 ? 38.66400   51.73400  13.25400  1.000 75.34431  ?  1548 ASN   B O   1 
ATOM   26247 C  CB  . ASN   B 1 1550 ? 41.54200   53.50000  12.26900  1.000 76.93423  ?  1548 ASN   B CB  1 
ATOM   26248 C  CG  . ASN   B 1 1550 ? 40.53500   54.63800  12.33100  1.000 72.84824  ?  1548 ASN   B CG  1 
ATOM   26249 O  OD1 . ASN   B 1 1550 ? 39.50000   54.60800  11.66300  1.000 62.84720  ?  1548 ASN   B OD1 1 
ATOM   26250 N  ND2 . ASN   B 1 1550 ? 40.84300   55.65400  13.12800  1.000 69.93940  ?  1548 ASN   B ND2 1 
ATOM   26251 N  N   . ARG   B 1 1551 ? 40.19100   52.54700  14.69100  1.000 63.14342  ?  1549 ARG   B N   1 
ATOM   26252 C  CA  . ARG   B 1 1551 ? 39.27400   52.48400  15.82300  1.000 65.04054  ?  1549 ARG   B CA  1 
ATOM   26253 C  C   . ARG   B 1 1551 ? 38.09200   53.43500  15.69700  1.000 61.77824  ?  1549 ARG   B C   1 
ATOM   26254 O  O   . ARG   B 1 1551 ? 37.17700   53.36200  16.52300  1.000 74.17623  ?  1549 ARG   B O   1 
ATOM   26255 C  CB  . ARG   B 1 1551 ? 40.01800   52.77500  17.12400  1.000 62.48792  ?  1549 ARG   B CB  1 
ATOM   26256 C  CG  . ARG   B 1 1551 ? 41.52000   52.59200  17.04900  1.000 81.84232  ?  1549 ARG   B CG  1 
ATOM   26257 C  CD  . ARG   B 1 1551 ? 42.16400   52.96700  18.37300  1.000 96.77162  ?  1549 ARG   B CD  1 
ATOM   26258 N  NE  . ARG   B 1 1551 ? 42.10000   54.40300  18.62300  1.000 94.52286  ?  1549 ARG   B NE  1 
ATOM   26259 C  CZ  . ARG   B 1 1551 ? 41.21100   54.99000  19.41300  1.000 99.81280  ?  1549 ARG   B CZ  1 
ATOM   26260 N  NH1 . ARG   B 1 1551 ? 40.28800   54.29200  20.05500  1.000 101.42761 ?  1549 ARG   B NH1 1 
ATOM   26261 N  NH2 . ARG   B 1 1551 ? 41.24700   56.31100  19.56100  1.000 84.02154  ?  1549 ARG   B NH2 1 
ATOM   26262 N  N   . HIS   B 1 1552 ? 38.08000   54.31900  14.70200  1.000 64.38680  ?  1550 HIS   B N   1 
ATOM   26263 C  CA  . HIS   B 1 1552 ? 36.96700   55.23500  14.49500  1.000 64.82585  ?  1550 HIS   B CA  1 
ATOM   26264 C  C   . HIS   B 1 1552 ? 36.15900   54.89700  13.25000  1.000 61.07624  ?  1550 HIS   B C   1 
ATOM   26265 O  O   . HIS   B 1 1552 ? 35.33000   55.70700  12.82200  1.000 61.32999  ?  1550 HIS   B O   1 
ATOM   26266 C  CB  . HIS   B 1 1552 ? 37.47400   56.67700  14.42500  1.000 69.17620  ?  1550 HIS   B CB  1 
ATOM   26267 C  CG  . HIS   B 1 1552 ? 38.23500   57.10700  15.64000  1.000 70.24034  ?  1550 HIS   B CG  1 
ATOM   26268 N  ND1 . HIS   B 1 1552 ? 37.64500   57.25300  16.87600  1.000 76.10008  ?  1550 HIS   B ND1 1 
ATOM   26269 C  CD2 . HIS   B 1 1552 ? 39.54400   57.41100  15.81100  1.000 75.53911  ?  1550 HIS   B CD2 1 
ATOM   26270 C  CE1 . HIS   B 1 1552 ? 38.55500   57.63300  17.75500  1.000 71.45034  ?  1550 HIS   B CE1 1 
ATOM   26271 N  NE2 . HIS   B 1 1552 ? 39.71600   57.73600  17.13500  1.000 74.08995  ?  1550 HIS   B NE2 1 
ATOM   26272 N  N   . GLY   B 1 1553 ? 36.38000   53.72500  12.66100  1.000 58.40110  ?  1551 GLY   B N   1 
ATOM   26273 C  CA  . GLY   B 1 1553 ? 35.59000   53.30400  11.52200  1.000 61.11575  ?  1551 GLY   B CA  1 
ATOM   26274 C  C   . GLY   B 1 1553 ? 35.96300   53.95100  10.21000  1.000 65.27851  ?  1551 GLY   B C   1 
ATOM   26275 O  O   . GLY   B 1 1553 ? 35.11100   54.07500  9.32400   1.000 60.26465  ?  1551 GLY   B O   1 
ATOM   26276 N  N   . GLN   B 1 1554 ? 37.21100   54.37500  10.05600  1.000 77.25401  ?  1552 GLN   B N   1 
ATOM   26277 C  CA  . GLN   B 1 1554 ? 37.69200   54.96500  8.81800   1.000 78.14268  ?  1552 GLN   B CA  1 
ATOM   26278 C  C   . GLN   B 1 1554 ? 38.65600   54.00200  8.14400   1.000 64.78826  ?  1552 GLN   B C   1 
ATOM   26279 O  O   . GLN   B 1 1554 ? 39.46000   53.34600  8.81600   1.000 58.72053  ?  1552 GLN   B O   1 
ATOM   26280 C  CB  . GLN   B 1 1554 ? 38.38400   56.30600  9.07600   1.000 77.42914  ?  1552 GLN   B CB  1 
ATOM   26281 C  CG  . GLN   B 1 1554 ? 37.55900   57.27600  9.90200   1.000 76.73545  ?  1552 GLN   B CG  1 
ATOM   26282 C  CD  . GLN   B 1 1554 ? 38.32000   58.54000  10.24300  1.000 82.90597  ?  1552 GLN   B CD  1 
ATOM   26283 O  OE1 . GLN   B 1 1554 ? 39.45300   58.48700  10.72100  1.000 85.79548  ?  1552 GLN   B OE1 1 
ATOM   26284 N  NE2 . GLN   B 1 1554 ? 37.69900   59.68700  9.99500   1.000 78.87697  ?  1552 GLN   B NE2 1 
ATOM   26285 N  N   . LEU   B 1 1555 ? 38.56300   53.91500  6.81900   1.000 57.38253  ?  1553 LEU   B N   1 
ATOM   26286 C  CA  . LEU   B 1 1555 ? 39.44700   53.04000  6.06400   1.000 57.65790  ?  1553 LEU   B CA  1 
ATOM   26287 C  C   . LEU   B 1 1555 ? 40.90200   53.36800  6.37600   1.000 58.93397  ?  1553 LEU   B C   1 
ATOM   26288 O  O   . LEU   B 1 1555 ? 41.25300   54.52000  6.64000   1.000 69.47228  ?  1553 LEU   B O   1 
ATOM   26289 C  CB  . LEU   B 1 1555 ? 39.17000   53.18100  4.56500   1.000 62.35814  ?  1553 LEU   B CB  1 
ATOM   26290 C  CG  . LEU   B 1 1555 ? 39.72500   52.10600  3.62800   1.000 74.90678  ?  1553 LEU   B CG  1 
ATOM   26291 C  CD1 . LEU   B 1 1555 ? 39.63500   50.72300  4.26700   1.000 62.95056  ?  1553 LEU   B CD1 1 
ATOM   26292 C  CD2 . LEU   B 1 1555 ? 38.98800   52.13800  2.29300   1.000 51.50471  ?  1553 LEU   B CD2 1 
ATOM   26293 N  N   . GLN   B 1 1556 ? 41.74300   52.33500  6.40100   1.000 54.19421  ?  1554 GLN   B N   1 
ATOM   26294 C  CA  . GLN   B 1 1556 ? 43.15300   52.61900  6.60700   1.000 49.68811  ?  1554 GLN   B CA  1 
ATOM   26295 C  C   . GLN   B 1 1556 ? 43.90200   52.54200  5.28400   1.000 52.18374  ?  1554 GLN   B C   1 
ATOM   26296 O  O   . GLN   B 1 1556 ? 43.48600   51.82100  4.37100   1.000 58.15304  ?  1554 GLN   B O   1 
ATOM   26297 C  CB  . GLN   B 1 1556 ? 43.77000   51.62900  7.59900   1.000 50.85525  ?  1554 GLN   B CB  1 
ATOM   26298 C  CG  . GLN   B 1 1556 ? 43.24500   51.75200  9.01800   1.000 58.13440  ?  1554 GLN   B CG  1 
ATOM   26299 C  CD  . GLN   B 1 1556 ? 44.05200   52.72100  9.85800   1.000 65.91733  ?  1554 GLN   B CD  1 
ATOM   26300 O  OE1 . GLN   B 1 1556 ? 44.06700   53.92400  9.60000   1.000 80.50287  ?  1554 GLN   B OE1 1 
ATOM   26301 N  NE2 . GLN   B 1 1556 ? 44.73200   52.19700  10.87000  1.000 65.28912  ?  1554 GLN   B NE2 1 
ATOM   26302 N  N   . PRO   B 1 1557 ? 45.00300   53.28500  5.12900   1.000 54.63871  ?  1555 PRO   B N   1 
ATOM   26303 C  CA  . PRO   B 1 1557 ? 45.79200   53.16800  3.89800   1.000 58.32707  ?  1555 PRO   B CA  1 
ATOM   26304 C  C   . PRO   B 1 1557 ? 46.82100   52.05400  3.98200   1.000 51.57771  ?  1555 PRO   B C   1 
ATOM   26305 O  O   . PRO   B 1 1557 ? 46.95000   51.38100  5.00900   1.000 44.16387  ?  1555 PRO   B O   1 
ATOM   26306 C  CB  . PRO   B 1 1557 ? 46.45600   54.54300  3.78100   1.000 66.17643  ?  1555 PRO   B CB  1 
ATOM   26307 C  CG  . PRO   B 1 1557 ? 46.65300   54.95900  5.20000   1.000 68.67307  ?  1555 PRO   B CG  1 
ATOM   26308 C  CD  . PRO   B 1 1557 ? 45.51100   54.35800  6.00200   1.000 63.58847  ?  1555 PRO   B CD  1 
ATOM   26309 N  N   . ILE   B 1 1558 ? 47.56000   51.86000  2.89200   1.000 45.56973  ?  1556 ILE   B N   1 
ATOM   26310 C  CA  . ILE   B 1 1558 ? 48.54100   50.78800  2.82300   1.000 45.11303  ?  1556 ILE   B CA  1 
ATOM   26311 C  C   . ILE   B 1 1558 ? 49.55500   50.94200  3.94500   1.000 52.65392  ?  1556 ILE   B C   1 
ATOM   26312 O  O   . ILE   B 1 1558 ? 50.08200   52.03600  4.18300   1.000 73.95508  ?  1556 ILE   B O   1 
ATOM   26313 C  CB  . ILE   B 1 1558 ? 49.21800   50.81500  1.45000   1.000 45.61435  ?  1556 ILE   B CB  1 
ATOM   26314 C  CG1 . ILE   B 1 1558 ? 48.13500   50.74000  0.36800   1.000 42.69110  ?  1556 ILE   B CG1 1 
ATOM   26315 C  CG2 . ILE   B 1 1558 ? 50.27700   49.71500  1.36700   1.000 61.91538  ?  1556 ILE   B CG2 1 
ATOM   26316 C  CD1 . ILE   B 1 1558 ? 48.59600   50.21100  -0.95600  1.000 48.57290  ?  1556 ILE   B CD1 1 
ATOM   26317 N  N   . GLY   B 1 1559 ? 49.82700   49.84700  4.64800   1.000 47.34855  ?  1557 GLY   B N   1 
ATOM   26318 C  CA  . GLY   B 1 1559 ? 50.84200   49.85500  5.68100   1.000 36.08552  ?  1557 GLY   B CA  1 
ATOM   26319 C  C   . GLY   B 1 1559 ? 50.30000   50.03700  7.08400   1.000 53.10116  ?  1557 GLY   B C   1 
ATOM   26320 O  O   . GLY   B 1 1559 ? 50.76300   49.37700  8.01900   1.000 65.50591  ?  1557 GLY   B O   1 
ATOM   26321 N  N   . VAL   B 1 1560 ? 49.32000   50.92100  7.24500   1.000 48.42890  ?  1558 VAL   B N   1 
ATOM   26322 C  CA  . VAL   B 1 1560 ? 48.78100   51.24900  8.56400   1.000 56.32046  ?  1558 VAL   B CA  1 
ATOM   26323 C  C   . VAL   B 1 1560 ? 47.88800   50.11200  9.05000   1.000 57.99463  ?  1558 VAL   B C   1 
ATOM   26324 O  O   . VAL   B 1 1560 ? 46.87700   49.79700  8.40500   1.000 51.92886  ?  1558 VAL   B O   1 
ATOM   26325 C  CB  . VAL   B 1 1560 ? 48.01600   52.58200  8.53600   1.000 56.73544  ?  1558 VAL   B CB  1 
ATOM   26326 C  CG1 . VAL   B 1 1560 ? 47.78200   53.08400  9.94800   1.000 58.21938  ?  1558 VAL   B CG1 1 
ATOM   26327 C  CG2 . VAL   B 1 1560 ? 48.78400   53.61500  7.72800   1.000 56.32234  ?  1558 VAL   B CG2 1 
ATOM   26328 N  N   . PRO   B 1 1561 ? 48.22000   49.47200  10.17100  1.000 60.61886  ?  1559 PRO   B N   1 
ATOM   26329 C  CA  . PRO   B 1 1561 ? 47.41600   48.34000  10.64400  1.000 51.17746  ?  1559 PRO   B CA  1 
ATOM   26330 C  C   . PRO   B 1 1561 ? 46.05400   48.77500  11.15900  1.000 53.49287  ?  1559 PRO   B C   1 
ATOM   26331 O  O   . PRO   B 1 1561 ? 45.87500   49.88200  11.67100  1.000 64.98289  ?  1559 PRO   B O   1 
ATOM   26332 C  CB  . PRO   B 1 1561 ? 48.26600   47.74700  11.77600  1.000 30.88371  ?  1559 PRO   B CB  1 
ATOM   26333 C  CG  . PRO   B 1 1561 ? 49.64200   48.27800  11.55200  1.000 49.35187  ?  1559 PRO   B CG  1 
ATOM   26334 C  CD  . PRO   B 1 1561 ? 49.44600   49.64100  10.96600  1.000 69.98531  ?  1559 PRO   B CD  1 
ATOM   26335 N  N   . GLY   B 1 1562 ? 45.09100   47.87200  11.02300  1.000 67.06407  ?  1560 GLY   B N   1 
ATOM   26336 C  CA  . GLY   B 1 1562 ? 43.75500   48.09100  11.52500  1.000 60.78016  ?  1560 GLY   B CA  1 
ATOM   26337 C  C   . GLY   B 1 1562 ? 43.02900   46.77100  11.65800  1.000 62.47943  ?  1560 GLY   B C   1 
ATOM   26338 O  O   . GLY   B 1 1562 ? 43.61000   45.70000  11.47000  1.000 66.10757  ?  1560 GLY   B O   1 
ATOM   26339 N  N   . GLU   B 1 1563 ? 41.74200   46.85800  11.98500  1.000 57.94032  ?  1561 GLU   B N   1 
ATOM   26340 C  CA  . GLU   B 1 1563 ? 40.92100   45.67100  12.18000  1.000 56.99421  ?  1561 GLU   B CA  1 
ATOM   26341 C  C   . GLU   B 1 1563 ? 40.34800   45.20400  10.84900  1.000 61.32902  ?  1561 GLU   B C   1 
ATOM   26342 O  O   . GLU   B 1 1563 ? 39.74100   45.99000  10.11500  1.000 60.93373  ?  1561 GLU   B O   1 
ATOM   26343 C  CB  . GLU   B 1 1563 ? 39.78500   45.94100  13.16700  1.000 73.33706  ?  1561 GLU   B CB  1 
ATOM   26344 C  CG  . GLU   B 1 1563 ? 38.96900   44.69700  13.50400  1.000 78.48706  ?  1561 GLU   B CG  1 
ATOM   26345 C  CD  . GLU   B 1 1563 ? 37.86200   44.96400  14.50800  1.000 75.18268  ?  1561 GLU   B CD  1 
ATOM   26346 O  OE1 . GLU   B 1 1563 ? 38.16500   45.14300  15.70600  1.000 84.20641  ?  1561 GLU   B OE1 1 
ATOM   26347 O  OE2 . GLU   B 1 1563 ? 36.68300   44.99000  14.10200  1.000 81.63549  -1 1561 GLU   B OE2 1 
ATOM   26348 N  N   . LEU   B 1 1564 ? 40.53500   43.92200  10.55100  1.000 55.43731  ?  1562 LEU   B N   1 
ATOM   26349 C  CA  . LEU   B 1 1564 ? 39.98600   43.34800  9.33200   1.000 58.83707  ?  1562 LEU   B CA  1 
ATOM   26350 C  C   . LEU   B 1 1564 ? 38.46700   43.25400  9.42800   1.000 55.13906  ?  1562 LEU   B C   1 
ATOM   26351 O  O   . LEU   B 1 1564 ? 37.91800   42.84700  10.45600  1.000 48.24752  ?  1562 LEU   B O   1 
ATOM   26352 C  CB  . LEU   B 1 1564 ? 40.59500   41.97000  9.08700   1.000 47.23653  ?  1562 LEU   B CB  1 
ATOM   26353 C  CG  . LEU   B 1 1564 ? 40.44400   41.35000  7.70000   1.000 50.01327  ?  1562 LEU   B CG  1 
ATOM   26354 C  CD1 . LEU   B 1 1564 ? 40.58900   42.40100  6.59900   1.000 51.23225  ?  1562 LEU   B CD1 1 
ATOM   26355 C  CD2 . LEU   B 1 1564 ? 41.46800   40.23600  7.53800   1.000 29.63069  ?  1562 LEU   B CD2 1 
ATOM   26356 N  N   . CYS   B 1 1565 ? 37.78400   43.64300  8.35200   1.000 48.17726  ?  1563 CYS   B N   1 
ATOM   26357 C  CA  . CYS   B 1 1565 ? 36.32600   43.64200  8.32300   1.000 49.59810  ?  1563 CYS   B CA  1 
ATOM   26358 C  C   . CYS   B 1 1565 ? 35.84400   43.11700  6.98000   1.000 54.41545  ?  1563 CYS   B C   1 
ATOM   26359 O  O   . CYS   B 1 1565 ? 36.31400   43.56900  5.93300   1.000 65.37369  ?  1563 CYS   B O   1 
ATOM   26360 C  CB  . CYS   B 1 1565 ? 35.76300   45.04500  8.57900   1.000 50.96806  ?  1563 CYS   B CB  1 
ATOM   26361 S  SG  . CYS   B 1 1565 ? 36.02000   45.65200  10.26600  1.000 62.08815  ?  1563 CYS   B SG  1 
ATOM   26362 N  N   . ILE   B 1 1566 ? 34.90300   42.17500  7.01200   1.000 54.37592  ?  1564 ILE   B N   1 
ATOM   26363 C  CA  . ILE   B 1 1566 ? 34.45900   41.47300  5.81300   1.000 60.87032  ?  1564 ILE   B CA  1 
ATOM   26364 C  C   . ILE   B 1 1566 ? 33.02300   41.86200  5.48700   1.000 51.55198  ?  1564 ILE   B C   1 
ATOM   26365 O  O   . ILE   B 1 1566 ? 32.23300   42.22200  6.36600   1.000 52.13437  ?  1564 ILE   B O   1 
ATOM   26366 C  CB  . ILE   B 1 1566 ? 34.57600   39.94000  5.96400   1.000 47.86927  ?  1564 ILE   B CB  1 
ATOM   26367 C  CG1 . ILE   B 1 1566 ? 35.39100   39.57600  7.21200   1.000 47.70042  ?  1564 ILE   B CG1 1 
ATOM   26368 C  CG2 . ILE   B 1 1566 ? 35.16000   39.31800  4.69700   1.000 49.21969  ?  1564 ILE   B CG2 1 
ATOM   26369 C  CD1 . ILE   B 1 1566 ? 36.81700   39.14700  6.92400   1.000 57.15985  ?  1564 ILE   B CD1 1 
ATOM   26370 N  N   . ALA   B 1 1567 ? 32.68700   41.77200  4.20200   1.000 54.34473  ?  1565 ALA   B N   1 
ATOM   26371 C  CA  . ALA   B 1 1567 ? 31.33100   42.01000  3.73200   1.000 56.70228  ?  1565 ALA   B CA  1 
ATOM   26372 C  C   . ALA   B 1 1567 ? 31.14200   41.28400  2.41000   1.000 65.93879  ?  1565 ALA   B C   1 
ATOM   26373 O  O   . ALA   B 1 1567 ? 32.10800   40.86200  1.77000   1.000 65.72728  ?  1565 ALA   B O   1 
ATOM   26374 C  CB  . ALA   B 1 1567 ? 31.04100   43.50500  3.56700   1.000 71.66973  ?  1565 ALA   B CB  1 
ATOM   26375 N  N   . GLY   B 1 1568 ? 29.88700   41.15000  2.00600   1.000 62.45205  ?  1566 GLY   B N   1 
ATOM   26376 C  CA  . GLY   B 1 1568 ? 29.56200   40.52300  0.74700   1.000 58.37755  ?  1566 GLY   B CA  1 
ATOM   26377 C  C   . GLY   B 1 1568 ? 28.35900   39.61800  0.89200   1.000 66.27492  ?  1566 GLY   B C   1 
ATOM   26378 O  O   . GLY   B 1 1568 ? 27.61000   39.70900  1.86400   1.000 65.57036  ?  1566 GLY   B O   1 
ATOM   26379 N  N   . ALA   B 1 1569 ? 28.19000   38.73200  -0.09400  1.000 61.68154  ?  1567 ALA   B N   1 
ATOM   26380 C  CA  . ALA   B 1 1569 ? 27.03300   37.84200  -0.12500  1.000 56.68463  ?  1567 ALA   B CA  1 
ATOM   26381 C  C   . ALA   B 1 1569 ? 27.16100   36.70000  0.87900   1.000 61.22327  ?  1567 ALA   B C   1 
ATOM   26382 O  O   . ALA   B 1 1569 ? 26.16400   36.29800  1.49200   1.000 72.11049  ?  1567 ALA   B O   1 
ATOM   26383 C  CB  . ALA   B 1 1569 ? 26.83700   37.29000  -1.53700  1.000 66.89906  ?  1567 ALA   B CB  1 
ATOM   26384 N  N   . SER   B 1 1570 ? 28.36700   36.16700  1.05900   1.000 60.78534  ?  1568 SER   B N   1 
ATOM   26385 C  CA  . SER   B 1 1570 ? 28.61600   35.05200  1.97300   1.000 67.55448  ?  1568 SER   B CA  1 
ATOM   26386 C  C   . SER   B 1 1570 ? 28.82700   35.50100  3.41200   1.000 57.96581  ?  1568 SER   B C   1 
ATOM   26387 O  O   . SER   B 1 1570 ? 29.58900   34.88800  4.16500   1.000 53.27933  ?  1568 SER   B O   1 
ATOM   26388 C  CB  . SER   B 1 1570 ? 29.80300   34.24000  1.47000   1.000 67.68958  ?  1568 SER   B CB  1 
ATOM   26389 O  OG  . SER   B 1 1570 ? 29.75000   34.11200  0.06100   1.000 75.42850  ?  1568 SER   B OG  1 
ATOM   26390 N  N   . LEU   B 1 1571 ? 28.15100   36.56800  3.83100   1.000 49.22266  ?  1569 LEU   B N   1 
ATOM   26391 C  CA  . LEU   B 1 1571 ? 28.24400   37.05100  5.20200   1.000 58.96126  ?  1569 LEU   B CA  1 
ATOM   26392 C  C   . LEU   B 1 1571 ? 27.16200   36.39500  6.05000   1.000 61.19169  ?  1569 LEU   B C   1 
ATOM   26393 O  O   . LEU   B 1 1571 ? 26.03000   36.20900  5.59300   1.000 72.23969  ?  1569 LEU   B O   1 
ATOM   26394 C  CB  . LEU   B 1 1571 ? 28.10300   38.57400  5.23500   1.000 64.98647  ?  1569 LEU   B CB  1 
ATOM   26395 C  CG  . LEU   B 1 1571 ? 28.77500   39.31800  6.38900   1.000 70.57910  ?  1569 LEU   B CG  1 
ATOM   26396 C  CD1 . LEU   B 1 1571 ? 30.28900   39.18200  6.30500   1.000 51.22395  ?  1569 LEU   B CD1 1 
ATOM   26397 C  CD2 . LEU   B 1 1571 ? 28.36000   40.78000  6.36700   1.000 66.39534  ?  1569 LEU   B CD2 1 
ATOM   26398 N  N   . ALA   B 1 1572 ? 27.51500   36.04100  7.28500   1.000 57.74790  ?  1570 ALA   B N   1 
ATOM   26399 C  CA  . ALA   B 1 1572 ? 26.59200   35.32000  8.15400   1.000 62.13705  ?  1570 ALA   B CA  1 
ATOM   26400 C  C   . ALA   B 1 1572 ? 25.36000   36.16000  8.47700   1.000 67.66175  ?  1570 ALA   B C   1 
ATOM   26401 O  O   . ALA   B 1 1572 ? 25.39700   37.39400  8.46400   1.000 79.82870  ?  1570 ALA   B O   1 
ATOM   26402 C  CB  . ALA   B 1 1572 ? 27.28400   34.90700  9.45200   1.000 55.42671  ?  1570 ALA   B CB  1 
ATOM   26403 N  N   . ARG   B 1 1573 ? 24.25400   35.47100  8.77000   1.000 64.48274  ?  1571 ARG   B N   1 
ATOM   26404 C  CA  . ARG   B 1 1573 ? 23.02800   36.15200  9.16700   1.000 55.61119  ?  1571 ARG   B CA  1 
ATOM   26405 C  C   . ARG   B 1 1573 ? 23.08500   36.66100  10.60100  1.000 60.26681  ?  1571 ARG   B C   1 
ATOM   26406 O  O   . ARG   B 1 1573 ? 22.25500   37.49200  10.98500  1.000 75.47696  ?  1571 ARG   B O   1 
ATOM   26407 C  CB  . ARG   B 1 1573 ? 21.82400   35.22200  8.99200   1.000 51.06641  ?  1571 ARG   B CB  1 
ATOM   26408 C  CG  . ARG   B 1 1573 ? 20.49500   35.96300  8.93400   1.000 64.35790  ?  1571 ARG   B CG  1 
ATOM   26409 C  CD  . ARG   B 1 1573 ? 19.31400   35.06700  9.25700   1.000 55.59983  ?  1571 ARG   B CD  1 
ATOM   26410 N  NE  . ARG   B 1 1573 ? 18.82800   34.34000  8.09100   1.000 65.15491  ?  1571 ARG   B NE  1 
ATOM   26411 C  CZ  . ARG   B 1 1573 ? 17.82800   33.47000  8.12000   1.000 63.88277  ?  1571 ARG   B CZ  1 
ATOM   26412 N  NH1 . ARG   B 1 1573 ? 17.19500   33.18300  9.24600   1.000 54.13669  ?  1571 ARG   B NH1 1 
ATOM   26413 N  NH2 . ARG   B 1 1573 ? 17.45900   32.86600  6.99200   1.000 44.39668  ?  1571 ARG   B NH2 1 
ATOM   26414 N  N   . GLY   B 1 1574 ? 24.04300   36.19100  11.39400  1.000 45.18201  ?  1572 GLY   B N   1 
ATOM   26415 C  CA  . GLY   B 1 1574 ? 24.23400   36.63400  12.75400  1.000 45.21359  ?  1572 GLY   B CA  1 
ATOM   26416 C  C   . GLY   B 1 1574 ? 24.41900   35.45900  13.68200  1.000 52.61529  ?  1572 GLY   B C   1 
ATOM   26417 O  O   . GLY   B 1 1574 ? 24.50800   34.30200  13.25600  1.000 65.05199  ?  1572 GLY   B O   1 
ATOM   26418 N  N   . TYR   B 1 1575 ? 24.48300   35.75500  14.97600  1.000 42.89144  ?  1573 TYR   B N   1 
ATOM   26419 C  CA  . TYR   B 1 1575 ? 24.61600   34.72900  15.99600  1.000 58.97908  ?  1573 TYR   B CA  1 
ATOM   26420 C  C   . TYR   B 1 1575 ? 23.24100   34.22400  16.42900  1.000 81.66250  ?  1573 TYR   B C   1 
ATOM   26421 O  O   . TYR   B 1 1575 ? 22.22600   34.91500  16.30200  1.000 84.96258  ?  1573 TYR   B O   1 
ATOM   26422 C  CB  . TYR   B 1 1575 ? 25.39900   35.26200  17.19800  1.000 49.71984  ?  1573 TYR   B CB  1 
ATOM   26423 C  CG  . TYR   B 1 1575 ? 26.80600   35.69400  16.84600  1.000 69.08511  ?  1573 TYR   B CG  1 
ATOM   26424 C  CD1 . TYR   B 1 1575 ? 27.81800   34.75900  16.67400  1.000 68.87344  ?  1573 TYR   B CD1 1 
ATOM   26425 C  CD2 . TYR   B 1 1575 ? 27.12000   37.03600  16.67300  1.000 81.09159  ?  1573 TYR   B CD2 1 
ATOM   26426 C  CE1 . TYR   B 1 1575 ? 29.10600   35.14800  16.34500  1.000 62.10997  ?  1573 TYR   B CE1 1 
ATOM   26427 C  CE2 . TYR   B 1 1575 ? 28.40500   37.43500  16.34400  1.000 63.90062  ?  1573 TYR   B CE2 1 
ATOM   26428 C  CZ  . TYR   B 1 1575 ? 29.39300   36.48600  16.18100  1.000 63.37532  ?  1573 TYR   B CZ  1 
ATOM   26429 O  OH  . TYR   B 1 1575 ? 30.67400   36.87200  15.85500  1.000 62.14689  ?  1573 TYR   B OH  1 
ATOM   26430 N  N   . LEU   B 1 1576 ? 23.22200   32.99700  16.94000  1.000 78.74476  ?  1574 LEU   B N   1 
ATOM   26431 C  CA  . LEU   B 1 1576 ? 21.98400   32.30900  17.27800  1.000 70.11101  ?  1574 LEU   B CA  1 
ATOM   26432 C  C   . LEU   B 1 1576 ? 21.53600   32.70500  18.67900  1.000 84.21589  ?  1574 LEU   B C   1 
ATOM   26433 O  O   . LEU   B 1 1576 ? 22.23100   32.42200  19.66200  1.000 82.22048  ?  1574 LEU   B O   1 
ATOM   26434 C  CB  . LEU   B 1 1576 ? 22.17700   30.79800  17.17800  1.000 82.06748  ?  1574 LEU   B CB  1 
ATOM   26435 C  CG  . LEU   B 1 1576 ? 20.93300   29.91400  17.21000  1.000 67.21452  ?  1574 LEU   B CG  1 
ATOM   26436 C  CD1 . LEU   B 1 1576 ? 20.14300   30.04900  15.92600  1.000 49.11899  ?  1574 LEU   B CD1 1 
ATOM   26437 C  CD2 . LEU   B 1 1576 ? 21.36300   28.47700  17.41300  1.000 67.21274  ?  1574 LEU   B CD2 1 
ATOM   26438 N  N   . ASN   B 1 1577 ? 20.37400   33.35700  18.76100  1.000 89.46159  ?  1575 ASN   B N   1 
ATOM   26439 C  CA  . ASN   B 1 1577 ? 19.76500   33.76000  20.03100  1.000 92.14428  ?  1575 ASN   B CA  1 
ATOM   26440 C  C   . ASN   B 1 1577 ? 20.68600   34.67900  20.83400  1.000 95.25035  ?  1575 ASN   B C   1 
ATOM   26441 O  O   . ASN   B 1 1577 ? 20.73200   34.62400  22.06500  1.000 80.18800  ?  1575 ASN   B O   1 
ATOM   26442 C  CB  . ASN   B 1 1577 ? 19.35000   32.54100  20.85800  1.000 85.02497  ?  1575 ASN   B CB  1 
ATOM   26443 C  CG  . ASN   B 1 1577 ? 18.25500   31.73200  20.18800  1.000 97.06276  ?  1575 ASN   B CG  1 
ATOM   26444 O  OD1 . ASN   B 1 1577 ? 18.02900   30.57000  20.52500  1.000 92.60008  ?  1575 ASN   B OD1 1 
ATOM   26445 N  ND2 . ASN   B 1 1577 ? 17.57000   32.34500  19.22800  1.000 80.71358  ?  1575 ASN   B ND2 1 
ATOM   26446 N  N   . ASN   B 1 1578 ? 21.42200   35.53500  20.12700  1.000 90.73256  ?  1576 ASN   B N   1 
ATOM   26447 C  CA  . ASN   B 1 1578 ? 22.23200   36.58700  20.74500  1.000 81.17659  ?  1576 ASN   B CA  1 
ATOM   26448 C  C   . ASN   B 1 1578 ? 22.20400   37.81000  19.84000  1.000 85.40218  ?  1576 ASN   B C   1 
ATOM   26449 O  O   . ASN   B 1 1578 ? 23.19500   38.14100  19.17900  1.000 84.93845  ?  1576 ASN   B O   1 
ATOM   26450 C  CB  . ASN   B 1 1578 ? 23.66500   36.10900  20.99000  1.000 62.33123  ?  1576 ASN   B CB  1 
ATOM   26451 C  CG  . ASN   B 1 1578 ? 24.39500   36.95500  22.02100  1.000 71.69122  ?  1576 ASN   B CG  1 
ATOM   26452 O  OD1 . ASN   B 1 1578 ? 23.90600   38.00600  22.43700  1.000 81.61757  ?  1576 ASN   B OD1 1 
ATOM   26453 N  ND2 . ASN   B 1 1578 ? 25.57300   36.50000  22.43400  1.000 72.14075  ?  1576 ASN   B ND2 1 
ATOM   26454 N  N   . PRO   B 1 1579 ? 21.06600   38.50900  19.78300  1.000 84.22241  ?  1577 PRO   B N   1 
ATOM   26455 C  CA  . PRO   B 1 1579 ? 20.98700   39.70800  18.93300  1.000 78.86410  ?  1577 PRO   B CA  1 
ATOM   26456 C  C   . PRO   B 1 1579 ? 21.87300   40.84100  19.41400  1.000 79.97816  ?  1577 PRO   B C   1 
ATOM   26457 O  O   . PRO   B 1 1579 ? 22.18700   41.73800  18.62000  1.000 67.58368  ?  1577 PRO   B O   1 
ATOM   26458 C  CB  . PRO   B 1 1579 ? 19.50100   40.09400  18.99700  1.000 80.78225  ?  1577 PRO   B CB  1 
ATOM   26459 C  CG  . PRO   B 1 1579 ? 18.80000   38.90300  19.60300  1.000 81.04229  ?  1577 PRO   B CG  1 
ATOM   26460 C  CD  . PRO   B 1 1579 ? 19.80500   38.26100  20.49700  1.000 72.47896  ?  1577 PRO   B CD  1 
ATOM   26461 N  N   . ALA   B 1 1580 ? 22.28000   40.83200  20.68600  1.000 70.55311  ?  1578 ALA   B N   1 
ATOM   26462 C  CA  . ALA   B 1 1580 ? 23.21300   41.83900  21.17900  1.000 69.23203  ?  1578 ALA   B CA  1 
ATOM   26463 C  C   . ALA   B 1 1580 ? 24.57900   41.68500  20.52200  1.000 71.71530  ?  1578 ALA   B C   1 
ATOM   26464 O  O   . ALA   B 1 1580 ? 25.12200   42.64400  19.96200  1.000 84.26650  ?  1578 ALA   B O   1 
ATOM   26465 C  CB  . ALA   B 1 1580 ? 23.33100   41.74500  22.70000  1.000 66.12294  ?  1578 ALA   B CB  1 
ATOM   26466 N  N   . LEU   B 1 1581 ? 25.15100   40.48000  20.58100  1.000 81.27855  ?  1579 LEU   B N   1 
ATOM   26467 C  CA  . LEU   B 1 1581 ? 26.43300   40.24400  19.92700  1.000 79.07056  ?  1579 LEU   B CA  1 
ATOM   26468 C  C   . LEU   B 1 1581 ? 26.31000   40.31300  18.41000  1.000 68.62513  ?  1579 LEU   B C   1 
ATOM   26469 O  O   . LEU   B 1 1581 ? 27.27400   40.68300  17.73000  1.000 66.39987  ?  1579 LEU   B O   1 
ATOM   26470 C  CB  . LEU   B 1 1581 ? 27.00300   38.89300  20.35600  1.000 69.38608  ?  1579 LEU   B CB  1 
ATOM   26471 C  CG  . LEU   B 1 1581 ? 28.52300   38.75200  20.25600  1.000 79.27087  ?  1579 LEU   B CG  1 
ATOM   26472 C  CD1 . LEU   B 1 1581 ? 29.21500   39.70400  21.22300  1.000 75.58998  ?  1579 LEU   B CD1 1 
ATOM   26473 C  CD2 . LEU   B 1 1581 ? 28.94700   37.31300  20.51200  1.000 71.74508  ?  1579 LEU   B CD2 1 
ATOM   26474 N  N   . THR   B 1 1582 ? 25.14200   39.96400  17.86300  1.000 63.13434  ?  1580 THR   B N   1 
ATOM   26475 C  CA  . THR   B 1 1582 ? 24.93400   40.08900  16.42300  1.000 69.68966  ?  1580 THR   B CA  1 
ATOM   26476 C  C   . THR   B 1 1582 ? 24.96500   41.55100  15.99100  1.000 74.69788  ?  1580 THR   B C   1 
ATOM   26477 O  O   . THR   B 1 1582 ? 25.58100   41.89200  14.97500  1.000 72.35459  ?  1580 THR   B O   1 
ATOM   26478 C  CB  . THR   B 1 1582 ? 23.60900   39.43600  16.02100  1.000 69.36307  ?  1580 THR   B CB  1 
ATOM   26479 O  OG1 . THR   B 1 1582 ? 23.74800   38.01000  16.05000  1.000 71.96476  ?  1580 THR   B OG1 1 
ATOM   26480 C  CG2 . THR   B 1 1582 ? 23.19700   39.86300  14.61700  1.000 46.55703  ?  1580 THR   B CG2 1 
ATOM   26481 N  N   . GLU   B 1 1583 ? 24.31500   42.43100  16.75700  1.000 77.75473  ?  1581 GLU   B N   1 
ATOM   26482 C  CA  . GLU   B 1 1583 ? 24.35300   43.85500  16.44200  1.000 79.84731  ?  1581 GLU   B CA  1 
ATOM   26483 C  C   . GLU   B 1 1583 ? 25.73000   44.45300  16.70600  1.000 72.26841  ?  1581 GLU   B C   1 
ATOM   26484 O  O   . GLU   B 1 1583 ? 26.16700   45.34900  15.97500  1.000 61.64657  ?  1581 GLU   B O   1 
ATOM   26485 C  CB  . GLU   B 1 1583 ? 23.28900   44.59900  17.24900  1.000 78.51080  ?  1581 GLU   B CB  1 
ATOM   26486 C  CG  . GLU   B 1 1583 ? 22.10800   45.08800  16.42500  1.000 89.24275  ?  1581 GLU   B CG  1 
ATOM   26487 C  CD  . GLU   B 1 1583 ? 21.43100   46.29600  17.04100  1.000 103.20967 ?  1581 GLU   B CD  1 
ATOM   26488 O  OE1 . GLU   B 1 1583 ? 21.22200   46.30000  18.27300  1.000 92.01945  ?  1581 GLU   B OE1 1 
ATOM   26489 O  OE2 . GLU   B 1 1583 ? 21.10900   47.24200  16.29200  1.000 115.65175 -1 1581 GLU   B OE2 1 
ATOM   26490 N  N   . GLU   B 1 1584 ? 26.42700   43.96800  17.73600  1.000 75.39164  ?  1582 GLU   B N   1 
ATOM   26491 C  CA  . GLU   B 1 1584 ? 27.73400   44.51700  18.07800  1.000 62.55634  ?  1582 GLU   B CA  1 
ATOM   26492 C  C   . GLU   B 1 1584 ? 28.80000   44.11400  17.06500  1.000 67.69055  ?  1582 GLU   B C   1 
ATOM   26493 O  O   . GLU   B 1 1584 ? 29.75000   44.87100  16.83200  1.000 79.59882  ?  1582 GLU   B O   1 
ATOM   26494 C  CB  . GLU   B 1 1584 ? 28.12100   44.07300  19.49200  1.000 59.01805  ?  1582 GLU   B CB  1 
ATOM   26495 C  CG  . GLU   B 1 1584 ? 29.61200   43.95800  19.76200  1.000 66.96773  ?  1582 GLU   B CG  1 
ATOM   26496 C  CD  . GLU   B 1 1584 ? 29.91000   43.60200  21.20500  1.000 86.99543  ?  1582 GLU   B CD  1 
ATOM   26497 O  OE1 . GLU   B 1 1584 ? 28.95300   43.51700  22.00500  1.000 82.70119  ?  1582 GLU   B OE1 1 
ATOM   26498 O  OE2 . GLU   B 1 1584 ? 31.09900   43.40800  21.53900  1.000 81.60445  -1 1582 GLU   B OE2 1 
ATOM   26499 N  N   . LYS   B 1 1585 ? 28.65200   42.94800  16.43500  1.000 63.65970  ?  1583 LYS   B N   1 
ATOM   26500 C  CA  . LYS   B 1 1585 ? 29.65900   42.43700  15.51200  1.000 64.09925  ?  1583 LYS   B CA  1 
ATOM   26501 C  C   . LYS   B 1 1585 ? 29.28900   42.62100  14.04600  1.000 70.14977  ?  1583 LYS   B C   1 
ATOM   26502 O  O   . LYS   B 1 1585 ? 30.17100   42.88600  13.22200  1.000 61.34423  ?  1583 LYS   B O   1 
ATOM   26503 C  CB  . LYS   B 1 1585 ? 29.92500   40.95500  15.79100  1.000 50.70903  ?  1583 LYS   B CB  1 
ATOM   26504 C  CG  . LYS   B 1 1585 ? 30.71700   40.71400  17.06500  1.000 56.45416  ?  1583 LYS   B CG  1 
ATOM   26505 C  CD  . LYS   B 1 1585 ? 31.93600   41.62300  17.12800  1.000 58.30256  ?  1583 LYS   B CD  1 
ATOM   26506 C  CE  . LYS   B 1 1585 ? 33.11300   40.93800  17.80600  1.000 71.56393  ?  1583 LYS   B CE  1 
ATOM   26507 N  NZ  . LYS   B 1 1585 ? 33.12900   41.18300  19.27600  1.000 63.55904  ?  1583 LYS   B NZ  1 
ATOM   26508 N  N   . PHE   B 1 1586 ? 28.01100   42.48200  13.69400  1.000 67.42606  ?  1584 PHE   B N   1 
ATOM   26509 C  CA  . PHE   B 1 1586 ? 27.54400   42.69100  12.32100  1.000 71.70033  ?  1584 PHE   B CA  1 
