data_9IP4
# 
_entry.id   9IP4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9IP4         pdb_00009ip4 10.2210/pdb9ip4/pdb 
WWPDB D_1300049251 ?            ?                   
EMDB  EMD-60757    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-09 ? 
2 'Structure model' 1 1 2025-04-16 ? 
# 
_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' 'Data collection'     
2 2 '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' em_admin 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.page_last'               
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
4 2 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IP4 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB  .                                                                                  9IP2      unspecified            
PDB  .                                                                                  9IP3      unspecified            
EMDB 'Cryo-EM structure of the RNA-dependent RNA polymerase complex from Marburg virus' EMD-60757 'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              hengru@zju.edu.cn 
_pdbx_contact_author.name_first         Heng 
_pdbx_contact_author.name_last          Ru 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7761-193X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, G.'   1 ? 
'Du, T.'   2 ? 
'Wang, J.' 3 ? 
'Wu, S.'   4 ? 
'Ru, H.'   5 ? 
# 
_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            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                3080 
_citation.page_last                 3080 
_citation.title                     
'Structural insights into the RNA-dependent RNA polymerase complexes from highly pathogenic Marburg and Ebola viruses.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-58308-1 
_citation.pdbx_database_id_PubMed   40164610 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Li, G.'    1 ? 
primary 'Du, T.'    2 ? 
primary 'Wang, J.'  3 ? 
primary 'Jie, K.'   4 ? 
primary 'Ren, Z.'   5 ? 
primary 'Zhang, X.' 6 ? 
primary 'Zhang, L.' 7 ? 
primary 'Wu, S.'    8 ? 
primary 'Ru, H.'    9 ? 
# 
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 'RNA-directed RNA polymerase L,Maltose/maltodextrin-binding periplasmic protein' 210152.953 1 
2.7.7.48,3.6.1.-,2.7.7.88,2.1.1.375 ? ? ? 
2 polymer     man 'Maltose/maltodextrin-binding periplasmic protein,Polymerase cofactor VP35'      73655.586  4 ? ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                       65.409     1 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Protein L,Large structural protein,Replicase,Transcriptase,MMBP,Maltodextrin-binding protein,Maltose-binding protein,MBP' 
2 'MMBP,Maltodextrin-binding protein,Maltose-binding protein,MBP,Marburg VP35,mVP35'                                         
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MQHPTQYPDARLSSPIILDQCDLLARSLGLYSHYSHNPKLRNCRIPHHIYRLRNSTALKTFLQNCSILTVPFHSIWDHIL
TSIQYDAINHVDDFKYLLPSELVKYANWDNEFLKAYLNKILGLDHVFSASARSQCEDFSPKENPYYWGMLLLVHLSQLAR
RIKGQRGSLRSNWKFIGTDLELFGIADFVIFKVPVKTIIRNAVSLQASKPGLRIWYRDQNLTPYLCDDEFIVSVASYECF
IMIKDVFIERYNTWEICARAWLEDSDGADYPPLDVLGELYNQGDQIIAMYLEDGFKLIKHLEPLCVSCIQTHGIFTPRKY
WFQSQMIKSYYDELHDLNLKLQISDNKAECAQNFIKTIVQAKLTPQQYCELFSLQKHWGHPVLYNDVALDKVKKHAQSTK
ILKPKVMFETFCVFKFIVAKNHYHSQGSWYKTTHDLHLTPYLRQHIVSNSFPSQAEIYQHLWEWYFVEHEPLFSTKIISD
LSIFIKDRATAVNQECWDSVFDRSVLGYNPPVRFQSKRVPEQFLGQADFSLNQILEFAEKLEYLAPSYRNFSFSLKEKEL
NIGRTFGKLPYRVRNVQTLAEALLADGLAKAFPSNMMVVTEREQKEALLHQASWHHNSASIGENAIVRGASFVTDLEKYN
LAFRYEFTRHFIDYCNRCYGVKNLFDWMHFLIPLCYMHVSDFYSPPHCVTEDNRNNPPDCANAYHYHLGGIEGLQQKLWT
CISCAQITLVELKTKLKLKSSVMGDNQCITTLSLFPIDAPNDYQENEAELNAARVAVELAITTGYSGIFLKPEETFVHSG
FIYFGKKQYLNGVQLPQSLKTMARCGPLSDSIFDDLQGSLASIGTSFERGTSETRHIFPSRWIASFHSMLAINLLNQNHL
GFPLGFNIDISCFKKPLTFSEKLIALITPQVLGGLSFLNPEKLFYRNISDPLTSGLFQLKNALEFLEKEELFYILISKKP
GLADASDFVMNPLGLNVPGSKEIITFLRQTVRENITITSQNRIINSLFHIGSDLEDQRVCEWLLSSNPVMSRFAADIFSR
TPSGKRLQVLGYLEGTRTLLASRTISLTTEGTMLMKLRELTRNRWKSWFSYIDALDDDLSESLEKFTCTVDVANFLRAYS
WSDVLKGKRLIGATLPCLLEQFEVKWINLSEDLREQFNLSSDSKSTINLLPYDCKELRLEGSNDTELNYVSCALDRKVVQ
KHPSVNRLAWTIGNRAPYIGSRTEDKIGYPPLRVNCPSAALKEAIEMVSRLLWVTQGTADREKLLIPLLNSRVNLDYQTV
LNFLPTHYSGNIVHRYNDQYGQHSFMANRMSNTSTRAIISTNTLGKYAGGGQAAIDSNIIFQNTINLGVAVLDIALSLAK
LSSASNVTFRLMLNKCCTRHVPSEYLYFDKPLDVDLNKYMDNELVYDNDPLCSGIKGRLGRVSRSSRENLYFQGSGWSHP
QFEKGGGSGGGSGGSAWSHPQFEKGSASHHHHHHGTKTEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLE
EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPN
PPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHM
NADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYL
LTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDA
QTGDYKDDDDK
;
;MQHPTQYPDARLSSPIILDQCDLLARSLGLYSHYSHNPKLRNCRIPHHIYRLRNSTALKTFLQNCSILTVPFHSIWDHIL
TSIQYDAINHVDDFKYLLPSELVKYANWDNEFLKAYLNKILGLDHVFSASARSQCEDFSPKENPYYWGMLLLVHLSQLAR
RIKGQRGSLRSNWKFIGTDLELFGIADFVIFKVPVKTIIRNAVSLQASKPGLRIWYRDQNLTPYLCDDEFIVSVASYECF
IMIKDVFIERYNTWEICARAWLEDSDGADYPPLDVLGELYNQGDQIIAMYLEDGFKLIKHLEPLCVSCIQTHGIFTPRKY
WFQSQMIKSYYDELHDLNLKLQISDNKAECAQNFIKTIVQAKLTPQQYCELFSLQKHWGHPVLYNDVALDKVKKHAQSTK
ILKPKVMFETFCVFKFIVAKNHYHSQGSWYKTTHDLHLTPYLRQHIVSNSFPSQAEIYQHLWEWYFVEHEPLFSTKIISD
LSIFIKDRATAVNQECWDSVFDRSVLGYNPPVRFQSKRVPEQFLGQADFSLNQILEFAEKLEYLAPSYRNFSFSLKEKEL
NIGRTFGKLPYRVRNVQTLAEALLADGLAKAFPSNMMVVTEREQKEALLHQASWHHNSASIGENAIVRGASFVTDLEKYN
LAFRYEFTRHFIDYCNRCYGVKNLFDWMHFLIPLCYMHVSDFYSPPHCVTEDNRNNPPDCANAYHYHLGGIEGLQQKLWT
CISCAQITLVELKTKLKLKSSVMGDNQCITTLSLFPIDAPNDYQENEAELNAARVAVELAITTGYSGIFLKPEETFVHSG
FIYFGKKQYLNGVQLPQSLKTMARCGPLSDSIFDDLQGSLASIGTSFERGTSETRHIFPSRWIASFHSMLAINLLNQNHL
GFPLGFNIDISCFKKPLTFSEKLIALITPQVLGGLSFLNPEKLFYRNISDPLTSGLFQLKNALEFLEKEELFYILISKKP
GLADASDFVMNPLGLNVPGSKEIITFLRQTVRENITITSQNRIINSLFHIGSDLEDQRVCEWLLSSNPVMSRFAADIFSR
TPSGKRLQVLGYLEGTRTLLASRTISLTTEGTMLMKLRELTRNRWKSWFSYIDALDDDLSESLEKFTCTVDVANFLRAYS
WSDVLKGKRLIGATLPCLLEQFEVKWINLSEDLREQFNLSSDSKSTINLLPYDCKELRLEGSNDTELNYVSCALDRKVVQ
KHPSVNRLAWTIGNRAPYIGSRTEDKIGYPPLRVNCPSAALKEAIEMVSRLLWVTQGTADREKLLIPLLNSRVNLDYQTV
LNFLPTHYSGNIVHRYNDQYGQHSFMANRMSNTSTRAIISTNTLGKYAGGGQAAIDSNIIFQNTINLGVAVLDIALSLAK
LSSASNVTFRLMLNKCCTRHVPSEYLYFDKPLDVDLNKYMDNELVYDNDPLCSGIKGRLGRVSRSSRENLYFQGSGWSHP
QFEKGGGSGGGSGGSAWSHPQFEKGSASHHHHHHGTKTEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLE
EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPN
PPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHM
NADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYL
LTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDA
QTGDYKDDDDK
;
A       ? 
2 'polypeptide(L)' no no 
;MGSSHHHHHHGTKTEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFG
GYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALM
FNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTING
PWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYE
EELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTGTDYDIPTTLEVLFQGPLGSST
DDIIWDQLIVKRTLADLLIPINRQISDIQSTLSEVTTRVHEIERQLHEITPVLKMGRTLEAISKGMSEMLAKYDHLVIST
GRTTAPAAAFDAYLNEHGVPPPQPAIFKDLGVAQQACSKGTMVKNATTDAADKMSKVLELSEETFSKPNLSAKDLALLLF
THLPGNNTPFHILAQVLSKIAYKSGKSGAFLDAFHQILSEGENAQAALTRLSRTFDAFLGVVPPVIRVKNFQTVPRPCQK
SLRAVPPNPTIDKGWVCVYSSEQGETRALKI
;
;MGSSHHHHHHGTKTEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFG
GYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALM
FNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTING
PWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYE
EELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTGTDYDIPTTLEVLFQGPLGSST
DDIIWDQLIVKRTLADLLIPINRQISDIQSTLSEVTTRVHEIERQLHEITPVLKMGRTLEAISKGMSEMLAKYDHLVIST
GRTTAPAAAFDAYLNEHGVPPPQPAIFKDLGVAQQACSKGTMVKNATTDAADKMSKVLELSEETFSKPNLSAKDLALLLF
THLPGNNTPFHILAQVLSKIAYKSGKSGAFLDAFHQILSEGENAQAALTRLSRTFDAFLGVVPPVIRVKNFQTVPRPCQK
SLRAVPPNPTIDKGWVCVYSSEQGETRALKI
;
B,C,D,E ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        'ZINC ION' 
_pdbx_entity_nonpoly.comp_id     ZN 
# 
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    GLN n 
1 3    HIS n 
1 4    PRO n 
1 5    THR n 
1 6    GLN n 
1 7    TYR n 
1 8    PRO n 
1 9    ASP n 
1 10   ALA n 
1 11   ARG n 
1 12   LEU n 
1 13   SER n 
1 14   SER n 
1 15   PRO n 
1 16   ILE n 
1 17   ILE n 
1 18   LEU n 
1 19   ASP n 
1 20   GLN n 
1 21   CYS n 
1 22   ASP n 
1 23   LEU n 
1 24   LEU n 
1 25   ALA n 
1 26   ARG n 
1 27   SER n 
1 28   LEU n 
1 29   GLY n 
1 30   LEU n 
1 31   TYR n 
1 32   SER n 
1 33   HIS n 
1 34   TYR n 
1 35   SER n 
1 36   HIS n 
1 37   ASN n 
1 38   PRO n 
1 39   LYS n 
1 40   LEU n 
1 41   ARG n 
1 42   ASN n 
1 43   CYS n 
1 44   ARG n 
1 45   ILE n 
1 46   PRO n 
1 47   HIS n 
1 48   HIS n 
1 49   ILE n 
1 50   TYR n 
1 51   ARG n 
1 52   LEU n 
1 53   ARG n 
1 54   ASN n 
1 55   SER n 
1 56   THR n 
1 57   ALA n 
1 58   LEU n 
1 59   LYS n 
1 60   THR n 
1 61   PHE n 
1 62   LEU n 
1 63   GLN n 
1 64   ASN n 
1 65   CYS n 
1 66   SER n 
1 67   ILE n 
1 68   LEU n 
1 69   THR n 
1 70   VAL n 
1 71   PRO n 
1 72   PHE n 
1 73   HIS n 
1 74   SER n 
1 75   ILE n 
1 76   TRP n 
1 77   ASP n 
1 78   HIS n 
1 79   ILE n 
1 80   LEU n 
1 81   THR n 
1 82   SER n 
1 83   ILE n 
1 84   GLN n 
1 85   TYR n 
1 86   ASP n 
1 87   ALA n 
1 88   ILE n 
1 89   ASN n 
1 90   HIS n 
1 91   VAL n 
1 92   ASP n 
1 93   ASP n 
1 94   PHE n 
1 95   LYS n 
1 96   TYR n 
1 97   LEU n 
1 98   LEU n 
1 99   PRO n 
1 100  SER n 
1 101  GLU n 
1 102  LEU n 
1 103  VAL n 
1 104  LYS n 
1 105  TYR n 
1 106  ALA n 
1 107  ASN n 
1 108  TRP n 
1 109  ASP n 
1 110  ASN n 
1 111  GLU n 
1 112  PHE n 
1 113  LEU n 
1 114  LYS n 
1 115  ALA n 
1 116  TYR n 
1 117  LEU n 
1 118  ASN n 
1 119  LYS n 
1 120  ILE n 
1 121  LEU n 
1 122  GLY n 
1 123  LEU n 
1 124  ASP n 
1 125  HIS n 
1 126  VAL n 
1 127  PHE n 
1 128  SER n 
1 129  ALA n 
1 130  SER n 
1 131  ALA n 
1 132  ARG n 
1 133  SER n 
1 134  GLN n 
1 135  CYS n 
1 136  GLU n 
1 137  ASP n 
1 138  PHE n 
1 139  SER n 
1 140  PRO n 
1 141  LYS n 
1 142  GLU n 
1 143  ASN n 
1 144  PRO n 
1 145  TYR n 
1 146  TYR n 
1 147  TRP n 
1 148  GLY n 
1 149  MET n 
1 150  LEU n 
1 151  LEU n 
1 152  LEU n 
1 153  VAL n 
1 154  HIS n 
1 155  LEU n 
1 156  SER n 
1 157  GLN n 
1 158  LEU n 
1 159  ALA n 
1 160  ARG n 
1 161  ARG n 
1 162  ILE n 
1 163  LYS n 
1 164  GLY n 
1 165  GLN n 
1 166  ARG n 
1 167  GLY n 
1 168  SER n 
1 169  LEU n 
1 170  ARG n 
1 171  SER n 
1 172  ASN n 
1 173  TRP n 
1 174  LYS n 
1 175  PHE n 
1 176  ILE n 
1 177  GLY n 
1 178  THR n 
1 179  ASP n 
1 180  LEU n 
1 181  GLU n 
1 182  LEU n 
1 183  PHE n 
1 184  GLY n 
1 185  ILE n 
1 186  ALA n 
1 187  ASP n 
1 188  PHE n 
1 189  VAL n 
1 190  ILE n 
1 191  PHE n 
1 192  LYS n 
1 193  VAL n 
1 194  PRO n 
1 195  VAL n 
1 196  LYS n 
1 197  THR n 
1 198  ILE n 
1 199  ILE n 
1 200  ARG n 
1 201  ASN n 
1 202  ALA n 
1 203  VAL n 
1 204  SER n 
1 205  LEU n 
1 206  GLN n 
1 207  ALA n 
1 208  SER n 
1 209  LYS n 
1 210  PRO n 
1 211  GLY n 
1 212  LEU n 
1 213  ARG n 
1 214  ILE n 
1 215  TRP n 
1 216  TYR n 
1 217  ARG n 
1 218  ASP n 
1 219  GLN n 
1 220  ASN n 
1 221  LEU n 
1 222  THR n 
1 223  PRO n 
1 224  TYR n 
1 225  LEU n 
1 226  CYS n 
1 227  ASP n 
1 228  ASP n 
1 229  GLU n 
1 230  PHE n 
1 231  ILE n 
1 232  VAL n 
1 233  SER n 
1 234  VAL n 
1 235  ALA n 
1 236  SER n 
1 237  TYR n 
1 238  GLU n 
1 239  CYS n 
1 240  PHE n 
1 241  ILE n 
1 242  MET n 
1 243  ILE n 
1 244  LYS n 
1 245  ASP n 
1 246  VAL n 
1 247  PHE n 
1 248  ILE n 
1 249  GLU n 
1 250  ARG n 
1 251  TYR n 
1 252  ASN n 
1 253  THR n 
1 254  TRP n 
1 255  GLU n 
1 256  ILE n 
1 257  CYS n 
1 258  ALA n 
1 259  ARG n 
1 260  ALA n 
1 261  TRP n 
1 262  LEU n 
1 263  GLU n 
1 264  ASP n 
1 265  SER n 
1 266  ASP n 
1 267  GLY n 
1 268  ALA n 
1 269  ASP n 
1 270  TYR n 
1 271  PRO n 
1 272  PRO n 
1 273  LEU n 
1 274  ASP n 
1 275  VAL n 
1 276  LEU n 
1 277  GLY n 
1 278  GLU n 
1 279  LEU n 
1 280  TYR n 
1 281  ASN n 
1 282  GLN n 
1 283  GLY n 
1 284  ASP n 
1 285  GLN n 
1 286  ILE n 
1 287  ILE n 
1 288  ALA n 
1 289  MET n 
1 290  TYR n 
1 291  LEU n 
1 292  GLU n 
1 293  ASP n 
1 294  GLY n 
1 295  PHE n 
1 296  LYS n 
1 297  LEU n 
1 298  ILE n 
1 299  LYS n 
1 300  HIS n 
1 301  LEU n 
1 302  GLU n 
1 303  PRO n 
1 304  LEU n 
1 305  CYS n 
1 306  VAL n 
1 307  SER n 
1 308  CYS n 
1 309  ILE n 
1 310  GLN n 
1 311  THR n 
1 312  HIS n 
1 313  GLY n 
1 314  ILE n 
1 315  PHE n 
1 316  THR n 
1 317  PRO n 
1 318  ARG n 
1 319  LYS n 
1 320  TYR n 
1 321  TRP n 
1 322  PHE n 
1 323  GLN n 
1 324  SER n 
1 325  GLN n 
1 326  MET n 
1 327  ILE n 
1 328  LYS n 
1 329  SER n 
1 330  TYR n 
1 331  TYR n 
1 332  ASP n 
1 333  GLU n 
1 334  LEU n 
1 335  HIS n 
1 336  ASP n 
1 337  LEU n 
1 338  ASN n 
1 339  LEU n 
1 340  LYS n 
1 341  LEU n 
1 342  GLN n 
1 343  ILE n 
1 344  SER n 
1 345  ASP n 
1 346  ASN n 
1 347  LYS n 
1 348  ALA n 
1 349  GLU n 
1 350  CYS n 
1 351  ALA n 
1 352  GLN n 
1 353  ASN n 
1 354  PHE n 
1 355  ILE n 
1 356  LYS n 
1 357  THR n 
1 358  ILE n 
1 359  VAL n 
1 360  GLN n 
1 361  ALA n 
1 362  LYS n 
1 363  LEU n 
1 364  THR n 
1 365  PRO n 
1 366  GLN n 
1 367  GLN n 
1 368  TYR n 
1 369  CYS n 
1 370  GLU n 
1 371  LEU n 
1 372  PHE n 
1 373  SER n 
1 374  LEU n 
1 375  GLN n 
1 376  LYS n 
1 377  HIS n 
1 378  TRP n 
1 379  GLY n 
1 380  HIS n 
1 381  PRO n 
1 382  VAL n 
1 383  LEU n 
1 384  TYR n 
1 385  ASN n 
1 386  ASP n 
1 387  VAL n 
1 388  ALA n 
1 389  LEU n 
1 390  ASP n 
1 391  LYS n 
1 392  VAL n 
1 393  LYS n 
1 394  LYS n 
1 395  HIS n 
1 396  ALA n 
1 397  GLN n 
1 398  SER n 
1 399  THR n 
1 400  LYS n 
1 401  ILE n 
1 402  LEU n 
1 403  LYS n 
1 404  PRO n 
1 405  LYS n 
1 406  VAL n 
1 407  MET n 
1 408  PHE n 
1 409  GLU n 
1 410  THR n 
1 411  PHE n 
1 412  CYS n 
1 413  VAL n 
1 414  PHE n 
1 415  LYS n 
1 416  PHE n 
1 417  ILE n 
1 418  VAL n 
1 419  ALA n 
1 420  LYS n 
1 421  ASN n 
1 422  HIS n 
1 423  TYR n 
1 424  HIS n 
1 425  SER n 
1 426  GLN n 
1 427  GLY n 
1 428  SER n 
1 429  TRP n 
1 430  TYR n 
1 431  LYS n 
1 432  THR n 
1 433  THR n 
1 434  HIS n 
1 435  ASP n 
1 436  LEU n 
1 437  HIS n 
1 438  LEU n 
1 439  THR n 
1 440  PRO n 
1 441  TYR n 
1 442  LEU n 
1 443  ARG n 
1 444  GLN n 
1 445  HIS n 
1 446  ILE n 
1 447  VAL n 
1 448  SER n 
1 449  ASN n 
1 450  SER n 
1 451  PHE n 
1 452  PRO n 
1 453  SER n 
1 454  GLN n 
1 455  ALA n 
1 456  GLU n 
1 457  ILE n 
1 458  TYR n 
1 459  GLN n 
1 460  HIS n 
1 461  LEU n 
1 462  TRP n 
1 463  GLU n 
1 464  TRP n 
1 465  TYR n 
1 466  PHE n 
1 467  VAL n 
1 468  GLU n 
1 469  HIS n 
1 470  GLU n 
1 471  PRO n 
1 472  LEU n 
1 473  PHE n 
1 474  SER n 
1 475  THR n 
1 476  LYS n 
1 477  ILE n 
1 478  ILE n 
1 479  SER n 
1 480  ASP n 
1 481  LEU n 
1 482  SER n 
1 483  ILE n 
1 484  PHE n 
1 485  ILE n 
1 486  LYS n 
1 487  ASP n 
1 488  ARG n 
1 489  ALA n 
1 490  THR n 
1 491  ALA n 
1 492  VAL n 
1 493  ASN n 
1 494  GLN n 
1 495  GLU n 
1 496  CYS n 
1 497  TRP n 
1 498  ASP n 
1 499  SER n 
1 500  VAL n 
1 501  PHE n 
1 502  ASP n 
1 503  ARG n 
1 504  SER n 
1 505  VAL n 
1 506  LEU n 
1 507  GLY n 
1 508  TYR n 
1 509  ASN n 
1 510  PRO n 
1 511  PRO n 
1 512  VAL n 
1 513  ARG n 
1 514  PHE n 
1 515  GLN n 
1 516  SER n 
1 517  LYS n 
1 518  ARG n 
1 519  VAL n 
1 520  PRO n 
1 521  GLU n 
1 522  GLN n 
1 523  PHE n 
1 524  LEU n 
1 525  GLY n 
1 526  GLN n 
1 527  ALA n 
1 528  ASP n 
1 529  PHE n 
1 530  SER n 
1 531  LEU n 
1 532  ASN n 
1 533  GLN n 
1 534  ILE n 
1 535  LEU n 
1 536  GLU n 
1 537  PHE n 
1 538  ALA n 
1 539  GLU n 
1 540  LYS n 
1 541  LEU n 
1 542  GLU n 
1 543  TYR n 
1 544  LEU n 
1 545  ALA n 
1 546  PRO n 
1 547  SER n 
1 548  TYR n 
1 549  ARG n 
1 550  ASN n 
1 551  PHE n 
1 552  SER n 
1 553  PHE n 
1 554  SER n 
1 555  LEU n 
1 556  LYS n 
1 557  GLU n 
1 558  LYS n 
1 559  GLU n 
1 560  LEU n 
1 561  ASN n 
1 562  ILE n 
1 563  GLY n 
1 564  ARG n 
1 565  THR n 
1 566  PHE n 
1 567  GLY n 
1 568  LYS n 
1 569  LEU n 
1 570  PRO n 
1 571  TYR n 
1 572  ARG n 
1 573  VAL n 
1 574  ARG n 
1 575  ASN n 
1 576  VAL n 
1 577  GLN n 
1 578  THR n 
1 579  LEU n 
1 580  ALA n 
1 581  GLU n 
1 582  ALA n 
1 583  LEU n 
1 584  LEU n 
1 585  ALA n 
1 586  ASP n 
1 587  GLY n 
1 588  LEU n 
1 589  ALA n 
1 590  LYS n 
1 591  ALA n 
1 592  PHE n 
1 593  PRO n 
1 594  SER n 
1 595  ASN n 
1 596  MET n 
1 597  MET n 
1 598  VAL n 
1 599  VAL n 
1 600  THR n 
1 601  GLU n 
1 602  ARG n 
1 603  GLU n 
1 604  GLN n 
1 605  LYS n 
1 606  GLU n 
1 607  ALA n 
1 608  LEU n 
1 609  LEU n 
1 610  HIS n 
1 611  GLN n 
1 612  ALA n 
1 613  SER n 
1 614  TRP n 
1 615  HIS n 
1 616  HIS n 
1 617  ASN n 
1 618  SER n 
1 619  ALA n 
1 620  SER n 
1 621  ILE n 
1 622  GLY n 
1 623  GLU n 
1 624  ASN n 
1 625  ALA n 
1 626  ILE n 
1 627  VAL n 
1 628  ARG n 
1 629  GLY n 
1 630  ALA n 
1 631  SER n 
1 632  PHE n 
1 633  VAL n 
1 634  THR n 
1 635  ASP n 
1 636  LEU n 
1 637  GLU n 
1 638  LYS n 
1 639  TYR n 
1 640  ASN n 
1 641  LEU n 
1 642  ALA n 
1 643  PHE n 
1 644  ARG n 
1 645  TYR n 
1 646  GLU n 
1 647  PHE n 
1 648  THR n 
1 649  ARG n 
1 650  HIS n 
1 651  PHE n 
1 652  ILE n 
1 653  ASP n 
1 654  TYR n 
1 655  CYS n 
1 656  ASN n 
1 657  ARG n 
1 658  CYS n 
1 659  TYR n 
1 660  GLY n 
1 661  VAL n 
1 662  LYS n 
1 663  ASN n 
1 664  LEU n 
1 665  PHE n 
1 666  ASP n 
1 667  TRP n 
1 668  MET n 
1 669  HIS n 
1 670  PHE n 
1 671  LEU n 
1 672  ILE n 
1 673  PRO n 
1 674  LEU n 
1 675  CYS n 
1 676  TYR n 
1 677  MET n 
1 678  HIS n 
1 679  VAL n 
1 680  SER n 
1 681  ASP n 
1 682  PHE n 
1 683  TYR n 
1 684  SER n 
1 685  PRO n 
1 686  PRO n 
1 687  HIS n 
1 688  CYS n 
1 689  VAL n 
1 690  THR n 
1 691  GLU n 
1 692  ASP n 
1 693  ASN n 
1 694  ARG n 
1 695  ASN n 
1 696  ASN n 
1 697  PRO n 
1 698  PRO n 
1 699  ASP n 
1 700  CYS n 
1 701  ALA n 
1 702  ASN n 
1 703  ALA n 
1 704  TYR n 
1 705  HIS n 
1 706  TYR n 
1 707  HIS n 
1 708  LEU n 
1 709  GLY n 
1 710  GLY n 
1 711  ILE n 
1 712  GLU n 
1 713  GLY n 
1 714  LEU n 
1 715  GLN n 
1 716  GLN n 
1 717  LYS n 
1 718  LEU n 
1 719  TRP n 
1 720  THR n 
1 721  CYS n 
1 722  ILE n 
1 723  SER n 
1 724  CYS n 
1 725  ALA n 
1 726  GLN n 
1 727  ILE n 
1 728  THR n 
1 729  LEU n 
1 730  VAL n 
1 731  GLU n 
1 732  LEU n 
1 733  LYS n 
1 734  THR n 
1 735  LYS n 
1 736  LEU n 
1 737  LYS n 
1 738  LEU n 
1 739  LYS n 
1 740  SER n 
1 741  SER n 
1 742  VAL n 
1 743  MET n 
1 744  GLY n 
1 745  ASP n 
1 746  ASN n 
1 747  GLN n 
1 748  CYS n 
1 749  ILE n 
1 750  THR n 
1 751  THR n 
1 752  LEU n 
1 753  SER n 
1 754  LEU n 
1 755  PHE n 
1 756  PRO n 
1 757  ILE n 
1 758  ASP n 
1 759  ALA n 
1 760  PRO n 
1 761  ASN n 
1 762  ASP n 
1 763  TYR n 
1 764  GLN n 
1 765  GLU n 
1 766  ASN n 
1 767  GLU n 
1 768  ALA n 
1 769  GLU n 
1 770  LEU n 
1 771  ASN n 
1 772  ALA n 
1 773  ALA n 
1 774  ARG n 
1 775  VAL n 
1 776  ALA n 
1 777  VAL n 
1 778  GLU n 
1 779  LEU n 
1 780  ALA n 
1 781  ILE n 
1 782  THR n 
1 783  THR n 
1 784  GLY n 
1 785  TYR n 
1 786  SER n 
1 787  GLY n 
1 788  ILE n 
1 789  PHE n 
1 790  LEU n 
1 791  LYS n 
1 792  PRO n 
1 793  GLU n 
1 794  GLU n 
1 795  THR n 
1 796  PHE n 
1 797  VAL n 
1 798  HIS n 
1 799  SER n 
1 800  GLY n 
1 801  PHE n 
1 802  ILE n 
1 803  TYR n 
1 804  PHE n 
1 805  GLY n 
1 806  LYS n 
1 807  LYS n 
1 808  GLN n 
1 809  TYR n 
1 810  LEU n 
1 811  ASN n 
1 812  GLY n 
1 813  VAL n 
1 814  GLN n 
1 815  LEU n 
1 816  PRO n 
1 817  GLN n 
1 818  SER n 
1 819  LEU n 
1 820  LYS n 
1 821  THR n 
1 822  MET n 
1 823  ALA n 
1 824  ARG n 
1 825  CYS n 
1 826  GLY n 
1 827  PRO n 
1 828  LEU n 
1 829  SER n 
1 830  ASP n 
1 831  SER n 
1 832  ILE n 
1 833  PHE n 
1 834  ASP n 
1 835  ASP n 
1 836  LEU n 
1 837  GLN n 
1 838  GLY n 
1 839  SER n 
1 840  LEU n 
1 841  ALA n 
1 842  SER n 
1 843  ILE n 
1 844  GLY n 
1 845  THR n 
1 846  SER n 
1 847  PHE n 
1 848  GLU n 
1 849  ARG n 
1 850  GLY n 
1 851  THR n 
1 852  SER n 
1 853  GLU n 
1 854  THR n 
1 855  ARG n 
1 856  HIS n 
1 857  ILE n 
1 858  PHE n 
1 859  PRO n 
1 860  SER n 
1 861  ARG n 
1 862  TRP n 
1 863  ILE n 
1 864  ALA n 
1 865  SER n 
1 866  PHE n 
1 867  HIS n 
1 868  SER n 
1 869  MET n 
1 870  LEU n 
1 871  ALA n 
1 872  ILE n 
1 873  ASN n 
1 874  LEU n 
1 875  LEU n 
1 876  ASN n 
1 877  GLN n 
1 878  ASN n 
1 879  HIS n 
1 880  LEU n 
1 881  GLY n 
1 882  PHE n 
1 883  PRO n 
1 884  LEU n 
1 885  GLY n 
1 886  PHE n 
1 887  ASN n 
1 888  ILE n 
1 889  ASP n 
1 890  ILE n 
1 891  SER n 
1 892  CYS n 
1 893  PHE n 
1 894  LYS n 
1 895  LYS n 
1 896  PRO n 
1 897  LEU n 
1 898  THR n 
1 899  PHE n 
1 900  SER n 
1 901  GLU n 
1 902  LYS n 
1 903  LEU n 
1 904  ILE n 
1 905  ALA n 
1 906  LEU n 
1 907  ILE n 
1 908  THR n 
1 909  PRO n 
1 910  GLN n 
1 911  VAL n 
1 912  LEU n 
1 913  GLY n 
1 914  GLY n 
1 915  LEU n 
1 916  SER n 
1 917  PHE n 
1 918  LEU n 
1 919  ASN n 
1 920  PRO n 
1 921  GLU n 
1 922  LYS n 
1 923  LEU n 
1 924  PHE n 
1 925  TYR n 
1 926  ARG n 
1 927  ASN n 
1 928  ILE n 
1 929  SER n 
1 930  ASP n 
1 931  PRO n 
1 932  LEU n 
1 933  THR n 
1 934  SER n 
1 935  GLY n 
1 936  LEU n 
1 937  PHE n 
1 938  GLN n 
1 939  LEU n 
1 940  LYS n 
1 941  ASN n 
1 942  ALA n 
1 943  LEU n 
1 944  GLU n 
1 945  PHE n 
1 946  LEU n 
1 947  GLU n 
1 948  LYS n 
1 949  GLU n 
1 950  GLU n 
1 951  LEU n 
1 952  PHE n 
1 953  TYR n 
1 954  ILE n 
1 955  LEU n 
1 956  ILE n 
1 957  SER n 
1 958  LYS n 
1 959  LYS n 
1 960  PRO n 
1 961  GLY n 
1 962  LEU n 
1 963  ALA n 
1 964  ASP n 
1 965  ALA n 
1 966  SER n 
1 967  ASP n 
1 968  PHE n 
1 969  VAL n 
1 970  MET n 
1 971  ASN n 
1 972  PRO n 
1 973  LEU n 
1 974  GLY n 
1 975  LEU n 
1 976  ASN n 
1 977  VAL n 
1 978  PRO n 
1 979  GLY n 
1 980  SER n 
1 981  LYS n 
1 982  GLU n 
1 983  ILE n 
1 984  ILE n 
1 985  THR n 
1 986  PHE n 
1 987  LEU n 
1 988  ARG n 
1 989  GLN n 
1 990  THR n 
1 991  VAL n 
1 992  ARG n 
1 993  GLU n 
1 994  ASN n 
1 995  ILE n 
1 996  THR n 
1 997  ILE n 
1 998  THR n 
1 999  SER n 
1 1000 GLN n 
1 1001 ASN n 
1 1002 ARG n 
1 1003 ILE n 
1 1004 ILE n 
1 1005 ASN n 
1 1006 SER n 
1 1007 LEU n 
1 1008 PHE n 
1 1009 HIS n 
1 1010 ILE n 
1 1011 GLY n 
1 1012 SER n 
1 1013 ASP n 
1 1014 LEU n 
1 1015 GLU n 
1 1016 ASP n 
1 1017 GLN n 
1 1018 ARG n 
1 1019 VAL n 
1 1020 CYS n 
1 1021 GLU n 
1 1022 TRP n 
1 1023 LEU n 
1 1024 LEU n 
1 1025 SER n 
1 1026 SER n 
1 1027 ASN n 
1 1028 PRO n 
1 1029 VAL n 
1 1030 MET n 
1 1031 SER n 
1 1032 ARG n 
1 1033 PHE n 
1 1034 ALA n 
1 1035 ALA n 
1 1036 ASP n 
1 1037 ILE n 
1 1038 PHE n 
1 1039 SER n 
1 1040 ARG n 
1 1041 THR n 
1 1042 PRO n 
1 1043 SER n 
1 1044 GLY n 
1 1045 LYS n 
1 1046 ARG n 
1 1047 LEU n 
1 1048 GLN n 
1 1049 VAL n 
1 1050 LEU n 
1 1051 GLY n 
1 1052 TYR n 
1 1053 LEU n 
1 1054 GLU n 
1 1055 GLY n 
1 1056 THR n 
1 1057 ARG n 
1 1058 THR n 
1 1059 LEU n 
1 1060 LEU n 
1 1061 ALA n 
1 1062 SER n 
1 1063 ARG n 
1 1064 THR n 
1 1065 ILE n 
1 1066 SER n 
1 1067 LEU n 
1 1068 THR n 
1 1069 THR n 
1 1070 GLU n 
1 1071 GLY n 
1 1072 THR n 
1 1073 MET n 
1 1074 LEU n 
1 1075 MET n 
1 1076 LYS n 
1 1077 LEU n 
1 1078 ARG n 
1 1079 GLU n 
1 1080 LEU n 
1 1081 THR n 
1 1082 ARG n 
1 1083 ASN n 
1 1084 ARG n 
1 1085 TRP n 
1 1086 LYS n 
1 1087 SER n 
1 1088 TRP n 
1 1089 PHE n 
1 1090 SER n 
1 1091 TYR n 
1 1092 ILE n 
1 1093 ASP n 
1 1094 ALA n 
1 1095 LEU n 
1 1096 ASP n 
1 1097 ASP n 
1 1098 ASP n 
1 1099 LEU n 
1 1100 SER n 
1 1101 GLU n 
1 1102 SER n 
1 1103 LEU n 
1 1104 GLU n 
1 1105 LYS n 
1 1106 PHE n 
1 1107 THR n 
1 1108 CYS n 
1 1109 THR n 
1 1110 VAL n 
1 1111 ASP n 
1 1112 VAL n 
1 1113 ALA n 
1 1114 ASN n 
1 1115 PHE n 
1 1116 LEU n 
1 1117 ARG n 
1 1118 ALA n 
1 1119 TYR n 
1 1120 SER n 
1 1121 TRP n 
1 1122 SER n 
1 1123 ASP n 
1 1124 VAL n 
1 1125 LEU n 
1 1126 LYS n 
1 1127 GLY n 
1 1128 LYS n 
1 1129 ARG n 
1 1130 LEU n 
1 1131 ILE n 
1 1132 GLY n 
1 1133 ALA n 
1 1134 THR n 
1 1135 LEU n 
1 1136 PRO n 
1 1137 CYS n 
1 1138 LEU n 
1 1139 LEU n 
1 1140 GLU n 
1 1141 GLN n 
1 1142 PHE n 
1 1143 GLU n 
1 1144 VAL n 
1 1145 LYS n 
1 1146 TRP n 
1 1147 ILE n 
1 1148 ASN n 
1 1149 LEU n 
1 1150 SER n 
1 1151 GLU n 
1 1152 ASP n 
1 1153 LEU n 
1 1154 ARG n 
1 1155 GLU n 
1 1156 GLN n 
1 1157 PHE n 
1 1158 ASN n 
1 1159 LEU n 
1 1160 SER n 
1 1161 SER n 
1 1162 ASP n 
1 1163 SER n 
1 1164 LYS n 
1 1165 SER n 
1 1166 THR n 
1 1167 ILE n 
1 1168 ASN n 
1 1169 LEU n 
1 1170 LEU n 
1 1171 PRO n 
1 1172 TYR n 
1 1173 ASP n 
1 1174 CYS n 
1 1175 LYS n 
1 1176 GLU n 
1 1177 LEU n 
1 1178 ARG n 
1 1179 LEU n 
1 1180 GLU n 
1 1181 GLY n 
1 1182 SER n 
1 1183 ASN n 
1 1184 ASP n 
1 1185 THR n 
1 1186 GLU n 
1 1187 LEU n 
1 1188 ASN n 
1 1189 TYR n 
1 1190 VAL n 
1 1191 SER n 
1 1192 CYS n 
1 1193 ALA n 
1 1194 LEU n 
1 1195 ASP n 
1 1196 ARG n 
1 1197 LYS n 
1 1198 VAL n 
1 1199 VAL n 
1 1200 GLN n 
1 1201 LYS n 
1 1202 HIS n 
1 1203 PRO n 
1 1204 SER n 
1 1205 VAL n 
1 1206 ASN n 
1 1207 ARG n 
1 1208 LEU n 
1 1209 ALA n 
1 1210 TRP n 
1 1211 THR n 
1 1212 ILE n 
1 1213 GLY n 
1 1214 ASN n 
1 1215 ARG n 
1 1216 ALA n 
1 1217 PRO n 
1 1218 TYR n 
1 1219 ILE n 
1 1220 GLY n 
1 1221 SER n 
1 1222 ARG n 
1 1223 THR n 
1 1224 GLU n 
1 1225 ASP n 
1 1226 LYS n 
1 1227 ILE n 
1 1228 GLY n 
1 1229 TYR n 
1 1230 PRO n 
1 1231 PRO n 
1 1232 LEU n 
1 1233 ARG n 
1 1234 VAL n 
1 1235 ASN n 
1 1236 CYS n 
1 1237 PRO n 
1 1238 SER n 
1 1239 ALA n 
1 1240 ALA n 
1 1241 LEU n 
1 1242 LYS n 
1 1243 GLU n 
1 1244 ALA n 
1 1245 ILE n 
1 1246 GLU n 
1 1247 MET n 
1 1248 VAL n 
1 1249 SER n 
1 1250 ARG n 
1 1251 LEU n 
1 1252 LEU n 
1 1253 TRP n 
1 1254 VAL n 
1 1255 THR n 
1 1256 GLN n 
1 1257 GLY n 
1 1258 THR n 
1 1259 ALA n 
1 1260 ASP n 
1 1261 ARG n 
1 1262 GLU n 
1 1263 LYS n 
1 1264 LEU n 
1 1265 LEU n 
1 1266 ILE n 
1 1267 PRO n 
1 1268 LEU n 
1 1269 LEU n 
1 1270 ASN n 
1 1271 SER n 
1 1272 ARG n 
1 1273 VAL n 
1 1274 ASN n 
1 1275 LEU n 
1 1276 ASP n 
1 1277 TYR n 
1 1278 GLN n 
1 1279 THR n 
1 1280 VAL n 
1 1281 LEU n 
1 1282 ASN n 
1 1283 PHE n 
1 1284 LEU n 
1 1285 PRO n 
1 1286 THR n 
1 1287 HIS n 
1 1288 TYR n 
1 1289 SER n 
1 1290 GLY n 
1 1291 ASN n 
1 1292 ILE n 
1 1293 VAL n 
1 1294 HIS n 
1 1295 ARG n 
1 1296 TYR n 
1 1297 ASN n 
1 1298 ASP n 
1 1299 GLN n 
1 1300 TYR n 
1 1301 GLY n 
1 1302 GLN n 
1 1303 HIS n 
1 1304 SER n 
1 1305 PHE n 
1 1306 MET n 
1 1307 ALA n 
1 1308 ASN n 
1 1309 ARG n 
1 1310 MET n 
1 1311 SER n 
1 1312 ASN n 
1 1313 THR n 
1 1314 SER n 
1 1315 THR n 
1 1316 ARG n 
1 1317 ALA n 
1 1318 ILE n 
1 1319 ILE n 
1 1320 SER n 
1 1321 THR n 
1 1322 ASN n 
1 1323 THR n 
1 1324 LEU n 
1 1325 GLY n 
1 1326 LYS n 
1 1327 TYR n 
1 1328 ALA n 
1 1329 GLY n 
1 1330 GLY n 
1 1331 GLY n 
1 1332 GLN n 
1 1333 ALA n 
1 1334 ALA n 
1 1335 ILE n 
1 1336 ASP n 
1 1337 SER n 
1 1338 ASN n 
1 1339 ILE n 
1 1340 ILE n 
1 1341 PHE n 
1 1342 GLN n 
1 1343 ASN n 
1 1344 THR n 
1 1345 ILE n 
1 1346 ASN n 
1 1347 LEU n 
1 1348 GLY n 
1 1349 VAL n 
1 1350 ALA n 
1 1351 VAL n 
1 1352 LEU n 
1 1353 ASP n 
1 1354 ILE n 
1 1355 ALA n 
1 1356 LEU n 
1 1357 SER n 
1 1358 LEU n 
1 1359 ALA n 
1 1360 LYS n 
1 1361 LEU n 
1 1362 SER n 
1 1363 SER n 
1 1364 ALA n 
1 1365 SER n 
1 1366 ASN n 
1 1367 VAL n 
1 1368 THR n 
1 1369 PHE n 
1 1370 ARG n 
1 1371 LEU n 
1 1372 MET n 
1 1373 LEU n 
1 1374 ASN n 
1 1375 LYS n 
1 1376 CYS n 
1 1377 CYS n 
1 1378 THR n 
1 1379 ARG n 
1 1380 HIS n 
1 1381 VAL n 
1 1382 PRO n 
1 1383 SER n 
1 1384 GLU n 
1 1385 TYR n 
1 1386 LEU n 
1 1387 TYR n 
1 1388 PHE n 
1 1389 ASP n 
1 1390 LYS n 
1 1391 PRO n 
1 1392 LEU n 
1 1393 ASP n 
1 1394 VAL n 
1 1395 ASP n 
1 1396 LEU n 
1 1397 ASN n 
1 1398 LYS n 
1 1399 TYR n 
1 1400 MET n 
1 1401 ASP n 
1 1402 ASN n 
1 1403 GLU n 
1 1404 LEU n 
1 1405 VAL n 
1 1406 TYR n 
1 1407 ASP n 
1 1408 ASN n 
1 1409 ASP n 
1 1410 PRO n 
1 1411 LEU n 
1 1412 CYS n 
1 1413 SER n 
1 1414 GLY n 
1 1415 ILE n 
1 1416 LYS n 
1 1417 GLY n 
1 1418 ARG n 
1 1419 LEU n 
1 1420 GLY n 
1 1421 ARG n 
1 1422 VAL n 
1 1423 SER n 
1 1424 ARG n 
1 1425 SER n 
1 1426 SER n 
1 1427 ARG n 
1 1428 GLU n 
1 1429 ASN n 
1 1430 LEU n 
1 1431 TYR n 
1 1432 PHE n 
1 1433 GLN n 
1 1434 GLY n 
1 1435 SER n 
1 1436 GLY n 
1 1437 TRP n 
1 1438 SER n 
1 1439 HIS n 
1 1440 PRO n 
1 1441 GLN n 
1 1442 PHE n 
1 1443 GLU n 
1 1444 LYS n 
1 1445 GLY n 
1 1446 GLY n 
1 1447 GLY n 
1 1448 SER n 
1 1449 GLY n 
1 1450 GLY n 
1 1451 GLY n 
1 1452 SER n 
1 1453 GLY n 
1 1454 GLY n 
1 1455 SER n 
1 1456 ALA n 
1 1457 TRP n 
1 1458 SER n 
1 1459 HIS n 
1 1460 PRO n 
1 1461 GLN n 
1 1462 PHE n 
1 1463 GLU n 
1 1464 LYS n 
1 1465 GLY n 
1 1466 SER n 
1 1467 ALA n 
1 1468 SER n 
1 1469 HIS n 
1 1470 HIS n 
1 1471 HIS n 
1 1472 HIS n 
1 1473 HIS n 
1 1474 HIS n 
1 1475 GLY n 
1 1476 THR n 
1 1477 LYS n 
1 1478 THR n 
1 1479 GLU n 
1 1480 GLU n 
1 1481 GLY n 
1 1482 LYS n 
1 1483 LEU n 
1 1484 VAL n 
1 1485 ILE n 
1 1486 TRP n 
1 1487 ILE n 
1 1488 ASN n 
1 1489 GLY n 
1 1490 ASP n 
1 1491 LYS n 
1 1492 GLY n 
1 1493 TYR n 
1 1494 ASN n 
1 1495 GLY n 
1 1496 LEU n 
1 1497 ALA n 
1 1498 GLU n 
1 1499 VAL n 
1 1500 GLY n 
1 1501 LYS n 
1 1502 LYS n 
1 1503 PHE n 
1 1504 GLU n 
1 1505 LYS n 
1 1506 ASP n 
1 1507 THR n 
1 1508 GLY n 
1 1509 ILE n 
1 1510 LYS n 
1 1511 VAL n 
1 1512 THR n 
1 1513 VAL n 
1 1514 GLU n 
1 1515 HIS n 
1 1516 PRO n 
1 1517 ASP n 
1 1518 LYS n 
1 1519 LEU n 
1 1520 GLU n 
1 1521 GLU n 
1 1522 LYS n 
1 1523 PHE n 
1 1524 PRO n 
1 1525 GLN n 
1 1526 VAL n 
1 1527 ALA n 
1 1528 ALA n 
1 1529 THR n 
1 1530 GLY n 
1 1531 ASP n 
1 1532 GLY n 
1 1533 PRO n 
1 1534 ASP n 
1 1535 ILE n 
1 1536 ILE n 
1 1537 PHE n 
1 1538 TRP n 
1 1539 ALA n 
1 1540 HIS n 
1 1541 ASP n 
1 1542 ARG n 
1 1543 PHE n 
1 1544 GLY n 
1 1545 GLY n 
1 1546 TYR n 
1 1547 ALA n 
1 1548 GLN n 
1 1549 SER n 
1 1550 GLY n 
1 1551 LEU n 
1 1552 LEU n 
1 1553 ALA n 
1 1554 GLU n 
1 1555 ILE n 
1 1556 THR n 
1 1557 PRO n 
1 1558 ASP n 
1 1559 LYS n 
1 1560 ALA n 
1 1561 PHE n 
1 1562 GLN n 
1 1563 ASP n 
1 1564 LYS n 
1 1565 LEU n 
1 1566 TYR n 
1 1567 PRO n 
1 1568 PHE n 
1 1569 THR n 
1 1570 TRP n 
1 1571 ASP n 
1 1572 ALA n 
1 1573 VAL n 
1 1574 ARG n 
1 1575 TYR n 
1 1576 ASN n 
1 1577 GLY n 
1 1578 LYS n 
1 1579 LEU n 
1 1580 ILE n 
1 1581 ALA n 
1 1582 TYR n 
1 1583 PRO n 
1 1584 ILE n 
1 1585 ALA n 
1 1586 VAL n 
1 1587 GLU n 
1 1588 ALA n 
1 1589 LEU n 
1 1590 SER n 
1 1591 LEU n 
1 1592 ILE n 
1 1593 TYR n 
1 1594 ASN n 
1 1595 LYS n 
1 1596 ASP n 
1 1597 LEU n 
1 1598 LEU n 
1 1599 PRO n 
1 1600 ASN n 
1 1601 PRO n 
1 1602 PRO n 
1 1603 LYS n 
1 1604 THR n 
1 1605 TRP n 
1 1606 GLU n 
1 1607 GLU n 
1 1608 ILE n 
1 1609 PRO n 
1 1610 ALA n 
1 1611 LEU n 
1 1612 ASP n 
1 1613 LYS n 
1 1614 GLU n 
1 1615 LEU n 
1 1616 LYS n 
1 1617 ALA n 
1 1618 LYS n 
1 1619 GLY n 
1 1620 LYS n 
1 1621 SER n 
1 1622 ALA n 
1 1623 LEU n 
1 1624 MET n 
1 1625 PHE n 
1 1626 ASN n 
1 1627 LEU n 
1 1628 GLN n 
1 1629 GLU n 
1 1630 PRO n 
1 1631 TYR n 
1 1632 PHE n 
1 1633 THR n 
1 1634 TRP n 
1 1635 PRO n 
1 1636 LEU n 
1 1637 ILE n 
1 1638 ALA n 
1 1639 ALA n 
1 1640 ASP n 
1 1641 GLY n 
1 1642 GLY n 
1 1643 TYR n 
1 1644 ALA n 
1 1645 PHE n 
1 1646 LYS n 
1 1647 TYR n 
1 1648 GLU n 
1 1649 ASN n 
1 1650 GLY n 
1 1651 LYS n 
1 1652 TYR n 
1 1653 ASP n 
1 1654 ILE n 
1 1655 LYS n 
1 1656 ASP n 
1 1657 VAL n 
1 1658 GLY n 
1 1659 VAL n 
1 1660 ASP n 
1 1661 ASN n 
1 1662 ALA n 
1 1663 GLY n 
1 1664 ALA n 
1 1665 LYS n 
1 1666 ALA n 
1 1667 GLY n 
1 1668 LEU n 
1 1669 THR n 
1 1670 PHE n 
1 1671 LEU n 
1 1672 VAL n 
1 1673 ASP n 
1 1674 LEU n 
1 1675 ILE n 
1 1676 LYS n 
1 1677 ASN n 
1 1678 LYS n 
1 1679 HIS n 
1 1680 MET n 
1 1681 ASN n 
1 1682 ALA n 
1 1683 ASP n 
1 1684 THR n 
1 1685 ASP n 
1 1686 TYR n 
1 1687 SER n 
1 1688 ILE n 
1 1689 ALA n 
1 1690 GLU n 
1 1691 ALA n 
1 1692 ALA n 
1 1693 PHE n 
1 1694 ASN n 
1 1695 LYS n 
1 1696 GLY n 
1 1697 GLU n 
1 1698 THR n 
1 1699 ALA n 
1 1700 MET n 
1 1701 THR n 
1 1702 ILE n 
1 1703 ASN n 
1 1704 GLY n 
1 1705 PRO n 
1 1706 TRP n 
1 1707 ALA n 
1 1708 TRP n 
1 1709 SER n 
1 1710 ASN n 
1 1711 ILE n 
1 1712 ASP n 
1 1713 THR n 
1 1714 SER n 
1 1715 LYS n 
1 1716 VAL n 
1 1717 ASN n 
1 1718 TYR n 
1 1719 GLY n 
1 1720 VAL n 
1 1721 THR n 
1 1722 VAL n 
1 1723 LEU n 
1 1724 PRO n 
1 1725 THR n 
1 1726 PHE n 
1 1727 LYS n 
1 1728 GLY n 
1 1729 GLN n 
1 1730 PRO n 
1 1731 SER n 
1 1732 LYS n 
1 1733 PRO n 
1 1734 PHE n 
1 1735 VAL n 
1 1736 GLY n 
1 1737 VAL n 
1 1738 LEU n 
1 1739 SER n 
1 1740 ALA n 
1 1741 GLY n 
1 1742 ILE n 
1 1743 ASN n 
1 1744 ALA n 
1 1745 ALA n 
1 1746 SER n 
1 1747 PRO n 
1 1748 ASN n 
1 1749 LYS n 
1 1750 GLU n 
1 1751 LEU n 
1 1752 ALA n 
1 1753 LYS n 
1 1754 GLU n 
1 1755 PHE n 
1 1756 LEU n 
1 1757 GLU n 
1 1758 ASN n 
1 1759 TYR n 
1 1760 LEU n 
1 1761 LEU n 
1 1762 THR n 
1 1763 ASP n 
1 1764 GLU n 
1 1765 GLY n 
1 1766 LEU n 
1 1767 GLU n 
1 1768 ALA n 
1 1769 VAL n 
1 1770 ASN n 
1 1771 LYS n 
1 1772 ASP n 
1 1773 LYS n 
1 1774 PRO n 
1 1775 LEU n 
1 1776 GLY n 
1 1777 ALA n 
1 1778 VAL n 
1 1779 ALA n 
1 1780 LEU n 
1 1781 LYS n 
1 1782 SER n 
1 1783 TYR n 
1 1784 GLU n 
1 1785 GLU n 
1 1786 GLU n 
1 1787 LEU n 
1 1788 ALA n 
1 1789 LYS n 
1 1790 ASP n 
1 1791 PRO n 
1 1792 ARG n 
1 1793 ILE n 
1 1794 ALA n 
1 1795 ALA n 
1 1796 THR n 
1 1797 MET n 
1 1798 GLU n 
1 1799 ASN n 
1 1800 ALA n 
1 1801 GLN n 
1 1802 LYS n 
1 1803 GLY n 
1 1804 GLU n 
1 1805 ILE n 
1 1806 MET n 
1 1807 PRO n 
1 1808 ASN n 
1 1809 ILE n 
1 1810 PRO n 
1 1811 GLN n 
1 1812 MET n 
1 1813 SER n 
1 1814 ALA n 
1 1815 PHE n 
1 1816 TRP n 
1 1817 TYR n 
1 1818 ALA n 
1 1819 VAL n 
1 1820 ARG n 
1 1821 THR n 
1 1822 ALA n 
1 1823 VAL n 
1 1824 ILE n 
1 1825 ASN n 
1 1826 ALA n 
1 1827 ALA n 
1 1828 SER n 
1 1829 GLY n 
1 1830 ARG n 
1 1831 GLN n 
1 1832 THR n 
1 1833 VAL n 
1 1834 ASP n 
1 1835 GLU n 
1 1836 ALA n 
1 1837 LEU n 
1 1838 LYS n 
1 1839 ASP n 
1 1840 ALA n 
1 1841 GLN n 
1 1842 THR n 
1 1843 GLY n 
1 1844 ASP n 
1 1845 TYR n 
1 1846 LYS n 
1 1847 ASP n 
1 1848 ASP n 
1 1849 ASP n 
1 1850 ASP n 
1 1851 LYS n 
2 1    MET n 
2 2    GLY n 
2 3    SER n 
2 4    SER n 
2 5    HIS n 
2 6    HIS n 
2 7    HIS n 
2 8    HIS n 
2 9    HIS n 
2 10   HIS n 
2 11   GLY n 
2 12   THR n 
2 13   LYS n 
2 14   THR n 
2 15   GLU n 
2 16   GLU n 
2 17   GLY n 
2 18   LYS n 
2 19   LEU n 
2 20   VAL n 
2 21   ILE n 
2 22   TRP n 
2 23   ILE n 
2 24   ASN n 
2 25   GLY n 
2 26   ASP n 
2 27   LYS n 
2 28   GLY n 
2 29   TYR n 
2 30   ASN n 
2 31   GLY n 
2 32   LEU n 
2 33   ALA n 
2 34   GLU n 
2 35   VAL n 
2 36   GLY n 
2 37   LYS n 
2 38   LYS n 
2 39   PHE n 
2 40   GLU n 
2 41   LYS n 
2 42   ASP n 