ATOM   26510 C  C   . PHE   B 1 1586 ? 26.92600   44.08400  12.25800  1.000 70.62395  ?  1584 PHE   B C   1 
ATOM   26511 O  O   . PHE   B 1 1586 ? 25.73200   44.26600  12.49500  1.000 81.48571  ?  1584 PHE   B O   1 
ATOM   26512 C  CB  . PHE   B 1 1586 ? 26.55200   41.60900  11.90600  1.000 78.83516  ?  1584 PHE   B CB  1 
ATOM   26513 C  CG  . PHE   B 1 1586 ? 27.17200   40.25100  11.72200  1.000 78.24679  ?  1584 PHE   B CG  1 
ATOM   26514 C  CD1 . PHE   B 1 1586 ? 27.43400   39.43900  12.81600  1.000 72.37470  ?  1584 PHE   B CD1 1 
ATOM   26515 C  CD2 . PHE   B 1 1586 ? 27.48900   39.78500  10.45600  1.000 71.24144  ?  1584 PHE   B CD2 1 
ATOM   26516 C  CE1 . PHE   B 1 1586 ? 28.00400   38.18900  12.65000  1.000 65.74362  ?  1584 PHE   B CE1 1 
ATOM   26517 C  CE2 . PHE   B 1 1586 ? 28.05900   38.53500  10.28300  1.000 59.32295  ?  1584 PHE   B CE2 1 
ATOM   26518 C  CZ  . PHE   B 1 1586 ? 28.31600   37.73700  11.38100  1.000 64.04729  ?  1584 PHE   B CZ  1 
ATOM   26519 N  N   . THR   B 1 1587 ? 27.75800   45.07900  11.93000  1.000 78.72250  ?  1585 THR   B N   1 
ATOM   26520 C  CA  . THR   B 1 1587 ? 27.35800   46.47700  11.95300  1.000 73.31818  ?  1585 THR   B CA  1 
ATOM   26521 C  C   . THR   B 1 1587 ? 27.29400   47.05500  10.54400  1.000 70.90286  ?  1585 THR   B C   1 
ATOM   26522 O  O   . THR   B 1 1587 ? 28.10900   46.69300  9.68800   1.000 73.53664  ?  1585 THR   B O   1 
ATOM   26523 C  CB  . THR   B 1 1587 ? 28.33600   47.31300  12.78700  1.000 71.00587  ?  1585 THR   B CB  1 
ATOM   26524 O  OG1 . THR   B 1 1587 ? 29.58000   47.43000  12.08400  1.000 69.27311  ?  1585 THR   B OG1 1 
ATOM   26525 C  CG2 . THR   B 1 1587 ? 28.58300   46.66300  14.14600  1.000 64.67579  ?  1585 THR   B CG2 1 
ATOM   26526 N  N   . PRO   B 1 1588 ? 26.34200   47.94400  10.27200  1.000 65.50216  ?  1586 PRO   B N   1 
ATOM   26527 C  CA  . PRO   B 1 1588 ? 26.33300   48.65000  8.98900   1.000 79.09421  ?  1586 PRO   B CA  1 
ATOM   26528 C  C   . PRO   B 1 1588 ? 27.38300   49.74900  8.95500   1.000 85.43749  ?  1586 PRO   B C   1 
ATOM   26529 O  O   . PRO   B 1 1588 ? 27.73500   50.34600  9.97600   1.000 80.32032  ?  1586 PRO   B O   1 
ATOM   26530 C  CB  . PRO   B 1 1588 ? 24.91600   49.23700  8.91000   1.000 71.01016  ?  1586 PRO   B CB  1 
ATOM   26531 C  CG  . PRO   B 1 1588 ? 24.14200   48.59100  10.03300  1.000 69.90972  ?  1586 PRO   B CG  1 
ATOM   26532 C  CD  . PRO   B 1 1588 ? 25.15100   48.25500  11.07600  1.000 68.57815  ?  1586 PRO   B CD  1 
ATOM   26533 N  N   . HIS   B 1 1589 ? 27.88200   50.01400  7.75300   1.000 79.24475  ?  1587 HIS   B N   1 
ATOM   26534 C  CA  . HIS   B 1 1589 ? 28.97800   50.94700  7.56200   1.000 67.77844  ?  1587 HIS   B CA  1 
ATOM   26535 C  C   . HIS   B 1 1589 ? 28.76100   51.73300  6.28000   1.000 80.45617  ?  1587 HIS   B C   1 
ATOM   26536 O  O   . HIS   B 1 1589 ? 28.19300   51.20700  5.31400   1.000 77.94253  ?  1587 HIS   B O   1 
ATOM   26537 C  CB  . HIS   B 1 1589 ? 30.32800   50.21600  7.49300   1.000 75.52944  ?  1587 HIS   B CB  1 
ATOM   26538 C  CG  . HIS   B 1 1589 ? 31.49600   51.06800  7.88100   1.000 77.08419  ?  1587 HIS   B CG  1 
ATOM   26539 N  ND1 . HIS   B 1 1589 ? 32.21000   51.81200  6.96700   1.000 60.39817  ?  1587 HIS   B ND1 1 
ATOM   26540 C  CD2 . HIS   B 1 1589 ? 32.07100   51.29600  9.08500   1.000 70.86596  ?  1587 HIS   B CD2 1 
ATOM   26541 C  CE1 . HIS   B 1 1589 ? 33.17600   52.46200  7.59200   1.000 62.09157  ?  1587 HIS   B CE1 1 
ATOM   26542 N  NE2 . HIS   B 1 1589 ? 33.11400   52.16500  8.87700   1.000 67.57119  ?  1587 HIS   B NE2 1 
ATOM   26543 N  N   . PRO   B 1 1590 ? 29.19000   52.99700  6.24400   1.000 80.80009  ?  1588 PRO   B N   1 
ATOM   26544 C  CA  . PRO   B 1 1590 ? 29.09400   53.76300  4.99200   1.000 72.94325  ?  1588 PRO   B CA  1 
ATOM   26545 C  C   . PRO   B 1 1590 ? 29.90400   53.16400  3.85700   1.000 80.15045  ?  1588 PRO   B C   1 
ATOM   26546 O  O   . PRO   B 1 1590 ? 29.55800   53.37700  2.68700   1.000 76.09713  ?  1588 PRO   B O   1 
ATOM   26547 C  CB  . PRO   B 1 1590 ? 29.61900   55.15100  5.38800   1.000 83.01063  ?  1588 PRO   B CB  1 
ATOM   26548 C  CG  . PRO   B 1 1590 ? 30.38800   54.92900  6.65900   1.000 76.36836  ?  1588 PRO   B CG  1 
ATOM   26549 C  CD  . PRO   B 1 1590 ? 29.66800   53.82700  7.36100   1.000 65.59137  ?  1588 PRO   B CD  1 
ATOM   26550 N  N   . LEU   B 1 1591 ? 30.97500   52.42200  4.16500   1.000 65.62923  ?  1589 LEU   B N   1 
ATOM   26551 C  CA  . LEU   B 1 1591 ? 31.75900   51.78500  3.11000   1.000 61.82996  ?  1589 LEU   B CA  1 
ATOM   26552 C  C   . LEU   B 1 1591 ? 30.91800   50.80400  2.30300   1.000 72.66768  ?  1589 LEU   B C   1 
ATOM   26553 O  O   . LEU   B 1 1591 ? 31.20100   50.57000  1.12300   1.000 80.51887  ?  1589 LEU   B O   1 
ATOM   26554 C  CB  . LEU   B 1 1591 ? 32.98000   51.07600  3.70100   1.000 56.82967  ?  1589 LEU   B CB  1 
ATOM   26555 C  CG  . LEU   B 1 1591 ? 34.19800   51.95200  4.01500   1.000 61.00840  ?  1589 LEU   B CG  1 
ATOM   26556 C  CD1 . LEU   B 1 1591 ? 35.06500   51.32900  5.09600   1.000 60.96517  ?  1589 LEU   B CD1 1 
ATOM   26557 C  CD2 . LEU   B 1 1591 ? 35.01800   52.21400  2.76400   1.000 60.56668  ?  1589 LEU   B CD2 1 
ATOM   26558 N  N   . GLU   B 1 1592 ? 29.88500   50.22600  2.91600   1.000 70.62912  ?  1590 GLU   B N   1 
ATOM   26559 C  CA  . GLU   B 1 1592 ? 28.95000   49.34400  2.23100   1.000 72.60652  ?  1590 GLU   B CA  1 
ATOM   26560 C  C   . GLU   B 1 1592 ? 27.63000   50.03800  1.90600   1.000 84.09537  ?  1590 GLU   B C   1 
ATOM   26561 O  O   . GLU   B 1 1592 ? 26.64500   49.36300  1.58400   1.000 79.28914  ?  1590 GLU   B O   1 
ATOM   26562 C  CB  . GLU   B 1 1592 ? 28.70200   48.08600  3.06600   1.000 67.89585  ?  1590 GLU   B CB  1 
ATOM   26563 C  CG  . GLU   B 1 1592 ? 29.82700   47.06100  2.99200   1.000 63.16937  ?  1590 GLU   B CG  1 
ATOM   26564 C  CD  . GLU   B 1 1592 ? 29.91200   46.38000  1.63800   1.000 74.73546  ?  1590 GLU   B CD  1 
ATOM   26565 O  OE1 . GLU   B 1 1592 ? 28.85000   46.02200  1.08500   1.000 67.75810  ?  1590 GLU   B OE1 1 
ATOM   26566 O  OE2 . GLU   B 1 1592 ? 31.04000   46.20100  1.12600   1.000 60.59812  -1 1590 GLU   B OE2 1 
ATOM   26567 N  N   . LYS   B 1 1593 ? 27.59700   51.37200  1.99000   1.000 89.87471  ?  1591 LYS   B N   1 
ATOM   26568 C  CA  . LYS   B 1 1593 ? 26.41700   52.17400  1.65100   1.000 84.78916  ?  1591 LYS   B CA  1 
ATOM   26569 C  C   . LYS   B 1 1593 ? 25.19200   51.74600  2.45700   1.000 76.97580  ?  1591 LYS   B C   1 
ATOM   26570 O  O   . LYS   B 1 1593 ? 24.08400   51.64000  1.92800   1.000 86.57781  ?  1591 LYS   B O   1 
ATOM   26571 C  CB  . LYS   B 1 1593 ? 26.12700   52.12100  0.14800   1.000 65.78980  ?  1591 LYS   B CB  1 
ATOM   26572 C  CG  . LYS   B 1 1593 ? 27.14000   52.88000  -0.69700  1.000 73.13346  ?  1591 LYS   B CG  1 
ATOM   26573 C  CD  . LYS   B 1 1593 ? 27.34400   52.22700  -2.05400  1.000 74.83526  ?  1591 LYS   B CD  1 
ATOM   26574 C  CE  . LYS   B 1 1593 ? 26.32900   52.72300  -3.06800  1.000 78.84349  ?  1591 LYS   B CE  1 
ATOM   26575 N  NZ  . LYS   B 1 1593 ? 26.81300   52.54500  -4.46600  1.000 89.98477  ?  1591 LYS   B NZ  1 
ATOM   26576 N  N   . GLY   B 1 1594 ? 25.39300   51.49800  3.75100   1.000 80.23918  ?  1592 GLY   B N   1 
ATOM   26577 C  CA  . GLY   B 1 1594 ? 24.33200   51.08900  4.64100   1.000 87.83279  ?  1592 GLY   B CA  1 
ATOM   26578 C  C   . GLY   B 1 1594 ? 24.27800   49.60100  4.93000   1.000 95.41217  ?  1592 GLY   B C   1 
ATOM   26579 O  O   . GLY   B 1 1594 ? 23.68300   49.20400  5.93900   1.000 93.44438  ?  1592 GLY   B O   1 
ATOM   26580 N  N   . GLU   B 1 1595 ? 24.87300   48.77100  4.07500   1.000 79.81947  ?  1593 GLU   B N   1 
ATOM   26581 C  CA  . GLU   B 1 1595 ? 24.89300   47.33400  4.30200   1.000 77.11201  ?  1593 GLU   B CA  1 
ATOM   26582 C  C   . GLU   B 1 1595 ? 25.90500   46.98600  5.39500   1.000 79.14404  ?  1593 GLU   B C   1 
ATOM   26583 O  O   . GLU   B 1 1595 ? 26.64700   47.84000  5.88800   1.000 80.53131  ?  1593 GLU   B O   1 
ATOM   26584 C  CB  . GLU   B 1 1595 ? 25.18500   46.59300  3.00100   1.000 76.30279  ?  1593 GLU   B CB  1 
ATOM   26585 C  CG  . GLU   B 1 1595 ? 23.95300   46.37100  2.13400   1.000 78.89218  ?  1593 GLU   B CG  1 
ATOM   26586 C  CD  . GLU   B 1 1595 ? 22.79300   45.76900  2.91200   1.000 110.82211 ?  1593 GLU   B CD  1 
ATOM   26587 O  OE1 . GLU   B 1 1595 ? 23.00000   44.75700  3.61600   1.000 104.54720 ?  1593 GLU   B OE1 1 
ATOM   26588 O  OE2 . GLU   B 1 1595 ? 21.67200   46.31300  2.82000   1.000 113.26905 -1 1593 GLU   B OE2 1 
ATOM   26589 N  N   . ARG   B 1 1596 ? 25.94100   45.71300  5.78000   1.000 77.39389  ?  1594 ARG   B N   1 
ATOM   26590 C  CA  . ARG   B 1 1596 ? 26.66500   45.29000  6.97000   1.000 76.96156  ?  1594 ARG   B CA  1 
ATOM   26591 C  C   . ARG   B 1 1596 ? 28.08700   44.84200  6.64900   1.000 68.13339  ?  1594 ARG   B C   1 
ATOM   26592 O  O   . ARG   B 1 1596 ? 28.39500   44.40500  5.53600   1.000 61.54809  ?  1594 ARG   B O   1 
ATOM   26593 C  CB  . ARG   B 1 1596 ? 25.92300   44.15300  7.67800   1.000 77.08646  ?  1594 ARG   B CB  1 
ATOM   26594 C  CG  . ARG   B 1 1596 ? 24.40900   44.22900  7.56800   1.000 72.25685  ?  1594 ARG   B CG  1 
ATOM   26595 C  CD  . ARG   B 1 1596 ? 23.77300   42.87800  7.84600   1.000 83.87723  ?  1594 ARG   B CD  1 
ATOM   26596 N  NE  . ARG   B 1 1596 ? 24.03400   41.92400  6.77400   1.000 95.79272  ?  1594 ARG   B NE  1 
ATOM   26597 C  CZ  . ARG   B 1 1596 ? 24.34400   40.64900  6.96400   1.000 85.81706  ?  1594 ARG   B CZ  1 
ATOM   26598 N  NH1 . ARG   B 1 1596 ? 24.45100   40.13800  8.18100   1.000 67.29336  ?  1594 ARG   B NH1 1 
ATOM   26599 N  NH2 . ARG   B 1 1596 ? 24.55700   39.86800  5.90800   1.000 69.99584  ?  1594 ARG   B NH2 1 
ATOM   26600 N  N   . ILE   B 1 1597 ? 28.95400   44.96100  7.65200   1.000 54.61392  ?  1595 ILE   B N   1 
ATOM   26601 C  CA  . ILE   B 1 1597 ? 30.30900   44.43100  7.61900   1.000 58.10023  ?  1595 ILE   B CA  1 
ATOM   26602 C  C   . ILE   B 1 1597 ? 30.52300   43.65700  8.91100   1.000 66.30719  ?  1595 ILE   B C   1 
ATOM   26603 O  O   . ILE   B 1 1597 ? 29.93800   43.98200  9.94900   1.000 67.48442  ?  1595 ILE   B O   1 
ATOM   26604 C  CB  . ILE   B 1 1597 ? 31.37300   45.54400  7.46000   1.000 63.56486  ?  1595 ILE   B CB  1 
ATOM   26605 C  CG1 . ILE   B 1 1597 ? 31.07700   46.72200  8.39200   1.000 64.10161  ?  1595 ILE   B CG1 1 
ATOM   26606 C  CG2 . ILE   B 1 1597 ? 31.43700   46.02400  6.02700   1.000 58.60426  ?  1595 ILE   B CG2 1 
ATOM   26607 C  CD1 . ILE   B 1 1597 ? 31.81000   46.67000  9.72000   1.000 66.67408  ?  1595 ILE   B CD1 1 
ATOM   26608 N  N   . TYR   B 1 1598 ? 31.35300   42.62000  8.84700   1.000 43.17891  ?  1596 TYR   B N   1 
ATOM   26609 C  CA  . TYR   B 1 1598 ? 31.65700   41.82300  10.02500  1.000 53.81450  ?  1596 TYR   B CA  1 
ATOM   26610 C  C   . TYR   B 1 1598 ? 33.02100   42.21300  10.57500  1.000 52.01059  ?  1596 TYR   B C   1 
ATOM   26611 O  O   . TYR   B 1 1598 ? 33.98000   42.37900  9.81800   1.000 48.73832  ?  1596 TYR   B O   1 
ATOM   26612 C  CB  . TYR   B 1 1598 ? 31.63600   40.32200  9.72600   1.000 56.90443  ?  1596 TYR   B CB  1 
ATOM   26613 C  CG  . TYR   B 1 1598 ? 32.22600   39.52100  10.86600  1.000 48.23692  ?  1596 TYR   B CG  1 
ATOM   26614 C  CD1 . TYR   B 1 1598 ? 31.57700   39.44400  12.09300  1.000 46.30395  ?  1596 TYR   B CD1 1 
ATOM   26615 C  CD2 . TYR   B 1 1598 ? 33.45000   38.87800  10.73200  1.000 43.19557  ?  1596 TYR   B CD2 1 
ATOM   26616 C  CE1 . TYR   B 1 1598 ? 32.12100   38.73300  13.14900  1.000 49.26226  ?  1596 TYR   B CE1 1 
ATOM   26617 C  CE2 . TYR   B 1 1598 ? 34.00100   38.16300  11.78200  1.000 49.65418  ?  1596 TYR   B CE2 1 
ATOM   26618 C  CZ  . TYR   B 1 1598 ? 33.33400   38.09400  12.98700  1.000 49.09316  ?  1596 TYR   B CZ  1 
ATOM   26619 O  OH  . TYR   B 1 1598 ? 33.88400   37.38300  14.02900  1.000 53.55640  ?  1596 TYR   B OH  1 
ATOM   26620 N  N   . ARG   B 1 1599 ? 33.10100   42.34400  11.89800  1.000 52.48363  ?  1597 ARG   B N   1 
ATOM   26621 C  CA  . ARG   B 1 1599 ? 34.32500   42.74600  12.58400  1.000 45.25584  ?  1597 ARG   B CA  1 
ATOM   26622 C  C   . ARG   B 1 1599 ? 35.01700   41.50700  13.14200  1.000 50.50861  ?  1597 ARG   B C   1 
ATOM   26623 O  O   . ARG   B 1 1599 ? 34.52800   40.88400  14.09000  1.000 57.70564  ?  1597 ARG   B O   1 
ATOM   26624 C  CB  . ARG   B 1 1599 ? 34.01100   43.75700  13.68200  1.000 62.95463  ?  1597 ARG   B CB  1 
ATOM   26625 C  CG  . ARG   B 1 1599 ? 33.64300   45.11700  13.11900  1.000 66.27027  ?  1597 ARG   B CG  1 
ATOM   26626 C  CD  . ARG   B 1 1599 ? 32.58900   45.83000  13.93800  1.000 70.39001  ?  1597 ARG   B CD  1 
ATOM   26627 N  NE  . ARG   B 1 1599 ? 32.14500   47.03600  13.25100  1.000 70.98969  ?  1597 ARG   B NE  1 
ATOM   26628 C  CZ  . ARG   B 1 1599 ? 32.78600   48.19600  13.29200  1.000 67.34897  ?  1597 ARG   B CZ  1 
ATOM   26629 N  NH1 . ARG   B 1 1599 ? 33.88600   48.35000  14.01100  1.000 50.94020  ?  1597 ARG   B NH1 1 
ATOM   26630 N  NH2 . ARG   B 1 1599 ? 32.31300   49.22500  12.59200  1.000 44.85766  ?  1597 ARG   B NH2 1 
ATOM   26631 N  N   . THR   B 1 1600 ? 36.17100   41.16700  12.56100  1.000 51.47206  ?  1598 THR   B N   1 
ATOM   26632 C  CA  . THR   B 1 1600 ? 36.84500   39.91800  12.89900  1.000 52.56506  ?  1598 THR   B CA  1 
ATOM   26633 C  C   . THR   B 1 1600 ? 37.53100   39.97400  14.25700  1.000 54.24821  ?  1598 THR   B C   1 
ATOM   26634 O  O   . THR   B 1 1600 ? 37.63800   38.94600  14.93400  1.000 57.64473  ?  1598 THR   B O   1 
ATOM   26635 C  CB  . THR   B 1 1600 ? 37.88300   39.57500  11.83400  1.000 56.79235  ?  1598 THR   B CB  1 
ATOM   26636 O  OG1 . THR   B 1 1600 ? 38.97600   40.50000  11.92200  1.000 53.36915  ?  1598 THR   B OG1 1 
ATOM   26637 C  CG2 . THR   B 1 1600 ? 37.26700   39.64900  10.44800  1.000 51.48312  ?  1598 THR   B CG2 1 
ATOM   26638 N  N   . GLY   B 1 1601 ? 38.01400   41.14300  14.66500  1.000 51.72977  ?  1599 GLY   B N   1 
ATOM   26639 C  CA  . GLY   B 1 1601 ? 38.89800   41.19700  15.80900  1.000 49.40265  ?  1599 GLY   B CA  1 
ATOM   26640 C  C   . GLY   B 1 1601 ? 40.31600   40.78700  15.49600  1.000 57.81791  ?  1599 GLY   B C   1 
ATOM   26641 O  O   . GLY   B 1 1601 ? 41.07400   40.45500  16.41300  1.000 57.42798  ?  1599 GLY   B O   1 
ATOM   26642 N  N   . ASP   B 1 1602 ? 40.69100   40.78400  14.22000  1.000 63.53730  ?  1600 ASP   B N   1 
ATOM   26643 C  CA  . ASP   B 1 1602 ? 42.03400   40.44100  13.77900  1.000 66.12831  ?  1600 ASP   B CA  1 
ATOM   26644 C  C   . ASP   B 1 1602 ? 42.72900   41.68900  13.25600  1.000 65.11992  ?  1600 ASP   B C   1 
ATOM   26645 O  O   . ASP   B 1 1602 ? 42.11600   42.51100  12.56700  1.000 57.33198  ?  1600 ASP   B O   1 
ATOM   26646 C  CB  . ASP   B 1 1602 ? 42.00400   39.37000  12.68300  1.000 64.87306  ?  1600 ASP   B CB  1 
ATOM   26647 C  CG  . ASP   B 1 1602 ? 41.45300   38.04500  13.17200  1.000 67.95890  ?  1600 ASP   B CG  1 
ATOM   26648 O  OD1 . ASP   B 1 1602 ? 40.22700   37.95400  13.39300  1.000 69.37701  ?  1600 ASP   B OD1 1 
ATOM   26649 O  OD2 . ASP   B 1 1602 ? 42.24700   37.09300  13.33300  1.000 69.14616  -1 1600 ASP   B OD2 1 
ATOM   26650 N  N   . LEU   B 1 1603 ? 44.00900   41.82700  13.58600  1.000 67.66935  ?  1601 LEU   B N   1 
ATOM   26651 C  CA  . LEU   B 1 1603 ? 44.80500   42.94800  13.11100  1.000 63.88337  ?  1601 LEU   B CA  1 
ATOM   26652 C  C   . LEU   B 1 1603 ? 45.40500   42.60800  11.75400  1.000 62.28387  ?  1601 LEU   B C   1 
ATOM   26653 O  O   . LEU   B 1 1603 ? 45.97900   41.53000  11.57500  1.000 69.49340  ?  1601 LEU   B O   1 
ATOM   26654 C  CB  . LEU   B 1 1603 ? 45.91200   43.29300  14.10700  1.000 72.04926  ?  1601 LEU   B CB  1 
ATOM   26655 C  CG  . LEU   B 1 1603 ? 46.61500   44.61100  13.78900  1.000 65.88619  ?  1601 LEU   B CG  1 
ATOM   26656 C  CD1 . LEU   B 1 1603 ? 45.68000   45.78200  14.06600  1.000 40.35238  ?  1601 LEU   B CD1 1 
ATOM   26657 C  CD2 . LEU   B 1 1603 ? 47.91100   44.74700  14.57000  1.000 56.68260  ?  1601 LEU   B CD2 1 
ATOM   26658 N  N   . ALA   B 1 1604 ? 45.27000   43.53100  10.80500  1.000 69.51051  ?  1602 ALA   B N   1 
ATOM   26659 C  CA  . ALA   B 1 1604 ? 45.76200   43.32100  9.45200   1.000 64.82401  ?  1602 ALA   B CA  1 
ATOM   26660 C  C   . ALA   B 1 1604 ? 46.15300   44.66200  8.84800   1.000 58.73964  ?  1602 ALA   B C   1 
ATOM   26661 O  O   . ALA   B 1 1604 ? 45.81700   45.72700  9.37400   1.000 58.15824  ?  1602 ALA   B O   1 
ATOM   26662 C  CB  . ALA   B 1 1604 ? 44.71600   42.61500  8.58400   1.000 37.77410  ?  1602 ALA   B CB  1 
ATOM   26663 N  N   . ARG   B 1 1605 ? 46.87000   44.60000  7.72900   1.000 47.96049  ?  1603 ARG   B N   1 
ATOM   26664 C  CA  . ARG   B 1 1605 ? 47.26800   45.80200  7.01200   1.000 59.60725  ?  1603 ARG   B CA  1 
ATOM   26665 C  C   . ARG   B 1 1605 ? 47.34000   45.49300  5.52500   1.000 53.96686  ?  1603 ARG   B C   1 
ATOM   26666 O  O   . ARG   B 1 1605 ? 47.63700   44.36400  5.12200   1.000 47.88589  ?  1603 ARG   B O   1 
ATOM   26667 C  CB  . ARG   B 1 1605 ? 48.61100   46.35100  7.51600   1.000 52.40443  ?  1603 ARG   B CB  1 
ATOM   26668 C  CG  . ARG   B 1 1605 ? 49.83600   45.56300  7.07400   1.000 53.52752  ?  1603 ARG   B CG  1 
ATOM   26669 C  CD  . ARG   B 1 1605 ? 51.09000   46.07400  7.76900   1.000 71.90561  ?  1603 ARG   B CD  1 
ATOM   26670 N  NE  . ARG   B 1 1605 ? 52.25300   46.08200  6.88800   1.000 85.39139  ?  1603 ARG   B NE  1 
ATOM   26671 C  CZ  . ARG   B 1 1605 ? 53.38500   45.43800  7.13700   1.000 83.91560  ?  1603 ARG   B CZ  1 
ATOM   26672 N  NH1 . ARG   B 1 1605 ? 53.54600   44.72500  8.23900   1.000 75.18003  ?  1603 ARG   B NH1 1 
ATOM   26673 N  NH2 . ARG   B 1 1605 ? 54.38100   45.51400  6.25800   1.000 82.03255  ?  1603 ARG   B NH2 1 
ATOM   26674 N  N   . TYR   B 1 1606 ? 47.04700   46.50500  4.71500   1.000 53.05043  ?  1604 TYR   B N   1 
ATOM   26675 C  CA  . TYR   B 1 1606 ? 47.13300   46.37200  3.27000   1.000 47.36239  ?  1604 TYR   B CA  1 
ATOM   26676 C  C   . TYR   B 1 1606 ? 48.58600   46.43700  2.81300   1.000 63.86499  ?  1604 TYR   B C   1 
ATOM   26677 O  O   . TYR   B 1 1606 ? 49.41300   47.14400  3.39600   1.000 75.53674  ?  1604 TYR   B O   1 
ATOM   26678 C  CB  . TYR   B 1 1606 ? 46.33900   47.48000  2.57600   1.000 47.11395  ?  1604 TYR   B CB  1 
ATOM   26679 C  CG  . TYR   B 1 1606 ? 44.83900   47.39600  2.73000   1.000 53.05140  ?  1604 TYR   B CG  1 
ATOM   26680 C  CD1 . TYR   B 1 1606 ? 44.11500   46.36600  2.14300   1.000 55.28611  ?  1604 TYR   B CD1 1 
ATOM   26681 C  CD2 . TYR   B 1 1606 ? 44.14200   48.36400  3.44000   1.000 60.99990  ?  1604 TYR   B CD2 1 
ATOM   26682 C  CE1 . TYR   B 1 1606 ? 42.74200   46.29800  2.27400   1.000 55.38073  ?  1604 TYR   B CE1 1 
ATOM   26683 C  CE2 . TYR   B 1 1606 ? 42.77200   48.30300  3.57600   1.000 55.44838  ?  1604 TYR   B CE2 1 
ATOM   26684 C  CZ  . TYR   B 1 1606 ? 42.07800   47.27000  2.99300   1.000 52.97003  ?  1604 TYR   B CZ  1 
ATOM   26685 O  OH  . TYR   B 1 1606 ? 40.71200   47.21500  3.13100   1.000 73.60251  ?  1604 TYR   B OH  1 
ATOM   26686 N  N   . ARG   B 1 1607 ? 48.89200   45.68700  1.75900   1.000 58.55203  ?  1605 ARG   B N   1 
ATOM   26687 C  CA  . ARG   B 1 1607 ? 50.14600   45.82600  1.03500   1.000 51.35807  ?  1605 ARG   B CA  1 
ATOM   26688 C  C   . ARG   B 1 1607 ? 49.94300   46.72900  -0.17400  1.000 67.75449  ?  1605 ARG   B C   1 
ATOM   26689 O  O   . ARG   B 1 1607 ? 48.81800   47.05800  -0.55600  1.000 70.52191  ?  1605 ARG   B O   1 
ATOM   26690 C  CB  . ARG   B 1 1607 ? 50.67300   44.46600  0.57400   1.000 59.59894  ?  1605 ARG   B CB  1 
ATOM   26691 C  CG  . ARG   B 1 1607 ? 51.11500   43.55800  1.68600   1.000 65.35802  ?  1605 ARG   B CG  1 
ATOM   26692 C  CD  . ARG   B 1 1607 ? 52.07600   42.50200  1.17800   1.000 58.99577  ?  1605 ARG   B CD  1 
ATOM   26693 N  NE  . ARG   B 1 1607 ? 51.72400   42.03500  -0.15800  1.000 73.82140  ?  1605 ARG   B NE  1 
ATOM   26694 C  CZ  . ARG   B 1 1607 ? 52.34800   41.05200  -0.79200  1.000 67.16443  ?  1605 ARG   B CZ  1 
ATOM   26695 N  NH1 . ARG   B 1 1607 ? 53.34600   40.39000  -0.22900  1.000 46.50615  ?  1605 ARG   B NH1 1 
ATOM   26696 N  NH2 . ARG   B 1 1607 ? 51.95600   40.72000  -2.01900  1.000 55.33766  ?  1605 ARG   B NH2 1 
ATOM   26697 N  N   . GLU   B 1 1608 ? 51.06000   47.13100  -0.78500  1.000 66.70388  ?  1606 GLU   B N   1 
ATOM   26698 C  CA  . GLU   B 1 1608 ? 50.96500   47.82500  -2.06400  1.000 64.79146  ?  1606 GLU   B CA  1 
ATOM   26699 C  C   . GLU   B 1 1608 ? 50.24000   46.96400  -3.09000  1.000 85.95647  ?  1606 GLU   B C   1 
ATOM   26700 O  O   . GLU   B 1 1608 ? 49.36800   47.45200  -3.81600  1.000 79.96310  ?  1606 GLU   B O   1 
ATOM   26701 C  CB  . GLU   B 1 1608 ? 52.35500   48.21500  -2.56600  1.000 73.94254  ?  1606 GLU   B CB  1 
ATOM   26702 C  CG  . GLU   B 1 1608 ? 52.66500   49.71000  -2.46700  1.000 90.44204  ?  1606 GLU   B CG  1 
ATOM   26703 C  CD  . GLU   B 1 1608 ? 52.08100   50.52300  -3.62000  1.000 96.84072  ?  1606 GLU   B CD  1 
ATOM   26704 O  OE1 . GLU   B 1 1608 ? 51.68500   49.92200  -4.64300  1.000 85.61776  ?  1606 GLU   B OE1 1 
ATOM   26705 O  OE2 . GLU   B 1 1608 ? 52.01700   51.76700  -3.50200  1.000 85.13954  -1 1606 GLU   B OE2 1 
ATOM   26706 N  N   . ASP   B 1 1609 ? 50.56700   45.66900  -3.13700  1.000 89.25860  ?  1607 ASP   B N   1 
ATOM   26707 C  CA  . ASP   B 1 1609 ? 49.91900   44.74600  -4.06600  1.000 78.60300  ?  1607 ASP   B CA  1 
ATOM   26708 C  C   . ASP   B 1 1609 ? 48.40200   44.77200  -3.93200  1.000 77.36194  ?  1607 ASP   B C   1 
ATOM   26709 O  O   . ASP   B 1 1609 ? 47.67800   44.64500  -4.92700  1.000 76.18184  ?  1607 ASP   B O   1 
ATOM   26710 C  CB  . ASP   B 1 1609 ? 50.44000   43.33000  -3.82200  1.000 71.36413  ?  1607 ASP   B CB  1 
ATOM   26711 C  CG  . ASP   B 1 1609 ? 50.79200   42.61100  -5.10100  1.000 102.79795 ?  1607 ASP   B CG  1 
ATOM   26712 O  OD1 . ASP   B 1 1609 ? 50.27700   43.01000  -6.16600  1.000 113.11670 ?  1607 ASP   B OD1 1 
ATOM   26713 O  OD2 . ASP   B 1 1609 ? 51.58000   41.64400  -5.03800  1.000 107.97273 -1 1607 ASP   B OD2 1 
ATOM   26714 N  N   . GLY   B 1 1610 ? 47.90500   44.94500  -2.71100  1.000 79.46075  ?  1608 GLY   B N   1 
ATOM   26715 C  CA  . GLY   B 1 1610 ? 46.51000   44.75200  -2.38600  1.000 70.44726  ?  1608 GLY   B CA  1 
ATOM   26716 C  C   . GLY   B 1 1610 ? 46.27000   43.54700  -1.50700  1.000 64.72269  ?  1608 GLY   B C   1 
ATOM   26717 O  O   . GLY   B 1 1610 ? 45.22400   43.47100  -0.84800  1.000 53.63814  ?  1608 GLY   B O   1 
ATOM   26718 N  N   . ASN   B 1 1611 ? 47.21200   42.60600  -1.48500  1.000 65.04394  ?  1609 ASN   B N   1 
ATOM   26719 C  CA  . ASN   B 1 1611 ? 47.13400   41.47900  -0.57000  1.000 65.18343  ?  1609 ASN   B CA  1 
ATOM   26720 C  C   . ASN   B 1 1611 ? 47.17000   41.97700  0.86800   1.000 57.82715  ?  1609 ASN   B C   1 
ATOM   26721 O  O   . ASN   B 1 1611 ? 47.86200   42.94600  1.19100   1.000 62.22928  ?  1609 ASN   B O   1 
ATOM   26722 C  CB  . ASN   B 1 1611 ? 48.29100   40.50900  -0.82100  1.000 69.11726  ?  1609 ASN   B CB  1 
ATOM   26723 C  CG  . ASN   B 1 1611 ? 48.18900   39.81200  -2.16600  1.000 71.14857  ?  1609 ASN   B CG  1 
ATOM   26724 O  OD1 . ASN   B 1 1611 ? 47.23500   39.08200  -2.42900  1.000 77.32772  ?  1609 ASN   B OD1 1 
ATOM   26725 N  ND2 . ASN   B 1 1611 ? 49.17600   40.03700  -3.02500  1.000 78.98834  ?  1609 ASN   B ND2 1 
ATOM   26726 N  N   . ILE   B 1 1612 ? 46.41500   41.31500  1.73000   1.000 49.23706  ?  1610 ILE   B N   1 
ATOM   26727 C  CA  . ILE   B 1 1612 ? 46.31700   41.69200  3.13300   1.000 47.10425  ?  1610 ILE   B CA  1 
ATOM   26728 C  C   . ILE   B 1 1612 ? 47.25500   40.80400  3.93600   1.000 50.40999  ?  1610 ILE   B C   1 
ATOM   26729 O  O   . ILE   B 1 1612 ? 47.42000   39.61800  3.62600   1.000 53.17266  ?  1610 ILE   B O   1 
ATOM   26730 C  CB  . ILE   B 1 1612 ? 44.86100   41.58200  3.62700   1.000 45.60324  ?  1610 ILE   B CB  1 
ATOM   26731 C  CG1 . ILE   B 1 1612 ? 44.01100   42.68800  3.00000   1.000 44.70621  ?  1610 ILE   B CG1 1 
ATOM   26732 C  CG2 . ILE   B 1 1612 ? 44.78800   41.67400  5.13700   1.000 37.96938  ?  1610 ILE   B CG2 1 
ATOM   26733 C  CD1 . ILE   B 1 1612 ? 42.87400   42.17400  2.14800   1.000 54.82482  ?  1610 ILE   B CD1 1 
ATOM   26734 N  N   . GLU   B 1 1613 ? 47.89500   41.38200  4.94900   1.000 50.83922  ?  1611 GLU   B N   1 
ATOM   26735 C  CA  . GLU   B 1 1613 ? 48.81600   40.66100  5.81600   1.000 53.03132  ?  1611 GLU   B CA  1 
ATOM   26736 C  C   . GLU   B 1 1613 ? 48.16100   40.43200  7.17000   1.000 52.70455  ?  1611 GLU   B C   1 
ATOM   26737 O  O   . GLU   B 1 1613 ? 47.61600   41.36600  7.76600   1.000 55.94825  ?  1611 GLU   B O   1 
ATOM   26738 C  CB  . GLU   B 1 1613 ? 50.12700   41.43100  5.98700   1.000 63.33812  ?  1611 GLU   B CB  1 
ATOM   26739 C  CG  . GLU   B 1 1613 ? 50.69800   41.96500  4.68800   1.000 67.43354  ?  1611 GLU   B CG  1 
ATOM   26740 C  CD  . GLU   B 1 1613 ? 52.21500   41.91100  4.63800   1.000 82.89716  ?  1611 GLU   B CD  1 
ATOM   26741 O  OE1 . GLU   B 1 1613 ? 52.86800   42.70200  5.35200   1.000 65.41288  ?  1611 GLU   B OE1 1 
ATOM   26742 O  OE2 . GLU   B 1 1613 ? 52.75500   41.07700  3.87900   1.000 82.52727  -1 1611 GLU   B OE2 1 
ATOM   26743 N  N   . TYR   B 1 1614 ? 48.21700   39.19400  7.65000   1.000 51.67265  ?  1612 TYR   B N   1 
ATOM   26744 C  CA  . TYR   B 1 1614 ? 47.65900   38.85300  8.95200   1.000 50.80347  ?  1612 TYR   B CA  1 
ATOM   26745 C  C   . TYR   B 1 1614 ? 48.66000   39.21000  10.04100  1.000 59.39215  ?  1612 TYR   B C   1 
ATOM   26746 O  O   . TYR   B 1 1614 ? 49.78100   38.68900  10.05600  1.000 65.01735  ?  1612 TYR   B O   1 
ATOM   26747 C  CB  . TYR   B 1 1614 ? 47.31400   37.37000  9.00800   1.000 50.81863  ?  1612 TYR   B CB  1 
ATOM   26748 C  CG  . TYR   B 1 1614 ? 46.65700   36.94100  10.29400  1.000 53.71046  ?  1612 TYR   B CG  1 
ATOM   26749 C  CD1 . TYR   B 1 1614 ? 45.33200   37.25500  10.55400  1.000 50.10527  ?  1612 TYR   B CD1 1 
ATOM   26750 C  CD2 . TYR   B 1 1614 ? 47.35900   36.21300  11.24600  1.000 53.88378  ?  1612 TYR   B CD2 1 
ATOM   26751 C  CE1 . TYR   B 1 1614 ? 44.72200   36.85900  11.72600  1.000 59.42174  ?  1612 TYR   B CE1 1 
ATOM   26752 C  CE2 . TYR   B 1 1614 ? 46.75800   35.81000  12.42300  1.000 45.68999  ?  1612 TYR   B CE2 1 
ATOM   26753 C  CZ  . TYR   B 1 1614 ? 45.43800   36.13800  12.65800  1.000 51.09397  ?  1612 TYR   B CZ  1 
ATOM   26754 O  OH  . TYR   B 1 1614 ? 44.82800   35.74500  13.82700  1.000 68.64678  ?  1612 TYR   B OH  1 
ATOM   26755 N  N   . LEU   B 1 1615 ? 48.25800   40.09200  10.95400  1.000 60.86274  ?  1613 LEU   B N   1 
ATOM   26756 C  CA  . LEU   B 1 1615 ? 49.13000   40.55200  12.02600  1.000 77.71956  ?  1613 LEU   B CA  1 
ATOM   26757 C  C   . LEU   B 1 1615 ? 48.74200   39.97700  13.38100  1.000 78.80601  ?  1613 LEU   B C   1 
ATOM   26758 O  O   . LEU   B 1 1615 ? 49.33400   40.35600  14.39700  1.000 83.31096  ?  1613 LEU   B O   1 
ATOM   26759 C  CB  . LEU   B 1 1615 ? 49.13300   42.08100  12.08100  1.000 72.63346  ?  1613 LEU   B CB  1 
ATOM   26760 C  CG  . LEU   B 1 1615 ? 49.65700   42.76900  10.81900  1.000 62.66031  ?  1613 LEU   B CG  1 
ATOM   26761 C  CD1 . LEU   B 1 1615 ? 49.64500   44.28300  10.97300  1.000 63.11800  ?  1613 LEU   B CD1 1 
ATOM   26762 C  CD2 . LEU   B 1 1615 ? 51.05100   42.27100  10.48400  1.000 44.85074  ?  1613 LEU   B CD2 1 
ATOM   26763 N  N   . GLY   B 1 1616 ? 47.77100   39.07200  13.42200  1.000 58.87363  ?  1614 GLY   B N   1 
ATOM   26764 C  CA  . GLY   B 1 1616 ? 47.35600   38.44400  14.66000  1.000 61.39039  ?  1614 GLY   B CA  1 
ATOM   26765 C  C   . GLY   B 1 1616 ? 46.07600   39.04700  15.20200  1.000 67.26205  ?  1614 GLY   B C   1 
ATOM   26766 O  O   . GLY   B 1 1616 ? 45.45200   39.93000  14.60400  1.000 70.19783  ?  1614 GLY   B O   1 
ATOM   26767 N  N   . ARG   B 1 1617 ? 45.68100   38.53900  16.36500  1.000 69.78906  ?  1615 ARG   B N   1 
ATOM   26768 C  CA  . ARG   B 1 1617 ? 44.50400   39.04700  17.05200  1.000 74.27570  ?  1615 ARG   B CA  1 
ATOM   26769 C  C   . ARG   B 1 1617 ? 44.85400   40.32600  17.80100  1.000 84.70914  ?  1615 ARG   B C   1 
ATOM   26770 O  O   . ARG   B 1 1617 ? 45.93600   40.44500  18.38200  1.000 87.06798  ?  1615 ARG   B O   1 
ATOM   26771 C  CB  . ARG   B 1 1617 ? 43.95900   37.99900  18.02200  1.000 75.57352  ?  1615 ARG   B CB  1 
ATOM   26772 C  CG  . ARG   B 1 1617 ? 43.53800   36.69700  17.35600  1.000 71.83069  ?  1615 ARG   B CG  1 
ATOM   26773 C  CD  . ARG   B 1 1617 ? 42.17300   36.82800  16.70300  1.000 57.66915  ?  1615 ARG   B CD  1 
ATOM   26774 N  NE  . ARG   B 1 1617 ? 41.12600   37.07300  17.68700  1.000 56.35732  ?  1615 ARG   B NE  1 
ATOM   26775 C  CZ  . ARG   B 1 1617 ? 39.87900   37.41300  17.38800  1.000 62.53507  ?  1615 ARG   B CZ  1 
ATOM   26776 N  NH1 . ARG   B 1 1617 ? 39.48600   37.57000  16.13400  1.000 49.29172  ?  1615 ARG   B NH1 1 
ATOM   26777 N  NH2 . ARG   B 1 1617 ? 39.00500   37.60300  18.37300  1.000 49.84376  ?  1615 ARG   B NH2 1 
ATOM   26778 N  N   . MET   B 1 1618 ? 43.93000   41.28900  17.78400  1.000 84.51062  ?  1616 MET   B N   1 
ATOM   26779 C  CA  . MET   B 1 1618 ? 44.19400   42.57300  18.42200  1.000 87.63894  ?  1616 MET   B CA  1 
ATOM   26780 C  C   . MET   B 1 1618 ? 44.00100   42.53400  19.93100  1.000 86.84982  ?  1616 MET   B C   1 
ATOM   26781 O  O   . MET   B 1 1618 ? 44.48400   43.43400  20.62700  1.000 97.74022  ?  1616 MET   B O   1 
ATOM   26782 C  CB  . MET   B 1 1618 ? 43.30900   43.66400  17.81600  1.000 73.91745  ?  1616 MET   B CB  1 
ATOM   26783 C  CG  . MET   B 1 1618 ? 41.86100   43.27100  17.61200  1.000 68.11900  ?  1616 MET   B CG  1 
ATOM   26784 S  SD  . MET   B 1 1618 ? 41.02000   44.42300  16.51000  1.000 76.58465  ?  1616 MET   B SD  1 
ATOM   26785 C  CE  . MET   B 1 1618 ? 42.38100   44.95800  15.47500  1.000 63.83427  ?  1616 MET   B CE  1 
ATOM   26786 N  N   . ASP   B 1 1619 ? 43.30900   41.52100  20.45300  1.000 81.31583  ?  1617 ASP   B N   1 
ATOM   26787 C  CA  . ASP   B 1 1619 ? 43.22700   41.34300  21.89500  1.000 88.02275  ?  1617 ASP   B CA  1 
ATOM   26788 C  C   . ASP   B 1 1619 ? 44.44800   40.62800  22.45700  1.000 105.52149 ?  1617 ASP   B C   1 
ATOM   26789 O  O   . ASP   B 1 1619 ? 44.75900   40.79600  23.64100  1.000 116.26651 ?  1617 ASP   B O   1 
ATOM   26790 C  CB  . ASP   B 1 1619 ? 41.95900   40.56900  22.26100  1.000 81.42147  ?  1617 ASP   B CB  1 
ATOM   26791 N  N   . HIS   B 1 1620 ? 45.15100   39.85100  21.63400  1.000 90.90017  ?  1618 HIS   B N   1 
ATOM   26792 C  CA  . HIS   B 1 1620 ? 46.31300   39.10200  22.09200  1.000 75.47001  ?  1618 HIS   B CA  1 
ATOM   26793 C  C   . HIS   B 1 1620 ? 47.59100   39.61700  21.44300  1.000 76.35732  ?  1618 HIS   B C   1 
ATOM   26794 O  O   . HIS   B 1 1620 ? 48.40200   38.82800  20.94900  1.000 84.36458  ?  1618 HIS   B O   1 
ATOM   26795 C  CB  . HIS   B 1 1620 ? 46.13300   37.61100  21.79700  1.000 81.33180  ?  1618 HIS   B CB  1 
ATOM   26796 N  N   . GLN   B 1 1621 ? 47.78500   40.93300  21.43900  1.000 83.02565  ?  1619 GLN   B N   1 
ATOM   26797 C  CA  . GLN   B 1 1621 ? 48.96400   41.53100  20.82900  1.000 93.88205  ?  1619 GLN   B CA  1 
ATOM   26798 C  C   . GLN   B 1 1621 ? 50.08000   41.67800  21.85600  1.000 93.92166  ?  1619 GLN   B C   1 
ATOM   26799 O  O   . GLN   B 1 1621 ? 49.82800   41.96900  23.02800  1.000 104.76086 ?  1619 GLN   B O   1 
ATOM   26800 C  CB  . GLN   B 1 1621 ? 48.62900   42.89200  20.21800  1.000 84.87378  ?  1619 GLN   B CB  1 
ATOM   26801 C  CG  . GLN   B 1 1621 ? 48.15700   42.82300  18.77200  1.000 78.09310  ?  1619 GLN   B CG  1 
ATOM   26802 C  CD  . GLN   B 1 1621 ? 49.26300   42.44300  17.80100  1.000 90.33853  ?  1619 GLN   B CD  1 
ATOM   26803 O  OE1 . GLN   B 1 1621 ? 50.39800   42.17500  18.19800  1.000 95.47949  ?  1619 GLN   B OE1 1 
ATOM   26804 N  NE2 . GLN   B 1 1621 ? 48.93100   42.41300  16.51800  1.000 86.03646  ?  1619 GLN   B NE2 1 
ATOM   26805 N  N   . VAL   B 1 1622 ? 51.31500   41.47500  21.40400  1.000 91.84295  ?  1620 VAL   B N   1 
ATOM   26806 C  CA  . VAL   B 1 1622 ? 52.49600   41.52100  22.26000  1.000 94.49633  ?  1620 VAL   B CA  1 
ATOM   26807 C  C   . VAL   B 1 1622 ? 53.27900   42.78600  21.94100  1.000 101.04089 ?  1620 VAL   B C   1 
ATOM   26808 O  O   . VAL   B 1 1622 ? 53.62800   43.03400  20.78000  1.000 98.59392  ?  1620 VAL   B O   1 
ATOM   26809 C  CB  . VAL   B 1 1622 ? 53.37100   40.26800  22.08000  1.000 80.41229  ?  1620 VAL   B CB  1 
ATOM   26810 C  CG1 . VAL   B 1 1622 ? 52.82600   39.12000  22.91200  1.000 77.18924  ?  1620 VAL   B CG1 1 
ATOM   26811 C  CG2 . VAL   B 1 1622 ? 53.43200   39.87400  20.61500  1.000 95.81742  ?  1620 VAL   B CG2 1 
ATOM   26812 N  N   . LYS   B 1 1623 ? 53.56000   43.58200  22.97100  1.000 104.07448 ?  1621 LYS   B N   1 
ATOM   26813 C  CA  . LYS   B 1 1623 ? 54.26100   44.84900  22.81700  1.000 107.80324 ?  1621 LYS   B CA  1 
ATOM   26814 C  C   . LYS   B 1 1623 ? 55.40100   44.93000  23.82100  1.000 109.02313 ?  1621 LYS   B C   1 
ATOM   26815 O  O   . LYS   B 1 1623 ? 55.21600   44.61900  25.00200  1.000 111.47817 ?  1621 LYS   B O   1 
ATOM   26816 C  CB  . LYS   B 1 1623 ? 53.30900   46.03600  23.00900  1.000 96.79117  ?  1621 LYS   B CB  1 
ATOM   26817 C  CG  . LYS   B 1 1623 ? 52.18800   46.12000  21.98500  1.000 98.80292  ?  1621 LYS   B CG  1 
ATOM   26818 C  CD  . LYS   B 1 1623 ? 52.06200   47.53100  21.42800  1.000 92.90780  ?  1621 LYS   B CD  1 
ATOM   26819 C  CE  . LYS   B 1 1623 ? 50.65900   47.79700  20.90600  1.000 86.76675  ?  1621 LYS   B CE  1 
ATOM   26820 N  NZ  . LYS   B 1 1623 ? 50.41800   49.24600  20.65700  1.000 93.64320  ?  1621 LYS   B NZ  1 
ATOM   26821 N  N   . ILE   B 1 1624 ? 56.57300   45.34700  23.34900  1.000 114.81766 ?  1622 ILE   B N   1 
ATOM   26822 C  CA  . ILE   B 1 1624 ? 57.73100   45.61400  24.19700  1.000 117.76922 ?  1622 ILE   B CA  1 
ATOM   26823 C  C   . ILE   B 1 1624 ? 58.07200   47.08900  24.05000  1.000 120.69568 ?  1622 ILE   B C   1 
ATOM   26824 O  O   . ILE   B 1 1624 ? 58.39300   47.54800  22.94500  1.000 121.67533 ?  1622 ILE   B O   1 
ATOM   26825 C  CB  . ILE   B 1 1624 ? 58.93400   44.73300  23.82700  1.000 103.33296 ?  1622 ILE   B CB  1 
ATOM   26826 C  CG1 . ILE   B 1 1624 ? 58.71900   43.29800  24.31200  1.000 98.16876  ?  1622 ILE   B CG1 1 
ATOM   26827 C  CG2 . ILE   B 1 1624 ? 60.21800   45.31000  24.41000  1.000 104.02191 ?  1622 ILE   B CG2 1 
ATOM   26828 C  CD1 . ILE   B 1 1624 ? 58.46900   43.18800  25.79900  1.000 81.94555  ?  1622 ILE   B CD1 1 
ATOM   26829 N  N   . ARG   B 1 1625 ? 57.99200   47.83100  25.15600  1.000 115.78697 ?  1623 ARG   B N   1 
ATOM   26830 C  CA  . ARG   B 1 1625 ? 58.21300   49.27500  25.17000  1.000 113.95046 ?  1623 ARG   B CA  1 
ATOM   26831 C  C   . ARG   B 1 1625 ? 57.23000   50.00500  24.25400  1.000 129.64217 ?  1623 ARG   B C   1 
ATOM   26832 O  O   . ARG   B 1 1625 ? 57.48600   51.13400  23.82400  1.000 143.91951 ?  1623 ARG   B O   1 
ATOM   26833 C  CB  . ARG   B 1 1625 ? 59.66600   49.60600  24.79600  1.000 104.51832 ?  1623 ARG   B CB  1 
ATOM   26834 C  CG  . ARG   B 1 1625 ? 60.14900   51.00200  25.16600  1.000 105.14290 ?  1623 ARG   B CG  1 
ATOM   26835 C  CD  . ARG   B 1 1625 ? 61.66200   51.00900  25.27300  1.000 106.96983 ?  1623 ARG   B CD  1 
ATOM   26836 N  NE  . ARG   B 1 1625 ? 62.14600   49.74600  25.82100  1.000 86.24361  ?  1623 ARG   B NE  1 
ATOM   26837 C  CZ  . ARG   B 1 1625 ? 62.98400   48.92600  25.20100  1.000 88.78750  ?  1623 ARG   B CZ  1 
ATOM   26838 N  NH1 . ARG   B 1 1625 ? 63.47200   49.20900  24.00500  1.000 92.22362  ?  1623 ARG   B NH1 1 
ATOM   26839 N  NH2 . ARG   B 1 1625 ? 63.33600   47.79000  25.79500  1.000 93.01732  ?  1623 ARG   B NH2 1 
ATOM   26840 N  N   . GLY   B 1 1626 ? 56.09700   49.38000  23.94900  1.000 115.52291 ?  1624 GLY   B N   1 
ATOM   26841 C  CA  . GLY   B 1 1626 ? 55.13900   49.94500  23.02400  1.000 114.17854 ?  1624 GLY   B CA  1 
ATOM   26842 C  C   . GLY   B 1 1626 ? 55.34200   49.57300  21.57200  1.000 105.27616 ?  1624 GLY   B C   1 
ATOM   26843 O  O   . GLY   B 1 1626 ? 54.66600   50.14200  20.70700  1.000 116.14842 ?  1624 GLY   B O   1 
ATOM   26844 N  N   . TYR   B 1 1627 ? 56.24500   48.64200  21.27500  1.000 106.46622 ?  1625 TYR   B N   1 
ATOM   26845 C  CA  . TYR   B 1 1627 ? 56.50600   48.19800  19.91100  1.000 112.81018 ?  1625 TYR   B CA  1 
ATOM   26846 C  C   . TYR   B 1 1627 ? 55.97700   46.78100  19.74400  1.000 116.15279 ?  1625 TYR   B C   1 
ATOM   26847 O  O   . TYR   B 1 1627 ? 56.38500   45.87300  20.47700  1.000 119.47146 ?  1625 TYR   B O   1 
ATOM   26848 C  CB  . TYR   B 1 1627 ? 58.00000   48.26400  19.58800  1.000 111.71181 ?  1625 TYR   B CB  1 
ATOM   26849 C  CG  . TYR   B 1 1627 ? 58.48200   49.66600  19.30300  1.000 116.20281 ?  1625 TYR   B CG  1 
ATOM   26850 C  CD1 . TYR   B 1 1627 ? 58.03600   50.35500  18.18300  1.000 111.25091 ?  1625 TYR   B CD1 1 
ATOM   26851 C  CD2 . TYR   B 1 1627 ? 59.37100   50.30600  20.15600  1.000 101.91674 ?  1625 TYR   B CD2 1 
ATOM   26852 C  CE1 . TYR   B 1 1627 ? 58.46500   51.64000  17.91500  1.000 102.34878 ?  1625 TYR   B CE1 1 
ATOM   26853 C  CE2 . TYR   B 1 1627 ? 59.80600   51.59400  19.89700  1.000 108.05909 ?  1625 TYR   B CE2 1 
ATOM   26854 C  CZ  . TYR   B 1 1627 ? 59.34900   52.25500  18.77400  1.000 109.24530 ?  1625 TYR   B CZ  1 
ATOM   26855 O  OH  . TYR   B 1 1627 ? 59.77700   53.53700  18.50800  1.000 96.85310  ?  1625 TYR   B OH  1 
ATOM   26856 N  N   . ARG   B 1 1628 ? 55.07100   46.59800  18.78400  1.000 113.05920 ?  1626 ARG   B N   1 
ATOM   26857 C  CA  . ARG   B 1 1628 ? 54.47500   45.28900  18.54700  1.000 105.88395 ?  1626 ARG   B CA  1 
ATOM   26858 C  C   . ARG   B 1 1628 ? 55.54900   44.27200  18.18300  1.000 105.86221 ?  1626 ARG   B C   1 
ATOM   26859 O  O   . ARG   B 1 1628 ? 56.42600   44.54100  17.35600  1.000 86.90652  ?  1626 ARG   B O   1 
ATOM   26860 C  CB  . ARG   B 1 1628 ? 53.42900   45.37800  17.43500  1.000 91.54129  ?  1626 ARG   B CB  1 
ATOM   26861 C  CG  . ARG   B 1 1628 ? 52.78300   44.04700  17.08800  1.000 86.53696  ?  1626 ARG   B CG  1 
ATOM   26862 C  CD  . ARG   B 1 1628 ? 52.12900   44.08000  15.71700  1.000 69.54767  ?  1626 ARG   B CD  1 
ATOM   26863 N  NE  . ARG   B 1 1628 ? 51.88000   42.73700  15.20500  1.000 83.45784  ?  1626 ARG   B NE  1 
ATOM   26864 C  CZ  . ARG   B 1 1628 ? 52.70600   42.07300  14.40800  1.000 84.84030  ?  1626 ARG   B CZ  1 
ATOM   26865 N  NH1 . ARG   B 1 1628 ? 53.84800   42.60100  14.00000  1.000 74.50169  ?  1626 ARG   B NH1 1 
ATOM   26866 N  NH2 . ARG   B 1 1628 ? 52.37700   40.84600  14.01100  1.000 81.66857  ?  1626 ARG   B NH2 1 
ATOM   26867 N  N   . ILE   B 1 1629 ? 55.47600   43.09800  18.80500  1.000 92.82229  ?  1627 ILE   B N   1 
ATOM   26868 C  CA  . ILE   B 1 1629 ? 56.49600   42.06600  18.66800  1.000 98.87060  ?  1627 ILE   B CA  1 
ATOM   26869 C  C   . ILE   B 1 1629 ? 55.98000   40.97900  17.73800  1.000 95.84417  ?  1627 ILE   B C   1 
ATOM   26870 O  O   . ILE   B 1 1629 ? 54.84800   40.50300  17.88800  1.000 79.26344  ?  1627 ILE   B O   1 
ATOM   26871 C  CB  . ILE   B 1 1629 ? 56.88000   41.48200  20.03800  1.000 103.45654 ?  1627 ILE   B CB  1 
ATOM   26872 C  CG1 . ILE   B 1 1629 ? 57.42400   42.58700  20.94500  1.000 101.61365 ?  1627 ILE   B CG1 1 
ATOM   26873 C  CG2 . ILE   B 1 1629 ? 57.90100   40.36400  19.87800  1.000 87.87083  ?  1627 ILE   B CG2 1 
ATOM   26874 C  CD1 . ILE   B 1 1629 ? 58.62400   43.31200  20.37200  1.000 103.69937 ?  1627 ILE   B CD1 1 
ATOM   26875 N  N   . GLU   B 1 1630 ? 56.80700   40.59300  16.77000  1.000 106.32699 ?  1628 GLU   B N   1 
ATOM   26876 C  CA  . GLU   B 1 1630 ? 56.52300   39.46200  15.89100  1.000 104.43854 ?  1628 GLU   B CA  1 
ATOM   26877 C  C   . GLU   B 1 1630 ? 57.32200   38.27900  16.42900  1.000 96.75395  ?  1628 GLU   B C   1 
ATOM   26878 O  O   . GLU   B 1 1630 ? 58.47900   38.07000  16.06500  1.000 96.44495  ?  1628 GLU   B O   1 
ATOM   26879 C  CB  . GLU   B 1 1630 ? 56.88100   39.78500  14.44400  1.000 88.45327  ?  1628 GLU   B CB  1 
ATOM   26880 N  N   . LEU   B 1 1631 ? 56.69200   37.50900  17.32200  1.000 93.55112  ?  1629 LEU   B N   1 
ATOM   26881 C  CA  . LEU   B 1 1631 ? 57.36800   36.37000  17.93500  1.000 104.18888 ?  1629 LEU   B CA  1 
ATOM   26882 C  C   . LEU   B 1 1631 ? 57.85700   35.37700  16.89000  1.000 111.31883 ?  1629 LEU   B C   1 
ATOM   26883 O  O   . LEU   B 1 1631 ? 58.88600   34.72000  17.09000  1.000 110.33225 ?  1629 LEU   B O   1 
ATOM   26884 C  CB  . LEU   B 1 1631 ? 56.43400   35.67600  18.92700  1.000 96.16407  ?  1629 LEU   B CB  1 
ATOM   26885 C  CG  . LEU   B 1 1631 ? 55.82500   36.54900  20.02600  1.000 84.93467  ?  1629 LEU   B CG  1 
ATOM   26886 C  CD1 . LEU   B 1 1631 ? 54.73700   35.79300  20.77100  1.000 74.52264  ?  1629 LEU   B CD1 1 
ATOM   26887 C  CD2 . LEU   B 1 1631 ? 56.90200   37.01500  20.98800  1.000 103.92980 ?  1629 LEU   B CD2 1 
ATOM   26888 N  N   . ASP   B 1 1632 ? 57.13800   35.25500  15.77200  1.000 109.12483 ?  1630 ASP   B N   1 
ATOM   26889 C  CA  . ASP   B 1 1632 ? 57.58800   34.37800  14.69800  1.000 111.70247 ?  1630 ASP   B CA  1 
ATOM   26890 C  C   . ASP   B 1 1632 ? 58.83400   34.92400  14.01300  1.000 107.99458 ?  1630 ASP   B C   1 
ATOM   26891 O  O   . ASP   B 1 1632 ? 59.68000   34.14400  13.56000  1.000 120.75194 ?  1630 ASP   B O   1 
ATOM   26892 C  CB  . ASP   B 1 1632 ? 56.46500   34.17600  13.68000  1.000 101.49156 ?  1630 ASP   B CB  1 
ATOM   26893 N  N   . GLU   B 1 1633 ? 58.96900   36.25100  13.93000  1.000 100.48951 ?  1631 GLU   B N   1 
ATOM   26894 C  CA  . GLU   B 1 1633 ? 60.14700   36.83600  13.29500  1.000 96.94626  ?  1631 GLU   B CA  1 
ATOM   26895 C  C   . GLU   B 1 1633 ? 61.41900   36.47800  14.05300  1.000 98.25372  ?  1631 GLU   B C   1 
ATOM   26896 O  O   . GLU   B 1 1633 ? 62.47000   36.25000  13.44300  1.000 96.52841  ?  1631 GLU   B O   1 
ATOM   26897 C  CB  . GLU   B 1 1633 ? 59.99100   38.35400  13.19100  1.000 78.17559  ?  1631 GLU   B CB  1 
ATOM   26898 N  N   . ILE   B 1 1634 ? 61.34400   36.42100  15.38500  1.000 101.15198 ?  1632 ILE   B N   1 
ATOM   26899 C  CA  . ILE   B 1 1634 ? 62.49900   35.99500  16.16900  1.000 98.96648  ?  1632 ILE   B CA  1 
ATOM   26900 C  C   . ILE   B 1 1634 ? 62.68700   34.48800  16.07000  1.000 106.14397 ?  1632 ILE   B C   1 
ATOM   26901 O  O   . ILE   B 1 1634 ? 63.82300   33.99500  16.06100  1.000 104.68208 ?  1632 ILE   B O   1 
ATOM   26902 C  CB  . ILE   B 1 1634 ? 62.35200   36.44700  17.63400  1.000 98.35795  ?  1632 ILE   B CB  1 
ATOM   26903 C  CG1 . ILE   B 1 1634 ? 61.84900   37.89000  17.70100  1.000 94.31908  ?  1632 ILE   B CG1 1 
ATOM   26904 C  CG2 . ILE   B 1 1634 ? 63.67900   36.30300  18.37300  1.000 83.67492  ?  1632 ILE   B CG2 1 
ATOM   26905 C  CD1 . ILE   B 1 1634 ? 61.62000   38.39500  19.10900  1.000 86.28562  ?  1632 ILE   B CD1 1 
ATOM   26906 N  N   . ARG   B 1 1635 ? 61.58900   33.73200  15.99000  1.000 111.15186 ?  1633 ARG   B N   1 
ATOM   26907 C  CA  . ARG   B 1 1635 ? 61.69400   32.28000  15.89800  1.000 107.50681 ?  1633 ARG   B CA  1 
ATOM   26908 C  C   . ARG   B 1 1635 ? 62.26500   31.84700  14.55200  1.000 114.44544 ?  1633 ARG   B C   1 
ATOM   26909 O  O   . ARG   B 1 1635 ? 63.06900   30.91000  14.48800  1.000 121.86902 ?  1633 ARG   B O   1 
ATOM   26910 C  CB  . ARG   B 1 1635 ? 60.32500   31.64100  16.13500  1.000 98.39213  ?  1633 ARG   B CB  1 
ATOM   26911 N  N   . SER   B 1 1636 ? 61.86700   32.51800  13.46600  1.000 111.78628 ?  1634 SER   B N   1 
ATOM   26912 C  CA  . SER   B 1 1636 ? 62.35800   32.14200  12.14200  1.000 116.18354 ?  1634 SER   B CA  1 
ATOM   26913 C  C   . SER   B 1 1636 ? 63.83500   32.48000  11.97900  1.000 123.78146 ?  1634 SER   B C   1 
ATOM   26914 O  O   . SER   B 1 1636 ? 64.58300   31.72800  11.34300  1.000 118.83181 ?  1634 SER   B O   1 
ATOM   26915 C  CB  . SER   B 1 1636 ? 61.52600   32.83100  11.05900  1.000 110.43919 ?  1634 SER   B CB  1 
ATOM   26916 O  OG  . SER   B 1 1636 ? 62.18500   32.80100  9.80400   1.000 119.40175 ?  1634 SER   B OG  1 
ATOM   26917 N  N   . LYS   B 1 1637 ? 64.27500   33.60700  12.54500  1.000 124.35060 ?  1635 LYS   B N   1 
ATOM   26918 C  CA  . LYS   B 1 1637 ? 65.68600   33.97000  12.46400  1.000 124.14475 ?  1635 LYS   B CA  1 
ATOM   26919 C  C   . LYS   B 1 1637 ? 66.54600   33.08200  13.35400  1.000 120.32847 ?  1635 LYS   B C   1 
ATOM   26920 O  O   . LYS   B 1 1637 ? 67.73600   32.89500  13.07500  1.000 117.94378 ?  1635 LYS   B O   1 
ATOM   26921 C  CB  . LYS   B 1 1637 ? 65.87300   35.44100  12.83800  1.000 105.06473 ?  1635 LYS   B CB  1 
ATOM   26922 N  N   . LEU   B 1 1638 ? 65.96600   32.52400  14.41900  1.000 113.19651 ?  1636 LEU   B N   1 
ATOM   26923 C  CA  . LEU   B 1 1638 ? 66.71900   31.65400  15.31500  1.000 111.52533 ?  1636 LEU   B CA  1 
ATOM   26924 C  C   . LEU   B 1 1638 ? 67.00400   30.29000  14.69800  1.000 118.80515 ?  1636 LEU   B C   1 
ATOM   26925 O  O   . LEU   B 1 1638 ? 67.94200   29.61200  15.13200  1.000 114.50809 ?  1636 LEU   B O   1 
ATOM   26926 C  CB  . LEU   B 1 1638 ? 65.96000   31.48600  16.63300  1.000 103.51240 ?  1636 LEU   B CB  1 
ATOM   26927 C  CG  . LEU   B 1 1638 ? 66.77900   31.59400  17.92200  1.000 99.45191  ?  1636 LEU   B CG  1 
ATOM   26928 C  CD1 . LEU   B 1 1638 ? 65.91800   32.12100  19.06200  1.000 78.83039  ?  1636 LEU   B CD1 1 
ATOM   26929 C  CD2 . LEU   B 1 1638 ? 67.39300   30.25100  18.28700  1.000 102.61892 ?  1636 LEU   B CD2 1 
ATOM   26930 N  N   . ILE   B 1 1639 ? 66.22600   29.87600  13.70200  1.000 112.21111 ?  1637 ILE   B N   1 
ATOM   26931 C  CA  . ILE   B 1 1639 ? 66.42600   28.58200  13.06000  1.000 108.40353 ?  1637 ILE   B CA  1 
ATOM   26932 C  C   . ILE   B 1 1639 ? 67.34700   28.72800  11.85400  1.000 98.62267  ?  1637 ILE   B C   1 
ATOM   26933 O  O   . ILE   B 1 1639 ? 68.52100   28.36400  11.91000  1.000 97.50472  ?  1637 ILE   B O   1 
ATOM   26934 C  CB  . ILE   B 1 1639 ? 65.08500   27.95100  12.64700  1.000 104.37890 ?  1637 ILE   B CB  1 
ATOM   26935 N  N   . ASP   B 1 1654 ? 59.17400   32.08500  20.38900  1.000 95.93139  ?  1652 ASP   B N   1 
ATOM   26936 C  CA  . ASP   B 1 1654 ? 59.29300   32.94700  21.55900  1.000 107.24516 ?  1652 ASP   B CA  1 
ATOM   26937 C  C   . ASP   B 1 1654 ? 57.91500   33.37500  22.05000  1.000 103.20542 ?  1652 ASP   B C   1 
ATOM   26938 O  O   . ASP   B 1 1654 ? 56.96900   33.41500  21.26100  1.000 109.99297 ?  1652 ASP   B O   1 
ATOM   26939 C  CB  . ASP   B 1 1654 ? 60.14400   34.17700  21.23400  1.000 81.29198  ?  1652 ASP   B CB  1 
ATOM   26940 N  N   . GLN   B 1 1655 ? 57.81300   33.68600  23.35000  1.000 89.95717  ?  1653 GLN   B N   1 
ATOM   26941 C  CA  . GLN   B 1 1655 ? 56.58100   34.19200  23.95500  1.000 101.66678 ?  1653 GLN   B CA  1 
ATOM   26942 C  C   . GLN   B 1 1655 ? 56.71500   34.44800  25.45400  1.000 102.96536 ?  1653 GLN   B C   1 
ATOM   26943 O  O   . GLN   B 1 1655 ? 57.81700   34.68800  25.96200  1.000 94.63943  ?  1653 GLN   B O   1 
ATOM   26944 C  CB  . GLN   B 1 1655 ? 55.41900   33.21900  23.73300  1.000 85.82736  ?  1653 GLN   B CB  1 
ATOM   26945 N  N   . ASN   B 1 1656 ? 55.57200   34.42600  26.14800  1.000 111.90933 ?  1654 ASN   B N   1 
ATOM   26946 C  CA  . ASN   B 1 1656 ? 55.45700   34.45800  27.60500  1.000 100.13865 ?  1654 ASN   B CA  1 
ATOM   26947 C  C   . ASN   B 1 1656 ? 55.79100   35.81800  28.20400  1.000 97.79461  ?  1654 ASN   B C   1 
ATOM   26948 O  O   . ASN   B 1 1656 ? 56.14200   36.76200  27.48800  1.000 95.37244  ?  1654 ASN   B O   1 
ATOM   26949 C  CB  . ASN   B 1 1656 ? 56.34300   33.38200  28.24100  1.000 82.43092  ?  1654 ASN   B CB  1 
ATOM   26950 N  N   . GLY   B 1 1657 ? 55.66500   35.91900  29.52500  1.000 93.23682  ?  1655 GLY   B N   1 
ATOM   26951 C  CA  . GLY   B 1 1657 ? 55.99800   37.12900  30.24500  1.000 84.63165  ?  1655 GLY   B CA  1 
ATOM   26952 C  C   . GLY   B 1 1657 ? 54.80000   37.86200  30.81000  1.000 103.36479 ?  1655 GLY   B C   1 
ATOM   26953 O  O   . GLY   B 1 1657 ? 53.88500   38.23800  30.07000  1.000 114.77337 ?  1655 GLY   B O   1 
ATOM   26954 N  N   . GLN   B 1 1658 ? 54.79400   38.07600  32.12700  1.000 109.81067 ?  1656 GLN   B N   1 
ATOM   26955 C  CA  . GLN   B 1 1658 ? 53.77800   38.93700  32.72000  1.000 105.08431 ?  1656 GLN   B CA  1 
ATOM   26956 C  C   . GLN   B 1 1658 ? 53.95700   40.39800  32.31300  1.000 118.86465 ?  1656 GLN   B C   1 
ATOM   26957 O  O   . GLN   B 1 1658 ? 52.98600   41.16300  32.35700  1.000 120.69986 ?  1656 GLN   B O   1 
ATOM   26958 C  CB  . GLN   B 1 1658 ? 53.79300   38.80000  34.24900  1.000 104.47189 ?  1656 GLN   B CB  1 
ATOM   26959 C  CG  . GLN   B 1 1658 ? 54.62300   39.84700  34.98200  1.000 111.71207 ?  1656 GLN   B CG  1 
ATOM   26960 C  CD  . GLN   B 1 1658 ? 56.08900   39.47200  35.08800  1.000 115.57086 ?  1656 GLN   B CD  1 
ATOM   26961 O  OE1 . GLN   B 1 1658 ? 56.63700   38.80500  34.21000  1.000 121.11159 ?  1656 GLN   B OE1 1 
ATOM   26962 N  NE2 . GLN   B 1 1658 ? 56.73300   39.90200  36.16700  1.000 96.11666  ?  1656 GLN   B NE2 1 
ATOM   26963 N  N   . ALA   B 1 1659 ? 55.16800   40.80000  31.90900  1.000 121.58777 ?  1657 ALA   B N   1 
ATOM   26964 C  CA  . ALA   B 1 1659 ? 55.42900   42.17400  31.49000  1.000 109.83674 ?  1657 ALA   B CA  1 
ATOM   26965 C  C   . ALA   B 1 1659 ? 56.54800   42.23100  30.45500  1.000 107.02245 ?  1657 ALA   B C   1 
ATOM   26966 O  O   . ALA   B 1 1659 ? 56.63100   43.19100  29.68300  1.000 96.55514  ?  1657 ALA   B O   1 
ATOM   26967 C  CB  . ALA   B 1 1659 ? 55.76900   43.05700  32.69600  1.000 86.68019  ?  1657 ALA   B CB  1 
ATOM   26968 N  N   . TYR   B 1 1660 ? 57.38500   41.20200  30.40000  1.000 104.46972 ?  1658 TYR   B N   1 
ATOM   26969 C  CA  . TYR   B 1 1660 ? 58.52400   41.17500  29.49200  1.000 94.98067  ?  1658 TYR   B CA  1 
ATOM   26970 C  C   . TYR   B 1 1660 ? 58.45400   39.94400  28.58400  1.000 102.27659 ?  1658 TYR   B C   1 
ATOM   26971 O  O   . TYR   B 1 1660 ? 57.42200   39.27600  28.47700  1.000 105.76656 ?  1658 TYR   B O   1 
ATOM   26972 C  CB  . TYR   B 1 1660 ? 59.82700   41.22000  30.28900  1.000 91.16273  ?  1658 TYR   B CB  1 
ATOM   26973 N  N   . LEU   B 1 1661 ? 59.56900   39.65800  27.91500  1.000 103.28772 ?  1659 LEU   B N   1 
ATOM   26974 C  CA  . LEU   B 1 1661 ? 59.65500   38.51300  27.01300  1.000 95.32967  ?  1659 LEU   B CA  1 
ATOM   26975 C  C   . LEU   B 1 1661 ? 60.82000   37.60300  27.38500  1.000 87.03898  ?  1659 LEU   B C   1 
ATOM   26976 O  O   . LEU   B 1 1661 ? 61.97900   37.92700  27.13000  1.000 90.75135  ?  1659 LEU   B O   1 
ATOM   26977 C  CB  . LEU   B 1 1661 ? 59.80200   38.97500  25.56100  1.000 73.86658  ?  1659 LEU   B CB  1 
ATOM   26978 N  N   . GLY   B 1 1674 ? 74.51600   34.37100  27.19300  1.000 94.31686  ?  1672 GLY   B N   1 
ATOM   26979 C  CA  . GLY   B 1 1674 ? 75.27900   35.51200  26.72200  1.000 110.54989 ?  1672 GLY   B CA  1 
ATOM   26980 C  C   . GLY   B 1 1674 ? 75.50800   35.50100  25.22300  1.000 116.01925 ?  1672 GLY   B C   1 
ATOM   26981 O  O   . GLY   B 1 1674 ? 75.26500   36.49800  24.54300  1.000 113.46043 ?  1672 GLY   B O   1 
ATOM   26982 N  N   . GLN   B 1 1675 ? 75.98000   34.36200  24.70700  1.000 116.78737 ?  1673 GLN   B N   1 
ATOM   26983 C  CA  . GLN   B 1 1675 ? 76.22800   34.23600  23.27500  1.000 107.86602 ?  1673 GLN   B CA  1 
ATOM   26984 C  C   . GLN   B 1 1675 ? 74.94800   34.33300  22.45900  1.000 120.34489 ?  1673 GLN   B C   1 
ATOM   26985 O  O   . GLN   B 1 1675 ? 75.00900   34.66200  21.26900  1.000 123.48803 ?  1673 GLN   B O   1 
ATOM   26986 C  CB  . GLN   B 1 1675 ? 76.93700   32.91400  22.97500  1.000 85.93257  ?  1673 GLN   B CB  1 
ATOM   26987 N  N   . LEU   B 1 1676 ? 73.79200   34.05400  23.06900  1.000 120.23848 ?  1674 LEU   B N   1 
ATOM   26988 C  CA  . LEU   B 1 1676 ? 72.52800   34.18800  22.35500  1.000 121.34370 ?  1674 LEU   B CA  1 
ATOM   26989 C  C   . LEU   B 1 1676 ? 72.21800   35.64300  22.02400  1.000 122.16738 ?  1674 LEU   B C   1 
ATOM   26990 O  O   . LEU   B 1 1676 ? 71.62800   35.92400  20.97400  1.000 125.78048 ?  1674 LEU   B O   1 
ATOM   26991 C  CB  . LEU   B 1 1676 ? 71.39200   33.57600  23.17900  1.000 78.47661  ?  1674 LEU   B CB  1 
ATOM   26992 N  N   . ARG   B 1 1677 ? 72.60800   36.57700  22.89900  1.000 111.86425 ?  1675 ARG   B N   1 
ATOM   26993 C  CA  . ARG   B 1 1677 ? 72.33100   37.98900  22.65100  1.000 96.29611  ?  1675 ARG   B CA  1 
ATOM   26994 C  C   . ARG   B 1 1677 ? 73.08000   38.50900  21.43000  1.000 112.53659 ?  1675 ARG   B C   1 
ATOM   26995 O  O   . ARG   B 1 1677 ? 72.60800   39.43600  20.76400  1.000 105.35457 ?  1675 ARG   B O   1 
ATOM   26996 C  CB  . ARG   B 1 1677 ? 72.68800   38.82100  23.88400  1.000 87.22563  ?  1675 ARG   B CB  1 
ATOM   26997 N  N   . GLU   B 1 1678 ? 74.24500   37.93300  21.12200  1.000 123.50996 ?  1676 GLU   B N   1 
ATOM   26998 C  CA  . GLU   B 1 1678 ? 74.97600   38.33500  19.92300  1.000 126.14368 ?  1676 GLU   B CA  1 
ATOM   26999 C  C   . GLU   B 1 1678 ? 74.23700   37.89900  18.66200  1.000 132.62165 ?  1676 GLU   B C   1 
ATOM   27000 O  O   . GLU   B 1 1678 ? 74.00200   38.70800  17.75600  1.000 133.08631 ?  1676 GLU   B O   1 
ATOM   27001 C  CB  . GLU   B 1 1678 ? 76.39100   37.75700  19.95400  1.000 101.72393 ?  1676 GLU   B CB  1 
ATOM   27002 N  N   . LEU   B 1 1679 ? 73.86200   36.62300  18.58700  1.000 126.41209 ?  1677 LEU   B N   1 
ATOM   27003 C  CA  . LEU   B 1 1679 ? 72.97400   36.16600  17.53000  1.000 121.39133 ?  1677 LEU   B CA  1 
ATOM   27004 C  C   . LEU   B 1 1679 ? 71.64500   36.91400  17.60800  1.000 125.80039 ?  1677 LEU   B C   1 
ATOM   27005 O  O   . LEU   B 1 1679 ? 71.32600   37.56400  18.60800  1.000 128.50551 ?  1677 LEU   B O   1 
ATOM   27006 C  CB  . LEU   B 1 1679 ? 72.74500   34.65700  17.63500  1.000 102.93951 ?  1677 LEU   B CB  1 
ATOM   27007 C  CG  . LEU   B 1 1679 ? 73.53600   33.75700  16.68000  1.000 110.56685 ?  1677 LEU   B CG  1 
ATOM   27008 C  CD1 . LEU   B 1 1679 ? 72.90000   33.73300  15.29600  1.000 89.98995  ?  1677 LEU   B CD1 1 
ATOM   27009 C  CD2 . LEU   B 1 1679 ? 74.99600   34.18800  16.59800  1.000 105.92456 ?  1677 LEU   B CD2 1 
ATOM   27010 N  N   . LEU   B 1 1680 ? 70.86900   36.82400  16.52600  1.000 127.35510 ?  1678 LEU   B N   1 
ATOM   27011 C  CA  . LEU   B 1 1680 ? 69.59800   37.53400  16.39500  1.000 133.22173 ?  1678 LEU   B CA  1 
ATOM   27012 C  C   . LEU   B 1 1680 ? 69.79800   39.04800  16.39600  1.000 134.20800 ?  1678 LEU   B C   1 
ATOM   27013 O  O   . LEU   B 1 1680 ? 69.49200   39.70700  15.39800  1.000 143.89486 ?  1678 LEU   B O   1 
ATOM   27014 C  CB  . LEU   B 1 1680 ? 68.61800   37.11800  17.49800  1.000 111.62816 ?  1678 LEU   B CB  1 
ATOM   27015 N  N   . ARG   B 1 1681 ? 70.32300   39.60900  17.49500  1.000 121.77045 ?  1679 ARG   B N   1 
ATOM   27016 C  CA  . ARG   B 1 1681 ? 70.51400   41.05700  17.58400  1.000 111.28821 ?  1679 ARG   B CA  1 
ATOM   27017 C  C   . ARG   B 1 1681 ? 71.33300   41.60700  16.42400  1.000 115.05636 ?  1679 ARG   B C   1 
ATOM   27018 O  O   . ARG   B 1 1681 ? 71.22800   42.79500  16.09800  1.000 114.09518 ?  1679 ARG   B O   1 
ATOM   27019 C  CB  . ARG   B 1 1681 ? 71.18400   41.42600  18.90900  1.000 95.55032  ?  1679 ARG   B CB  1 
ATOM   27020 N  N   . ARG   B 1 1682 ? 72.15900   40.76400  15.79400  1.000 113.96178 ?  1680 ARG   B N   1 
ATOM   27021 C  CA  . ARG   B 1 1682 ? 72.82000   41.15900  14.55500  1.000 108.69050 ?  1680 ARG   B CA  1 
ATOM   27022 C  C   . ARG   B 1 1682 ? 71.80500   41.60500  13.50900  1.000 111.75326 ?  1680 ARG   B C   1 
ATOM   27023 O  O   . ARG   B 1 1682 ? 72.04800   42.55900  12.76100  1.000 119.90978 ?  1680 ARG   B O   1 
ATOM   27024 C  CB  . ARG   B 1 1682 ? 73.66500   40.00100  14.02100  1.000 101.08153 ?  1680 ARG   B CB  1 
ATOM   27025 N  N   . GLU   B 1 1683 ? 70.65500   40.93300  13.44900  1.000 120.10977 ?  1681 GLU   B N   1 
ATOM   27026 C  CA  . GLU   B 1 1683 ? 69.57500   41.25900  12.52400  1.000 107.03573 ?  1681 GLU   B CA  1 
ATOM   27027 C  C   . GLU   B 1 1683 ? 68.25700   41.42400  13.27000  1.000 109.65325 ?  1681 GLU   B C   1 
ATOM   27028 O  O   . GLU   B 1 1683 ? 67.19400   41.01800  12.79200  1.000 114.98143 ?  1681 GLU   B O   1 
ATOM   27029 C  CB  . GLU   B 1 1683 ? 69.44200   40.19500  11.43700  1.000 105.93532 ?  1681 GLU   B CB  1 
ATOM   27030 C  CG  . GLU   B 1 1683 ? 70.56100   40.21000  10.40400  1.000 120.73587 ?  1681 GLU   B CG  1 
ATOM   27031 C  CD  . GLU   B 1 1683 ? 70.07100   40.58300  9.01500   1.000 121.52061 ?  1681 GLU   B CD  1 
ATOM   27032 O  OE1 . GLU   B 1 1683 ? 68.90500   41.01600  8.89200   1.000 125.27777 ?  1681 GLU   B OE1 1 
ATOM   27033 O  OE2 . GLU   B 1 1683 ? 70.85200   40.44000  8.04800   1.000 119.08967 ?  1681 GLU   B OE2 1 
ATOM   27034 N  N   . LEU   B 1 1684 ? 68.30500   42.01700  14.46100  1.000 115.70245 ?  1682 LEU   B N   1 
ATOM   27035 C  CA  . LEU   B 1 1684 ? 67.10600   42.22600  15.25900  1.000 111.44751 ?  1682 LEU   B CA  1 
ATOM   27036 C  C   . LEU   B 1 1684 ? 67.27800   43.48800  16.08500  1.000 111.57872 ?  1682 LEU   B C   1 