2 43   THR n 
2 44   GLY n 
2 45   ILE n 
2 46   LYS n 
2 47   VAL n 
2 48   THR n 
2 49   VAL n 
2 50   GLU n 
2 51   HIS n 
2 52   PRO n 
2 53   ASP n 
2 54   LYS n 
2 55   LEU n 
2 56   GLU n 
2 57   GLU n 
2 58   LYS n 
2 59   PHE n 
2 60   PRO n 
2 61   GLN n 
2 62   VAL n 
2 63   ALA n 
2 64   ALA n 
2 65   THR n 
2 66   GLY n 
2 67   ASP n 
2 68   GLY n 
2 69   PRO n 
2 70   ASP n 
2 71   ILE n 
2 72   ILE n 
2 73   PHE n 
2 74   TRP n 
2 75   ALA n 
2 76   HIS n 
2 77   ASP n 
2 78   ARG n 
2 79   PHE n 
2 80   GLY n 
2 81   GLY n 
2 82   TYR n 
2 83   ALA n 
2 84   GLN n 
2 85   SER n 
2 86   GLY n 
2 87   LEU n 
2 88   LEU n 
2 89   ALA n 
2 90   GLU n 
2 91   ILE n 
2 92   THR n 
2 93   PRO n 
2 94   ASP n 
2 95   LYS n 
2 96   ALA n 
2 97   PHE n 
2 98   GLN n 
2 99   ASP n 
2 100  LYS n 
2 101  LEU n 
2 102  TYR n 
2 103  PRO n 
2 104  PHE n 
2 105  THR n 
2 106  TRP n 
2 107  ASP n 
2 108  ALA n 
2 109  VAL n 
2 110  ARG n 
2 111  TYR n 
2 112  ASN n 
2 113  GLY n 
2 114  LYS n 
2 115  LEU n 
2 116  ILE n 
2 117  ALA n 
2 118  TYR n 
2 119  PRO n 
2 120  ILE n 
2 121  ALA n 
2 122  VAL n 
2 123  GLU n 
2 124  ALA n 
2 125  LEU n 
2 126  SER n 
2 127  LEU n 
2 128  ILE n 
2 129  TYR n 
2 130  ASN n 
2 131  LYS n 
2 132  ASP n 
2 133  LEU n 
2 134  LEU n 
2 135  PRO n 
2 136  ASN n 
2 137  PRO n 
2 138  PRO n 
2 139  LYS n 
2 140  THR n 
2 141  TRP n 
2 142  GLU n 
2 143  GLU n 
2 144  ILE n 
2 145  PRO n 
2 146  ALA n 
2 147  LEU n 
2 148  ASP n 
2 149  LYS n 
2 150  GLU n 
2 151  LEU n 
2 152  LYS n 
2 153  ALA n 
2 154  LYS n 
2 155  GLY n 
2 156  LYS n 
2 157  SER n 
2 158  ALA n 
2 159  LEU n 
2 160  MET n 
2 161  PHE n 
2 162  ASN n 
2 163  LEU n 
2 164  GLN n 
2 165  GLU n 
2 166  PRO n 
2 167  TYR n 
2 168  PHE n 
2 169  THR n 
2 170  TRP n 
2 171  PRO n 
2 172  LEU n 
2 173  ILE n 
2 174  ALA n 
2 175  ALA n 
2 176  ASP n 
2 177  GLY n 
2 178  GLY n 
2 179  TYR n 
2 180  ALA n 
2 181  PHE n 
2 182  LYS n 
2 183  TYR n 
2 184  GLU n 
2 185  ASN n 
2 186  GLY n 
2 187  LYS n 
2 188  TYR n 
2 189  ASP n 
2 190  ILE n 
2 191  LYS n 
2 192  ASP n 
2 193  VAL n 
2 194  GLY n 
2 195  VAL n 
2 196  ASP n 
2 197  ASN n 
2 198  ALA n 
2 199  GLY n 
2 200  ALA n 
2 201  LYS n 
2 202  ALA n 
2 203  GLY n 
2 204  LEU n 
2 205  THR n 
2 206  PHE n 
2 207  LEU n 
2 208  VAL n 
2 209  ASP n 
2 210  LEU n 
2 211  ILE n 
2 212  LYS n 
2 213  ASN n 
2 214  LYS n 
2 215  HIS n 
2 216  MET n 
2 217  ASN n 
2 218  ALA n 
2 219  ASP n 
2 220  THR n 
2 221  ASP n 
2 222  TYR n 
2 223  SER n 
2 224  ILE n 
2 225  ALA n 
2 226  GLU n 
2 227  ALA n 
2 228  ALA n 
2 229  PHE n 
2 230  ASN n 
2 231  LYS n 
2 232  GLY n 
2 233  GLU n 
2 234  THR n 
2 235  ALA n 
2 236  MET n 
2 237  THR n 
2 238  ILE n 
2 239  ASN n 
2 240  GLY n 
2 241  PRO n 
2 242  TRP n 
2 243  ALA n 
2 244  TRP n 
2 245  SER n 
2 246  ASN n 
2 247  ILE n 
2 248  ASP n 
2 249  THR n 
2 250  SER n 
2 251  LYS n 
2 252  VAL n 
2 253  ASN n 
2 254  TYR n 
2 255  GLY n 
2 256  VAL n 
2 257  THR n 
2 258  VAL n 
2 259  LEU n 
2 260  PRO n 
2 261  THR n 
2 262  PHE n 
2 263  LYS n 
2 264  GLY n 
2 265  GLN n 
2 266  PRO n 
2 267  SER n 
2 268  LYS n 
2 269  PRO n 
2 270  PHE n 
2 271  VAL n 
2 272  GLY n 
2 273  VAL n 
2 274  LEU n 
2 275  SER n 
2 276  ALA n 
2 277  GLY n 
2 278  ILE n 
2 279  ASN n 
2 280  ALA n 
2 281  ALA n 
2 282  SER n 
2 283  PRO n 
2 284  ASN n 
2 285  LYS n 
2 286  GLU n 
2 287  LEU n 
2 288  ALA n 
2 289  LYS n 
2 290  GLU n 
2 291  PHE n 
2 292  LEU n 
2 293  GLU n 
2 294  ASN n 
2 295  TYR n 
2 296  LEU n 
2 297  LEU n 
2 298  THR n 
2 299  ASP n 
2 300  GLU n 
2 301  GLY n 
2 302  LEU n 
2 303  GLU n 
2 304  ALA n 
2 305  VAL n 
2 306  ASN n 
2 307  LYS n 
2 308  ASP n 
2 309  LYS n 
2 310  PRO n 
2 311  LEU n 
2 312  GLY n 
2 313  ALA n 
2 314  VAL n 
2 315  ALA n 
2 316  LEU n 
2 317  LYS n 
2 318  SER n 
2 319  TYR n 
2 320  GLU n 
2 321  GLU n 
2 322  GLU n 
2 323  LEU n 
2 324  ALA n 
2 325  LYS n 
2 326  ASP n 
2 327  PRO n 
2 328  ARG n 
2 329  ILE n 
2 330  ALA n 
2 331  ALA n 
2 332  THR n 
2 333  MET n 
2 334  GLU n 
2 335  ASN n 
2 336  ALA n 
2 337  GLN n 
2 338  LYS n 
2 339  GLY n 
2 340  GLU n 
2 341  ILE n 
2 342  MET n 
2 343  PRO n 
2 344  ASN n 
2 345  ILE n 
2 346  PRO n 
2 347  GLN n 
2 348  MET n 
2 349  SER n 
2 350  ALA n 
2 351  PHE n 
2 352  TRP n 
2 353  TYR n 
2 354  ALA n 
2 355  VAL n 
2 356  ARG n 
2 357  THR n 
2 358  ALA n 
2 359  VAL n 
2 360  ILE n 
2 361  ASN n 
2 362  ALA n 
2 363  ALA n 
2 364  SER n 
2 365  GLY n 
2 366  ARG n 
2 367  GLN n 
2 368  THR n 
2 369  VAL n 
2 370  ASP n 
2 371  GLU n 
2 372  ALA n 
2 373  LEU n 
2 374  LYS n 
2 375  ASP n 
2 376  ALA n 
2 377  GLN n 
2 378  THR n 
2 379  GLY n 
2 380  THR n 
2 381  ASP n 
2 382  TYR n 
2 383  ASP n 
2 384  ILE n 
2 385  PRO n 
2 386  THR n 
2 387  THR n 
2 388  LEU n 
2 389  GLU n 
2 390  VAL n 
2 391  LEU n 
2 392  PHE n 
2 393  GLN n 
2 394  GLY n 
2 395  PRO n 
2 396  LEU n 
2 397  GLY n 
2 398  SER n 
2 399  SER n 
2 400  THR n 
2 401  ASP n 
2 402  ASP n 
2 403  ILE n 
2 404  ILE n 
2 405  TRP n 
2 406  ASP n 
2 407  GLN n 
2 408  LEU n 
2 409  ILE n 
2 410  VAL n 
2 411  LYS n 
2 412  ARG n 
2 413  THR n 
2 414  LEU n 
2 415  ALA n 
2 416  ASP n 
2 417  LEU n 
2 418  LEU n 
2 419  ILE n 
2 420  PRO n 
2 421  ILE n 
2 422  ASN n 
2 423  ARG n 
2 424  GLN n 
2 425  ILE n 
2 426  SER n 
2 427  ASP n 
2 428  ILE n 
2 429  GLN n 
2 430  SER n 
2 431  THR n 
2 432  LEU n 
2 433  SER n 
2 434  GLU n 
2 435  VAL n 
2 436  THR n 
2 437  THR n 
2 438  ARG n 
2 439  VAL n 
2 440  HIS n 
2 441  GLU n 
2 442  ILE n 
2 443  GLU n 
2 444  ARG n 
2 445  GLN n 
2 446  LEU n 
2 447  HIS n 
2 448  GLU n 
2 449  ILE n 
2 450  THR n 
2 451  PRO n 
2 452  VAL n 
2 453  LEU n 
2 454  LYS n 
2 455  MET n 
2 456  GLY n 
2 457  ARG n 
2 458  THR n 
2 459  LEU n 
2 460  GLU n 
2 461  ALA n 
2 462  ILE n 
2 463  SER n 
2 464  LYS n 
2 465  GLY n 
2 466  MET n 
2 467  SER n 
2 468  GLU n 
2 469  MET n 
2 470  LEU n 
2 471  ALA n 
2 472  LYS n 
2 473  TYR n 
2 474  ASP n 
2 475  HIS n 
2 476  LEU n 
2 477  VAL n 
2 478  ILE n 
2 479  SER n 
2 480  THR n 
2 481  GLY n 
2 482  ARG n 
2 483  THR n 
2 484  THR n 
2 485  ALA n 
2 486  PRO n 
2 487  ALA n 
2 488  ALA n 
2 489  ALA n 
2 490  PHE n 
2 491  ASP n 
2 492  ALA n 
2 493  TYR n 
2 494  LEU n 
2 495  ASN n 
2 496  GLU n 
2 497  HIS n 
2 498  GLY n 
2 499  VAL n 
2 500  PRO n 
2 501  PRO n 
2 502  PRO n 
2 503  GLN n 
2 504  PRO n 
2 505  ALA n 
2 506  ILE n 
2 507  PHE n 
2 508  LYS n 
2 509  ASP n 
2 510  LEU n 
2 511  GLY n 
2 512  VAL n 
2 513  ALA n 
2 514  GLN n 
2 515  GLN n 
2 516  ALA n 
2 517  CYS n 
2 518  SER n 
2 519  LYS n 
2 520  GLY n 
2 521  THR n 
2 522  MET n 
2 523  VAL n 
2 524  LYS n 
2 525  ASN n 
2 526  ALA n 
2 527  THR n 
2 528  THR n 
2 529  ASP n 
2 530  ALA n 
2 531  ALA n 
2 532  ASP n 
2 533  LYS n 
2 534  MET n 
2 535  SER n 
2 536  LYS n 
2 537  VAL n 
2 538  LEU n 
2 539  GLU n 
2 540  LEU n 
2 541  SER n 
2 542  GLU n 
2 543  GLU n 
2 544  THR n 
2 545  PHE n 
2 546  SER n 
2 547  LYS n 
2 548  PRO n 
2 549  ASN n 
2 550  LEU n 
2 551  SER n 
2 552  ALA n 
2 553  LYS n 
2 554  ASP n 
2 555  LEU n 
2 556  ALA n 
2 557  LEU n 
2 558  LEU n 
2 559  LEU n 
2 560  PHE n 
2 561  THR n 
2 562  HIS n 
2 563  LEU n 
2 564  PRO n 
2 565  GLY n 
2 566  ASN n 
2 567  ASN n 
2 568  THR n 
2 569  PRO n 
2 570  PHE n 
2 571  HIS n 
2 572  ILE n 
2 573  LEU n 
2 574  ALA n 
2 575  GLN n 
2 576  VAL n 
2 577  LEU n 
2 578  SER n 
2 579  LYS n 
2 580  ILE n 
2 581  ALA n 
2 582  TYR n 
2 583  LYS n 
2 584  SER n 
2 585  GLY n 
2 586  LYS n 
2 587  SER n 
2 588  GLY n 
2 589  ALA n 
2 590  PHE n 
2 591  LEU n 
2 592  ASP n 
2 593  ALA n 
2 594  PHE n 
2 595  HIS n 
2 596  GLN n 
2 597  ILE n 
2 598  LEU n 
2 599  SER n 
2 600  GLU n 
2 601  GLY n 
2 602  GLU n 
2 603  ASN n 
2 604  ALA n 
2 605  GLN n 
2 606  ALA n 
2 607  ALA n 
2 608  LEU n 
2 609  THR n 
2 610  ARG n 
2 611  LEU n 
2 612  SER n 
2 613  ARG n 
2 614  THR n 
2 615  PHE n 
2 616  ASP n 
2 617  ALA n 
2 618  PHE n 
2 619  LEU n 
2 620  GLY n 
2 621  VAL n 
2 622  VAL n 
2 623  PRO n 
2 624  PRO n 
2 625  VAL n 
2 626  ILE n 
2 627  ARG n 
2 628  VAL n 
2 629  LYS n 
2 630  ASN n 
2 631  PHE n 
2 632  GLN n 
2 633  THR n 
2 634  VAL n 
2 635  PRO n 
2 636  ARG n 
2 637  PRO n 
2 638  CYS n 
2 639  GLN n 
2 640  LYS n 
2 641  SER n 
2 642  LEU n 
2 643  ARG n 
2 644  ALA n 
2 645  VAL n 
2 646  PRO n 
2 647  PRO n 
2 648  ASN n 
2 649  PRO n 
2 650  THR n 
2 651  ILE n 
2 652  ASP n 
2 653  LYS n 
2 654  GLY n 
2 655  TRP n 
2 656  VAL n 
2 657  CYS n 
2 658  VAL n 
2 659  TYR n 
2 660  SER n 
2 661  SER n 
2 662  GLU n 
2 663  GLN n 
2 664  GLY n 
2 665  GLU n 
2 666  THR n 
2 667  ARG n 
2 668  ALA n 
2 669  LEU n 
2 670  LYS n 
2 671  ILE n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1    1425 ? ? ?                     ? ? ? ? ? ? 'Marburg virus - Musoke, Kenya, 1980' 33727 ? ? ? 
? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 1426 1851 ? ? 'malE, b4034, JW3994' ? ? ? ? ? ? 'Escherichia coli K-12'               83333 ? ? ? 
? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1    398  ? ? 'malE, b4034, JW3994' ? ? ? ? ? ? 'Escherichia coli K-12'               83333 ? ? ? 
? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 2 sample 'Biological sequence' 399  671  ? ? VP35                  ? ? ? ? ? ? 'Marburg virus - Musoke, Kenya, 1980' 33727 ? ? ? 
? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
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  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
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    ?    ?   ?   A . n 
A 1 2    GLN 2    2    ?    ?   ?   A . n 
A 1 3    HIS 3    3    ?    ?   ?   A . n 
A 1 4    PRO 4    4    4    PRO PRO A . n 
A 1 5    THR 5    5    5    THR THR A . n 
A 1 6    GLN 6    6    6    GLN GLN A . n 
A 1 7    TYR 7    7    7    TYR TYR A . n 
A 1 8    PRO 8    8    8    PRO PRO A . n 
A 1 9    ASP 9    9    9    ASP ASP A . n 
A 1 10   ALA 10   10   10   ALA ALA A . n 
A 1 11   ARG 11   11   11   ARG ARG A . n 
A 1 12   LEU 12   12   12   LEU LEU A . n 
A 1 13   SER 13   13   13   SER SER A . n 
A 1 14   SER 14   14   14   SER SER A . n 
A 1 15   PRO 15   15   15   PRO PRO A . n 
A 1 16   ILE 16   16   16   ILE ILE A . n 
A 1 17   ILE 17   17   17   ILE ILE A . n 
A 1 18   LEU 18   18   18   LEU LEU A . n 
A 1 19   ASP 19   19   19   ASP ASP A . n 
A 1 20   GLN 20   20   20   GLN GLN A . n 
A 1 21   CYS 21   21   21   CYS CYS A . n 
A 1 22   ASP 22   22   22   ASP ASP A . n 
A 1 23   LEU 23   23   23   LEU LEU A . n 
A 1 24   LEU 24   24   24   LEU LEU A . n 
A 1 25   ALA 25   25   25   ALA ALA A . n 
A 1 26   ARG 26   26   26   ARG ARG A . n 
A 1 27   SER 27   27   27   SER SER A . n 
A 1 28   LEU 28   28   28   LEU LEU A . n 
A 1 29   GLY 29   29   29   GLY GLY A . n 
A 1 30   LEU 30   30   30   LEU LEU A . n 
A 1 31   TYR 31   31   31   TYR TYR A . n 
A 1 32   SER 32   32   32   SER SER A . n 
A 1 33   HIS 33   33   33   HIS HIS A . n 
A 1 34   TYR 34   34   34   TYR TYR A . n 
A 1 35   SER 35   35   35   SER SER A . n 
A 1 36   HIS 36   36   36   HIS HIS A . n 
A 1 37   ASN 37   37   37   ASN ASN A . n 
A 1 38   PRO 38   38   38   PRO PRO A . n 
A 1 39   LYS 39   39   39   LYS LYS A . n 
A 1 40   LEU 40   40   40   LEU LEU A . n 
A 1 41   ARG 41   41   41   ARG ARG A . n 
A 1 42   ASN 42   42   42   ASN ASN A . n 
A 1 43   CYS 43   43   43   CYS CYS A . n 
A 1 44   ARG 44   44   44   ARG ARG A . n 
A 1 45   ILE 45   45   45   ILE ILE A . n 
A 1 46   PRO 46   46   46   PRO PRO A . n 
A 1 47   HIS 47   47   47   HIS HIS A . n 
A 1 48   HIS 48   48   48   HIS HIS A . n 
A 1 49   ILE 49   49   49   ILE ILE A . n 
A 1 50   TYR 50   50   50   TYR TYR A . n 
A 1 51   ARG 51   51   51   ARG ARG A . n 
A 1 52   LEU 52   52   52   LEU LEU A . n 
A 1 53   ARG 53   53   53   ARG ARG A . n 
A 1 54   ASN 54   54   54   ASN ASN A . n 
A 1 55   SER 55   55   55   SER SER A . n 
A 1 56   THR 56   56   56   THR THR A . n 
A 1 57   ALA 57   57   57   ALA ALA A . n 
A 1 58   LEU 58   58   58   LEU LEU A . n 
A 1 59   LYS 59   59   59   LYS LYS A . n 
A 1 60   THR 60   60   60   THR THR A . n 
A 1 61   PHE 61   61   61   PHE PHE A . n 
A 1 62   LEU 62   62   62   LEU LEU A . n 
A 1 63   GLN 63   63   63   GLN GLN A . n 
A 1 64   ASN 64   64   64   ASN ASN A . n 
A 1 65   CYS 65   65   65   CYS CYS A . n 
A 1 66   SER 66   66   66   SER SER A . n 
A 1 67   ILE 67   67   67   ILE ILE A . n 
A 1 68   LEU 68   68   68   LEU LEU A . n 
A 1 69   THR 69   69   69   THR THR A . n 
A 1 70   VAL 70   70   70   VAL VAL A . n 
A 1 71   PRO 71   71   71   PRO PRO A . n 
A 1 72   PHE 72   72   72   PHE PHE A . n 
A 1 73   HIS 73   73   73   HIS HIS A . n 
A 1 74   SER 74   74   74   SER SER A . n 
A 1 75   ILE 75   75   75   ILE ILE A . n 
A 1 76   TRP 76   76   76   TRP TRP A . n 
A 1 77   ASP 77   77   77   ASP ASP A . n 
A 1 78   HIS 78   78   78   HIS HIS A . n 
A 1 79   ILE 79   79   79   ILE ILE A . n 
A 1 80   LEU 80   80   80   LEU LEU A . n 
A 1 81   THR 81   81   81   THR THR A . n 
A 1 82   SER 82   82   82   SER SER A . n 
A 1 83   ILE 83   83   83   ILE ILE A . n 
A 1 84   GLN 84   84   84   GLN GLN A . n 
A 1 85   TYR 85   85   85   TYR TYR A . n 
A 1 86   ASP 86   86   86   ASP ASP A . n 
A 1 87   ALA 87   87   87   ALA ALA A . n 
A 1 88   ILE 88   88   88   ILE ILE A . n 
A 1 89   ASN 89   89   89   ASN ASN A . n 
A 1 90   HIS 90   90   90   HIS HIS A . n 
A 1 91   VAL 91   91   91   VAL VAL A . n 
A 1 92   ASP 92   92   92   ASP ASP A . n 
A 1 93   ASP 93   93   93   ASP ASP A . n 
A 1 94   PHE 94   94   94   PHE PHE A . n 
A 1 95   LYS 95   95   95   LYS LYS A . n 
A 1 96   TYR 96   96   96   TYR TYR A . n 
A 1 97   LEU 97   97   97   LEU LEU A . n 
A 1 98   LEU 98   98   98   LEU LEU A . n 
A 1 99   PRO 99   99   99   PRO PRO A . n 
A 1 100  SER 100  100  100  SER SER A . n 
A 1 101  GLU 101  101  101  GLU GLU A . n 
A 1 102  LEU 102  102  102  LEU LEU A . n 
A 1 103  VAL 103  103  103  VAL VAL A . n 
A 1 104  LYS 104  104  104  LYS LYS A . n 
A 1 105  TYR 105  105  105  TYR TYR A . n 
A 1 106  ALA 106  106  106  ALA ALA A . n 
A 1 107  ASN 107  107  107  ASN ASN A . n 
A 1 108  TRP 108  108  108  TRP TRP A . n 
A 1 109  ASP 109  109  109  ASP ASP A . n 
A 1 110  ASN 110  110  110  ASN ASN A . n 
A 1 111  GLU 111  111  111  GLU GLU A . n 
A 1 112  PHE 112  112  112  PHE PHE A . n 
A 1 113  LEU 113  113  113  LEU LEU A . n 
A 1 114  LYS 114  114  114  LYS LYS A . n 
A 1 115  ALA 115  115  115  ALA ALA A . n 
A 1 116  TYR 116  116  116  TYR TYR A . n 
A 1 117  LEU 117  117  117  LEU LEU A . n 
A 1 118  ASN 118  118  118  ASN ASN A . n 
A 1 119  LYS 119  119  119  LYS LYS A . n 
A 1 120  ILE 120  120  120  ILE ILE A . n 
A 1 121  LEU 121  121  121  LEU LEU A . n 
A 1 122  GLY 122  122  122  GLY GLY A . n 
A 1 123  LEU 123  123  123  LEU LEU A . n 
A 1 124  ASP 124  124  124  ASP ASP A . n 
A 1 125  HIS 125  125  125  HIS HIS A . n 
A 1 126  VAL 126  126  126  VAL VAL A . n 
A 1 127  PHE 127  127  127  PHE PHE A . n 
A 1 128  SER 128  128  128  SER SER A . n 
A 1 129  ALA 129  129  129  ALA ALA A . n 
A 1 130  SER 130  130  130  SER SER A . n 
A 1 131  ALA 131  131  131  ALA ALA A . n 
A 1 132  ARG 132  132  132  ARG ARG A . n 
A 1 133  SER 133  133  133  SER SER A . n 
A 1 134  GLN 134  134  134  GLN GLN A . n 
A 1 135  CYS 135  135  135  CYS CYS A . n 
A 1 136  GLU 136  136  136  GLU GLU A . n 
A 1 137  ASP 137  137  137  ASP ASP A . n 
A 1 138  PHE 138  138  138  PHE PHE A . n 
A 1 139  SER 139  139  139  SER SER A . n 
A 1 140  PRO 140  140  140  PRO PRO A . n 
A 1 141  LYS 141  141  141  LYS LYS A . n 
A 1 142  GLU 142  142  142  GLU GLU A . n 
A 1 143  ASN 143  143  143  ASN ASN A . n 
A 1 144  PRO 144  144  144  PRO PRO A . n 
A 1 145  TYR 145  145  145  TYR TYR A . n 
A 1 146  TYR 146  146  146  TYR TYR A . n 
A 1 147  TRP 147  147  147  TRP TRP A . n 
A 1 148  GLY 148  148  148  GLY GLY A . n 
A 1 149  MET 149  149  149  MET MET A . n 
A 1 150  LEU 150  150  150  LEU LEU A . n 
A 1 151  LEU 151  151  151  LEU LEU A . n 
A 1 152  LEU 152  152  152  LEU LEU A . n 
A 1 153  VAL 153  153  153  VAL VAL A . n 
A 1 154  HIS 154  154  154  HIS HIS A . n 
A 1 155  LEU 155  155  155  LEU LEU A . n 
A 1 156  SER 156  156  156  SER SER A . n 
A 1 157  GLN 157  157  157  GLN GLN A . n 
A 1 158  LEU 158  158  158  LEU LEU A . n 
A 1 159  ALA 159  159  159  ALA ALA A . n 
A 1 160  ARG 160  160  160  ARG ARG A . n 
A 1 161  ARG 161  161  161  ARG ARG A . n 
A 1 162  ILE 162  162  162  ILE ILE A . n 
A 1 163  LYS 163  163  163  LYS LYS A . n 
A 1 164  GLY 164  164  164  GLY GLY A . n 
A 1 165  GLN 165  165  165  GLN GLN A . n 
A 1 166  ARG 166  166  166  ARG ARG A . n 
A 1 167  GLY 167  167  167  GLY GLY A . n 
A 1 168  SER 168  168  168  SER SER A . n 
A 1 169  LEU 169  169  169  LEU LEU A . n 
A 1 170  ARG 170  170  170  ARG ARG A . n 
A 1 171  SER 171  171  171  SER SER A . n 
A 1 172  ASN 172  172  172  ASN ASN A . n 
A 1 173  TRP 173  173  173  TRP TRP A . n 
A 1 174  LYS 174  174  174  LYS LYS A . n 
A 1 175  PHE 175  175  175  PHE PHE A . n 
A 1 176  ILE 176  176  176  ILE ILE A . n 
A 1 177  GLY 177  177  177  GLY GLY A . n 
A 1 178  THR 178  178  178  THR THR A . n 
A 1 179  ASP 179  179  179  ASP ASP A . n 
A 1 180  LEU 180  180  180  LEU LEU A . n 
A 1 181  GLU 181  181  181  GLU GLU A . n 
A 1 182  LEU 182  182  182  LEU LEU A . n 
A 1 183  PHE 183  183  183  PHE PHE A . n 
A 1 184  GLY 184  184  184  GLY GLY A . n 
A 1 185  ILE 185  185  185  ILE ILE A . n 
A 1 186  ALA 186  186  186  ALA ALA A . n 
A 1 187  ASP 187  187  187  ASP ASP A . n 
A 1 188  PHE 188  188  188  PHE PHE A . n 
A 1 189  VAL 189  189  189  VAL VAL A . n 
A 1 190  ILE 190  190  190  ILE ILE A . n 
A 1 191  PHE 191  191  191  PHE PHE A . n 
A 1 192  LYS 192  192  192  LYS LYS A . n 
A 1 193  VAL 193  193  193  VAL VAL A . n 
A 1 194  PRO 194  194  194  PRO PRO A . n 
A 1 195  VAL 195  195  195  VAL VAL A . n 
A 1 196  LYS 196  196  196  LYS LYS A . n 
A 1 197  THR 197  197  197  THR THR A . n 
A 1 198  ILE 198  198  198  ILE ILE A . n 
A 1 199  ILE 199  199  199  ILE ILE A . n 
A 1 200  ARG 200  200  200  ARG ARG A . n 
A 1 201  ASN 201  201  201  ASN ASN A . n 
A 1 202  ALA 202  202  202  ALA ALA A . n 
A 1 203  VAL 203  203  203  VAL VAL A . n 
A 1 204  SER 204  204  204  SER SER A . n 
A 1 205  LEU 205  205  205  LEU LEU A . n 
A 1 206  GLN 206  206  206  GLN GLN A . n 
A 1 207  ALA 207  207  207  ALA ALA A . n 
A 1 208  SER 208  208  208  SER SER A . n 
A 1 209  LYS 209  209  209  LYS LYS A . n 
A 1 210  PRO 210  210  210  PRO PRO A . n 
A 1 211  GLY 211  211  211  GLY GLY A . n 
A 1 212  LEU 212  212  212  LEU LEU A . n 
A 1 213  ARG 213  213  213  ARG ARG A . n 
A 1 214  ILE 214  214  214  ILE ILE A . n 
A 1 215  TRP 215  215  215  TRP TRP A . n 
A 1 216  TYR 216  216  216  TYR TYR A . n 
A 1 217  ARG 217  217  217  ARG ARG A . n 
A 1 218  ASP 218  218  218  ASP ASP A . n 
A 1 219  GLN 219  219  219  GLN GLN A . n 
A 1 220  ASN 220  220  220  ASN ASN A . n 
A 1 221  LEU 221  221  221  LEU LEU A . n 
A 1 222  THR 222  222  222  THR THR A . n 
A 1 223  PRO 223  223  223  PRO PRO A . n 
A 1 224  TYR 224  224  224  TYR TYR A . n 
A 1 225  LEU 225  225  225  LEU LEU A . n 
A 1 226  CYS 226  226  226  CYS CYS A . n 
A 1 227  ASP 227  227  227  ASP ASP A . n 
A 1 228  ASP 228  228  228  ASP ASP A . n 
A 1 229  GLU 229  229  229  GLU GLU A . n 
A 1 230  PHE 230  230  230  PHE PHE A . n 
A 1 231  ILE 231  231  231  ILE ILE A . n 
A 1 232  VAL 232  232  232  VAL VAL A . n 
A 1 233  SER 233  233  233  SER SER A . n 
A 1 234  VAL 234  234  234  VAL VAL A . n 
A 1 235  ALA 235  235  235  ALA ALA A . n 
A 1 236  SER 236  236  236  SER SER A . n 
A 1 237  TYR 237  237  237  TYR TYR A . n 
A 1 238  GLU 238  238  238  GLU GLU A . n 
A 1 239  CYS 239  239  239  CYS CYS A . n 
A 1 240  PHE 240  240  240  PHE PHE A . n 
A 1 241  ILE 241  241  241  ILE ILE A . n 
A 1 242  MET 242  242  242  MET MET A . n 
A 1 243  ILE 243  243  243  ILE ILE A . n 
A 1 244  LYS 244  244  244  LYS LYS A . n 
A 1 245  ASP 245  245  245  ASP ASP A . n 
A 1 246  VAL 246  246  246  VAL VAL A . n 
A 1 247  PHE 247  247  247  PHE PHE A . n 
A 1 248  ILE 248  248  248  ILE ILE A . n 
A 1 249  GLU 249  249  249  GLU GLU A . n 
A 1 250  ARG 250  250  250  ARG ARG A . n 
A 1 251  TYR 251  251  251  TYR TYR A . n 
A 1 252  ASN 252  252  252  ASN ASN A . n 
A 1 253  THR 253  253  253  THR THR A . n 
A 1 254  TRP 254  254  254  TRP TRP A . n 
A 1 255  GLU 255  255  255  GLU GLU A . n 
A 1 256  ILE 256  256  256  ILE ILE A . n 
A 1 257  CYS 257  257  257  CYS CYS A . n 
A 1 258  ALA 258  258  258  ALA ALA A . n 
A 1 259  ARG 259  259  259  ARG ARG A . n 
A 1 260  ALA 260  260  260  ALA ALA A . n 
A 1 261  TRP 261  261  261  TRP TRP A . n 
A 1 262  LEU 262  262  262  LEU LEU A . n 
A 1 263  GLU 263  263  263  GLU GLU A . n 
A 1 264  ASP 264  264  264  ASP ASP A . n 
A 1 265  SER 265  265  265  SER SER A . n 
A 1 266  ASP 266  266  266  ASP ASP A . n 
A 1 267  GLY 267  267  267  GLY GLY A . n 
A 1 268  ALA 268  268  268  ALA ALA A . n 
A 1 269  ASP 269  269  269  ASP ASP A . n 
A 1 270  TYR 270  270  270  TYR TYR A . n 
A 1 271  PRO 271  271  271  PRO PRO A . n 
A 1 272  PRO 272  272  272  PRO PRO A . n 
A 1 273  LEU 273  273  273  LEU LEU A . n 
A 1 274  ASP 274  274  274  ASP ASP A . n 
A 1 275  VAL 275  275  275  VAL VAL A . n 
A 1 276  LEU 276  276  276  LEU LEU A . n 
A 1 277  GLY 277  277  277  GLY GLY A . n 
A 1 278  GLU 278  278  278  GLU GLU A . n 
A 1 279  LEU 279  279  279  LEU LEU A . n 
A 1 280  TYR 280  280  280  TYR TYR A . n 
A 1 281  ASN 281  281  281  ASN ASN A . n 
A 1 282  GLN 282  282  282  GLN GLN A . n 
A 1 283  GLY 283  283  283  GLY GLY A . n 
A 1 284  ASP 284  284  284  ASP ASP A . n 
A 1 285  GLN 285  285  285  GLN GLN A . n 
A 1 286  ILE 286  286  286  ILE ILE A . n 
A 1 287  ILE 287  287  287  ILE ILE A . n 
A 1 288  ALA 288  288  288  ALA ALA A . n 
A 1 289  MET 289  289  289  MET MET A . n 
A 1 290  TYR 290  290  290  TYR TYR A . n 
A 1 291  LEU 291  291  291  LEU LEU A . n 
A 1 292  GLU 292  292  292  GLU GLU A . n 
A 1 293  ASP 293  293  293  ASP ASP A . n 
A 1 294  GLY 294  294  294  GLY GLY A . n 
A 1 295  PHE 295  295  295  PHE PHE A . n 
A 1 296  LYS 296  296  296  LYS LYS A . n 
A 1 297  LEU 297  297  297  LEU LEU A . n 
A 1 298  ILE 298  298  298  ILE ILE A . n 
A 1 299  LYS 299  299  299  LYS LYS A . n 
A 1 300  HIS 300  300  300  HIS HIS A . n 
A 1 301  LEU 301  301  301  LEU LEU A . n 
A 1 302  GLU 302  302  302  GLU GLU A . n 
A 1 303  PRO 303  303  303  PRO PRO A . n 
A 1 304  LEU 304  304  304  LEU LEU A . n 
A 1 305  CYS 305  305  305  CYS CYS A . n 
A 1 306  VAL 306  306  306  VAL VAL A . n 
A 1 307  SER 307  307  307  SER SER A . n 
A 1 308  CYS 308  308  308  CYS CYS A . n 
A 1 309  ILE 309  309  309  ILE ILE A . n 
A 1 310  GLN 310  310  310  GLN GLN A . n 
A 1 311  THR 311  311  311  THR THR A . n 
A 1 312  HIS 312  312  312  HIS HIS A . n 
A 1 313  GLY 313  313  313  GLY GLY A . n 
A 1 314  ILE 314  314  314  ILE ILE A . n 
A 1 315  PHE 315  315  315  PHE PHE A . n 
A 1 316  THR 316  316  316  THR THR A . n 
A 1 317  PRO 317  317  317  PRO PRO A . n 
A 1 318  ARG 318  318  318  ARG ARG A . n 
A 1 319  LYS 319  319  319  LYS LYS A . n 
A 1 320  TYR 320  320  320  TYR TYR A . n 
A 1 321  TRP 321  321  321  TRP TRP A . n 
A 1 322  PHE 322  322  322  PHE PHE A . n 
A 1 323  GLN 323  323  323  GLN GLN A . n 
A 1 324  SER 324  324  324  SER SER A . n 
A 1 325  GLN 325  325  325  GLN GLN A . n 
A 1 326  MET 326  326  326  MET MET A . n 
A 1 327  ILE 327  327  327  ILE ILE A . n 
A 1 328  LYS 328  328  328  LYS LYS A . n 
A 1 329  SER 329  329  329  SER SER A . n 
A 1 330  TYR 330  330  330  TYR TYR A . n 
A 1 331  TYR 331  331  331  TYR TYR A . n 
A 1 332  ASP 332  332  332  ASP ASP A . n 
A 1 333  GLU 333  333  333  GLU GLU A . n 
A 1 334  LEU 334  334  334  LEU LEU A . n 
A 1 335  HIS 335  335  335  HIS HIS A . n 
A 1 336  ASP 336  336  336  ASP ASP A . n 
A 1 337  LEU 337  337  337  LEU LEU A . n 
A 1 338  ASN 338  338  338  ASN ASN A . n 
A 1 339  LEU 339  339  339  LEU LEU A . n 
A 1 340  LYS 340  340  340  LYS LYS A . n 
A 1 341  LEU 341  341  341  LEU LEU A . n 
A 1 342  GLN 342  342  342  GLN GLN A . n 
A 1 343  ILE 343  343  343  ILE ILE A . n 
A 1 344  SER 344  344  344  SER SER A . n 
A 1 345  ASP 345  345  345  ASP ASP A . n 
A 1 346  ASN 346  346  346  ASN ASN A . n 
A 1 347  LYS 347  347  347  LYS LYS A . n 
A 1 348  ALA 348  348  348  ALA ALA A . n 
A 1 349  GLU 349  349  349  GLU GLU A . n 
A 1 350  CYS 350  350  350  CYS CYS A . n 
A 1 351  ALA 351  351  351  ALA ALA A . n 
A 1 352  GLN 352  352  352  GLN GLN A . n 
A 1 353  ASN 353  353  353  ASN ASN A . n 
A 1 354  PHE 354  354  354  PHE PHE A . n 
A 1 355  ILE 355  355  355  ILE ILE A . n 
A 1 356  LYS 356  356  356  LYS LYS A . n 
A 1 357  THR 357  357  357  THR THR A . n 
A 1 358  ILE 358  358  358  ILE ILE A . n 
A 1 359  VAL 359  359  359  VAL VAL A . n 
A 1 360  GLN 360  360  360  GLN GLN A . n 
A 1 361  ALA 361  361  361  ALA ALA A . n 
A 1 362  LYS 362  362  362  LYS LYS A . n 
A 1 363  LEU 363  363  363  LEU LEU A . n 
A 1 364  THR 364  364  364  THR THR A . n 
A 1 365  PRO 365  365  365  PRO PRO A . n 
A 1 366  GLN 366  366  366  GLN GLN A . n 
A 1 367  GLN 367  367  367  GLN GLN A . n 
A 1 368  TYR 368  368  368  TYR TYR A . n 
A 1 369  CYS 369  369  369  CYS CYS A . n 
A 1 370  GLU 370  370  370  GLU GLU A . n 
A 1 371  LEU 371  371  371  LEU LEU A . n 
A 1 372  PHE 372  372  372  PHE PHE A . n 
A 1 373  SER 373  373  373  SER SER A . n 
A 1 374  LEU 374  374  374  LEU LEU A . n 
A 1 375  GLN 375  375  375  GLN GLN A . n 
A 1 376  LYS 376  376  376  LYS LYS A . n 
A 1 377  HIS 377  377  377  HIS HIS A . n 
A 1 378  TRP 378  378  378  TRP TRP A . n 
A 1 379  GLY 379  379  379  GLY GLY A . n 
A 1 380  HIS 380  380  380  HIS HIS A . n 
A 1 381  PRO 381  381  381  PRO PRO A . n 
A 1 382  VAL 382  382  382  VAL VAL A . n 
A 1 383  LEU 383  383  383  LEU LEU A . n 
A 1 384  TYR 384  384  384  TYR TYR A . n 
A 1 385  ASN 385  385  385  ASN ASN A . n 
A 1 386  ASP 386  386  386  ASP ASP A . n 
A 1 387  VAL 387  387  387  VAL VAL A . n 
A 1 388  ALA 388  388  388  ALA ALA A . n 
A 1 389  LEU 389  389  389  LEU LEU A . n 
A 1 390  ASP 390  390  390  ASP ASP A . n 
A 1 391  LYS 391  391  391  LYS LYS A . n 
A 1 392  VAL 392  392  392  VAL VAL A . n 
A 1 393  LYS 393  393  393  LYS LYS A . n 
A 1 394  LYS 394  394  394  LYS LYS A . n 
A 1 395  HIS 395  395  395  HIS HIS A . n 
A 1 396  ALA 396  396  396  ALA ALA A . n 
A 1 397  GLN 397  397  397  GLN GLN A . n 
A 1 398  SER 398  398  398  SER SER A . n 
A 1 399  THR 399  399  399  THR THR A . n 
A 1 400  LYS 400  400  400  LYS LYS A . n 
A 1 401  ILE 401  401  401  ILE ILE A . n 
A 1 402  LEU 402  402  402  LEU LEU A . n 
A 1 403  LYS 403  403  403  LYS LYS A . n 
A 1 404  PRO 404  404  404  PRO PRO A . n 
A 1 405  LYS 405  405  405  LYS LYS A . n 
A 1 406  VAL 406  406  406  VAL VAL A . n 
A 1 407  MET 407  407  407  MET MET A . n 
A 1 408  PHE 408  408  408  PHE PHE A . n 
A 1 409  GLU 409  409  409  GLU GLU A . n 
A 1 410  THR 410  410  410  THR THR A . n 
A 1 411  PHE 411  411  411  PHE PHE A . n 
A 1 412  CYS 412  412  412  CYS CYS A . n 
A 1 413  VAL 413  413  413  VAL VAL A . n 
A 1 414  PHE 414  414  414  PHE PHE A . n 
A 1 415  LYS 415  415  415  LYS LYS A . n 
A 1 416  PHE 416  416  416  PHE PHE A . n 
A 1 417  ILE 417  417  417  ILE ILE A . n 
A 1 418  VAL 418  418  418  VAL VAL A . n 
A 1 419  ALA 419  419  419  ALA ALA A . n 
A 1 420  LYS 420  420  420  LYS LYS A . n 
A 1 421  ASN 421  421  421  ASN ASN A . n 
A 1 422  HIS 422  422  422  HIS HIS A . n 
A 1 423  TYR 423  423  423  TYR TYR A . n 
A 1 424  HIS 424  424  424  HIS HIS A . n 
A 1 425  SER 425  425  425  SER SER A . n 
A 1 426  GLN 426  426  426  GLN GLN A . n 
A 1 427  GLY 427  427  427  GLY GLY A . n 
A 1 428  SER 428  428  428  SER SER A . n 
A 1 429  TRP 429  429  429  TRP TRP A . n 
A 1 430  TYR 430  430  430  TYR TYR A . n 
A 1 431  LYS 431  431  431  LYS LYS A . n 
A 1 432  THR 432  432  432  THR THR A . n 
A 1 433  THR 433  433  433  THR THR A . n 
A 1 434  HIS 434  434  434  HIS HIS A . n 
A 1 435  ASP 435  435  435  ASP ASP A . n 
A 1 436  LEU 436  436  436  LEU LEU A . n 
A 1 437  HIS 437  437  437  HIS HIS A . n 
A 1 438  LEU 438  438  438  LEU LEU A . n 
A 1 439  THR 439  439  439  THR THR A . n 
A 1 440  PRO 440  440  440  PRO PRO A . n 
A 1 441  TYR 441  441  441  TYR TYR A . n 
A 1 442  LEU 442  442  442  LEU LEU A . n 
A 1 443  ARG 443  443  443  ARG ARG A . n 
A 1 444  GLN 444  444  444  GLN GLN A . n 
A 1 445  HIS 445  445  445  HIS HIS A . n 
A 1 446  ILE 446  446  446  ILE ILE A . n 
A 1 447  VAL 447  447  447  VAL VAL A . n 
A 1 448  SER 448  448  448  SER SER A . n 
A 1 449  ASN 449  449  449  ASN ASN A . n 
A 1 450  SER 450  450  450  SER SER A . n 
A 1 451  PHE 451  451  451  PHE PHE A . n 
A 1 452  PRO 452  452  452  PRO PRO A . n 
A 1 453  SER 453  453  453  SER SER A . n 
A 1 454  GLN 454  454  454  GLN GLN A . n 
A 1 455  ALA 455  455  455  ALA ALA A . n 
A 1 456  GLU 456  456  456  GLU GLU A . n 
A 1 457  ILE 457  457  457  ILE ILE A . n 
A 1 458  TYR 458  458  458  TYR TYR A . n 
A 1 459  GLN 459  459  459  GLN GLN A . n 
A 1 460  HIS 460  460  460  HIS HIS A . n 
A 1 461  LEU 461  461  461  LEU LEU A . n 
A 1 462  TRP 462  462  462  TRP TRP A . n 
A 1 463  GLU 463  463  463  GLU GLU A . n 
A 1 464  TRP 464  464  464  TRP TRP A . n 
A 1 465  TYR 465  465  465  TYR TYR A . n 
A 1 466  PHE 466  466  466  PHE PHE A . n 
A 1 467  VAL 467  467  467  VAL VAL A . n 
A 1 468  GLU 468  468  468  GLU GLU A . n 
A 1 469  HIS 469  469  469  HIS HIS A . n 
A 1 470  GLU 470  470  470  GLU GLU A . n 
A 1 471  PRO 471  471  471  PRO PRO A . n 
A 1 472  LEU 472  472  472  LEU LEU A . n 
A 1 473  PHE 473  473  473  PHE PHE A . n 
A 1 474  SER 474  474  474  SER SER A . n 
A 1 475  THR 475  475  475  THR THR A . n 
A 1 476  LYS 476  476  476  LYS LYS A . n 
A 1 477  ILE 477  477  477  ILE ILE A . n 
A 1 478  ILE 478  478  478  ILE ILE A . n 
A 1 479  SER 479  479  479  SER SER A . n 
A 1 480  ASP 480  480  480  ASP ASP A . n 
A 1 481  LEU 481  481  481  LEU LEU A . n 
A 1 482  SER 482  482  482  SER SER A . n 
A 1 483  ILE 483  483  483  ILE ILE A . n 
A 1 484  PHE 484  484  484  PHE PHE A . n 
A 1 485  ILE 485  485  485  ILE ILE A . n 
A 1 486  LYS 486  486  486  LYS LYS A . n 
A 1 487  ASP 487  487  487  ASP ASP A . n 
A 1 488  ARG 488  488  488  ARG ARG A . n 
A 1 489  ALA 489  489  489  ALA ALA A . n 
A 1 490  THR 490  490  490  THR THR A . n 
A 1 491  ALA 491  491  491  ALA ALA A . n 
A 1 492  VAL 492  492  492  VAL VAL A . n 
A 1 493  ASN 493  493  493  ASN ASN A . n 
A 1 494  GLN 494  494  494  GLN GLN A . n 
A 1 495  GLU 495  495  495  GLU GLU A . n 
A 1 496  CYS 496  496  496  CYS CYS A . n 
A 1 497  TRP 497  497  497  TRP TRP A . n 
A 1 498  ASP 498  498  498  ASP ASP A . n 
A 1 499  SER 499  499  499  SER SER A . n 
A 1 500  VAL 500  500  500  VAL VAL A . n 
A 1 501  PHE 501  501  501  PHE PHE A . n 
A 1 502  ASP 502  502  502  ASP ASP A . n 
A 1 503  ARG 503  503  503  ARG ARG A . n 
A 1 504  SER 504  504  504  SER SER A . n 
A 1 505  VAL 505  505  505  VAL VAL A . n 
A 1 506  LEU 506  506  506  LEU LEU A . n 
A 1 507  GLY 507  507  507  GLY GLY A . n 
A 1 508  TYR 508  508  508  TYR TYR A . n 
A 1 509  ASN 509  509  509  ASN ASN A . n 
A 1 510  PRO 510  510  510  PRO PRO A . n 
A 1 511  PRO 511  511  511  PRO PRO A . n 
A 1 512  VAL 512  512  512  VAL VAL A . n 
A 1 513  ARG 513  513  513  ARG ARG A . n 
A 1 514  PHE 514  514  514  PHE PHE A . n 
A 1 515  GLN 515  515  515  GLN GLN A . n 
A 1 516  SER 516  516  516  SER SER A . n 
A 1 517  LYS 517  517  517  LYS LYS A . n 
A 1 518  ARG 518  518  518  ARG ARG A . n 
A 1 519  VAL 519  519  519  VAL VAL A . n 
A 1 520  PRO 520  520  520  PRO PRO A . n 
A 1 521  GLU 521  521  521  GLU GLU A . n 
A 1 522  GLN 522  522  522  GLN GLN A . n 
A 1 523  PHE 523  523  523  PHE PHE A . n 
A 1 524  LEU 524  524  524  LEU LEU A . n 
A 1 525  GLY 525  525  525  GLY GLY A . n 
A 1 526  GLN 526  526  526  GLN GLN A . n 
A 1 527  ALA 527  527  527  ALA ALA A . n 
A 1 528  ASP 528  528  528  ASP ASP A . n 
A 1 529  PHE 529  529  529  PHE PHE A . n 
A 1 530  SER 530  530  530  SER SER A . n 
A 1 531  LEU 531  531  531  LEU LEU A . n 
A 1 532  ASN 532  532  532  ASN ASN A . n 
A 1 533  GLN 533  533  533  GLN GLN A . n 
A 1 534  ILE 534  534  534  ILE ILE A . n 
A 1 535  LEU 535  535  535  LEU LEU A . n 
A 1 536  GLU 536  536  536  GLU GLU A . n 
A 1 537  PHE 537  537  537  PHE PHE A . n 
A 1 538  ALA 538  538  538  ALA ALA A . n 
A 1 539  GLU 539  539  539  GLU GLU A . n 
A 1 540  LYS 540  540  540  LYS LYS A . n 
A 1 541  LEU 541  541  541  LEU LEU A . n 
A 1 542  GLU 542  542  542  GLU GLU A . n 
A 1 543  TYR 543  543  543  TYR TYR A . n 
A 1 544  LEU 544  544  544  LEU LEU A . n 
A 1 545  ALA 545  545  545  ALA ALA A . n 
A 1 546  PRO 546  546  546  PRO PRO A . n 
A 1 547  SER 547  547  547  SER SER A . n 
A 1 548  TYR 548  548  548  TYR TYR A . n 
A 1 549  ARG 549  549  549  ARG ARG A . n 
A 1 550  ASN 550  550  550  ASN ASN A . n 
A 1 551  PHE 551  551  551  PHE PHE A . n 
A 1 552  SER 552  552  552  SER SER A . n 
A 1 553  PHE 553  553  553  PHE PHE A . n 
A 1 554  SER 554  554  554  SER SER A . n 
A 1 555  LEU 555  555  555  LEU LEU A . n 
A 1 556  LYS 556  556  556  LYS LYS A . n 
A 1 557  GLU 557  557  557  GLU GLU A . n 
A 1 558  LYS 558  558  558  LYS LYS A . n 
A 1 559  GLU 559  559  559  GLU GLU A . n 
A 1 560  LEU 560  560  560  LEU LEU A . n 
A 1 561  ASN 561  561  561  ASN ASN A . n 
A 1 562  ILE 562  562  562  ILE ILE A . n 
A 1 563  GLY 563  563  563  GLY GLY A . n 
A 1 564  ARG 564  564  564  ARG ARG A . n 
A 1 565  THR 565  565  565  THR THR A . n 
A 1 566  PHE 566  566  566  PHE PHE A . n 
A 1 567  GLY 567  567  567  GLY GLY A . n 
A 1 568  LYS 568  568  568  LYS LYS A . n 
A 1 569  LEU 569  569  569  LEU LEU A . n 
A 1 570  PRO 570  570  570  PRO PRO A . n 
A 1 571  TYR 571  571  571  TYR TYR A . n 
A 1 572  ARG 572  572  572  ARG ARG A . n 
A 1 573  VAL 573  573  573  VAL VAL A . n 
A 1 574  ARG 574  574  574  ARG ARG A . n 
A 1 575  ASN 575  575  575  ASN ASN A . n 