ATOM   27037 O  O   . LEU   B 1 1684 ? 68.39400   43.79200  16.52300  1.000 110.82088 ?  1682 LEU   B O   1 
ATOM   27038 C  CB  . LEU   B 1 1684 ? 66.81600   41.03600  16.18600  1.000 96.55428  ?  1682 LEU   B CB  1 
ATOM   27039 N  N   . PRO   B 1 1685 ? 66.20500   44.24000  16.31300  1.000 114.33245 ?  1683 PRO   B N   1 
ATOM   27040 C  CA  . PRO   B 1 1685 ? 66.28200   45.36600  17.24500  1.000 104.99384 ?  1683 PRO   B CA  1 
ATOM   27041 C  C   . PRO   B 1 1685 ? 66.37400   44.87200  18.68000  1.000 112.01329 ?  1683 PRO   B C   1 
ATOM   27042 O  O   . PRO   B 1 1685 ? 66.06900   43.72000  18.99400  1.000 112.02818 ?  1683 PRO   B O   1 
ATOM   27043 C  CB  . PRO   B 1 1685 ? 64.97700   46.12600  16.99900  1.000 97.87140  ?  1683 PRO   B CB  1 
ATOM   27044 C  CG  . PRO   B 1 1685 ? 64.03500   45.10300  16.46100  1.000 100.57237 ?  1683 PRO   B CG  1 
ATOM   27045 C  CD  . PRO   B 1 1685 ? 64.85500   44.06300  15.75100  1.000 114.20896 ?  1683 PRO   B CD  1 
ATOM   27046 N  N   . GLU   B 1 1686 ? 66.81200   45.77600  19.56000  1.000 114.36379 ?  1684 GLU   B N   1 
ATOM   27047 C  CA  . GLU   B 1 1686 ? 66.89800   45.43700  20.97600  1.000 110.17335 ?  1684 GLU   B CA  1 
ATOM   27048 C  C   . GLU   B 1 1686 ? 65.52400   45.09600  21.54500  1.000 106.67689 ?  1684 GLU   B C   1 
ATOM   27049 O  O   . GLU   B 1 1686 ? 65.37700   44.10900  22.27700  1.000 102.92860 ?  1684 GLU   B O   1 
ATOM   27050 C  CB  . GLU   B 1 1686 ? 67.54000   46.58900  21.75100  1.000 91.62941  ?  1684 GLU   B CB  1 
ATOM   27051 N  N   . TYR   B 1 1687 ? 64.50000   45.88500  21.19800  1.000 102.60448 ?  1685 TYR   B N   1 
ATOM   27052 C  CA  . TYR   B 1 1687 ? 63.14000   45.60800  21.65500  1.000 108.20565 ?  1685 TYR   B CA  1 
ATOM   27053 C  C   . TYR   B 1 1687 ? 62.64800   44.22500  21.23800  1.000 108.58878 ?  1685 TYR   B C   1 
ATOM   27054 O  O   . TYR   B 1 1687 ? 61.73400   43.69000  21.87700  1.000 99.40760  ?  1685 TYR   B O   1 
ATOM   27055 C  CB  . TYR   B 1 1687 ? 62.17400   46.67500  21.12600  1.000 76.72917  ?  1685 TYR   B CB  1 
ATOM   27056 N  N   . MET   B 1 1688 ? 63.21200   43.64600  20.17900  1.000 100.94922 ?  1686 MET   B N   1 
ATOM   27057 C  CA  . MET   B 1 1688 ? 62.87600   42.29400  19.72800  1.000 105.52956 ?  1686 MET   B CA  1 
ATOM   27058 C  C   . MET   B 1 1688 ? 63.93400   41.27700  20.13800  1.000 114.07072 ?  1686 MET   B C   1 
ATOM   27059 O  O   . MET   B 1 1688 ? 64.28400   40.38100  19.36300  1.000 119.60276 ?  1686 MET   B O   1 
ATOM   27060 C  CB  . MET   B 1 1688 ? 62.67300   42.27000  18.21600  1.000 104.39572 ?  1686 MET   B CB  1 
ATOM   27061 N  N   . ILE   B 1 1689 ? 64.46500   41.39600  21.35000  1.000 104.46930 ?  1687 ILE   B N   1 
ATOM   27062 C  CA  . ILE   B 1 1689 ? 65.44100   40.46100  21.89000  1.000 101.77220 ?  1687 ILE   B CA  1 
ATOM   27063 C  C   . ILE   B 1 1689 ? 64.90000   39.94100  23.21700  1.000 100.27245 ?  1687 ILE   B C   1 
ATOM   27064 O  O   . ILE   B 1 1689 ? 64.58000   40.73600  24.10500  1.000 96.21615  ?  1687 ILE   B O   1 
ATOM   27065 C  CB  . ILE   B 1 1689 ? 66.82300   41.10800  22.08300  1.000 88.99228  ?  1687 ILE   B CB  1 
ATOM   27066 N  N   . PRO   B 1 1690 ? 64.77300   38.62700  23.40000  1.000 100.25808 ?  1688 PRO   B N   1 
ATOM   27067 C  CA  . PRO   B 1 1690 ? 64.23600   38.10500  24.66400  1.000 97.67328  ?  1688 PRO   B CA  1 
ATOM   27068 C  C   . PRO   B 1 1690 ? 65.13400   38.45800  25.84100  1.000 106.80676 ?  1688 PRO   B C   1 
ATOM   27069 O  O   . PRO   B 1 1690 ? 66.35700   38.31100  25.78000  1.000 102.12424 ?  1688 PRO   B O   1 
ATOM   27070 C  CB  . PRO   B 1 1690 ? 64.18000   36.59000  24.42800  1.000 90.35685  ?  1688 PRO   B CB  1 
ATOM   27071 C  CG  . PRO   B 1 1690 ? 65.11800   36.33700  23.28500  1.000 87.58200  ?  1688 PRO   B CG  1 
ATOM   27072 C  CD  . PRO   B 1 1690 ? 65.04400   37.55800  22.42600  1.000 93.88569  ?  1688 PRO   B CD  1 
ATOM   27073 N  N   . ALA   B 1 1691 ? 64.51400   38.93000  26.91900  1.000 101.86388 ?  1689 ALA   B N   1 
ATOM   27074 C  CA  . ALA   B 1 1691 ? 65.24300   39.31900  28.12000  1.000 94.69337  ?  1689 ALA   B CA  1 
ATOM   27075 C  C   . ALA   B 1 1691 ? 65.56900   38.10500  28.98800  1.000 94.76879  ?  1689 ALA   B C   1 
ATOM   27076 O  O   . ALA   B 1 1691 ? 64.83500   37.77900  29.92300  1.000 103.94546 ?  1689 ALA   B O   1 
ATOM   27077 C  CB  . ALA   B 1 1691 ? 64.44400   40.34100  28.91400  1.000 80.87676  ?  1689 ALA   B CB  1 
ATOM   27078 N  N   . PRO   B 1 1728 ? 93.40600   38.67400  26.99100  1.000 99.65204  ?  1726 PRO   B N   1 
ATOM   27079 C  CA  . PRO   B 1 1728 ? 94.60600   39.51300  27.07000  1.000 92.49890  ?  1726 PRO   B CA  1 
ATOM   27080 C  C   . PRO   B 1 1728 ? 95.83900   38.81300  26.51000  1.000 96.40885  ?  1726 PRO   B C   1 
ATOM   27081 O  O   . PRO   B 1 1728 ? 96.76300   38.50800  27.26300  1.000 105.49111 ?  1726 PRO   B O   1 
ATOM   27082 C  CB  . PRO   B 1 1728 ? 94.75600   39.76300  28.57100  1.000 84.39179  ?  1726 PRO   B CB  1 
ATOM   27083 C  CG  . PRO   B 1 1728 ? 93.36300   39.70200  29.09300  1.000 95.70490  ?  1726 PRO   B CG  1 
ATOM   27084 C  CD  . PRO   B 1 1728 ? 92.64700   38.67300  28.25500  1.000 94.66942  ?  1726 PRO   B CD  1 
ATOM   27085 N  N   . ARG   B 1 1729 ? 95.84700   38.56600  25.19900  1.000 92.29052  ?  1727 ARG   B N   1 
ATOM   27086 C  CA  . ARG   B 1 1729 ? 96.94400   37.83100  24.55600  1.000 93.68531  ?  1727 ARG   B CA  1 
ATOM   27087 C  C   . ARG   B 1 1729 ? 98.05300   38.78000  24.10800  1.000 103.23510 ?  1727 ARG   B C   1 
ATOM   27088 O  O   . ARG   B 1 1729 ? 99.14200   38.79600  24.69000  1.000 92.19191  ?  1727 ARG   B O   1 
ATOM   27089 C  CB  . ARG   B 1 1729 ? 96.40700   37.01100  23.38100  1.000 83.11709  ?  1727 ARG   B CB  1 
ATOM   27090 N  N   . THR   B 1 1730 ? 97.78700   39.57200  23.07200  1.000 105.99042 ?  1728 THR   B N   1 
ATOM   27091 C  CA  . THR   B 1 1730 ? 98.79700   40.45800  22.51500  1.000 97.81765  ?  1728 THR   B CA  1 
ATOM   27092 C  C   . THR   B 1 1730 ? 98.92600   41.73300  23.34400  1.000 95.79802  ?  1728 THR   B C   1 
ATOM   27093 O  O   . THR   B 1 1730 ? 98.03000   42.10700  24.10600  1.000 93.36236  ?  1728 THR   B O   1 
ATOM   27094 C  CB  . THR   B 1 1730 ? 98.46100   40.81800  21.06600  1.000 81.73821  ?  1728 THR   B CB  1 
ATOM   27095 N  N   . GLU   B 1 1731 ? 100.07200  42.40100  23.18800  1.000 102.27902 ?  1729 GLU   B N   1 
ATOM   27096 C  CA  . GLU   B 1 1731 ? 100.25900  43.69800  23.82700  1.000 96.94660  ?  1729 GLU   B CA  1 
ATOM   27097 C  C   . GLU   B 1 1731 ? 99.23700   44.70800  23.32800  1.000 88.38746  ?  1729 GLU   B C   1 
ATOM   27098 O  O   . GLU   B 1 1731 ? 98.80100   45.57900  24.08900  1.000 81.83190  ?  1729 GLU   B O   1 
ATOM   27099 C  CB  . GLU   B 1 1731 ? 101.67900  44.21000  23.58100  1.000 94.34773  ?  1729 GLU   B CB  1 
ATOM   27100 C  CG  . GLU   B 1 1731 ? 102.77600  43.25800  24.03000  1.000 112.14297 ?  1729 GLU   B CG  1 
ATOM   27101 C  CD  . GLU   B 1 1731 ? 103.23000  43.52100  25.45500  1.000 131.43775 ?  1729 GLU   B CD  1 
ATOM   27102 O  OE1 . GLU   B 1 1731 ? 102.36300  43.73600  26.32800  1.000 136.68032 ?  1729 GLU   B OE1 1 
ATOM   27103 O  OE2 . GLU   B 1 1731 ? 104.45500  43.51400  25.70200  1.000 119.11234 -1 1729 GLU   B OE2 1 
ATOM   27104 N  N   . LEU   B 1 1732 ? 98.84500   44.60500  22.05600  1.000 86.18332  ?  1730 LEU   B N   1 
ATOM   27105 C  CA  . LEU   B 1 1732 ? 97.78800   45.46100  21.53200  1.000 81.36608  ?  1730 LEU   B CA  1 
ATOM   27106 C  C   . LEU   B 1 1732 ? 96.47700   45.21300  22.26400  1.000 83.35181  ?  1730 LEU   B C   1 
ATOM   27107 O  O   . LEU   B 1 1732 ? 95.81700   46.15500  22.71700  1.000 75.64529  ?  1730 LEU   B O   1 
ATOM   27108 C  CB  . LEU   B 1 1732 ? 97.62000   45.22600  20.03100  1.000 79.19083  ?  1730 LEU   B CB  1 
ATOM   27109 C  CG  . LEU   B 1 1732 ? 96.70400   46.21100  19.30500  1.000 78.35515  ?  1730 LEU   B CG  1 
ATOM   27110 C  CD1 . LEU   B 1 1732 ? 97.06900   47.64700  19.65400  1.000 60.55831  ?  1730 LEU   B CD1 1 
ATOM   27111 C  CD2 . LEU   B 1 1732 ? 96.75400   45.98300  17.80200  1.000 69.68450  ?  1730 LEU   B CD2 1 
ATOM   27112 N  N   . GLU   B 1 1733 ? 96.08800   43.94000  22.38900  1.000 91.87836  ?  1731 GLU   B N   1 
ATOM   27113 C  CA  . GLU   B 1 1733 ? 94.88600   43.59400  23.14100  1.000 85.60572  ?  1731 GLU   B CA  1 
ATOM   27114 C  C   . GLU   B 1 1733 ? 94.97200   44.09400  24.57700  1.000 80.80216  ?  1731 GLU   B C   1 
ATOM   27115 O  O   . GLU   B 1 1733 ? 94.00500   44.65800  25.10500  1.000 87.96827  ?  1731 GLU   B O   1 
ATOM   27116 C  CB  . GLU   B 1 1733 ? 94.67100   42.08000  23.11700  1.000 82.81215  ?  1731 GLU   B CB  1 
ATOM   27117 C  CG  . GLU   B 1 1733 ? 93.85300   41.57500  21.94000  1.000 97.18276  ?  1731 GLU   B CG  1 
ATOM   27118 C  CD  . GLU   B 1 1733 ? 94.70700   41.24500  20.73200  1.000 105.35348 ?  1731 GLU   B CD  1 
ATOM   27119 O  OE1 . GLU   B 1 1733 ? 95.57800   42.06600  20.37400  1.000 105.64917 ?  1731 GLU   B OE1 1 
ATOM   27120 O  OE2 . GLU   B 1 1733 ? 94.50500   40.16400  20.13800  1.000 100.75447 -1 1731 GLU   B OE2 1 
ATOM   27121 N  N   . ALA   B 1 1734 ? 96.12500   43.90200  25.22300  1.000 68.14310  ?  1732 ALA   B N   1 
ATOM   27122 C  CA  . ALA   B 1 1734 ? 96.29500   44.37200  26.59300  1.000 71.21704  ?  1732 ALA   B CA  1 
ATOM   27123 C  C   . ALA   B 1 1734 ? 96.18600   45.89000  26.67700  1.000 79.76707  ?  1732 ALA   B C   1 
ATOM   27124 O  O   . ALA   B 1 1734 ? 95.55300   46.42400  27.59400  1.000 76.66989  ?  1732 ALA   B O   1 
ATOM   27125 C  CB  . ALA   B 1 1734 ? 97.63900   43.89800  27.14600  1.000 76.34221  ?  1732 ALA   B CB  1 
ATOM   27126 N  N   . THR   B 1 1735 ? 96.79800   46.60200  25.72800  1.000 79.81198  ?  1733 THR   B N   1 
ATOM   27127 C  CA  . THR   B 1 1735 ? 96.71300   48.05900  25.73200  1.000 81.51523  ?  1733 THR   B CA  1 
ATOM   27128 C  C   . THR   B 1 1735 ? 95.29700   48.52400  25.41100  1.000 80.89993  ?  1733 THR   B C   1 
ATOM   27129 O  O   . THR   B 1 1735 ? 94.76100   49.41700  26.07800  1.000 72.45640  ?  1733 THR   B O   1 
ATOM   27130 C  CB  . THR   B 1 1735 ? 97.71300   48.65000  24.73600  1.000 80.88466  ?  1733 THR   B CB  1 
ATOM   27131 O  OG1 . THR   B 1 1735 ? 98.93600   47.90400  24.78600  1.000 81.87134  ?  1733 THR   B OG1 1 
ATOM   27132 C  CG2 . THR   B 1 1735 ? 97.99800   50.11000  25.06500  1.000 67.55362  ?  1733 THR   B CG2 1 
ATOM   27133 N  N   . LEU   B 1 1736 ? 94.67800   47.92500  24.38900  1.000 86.43749  ?  1734 LEU   B N   1 
ATOM   27134 C  CA  . LEU   B 1 1736 ? 93.31200   48.29000  24.02400  1.000 72.64250  ?  1734 LEU   B CA  1 
ATOM   27135 C  C   . LEU   B 1 1736 ? 92.35500   48.07600  25.18800  1.000 79.89926  ?  1734 LEU   B C   1 
ATOM   27136 O  O   . LEU   B 1 1736 ? 91.49400   48.92300  25.45900  1.000 74.33790  ?  1734 LEU   B O   1 
ATOM   27137 C  CB  . LEU   B 1 1736 ? 92.86100   47.48100  22.80700  1.000 59.92832  ?  1734 LEU   B CB  1 
ATOM   27138 C  CG  . LEU   B 1 1736 ? 93.35000   47.94800  21.43400  1.000 67.16231  ?  1734 LEU   B CG  1 
ATOM   27139 C  CD1 . LEU   B 1 1736 ? 93.14100   46.85900  20.38800  1.000 65.84155  ?  1734 LEU   B CD1 1 
ATOM   27140 C  CD2 . LEU   B 1 1736 ? 92.64700   49.23400  21.02600  1.000 69.46264  ?  1734 LEU   B CD2 1 
ATOM   27141 N  N   . ALA   B 1 1737 ? 92.49600   46.95200  25.89400  1.000 75.78543  ?  1735 ALA   B N   1 
ATOM   27142 C  CA  . ALA   B 1 1737 ? 91.64100   46.68100  27.04500  1.000 80.82904  ?  1735 ALA   B CA  1 
ATOM   27143 C  C   . ALA   B 1 1737 ? 91.85600   47.71500  28.14300  1.000 76.42500  ?  1735 ALA   B C   1 
ATOM   27144 O  O   . ALA   B 1 1737 ? 90.89400   48.22800  28.72600  1.000 88.62101  ?  1735 ALA   B O   1 
ATOM   27145 C  CB  . ALA   B 1 1737 ? 91.90300   45.26900  27.56800  1.000 72.58340  ?  1735 ALA   B CB  1 
ATOM   27146 N  N   . HIS   B 1 1738 ? 93.11800   48.03600  28.43800  1.000 59.01826  ?  1736 HIS   B N   1 
ATOM   27147 C  CA  . HIS   B 1 1738 ? 93.41000   49.06500  29.43000  1.000 71.97690  ?  1736 HIS   B CA  1 
ATOM   27148 C  C   . HIS   B 1 1738 ? 92.83400   50.41300  29.01300  1.000 85.96710  ?  1736 HIS   B C   1 
ATOM   27149 O  O   . HIS   B 1 1738 ? 92.29600   51.15200  29.84600  1.000 88.35281  ?  1736 HIS   B O   1 
ATOM   27150 C  CB  . HIS   B 1 1738 ? 94.92000   49.16700  29.64700  1.000 74.93423  ?  1736 HIS   B CB  1 
ATOM   27151 C  CG  . HIS   B 1 1738 ? 95.32700   50.28400  30.55500  1.000 71.25202  ?  1736 HIS   B CG  1 
ATOM   27152 N  ND1 . HIS   B 1 1738 ? 95.99600   51.40200  30.10500  1.000 93.32644  ?  1736 HIS   B ND1 1 
ATOM   27153 C  CD2 . HIS   B 1 1738 ? 95.16700   50.45400  31.88900  1.000 84.69369  ?  1736 HIS   B CD2 1 
ATOM   27154 C  CE1 . HIS   B 1 1738 ? 96.22600   52.21500  31.12100  1.000 92.40456  ?  1736 HIS   B CE1 1 
ATOM   27155 N  NE2 . HIS   B 1 1738 ? 95.73300   51.66300  32.21500  1.000 97.45285  ?  1736 HIS   B NE2 1 
ATOM   27156 N  N   . ILE   B 1 1739 ? 92.93100   50.74700  27.72400  1.000 82.76521  ?  1737 ILE   B N   1 
ATOM   27157 C  CA  . ILE   B 1 1739 ? 92.37700   52.00500  27.23200  1.000 85.64063  ?  1737 ILE   B CA  1 
ATOM   27158 C  C   . ILE   B 1 1739 ? 90.85400   51.96900  27.27300  1.000 90.85317  ?  1737 ILE   B C   1 
ATOM   27159 O  O   . ILE   B 1 1739 ? 90.21000   52.89100  27.78800  1.000 90.06823  ?  1737 ILE   B O   1 
ATOM   27160 C  CB  . ILE   B 1 1739 ? 92.89500   52.30300  25.81200  1.000 88.78168  ?  1737 ILE   B CB  1 
ATOM   27161 C  CG1 . ILE   B 1 1739 ? 94.37400   52.69100  25.85100  1.000 73.57427  ?  1737 ILE   B CG1 1 
ATOM   27162 C  CG2 . ILE   B 1 1739 ? 92.07000   53.40400  25.15700  1.000 92.21304  ?  1737 ILE   B CG2 1 
ATOM   27163 C  CD1 . ILE   B 1 1739 ? 94.65400   53.94700  26.64500  1.000 73.36837  ?  1737 ILE   B CD1 1 
ATOM   27164 N  N   . TRP   B 1 1740 ? 90.25800   50.90600  26.72100  1.000 80.68149  ?  1738 TRP   B N   1 
ATOM   27165 C  CA  . TRP   B 1 1740 ? 88.80500   50.75100  26.75600  1.000 72.75741  ?  1738 TRP   B CA  1 
ATOM   27166 C  C   . TRP   B 1 1740 ? 88.27200   50.91100  28.17300  1.000 85.25392  ?  1738 TRP   B C   1 
ATOM   27167 O  O   . TRP   B 1 1740 ? 87.33800   51.68200  28.41700  1.000 97.88984  ?  1738 TRP   B O   1 
ATOM   27168 C  CB  . TRP   B 1 1740 ? 88.40700   49.38400  26.19700  1.000 66.88045  ?  1738 TRP   B CB  1 
ATOM   27169 C  CG  . TRP   B 1 1740 ? 88.36400   49.30100  24.70300  1.000 70.14414  ?  1738 TRP   B CG  1 
ATOM   27170 C  CD1 . TRP   B 1 1740 ? 89.17500   49.95000  23.81800  1.000 87.55360  ?  1738 TRP   B CD1 1 
ATOM   27171 C  CD2 . TRP   B 1 1740 ? 87.47000   48.50500  23.91800  1.000 81.10793  ?  1738 TRP   B CD2 1 
ATOM   27172 N  NE1 . TRP   B 1 1740 ? 88.83600   49.61300  22.52900  1.000 92.91021  ?  1738 TRP   B NE1 1 
ATOM   27173 C  CE2 . TRP   B 1 1740 ? 87.79200   48.72600  22.56400  1.000 96.75588  ?  1738 TRP   B CE2 1 
ATOM   27174 C  CE3 . TRP   B 1 1740 ? 86.42600   47.62800  24.22800  1.000 87.26056  ?  1738 TRP   B CE3 1 
ATOM   27175 C  CZ2 . TRP   B 1 1740 ? 87.10700   48.10300  21.52200  1.000 92.58381  ?  1738 TRP   B CZ2 1 
ATOM   27176 C  CZ3 . TRP   B 1 1740 ? 85.74700   47.01100  23.19400  1.000 102.03053 ?  1738 TRP   B CZ3 1 
ATOM   27177 C  CH2 . TRP   B 1 1740 ? 86.09000   47.25100  21.85700  1.000 93.06468  ?  1738 TRP   B CH2 1 
ATOM   27178 N  N   . GLY   B 1 1741 ? 88.87600   50.20200  29.12700  1.000 76.17212  ?  1739 GLY   B N   1 
ATOM   27179 C  CA  . GLY   B 1 1741 ? 88.37000   50.23400  30.48800  1.000 83.08845  ?  1739 GLY   B CA  1 
ATOM   27180 C  C   . GLY   B 1 1741 ? 88.57900   51.57000  31.17500  1.000 82.39249  ?  1739 GLY   B C   1 
ATOM   27181 O  O   . GLY   B 1 1741 ? 87.73600   52.01000  31.96100  1.000 102.74434 ?  1739 GLY   B O   1 
ATOM   27182 N  N   . GLU   B 1 1742 ? 89.69900   52.23800  30.88900  1.000 82.42227  ?  1740 GLU   B N   1 
ATOM   27183 C  CA  . GLU   B 1 1742 ? 90.01800   53.47700  31.59000  1.000 97.19712  ?  1740 GLU   B CA  1 
ATOM   27184 C  C   . GLU   B 1 1742 ? 89.04600   54.60600  31.26400  1.000 101.09504 ?  1740 GLU   B C   1 
ATOM   27185 O  O   . GLU   B 1 1742 ? 88.99300   55.59100  32.00900  1.000 104.75386 ?  1740 GLU   B O   1 
ATOM   27186 C  CB  . GLU   B 1 1742 ? 91.44900   53.91200  31.26900  1.000 94.05928  ?  1740 GLU   B CB  1 
ATOM   27187 C  CG  . GLU   B 1 1742 ? 92.06500   54.83800  32.30900  1.000 100.28084 ?  1740 GLU   B CG  1 
ATOM   27188 C  CD  . GLU   B 1 1742 ? 93.47100   54.42700  32.70000  1.000 121.05299 ?  1740 GLU   B CD  1 
ATOM   27189 O  OE1 . GLU   B 1 1742 ? 93.61300   53.49200  33.51700  1.000 120.73431 ?  1740 GLU   B OE1 1 
ATOM   27190 O  OE2 . GLU   B 1 1742 ? 94.43400   55.04000  32.19400  1.000 130.96211 -1 1740 GLU   B OE2 1 
ATOM   27191 N  N   . VAL   B 1 1743 ? 88.27900   54.49200  30.18100  1.000 93.61934  ?  1741 VAL   B N   1 
ATOM   27192 C  CA  . VAL   B 1 1743 ? 87.32100   55.53300  29.82300  1.000 94.99805  ?  1741 VAL   B CA  1 
ATOM   27193 C  C   . VAL   B 1 1743 ? 85.91600   55.07500  30.19500  1.000 98.44757  ?  1741 VAL   B C   1 
ATOM   27194 O  O   . VAL   B 1 1743 ? 85.03900   55.89800  30.48000  1.000 103.62486 ?  1741 VAL   B O   1 
ATOM   27195 C  CB  . VAL   B 1 1743 ? 87.41700   55.90500  28.32900  1.000 97.99093  ?  1741 VAL   B CB  1 
ATOM   27196 C  CG1 . VAL   B 1 1743 ? 88.87200   56.00300  27.89400  1.000 86.98731  ?  1741 VAL   B CG1 1 
ATOM   27197 C  CG2 . VAL   B 1 1743 ? 86.66700   54.90700  27.46300  1.000 85.46624  ?  1741 VAL   B CG2 1 
ATOM   27198 N  N   . LEU   B 1 1744 ? 85.69600   53.75900  30.20800  1.000 93.52732  ?  1742 LEU   B N   1 
ATOM   27199 C  CA  . LEU   B 1 1744 ? 84.39100   53.20800  30.54800  1.000 80.39519  ?  1742 LEU   B CA  1 
ATOM   27200 C  C   . LEU   B 1 1744 ? 84.24800   52.88500  32.02800  1.000 86.23104  ?  1742 LEU   B C   1 
ATOM   27201 O  O   . LEU   B 1 1744 ? 83.11700   52.77800  32.51500  1.000 110.89287 ?  1742 LEU   B O   1 
ATOM   27202 C  CB  . LEU   B 1 1744 ? 84.11700   51.94000  29.73200  1.000 77.09785  ?  1742 LEU   B CB  1 
ATOM   27203 C  CG  . LEU   B 1 1744 ? 84.23300   52.01400  28.20800  1.000 90.74402  ?  1742 LEU   B CG  1 
ATOM   27204 C  CD1 . LEU   B 1 1744 ? 84.33800   50.61500  27.61300  1.000 90.19897  ?  1742 LEU   B CD1 1 
ATOM   27205 C  CD2 . LEU   B 1 1744 ? 83.06000   52.77000  27.60600  1.000 112.88799 ?  1742 LEU   B CD2 1 
ATOM   27206 N  N   . GLY   B 1 1745 ? 85.35900   52.73100  32.75100  1.000 102.67609 ?  1743 GLY   B N   1 
ATOM   27207 C  CA  . GLY   B 1 1745 ? 85.33700   52.36600  34.15100  1.000 100.48706 ?  1743 GLY   B CA  1 
ATOM   27208 C  C   . GLY   B 1 1745 ? 85.40400   50.87800  34.42400  1.000 95.24446  ?  1743 GLY   B C   1 
ATOM   27209 O  O   . GLY   B 1 1745 ? 85.56500   50.48400  35.58600  1.000 85.59981  ?  1743 GLY   B O   1 
ATOM   27210 N  N   . ILE   B 1 1746 ? 85.29600   50.04000  33.39000  1.000 90.64413  ?  1744 ILE   B N   1 
ATOM   27211 C  CA  . ILE   B 1 1746 ? 85.26400   48.58800  33.52400  1.000 96.29300  ?  1744 ILE   B CA  1 
ATOM   27212 C  C   . ILE   B 1 1746 ? 86.69800   48.06700  33.56600  1.000 110.66884 ?  1744 ILE   B C   1 
ATOM   27213 O  O   . ILE   B 1 1746 ? 87.62400   48.69100  33.04100  1.000 107.24490 ?  1744 ILE   B O   1 
ATOM   27214 C  CB  . ILE   B 1 1746 ? 84.43900   47.96000  32.37200  1.000 90.76982  ?  1744 ILE   B CB  1 
ATOM   27215 C  CG1 . ILE   B 1 1746 ? 82.94500   48.25900  32.54200  1.000 97.37265  ?  1744 ILE   B CG1 1 
ATOM   27216 C  CG2 . ILE   B 1 1746 ? 84.61900   46.44900  32.28500  1.000 89.02814  ?  1744 ILE   B CG2 1 
ATOM   27217 C  CD1 . ILE   B 1 1746 ? 82.48900   49.58800  31.97800  1.000 93.20724  ?  1744 ILE   B CD1 1 
ATOM   27218 N  N   . GLU   B 1 1747 ? 86.89200   46.92700  34.22800  1.000 119.49729 ?  1745 GLU   B N   1 
ATOM   27219 C  CA  . GLU   B 1 1747 ? 88.18800   46.27700  34.32800  1.000 110.98329 ?  1745 GLU   B CA  1 
ATOM   27220 C  C   . GLU   B 1 1747 ? 88.13300   44.90300  33.66900  1.000 107.21114 ?  1745 GLU   B C   1 
ATOM   27221 O  O   . GLU   B 1 1747 ? 87.06000   44.31800  33.49500  1.000 106.60568 ?  1745 GLU   B O   1 
ATOM   27222 C  CB  . GLU   B 1 1747 ? 88.62800   46.14600  35.79500  1.000 91.76806  ?  1745 GLU   B CB  1 
ATOM   27223 C  CG  . GLU   B 1 1747 ? 90.10400   45.82900  35.98500  1.000 104.44783 ?  1745 GLU   B CG  1 
ATOM   27224 C  CD  . GLU   B 1 1747 ? 91.00400   46.71400  35.14100  1.000 131.74657 ?  1745 GLU   B CD  1 
ATOM   27225 O  OE1 . GLU   B 1 1747 ? 91.15500   47.90800  35.47600  1.000 124.14538 ?  1745 GLU   B OE1 1 
ATOM   27226 O  OE2 . GLU   B 1 1747 ? 91.55900   46.21500  34.13900  1.000 135.70833 ?  1745 GLU   B OE2 1 
ATOM   27227 N  N   . ARG   B 1 1748 ? 89.31300   44.40400  33.28900  1.000 106.04035 ?  1746 ARG   B N   1 
ATOM   27228 C  CA  . ARG   B 1 1748 ? 89.47000   43.06600  32.71600  1.000 105.09811 ?  1746 ARG   B CA  1 
ATOM   27229 C  C   . ARG   B 1 1748 ? 88.60700   42.89000  31.46700  1.000 100.48512 ?  1746 ARG   B C   1 
ATOM   27230 O  O   . ARG   B 1 1748 ? 87.90600   41.88900  31.30100  1.000 104.04784 ?  1746 ARG   B O   1 
ATOM   27231 C  CB  . ARG   B 1 1748 ? 89.16200   41.98300  33.75400  1.000 96.23323  ?  1746 ARG   B CB  1 
ATOM   27232 N  N   . ILE   B 1 1749 ? 88.66400   43.88600  30.58100  1.000 100.48271 ?  1747 ILE   B N   1 
ATOM   27233 C  CA  . ILE   B 1 1749 ? 87.91000   43.82700  29.33300  1.000 104.51001 ?  1747 ILE   B CA  1 
ATOM   27234 C  C   . ILE   B 1 1749 ? 88.38100   42.62600  28.52600  1.000 92.90141  ?  1747 ILE   B C   1 
ATOM   27235 O  O   . ILE   B 1 1749 ? 89.53900   42.56100  28.09700  1.000 113.89298 ?  1747 ILE   B O   1 
ATOM   27236 C  CB  . ILE   B 1 1749 ? 88.06900   45.13200  28.54400  1.000 106.92325 ?  1747 ILE   B CB  1 
ATOM   27237 C  CG1 . ILE   B 1 1749 ? 87.93000   46.34600  29.47200  1.000 101.65788 ?  1747 ILE   B CG1 1 
ATOM   27238 C  CG2 . ILE   B 1 1749 ? 87.08000   45.18200  27.37800  1.000 94.14591  ?  1747 ILE   B CG2 1 
ATOM   27239 C  CD1 . ILE   B 1 1749 ? 86.60000   47.07100  29.36900  1.000 100.91546 ?  1747 ILE   B CD1 1 
ATOM   27240 N  N   . GLY   B 1 1750 ? 87.48700   41.66200  28.32300  1.000 83.38865  ?  1748 GLY   B N   1 
ATOM   27241 C  CA  . GLY   B 1 1750 ? 87.83400   40.49600  27.54200  1.000 93.19275  ?  1748 GLY   B CA  1 
ATOM   27242 C  C   . GLY   B 1 1750 ? 87.93900   40.80500  26.06100  1.000 97.13088  ?  1748 GLY   B C   1 
ATOM   27243 O  O   . GLY   B 1 1750 ? 87.43300   41.81200  25.56400  1.000 101.33129 ?  1748 GLY   B O   1 
ATOM   27244 N  N   . ILE   B 1 1751 ? 88.62200   39.90800  25.34500  1.000 84.42953  ?  1749 ILE   B N   1 
ATOM   27245 C  CA  . ILE   B 1 1751 ? 88.78400   40.07100  23.90200  1.000 97.97525  ?  1749 ILE   B CA  1 
ATOM   27246 C  C   . ILE   B 1 1751 ? 87.42700   40.10500  23.21100  1.000 106.93271 ?  1749 ILE   B C   1 
ATOM   27247 O  O   . ILE   B 1 1751 ? 87.20500   40.89200  22.28200  1.000 101.47589 ?  1749 ILE   B O   1 
ATOM   27248 C  CB  . ILE   B 1 1751 ? 89.67600   38.95000  23.33700  1.000 101.94696 ?  1749 ILE   B CB  1 
ATOM   27249 C  CG1 . ILE   B 1 1751 ? 89.43200   37.64700  24.10100  1.000 112.15351 ?  1749 ILE   B CG1 1 
ATOM   27250 C  CG2 . ILE   B 1 1751 ? 91.14300   39.35000  23.40000  1.000 102.02025 ?  1749 ILE   B CG2 1 
ATOM   27251 C  CD1 . ILE   B 1 1751 ? 89.95300   36.41500  23.39600  1.000 117.68542 ?  1749 ILE   B CD1 1 
ATOM   27252 N  N   . ARG   B 1 1752 ? 86.49800   39.25600  23.65000  1.000 120.80754 ?  1750 ARG   B N   1 
ATOM   27253 C  CA  . ARG   B 1 1752 ? 85.16000   39.19100  23.06200  1.000 120.52718 ?  1750 ARG   B CA  1 
ATOM   27254 C  C   . ARG   B 1 1752 ? 84.17500   39.95500  23.94700  1.000 116.10965 ?  1750 ARG   B C   1 
ATOM   27255 O  O   . ARG   B 1 1752 ? 83.35200   39.38800  24.66800  1.000 117.59783 ?  1750 ARG   B O   1 
ATOM   27256 C  CB  . ARG   B 1 1752 ? 84.73700   37.73800  22.86700  1.000 108.13876 ?  1750 ARG   B CB  1 
ATOM   27257 N  N   . ASP   B 1 1753 ? 84.28300   41.28000  23.87500  1.000 114.17625 ?  1751 ASP   B N   1 
ATOM   27258 C  CA  . ASP   B 1 1753 ? 83.45500   42.18600  24.66400  1.000 107.31727 ?  1751 ASP   B CA  1 
ATOM   27259 C  C   . ASP   B 1 1753 ? 82.95500   43.29700  23.74700  1.000 109.70064 ?  1751 ASP   B C   1 
ATOM   27260 O  O   . ASP   B 1 1753 ? 83.74600   44.12000  23.27300  1.000 107.44617 ?  1751 ASP   B O   1 
ATOM   27261 C  CB  . ASP   B 1 1753 ? 84.23500   42.74700  25.85600  1.000 118.16382 ?  1751 ASP   B CB  1 
ATOM   27262 C  CG  . ASP   B 1 1753 ? 84.38400   41.73900  26.99200  1.000 106.18637 ?  1751 ASP   B CG  1 
ATOM   27263 O  OD1 . ASP   B 1 1753 ? 84.44900   40.52100  26.71900  1.000 87.99640  ?  1751 ASP   B OD1 1 
ATOM   27264 O  OD2 . ASP   B 1 1753 ? 84.43600   42.16900  28.16400  1.000 92.43179  -1 1751 ASP   B OD2 1 
ATOM   27265 N  N   . ASN   B 1 1754 ? 81.64600   43.31400  23.49700  1.000 118.82314 ?  1752 ASN   B N   1 
ATOM   27266 C  CA  . ASN   B 1 1754 ? 81.04600   44.26500  22.56500  1.000 117.37244 ?  1752 ASN   B CA  1 
ATOM   27267 C  C   . ASN   B 1 1754 ? 81.01100   45.66200  23.17300  1.000 112.45286 ?  1752 ASN   B C   1 
ATOM   27268 O  O   . ASN   B 1 1754 ? 80.32800   45.88600  24.17700  1.000 118.17587 ?  1752 ASN   B O   1 
ATOM   27269 C  CB  . ASN   B 1 1754 ? 79.63600   43.81500  22.19400  1.000 102.29855 ?  1752 ASN   B CB  1 
ATOM   27270 C  CG  . ASN   B 1 1754 ? 79.09500   44.54100  20.98100  1.000 110.69785 ?  1752 ASN   B CG  1 
ATOM   27271 O  OD1 . ASN   B 1 1754 ? 78.63100   45.67800  21.07600  1.000 112.03606 ?  1752 ASN   B OD1 1 
ATOM   27272 N  ND2 . ASN   B 1 1754 ? 79.15500   43.88600  19.82900  1.000 97.52527  ?  1752 ASN   B ND2 1 
ATOM   27273 N  N   . PHE   B 1 1755 ? 81.70400   46.61100  22.53100  1.000 93.95828  ?  1753 PHE   B N   1 
ATOM   27274 C  CA  . PHE   B 1 1755 ? 81.93600   47.92600  23.13000  1.000 105.14171 ?  1753 PHE   B CA  1 
ATOM   27275 C  C   . PHE   B 1 1755 ? 80.63900   48.59600  23.57100  1.000 120.24805 ?  1753 PHE   B C   1 
ATOM   27276 O  O   . PHE   B 1 1755 ? 80.53400   49.09500  24.69700  1.000 120.64543 ?  1753 PHE   B O   1 
ATOM   27277 C  CB  . PHE   B 1 1755 ? 82.69000   48.82700  22.15000  1.000 101.13334 ?  1753 PHE   B CB  1 
ATOM   27278 C  CG  . PHE   B 1 1755 ? 82.94600   50.21700  22.67800  1.000 109.76912 ?  1753 PHE   B CG  1 
ATOM   27279 C  CD1 . PHE   B 1 1755 ? 83.83800   50.42300  23.71700  1.000 114.45719 ?  1753 PHE   B CD1 1 
ATOM   27280 C  CD2 . PHE   B 1 1755 ? 82.28300   51.31400  22.14600  1.000 99.17540  ?  1753 PHE   B CD2 1 
ATOM   27281 C  CE1 . PHE   B 1 1755 ? 84.06800   51.69200  24.20900  1.000 101.77088 ?  1753 PHE   B CE1 1 
ATOM   27282 C  CE2 . PHE   B 1 1755 ? 82.51500   52.58600  22.63200  1.000 100.58893 ?  1753 PHE   B CE2 1 
ATOM   27283 C  CZ  . PHE   B 1 1755 ? 83.40800   52.77400  23.66600  1.000 100.22975 ?  1753 PHE   B CZ  1 
ATOM   27284 N  N   . PHE   B 1 1756 ? 79.64000   48.62600  22.68700  1.000 123.66747 ?  1754 PHE   B N   1 
ATOM   27285 C  CA  . PHE   B 1 1756 ? 78.37100   49.26100  23.02600  1.000 105.80800 ?  1754 PHE   B CA  1 
ATOM   27286 C  C   . PHE   B 1 1756 ? 77.66400   48.51700  24.15300  1.000 115.16317 ?  1754 PHE   B C   1 
ATOM   27287 O  O   . PHE   B 1 1756 ? 77.02300   49.13800  25.00900  1.000 101.94379 ?  1754 PHE   B O   1 
ATOM   27288 C  CB  . PHE   B 1 1756 ? 77.50100   49.34500  21.77500  1.000 93.77832  ?  1754 PHE   B CB  1 
ATOM   27289 C  CG  . PHE   B 1 1756 ? 78.25100   49.81400  20.55900  1.000 107.89536 ?  1754 PHE   B CG  1 
ATOM   27290 C  CD1 . PHE   B 1 1756 ? 78.86600   51.05600  20.54800  1.000 109.04898 ?  1754 PHE   B CD1 1 
ATOM   27291 C  CD2 . PHE   B 1 1756 ? 78.36900   49.00400  19.44000  1.000 109.32962 ?  1754 PHE   B CD2 1 
ATOM   27292 C  CE1 . PHE   B 1 1756 ? 79.56600   51.49000  19.43700  1.000 108.15860 ?  1754 PHE   B CE1 1 
ATOM   27293 C  CE2 . PHE   B 1 1756 ? 79.06900   49.43300  18.32600  1.000 91.73265  ?  1754 PHE   B CE2 1 
ATOM   27294 C  CZ  . PHE   B 1 1756 ? 79.66700   50.67600  18.32500  1.000 97.30734  ?  1754 PHE   B CZ  1 
ATOM   27295 N  N   . GLU   B 1 1757 ? 77.78100   47.18600  24.17400  1.000 129.55970 ?  1755 GLU   B N   1 
ATOM   27296 C  CA  . GLU   B 1 1757 ? 77.28000   46.41800  25.30900  1.000 120.22604 ?  1755 GLU   B CA  1 
ATOM   27297 C  C   . GLU   B 1 1757 ? 78.01200   46.79500  26.59300  1.000 113.90818 ?  1755 GLU   B C   1 
ATOM   27298 O  O   . GLU   B 1 1757 ? 77.39400   46.89600  27.65900  1.000 113.27883 ?  1755 GLU   B O   1 
ATOM   27299 C  CB  . GLU   B 1 1757 ? 77.41000   44.91900  25.03000  1.000 112.88233 ?  1755 GLU   B CB  1 
ATOM   27300 N  N   . LEU   B 1 1758 ? 79.32900   47.02800  26.51200  1.000 117.90787 ?  1756 LEU   B N   1 
ATOM   27301 C  CA  . LEU   B 1 1758 ? 80.06800   47.49900  27.68100  1.000 105.83248 ?  1756 LEU   B CA  1 
ATOM   27302 C  C   . LEU   B 1 1758 ? 79.62800   48.88000  28.14100  1.000 102.45119 ?  1756 LEU   B C   1 
ATOM   27303 O  O   . LEU   B 1 1758 ? 80.02900   49.30400  29.22900  1.000 103.73522 ?  1756 LEU   B O   1 
ATOM   27304 C  CB  . LEU   B 1 1758 ? 81.57800   47.53600  27.42200  1.000 101.25114 ?  1756 LEU   B CB  1 
ATOM   27305 C  CG  . LEU   B 1 1758 ? 82.18100   46.47000  26.51800  1.000 104.61798 ?  1756 LEU   B CG  1 
ATOM   27306 C  CD1 . LEU   B 1 1758 ? 83.58200   46.84900  26.06300  1.000 124.23505 ?  1756 LEU   B CD1 1 
ATOM   27307 C  CD2 . LEU   B 1 1758 ? 82.17900   45.15400  27.25600  1.000 98.45895  ?  1756 LEU   B CD2 1 
ATOM   27308 N  N   . GLY   B 1 1759 ? 78.83000   49.59100  27.34900  1.000 91.42970  ?  1757 GLY   B N   1 
ATOM   27309 C  CA  . GLY   B 1 1759 ? 78.35800   50.90100  27.74500  1.000 108.76674 ?  1757 GLY   B CA  1 
ATOM   27310 C  C   . GLY   B 1 1759 ? 79.19000   52.02900  27.17400  1.000 109.28072 ?  1757 GLY   B C   1 
ATOM   27311 O  O   . GLY   B 1 1759 ? 79.71000   52.86600  27.91800  1.000 91.14800  ?  1757 GLY   B O   1 
ATOM   27312 N  N   . GLY   B 1 1760 ? 79.31700   52.06900  25.85100  1.000 94.85741  ?  1758 GLY   B N   1 
ATOM   27313 C  CA  . GLY   B 1 1760 ? 80.12300   53.08900  25.21200  1.000 99.36456  ?  1758 GLY   B CA  1 
ATOM   27314 C  C   . GLY   B 1 1760 ? 79.40100   53.87100  24.13400  1.000 109.69630 ?  1758 GLY   B C   1 
ATOM   27315 O  O   . GLY   B 1 1760 ? 78.81500   53.28800  23.21700  1.000 96.07093  ?  1758 GLY   B O   1 
ATOM   27316 N  N   . ASP   B 1 1761 ? 79.44500   55.19700  24.23300  1.000 104.08617 ?  1759 ASP   B N   1 
ATOM   27317 C  CA  . ASP   B 1 1761 ? 78.85600   56.07800  23.23900  1.000 96.83697  ?  1759 ASP   B CA  1 
ATOM   27318 C  C   . ASP   B 1 1761 ? 79.87200   56.34900  22.12900  1.000 86.30888  ?  1759 ASP   B C   1 
ATOM   27319 O  O   . ASP   B 1 1761 ? 80.98500   55.81800  22.12300  1.000 85.52706  ?  1759 ASP   B O   1 
ATOM   27320 C  CB  . ASP   B 1 1761 ? 78.38200   57.37300  23.90500  1.000 100.80469 ?  1759 ASP   B CB  1 
ATOM   27321 C  CG  . ASP   B 1 1761 ? 77.58000   58.26700  22.96600  1.000 118.83411 ?  1759 ASP   B CG  1 
ATOM   27322 O  OD1 . ASP   B 1 1761 ? 77.67300   58.08300  21.73200  1.000 124.27255 ?  1759 ASP   B OD1 1 
ATOM   27323 O  OD2 . ASP   B 1 1761 ? 76.86200   59.15900  23.46400  1.000 120.41801 -1 1759 ASP   B OD2 1 
ATOM   27324 N  N   . SER   B 1 1762 ? 79.47500   57.18000  21.16100  1.000 98.02796  ?  1760 SER   B N   1 
ATOM   27325 C  CA  . SER   B 1 1762 ? 80.40900   57.63200  20.13700  1.000 93.86937  ?  1760 SER   B CA  1 
ATOM   27326 C  C   . SER   B 1 1762 ? 81.51200   58.48900  20.74500  1.000 91.33629  ?  1760 SER   B C   1 
ATOM   27327 O  O   . SER   B 1 1762 ? 82.67900   58.38600  20.34800  1.000 84.63612  ?  1760 SER   B O   1 
ATOM   27328 C  CB  . SER   B 1 1762 ? 79.66200   58.41500  19.05400  1.000 97.54551  ?  1760 SER   B CB  1 
ATOM   27329 O  OG  . SER   B 1 1762 ? 78.61600   57.65200  18.47500  1.000 91.69346  ?  1760 SER   B OG  1 
ATOM   27330 N  N   . ILE   B 1 1763 ? 81.16100   59.34000  21.71600  1.000 90.91023  ?  1761 ILE   B N   1 
ATOM   27331 C  CA  . ILE   B 1 1763 ? 82.15500   60.18800  22.37200  1.000 81.32306  ?  1761 ILE   B CA  1 
ATOM   27332 C  C   . ILE   B 1 1763 ? 83.21100   59.34100  23.06900  1.000 75.69723  ?  1761 ILE   B C   1 
ATOM   27333 O  O   . ILE   B 1 1763 ? 84.39300   59.70900  23.10200  1.000 77.64962  ?  1761 ILE   B O   1 
ATOM   27334 C  CB  . ILE   B 1 1763 ? 81.45900   61.15700  23.35200  1.000 73.92954  ?  1761 ILE   B CB  1 
ATOM   27335 C  CG1 . ILE   B 1 1763 ? 82.47300   61.78700  24.31100  1.000 80.78880  ?  1761 ILE   B CG1 1 
ATOM   27336 C  CG2 . ILE   B 1 1763 ? 80.36800   60.44100  24.12900  1.000 77.52315  ?  1761 ILE   B CG2 1 
ATOM   27337 C  CD1 . ILE   B 1 1763 ? 81.87700   62.81300  25.25400  1.000 69.04616  ?  1761 ILE   B CD1 1 
ATOM   27338 N  N   . LYS   B 1 1764 ? 82.81500   58.18900  23.61600  1.000 87.46941  ?  1762 LYS   B N   1 
ATOM   27339 C  CA  . LYS   B 1 1764 ? 83.77700   57.29400  24.25200  1.000 83.59337  ?  1762 LYS   B CA  1 
ATOM   27340 C  C   . LYS   B 1 1764 ? 84.81400   56.79600  23.25100  1.000 74.20043  ?  1762 LYS   B C   1 
ATOM   27341 O  O   . LYS   B 1 1764 ? 86.00000   56.67800  23.58100  1.000 79.31938  ?  1762 LYS   B O   1 
ATOM   27342 C  CB  . LYS   B 1 1764 ? 83.04700   56.11400  24.89700  1.000 84.86277  ?  1762 LYS   B CB  1 
ATOM   27343 C  CG  . LYS   B 1 1764 ? 82.31400   56.42600  26.20300  1.000 88.54832  ?  1762 LYS   B CG  1 
ATOM   27344 C  CD  . LYS   B 1 1764 ? 82.76200   57.73900  26.83000  1.000 94.77894  ?  1762 LYS   B CD  1 
ATOM   27345 C  CE  . LYS   B 1 1764 ? 82.30500   57.84000  28.27700  1.000 91.85881  ?  1762 LYS   B CE  1 
ATOM   27346 N  NZ  . LYS   B 1 1764 ? 83.17800   57.05200  29.19000  1.000 101.77227 ?  1762 LYS   B NZ  1 
ATOM   27347 N  N   . GLY   B 1 1765 ? 84.38500   56.49700  22.02200  1.000 72.42326  ?  1763 GLY   B N   1 
ATOM   27348 C  CA  . GLY   B 1 1765 ? 85.32100   56.05600  21.00200  1.000 64.51009  ?  1763 GLY   B CA  1 
ATOM   27349 C  C   . GLY   B 1 1765 ? 86.29600   57.13500  20.58000  1.000 63.33193  ?  1763 GLY   B C   1 
ATOM   27350 O  O   . GLY   B 1 1765 ? 87.44200   56.83800  20.22900  1.000 69.65505  ?  1763 GLY   B O   1 
ATOM   27351 N  N   . LEU   B 1 1766 ? 85.85800   58.39500  20.59500  1.000 61.92920  ?  1764 LEU   B N   1 
ATOM   27352 C  CA  . LEU   B 1 1766 ? 86.77700   59.50500  20.37100  1.000 65.61417  ?  1764 LEU   B CA  1 
ATOM   27353 C  C   . LEU   B 1 1766 ? 87.76600   59.63200  21.52400  1.000 77.72866  ?  1764 LEU   B C   1 
ATOM   27354 O  O   . LEU   B 1 1766 ? 88.98100   59.72100  21.30600  1.000 68.24293  ?  1764 LEU   B O   1 
ATOM   27355 C  CB  . LEU   B 1 1766 ? 85.99000   60.80200  20.18500  1.000 56.83031  ?  1764 LEU   B CB  1 
ATOM   27356 C  CG  . LEU   B 1 1766 ? 86.78500   62.05300  19.80400  1.000 44.11029  ?  1764 LEU   B CG  1 
ATOM   27357 C  CD1 . LEU   B 1 1766 ? 87.79500   61.76500  18.70000  1.000 54.72486  ?  1764 LEU   B CD1 1 
ATOM   27358 C  CD2 . LEU   B 1 1766 ? 85.84300   63.17600  19.40500  1.000 57.62773  ?  1764 LEU   B CD2 1 
ATOM   27359 N  N   . GLN   B 1 1767 ? 87.25700   59.63900  22.76500  1.000 68.76370  ?  1765 GLN   B N   1 
ATOM   27360 C  CA  . GLN   B 1 1767 ? 88.12300   59.64100  23.94100  1.000 58.93964  ?  1765 GLN   B CA  1 
ATOM   27361 C  C   . GLN   B 1 1767 ? 89.07500   58.45600  23.93700  1.000 70.77715  ?  1765 GLN   B C   1 
ATOM   27362 O  O   . GLN   B 1 1767 ? 90.21700   58.57400  24.39100  1.000 74.71393  ?  1765 GLN   B O   1 
ATOM   27363 C  CB  . GLN   B 1 1767 ? 87.28200   59.61100  25.21600  1.000 68.79426  ?  1765 GLN   B CB  1 
ATOM   27364 C  CG  . GLN   B 1 1767 ? 86.63000   60.92400  25.56300  1.000 94.99870  ?  1765 GLN   B CG  1 
ATOM   27365 C  CD  . GLN   B 1 1767 ? 86.12100   60.94600  26.98600  1.000 89.82931  ?  1765 GLN   B CD  1 
ATOM   27366 O  OE1 . GLN   B 1 1767 ? 85.90800   59.89800  27.59900  1.000 88.95260  ?  1765 GLN   B OE1 1 
ATOM   27367 N  NE2 . GLN   B 1 1767 ? 85.91000   62.14200  27.51700  1.000 84.61768  ?  1765 GLN   B NE2 1 
ATOM   27368 N  N   . ILE   B 1 1768 ? 88.61700   57.30500  23.44900  1.000 63.52603  ?  1766 ILE   B N   1 
ATOM   27369 C  CA  . ILE   B 1 1768 ? 89.51100   56.16900  23.27100  1.000 53.11369  ?  1766 ILE   B CA  1 
ATOM   27370 C  C   . ILE   B 1 1768 ? 90.54100   56.48300  22.19300  1.000 59.91270  ?  1766 ILE   B C   1 
ATOM   27371 O  O   . ILE   B 1 1768 ? 91.72600   56.65800  22.48900  1.000 72.58384  ?  1766 ILE   B O   1 
ATOM   27372 C  CB  . ILE   B 1 1768 ? 88.69900   54.89400  22.97000  1.000 59.88322  ?  1766 ILE   B CB  1 
ATOM   27373 C  CG1 . ILE   B 1 1768 ? 88.28000   54.23500  24.27600  1.000 64.57656  ?  1766 ILE   B CG1 1 
ATOM   27374 C  CG2 . ILE   B 1 1768 ? 89.49100   53.87600  22.19500  1.000 48.73067  ?  1766 ILE   B CG2 1 
ATOM   27375 C  CD1 . ILE   B 1 1768 ? 87.05900   53.40300  24.14400  1.000 73.65772  ?  1766 ILE   B CD1 1 
ATOM   27376 N  N   . ALA   B 1 1769 ? 90.08700   56.65000  20.93800  1.000 54.27642  ?  1767 ALA   B N   1 
ATOM   27377 C  CA  . ALA   B 1 1769 ? 90.99700   56.85800  19.81000  1.000 51.58428  ?  1767 ALA   B CA  1 
ATOM   27378 C  C   . ALA   B 1 1769 ? 92.05300   57.92200  20.08100  1.000 62.05015  ?  1767 ALA   B C   1 
ATOM   27379 O  O   . ALA   B 1 1769 ? 93.15700   57.85400  19.52400  1.000 47.15485  ?  1767 ALA   B O   1 
ATOM   27380 C  CB  . ALA   B 1 1769 ? 90.19700   57.23700  18.56000  1.000 46.27478  ?  1767 ALA   B CB  1 
ATOM   27381 N  N   . SER   B 1 1770 ? 91.74200   58.90600  20.92900  1.000 65.83160  ?  1768 SER   B N   1 
ATOM   27382 C  CA  . SER   B 1 1770 ? 92.70800   59.95000  21.25600  1.000 61.72369  ?  1768 SER   B CA  1 
ATOM   27383 C  C   . SER   B 1 1770 ? 93.90000   59.38300  22.01800  1.000 69.41162  ?  1768 SER   B C   1 
ATOM   27384 O  O   . SER   B 1 1770 ? 95.05500   59.71200  21.72200  1.000 84.94506  ?  1768 SER   B O   1 
ATOM   27385 C  CB  . SER   B 1 1770 ? 92.03100   61.05300  22.06900  1.000 65.08651  ?  1768 SER   B CB  1 
ATOM   27386 O  OG  . SER   B 1 1770 ? 90.97000   61.64000  21.33600  1.000 84.59586  ?  1768 SER   B OG  1 
ATOM   27387 N  N   . ARG   B 1 1771 ? 93.64200   58.53600  23.01700  1.000 60.96279  ?  1769 ARG   B N   1 
ATOM   27388 C  CA  . ARG   B 1 1771 ? 94.74200   57.94900  23.77200  1.000 56.99890  ?  1769 ARG   B CA  1 
ATOM   27389 C  C   . ARG   B 1 1771 ? 95.61300   57.07400  22.88200  1.000 59.61953  ?  1769 ARG   B C   1 
ATOM   27390 O  O   . ARG   B 1 1771 ? 96.83800   57.04300  23.04400  1.000 72.31579  ?  1769 ARG   B O   1 
ATOM   27391 C  CB  . ARG   B 1 1771 ? 94.21300   57.13500  24.95200  1.000 69.62376  ?  1769 ARG   B CB  1 
ATOM   27392 C  CG  . ARG   B 1 1771 ? 92.90800   57.62800  25.53800  1.000 62.75102  ?  1769 ARG   B CG  1 
ATOM   27393 C  CD  . ARG   B 1 1771 ? 93.08800   58.93600  26.29100  1.000 71.73644  ?  1769 ARG   B CD  1 
ATOM   27394 N  NE  . ARG   B 1 1771 ? 91.91000   59.26900  27.08400  1.000 94.81631  ?  1769 ARG   B NE  1 
ATOM   27395 C  CZ  . ARG   B 1 1771 ? 91.64100   58.76100  28.28000  1.000 90.91737  ?  1769 ARG   B CZ  1 
ATOM   27396 N  NH1 . ARG   B 1 1771 ? 92.45600   57.89900  28.86600  1.000 94.42000  ?  1769 ARG   B NH1 1 
ATOM   27397 N  NH2 . ARG   B 1 1771 ? 90.52600   59.13100  28.90500  1.000 84.52636  ?  1769 ARG   B NH2 1 
ATOM   27398 N  N   . LEU   B 1 1772 ? 95.00100   56.35800  21.93000  1.000 49.45972  ?  1770 LEU   B N   1 
ATOM   27399 C  CA  . LEU   B 1 1772 ? 95.78300   55.42600  21.12200  1.000 55.81928  ?  1770 LEU   B CA  1 
ATOM   27400 C  C   . LEU   B 1 1772 ? 96.76500   56.15200  20.21600  1.000 64.96099  ?  1770 LEU   B C   1 
ATOM   27401 O  O   . LEU   B 1 1772 ? 97.88500   55.67300  20.01100  1.000 68.31489  ?  1770 LEU   B O   1 
ATOM   27402 C  CB  . LEU   B 1 1772 ? 94.88900   54.50800  20.28600  1.000 60.80162  ?  1770 LEU   B CB  1 
ATOM   27403 C  CG  . LEU   B 1 1772 ? 94.05500   53.43800  20.99000  1.000 69.51430  ?  1770 LEU   B CG  1 
ATOM   27404 C  CD1 . LEU   B 1 1772 ? 94.79500   52.83800  22.17800  1.000 53.05325  ?  1770 LEU   B CD1 1 
ATOM   27405 C  CD2 . LEU   B 1 1772 ? 92.73100   53.99000  21.41200  1.000 67.75190  ?  1770 LEU   B CD2 1 
ATOM   27406 N  N   . GLN   B 1 1773 ? 96.37300   57.29600  19.65000  1.000 70.86490  ?  1771 GLN   B N   1 
ATOM   27407 C  CA  . GLN   B 1 1773 ? 97.30900   58.01000  18.78800  1.000 68.86501  ?  1771 GLN   B CA  1 
ATOM   27408 C  C   . GLN   B 1 1773 ? 98.41200   58.67900  19.59900  1.000 73.76844  ?  1771 GLN   B C   1 
ATOM   27409 O  O   . GLN   B 1 1773 ? 99.52400   58.86600  19.09100  1.000 84.07625  ?  1771 GLN   B O   1 
ATOM   27410 C  CB  . GLN   B 1 1773 ? 96.57500   59.03500  17.92500  1.000 65.22781  ?  1771 GLN   B CB  1 
ATOM   27411 C  CG  . GLN   B 1 1773 ? 95.50900   59.82800  18.65000  1.000 71.40382  ?  1771 GLN   B CG  1 
ATOM   27412 C  CD  . GLN   B 1 1773 ? 96.01800   61.16800  19.14200  1.000 90.51200  ?  1771 GLN   B CD  1 
ATOM   27413 O  OE1 . GLN   B 1 1773 ? 97.05400   61.65500  18.68800  1.000 100.44860 ?  1771 GLN   B OE1 1 
ATOM   27414 N  NE2 . GLN   B 1 1773 ? 95.28500   61.77800  20.06600  1.000 93.36320  ?  1771 GLN   B NE2 1 
ATOM   27415 N  N   . ARG   B 1 1774 ? 98.13100   59.04100  20.85500  1.000 61.34689  ?  1772 ARG   B N   1 
ATOM   27416 C  CA  . ARG   B 1 1774 ? 99.19300   59.52800  21.73000  1.000 60.79255  ?  1772 ARG   B CA  1 
ATOM   27417 C  C   . ARG   B 1 1774 ? 100.28200  58.48000  21.91200  1.000 64.43542  ?  1772 ARG   B C   1 
ATOM   27418 O  O   . ARG   B 1 1774 ? 101.46200  58.82600  22.03800  1.000 68.60693  ?  1772 ARG   B O   1 
ATOM   27419 C  CB  . ARG   B 1 1774 ? 98.62300   59.94200  23.08800  1.000 59.42810  ?  1772 ARG   B CB  1 
ATOM   27420 C  CG  . ARG   B 1 1774 ? 97.65400   61.11400  23.03300  1.000 59.07558  ?  1772 ARG   B CG  1 
ATOM   27421 C  CD  . ARG   B 1 1774 ? 97.86900   62.05800  24.20800  1.000 87.16276  ?  1772 ARG   B CD  1 
ATOM   27422 N  NE  . ARG   B 1 1774 ? 96.78700   62.00700  25.18500  1.000 97.26171  ?  1772 ARG   B NE  1 
ATOM   27423 C  CZ  . ARG   B 1 1774 ? 96.89200   61.47700  26.39600  1.000 98.73284  ?  1772 ARG   B CZ  1 
ATOM   27424 N  NH1 . ARG   B 1 1774 ? 98.00700   60.89700  26.80100  1.000 103.03297 ?  1772 ARG   B NH1 1 
ATOM   27425 N  NH2 . ARG   B 1 1774 ? 95.85000   61.52400  27.22000  1.000 92.57911  ?  1772 ARG   B NH2 1 
ATOM   27426 N  N   . ILE   B 1 1775 ? 99.91000   57.20300  21.92000  1.000 63.51142  ?  1773 ILE   B N   1 
ATOM   27427 C  CA  . ILE   B 1 1775 ? 100.87000  56.11100  21.97500  1.000 61.71461  ?  1773 ILE   B CA  1 
ATOM   27428 C  C   . ILE   B 1 1775 ? 101.08600  55.48900  20.59400  1.000 60.48115  ?  1773 ILE   B C   1 
ATOM   27429 O  O   . ILE   B 1 1775 ? 101.52600  54.34300  20.49300  1.000 53.76908  ?  1773 ILE   B O   1 
ATOM   27430 C  CB  . ILE   B 1 1775 ? 100.45600  55.05000  23.00500  1.000 56.65650  ?  1773 ILE   B CB  1 
ATOM   27431 C  CG1 . ILE   B 1 1775 ? 98.98900   54.66300  22.80800  1.000 59.54216  ?  1773 ILE   B CG1 1 
ATOM   27432 C  CG2 . ILE   B 1 1775 ? 100.69800  55.56500  24.41500  1.000 57.44979  ?  1773 ILE   B CG2 1 
ATOM   27433 C  CD1 . ILE   B 1 1775 ? 98.38700   53.89600  23.96600  1.000 64.18397  ?  1773 ILE   B CD1 1 
ATOM   27434 N  N   . ASN   B 1 1776 ? 100.76400  56.22800  19.52800  1.000 52.01845  ?  1774 ASN   B N   1 
ATOM   27435 C  CA  . ASN   B 1 1776 ? 101.00900  55.81000  18.14600  1.000 68.25354  ?  1774 ASN   B CA  1 
ATOM   27436 C  C   . ASN   B 1 1776 ? 100.24300  54.53200  17.79300  1.000 69.56008  ?  1774 ASN   B C   1 
ATOM   27437 O  O   . ASN   B 1 1776 ? 100.81300  53.54600  17.32100  1.000 69.73523  ?  1774 ASN   B O   1 
ATOM   27438 C  CB  . ASN   B 1 1776 ? 102.50900  55.64900  17.88100  1.000 72.59198  ?  1774 ASN   B CB  1 
ATOM   27439 C  CG  . ASN   B 1 1776 ? 103.25000  56.97200  17.91400  1.000 64.64765  ?  1774 ASN   B CG  1 
ATOM   27440 O  OD1 . ASN   B 1 1776 ? 103.32300  57.68100  16.91000  1.000 79.39517  ?  1774 ASN   B OD1 1 
ATOM   27441 N  ND2 . ASN   B 1 1776 ? 103.79600  57.31600  19.07500  1.000 70.80348  ?  1774 ASN   B ND2 1 
ATOM   27442 N  N   . TRP   B 1 1777 ? 98.93000   54.56400  18.01800  1.000 76.31609  ?  1775 TRP   B N   1 
ATOM   27443 C  CA  . TRP   B 1 1777 ? 98.02200   53.49700  17.60500  1.000 67.09820  ?  1775 TRP   B CA  1 
ATOM   27444 C  C   . TRP   B 1 1777 ? 96.85600   54.13400  16.86400  1.000 69.37417  ?  1775 TRP   B C   1 
ATOM   27445 O  O   . TRP   B 1 1777 ? 96.14300   54.97100  17.42800  1.000 64.20684  ?  1775 TRP   B O   1 
ATOM   27446 C  CB  . TRP   B 1 1777 ? 97.51700   52.69100  18.80700  1.000 56.78637  ?  1775 TRP   B CB  1 
ATOM   27447 C  CG  . TRP   B 1 1777 ? 98.47900   51.65400  19.31600  1.000 66.96554  ?  1775 TRP   B CG  1 
ATOM   27448 C  CD1 . TRP   B 1 1777 ? 99.04900   51.60300  20.55700  1.000 53.28862  ?  1775 TRP   B CD1 1 
ATOM   27449 C  CD2 . TRP   B 1 1777 ? 98.97400   50.51300  18.60100  1.000 63.30427  ?  1775 TRP   B CD2 1 
ATOM   27450 N  NE1 . TRP   B 1 1777 ? 99.86900   50.50400  20.65600  1.000 54.29191  ?  1775 TRP   B NE1 1 
ATOM   27451 C  CE2 . TRP   B 1 1777 ? 99.84100   49.82000  19.47000  1.000 49.48362  ?  1775 TRP   B CE2 1 
ATOM   27452 C  CE3 . TRP   B 1 1777 ? 98.77000   50.01300  17.31100  1.000 67.46440  ?  1775 TRP   B CE3 1 
ATOM   27453 C  CZ2 . TRP   B 1 1777 ? 100.50200  48.65400  19.08900  1.000 52.96456  ?  1775 TRP   B CZ2 1 
ATOM   27454 C  CZ3 . TRP   B 1 1777 ? 99.42700   48.85500  16.93600  1.000 64.38296  ?  1775 TRP   B CZ3 1 
ATOM   27455 C  CH2 . TRP   B 1 1777 ? 100.28300  48.18900  17.82200  1.000 59.10265  ?  1775 TRP   B CH2 1 
ATOM   27456 N  N   . THR   B 1 1778 ? 96.66200   53.74800  15.60600  1.000 74.55755  ?  1776 THR   B N   1 
ATOM   27457 C  CA  . THR   B 1 1778 ? 95.63500   54.34800  14.75500  1.000 67.38368  ?  1776 THR   B CA  1 
ATOM   27458 C  C   . THR   B 1 1778 ? 94.42300   53.42500  14.72900  1.000 71.52117  ?  1776 THR   B C   1 
ATOM   27459 O  O   . THR   B 1 1778 ? 94.41800   52.40500  14.03500  1.000 70.02764  ?  1776 THR   B O   1 
ATOM   27460 C  CB  . THR   B 1 1778 ? 96.16900   54.60300  13.35000  1.000 69.24348  ?  1776 THR   B CB  1 
ATOM   27461 O  OG1 . THR   B 1 1778 ? 97.45300   55.23300  13.43000  1.000 74.94148  ?  1776 THR   B OG1 1 
ATOM   27462 C  CG2 . THR   B 1 1778 ? 95.21500   55.50600  12.58000  1.000 62.46785  ?  1776 THR   B CG2 1 
ATOM   27463 N  N   . MET   B 1 1779 ? 93.39200   53.78700  15.48800  1.000 65.60857  ?  1777 MET   B N   1 
ATOM   27464 C  CA  . MET   B 1 1779 ? 92.12800   53.06400  15.50800  1.000 64.98549  ?  1777 MET   B CA  1 
ATOM   27465 C  C   . MET   B 1 1779 ? 91.02500   53.99500  15.03000  1.000 67.05501  ?  1777 MET   B C   1 
ATOM   27466 O  O   . MET   B 1 1779 ? 90.85200   55.09100  15.57400  1.000 63.38751  ?  1777 MET   B O   1 
ATOM   27467 C  CB  . MET   B 1 1779 ? 91.80200   52.53800  16.90900  1.000 79.34568  ?  1777 MET   B CB  1 
ATOM   27468 C  CG  . MET   B 1 1779 ? 90.48400   51.77500  16.99500  1.000 75.59470  ?  1777 MET   B CG  1 
ATOM   27469 S  SD  . MET   B 1 1779 ? 89.64000   51.99000  18.57300  1.000 78.11559  ?  1777 MET   B SD  1 
ATOM   27470 C  CE  . MET   B 1 1779 ? 89.48700   53.76900  18.61000  1.000 68.93246  ?  1777 MET   B CE  1 
ATOM   27471 N  N   . VAL   B 1 1780 ? 90.28600   53.55800  14.01800  1.000 74.85926  ?  1778 VAL   B N   1 
ATOM   27472 C  CA  . VAL   B 1 1780 ? 89.21400   54.36800  13.45400  1.000 80.79742  ?  1778 VAL   B CA  1 
ATOM   27473 C  C   . VAL   B 1 1780 ? 87.96100   54.19100  14.29900  1.000 69.98071  ?  1778 VAL   B C   1 
ATOM   27474 O  O   . VAL   B 1 1780 ? 87.59800   53.06700  14.66700  1.000 69.31134  ?  1778 VAL   B O   1 
ATOM   27475 C  CB  . VAL   B 1 1780 ? 88.95700   53.98800  11.98800  1.000 72.76655  ?  1778 VAL   B CB  1 
ATOM   27476 C  CG1 . VAL   B 1 1780 ? 88.25100   55.12100  11.26700  1.000 87.46628  ?  1778 VAL   B CG1 1 
ATOM   27477 C  CG2 . VAL   B 1 1780 ? 90.26800   53.65300  11.29400  1.000 65.24329  ?  1778 VAL   B CG2 1 
ATOM   27478 N  N   . ILE   B 1 1781 ? 87.30200   55.30700  14.61900  1.000 65.28565  ?  1779 ILE   B N   1 
ATOM   27479 C  CA  . ILE   B 1 1781 ? 86.06000   55.24300  15.38500  1.000 60.91361  ?  1779 ILE   B CA  1 
ATOM   27480 C  C   . ILE   B 1 1781 ? 84.98700   54.50700  14.59500  1.000 87.46285  ?  1779 ILE   B C   1 
ATOM   27481 O  O   . ILE   B 1 1781 ? 84.21300   53.71800  15.15300  1.000 75.21802  ?  1779 ILE   B O   1 
ATOM   27482 C  CB  . ILE   B 1 1781 ? 85.60600   56.66000  15.77800  1.000 55.02408  ?  1779 ILE   B CB  1 
ATOM   27483 C  CG1 . ILE   B 1 1781 ? 86.74800   57.41200  16.46100  1.000 57.09443  ?  1779 ILE   B CG1 1 
ATOM   27484 C  CG2 . ILE   B 1 1781 ? 84.38700   56.59900  16.68100  1.000 54.84873  ?  1779 ILE   B CG2 1 
ATOM   27485 C  CD1 . ILE   B 1 1781 ? 86.52800   58.90100  16.54700  1.000 59.31281  ?  1779 ILE   B CD1 1 
ATOM   27486 N  N   . ASN   B 1 1782 ? 84.93100   54.74700  13.28100  1.000 101.05589 ?  1780 ASN   B N   1 
ATOM   27487 C  CA  . ASN   B 1 1782 ? 83.96300   54.05900  12.43100  1.000 98.58224  ?  1780 ASN   B CA  1 
ATOM   27488 C  C   . ASN   B 1 1782 ? 84.23100   52.56000  12.36500  1.000 94.67149  ?  1780 ASN   B C   1 
ATOM   27489 O  O   . ASN   B 1 1782 ? 83.28700   51.77100  12.24100  1.000 99.56454  ?  1780 ASN   B O   1 
ATOM   27490 C  CB  . ASN   B 1 1782 ? 83.97900   54.66400  11.02600  1.000 95.96543  ?  1780 ASN   B CB  1 
ATOM   27491 C  CG  . ASN   B 1 1782 ? 82.88800   54.10000  10.13600  1.000 89.34153  ?  1780 ASN   B CG  1 
ATOM   27492 O  OD1 . ASN   B 1 1782 ? 81.86600   53.61500  10.62000  1.000 102.00589 ?  1780 ASN   B OD1 1 
ATOM   27493 N  ND2 . ASN   B 1 1782 ? 83.10300   54.15700  8.82700   1.000 83.19828  ?  1780 ASN   B ND2 1 
ATOM   27494 N  N   . HIS   B 1 1783 ? 85.50000   52.14800  12.44700  1.000 86.08992  ?  1781 HIS   B N   1 
ATOM   27495 C  CA  . HIS   B 1 1783 ? 85.83000   50.72600  12.44100  1.000 80.14702  ?  1781 HIS   B CA  1 
ATOM   27496 C  C   . HIS   B 1 1783 ? 85.28000   49.99500  13.65600  1.000 86.93006  ?  1781 HIS   B C   1 
ATOM   27497 O  O   . HIS   B 1 1783 ? 85.12100   48.77100  13.60800  1.000 99.58047  ?  1781 HIS   B O   1 
ATOM   27498 C  CB  . HIS   B 1 1783 ? 87.34600   50.52800  12.37900  1.000 67.81426  ?  1781 HIS   B CB  1 
ATOM   27499 C  CG  . HIS   B 1 1783 ? 87.90200   50.57400  10.99200  1.000 79.01150  ?  1781 HIS   B CG  1 
ATOM   27500 N  ND1 . HIS   B 1 1783 ? 89.25500   50.58000  10.73000  1.000 92.39134  ?  1781 HIS   B ND1 1 
ATOM   27501 C  CD2 . HIS   B 1 1783 ? 87.28500   50.62200  9.78800   1.000 98.13416  ?  1781 HIS   B CD2 1 
ATOM   27502 C  CE1 . HIS   B 1 1783 ? 89.44800   50.62900  9.42400   1.000 103.09175 ?  1781 HIS   B CE1 1 
ATOM   27503 N  NE2 . HIS   B 1 1783 ? 88.26800   50.65600  8.82900   1.000 110.69378 ?  1781 HIS   B NE2 1 
ATOM   27504 N  N   . LEU   B 1 1784 ? 84.98800   50.71100  14.74200  1.000 73.58610  ?  1782 LEU   B N   1 
ATOM   27505 C  CA  . LEU   B 1 1784 ? 84.48900   50.05600  15.94400  1.000 82.24293  ?  1782 LEU   B CA  1 
ATOM   27506 C  C   . LEU   B 1 1784 ? 83.02700   49.64100  15.81000  1.000 100.73677 ?  1782 LEU   B C   1 
ATOM   27507 O  O   . LEU   B 1 1784 ? 82.60800   48.66400  16.44100  1.000 105.95986 ?  1782 LEU   B O   1 
ATOM   27508 C  CB  . LEU   B 1 1784 ? 84.68000   50.97500  17.15000  1.000 71.52848  ?  1782 LEU   B CB  1 
ATOM   27509 C  CG  . LEU   B 1 1784 ? 84.63600   50.28200  18.50900  1.000 77.03341  ?  1782 LEU   B CG  1 
ATOM   27510 C  CD1 . LEU   B 1 1784 ? 85.63400   50.90700  19.46800  1.000 82.99661  ?  1782 LEU   B CD1 1 
ATOM   27511 C  CD2 . LEU   B 1 1784 ? 83.23700   50.36300  19.06700  1.000 81.32330  ?  1782 LEU   B CD2 1 
ATOM   27512 N  N   . PHE   B 1 1785 ? 82.24000   50.35800  15.00200  1.000 110.64766 ?  1783 PHE   B N   1 
ATOM   27513 C  CA  . PHE   B 1 1785 ? 80.84400   49.97800  14.80000  1.000 110.35694 ?  1783 PHE   B CA  1 
ATOM   27514 C  C   . PHE   B 1 1785 ? 80.72400   48.66500  14.03800  1.000 102.56306 ?  1783 PHE   B C   1 
ATOM   27515 O  O   . PHE   B 1 1785 ? 79.75700   47.92000  14.23700  1.000 103.37839 ?  1783 PHE   B O   1 
ATOM   27516 C  CB  . PHE   B 1 1785 ? 80.09300   51.08900  14.06300  1.000 107.48385 ?  1783 PHE   B CB  1 
ATOM   27517 C  CG  . PHE   B 1 1785 ? 79.92100   52.34200  14.87200  1.000 100.63090 ?  1783 PHE   B CG  1 
ATOM   27518 C  CD1 . PHE   B 1 1785 ? 80.92400   53.29500  14.91700  1.000 95.12400  ?  1783 PHE   B CD1 1 
ATOM   27519 C  CD2 . PHE   B 1 1785 ? 78.75900   52.56500  15.59200  1.000 86.95867  ?  1783 PHE   B CD2 1 
ATOM   27520 C  CE1 . PHE   B 1 1785 ? 80.77400   54.44400  15.66900  1.000 81.61835  ?  1783 PHE   B CE1 1 
ATOM   27521 C  CE2 . PHE   B 1 1785 ? 78.60200   53.71600  16.34300  1.000 95.03551  ?  1783 PHE   B CE2 1 
ATOM   27522 C  CZ  . PHE   B 1 1785 ? 79.61100   54.65700  16.37900  1.000 86.27100  ?  1783 PHE   B CZ  1 
ATOM   27523 N  N   . LEU   B 1 1786 ? 81.69200   48.36400  13.17100  1.000 93.06062  ?  1784 LEU   B N   1 
ATOM   27524 C  CA  . LEU   B 1 1786 ? 81.66900   47.11300  12.42500  1.000 95.76466  ?  1784 LEU   B CA  1 
ATOM   27525 C  C   . LEU   B 1 1786 ? 82.23500   45.95100  13.23300  1.000 104.35754 ?  1784 LEU   B C   1 
ATOM   27526 O  O   . LEU   B 1 1786 ? 81.80700   44.80700  13.04400  1.000 105.85284 ?  1784 LEU   B O   1 
ATOM   27527 C  CB  . LEU   B 1 1786 ? 82.44600   47.26900  11.11700  1.000 101.33472 ?  1784 LEU   B CB  1 
ATOM   27528 C  CG  . LEU   B 1 1786 ? 82.04100   48.43800  10.21800  1.000 88.88701  ?  1784 LEU   B CG  1 
ATOM   27529 C  CD1 . LEU   B 1 1786 ? 83.20200   49.40400  10.05100  1.000 79.94632  ?  1784 LEU   B CD1 1 
ATOM   27530 C  CD2 . LEU   B 1 1786 ? 81.55700   47.93900  8.86600   1.000 81.40932  ?  1784 LEU   B CD2 1 
ATOM   27531 N  N   . TYR   B 1 1787 ? 83.18500   46.21300  14.12900  1.000 109.75516 ?  1785 TYR   B N   1 
ATOM   27532 C  CA  . TYR   B 1 1787 ? 83.80400   45.17000  14.95200  1.000 100.25483 ?  1785 TYR   B CA  1 
ATOM   27533 C  C   . TYR   B 1 1787 ? 83.90900   45.64400  16.39700  1.000 95.04809  ?  1785 TYR   B C   1 
ATOM   27534 O  O   . TYR   B 1 1787 ? 84.98700   46.02300  16.86700  1.000 99.95784  ?  1785 TYR   B O   1 
ATOM   27535 C  CB  . TYR   B 1 1787 ? 85.18100   44.79600  14.39700  1.000 94.92822  ?  1785 TYR   B CB  1 
ATOM   27536 C  CG  . TYR   B 1 1787 ? 85.30500   44.94900  12.89500  1.000 93.28341  ?  1785 TYR   B CG  1 
ATOM   27537 C  CD1 . TYR   B 1 1787 ? 84.93000   43.92200  12.03800  1.000 100.86448 ?  1785 TYR   B CD1 1 
ATOM   27538 C  CD2 . TYR   B 1 1787 ? 85.79000   46.12400  12.33400  1.000 94.06659  ?  1785 TYR   B CD2 1 
ATOM   27539 C  CE1 . TYR   B 1 1787 ? 85.03400   44.06400  10.66500  1.000 107.44103 ?  1785 TYR   B CE1 1 
ATOM   27540 C  CE2 . TYR   B 1 1787 ? 85.89500   46.27500  10.96900  1.000 101.63381 ?  1785 TYR   B CE2 1 
ATOM   27541 C  CZ  . TYR   B 1 1787 ? 85.51800   45.24300  10.13900  1.000 99.96100  ?  1785 TYR   B CZ  1 
ATOM   27542 O  OH  . TYR   B 1 1787 ? 85.62700   45.39500  8.77600   1.000 106.82522 ?  1785 TYR   B OH  1 
ATOM   27543 N  N   . PRO   B 1 1788 ? 82.78900   45.63200  17.14700  1.000 90.19691  ?  1786 PRO   B N   1 
ATOM   27544 C  CA  . PRO   B 1 1788 ? 82.82500   46.17900  18.51500  1.000 92.40580  ?  1786 PRO   B CA  1 
ATOM   27545 C  C   . PRO   B 1 1788 ? 83.49500   45.27200  19.54200  1.000 85.01843  ?  1786 PRO   B C   1 
ATOM   27546 O  O   . PRO   B 1 1788 ? 83.38200   45.53000  20.74400  1.000 79.72385  ?  1786 PRO   B O   1 
ATOM   27547 C  CB  . PRO   B 1 1788 ? 81.34500   46.39700  18.86500  1.000 100.79785 ?  1786 PRO   B CB  1 
ATOM   27548 C  CG  . PRO   B 1 1788 ? 80.58000   46.25300  17.61100  1.000 106.28687 ?  1786 PRO   B CG  1 
ATOM   27549 C  CD  . PRO   B 1 1788 ? 81.41800   45.50700  16.61900  1.000 81.43974  ?  1786 PRO   B CD  1 
ATOM   27550 N  N   . THR   B 1 1789 ? 84.19200   44.22500  19.10900  1.000 96.47079  ?  1787 THR   B N   1 
ATOM   27551 C  CA  . THR   B 1 1789 ? 84.93600   43.37000  20.02400  1.000 111.64129 ?  1787 THR   B CA  1 
ATOM   27552 C  C   . THR   B 1 1789 ? 86.43200   43.60000  19.85100  1.000 107.79572 ?  1787 THR   B C   1 
ATOM   27553 O  O   . THR   B 1 1789 ? 86.90900   43.88700  18.74900  1.000 98.34798  ?  1787 THR   B O   1 
ATOM   27554 C  CB  . THR   B 1 1789 ? 84.60500   41.88500  19.81400  1.000 94.62139  ?  1787 THR   B CB  1 
ATOM   27555 O  OG1 . THR   B 1 1789 ? 85.30500   41.38600  18.66800  1.000 93.01522  ?  1787 THR   B OG1 1 
ATOM   27556 C  CG2 . THR   B 1 1789 ? 83.10800   41.69400  19.61700  1.000 82.68568  ?  1787 THR   B CG2 1 
ATOM   27557 N  N   . ILE   B 1 1790 ? 87.16500   43.47500  20.96200  1.000 103.07390 ?  1788 ILE   B N   1 
ATOM   27558 C  CA  . ILE   B 1 1790 ? 88.60100   43.75300  20.95400  1.000 97.61665  ?  1788 ILE   B CA  1 
ATOM   27559 C  C   . ILE   B 1 1790 ? 89.31000   42.87600  19.93000  1.000 92.40139  ?  1788 ILE   B C   1 
ATOM   27560 O  O   . ILE   B 1 1790 ? 90.07400   43.36600  19.09000  1.000 85.44432  ?  1788 ILE   B O   1 
ATOM   27561 C  CB  . ILE   B 1 1790 ? 89.19700   43.56200  22.36000  1.000 94.84061  ?  1788 ILE   B CB  1 
ATOM   27562 C  CG1 . ILE   B 1 1790 ? 88.71500   44.66600  23.30800  1.000 82.52661  ?  1788 ILE   B CG1 1 
ATOM   27563 C  CG2 . ILE   B 1 1790 ? 90.71300   43.51800  22.27700  1.000 72.45782  ?  1788 ILE   B CG2 1 
ATOM   27564 C  CD1 . ILE   B 1 1790 ? 89.65500   44.94100  24.47000  1.000 66.38307  ?  1788 ILE   B CD1 1 