A 1 576  VAL 576  576  576  VAL VAL A . n 
A 1 577  GLN 577  577  577  GLN GLN A . n 
A 1 578  THR 578  578  578  THR THR A . n 
A 1 579  LEU 579  579  579  LEU LEU A . n 
A 1 580  ALA 580  580  580  ALA ALA A . n 
A 1 581  GLU 581  581  581  GLU GLU A . n 
A 1 582  ALA 582  582  582  ALA ALA A . n 
A 1 583  LEU 583  583  583  LEU LEU A . n 
A 1 584  LEU 584  584  584  LEU LEU A . n 
A 1 585  ALA 585  585  585  ALA ALA A . n 
A 1 586  ASP 586  586  586  ASP ASP A . n 
A 1 587  GLY 587  587  587  GLY GLY A . n 
A 1 588  LEU 588  588  588  LEU LEU A . n 
A 1 589  ALA 589  589  589  ALA ALA A . n 
A 1 590  LYS 590  590  590  LYS LYS A . n 
A 1 591  ALA 591  591  591  ALA ALA A . n 
A 1 592  PHE 592  592  592  PHE PHE A . n 
A 1 593  PRO 593  593  593  PRO PRO A . n 
A 1 594  SER 594  594  594  SER SER A . n 
A 1 595  ASN 595  595  595  ASN ASN A . n 
A 1 596  MET 596  596  596  MET MET A . n 
A 1 597  MET 597  597  597  MET MET A . n 
A 1 598  VAL 598  598  598  VAL VAL A . n 
A 1 599  VAL 599  599  599  VAL VAL A . n 
A 1 600  THR 600  600  600  THR THR A . n 
A 1 601  GLU 601  601  601  GLU GLU A . n 
A 1 602  ARG 602  602  602  ARG ARG A . n 
A 1 603  GLU 603  603  603  GLU GLU A . n 
A 1 604  GLN 604  604  604  GLN GLN A . n 
A 1 605  LYS 605  605  605  LYS LYS A . n 
A 1 606  GLU 606  606  606  GLU GLU A . n 
A 1 607  ALA 607  607  607  ALA ALA A . n 
A 1 608  LEU 608  608  608  LEU LEU A . n 
A 1 609  LEU 609  609  609  LEU LEU A . n 
A 1 610  HIS 610  610  610  HIS HIS A . n 
A 1 611  GLN 611  611  611  GLN GLN A . n 
A 1 612  ALA 612  612  612  ALA ALA A . n 
A 1 613  SER 613  613  613  SER SER A . n 
A 1 614  TRP 614  614  614  TRP TRP A . n 
A 1 615  HIS 615  615  615  HIS HIS A . n 
A 1 616  HIS 616  616  616  HIS HIS A . n 
A 1 617  ASN 617  617  ?    ?   ?   A . n 
A 1 618  SER 618  618  ?    ?   ?   A . n 
A 1 619  ALA 619  619  ?    ?   ?   A . n 
A 1 620  SER 620  620  ?    ?   ?   A . n 
A 1 621  ILE 621  621  ?    ?   ?   A . n 
A 1 622  GLY 622  622  ?    ?   ?   A . n 
A 1 623  GLU 623  623  623  GLU GLU A . n 
A 1 624  ASN 624  624  624  ASN ASN A . n 
A 1 625  ALA 625  625  625  ALA ALA A . n 
A 1 626  ILE 626  626  626  ILE ILE A . n 
A 1 627  VAL 627  627  627  VAL VAL A . n 
A 1 628  ARG 628  628  628  ARG ARG A . n 
A 1 629  GLY 629  629  629  GLY GLY A . n 
A 1 630  ALA 630  630  630  ALA ALA A . n 
A 1 631  SER 631  631  631  SER SER A . n 
A 1 632  PHE 632  632  632  PHE PHE A . n 
A 1 633  VAL 633  633  633  VAL VAL A . n 
A 1 634  THR 634  634  634  THR THR A . n 
A 1 635  ASP 635  635  635  ASP ASP A . n 
A 1 636  LEU 636  636  636  LEU LEU A . n 
A 1 637  GLU 637  637  637  GLU GLU A . n 
A 1 638  LYS 638  638  638  LYS LYS A . n 
A 1 639  TYR 639  639  639  TYR TYR A . n 
A 1 640  ASN 640  640  640  ASN ASN A . n 
A 1 641  LEU 641  641  641  LEU LEU A . n 
A 1 642  ALA 642  642  642  ALA ALA A . n 
A 1 643  PHE 643  643  643  PHE PHE A . n 
A 1 644  ARG 644  644  644  ARG ARG A . n 
A 1 645  TYR 645  645  645  TYR TYR A . n 
A 1 646  GLU 646  646  646  GLU GLU A . n 
A 1 647  PHE 647  647  647  PHE PHE A . n 
A 1 648  THR 648  648  648  THR THR A . n 
A 1 649  ARG 649  649  649  ARG ARG A . n 
A 1 650  HIS 650  650  650  HIS HIS A . n 
A 1 651  PHE 651  651  651  PHE PHE A . n 
A 1 652  ILE 652  652  652  ILE ILE A . n 
A 1 653  ASP 653  653  653  ASP ASP A . n 
A 1 654  TYR 654  654  654  TYR TYR A . n 
A 1 655  CYS 655  655  655  CYS CYS A . n 
A 1 656  ASN 656  656  656  ASN ASN A . n 
A 1 657  ARG 657  657  657  ARG ARG A . n 
A 1 658  CYS 658  658  658  CYS CYS A . n 
A 1 659  TYR 659  659  659  TYR TYR A . n 
A 1 660  GLY 660  660  660  GLY GLY A . n 
A 1 661  VAL 661  661  661  VAL VAL A . n 
A 1 662  LYS 662  662  662  LYS LYS A . n 
A 1 663  ASN 663  663  663  ASN ASN A . n 
A 1 664  LEU 664  664  664  LEU LEU A . n 
A 1 665  PHE 665  665  665  PHE PHE A . n 
A 1 666  ASP 666  666  666  ASP ASP A . n 
A 1 667  TRP 667  667  667  TRP TRP A . n 
A 1 668  MET 668  668  668  MET MET A . n 
A 1 669  HIS 669  669  669  HIS HIS A . n 
A 1 670  PHE 670  670  670  PHE PHE A . n 
A 1 671  LEU 671  671  671  LEU LEU A . n 
A 1 672  ILE 672  672  672  ILE ILE A . n 
A 1 673  PRO 673  673  673  PRO PRO A . n 
A 1 674  LEU 674  674  674  LEU LEU A . n 
A 1 675  CYS 675  675  675  CYS CYS A . n 
A 1 676  TYR 676  676  676  TYR TYR A . n 
A 1 677  MET 677  677  677  MET MET A . n 
A 1 678  HIS 678  678  678  HIS HIS A . n 
A 1 679  VAL 679  679  679  VAL VAL A . n 
A 1 680  SER 680  680  680  SER SER A . n 
A 1 681  ASP 681  681  681  ASP ASP A . n 
A 1 682  PHE 682  682  682  PHE PHE A . n 
A 1 683  TYR 683  683  683  TYR TYR A . n 
A 1 684  SER 684  684  684  SER SER A . n 
A 1 685  PRO 685  685  685  PRO PRO A . n 
A 1 686  PRO 686  686  686  PRO PRO A . n 
A 1 687  HIS 687  687  687  HIS HIS A . n 
A 1 688  CYS 688  688  688  CYS CYS A . n 
A 1 689  VAL 689  689  689  VAL VAL A . n 
A 1 690  THR 690  690  690  THR THR A . n 
A 1 691  GLU 691  691  691  GLU GLU A . n 
A 1 692  ASP 692  692  692  ASP ASP A . n 
A 1 693  ASN 693  693  693  ASN ASN A . n 
A 1 694  ARG 694  694  694  ARG ARG A . n 
A 1 695  ASN 695  695  695  ASN ASN A . n 
A 1 696  ASN 696  696  696  ASN ASN A . n 
A 1 697  PRO 697  697  697  PRO PRO A . n 
A 1 698  PRO 698  698  698  PRO PRO A . n 
A 1 699  ASP 699  699  699  ASP ASP A . n 
A 1 700  CYS 700  700  700  CYS CYS A . n 
A 1 701  ALA 701  701  701  ALA ALA A . n 
A 1 702  ASN 702  702  702  ASN ASN A . n 
A 1 703  ALA 703  703  703  ALA ALA A . n 
A 1 704  TYR 704  704  704  TYR TYR A . n 
A 1 705  HIS 705  705  705  HIS HIS A . n 
A 1 706  TYR 706  706  706  TYR TYR A . n 
A 1 707  HIS 707  707  707  HIS HIS A . n 
A 1 708  LEU 708  708  708  LEU LEU A . n 
A 1 709  GLY 709  709  709  GLY GLY A . n 
A 1 710  GLY 710  710  710  GLY GLY A . n 
A 1 711  ILE 711  711  711  ILE ILE A . n 
A 1 712  GLU 712  712  712  GLU GLU A . n 
A 1 713  GLY 713  713  713  GLY GLY A . n 
A 1 714  LEU 714  714  714  LEU LEU A . n 
A 1 715  GLN 715  715  715  GLN GLN A . n 
A 1 716  GLN 716  716  716  GLN GLN A . n 
A 1 717  LYS 717  717  717  LYS LYS A . n 
A 1 718  LEU 718  718  718  LEU LEU A . n 
A 1 719  TRP 719  719  719  TRP TRP A . n 
A 1 720  THR 720  720  720  THR THR A . n 
A 1 721  CYS 721  721  721  CYS CYS A . n 
A 1 722  ILE 722  722  722  ILE ILE A . n 
A 1 723  SER 723  723  723  SER SER A . n 
A 1 724  CYS 724  724  724  CYS CYS A . n 
A 1 725  ALA 725  725  725  ALA ALA A . n 
A 1 726  GLN 726  726  726  GLN GLN A . n 
A 1 727  ILE 727  727  727  ILE ILE A . n 
A 1 728  THR 728  728  728  THR THR A . n 
A 1 729  LEU 729  729  729  LEU LEU A . n 
A 1 730  VAL 730  730  730  VAL VAL A . n 
A 1 731  GLU 731  731  731  GLU GLU A . n 
A 1 732  LEU 732  732  732  LEU LEU A . n 
A 1 733  LYS 733  733  733  LYS LYS A . n 
A 1 734  THR 734  734  734  THR THR A . n 
A 1 735  LYS 735  735  735  LYS LYS A . n 
A 1 736  LEU 736  736  736  LEU LEU A . n 
A 1 737  LYS 737  737  737  LYS LYS A . n 
A 1 738  LEU 738  738  738  LEU LEU A . n 
A 1 739  LYS 739  739  739  LYS LYS A . n 
A 1 740  SER 740  740  740  SER SER A . n 
A 1 741  SER 741  741  741  SER SER A . n 
A 1 742  VAL 742  742  742  VAL VAL A . n 
A 1 743  MET 743  743  743  MET MET A . n 
A 1 744  GLY 744  744  744  GLY GLY A . n 
A 1 745  ASP 745  745  745  ASP ASP A . n 
A 1 746  ASN 746  746  746  ASN ASN A . n 
A 1 747  GLN 747  747  747  GLN GLN A . n 
A 1 748  CYS 748  748  748  CYS CYS A . n 
A 1 749  ILE 749  749  749  ILE ILE A . n 
A 1 750  THR 750  750  750  THR THR A . n 
A 1 751  THR 751  751  751  THR THR A . n 
A 1 752  LEU 752  752  752  LEU LEU A . n 
A 1 753  SER 753  753  753  SER SER A . n 
A 1 754  LEU 754  754  754  LEU LEU A . n 
A 1 755  PHE 755  755  755  PHE PHE A . n 
A 1 756  PRO 756  756  756  PRO PRO A . n 
A 1 757  ILE 757  757  757  ILE ILE A . n 
A 1 758  ASP 758  758  758  ASP ASP A . n 
A 1 759  ALA 759  759  759  ALA ALA A . n 
A 1 760  PRO 760  760  760  PRO PRO A . n 
A 1 761  ASN 761  761  761  ASN ASN A . n 
A 1 762  ASP 762  762  762  ASP ASP A . n 
A 1 763  TYR 763  763  763  TYR TYR A . n 
A 1 764  GLN 764  764  764  GLN GLN A . n 
A 1 765  GLU 765  765  765  GLU GLU A . n 
A 1 766  ASN 766  766  766  ASN ASN A . n 
A 1 767  GLU 767  767  767  GLU GLU A . n 
A 1 768  ALA 768  768  768  ALA ALA A . n 
A 1 769  GLU 769  769  769  GLU GLU A . n 
A 1 770  LEU 770  770  770  LEU LEU A . n 
A 1 771  ASN 771  771  771  ASN ASN A . n 
A 1 772  ALA 772  772  772  ALA ALA A . n 
A 1 773  ALA 773  773  773  ALA ALA A . n 
A 1 774  ARG 774  774  774  ARG ARG A . n 
A 1 775  VAL 775  775  775  VAL VAL A . n 
A 1 776  ALA 776  776  776  ALA ALA A . n 
A 1 777  VAL 777  777  777  VAL VAL A . n 
A 1 778  GLU 778  778  778  GLU GLU A . n 
A 1 779  LEU 779  779  779  LEU LEU A . n 
A 1 780  ALA 780  780  780  ALA ALA A . n 
A 1 781  ILE 781  781  781  ILE ILE A . n 
A 1 782  THR 782  782  782  THR THR A . n 
A 1 783  THR 783  783  783  THR THR A . n 
A 1 784  GLY 784  784  784  GLY GLY A . n 
A 1 785  TYR 785  785  785  TYR TYR A . n 
A 1 786  SER 786  786  786  SER SER A . n 
A 1 787  GLY 787  787  787  GLY GLY A . n 
A 1 788  ILE 788  788  788  ILE ILE A . n 
A 1 789  PHE 789  789  789  PHE PHE A . n 
A 1 790  LEU 790  790  790  LEU LEU A . n 
A 1 791  LYS 791  791  791  LYS LYS A . n 
A 1 792  PRO 792  792  792  PRO PRO A . n 
A 1 793  GLU 793  793  793  GLU GLU A . n 
A 1 794  GLU 794  794  794  GLU GLU A . n 
A 1 795  THR 795  795  795  THR THR A . n 
A 1 796  PHE 796  796  796  PHE PHE A . n 
A 1 797  VAL 797  797  797  VAL VAL A . n 
A 1 798  HIS 798  798  798  HIS HIS A . n 
A 1 799  SER 799  799  799  SER SER A . n 
A 1 800  GLY 800  800  800  GLY GLY A . n 
A 1 801  PHE 801  801  801  PHE PHE A . n 
A 1 802  ILE 802  802  802  ILE ILE A . n 
A 1 803  TYR 803  803  803  TYR TYR A . n 
A 1 804  PHE 804  804  804  PHE PHE A . n 
A 1 805  GLY 805  805  805  GLY GLY A . n 
A 1 806  LYS 806  806  806  LYS LYS A . n 
A 1 807  LYS 807  807  807  LYS LYS A . n 
A 1 808  GLN 808  808  808  GLN GLN A . n 
A 1 809  TYR 809  809  809  TYR TYR A . n 
A 1 810  LEU 810  810  810  LEU LEU A . n 
A 1 811  ASN 811  811  811  ASN ASN A . n 
A 1 812  GLY 812  812  812  GLY GLY A . n 
A 1 813  VAL 813  813  813  VAL VAL A . n 
A 1 814  GLN 814  814  814  GLN GLN A . n 
A 1 815  LEU 815  815  815  LEU LEU A . n 
A 1 816  PRO 816  816  816  PRO PRO A . n 
A 1 817  GLN 817  817  817  GLN GLN A . n 
A 1 818  SER 818  818  818  SER SER A . n 
A 1 819  LEU 819  819  819  LEU LEU A . n 
A 1 820  LYS 820  820  820  LYS LYS A . n 
A 1 821  THR 821  821  821  THR THR A . n 
A 1 822  MET 822  822  822  MET MET A . n 
A 1 823  ALA 823  823  823  ALA ALA A . n 
A 1 824  ARG 824  824  824  ARG ARG A . n 
A 1 825  CYS 825  825  825  CYS CYS A . n 
A 1 826  GLY 826  826  826  GLY GLY A . n 
A 1 827  PRO 827  827  827  PRO PRO A . n 
A 1 828  LEU 828  828  828  LEU LEU A . n 
A 1 829  SER 829  829  829  SER SER A . n 
A 1 830  ASP 830  830  830  ASP ASP A . n 
A 1 831  SER 831  831  831  SER SER A . n 
A 1 832  ILE 832  832  832  ILE ILE A . n 
A 1 833  PHE 833  833  833  PHE PHE A . n 
A 1 834  ASP 834  834  834  ASP ASP A . n 
A 1 835  ASP 835  835  835  ASP ASP A . n 
A 1 836  LEU 836  836  836  LEU LEU A . n 
A 1 837  GLN 837  837  837  GLN GLN A . n 
A 1 838  GLY 838  838  838  GLY GLY A . n 
A 1 839  SER 839  839  839  SER SER A . n 
A 1 840  LEU 840  840  840  LEU LEU A . n 
A 1 841  ALA 841  841  841  ALA ALA A . n 
A 1 842  SER 842  842  842  SER SER A . n 
A 1 843  ILE 843  843  843  ILE ILE A . n 
A 1 844  GLY 844  844  844  GLY GLY A . n 
A 1 845  THR 845  845  845  THR THR A . n 
A 1 846  SER 846  846  846  SER SER A . n 
A 1 847  PHE 847  847  847  PHE PHE A . n 
A 1 848  GLU 848  848  848  GLU GLU A . n 
A 1 849  ARG 849  849  849  ARG ARG A . n 
A 1 850  GLY 850  850  850  GLY GLY A . n 
A 1 851  THR 851  851  851  THR THR A . n 
A 1 852  SER 852  852  852  SER SER A . n 
A 1 853  GLU 853  853  853  GLU GLU A . n 
A 1 854  THR 854  854  854  THR THR A . n 
A 1 855  ARG 855  855  855  ARG ARG A . n 
A 1 856  HIS 856  856  856  HIS HIS A . n 
A 1 857  ILE 857  857  857  ILE ILE A . n 
A 1 858  PHE 858  858  858  PHE PHE A . n 
A 1 859  PRO 859  859  859  PRO PRO A . n 
A 1 860  SER 860  860  860  SER SER A . n 
A 1 861  ARG 861  861  861  ARG ARG A . n 
A 1 862  TRP 862  862  862  TRP TRP A . n 
A 1 863  ILE 863  863  863  ILE ILE A . n 
A 1 864  ALA 864  864  864  ALA ALA A . n 
A 1 865  SER 865  865  865  SER SER A . n 
A 1 866  PHE 866  866  866  PHE PHE A . n 
A 1 867  HIS 867  867  867  HIS HIS A . n 
A 1 868  SER 868  868  868  SER SER A . n 
A 1 869  MET 869  869  869  MET MET A . n 
A 1 870  LEU 870  870  870  LEU LEU A . n 
A 1 871  ALA 871  871  871  ALA ALA A . n 
A 1 872  ILE 872  872  872  ILE ILE A . n 
A 1 873  ASN 873  873  873  ASN ASN A . n 
A 1 874  LEU 874  874  874  LEU LEU A . n 
A 1 875  LEU 875  875  875  LEU LEU A . n 
A 1 876  ASN 876  876  876  ASN ASN A . n 
A 1 877  GLN 877  877  877  GLN GLN A . n 
A 1 878  ASN 878  878  878  ASN ASN A . n 
A 1 879  HIS 879  879  879  HIS HIS A . n 
A 1 880  LEU 880  880  880  LEU LEU A . n 
A 1 881  GLY 881  881  881  GLY GLY A . n 
A 1 882  PHE 882  882  882  PHE PHE A . n 
A 1 883  PRO 883  883  883  PRO PRO A . n 
A 1 884  LEU 884  884  884  LEU LEU A . n 
A 1 885  GLY 885  885  885  GLY GLY A . n 
A 1 886  PHE 886  886  886  PHE PHE A . n 
A 1 887  ASN 887  887  887  ASN ASN A . n 
A 1 888  ILE 888  888  888  ILE ILE A . n 
A 1 889  ASP 889  889  889  ASP ASP A . n 
A 1 890  ILE 890  890  890  ILE ILE A . n 
A 1 891  SER 891  891  891  SER SER A . n 
A 1 892  CYS 892  892  892  CYS CYS A . n 
A 1 893  PHE 893  893  893  PHE PHE A . n 
A 1 894  LYS 894  894  894  LYS LYS A . n 
A 1 895  LYS 895  895  895  LYS LYS A . n 
A 1 896  PRO 896  896  896  PRO PRO A . n 
A 1 897  LEU 897  897  897  LEU LEU A . n 
A 1 898  THR 898  898  898  THR THR A . n 
A 1 899  PHE 899  899  899  PHE PHE A . n 
A 1 900  SER 900  900  900  SER SER A . n 
A 1 901  GLU 901  901  901  GLU GLU A . n 
A 1 902  LYS 902  902  902  LYS LYS A . n 
A 1 903  LEU 903  903  903  LEU LEU A . n 
A 1 904  ILE 904  904  904  ILE ILE A . n 
A 1 905  ALA 905  905  905  ALA ALA A . n 
A 1 906  LEU 906  906  906  LEU LEU A . n 
A 1 907  ILE 907  907  907  ILE ILE A . n 
A 1 908  THR 908  908  908  THR THR A . n 
A 1 909  PRO 909  909  909  PRO PRO A . n 
A 1 910  GLN 910  910  910  GLN GLN A . n 
A 1 911  VAL 911  911  911  VAL VAL A . n 
A 1 912  LEU 912  912  912  LEU LEU A . n 
A 1 913  GLY 913  913  913  GLY GLY A . n 
A 1 914  GLY 914  914  914  GLY GLY A . n 
A 1 915  LEU 915  915  915  LEU LEU A . n 
A 1 916  SER 916  916  916  SER SER A . n 
A 1 917  PHE 917  917  917  PHE PHE A . n 
A 1 918  LEU 918  918  918  LEU LEU A . n 
A 1 919  ASN 919  919  919  ASN ASN A . n 
A 1 920  PRO 920  920  920  PRO PRO A . n 
A 1 921  GLU 921  921  921  GLU GLU A . n 
A 1 922  LYS 922  922  922  LYS LYS A . n 
A 1 923  LEU 923  923  923  LEU LEU A . n 
A 1 924  PHE 924  924  924  PHE PHE A . n 
A 1 925  TYR 925  925  925  TYR TYR A . n 
A 1 926  ARG 926  926  926  ARG ARG A . n 
A 1 927  ASN 927  927  927  ASN ASN A . n 
A 1 928  ILE 928  928  928  ILE ILE A . n 
A 1 929  SER 929  929  929  SER SER A . n 
A 1 930  ASP 930  930  930  ASP ASP A . n 
A 1 931  PRO 931  931  931  PRO PRO A . n 
A 1 932  LEU 932  932  932  LEU LEU A . n 
A 1 933  THR 933  933  933  THR THR A . n 
A 1 934  SER 934  934  934  SER SER A . n 
A 1 935  GLY 935  935  935  GLY GLY A . n 
A 1 936  LEU 936  936  936  LEU LEU A . n 
A 1 937  PHE 937  937  937  PHE PHE A . n 
A 1 938  GLN 938  938  938  GLN GLN A . n 
A 1 939  LEU 939  939  939  LEU LEU A . n 
A 1 940  LYS 940  940  940  LYS LYS A . n 
A 1 941  ASN 941  941  941  ASN ASN A . n 
A 1 942  ALA 942  942  942  ALA ALA A . n 
A 1 943  LEU 943  943  943  LEU LEU A . n 
A 1 944  GLU 944  944  944  GLU GLU A . n 
A 1 945  PHE 945  945  945  PHE PHE A . n 
A 1 946  LEU 946  946  946  LEU LEU A . n 
A 1 947  GLU 947  947  947  GLU GLU A . n 
A 1 948  LYS 948  948  948  LYS LYS A . n 
A 1 949  GLU 949  949  949  GLU GLU A . n 
A 1 950  GLU 950  950  950  GLU GLU A . n 
A 1 951  LEU 951  951  951  LEU LEU A . n 
A 1 952  PHE 952  952  952  PHE PHE A . n 
A 1 953  TYR 953  953  953  TYR TYR A . n 
A 1 954  ILE 954  954  954  ILE ILE A . n 
A 1 955  LEU 955  955  955  LEU LEU A . n 
A 1 956  ILE 956  956  956  ILE ILE A . n 
A 1 957  SER 957  957  957  SER SER A . n 
A 1 958  LYS 958  958  958  LYS LYS A . n 
A 1 959  LYS 959  959  959  LYS LYS A . n 
A 1 960  PRO 960  960  960  PRO PRO A . n 
A 1 961  GLY 961  961  961  GLY GLY A . n 
A 1 962  LEU 962  962  962  LEU LEU A . n 
A 1 963  ALA 963  963  963  ALA ALA A . n 
A 1 964  ASP 964  964  964  ASP ASP A . n 
A 1 965  ALA 965  965  965  ALA ALA A . n 
A 1 966  SER 966  966  966  SER SER A . n 
A 1 967  ASP 967  967  967  ASP ASP A . n 
A 1 968  PHE 968  968  968  PHE PHE A . n 
A 1 969  VAL 969  969  969  VAL VAL A . n 
A 1 970  MET 970  970  970  MET MET A . n 
A 1 971  ASN 971  971  971  ASN ASN A . n 
A 1 972  PRO 972  972  972  PRO PRO A . n 
A 1 973  LEU 973  973  973  LEU LEU A . n 
A 1 974  GLY 974  974  974  GLY GLY A . n 
A 1 975  LEU 975  975  975  LEU LEU A . n 
A 1 976  ASN 976  976  976  ASN ASN A . n 
A 1 977  VAL 977  977  977  VAL VAL A . n 
A 1 978  PRO 978  978  978  PRO PRO A . n 
A 1 979  GLY 979  979  979  GLY GLY A . n 
A 1 980  SER 980  980  980  SER SER A . n 
A 1 981  LYS 981  981  981  LYS LYS A . n 
A 1 982  GLU 982  982  982  GLU GLU A . n 
A 1 983  ILE 983  983  983  ILE ILE A . n 
A 1 984  ILE 984  984  984  ILE ILE A . n 
A 1 985  THR 985  985  985  THR THR A . n 
A 1 986  PHE 986  986  986  PHE PHE A . n 
A 1 987  LEU 987  987  987  LEU LEU A . n 
A 1 988  ARG 988  988  988  ARG ARG A . n 
A 1 989  GLN 989  989  989  GLN GLN A . n 
A 1 990  THR 990  990  990  THR THR A . n 
A 1 991  VAL 991  991  991  VAL VAL A . n 
A 1 992  ARG 992  992  992  ARG ARG A . n 
A 1 993  GLU 993  993  993  GLU GLU A . n 
A 1 994  ASN 994  994  994  ASN ASN A . n 
A 1 995  ILE 995  995  995  ILE ILE A . n 
A 1 996  THR 996  996  996  THR THR A . n 
A 1 997  ILE 997  997  997  ILE ILE A . n 
A 1 998  THR 998  998  998  THR THR A . n 
A 1 999  SER 999  999  999  SER SER A . n 
A 1 1000 GLN 1000 1000 1000 GLN GLN A . n 
A 1 1001 ASN 1001 1001 1001 ASN ASN A . n 
A 1 1002 ARG 1002 1002 1002 ARG ARG A . n 
A 1 1003 ILE 1003 1003 1003 ILE ILE A . n 
A 1 1004 ILE 1004 1004 1004 ILE ILE A . n 
A 1 1005 ASN 1005 1005 1005 ASN ASN A . n 
A 1 1006 SER 1006 1006 1006 SER SER A . n 
A 1 1007 LEU 1007 1007 1007 LEU LEU A . n 
A 1 1008 PHE 1008 1008 1008 PHE PHE A . n 
A 1 1009 HIS 1009 1009 1009 HIS HIS A . n 
A 1 1010 ILE 1010 1010 1010 ILE ILE A . n 
A 1 1011 GLY 1011 1011 1011 GLY GLY A . n 
A 1 1012 SER 1012 1012 1012 SER SER A . n 
A 1 1013 ASP 1013 1013 1013 ASP ASP A . n 
A 1 1014 LEU 1014 1014 1014 LEU LEU A . n 
A 1 1015 GLU 1015 1015 1015 GLU GLU A . n 
A 1 1016 ASP 1016 1016 1016 ASP ASP A . n 
A 1 1017 GLN 1017 1017 1017 GLN GLN A . n 
A 1 1018 ARG 1018 1018 1018 ARG ARG A . n 
A 1 1019 VAL 1019 1019 1019 VAL VAL A . n 
A 1 1020 CYS 1020 1020 1020 CYS CYS A . n 
A 1 1021 GLU 1021 1021 1021 GLU GLU A . n 
A 1 1022 TRP 1022 1022 1022 TRP TRP A . n 
A 1 1023 LEU 1023 1023 1023 LEU LEU A . n 
A 1 1024 LEU 1024 1024 1024 LEU LEU A . n 
A 1 1025 SER 1025 1025 1025 SER SER A . n 
A 1 1026 SER 1026 1026 1026 SER SER A . n 
A 1 1027 ASN 1027 1027 1027 ASN ASN A . n 
A 1 1028 PRO 1028 1028 1028 PRO PRO A . n 
A 1 1029 VAL 1029 1029 1029 VAL VAL A . n 
A 1 1030 MET 1030 1030 1030 MET MET A . n 
A 1 1031 SER 1031 1031 1031 SER SER A . n 
A 1 1032 ARG 1032 1032 1032 ARG ARG A . n 
A 1 1033 PHE 1033 1033 1033 PHE PHE A . n 
A 1 1034 ALA 1034 1034 1034 ALA ALA A . n 
A 1 1035 ALA 1035 1035 1035 ALA ALA A . n 
A 1 1036 ASP 1036 1036 1036 ASP ASP A . n 
A 1 1037 ILE 1037 1037 1037 ILE ILE A . n 
A 1 1038 PHE 1038 1038 1038 PHE PHE A . n 
A 1 1039 SER 1039 1039 1039 SER SER A . n 
A 1 1040 ARG 1040 1040 1040 ARG ARG A . n 
A 1 1041 THR 1041 1041 1041 THR THR A . n 
A 1 1042 PRO 1042 1042 1042 PRO PRO A . n 
A 1 1043 SER 1043 1043 1043 SER SER A . n 
A 1 1044 GLY 1044 1044 1044 GLY GLY A . n 
A 1 1045 LYS 1045 1045 1045 LYS LYS A . n 
A 1 1046 ARG 1046 1046 1046 ARG ARG A . n 
A 1 1047 LEU 1047 1047 1047 LEU LEU A . n 
A 1 1048 GLN 1048 1048 1048 GLN GLN A . n 
A 1 1049 VAL 1049 1049 1049 VAL VAL A . n 
A 1 1050 LEU 1050 1050 1050 LEU LEU A . n 
A 1 1051 GLY 1051 1051 1051 GLY GLY A . n 
A 1 1052 TYR 1052 1052 1052 TYR TYR A . n 
A 1 1053 LEU 1053 1053 1053 LEU LEU A . n 
A 1 1054 GLU 1054 1054 1054 GLU GLU A . n 
A 1 1055 GLY 1055 1055 1055 GLY GLY A . n 
A 1 1056 THR 1056 1056 1056 THR THR A . n 
A 1 1057 ARG 1057 1057 1057 ARG ARG A . n 
A 1 1058 THR 1058 1058 1058 THR THR A . n 
A 1 1059 LEU 1059 1059 1059 LEU LEU A . n 
A 1 1060 LEU 1060 1060 1060 LEU LEU A . n 
A 1 1061 ALA 1061 1061 1061 ALA ALA A . n 
A 1 1062 SER 1062 1062 1062 SER SER A . n 
A 1 1063 ARG 1063 1063 ?    ?   ?   A . n 
A 1 1064 THR 1064 1064 ?    ?   ?   A . n 
A 1 1065 ILE 1065 1065 ?    ?   ?   A . n 
A 1 1066 SER 1066 1066 ?    ?   ?   A . n 
A 1 1067 LEU 1067 1067 ?    ?   ?   A . n 
A 1 1068 THR 1068 1068 ?    ?   ?   A . n 
A 1 1069 THR 1069 1069 ?    ?   ?   A . n 
A 1 1070 GLU 1070 1070 ?    ?   ?   A . n 
A 1 1071 GLY 1071 1071 1071 GLY GLY A . n 
A 1 1072 THR 1072 1072 1072 THR THR A . n 
A 1 1073 MET 1073 1073 1073 MET MET A . n 
A 1 1074 LEU 1074 1074 1074 LEU LEU A . n 
A 1 1075 MET 1075 1075 1075 MET MET A . n 
A 1 1076 LYS 1076 1076 1076 LYS LYS A . n 
A 1 1077 LEU 1077 1077 1077 LEU LEU A . n 
A 1 1078 ARG 1078 1078 1078 ARG ARG A . n 
A 1 1079 GLU 1079 1079 1079 GLU GLU A . n 
A 1 1080 LEU 1080 1080 1080 LEU LEU A . n 
A 1 1081 THR 1081 1081 1081 THR THR A . n 
A 1 1082 ARG 1082 1082 1082 ARG ARG A . n 
A 1 1083 ASN 1083 1083 1083 ASN ASN A . n 
A 1 1084 ARG 1084 1084 1084 ARG ARG A . n 
A 1 1085 TRP 1085 1085 1085 TRP TRP A . n 
A 1 1086 LYS 1086 1086 1086 LYS LYS A . n 
A 1 1087 SER 1087 1087 1087 SER SER A . n 
A 1 1088 TRP 1088 1088 1088 TRP TRP A . n 
A 1 1089 PHE 1089 1089 1089 PHE PHE A . n 
A 1 1090 SER 1090 1090 1090 SER SER A . n 
A 1 1091 TYR 1091 1091 1091 TYR TYR A . n 
A 1 1092 ILE 1092 1092 1092 ILE ILE A . n 
A 1 1093 ASP 1093 1093 1093 ASP ASP A . n 
A 1 1094 ALA 1094 1094 1094 ALA ALA A . n 
A 1 1095 LEU 1095 1095 1095 LEU LEU A . n 
A 1 1096 ASP 1096 1096 1096 ASP ASP A . n 
A 1 1097 ASP 1097 1097 1097 ASP ASP A . n 
A 1 1098 ASP 1098 1098 1098 ASP ASP A . n 
A 1 1099 LEU 1099 1099 1099 LEU LEU A . n 
A 1 1100 SER 1100 1100 1100 SER SER A . n 
A 1 1101 GLU 1101 1101 1101 GLU GLU A . n 
A 1 1102 SER 1102 1102 1102 SER SER A . n 
A 1 1103 LEU 1103 1103 1103 LEU LEU A . n 
A 1 1104 GLU 1104 1104 1104 GLU GLU A . n 
A 1 1105 LYS 1105 1105 1105 LYS LYS A . n 
A 1 1106 PHE 1106 1106 1106 PHE PHE A . n 
A 1 1107 THR 1107 1107 1107 THR THR A . n 
A 1 1108 CYS 1108 1108 1108 CYS CYS A . n 
A 1 1109 THR 1109 1109 1109 THR THR A . n 
A 1 1110 VAL 1110 1110 1110 VAL VAL A . n 
A 1 1111 ASP 1111 1111 1111 ASP ASP A . n 
A 1 1112 VAL 1112 1112 1112 VAL VAL A . n 
A 1 1113 ALA 1113 1113 1113 ALA ALA A . n 
A 1 1114 ASN 1114 1114 1114 ASN ASN A . n 
A 1 1115 PHE 1115 1115 1115 PHE PHE A . n 
A 1 1116 LEU 1116 1116 1116 LEU LEU A . n 
A 1 1117 ARG 1117 1117 1117 ARG ARG A . n 
A 1 1118 ALA 1118 1118 1118 ALA ALA A . n 
A 1 1119 TYR 1119 1119 1119 TYR TYR A . n 
A 1 1120 SER 1120 1120 1120 SER SER A . n 
A 1 1121 TRP 1121 1121 1121 TRP TRP A . n 
A 1 1122 SER 1122 1122 1122 SER SER A . n 
A 1 1123 ASP 1123 1123 1123 ASP ASP A . n 
A 1 1124 VAL 1124 1124 1124 VAL VAL A . n 
A 1 1125 LEU 1125 1125 1125 LEU LEU A . n 
A 1 1126 LYS 1126 1126 1126 LYS LYS A . n 
A 1 1127 GLY 1127 1127 1127 GLY GLY A . n 
A 1 1128 LYS 1128 1128 1128 LYS LYS A . n 
A 1 1129 ARG 1129 1129 1129 ARG ARG A . n 
A 1 1130 LEU 1130 1130 1130 LEU LEU A . n 
A 1 1131 ILE 1131 1131 1131 ILE ILE A . n 
A 1 1132 GLY 1132 1132 1132 GLY GLY A . n 
A 1 1133 ALA 1133 1133 1133 ALA ALA A . n 
A 1 1134 THR 1134 1134 1134 THR THR A . n 
A 1 1135 LEU 1135 1135 1135 LEU LEU A . n 
A 1 1136 PRO 1136 1136 1136 PRO PRO A . n 
A 1 1137 CYS 1137 1137 1137 CYS CYS A . n 
A 1 1138 LEU 1138 1138 1138 LEU LEU A . n 
A 1 1139 LEU 1139 1139 1139 LEU LEU A . n 
A 1 1140 GLU 1140 1140 1140 GLU GLU A . n 
A 1 1141 GLN 1141 1141 1141 GLN GLN A . n 
A 1 1142 PHE 1142 1142 1142 PHE PHE A . n 
A 1 1143 GLU 1143 1143 1143 GLU GLU A . n 
A 1 1144 VAL 1144 1144 1144 VAL VAL A . n 
A 1 1145 LYS 1145 1145 1145 LYS LYS A . n 
A 1 1146 TRP 1146 1146 1146 TRP TRP A . n 
A 1 1147 ILE 1147 1147 1147 ILE ILE A . n 
A 1 1148 ASN 1148 1148 1148 ASN ASN A . n 
A 1 1149 LEU 1149 1149 1149 LEU LEU A . n 
A 1 1150 SER 1150 1150 1150 SER SER A . n 
A 1 1151 GLU 1151 1151 1151 GLU GLU A . n 
A 1 1152 ASP 1152 1152 1152 ASP ASP A . n 
A 1 1153 LEU 1153 1153 1153 LEU LEU A . n 
A 1 1154 ARG 1154 1154 1154 ARG ARG A . n 
A 1 1155 GLU 1155 1155 1155 GLU GLU A . n 
A 1 1156 GLN 1156 1156 1156 GLN GLN A . n 
A 1 1157 PHE 1157 1157 1157 PHE PHE A . n 
A 1 1158 ASN 1158 1158 1158 ASN ASN A . n 
A 1 1159 LEU 1159 1159 1159 LEU LEU A . n 
A 1 1160 SER 1160 1160 1160 SER SER A . n 
A 1 1161 SER 1161 1161 1161 SER SER A . n 
A 1 1162 ASP 1162 1162 ?    ?   ?   A . n 
A 1 1163 SER 1163 1163 ?    ?   ?   A . n 
A 1 1164 LYS 1164 1164 ?    ?   ?   A . n 
A 1 1165 SER 1165 1165 ?    ?   ?   A . n 
A 1 1166 THR 1166 1166 ?    ?   ?   A . n 
A 1 1167 ILE 1167 1167 ?    ?   ?   A . n 
A 1 1168 ASN 1168 1168 ?    ?   ?   A . n 
A 1 1169 LEU 1169 1169 ?    ?   ?   A . n 
A 1 1170 LEU 1170 1170 ?    ?   ?   A . n 
A 1 1171 PRO 1171 1171 ?    ?   ?   A . n 
A 1 1172 TYR 1172 1172 ?    ?   ?   A . n 
A 1 1173 ASP 1173 1173 ?    ?   ?   A . n 
A 1 1174 CYS 1174 1174 ?    ?   ?   A . n 
A 1 1175 LYS 1175 1175 ?    ?   ?   A . n 
A 1 1176 GLU 1176 1176 ?    ?   ?   A . n 
A 1 1177 LEU 1177 1177 ?    ?   ?   A . n 
A 1 1178 ARG 1178 1178 ?    ?   ?   A . n 
A 1 1179 LEU 1179 1179 ?    ?   ?   A . n 
A 1 1180 GLU 1180 1180 ?    ?   ?   A . n 
A 1 1181 GLY 1181 1181 ?    ?   ?   A . n 
A 1 1182 SER 1182 1182 ?    ?   ?   A . n 
A 1 1183 ASN 1183 1183 ?    ?   ?   A . n 
A 1 1184 ASP 1184 1184 ?    ?   ?   A . n 
A 1 1185 THR 1185 1185 ?    ?   ?   A . n 
A 1 1186 GLU 1186 1186 ?    ?   ?   A . n 
A 1 1187 LEU 1187 1187 1187 LEU LEU A . n 
A 1 1188 ASN 1188 1188 1188 ASN ASN A . n 
A 1 1189 TYR 1189 1189 1189 TYR TYR A . n 
A 1 1190 VAL 1190 1190 1190 VAL VAL A . n 
A 1 1191 SER 1191 1191 1191 SER SER A . n 
A 1 1192 CYS 1192 1192 1192 CYS CYS A . n 
A 1 1193 ALA 1193 1193 1193 ALA ALA A . n 
A 1 1194 LEU 1194 1194 1194 LEU LEU A . n 
A 1 1195 ASP 1195 1195 1195 ASP ASP A . n 
A 1 1196 ARG 1196 1196 1196 ARG ARG A . n 
A 1 1197 LYS 1197 1197 1197 LYS LYS A . n 
A 1 1198 VAL 1198 1198 1198 VAL VAL A . n 
A 1 1199 VAL 1199 1199 1199 VAL VAL A . n 
A 1 1200 GLN 1200 1200 1200 GLN GLN A . n 
A 1 1201 LYS 1201 1201 1201 LYS LYS A . n 
A 1 1202 HIS 1202 1202 1202 HIS HIS A . n 
A 1 1203 PRO 1203 1203 1203 PRO PRO A . n 
A 1 1204 SER 1204 1204 1204 SER SER A . n 
A 1 1205 VAL 1205 1205 1205 VAL VAL A . n 
A 1 1206 ASN 1206 1206 1206 ASN ASN A . n 
A 1 1207 ARG 1207 1207 1207 ARG ARG A . n 
A 1 1208 LEU 1208 1208 1208 LEU LEU A . n 
A 1 1209 ALA 1209 1209 1209 ALA ALA A . n 
A 1 1210 TRP 1210 1210 1210 TRP TRP A . n 
A 1 1211 THR 1211 1211 1211 THR THR A . n 
A 1 1212 ILE 1212 1212 1212 ILE ILE A . n 
A 1 1213 GLY 1213 1213 1213 GLY GLY A . n 
A 1 1214 ASN 1214 1214 1214 ASN ASN A . n 
A 1 1215 ARG 1215 1215 1215 ARG ARG A . n 
A 1 1216 ALA 1216 1216 1216 ALA ALA A . n 
A 1 1217 PRO 1217 1217 1217 PRO PRO A . n 
A 1 1218 TYR 1218 1218 1218 TYR TYR A . n 
A 1 1219 ILE 1219 1219 1219 ILE ILE A . n 
A 1 1220 GLY 1220 1220 1220 GLY GLY A . n 
A 1 1221 SER 1221 1221 1221 SER SER A . n 
A 1 1222 ARG 1222 1222 ?    ?   ?   A . n 
A 1 1223 THR 1223 1223 ?    ?   ?   A . n 
A 1 1224 GLU 1224 1224 ?    ?   ?   A . n 
A 1 1225 ASP 1225 1225 ?    ?   ?   A . n 
A 1 1226 LYS 1226 1226 ?    ?   ?   A . n 
A 1 1227 ILE 1227 1227 ?    ?   ?   A . n 
A 1 1228 GLY 1228 1228 ?    ?   ?   A . n 
A 1 1229 TYR 1229 1229 ?    ?   ?   A . n 
A 1 1230 PRO 1230 1230 1230 PRO PRO A . n 
A 1 1231 PRO 1231 1231 1231 PRO PRO A . n 
A 1 1232 LEU 1232 1232 1232 LEU LEU A . n 
A 1 1233 ARG 1233 1233 1233 ARG ARG A . n 
A 1 1234 VAL 1234 1234 1234 VAL VAL A . n 
A 1 1235 ASN 1235 1235 1235 ASN ASN A . n 
A 1 1236 CYS 1236 1236 1236 CYS CYS A . n 
A 1 1237 PRO 1237 1237 1237 PRO PRO A . n 
A 1 1238 SER 1238 1238 1238 SER SER A . n 
A 1 1239 ALA 1239 1239 1239 ALA ALA A . n 
A 1 1240 ALA 1240 1240 1240 ALA ALA A . n 
A 1 1241 LEU 1241 1241 1241 LEU LEU A . n 
A 1 1242 LYS 1242 1242 1242 LYS LYS A . n 
A 1 1243 GLU 1243 1243 1243 GLU GLU A . n 
A 1 1244 ALA 1244 1244 1244 ALA ALA A . n 
A 1 1245 ILE 1245 1245 1245 ILE ILE A . n 
A 1 1246 GLU 1246 1246 1246 GLU GLU A . n 
A 1 1247 MET 1247 1247 1247 MET MET A . n 
A 1 1248 VAL 1248 1248 1248 VAL VAL A . n 
A 1 1249 SER 1249 1249 1249 SER SER A . n 
A 1 1250 ARG 1250 1250 1250 ARG ARG A . n 
A 1 1251 LEU 1251 1251 1251 LEU LEU A . n 
A 1 1252 LEU 1252 1252 1252 LEU LEU A . n 
A 1 1253 TRP 1253 1253 1253 TRP TRP A . n 
A 1 1254 VAL 1254 1254 1254 VAL VAL A . n 
A 1 1255 THR 1255 1255 1255 THR THR A . n 
A 1 1256 GLN 1256 1256 1256 GLN GLN A . n 
A 1 1257 GLY 1257 1257 1257 GLY GLY A . n 
A 1 1258 THR 1258 1258 1258 THR THR A . n 
A 1 1259 ALA 1259 1259 1259 ALA ALA A . n 
A 1 1260 ASP 1260 1260 1260 ASP ASP A . n 
A 1 1261 ARG 1261 1261 1261 ARG ARG A . n 
A 1 1262 GLU 1262 1262 1262 GLU GLU A . n 
A 1 1263 LYS 1263 1263 1263 LYS LYS A . n 
A 1 1264 LEU 1264 1264 1264 LEU LEU A . n 
A 1 1265 LEU 1265 1265 1265 LEU LEU A . n 
A 1 1266 ILE 1266 1266 1266 ILE ILE A . n 
A 1 1267 PRO 1267 1267 1267 PRO PRO A . n 
A 1 1268 LEU 1268 1268 1268 LEU LEU A . n 
A 1 1269 LEU 1269 1269 1269 LEU LEU A . n 
A 1 1270 ASN 1270 1270 1270 ASN ASN A . n 
A 1 1271 SER 1271 1271 1271 SER SER A . n 
A 1 1272 ARG 1272 1272 1272 ARG ARG A . n 
A 1 1273 VAL 1273 1273 1273 VAL VAL A . n 
A 1 1274 ASN 1274 1274 1274 ASN ASN A . n 
A 1 1275 LEU 1275 1275 1275 LEU LEU A . n 
A 1 1276 ASP 1276 1276 1276 ASP ASP A . n 
A 1 1277 TYR 1277 1277 1277 TYR TYR A . n 
A 1 1278 GLN 1278 1278 1278 GLN GLN A . n 
A 1 1279 THR 1279 1279 1279 THR THR A . n 
A 1 1280 VAL 1280 1280 1280 VAL VAL A . n 
A 1 1281 LEU 1281 1281 1281 LEU LEU A . n 
A 1 1282 ASN 1282 1282 1282 ASN ASN A . n 
A 1 1283 PHE 1283 1283 1283 PHE PHE A . n 
A 1 1284 LEU 1284 1284 1284 LEU LEU A . n 
A 1 1285 PRO 1285 1285 1285 PRO PRO A . n 
A 1 1286 THR 1286 1286 1286 THR THR A . n 
A 1 1287 HIS 1287 1287 1287 HIS HIS A . n 
A 1 1288 TYR 1288 1288 1288 TYR TYR A . n 
A 1 1289 SER 1289 1289 1289 SER SER A . n 
A 1 1290 GLY 1290 1290 1290 GLY GLY A . n 
A 1 1291 ASN 1291 1291 1291 ASN ASN A . n 
A 1 1292 ILE 1292 1292 1292 ILE ILE A . n 
A 1 1293 VAL 1293 1293 1293 VAL VAL A . n 
A 1 1294 HIS 1294 1294 1294 HIS HIS A . n 
A 1 1295 ARG 1295 1295 1295 ARG ARG A . n 
A 1 1296 TYR 1296 1296 1296 TYR TYR A . n 
A 1 1297 ASN 1297 1297 1297 ASN ASN A . n 
A 1 1298 ASP 1298 1298 1298 ASP ASP A . n 
A 1 1299 GLN 1299 1299 1299 GLN GLN A . n 
A 1 1300 TYR 1300 1300 1300 TYR TYR A . n 
A 1 1301 GLY 1301 1301 1301 GLY GLY A . n 
A 1 1302 GLN 1302 1302 1302 GLN GLN A . n 
A 1 1303 HIS 1303 1303 1303 HIS HIS A . n 
A 1 1304 SER 1304 1304 1304 SER SER A . n 
A 1 1305 PHE 1305 1305 1305 PHE PHE A . n 
A 1 1306 MET 1306 1306 1306 MET MET A . n 
A 1 1307 ALA 1307 1307 1307 ALA ALA A . n 
A 1 1308 ASN 1308 1308 1308 ASN ASN A . n 
A 1 1309 ARG 1309 1309 1309 ARG ARG A . n 
A 1 1310 MET 1310 1310 1310 MET MET A . n 
A 1 1311 SER 1311 1311 1311 SER SER A . n 
A 1 1312 ASN 1312 1312 1312 ASN ASN A . n 
A 1 1313 THR 1313 1313 1313 THR THR A . n 
A 1 1314 SER 1314 1314 1314 SER SER A . n 
A 1 1315 THR 1315 1315 1315 THR THR A . n 
A 1 1316 ARG 1316 1316 1316 ARG ARG A . n 
A 1 1317 ALA 1317 1317 1317 ALA ALA A . n 
A 1 1318 ILE 1318 1318 1318 ILE ILE A . n 
A 1 1319 ILE 1319 1319 1319 ILE ILE A . n 
A 1 1320 SER 1320 1320 1320 SER SER A . n 
A 1 1321 THR 1321 1321 1321 THR THR A . n 
A 1 1322 ASN 1322 1322 1322 ASN ASN A . n 
A 1 1323 THR 1323 1323 1323 THR THR A . n 
A 1 1324 LEU 1324 1324 1324 LEU LEU A . n 
A 1 1325 GLY 1325 1325 1325 GLY GLY A . n 
A 1 1326 LYS 1326 1326 1326 LYS LYS A . n 
A 1 1327 TYR 1327 1327 1327 TYR TYR A . n 
A 1 1328 ALA 1328 1328 1328 ALA ALA A . n 
A 1 1329 GLY 1329 1329 ?    ?   ?   A . n 
A 1 1330 GLY 1330 1330 ?    ?   ?   A . n 
A 1 1331 GLY 1331 1331 1331 GLY GLY A . n 
A 1 1332 GLN 1332 1332 1332 GLN GLN A . n 
A 1 1333 ALA 1333 1333 1333 ALA ALA A . n 
A 1 1334 ALA 1334 1334 1334 ALA ALA A . n 
A 1 1335 ILE 1335 1335 1335 ILE ILE A . n 
A 1 1336 ASP 1336 1336 1336 ASP ASP A . n 
A 1 1337 SER 1337 1337 1337 SER SER A . n 
A 1 1338 ASN 1338 1338 1338 ASN ASN A . n 
A 1 1339 ILE 1339 1339 1339 ILE ILE A . n 
A 1 1340 ILE 1340 1340 1340 ILE ILE A . n 
A 1 1341 PHE 1341 1341 1341 PHE PHE A . n 
A 1 1342 GLN 1342 1342 1342 GLN GLN A . n 
A 1 1343 ASN 1343 1343 1343 ASN ASN A . n 
A 1 1344 THR 1344 1344 1344 THR THR A . n 
A 1 1345 ILE 1345 1345 1345 ILE ILE A . n 
A 1 1346 ASN 1346 1346 1346 ASN ASN A . n 
A 1 1347 LEU 1347 1347 1347 LEU LEU A . n 
A 1 1348 GLY 1348 1348 1348 GLY GLY A . n 
A 1 1349 VAL 1349 1349 1349 VAL VAL A . n 
A 1 1350 ALA 1350 1350 1350 ALA ALA A . n 
A 1 1351 VAL 1351 1351 1351 VAL VAL A . n 
A 1 1352 LEU 1352 1352 1352 LEU LEU A . n 
A 1 1353 ASP 1353 1353 1353 ASP ASP A . n 
A 1 1354 ILE 1354 1354 1354 ILE ILE A . n 
A 1 1355 ALA 1355 1355 1355 ALA ALA A . n 
A 1 1356 LEU 1356 1356 1356 LEU LEU A . n 
A 1 1357 SER 1357 1357 1357 SER SER A . n 
A 1 1358 LEU 1358 1358 1358 LEU LEU A . n 
A 1 1359 ALA 1359 1359 1359 ALA ALA A . n 
A 1 1360 LYS 1360 1360 1360 LYS LYS A . n 
A 1 1361 LEU 1361 1361 1361 LEU LEU A . n 
A 1 1362 SER 1362 1362 1362 SER SER A . n 
A 1 1363 SER 1363 1363 1363 SER SER A . n 
A 1 1364 ALA 1364 1364 1364 ALA ALA A . n 
A 1 1365 SER 1365 1365 1365 SER SER A . n 
A 1 1366 ASN 1366 1366 1366 ASN ASN A . n 
A 1 1367 VAL 1367 1367 1367 VAL VAL A . n 
A 1 1368 THR 1368 1368 1368 THR THR A . n 
A 1 1369 PHE 1369 1369 1369 PHE PHE A . n 
A 1 1370 ARG 1370 1370 1370 ARG ARG A . n 
A 1 1371 LEU 1371 1371 1371 LEU LEU A . n 
A 1 1372 MET 1372 1372 1372 MET MET A . n 
A 1 1373 LEU 1373 1373 1373 LEU LEU A . n 
A 1 1374 ASN 1374 1374 1374 ASN ASN A . n 
A 1 1375 LYS 1375 1375 1375 LYS LYS A . n 