ATOM   27565 N  N   . GLU   B 1 1791 ? 89.06000   41.56500  19.98000  1.000 91.36103  ?  1789 GLU   B N   1 
ATOM   27566 C  CA  . GLU   B 1 1791 ? 89.71000   40.64200  19.05600  1.000 95.33531  ?  1789 GLU   B CA  1 
ATOM   27567 C  C   . GLU   B 1 1791 ? 89.35000   40.92200  17.60200  1.000 94.66814  ?  1789 GLU   B C   1 
ATOM   27568 O  O   . GLU   B 1 1791 ? 90.07800   40.49000  16.70200  1.000 92.22073  ?  1789 GLU   B O   1 
ATOM   27569 C  CB  . GLU   B 1 1791 ? 89.34800   39.19900  19.41300  1.000 87.25272  ?  1789 GLU   B CB  1 
ATOM   27570 N  N   . GLN   B 1 1792 ? 88.24600   41.62700  17.34900  1.000 92.80522  ?  1790 GLN   B N   1 
ATOM   27571 C  CA  . GLN   B 1 1792 ? 87.88700   42.02600  15.99600  1.000 96.45830  ?  1790 GLN   B CA  1 
ATOM   27572 C  C   . GLN   B 1 1792 ? 88.28300   43.45900  15.67000  1.000 106.88549 ?  1790 GLN   B C   1 
ATOM   27573 O  O   . GLN   B 1 1792 ? 88.44800   43.78400  14.48800  1.000 105.29805 ?  1790 GLN   B O   1 
ATOM   27574 C  CB  . GLN   B 1 1792 ? 86.37900   41.85200  15.77100  1.000 94.24845  ?  1790 GLN   B CB  1 
ATOM   27575 N  N   . ILE   B 1 1793 ? 88.44000   44.31800  16.67700  1.000 111.55352 ?  1791 ILE   B N   1 
ATOM   27576 C  CA  . ILE   B 1 1793 ? 88.93000   45.67100  16.43700  1.000 99.02253  ?  1791 ILE   B CA  1 
ATOM   27577 C  C   . ILE   B 1 1793 ? 90.45600   45.71100  16.38400  1.000 95.10054  ?  1791 ILE   B C   1 
ATOM   27578 O  O   . ILE   B 1 1793 ? 91.02300   46.54200  15.66900  1.000 99.68250  ?  1791 ILE   B O   1 
ATOM   27579 C  CB  . ILE   B 1 1793 ? 88.37500   46.65000  17.49600  1.000 93.34894  ?  1791 ILE   B CB  1 
ATOM   27580 C  CG1 . ILE   B 1 1793 ? 87.89700   47.95900  16.85000  1.000 81.47708  ?  1791 ILE   B CG1 1 
ATOM   27581 C  CG2 . ILE   B 1 1793 ? 89.39900   46.95500  18.58900  1.000 82.09187  ?  1791 ILE   B CG2 1 
ATOM   27582 C  CD1 . ILE   B 1 1793 ? 87.91700   47.96500  15.33100  1.000 87.11659  ?  1791 ILE   B CD1 1 
ATOM   27583 N  N   . ALA   B 1 1794 ? 91.13000   44.80900  17.10400  1.000 89.99320  ?  1792 ALA   B N   1 
ATOM   27584 C  CA  . ALA   B 1 1794 ? 92.59200   44.79100  17.14300  1.000 89.15996  ?  1792 ALA   B CA  1 
ATOM   27585 C  C   . ALA   B 1 1794 ? 93.24800   44.67500  15.77100  1.000 92.23630  ?  1792 ALA   B C   1 
ATOM   27586 O  O   . ALA   B 1 1794 ? 94.20600   45.42000  15.51200  1.000 102.63072 ?  1792 ALA   B O   1 
ATOM   27587 C  CB  . ALA   B 1 1794 ? 93.06300   43.66000  18.06900  1.000 87.39547  ?  1792 ALA   B CB  1 
ATOM   27588 N  N   . PRO   B 1 1795 ? 92.81200   43.79500  14.86000  1.000 85.00835  ?  1793 PRO   B N   1 
ATOM   27589 C  CA  . PRO   B 1 1795 ? 93.47400   43.71400  13.54800  1.000 93.55663  ?  1793 PRO   B CA  1 
ATOM   27590 C  C   . PRO   B 1 1795 ? 93.27100   44.93400  12.66200  1.000 98.33806  ?  1793 PRO   B C   1 
ATOM   27591 O  O   . PRO   B 1 1795 ? 93.80000   44.95400  11.54500  1.000 86.68399  ?  1793 PRO   B O   1 
ATOM   27592 C  CB  . PRO   B 1 1795 ? 92.83700   42.46400  12.91600  1.000 71.51896  ?  1793 PRO   B CB  1 
ATOM   27593 C  CG  . PRO   B 1 1795 ? 92.31600   41.68500  14.08200  1.000 87.89954  ?  1793 PRO   B CG  1 
ATOM   27594 C  CD  . PRO   B 1 1795 ? 91.78600   42.74600  14.98300  1.000 86.34604  ?  1793 PRO   B CD  1 
ATOM   27595 N  N   . PHE   B 1 1796 ? 92.52700   45.94400  13.10900  1.000 106.15586 ?  1794 PHE   B N   1 
ATOM   27596 C  CA  . PHE   B 1 1796 ? 92.36900   47.18900  12.36800  1.000 107.95887 ?  1794 PHE   B CA  1 
ATOM   27597 C  C   . PHE   B 1 1796 ? 92.97400   48.37700  13.10400  1.000 103.72864 ?  1794 PHE   B C   1 
ATOM   27598 O  O   . PHE   B 1 1796 ? 92.83000   49.51700  12.64900  1.000 100.41714 ?  1794 PHE   B O   1 
ATOM   27599 C  CB  . PHE   B 1 1796 ? 90.89100   47.43700  12.06200  1.000 105.52573 ?  1794 PHE   B CB  1 
ATOM   27600 C  CG  . PHE   B 1 1796 ? 90.30100   46.43700  11.11000  1.000 107.43073 ?  1794 PHE   B CG  1 
ATOM   27601 C  CD1 . PHE   B 1 1796 ? 90.77400   46.33600  9.81200   1.000 111.68325 ?  1794 PHE   B CD1 1 
ATOM   27602 C  CD2 . PHE   B 1 1796 ? 89.29500   45.57900  11.52000  1.000 110.22943 ?  1794 PHE   B CD2 1 
ATOM   27603 C  CE1 . PHE   B 1 1796 ? 90.24200   45.41100  8.93500   1.000 113.85082 ?  1794 PHE   B CE1 1 
ATOM   27604 C  CE2 . PHE   B 1 1796 ? 88.76100   44.65000  10.64700  1.000 115.88747 ?  1794 PHE   B CE2 1 
ATOM   27605 C  CZ  . PHE   B 1 1796 ? 89.23400   44.56700  9.35300   1.000 117.01096 ?  1794 PHE   B CZ  1 
ATOM   27606 N  N   . VAL   B 1 1797 ? 93.64100   48.13600  14.23000  1.000 92.04855  ?  1795 VAL   B N   1 
ATOM   27607 C  CA  . VAL   B 1 1797 ? 94.41500   49.15900  14.92300  1.000 90.91697  ?  1795 VAL   B CA  1 
ATOM   27608 C  C   . VAL   B 1 1797 ? 95.82600   49.12800  14.34800  1.000 81.71557  ?  1795 VAL   B C   1 
ATOM   27609 O  O   . VAL   B 1 1797 ? 96.58900   48.19300  14.60100  1.000 80.31049  ?  1795 VAL   B O   1 
ATOM   27610 C  CB  . VAL   B 1 1797 ? 94.42800   48.93400  16.43900  1.000 76.48347  ?  1795 VAL   B CB  1 
ATOM   27611 C  CG1 . VAL   B 1 1797 ? 94.89700   50.19000  17.15300  1.000 73.45362  ?  1795 VAL   B CG1 1 
ATOM   27612 C  CG2 . VAL   B 1 1797 ? 93.05300   48.53300  16.92800  1.000 74.04939  ?  1795 VAL   B CG2 1 
ATOM   27613 N  N   . THR   B 1 1798 ? 96.17000   50.15100  13.57300  1.000 78.17227  ?  1796 THR   B N   1 
ATOM   27614 C  CA  . THR   B 1 1798 ? 97.44700   50.22400  12.88100  1.000 84.62737  ?  1796 THR   B CA  1 
ATOM   27615 C  C   . THR   B 1 1798 ? 98.42600   51.09300  13.66300  1.000 81.36715  ?  1796 THR   B C   1 
ATOM   27616 O  O   . THR   B 1 1798 ? 98.03700   52.06200  14.32100  1.000 68.19406  ?  1796 THR   B O   1 
ATOM   27617 C  CB  . THR   B 1 1798 ? 97.26400   50.78000  11.46600  1.000 90.68216  ?  1796 THR   B CB  1 
ATOM   27618 O  OG1 . THR   B 1 1798 ? 96.19900   50.07700  10.81400  1.000 100.61556 ?  1796 THR   B OG1 1 
ATOM   27619 C  CG2 . THR   B 1 1798 ? 98.53400   50.60100  10.64800  1.000 77.11486  ?  1796 THR   B CG2 1 
ATOM   27620 N  N   . SER   B 1 1799 ? 99.70400   50.73000  13.58900  1.000 81.92671  ?  1797 SER   B N   1 
ATOM   27621 C  CA  . SER   B 1 1799 ? 100.76600  51.41000  14.31800  1.000 73.02766  ?  1797 SER   B CA  1 
ATOM   27622 C  C   . SER   B 1 1799 ? 101.42600  52.45400  13.42900  1.000 75.65263  ?  1797 SER   B C   1 
ATOM   27623 O  O   . SER   B 1 1799 ? 101.79000  52.16300  12.28400  1.000 94.36384  ?  1797 SER   B O   1 
ATOM   27624 C  CB  . SER   B 1 1799 ? 101.81300  50.41000  14.81100  1.000 65.14744  ?  1797 SER   B CB  1 
ATOM   27625 O  OG  . SER   B 1 1799 ? 103.08600  50.68900  14.25400  1.000 78.52895  ?  1797 SER   B OG  1 
ATOM   27626 N  N   . GLU   B 1 1800 ? 101.57500  53.66500  13.95700  1.000 75.03990  ?  1798 GLU   B N   1 
ATOM   27627 C  CA  . GLU   B 1 1800 ? 102.32100  54.72300  13.28200  1.000 91.36962  ?  1798 GLU   B CA  1 
ATOM   27628 C  C   . GLU   B 1 1800 ? 103.80500  54.42400  13.45200  1.000 95.71631  ?  1798 GLU   B C   1 
ATOM   27629 O  O   . GLU   B 1 1800 ? 104.38300  54.66700  14.51400  1.000 97.67604  ?  1798 GLU   B O   1 
ATOM   27630 C  CB  . GLU   B 1 1800 ? 101.95400  56.08800  13.85400  1.000 94.84298  ?  1798 GLU   B CB  1 
ATOM   27631 C  CG  . GLU   B 1 1800 ? 102.51400  57.27100  13.07600  1.000 106.09053 ?  1798 GLU   B CG  1 
ATOM   27632 C  CD  . GLU   B 1 1800 ? 102.48200  58.56100  13.87500  1.000 111.26188 ?  1798 GLU   B CD  1 
ATOM   27633 O  OE1 . GLU   B 1 1800 ? 101.38400  58.96000  14.31700  1.000 112.65867 ?  1798 GLU   B OE1 1 
ATOM   27634 O  OE2 . GLU   B 1 1800 ? 103.55300  59.17600  14.06200  1.000 113.51255 ?  1798 GLU   B OE2 1 
ATOM   27635 N  N   . GLN   B 1 1801 ? 104.42300  53.88100  12.40500  1.000 85.93095  ?  1799 GLN   B N   1 
ATOM   27636 C  CA  . GLN   B 1 1801 ? 105.83000  53.51300  12.47900  1.000 100.30101 ?  1799 GLN   B CA  1 
ATOM   27637 C  C   . GLN   B 1 1801 ? 106.70800  54.75700  12.43200  1.000 96.81427  ?  1799 GLN   B C   1 
ATOM   27638 O  O   . GLN   B 1 1801 ? 106.43500  55.70500  11.68900  1.000 79.93255  ?  1799 GLN   B O   1 
ATOM   27639 C  CB  . GLN   B 1 1801 ? 106.19200  52.56500  11.33600  1.000 99.02092  ?  1799 GLN   B CB  1 
ATOM   27640 C  CG  . GLN   B 1 1801 ? 107.15100  51.45200  11.73200  1.000 99.78707  ?  1799 GLN   B CG  1 
ATOM   27641 C  CD  . GLN   B 1 1801 ? 108.57400  51.71600  11.28200  1.000 107.84145 ?  1799 GLN   B CD  1 
ATOM   27642 O  OE1 . GLN   B 1 1801 ? 108.81000  52.17100  10.16300  1.000 113.95056 ?  1799 GLN   B OE1 1 
ATOM   27643 N  NE2 . GLN   B 1 1801 ? 109.53400  51.42700  12.15400  1.000 99.14745  ?  1799 GLN   B NE2 1 
ATOM   27644 N  N   . VAL   B 1 1802 ? 107.76800  54.75300  13.23800  1.000 87.38980  ?  1800 VAL   B N   1 
ATOM   27645 C  CA  . VAL   B 1 1802 ? 108.67000  55.89000  13.36000  1.000 84.56483  ?  1800 VAL   B CA  1 
ATOM   27646 C  C   . VAL   B 1 1802 ? 110.07000  55.45600  12.95000  1.000 69.72771  ?  1800 VAL   B C   1 
ATOM   27647 O  O   . VAL   B 1 1802 ? 110.46700  54.30600  13.16700  1.000 81.32482  ?  1800 VAL   B O   1 
ATOM   27648 C  CB  . VAL   B 1 1802 ? 108.66200  56.47500  14.79100  1.000 90.45215  ?  1800 VAL   B CB  1 
ATOM   27649 C  CG1 . VAL   B 1 1802 ? 107.23600  56.56200  15.32600  1.000 70.83255  ?  1800 VAL   B CG1 1 
ATOM   27650 C  CG2 . VAL   B 1 1802 ? 109.53700  55.65900  15.72700  1.000 97.50369  ?  1800 VAL   B CG2 1 
ATOM   27651 N  N   . VAL   B 1 1803 ? 110.80500  56.37400  12.33200  1.000 74.44480  ?  1801 VAL   B N   1 
ATOM   27652 C  CA  . VAL   B 1 1803 ? 112.18100  56.13900  11.91100  1.000 74.89724  ?  1801 VAL   B CA  1 
ATOM   27653 C  C   . VAL   B 1 1803 ? 113.08800  56.77600  12.95300  1.000 67.32086  ?  1801 VAL   B C   1 
ATOM   27654 O  O   . VAL   B 1 1803 ? 113.19000  58.00500  13.03400  1.000 67.61913  ?  1801 VAL   B O   1 
ATOM   27655 C  CB  . VAL   B 1 1803 ? 112.45200  56.70400  10.51000  1.000 71.51756  ?  1801 VAL   B CB  1 
ATOM   27656 C  CG1 . VAL   B 1 1803 ? 113.64600  56.00800  9.88400   1.000 66.52877  ?  1801 VAL   B CG1 1 
ATOM   27657 C  CG2 . VAL   B 1 1803 ? 111.22300  56.55500  9.62800   1.000 80.21540  ?  1801 VAL   B CG2 1 
ATOM   27658 N  N   . ILE   B 1 1804 ? 113.74600  55.94100  13.76100  1.000 70.84562  ?  1802 ILE   B N   1 
ATOM   27659 C  CA  . ILE   B 1 1804 ? 114.60400  56.46900  14.81600  1.000 76.01177  ?  1802 ILE   B CA  1 
ATOM   27660 C  C   . ILE   B 1 1804 ? 115.83700  57.14800  14.22800  1.000 69.29921  ?  1802 ILE   B C   1 
ATOM   27661 O  O   . ILE   B 1 1804 ? 116.36400  58.10200  14.81000  1.000 79.92391  ?  1802 ILE   B O   1 
ATOM   27662 C  CB  . ILE   B 1 1804 ? 114.98300  55.35100  15.80800  1.000 57.66480  ?  1802 ILE   B CB  1 
ATOM   27663 C  CG1 . ILE   B 1 1804 ? 116.10000  54.47100  15.23900  1.000 84.42757  ?  1802 ILE   B CG1 1 
ATOM   27664 C  CG2 . ILE   B 1 1804 ? 113.76500  54.50400  16.14000  1.000 48.24403  ?  1802 ILE   B CG2 1 
ATOM   27665 C  CD1 . ILE   B 1 1804 ? 116.91200  53.73900  16.28900  1.000 87.55295  ?  1802 ILE   B CD1 1 
ATOM   27666 N  N   . GLU   B 1 1805 ? 116.30200  56.69400  13.06700  1.000 64.90447  ?  1803 GLU   B N   1 
ATOM   27667 C  CA  . GLU   B 1 1805 ? 117.49800  57.25300  12.45600  1.000 54.64270  ?  1803 GLU   B CA  1 
ATOM   27668 C  C   . GLU   B 1 1805 ? 117.16800  58.55100  11.73400  1.000 59.95825  ?  1803 GLU   B C   1 
ATOM   27669 O  O   . GLU   B 1 1805 ? 116.10200  58.68600  11.12600  1.000 73.61568  ?  1803 GLU   B O   1 
ATOM   27670 C  CB  . GLU   B 1 1805 ? 118.10900  56.24900  11.48000  1.000 66.15937  ?  1803 GLU   B CB  1 
ATOM   27671 C  CG  . GLU   B 1 1805 ? 118.14700  54.82100  12.00700  1.000 91.78313  ?  1803 GLU   B CG  1 
ATOM   27672 C  CD  . GLU   B 1 1805 ? 117.10600  53.92300  11.35900  1.000 110.30834 ?  1803 GLU   B CD  1 
ATOM   27673 O  OE1 . GLU   B 1 1805 ? 115.89700  54.20800  11.49600  1.000 97.02840  ?  1803 GLU   B OE1 1 
ATOM   27674 O  OE2 . GLU   B 1 1805 ? 117.49700  52.92900  10.71300  1.000 124.46426 -1 1803 GLU   B OE2 1 
ATOM   27675 N  N   . ALA   B 1 1806 ? 118.08500  59.50800  11.80300  1.000 51.35155  ?  1804 ALA   B N   1 
ATOM   27676 C  CA  . ALA   B 1 1806 ? 117.92900  60.78800  11.13100  1.000 29.14347  ?  1804 ALA   B CA  1 
ATOM   27677 C  C   . ALA   B 1 1806 ? 118.64700  60.77100  9.78700   1.000 41.54219  ?  1804 ALA   B C   1 
ATOM   27678 O  O   . ALA   B 1 1806 ? 119.51600  59.93300  9.52900   1.000 54.55984  ?  1804 ALA   B O   1 
ATOM   27679 C  CB  . ALA   B 1 1806 ? 118.46200  61.92700  12.00100  1.000 31.52837  ?  1804 ALA   B CB  1 
ATOM   27680 N  N   . ALA   B 1 1807 ? 118.26300  61.71200  8.92100   1.000 41.20219  ?  1805 ALA   B N   1 
ATOM   27681 C  CA  . ALA   B 1 1807 ? 118.89800  61.81700  7.61100   1.000 42.88277  ?  1805 ALA   B CA  1 
ATOM   27682 C  C   . ALA   B 1 1807 ? 120.37900  62.13800  7.75200   1.000 36.29030  ?  1805 ALA   B C   1 
ATOM   27683 O  O   . ALA   B 1 1807 ? 121.23200  61.48700  7.13600   1.000 42.20535  ?  1805 ALA   B O   1 
ATOM   27684 C  CB  . ALA   B 1 1807 ? 118.19100  62.87700  6.76700   1.000 42.01489  ?  1805 ALA   B CB  1 
ATOM   27685 N  N   . ALA   B 1 1808 ? 120.70300  63.14000  8.56400   1.000 39.99025  ?  1806 ALA   B N   1 
ATOM   27686 C  CA  . ALA   B 1 1808 ? 122.08100  63.46300  8.91400   1.000 44.18758  ?  1806 ALA   B CA  1 
ATOM   27687 C  C   . ALA   B 1 1808 ? 122.36800  62.87200  10.29000  1.000 49.78930  ?  1806 ALA   B C   1 
ATOM   27688 O  O   . ALA   B 1 1808 ? 121.78000  63.29900  11.29000  1.000 54.53057  ?  1806 ALA   B O   1 
ATOM   27689 C  CB  . ALA   B 1 1808 ? 122.31100  64.97300  8.90100   1.000 31.75410  ?  1806 ALA   B CB  1 
ATOM   27690 N  N   . GLU   B 1 1809 ? 123.26000  61.88700  10.33900  1.000 55.84200  ?  1807 GLU   B N   1 
ATOM   27691 C  CA  . GLU   B 1 1809 ? 123.65400  61.24900  11.59000  1.000 65.85161  ?  1807 GLU   B CA  1 
ATOM   27692 C  C   . GLU   B 1 1809 ? 125.03100  61.67300  12.07400  1.000 61.25299  ?  1807 GLU   B C   1 
ATOM   27693 O  O   . GLU   B 1 1809 ? 125.23300  61.83800  13.28000  1.000 73.02941  ?  1807 GLU   B O   1 
ATOM   27694 C  CB  . GLU   B 1 1809 ? 123.61400  59.72400  11.43600  1.000 68.60544  ?  1807 GLU   B CB  1 
ATOM   27695 C  CG  . GLU   B 1 1809 ? 122.20800  59.14900  11.47600  1.000 73.04138  ?  1807 GLU   B CG  1 
ATOM   27696 C  CD  . GLU   B 1 1809 ? 122.07300  57.86800  10.67500  1.000 95.86608  ?  1807 GLU   B CD  1 
ATOM   27697 O  OE1 . GLU   B 1 1809 ? 122.01900  57.95300  9.42900   1.000 97.05106  ?  1807 GLU   B OE1 1 
ATOM   27698 O  OE2 . GLU   B 1 1809 ? 122.01000  56.78000  11.28900  1.000 91.39136  ?  1807 GLU   B OE2 1 
ATOM   27699 N  N   . ASN   B 1 1810 ? 125.98100  61.86200  11.16300  1.000 55.39385  ?  1808 ASN   B N   1 
ATOM   27700 C  CA  . ASN   B 1 1810 ? 127.32100  62.32700  11.49200  1.000 60.75945  ?  1808 ASN   B CA  1 
ATOM   27701 C  C   . ASN   B 1 1810 ? 127.54800  63.69800  10.86900  1.000 49.67281  ?  1808 ASN   B C   1 
ATOM   27702 O  O   . ASN   B 1 1810 ? 127.13400  63.94800  9.73200   1.000 52.25799  ?  1808 ASN   B O   1 
ATOM   27703 C  CB  . ASN   B 1 1810 ? 128.38200  61.33700  11.00000  1.000 57.63429  ?  1808 ASN   B CB  1 
ATOM   27704 C  CG  . ASN   B 1 1810 ? 127.94200  59.89300  11.15400  1.000 79.79273  ?  1808 ASN   B CG  1 
ATOM   27705 O  OD1 . ASN   B 1 1810 ? 127.94200  59.34600  12.25700  1.000 77.62962  ?  1808 ASN   B OD1 1 
ATOM   27706 N  ND2 . ASN   B 1 1810 ? 127.54700  59.27300  10.04700  1.000 74.70247  ?  1808 ASN   B ND2 1 
ATOM   27707 N  N   . LEU   B 1 1811 ? 128.20000  64.58600  11.61700  1.000 50.12857  ?  1809 LEU   B N   1 
ATOM   27708 C  CA  . LEU   B 1 1811 ? 128.41800  65.96300  11.19200  1.000 43.28058  ?  1809 LEU   B CA  1 
ATOM   27709 C  C   . LEU   B 1 1811 ? 129.90000  66.28900  11.27400  1.000 48.56099  ?  1809 LEU   B C   1 
ATOM   27710 O  O   . LEU   B 1 1811 ? 130.54000  66.02800  12.29800  1.000 55.33786  ?  1809 LEU   B O   1 
ATOM   27711 C  CB  . LEU   B 1 1811 ? 127.61400  66.94400  12.05100  1.000 41.32585  ?  1809 LEU   B CB  1 
ATOM   27712 C  CG  . LEU   B 1 1811 ? 126.88200  68.03400  11.27000  1.000 46.08650  ?  1809 LEU   B CG  1 
ATOM   27713 C  CD1 . LEU   B 1 1811 ? 125.79300  67.42500  10.40600  1.000 41.39255  ?  1809 LEU   B CD1 1 
ATOM   27714 C  CD2 . LEU   B 1 1811 ? 126.30100  69.07700  12.20500  1.000 45.69615  ?  1809 LEU   B CD2 1 
ATOM   27715 N  N   . TYR   B 1 1812 ? 130.43900  66.86100  10.19600  1.000 42.03729  ?  1810 TYR   B N   1 
ATOM   27716 C  CA  . TYR   B 1 1812 ? 131.85100  67.21600  10.10300  1.000 37.17115  ?  1810 TYR   B CA  1 
ATOM   27717 C  C   . TYR   B 1 1812 ? 131.96500  68.67400  9.68200   1.000 39.50111  ?  1810 TYR   B C   1 
ATOM   27718 O  O   . TYR   B 1 1812 ? 131.42500  69.06600  8.64200   1.000 51.37206  ?  1810 TYR   B O   1 
ATOM   27719 C  CB  . TYR   B 1 1812 ? 132.58600  66.30800  9.11100   1.000 31.68005  ?  1810 TYR   B CB  1 
ATOM   27720 C  CG  . TYR   B 1 1812 ? 132.51600  64.83700  9.46600   1.000 36.53842  ?  1810 TYR   B CG  1 
ATOM   27721 C  CD1 . TYR   B 1 1812 ? 133.30900  64.30900  10.47400  1.000 45.45172  ?  1810 TYR   B CD1 1 
ATOM   27722 C  CD2 . TYR   B 1 1812 ? 131.65400  63.97900  8.79500   1.000 48.81832  ?  1810 TYR   B CD2 1 
ATOM   27723 C  CE1 . TYR   B 1 1812 ? 133.24700  62.97100  10.80600  1.000 48.43255  ?  1810 TYR   B CE1 1 
ATOM   27724 C  CE2 . TYR   B 1 1812 ? 131.58600  62.63600  9.12200   1.000 61.09255  ?  1810 TYR   B CE2 1 
ATOM   27725 C  CZ  . TYR   B 1 1812 ? 132.38500  62.14000  10.12800  1.000 73.86255  ?  1810 TYR   B CZ  1 
ATOM   27726 O  OH  . TYR   B 1 1812 ? 132.32400  60.80700  10.45900  1.000 82.17255  ?  1810 TYR   B OH  1 
ATOM   27727 N  N   . PHE   B 1 1813 ? 132.66500  69.46900  10.48700  1.000 39.91173  ?  1811 PHE   B N   1 
ATOM   27728 C  CA  . PHE   B 1 1813 ? 132.87700  70.88400  10.20900  1.000 43.67176  ?  1811 PHE   B CA  1 
ATOM   27729 C  C   . PHE   B 1 1813 ? 134.15400  71.07700  9.39700   1.000 54.59231  ?  1811 PHE   B C   1 
ATOM   27730 O  O   . PHE   B 1 1813 ? 135.20400  70.52300  9.73900   1.000 50.14023  ?  1811 PHE   B O   1 
ATOM   27731 C  CB  . PHE   B 1 1813 ? 132.97300  71.68300  11.51300  1.000 40.87595  ?  1811 PHE   B CB  1 
ATOM   27732 C  CG  . PHE   B 1 1813 ? 131.64300  72.03300  12.11700  1.000 43.16935  ?  1811 PHE   B CG  1 
ATOM   27733 C  CD1 . PHE   B 1 1813 ? 130.73600  71.04200  12.45600  1.000 55.08403  ?  1811 PHE   B CD1 1 
ATOM   27734 C  CD2 . PHE   B 1 1813 ? 131.29800  73.35500  12.34500  1.000 47.66317  ?  1811 PHE   B CD2 1 
ATOM   27735 C  CE1 . PHE   B 1 1813 ? 129.50900  71.36000  13.00900  1.000 60.72037  ?  1811 PHE   B CE1 1 
ATOM   27736 C  CE2 . PHE   B 1 1813 ? 130.07000  73.68200  12.89900  1.000 52.77004  ?  1811 PHE   B CE2 1 
ATOM   27737 C  CZ  . PHE   B 1 1813 ? 129.17500  72.68200  13.23100  1.000 53.31418  ?  1811 PHE   B CZ  1 
ATOM   27738 N  N   . GLN   B 1 1814 ? 134.06100  71.85800  8.32400   1.000 59.44636  ?  1812 GLN   B N   1 
ATOM   27739 C  CA  . GLN   B 1 1814 ? 135.25500  72.38900  7.67300   1.000 68.80550  ?  1812 GLN   B CA  1 
ATOM   27740 C  C   . GLN   B 1 1814 ? 135.51400  73.79400  8.22500   1.000 86.57653  ?  1812 GLN   B C   1 
ATOM   27741 O  O   . GLN   B 1 1814 ? 134.93300  74.18500  9.24100   1.000 76.04992  ?  1812 GLN   B O   1 
ATOM   27742 C  CB  . GLN   B 1 1814 ? 135.10400  72.43200  6.15300   1.000 50.10107  ?  1812 GLN   B CB  1 
ATOM   27743 C  CG  . GLN   B 1 1814 ? 134.23800  71.32900  5.57200   1.000 54.47998  ?  1812 GLN   B CG  1 
ATOM   27744 C  CD  . GLN   B 1 1814 ? 134.20300  71.37000  4.05900   1.000 63.62204  ?  1812 GLN   B CD  1 
ATOM   27745 O  OE1 . GLN   B 1 1814 ? 134.73400  72.29500  3.43900   1.000 55.72220  ?  1812 GLN   B OE1 1 
ATOM   27746 N  NE2 . GLN   B 1 1814 ? 133.59200  70.35900  3.45300   1.000 71.11098  ?  1812 GLN   B NE2 1 
ATOM   27747 O  OXT . GLN   B 1 1814 ? 136.29100  74.58700  7.68400   1.000 86.60135  ?  1812 GLN   B OXT 1 
HETATM 27748 C  C1  . GOL   C 2 .    ? 9.25000    90.09400  46.86100  1.000 59.98218  ?  1901 GOL   A C1  1 
HETATM 27749 O  O1  . GOL   C 2 .    ? 10.60900   90.51800  46.78800  1.000 38.25106  ?  1901 GOL   A O1  1 
HETATM 27750 C  C2  . GOL   C 2 .    ? 8.31700    91.25000  47.15600  1.000 49.55999  ?  1901 GOL   A C2  1 
HETATM 27751 O  O2  . GOL   C 2 .    ? 6.96700    90.79300  47.22300  1.000 44.42899  ?  1901 GOL   A O2  1 
HETATM 27752 C  C3  . GOL   C 2 .    ? 8.67300    91.99900  48.42200  1.000 58.47401  ?  1901 GOL   A C3  1 
HETATM 27753 O  O3  . GOL   C 2 .    ? 8.68000    91.13300  49.55500  1.000 62.13021  ?  1901 GOL   A O3  1 
HETATM 27754 C  C1  . GOL   D 2 .    ? -18.37900  92.96100  25.91300  1.000 36.46001  ?  1902 GOL   A C1  1 
HETATM 27755 O  O1  . GOL   D 2 .    ? -17.09200  93.22300  25.36300  1.000 52.49268  ?  1902 GOL   A O1  1 
HETATM 27756 C  C2  . GOL   D 2 .    ? -18.96800  94.20400  26.54500  1.000 70.04881  ?  1902 GOL   A C2  1 
HETATM 27757 O  O2  . GOL   D 2 .    ? -20.22300  93.90900  27.15800  1.000 52.12447  ?  1902 GOL   A O2  1 
HETATM 27758 C  C3  . GOL   D 2 .    ? -19.10400  95.36100  25.57800  1.000 77.80528  ?  1902 GOL   A C3  1 
HETATM 27759 O  O3  . GOL   D 2 .    ? -19.86700  95.00100  24.42900  1.000 84.87977  ?  1902 GOL   A O3  1 
HETATM 27760 C  C02 . JQG   E 3 .    ? -54.62700  74.54300  -5.04600  1.000 64.61513  ?  1903 JQG   A C02 1 
HETATM 27761 C  C04 . JQG   E 3 .    ? -52.54600  74.86900  -6.41500  1.000 59.69152  ?  1903 JQG   A C04 1 
HETATM 27762 C  C05 . JQG   E 3 .    ? -51.51500  75.92900  -6.02500  1.000 44.92796  ?  1903 JQG   A C05 1 
HETATM 27763 C  C07 . JQG   E 3 .    ? -51.10100  76.95300  -8.32200  1.000 40.72869  ?  1903 JQG   A C07 1 
HETATM 27764 C  C08 . JQG   E 3 .    ? -50.14100  77.20800  -9.50200  1.000 41.85007  ?  1903 JQG   A C08 1 
HETATM 27765 C  C09 . JQG   E 3 .    ? -49.65500  78.67100  -9.58600  1.000 37.53537  ?  1903 JQG   A C09 1 
HETATM 27766 C  C11 . JQG   E 3 .    ? -48.25700  78.42200  -11.71000 1.000 36.19841  ?  1903 JQG   A C11 1 
HETATM 27767 C  C12 . JQG   E 3 .    ? -46.88900  78.46800  -12.40500 1.000 37.93610  ?  1903 JQG   A C12 1 
HETATM 27768 C  C14 . JQG   E 3 .    ? -46.20500  77.09000  -12.40300 1.000 38.61064  ?  1903 JQG   A C14 1 
HETATM 27769 C  C15 . JQG   E 3 .    ? -46.24000  76.45600  -11.01400 1.000 42.91526  ?  1903 JQG   A C15 1 
HETATM 27770 C  C16 . JQG   E 3 .    ? -44.74300  77.23900  -12.78900 1.000 35.79622  ?  1903 JQG   A C16 1 
HETATM 27771 C  C22 . JQG   E 3 .    ? -46.89800  76.17900  -13.41300 1.000 34.36951  ?  1903 JQG   A C22 1 
HETATM 27772 C  C25 . JQG   E 3 .    ? -55.40900  73.99000  -3.84300  1.000 74.45159  ?  1903 JQG   A C25 1 
HETATM 27773 C  C26 . JQG   E 3 .    ? -56.34700  75.09300  -3.31300  1.000 73.30211  ?  1903 JQG   A C26 1 
HETATM 27774 C  C27 . JQG   E 3 .    ? -55.70100  76.11700  -2.37200  1.000 66.24287  ?  1903 JQG   A C27 1 
HETATM 27775 C  C28 . JQG   E 3 .    ? -57.60500  74.48900  -2.72800  1.000 68.48727  ?  1903 JQG   A C28 1 
HETATM 27776 C  C30 . JQG   E 3 .    ? -53.31500  73.79900  -2.29000  1.000 68.97014  ?  1903 JQG   A C30 1 
HETATM 27777 N  N03 . JQG   E 3 .    ? -53.19500  74.31100  -5.23500  1.000 54.99608  ?  1903 JQG   A N03 1 
HETATM 27778 N  N06 . JQG   E 3 .    ? -50.62600  76.19200  -7.16300  1.000 40.53565  ?  1903 JQG   A N06 1 
HETATM 27779 N  N10 . JQG   E 3 .    ? -48.36200  78.71400  -10.27900 1.000 43.59774  ?  1903 JQG   A N10 1 
HETATM 27780 N  N29 . JQG   E 3 .    ? -54.62000  73.35800  -2.78300  1.000 67.26826  ?  1903 JQG   A N29 1 
HETATM 27781 O  O01 . JQG   E 3 .    ? -55.20900  75.17700  -5.85700  1.000 54.91306  ?  1903 JQG   A O01 1 
HETATM 27782 O  O13 . JQG   E 3 .    ? -47.07500  78.88100  -13.72800 1.000 39.13505  ?  1903 JQG   A O13 1 
HETATM 27783 O  O17 . JQG   E 3 .    ? -44.47900  78.61400  -12.81400 1.000 41.31944  ?  1903 JQG   A O17 1 
HETATM 27784 O  O19 . JQG   E 3 .    ? -41.85900  78.04000  -13.24300 1.000 47.75730  ?  1903 JQG   A O19 1 
HETATM 27785 O  O21 . JQG   E 3 .    ? -42.63900  79.75700  -11.48900 1.000 47.26689  ?  1903 JQG   A O21 1 
HETATM 27786 O  O23 . JQG   E 3 .    ? -49.22200  78.16500  -12.34600 1.000 30.80426  ?  1903 JQG   A O23 1 
HETATM 27787 O  O24 . JQG   E 3 .    ? -52.21100  77.37100  -8.35400  1.000 54.52203  ?  1903 JQG   A O24 1 
HETATM 27788 O  O31 . JQG   E 3 .    ? -52.78800  74.75600  -2.75000  1.000 77.32803  ?  1903 JQG   A O31 1 
HETATM 27789 P  P18 . JQG   E 3 .    ? -42.94600  79.19400  -12.82400 1.000 38.06597  ?  1903 JQG   A P18 1 
HETATM 27790 O  O13 . A1AMO F 4 .    ? -58.65800  61.51300  -13.29000 1.000 99.02402  ?  1904 A1AMO A O13 1 
HETATM 27791 O  O21 . A1AMO F 4 .    ? -61.51300  57.63700  -12.97700 1.000 95.61328  ?  1904 A1AMO A O21 1 
HETATM 27792 C  C11 . A1AMO F 4 .    ? -59.43400  63.73600  -12.86200 1.000 85.08703  ?  1904 A1AMO A C11 1 
HETATM 27793 C  C12 . A1AMO F 4 .    ? -59.82600  62.27100  -13.14100 1.000 99.81291  ?  1904 A1AMO A C12 1 
HETATM 27794 C  C02 . A1AMO F 4 .    ? -55.52200  69.43800  -7.07000  1.000 81.86314  ?  1904 A1AMO A C02 1 
HETATM 27795 C  C04 . A1AMO F 4 .    ? -57.15100  69.32500  -9.00900  1.000 75.48211  ?  1904 A1AMO A C04 1 
HETATM 27796 C  C05 . A1AMO F 4 .    ? -57.53400  67.84300  -8.94200  1.000 71.55408  ?  1904 A1AMO A C05 1 
HETATM 27797 C  C07 . A1AMO F 4 .    ? -56.47500  66.07700  -10.42500 1.000 78.65913  ?  1904 A1AMO A C07 1 
HETATM 27798 C  C08 . A1AMO F 4 .    ? -57.83000  65.89100  -11.14000 1.000 79.43071  ?  1904 A1AMO A C08 1 
HETATM 27799 C  C09 . A1AMO F 4 .    ? -57.65600  65.53400  -12.63000 1.000 86.30497  ?  1904 A1AMO A C09 1 
HETATM 27800 C  C14 . A1AMO F 4 .    ? -60.67500  62.14600  -14.41900 1.000 96.83592  ?  1904 A1AMO A C14 1 
HETATM 27801 C  C15 . A1AMO F 4 .    ? -60.04600  62.99000  -15.52100 1.000 88.69446  ?  1904 A1AMO A C15 1 
HETATM 27802 C  C16 . A1AMO F 4 .    ? -60.74200  60.70700  -14.91600 1.000 90.43321  ?  1904 A1AMO A C16 1 
HETATM 27803 C  C22 . A1AMO F 4 .    ? -62.10300  62.63200  -14.18000 1.000 82.38609  ?  1904 A1AMO A C22 1 
HETATM 27804 C  C25 . A1AMO F 4 .    ? -55.16200  69.93300  -5.67000  1.000 72.52081  ?  1904 A1AMO A C25 1 
HETATM 27805 N  N03 . A1AMO F 4 .    ? -56.80800  69.79700  -7.67400  1.000 78.95629  ?  1904 A1AMO A N03 1 
HETATM 27806 N  N06 . A1AMO F 4 .    ? -56.36400  67.04700  -9.33400  1.000 72.68810  ?  1904 A1AMO A N06 1 
HETATM 27807 N  N10 . A1AMO F 4 .    ? -58.03000  64.13900  -12.89200 1.000 87.04228  ?  1904 A1AMO A N10 1 
HETATM 27808 N  N29 . A1AMO F 4 .    ? -54.75400  71.32000  -5.75300  1.000 75.38631  ?  1904 A1AMO A N29 1 
HETATM 27809 O  O01 . A1AMO F 4 .    ? -54.75600  68.76100  -7.66400  1.000 76.98207  ?  1904 A1AMO A O01 1 
HETATM 27810 O  O17 . A1AMO F 4 .    ? -60.60100  59.82200  -13.83800 1.000 111.11494 ?  1904 A1AMO A O17 1 
HETATM 27811 O  O19 . A1AMO F 4 .    ? -61.99200  59.68700  -11.61900 1.000 92.22235  ?  1904 A1AMO A O19 1 
HETATM 27812 O  O23 . A1AMO F 4 .    ? -60.25600  64.55000  -12.61700 1.000 106.08277 ?  1904 A1AMO A O23 1 
HETATM 27813 O  O24 . A1AMO F 4 .    ? -55.53300  65.43100  -10.75100 1.000 83.48482  ?  1904 A1AMO A O24 1 
HETATM 27814 P  P18 . A1AMO F 4 .    ? -61.85800  59.06400  -13.12700 1.000 104.10309 ?  1904 A1AMO A P18 1 
HETATM 27815 MN MN  . MN    G 5 .    ? -60.63200  66.16900  33.54200  1.000 107.05287 ?  1905 MN    A MN  1 
HETATM 27816 C  C1  . GOL   H 2 .    ? 35.98100   94.50200  -22.78700 1.000 55.73194  ?  1901 GOL   B C1  1 
HETATM 27817 O  O1  . GOL   H 2 .    ? 35.45700   95.80800  -23.01300 1.000 76.12811  ?  1901 GOL   B O1  1 
HETATM 27818 C  C2  . GOL   H 2 .    ? 34.94600   93.57000  -22.19100 1.000 42.69814  ?  1901 GOL   B C2  1 
HETATM 27819 O  O2  . GOL   H 2 .    ? 34.54200   94.02700  -20.90000 1.000 38.59930  ?  1901 GOL   B O2  1 
HETATM 27820 C  C3  . GOL   H 2 .    ? 33.73800   93.35100  -23.07800 1.000 39.64988  ?  1901 GOL   B C3  1 
HETATM 27821 O  O3  . GOL   H 2 .    ? 33.11200   94.58000  -23.43500 1.000 34.19584  ?  1901 GOL   B O3  1 
HETATM 27822 C  C02 . JQG   I 3 .    ? 69.31100   74.66700  10.13200  1.000 61.88241  ?  1902 JQG   B C02 1 
HETATM 27823 C  C04 . JQG   I 3 .    ? 67.25300   75.83100  10.98900  1.000 42.42611  ?  1902 JQG   B C04 1 
HETATM 27824 C  C05 . JQG   I 3 .    ? 65.74000   75.60200  11.01700  1.000 58.09877  ?  1902 JQG   B C05 1 
HETATM 27825 C  C07 . JQG   I 3 .    ? 65.28100   77.37200  12.80700  1.000 62.43709  ?  1902 JQG   B C07 1 
HETATM 27826 C  C08 . JQG   I 3 .    ? 64.52900   78.65000  13.22500  1.000 69.59828  ?  1902 JQG   B C08 1 
HETATM 27827 C  C09 . JQG   I 3 .    ? 64.60900   78.88000  14.74500  1.000 51.52843  ?  1902 JQG   B C09 1 
HETATM 27828 C  C11 . JQG   I 3 .    ? 62.84400   78.79500  16.56700  1.000 68.11356  ?  1902 JQG   B C11 1 