A 1 1376 CYS 1376 1376 1376 CYS CYS A . n 
A 1 1377 CYS 1377 1377 1377 CYS CYS A . n 
A 1 1378 THR 1378 1378 1378 THR THR A . n 
A 1 1379 ARG 1379 1379 1379 ARG ARG A . n 
A 1 1380 HIS 1380 1380 1380 HIS HIS A . n 
A 1 1381 VAL 1381 1381 1381 VAL VAL A . n 
A 1 1382 PRO 1382 1382 1382 PRO PRO A . n 
A 1 1383 SER 1383 1383 1383 SER SER A . n 
A 1 1384 GLU 1384 1384 1384 GLU GLU A . n 
A 1 1385 TYR 1385 1385 1385 TYR TYR A . n 
A 1 1386 LEU 1386 1386 1386 LEU LEU A . n 
A 1 1387 TYR 1387 1387 1387 TYR TYR A . n 
A 1 1388 PHE 1388 1388 1388 PHE PHE A . n 
A 1 1389 ASP 1389 1389 1389 ASP ASP A . n 
A 1 1390 LYS 1390 1390 1390 LYS LYS A . n 
A 1 1391 PRO 1391 1391 1391 PRO PRO A . n 
A 1 1392 LEU 1392 1392 1392 LEU LEU A . n 
A 1 1393 ASP 1393 1393 1393 ASP ASP A . n 
A 1 1394 VAL 1394 1394 1394 VAL VAL A . n 
A 1 1395 ASP 1395 1395 1395 ASP ASP A . n 
A 1 1396 LEU 1396 1396 1396 LEU LEU A . n 
A 1 1397 ASN 1397 1397 1397 ASN ASN A . n 
A 1 1398 LYS 1398 1398 1398 LYS LYS A . n 
A 1 1399 TYR 1399 1399 1399 TYR TYR A . n 
A 1 1400 MET 1400 1400 1400 MET MET A . n 
A 1 1401 ASP 1401 1401 1401 ASP ASP A . n 
A 1 1402 ASN 1402 1402 1402 ASN ASN A . n 
A 1 1403 GLU 1403 1403 1403 GLU GLU A . n 
A 1 1404 LEU 1404 1404 1404 LEU LEU A . n 
A 1 1405 VAL 1405 1405 1405 VAL VAL A . n 
A 1 1406 TYR 1406 1406 1406 TYR TYR A . n 
A 1 1407 ASP 1407 1407 1407 ASP ASP A . n 
A 1 1408 ASN 1408 1408 1408 ASN ASN A . n 
A 1 1409 ASP 1409 1409 1409 ASP ASP A . n 
A 1 1410 PRO 1410 1410 1410 PRO PRO A . n 
A 1 1411 LEU 1411 1411 1411 LEU LEU A . n 
A 1 1412 CYS 1412 1412 1412 CYS CYS A . n 
A 1 1413 SER 1413 1413 1413 SER SER A . n 
A 1 1414 GLY 1414 1414 1414 GLY GLY A . n 
A 1 1415 ILE 1415 1415 1415 ILE ILE A . n 
A 1 1416 LYS 1416 1416 1416 LYS LYS A . n 
A 1 1417 GLY 1417 1417 ?    ?   ?   A . n 
A 1 1418 ARG 1418 1418 ?    ?   ?   A . n 
A 1 1419 LEU 1419 1419 ?    ?   ?   A . n 
A 1 1420 GLY 1420 1420 ?    ?   ?   A . n 
A 1 1421 ARG 1421 1421 ?    ?   ?   A . n 
A 1 1422 VAL 1422 1422 ?    ?   ?   A . n 
A 1 1423 SER 1423 1423 ?    ?   ?   A . n 
A 1 1424 ARG 1424 1424 ?    ?   ?   A . n 
A 1 1425 SER 1425 1425 ?    ?   ?   A . n 
A 1 1426 SER 1426 1426 ?    ?   ?   A . n 
A 1 1427 ARG 1427 1427 ?    ?   ?   A . n 
A 1 1428 GLU 1428 1428 ?    ?   ?   A . n 
A 1 1429 ASN 1429 1429 ?    ?   ?   A . n 
A 1 1430 LEU 1430 1430 ?    ?   ?   A . n 
A 1 1431 TYR 1431 1431 ?    ?   ?   A . n 
A 1 1432 PHE 1432 1432 ?    ?   ?   A . n 
A 1 1433 GLN 1433 1433 ?    ?   ?   A . n 
A 1 1434 GLY 1434 1434 ?    ?   ?   A . n 
A 1 1435 SER 1435 1435 ?    ?   ?   A . n 
A 1 1436 GLY 1436 1436 ?    ?   ?   A . n 
A 1 1437 TRP 1437 1437 ?    ?   ?   A . n 
A 1 1438 SER 1438 1438 ?    ?   ?   A . n 
A 1 1439 HIS 1439 1439 ?    ?   ?   A . n 
A 1 1440 PRO 1440 1440 ?    ?   ?   A . n 
A 1 1441 GLN 1441 1441 ?    ?   ?   A . n 
A 1 1442 PHE 1442 1442 ?    ?   ?   A . n 
A 1 1443 GLU 1443 1443 ?    ?   ?   A . n 
A 1 1444 LYS 1444 1444 ?    ?   ?   A . n 
A 1 1445 GLY 1445 1445 ?    ?   ?   A . n 
A 1 1446 GLY 1446 1446 ?    ?   ?   A . n 
A 1 1447 GLY 1447 1447 ?    ?   ?   A . n 
A 1 1448 SER 1448 1448 ?    ?   ?   A . n 
A 1 1449 GLY 1449 1449 ?    ?   ?   A . n 
A 1 1450 GLY 1450 1450 ?    ?   ?   A . n 
A 1 1451 GLY 1451 1451 ?    ?   ?   A . n 
A 1 1452 SER 1452 1452 ?    ?   ?   A . n 
A 1 1453 GLY 1453 1453 ?    ?   ?   A . n 
A 1 1454 GLY 1454 1454 ?    ?   ?   A . n 
A 1 1455 SER 1455 1455 ?    ?   ?   A . n 
A 1 1456 ALA 1456 1456 ?    ?   ?   A . n 
A 1 1457 TRP 1457 1457 ?    ?   ?   A . n 
A 1 1458 SER 1458 1458 ?    ?   ?   A . n 
A 1 1459 HIS 1459 1459 ?    ?   ?   A . n 
A 1 1460 PRO 1460 1460 ?    ?   ?   A . n 
A 1 1461 GLN 1461 1461 ?    ?   ?   A . n 
A 1 1462 PHE 1462 1462 ?    ?   ?   A . n 
A 1 1463 GLU 1463 1463 ?    ?   ?   A . n 
A 1 1464 LYS 1464 1464 ?    ?   ?   A . n 
A 1 1465 GLY 1465 1465 ?    ?   ?   A . n 
A 1 1466 SER 1466 1466 ?    ?   ?   A . n 
A 1 1467 ALA 1467 1467 ?    ?   ?   A . n 
A 1 1468 SER 1468 1468 ?    ?   ?   A . n 
A 1 1469 HIS 1469 1469 ?    ?   ?   A . n 
A 1 1470 HIS 1470 1470 ?    ?   ?   A . n 
A 1 1471 HIS 1471 1471 ?    ?   ?   A . n 
A 1 1472 HIS 1472 1472 ?    ?   ?   A . n 
A 1 1473 HIS 1473 1473 ?    ?   ?   A . n 
A 1 1474 HIS 1474 1474 ?    ?   ?   A . n 
A 1 1475 GLY 1475 1475 ?    ?   ?   A . n 
A 1 1476 THR 1476 1476 ?    ?   ?   A . n 
A 1 1477 LYS 1477 1477 ?    ?   ?   A . n 
A 1 1478 THR 1478 1478 ?    ?   ?   A . n 
A 1 1479 GLU 1479 1479 ?    ?   ?   A . n 
A 1 1480 GLU 1480 1480 ?    ?   ?   A . n 
A 1 1481 GLY 1481 1481 ?    ?   ?   A . n 
A 1 1482 LYS 1482 1482 ?    ?   ?   A . n 
A 1 1483 LEU 1483 1483 ?    ?   ?   A . n 
A 1 1484 VAL 1484 1484 ?    ?   ?   A . n 
A 1 1485 ILE 1485 1485 ?    ?   ?   A . n 
A 1 1486 TRP 1486 1486 ?    ?   ?   A . n 
A 1 1487 ILE 1487 1487 ?    ?   ?   A . n 
A 1 1488 ASN 1488 1488 ?    ?   ?   A . n 
A 1 1489 GLY 1489 1489 ?    ?   ?   A . n 
A 1 1490 ASP 1490 1490 ?    ?   ?   A . n 
A 1 1491 LYS 1491 1491 ?    ?   ?   A . n 
A 1 1492 GLY 1492 1492 ?    ?   ?   A . n 
A 1 1493 TYR 1493 1493 ?    ?   ?   A . n 
A 1 1494 ASN 1494 1494 ?    ?   ?   A . n 
A 1 1495 GLY 1495 1495 ?    ?   ?   A . n 
A 1 1496 LEU 1496 1496 ?    ?   ?   A . n 
A 1 1497 ALA 1497 1497 ?    ?   ?   A . n 
A 1 1498 GLU 1498 1498 ?    ?   ?   A . n 
A 1 1499 VAL 1499 1499 ?    ?   ?   A . n 
A 1 1500 GLY 1500 1500 ?    ?   ?   A . n 
A 1 1501 LYS 1501 1501 ?    ?   ?   A . n 
A 1 1502 LYS 1502 1502 ?    ?   ?   A . n 
A 1 1503 PHE 1503 1503 ?    ?   ?   A . n 
A 1 1504 GLU 1504 1504 ?    ?   ?   A . n 
A 1 1505 LYS 1505 1505 ?    ?   ?   A . n 
A 1 1506 ASP 1506 1506 ?    ?   ?   A . n 
A 1 1507 THR 1507 1507 ?    ?   ?   A . n 
A 1 1508 GLY 1508 1508 ?    ?   ?   A . n 
A 1 1509 ILE 1509 1509 ?    ?   ?   A . n 
A 1 1510 LYS 1510 1510 ?    ?   ?   A . n 
A 1 1511 VAL 1511 1511 ?    ?   ?   A . n 
A 1 1512 THR 1512 1512 ?    ?   ?   A . n 
A 1 1513 VAL 1513 1513 ?    ?   ?   A . n 
A 1 1514 GLU 1514 1514 ?    ?   ?   A . n 
A 1 1515 HIS 1515 1515 ?    ?   ?   A . n 
A 1 1516 PRO 1516 1516 ?    ?   ?   A . n 
A 1 1517 ASP 1517 1517 ?    ?   ?   A . n 
A 1 1518 LYS 1518 1518 ?    ?   ?   A . n 
A 1 1519 LEU 1519 1519 ?    ?   ?   A . n 
A 1 1520 GLU 1520 1520 ?    ?   ?   A . n 
A 1 1521 GLU 1521 1521 ?    ?   ?   A . n 
A 1 1522 LYS 1522 1522 ?    ?   ?   A . n 
A 1 1523 PHE 1523 1523 ?    ?   ?   A . n 
A 1 1524 PRO 1524 1524 ?    ?   ?   A . n 
A 1 1525 GLN 1525 1525 ?    ?   ?   A . n 
A 1 1526 VAL 1526 1526 ?    ?   ?   A . n 
A 1 1527 ALA 1527 1527 ?    ?   ?   A . n 
A 1 1528 ALA 1528 1528 ?    ?   ?   A . n 
A 1 1529 THR 1529 1529 ?    ?   ?   A . n 
A 1 1530 GLY 1530 1530 ?    ?   ?   A . n 
A 1 1531 ASP 1531 1531 ?    ?   ?   A . n 
A 1 1532 GLY 1532 1532 ?    ?   ?   A . n 
A 1 1533 PRO 1533 1533 ?    ?   ?   A . n 
A 1 1534 ASP 1534 1534 ?    ?   ?   A . n 
A 1 1535 ILE 1535 1535 ?    ?   ?   A . n 
A 1 1536 ILE 1536 1536 ?    ?   ?   A . n 
A 1 1537 PHE 1537 1537 ?    ?   ?   A . n 
A 1 1538 TRP 1538 1538 ?    ?   ?   A . n 
A 1 1539 ALA 1539 1539 ?    ?   ?   A . n 
A 1 1540 HIS 1540 1540 ?    ?   ?   A . n 
A 1 1541 ASP 1541 1541 ?    ?   ?   A . n 
A 1 1542 ARG 1542 1542 ?    ?   ?   A . n 
A 1 1543 PHE 1543 1543 ?    ?   ?   A . n 
A 1 1544 GLY 1544 1544 ?    ?   ?   A . n 
A 1 1545 GLY 1545 1545 ?    ?   ?   A . n 
A 1 1546 TYR 1546 1546 ?    ?   ?   A . n 
A 1 1547 ALA 1547 1547 ?    ?   ?   A . n 
A 1 1548 GLN 1548 1548 ?    ?   ?   A . n 
A 1 1549 SER 1549 1549 ?    ?   ?   A . n 
A 1 1550 GLY 1550 1550 ?    ?   ?   A . n 
A 1 1551 LEU 1551 1551 ?    ?   ?   A . n 
A 1 1552 LEU 1552 1552 ?    ?   ?   A . n 
A 1 1553 ALA 1553 1553 ?    ?   ?   A . n 
A 1 1554 GLU 1554 1554 ?    ?   ?   A . n 
A 1 1555 ILE 1555 1555 ?    ?   ?   A . n 
A 1 1556 THR 1556 1556 ?    ?   ?   A . n 
A 1 1557 PRO 1557 1557 ?    ?   ?   A . n 
A 1 1558 ASP 1558 1558 ?    ?   ?   A . n 
A 1 1559 LYS 1559 1559 ?    ?   ?   A . n 
A 1 1560 ALA 1560 1560 ?    ?   ?   A . n 
A 1 1561 PHE 1561 1561 ?    ?   ?   A . n 
A 1 1562 GLN 1562 1562 ?    ?   ?   A . n 
A 1 1563 ASP 1563 1563 ?    ?   ?   A . n 
A 1 1564 LYS 1564 1564 ?    ?   ?   A . n 
A 1 1565 LEU 1565 1565 ?    ?   ?   A . n 
A 1 1566 TYR 1566 1566 ?    ?   ?   A . n 
A 1 1567 PRO 1567 1567 ?    ?   ?   A . n 
A 1 1568 PHE 1568 1568 ?    ?   ?   A . n 
A 1 1569 THR 1569 1569 ?    ?   ?   A . n 
A 1 1570 TRP 1570 1570 ?    ?   ?   A . n 
A 1 1571 ASP 1571 1571 ?    ?   ?   A . n 
A 1 1572 ALA 1572 1572 ?    ?   ?   A . n 
A 1 1573 VAL 1573 1573 ?    ?   ?   A . n 
A 1 1574 ARG 1574 1574 ?    ?   ?   A . n 
A 1 1575 TYR 1575 1575 ?    ?   ?   A . n 
A 1 1576 ASN 1576 1576 ?    ?   ?   A . n 
A 1 1577 GLY 1577 1577 ?    ?   ?   A . n 
A 1 1578 LYS 1578 1578 ?    ?   ?   A . n 
A 1 1579 LEU 1579 1579 ?    ?   ?   A . n 
A 1 1580 ILE 1580 1580 ?    ?   ?   A . n 
A 1 1581 ALA 1581 1581 ?    ?   ?   A . n 
A 1 1582 TYR 1582 1582 ?    ?   ?   A . n 
A 1 1583 PRO 1583 1583 ?    ?   ?   A . n 
A 1 1584 ILE 1584 1584 ?    ?   ?   A . n 
A 1 1585 ALA 1585 1585 ?    ?   ?   A . n 
A 1 1586 VAL 1586 1586 ?    ?   ?   A . n 
A 1 1587 GLU 1587 1587 ?    ?   ?   A . n 
A 1 1588 ALA 1588 1588 ?    ?   ?   A . n 
A 1 1589 LEU 1589 1589 ?    ?   ?   A . n 
A 1 1590 SER 1590 1590 ?    ?   ?   A . n 
A 1 1591 LEU 1591 1591 ?    ?   ?   A . n 
A 1 1592 ILE 1592 1592 ?    ?   ?   A . n 
A 1 1593 TYR 1593 1593 ?    ?   ?   A . n 
A 1 1594 ASN 1594 1594 ?    ?   ?   A . n 
A 1 1595 LYS 1595 1595 ?    ?   ?   A . n 
A 1 1596 ASP 1596 1596 ?    ?   ?   A . n 
A 1 1597 LEU 1597 1597 ?    ?   ?   A . n 
A 1 1598 LEU 1598 1598 ?    ?   ?   A . n 
A 1 1599 PRO 1599 1599 ?    ?   ?   A . n 
A 1 1600 ASN 1600 1600 ?    ?   ?   A . n 
A 1 1601 PRO 1601 1601 ?    ?   ?   A . n 
A 1 1602 PRO 1602 1602 ?    ?   ?   A . n 
A 1 1603 LYS 1603 1603 ?    ?   ?   A . n 
A 1 1604 THR 1604 1604 ?    ?   ?   A . n 
A 1 1605 TRP 1605 1605 ?    ?   ?   A . n 
A 1 1606 GLU 1606 1606 ?    ?   ?   A . n 
A 1 1607 GLU 1607 1607 ?    ?   ?   A . n 
A 1 1608 ILE 1608 1608 ?    ?   ?   A . n 
A 1 1609 PRO 1609 1609 ?    ?   ?   A . n 
A 1 1610 ALA 1610 1610 ?    ?   ?   A . n 
A 1 1611 LEU 1611 1611 ?    ?   ?   A . n 
A 1 1612 ASP 1612 1612 ?    ?   ?   A . n 
A 1 1613 LYS 1613 1613 ?    ?   ?   A . n 
A 1 1614 GLU 1614 1614 ?    ?   ?   A . n 
A 1 1615 LEU 1615 1615 ?    ?   ?   A . n 
A 1 1616 LYS 1616 1616 ?    ?   ?   A . n 
A 1 1617 ALA 1617 1617 ?    ?   ?   A . n 
A 1 1618 LYS 1618 1618 ?    ?   ?   A . n 
A 1 1619 GLY 1619 1619 ?    ?   ?   A . n 
A 1 1620 LYS 1620 1620 ?    ?   ?   A . n 
A 1 1621 SER 1621 1621 ?    ?   ?   A . n 
A 1 1622 ALA 1622 1622 ?    ?   ?   A . n 
A 1 1623 LEU 1623 1623 ?    ?   ?   A . n 
A 1 1624 MET 1624 1624 ?    ?   ?   A . n 
A 1 1625 PHE 1625 1625 ?    ?   ?   A . n 
A 1 1626 ASN 1626 1626 ?    ?   ?   A . n 
A 1 1627 LEU 1627 1627 ?    ?   ?   A . n 
A 1 1628 GLN 1628 1628 ?    ?   ?   A . n 
A 1 1629 GLU 1629 1629 ?    ?   ?   A . n 
A 1 1630 PRO 1630 1630 ?    ?   ?   A . n 
A 1 1631 TYR 1631 1631 ?    ?   ?   A . n 
A 1 1632 PHE 1632 1632 ?    ?   ?   A . n 
A 1 1633 THR 1633 1633 ?    ?   ?   A . n 
A 1 1634 TRP 1634 1634 ?    ?   ?   A . n 
A 1 1635 PRO 1635 1635 ?    ?   ?   A . n 
A 1 1636 LEU 1636 1636 ?    ?   ?   A . n 
A 1 1637 ILE 1637 1637 ?    ?   ?   A . n 
A 1 1638 ALA 1638 1638 ?    ?   ?   A . n 
A 1 1639 ALA 1639 1639 ?    ?   ?   A . n 
A 1 1640 ASP 1640 1640 ?    ?   ?   A . n 
A 1 1641 GLY 1641 1641 ?    ?   ?   A . n 
A 1 1642 GLY 1642 1642 ?    ?   ?   A . n 
A 1 1643 TYR 1643 1643 ?    ?   ?   A . n 
A 1 1644 ALA 1644 1644 ?    ?   ?   A . n 
A 1 1645 PHE 1645 1645 ?    ?   ?   A . n 
A 1 1646 LYS 1646 1646 ?    ?   ?   A . n 
A 1 1647 TYR 1647 1647 ?    ?   ?   A . n 
A 1 1648 GLU 1648 1648 ?    ?   ?   A . n 
A 1 1649 ASN 1649 1649 ?    ?   ?   A . n 
A 1 1650 GLY 1650 1650 ?    ?   ?   A . n 
A 1 1651 LYS 1651 1651 ?    ?   ?   A . n 
A 1 1652 TYR 1652 1652 ?    ?   ?   A . n 
A 1 1653 ASP 1653 1653 ?    ?   ?   A . n 
A 1 1654 ILE 1654 1654 ?    ?   ?   A . n 
A 1 1655 LYS 1655 1655 ?    ?   ?   A . n 
A 1 1656 ASP 1656 1656 ?    ?   ?   A . n 
A 1 1657 VAL 1657 1657 ?    ?   ?   A . n 
A 1 1658 GLY 1658 1658 ?    ?   ?   A . n 
A 1 1659 VAL 1659 1659 ?    ?   ?   A . n 
A 1 1660 ASP 1660 1660 ?    ?   ?   A . n 
A 1 1661 ASN 1661 1661 ?    ?   ?   A . n 
A 1 1662 ALA 1662 1662 ?    ?   ?   A . n 
A 1 1663 GLY 1663 1663 ?    ?   ?   A . n 
A 1 1664 ALA 1664 1664 ?    ?   ?   A . n 
A 1 1665 LYS 1665 1665 ?    ?   ?   A . n 
A 1 1666 ALA 1666 1666 ?    ?   ?   A . n 
A 1 1667 GLY 1667 1667 ?    ?   ?   A . n 
A 1 1668 LEU 1668 1668 ?    ?   ?   A . n 
A 1 1669 THR 1669 1669 ?    ?   ?   A . n 
A 1 1670 PHE 1670 1670 ?    ?   ?   A . n 
A 1 1671 LEU 1671 1671 ?    ?   ?   A . n 
A 1 1672 VAL 1672 1672 ?    ?   ?   A . n 
A 1 1673 ASP 1673 1673 ?    ?   ?   A . n 
A 1 1674 LEU 1674 1674 ?    ?   ?   A . n 
A 1 1675 ILE 1675 1675 ?    ?   ?   A . n 
A 1 1676 LYS 1676 1676 ?    ?   ?   A . n 
A 1 1677 ASN 1677 1677 ?    ?   ?   A . n 
A 1 1678 LYS 1678 1678 ?    ?   ?   A . n 
A 1 1679 HIS 1679 1679 ?    ?   ?   A . n 
A 1 1680 MET 1680 1680 ?    ?   ?   A . n 
A 1 1681 ASN 1681 1681 ?    ?   ?   A . n 
A 1 1682 ALA 1682 1682 ?    ?   ?   A . n 
A 1 1683 ASP 1683 1683 ?    ?   ?   A . n 
A 1 1684 THR 1684 1684 ?    ?   ?   A . n 
A 1 1685 ASP 1685 1685 ?    ?   ?   A . n 
A 1 1686 TYR 1686 1686 ?    ?   ?   A . n 
A 1 1687 SER 1687 1687 ?    ?   ?   A . n 
A 1 1688 ILE 1688 1688 ?    ?   ?   A . n 
A 1 1689 ALA 1689 1689 ?    ?   ?   A . n 
A 1 1690 GLU 1690 1690 ?    ?   ?   A . n 
A 1 1691 ALA 1691 1691 ?    ?   ?   A . n 
A 1 1692 ALA 1692 1692 ?    ?   ?   A . n 
A 1 1693 PHE 1693 1693 ?    ?   ?   A . n 
A 1 1694 ASN 1694 1694 ?    ?   ?   A . n 
A 1 1695 LYS 1695 1695 ?    ?   ?   A . n 
A 1 1696 GLY 1696 1696 ?    ?   ?   A . n 
A 1 1697 GLU 1697 1697 ?    ?   ?   A . n 
A 1 1698 THR 1698 1698 ?    ?   ?   A . n 
A 1 1699 ALA 1699 1699 ?    ?   ?   A . n 
A 1 1700 MET 1700 1700 ?    ?   ?   A . n 
A 1 1701 THR 1701 1701 ?    ?   ?   A . n 
A 1 1702 ILE 1702 1702 ?    ?   ?   A . n 
A 1 1703 ASN 1703 1703 ?    ?   ?   A . n 
A 1 1704 GLY 1704 1704 ?    ?   ?   A . n 
A 1 1705 PRO 1705 1705 ?    ?   ?   A . n 
A 1 1706 TRP 1706 1706 ?    ?   ?   A . n 
A 1 1707 ALA 1707 1707 ?    ?   ?   A . n 
A 1 1708 TRP 1708 1708 ?    ?   ?   A . n 
A 1 1709 SER 1709 1709 ?    ?   ?   A . n 
A 1 1710 ASN 1710 1710 ?    ?   ?   A . n 
A 1 1711 ILE 1711 1711 ?    ?   ?   A . n 
A 1 1712 ASP 1712 1712 ?    ?   ?   A . n 
A 1 1713 THR 1713 1713 ?    ?   ?   A . n 
A 1 1714 SER 1714 1714 ?    ?   ?   A . n 
A 1 1715 LYS 1715 1715 ?    ?   ?   A . n 
A 1 1716 VAL 1716 1716 ?    ?   ?   A . n 
A 1 1717 ASN 1717 1717 ?    ?   ?   A . n 
A 1 1718 TYR 1718 1718 ?    ?   ?   A . n 
A 1 1719 GLY 1719 1719 ?    ?   ?   A . n 
A 1 1720 VAL 1720 1720 ?    ?   ?   A . n 
A 1 1721 THR 1721 1721 ?    ?   ?   A . n 
A 1 1722 VAL 1722 1722 ?    ?   ?   A . n 
A 1 1723 LEU 1723 1723 ?    ?   ?   A . n 
A 1 1724 PRO 1724 1724 ?    ?   ?   A . n 
A 1 1725 THR 1725 1725 ?    ?   ?   A . n 
A 1 1726 PHE 1726 1726 ?    ?   ?   A . n 
A 1 1727 LYS 1727 1727 ?    ?   ?   A . n 
A 1 1728 GLY 1728 1728 ?    ?   ?   A . n 
A 1 1729 GLN 1729 1729 ?    ?   ?   A . n 
A 1 1730 PRO 1730 1730 ?    ?   ?   A . n 
A 1 1731 SER 1731 1731 ?    ?   ?   A . n 
A 1 1732 LYS 1732 1732 ?    ?   ?   A . n 
A 1 1733 PRO 1733 1733 ?    ?   ?   A . n 
A 1 1734 PHE 1734 1734 ?    ?   ?   A . n 
A 1 1735 VAL 1735 1735 ?    ?   ?   A . n 
A 1 1736 GLY 1736 1736 ?    ?   ?   A . n 
A 1 1737 VAL 1737 1737 ?    ?   ?   A . n 
A 1 1738 LEU 1738 1738 ?    ?   ?   A . n 
A 1 1739 SER 1739 1739 ?    ?   ?   A . n 
A 1 1740 ALA 1740 1740 ?    ?   ?   A . n 
A 1 1741 GLY 1741 1741 ?    ?   ?   A . n 
A 1 1742 ILE 1742 1742 ?    ?   ?   A . n 
A 1 1743 ASN 1743 1743 ?    ?   ?   A . n 
A 1 1744 ALA 1744 1744 ?    ?   ?   A . n 
A 1 1745 ALA 1745 1745 ?    ?   ?   A . n 
A 1 1746 SER 1746 1746 ?    ?   ?   A . n 
A 1 1747 PRO 1747 1747 ?    ?   ?   A . n 
A 1 1748 ASN 1748 1748 ?    ?   ?   A . n 
A 1 1749 LYS 1749 1749 ?    ?   ?   A . n 
A 1 1750 GLU 1750 1750 ?    ?   ?   A . n 
A 1 1751 LEU 1751 1751 ?    ?   ?   A . n 
A 1 1752 ALA 1752 1752 ?    ?   ?   A . n 
A 1 1753 LYS 1753 1753 ?    ?   ?   A . n 
A 1 1754 GLU 1754 1754 ?    ?   ?   A . n 
A 1 1755 PHE 1755 1755 ?    ?   ?   A . n 
A 1 1756 LEU 1756 1756 ?    ?   ?   A . n 
A 1 1757 GLU 1757 1757 ?    ?   ?   A . n 
A 1 1758 ASN 1758 1758 ?    ?   ?   A . n 
A 1 1759 TYR 1759 1759 ?    ?   ?   A . n 
A 1 1760 LEU 1760 1760 ?    ?   ?   A . n 
A 1 1761 LEU 1761 1761 ?    ?   ?   A . n 
A 1 1762 THR 1762 1762 ?    ?   ?   A . n 
A 1 1763 ASP 1763 1763 ?    ?   ?   A . n 
A 1 1764 GLU 1764 1764 ?    ?   ?   A . n 
A 1 1765 GLY 1765 1765 ?    ?   ?   A . n 
A 1 1766 LEU 1766 1766 ?    ?   ?   A . n 
A 1 1767 GLU 1767 1767 ?    ?   ?   A . n 
A 1 1768 ALA 1768 1768 ?    ?   ?   A . n 
A 1 1769 VAL 1769 1769 ?    ?   ?   A . n 
A 1 1770 ASN 1770 1770 ?    ?   ?   A . n 
A 1 1771 LYS 1771 1771 ?    ?   ?   A . n 
A 1 1772 ASP 1772 1772 ?    ?   ?   A . n 
A 1 1773 LYS 1773 1773 ?    ?   ?   A . n 
A 1 1774 PRO 1774 1774 ?    ?   ?   A . n 
A 1 1775 LEU 1775 1775 ?    ?   ?   A . n 
A 1 1776 GLY 1776 1776 ?    ?   ?   A . n 
A 1 1777 ALA 1777 1777 ?    ?   ?   A . n 
A 1 1778 VAL 1778 1778 ?    ?   ?   A . n 
A 1 1779 ALA 1779 1779 ?    ?   ?   A . n 
A 1 1780 LEU 1780 1780 ?    ?   ?   A . n 
A 1 1781 LYS 1781 1781 ?    ?   ?   A . n 
A 1 1782 SER 1782 1782 ?    ?   ?   A . n 
A 1 1783 TYR 1783 1783 ?    ?   ?   A . n 
A 1 1784 GLU 1784 1784 ?    ?   ?   A . n 
A 1 1785 GLU 1785 1785 ?    ?   ?   A . n 
A 1 1786 GLU 1786 1786 ?    ?   ?   A . n 
A 1 1787 LEU 1787 1787 ?    ?   ?   A . n 
A 1 1788 ALA 1788 1788 ?    ?   ?   A . n 
A 1 1789 LYS 1789 1789 ?    ?   ?   A . n 
A 1 1790 ASP 1790 1790 ?    ?   ?   A . n 
A 1 1791 PRO 1791 1791 ?    ?   ?   A . n 
A 1 1792 ARG 1792 1792 ?    ?   ?   A . n 
A 1 1793 ILE 1793 1793 ?    ?   ?   A . n 
A 1 1794 ALA 1794 1794 ?    ?   ?   A . n 
A 1 1795 ALA 1795 1795 ?    ?   ?   A . n 
A 1 1796 THR 1796 1796 ?    ?   ?   A . n 
A 1 1797 MET 1797 1797 ?    ?   ?   A . n 
A 1 1798 GLU 1798 1798 ?    ?   ?   A . n 
A 1 1799 ASN 1799 1799 ?    ?   ?   A . n 
A 1 1800 ALA 1800 1800 ?    ?   ?   A . n 
A 1 1801 GLN 1801 1801 ?    ?   ?   A . n 
A 1 1802 LYS 1802 1802 ?    ?   ?   A . n 
A 1 1803 GLY 1803 1803 ?    ?   ?   A . n 
A 1 1804 GLU 1804 1804 ?    ?   ?   A . n 
A 1 1805 ILE 1805 1805 ?    ?   ?   A . n 
A 1 1806 MET 1806 1806 ?    ?   ?   A . n 
A 1 1807 PRO 1807 1807 ?    ?   ?   A . n 
A 1 1808 ASN 1808 1808 ?    ?   ?   A . n 
A 1 1809 ILE 1809 1809 ?    ?   ?   A . n 
A 1 1810 PRO 1810 1810 ?    ?   ?   A . n 
A 1 1811 GLN 1811 1811 ?    ?   ?   A . n 
A 1 1812 MET 1812 1812 ?    ?   ?   A . n 
A 1 1813 SER 1813 1813 ?    ?   ?   A . n 
A 1 1814 ALA 1814 1814 ?    ?   ?   A . n 
A 1 1815 PHE 1815 1815 ?    ?   ?   A . n 
A 1 1816 TRP 1816 1816 ?    ?   ?   A . n 
A 1 1817 TYR 1817 1817 ?    ?   ?   A . n 
A 1 1818 ALA 1818 1818 ?    ?   ?   A . n 
A 1 1819 VAL 1819 1819 ?    ?   ?   A . n 
A 1 1820 ARG 1820 1820 ?    ?   ?   A . n 
A 1 1821 THR 1821 1821 ?    ?   ?   A . n 
A 1 1822 ALA 1822 1822 ?    ?   ?   A . n 
A 1 1823 VAL 1823 1823 ?    ?   ?   A . n 
A 1 1824 ILE 1824 1824 ?    ?   ?   A . n 
A 1 1825 ASN 1825 1825 ?    ?   ?   A . n 
A 1 1826 ALA 1826 1826 ?    ?   ?   A . n 
A 1 1827 ALA 1827 1827 ?    ?   ?   A . n 
A 1 1828 SER 1828 1828 ?    ?   ?   A . n 
A 1 1829 GLY 1829 1829 ?    ?   ?   A . n 
A 1 1830 ARG 1830 1830 ?    ?   ?   A . n 
A 1 1831 GLN 1831 1831 ?    ?   ?   A . n 
A 1 1832 THR 1832 1832 ?    ?   ?   A . n 
A 1 1833 VAL 1833 1833 ?    ?   ?   A . n 
A 1 1834 ASP 1834 1834 ?    ?   ?   A . n 
A 1 1835 GLU 1835 1835 ?    ?   ?   A . n 
A 1 1836 ALA 1836 1836 ?    ?   ?   A . n 
A 1 1837 LEU 1837 1837 ?    ?   ?   A . n 
A 1 1838 LYS 1838 1838 ?    ?   ?   A . n 
A 1 1839 ASP 1839 1839 ?    ?   ?   A . n 
A 1 1840 ALA 1840 1840 ?    ?   ?   A . n 
A 1 1841 GLN 1841 1841 ?    ?   ?   A . n 
A 1 1842 THR 1842 1842 ?    ?   ?   A . n 
A 1 1843 GLY 1843 1843 ?    ?   ?   A . n 
A 1 1844 ASP 1844 1844 ?    ?   ?   A . n 
A 1 1845 TYR 1845 1845 ?    ?   ?   A . n 
A 1 1846 LYS 1846 1846 ?    ?   ?   A . n 
A 1 1847 ASP 1847 1847 ?    ?   ?   A . n 
A 1 1848 ASP 1848 1848 ?    ?   ?   A . n 
A 1 1849 ASP 1849 1849 ?    ?   ?   A . n 
A 1 1850 ASP 1850 1850 ?    ?   ?   A . n 
A 1 1851 LYS 1851 1851 ?    ?   ?   A . n 
B 2 1    MET 1    -341 ?    ?   ?   B . n 
B 2 2    GLY 2    -340 ?    ?   ?   B . n 
B 2 3    SER 3    -339 ?    ?   ?   B . n 
B 2 4    SER 4    -338 ?    ?   ?   B . n 
B 2 5    HIS 5    -337 ?    ?   ?   B . n 
B 2 6    HIS 6    -336 ?    ?   ?   B . n 
B 2 7    HIS 7    -335 ?    ?   ?   B . n 
B 2 8    HIS 8    -334 ?    ?   ?   B . n 
B 2 9    HIS 9    -333 ?    ?   ?   B . n 
B 2 10   HIS 10   -332 ?    ?   ?   B . n 
B 2 11   GLY 11   -331 ?    ?   ?   B . n 
B 2 12   THR 12   -330 ?    ?   ?   B . n 
B 2 13   LYS 13   -329 ?    ?   ?   B . n 
B 2 14   THR 14   -328 ?    ?   ?   B . n 
B 2 15   GLU 15   -327 ?    ?   ?   B . n 
B 2 16   GLU 16   -326 ?    ?   ?   B . n 
B 2 17   GLY 17   -325 ?    ?   ?   B . n 
B 2 18   LYS 18   -324 ?    ?   ?   B . n 
B 2 19   LEU 19   -323 ?    ?   ?   B . n 
B 2 20   VAL 20   -322 ?    ?   ?   B . n 
B 2 21   ILE 21   -321 ?    ?   ?   B . n 
B 2 22   TRP 22   -320 ?    ?   ?   B . n 
B 2 23   ILE 23   -319 ?    ?   ?   B . n 
B 2 24   ASN 24   -318 ?    ?   ?   B . n 
B 2 25   GLY 25   -317 ?    ?   ?   B . n 
B 2 26   ASP 26   -316 ?    ?   ?   B . n 
B 2 27   LYS 27   -315 ?    ?   ?   B . n 
B 2 28   GLY 28   -314 ?    ?   ?   B . n 
B 2 29   TYR 29   -313 ?    ?   ?   B . n 
B 2 30   ASN 30   -312 ?    ?   ?   B . n 
B 2 31   GLY 31   -311 ?    ?   ?   B . n 
B 2 32   LEU 32   -310 ?    ?   ?   B . n 
B 2 33   ALA 33   -309 ?    ?   ?   B . n 
B 2 34   GLU 34   -308 ?    ?   ?   B . n 
B 2 35   VAL 35   -307 ?    ?   ?   B . n 
B 2 36   GLY 36   -306 ?    ?   ?   B . n 
B 2 37   LYS 37   -305 ?    ?   ?   B . n 
B 2 38   LYS 38   -304 ?    ?   ?   B . n 
B 2 39   PHE 39   -303 ?    ?   ?   B . n 
B 2 40   GLU 40   -302 ?    ?   ?   B . n 
B 2 41   LYS 41   -301 ?    ?   ?   B . n 
B 2 42   ASP 42   -300 ?    ?   ?   B . n 
B 2 43   THR 43   -299 ?    ?   ?   B . n 
B 2 44   GLY 44   -298 ?    ?   ?   B . n 
B 2 45   ILE 45   -297 ?    ?   ?   B . n 
B 2 46   LYS 46   -296 ?    ?   ?   B . n 
B 2 47   VAL 47   -295 ?    ?   ?   B . n 
B 2 48   THR 48   -294 ?    ?   ?   B . n 
B 2 49   VAL 49   -293 ?    ?   ?   B . n 
B 2 50   GLU 50   -292 ?    ?   ?   B . n 
B 2 51   HIS 51   -291 ?    ?   ?   B . n 
B 2 52   PRO 52   -290 ?    ?   ?   B . n 
B 2 53   ASP 53   -289 ?    ?   ?   B . n 
B 2 54   LYS 54   -288 ?    ?   ?   B . n 
B 2 55   LEU 55   -287 ?    ?   ?   B . n 
B 2 56   GLU 56   -286 ?    ?   ?   B . n 
B 2 57   GLU 57   -285 ?    ?   ?   B . n 
B 2 58   LYS 58   -284 ?    ?   ?   B . n 
B 2 59   PHE 59   -283 ?    ?   ?   B . n 
B 2 60   PRO 60   -282 ?    ?   ?   B . n 
B 2 61   GLN 61   -281 ?    ?   ?   B . n 
B 2 62   VAL 62   -280 ?    ?   ?   B . n 
B 2 63   ALA 63   -279 ?    ?   ?   B . n 
B 2 64   ALA 64   -278 ?    ?   ?   B . n 
B 2 65   THR 65   -277 ?    ?   ?   B . n 
B 2 66   GLY 66   -276 ?    ?   ?   B . n 
B 2 67   ASP 67   -275 ?    ?   ?   B . n 
B 2 68   GLY 68   -274 ?    ?   ?   B . n 
B 2 69   PRO 69   -273 ?    ?   ?   B . n 
B 2 70   ASP 70   -272 ?    ?   ?   B . n 
B 2 71   ILE 71   -271 ?    ?   ?   B . n 
B 2 72   ILE 72   -270 ?    ?   ?   B . n 
B 2 73   PHE 73   -269 ?    ?   ?   B . n 
B 2 74   TRP 74   -268 ?    ?   ?   B . n 
B 2 75   ALA 75   -267 ?    ?   ?   B . n 
B 2 76   HIS 76   -266 ?    ?   ?   B . n 
B 2 77   ASP 77   -265 ?    ?   ?   B . n 
B 2 78   ARG 78   -264 ?    ?   ?   B . n 
B 2 79   PHE 79   -263 ?    ?   ?   B . n 
B 2 80   GLY 80   -262 ?    ?   ?   B . n 
B 2 81   GLY 81   -261 ?    ?   ?   B . n 
B 2 82   TYR 82   -260 ?    ?   ?   B . n 
B 2 83   ALA 83   -259 ?    ?   ?   B . n 
B 2 84   GLN 84   -258 ?    ?   ?   B . n 
B 2 85   SER 85   -257 ?    ?   ?   B . n 
B 2 86   GLY 86   -256 ?    ?   ?   B . n 
B 2 87   LEU 87   -255 ?    ?   ?   B . n 
B 2 88   LEU 88   -254 ?    ?   ?   B . n 
B 2 89   ALA 89   -253 ?    ?   ?   B . n 
B 2 90   GLU 90   -252 ?    ?   ?   B . n 
B 2 91   ILE 91   -251 ?    ?   ?   B . n 
B 2 92   THR 92   -250 ?    ?   ?   B . n 
B 2 93   PRO 93   -249 ?    ?   ?   B . n 
B 2 94   ASP 94   -248 ?    ?   ?   B . n 
B 2 95   LYS 95   -247 ?    ?   ?   B . n 
B 2 96   ALA 96   -246 ?    ?   ?   B . n 
B 2 97   PHE 97   -245 ?    ?   ?   B . n 
B 2 98   GLN 98   -244 ?    ?   ?   B . n 
B 2 99   ASP 99   -243 ?    ?   ?   B . n 
B 2 100  LYS 100  -242 ?    ?   ?   B . n 
B 2 101  LEU 101  -241 ?    ?   ?   B . n 
B 2 102  TYR 102  -240 ?    ?   ?   B . n 
B 2 103  PRO 103  -239 ?    ?   ?   B . n 
B 2 104  PHE 104  -238 ?    ?   ?   B . n 
B 2 105  THR 105  -237 ?    ?   ?   B . n 
B 2 106  TRP 106  -236 ?    ?   ?   B . n 
B 2 107  ASP 107  -235 ?    ?   ?   B . n 
B 2 108  ALA 108  -234 ?    ?   ?   B . n 
B 2 109  VAL 109  -233 ?    ?   ?   B . n 
B 2 110  ARG 110  -232 ?    ?   ?   B . n 
B 2 111  TYR 111  -231 ?    ?   ?   B . n 
B 2 112  ASN 112  -230 ?    ?   ?   B . n 
B 2 113  GLY 113  -229 ?    ?   ?   B . n 
B 2 114  LYS 114  -228 ?    ?   ?   B . n 
B 2 115  LEU 115  -227 ?    ?   ?   B . n 
B 2 116  ILE 116  -226 ?    ?   ?   B . n 
B 2 117  ALA 117  -225 ?    ?   ?   B . n 
B 2 118  TYR 118  -224 ?    ?   ?   B . n 
B 2 119  PRO 119  -223 ?    ?   ?   B . n 
B 2 120  ILE 120  -222 ?    ?   ?   B . n 
B 2 121  ALA 121  -221 ?    ?   ?   B . n 
B 2 122  VAL 122  -220 ?    ?   ?   B . n 
B 2 123  GLU 123  -219 ?    ?   ?   B . n 
B 2 124  ALA 124  -218 ?    ?   ?   B . n 
B 2 125  LEU 125  -217 ?    ?   ?   B . n 
B 2 126  SER 126  -216 ?    ?   ?   B . n 
B 2 127  LEU 127  -215 ?    ?   ?   B . n 
B 2 128  ILE 128  -214 ?    ?   ?   B . n 
B 2 129  TYR 129  -213 ?    ?   ?   B . n 
B 2 130  ASN 130  -212 ?    ?   ?   B . n 
B 2 131  LYS 131  -211 ?    ?   ?   B . n 
B 2 132  ASP 132  -210 ?    ?   ?   B . n 
B 2 133  LEU 133  -209 ?    ?   ?   B . n 
B 2 134  LEU 134  -208 ?    ?   ?   B . n 
B 2 135  PRO 135  -207 ?    ?   ?   B . n 
B 2 136  ASN 136  -206 ?    ?   ?   B . n 
B 2 137  PRO 137  -205 ?    ?   ?   B . n 
B 2 138  PRO 138  -204 ?    ?   ?   B . n 
B 2 139  LYS 139  -203 ?    ?   ?   B . n 
B 2 140  THR 140  -202 ?    ?   ?   B . n 
B 2 141  TRP 141  -201 ?    ?   ?   B . n 
B 2 142  GLU 142  -200 ?    ?   ?   B . n 
B 2 143  GLU 143  -199 ?    ?   ?   B . n 
B 2 144  ILE 144  -198 ?    ?   ?   B . n 
B 2 145  PRO 145  -197 ?    ?   ?   B . n 
B 2 146  ALA 146  -196 ?    ?   ?   B . n 
B 2 147  LEU 147  -195 ?    ?   ?   B . n 
B 2 148  ASP 148  -194 ?    ?   ?   B . n 
B 2 149  LYS 149  -193 ?    ?   ?   B . n 
B 2 150  GLU 150  -192 ?    ?   ?   B . n 
B 2 151  LEU 151  -191 ?    ?   ?   B . n 
B 2 152  LYS 152  -190 ?    ?   ?   B . n 
B 2 153  ALA 153  -189 ?    ?   ?   B . n 
B 2 154  LYS 154  -188 ?    ?   ?   B . n 
B 2 155  GLY 155  -187 ?    ?   ?   B . n 
B 2 156  LYS 156  -186 ?    ?   ?   B . n 
B 2 157  SER 157  -185 ?    ?   ?   B . n 
B 2 158  ALA 158  -184 ?    ?   ?   B . n 
B 2 159  LEU 159  -183 ?    ?   ?   B . n 
B 2 160  MET 160  -182 ?    ?   ?   B . n 
B 2 161  PHE 161  -181 ?    ?   ?   B . n 
B 2 162  ASN 162  -180 ?    ?   ?   B . n 
B 2 163  LEU 163  -179 ?    ?   ?   B . n 
B 2 164  GLN 164  -178 ?    ?   ?   B . n 
B 2 165  GLU 165  -177 ?    ?   ?   B . n 
B 2 166  PRO 166  -176 ?    ?   ?   B . n 
B 2 167  TYR 167  -175 ?    ?   ?   B . n 
B 2 168  PHE 168  -174 ?    ?   ?   B . n 
B 2 169  THR 169  -173 ?    ?   ?   B . n 
B 2 170  TRP 170  -172 ?    ?   ?   B . n 
B 2 171  PRO 171  -171 ?    ?   ?   B . n 
B 2 172  LEU 172  -170 ?    ?   ?   B . n 
B 2 173  ILE 173  -169 ?    ?   ?   B . n 
B 2 174  ALA 174  -168 ?    ?   ?   B . n 
B 2 175  ALA 175  -167 ?    ?   ?   B . n 
B 2 176  ASP 176  -166 ?    ?   ?   B . n 
B 2 177  GLY 177  -165 ?    ?   ?   B . n 
B 2 178  GLY 178  -164 ?    ?   ?   B . n 
B 2 179  TYR 179  -163 ?    ?   ?   B . n 
B 2 180  ALA 180  -162 ?    ?   ?   B . n 
B 2 181  PHE 181  -161 ?    ?   ?   B . n 
B 2 182  LYS 182  -160 ?    ?   ?   B . n 
B 2 183  TYR 183  -159 ?    ?   ?   B . n 
B 2 184  GLU 184  -158 ?    ?   ?   B . n 
B 2 185  ASN 185  -157 ?    ?   ?   B . n 
B 2 186  GLY 186  -156 ?    ?   ?   B . n 
B 2 187  LYS 187  -155 ?    ?   ?   B . n 
B 2 188  TYR 188  -154 ?    ?   ?   B . n 
B 2 189  ASP 189  -153 ?    ?   ?   B . n 
B 2 190  ILE 190  -152 ?    ?   ?   B . n 
B 2 191  LYS 191  -151 ?    ?   ?   B . n 
B 2 192  ASP 192  -150 ?    ?   ?   B . n 
B 2 193  VAL 193  -149 ?    ?   ?   B . n 
B 2 194  GLY 194  -148 ?    ?   ?   B . n 
B 2 195  VAL 195  -147 ?    ?   ?   B . n 
B 2 196  ASP 196  -146 ?    ?   ?   B . n 
B 2 197  ASN 197  -145 ?    ?   ?   B . n 
B 2 198  ALA 198  -144 ?    ?   ?   B . n 
B 2 199  GLY 199  -143 ?    ?   ?   B . n 
B 2 200  ALA 200  -142 ?    ?   ?   B . n 
B 2 201  LYS 201  -141 ?    ?   ?   B . n 
B 2 202  ALA 202  -140 ?    ?   ?   B . n 
B 2 203  GLY 203  -139 ?    ?   ?   B . n 
B 2 204  LEU 204  -138 ?    ?   ?   B . n 
B 2 205  THR 205  -137 ?    ?   ?   B . n 
B 2 206  PHE 206  -136 ?    ?   ?   B . n 
B 2 207  LEU 207  -135 ?    ?   ?   B . n 
B 2 208  VAL 208  -134 ?    ?   ?   B . n 
B 2 209  ASP 209  -133 ?    ?   ?   B . n 
B 2 210  LEU 210  -132 ?    ?   ?   B . n 
B 2 211  ILE 211  -131 ?    ?   ?   B . n 
B 2 212  LYS 212  -130 ?    ?   ?   B . n 
B 2 213  ASN 213  -129 ?    ?   ?   B . n 
B 2 214  LYS 214  -128 ?    ?   ?   B . n 
B 2 215  HIS 215  -127 ?    ?   ?   B . n 
B 2 216  MET 216  -126 ?    ?   ?   B . n 
B 2 217  ASN 217  -125 ?    ?   ?   B . n 
B 2 218  ALA 218  -124 ?    ?   ?   B . n 
B 2 219  ASP 219  -123 ?    ?   ?   B . n 
B 2 220  THR 220  -122 ?    ?   ?   B . n 
B 2 221  ASP 221  -121 ?    ?   ?   B . n 
B 2 222  TYR 222  -120 ?    ?   ?   B . n 
B 2 223  SER 223  -119 ?    ?   ?   B . n 
B 2 224  ILE 224  -118 ?    ?   ?   B . n 
B 2 225  ALA 225  -117 ?    ?   ?   B . n 
B 2 226  GLU 226  -116 ?    ?   ?   B . n 
B 2 227  ALA 227  -115 ?    ?   ?   B . n 
B 2 228  ALA 228  -114 ?    ?   ?   B . n 
B 2 229  PHE 229  -113 ?    ?   ?   B . n 
B 2 230  ASN 230  -112 ?    ?   ?   B . n 
B 2 231  LYS 231  -111 ?    ?   ?   B . n 
B 2 232  GLY 232  -110 ?    ?   ?   B . n 
B 2 233  GLU 233  -109 ?    ?   ?   B . n 
B 2 234  THR 234  -108 ?    ?   ?   B . n 
B 2 235  ALA 235  -107 ?    ?   ?   B . n 
B 2 236  MET 236  -106 ?    ?   ?   B . n 
B 2 237  THR 237  -105 ?    ?   ?   B . n 
B 2 238  ILE 238  -104 ?    ?   ?   B . n 
B 2 239  ASN 239  -103 ?    ?   ?   B . n 
B 2 240  GLY 240  -102 ?    ?   ?   B . n 
B 2 241  PRO 241  -101 ?    ?   ?   B . n 
B 2 242  TRP 242  -100 ?    ?   ?   B . n 
B 2 243  ALA 243  -99  ?    ?   ?   B . n 
B 2 244  TRP 244  -98  ?    ?   ?   B . n 
B 2 245  SER 245  -97  ?    ?   ?   B . n 
B 2 246  ASN 246  -96  ?    ?   ?   B . n 
B 2 247  ILE 247  -95  ?    ?   ?   B . n 
B 2 248  ASP 248  -94  ?    ?   ?   B . n 
B 2 249  THR 249  -93  ?    ?   ?   B . n 
B 2 250  SER 250  -92  ?    ?   ?   B . n 
B 2 251  LYS 251  -91  ?    ?   ?   B . n 
B 2 252  VAL 252  -90  ?    ?   ?   B . n 
B 2 253  ASN 253  -89  ?    ?   ?   B . n 
B 2 254  TYR 254  -88  ?    ?   ?   B . n 
B 2 255  GLY 255  -87  ?    ?   ?   B . n 
B 2 256  VAL 256  -86  ?    ?   ?   B . n 
B 2 257  THR 257  -85  ?    ?   ?   B . n 
B 2 258  VAL 258  -84  ?    ?   ?   B . n 
B 2 259  LEU 259  -83  ?    ?   ?   B . n 
B 2 260  PRO 260  -82  ?    ?   ?   B . n 
B 2 261  THR 261  -81  ?    ?   ?   B . n 
B 2 262  PHE 262  -80  ?    ?   ?   B . n 
B 2 263  LYS 263  -79  ?    ?   ?   B . n 
B 2 264  GLY 264  -78  ?    ?   ?   B . n 
B 2 265  GLN 265  -77  ?    ?   ?   B . n 
B 2 266  PRO 266  -76  ?    ?   ?   B . n 
B 2 267  SER 267  -75  ?    ?   ?   B . n 
B 2 268  LYS 268  -74  ?    ?   ?   B . n 
B 2 269  PRO 269  -73  ?    ?   ?   B . n 
B 2 270  PHE 270  -72  ?    ?   ?   B . n 
B 2 271  VAL 271  -71  ?    ?   ?   B . n 
B 2 272  GLY 272  -70  ?    ?   ?   B . n 
B 2 273  VAL 273  -69  ?    ?   ?   B . n 
B 2 274  LEU 274  -68  ?    ?   ?   B . n 
B 2 275  SER 275  -67  ?    ?   ?   B . n 
B 2 276  ALA 276  -66  ?    ?   ?   B . n 
B 2 277  GLY 277  -65  ?    ?   ?   B . n 
B 2 278  ILE 278  -64  ?    ?   ?   B . n 
B 2 279  ASN 279  -63  ?    ?   ?   B . n 
B 2 280  ALA 280  -62  ?    ?   ?   B . n 
B 2 281  ALA 281  -61  ?    ?   ?   B . n 
B 2 282  SER 282  -60  ?    ?   ?   B . n 
B 2 283  PRO 283  -59  ?    ?   ?   B . n 
B 2 284  ASN 284  -58  ?    ?   ?   B . n 
B 2 285  LYS 285  -57  ?    ?   ?   B . n 
B 2 286  GLU 286  -56  ?    ?   ?   B . n 
B 2 287  LEU 287  -55  ?    ?   ?   B . n 
B 2 288  ALA 288  -54  ?    ?   ?   B . n 
B 2 289  LYS 289  -53  ?    ?   ?   B . n 
B 2 290  GLU 290  -52  ?    ?   ?   B . n 
B 2 291  PHE 291  -51  ?    ?   ?   B . n 
B 2 292  LEU 292  -50  ?    ?   ?   B . n 
B 2 293  GLU 293  -49  ?    ?   ?   B . n 
B 2 294  ASN 294  -48  ?    ?   ?   B . n 
B 2 295  TYR 295  -47  ?    ?   ?   B . n 
B 2 296  LEU 296  -46  ?    ?   ?   B . n 
B 2 297  LEU 297  -45  ?    ?   ?   B . n 
B 2 298  THR 298  -44  ?    ?   ?   B . n 
B 2 299  ASP 299  -43  ?    ?   ?   B . n 
B 2 300  GLU 300  -42  ?    ?   ?   B . n 
B 2 301  GLY 301  -41  ?    ?   ?   B . n 
B 2 302  LEU 302  -40  ?    ?   ?   B . n 
B 2 303  GLU 303  -39  ?    ?   ?   B . n 
B 2 304  ALA 304  -38  ?    ?   ?   B . n 
B 2 305  VAL 305  -37  ?    ?   ?   B . n 
B 2 306  ASN 306  -36  ?    ?   ?   B . n 
B 2 307  LYS 307  -35  ?    ?   ?   B . n 
B 2 308  ASP 308  -34  ?    ?   ?   B . n 
B 2 309  LYS 309  -33  ?    ?   ?   B . n 
B 2 310  PRO 310  -32  ?    ?   ?   B . n 
B 2 311  LEU 311  -31  ?    ?   ?   B . n 
B 2 312  GLY 312  -30  ?    ?   ?   B . n 
B 2 313  ALA 313  -29  ?    ?   ?   B . n 
B 2 314  VAL 314  -28  ?    ?   ?   B . n 
B 2 315  ALA 315  -27  ?    ?   ?   B . n 
B 2 316  LEU 316  -26  ?    ?   ?   B . n 
B 2 317  LYS 317  -25  ?    ?   ?   B . n 
B 2 318  SER 318  -24  ?    ?   ?   B . n 
B 2 319  TYR 319  -23  ?    ?   ?   B . n 
B 2 320  GLU 320  -22  ?    ?   ?   B . n 
B 2 321  GLU 321  -21  ?    ?   ?   B . n 
B 2 322  GLU 322  -20  ?    ?   ?   B . n 
B 2 323  LEU 323  -19  ?    ?   ?   B . n 
B 2 324  ALA 324  -18  ?    ?   ?   B . n 
B 2 325  LYS 325  -17  ?    ?   ?   B . n 
B 2 326  ASP 326  -16  ?    ?   ?   B . n 
B 2 327  PRO 327  -15  ?    ?   ?   B . n 
B 2 328  ARG 328  -14  ?    ?   ?   B . n 
B 2 329  ILE 329  -13  ?    ?   ?   B . n 
B 2 330  ALA 330  -12  ?    ?   ?   B . n 
B 2 331  ALA 331  -11  ?    ?   ?   B . n 
B 2 332  THR 332  -10  ?    ?   ?   B . n 
B 2 333  MET 333  -9   ?    ?   ?   B . n 
B 2 334  GLU 334  -8   ?    ?   ?   B . n 
B 2 335  ASN 335  -7   ?    ?   ?   B . n 
B 2 336  ALA 336  -6   ?    ?   ?   B . n 
B 2 337  GLN 337  -5   ?    ?   ?   B . n 
B 2 338  LYS 338  -4   ?    ?   ?   B . n 
B 2 339  GLY 339  -3   ?    ?   ?   B . n 
B 2 340  GLU 340  -2   ?    ?   ?   B . n 
B 2 341  ILE 341  -1   ?    ?   ?   B . n 
B 2 342  MET 342  0    ?    ?   ?   B . n 
B 2 343  PRO 343  1    ?    ?   ?   B . n 
B 2 344  ASN 344  2    ?    ?   ?   B . n 
B 2 345  ILE 345  3    ?    ?   ?   B . n 
B 2 346  PRO 346  4    ?    ?   ?   B . n 
B 2 347  GLN 347  5    ?    ?   ?   B . n 
B 2 348  MET 348  6    ?    ?   ?   B . n 
B 2 349  SER 349  7    ?    ?   ?   B . n 
B 2 350  ALA 350  8    ?    ?   ?   B . n 
B 2 351  PHE 351  9    ?    ?   ?   B . n 
B 2 352  TRP 352  10   ?    ?   ?   B . n 
B 2 353  TYR 353  11   ?    ?   ?   B . n 
B 2 354  ALA 354  12   ?    ?   ?   B . n 
B 2 355  VAL 355  13   ?    ?   ?   B . n 
B 2 356  ARG 356  14   ?    ?   ?   B . n 
B 2 357  THR 357  15   ?    ?   ?   B . n 
B 2 358  ALA 358  16   ?    ?   ?   B . n 
B 2 359  VAL 359  17   ?    ?   ?   B . n 
B 2 360  ILE 360  18   ?    ?   ?   B . n 
B 2 361  ASN 361  19   ?    ?   ?   B . n 
B 2 362  ALA 362  20   ?    ?   ?   B . n 
B 2 363  ALA 363  21   ?    ?   ?   B . n 
B 2 364  SER 364  22   ?    ?   ?   B . n 
B 2 365  GLY 365  23   ?    ?   ?   B . n 
B 2 366  ARG 366  24   ?    ?   ?   B . n 
B 2 367  GLN 367  25   ?    ?   ?   B . n 
B 2 368  THR 368  26   ?    ?   ?   B . n 
B 2 369  VAL 369  27   ?    ?   ?   B . n 
B 2 370  ASP 370  28   ?    ?   ?   B . n 
B 2 371  GLU 371  29   ?    ?   ?   B . n 
B 2 372  ALA 372  30   ?    ?   ?   B . n 
B 2 373  LEU 373  31   ?    ?   ?   B . n 
B 2 374  LYS 374  32   ?    ?   ?   B . n 
B 2 375  ASP 375  33   ?    ?   ?   B . n 
B 2 376  ALA 376  34   ?    ?   ?   B . n 
B 2 377  GLN 377  35   ?    ?   ?   B . n 
B 2 378  THR 378  36   ?    ?   ?   B . n 
B 2 379  GLY 379  37   ?    ?   ?   B . n 
B 2 380  THR 380  38   ?    ?   ?   B . n 
B 2 381  ASP 381  39   ?    ?   ?   B . n 
B 2 382  TYR 382  40   ?    ?   ?   B . n 
B 2 383  ASP 383  41   ?    ?   ?   B . n 
B 2 384  ILE 384  42   ?    ?   ?   B . n 
B 2 385  PRO 385  43   ?    ?   ?   B . n 
B 2 386  THR 386  44   ?    ?   ?   B . n 
B 2 387  THR 387  45   ?    ?   ?   B . n 
B 2 388  LEU 388  46   ?    ?   ?   B . n 
B 2 389  GLU 389  47   ?    ?   ?   B . n 
B 2 390  VAL 390  48   ?    ?   ?   B . n 
B 2 391  LEU 391  49   ?    ?   ?   B . n 
B 2 392  PHE 392  50   ?    ?   ?   B . n 
B 2 393  GLN 393  51   ?    ?   ?   B . n 
B 2 394  GLY 394  52   ?    ?   ?   B . n 
B 2 395  PRO 395  53   ?    ?   ?   B . n 
B 2 396  LEU 396  54   ?    ?   ?   B . n 
B 2 397  GLY 397  55   ?    ?   ?   B . n 
B 2 398  SER 398  56   ?    ?   ?   B . n 
B 2 399  SER 399  57   ?    ?   ?   B . n 
B 2 400  THR 400  58   ?    ?   ?   B . n 
B 2 401  ASP 401  59   ?    ?   ?   B . n 
B 2 402  ASP 402  60   ?    ?   ?   B . n 
B 2 403  ILE 403  61   ?    ?   ?   B . n 
B 2 404  ILE 404  62   ?    ?   ?   B . n 
B 2 405  TRP 405  63   ?    ?   ?   B . n 
B 2 406  ASP 406  64   ?    ?   ?   B . n 
B 2 407  GLN 407  65   ?    ?   ?   B . n 
B 2 408  LEU 408  66   ?    ?   ?   B . n 
B 2 409  ILE 409  67   ?    ?   ?   B . n 
B 2 410  VAL 410  68   ?    ?   ?   B . n 
B 2 411  LYS 411  69   ?    ?   ?   B . n 
B 2 412  ARG 412  70   ?    ?   ?   B . n 
B 2 413  THR 413  71   ?    ?   ?   B . n 
B 2 414  LEU 414  72   ?    ?   ?   B . n 
B 2 415  ALA 415  73   ?    ?   ?   B . n 
B 2 416  ASP 416  74   ?    ?   ?   B . n 
B 2 417  LEU 417  75   ?    ?   ?   B . n 
B 2 418  LEU 418  76   ?    ?   ?   B . n 
B 2 419  ILE 419  77   ?    ?   ?   B . n 
B 2 420  PRO 420  78   ?    ?   ?   B . n 
B 2 421  ILE 421  79   ?    ?   ?   B . n 
B 2 422  ASN 422  80   ?    ?   ?   B . n 
B 2 423  ARG 423  81   ?    ?   ?   B . n 
B 2 424  GLN 424  82   ?    ?   ?   B . n 
B 2 425  ILE 425  83   ?    ?   ?   B . n 
B 2 426  SER 426  84   ?    ?   ?   B . n 
B 2 427  ASP 427  85   ?    ?   ?   B . n 
B 2 428  ILE 428  86   ?    ?   ?   B . n 
B 2 429  GLN 429  87   ?    ?   ?   B . n 
B 2 430  SER 430  88   ?    ?   ?   B . n 
B 2 431  THR 431  89   ?    ?   ?   B . n 
B 2 432  LEU 432  90   ?    ?   ?   B . n 
B 2 433  SER 433  91   ?    ?   ?   B . n 
B 2 434  GLU 434  92   ?    ?   ?   B . n 
B 2 435  VAL 435  93   ?    ?   ?   B . n 
B 2 436  THR 436  94   ?    ?   ?   B . n 
B 2 437  THR 437  95   ?    ?   ?   B . n 
B 2 438  ARG 438  96   ?    ?   ?   B . n 
B 2 439  VAL 439  97   ?    ?   ?   B . n 
B 2 440  HIS 440  98   ?    ?   ?   B . n 
B 2 441  GLU 441  99   ?    ?   ?   B . n 
B 2 442  ILE 442  100  ?    ?   ?   B . n 
B 2 443  GLU 443  101  ?    ?   ?   B . n 
B 2 444  ARG 444  102  ?    ?   ?   B . n 
B 2 445  GLN 445  103  ?    ?   ?   B . n 
B 2 446  LEU 446  104  ?    ?   ?   B . n 
B 2 447  HIS 447  105  ?    ?   ?   B . n 
B 2 448  GLU 448  106  ?    ?   ?   B . n 
B 2 449  ILE 449  107  ?    ?   ?   B . n 
B 2 450  THR 450  108  ?    ?   ?   B . n 
B 2 451  PRO 451  109  ?    ?   ?   B . n 
B 2 452  VAL 452  110  ?    ?   ?   B . n 
B 2 453  LEU 453  111  ?    ?   ?   B . n 
B 2 454  LYS 454  112  ?    ?   ?   B . n 
B 2 455  MET 455  113  113  MET MET B . n 
B 2 456  GLY 456  114  114  GLY GLY B . n 
B 2 457  ARG 457  115  115  ARG ARG B . n 
B 2 458  THR 458  116  116  THR THR B . n 
B 2 459  LEU 459  117  117  LEU LEU B . n 
B 2 460  GLU 460  118  118  GLU GLU B . n 
B 2 461  ALA 461  119  119  ALA ALA B . n 
B 2 462  ILE 462  120  120  ILE ILE B . n 
B 2 463  SER 463  121  121  SER SER B . n 
B 2 464  LYS 464  122  122  LYS LYS B . n 
B 2 465  GLY 465  123  123  GLY GLY B . n 
B 2 466  MET 466  124  124  MET MET B . n 
B 2 467  SER 467  125  125  SER SER B . n 
B 2 468  GLU 468  126  126  GLU GLU B . n 
B 2 469  MET 469  127  127  MET MET B . n 
B 2 470  LEU 470  128  128  LEU LEU B . n 
B 2 471  ALA 471  129  129  ALA ALA B . n 
B 2 472  LYS 472  130  130  LYS LYS B . n 
B 2 473  TYR 473  131  131  TYR TYR B . n 
B 2 474  ASP 474  132  132  ASP ASP B . n 
B 2 475  HIS 475  133  133  HIS HIS B . n 
B 2 476  LEU 476  134  134  LEU LEU B . n 
B 2 477  VAL 477  135  135  VAL VAL B . n 
B 2 478  ILE 478  136  136  ILE ILE B . n 
B 2 479  SER 479  137  137  SER SER B . n 
B 2 480  THR 480  138  138  THR THR B . n 
B 2 481  GLY 481  139  139  GLY GLY B . n 
B 2 482  ARG 482  140  140  ARG ARG B . n 
B 2 483  THR 483  141  141  THR THR B . n 
B 2 484  THR 484  142  142  THR THR B . n 
B 2 485  ALA 485  143  143  ALA ALA B . n 
B 2 486  PRO 486  144  144  PRO PRO B . n 
B 2 487  ALA 487  145  145  ALA ALA B . n 
B 2 488  ALA 488  146  146  ALA ALA B . n 
B 2 489  ALA 489  147  147  ALA ALA B . n 
B 2 490  PHE 490  148  148  PHE PHE B . n 
B 2 491  ASP 491  149  149  ASP ASP B . n 
B 2 492  ALA 492  150  150  ALA ALA B . n 
B 2 493  TYR 493  151  151  TYR TYR B . n 
B 2 494  LEU 494  152  152  LEU LEU B . n 
B 2 495  ASN 495  153  153  ASN ASN B . n 
B 2 496  GLU 496  154  154  GLU GLU B . n 
B 2 497  HIS 497  155  155  HIS HIS B . n 
B 2 498  GLY 498  156  156  GLY GLY B . n 
B 2 499  VAL 499  157  157  VAL VAL B . n 
B 2 500  PRO 500  158  158  PRO PRO B . n 
B 2 501  PRO 501  159  159  PRO PRO B . n 
B 2 502  PRO 502  160  160  PRO PRO B . n 
B 2 503  GLN 503  161  161  GLN GLN B . n 
B 2 504  PRO 504  162  162  PRO PRO B . n 
B 2 505  ALA 505  163  163  ALA ALA B . n 
B 2 506  ILE 506  164  164  ILE ILE B . n 
B 2 507  PHE 507  165  165  PHE PHE B . n 
B 2 508  LYS 508  166  166  LYS LYS B . n 
B 2 509  ASP 509  167  167  ASP ASP B . n 
B 2 510  LEU 510  168  168  LEU LEU B . n 
B 2 511  GLY 511  169  169  GLY GLY B . n 
B 2 512  VAL 512  170  170  VAL VAL B . n 
B 2 513  ALA 513  171  171  ALA ALA B . n 
B 2 514  GLN 514  172  172  GLN GLN B . n 
B 2 515  GLN 515  173  173  GLN GLN B . n 
B 2 516  ALA 516  174  174  ALA ALA B . n 
B 2 517  CYS 517  175  175  CYS CYS B . n 
B 2 518  SER 518  176  176  SER SER B . n 
B 2 519  LYS 519  177  177  LYS LYS B . n 
B 2 520  GLY 520  178  178  GLY GLY B . n 
B 2 521  THR 521  179  179  THR THR B . n 
B 2 522  MET 522  180  180  MET MET B . n 
B 2 523  VAL 523  181  181  VAL VAL B . n 
B 2 524  LYS 524  182  182  LYS LYS B . n 
B 2 525  ASN 525  183  183  ASN ASN B . n 
B 2 526  ALA 526  184  184  ALA ALA B . n 
B 2 527  THR 527  185  185  THR THR B . n 
B 2 528  THR 528  186  186  THR THR B . n 
B 2 529  ASP 529  187  187  ASP ASP B . n 
B 2 530  ALA 530  188  188  ALA ALA B . n 
B 2 531  ALA 531  189  189  ALA ALA B . n 
B 2 532  ASP 532  190  190  ASP ASP B . n 
B 2 533  LYS 533  191  191  LYS LYS B . n 
B 2 534  MET 534  192  192  MET MET B . n 
B 2 535  SER 535  193  193  SER SER B . n 
B 2 536  LYS 536  194  194  LYS LYS B . n 
B 2 537  VAL 537  195  195  VAL VAL B . n 
B 2 538  LEU 538  196  196  LEU LEU B . n 
B 2 539  GLU 539  197  197  GLU GLU B . n 
B 2 540  LEU 540  198  198  LEU LEU B . n 
B 2 541  SER 541  199  199  SER SER B . n 
B 2 542  GLU 542  200  200  GLU GLU B . n 
B 2 543  GLU 543  201  201  GLU GLU B . n 
B 2 544  THR 544  202  202  THR THR B . n 
B 2 545  PHE 545  203  203  PHE PHE B . n 
B 2 546  SER 546  204  204  SER SER B . n 
B 2 547  LYS 547  205  205  LYS LYS B . n 
B 2 548  PRO 548  206  206  PRO PRO B . n 
B 2 549  ASN 549  207  207  ASN ASN B . n 
B 2 550  LEU 550  208  208  LEU LEU B . n 
B 2 551  SER 551  209  209  SER SER B . n 
B 2 552  ALA 552  210  210  ALA ALA B . n 
B 2 553  LYS 553  211  211  LYS LYS B . n 
B 2 554  ASP 554  212  212  ASP ASP B . n 
B 2 555  LEU 555  213  213  LEU LEU B . n 
B 2 556  ALA 556  214  214  ALA ALA B . n 
B 2 557  LEU 557  215  215  LEU LEU B . n 
B 2 558  LEU 558  216  216  LEU LEU B . n 
B 2 559  LEU 559  217  217  LEU LEU B . n 
B 2 560  PHE 560  218  218  PHE PHE B . n 
B 2 561  THR 561  219  219  THR THR B . n 
B 2 562  HIS 562  220  220  HIS HIS B . n 
B 2 563  LEU 563  221  221  LEU LEU B . n 
B 2 564  PRO 564  222  222  PRO PRO B . n 
B 2 565  GLY 565  223  223  GLY GLY B . n 
B 2 566  ASN 566  224  224  ASN ASN B . n 
B 2 567  ASN 567  225  225  ASN ASN B . n 
B 2 568  THR 568  226  226  THR THR B . n 
B 2 569  PRO 569  227  227  PRO PRO B . n 
B 2 570  PHE 570  228  228  PHE PHE B . n 
B 2 571  HIS 571  229  229  HIS HIS B . n 
B 2 572  ILE 572  230  230  ILE ILE B . n 
B 2 573  LEU 573  231  231  LEU LEU B . n 
B 2 574  ALA 574  232  232  ALA ALA B . n 
B 2 575  GLN 575  233  233  GLN GLN B . n 
B 2 576  VAL 576  234  234  VAL VAL B . n 
B 2 577  LEU 577  235  235  LEU LEU B . n 
B 2 578  SER 578  236  236  SER SER B . n 
B 2 579  LYS 579  237  237  LYS LYS B . n 
B 2 580  ILE 580  238  238  ILE ILE B . n 
B 2 581  ALA 581  239  239  ALA ALA B . n 
B 2 582  TYR 582  240  240  TYR TYR B . n 
B 2 583  LYS 583  241  241  LYS LYS B . n 
B 2 584  SER 584  242  242  SER SER B . n 
B 2 585  GLY 585  243  243  GLY GLY B . n 
B 2 586  LYS 586  244  244  LYS LYS B . n 
B 2 587  SER 587  245  245  SER SER B . n 
B 2 588  GLY 588  246  246  GLY GLY B . n 
B 2 589  ALA 589  247  247  ALA ALA B . n 
B 2 590  PHE 590  248  248  PHE PHE B . n 
B 2 591  LEU 591  249  249  LEU LEU B . n 
B 2 592  ASP 592  250  250  ASP ASP B . n 
B 2 593  ALA 593  251  251  ALA ALA B . n 
B 2 594  PHE 594  252  252  PHE PHE B . n 
B 2 595  HIS 595  253  253  HIS HIS B . n 
B 2 596  GLN 596  254  254  GLN GLN B . n 
B 2 597  ILE 597  255  255  ILE ILE B . n 
B 2 598  LEU 598  256  256  LEU LEU B . n 
B 2 599  SER 599  257  257  SER SER B . n 
B 2 600  GLU 600  258  258  GLU GLU B . n 
B 2 601  GLY 601  259  259  GLY GLY B . n 
B 2 602  GLU 602  260  260  GLU GLU B . n 
B 2 603  ASN 603  261  261  ASN ASN B . n 
B 2 604  ALA 604  262  262  ALA ALA B . n 
B 2 605  GLN 605  263  263  GLN GLN B . n 
B 2 606  ALA 606  264  264  ALA ALA B . n 
B 2 607  ALA 607  265  265  ALA ALA B . n 
B 2 608  LEU 608  266  266  LEU LEU B . n 
B 2 609  THR 609  267  267  THR THR B . n 
B 2 610  ARG 610  268  268  ARG ARG B . n 
B 2 611  LEU 611  269  269  LEU LEU B . n 
B 2 612  SER 612  270  270  SER SER B . n 
B 2 613  ARG 613  271  271  ARG ARG B . n 
B 2 614  THR 614  272  272  THR THR B . n 
B 2 615  PHE 615  273  273  PHE PHE B . n 
B 2 616  ASP 616  274  274  ASP ASP B . n 
B 2 617  ALA 617  275  275  ALA ALA B . n 
B 2 618  PHE 618  276  276  PHE PHE B . n 
B 2 619  LEU 619  277  277  LEU LEU B . n 
B 2 620  GLY 620  278  278  GLY GLY B . n 
B 2 621  VAL 621  279  279  VAL VAL B . n 
B 2 622  VAL 622  280  280  VAL VAL B . n 
B 2 623  PRO 623  281  281  PRO PRO B . n 
B 2 624  PRO 624  282  282  PRO PRO B . n 
B 2 625  VAL 625  283  283  VAL VAL B . n 
B 2 626  ILE 626  284  284  ILE ILE B . n 
B 2 627  ARG 627  285  285  ARG ARG B . n 
B 2 628  VAL 628  286  286  VAL VAL B . n 
B 2 629  LYS 629  287  287  LYS LYS B . n 
B 2 630  ASN 630  288  288  ASN ASN B . n 
B 2 631  PHE 631  289  289  PHE PHE B . n 
B 2 632  GLN 632  290  290  GLN GLN B . n 
B 2 633  THR 633  291  291  THR THR B . n 
B 2 634  VAL 634  292  292  VAL VAL B . n 
B 2 635  PRO 635  293  293  PRO PRO B . n 
B 2 636  ARG 636  294  294  ARG ARG B . n 
B 2 637  PRO 637  295  295  PRO PRO B . n 
B 2 638  CYS 638  296  296  CYS CYS B . n 
B 2 639  GLN 639  297  297  GLN GLN B . n 
B 2 640  LYS 640  298  298  LYS LYS B . n 
B 2 641  SER 641  299  299  SER SER B . n 
B 2 642  LEU 642  300  300  LEU LEU B . n 
B 2 643  ARG 643  301  301  ARG ARG B . n 
B 2 644  ALA 644  302  302  ALA ALA B . n 
B 2 645  VAL 645  303  303  VAL VAL B . n 
B 2 646  PRO 646  304  304  PRO PRO B . n 
B 2 647  PRO 647  305  305  PRO PRO B . n 
B 2 648  ASN 648  306  306  ASN ASN B . n 
B 2 649  PRO 649  307  307  PRO PRO B . n 
B 2 650  THR 650  308  308  THR THR B . n 
B 2 651  ILE 651  309  309  ILE ILE B . n 
B 2 652  ASP 652  310  310  ASP ASP B . n 
B 2 653  LYS 653  311  311  LYS LYS B . n 
B 2 654  GLY 654  312  312  GLY GLY B . n 
B 2 655  TRP 655  313  313  TRP TRP B . n 
B 2 656  VAL 656  314  314  VAL VAL B . n 
B 2 657  CYS 657  315  315  CYS CYS B . n 
B 2 658  VAL 658  316  316  VAL VAL B . n 
B 2 659  TYR 659  317  317  TYR TYR B . n 
B 2 660  SER 660  318  318  SER SER B . n 
B 2 661  SER 661  319  319  SER SER B . n 
B 2 662  GLU 662  320  320  GLU GLU B . n 
B 2 663  GLN 663  321  321  GLN GLN B . n 
B 2 664  GLY 664  322  322  GLY GLY B . n 
B 2 665  GLU 665  323  323  GLU GLU B . n 
B 2 666  THR 666  324  324  THR THR B . n 
B 2 667  ARG 667  325  325  ARG ARG B . n 
B 2 668  ALA 668  326  326  ALA ALA B . n 
B 2 669  LEU 669  327  327  LEU LEU B . n 
B 2 670  LYS 670  328  328  LYS LYS B . n 
B 2 671  ILE 671  329  329  ILE ILE B . n 
C 2 1    MET 1    -341 ?    ?   ?   C . n 
C 2 2    GLY 2    -340 ?    ?   ?   C . n 
C 2 3    SER 3    -339 ?    ?   ?   C . n 
C 2 4    SER 4    -338 ?    ?   ?   C . n 
C 2 5    HIS 5    -337 ?    ?   ?   C . n 
C 2 6    HIS 6    -336 ?    ?   ?   C . n 
C 2 7    HIS 7    -335 ?    ?   ?   C . n 
C 2 8    HIS 8    -334 ?    ?   ?   C . n 
C 2 9    HIS 9    -333 ?    ?   ?   C . n 
C 2 10   HIS 10   -332 ?    ?   ?   C . n 
C 2 11   GLY 11   -331 ?    ?   ?   C . n 
C 2 12   THR 12   -330 ?    ?   ?   C . n 
C 2 13   LYS 13   -329 ?    ?   ?   C . n 
C 2 14   THR 14   -328 ?    ?   ?   C . n 
C 2 15   GLU 15   -327 ?    ?   ?   C . n 
C 2 16   GLU 16   -326 ?    ?   ?   C . n 
C 2 17   GLY 17   -325 ?    ?   ?   C . n 
C 2 18   LYS 18   -324 ?    ?   ?   C . n 
C 2 19   LEU 19   -323 ?    ?   ?   C . n 
C 2 20   VAL 20   -322 ?    ?   ?   C . n 
C 2 21   ILE 21   -321 ?    ?   ?   C . n 
C 2 22   TRP 22   -320 ?    ?   ?   C . n 
C 2 23   ILE 23   -319 ?    ?   ?   C . n 
C 2 24   ASN 24   -318 ?    ?   ?   C . n 
C 2 25   GLY 25   -317 ?    ?   ?   C . n 
C 2 26   ASP 26   -316 ?    ?   ?   C . n 
C 2 27   LYS 27   -315 ?    ?   ?   C . n 
C 2 28   GLY 28   -314 ?    ?   ?   C . n 
C 2 29   TYR 29   -313 ?    ?   ?   C . n 
C 2 30   ASN 30   -312 ?    ?   ?   C . n 
C 2 31   GLY 31   -311 ?    ?   ?   C . n 
C 2 32   LEU 32   -310 ?    ?   ?   C . n 
C 2 33   ALA 33   -309 ?    ?   ?   C . n 
C 2 34   GLU 34   -308 ?    ?   ?   C . n 
C 2 35   VAL 35   -307 ?    ?   ?   C . n 
C 2 36   GLY 36   -306 ?    ?   ?   C . n 
C 2 37   LYS 37   -305 ?    ?   ?   C . n 
C 2 38   LYS 38   -304 ?    ?   ?   C . n 
C 2 39   PHE 39   -303 ?    ?   ?   C . n 
C 2 40   GLU 40   -302 ?    ?   ?   C . n 
C 2 41   LYS 41   -301 ?    ?   ?   C . n 
C 2 42   ASP 42   -300 ?    ?   ?   C . n 
C 2 43   THR 43   -299 ?    ?   ?   C . n 
C 2 44   GLY 44   -298 ?    ?   ?   C . n 
C 2 45   ILE 45   -297 ?    ?   ?   C . n 
C 2 46   LYS 46   -296 ?    ?   ?   C . n 
C 2 47   VAL 47   -295 ?    ?   ?   C . n 
C 2 48   THR 48   -294 ?    ?   ?   C . n 
C 2 49   VAL 49   -293 ?    ?   ?   C . n 
C 2 50   GLU 50   -292 ?    ?   ?   C . n 
C 2 51   HIS 51   -291 ?    ?   ?   C . n 
C 2 52   PRO 52   -290 ?    ?   ?   C . n 
C 2 53   ASP 53   -289 ?    ?   ?   C . n 
C 2 54   LYS 54   -288 ?    ?   ?   C . n 
C 2 55   LEU 55   -287 ?    ?   ?   C . n 
C 2 56   GLU 56   -286 ?    ?   ?   C . n 
C 2 57   GLU 57   -285 ?    ?   ?   C . n 
C 2 58   LYS 58   -284 ?    ?   ?   C . n 
C 2 59   PHE 59   -283 ?    ?   ?   C . n 
C 2 60   PRO 60   -282 ?    ?   ?   C . n 
C 2 61   GLN 61   -281 ?    ?   ?   C . n 
C 2 62   VAL 62   -280 ?    ?   ?   C . n 
C 2 63   ALA 63   -279 ?    ?   ?   C . n 
C 2 64   ALA 64   -278 ?    ?   ?   C . n 
C 2 65   THR 65   -277 ?    ?   ?   C . n 
C 2 66   GLY 66   -276 ?    ?   ?   C . n 
C 2 67   ASP 67   -275 ?    ?   ?   C . n 
C 2 68   GLY 68   -274 ?    ?   ?   C . n 
C 2 69   PRO 69   -273 ?    ?   ?   C . n 
C 2 70   ASP 70   -272 ?    ?   ?   C . n 
C 2 71   ILE 71   -271 ?    ?   ?   C . n 
C 2 72   ILE 72   -270 ?    ?   ?   C . n 
C 2 73   PHE 73   -269 ?    ?   ?   C . n 
C 2 74   TRP 74   -268 ?    ?   ?   C . n 
C 2 75   ALA 75   -267 ?    ?   ?   C . n 
C 2 76   HIS 76   -266 ?    ?   ?   C . n 
C 2 77   ASP 77   -265 ?    ?   ?   C . n 
C 2 78   ARG 78   -264 ?    ?   ?   C . n 
C 2 79   PHE 79   -263 ?    ?   ?   C . n 
C 2 80   GLY 80   -262 ?    ?   ?   C . n 
C 2 81   GLY 81   -261 ?    ?   ?   C . n 
C 2 82   TYR 82   -260 ?    ?   ?   C . n 
C 2 83   ALA 83   -259 ?    ?   ?   C . n 
C 2 84   GLN 84   -258 ?    ?   ?   C . n 
C 2 85   SER 85   -257 ?    ?   ?   C . n 
C 2 86   GLY 86   -256 ?    ?   ?   C . n 
C 2 87   LEU 87   -255 ?    ?   ?   C . n 
C 2 88   LEU 88   -254 ?    ?   ?   C . n 
C 2 89   ALA 89   -253 ?    ?   ?   C . n 
C 2 90   GLU 90   -252 ?    ?   ?   C . n 
C 2 91   ILE 91   -251 ?    ?   ?   C . n 
C 2 92   THR 92   -250 ?    ?   ?   C . n 
C 2 93   PRO 93   -249 ?    ?   ?   C . n 
C 2 94   ASP 94   -248 ?    ?   ?   C . n 
C 2 95   LYS 95   -247 ?    ?   ?   C . n 
C 2 96   ALA 96   -246 ?    ?   ?   C . n 
C 2 97   PHE 97   -245 ?    ?   ?   C . n 
C 2 98   GLN 98   -244 ?    ?   ?   C . n 
C 2 99   ASP 99   -243 ?    ?   ?   C . n 
C 2 100  LYS 100  -242 ?    ?   ?   C . n 
C 2 101  LEU 101  -241 ?    ?   ?   C . n 
C 2 102  TYR 102  -240 ?    ?   ?   C . n 
C 2 103  PRO 103  -239 ?    ?   ?   C . n 
C 2 104  PHE 104  -238 ?    ?   ?   C . n 
C 2 105  THR 105  -237 ?    ?   ?   C . n 
C 2 106  TRP 106  -236 ?    ?   ?   C . n 
C 2 107  ASP 107  -235 ?    ?   ?   C . n 
C 2 108  ALA 108  -234 ?    ?   ?   C . n 
C 2 109  VAL 109  -233 ?    ?   ?   C . n 
C 2 110  ARG 110  -232 ?    ?   ?   C . n 
C 2 111  TYR 111  -231 ?    ?   ?   C . n 
C 2 112  ASN 112  -230 ?    ?   ?   C . n 
C 2 113  GLY 113  -229 ?    ?   ?   C . n 
C 2 114  LYS 114  -228 ?    ?   ?   C . n 
C 2 115  LEU 115  -227 ?    ?   ?   C . n 
C 2 116  ILE 116  -226 ?    ?   ?   C . n 
C 2 117  ALA 117  -225 ?    ?   ?   C . n 
C 2 118  TYR 118  -224 ?    ?   ?   C . n 
C 2 119  PRO 119  -223 ?    ?   ?   C . n 
C 2 120  ILE 120  -222 ?    ?   ?   C . n 
C 2 121  ALA 121  -221 ?    ?   ?   C . n 
C 2 122  VAL 122  -220 ?    ?   ?   C . n 
C 2 123  GLU 123  -219 ?    ?   ?   C . n 
C 2 124  ALA 124  -218 ?    ?   ?   C . n 
C 2 125  LEU 125  -217 ?    ?   ?   C . n 
C 2 126  SER 126  -216 ?    ?   ?   C . n 
C 2 127  LEU 127  -215 ?    ?   ?   C . n 
C 2 128  ILE 128  -214 ?    ?   ?   C . n 
C 2 129  TYR 129  -213 ?    ?   ?   C . n 
C 2 130  ASN 130  -212 ?    ?   ?   C . n 
C 2 131  LYS 131  -211 ?    ?   ?   C . n 
C 2 132  ASP 132  -210 ?    ?   ?   C . n 
C 2 133  LEU 133  -209 ?    ?   ?   C . n 
C 2 134  LEU 134  -208 ?    ?   ?   C . n 
C 2 135  PRO 135  -207 ?    ?   ?   C . n 
C 2 136  ASN 136  -206 ?    ?   ?   C . n 
C 2 137  PRO 137  -205 ?    ?   ?   C . n 
C 2 138  PRO 138  -204 ?    ?   ?   C . n 
C 2 139  LYS 139  -203 ?    ?   ?   C . n 
C 2 140  THR 140  -202 ?    ?   ?   C . n 
C 2 141  TRP 141  -201 ?    ?   ?   C . n 
C 2 142  GLU 142  -200 ?    ?   ?   C . n 
C 2 143  GLU 143  -199 ?    ?   ?   C . n 
C 2 144  ILE 144  -198 ?    ?   ?   C . n 
C 2 145  PRO 145  -197 ?    ?   ?   C . n 
C 2 146  ALA 146  -196 ?    ?   ?   C . n 
C 2 147  LEU 147  -195 ?    ?   ?   C . n 
C 2 148  ASP 148  -194 ?    ?   ?   C . n 
C 2 149  LYS 149  -193 ?    ?   ?   C . n 
C 2 150  GLU 150  -192 ?    ?   ?   C . n 
C 2 151  LEU 151  -191 ?    ?   ?   C . n 
C 2 152  LYS 152  -190 ?    ?   ?   C . n 
C 2 153  ALA 153  -189 ?    ?   ?   C . n 
C 2 154  LYS 154  -188 ?    ?   ?   C . n 
C 2 155  GLY 155  -187 ?    ?   ?   C . n 
C 2 156  LYS 156  -186 ?    ?   ?   C . n 
C 2 157  SER 157  -185 ?    ?   ?   C . n 
C 2 158  ALA 158  -184 ?    ?   ?   C . n 
C 2 159  LEU 159  -183 ?    ?   ?   C . n 
C 2 160  MET 160  -182 ?    ?   ?   C . n 
C 2 161  PHE 161  -181 ?    ?   ?   C . n 
C 2 162  ASN 162  -180 ?    ?   ?   C . n 
C 2 163  LEU 163  -179 ?    ?   ?   C . n 
C 2 164  GLN 164  -178 ?    ?   ?   C . n 
C 2 165  GLU 165  -177 ?    ?   ?   C . n 
C 2 166  PRO 166  -176 ?    ?   ?   C . n 
C 2 167  TYR 167  -175 ?    ?   ?   C . n 
C 2 168  PHE 168  -174 ?    ?   ?   C . n 
C 2 169  THR 169  -173 ?    ?   ?   C . n 
C 2 170  TRP 170  -172 ?    ?   ?   C . n 
C 2 171  PRO 171  -171 ?    ?   ?   C . n 
C 2 172  LEU 172  -170 ?    ?   ?   C . n 
C 2 173  ILE 173  -169 ?    ?   ?   C . n 
C 2 174  ALA 174  -168 ?    ?   ?   C . n 
C 2 175  ALA 175  -167 ?    ?   ?   C . n 
C 2 176  ASP 176  -166 ?    ?   ?   C . n 
C 2 177  GLY 177  -165 ?    ?   ?   C . n 
C 2 178  GLY 178  -164 ?    ?   ?   C . n 
C 2 179  TYR 179  -163 ?    ?   ?   C . n 
C 2 180  ALA 180  -162 ?    ?   ?   C . n 
C 2 181  PHE 181  -161 ?    ?   ?   C . n 
C 2 182  LYS 182  -160 ?    ?   ?   C . n 
C 2 183  TYR 183  -159 ?    ?   ?   C . n 
C 2 184  GLU 184  -158 ?    ?   ?   C . n 
C 2 185  ASN 185  -157 ?    ?   ?   C . n 
C 2 186  GLY 186  -156 ?    ?   ?   C . n 
C 2 187  LYS 187  -155 ?    ?   ?   C . n 
C 2 188  TYR 188  -154 ?    ?   ?   C . n 
C 2 189  ASP 189  -153 ?    ?   ?   C . n 
C 2 190  ILE 190  -152 ?    ?   ?   C . n 
C 2 191  LYS 191  -151 ?    ?   ?   C . n 
C 2 192  ASP 192  -150 ?    ?   ?   C . n 
C 2 193  VAL 193  -149 ?    ?   ?   C . n 
C 2 194  GLY 194  -148 ?    ?   ?   C . n 
C 2 195  VAL 195  -147 ?    ?   ?   C . n 
C 2 196  ASP 196  -146 ?    ?   ?   C . n 
C 2 197  ASN 197  -145 ?    ?   ?   C . n 
C 2 198  ALA 198  -144 ?    ?   ?   C . n 
C 2 199  GLY 199  -143 ?    ?   ?   C . n 
C 2 200  ALA 200  -142 ?    ?   ?   C . n 
C 2 201  LYS 201  -141 ?    ?   ?   C . n 
C 2 202  ALA 202  -140 ?    ?   ?   C . n 
C 2 203  GLY 203  -139 ?    ?   ?   C . n 
C 2 204  LEU 204  -138 ?    ?   ?   C . n 
C 2 205  THR 205  -137 ?    ?   ?   C . n 
C 2 206  PHE 206  -136 ?    ?   ?   C . n 
C 2 207  LEU 207  -135 ?    ?   ?   C . n 
C 2 208  VAL 208  -134 ?    ?   ?   C . n 
C 2 209  ASP 209  -133 ?    ?   ?   C . n 
C 2 210  LEU 210  -132 ?    ?   ?   C . n 
C 2 211  ILE 211  -131 ?    ?   ?   C . n 
C 2 212  LYS 212  -130 ?    ?   ?   C . n 
C 2 213  ASN 213  -129 ?    ?   ?   C . n 
C 2 214  LYS 214  -128 ?    ?   ?   C . n 
C 2 215  HIS 215  -127 ?    ?   ?   C . n 
C 2 216  MET 216  -126 ?    ?   ?   C . n 
C 2 217  ASN 217  -125 ?    ?   ?   C . n 
C 2 218  ALA 218  -124 ?    ?   ?   C . n 
C 2 219  ASP 219  -123 ?    ?   ?   C . n 
C 2 220  THR 220  -122 ?    ?   ?   C . n 
C 2 221  ASP 221  -121 ?    ?   ?   C . n 
C 2 222  TYR 222  -120 ?    ?   ?   C . n 
C 2 223  SER 223  -119 ?    ?   ?   C . n 
C 2 224  ILE 224  -118 ?    ?   ?   C . n 
C 2 225  ALA 225  -117 ?    ?   ?   C . n 
C 2 226  GLU 226  -116 ?    ?   ?   C . n 
C 2 227  ALA 227  -115 ?    ?   ?   C . n 
C 2 228  ALA 228  -114 ?    ?   ?   C . n 
C 2 229  PHE 229  -113 ?    ?   ?   C . n 
C 2 230  ASN 230  -112 ?    ?   ?   C . n 
C 2 231  LYS 231  -111 ?    ?   ?   C . n 
C 2 232  GLY 232  -110 ?    ?   ?   C . n 
C 2 233  GLU 233  -109 ?    ?   ?   C . n 
C 2 234  THR 234  -108 ?    ?   ?   C . n 
C 2 235  ALA 235  -107 ?    ?   ?   C . n 
C 2 236  MET 236  -106 ?    ?   ?   C . n 
C 2 237  THR 237  -105 ?    ?   ?   C . n 
C 2 238  ILE 238  -104 ?    ?   ?   C . n 
C 2 239  ASN 239  -103 ?    ?   ?   C . n 
C 2 240  GLY 240  -102 ?    ?   ?   C . n 
C 2 241  PRO 241  -101 ?    ?   ?   C . n 
C 2 242  TRP 242  -100 ?    ?   ?   C . n 
C 2 243  ALA 243  -99  ?    ?   ?   C . n 
C 2 244  TRP 244  -98  ?    ?   ?   C . n 
C 2 245  SER 245  -97  ?    ?   ?   C . n 
C 2 246  ASN 246  -96  ?    ?   ?   C . n 
C 2 247  ILE 247  -95  ?    ?   ?   C . n 
C 2 248  ASP 248  -94  ?    ?   ?   C . n 
C 2 249  THR 249  -93  ?    ?   ?   C . n 
C 2 250  SER 250  -92  ?    ?   ?   C . n 
C 2 251  LYS 251  -91  ?    ?   ?   C . n 
C 2 252  VAL 252  -90  ?    ?   ?   C . n 
C 2 253  ASN 253  -89  ?    ?   ?   C . n 
C 2 254  TYR 254  -88  ?    ?   ?   C . n 
C 2 255  GLY 255  -87  ?    ?   ?   C . n 
C 2 256  VAL 256  -86  ?    ?   ?   C . n 
C 2 257  THR 257  -85  ?    ?   ?   C . n 
C 2 258  VAL 258  -84  ?    ?   ?   C . n 
C 2 259  LEU 259  -83  ?    ?   ?   C . n 
C 2 260  PRO 260  -82  ?    ?   ?   C . n 
C 2 261  THR 261  -81  ?    ?   ?   C . n 
C 2 262  PHE 262  -80  ?    ?   ?   C . n 
C 2 263  LYS 263  -79  ?    ?   ?   C . n 
C 2 264  GLY 264  -78  ?    ?   ?   C . n 
C 2 265  GLN 265  -77  ?    ?   ?   C . n 
C 2 266  PRO 266  -76  ?    ?   ?   C . n 
C 2 267  SER 267  -75  ?    ?   ?   C . n 
C 2 268  LYS 268  -74  ?    ?   ?   C . n 
C 2 269  PRO 269  -73  ?    ?   ?   C . n 
C 2 270  PHE 270  -72  ?    ?   ?   C . n 
C 2 271  VAL 271  -71  ?    ?   ?   C . n 
C 2 272  GLY 272  -70  ?    ?   ?   C . n 
C 2 273  VAL 273  -69  ?    ?   ?   C . n 
C 2 274  LEU 274  -68  ?    ?   ?   C . n 
C 2 275  SER 275  -67  ?    ?   ?   C . n 
C 2 276  ALA 276  -66  ?    ?   ?   C . n 
C 2 277  GLY 277  -65  ?    ?   ?   C . n 
C 2 278  ILE 278  -64  ?    ?   ?   C . n 
C 2 279  ASN 279  -63  ?    ?   ?   C . n 
C 2 280  ALA 280  -62  ?    ?   ?   C . n 
C 2 281  ALA 281  -61  ?    ?   ?   C . n 
C 2 282  SER 282  -60  ?    ?   ?   C . n 
C 2 283  PRO 283  -59  ?    ?   ?   C . n 
C 2 284  ASN 284  -58  ?    ?   ?   C . n 
C 2 285  LYS 285  -57  ?    ?   ?   C . n 
C 2 286  GLU 286  -56  ?    ?   ?   C . n 
C 2 287  LEU 287  -55  ?    ?   ?   C . n 
C 2 288  ALA 288  -54  ?    ?   ?   C . n 
C 2 289  LYS 289  -53  ?    ?   ?   C . n 
C 2 290  GLU 290  -52  ?    ?   ?   C . n 
C 2 291  PHE 291  -51  ?    ?   ?   C . n 
C 2 292  LEU 292  -50  ?    ?   ?   C . n 
C 2 293  GLU 293  -49  ?    ?   ?   C . n 
C 2 294  ASN 294  -48  ?    ?   ?   C . n 
C 2 295  TYR 295  -47  ?    ?   ?   C . n 
C 2 296  LEU 296  -46  ?    ?   ?   C . n 
C 2 297  LEU 297  -45  ?    ?   ?   C . n 
C 2 298  THR 298  -44  ?    ?   ?   C . n 
C 2 299  ASP 299  -43  ?    ?   ?   C . n 
C 2 300  GLU 300  -42  ?    ?   ?   C . n 
C 2 301  GLY 301  -41  ?    ?   ?   C . n 
C 2 302  LEU 302  -40  ?    ?   ?   C . n 
C 2 303  GLU 303  -39  ?    ?   ?   C . n 
C 2 304  ALA 304  -38  ?    ?   ?   C . n 
C 2 305  VAL 305  -37  ?    ?   ?   C . n 
C 2 306  ASN 306  -36  ?    ?   ?   C . n 
C 2 307  LYS 307  -35  ?    ?   ?   C . n 
C 2 308  ASP 308  -34  ?    ?   ?   C . n 
C 2 309  LYS 309  -33  ?    ?   ?   C . n 
C 2 310  PRO 310  -32  ?    ?   ?   C . n 
C 2 311  LEU 311  -31  ?    ?   ?   C . n 
C 2 312  GLY 312  -30  ?    ?   ?   C . n 
C 2 313  ALA 313  -29  ?    ?   ?   C . n 
C 2 314  VAL 314  -28  ?    ?   ?   C . n 
C 2 315  ALA 315  -27  ?    ?   ?   C . n 
C 2 316  LEU 316  -26  ?    ?   ?   C . n 
C 2 317  LYS 317  -25  ?    ?   ?   C . n 
C 2 318  SER 318  -24  ?    ?   ?   C . n 
C 2 319  TYR 319  -23  ?    ?   ?   C . n 
C 2 320  GLU 320  -22  ?    ?   ?   C . n 
C 2 321  GLU 321  -21  ?    ?   ?   C . n 
C 2 322  GLU 322  -20  ?    ?   ?   C . n 
C 2 323  LEU 323  -19  ?    ?   ?   C . n 
C 2 324  ALA 324  -18  ?    ?   ?   C . n 
C 2 325  LYS 325  -17  ?    ?   ?   C . n 
C 2 326  ASP 326  -16  ?    ?   ?   C . n 
C 2 327  PRO 327  -15  ?    ?   ?   C . n 
C 2 328  ARG 328  -14  ?    ?   ?   C . n 
C 2 329  ILE 329  -13  ?    ?   ?   C . n 
C 2 330  ALA 330  -12  ?    ?   ?   C . n 
C 2 331  ALA 331  -11  ?    ?   ?   C . n 
C 2 332  THR 332  -10  ?    ?   ?   C . n 
C 2 333  MET 333  -9   ?    ?   ?   C . n 
C 2 334  GLU 334  -8   ?    ?   ?   C . n 
C 2 335  ASN 335  -7   ?    ?   ?   C . n 
C 2 336  ALA 336  -6   ?    ?   ?   C . n 
C 2 337  GLN 337  -5   ?    ?   ?   C . n 
C 2 338  LYS 338  -4   ?    ?   ?   C . n 
C 2 339  GLY 339  -3   ?    ?   ?   C . n 
C 2 340  GLU 340  -2   ?    ?   ?   C . n 
C 2 341  ILE 341  -1   ?    ?   ?   C . n 
C 2 342  MET 342  0    ?    ?   ?   C . n 
C 2 343  PRO 343  1    ?    ?   ?   C . n 
C 2 344  ASN 344  2    ?    ?   ?   C . n 
C 2 345  ILE 345  3    ?    ?   ?   C . n 
C 2 346  PRO 346  4    ?    ?   ?   C . n 
C 2 347  GLN 347  5    ?    ?   ?   C . n 
C 2 348  MET 348  6    ?    ?   ?   C . n 
C 2 349  SER 349  7    ?    ?   ?   C . n 
C 2 350  ALA 350  8    ?    ?   ?   C . n 
C 2 351  PHE 351  9    ?    ?   ?   C . n 
C 2 352  TRP 352  10   ?    ?   ?   C . n 
C 2 353  TYR 353  11   ?    ?   ?   C . n 
C 2 354  ALA 354  12   ?    ?   ?   C . n 
C 2 355  VAL 355  13   ?    ?   ?   C . n 
C 2 356  ARG 356  14   ?    ?   ?   C . n 
C 2 357  THR 357  15   ?    ?   ?   C . n 
C 2 358  ALA 358  16   ?    ?   ?   C . n 
C 2 359  VAL 359  17   ?    ?   ?   C . n 
C 2 360  ILE 360  18   ?    ?   ?   C . n 
C 2 361  ASN 361  19   ?    ?   ?   C . n 
C 2 362  ALA 362  20   ?    ?   ?   C . n 
C 2 363  ALA 363  21   ?    ?   ?   C . n 
C 2 364  SER 364  22   ?    ?   ?   C . n 
C 2 365  GLY 365  23   ?    ?   ?   C . n 
C 2 366  ARG 366  24   ?    ?   ?   C . n 
C 2 367  GLN 367  25   ?    ?   ?   C . n 
C 2 368  THR 368  26   ?    ?   ?   C . n 
C 2 369  VAL 369  27   ?    ?   ?   C . n 
C 2 370  ASP 370  28   ?    ?   ?   C . n 
C 2 371  GLU 371  29   ?    ?   ?   C . n 
C 2 372  ALA 372  30   ?    ?   ?   C . n 
C 2 373  LEU 373  31   ?    ?   ?   C . n 
C 2 374  LYS 374  32   ?    ?   ?   C . n 
C 2 375  ASP 375  33   ?    ?   ?   C . n 
C 2 376  ALA 376  34   ?    ?   ?   C . n 
C 2 377  GLN 377  35   ?    ?   ?   C . n 
C 2 378  THR 378  36   ?    ?   ?   C . n 
C 2 379  GLY 379  37   ?    ?   ?   C . n 
C 2 380  THR 380  38   ?    ?   ?   C . n 
C 2 381  ASP 381  39   ?    ?   ?   C . n 
C 2 382  TYR 382  40   ?    ?   ?   C . n 
C 2 383  ASP 383  41   ?    ?   ?   C . n 
C 2 384  ILE 384  42   ?    ?   ?   C . n 
C 2 385  PRO 385  43   ?    ?   ?   C . n 
C 2 386  THR 386  44   ?    ?   ?   C . n 
C 2 387  THR 387  45   ?    ?   ?   C . n 
C 2 388  LEU 388  46   ?    ?   ?   C . n 
C 2 389  GLU 389  47   ?    ?   ?   C . n 
C 2 390  VAL 390  48   ?    ?   ?   C . n 
C 2 391  LEU 391  49   ?    ?   ?   C . n 
C 2 392  PHE 392  50   ?    ?   ?   C . n 
C 2 393  GLN 393  51   ?    ?   ?   C . n 
C 2 394  GLY 394  52   ?    ?   ?   C . n 
C 2 395  PRO 395  53   ?    ?   ?   C . n 
C 2 396  LEU 396  54   ?    ?   ?   C . n 
C 2 397  GLY 397  55   ?    ?   ?   C . n 
C 2 398  SER 398  56   ?    ?   ?   C . n 
C 2 399  SER 399  57   ?    ?   ?   C . n 
C 2 400  THR 400  58   ?    ?   ?   C . n 
C 2 401  ASP 401  59   ?    ?   ?   C . n 
C 2 402  ASP 402  60   ?    ?   ?   C . n 
C 2 403  ILE 403  61   ?    ?   ?   C . n 
C 2 404  ILE 404  62   ?    ?   ?   C . n 
C 2 405  TRP 405  63   ?    ?   ?   C . n 
C 2 406  ASP 406  64   ?    ?   ?   C . n 
C 2 407  GLN 407  65   ?    ?   ?   C . n 
C 2 408  LEU 408  66   ?    ?   ?   C . n 
C 2 409  ILE 409  67   ?    ?   ?   C . n 
C 2 410  VAL 410  68   ?    ?   ?   C . n 
C 2 411  LYS 411  69   ?    ?   ?   C . n 
C 2 412  ARG 412  70   ?    ?   ?   C . n 
C 2 413  THR 413  71   ?    ?   ?   C . n 
C 2 414  LEU 414  72   ?    ?   ?   C . n 
C 2 415  ALA 415  73   ?    ?   ?   C . n 
C 2 416  ASP 416  74   ?    ?   ?   C . n 
C 2 417  LEU 417  75   ?    ?   ?   C . n 
C 2 418  LEU 418  76   ?    ?   ?   C . n 
C 2 419  ILE 419  77   ?    ?   ?   C . n 
C 2 420  PRO 420  78   ?    ?   ?   C . n 
C 2 421  ILE 421  79   ?    ?   ?   C . n 
C 2 422  ASN 422  80   ?    ?   ?   C . n 
C 2 423  ARG 423  81   ?    ?   ?   C . n 
C 2 424  GLN 424  82   ?    ?   ?   C . n 
C 2 425  ILE 425  83   ?    ?   ?   C . n 
C 2 426  SER 426  84   ?    ?   ?   C . n 
C 2 427  ASP 427  85   ?    ?   ?   C . n 
C 2 428  ILE 428  86   ?    ?   ?   C . n 
C 2 429  GLN 429  87   ?    ?   ?   C . n 
C 2 430  SER 430  88   ?    ?   ?   C . n 
C 2 431  THR 431  89   ?    ?   ?   C . n 
C 2 432  LEU 432  90   ?    ?   ?   C . n 
C 2 433  SER 433  91   ?    ?   ?   C . n 
C 2 434  GLU 434  92   ?    ?   ?   C . n 
C 2 435  VAL 435  93   ?    ?   ?   C . n 
C 2 436  THR 436  94   ?    ?   ?   C . n 
C 2 437  THR 437  95   ?    ?   ?   C . n 
C 2 438  ARG 438  96   ?    ?   ?   C . n 
C 2 439  VAL 439  97   ?    ?   ?   C . n 
C 2 440  HIS 440  98   ?    ?   ?   C . n 
C 2 441  GLU 441  99   ?    ?   ?   C . n 
C 2 442  ILE 442  100  ?    ?   ?   C . n 
C 2 443  GLU 443  101  ?    ?   ?   C . n 
C 2 444  ARG 444  102  ?    ?   ?   C . n 
C 2 445  GLN 445  103  ?    ?   ?   C . n 
C 2 446  LEU 446  104  ?    ?   ?   C . n 
C 2 447  HIS 447  105  ?    ?   ?   C . n 
C 2 448  GLU 448  106  ?    ?   ?   C . n 
C 2 449  ILE 449  107  ?    ?   ?   C . n 
C 2 450  THR 450  108  ?    ?   ?   C . n 
C 2 451  PRO 451  109  ?    ?   ?   C . n 
C 2 452  VAL 452  110  110  VAL VAL C . n 
C 2 453  LEU 453  111  111  LEU LEU C . n 