HETATM 27829 C  C12 . JQG   I 3 .    ? 61.41300   79.11300  17.01100  1.000 67.61276  ?  1902 JQG   B C12 1 
HETATM 27830 C  C14 . JQG   I 3 .    ? 60.49100   77.91700  16.74600  1.000 64.61850  ?  1902 JQG   B C14 1 
HETATM 27831 C  C15 . JQG   I 3 .    ? 61.14500   76.88400  15.82900  1.000 71.73842  ?  1902 JQG   B C15 1 
HETATM 27832 C  C16 . JQG   I 3 .    ? 59.23500   78.42700  16.06800  1.000 51.54679  ?  1902 JQG   B C16 1 
HETATM 27833 C  C22 . JQG   I 3 .    ? 60.13400   77.24200  18.06500  1.000 63.49216  ?  1902 JQG   B C22 1 
HETATM 27834 C  C25 . JQG   I 3 .    ? 70.01800   73.68500  9.18500   1.000 73.76270  ?  1902 JQG   B C25 1 
HETATM 27835 C  C26 . JQG   I 3 .    ? 71.01700   74.42400  8.27200   1.000 63.12326  ?  1902 JQG   B C26 1 
HETATM 27836 C  C27 . JQG   I 3 .    ? 71.43700   73.55900  7.08000   1.000 72.70568  ?  1902 JQG   B C27 1 
HETATM 27837 C  C28 . JQG   I 3 .    ? 70.55900   75.81200  7.84800   1.000 42.80146  ?  1902 JQG   B C28 1 
HETATM 27838 C  C30 . JQG   I 3 .    ? 68.04100   73.30100  7.53100   1.000 79.03082  ?  1902 JQG   B C30 1 
HETATM 27839 N  N03 . JQG   I 3 .    ? 67.86900   74.89100  10.06700  1.000 53.73220  ?  1902 JQG   B N03 1 
HETATM 27840 N  N06 . JQG   I 3 .    ? 65.05200   76.81800  11.46600  1.000 67.33908  ?  1902 JQG   B N06 1 
HETATM 27841 N  N10 . JQG   I 3 .    ? 63.25800   79.16700  15.21900  1.000 57.65798  ?  1902 JQG   B N10 1 
HETATM 27842 N  N29 . JQG   I 3 .    ? 69.11100   72.83400  8.41700   1.000 86.44333  ?  1902 JQG   B N29 1 
HETATM 27843 O  O01 . JQG   I 3 .    ? 69.94000   75.25200  10.94500  1.000 60.73015  ?  1902 JQG   B O01 1 
HETATM 27844 O  O13 . JQG   I 3 .    ? 61.39900   79.43000  18.37300  1.000 72.09265  ?  1902 JQG   B O13 1 
HETATM 27845 O  O17 . JQG   I 3 .    ? 58.25100   78.59100  17.05100  1.000 59.27549  ?  1902 JQG   B O17 1 
HETATM 27846 O  O19 . JQG   I 3 .    ? 55.72100   79.40100  17.41800  1.000 49.39735  ?  1902 JQG   B O19 1 
HETATM 27847 O  O21 . JQG   I 3 .    ? 57.12600   80.32500  15.52000  1.000 45.27463  ?  1902 JQG   B O21 1 
HETATM 27848 O  O23 . JQG   I 3 .    ? 63.59500   78.26200  17.30700  1.000 58.64813  ?  1902 JQG   B O23 1 
HETATM 27849 O  O24 . JQG   I 3 .    ? 66.03100   76.86100  13.57400  1.000 44.36090  ?  1902 JQG   B O24 1 
HETATM 27850 O  O31 . JQG   I 3 .    ? 67.82300   74.45600  7.37700   1.000 77.62349  ?  1902 JQG   B O31 1 
HETATM 27851 P  P18 . JQG   I 3 .    ? 57.21500   79.85400  16.91700  1.000 51.38397  ?  1902 JQG   B P18 1 
HETATM 27852 MN MN  . MN    J 5 .    ? 130.56900  76.11700  16.14600  1.000 79.79245  ?  1903 MN    B MN  1 
HETATM 27853 MN MN  . MN    K 5 .    ? 137.58200  65.98500  11.70900  1.000 140.03786 ?  1904 MN    B MN  1 
HETATM 27854 MN MN  . MN    L 5 .    ? 45.09500   91.31200  -38.14000 1.000 224.26255 ?  1905 MN    B MN  1 
HETATM 27855 O  O   . HOH   M 6 .    ? -62.42900  58.54100  -9.69800  1.000 71.36540  ?  2001 HOH   A O   1 
HETATM 27856 O  O   . HOH   M 6 .    ? -16.76700  102.66300 54.32900  1.000 33.93680  ?  2002 HOH   A O   1 
HETATM 27857 O  O   . HOH   M 6 .    ? -32.87100  83.25200  9.86100   1.000 70.39932  ?  2003 HOH   A O   1 
HETATM 27858 O  O   . HOH   M 6 .    ? -41.70500  100.68100 -37.82200 1.000 102.46607 ?  2004 HOH   A O   1 
HETATM 27859 O  O   . HOH   M 6 .    ? -9.10800   93.05200  56.85000  1.000 57.83139  ?  2005 HOH   A O   1 
HETATM 27860 O  O   . HOH   M 6 .    ? -30.80000  52.46300  -18.61200 1.000 76.64702  ?  2006 HOH   A O   1 
HETATM 27861 O  O   . HOH   M 6 .    ? -16.08800  92.32800  52.31100  1.000 54.01383  ?  2007 HOH   A O   1 
HETATM 27862 O  O   . HOH   M 6 .    ? -24.48400  87.90000  13.35400  1.000 49.62365  ?  2008 HOH   A O   1 
HETATM 27863 O  O   . HOH   M 6 .    ? -37.43100  54.09100  1.65200   1.000 44.54938  ?  2009 HOH   A O   1 
HETATM 27864 O  O   . HOH   M 6 .    ? -62.13900  90.55100  -6.15900  1.000 54.99144  ?  2010 HOH   A O   1 
HETATM 27865 O  O   . HOH   M 6 .    ? -28.25000  65.11800  -21.86500 1.000 50.40271  ?  2011 HOH   A O   1 
HETATM 27866 O  O   . HOH   M 6 .    ? -28.55900  84.14400  3.69700   1.000 43.34884  ?  2012 HOH   A O   1 
HETATM 27867 O  O   . HOH   M 6 .    ? 7.17300    96.59900  29.98300  1.000 47.19654  ?  2013 HOH   A O   1 
HETATM 27868 O  O   . HOH   M 6 .    ? -11.29800  85.92400  1.91100   1.000 50.94616  ?  2014 HOH   A O   1 
HETATM 27869 O  O   . HOH   M 6 .    ? -34.84500  89.31100  -34.79300 1.000 54.10355  ?  2015 HOH   A O   1 
HETATM 27870 O  O   . HOH   M 6 .    ? -51.09800  76.34300  5.05400   1.000 51.94973  ?  2016 HOH   A O   1 
HETATM 27871 O  O   . HOH   M 6 .    ? -12.95000  86.69200  -8.57400  1.000 63.71977  ?  2017 HOH   A O   1 
HETATM 27872 O  O   . HOH   M 6 .    ? -89.094    55.993    -15.297   1.000 44.78507  ?  2018 HOH   A O   1 
HETATM 27873 O  O   . HOH   M 6 .    ? -52.27600  76.78900  0.37800   1.000 51.10658  ?  2019 HOH   A O   1 
HETATM 27874 O  O   . HOH   M 6 .    ? -75.04900  61.62800  -8.58600  1.000 52.15083  ?  2020 HOH   A O   1 
HETATM 27875 O  O   . HOH   M 6 .    ? -28.37000  17.17500  5.27100   1.000 46.63046  ?  2021 HOH   A O   1 
HETATM 27876 O  O   . HOH   M 6 .    ? -18.74600  77.99000  30.87900  1.000 46.44197  ?  2022 HOH   A O   1 
HETATM 27877 O  O   . HOH   M 6 .    ? -6.76500   91.32500  28.45200  1.000 34.83657  ?  2023 HOH   A O   1 
HETATM 27878 O  O   . HOH   M 6 .    ? -21.62400  68.71200  -4.12900  1.000 47.79248  ?  2024 HOH   A O   1 
HETATM 27879 O  O   . HOH   M 6 .    ? -66.73100  76.80300  15.41000  1.000 46.68203  ?  2025 HOH   A O   1 
HETATM 27880 O  O   . HOH   M 6 .    ? -19.36200  88.06500  16.70200  1.000 42.67988  ?  2026 HOH   A O   1 
HETATM 27881 O  O   . HOH   M 6 .    ? -28.66400  91.55200  -9.21900  1.000 44.37267  ?  2027 HOH   A O   1 
HETATM 27882 O  O   . HOH   M 6 .    ? -4.55800   80.91700  40.38300  1.000 53.06455  ?  2028 HOH   A O   1 
HETATM 27883 O  O   . HOH   M 6 .    ? -66.95900  72.47200  -21.07000 1.000 36.04524  ?  2029 HOH   A O   1 
HETATM 27884 O  O   . HOH   M 6 .    ? -36.27300  81.76700  -28.16200 1.000 46.94996  ?  2030 HOH   A O   1 
HETATM 27885 O  O   . HOH   M 6 .    ? -66.24500  83.40300  19.48200  1.000 61.26524  ?  2031 HOH   A O   1 
HETATM 27886 O  O   . HOH   M 6 .    ? -35.54200  103.59900 -17.03300 1.000 59.73882  ?  2032 HOH   A O   1 
HETATM 27887 O  O   . HOH   M 6 .    ? -30.76800  106.72300 -29.18200 1.000 53.69289  ?  2033 HOH   A O   1 
HETATM 27888 O  O   . HOH   M 6 .    ? -17.88400  96.00500  -13.70400 1.000 49.75429  ?  2034 HOH   A O   1 
HETATM 27889 O  O   . HOH   M 6 .    ? -67.46800  69.97700  16.42700  1.000 44.65652  ?  2035 HOH   A O   1 
HETATM 27890 O  O   . HOH   M 6 .    ? -5.90900   88.97400  54.38000  1.000 48.80588  ?  2036 HOH   A O   1 
HETATM 27891 O  O   . HOH   M 6 .    ? -35.30300  82.73900  -10.74100 1.000 40.27981  ?  2037 HOH   A O   1 
HETATM 27892 O  O   . HOH   M 6 .    ? -29.41300  98.17600  -16.69200 1.000 34.33598  ?  2038 HOH   A O   1 
HETATM 27893 O  O   . HOH   M 6 .    ? -34.33500  79.64300  19.08600  1.000 41.25588  ?  2039 HOH   A O   1 
HETATM 27894 O  O   . HOH   M 6 .    ? -21.48100  87.22200  35.75200  1.000 31.32213  ?  2040 HOH   A O   1 
HETATM 27895 O  O   . HOH   M 6 .    ? -62.54600  64.24400  39.41300  1.000 47.63647  ?  2041 HOH   A O   1 
HETATM 27896 O  O   . HOH   M 6 .    ? -47.83500  79.79000  -17.92800 1.000 37.30593  ?  2042 HOH   A O   1 
HETATM 27897 O  O   . HOH   M 6 .    ? -64.30100  66.53500  32.38000  1.000 50.06665  ?  2043 HOH   A O   1 
HETATM 27898 O  O   . HOH   M 6 .    ? -15.47200  119.77000 34.90400  1.000 57.28187  ?  2044 HOH   A O   1 
HETATM 27899 O  O   . HOH   M 6 .    ? -17.86400  110.42400 47.30700  1.000 58.68109  ?  2045 HOH   A O   1 
HETATM 27900 O  O   . HOH   M 6 .    ? -22.16000  31.13200  -7.65500  1.000 45.45442  ?  2046 HOH   A O   1 
HETATM 27901 O  O   . HOH   M 6 .    ? -59.52600  56.23300  -11.66400 1.000 76.01262  ?  2047 HOH   A O   1 
HETATM 27902 O  O   . HOH   M 6 .    ? -16.37100  97.76800  47.30000  1.000 41.91534  ?  2048 HOH   A O   1 
HETATM 27903 O  O   . HOH   M 6 .    ? -4.02200   80.92200  43.06600  1.000 53.81196  ?  2049 HOH   A O   1 
HETATM 27904 O  O   . HOH   M 6 .    ? -1.88200   80.07200  11.60300  1.000 47.68387  ?  2050 HOH   A O   1 
HETATM 27905 O  O   . HOH   M 6 .    ? -65.13500  89.03500  21.69400  1.000 54.98469  ?  2051 HOH   A O   1 
HETATM 27906 O  O   . HOH   M 6 .    ? -65.93900  68.08200  36.30400  1.000 45.64783  ?  2052 HOH   A O   1 
HETATM 27907 O  O   . HOH   M 6 .    ? -62.03600  63.55000  19.08100  1.000 46.42805  ?  2053 HOH   A O   1 
HETATM 27908 O  O   . HOH   M 6 .    ? -65.76600  85.70900  -7.71700  1.000 45.26938  ?  2054 HOH   A O   1 
HETATM 27909 O  O   . HOH   M 6 .    ? -67.70100  67.11000  -0.15600  1.000 37.85153  ?  2055 HOH   A O   1 
HETATM 27910 O  O   . HOH   M 6 .    ? -38.04100  70.26500  8.27900   1.000 46.77407  ?  2056 HOH   A O   1 
HETATM 27911 O  O   . HOH   M 6 .    ? -22.73800  76.28100  29.66800  1.000 45.97705  ?  2057 HOH   A O   1 
HETATM 27912 O  O   . HOH   M 6 .    ? -61.50800  55.89600  -22.48700 1.000 62.01251  ?  2058 HOH   A O   1 
HETATM 27913 O  O   . HOH   M 6 .    ? -9.41000   78.33300  17.99100  1.000 38.99640  ?  2059 HOH   A O   1 
HETATM 27914 O  O   . HOH   M 6 .    ? 7.28300    90.58800  16.73900  1.000 43.27102  ?  2060 HOH   A O   1 
HETATM 27915 O  O   . HOH   M 6 .    ? -27.78900  62.78500  13.04700  1.000 44.02997  ?  2061 HOH   A O   1 
HETATM 27916 O  O   . HOH   M 6 .    ? 7.50000    87.33100  14.70400  1.000 52.10559  ?  2062 HOH   A O   1 
HETATM 27917 O  O   . HOH   M 6 .    ? -59.81400  60.26600  -9.92700  1.000 68.91830  ?  2063 HOH   A O   1 
HETATM 27918 O  O   . HOH   M 6 .    ? -67.32700  88.66700  19.99400  1.000 62.25128  ?  2064 HOH   A O   1 
HETATM 27919 O  O   . HOH   M 6 .    ? -21.53800  24.79000  -5.38600  1.000 50.49509  ?  2065 HOH   A O   1 
HETATM 27920 O  O   . HOH   M 6 .    ? -56.81700  66.71000  26.07000  1.000 45.50996  ?  2066 HOH   A O   1 
HETATM 27921 O  O   . HOH   M 6 .    ? -10.15600  116.54900 28.75100  1.000 55.67490  ?  2067 HOH   A O   1 
HETATM 27922 O  O   . HOH   M 6 .    ? -45.59400  59.14500  -11.27900 1.000 43.45138  ?  2068 HOH   A O   1 
HETATM 27923 O  O   . HOH   M 6 .    ? -4.57400   114.56600 49.38600  1.000 63.06443  ?  2069 HOH   A O   1 
HETATM 27924 O  O   . HOH   M 6 .    ? -40.28600  92.15100  -8.49400  1.000 37.04851  ?  2070 HOH   A O   1 
HETATM 27925 O  O   . HOH   M 6 .    ? -34.80600  64.88200  27.86500  1.000 40.87687  ?  2071 HOH   A O   1 
HETATM 27926 O  O   . HOH   M 6 .    ? -61.12000  74.34300  -17.90400 1.000 44.96463  ?  2072 HOH   A O   1 
HETATM 27927 O  O   . HOH   M 6 .    ? -32.83700  73.50900  5.52800   1.000 44.73251  ?  2073 HOH   A O   1 
HETATM 27928 O  O   . HOH   M 6 .    ? -45.89000  84.57200  27.55300  1.000 35.63414  ?  2074 HOH   A O   1 
HETATM 27929 O  O   . HOH   M 6 .    ? -20.83600  53.05000  9.08200   1.000 65.45438  ?  2075 HOH   A O   1 
HETATM 27930 O  O   . HOH   M 6 .    ? -25.89800  42.97800  13.41800  1.000 48.44665  ?  2076 HOH   A O   1 
HETATM 27931 O  O   . HOH   M 6 .    ? -26.35000  40.01500  10.77100  1.000 44.56630  ?  2077 HOH   A O   1 
HETATM 27932 O  O   . HOH   M 6 .    ? -28.22800  4.45800   8.06900   1.000 52.77963  ?  2078 HOH   A O   1 
HETATM 27933 O  O   . HOH   M 6 .    ? -21.85800  97.88800  17.55400  1.000 49.55622  ?  2079 HOH   A O   1 
HETATM 27934 O  O   . HOH   M 6 .    ? -31.85500  59.93800  7.52900   1.000 46.76045  ?  2080 HOH   A O   1 
HETATM 27935 O  O   . HOH   M 6 .    ? -53.02500  67.50600  -5.72200  1.000 68.68760  ?  2081 HOH   A O   1 
HETATM 27936 O  O   . HOH   M 6 .    ? -27.21900  76.36500  26.33600  1.000 54.10920  ?  2082 HOH   A O   1 
HETATM 27937 O  O   . HOH   M 6 .    ? -29.25300  16.30300  -2.76600  1.000 55.28104  ?  2083 HOH   A O   1 
HETATM 27938 O  O   . HOH   M 6 .    ? -23.32100  9.63300   -4.31600  1.000 49.74505  ?  2084 HOH   A O   1 
HETATM 27939 O  O   . HOH   M 6 .    ? -15.53000  95.89700  14.61100  1.000 47.56988  ?  2085 HOH   A O   1 
HETATM 27940 O  O   . HOH   M 6 .    ? -51.78600  79.35900  2.74900   1.000 50.82203  ?  2086 HOH   A O   1 
HETATM 27941 O  O   . HOH   M 6 .    ? -45.40700  85.39800  38.25900  1.000 47.10042  ?  2087 HOH   A O   1 
HETATM 27942 O  O   . HOH   M 6 .    ? -88.88100  59.62000  -12.15500 1.000 56.78163  ?  2088 HOH   A O   1 
HETATM 27943 O  O   . HOH   M 6 .    ? -12.47300  79.14300  43.91800  1.000 62.30448  ?  2089 HOH   A O   1 
HETATM 27944 O  O   . HOH   M 6 .    ? -20.42700  85.84100  11.91000  1.000 48.23579  ?  2090 HOH   A O   1 
HETATM 27945 O  O   . HOH   M 6 .    ? -22.22000  77.36700  -5.48600  1.000 45.37134  ?  2091 HOH   A O   1 
HETATM 27946 O  O   . HOH   M 6 .    ? 10.45900   95.72400  25.91200  1.000 48.63461  ?  2092 HOH   A O   1 
HETATM 27947 O  O   . HOH   M 6 .    ? -66.54300  97.48000  1.16700   1.000 61.92812  ?  2093 HOH   A O   1 
HETATM 27948 O  O   . HOH   M 6 .    ? -69.57500  93.01200  -6.79600  1.000 56.85303  ?  2094 HOH   A O   1 
HETATM 27949 O  O   . HOH   M 6 .    ? -40.66500  79.80300  -9.25300  1.000 36.64236  ?  2095 HOH   A O   1 
HETATM 27950 O  O   . HOH   M 6 .    ? -48.10500  76.89800  10.46700  1.000 106.98485 ?  2096 HOH   A O   1 
HETATM 27951 O  O   . HOH   M 6 .    ? -51.725    68.115    13.388    1.000 44.45340  ?  2097 HOH   A O   1 
HETATM 27952 O  O   . HOH   M 6 .    ? -39.14400  69.57400  34.35800  1.000 67.62550  ?  2098 HOH   A O   1 
HETATM 27953 O  O   . HOH   M 6 .    ? -43.29000  71.26900  35.28000  1.000 43.92669  ?  2099 HOH   A O   1 
HETATM 27954 O  O   . HOH   M 6 .    ? -34.40500  87.24300  2.65800   1.000 43.75673  ?  2100 HOH   A O   1 
HETATM 27955 O  O   . HOH   M 6 .    ? -4.29900   77.46000  25.84400  1.000 51.92962  ?  2101 HOH   A O   1 
HETATM 27956 O  O   . HOH   M 6 .    ? -48.90100  86.58900  -27.94900 1.000 64.74883  ?  2102 HOH   A O   1 
HETATM 27957 O  O   . HOH   M 6 .    ? -56.98900  70.54600  -12.03300 1.000 40.79823  ?  2103 HOH   A O   1 
HETATM 27958 O  O   . HOH   M 6 .    ? -45.31000  83.41600  18.79000  1.000 52.76800  ?  2104 HOH   A O   1 
HETATM 27959 O  O   . HOH   M 6 .    ? -26.74000  66.78700  3.49200   1.000 47.76123  ?  2105 HOH   A O   1 
HETATM 27960 O  O   . HOH   M 6 .    ? -13.07900  41.24300  6.88000   1.000 50.80114  ?  2106 HOH   A O   1 
HETATM 27961 O  O   . HOH   M 6 .    ? -27.68500  82.61300  1.14400   1.000 34.13554  ?  2107 HOH   A O   1 
HETATM 27962 O  O   . HOH   M 6 .    ? -30.01100  105.16600 -5.03400  1.000 62.49196  ?  2108 HOH   A O   1 
HETATM 27963 O  O   . HOH   M 6 .    ? -41.29600  97.09300  -39.29400 1.000 38.12042  ?  2109 HOH   A O   1 
HETATM 27964 O  O   . HOH   M 6 .    ? -29.74500  78.79900  28.40500  1.000 47.58104  ?  2110 HOH   A O   1 
HETATM 27965 O  O   . HOH   M 6 .    ? -41.44900  84.35100  2.14800   1.000 32.33933  ?  2111 HOH   A O   1 
HETATM 27966 O  O   . HOH   M 6 .    ? -40.43900  73.27700  15.96300  1.000 39.04519  ?  2112 HOH   A O   1 
HETATM 27967 O  O   . HOH   M 6 .    ? -13.18600  81.31800  -1.32000  1.000 50.97972  ?  2113 HOH   A O   1 
HETATM 27968 O  O   . HOH   M 6 .    ? -31.64200  105.53300 -6.95000  1.000 65.64712  ?  2114 HOH   A O   1 
HETATM 27969 O  O   . HOH   M 6 .    ? -117.363   69.066    2.906     1.000 43.98633  ?  2115 HOH   A O   1 
HETATM 27970 O  O   . HOH   M 6 .    ? -24.99900  24.54500  -4.58900  1.000 60.84568  ?  2116 HOH   A O   1 
HETATM 27971 O  O   . HOH   M 6 .    ? -42.29900  53.82000  11.48400  1.000 52.57301  ?  2117 HOH   A O   1 
HETATM 27972 O  O   . HOH   M 6 .    ? -35.96700  55.45000  0.07400   1.000 37.78934  ?  2118 HOH   A O   1 
HETATM 27973 O  O   . HOH   M 6 .    ? -12.38600  45.45700  -12.63300 1.000 58.29243  ?  2119 HOH   A O   1 
HETATM 27974 O  O   . HOH   M 6 .    ? -30.59200  69.54300  24.37900  1.000 57.15209  ?  2120 HOH   A O   1 
HETATM 27975 O  O   . HOH   M 6 .    ? -21.02700  32.52200  -10.86200 1.000 54.53358  ?  2121 HOH   A O   1 
HETATM 27976 O  O   . HOH   M 6 .    ? -25.61600  23.52000  6.41800   1.000 33.50957  ?  2122 HOH   A O   1 
HETATM 27977 O  O   . HOH   M 6 .    ? -23.59600  69.29800  -22.30300 1.000 63.54189  ?  2123 HOH   A O   1 
HETATM 27978 O  O   . HOH   M 6 .    ? -74.43300  75.18100  2.71500   1.000 36.01316  ?  2124 HOH   A O   1 
HETATM 27979 O  O   . HOH   M 6 .    ? -43.60700  81.60700  16.92800  1.000 36.79132  ?  2125 HOH   A O   1 
HETATM 27980 O  O   . HOH   M 6 .    ? -30.26900  83.82200  7.23500   1.000 45.36421  ?  2126 HOH   A O   1 
HETATM 27981 O  O   . HOH   M 6 .    ? -45.33900  80.60100  -8.94600  1.000 44.09277  ?  2127 HOH   A O   1 
HETATM 27982 O  O   . HOH   M 6 .    ? -73.95100  72.97800  3.22800   1.000 48.16924  ?  2128 HOH   A O   1 
HETATM 27983 O  O   . HOH   M 6 .    ? -11.79300  92.41300  58.18500  1.000 57.21339  ?  2129 HOH   A O   1 
HETATM 27984 O  O   . HOH   M 6 .    ? -71.12200  64.85300  -19.02800 1.000 43.71692  ?  2130 HOH   A O   1 
HETATM 27985 O  O   . HOH   M 6 .    ? -16.47800  76.70100  36.38500  1.000 47.67033  ?  2131 HOH   A O   1 
HETATM 27986 O  O   . HOH   M 6 .    ? 7.58600    84.59200  21.91400  1.000 42.01039  ?  2132 HOH   A O   1 
HETATM 27987 O  O   . HOH   M 6 .    ? 5.17000    83.69300  36.35000  1.000 51.44839  ?  2133 HOH   A O   1 
HETATM 27988 O  O   . HOH   M 6 .    ? -6.64000   1.75800   9.74000   1.000 52.96190  ?  2134 HOH   A O   1 
HETATM 27989 O  O   . HOH   M 6 .    ? 4.83200    83.90800  45.80900  1.000 37.35173  ?  2135 HOH   A O   1 
HETATM 27990 O  O   . HOH   M 6 .    ? -68.67100  48.66200  37.10800  1.000 44.97100  ?  2136 HOH   A O   1 
HETATM 27991 O  O   . HOH   M 6 .    ? -24.75300  97.34100  -17.74400 1.000 50.14682  ?  2137 HOH   A O   1 
HETATM 27992 O  O   . HOH   M 6 .    ? -27.64800  30.93000  -2.88300  1.000 48.05855  ?  2138 HOH   A O   1 
HETATM 27993 O  O   . HOH   M 6 .    ? -74.15500  71.37100  0.93500   1.000 55.46158  ?  2139 HOH   A O   1 
HETATM 27994 O  O   . HOH   M 6 .    ? -17.20600  27.94300  17.60000  1.000 51.97172  ?  2140 HOH   A O   1 
HETATM 27995 O  O   . HOH   M 6 .    ? -39.18500  83.05000  0.02700   1.000 40.31913  ?  2141 HOH   A O   1 
HETATM 27996 O  O   . HOH   M 6 .    ? -21.30400  108.39200 53.26200  1.000 55.54972  ?  2142 HOH   A O   1 
HETATM 27997 O  O   . HOH   M 6 .    ? -27.93500  4.93400   4.08400   1.000 56.73360  ?  2143 HOH   A O   1 
HETATM 27998 O  O   . HOH   M 6 .    ? -19.85500  72.01600  -8.83200  1.000 46.18973  ?  2144 HOH   A O   1 
HETATM 27999 O  O   . HOH   M 6 .    ? -54.257    73.904    18.626    1.000 40.70189  ?  2145 HOH   A O   1 
HETATM 28000 O  O   . HOH   M 6 .    ? -0.96200   117.65400 45.58800  1.000 52.40300  ?  2146 HOH   A O   1 
HETATM 28001 O  O   . HOH   M 6 .    ? -54.80300  56.53400  18.87600  1.000 44.41486  ?  2147 HOH   A O   1 
HETATM 28002 O  O   . HOH   M 6 .    ? -9.15500   82.06300  43.68300  1.000 59.21418  ?  2148 HOH   A O   1 
HETATM 28003 O  O   . HOH   M 6 .    ? -28.04800  92.69600  -21.90700 1.000 52.00479  ?  2149 HOH   A O   1 
HETATM 28004 O  O   . HOH   M 6 .    ? 1.77500    98.96100  58.79800  1.000 63.65497  ?  2150 HOH   A O   1 
HETATM 28005 O  O   . HOH   M 6 .    ? -79.11800  67.61000  -10.53500 1.000 46.41693  ?  2151 HOH   A O   1 
HETATM 28006 O  O   . HOH   M 6 .    ? -37.02500  83.14600  -30.62500 1.000 51.98877  ?  2152 HOH   A O   1 
HETATM 28007 O  O   . HOH   M 6 .    ? -70.24100  72.69700  10.07600  1.000 36.38229  ?  2153 HOH   A O   1 
HETATM 28008 O  O   . HOH   M 6 .    ? -57.37400  61.91900  -7.75200  1.000 52.55671  ?  2154 HOH   A O   1 
HETATM 28009 O  O   . HOH   M 6 .    ? -13.70300  83.69900  5.02800   1.000 48.26895  ?  2155 HOH   A O   1 
HETATM 28010 O  O   . HOH   M 6 .    ? -39.89100  44.87500  8.24500   1.000 74.20499  ?  2156 HOH   A O   1 
HETATM 28011 O  O   . HOH   M 6 .    ? -18.85800  100.88800 -7.02200  1.000 55.43814  ?  2157 HOH   A O   1 
HETATM 28012 O  O   . HOH   M 6 .    ? -41.95600  97.73000  -32.59300 1.000 52.60213  ?  2158 HOH   A O   1 
HETATM 28013 O  O   . HOH   M 6 .    ? -29.44600  19.80700  -1.06900  1.000 59.66878  ?  2159 HOH   A O   1 
HETATM 28014 O  O   . HOH   M 6 .    ? -19.39900  83.38800  -10.08700 1.000 50.87349  ?  2160 HOH   A O   1 
HETATM 28015 O  O   . HOH   M 6 .    ? -32.94700  74.80900  -22.33500 1.000 39.70256  ?  2161 HOH   A O   1 
HETATM 28016 O  O   . HOH   M 6 .    ? -43.12500  47.46400  -3.84000  1.000 52.30392  ?  2162 HOH   A O   1 
HETATM 28017 O  O   . HOH   M 6 .    ? -57.34200  69.92700  -0.06700  1.000 51.30282  ?  2163 HOH   A O   1 
HETATM 28018 O  O   . HOH   M 6 .    ? -35.34800  96.13100  24.06800  1.000 46.87040  ?  2164 HOH   A O   1 
HETATM 28019 O  O   . HOH   M 6 .    ? -34.81000  65.89900  7.71000   1.000 42.41732  ?  2165 HOH   A O   1 
HETATM 28020 O  O   . HOH   M 6 .    ? -29.06700  23.29500  2.31200   1.000 43.56786  ?  2166 HOH   A O   1 
HETATM 28021 O  O   . HOH   M 6 .    ? -75.52800  62.80900  17.59300  1.000 59.93804  ?  2167 HOH   A O   1 
HETATM 28022 O  O   . HOH   M 6 .    ? -59.53800  93.45100  -3.69100  1.000 53.48496  ?  2168 HOH   A O   1 
HETATM 28023 O  O   . HOH   M 6 .    ? -32.20100  107.89000 -17.00600 1.000 49.58830  ?  2169 HOH   A O   1 
HETATM 28024 O  O   . HOH   M 6 .    ? -14.90200  97.41600  26.23200  1.000 40.89194  ?  2170 HOH   A O   1 
HETATM 28025 O  O   . HOH   M 6 .    ? -37.39900  50.56700  -8.97000  1.000 45.34240  ?  2171 HOH   A O   1 
HETATM 28026 O  O   . HOH   M 6 .    ? -25.94700  73.16800  26.36200  1.000 56.19005  ?  2172 HOH   A O   1 
HETATM 28027 O  O   . HOH   M 6 .    ? -32.92500  97.58000  41.13800  1.000 49.26541  ?  2173 HOH   A O   1 
HETATM 28028 O  O   . HOH   M 6 .    ? -30.23800  87.00800  -7.66400  1.000 51.70464  ?  2174 HOH   A O   1 
HETATM 28029 O  O   . HOH   M 6 .    ? -21.65100  64.62900  -4.15200  1.000 41.36225  ?  2175 HOH   A O   1 
HETATM 28030 O  O   . HOH   M 6 .    ? -72.97500  66.44500  -4.76000  1.000 52.53061  ?  2176 HOH   A O   1 
HETATM 28031 O  O   . HOH   M 6 .    ? -25.39100  77.93500  1.61300   1.000 62.16949  ?  2177 HOH   A O   1 
HETATM 28032 O  O   . HOH   M 6 .    ? -43.07000  78.17100  34.09800  1.000 45.51586  ?  2178 HOH   A O   1 
HETATM 28033 O  O   . HOH   M 6 .    ? -30.75300  80.55300  7.59400   1.000 51.60886  ?  2179 HOH   A O   1 
HETATM 28034 O  O   . HOH   M 6 .    ? -21.85500  12.77100  -4.21900  1.000 34.52066  ?  2180 HOH   A O   1 
HETATM 28035 O  O   . HOH   M 6 .    ? -64.32600  52.71700  16.02800  1.000 52.55350  ?  2181 HOH   A O   1 
HETATM 28036 O  O   . HOH   M 6 .    ? -50.61100  82.40100  -3.96500  1.000 46.25554  ?  2182 HOH   A O   1 
HETATM 28037 O  O   . HOH   M 6 .    ? -57.76100  67.20800  2.82300   1.000 44.58716  ?  2183 HOH   A O   1 
HETATM 28038 O  O   . HOH   M 6 .    ? -59.21800  52.26300  -9.54200  1.000 59.99347  ?  2184 HOH   A O   1 
HETATM 28039 O  O   . HOH   M 6 .    ? -6.85600   42.13100  -9.51500  1.000 52.59779  ?  2185 HOH   A O   1 
HETATM 28040 O  O   . HOH   M 6 .    ? -55.64100  68.21000  -0.24400  1.000 54.73947  ?  2186 HOH   A O   1 
HETATM 28041 O  O   . HOH   M 6 .    ? -77.45600  86.63500  9.80100   1.000 58.25468  ?  2187 HOH   A O   1 
HETATM 28042 O  O   . HOH   M 6 .    ? -72.60000  72.84700  14.00500  1.000 50.10948  ?  2188 HOH   A O   1 
HETATM 28043 O  O   . HOH   M 6 .    ? -74.88300  83.22900  11.70900  1.000 60.28415  ?  2189 HOH   A O   1 
HETATM 28044 O  O   . HOH   M 6 .    ? 10.70800   86.75400  26.62800  1.000 37.86345  ?  2190 HOH   A O   1 
HETATM 28045 O  O   . HOH   M 6 .    ? -33.05300  100.45600 -10.37700 1.000 41.33100  ?  2191 HOH   A O   1 
HETATM 28046 O  O   . HOH   M 6 .    ? -56.24800  53.19200  6.90400   1.000 39.30974  ?  2192 HOH   A O   1 
HETATM 28047 O  O   . HOH   M 6 .    ? -23.28300  79.29000  10.43400  1.000 52.95379  ?  2193 HOH   A O   1 
HETATM 28048 O  O   . HOH   M 6 .    ? -9.51000   77.67900  13.44300  1.000 47.65212  ?  2194 HOH   A O   1 
HETATM 28049 O  O   . HOH   M 6 .    ? -45.58700  55.32200  27.92300  1.000 44.61231  ?  2195 HOH   A O   1 
HETATM 28050 O  O   . HOH   M 6 .    ? -33.70800  89.02200  7.08000   1.000 48.75319  ?  2196 HOH   A O   1 
HETATM 28051 O  O   . HOH   M 6 .    ? -13.09200  75.16000  28.10300  1.000 36.38379  ?  2197 HOH   A O   1 
HETATM 28052 O  O   . HOH   M 6 .    ? -42.30100  55.44500  22.30200  1.000 50.54938  ?  2198 HOH   A O   1 
HETATM 28053 O  O   . HOH   M 6 .    ? -38.90000  82.10300  -8.34800  1.000 38.43854  ?  2199 HOH   A O   1 
HETATM 28054 O  O   . HOH   M 6 .    ? -21.24800  44.39700  -11.93500 1.000 58.78481  ?  2200 HOH   A O   1 
HETATM 28055 O  O   . HOH   M 6 .    ? -46.84400  46.12600  -4.88900  1.000 56.98158  ?  2201 HOH   A O   1 
HETATM 28056 O  O   . HOH   M 6 .    ? 12.941     90.883    25.046    1.000 53.82147  ?  2202 HOH   A O   1 
HETATM 28057 O  O   . HOH   M 6 .    ? -70.09800  52.43900  -31.49200 1.000 47.36605  ?  2203 HOH   A O   1 
HETATM 28058 O  O   . HOH   M 6 .    ? -65.460    60.482    4.010     1.000 50.86079  ?  2204 HOH   A O   1 
HETATM 28059 O  O   . HOH   M 6 .    ? -3.52800   109.68200 56.06700  1.000 45.95572  ?  2205 HOH   A O   1 
HETATM 28060 O  O   . HOH   M 6 .    ? -48.70100  88.68900  -8.54900  1.000 50.36847  ?  2206 HOH   A O   1 
HETATM 28061 O  O   . HOH   M 6 .    ? -45.22600  73.63700  -28.44900 1.000 40.70521  ?  2207 HOH   A O   1 
HETATM 28062 O  O   . HOH   M 6 .    ? -3.15200   27.32700  -6.69500  1.000 52.73220  ?  2208 HOH   A O   1 
HETATM 28063 O  O   . HOH   M 6 .    ? -57.62900  59.76000  -29.42700 1.000 61.33449  ?  2209 HOH   A O   1 
HETATM 28064 O  O   . HOH   M 6 .    ? -72.43100  47.93200  -1.03800  1.000 57.73929  ?  2210 HOH   A O   1 
HETATM 28065 O  O   . HOH   M 6 .    ? -21.08900  98.17100  57.15000  1.000 43.06724  ?  2211 HOH   A O   1 
HETATM 28066 O  O   . HOH   M 6 .    ? -23.65600  6.11100   19.06900  1.000 44.29372  ?  2212 HOH   A O   1 
HETATM 28067 O  O   . HOH   M 6 .    ? -16.21300  81.45200  52.97500  1.000 50.09153  ?  2213 HOH   A O   1 
HETATM 28068 O  O   . HOH   M 6 .    ? -20.03200  80.67100  -3.55400  1.000 44.04554  ?  2214 HOH   A O   1 
HETATM 28069 O  O   . HOH   M 6 .    ? -78.60700  50.98100  31.61100  1.000 57.17949  ?  2215 HOH   A O   1 
HETATM 28070 O  O   . HOH   M 6 .    ? -17.17000  72.96100  -10.90100 1.000 51.56086  ?  2216 HOH   A O   1 
HETATM 28071 O  O   . HOH   M 6 .    ? -42.13700  93.95100  -1.45700  1.000 47.04903  ?  2217 HOH   A O   1 
HETATM 28072 O  O   . HOH   M 6 .    ? -86.87400  61.62900  -12.75700 1.000 68.57315  ?  2218 HOH   A O   1 
HETATM 28073 O  O   . HOH   M 6 .    ? -4.66700   79.19000  13.33000  1.000 46.90854  ?  2219 HOH   A O   1 
HETATM 28074 O  O   . HOH   M 6 .    ? -29.823    89.480    48.909    1.000 53.74375  ?  2220 HOH   A O   1 
HETATM 28075 O  O   . HOH   M 6 .    ? -18.74100  95.24600  11.25400  1.000 45.53936  ?  2221 HOH   A O   1 
HETATM 28076 O  O   . HOH   M 6 .    ? -52.05100  69.56600  -1.07000  1.000 60.50167  ?  2222 HOH   A O   1 
HETATM 28077 O  O   . HOH   M 6 .    ? -49.09500  57.76700  9.62100   1.000 55.04561  ?  2223 HOH   A O   1 
HETATM 28078 O  O   . HOH   M 6 .    ? -50.23000  78.21600  15.08500  1.000 58.74698  ?  2224 HOH   A O   1 
HETATM 28079 O  O   . HOH   M 6 .    ? -18.32300  101.32600 21.74300  1.000 61.21132  ?  2225 HOH   A O   1 
HETATM 28080 O  O   . HOH   M 6 .    ? -1.59600   32.50500  5.94200   1.000 39.69533  ?  2226 HOH   A O   1 
HETATM 28081 O  O   . HOH   M 6 .    ? -39.89800  48.27100  2.05700   1.000 45.29202  ?  2227 HOH   A O   1 
HETATM 28082 O  O   . HOH   M 6 .    ? -64.73600  91.88900  20.65500  1.000 57.65161  ?  2228 HOH   A O   1 
HETATM 28083 O  O   . HOH   M 6 .    ? -16.22100  70.35300  13.99800  1.000 58.09441  ?  2229 HOH   A O   1 
HETATM 28084 O  O   . HOH   M 6 .    ? -71.90400  69.53600  16.56200  1.000 62.20365  ?  2230 HOH   A O   1 
HETATM 28085 O  O   . HOH   M 6 .    ? -53.73600  88.29900  10.90200  1.000 36.52137  ?  2231 HOH   A O   1 
HETATM 28086 O  O   . HOH   M 6 .    ? -121.415   77.419    -1.616    1.000 64.65175  ?  2232 HOH   A O   1 
HETATM 28087 O  O   . HOH   M 6 .    ? -26.82500  101.90000 -25.17300 1.000 37.74337  ?  2233 HOH   A O   1 
HETATM 28088 O  O   . HOH   M 6 .    ? -34.23900  86.74000  -7.04600  1.000 50.81201  ?  2234 HOH   A O   1 
HETATM 28089 O  O   . HOH   M 6 .    ? -22.63000  49.50800  6.68900   1.000 53.65669  ?  2235 HOH   A O   1 
HETATM 28090 O  O   . HOH   M 6 .    ? -33.13300  88.61700  -31.63300 1.000 52.42115  ?  2236 HOH   A O   1 
HETATM 28091 O  O   . HOH   M 6 .    ? -53.72200  92.14300  -19.72000 1.000 44.77350  ?  2237 HOH   A O   1 