C 2 454  LYS 454  112  112  LYS LYS C . n 
C 2 455  MET 455  113  113  MET MET C . n 
C 2 456  GLY 456  114  114  GLY GLY C . n 
C 2 457  ARG 457  115  115  ARG ARG C . n 
C 2 458  THR 458  116  116  THR THR C . n 
C 2 459  LEU 459  117  117  LEU LEU C . n 
C 2 460  GLU 460  118  118  GLU GLU C . n 
C 2 461  ALA 461  119  119  ALA ALA C . n 
C 2 462  ILE 462  120  120  ILE ILE C . n 
C 2 463  SER 463  121  121  SER SER C . n 
C 2 464  LYS 464  122  122  LYS LYS C . n 
C 2 465  GLY 465  123  123  GLY GLY C . n 
C 2 466  MET 466  124  124  MET MET C . n 
C 2 467  SER 467  125  125  SER SER C . n 
C 2 468  GLU 468  126  126  GLU GLU C . n 
C 2 469  MET 469  127  127  MET MET C . n 
C 2 470  LEU 470  128  128  LEU LEU C . n 
C 2 471  ALA 471  129  129  ALA ALA C . n 
C 2 472  LYS 472  130  130  LYS LYS C . n 
C 2 473  TYR 473  131  131  TYR TYR C . n 
C 2 474  ASP 474  132  132  ASP ASP C . n 
C 2 475  HIS 475  133  133  HIS HIS C . n 
C 2 476  LEU 476  134  134  LEU LEU C . n 
C 2 477  VAL 477  135  135  VAL VAL C . n 
C 2 478  ILE 478  136  136  ILE ILE C . n 
C 2 479  SER 479  137  137  SER SER C . n 
C 2 480  THR 480  138  138  THR THR C . n 
C 2 481  GLY 481  139  139  GLY GLY C . n 
C 2 482  ARG 482  140  140  ARG ARG C . n 
C 2 483  THR 483  141  141  THR THR C . n 
C 2 484  THR 484  142  142  THR THR C . n 
C 2 485  ALA 485  143  143  ALA ALA C . n 
C 2 486  PRO 486  144  144  PRO PRO C . n 
C 2 487  ALA 487  145  145  ALA ALA C . n 
C 2 488  ALA 488  146  146  ALA ALA C . n 
C 2 489  ALA 489  147  147  ALA ALA C . n 
C 2 490  PHE 490  148  148  PHE PHE C . n 
C 2 491  ASP 491  149  149  ASP ASP C . n 
C 2 492  ALA 492  150  150  ALA ALA C . n 
C 2 493  TYR 493  151  151  TYR TYR C . n 
C 2 494  LEU 494  152  152  LEU LEU C . n 
C 2 495  ASN 495  153  153  ASN ASN C . n 
C 2 496  GLU 496  154  154  GLU GLU C . n 
C 2 497  HIS 497  155  155  HIS HIS C . n 
C 2 498  GLY 498  156  156  GLY GLY C . n 
C 2 499  VAL 499  157  157  VAL VAL C . n 
C 2 500  PRO 500  158  158  PRO PRO C . n 
C 2 501  PRO 501  159  159  PRO PRO C . n 
C 2 502  PRO 502  160  160  PRO PRO C . n 
C 2 503  GLN 503  161  161  GLN GLN C . n 
C 2 504  PRO 504  162  162  PRO PRO C . n 
C 2 505  ALA 505  163  163  ALA ALA C . n 
C 2 506  ILE 506  164  164  ILE ILE C . n 
C 2 507  PHE 507  165  165  PHE PHE C . n 
C 2 508  LYS 508  166  166  LYS LYS C . n 
C 2 509  ASP 509  167  167  ASP ASP C . n 
C 2 510  LEU 510  168  168  LEU LEU C . n 
C 2 511  GLY 511  169  169  GLY GLY C . n 
C 2 512  VAL 512  170  170  VAL VAL C . n 
C 2 513  ALA 513  171  171  ALA ALA C . n 
C 2 514  GLN 514  172  172  GLN GLN C . n 
C 2 515  GLN 515  173  ?    ?   ?   C . n 
C 2 516  ALA 516  174  ?    ?   ?   C . n 
C 2 517  CYS 517  175  ?    ?   ?   C . n 
C 2 518  SER 518  176  ?    ?   ?   C . n 
C 2 519  LYS 519  177  ?    ?   ?   C . n 
C 2 520  GLY 520  178  ?    ?   ?   C . n 
C 2 521  THR 521  179  ?    ?   ?   C . n 
C 2 522  MET 522  180  ?    ?   ?   C . n 
C 2 523  VAL 523  181  ?    ?   ?   C . n 
C 2 524  LYS 524  182  ?    ?   ?   C . n 
C 2 525  ASN 525  183  ?    ?   ?   C . n 
C 2 526  ALA 526  184  ?    ?   ?   C . n 
C 2 527  THR 527  185  ?    ?   ?   C . n 
C 2 528  THR 528  186  ?    ?   ?   C . n 
C 2 529  ASP 529  187  ?    ?   ?   C . n 
C 2 530  ALA 530  188  ?    ?   ?   C . n 
C 2 531  ALA 531  189  ?    ?   ?   C . n 
C 2 532  ASP 532  190  ?    ?   ?   C . n 
C 2 533  LYS 533  191  ?    ?   ?   C . n 
C 2 534  MET 534  192  ?    ?   ?   C . n 
C 2 535  SER 535  193  ?    ?   ?   C . n 
C 2 536  LYS 536  194  ?    ?   ?   C . n 
C 2 537  VAL 537  195  ?    ?   ?   C . n 
C 2 538  LEU 538  196  ?    ?   ?   C . n 
C 2 539  GLU 539  197  ?    ?   ?   C . n 
C 2 540  LEU 540  198  ?    ?   ?   C . n 
C 2 541  SER 541  199  ?    ?   ?   C . n 
C 2 542  GLU 542  200  ?    ?   ?   C . n 
C 2 543  GLU 543  201  ?    ?   ?   C . n 
C 2 544  THR 544  202  ?    ?   ?   C . n 
C 2 545  PHE 545  203  ?    ?   ?   C . n 
C 2 546  SER 546  204  ?    ?   ?   C . n 
C 2 547  LYS 547  205  ?    ?   ?   C . n 
C 2 548  PRO 548  206  ?    ?   ?   C . n 
C 2 549  ASN 549  207  ?    ?   ?   C . n 
C 2 550  LEU 550  208  ?    ?   ?   C . n 
C 2 551  SER 551  209  ?    ?   ?   C . n 
C 2 552  ALA 552  210  ?    ?   ?   C . n 
C 2 553  LYS 553  211  ?    ?   ?   C . n 
C 2 554  ASP 554  212  ?    ?   ?   C . n 
C 2 555  LEU 555  213  ?    ?   ?   C . n 
C 2 556  ALA 556  214  ?    ?   ?   C . n 
C 2 557  LEU 557  215  ?    ?   ?   C . n 
C 2 558  LEU 558  216  ?    ?   ?   C . n 
C 2 559  LEU 559  217  ?    ?   ?   C . n 
C 2 560  PHE 560  218  ?    ?   ?   C . n 
C 2 561  THR 561  219  ?    ?   ?   C . n 
C 2 562  HIS 562  220  ?    ?   ?   C . n 
C 2 563  LEU 563  221  ?    ?   ?   C . n 
C 2 564  PRO 564  222  ?    ?   ?   C . n 
C 2 565  GLY 565  223  ?    ?   ?   C . n 
C 2 566  ASN 566  224  ?    ?   ?   C . n 
C 2 567  ASN 567  225  ?    ?   ?   C . n 
C 2 568  THR 568  226  ?    ?   ?   C . n 
C 2 569  PRO 569  227  ?    ?   ?   C . n 
C 2 570  PHE 570  228  ?    ?   ?   C . n 
C 2 571  HIS 571  229  ?    ?   ?   C . n 
C 2 572  ILE 572  230  ?    ?   ?   C . n 
C 2 573  LEU 573  231  ?    ?   ?   C . n 
C 2 574  ALA 574  232  ?    ?   ?   C . n 
C 2 575  GLN 575  233  ?    ?   ?   C . n 
C 2 576  VAL 576  234  ?    ?   ?   C . n 
C 2 577  LEU 577  235  ?    ?   ?   C . n 
C 2 578  SER 578  236  ?    ?   ?   C . n 
C 2 579  LYS 579  237  ?    ?   ?   C . n 
C 2 580  ILE 580  238  ?    ?   ?   C . n 
C 2 581  ALA 581  239  ?    ?   ?   C . n 
C 2 582  TYR 582  240  ?    ?   ?   C . n 
C 2 583  LYS 583  241  ?    ?   ?   C . n 
C 2 584  SER 584  242  ?    ?   ?   C . n 
C 2 585  GLY 585  243  ?    ?   ?   C . n 
C 2 586  LYS 586  244  ?    ?   ?   C . n 
C 2 587  SER 587  245  ?    ?   ?   C . n 
C 2 588  GLY 588  246  ?    ?   ?   C . n 
C 2 589  ALA 589  247  ?    ?   ?   C . n 
C 2 590  PHE 590  248  ?    ?   ?   C . n 
C 2 591  LEU 591  249  ?    ?   ?   C . n 
C 2 592  ASP 592  250  ?    ?   ?   C . n 
C 2 593  ALA 593  251  ?    ?   ?   C . n 
C 2 594  PHE 594  252  ?    ?   ?   C . n 
C 2 595  HIS 595  253  ?    ?   ?   C . n 
C 2 596  GLN 596  254  ?    ?   ?   C . n 
C 2 597  ILE 597  255  ?    ?   ?   C . n 
C 2 598  LEU 598  256  ?    ?   ?   C . n 
C 2 599  SER 599  257  ?    ?   ?   C . n 
C 2 600  GLU 600  258  ?    ?   ?   C . n 
C 2 601  GLY 601  259  ?    ?   ?   C . n 
C 2 602  GLU 602  260  ?    ?   ?   C . n 
C 2 603  ASN 603  261  ?    ?   ?   C . n 
C 2 604  ALA 604  262  ?    ?   ?   C . n 
C 2 605  GLN 605  263  ?    ?   ?   C . n 
C 2 606  ALA 606  264  ?    ?   ?   C . n 
C 2 607  ALA 607  265  ?    ?   ?   C . n 
C 2 608  LEU 608  266  ?    ?   ?   C . n 
C 2 609  THR 609  267  ?    ?   ?   C . n 
C 2 610  ARG 610  268  ?    ?   ?   C . n 
C 2 611  LEU 611  269  ?    ?   ?   C . n 
C 2 612  SER 612  270  ?    ?   ?   C . n 
C 2 613  ARG 613  271  ?    ?   ?   C . n 
C 2 614  THR 614  272  ?    ?   ?   C . n 
C 2 615  PHE 615  273  ?    ?   ?   C . n 
C 2 616  ASP 616  274  ?    ?   ?   C . n 
C 2 617  ALA 617  275  ?    ?   ?   C . n 
C 2 618  PHE 618  276  ?    ?   ?   C . n 
C 2 619  LEU 619  277  ?    ?   ?   C . n 
C 2 620  GLY 620  278  ?    ?   ?   C . n 
C 2 621  VAL 621  279  ?    ?   ?   C . n 
C 2 622  VAL 622  280  ?    ?   ?   C . n 
C 2 623  PRO 623  281  ?    ?   ?   C . n 
C 2 624  PRO 624  282  ?    ?   ?   C . n 
C 2 625  VAL 625  283  ?    ?   ?   C . n 
C 2 626  ILE 626  284  ?    ?   ?   C . n 
C 2 627  ARG 627  285  ?    ?   ?   C . n 
C 2 628  VAL 628  286  ?    ?   ?   C . n 
C 2 629  LYS 629  287  ?    ?   ?   C . n 
C 2 630  ASN 630  288  ?    ?   ?   C . n 
C 2 631  PHE 631  289  ?    ?   ?   C . n 
C 2 632  GLN 632  290  ?    ?   ?   C . n 
C 2 633  THR 633  291  ?    ?   ?   C . n 
C 2 634  VAL 634  292  ?    ?   ?   C . n 
C 2 635  PRO 635  293  ?    ?   ?   C . n 
C 2 636  ARG 636  294  ?    ?   ?   C . n 
C 2 637  PRO 637  295  ?    ?   ?   C . n 
C 2 638  CYS 638  296  ?    ?   ?   C . n 
C 2 639  GLN 639  297  ?    ?   ?   C . n 
C 2 640  LYS 640  298  ?    ?   ?   C . n 
C 2 641  SER 641  299  ?    ?   ?   C . n 
C 2 642  LEU 642  300  ?    ?   ?   C . n 
C 2 643  ARG 643  301  ?    ?   ?   C . n 
C 2 644  ALA 644  302  ?    ?   ?   C . n 
C 2 645  VAL 645  303  ?    ?   ?   C . n 
C 2 646  PRO 646  304  ?    ?   ?   C . n 
C 2 647  PRO 647  305  ?    ?   ?   C . n 
C 2 648  ASN 648  306  ?    ?   ?   C . n 
C 2 649  PRO 649  307  ?    ?   ?   C . n 
C 2 650  THR 650  308  ?    ?   ?   C . n 
C 2 651  ILE 651  309  ?    ?   ?   C . n 
C 2 652  ASP 652  310  ?    ?   ?   C . n 
C 2 653  LYS 653  311  ?    ?   ?   C . n 
C 2 654  GLY 654  312  ?    ?   ?   C . n 
C 2 655  TRP 655  313  ?    ?   ?   C . n 
C 2 656  VAL 656  314  ?    ?   ?   C . n 
C 2 657  CYS 657  315  ?    ?   ?   C . n 
C 2 658  VAL 658  316  ?    ?   ?   C . n 
C 2 659  TYR 659  317  ?    ?   ?   C . n 
C 2 660  SER 660  318  ?    ?   ?   C . n 
C 2 661  SER 661  319  ?    ?   ?   C . n 
C 2 662  GLU 662  320  ?    ?   ?   C . n 
C 2 663  GLN 663  321  ?    ?   ?   C . n 
C 2 664  GLY 664  322  ?    ?   ?   C . n 
C 2 665  GLU 665  323  ?    ?   ?   C . n 
C 2 666  THR 666  324  ?    ?   ?   C . n 
C 2 667  ARG 667  325  ?    ?   ?   C . n 
C 2 668  ALA 668  326  ?    ?   ?   C . n 
C 2 669  LEU 669  327  ?    ?   ?   C . n 
C 2 670  LYS 670  328  ?    ?   ?   C . n 
C 2 671  ILE 671  329  ?    ?   ?   C . n 
D 2 1    MET 1    -341 ?    ?   ?   D . n 
D 2 2    GLY 2    -340 ?    ?   ?   D . n 
D 2 3    SER 3    -339 ?    ?   ?   D . n 
D 2 4    SER 4    -338 ?    ?   ?   D . n 
D 2 5    HIS 5    -337 ?    ?   ?   D . n 
D 2 6    HIS 6    -336 ?    ?   ?   D . n 
D 2 7    HIS 7    -335 ?    ?   ?   D . n 
D 2 8    HIS 8    -334 ?    ?   ?   D . n 
D 2 9    HIS 9    -333 ?    ?   ?   D . n 
D 2 10   HIS 10   -332 ?    ?   ?   D . n 
D 2 11   GLY 11   -331 ?    ?   ?   D . n 
D 2 12   THR 12   -330 ?    ?   ?   D . n 
D 2 13   LYS 13   -329 ?    ?   ?   D . n 
D 2 14   THR 14   -328 ?    ?   ?   D . n 
D 2 15   GLU 15   -327 ?    ?   ?   D . n 
D 2 16   GLU 16   -326 ?    ?   ?   D . n 
D 2 17   GLY 17   -325 ?    ?   ?   D . n 
D 2 18   LYS 18   -324 ?    ?   ?   D . n 
D 2 19   LEU 19   -323 ?    ?   ?   D . n 
D 2 20   VAL 20   -322 ?    ?   ?   D . n 
D 2 21   ILE 21   -321 ?    ?   ?   D . n 
D 2 22   TRP 22   -320 ?    ?   ?   D . n 
D 2 23   ILE 23   -319 ?    ?   ?   D . n 
D 2 24   ASN 24   -318 ?    ?   ?   D . n 
D 2 25   GLY 25   -317 ?    ?   ?   D . n 
D 2 26   ASP 26   -316 ?    ?   ?   D . n 
D 2 27   LYS 27   -315 ?    ?   ?   D . n 
D 2 28   GLY 28   -314 ?    ?   ?   D . n 
D 2 29   TYR 29   -313 ?    ?   ?   D . n 
D 2 30   ASN 30   -312 ?    ?   ?   D . n 
D 2 31   GLY 31   -311 ?    ?   ?   D . n 
D 2 32   LEU 32   -310 ?    ?   ?   D . n 
D 2 33   ALA 33   -309 ?    ?   ?   D . n 
D 2 34   GLU 34   -308 ?    ?   ?   D . n 
D 2 35   VAL 35   -307 ?    ?   ?   D . n 
D 2 36   GLY 36   -306 ?    ?   ?   D . n 
D 2 37   LYS 37   -305 ?    ?   ?   D . n 
D 2 38   LYS 38   -304 ?    ?   ?   D . n 
D 2 39   PHE 39   -303 ?    ?   ?   D . n 
D 2 40   GLU 40   -302 ?    ?   ?   D . n 
D 2 41   LYS 41   -301 ?    ?   ?   D . n 
D 2 42   ASP 42   -300 ?    ?   ?   D . n 
D 2 43   THR 43   -299 ?    ?   ?   D . n 
D 2 44   GLY 44   -298 ?    ?   ?   D . n 
D 2 45   ILE 45   -297 ?    ?   ?   D . n 
D 2 46   LYS 46   -296 ?    ?   ?   D . n 
D 2 47   VAL 47   -295 ?    ?   ?   D . n 
D 2 48   THR 48   -294 ?    ?   ?   D . n 
D 2 49   VAL 49   -293 ?    ?   ?   D . n 
D 2 50   GLU 50   -292 ?    ?   ?   D . n 
D 2 51   HIS 51   -291 ?    ?   ?   D . n 
D 2 52   PRO 52   -290 ?    ?   ?   D . n 
D 2 53   ASP 53   -289 ?    ?   ?   D . n 
D 2 54   LYS 54   -288 ?    ?   ?   D . n 
D 2 55   LEU 55   -287 ?    ?   ?   D . n 
D 2 56   GLU 56   -286 ?    ?   ?   D . n 
D 2 57   GLU 57   -285 ?    ?   ?   D . n 
D 2 58   LYS 58   -284 ?    ?   ?   D . n 
D 2 59   PHE 59   -283 ?    ?   ?   D . n 
D 2 60   PRO 60   -282 ?    ?   ?   D . n 
D 2 61   GLN 61   -281 ?    ?   ?   D . n 
D 2 62   VAL 62   -280 ?    ?   ?   D . n 
D 2 63   ALA 63   -279 ?    ?   ?   D . n 
D 2 64   ALA 64   -278 ?    ?   ?   D . n 
D 2 65   THR 65   -277 ?    ?   ?   D . n 
D 2 66   GLY 66   -276 ?    ?   ?   D . n 
D 2 67   ASP 67   -275 ?    ?   ?   D . n 
D 2 68   GLY 68   -274 ?    ?   ?   D . n 
D 2 69   PRO 69   -273 ?    ?   ?   D . n 
D 2 70   ASP 70   -272 ?    ?   ?   D . n 
D 2 71   ILE 71   -271 ?    ?   ?   D . n 
D 2 72   ILE 72   -270 ?    ?   ?   D . n 
D 2 73   PHE 73   -269 ?    ?   ?   D . n 
D 2 74   TRP 74   -268 ?    ?   ?   D . n 
D 2 75   ALA 75   -267 ?    ?   ?   D . n 
D 2 76   HIS 76   -266 ?    ?   ?   D . n 
D 2 77   ASP 77   -265 ?    ?   ?   D . n 
D 2 78   ARG 78   -264 ?    ?   ?   D . n 
D 2 79   PHE 79   -263 ?    ?   ?   D . n 
D 2 80   GLY 80   -262 ?    ?   ?   D . n 
D 2 81   GLY 81   -261 ?    ?   ?   D . n 
D 2 82   TYR 82   -260 ?    ?   ?   D . n 
D 2 83   ALA 83   -259 ?    ?   ?   D . n 
D 2 84   GLN 84   -258 ?    ?   ?   D . n 
D 2 85   SER 85   -257 ?    ?   ?   D . n 
D 2 86   GLY 86   -256 ?    ?   ?   D . n 
D 2 87   LEU 87   -255 ?    ?   ?   D . n 
D 2 88   LEU 88   -254 ?    ?   ?   D . n 
D 2 89   ALA 89   -253 ?    ?   ?   D . n 
D 2 90   GLU 90   -252 ?    ?   ?   D . n 
D 2 91   ILE 91   -251 ?    ?   ?   D . n 
D 2 92   THR 92   -250 ?    ?   ?   D . n 
D 2 93   PRO 93   -249 ?    ?   ?   D . n 
D 2 94   ASP 94   -248 ?    ?   ?   D . n 
D 2 95   LYS 95   -247 ?    ?   ?   D . n 
D 2 96   ALA 96   -246 ?    ?   ?   D . n 
D 2 97   PHE 97   -245 ?    ?   ?   D . n 
D 2 98   GLN 98   -244 ?    ?   ?   D . n 
D 2 99   ASP 99   -243 ?    ?   ?   D . n 
D 2 100  LYS 100  -242 ?    ?   ?   D . n 
D 2 101  LEU 101  -241 ?    ?   ?   D . n 
D 2 102  TYR 102  -240 ?    ?   ?   D . n 
D 2 103  PRO 103  -239 ?    ?   ?   D . n 
D 2 104  PHE 104  -238 ?    ?   ?   D . n 
D 2 105  THR 105  -237 ?    ?   ?   D . n 
D 2 106  TRP 106  -236 ?    ?   ?   D . n 
D 2 107  ASP 107  -235 ?    ?   ?   D . n 
D 2 108  ALA 108  -234 ?    ?   ?   D . n 
D 2 109  VAL 109  -233 ?    ?   ?   D . n 
D 2 110  ARG 110  -232 ?    ?   ?   D . n 
D 2 111  TYR 111  -231 ?    ?   ?   D . n 
D 2 112  ASN 112  -230 ?    ?   ?   D . n 
D 2 113  GLY 113  -229 ?    ?   ?   D . n 
D 2 114  LYS 114  -228 ?    ?   ?   D . n 
D 2 115  LEU 115  -227 ?    ?   ?   D . n 
D 2 116  ILE 116  -226 ?    ?   ?   D . n 
D 2 117  ALA 117  -225 ?    ?   ?   D . n 
D 2 118  TYR 118  -224 ?    ?   ?   D . n 
D 2 119  PRO 119  -223 ?    ?   ?   D . n 
D 2 120  ILE 120  -222 ?    ?   ?   D . n 
D 2 121  ALA 121  -221 ?    ?   ?   D . n 
D 2 122  VAL 122  -220 ?    ?   ?   D . n 
D 2 123  GLU 123  -219 ?    ?   ?   D . n 
D 2 124  ALA 124  -218 ?    ?   ?   D . n 
D 2 125  LEU 125  -217 ?    ?   ?   D . n 
D 2 126  SER 126  -216 ?    ?   ?   D . n 
D 2 127  LEU 127  -215 ?    ?   ?   D . n 
D 2 128  ILE 128  -214 ?    ?   ?   D . n 
D 2 129  TYR 129  -213 ?    ?   ?   D . n 
D 2 130  ASN 130  -212 ?    ?   ?   D . n 
D 2 131  LYS 131  -211 ?    ?   ?   D . n 
D 2 132  ASP 132  -210 ?    ?   ?   D . n 
D 2 133  LEU 133  -209 ?    ?   ?   D . n 
D 2 134  LEU 134  -208 ?    ?   ?   D . n 
D 2 135  PRO 135  -207 ?    ?   ?   D . n 
D 2 136  ASN 136  -206 ?    ?   ?   D . n 
D 2 137  PRO 137  -205 ?    ?   ?   D . n 
D 2 138  PRO 138  -204 ?    ?   ?   D . n 
D 2 139  LYS 139  -203 ?    ?   ?   D . n 
D 2 140  THR 140  -202 ?    ?   ?   D . n 
D 2 141  TRP 141  -201 ?    ?   ?   D . n 
D 2 142  GLU 142  -200 ?    ?   ?   D . n 
D 2 143  GLU 143  -199 ?    ?   ?   D . n 
D 2 144  ILE 144  -198 ?    ?   ?   D . n 
D 2 145  PRO 145  -197 ?    ?   ?   D . n 
D 2 146  ALA 146  -196 ?    ?   ?   D . n 
D 2 147  LEU 147  -195 ?    ?   ?   D . n 
D 2 148  ASP 148  -194 ?    ?   ?   D . n 
D 2 149  LYS 149  -193 ?    ?   ?   D . n 
D 2 150  GLU 150  -192 ?    ?   ?   D . n 
D 2 151  LEU 151  -191 ?    ?   ?   D . n 
D 2 152  LYS 152  -190 ?    ?   ?   D . n 
D 2 153  ALA 153  -189 ?    ?   ?   D . n 
D 2 154  LYS 154  -188 ?    ?   ?   D . n 
D 2 155  GLY 155  -187 ?    ?   ?   D . n 
D 2 156  LYS 156  -186 ?    ?   ?   D . n 
D 2 157  SER 157  -185 ?    ?   ?   D . n 
D 2 158  ALA 158  -184 ?    ?   ?   D . n 
D 2 159  LEU 159  -183 ?    ?   ?   D . n 
D 2 160  MET 160  -182 ?    ?   ?   D . n 
D 2 161  PHE 161  -181 ?    ?   ?   D . n 
D 2 162  ASN 162  -180 ?    ?   ?   D . n 
D 2 163  LEU 163  -179 ?    ?   ?   D . n 
D 2 164  GLN 164  -178 ?    ?   ?   D . n 
D 2 165  GLU 165  -177 ?    ?   ?   D . n 
D 2 166  PRO 166  -176 ?    ?   ?   D . n 
D 2 167  TYR 167  -175 ?    ?   ?   D . n 
D 2 168  PHE 168  -174 ?    ?   ?   D . n 
D 2 169  THR 169  -173 ?    ?   ?   D . n 
D 2 170  TRP 170  -172 ?    ?   ?   D . n 
D 2 171  PRO 171  -171 ?    ?   ?   D . n 
D 2 172  LEU 172  -170 ?    ?   ?   D . n 
D 2 173  ILE 173  -169 ?    ?   ?   D . n 
D 2 174  ALA 174  -168 ?    ?   ?   D . n 
D 2 175  ALA 175  -167 ?    ?   ?   D . n 
D 2 176  ASP 176  -166 ?    ?   ?   D . n 
D 2 177  GLY 177  -165 ?    ?   ?   D . n 
D 2 178  GLY 178  -164 ?    ?   ?   D . n 
D 2 179  TYR 179  -163 ?    ?   ?   D . n 
D 2 180  ALA 180  -162 ?    ?   ?   D . n 
D 2 181  PHE 181  -161 ?    ?   ?   D . n 
D 2 182  LYS 182  -160 ?    ?   ?   D . n 
D 2 183  TYR 183  -159 ?    ?   ?   D . n 
D 2 184  GLU 184  -158 ?    ?   ?   D . n 
D 2 185  ASN 185  -157 ?    ?   ?   D . n 
D 2 186  GLY 186  -156 ?    ?   ?   D . n 
D 2 187  LYS 187  -155 ?    ?   ?   D . n 
D 2 188  TYR 188  -154 ?    ?   ?   D . n 
D 2 189  ASP 189  -153 ?    ?   ?   D . n 
D 2 190  ILE 190  -152 ?    ?   ?   D . n 
D 2 191  LYS 191  -151 ?    ?   ?   D . n 
D 2 192  ASP 192  -150 ?    ?   ?   D . n 
D 2 193  VAL 193  -149 ?    ?   ?   D . n 
D 2 194  GLY 194  -148 ?    ?   ?   D . n 
D 2 195  VAL 195  -147 ?    ?   ?   D . n 
D 2 196  ASP 196  -146 ?    ?   ?   D . n 
D 2 197  ASN 197  -145 ?    ?   ?   D . n 
D 2 198  ALA 198  -144 ?    ?   ?   D . n 
D 2 199  GLY 199  -143 ?    ?   ?   D . n 
D 2 200  ALA 200  -142 ?    ?   ?   D . n 
D 2 201  LYS 201  -141 ?    ?   ?   D . n 
D 2 202  ALA 202  -140 ?    ?   ?   D . n 
D 2 203  GLY 203  -139 ?    ?   ?   D . n 
D 2 204  LEU 204  -138 ?    ?   ?   D . n 
D 2 205  THR 205  -137 ?    ?   ?   D . n 
D 2 206  PHE 206  -136 ?    ?   ?   D . n 
D 2 207  LEU 207  -135 ?    ?   ?   D . n 
D 2 208  VAL 208  -134 ?    ?   ?   D . n 
D 2 209  ASP 209  -133 ?    ?   ?   D . n 
D 2 210  LEU 210  -132 ?    ?   ?   D . n 
D 2 211  ILE 211  -131 ?    ?   ?   D . n 
D 2 212  LYS 212  -130 ?    ?   ?   D . n 
D 2 213  ASN 213  -129 ?    ?   ?   D . n 
D 2 214  LYS 214  -128 ?    ?   ?   D . n 
D 2 215  HIS 215  -127 ?    ?   ?   D . n 
D 2 216  MET 216  -126 ?    ?   ?   D . n 
D 2 217  ASN 217  -125 ?    ?   ?   D . n 
D 2 218  ALA 218  -124 ?    ?   ?   D . n 
D 2 219  ASP 219  -123 ?    ?   ?   D . n 
D 2 220  THR 220  -122 ?    ?   ?   D . n 
D 2 221  ASP 221  -121 ?    ?   ?   D . n 
D 2 222  TYR 222  -120 ?    ?   ?   D . n 
D 2 223  SER 223  -119 ?    ?   ?   D . n 
D 2 224  ILE 224  -118 ?    ?   ?   D . n 
D 2 225  ALA 225  -117 ?    ?   ?   D . n 
D 2 226  GLU 226  -116 ?    ?   ?   D . n 
D 2 227  ALA 227  -115 ?    ?   ?   D . n 
D 2 228  ALA 228  -114 ?    ?   ?   D . n 
D 2 229  PHE 229  -113 ?    ?   ?   D . n 
D 2 230  ASN 230  -112 ?    ?   ?   D . n 
D 2 231  LYS 231  -111 ?    ?   ?   D . n 
D 2 232  GLY 232  -110 ?    ?   ?   D . n 
D 2 233  GLU 233  -109 ?    ?   ?   D . n 
D 2 234  THR 234  -108 ?    ?   ?   D . n 
D 2 235  ALA 235  -107 ?    ?   ?   D . n 
D 2 236  MET 236  -106 ?    ?   ?   D . n 
D 2 237  THR 237  -105 ?    ?   ?   D . n 
D 2 238  ILE 238  -104 ?    ?   ?   D . n 
D 2 239  ASN 239  -103 ?    ?   ?   D . n 
D 2 240  GLY 240  -102 ?    ?   ?   D . n 
D 2 241  PRO 241  -101 ?    ?   ?   D . n 
D 2 242  TRP 242  -100 ?    ?   ?   D . n 
D 2 243  ALA 243  -99  ?    ?   ?   D . n 
D 2 244  TRP 244  -98  ?    ?   ?   D . n 
D 2 245  SER 245  -97  ?    ?   ?   D . n 
D 2 246  ASN 246  -96  ?    ?   ?   D . n 
D 2 247  ILE 247  -95  ?    ?   ?   D . n 
D 2 248  ASP 248  -94  ?    ?   ?   D . n 
D 2 249  THR 249  -93  ?    ?   ?   D . n 
D 2 250  SER 250  -92  ?    ?   ?   D . n 
D 2 251  LYS 251  -91  ?    ?   ?   D . n 
D 2 252  VAL 252  -90  ?    ?   ?   D . n 
D 2 253  ASN 253  -89  ?    ?   ?   D . n 
D 2 254  TYR 254  -88  ?    ?   ?   D . n 
D 2 255  GLY 255  -87  ?    ?   ?   D . n 
D 2 256  VAL 256  -86  ?    ?   ?   D . n 
D 2 257  THR 257  -85  ?    ?   ?   D . n 
D 2 258  VAL 258  -84  ?    ?   ?   D . n 
D 2 259  LEU 259  -83  ?    ?   ?   D . n 
D 2 260  PRO 260  -82  ?    ?   ?   D . n 
D 2 261  THR 261  -81  ?    ?   ?   D . n 
D 2 262  PHE 262  -80  ?    ?   ?   D . n 
D 2 263  LYS 263  -79  ?    ?   ?   D . n 
D 2 264  GLY 264  -78  ?    ?   ?   D . n 
D 2 265  GLN 265  -77  ?    ?   ?   D . n 
D 2 266  PRO 266  -76  ?    ?   ?   D . n 
D 2 267  SER 267  -75  ?    ?   ?   D . n 
D 2 268  LYS 268  -74  ?    ?   ?   D . n 
D 2 269  PRO 269  -73  ?    ?   ?   D . n 
D 2 270  PHE 270  -72  ?    ?   ?   D . n 
D 2 271  VAL 271  -71  ?    ?   ?   D . n 
D 2 272  GLY 272  -70  ?    ?   ?   D . n 
D 2 273  VAL 273  -69  ?    ?   ?   D . n 
D 2 274  LEU 274  -68  ?    ?   ?   D . n 
D 2 275  SER 275  -67  ?    ?   ?   D . n 
D 2 276  ALA 276  -66  ?    ?   ?   D . n 
D 2 277  GLY 277  -65  ?    ?   ?   D . n 
D 2 278  ILE 278  -64  ?    ?   ?   D . n 
D 2 279  ASN 279  -63  ?    ?   ?   D . n 
D 2 280  ALA 280  -62  ?    ?   ?   D . n 
D 2 281  ALA 281  -61  ?    ?   ?   D . n 
D 2 282  SER 282  -60  ?    ?   ?   D . n 
D 2 283  PRO 283  -59  ?    ?   ?   D . n 
D 2 284  ASN 284  -58  ?    ?   ?   D . n 
D 2 285  LYS 285  -57  ?    ?   ?   D . n 
D 2 286  GLU 286  -56  ?    ?   ?   D . n 
D 2 287  LEU 287  -55  ?    ?   ?   D . n 
D 2 288  ALA 288  -54  ?    ?   ?   D . n 
D 2 289  LYS 289  -53  ?    ?   ?   D . n 
D 2 290  GLU 290  -52  ?    ?   ?   D . n 
D 2 291  PHE 291  -51  ?    ?   ?   D . n 
D 2 292  LEU 292  -50  ?    ?   ?   D . n 
D 2 293  GLU 293  -49  ?    ?   ?   D . n 
D 2 294  ASN 294  -48  ?    ?   ?   D . n 
D 2 295  TYR 295  -47  ?    ?   ?   D . n 
D 2 296  LEU 296  -46  ?    ?   ?   D . n 
D 2 297  LEU 297  -45  ?    ?   ?   D . n 
D 2 298  THR 298  -44  ?    ?   ?   D . n 
D 2 299  ASP 299  -43  ?    ?   ?   D . n 
D 2 300  GLU 300  -42  ?    ?   ?   D . n 
D 2 301  GLY 301  -41  ?    ?   ?   D . n 
D 2 302  LEU 302  -40  ?    ?   ?   D . n 
D 2 303  GLU 303  -39  ?    ?   ?   D . n 
D 2 304  ALA 304  -38  ?    ?   ?   D . n 
D 2 305  VAL 305  -37  ?    ?   ?   D . n 
D 2 306  ASN 306  -36  ?    ?   ?   D . n 
D 2 307  LYS 307  -35  ?    ?   ?   D . n 
D 2 308  ASP 308  -34  ?    ?   ?   D . n 
D 2 309  LYS 309  -33  ?    ?   ?   D . n 
D 2 310  PRO 310  -32  ?    ?   ?   D . n 
D 2 311  LEU 311  -31  ?    ?   ?   D . n 
D 2 312  GLY 312  -30  ?    ?   ?   D . n 
D 2 313  ALA 313  -29  ?    ?   ?   D . n 
D 2 314  VAL 314  -28  ?    ?   ?   D . n 
D 2 315  ALA 315  -27  ?    ?   ?   D . n 
D 2 316  LEU 316  -26  ?    ?   ?   D . n 
D 2 317  LYS 317  -25  ?    ?   ?   D . n 
D 2 318  SER 318  -24  ?    ?   ?   D . n 
D 2 319  TYR 319  -23  ?    ?   ?   D . n 
D 2 320  GLU 320  -22  ?    ?   ?   D . n 
D 2 321  GLU 321  -21  ?    ?   ?   D . n 
D 2 322  GLU 322  -20  ?    ?   ?   D . n 
D 2 323  LEU 323  -19  ?    ?   ?   D . n 
D 2 324  ALA 324  -18  ?    ?   ?   D . n 
D 2 325  LYS 325  -17  ?    ?   ?   D . n 
D 2 326  ASP 326  -16  ?    ?   ?   D . n 
D 2 327  PRO 327  -15  ?    ?   ?   D . n 
D 2 328  ARG 328  -14  ?    ?   ?   D . n 
D 2 329  ILE 329  -13  ?    ?   ?   D . n 
D 2 330  ALA 330  -12  ?    ?   ?   D . n 
D 2 331  ALA 331  -11  ?    ?   ?   D . n 
D 2 332  THR 332  -10  ?    ?   ?   D . n 
D 2 333  MET 333  -9   ?    ?   ?   D . n 
D 2 334  GLU 334  -8   ?    ?   ?   D . n 
D 2 335  ASN 335  -7   ?    ?   ?   D . n 
D 2 336  ALA 336  -6   ?    ?   ?   D . n 
D 2 337  GLN 337  -5   ?    ?   ?   D . n 
D 2 338  LYS 338  -4   ?    ?   ?   D . n 
D 2 339  GLY 339  -3   ?    ?   ?   D . n 
D 2 340  GLU 340  -2   ?    ?   ?   D . n 
D 2 341  ILE 341  -1   ?    ?   ?   D . n 
D 2 342  MET 342  0    ?    ?   ?   D . n 
D 2 343  PRO 343  1    ?    ?   ?   D . n 
D 2 344  ASN 344  2    ?    ?   ?   D . n 
D 2 345  ILE 345  3    ?    ?   ?   D . n 
D 2 346  PRO 346  4    ?    ?   ?   D . n 
D 2 347  GLN 347  5    ?    ?   ?   D . n 
D 2 348  MET 348  6    ?    ?   ?   D . n 
D 2 349  SER 349  7    ?    ?   ?   D . n 
D 2 350  ALA 350  8    ?    ?   ?   D . n 
D 2 351  PHE 351  9    ?    ?   ?   D . n 
D 2 352  TRP 352  10   ?    ?   ?   D . n 
D 2 353  TYR 353  11   ?    ?   ?   D . n 
D 2 354  ALA 354  12   ?    ?   ?   D . n 
D 2 355  VAL 355  13   ?    ?   ?   D . n 
D 2 356  ARG 356  14   ?    ?   ?   D . n 
D 2 357  THR 357  15   ?    ?   ?   D . n 
D 2 358  ALA 358  16   ?    ?   ?   D . n 
D 2 359  VAL 359  17   ?    ?   ?   D . n 
D 2 360  ILE 360  18   ?    ?   ?   D . n 
D 2 361  ASN 361  19   ?    ?   ?   D . n 
D 2 362  ALA 362  20   ?    ?   ?   D . n 
D 2 363  ALA 363  21   ?    ?   ?   D . n 
D 2 364  SER 364  22   ?    ?   ?   D . n 
D 2 365  GLY 365  23   ?    ?   ?   D . n 
D 2 366  ARG 366  24   ?    ?   ?   D . n 
D 2 367  GLN 367  25   ?    ?   ?   D . n 
D 2 368  THR 368  26   ?    ?   ?   D . n 
D 2 369  VAL 369  27   ?    ?   ?   D . n 
D 2 370  ASP 370  28   ?    ?   ?   D . n 
D 2 371  GLU 371  29   ?    ?   ?   D . n 
D 2 372  ALA 372  30   ?    ?   ?   D . n 
D 2 373  LEU 373  31   ?    ?   ?   D . n 
D 2 374  LYS 374  32   ?    ?   ?   D . n 
D 2 375  ASP 375  33   ?    ?   ?   D . n 
D 2 376  ALA 376  34   ?    ?   ?   D . n 
D 2 377  GLN 377  35   ?    ?   ?   D . n 
D 2 378  THR 378  36   ?    ?   ?   D . n 
D 2 379  GLY 379  37   ?    ?   ?   D . n 
D 2 380  THR 380  38   ?    ?   ?   D . n 
D 2 381  ASP 381  39   ?    ?   ?   D . n 
D 2 382  TYR 382  40   ?    ?   ?   D . n 
D 2 383  ASP 383  41   ?    ?   ?   D . n 
D 2 384  ILE 384  42   ?    ?   ?   D . n 
D 2 385  PRO 385  43   ?    ?   ?   D . n 
D 2 386  THR 386  44   ?    ?   ?   D . n 
D 2 387  THR 387  45   ?    ?   ?   D . n 
D 2 388  LEU 388  46   ?    ?   ?   D . n 
D 2 389  GLU 389  47   ?    ?   ?   D . n 
D 2 390  VAL 390  48   ?    ?   ?   D . n 
D 2 391  LEU 391  49   ?    ?   ?   D . n 
D 2 392  PHE 392  50   ?    ?   ?   D . n 
D 2 393  GLN 393  51   ?    ?   ?   D . n 
D 2 394  GLY 394  52   ?    ?   ?   D . n 
D 2 395  PRO 395  53   ?    ?   ?   D . n 
D 2 396  LEU 396  54   ?    ?   ?   D . n 
D 2 397  GLY 397  55   ?    ?   ?   D . n 
D 2 398  SER 398  56   ?    ?   ?   D . n 
D 2 399  SER 399  57   ?    ?   ?   D . n 
D 2 400  THR 400  58   ?    ?   ?   D . n 
D 2 401  ASP 401  59   ?    ?   ?   D . n 
D 2 402  ASP 402  60   ?    ?   ?   D . n 
D 2 403  ILE 403  61   ?    ?   ?   D . n 
D 2 404  ILE 404  62   ?    ?   ?   D . n 
D 2 405  TRP 405  63   ?    ?   ?   D . n 
D 2 406  ASP 406  64   ?    ?   ?   D . n 
D 2 407  GLN 407  65   ?    ?   ?   D . n 
D 2 408  LEU 408  66   ?    ?   ?   D . n 
D 2 409  ILE 409  67   ?    ?   ?   D . n 
D 2 410  VAL 410  68   ?    ?   ?   D . n 
D 2 411  LYS 411  69   ?    ?   ?   D . n 
D 2 412  ARG 412  70   ?    ?   ?   D . n 
D 2 413  THR 413  71   ?    ?   ?   D . n 
D 2 414  LEU 414  72   ?    ?   ?   D . n 
D 2 415  ALA 415  73   ?    ?   ?   D . n 
D 2 416  ASP 416  74   ?    ?   ?   D . n 
D 2 417  LEU 417  75   ?    ?   ?   D . n 
D 2 418  LEU 418  76   ?    ?   ?   D . n 
D 2 419  ILE 419  77   ?    ?   ?   D . n 
D 2 420  PRO 420  78   ?    ?   ?   D . n 
D 2 421  ILE 421  79   ?    ?   ?   D . n 
D 2 422  ASN 422  80   ?    ?   ?   D . n 
D 2 423  ARG 423  81   ?    ?   ?   D . n 
D 2 424  GLN 424  82   ?    ?   ?   D . n 
D 2 425  ILE 425  83   ?    ?   ?   D . n 
D 2 426  SER 426  84   ?    ?   ?   D . n 
D 2 427  ASP 427  85   ?    ?   ?   D . n 
D 2 428  ILE 428  86   ?    ?   ?   D . n 
D 2 429  GLN 429  87   ?    ?   ?   D . n 
D 2 430  SER 430  88   ?    ?   ?   D . n 
D 2 431  THR 431  89   ?    ?   ?   D . n 
D 2 432  LEU 432  90   ?    ?   ?   D . n 
D 2 433  SER 433  91   ?    ?   ?   D . n 
D 2 434  GLU 434  92   ?    ?   ?   D . n 
D 2 435  VAL 435  93   ?    ?   ?   D . n 
D 2 436  THR 436  94   ?    ?   ?   D . n 
D 2 437  THR 437  95   ?    ?   ?   D . n 
D 2 438  ARG 438  96   ?    ?   ?   D . n 
D 2 439  VAL 439  97   ?    ?   ?   D . n 
D 2 440  HIS 440  98   ?    ?   ?   D . n 
D 2 441  GLU 441  99   ?    ?   ?   D . n 
D 2 442  ILE 442  100  ?    ?   ?   D . n 
D 2 443  GLU 443  101  ?    ?   ?   D . n 
D 2 444  ARG 444  102  ?    ?   ?   D . n 
D 2 445  GLN 445  103  ?    ?   ?   D . n 
D 2 446  LEU 446  104  ?    ?   ?   D . n 
D 2 447  HIS 447  105  ?    ?   ?   D . n 
D 2 448  GLU 448  106  ?    ?   ?   D . n 
D 2 449  ILE 449  107  107  ILE ILE D . n 
D 2 450  THR 450  108  108  THR THR D . n 
D 2 451  PRO 451  109  109  PRO PRO D . n 
D 2 452  VAL 452  110  110  VAL VAL D . n 
D 2 453  LEU 453  111  111  LEU LEU D . n 
D 2 454  LYS 454  112  112  LYS LYS D . n 
D 2 455  MET 455  113  113  MET MET D . n 
D 2 456  GLY 456  114  114  GLY GLY D . n 
D 2 457  ARG 457  115  115  ARG ARG D . n 
D 2 458  THR 458  116  116  THR THR D . n 
D 2 459  LEU 459  117  117  LEU LEU D . n 
D 2 460  GLU 460  118  118  GLU GLU D . n 
D 2 461  ALA 461  119  119  ALA ALA D . n 
D 2 462  ILE 462  120  120  ILE ILE D . n 
D 2 463  SER 463  121  121  SER SER D . n 
D 2 464  LYS 464  122  122  LYS LYS D . n 
D 2 465  GLY 465  123  123  GLY GLY D . n 
D 2 466  MET 466  124  124  MET MET D . n 
D 2 467  SER 467  125  125  SER SER D . n 
D 2 468  GLU 468  126  126  GLU GLU D . n 
D 2 469  MET 469  127  127  MET MET D . n 
D 2 470  LEU 470  128  128  LEU LEU D . n 
D 2 471  ALA 471  129  129  ALA ALA D . n 
D 2 472  LYS 472  130  130  LYS LYS D . n 
D 2 473  TYR 473  131  131  TYR TYR D . n 
D 2 474  ASP 474  132  132  ASP ASP D . n 
D 2 475  HIS 475  133  133  HIS HIS D . n 
D 2 476  LEU 476  134  134  LEU LEU D . n 
D 2 477  VAL 477  135  135  VAL VAL D . n 
D 2 478  ILE 478  136  136  ILE ILE D . n 
D 2 479  SER 479  137  137  SER SER D . n 
D 2 480  THR 480  138  138  THR THR D . n 
D 2 481  GLY 481  139  ?    ?   ?   D . n 
D 2 482  ARG 482  140  ?    ?   ?   D . n 
D 2 483  THR 483  141  ?    ?   ?   D . n 
D 2 484  THR 484  142  ?    ?   ?   D . n 
D 2 485  ALA 485  143  ?    ?   ?   D . n 
D 2 486  PRO 486  144  ?    ?   ?   D . n 
D 2 487  ALA 487  145  ?    ?   ?   D . n 
D 2 488  ALA 488  146  ?    ?   ?   D . n 
D 2 489  ALA 489  147  ?    ?   ?   D . n 
D 2 490  PHE 490  148  ?    ?   ?   D . n 
D 2 491  ASP 491  149  ?    ?   ?   D . n 
D 2 492  ALA 492  150  ?    ?   ?   D . n 
D 2 493  TYR 493  151  ?    ?   ?   D . n 
D 2 494  LEU 494  152  ?    ?   ?   D . n 
D 2 495  ASN 495  153  ?    ?   ?   D . n 
D 2 496  GLU 496  154  ?    ?   ?   D . n 
D 2 497  HIS 497  155  ?    ?   ?   D . n 
D 2 498  GLY 498  156  ?    ?   ?   D . n 
D 2 499  VAL 499  157  ?    ?   ?   D . n 
D 2 500  PRO 500  158  ?    ?   ?   D . n 
D 2 501  PRO 501  159  ?    ?   ?   D . n 
D 2 502  PRO 502  160  ?    ?   ?   D . n 
D 2 503  GLN 503  161  ?    ?   ?   D . n 
D 2 504  PRO 504  162  ?    ?   ?   D . n 
D 2 505  ALA 505  163  ?    ?   ?   D . n 
D 2 506  ILE 506  164  ?    ?   ?   D . n 
D 2 507  PHE 507  165  ?    ?   ?   D . n 
D 2 508  LYS 508  166  ?    ?   ?   D . n 
D 2 509  ASP 509  167  ?    ?   ?   D . n 
D 2 510  LEU 510  168  ?    ?   ?   D . n 
D 2 511  GLY 511  169  ?    ?   ?   D . n 
D 2 512  VAL 512  170  ?    ?   ?   D . n 
D 2 513  ALA 513  171  ?    ?   ?   D . n 
D 2 514  GLN 514  172  ?    ?   ?   D . n 
D 2 515  GLN 515  173  ?    ?   ?   D . n 
D 2 516  ALA 516  174  ?    ?   ?   D . n 
D 2 517  CYS 517  175  ?    ?   ?   D . n 
D 2 518  SER 518  176  ?    ?   ?   D . n 
D 2 519  LYS 519  177  ?    ?   ?   D . n 
D 2 520  GLY 520  178  ?    ?   ?   D . n 
D 2 521  THR 521  179  ?    ?   ?   D . n 
D 2 522  MET 522  180  ?    ?   ?   D . n 
D 2 523  VAL 523  181  ?    ?   ?   D . n 
D 2 524  LYS 524  182  ?    ?   ?   D . n 
D 2 525  ASN 525  183  ?    ?   ?   D . n 
D 2 526  ALA 526  184  ?    ?   ?   D . n 
D 2 527  THR 527  185  ?    ?   ?   D . n 
D 2 528  THR 528  186  ?    ?   ?   D . n 
D 2 529  ASP 529  187  ?    ?   ?   D . n 
D 2 530  ALA 530  188  ?    ?   ?   D . n 
D 2 531  ALA 531  189  ?    ?   ?   D . n 
D 2 532  ASP 532  190  ?    ?   ?   D . n 
D 2 533  LYS 533  191  ?    ?   ?   D . n 
D 2 534  MET 534  192  ?    ?   ?   D . n 
D 2 535  SER 535  193  ?    ?   ?   D . n 
D 2 536  LYS 536  194  ?    ?   ?   D . n 
D 2 537  VAL 537  195  ?    ?   ?   D . n 
D 2 538  LEU 538  196  ?    ?   ?   D . n 
D 2 539  GLU 539  197  ?    ?   ?   D . n 
D 2 540  LEU 540  198  ?    ?   ?   D . n 
D 2 541  SER 541  199  ?    ?   ?   D . n 
D 2 542  GLU 542  200  ?    ?   ?   D . n 
D 2 543  GLU 543  201  ?    ?   ?   D . n 
D 2 544  THR 544  202  ?    ?   ?   D . n 
D 2 545  PHE 545  203  ?    ?   ?   D . n 
D 2 546  SER 546  204  ?    ?   ?   D . n 
D 2 547  LYS 547  205  ?    ?   ?   D . n 
D 2 548  PRO 548  206  ?    ?   ?   D . n 
D 2 549  ASN 549  207  ?    ?   ?   D . n 
D 2 550  LEU 550  208  ?    ?   ?   D . n 
D 2 551  SER 551  209  ?    ?   ?   D . n 
D 2 552  ALA 552  210  ?    ?   ?   D . n 
D 2 553  LYS 553  211  ?    ?   ?   D . n 
D 2 554  ASP 554  212  ?    ?   ?   D . n 
D 2 555  LEU 555  213  ?    ?   ?   D . n 
D 2 556  ALA 556  214  ?    ?   ?   D . n 
D 2 557  LEU 557  215  ?    ?   ?   D . n 
D 2 558  LEU 558  216  ?    ?   ?   D . n 
D 2 559  LEU 559  217  ?    ?   ?   D . n 
D 2 560  PHE 560  218  ?    ?   ?   D . n 
D 2 561  THR 561  219  ?    ?   ?   D . n 
D 2 562  HIS 562  220  ?    ?   ?   D . n 
D 2 563  LEU 563  221  ?    ?   ?   D . n 
D 2 564  PRO 564  222  ?    ?   ?   D . n 
D 2 565  GLY 565  223  ?    ?   ?   D . n 
D 2 566  ASN 566  224  ?    ?   ?   D . n 
D 2 567  ASN 567  225  ?    ?   ?   D . n 
D 2 568  THR 568  226  ?    ?   ?   D . n 
D 2 569  PRO 569  227  ?    ?   ?   D . n 
D 2 570  PHE 570  228  ?    ?   ?   D . n 
D 2 571  HIS 571  229  ?    ?   ?   D . n 
D 2 572  ILE 572  230  ?    ?   ?   D . n 
D 2 573  LEU 573  231  ?    ?   ?   D . n 
D 2 574  ALA 574  232  ?    ?   ?   D . n 
D 2 575  GLN 575  233  ?    ?   ?   D . n 
D 2 576  VAL 576  234  ?    ?   ?   D . n 
D 2 577  LEU 577  235  ?    ?   ?   D . n 
D 2 578  SER 578  236  ?    ?   ?   D . n 
D 2 579  LYS 579  237  ?    ?   ?   D . n 
D 2 580  ILE 580  238  ?    ?   ?   D . n 
D 2 581  ALA 581  239  ?    ?   ?   D . n 
D 2 582  TYR 582  240  ?    ?   ?   D . n 
D 2 583  LYS 583  241  ?    ?   ?   D . n 
D 2 584  SER 584  242  ?    ?   ?   D . n 
D 2 585  GLY 585  243  ?    ?   ?   D . n 
D 2 586  LYS 586  244  ?    ?   ?   D . n 
D 2 587  SER 587  245  ?    ?   ?   D . n 
D 2 588  GLY 588  246  ?    ?   ?   D . n 
D 2 589  ALA 589  247  ?    ?   ?   D . n 
D 2 590  PHE 590  248  ?    ?   ?   D . n 
D 2 591  LEU 591  249  ?    ?   ?   D . n 
D 2 592  ASP 592  250  ?    ?   ?   D . n 
D 2 593  ALA 593  251  ?    ?   ?   D . n 
D 2 594  PHE 594  252  ?    ?   ?   D . n 
D 2 595  HIS 595  253  ?    ?   ?   D . n 
D 2 596  GLN 596  254  ?    ?   ?   D . n 
D 2 597  ILE 597  255  ?    ?   ?   D . n 
D 2 598  LEU 598  256  ?    ?   ?   D . n 
D 2 599  SER 599  257  ?    ?   ?   D . n 
D 2 600  GLU 600  258  ?    ?   ?   D . n 
D 2 601  GLY 601  259  ?    ?   ?   D . n 
D 2 602  GLU 602  260  ?    ?   ?   D . n 
D 2 603  ASN 603  261  ?    ?   ?   D . n 
D 2 604  ALA 604  262  ?    ?   ?   D . n 
D 2 605  GLN 605  263  ?    ?   ?   D . n 
D 2 606  ALA 606  264  ?    ?   ?   D . n 
D 2 607  ALA 607  265  ?    ?   ?   D . n 
D 2 608  LEU 608  266  ?    ?   ?   D . n 
D 2 609  THR 609  267  ?    ?   ?   D . n 
D 2 610  ARG 610  268  ?    ?   ?   D . n 
D 2 611  LEU 611  269  ?    ?   ?   D . n 
D 2 612  SER 612  270  ?    ?   ?   D . n 
D 2 613  ARG 613  271  ?    ?   ?   D . n 
D 2 614  THR 614  272  ?    ?   ?   D . n 
D 2 615  PHE 615  273  ?    ?   ?   D . n 
D 2 616  ASP 616  274  ?    ?   ?   D . n 
D 2 617  ALA 617  275  ?    ?   ?   D . n 
D 2 618  PHE 618  276  ?    ?   ?   D . n 
D 2 619  LEU 619  277  ?    ?   ?   D . n 
D 2 620  GLY 620  278  ?    ?   ?   D . n 
D 2 621  VAL 621  279  ?    ?   ?   D . n 
D 2 622  VAL 622  280  ?    ?   ?   D . n 
D 2 623  PRO 623  281  ?    ?   ?   D . n 
D 2 624  PRO 624  282  ?    ?   ?   D . n 
D 2 625  VAL 625  283  ?    ?   ?   D . n 
D 2 626  ILE 626  284  ?    ?   ?   D . n 
D 2 627  ARG 627  285  ?    ?   ?   D . n 
D 2 628  VAL 628  286  ?    ?   ?   D . n 
D 2 629  LYS 629  287  ?    ?   ?   D . n 
D 2 630  ASN 630  288  ?    ?   ?   D . n 
D 2 631  PHE 631  289  ?    ?   ?   D . n 
D 2 632  GLN 632  290  ?    ?   ?   D . n 
D 2 633  THR 633  291  ?    ?   ?   D . n 
D 2 634  VAL 634  292  ?    ?   ?   D . n 
D 2 635  PRO 635  293  ?    ?   ?   D . n 
D 2 636  ARG 636  294  ?    ?   ?   D . n 
D 2 637  PRO 637  295  ?    ?   ?   D . n 
D 2 638  CYS 638  296  ?    ?   ?   D . n 
D 2 639  GLN 639  297  ?    ?   ?   D . n 
D 2 640  LYS 640  298  ?    ?   ?   D . n 
D 2 641  SER 641  299  ?    ?   ?   D . n 
D 2 642  LEU 642  300  ?    ?   ?   D . n 
D 2 643  ARG 643  301  ?    ?   ?   D . n 
D 2 644  ALA 644  302  ?    ?   ?   D . n 
D 2 645  VAL 645  303  ?    ?   ?   D . n 
D 2 646  PRO 646  304  ?    ?   ?   D . n 
D 2 647  PRO 647  305  ?    ?   ?   D . n 
D 2 648  ASN 648  306  ?    ?   ?   D . n 
D 2 649  PRO 649  307  ?    ?   ?   D . n 
D 2 650  THR 650  308  ?    ?   ?   D . n 
D 2 651  ILE 651  309  ?    ?   ?   D . n 
D 2 652  ASP 652  310  ?    ?   ?   D . n 
D 2 653  LYS 653  311  ?    ?   ?   D . n 
D 2 654  GLY 654  312  ?    ?   ?   D . n 
D 2 655  TRP 655  313  ?    ?   ?   D . n 
D 2 656  VAL 656  314  ?    ?   ?   D . n 
D 2 657  CYS 657  315  ?    ?   ?   D . n 
D 2 658  VAL 658  316  ?    ?   ?   D . n 
D 2 659  TYR 659  317  ?    ?   ?   D . n 
D 2 660  SER 660  318  ?    ?   ?   D . n 
D 2 661  SER 661  319  ?    ?   ?   D . n 
D 2 662  GLU 662  320  ?    ?   ?   D . n 
D 2 663  GLN 663  321  ?    ?   ?   D . n 
D 2 664  GLY 664  322  ?    ?   ?   D . n 
D 2 665  GLU 665  323  ?    ?   ?   D . n 
D 2 666  THR 666  324  ?    ?   ?   D . n 
D 2 667  ARG 667  325  ?    ?   ?   D . n 
D 2 668  ALA 668  326  ?    ?   ?   D . n 
D 2 669  LEU 669  327  ?    ?   ?   D . n 
D 2 670  LYS 670  328  ?    ?   ?   D . n 
D 2 671  ILE 671  329  ?    ?   ?   D . n 
E 2 1    MET 1    -341 ?    ?   ?   E . n 
E 2 2    GLY 2    -340 ?    ?   ?   E . n 
E 2 3    SER 3    -339 ?    ?   ?   E . n 
E 2 4    SER 4    -338 ?    ?   ?   E . n 
E 2 5    HIS 5    -337 ?    ?   ?   E . n 
E 2 6    HIS 6    -336 ?    ?   ?   E . n 
E 2 7    HIS 7    -335 ?    ?   ?   E . n 
E 2 8    HIS 8    -334 ?    ?   ?   E . n 
E 2 9    HIS 9    -333 ?    ?   ?   E . n 
E 2 10   HIS 10   -332 ?    ?   ?   E . n 
E 2 11   GLY 11   -331 ?    ?   ?   E . n 
E 2 12   THR 12   -330 ?    ?   ?   E . n 
E 2 13   LYS 13   -329 ?    ?   ?   E . n 
E 2 14   THR 14   -328 ?    ?   ?   E . n 
E 2 15   GLU 15   -327 ?    ?   ?   E . n 
E 2 16   GLU 16   -326 ?    ?   ?   E . n 
E 2 17   GLY 17   -325 ?    ?   ?   E . n 
E 2 18   LYS 18   -324 ?    ?   ?   E . n 
E 2 19   LEU 19   -323 ?    ?   ?   E . n 
E 2 20   VAL 20   -322 ?    ?   ?   E . n 
E 2 21   ILE 21   -321 ?    ?   ?   E . n 
E 2 22   TRP 22   -320 ?    ?   ?   E . n 
E 2 23   ILE 23   -319 ?    ?   ?   E . n 
E 2 24   ASN 24   -318 ?    ?   ?   E . n 
E 2 25   GLY 25   -317 ?    ?   ?   E . n 
E 2 26   ASP 26   -316 ?    ?   ?   E . n 
E 2 27   LYS 27   -315 ?    ?   ?   E . n 
E 2 28   GLY 28   -314 ?    ?   ?   E . n 
E 2 29   TYR 29   -313 ?    ?   ?   E . n 
E 2 30   ASN 30   -312 ?    ?   ?   E . n 
E 2 31   GLY 31   -311 ?    ?   ?   E . n 
E 2 32   LEU 32   -310 ?    ?   ?   E . n 
E 2 33   ALA 33   -309 ?    ?   ?   E . n 
E 2 34   GLU 34   -308 ?    ?   ?   E . n 
E 2 35   VAL 35   -307 ?    ?   ?   E . n 
E 2 36   GLY 36   -306 ?    ?   ?   E . n 
E 2 37   LYS 37   -305 ?    ?   ?   E . n 
E 2 38   LYS 38   -304 ?    ?   ?   E . n 
E 2 39   PHE 39   -303 ?    ?   ?   E . n 
E 2 40   GLU 40   -302 ?    ?   ?   E . n 
E 2 41   LYS 41   -301 ?    ?   ?   E . n 
E 2 42   ASP 42   -300 ?    ?   ?   E . n 
E 2 43   THR 43   -299 ?    ?   ?   E . n 
E 2 44   GLY 44   -298 ?    ?   ?   E . n 
E 2 45   ILE 45   -297 ?    ?   ?   E . n 
E 2 46   LYS 46   -296 ?    ?   ?   E . n 
E 2 47   VAL 47   -295 ?    ?   ?   E . n 
E 2 48   THR 48   -294 ?    ?   ?   E . n 
E 2 49   VAL 49   -293 ?    ?   ?   E . n 
E 2 50   GLU 50   -292 ?    ?   ?   E . n 
E 2 51   HIS 51   -291 ?    ?   ?   E . n 
E 2 52   PRO 52   -290 ?    ?   ?   E . n 
E 2 53   ASP 53   -289 ?    ?   ?   E . n 
E 2 54   LYS 54   -288 ?    ?   ?   E . n 
E 2 55   LEU 55   -287 ?    ?   ?   E . n 
E 2 56   GLU 56   -286 ?    ?   ?   E . n 
E 2 57   GLU 57   -285 ?    ?   ?   E . n 
E 2 58   LYS 58   -284 ?    ?   ?   E . n 
E 2 59   PHE 59   -283 ?    ?   ?   E . n 
E 2 60   PRO 60   -282 ?    ?   ?   E . n 
E 2 61   GLN 61   -281 ?    ?   ?   E . n 
E 2 62   VAL 62   -280 ?    ?   ?   E . n 
E 2 63   ALA 63   -279 ?    ?   ?   E . n 
E 2 64   ALA 64   -278 ?    ?   ?   E . n 
E 2 65   THR 65   -277 ?    ?   ?   E . n 
E 2 66   GLY 66   -276 ?    ?   ?   E . n 
E 2 67   ASP 67   -275 ?    ?   ?   E . n 
E 2 68   GLY 68   -274 ?    ?   ?   E . n 
E 2 69   PRO 69   -273 ?    ?   ?   E . n 
E 2 70   ASP 70   -272 ?    ?   ?   E . n 
E 2 71   ILE 71   -271 ?    ?   ?   E . n 
E 2 72   ILE 72   -270 ?    ?   ?   E . n 
E 2 73   PHE 73   -269 ?    ?   ?   E . n 
E 2 74   TRP 74   -268 ?    ?   ?   E . n 
E 2 75   ALA 75   -267 ?    ?   ?   E . n 
E 2 76   HIS 76   -266 ?    ?   ?   E . n 
E 2 77   ASP 77   -265 ?    ?   ?   E . n 
E 2 78   ARG 78   -264 ?    ?   ?   E . n 
E 2 79   PHE 79   -263 ?    ?   ?   E . n 
E 2 80   GLY 80   -262 ?    ?   ?   E . n 
E 2 81   GLY 81   -261 ?    ?   ?   E . n 
E 2 82   TYR 82   -260 ?    ?   ?   E . n 
E 2 83   ALA 83   -259 ?    ?   ?   E . n 
E 2 84   GLN 84   -258 ?    ?   ?   E . n 
E 2 85   SER 85   -257 ?    ?   ?   E . n 
E 2 86   GLY 86   -256 ?    ?   ?   E . n 
E 2 87   LEU 87   -255 ?    ?   ?   E . n 
E 2 88   LEU 88   -254 ?    ?   ?   E . n 
E 2 89   ALA 89   -253 ?    ?   ?   E . n 
E 2 90   GLU 90   -252 ?    ?   ?   E . n 
E 2 91   ILE 91   -251 ?    ?   ?   E . n 
E 2 92   THR 92   -250 ?    ?   ?   E . n 
E 2 93   PRO 93   -249 ?    ?   ?   E . n 
E 2 94   ASP 94   -248 ?    ?   ?   E . n 
E 2 95   LYS 95   -247 ?    ?   ?   E . n 
E 2 96   ALA 96   -246 ?    ?   ?   E . n 
E 2 97   PHE 97   -245 ?    ?   ?   E . n 
E 2 98   GLN 98   -244 ?    ?   ?   E . n 
E 2 99   ASP 99   -243 ?    ?   ?   E . n 
E 2 100  LYS 100  -242 ?    ?   ?   E . n 
E 2 101  LEU 101  -241 ?    ?   ?   E . n 
E 2 102  TYR 102  -240 ?    ?   ?   E . n 
E 2 103  PRO 103  -239 ?    ?   ?   E . n 
E 2 104  PHE 104  -238 ?    ?   ?   E . n 
E 2 105  THR 105  -237 ?    ?   ?   E . n 
E 2 106  TRP 106  -236 ?    ?   ?   E . n 
E 2 107  ASP 107  -235 ?    ?   ?   E . n 
E 2 108  ALA 108  -234 ?    ?   ?   E . n 
E 2 109  VAL 109  -233 ?    ?   ?   E . n 
E 2 110  ARG 110  -232 ?    ?   ?   E . n 
E 2 111  TYR 111  -231 ?    ?   ?   E . n 
E 2 112  ASN 112  -230 ?    ?   ?   E . n 
E 2 113  GLY 113  -229 ?    ?   ?   E . n 
E 2 114  LYS 114  -228 ?    ?   ?   E . n 
E 2 115  LEU 115  -227 ?    ?   ?   E . n 
E 2 116  ILE 116  -226 ?    ?   ?   E . n 
E 2 117  ALA 117  -225 ?    ?   ?   E . n 
E 2 118  TYR 118  -224 ?    ?   ?   E . n 
E 2 119  PRO 119  -223 ?    ?   ?   E . n 
E 2 120  ILE 120  -222 ?    ?   ?   E . n 
E 2 121  ALA 121  -221 ?    ?   ?   E . n 
E 2 122  VAL 122  -220 ?    ?   ?   E . n 
E 2 123  GLU 123  -219 ?    ?   ?   E . n 
E 2 124  ALA 124  -218 ?    ?   ?   E . n 
E 2 125  LEU 125  -217 ?    ?   ?   E . n 
E 2 126  SER 126  -216 ?    ?   ?   E . n 
E 2 127  LEU 127  -215 ?    ?   ?   E . n 
E 2 128  ILE 128  -214 ?    ?   ?   E . n 
E 2 129  TYR 129  -213 ?    ?   ?   E . n 
E 2 130  ASN 130  -212 ?    ?   ?   E . n 
E 2 131  LYS 131  -211 ?    ?   ?   E . n 
E 2 132  ASP 132  -210 ?    ?   ?   E . n 
E 2 133  LEU 133  -209 ?    ?   ?   E . n 
E 2 134  LEU 134  -208 ?    ?   ?   E . n 
E 2 135  PRO 135  -207 ?    ?   ?   E . n 
E 2 136  ASN 136  -206 ?    ?   ?   E . n 
E 2 137  PRO 137  -205 ?    ?   ?   E . n 
E 2 138  PRO 138  -204 ?    ?   ?   E . n 
E 2 139  LYS 139  -203 ?    ?   ?   E . n 
E 2 140  THR 140  -202 ?    ?   ?   E . n 
E 2 141  TRP 141  -201 ?    ?   ?   E . n 
E 2 142  GLU 142  -200 ?    ?   ?   E . n 
E 2 143  GLU 143  -199 ?    ?   ?   E . n 
E 2 144  ILE 144  -198 ?    ?   ?   E . n 
E 2 145  PRO 145  -197 ?    ?   ?   E . n 
E 2 146  ALA 146  -196 ?    ?   ?   E . n 
E 2 147  LEU 147  -195 ?    ?   ?   E . n 
E 2 148  ASP 148  -194 ?    ?   ?   E . n 
E 2 149  LYS 149  -193 ?    ?   ?   E . n 
E 2 150  GLU 150  -192 ?    ?   ?   E . n 
E 2 151  LEU 151  -191 ?    ?   ?   E . n 
E 2 152  LYS 152  -190 ?    ?   ?   E . n 
E 2 153  ALA 153  -189 ?    ?   ?   E . n 
E 2 154  LYS 154  -188 ?    ?   ?   E . n 
E 2 155  GLY 155  -187 ?    ?   ?   E . n 
E 2 156  LYS 156  -186 ?    ?   ?   E . n 
E 2 157  SER 157  -185 ?    ?   ?   E . n 
E 2 158  ALA 158  -184 ?    ?   ?   E . n 
E 2 159  LEU 159  -183 ?    ?   ?   E . n 
E 2 160  MET 160  -182 ?    ?   ?   E . n 
E 2 161  PHE 161  -181 ?    ?   ?   E . n 
E 2 162  ASN 162  -180 ?    ?   ?   E . n 
E 2 163  LEU 163  -179 ?    ?   ?   E . n 
E 2 164  GLN 164  -178 ?    ?   ?   E . n 
E 2 165  GLU 165  -177 ?    ?   ?   E . n 
E 2 166  PRO 166  -176 ?    ?   ?   E . n 
E 2 167  TYR 167  -175 ?    ?   ?   E . n 
E 2 168  PHE 168  -174 ?    ?   ?   E . n 
E 2 169  THR 169  -173 ?    ?   ?   E . n 
E 2 170  TRP 170  -172 ?    ?   ?   E . n 
E 2 171  PRO 171  -171 ?    ?   ?   E . n 
E 2 172  LEU 172  -170 ?    ?   ?   E . n 
E 2 173  ILE 173  -169 ?    ?   ?   E . n 
E 2 174  ALA 174  -168 ?    ?   ?   E . n 
E 2 175  ALA 175  -167 ?    ?   ?   E . n 
E 2 176  ASP 176  -166 ?    ?   ?   E . n 
E 2 177  GLY 177  -165 ?    ?   ?   E . n 
E 2 178  GLY 178  -164 ?    ?   ?   E . n 
E 2 179  TYR 179  -163 ?    ?   ?   E . n 
E 2 180  ALA 180  -162 ?    ?   ?   E . n 
E 2 181  PHE 181  -161 ?    ?   ?   E . n 
E 2 182  LYS 182  -160 ?    ?   ?   E . n 
E 2 183  TYR 183  -159 ?    ?   ?   E . n 
E 2 184  GLU 184  -158 ?    ?   ?   E . n 
E 2 185  ASN 185  -157 ?    ?   ?   E . n 
E 2 186  GLY 186  -156 ?    ?   ?   E . n 
E 2 187  LYS 187  -155 ?    ?   ?   E . n 
E 2 188  TYR 188  -154 ?    ?   ?   E . n 
E 2 189  ASP 189  -153 ?    ?   ?   E . n 
E 2 190  ILE 190  -152 ?    ?   ?   E . n 
E 2 191  LYS 191  -151 ?    ?   ?   E . n 
E 2 192  ASP 192  -150 ?    ?   ?   E . n 
E 2 193  VAL 193  -149 ?    ?   ?   E . n 
E 2 194  GLY 194  -148 ?    ?   ?   E . n 
E 2 195  VAL 195  -147 ?    ?   ?   E . n 
E 2 196  ASP 196  -146 ?    ?   ?   E . n 
E 2 197  ASN 197  -145 ?    ?   ?   E . n 
E 2 198  ALA 198  -144 ?    ?   ?   E . n 
E 2 199  GLY 199  -143 ?    ?   ?   E . n 
E 2 200  ALA 200  -142 ?    ?   ?   E . n 
E 2 201  LYS 201  -141 ?    ?   ?   E . n 
E 2 202  ALA 202  -140 ?    ?   ?   E . n 
E 2 203  GLY 203  -139 ?    ?   ?   E . n 
E 2 204  LEU 204  -138 ?    ?   ?   E . n 
E 2 205  THR 205  -137 ?    ?   ?   E . n 
E 2 206  PHE 206  -136 ?    ?   ?   E . n 
E 2 207  LEU 207  -135 ?    ?   ?   E . n 
E 2 208  VAL 208  -134 ?    ?   ?   E . n 
E 2 209  ASP 209  -133 ?    ?   ?   E . n 
E 2 210  LEU 210  -132 ?    ?   ?   E . n 
E 2 211  ILE 211  -131 ?    ?   ?   E . n 
E 2 212  LYS 212  -130 ?    ?   ?   E . n 
E 2 213  ASN 213  -129 ?    ?   ?   E . n 
E 2 214  LYS 214  -128 ?    ?   ?   E . n 
E 2 215  HIS 215  -127 ?    ?   ?   E . n 
E 2 216  MET 216  -126 ?    ?   ?   E . n 
E 2 217  ASN 217  -125 ?    ?   ?   E . n 
E 2 218  ALA 218  -124 ?    ?   ?   E . n 
E 2 219  ASP 219  -123 ?    ?   ?   E . n 
E 2 220  THR 220  -122 ?    ?   ?   E . n 
E 2 221  ASP 221  -121 ?    ?   ?   E . n 
E 2 222  TYR 222  -120 ?    ?   ?   E . n 
E 2 223  SER 223  -119 ?    ?   ?   E . n 
E 2 224  ILE 224  -118 ?    ?   ?   E . n 
E 2 225  ALA 225  -117 ?    ?   ?   E . n 
E 2 226  GLU 226  -116 ?    ?   ?   E . n 
E 2 227  ALA 227  -115 ?    ?   ?   E . n 
E 2 228  ALA 228  -114 ?    ?   ?   E . n 
E 2 229  PHE 229  -113 ?    ?   ?   E . n 
E 2 230  ASN 230  -112 ?    ?   ?   E . n 
E 2 231  LYS 231  -111 ?    ?   ?   E . n 
E 2 232  GLY 232  -110 ?    ?   ?   E . n 
E 2 233  GLU 233  -109 ?    ?   ?   E . n 
E 2 234  THR 234  -108 ?    ?   ?   E . n 
E 2 235  ALA 235  -107 ?    ?   ?   E . n 
E 2 236  MET 236  -106 ?    ?   ?   E . n 
E 2 237  THR 237  -105 ?    ?   ?   E . n 
E 2 238  ILE 238  -104 ?    ?   ?   E . n 
E 2 239  ASN 239  -103 ?    ?   ?   E . n 
E 2 240  GLY 240  -102 ?    ?   ?   E . n 
E 2 241  PRO 241  -101 ?    ?   ?   E . n 
E 2 242  TRP 242  -100 ?    ?   ?   E . n 
E 2 243  ALA 243  -99  ?    ?   ?   E . n 
E 2 244  TRP 244  -98  ?    ?   ?   E . n 
E 2 245  SER 245  -97  ?    ?   ?   E . n 
E 2 246  ASN 246  -96  ?    ?   ?   E . n 
E 2 247  ILE 247  -95  ?    ?   ?   E . n 
E 2 248  ASP 248  -94  ?    ?   ?   E . n 
E 2 249  THR 249  -93  ?    ?   ?   E . n 
E 2 250  SER 250  -92  ?    ?   ?   E . n 
E 2 251  LYS 251  -91  ?    ?   ?   E . n 
E 2 252  VAL 252  -90  ?    ?   ?   E . n 
E 2 253  ASN 253  -89  ?    ?   ?   E . n 
E 2 254  TYR 254  -88  ?    ?   ?   E . n 
E 2 255  GLY 255  -87  ?    ?   ?   E . n 
E 2 256  VAL 256  -86  ?    ?   ?   E . n 
E 2 257  THR 257  -85  ?    ?   ?   E . n 
E 2 258  VAL 258  -84  ?    ?   ?   E . n 
E 2 259  LEU 259  -83  ?    ?   ?   E . n 
E 2 260  PRO 260  -82  ?    ?   ?   E . n 
E 2 261  THR 261  -81  ?    ?   ?   E . n 
E 2 262  PHE 262  -80  ?    ?   ?   E . n 
E 2 263  LYS 263  -79  ?    ?   ?   E . n 
E 2 264  GLY 264  -78  ?    ?   ?   E . n 
E 2 265  GLN 265  -77  ?    ?   ?   E . n 
E 2 266  PRO 266  -76  ?    ?   ?   E . n 
E 2 267  SER 267  -75  ?    ?   ?   E . n 
E 2 268  LYS 268  -74  ?    ?   ?   E . n 
E 2 269  PRO 269  -73  ?    ?   ?   E . n 
E 2 270  PHE 270  -72  ?    ?   ?   E . n 
E 2 271  VAL 271  -71  ?    ?   ?   E . n 
E 2 272  GLY 272  -70  ?    ?   ?   E . n 
E 2 273  VAL 273  -69  ?    ?   ?   E . n 
E 2 274  LEU 274  -68  ?    ?   ?   E . n 
E 2 275  SER 275  -67  ?    ?   ?   E . n 
E 2 276  ALA 276  -66  ?    ?   ?   E . n 
E 2 277  GLY 277  -65  ?    ?   ?   E . n 
E 2 278  ILE 278  -64  ?    ?   ?   E . n 
E 2 279  ASN 279  -63  ?    ?   ?   E . n 
E 2 280  ALA 280  -62  ?    ?   ?   E . n 
E 2 281  ALA 281  -61  ?    ?   ?   E . n 
E 2 282  SER 282  -60  ?    ?   ?   E . n 
E 2 283  PRO 283  -59  ?    ?   ?   E . n 
E 2 284  ASN 284  -58  ?    ?   ?   E . n 
E 2 285  LYS 285  -57  ?    ?   ?   E . n 
E 2 286  GLU 286  -56  ?    ?   ?   E . n 
E 2 287  LEU 287  -55  ?    ?   ?   E . n 
E 2 288  ALA 288  -54  ?    ?   ?   E . n 
E 2 289  LYS 289  -53  ?    ?   ?   E . n 
E 2 290  GLU 290  -52  ?    ?   ?   E . n 
E 2 291  PHE 291  -51  ?    ?   ?   E . n 
E 2 292  LEU 292  -50  ?    ?   ?   E . n 
E 2 293  GLU 293  -49  ?    ?   ?   E . n 
E 2 294  ASN 294  -48  ?    ?   ?   E . n 
E 2 295  TYR 295  -47  ?    ?   ?   E . n 
E 2 296  LEU 296  -46  ?    ?   ?   E . n 
E 2 297  LEU 297  -45  ?    ?   ?   E . n 
E 2 298  THR 298  -44  ?    ?   ?   E . n 
E 2 299  ASP 299  -43  ?    ?   ?   E . n 
E 2 300  GLU 300  -42  ?    ?   ?   E . n 
E 2 301  GLY 301  -41  ?    ?   ?   E . n 
E 2 302  LEU 302  -40  ?    ?   ?   E . n 
E 2 303  GLU 303  -39  ?    ?   ?   E . n 
E 2 304  ALA 304  -38  ?    ?   ?   E . n 
E 2 305  VAL 305  -37  ?    ?   ?   E . n 
E 2 306  ASN 306  -36  ?    ?   ?   E . n 
E 2 307  LYS 307  -35  ?    ?   ?   E . n 
E 2 308  ASP 308  -34  ?    ?   ?   E . n 
E 2 309  LYS 309  -33  ?    ?   ?   E . n 
E 2 310  PRO 310  -32  ?    ?   ?   E . n 
E 2 311  LEU 311  -31  ?    ?   ?   E . n 
E 2 312  GLY 312  -30  ?    ?   ?   E . n 
E 2 313  ALA 313  -29  ?    ?   ?   E . n 
E 2 314  VAL 314  -28  ?    ?   ?   E . n 
E 2 315  ALA 315  -27  ?    ?   ?   E . n 
E 2 316  LEU 316  -26  ?    ?   ?   E . n 
E 2 317  LYS 317  -25  ?    ?   ?   E . n 
E 2 318  SER 318  -24  ?    ?   ?   E . n 
E 2 319  TYR 319  -23  ?    ?   ?   E . n 
E 2 320  GLU 320  -22  ?    ?   ?   E . n 
E 2 321  GLU 321  -21  ?    ?   ?   E . n 
E 2 322  GLU 322  -20  ?    ?   ?   E . n 
E 2 323  LEU 323  -19  ?    ?   ?   E . n 
E 2 324  ALA 324  -18  ?    ?   ?   E . n 
E 2 325  LYS 325  -17  ?    ?   ?   E . n 
E 2 326  ASP 326  -16  ?    ?   ?   E . n 
E 2 327  PRO 327  -15  ?    ?   ?   E . n 
E 2 328  ARG 328  -14  ?    ?   ?   E . n 
E 2 329  ILE 329  -13  ?    ?   ?   E . n 
E 2 330  ALA 330  -12  ?    ?   ?   E . n 
E 2 331  ALA 331  -11  ?    ?   ?   E . n 
E 2 332  THR 332  -10  ?    ?   ?   E . n 
E 2 333  MET 333  -9   ?    ?   ?   E . n 
E 2 334  GLU 334  -8   ?    ?   ?   E . n 
E 2 335  ASN 335  -7   ?    ?   ?   E . n 
E 2 336  ALA 336  -6   ?    ?   ?   E . n 
E 2 337  GLN 337  -5   ?    ?   ?   E . n 
E 2 338  LYS 338  -4   ?    ?   ?   E . n 
E 2 339  GLY 339  -3   ?    ?   ?   E . n 
E 2 340  GLU 340  -2   ?    ?   ?   E . n 
E 2 341  ILE 341  -1   ?    ?   ?   E . n 
E 2 342  MET 342  0    ?    ?   ?   E . n 
E 2 343  PRO 343  1    ?    ?   ?   E . n 
E 2 344  ASN 344  2    ?    ?   ?   E . n 
E 2 345  ILE 345  3    ?    ?   ?   E . n 
E 2 346  PRO 346  4    ?    ?   ?   E . n 
E 2 347  GLN 347  5    ?    ?   ?   E . n 
E 2 348  MET 348  6    ?    ?   ?   E . n 
E 2 349  SER 349  7    ?    ?   ?   E . n 
E 2 350  ALA 350  8    ?    ?   ?   E . n 
E 2 351  PHE 351  9    ?    ?   ?   E . n 
E 2 352  TRP 352  10   ?    ?   ?   E . n 
E 2 353  TYR 353  11   ?    ?   ?   E . n 
E 2 354  ALA 354  12   ?    ?   ?   E . n 
E 2 355  VAL 355  13   ?    ?   ?   E . n 
E 2 356  ARG 356  14   ?    ?   ?   E . n 
E 2 357  THR 357  15   ?    ?   ?   E . n 
E 2 358  ALA 358  16   ?    ?   ?   E . n 
E 2 359  VAL 359  17   ?    ?   ?   E . n 
E 2 360  ILE 360  18   ?    ?   ?   E . n 
E 2 361  ASN 361  19   ?    ?   ?   E . n 
E 2 362  ALA 362  20   ?    ?   ?   E . n 
E 2 363  ALA 363  21   ?    ?   ?   E . n 
E 2 364  SER 364  22   ?    ?   ?   E . n 
E 2 365  GLY 365  23   ?    ?   ?   E . n 
E 2 366  ARG 366  24   ?    ?   ?   E . n 
E 2 367  GLN 367  25   ?    ?   ?   E . n 
E 2 368  THR 368  26   ?    ?   ?   E . n 
E 2 369  VAL 369  27   ?    ?   ?   E . n 
E 2 370  ASP 370  28   ?    ?   ?   E . n 
E 2 371  GLU 371  29   ?    ?   ?   E . n 
E 2 372  ALA 372  30   ?    ?   ?   E . n 
E 2 373  LEU 373  31   ?    ?   ?   E . n 
E 2 374  LYS 374  32   ?    ?   ?   E . n 
E 2 375  ASP 375  33   ?    ?   ?   E . n 
E 2 376  ALA 376  34   ?    ?   ?   E . n 
E 2 377  GLN 377  35   ?    ?   ?   E . n 
E 2 378  THR 378  36   ?    ?   ?   E . n 
E 2 379  GLY 379  37   ?    ?   ?   E . n 
E 2 380  THR 380  38   ?    ?   ?   E . n 
E 2 381  ASP 381  39   ?    ?   ?   E . n 
E 2 382  TYR 382  40   ?    ?   ?   E . n 
E 2 383  ASP 383  41   ?    ?   ?   E . n 
E 2 384  ILE 384  42   ?    ?   ?   E . n 
E 2 385  PRO 385  43   ?    ?   ?   E . n 
E 2 386  THR 386  44   ?    ?   ?   E . n 
E 2 387  THR 387  45   ?    ?   ?   E . n 
E 2 388  LEU 388  46   ?    ?   ?   E . n 
E 2 389  GLU 389  47   ?    ?   ?   E . n 
E 2 390  VAL 390  48   ?    ?   ?   E . n 
E 2 391  LEU 391  49   ?    ?   ?   E . n 
E 2 392  PHE 392  50   ?    ?   ?   E . n 
E 2 393  GLN 393  51   ?    ?   ?   E . n 
E 2 394  GLY 394  52   ?    ?   ?   E . n 
E 2 395  PRO 395  53   ?    ?   ?   E . n 
E 2 396  LEU 396  54   ?    ?   ?   E . n 
E 2 397  GLY 397  55   ?    ?   ?   E . n 
E 2 398  SER 398  56   ?    ?   ?   E . n 
E 2 399  SER 399  57   ?    ?   ?   E . n 
E 2 400  THR 400  58   ?    ?   ?   E . n 
E 2 401  ASP 401  59   ?    ?   ?   E . n 
E 2 402  ASP 402  60   ?    ?   ?   E . n 
E 2 403  ILE 403  61   ?    ?   ?   E . n 
E 2 404  ILE 404  62   ?    ?   ?   E . n 
E 2 405  TRP 405  63   ?    ?   ?   E . n 
E 2 406  ASP 406  64   ?    ?   ?   E . n 
E 2 407  GLN 407  65   ?    ?   ?   E . n 
E 2 408  LEU 408  66   ?    ?   ?   E . n 
E 2 409  ILE 409  67   ?    ?   ?   E . n 
E 2 410  VAL 410  68   ?    ?   ?   E . n 
E 2 411  LYS 411  69   ?    ?   ?   E . n 
E 2 412  ARG 412  70   ?    ?   ?   E . n 
E 2 413  THR 413  71   ?    ?   ?   E . n 
E 2 414  LEU 414  72   ?    ?   ?   E . n 
E 2 415  ALA 415  73   ?    ?   ?   E . n 
E 2 416  ASP 416  74   ?    ?   ?   E . n 
E 2 417  LEU 417  75   ?    ?   ?   E . n 
E 2 418  LEU 418  76   ?    ?   ?   E . n 
E 2 419  ILE 419  77   ?    ?   ?   E . n 
E 2 420  PRO 420  78   ?    ?   ?   E . n 
E 2 421  ILE 421  79   ?    ?   ?   E . n 
E 2 422  ASN 422  80   ?    ?   ?   E . n 
E 2 423  ARG 423  81   ?    ?   ?   E . n 
E 2 424  GLN 424  82   ?    ?   ?   E . n 
E 2 425  ILE 425  83   ?    ?   ?   E . n 
E 2 426  SER 426  84   ?    ?   ?   E . n 
E 2 427  ASP 427  85   ?    ?   ?   E . n 
E 2 428  ILE 428  86   ?    ?   ?   E . n 
E 2 429  GLN 429  87   ?    ?   ?   E . n 
E 2 430  SER 430  88   ?    ?   ?   E . n 
E 2 431  THR 431  89   ?    ?   ?   E . n 
E 2 432  LEU 432  90   ?    ?   ?   E . n 
E 2 433  SER 433  91   ?    ?   ?   E . n 
E 2 434  GLU 434  92   ?    ?   ?   E . n 
E 2 435  VAL 435  93   ?    ?   ?   E . n 
E 2 436  THR 436  94   ?    ?   ?   E . n 
E 2 437  THR 437  95   ?    ?   ?   E . n 
E 2 438  ARG 438  96   ?    ?   ?   E . n 
E 2 439  VAL 439  97   ?    ?   ?   E . n 
E 2 440  HIS 440  98   ?    ?   ?   E . n 
E 2 441  GLU 441  99   ?    ?   ?   E . n 
E 2 442  ILE 442  100  ?    ?   ?   E . n 
E 2 443  GLU 443  101  ?    ?   ?   E . n 
E 2 444  ARG 444  102  ?    ?   ?   E . n 
E 2 445  GLN 445  103  ?    ?   ?   E . n 
E 2 446  LEU 446  104  ?    ?   ?   E . n 
E 2 447  HIS 447  105  ?    ?   ?   E . n 
E 2 448  GLU 448  106  ?    ?   ?   E . n 
E 2 449  ILE 449  107  ?    ?   ?   E . n 
E 2 450  THR 450  108  ?    ?   ?   E . n 
E 2 451  PRO 451  109  ?    ?   ?   E . n 
E 2 452  VAL 452  110  110  VAL VAL E . n 
E 2 453  LEU 453  111  111  LEU LEU E . n 
E 2 454  LYS 454  112  112  LYS LYS E . n 
E 2 455  MET 455  113  113  MET MET E . n 
E 2 456  GLY 456  114  114  GLY GLY E . n 
E 2 457  ARG 457  115  115  ARG ARG E . n 
E 2 458  THR 458  116  116  THR THR E . n 
E 2 459  LEU 459  117  117  LEU LEU E . n 
E 2 460  GLU 460  118  118  GLU GLU E . n 
E 2 461  ALA 461  119  119  ALA ALA E . n 
E 2 462  ILE 462  120  120  ILE ILE E . n 
E 2 463  SER 463  121  121  SER SER E . n 
E 2 464  LYS 464  122  122  LYS LYS E . n 
E 2 465  GLY 465  123  123  GLY GLY E . n 
E 2 466  MET 466  124  124  MET MET E . n 
E 2 467  SER 467  125  125  SER SER E . n 
E 2 468  GLU 468  126  126  GLU GLU E . n 
E 2 469  MET 469  127  127  MET MET E . n 
E 2 470  LEU 470  128  128  LEU LEU E . n 
E 2 471  ALA 471  129  129  ALA ALA E . n 
E 2 472  LYS 472  130  130  LYS LYS E . n 
E 2 473  TYR 473  131  131  TYR TYR E . n 
E 2 474  ASP 474  132  132  ASP ASP E . n 
E 2 475  HIS 475  133  133  HIS HIS E . n 
E 2 476  LEU 476  134  134  LEU LEU E . n 
E 2 477  VAL 477  135  135  VAL VAL E . n 
E 2 478  ILE 478  136  ?    ?   ?   E . n 
E 2 479  SER 479  137  ?    ?   ?   E . n 
E 2 480  THR 480  138  ?    ?   ?   E . n 
E 2 481  GLY 481  139  ?    ?   ?   E . n 
E 2 482  ARG 482  140  ?    ?   ?   E . n 
E 2 483  THR 483  141  ?    ?   ?   E . n 
E 2 484  THR 484  142  ?    ?   ?   E . n 
E 2 485  ALA 485  143  ?    ?   ?   E . n 
E 2 486  PRO 486  144  ?    ?   ?   E . n 
E 2 487  ALA 487  145  ?    ?   ?   E . n 
E 2 488  ALA 488  146  ?    ?   ?   E . n 
E 2 489  ALA 489  147  ?    ?   ?   E . n 
E 2 490  PHE 490  148  ?    ?   ?   E . n 
E 2 491  ASP 491  149  ?    ?   ?   E . n 
E 2 492  ALA 492  150  ?    ?   ?   E . n 
E 2 493  TYR 493  151  ?    ?   ?   E . n 
E 2 494  LEU 494  152  ?    ?   ?   E . n 
E 2 495  ASN 495  153  ?    ?   ?   E . n 
E 2 496  GLU 496  154  ?    ?   ?   E . n 
E 2 497  HIS 497  155  ?    ?   ?   E . n 
E 2 498  GLY 498  156  ?    ?   ?   E . n 
E 2 499  VAL 499  157  ?    ?   ?   E . n 
E 2 500  PRO 500  158  ?    ?   ?   E . n 
E 2 501  PRO 501  159  ?    ?   ?   E . n 
E 2 502  PRO 502  160  ?    ?   ?   E . n 
E 2 503  GLN 503  161  ?    ?   ?   E . n 
E 2 504  PRO 504  162  ?    ?   ?   E . n 
E 2 505  ALA 505  163  ?    ?   ?   E . n 
E 2 506  ILE 506  164  ?    ?   ?   E . n 
E 2 507  PHE 507  165  ?    ?   ?   E . n 
E 2 508  LYS 508  166  ?    ?   ?   E . n 
E 2 509  ASP 509  167  ?    ?   ?   E . n 
E 2 510  LEU 510  168  ?    ?   ?   E . n 
E 2 511  GLY 511  169  ?    ?   ?   E . n 
E 2 512  VAL 512  170  ?    ?   ?   E . n 
E 2 513  ALA 513  171  ?    ?   ?   E . n 
E 2 514  GLN 514  172  ?    ?   ?   E . n 
E 2 515  GLN 515  173  ?    ?   ?   E . n 
E 2 516  ALA 516  174  ?    ?   ?   E . n 
E 2 517  CYS 517  175  ?    ?   ?   E . n 
E 2 518  SER 518  176  ?    ?   ?   E . n 
E 2 519  LYS 519  177  ?    ?   ?   E . n 
E 2 520  GLY 520  178  ?    ?   ?   E . n 
E 2 521  THR 521  179  ?    ?   ?   E . n 
E 2 522  MET 522  180  ?    ?   ?   E . n 
E 2 523  VAL 523  181  ?    ?   ?   E . n 
E 2 524  LYS 524  182  ?    ?   ?   E . n 
E 2 525  ASN 525  183  ?    ?   ?   E . n 
E 2 526  ALA 526  184  ?    ?   ?   E . n 
E 2 527  THR 527  185  ?    ?   ?   E . n 
E 2 528  THR 528  186  ?    ?   ?   E . n 
E 2 529  ASP 529  187  ?    ?   ?   E . n 
E 2 530  ALA 530  188  ?    ?   ?   E . n 
E 2 531  ALA 531  189  ?    ?   ?   E . n 
E 2 532  ASP 532  190  ?    ?   ?   E . n 
E 2 533  LYS 533  191  ?    ?   ?   E . n 
E 2 534  MET 534  192  ?    ?   ?   E . n 
E 2 535  SER 535  193  ?    ?   ?   E . n 
E 2 536  LYS 536  194  ?    ?   ?   E . n 
E 2 537  VAL 537  195  ?    ?   ?   E . n 
E 2 538  LEU 538  196  ?    ?   ?   E . n 
E 2 539  GLU 539  197  ?    ?   ?   E . n 
E 2 540  LEU 540  198  ?    ?   ?   E . n 
E 2 541  SER 541  199  ?    ?   ?   E . n 
E 2 542  GLU 542  200  ?    ?   ?   E . n 
E 2 543  GLU 543  201  ?    ?   ?   E . n 
E 2 544  THR 544  202  ?    ?   ?   E . n 
E 2 545  PHE 545  203  ?    ?   ?   E . n 
E 2 546  SER 546  204  ?    ?   ?   E . n 
E 2 547  LYS 547  205  ?    ?   ?   E . n 
E 2 548  PRO 548  206  ?    ?   ?   E . n 
E 2 549  ASN 549  207  ?    ?   ?   E . n 
E 2 550  LEU 550  208  ?    ?   ?   E . n 
E 2 551  SER 551  209  ?    ?   ?   E . n 
E 2 552  ALA 552  210  ?    ?   ?   E . n 
E 2 553  LYS 553  211  ?    ?   ?   E . n 
E 2 554  ASP 554  212  ?    ?   ?   E . n 
E 2 555  LEU 555  213  ?    ?   ?   E . n 
E 2 556  ALA 556  214  ?    ?   ?   E . n 
E 2 557  LEU 557  215  ?    ?   ?   E . n 
E 2 558  LEU 558  216  ?    ?   ?   E . n 
E 2 559  LEU 559  217  ?    ?   ?   E . n 
E 2 560  PHE 560  218  ?    ?   ?   E . n 
E 2 561  THR 561  219  ?    ?   ?   E . n 
E 2 562  HIS 562  220  ?    ?   ?   E . n 
E 2 563  LEU 563  221  ?    ?   ?   E . n 
E 2 564  PRO 564  222  ?    ?   ?   E . n 
E 2 565  GLY 565  223  ?    ?   ?   E . n 
E 2 566  ASN 566  224  ?    ?   ?   E . n 
E 2 567  ASN 567  225  ?    ?   ?   E . n 
E 2 568  THR 568  226  ?    ?   ?   E . n 
E 2 569  PRO 569  227  ?    ?   ?   E . n 
E 2 570  PHE 570  228  ?    ?   ?   E . n 
E 2 571  HIS 571  229  ?    ?   ?   E . n 
E 2 572  ILE 572  230  ?    ?   ?   E . n 
E 2 573  LEU 573  231  ?    ?   ?   E . n 
E 2 574  ALA 574  232  ?    ?   ?   E . n 
E 2 575  GLN 575  233  ?    ?   ?   E . n 
E 2 576  VAL 576  234  ?    ?   ?   E . n 
E 2 577  LEU 577  235  ?    ?   ?   E . n 
E 2 578  SER 578  236  ?    ?   ?   E . n 
E 2 579  LYS 579  237  ?    ?   ?   E . n 
E 2 580  ILE 580  238  ?    ?   ?   E . n 
E 2 581  ALA 581  239  ?    ?   ?   E . n 
E 2 582  TYR 582  240  ?    ?   ?   E . n 
E 2 583  LYS 583  241  ?    ?   ?   E . n 
E 2 584  SER 584  242  ?    ?   ?   E . n 
E 2 585  GLY 585  243  ?    ?   ?   E . n 
E 2 586  LYS 586  244  ?    ?   ?   E . n 
E 2 587  SER 587  245  ?    ?   ?   E . n 
E 2 588  GLY 588  246  ?    ?   ?   E . n 
E 2 589  ALA 589  247  ?    ?   ?   E . n 
E 2 590  PHE 590  248  ?    ?   ?   E . n 
E 2 591  LEU 591  249  ?    ?   ?   E . n 
E 2 592  ASP 592  250  ?    ?   ?   E . n 
E 2 593  ALA 593  251  ?    ?   ?   E . n 
E 2 594  PHE 594  252  ?    ?   ?   E . n 
E 2 595  HIS 595  253  ?    ?   ?   E . n 
E 2 596  GLN 596  254  ?    ?   ?   E . n 
E 2 597  ILE 597  255  ?    ?   ?   E . n 
E 2 598  LEU 598  256  ?    ?   ?   E . n 
E 2 599  SER 599  257  ?    ?   ?   E . n 
E 2 600  GLU 600  258  ?    ?   ?   E . n 
E 2 601  GLY 601  259  ?    ?   ?   E . n 
E 2 602  GLU 602  260  ?    ?   ?   E . n 
E 2 603  ASN 603  261  ?    ?   ?   E . n 
E 2 604  ALA 604  262  ?    ?   ?   E . n 
E 2 605  GLN 605  263  ?    ?   ?   E . n 
E 2 606  ALA 606  264  ?    ?   ?   E . n 
E 2 607  ALA 607  265  ?    ?   ?   E . n 
E 2 608  LEU 608  266  ?    ?   ?   E . n 
E 2 609  THR 609  267  ?    ?   ?   E . n 
E 2 610  ARG 610  268  ?    ?   ?   E . n 
E 2 611  LEU 611  269  ?    ?   ?   E . n 
E 2 612  SER 612  270  ?    ?   ?   E . n 
E 2 613  ARG 613  271  ?    ?   ?   E . n 
E 2 614  THR 614  272  ?    ?   ?   E . n 
E 2 615  PHE 615  273  ?    ?   ?   E . n 
E 2 616  ASP 616  274  ?    ?   ?   E . n 
E 2 617  ALA 617  275  ?    ?   ?   E . n 
E 2 618  PHE 618  276  ?    ?   ?   E . n 
E 2 619  LEU 619  277  ?    ?   ?   E . n 
E 2 620  GLY 620  278  ?    ?   ?   E . n 
E 2 621  VAL 621  279  ?    ?   ?   E . n 
E 2 622  VAL 622  280  ?    ?   ?   E . n 
E 2 623  PRO 623  281  ?    ?   ?   E . n 
E 2 624  PRO 624  282  ?    ?   ?   E . n 
E 2 625  VAL 625  283  ?    ?   ?   E . n 
E 2 626  ILE 626  284  ?    ?   ?   E . n 
E 2 627  ARG 627  285  ?    ?   ?   E . n 
E 2 628  VAL 628  286  ?    ?   ?   E . n 
E 2 629  LYS 629  287  ?    ?   ?   E . n 
E 2 630  ASN 630  288  ?    ?   ?   E . n 
E 2 631  PHE 631  289  ?    ?   ?   E . n 
E 2 632  GLN 632  290  ?    ?   ?   E . n 
E 2 633  THR 633  291  ?    ?   ?   E . n 
E 2 634  VAL 634  292  ?    ?   ?   E . n 
E 2 635  PRO 635  293  ?    ?   ?   E . n 
E 2 636  ARG 636  294  ?    ?   ?   E . n 
E 2 637  PRO 637  295  ?    ?   ?   E . n 
E 2 638  CYS 638  296  ?    ?   ?   E . n 
E 2 639  GLN 639  297  ?    ?   ?   E . n 
E 2 640  LYS 640  298  ?    ?   ?   E . n 
E 2 641  SER 641  299  ?    ?   ?   E . n 
E 2 642  LEU 642  300  ?    ?   ?   E . n 
E 2 643  ARG 643  301  ?    ?   ?   E . n 
E 2 644  ALA 644  302  ?    ?   ?   E . n 
E 2 645  VAL 645  303  ?    ?   ?   E . n 
E 2 646  PRO 646  304  ?    ?   ?   E . n 
E 2 647  PRO 647  305  ?    ?   ?   E . n 
E 2 648  ASN 648  306  ?    ?   ?   E . n 
E 2 649  PRO 649  307  ?    ?   ?   E . n 
E 2 650  THR 650  308  ?    ?   ?   E . n 
E 2 651  ILE 651  309  ?    ?   ?   E . n 
E 2 652  ASP 652  310  ?    ?   ?   E . n 
E 2 653  LYS 653  311  ?    ?   ?   E . n 
E 2 654  GLY 654  312  ?    ?   ?   E . n 
E 2 655  TRP 655  313  ?    ?   ?   E . n 
E 2 656  VAL 656  314  ?    ?   ?   E . n 
E 2 657  CYS 657  315  ?    ?   ?   E . n 
E 2 658  VAL 658  316  ?    ?   ?   E . n 
E 2 659  TYR 659  317  ?    ?   ?   E . n 
E 2 660  SER 660  318  ?    ?   ?   E . n 
E 2 661  SER 661  319  ?    ?   ?   E . n 
E 2 662  GLU 662  320  ?    ?   ?   E . n 
E 2 663  GLN 663  321  ?    ?   ?   E . n 
E 2 664  GLY 664  322  ?    ?   ?   E . n 
E 2 665  GLU 665  323  ?    ?   ?   E . n 
E 2 666  THR 666  324  ?    ?   ?   E . n 
E 2 667  ARG 667  325  ?    ?   ?   E . n 
E 2 668  ALA 668  326  ?    ?   ?   E . n 
E 2 669  LEU 669  327  ?    ?   ?   E . n 
E 2 670  LYS 670  328  ?    ?   ?   E . n 
E 2 671  ILE 671  329  ?    ?   ?   E . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZN 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_pdbx_nonpoly_scheme.asym_id         F 
_pdbx_nonpoly_scheme.entity_id       3 
_pdbx_nonpoly_scheme.mon_id          ZN 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     2001 
_pdbx_nonpoly_scheme.auth_seq_num    2001 
_pdbx_nonpoly_scheme.pdb_mon_id      ZN 
_pdbx_nonpoly_scheme.auth_mon_id     ZN 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IP4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9IP4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9IP4 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9IP4 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.84 
_refine.ls_d_res_low                             2.84 
_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                     2742936 
_refine.ls_number_reflns_R_free                  1968 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 7.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.3094 
_refine.ls_R_factor_R_free                       0.3271 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.3094 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          0.18 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 44.83 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.26 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.006  ? 13923 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 1.065  ? 18870 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 15.888 ? 1833  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.059  ? 2106  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.007  ? 2400  ? f_plane_restr      ? ? 