HETATM 28092 O  O   . HOH   M 6 .    ? -49.81700  76.78500  -29.02500 1.000 53.46826  ?  2238 HOH   A O   1 
HETATM 28093 O  O   . HOH   M 6 .    ? -51.37600  80.45200  -5.16300  1.000 54.24447  ?  2239 HOH   A O   1 
HETATM 28094 O  O   . HOH   M 6 .    ? -46.194    67.138    10.239    1.000 55.71077  ?  2240 HOH   A O   1 
HETATM 28095 O  O   . HOH   M 6 .    ? -36.39800  84.69800  -7.94000  1.000 63.56842  ?  2241 HOH   A O   1 
HETATM 28096 O  O   . HOH   M 6 .    ? -22.45100  91.19000  19.03000  1.000 23.37192  ?  2242 HOH   A O   1 
HETATM 28097 O  O   . HOH   M 6 .    ? -43.05500  79.88100  -7.43900  1.000 34.34881  ?  2243 HOH   A O   1 
HETATM 28098 O  O   . HOH   M 6 .    ? -39.61200  85.60200  -6.70100  1.000 70.72604  ?  2244 HOH   A O   1 
HETATM 28099 O  O   . HOH   M 6 .    ? -21.55100  55.37700  -19.54900 1.000 56.32929  ?  2245 HOH   A O   1 
HETATM 28100 O  O   . HOH   M 6 .    ? 2.07800    85.51500  53.02800  1.000 59.44586  ?  2246 HOH   A O   1 
HETATM 28101 O  O   . HOH   M 6 .    ? -2.78400   102.91800 12.45700  1.000 50.85825  ?  2247 HOH   A O   1 
HETATM 28102 O  O   . HOH   M 6 .    ? -32.13100  97.70400  -5.25200  1.000 41.96124  ?  2248 HOH   A O   1 
HETATM 28103 O  O   . HOH   M 6 .    ? -35.59200  106.31400 -4.49800  1.000 57.94686  ?  2249 HOH   A O   1 
HETATM 28104 O  O   . HOH   M 6 .    ? 2.46400    96.68500  10.05300  1.000 59.19434  ?  2250 HOH   A O   1 
HETATM 28105 O  O   . HOH   M 6 .    ? -53.55700  87.83500  13.62400  1.000 40.71849  ?  2251 HOH   A O   1 
HETATM 28106 O  O   . HOH   M 6 .    ? -52.93000  85.61300  18.07100  1.000 47.63298  ?  2252 HOH   A O   1 
HETATM 28107 O  O   . HOH   M 6 .    ? -25.75800  89.12200  11.26100  1.000 44.21478  ?  2253 HOH   A O   1 
HETATM 28108 O  O   . HOH   M 6 .    ? -2.86900   125.22300 39.20100  1.000 66.30095  ?  2254 HOH   A O   1 
HETATM 28109 O  O   . HOH   M 6 .    ? -26.39200  93.61200  -14.45300 1.000 61.31440  ?  2255 HOH   A O   1 
HETATM 28110 O  O   . HOH   M 6 .    ? -17.60500  50.94700  12.12800  1.000 62.84074  ?  2256 HOH   A O   1 
HETATM 28111 O  O   . HOH   M 6 .    ? -5.47800   107.33400 57.98300  1.000 49.76845  ?  2257 HOH   A O   1 
HETATM 28112 O  O   . HOH   M 6 .    ? -84.86100  83.46700  -17.86400 1.000 57.48061  ?  2258 HOH   A O   1 
HETATM 28113 O  O   . HOH   M 6 .    ? -31.56100  31.60700  -4.62100  1.000 43.64618  ?  2259 HOH   A O   1 
HETATM 28114 O  O   . HOH   M 6 .    ? -47.16900  50.88400  24.09400  1.000 52.07382  ?  2260 HOH   A O   1 
HETATM 28115 O  O   . HOH   M 6 .    ? -41.28700  75.47300  14.90200  1.000 40.40285  ?  2261 HOH   A O   1 
HETATM 28116 O  O   . HOH   M 6 .    ? -57.09300  50.46000  53.57200  1.000 79.56747  ?  2262 HOH   A O   1 
HETATM 28117 O  O   . HOH   M 6 .    ? -50.11500  53.62200  37.02100  1.000 45.33734  ?  2263 HOH   A O   1 
HETATM 28118 O  O   . HOH   M 6 .    ? -52.71500  76.99900  26.69100  1.000 52.93014  ?  2264 HOH   A O   1 
HETATM 28119 O  O   . HOH   M 6 .    ? -41.12000  89.83100  -35.85000 1.000 65.25806  ?  2265 HOH   A O   1 
HETATM 28120 O  O   . HOH   M 6 .    ? -21.13000  53.32300  6.30000   1.000 71.81362  ?  2266 HOH   A O   1 
HETATM 28121 O  O   . HOH   M 6 .    ? -21.49600  69.24300  11.38800  1.000 50.78761  ?  2267 HOH   A O   1 
HETATM 28122 O  O   . HOH   M 6 .    ? -46.23500  89.82800  3.60100   1.000 50.27246  ?  2268 HOH   A O   1 
HETATM 28123 O  O   . HOH   M 6 .    ? -19.18000  73.32700  18.86900  1.000 46.75816  ?  2269 HOH   A O   1 
HETATM 28124 O  O   . HOH   M 6 .    ? -28.39400  24.70000  -6.57900  1.000 54.56160  ?  2270 HOH   A O   1 
HETATM 28125 O  O   . HOH   M 6 .    ? -71.83300  77.90900  24.22400  1.000 60.37513  ?  2271 HOH   A O   1 
HETATM 28126 O  O   . HOH   M 6 .    ? -43.52700  92.68100  31.98800  1.000 45.74031  ?  2272 HOH   A O   1 
HETATM 28127 O  O   . HOH   M 6 .    ? -75.94800  34.83000  -8.52800  1.000 59.04428  ?  2273 HOH   A O   1 
HETATM 28128 O  O   . HOH   M 6 .    ? -83.99800  67.83100  -12.99400 1.000 56.97985  ?  2274 HOH   A O   1 
HETATM 28129 O  O   . HOH   M 6 .    ? -48.64600  54.69000  16.24900  1.000 63.89299  ?  2275 HOH   A O   1 
HETATM 28130 O  O   . HOH   M 6 .    ? -58.49000  95.34200  -2.57100  1.000 64.08880  ?  2276 HOH   A O   1 
HETATM 28131 O  O   . HOH   M 6 .    ? -67.75200  91.06000  23.87800  1.000 58.52420  ?  2277 HOH   A O   1 
HETATM 28132 O  O   . HOH   N 6 .    ? 132.876    69.071    1.549     1.000 53.38657  ?  2001 HOH   B O   1 
HETATM 28133 O  O   . HOH   N 6 .    ? 70.53000   28.03400  13.24300  1.000 67.43891  ?  2002 HOH   B O   1 
HETATM 28134 O  O   . HOH   N 6 .    ? 21.18500   88.95000  -48.10300 1.000 34.86604  ?  2003 HOH   B O   1 
HETATM 28135 O  O   . HOH   N 6 .    ? 49.11500   41.90600  -8.02000  1.000 62.16007  ?  2004 HOH   B O   1 
HETATM 28136 O  O   . HOH   N 6 .    ? 46.21500   79.49400  -23.90500 1.000 42.41201  ?  2005 HOH   B O   1 
HETATM 28137 O  O   . HOH   N 6 .    ? 49.71700   83.45000  12.12600  1.000 40.27872  ?  2006 HOH   B O   1 
HETATM 28138 O  O   . HOH   N 6 .    ? 44.37800   96.30500  -9.98600  1.000 58.81790  ?  2007 HOH   B O   1 
HETATM 28139 O  O   . HOH   N 6 .    ? 25.70300   88.20900  -49.84700 1.000 40.88651  ?  2008 HOH   B O   1 
HETATM 28140 O  O   . HOH   N 6 .    ? 68.123     98.529    34.879    1.000 57.36823  ?  2009 HOH   B O   1 
HETATM 28141 O  O   . HOH   N 6 .    ? 13.15400   1.67200   6.06100   1.000 52.31940  ?  2010 HOH   B O   1 
HETATM 28142 O  O   . HOH   N 6 .    ? 36.84100   98.24200  -44.56800 1.000 31.28311  ?  2011 HOH   B O   1 
HETATM 28143 O  O   . HOH   N 6 .    ? 17.93500   23.20500  3.92100   1.000 47.95619  ?  2012 HOH   B O   1 
HETATM 28144 O  O   . HOH   N 6 .    ? 89.48700   79.17300  -10.71900 1.000 47.52935  ?  2013 HOH   B O   1 
HETATM 28145 O  O   . HOH   N 6 .    ? 38.87500   9.18200   -7.81100  1.000 58.05265  ?  2014 HOH   B O   1 
HETATM 28146 O  O   . HOH   N 6 .    ? 68.53100   88.05000  9.69000   1.000 59.11938  ?  2015 HOH   B O   1 
HETATM 28147 O  O   . HOH   N 6 .    ? 59.30200   22.34800  -7.06800  1.000 70.16786  ?  2016 HOH   B O   1 
HETATM 28148 O  O   . HOH   N 6 .    ? 19.60100   77.33500  -26.68600 1.000 44.76893  ?  2017 HOH   B O   1 
HETATM 28149 O  O   . HOH   N 6 .    ? 82.91400   69.24500  -10.38200 1.000 40.12714  ?  2018 HOH   B O   1 
HETATM 28150 O  O   . HOH   N 6 .    ? 44.33000   106.85700 -31.57400 1.000 49.93126  ?  2019 HOH   B O   1 
HETATM 28151 O  O   . HOH   N 6 .    ? 49.01400   96.11700  38.37000  1.000 32.22457  ?  2020 HOH   B O   1 
HETATM 28152 O  O   . HOH   N 6 .    ? 96.93300   82.40300  19.99700  1.000 62.05845  ?  2021 HOH   B O   1 
HETATM 28153 O  O   . HOH   N 6 .    ? 16.74500   13.21300  -9.38900  1.000 53.22712  ?  2022 HOH   B O   1 
HETATM 28154 O  O   . HOH   N 6 .    ? 37.80700   25.98200  11.37600  1.000 58.47403  ?  2023 HOH   B O   1 
HETATM 28155 O  O   . HOH   N 6 .    ? 50.59100   108.35600 24.70500  1.000 40.38449  ?  2024 HOH   B O   1 
HETATM 28156 O  O   . HOH   N 6 .    ? 77.11700   57.77900  -12.22400 1.000 57.66158  ?  2025 HOH   B O   1 
HETATM 28157 O  O   . HOH   N 6 .    ? 57.33400   69.97000  -30.75500 1.000 61.89964  ?  2026 HOH   B O   1 
HETATM 28158 O  O   . HOH   N 6 .    ? 66.89000   78.99100  2.35400   1.000 46.53702  ?  2027 HOH   B O   1 
HETATM 28159 O  O   . HOH   N 6 .    ? 14.10200   104.34000 -34.05200 1.000 55.75144  ?  2028 HOH   B O   1 
HETATM 28160 O  O   . HOH   N 6 .    ? 33.28900   77.48000  -17.73700 1.000 50.61294  ?  2029 HOH   B O   1 
HETATM 28161 O  O   . HOH   N 6 .    ? 64.25200   93.88700  15.79800  1.000 54.20521  ?  2030 HOH   B O   1 
HETATM 28162 O  O   . HOH   N 6 .    ? 66.883     76.453    3.651     1.000 49.92154  ?  2031 HOH   B O   1 
HETATM 28163 O  O   . HOH   N 6 .    ? 50.24300   65.98600  -24.79700 1.000 72.15264  ?  2032 HOH   B O   1 
HETATM 28164 O  O   . HOH   N 6 .    ? 34.69600   104.80000 -31.32500 1.000 48.79199  ?  2033 HOH   B O   1 
HETATM 28165 O  O   . HOH   N 6 .    ? 68.16600   77.53400  -20.27700 1.000 40.57230  ?  2034 HOH   B O   1 
HETATM 28166 O  O   . HOH   N 6 .    ? 51.95000   83.89200  32.39800  1.000 51.17141  ?  2035 HOH   B O   1 
HETATM 28167 O  O   . HOH   N 6 .    ? 34.14200   40.49800  21.78400  1.000 56.22716  ?  2036 HOH   B O   1 
HETATM 28168 O  O   . HOH   N 6 .    ? 30.01100   50.77700  11.53500  1.000 61.06254  ?  2037 HOH   B O   1 
HETATM 28169 O  O   . HOH   N 6 .    ? 42.37400   98.77900  15.13200  1.000 54.46618  ?  2038 HOH   B O   1 
HETATM 28170 O  O   . HOH   N 6 .    ? 15.50100   26.46300  17.06700  1.000 63.74643  ?  2039 HOH   B O   1 
HETATM 28171 O  O   . HOH   N 6 .    ? 39.08300   107.50500 -43.78000 1.000 47.26212  ?  2040 HOH   B O   1 
HETATM 28172 O  O   . HOH   N 6 .    ? 8.70600    85.08400  -7.94700  1.000 54.33922  ?  2041 HOH   B O   1 
HETATM 28173 O  O   . HOH   N 6 .    ? 48.69000   86.04300  -33.10100 1.000 35.46814  ?  2042 HOH   B O   1 
HETATM 28174 O  O   . HOH   N 6 .    ? 82.22600   97.24900  4.38800   1.000 58.79482  ?  2043 HOH   B O   1 
HETATM 28175 O  O   . HOH   N 6 .    ? 38.32400   96.58200  -17.69600 1.000 49.08735  ?  2044 HOH   B O   1 
HETATM 28176 O  O   . HOH   N 6 .    ? 11.63400   27.41600  11.47200  1.000 54.79875  ?  2045 HOH   B O   1 
HETATM 28177 O  O   . HOH   N 6 .    ? 43.34500   104.61600 -21.71100 1.000 52.69684  ?  2046 HOH   B O   1 
HETATM 28178 O  O   . HOH   N 6 .    ? 24.93600   2.87800   5.77200   1.000 54.55931  ?  2047 HOH   B O   1 
HETATM 28179 O  O   . HOH   N 6 .    ? 33.94000   32.21600  22.04700  1.000 73.75106  ?  2048 HOH   B O   1 
HETATM 28180 O  O   . HOH   N 6 .    ? 60.05600   56.12600  14.10300  1.000 66.67100  ?  2049 HOH   B O   1 
HETATM 28181 O  O   . HOH   N 6 .    ? 88.72400   73.90300  3.95500   1.000 37.13227  ?  2050 HOH   B O   1 
HETATM 28182 O  O   . HOH   N 6 .    ? 45.23000   88.04800  10.74600  1.000 47.30985  ?  2051 HOH   B O   1 
HETATM 28183 O  O   . HOH   N 6 .    ? 84.21600   92.16300  12.59400  1.000 55.44402  ?  2052 HOH   B O   1 
HETATM 28184 O  O   . HOH   N 6 .    ? 36.36300   108.97700 -3.67200  1.000 71.36754  ?  2053 HOH   B O   1 
HETATM 28185 O  O   . HOH   N 6 .    ? 51.79800   85.85700  -35.40000 1.000 37.13630  ?  2054 HOH   B O   1 
HETATM 28186 O  O   . HOH   N 6 .    ? 21.17300   109.26800 -53.06100 1.000 63.99421  ?  2055 HOH   B O   1 
HETATM 28187 O  O   . HOH   N 6 .    ? 41.40800   97.71300  -23.33100 1.000 35.39778  ?  2056 HOH   B O   1 
HETATM 28188 O  O   . HOH   N 6 .    ? 64.427     67.414    -6.741    1.000 36.34482  ?  2057 HOH   B O   1 
HETATM 28189 O  O   . HOH   N 6 .    ? 35.26300   81.06300  -34.38400 1.000 30.01727  ?  2058 HOH   B O   1 
HETATM 28190 O  O   . HOH   N 6 .    ? 69.28400   87.73300  -5.89500  1.000 36.19692  ?  2059 HOH   B O   1 
HETATM 28191 O  O   . HOH   N 6 .    ? 14.88400   104.24000 -42.45400 1.000 48.08241  ?  2060 HOH   B O   1 
HETATM 28192 O  O   . HOH   N 6 .    ? 71.93400   55.77000  25.67400  1.000 57.00148  ?  2061 HOH   B O   1 
HETATM 28193 O  O   . HOH   N 6 .    ? 70.06300   74.80700  -12.16200 1.000 26.22156  ?  2062 HOH   B O   1 
HETATM 28194 O  O   . HOH   N 6 .    ? 79.61400   76.56600  -28.05900 1.000 53.81411  ?  2063 HOH   B O   1 
HETATM 28195 O  O   . HOH   N 6 .    ? 60.23300   51.54900  10.97000  1.000 51.97125  ?  2064 HOH   B O   1 
HETATM 28196 O  O   . HOH   N 6 .    ? 15.27000   5.95400   15.80100  1.000 51.85662  ?  2065 HOH   B O   1 
HETATM 28197 O  O   . HOH   N 6 .    ? 27.79100   43.73800  2.51600   1.000 56.09759  ?  2066 HOH   B O   1 
HETATM 28198 O  O   . HOH   N 6 .    ? 41.47400   24.29400  4.79800   1.000 45.16843  ?  2067 HOH   B O   1 
HETATM 28199 O  O   . HOH   N 6 .    ? 75.82000   66.67400  -28.86400 1.000 38.59109  ?  2068 HOH   B O   1 
HETATM 28200 O  O   . HOH   N 6 .    ? 95.18000   79.55100  7.58900   1.000 55.46574  ?  2069 HOH   B O   1 
HETATM 28201 O  O   . HOH   N 6 .    ? 100.53800  60.62100  -33.80100 1.000 60.66938  ?  2070 HOH   B O   1 
HETATM 28202 O  O   . HOH   N 6 .    ? 29.29400   90.26500  -54.12700 1.000 53.39340  ?  2071 HOH   B O   1 
HETATM 28203 O  O   . HOH   N 6 .    ? 53.85400   84.94400  35.65600  1.000 47.18072  ?  2072 HOH   B O   1 
HETATM 28204 O  O   . HOH   N 6 .    ? 32.10200   84.68600  -4.33200  1.000 46.62908  ?  2073 HOH   B O   1 
HETATM 28205 O  O   . HOH   N 6 .    ? 52.32100   84.11900  14.18700  1.000 46.10441  ?  2074 HOH   B O   1 
HETATM 28206 O  O   . HOH   N 6 .    ? 37.45800   90.70800  -15.10800 1.000 53.75643  ?  2075 HOH   B O   1 
HETATM 28207 O  O   . HOH   N 6 .    ? 78.65600   93.01800  -10.54400 1.000 60.03767  ?  2076 HOH   B O   1 
HETATM 28208 O  O   . HOH   N 6 .    ? 47.60900   72.85900  -1.30900  1.000 45.02945  ?  2077 HOH   B O   1 
HETATM 28209 O  O   . HOH   N 6 .    ? 54.89700   81.34200  13.17100  1.000 46.11384  ?  2078 HOH   B O   1 
HETATM 28210 O  O   . HOH   N 6 .    ? 53.07200   93.98600  -34.32600 1.000 41.38666  ?  2079 HOH   B O   1 
HETATM 28211 O  O   . HOH   N 6 .    ? 34.46700   106.52600 15.36000  1.000 54.02670  ?  2080 HOH   B O   1 
HETATM 28212 O  O   . HOH   N 6 .    ? 56.60100   95.77800  -24.42000 1.000 44.75006  ?  2081 HOH   B O   1 
HETATM 28213 O  O   . HOH   N 6 .    ? 47.77000   81.07100  25.88200  1.000 57.37696  ?  2082 HOH   B O   1 
HETATM 28214 O  O   . HOH   N 6 .    ? 83.16900   87.97600  -14.26100 1.000 49.94558  ?  2083 HOH   B O   1 
HETATM 28215 O  O   . HOH   N 6 .    ? 16.58900   79.61100  -17.51300 1.000 54.57134  ?  2084 HOH   B O   1 
HETATM 28216 O  O   . HOH   N 6 .    ? 23.14800   34.97300  -7.99300  1.000 52.55718  ?  2085 HOH   B O   1 
HETATM 28217 O  O   . HOH   N 6 .    ? 49.03300   39.00900  -5.87900  1.000 57.83564  ?  2086 HOH   B O   1 
HETATM 28218 O  O   . HOH   N 6 .    ? 39.83700   97.23400  24.74100  1.000 58.61348  ?  2087 HOH   B O   1 
HETATM 28219 O  O   . HOH   N 6 .    ? 81.88200   67.23400  -31.29000 1.000 45.94477  ?  2088 HOH   B O   1 
HETATM 28220 O  O   . HOH   N 6 .    ? 100.02700  53.16200  -27.90200 1.000 39.74144  ?  2089 HOH   B O   1 
HETATM 28221 O  O   . HOH   N 6 .    ? 24.02700   37.17900  3.46900   1.000 50.71413  ?  2090 HOH   B O   1 
HETATM 28222 O  O   . HOH   N 6 .    ? 72.66100   76.25700  -20.56500 1.000 37.52590  ?  2091 HOH   B O   1 
HETATM 28223 O  O   . HOH   N 6 .    ? 77.51400   65.56000  -27.63300 1.000 36.06623  ?  2092 HOH   B O   1 
HETATM 28224 O  O   . HOH   N 6 .    ? 123.846    60.032    6.440     1.000 42.14792  ?  2093 HOH   B O   1 
HETATM 28225 O  O   . HOH   N 6 .    ? 7.41000    88.02800  -11.46600 1.000 44.26210  ?  2094 HOH   B O   1 
HETATM 28226 O  O   . HOH   N 6 .    ? 35.43300   29.01900  28.66000  1.000 73.52905  ?  2095 HOH   B O   1 
HETATM 28227 O  O   . HOH   N 6 .    ? 56.82300   59.54700  -24.68800 1.000 51.07091  ?  2096 HOH   B O   1 
HETATM 28228 O  O   . HOH   N 6 .    ? 29.25500   75.88600  -23.47600 1.000 35.81225  ?  2097 HOH   B O   1 
HETATM 28229 O  O   . HOH   N 6 .    ? 84.60200   71.91900  28.43200  1.000 66.86781  ?  2098 HOH   B O   1 
HETATM 28230 O  O   . HOH   N 6 .    ? 71.95700   72.14100  -21.28900 1.000 43.09594  ?  2099 HOH   B O   1 
HETATM 28231 O  O   . HOH   N 6 .    ? 41.62000   104.84800 -42.08900 1.000 48.06283  ?  2100 HOH   B O   1 
HETATM 28232 O  O   . HOH   N 6 .    ? 22.36800   34.65100  1.01000   1.000 61.34254  ?  2101 HOH   B O   1 
HETATM 28233 O  O   . HOH   N 6 .    ? 18.91500   117.07100 -41.84500 1.000 48.02505  ?  2102 HOH   B O   1 
HETATM 28234 O  O   . HOH   N 6 .    ? 44.20500   89.99500  24.06900  1.000 48.35177  ?  2103 HOH   B O   1 
HETATM 28235 O  O   . HOH   N 6 .    ? 40.24700   18.31200  11.81500  1.000 45.83303  ?  2104 HOH   B O   1 
HETATM 28236 O  O   . HOH   N 6 .    ? 27.31900   103.19000 -55.31300 1.000 45.76684  ?  2105 HOH   B O   1 
HETATM 28237 O  O   . HOH   N 6 .    ? 36.00600   1.78100   -2.07600  1.000 63.31747  ?  2106 HOH   B O   1 
HETATM 28238 O  O   . HOH   N 6 .    ? 45.08600   99.98800  5.36500   1.000 48.72226  ?  2107 HOH   B O   1 
HETATM 28239 O  O   . HOH   N 6 .    ? 39.10100   80.51400  -4.77100  1.000 51.28034  ?  2108 HOH   B O   1 
HETATM 28240 O  O   . HOH   N 6 .    ? 66.51400   92.95000  0.15400   1.000 35.59004  ?  2109 HOH   B O   1 
HETATM 28241 O  O   . HOH   N 6 .    ? 34.13100   26.68200  12.80400  1.000 49.53811  ?  2110 HOH   B O   1 
HETATM 28242 O  O   . HOH   N 6 .    ? 55.03800   67.23900  -29.64800 1.000 47.18366  ?  2111 HOH   B O   1 
HETATM 28243 O  O   . HOH   N 6 .    ? 89.10900   70.77100  4.67200   1.000 55.86172  ?  2112 HOH   B O   1 
HETATM 28244 O  O   . HOH   N 6 .    ? 19.48300   91.46100  -52.62300 1.000 43.92684  ?  2113 HOH   B O   1 
HETATM 28245 O  O   . HOH   N 6 .    ? 95.91100   69.36000  -21.99500 1.000 66.68309  ?  2114 HOH   B O   1 
HETATM 28246 O  O   . HOH   N 6 .    ? 70.39900   76.23300  -10.48300 1.000 33.82425  ?  2115 HOH   B O   1 
HETATM 28247 O  O   . HOH   N 6 .    ? 35.48100   103.04700 10.62300  1.000 67.05810  ?  2116 HOH   B O   1 
HETATM 28248 O  O   . HOH   N 6 .    ? 40.14400   76.80800  -32.32800 1.000 39.15873  ?  2117 HOH   B O   1 
HETATM 28249 O  O   . HOH   N 6 .    ? 93.88900   76.64400  8.60200   1.000 35.27718  ?  2118 HOH   B O   1 
HETATM 28250 O  O   . HOH   N 6 .    ? 12.02300   103.95000 -49.63800 1.000 55.35071  ?  2119 HOH   B O   1 
HETATM 28251 O  O   . HOH   N 6 .    ? 35.99500   82.57100  6.96300   1.000 52.69420  ?  2120 HOH   B O   1 
HETATM 28252 O  O   . HOH   N 6 .    ? 65.88000   76.70100  0.06600   1.000 36.38502  ?  2121 HOH   B O   1 
HETATM 28253 O  O   . HOH   N 6 .    ? 48.17300   69.85200  -13.56400 1.000 50.40513  ?  2122 HOH   B O   1 
HETATM 28254 O  O   . HOH   N 6 .    ? 52.36700   54.36300  3.21000   1.000 53.32499  ?  2123 HOH   B O   1 
HETATM 28255 O  O   . HOH   N 6 .    ? 85.54500   52.11600  7.81400   1.000 62.63911  ?  2124 HOH   B O   1 
HETATM 28256 O  O   . HOH   N 6 .    ? 90.72400   62.28300  -11.75500 1.000 60.74370  ?  2125 HOH   B O   1 
HETATM 28257 O  O   . HOH   N 6 .    ? 14.65200   78.41700  -43.36300 1.000 52.91776  ?  2126 HOH   B O   1 
HETATM 28258 O  O   . HOH   N 6 .    ? 34.66500   109.56600 -48.90100 1.000 58.32382  ?  2127 HOH   B O   1 
HETATM 28259 O  O   . HOH   N 6 .    ? 49.37400   66.23100  -4.01900  1.000 52.04299  ?  2128 HOH   B O   1 
HETATM 28260 O  O   . HOH   N 6 .    ? 50.69800   55.58600  4.61700   1.000 47.84772  ?  2129 HOH   B O   1 
HETATM 28261 O  O   . HOH   N 6 .    ? 83.51700   93.70500  24.15000  1.000 58.95079  ?  2130 HOH   B O   1 
HETATM 28262 O  O   . HOH   N 6 .    ? 56.88900   84.77000  1.94600   1.000 56.83337  ?  2131 HOH   B O   1 
HETATM 28263 O  O   . HOH   N 6 .    ? 42.76200   76.92400  -3.11200  1.000 57.25477  ?  2132 HOH   B O   1 
HETATM 28264 O  O   . HOH   N 6 .    ? 74.85900   87.80500  31.66100  1.000 61.43933  ?  2133 HOH   B O   1 
HETATM 28265 O  O   . HOH   N 6 .    ? 49.69600   107.47800 35.20300  1.000 49.67894  ?  2134 HOH   B O   1 
HETATM 28266 O  O   . HOH   N 6 .    ? 40.89500   98.74800  21.56100  1.000 46.00854  ?  2135 HOH   B O   1 
HETATM 28267 O  O   . HOH   N 6 .    ? 65.98400   55.32700  -15.26300 1.000 45.62025  ?  2136 HOH   B O   1 
HETATM 28268 O  O   . HOH   N 6 .    ? 55.92400   5.86100   1.84600   1.000 52.32436  ?  2137 HOH   B O   1 
HETATM 28269 O  O   . HOH   N 6 .    ? 19.48400   39.36100  10.83900  1.000 65.13972  ?  2138 HOH   B O   1 
HETATM 28270 O  O   . HOH   N 6 .    ? 41.75900   85.53800  -41.09900 1.000 45.73315  ?  2139 HOH   B O   1 
HETATM 28271 O  O   . HOH   N 6 .    ? 19.99100   90.19600  -57.06900 1.000 63.80142  ?  2140 HOH   B O   1 
HETATM 28272 O  O   . HOH   N 6 .    ? 62.59700   91.77000  2.18600   1.000 48.51601  ?  2141 HOH   B O   1 
HETATM 28273 O  O   . HOH   N 6 .    ? 38.81700   76.70800  -27.43500 1.000 40.66925  ?  2142 HOH   B O   1 
HETATM 28274 O  O   . HOH   N 6 .    ? 55.58100   103.54500 34.44400  1.000 52.01097  ?  2143 HOH   B O   1 
HETATM 28275 O  O   . HOH   N 6 .    ? 47.39600   76.39800  -6.01500  1.000 44.84711  ?  2144 HOH   B O   1 
HETATM 28276 O  O   . HOH   N 6 .    ? 21.16000   17.94100  22.90200  1.000 51.69600  ?  2145 HOH   B O   1 
HETATM 28277 O  O   . HOH   N 6 .    ? 36.35000   77.33600  8.12300   1.000 69.57211  ?  2146 HOH   B O   1 
HETATM 28278 O  O   . HOH   N 6 .    ? 47.74000   77.35600  25.89200  1.000 52.31472  ?  2147 HOH   B O   1 
HETATM 28279 O  O   . HOH   N 6 .    ? 34.10400   6.31100   -11.48400 1.000 73.21562  ?  2148 HOH   B O   1 
HETATM 28280 O  O   . HOH   N 6 .    ? 19.82700   80.14000  -38.54600 1.000 61.77486  ?  2149 HOH   B O   1 
HETATM 28281 O  O   . HOH   N 6 .    ? 45.92500   92.21300  -41.73100 1.000 45.59547  ?  2150 HOH   B O   1 
HETATM 28282 O  O   . HOH   N 6 .    ? 28.59600   119.13500 -44.47500 1.000 54.83053  ?  2151 HOH   B O   1 
HETATM 28283 O  O   . HOH   N 6 .    ? 10.344     87.900    -47.996   1.000 39.53951  ?  2152 HOH   B O   1 
HETATM 28284 O  O   . HOH   N 6 .    ? 27.49500   86.19500  -3.36700  1.000 51.88745  ?  2153 HOH   B O   1 
HETATM 28285 O  O   . HOH   N 6 .    ? 41.92000   94.09500  -20.24100 1.000 47.11457  ?  2154 HOH   B O   1 
HETATM 28286 O  O   . HOH   N 6 .    ? 24.77200   77.00600  -22.58600 1.000 44.01450  ?  2155 HOH   B O   1 
HETATM 28287 O  O   . HOH   N 6 .    ? 60.60300   38.07400  30.77500  1.000 71.12577  ?  2156 HOH   B O   1 
HETATM 28288 O  O   . HOH   N 6 .    ? 41.88700   66.68700  -1.21400  1.000 43.07887  ?  2157 HOH   B O   1 
HETATM 28289 O  O   . HOH   N 6 .    ? 13.38200   103.17400 -9.23200  1.000 57.46794  ?  2158 HOH   B O   1 
HETATM 28290 O  O   . HOH   N 6 .    ? 71.52700   65.81600  -37.72300 1.000 56.70594  ?  2159 HOH   B O   1 
HETATM 28291 O  O   . HOH   N 6 .    ? 66.57400   84.30100  -28.63200 1.000 44.51059  ?  2160 HOH   B O   1 
HETATM 28292 O  O   . HOH   N 6 .    ? 48.25400   89.86300  35.11600  1.000 34.81027  ?  2161 HOH   B O   1 
HETATM 28293 O  O   . HOH   N 6 .    ? 46.107     87.708    32.129    1.000 53.12572  ?  2162 HOH   B O   1 
HETATM 28294 O  O   . HOH   N 6 .    ? 38.93600   5.23400   3.08800   1.000 52.92090  ?  2163 HOH   B O   1 
HETATM 28295 O  O   . HOH   N 6 .    ? 83.85500   77.07000  -22.98300 1.000 45.92070  ?  2164 HOH   B O   1 
HETATM 28296 O  O   . HOH   N 6 .    ? 53.71200   89.07500  -11.02400 1.000 59.17408  ?  2165 HOH   B O   1 
HETATM 28297 O  O   . HOH   N 6 .    ? 54.65200   106.07100 -27.77100 1.000 56.58767  ?  2166 HOH   B O   1 
HETATM 28298 O  O   . HOH   N 6 .    ? 58.44100   105.52000 35.40800  1.000 57.96872  ?  2167 HOH   B O   1 
HETATM 28299 O  O   . HOH   N 6 .    ? 97.89100   84.16500  23.13400  1.000 78.30182  ?  2168 HOH   B O   1 
HETATM 28300 O  O   . HOH   N 6 .    ? 42.24600   91.64500  13.56400  1.000 41.04993  ?  2169 HOH   B O   1 
HETATM 28301 O  O   . HOH   N 6 .    ? 13.82300   10.29200  -7.62000  1.000 54.60639  ?  2170 HOH   B O   1 
HETATM 28302 O  O   . HOH   N 6 .    ? 61.89100   101.30000 33.34900  1.000 59.35067  ?  2171 HOH   B O   1 
HETATM 28303 O  O   . HOH   N 6 .    ? 12.72100   25.49600  16.35300  1.000 53.30942  ?  2172 HOH   B O   1 
HETATM 28304 O  O   . HOH   N 6 .    ? 41.36600   105.07500 23.33700  1.000 49.58212  ?  2173 HOH   B O   1 
HETATM 28305 O  O   . HOH   N 6 .    ? 20.04700   87.91700  -3.79600  1.000 46.03802  ?  2174 HOH   B O   1 
HETATM 28306 O  O   . HOH   N 6 .    ? 34.32200   14.22000  12.23900  1.000 37.65853  ?  2175 HOH   B O   1 
HETATM 28307 O  O   . HOH   N 6 .    ? 35.05200   46.25500  17.09300  1.000 66.79325  ?  2176 HOH   B O   1 
HETATM 28308 O  O   . HOH   N 6 .    ? 35.95300   96.95600  -8.05200  1.000 64.53008  ?  2177 HOH   B O   1 
HETATM 28309 O  O   . HOH   N 6 .    ? 64.60800   80.78300  10.79200  1.000 51.65698  ?  2178 HOH   B O   1 
HETATM 28310 O  O   . HOH   N 6 .    ? 34.91500   108.62100 -45.69800 1.000 50.14133  ?  2179 HOH   B O   1 
HETATM 28311 O  O   . HOH   N 6 .    ? 46.89500   80.43900  -32.43300 1.000 37.91933  ?  2180 HOH   B O   1 
HETATM 28312 O  O   . HOH   N 6 .    ? 40.77700   42.54800  -7.47500  1.000 59.15046  ?  2181 HOH   B O   1 
HETATM 28313 O  O   . HOH   N 6 .    ? 11.87900   86.77400  -5.48000  1.000 56.97329  ?  2182 HOH   B O   1 
HETATM 28314 O  O   . HOH   N 6 .    ? 22.31100   81.61300  -47.70700 1.000 48.57035  ?  2183 HOH   B O   1 
HETATM 28315 O  O   . HOH   N 6 .    ? 11.10100   30.98500  5.79100   1.000 53.79720  ?  2184 HOH   B O   1 
HETATM 28316 O  O   . HOH   N 6 .    ? 78.15400   60.24300  3.58800   1.000 34.00441  ?  2185 HOH   B O   1 
HETATM 28317 O  O   . HOH   N 6 .    ? 12.45400   113.55100 -38.12600 1.000 66.22616  ?  2186 HOH   B O   1 
HETATM 28318 O  O   . HOH   N 6 .    ? 16.01200   91.61000  -52.27000 1.000 54.39393  ?  2187 HOH   B O   1 
HETATM 28319 O  O   . HOH   N 6 .    ? 84.91300   50.54600  -33.14500 1.000 45.99206  ?  2188 HOH   B O   1 
HETATM 28320 O  O   . HOH   N 6 .    ? 74.64300   46.30600  9.43500   1.000 69.64337  ?  2189 HOH   B O   1 
HETATM 28321 O  O   . HOH   N 6 .    ? 39.01200   92.31900  -14.66500 1.000 32.54878  ?  2190 HOH   B O   1 
HETATM 28322 O  O   . HOH   N 6 .    ? 34.03500   106.59300 -21.06000 1.000 55.98963  ?  2191 HOH   B O   1 
HETATM 28323 O  O   . HOH   N 6 .    ? 56.11400   36.37400  37.40300  1.000 68.77503  ?  2192 HOH   B O   1 
HETATM 28324 O  O   . HOH   N 6 .    ? 56.11100   99.01900  39.31600  1.000 49.54286  ?  2193 HOH   B O   1 
HETATM 28325 O  O   . HOH   N 6 .    ? 6.06000    87.58200  -24.74600 1.000 44.63999  ?  2194 HOH   B O   1 
HETATM 28326 O  O   . HOH   N 6 .    ? 16.09600   29.72600  14.48600  1.000 54.10661  ?  2195 HOH   B O   1 
HETATM 28327 O  O   . HOH   N 6 .    ? 50.12900   70.73400  29.34000  1.000 39.06835  ?  2196 HOH   B O   1 
HETATM 28328 O  O   . HOH   N 6 .    ? 40.85600   40.01800  -6.17600  1.000 57.98962  ?  2197 HOH   B O   1 
HETATM 28329 O  O   . HOH   N 6 .    ? 11.01500   103.58300 -23.24000 1.000 79.68284  ?  2198 HOH   B O   1 
HETATM 28330 O  O   . HOH   N 6 .    ? 69.11800   76.70300  -22.25000 1.000 51.44832  ?  2199 HOH   B O   1 
HETATM 28331 O  O   . HOH   N 6 .    ? 42.82200   87.48000  -42.57900 1.000 55.12050  ?  2200 HOH   B O   1 
HETATM 28332 O  O   . HOH   N 6 .    ? 61.09000   77.08000  -5.09400  1.000 69.75775  ?  2201 HOH   B O   1 
HETATM 28333 O  O   . HOH   N 6 .    ? 40.07700   100.57900 -22.67300 1.000 43.72801  ?  2202 HOH   B O   1 
HETATM 28334 O  O   . HOH   N 6 .    ? 91.20900   85.47900  -12.09200 1.000 69.26830  ?  2203 HOH   B O   1 
HETATM 28335 O  O   . HOH   N 6 .    ? 45.91900   102.21700 -19.22800 1.000 62.82191  ?  2204 HOH   B O   1 
HETATM 28336 O  O   . HOH   N 6 .    ? 46.04500   84.14300  -36.28700 1.000 40.33517  ?  2205 HOH   B O   1 
HETATM 28337 O  O   . HOH   N 6 .    ? 52.81000   66.87900  -4.62300  1.000 65.30308  ?  2206 HOH   B O   1 
HETATM 28338 O  O   . HOH   N 6 .    ? 37.70100   37.90100  -7.57200  1.000 63.77060  ?  2207 HOH   B O   1 
HETATM 28339 O  O   . HOH   N 6 .    ? 55.30100   89.22200  -13.70800 1.000 41.52965  ?  2208 HOH   B O   1 
HETATM 28340 O  O   . HOH   N 6 .    ? 74.05900   96.37500  27.89800  1.000 49.89709  ?  2209 HOH   B O   1 
HETATM 28341 O  O   . HOH   N 6 .    ? 70.56300   88.09000  -7.95900  1.000 39.78590  ?  2210 HOH   B O   1 
HETATM 28342 O  O   . HOH   N 6 .    ? 45.09300   32.77300  10.83000  1.000 47.85415  ?  2211 HOH   B O   1 
HETATM 28343 O  O   . HOH   N 6 .    ? 32.38500   76.65400  -29.58000 1.000 36.85767  ?  2212 HOH   B O   1 
HETATM 28344 O  O   . HOH   N 6 .    ? 17.36600   100.77900 -58.74400 1.000 53.95680  ?  2213 HOH   B O   1 
HETATM 28345 O  O   . HOH   N 6 .    ? 37.38100   28.10100  27.81400  1.000 68.73837  ?  2214 HOH   B O   1 
HETATM 28346 O  O   . HOH   N 6 .    ? 68.75100   84.60200  -13.29100 1.000 41.26255  ?  2215 HOH   B O   1 
HETATM 28347 O  O   . HOH   N 6 .    ? 66.21700   82.45700  -11.03800 1.000 48.67499  ?  2216 HOH   B O   1 
HETATM 28348 O  O   . HOH   N 6 .    ? 11.934     -1.366    7.953     1.000 41.75307  ?  2217 HOH   B O   1 
HETATM 28349 O  O   . HOH   N 6 .    ? 43.21100   73.39700  -24.70300 1.000 41.87933  ?  2218 HOH   B O   1 
HETATM 28350 O  O   . HOH   N 6 .    ? 54.29100   49.24100  2.19900   1.000 46.72440  ?  2219 HOH   B O   1 
HETATM 28351 O  O   . HOH   N 6 .    ? 89.26500   64.19100  5.13500   1.000 51.66622  ?  2220 HOH   B O   1 
HETATM 28352 O  O   . HOH   N 6 .    ? 54.33000   52.63700  27.37200  1.000 60.83470  ?  2221 HOH   B O   1 
HETATM 28353 O  O   . HOH   N 6 .    ? 38.55800   75.01000  23.70200  1.000 51.67988  ?  2222 HOH   B O   1 
HETATM 28354 O  O   . HOH   N 6 .    ? 43.20200   83.34600  26.36100  1.000 46.41622  ?  2223 HOH   B O   1 
HETATM 28355 O  O   . HOH   N 6 .    ? 13.08200   75.76800  -43.08200 1.000 66.34512  ?  2224 HOH   B O   1 
# 