# 
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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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 
'ELECTRON MICROSCOPY' 2.80 2.87   . . 132 196688 100.00 . . . . 0.7988 . . . . . . . . . . . . . . . 0.7994 
'ELECTRON MICROSCOPY' 2.87 2.95   . . 144 195883 100.00 . . . . 0.5767 . . . . . . . . . . . . . . . 0.5201 
'ELECTRON MICROSCOPY' 2.95 3.03   . . 120 195458 100.00 . . . . 0.6122 . . . . . . . . . . . . . . . 0.6582 
'ELECTRON MICROSCOPY' 3.03 3.13   . . 168 195577 100.00 . . . . 0.5636 . . . . . . . . . . . . . . . 0.5657 
'ELECTRON MICROSCOPY' 3.13 3.24   . . 132 195587 100.00 . . . . 0.5174 . . . . . . . . . . . . . . . 0.4861 
'ELECTRON MICROSCOPY' 3.24 3.37   . . 144 196232 100.00 . . . . 0.4829 . . . . . . . . . . . . . . . 0.5142 
'ELECTRON MICROSCOPY' 3.37 3.53   . . 132 195614 100.00 . . . . 0.4412 . . . . . . . . . . . . . . . 0.4406 
'ELECTRON MICROSCOPY' 3.53 3.71   . . 156 195761 100.00 . . . . 0.3960 . . . . . . . . . . . . . . . 0.3990 
'ELECTRON MICROSCOPY' 3.71 3.95   . . 144 196047 100.00 . . . . 0.3358 . . . . . . . . . . . . . . . 0.3883 
'ELECTRON MICROSCOPY' 3.95 4.25   . . 132 195566 100.00 . . . . 0.2780 . . . . . . . . . . . . . . . 0.2841 
'ELECTRON MICROSCOPY' 4.25 4.68   . . 144 195651 100.00 . . . . 0.2315 . . . . . . . . . . . . . . . 0.2666 
'ELECTRON MICROSCOPY' 4.68 5.36   . . 156 196096 100.00 . . . . 0.2158 . . . . . . . . . . . . . . . 0.2314 
'ELECTRON MICROSCOPY' 5.36 6.75   . . 108 195654 100.00 . . . . 0.2462 . . . . . . . . . . . . . . . 0.2863 
'ELECTRON MICROSCOPY' 6.75 306.36 . . 156 195154 100.00 . . . . 0.1984 . . . . . . . . . . . . . . . 0.2180 
# 
_struct.entry_id                     9IP4 
_struct.title                        'Cryo-EM structure of the RNA-dependent RNA polymerase complex from Marburg virus' 
_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        9IP4 
_struct_keywords.text            'RNA-dependent RNA polymerase complex, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL 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 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP L_MABVM    P31352 ? 1 
;MQHPTQYPDARLSSPIILDQCDLLARSLGLYSHYSHNPKLRNCRIPHHIYRLRNSTALKTFLQNCSILTVPFHSIWDHIL
TSIQYDAINHVDDFKYLLPSELVKYANWDNEFLKAYLNKILGLDHVFSASARSQCEDFSPKENPYYWGMLLLVHLSQLAR
RIKGQRGSLRSNWKFIGTDLELFGIADFVIFKVPVKTIIRNAVSLQASKPGLRIWYRDQNLTPYLCDDEFIVSVASYECF
IMIKDVFIERYNTWEICARAWLEDSDGADYPPLDVLGELYNQGDQIIAMYLEDGFKLIKHLEPLCVSCIQTHGIFTPRKY
WFQSQMIKSYYDELHDLNLKLQISDNKAECAQNFIKTIVQAKLTPQQYCELFSLQKHWGHPVLYNDVALDKVKKHAQSTK
ILKPKVMFETFCVFKFIVAKNHYHSQGSWYKTTHDLHLTPYLRQHIVSNSFPSQAEIYQHLWEWYFVEHEPLFSTKIISD
LSIFIKDRLTAVNQECWDSVFDRSVLGYNPPVRFQSKRVPEQFLGQADFSLNQILEFAEKLEYLAPSYRNFSFSLKEKEL
NIGRTFGKLPYRVRNVQTLAEALLADGLAKAFPSNMMVVTEREQKEALLHQASWHHNSASIGENAIVRGASFVTDLEKYN
LAFRYEFTRHFIDYCNRCYGVKNLFDWMHFLIPLCYMHVSDFYSPPHCVTEDNRNNPPDCANAYHYHLGGIEGLQQKLWT
CISCAQITLVELKTKLKLKSSVMGDNQCITTLSLFPIDAPNDYQENEAELNAARVAVELAITTGYSGIFLKPEETFVHSG
FIYFGKKQYLNGVQLPQSLKTMARCGPLSDSIFDDLQGSLASIGTSFERGTSETRHIFPSRWIASFHSMLAINLLNQNHL
GFPLGFNIDISCFKKPLTFSEKLIALITPQVLGGLSFLNPEKLFYRNISDPLTSGLFQLKNALEFLEKEELFYILISKKP
GLADASDFVMNPLGLNVPRSKEIITFLRQTVRENITITSQNRIINSLFHIGSDLEDQRVCEWLLSSNPVMSRFAADIFSR
TPSGKRLQVLGYLEGTRTLLASRTISLTTEGTMLMKLRELTRNRWKSWFSYIDALDDDLSESLEKFTCTVDVANFLRAYS
WSDVLKGKRLIGATLPCLLEQFEVKWINLSEDLREQFNLSSDSKSTINLLPYDCKELRLEGSNDTELNYVSCALDRKVVQ
KHPSVNRLAWTIGNRAPYIGSRTEDKIGYPPLRVNCPSAALKEAIEMVSRLLWVTQGTADREKLLIPLLNSRVNLDYQTV
LNFLPTHYSGNIVHRYNDQYGQHSFMANRMSNTSTRAIISTNTLGKYAGGGQAAIDSNIIFQNTINLGVAVLDIALSLAK
LSSASNVTFRLMLNKCCTRHVPSEYLYFDKPLDVDLNKYMDNELVYDNDPLCSGIKGRLGRVSRS
;
1  
2 UNP MALE_ECOLI P0AEX9 ? 1 
;EEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD
KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIA
ADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNY
GVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATME
NAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQT
;
29 
3 UNP MALE_ECOLI P0AEX9 ? 2 
;EEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD
KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIA
ADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNY
GVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATME
NAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQT
;
29 
4 UNP VP35_MABVM P35259 ? 2 
;STDDIIWDQLIVKRTLADLLIPINRQISDIQSTLSEVTTRVHEIERQLHEITPVLKMGRTLEAISKGMSEMLAKYDHLVI
STGRTTAPAAAFDAYLNEHGVPPPQPAIFKDLGVAQQACSKGTMVKNATTDAADKMSKVLELSEETFSKPNLSAKDLALL
LFTHLPGNNTPFHILAQVLSKIAYKSGKSGAFLDAFHQILSEGENAQAALTRLSRTFDAFLGVVPPVIRVKNFQTVPRPS
QKSLRAVPPNPTIDKGWVCVYSSEQGETRALKI
;
57 
# 
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 9IP4 A 1    ? 1425 ? P31352 1  ? 1425 ? 1    1425 
2  2 9IP4 A 1479 ? 1842 ? P0AEX9 29 ? 392  ? 1479 1842 
3  3 9IP4 B 15   ? 378  ? P0AEX9 29 ? 392  ? -327 36   
4  4 9IP4 B 399  ? 671  ? P35259 57 ? 329  ? 57   329  
5  3 9IP4 C 15   ? 378  ? P0AEX9 29 ? 392  ? -327 36   
6  4 9IP4 C 399  ? 671  ? P35259 57 ? 329  ? 57   329  
7  3 9IP4 D 15   ? 378  ? P0AEX9 29 ? 392  ? -327 36   
8  4 9IP4 D 399  ? 671  ? P35259 57 ? 329  ? 57   329  
9  3 9IP4 E 15   ? 378  ? P0AEX9 29 ? 392  ? -327 36   
10 4 9IP4 E 399  ? 671  ? P35259 57 ? 329  ? 57   329  
# 
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  9IP4 ALA A 489  ? UNP P31352 LEU 489 conflict                489  1   
1  9IP4 GLY A 979  ? UNP P31352 ARG 979 conflict                979  2   
1  9IP4 SER A 1426 ? UNP P31352 ?   ?   linker                  1426 3   
1  9IP4 ARG A 1427 ? UNP P31352 ?   ?   linker                  1427 4   
1  9IP4 GLU A 1428 ? UNP P31352 ?   ?   linker                  1428 5   
1  9IP4 ASN A 1429 ? UNP P31352 ?   ?   linker                  1429 6   
1  9IP4 LEU A 1430 ? UNP P31352 ?   ?   linker                  1430 7   
1  9IP4 TYR A 1431 ? UNP P31352 ?   ?   linker                  1431 8   
1  9IP4 PHE A 1432 ? UNP P31352 ?   ?   linker                  1432 9   
1  9IP4 GLN A 1433 ? UNP P31352 ?   ?   linker                  1433 10  
1  9IP4 GLY A 1434 ? UNP P31352 ?   ?   linker                  1434 11  
1  9IP4 SER A 1435 ? UNP P31352 ?   ?   linker                  1435 12  
1  9IP4 GLY A 1436 ? UNP P31352 ?   ?   linker                  1436 13  
1  9IP4 TRP A 1437 ? UNP P31352 ?   ?   linker                  1437 14  
1  9IP4 SER A 1438 ? UNP P31352 ?   ?   linker                  1438 15  
1  9IP4 HIS A 1439 ? UNP P31352 ?   ?   linker                  1439 16  
1  9IP4 PRO A 1440 ? UNP P31352 ?   ?   linker                  1440 17  
1  9IP4 GLN A 1441 ? UNP P31352 ?   ?   linker                  1441 18  
1  9IP4 PHE A 1442 ? UNP P31352 ?   ?   linker                  1442 19  
1  9IP4 GLU A 1443 ? UNP P31352 ?   ?   linker                  1443 20  
1  9IP4 LYS A 1444 ? UNP P31352 ?   ?   linker                  1444 21  
1  9IP4 GLY A 1445 ? UNP P31352 ?   ?   linker                  1445 22  
1  9IP4 GLY A 1446 ? UNP P31352 ?   ?   linker                  1446 23  
1  9IP4 GLY A 1447 ? UNP P31352 ?   ?   linker                  1447 24  
1  9IP4 SER A 1448 ? UNP P31352 ?   ?   linker                  1448 25  
1  9IP4 GLY A 1449 ? UNP P31352 ?   ?   linker                  1449 26  
1  9IP4 GLY A 1450 ? UNP P31352 ?   ?   linker                  1450 27  
1  9IP4 GLY A 1451 ? UNP P31352 ?   ?   linker                  1451 28  
1  9IP4 SER A 1452 ? UNP P31352 ?   ?   linker                  1452 29  
1  9IP4 GLY A 1453 ? UNP P31352 ?   ?   linker                  1453 30  
1  9IP4 GLY A 1454 ? UNP P31352 ?   ?   linker                  1454 31  
1  9IP4 SER A 1455 ? UNP P31352 ?   ?   linker                  1455 32  
1  9IP4 ALA A 1456 ? UNP P31352 ?   ?   linker                  1456 33  
1  9IP4 TRP A 1457 ? UNP P31352 ?   ?   linker                  1457 34  
1  9IP4 SER A 1458 ? UNP P31352 ?   ?   linker                  1458 35  
1  9IP4 HIS A 1459 ? UNP P31352 ?   ?   linker                  1459 36  
1  9IP4 PRO A 1460 ? UNP P31352 ?   ?   linker                  1460 37  
1  9IP4 GLN A 1461 ? UNP P31352 ?   ?   linker                  1461 38  
1  9IP4 PHE A 1462 ? UNP P31352 ?   ?   linker                  1462 39  
1  9IP4 GLU A 1463 ? UNP P31352 ?   ?   linker                  1463 40  
1  9IP4 LYS A 1464 ? UNP P31352 ?   ?   linker                  1464 41  
1  9IP4 GLY A 1465 ? UNP P31352 ?   ?   linker                  1465 42  
1  9IP4 SER A 1466 ? UNP P31352 ?   ?   linker                  1466 43  
1  9IP4 ALA A 1467 ? UNP P31352 ?   ?   linker                  1467 44  
1  9IP4 SER A 1468 ? UNP P31352 ?   ?   linker                  1468 45  
1  9IP4 HIS A 1469 ? UNP P31352 ?   ?   linker                  1469 46  
1  9IP4 HIS A 1470 ? UNP P31352 ?   ?   linker                  1470 47  
1  9IP4 HIS A 1471 ? UNP P31352 ?   ?   linker                  1471 48  
1  9IP4 HIS A 1472 ? UNP P31352 ?   ?   linker                  1472 49  
1  9IP4 HIS A 1473 ? UNP P31352 ?   ?   linker                  1473 50  
1  9IP4 HIS A 1474 ? UNP P31352 ?   ?   linker                  1474 51  
1  9IP4 GLY A 1475 ? UNP P31352 ?   ?   linker                  1475 52  
1  9IP4 THR A 1476 ? UNP P31352 ?   ?   linker                  1476 53  
1  9IP4 LYS A 1477 ? UNP P31352 ?   ?   linker                  1477 54  
1  9IP4 THR A 1478 ? UNP P31352 ?   ?   linker                  1478 55  
2  9IP4 GLY A 1843 ? UNP P0AEX9 ?   ?   'expression tag'        1843 56  
2  9IP4 ASP A 1844 ? UNP P0AEX9 ?   ?   'expression tag'        1844 57  
2  9IP4 TYR A 1845 ? UNP P0AEX9 ?   ?   'expression tag'        1845 58  
2  9IP4 LYS A 1846 ? UNP P0AEX9 ?   ?   'expression tag'        1846 59  
2  9IP4 ASP A 1847 ? UNP P0AEX9 ?   ?   'expression tag'        1847 60  
2  9IP4 ASP A 1848 ? UNP P0AEX9 ?   ?   'expression tag'        1848 61  
2  9IP4 ASP A 1849 ? UNP P0AEX9 ?   ?   'expression tag'        1849 62  
2  9IP4 ASP A 1850 ? UNP P0AEX9 ?   ?   'expression tag'        1850 63  
2  9IP4 LYS A 1851 ? UNP P0AEX9 ?   ?   'expression tag'        1851 64  
3  9IP4 MET B 1    ? UNP P0AEX9 ?   ?   'initiating methionine' -341 65  
3  9IP4 GLY B 2    ? UNP P0AEX9 ?   ?   'expression tag'        -340 66  
3  9IP4 SER B 3    ? UNP P0AEX9 ?   ?   'expression tag'        -339 67  
3  9IP4 SER B 4    ? UNP P0AEX9 ?   ?   'expression tag'        -338 68  
3  9IP4 HIS B 5    ? UNP P0AEX9 ?   ?   'expression tag'        -337 69  
3  9IP4 HIS B 6    ? UNP P0AEX9 ?   ?   'expression tag'        -336 70  
3  9IP4 HIS B 7    ? UNP P0AEX9 ?   ?   'expression tag'        -335 71  
3  9IP4 HIS B 8    ? UNP P0AEX9 ?   ?   'expression tag'        -334 72  
3  9IP4 HIS B 9    ? UNP P0AEX9 ?   ?   'expression tag'        -333 73  
3  9IP4 HIS B 10   ? UNP P0AEX9 ?   ?   'expression tag'        -332 74  
3  9IP4 GLY B 11   ? UNP P0AEX9 ?   ?   'expression tag'        -331 75  
3  9IP4 THR B 12   ? UNP P0AEX9 ?   ?   'expression tag'        -330 76  
3  9IP4 LYS B 13   ? UNP P0AEX9 ?   ?   'expression tag'        -329 77  
3  9IP4 THR B 14   ? UNP P0AEX9 ?   ?   'expression tag'        -328 78  
3  9IP4 GLY B 379  ? UNP P0AEX9 ?   ?   linker                  37   79  
3  9IP4 THR B 380  ? UNP P0AEX9 ?   ?   linker                  38   80  
3  9IP4 ASP B 381  ? UNP P0AEX9 ?   ?   linker                  39   81  
3  9IP4 TYR B 382  ? UNP P0AEX9 ?   ?   linker                  40   82  
3  9IP4 ASP B 383  ? UNP P0AEX9 ?   ?   linker                  41   83  
3  9IP4 ILE B 384  ? UNP P0AEX9 ?   ?   linker                  42   84  
3  9IP4 PRO B 385  ? UNP P0AEX9 ?   ?   linker                  43   85  
3  9IP4 THR B 386  ? UNP P0AEX9 ?   ?   linker                  44   86  
3  9IP4 THR B 387  ? UNP P0AEX9 ?   ?   linker                  45   87  
3  9IP4 LEU B 388  ? UNP P0AEX9 ?   ?   linker                  46   88  
3  9IP4 GLU B 389  ? UNP P0AEX9 ?   ?   linker                  47   89  
3  9IP4 VAL B 390  ? UNP P0AEX9 ?   ?   linker                  48   90  
3  9IP4 LEU B 391  ? UNP P0AEX9 ?   ?   linker                  49   91  
3  9IP4 PHE B 392  ? UNP P0AEX9 ?   ?   linker                  50   92  
3  9IP4 GLN B 393  ? UNP P0AEX9 ?   ?   linker                  51   93  
3  9IP4 GLY B 394  ? UNP P0AEX9 ?   ?   linker                  52   94  
3  9IP4 PRO B 395  ? UNP P0AEX9 ?   ?   linker                  53   95  
3  9IP4 LEU B 396  ? UNP P0AEX9 ?   ?   linker                  54   96  
3  9IP4 GLY B 397  ? UNP P0AEX9 ?   ?   linker                  55   97  
3  9IP4 SER B 398  ? UNP P0AEX9 ?   ?   linker                  56   98  
4  9IP4 CYS B 638  ? UNP P35259 SER 296 conflict                296  99  
5  9IP4 MET C 1    ? UNP P0AEX9 ?   ?   'initiating methionine' -341 100 
5  9IP4 GLY C 2    ? UNP P0AEX9 ?   ?   'expression tag'        -340 101 
5  9IP4 SER C 3    ? UNP P0AEX9 ?   ?   'expression tag'        -339 102 
5  9IP4 SER C 4    ? UNP P0AEX9 ?   ?   'expression tag'        -338 103 
5  9IP4 HIS C 5    ? UNP P0AEX9 ?   ?   'expression tag'        -337 104 
5  9IP4 HIS C 6    ? UNP P0AEX9 ?   ?   'expression tag'        -336 105 
5  9IP4 HIS C 7    ? UNP P0AEX9 ?   ?   'expression tag'        -335 106 
5  9IP4 HIS C 8    ? UNP P0AEX9 ?   ?   'expression tag'        -334 107 
5  9IP4 HIS C 9    ? UNP P0AEX9 ?   ?   'expression tag'        -333 108 
5  9IP4 HIS C 10   ? UNP P0AEX9 ?   ?   'expression tag'        -332 109 
5  9IP4 GLY C 11   ? UNP P0AEX9 ?   ?   'expression tag'        -331 110 
5  9IP4 THR C 12   ? UNP P0AEX9 ?   ?   'expression tag'        -330 111 
5  9IP4 LYS C 13   ? UNP P0AEX9 ?   ?   'expression tag'        -329 112 
5  9IP4 THR C 14   ? UNP P0AEX9 ?   ?   'expression tag'        -328 113 
5  9IP4 GLY C 379  ? UNP P0AEX9 ?   ?   linker                  37   114 
5  9IP4 THR C 380  ? UNP P0AEX9 ?   ?   linker                  38   115 
5  9IP4 ASP C 381  ? UNP P0AEX9 ?   ?   linker                  39   116 
5  9IP4 TYR C 382  ? UNP P0AEX9 ?   ?   linker                  40   117 
5  9IP4 ASP C 383  ? UNP P0AEX9 ?   ?   linker                  41   118 
5  9IP4 ILE C 384  ? UNP P0AEX9 ?   ?   linker                  42   119 
5  9IP4 PRO C 385  ? UNP P0AEX9 ?   ?   linker                  43   120 
5  9IP4 THR C 386  ? UNP P0AEX9 ?   ?   linker                  44   121 
5  9IP4 THR C 387  ? UNP P0AEX9 ?   ?   linker                  45   122 
5  9IP4 LEU C 388  ? UNP P0AEX9 ?   ?   linker                  46   123 
5  9IP4 GLU C 389  ? UNP P0AEX9 ?   ?   linker                  47   124 
5  9IP4 VAL C 390  ? UNP P0AEX9 ?   ?   linker                  48   125 
5  9IP4 LEU C 391  ? UNP P0AEX9 ?   ?   linker                  49   126 
5  9IP4 PHE C 392  ? UNP P0AEX9 ?   ?   linker                  50   127 
5  9IP4 GLN C 393  ? UNP P0AEX9 ?   ?   linker                  51   128 
5  9IP4 GLY C 394  ? UNP P0AEX9 ?   ?   linker                  52   129 
5  9IP4 PRO C 395  ? UNP P0AEX9 ?   ?   linker                  53   130 
5  9IP4 LEU C 396  ? UNP P0AEX9 ?   ?   linker                  54   131 
5  9IP4 GLY C 397  ? UNP P0AEX9 ?   ?   linker                  55   132 
5  9IP4 SER C 398  ? UNP P0AEX9 ?   ?   linker                  56   133 
6  9IP4 CYS C 638  ? UNP P35259 SER 296 conflict                296  134 
7  9IP4 MET D 1    ? UNP P0AEX9 ?   ?   'initiating methionine' -341 135 
7  9IP4 GLY D 2    ? UNP P0AEX9 ?   ?   'expression tag'        -340 136 
7  9IP4 SER D 3    ? UNP P0AEX9 ?   ?   'expression tag'        -339 137 
7  9IP4 SER D 4    ? UNP P0AEX9 ?   ?   'expression tag'        -338 138 
7  9IP4 HIS D 5    ? UNP P0AEX9 ?   ?   'expression tag'        -337 139 
7  9IP4 HIS D 6    ? UNP P0AEX9 ?   ?   'expression tag'        -336 140 
7  9IP4 HIS D 7    ? UNP P0AEX9 ?   ?   'expression tag'        -335 141 
7  9IP4 HIS D 8    ? UNP P0AEX9 ?   ?   'expression tag'        -334 142 
7  9IP4 HIS D 9    ? UNP P0AEX9 ?   ?   'expression tag'        -333 143 
7  9IP4 HIS D 10   ? UNP P0AEX9 ?   ?   'expression tag'        -332 144 
7  9IP4 GLY D 11   ? UNP P0AEX9 ?   ?   'expression tag'        -331 145 
7  9IP4 THR D 12   ? UNP P0AEX9 ?   ?   'expression tag'        -330 146 
7  9IP4 LYS D 13   ? UNP P0AEX9 ?   ?   'expression tag'        -329 147 
7  9IP4 THR D 14   ? UNP P0AEX9 ?   ?   'expression tag'        -328 148 
7  9IP4 GLY D 379  ? UNP P0AEX9 ?   ?   linker                  37   149 
7  9IP4 THR D 380  ? UNP P0AEX9 ?   ?   linker                  38   150 
7  9IP4 ASP D 381  ? UNP P0AEX9 ?   ?   linker                  39   151 
7  9IP4 TYR D 382  ? UNP P0AEX9 ?   ?   linker                  40   152 
7  9IP4 ASP D 383  ? UNP P0AEX9 ?   ?   linker                  41   153 
7  9IP4 ILE D 384  ? UNP P0AEX9 ?   ?   linker                  42   154 
7  9IP4 PRO D 385  ? UNP P0AEX9 ?   ?   linker                  43   155 
7  9IP4 THR D 386  ? UNP P0AEX9 ?   ?   linker                  44   156 
7  9IP4 THR D 387  ? UNP P0AEX9 ?   ?   linker                  45   157 
7  9IP4 LEU D 388  ? UNP P0AEX9 ?   ?   linker                  46   158 
7  9IP4 GLU D 389  ? UNP P0AEX9 ?   ?   linker                  47   159 
7  9IP4 VAL D 390  ? UNP P0AEX9 ?   ?   linker                  48   160 
7  9IP4 LEU D 391  ? UNP P0AEX9 ?   ?   linker                  49   161 
7  9IP4 PHE D 392  ? UNP P0AEX9 ?   ?   linker                  50   162 
7  9IP4 GLN D 393  ? UNP P0AEX9 ?   ?   linker                  51   163 
7  9IP4 GLY D 394  ? UNP P0AEX9 ?   ?   linker                  52   164 
7  9IP4 PRO D 395  ? UNP P0AEX9 ?   ?   linker                  53   165 
7  9IP4 LEU D 396  ? UNP P0AEX9 ?   ?   linker                  54   166 
7  9IP4 GLY D 397  ? UNP P0AEX9 ?   ?   linker                  55   167 
7  9IP4 SER D 398  ? UNP P0AEX9 ?   ?   linker                  56   168 
8  9IP4 CYS D 638  ? UNP P35259 SER 296 conflict                296  169 
9  9IP4 MET E 1    ? UNP P0AEX9 ?   ?   'initiating methionine' -341 170 
9  9IP4 GLY E 2    ? UNP P0AEX9 ?   ?   'expression tag'        -340 171 
9  9IP4 SER E 3    ? UNP P0AEX9 ?   ?   'expression tag'        -339 172 
9  9IP4 SER E 4    ? UNP P0AEX9 ?   ?   'expression tag'        -338 173 
9  9IP4 HIS E 5    ? UNP P0AEX9 ?   ?   'expression tag'        -337 174 
9  9IP4 HIS E 6    ? UNP P0AEX9 ?   ?   'expression tag'        -336 175 
9  9IP4 HIS E 7    ? UNP P0AEX9 ?   ?   'expression tag'        -335 176 
9  9IP4 HIS E 8    ? UNP P0AEX9 ?   ?   'expression tag'        -334 177 
9  9IP4 HIS E 9    ? UNP P0AEX9 ?   ?   'expression tag'        -333 178 
9  9IP4 HIS E 10   ? UNP P0AEX9 ?   ?   'expression tag'        -332 179 
9  9IP4 GLY E 11   ? UNP P0AEX9 ?   ?   'expression tag'        -331 180 
9  9IP4 THR E 12   ? UNP P0AEX9 ?   ?   'expression tag'        -330 181 
9  9IP4 LYS E 13   ? UNP P0AEX9 ?   ?   'expression tag'        -329 182 
9  9IP4 THR E 14   ? UNP P0AEX9 ?   ?   'expression tag'        -328 183 
9  9IP4 GLY E 379  ? UNP P0AEX9 ?   ?   linker                  37   184 
9  9IP4 THR E 380  ? UNP P0AEX9 ?   ?   linker                  38   185 
9  9IP4 ASP E 381  ? UNP P0AEX9 ?   ?   linker                  39   186 
9  9IP4 TYR E 382  ? UNP P0AEX9 ?   ?   linker                  40   187 
9  9IP4 ASP E 383  ? UNP P0AEX9 ?   ?   linker                  41   188 
9  9IP4 ILE E 384  ? UNP P0AEX9 ?   ?   linker                  42   189 
9  9IP4 PRO E 385  ? UNP P0AEX9 ?   ?   linker                  43   190 
9  9IP4 THR E 386  ? UNP P0AEX9 ?   ?   linker                  44   191 
9  9IP4 THR E 387  ? UNP P0AEX9 ?   ?   linker                  45   192 
9  9IP4 LEU E 388  ? UNP P0AEX9 ?   ?   linker                  46   193 
9  9IP4 GLU E 389  ? UNP P0AEX9 ?   ?   linker                  47   194 
9  9IP4 VAL E 390  ? UNP P0AEX9 ?   ?   linker                  48   195 
9  9IP4 LEU E 391  ? UNP P0AEX9 ?   ?   linker                  49   196 
9  9IP4 PHE E 392  ? UNP P0AEX9 ?   ?   linker                  50   197 
9  9IP4 GLN E 393  ? UNP P0AEX9 ?   ?   linker                  51   198 
9  9IP4 GLY E 394  ? UNP P0AEX9 ?   ?   linker                  52   199 
9  9IP4 PRO E 395  ? UNP P0AEX9 ?   ?   linker                  53   200 
9  9IP4 LEU E 396  ? UNP P0AEX9 ?   ?   linker                  54   201 
9  9IP4 GLY E 397  ? UNP P0AEX9 ?   ?   linker                  55   202 
9  9IP4 SER E 398  ? UNP P0AEX9 ?   ?   linker                  56   203 
10 9IP4 CYS E 638  ? UNP P35259 SER 296 conflict                296  204 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   pentameric 
_pdbx_struct_assembly.oligomeric_count     5 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LEU A 18   ? LEU A 28   ? LEU A 18   LEU A 28   1 ? 11 
HELX_P HELX_P2  AA2 PRO A 38   ? CYS A 43   ? PRO A 38   CYS A 43   1 ? 6  
HELX_P HELX_P3  AA3 PRO A 46   ? ARG A 51   ? PRO A 46   ARG A 51   1 ? 6  
HELX_P HELX_P4  AA4 LEU A 52   ? ASN A 54   ? LEU A 52   ASN A 54   5 ? 3  
HELX_P HELX_P5  AA5 SER A 55   ? LEU A 62   ? SER A 55   LEU A 62   1 ? 8  
HELX_P HELX_P6  AA6 PHE A 72   ? ALA A 87   ? PHE A 72   ALA A 87   1 ? 16 
HELX_P HELX_P7  AA7 ILE A 88   ? LYS A 95   ? ILE A 88   LYS A 95   5 ? 8  
HELX_P HELX_P8  AA8 LEU A 98   ? GLY A 122  ? LEU A 98   GLY A 122  1 ? 25 
HELX_P HELX_P9  AA9 ASP A 137  ? ASN A 143  ? ASP A 137  ASN A 143  1 ? 7  
HELX_P HELX_P10 AB1 TYR A 145  ? GLN A 165  ? TYR A 145  GLN A 165  1 ? 21 
HELX_P HELX_P11 AB2 VAL A 195  ? ARG A 200  ? VAL A 195  ARG A 200  1 ? 6  
HELX_P HELX_P12 AB3 SER A 204  ? LYS A 209  ? SER A 204  LYS A 209  1 ? 6  
HELX_P HELX_P13 AB4 PRO A 210  ? TRP A 215  ? PRO A 210  TRP A 215  5 ? 6  
HELX_P HELX_P14 AB5 LEU A 221  ? LEU A 225  ? LEU A 221  LEU A 225  5 ? 5  
HELX_P HELX_P15 AB6 TYR A 237  ? ASP A 264  ? TYR A 237  ASP A 264  1 ? 28 
HELX_P HELX_P16 AB7 PRO A 272  ? LEU A 291  ? PRO A 272  LEU A 291  1 ? 20 
HELX_P HELX_P17 AB8 ASP A 293  ? LYS A 299  ? ASP A 293  LYS A 299  1 ? 7  
HELX_P HELX_P18 AB9 HIS A 300  ? GLN A 310  ? HIS A 300  GLN A 310  1 ? 11 
HELX_P HELX_P19 AC1 THR A 316  ? LYS A 319  ? THR A 316  LYS A 319  5 ? 4  
HELX_P HELX_P20 AC2 TYR A 320  ? LEU A 341  ? TYR A 320  LEU A 341  1 ? 22 
HELX_P HELX_P21 AC3 ALA A 348  ? ALA A 361  ? ALA A 348  ALA A 361  1 ? 14 
HELX_P HELX_P22 AC4 THR A 364  ? PHE A 372  ? THR A 364  PHE A 372  1 ? 9  
HELX_P HELX_P23 AC5 TYR A 384  ? SER A 398  ? TYR A 384  SER A 398  1 ? 15 
HELX_P HELX_P24 AC6 LYS A 403  ? GLY A 427  ? LYS A 403  GLY A 427  1 ? 25 
HELX_P HELX_P25 AC7 ASP A 435  ? LEU A 438  ? ASP A 435  LEU A 438  5 ? 4  
HELX_P HELX_P26 AC8 THR A 439  ? SER A 448  ? THR A 439  SER A 448  1 ? 10 
HELX_P HELX_P27 AC9 HIS A 460  ? PHE A 466  ? HIS A 460  PHE A 466  5 ? 7  
HELX_P HELX_P28 AD1 ASN A 493  ? PHE A 501  ? ASN A 493  PHE A 501  5 ? 9  
HELX_P HELX_P29 AD2 ASP A 502  ? GLY A 507  ? ASP A 502  GLY A 507  1 ? 6  
HELX_P HELX_P30 AD3 ARG A 518  ? LEU A 524  ? ARG A 518  LEU A 524  1 ? 7  
HELX_P HELX_P31 AD4 SER A 530  ? LYS A 540  ? SER A 530  LYS A 540  1 ? 11 
HELX_P HELX_P32 AD5 LEU A 541  ? ARG A 549  ? LEU A 541  ARG A 549  5 ? 9  
HELX_P HELX_P33 AD6 PRO A 570  ? GLY A 587  ? PRO A 570  GLY A 587  1 ? 18 
HELX_P HELX_P34 AD7 LEU A 588  ? PHE A 592  ? LEU A 588  PHE A 592  5 ? 5  
HELX_P HELX_P35 AD8 VAL A 599  ? GLU A 603  ? VAL A 599  GLU A 603  5 ? 5  
HELX_P HELX_P36 AD9 GLN A 604  ? ALA A 612  ? GLN A 604  ALA A 612  1 ? 9  
HELX_P HELX_P37 AE1 GLU A 637  ? PHE A 643  ? GLU A 637  PHE A 643  5 ? 7  
HELX_P HELX_P38 AE2 ARG A 644  ? GLY A 660  ? ARG A 644  GLY A 660  1 ? 17 
HELX_P HELX_P39 AE3 ASP A 666  ? ILE A 672  ? ASP A 666  ILE A 672  1 ? 7  
HELX_P HELX_P40 AE4 GLU A 691  ? ASN A 695  ? GLU A 691  ASN A 695  5 ? 5  
HELX_P HELX_P41 AE5 GLN A 715  ? LYS A 735  ? GLN A 715  LYS A 735  1 ? 21 
HELX_P HELX_P42 AE6 PRO A 760  ? TYR A 785  ? PRO A 760  TYR A 785  1 ? 26 
HELX_P HELX_P43 AE7 LYS A 791  ? THR A 795  ? LYS A 791  THR A 795  5 ? 5  
HELX_P HELX_P44 AE8 GLN A 817  ? ALA A 823  ? GLN A 817  ALA A 823  1 ? 7  
HELX_P HELX_P45 AE9 ASP A 835  ? GLU A 853  ? ASP A 835  GLU A 853  1 ? 19 
HELX_P HELX_P46 AF1 ILE A 857  ? ASN A 878  ? ILE A 857  ASN A 878  1 ? 22 
HELX_P HELX_P47 AF2 ASN A 887  ? LYS A 894  ? ASN A 887  LYS A 894  1 ? 8  
HELX_P HELX_P48 AF3 THR A 898  ? THR A 908  ? THR A 898  THR A 908  1 ? 11 
HELX_P HELX_P49 AF4 PRO A 909  ? GLY A 913  ? PRO A 909  GLY A 913  5 ? 5  
HELX_P HELX_P50 AF5 ASN A 919  ? PHE A 924  ? ASN A 919  PHE A 924  5 ? 6  
HELX_P HELX_P51 AF6 ASP A 930  ? GLU A 947  ? ASP A 930  GLU A 947  1 ? 18 
HELX_P HELX_P52 AF7 LYS A 948  ? GLU A 950  ? LYS A 948  GLU A 950  5 ? 3  
HELX_P HELX_P53 AF8 LEU A 951  ? SER A 957  ? LEU A 951  SER A 957  1 ? 7  
HELX_P HELX_P54 AF9 ASP A 964  ? ASN A 971  ? ASP A 964  ASN A 971  1 ? 8  
HELX_P HELX_P55 AG1 VAL A 977  ? LYS A 981  ? VAL A 977  LYS A 981  5 ? 5  
HELX_P HELX_P56 AG2 ILE A 983  ? SER A 999  ? ILE A 983  SER A 999  1 ? 17 
HELX_P HELX_P57 AG3 ASN A 1001 ? PHE A 1008 ? ASN A 1001 PHE A 1008 1 ? 8  
HELX_P HELX_P58 AG4 GLY A 1011 ? LEU A 1024 ? GLY A 1011 LEU A 1024 1 ? 14 
HELX_P HELX_P59 AG5 SER A 1031 ? SER A 1039 ? SER A 1031 SER A 1039 1 ? 9  
HELX_P HELX_P60 AG6 THR A 1041 ? GLY A 1055 ? THR A 1041 GLY A 1055 1 ? 15 
HELX_P HELX_P61 AG7 THR A 1072 ? SER A 1090 ? THR A 1072 SER A 1090 1 ? 19 
HELX_P HELX_P62 AG8 ASP A 1096 ? GLU A 1104 ? ASP A 1096 GLU A 1104 1 ? 9  
HELX_P HELX_P63 AG9 CYS A 1108 ? TRP A 1121 ? CYS A 1108 TRP A 1121 1 ? 14 
HELX_P HELX_P64 AH1 TRP A 1121 ? LYS A 1126 ? TRP A 1121 LYS A 1126 1 ? 6  
HELX_P HELX_P65 AH2 CYS A 1137 ? GLN A 1141 ? CYS A 1137 GLN A 1141 1 ? 5  
HELX_P HELX_P66 AH3 SER A 1150 ? PHE A 1157 ? SER A 1150 PHE A 1157 1 ? 8  
HELX_P HELX_P67 AH4 ARG A 1207 ? ALA A 1209 ? ARG A 1207 ALA A 1209 5 ? 3  
HELX_P HELX_P68 AH5 ALA A 1216 ? SER A 1221 ? ALA A 1216 SER A 1221 1 ? 6  
HELX_P HELX_P69 AH6 SER A 1238 ? THR A 1255 ? SER A 1238 THR A 1255 1 ? 18 
HELX_P HELX_P70 AH7 ASP A 1260 ? ASN A 1270 ? ASP A 1260 ASN A 1270 1 ? 11 
HELX_P HELX_P71 AH8 ASP A 1276 ? LEU A 1281 ? ASP A 1276 LEU A 1281 1 ? 6  
HELX_P HELX_P72 AH9 ASN A 1282 ? LEU A 1284 ? ASN A 1282 LEU A 1284 5 ? 3  
HELX_P HELX_P73 AI1 ASN A 1291 ? GLY A 1301 ? ASN A 1291 GLY A 1301 1 ? 11 
HELX_P HELX_P74 AI2 ASN A 1312 ? THR A 1315 ? ASN A 1312 THR A 1315 5 ? 4  
HELX_P HELX_P75 AI3 LEU A 1324 ? ALA A 1328 ? LEU A 1324 ALA A 1328 5 ? 5  
HELX_P HELX_P76 AI4 ILE A 1340 ? LEU A 1356 ? ILE A 1340 LEU A 1356 1 ? 17 
HELX_P HELX_P77 AI5 GLY B 456  ? THR B 480  ? GLY B 114  THR B 138  1 ? 25 
HELX_P HELX_P78 AI6 PRO B 486  ? GLY B 498  ? PRO B 144  GLY B 156  1 ? 13 
HELX_P HELX_P79 AI7 ASP B 509  ? GLN B 515  ? ASP B 167  GLN B 173  1 ? 7  
HELX_P HELX_P80 AI8 ASN B 525  ? GLU B 539  ? ASN B 183  GLU B 197  1 ? 15 
HELX_P HELX_P81 AI9 SER B 551  ? HIS B 562  ? SER B 209  HIS B 220  1 ? 12 
HELX_P HELX_P82 AJ1 THR B 568  ? SER B 584  ? THR B 226  SER B 242  1 ? 17 
HELX_P HELX_P83 AJ2 LYS B 586  ? GLU B 600  ? LYS B 244  GLU B 258  1 ? 15 
HELX_P HELX_P84 AJ3 ASN B 603  ? PHE B 615  ? ASN B 261  PHE B 273  1 ? 13 
HELX_P HELX_P85 AJ4 ASP B 616  ? LEU B 619  ? ASP B 274  LEU B 277  5 ? 4  
HELX_P HELX_P86 AJ5 PRO B 635  ? LYS B 640  ? PRO B 293  LYS B 298  5 ? 6  
HELX_P HELX_P87 AJ6 THR B 650  ? LYS B 653  ? THR B 308  LYS B 311  5 ? 4  
HELX_P HELX_P88 AJ7 LEU C 453  ? ASP C 474  ? LEU C 111  ASP C 132  1 ? 22 
HELX_P HELX_P89 AJ8 THR C 483  ? GLY C 498  ? THR C 141  GLY C 156  1 ? 16 
HELX_P HELX_P90 AJ9 PRO C 504  ? LEU C 510  ? PRO C 162  LEU C 168  1 ? 7  
HELX_P HELX_P91 AK1 THR D 450  ? VAL D 477  ? THR D 108  VAL D 135  1 ? 28 
HELX_P HELX_P92 AK2 LEU E 453  ? VAL E 477  ? LEU E 111  VAL E 135  1 ? 25 
# 
_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 
metalc1 metalc ? ? A CYS 1108 SG ? ? ? 1_555 F ZN . ZN ? ? A CYS 1108 A ZN 2001 1_555 ? ? ? ? ? ? ? 2.310 ? ? 
metalc2 metalc ? ? A CYS 1376 SG ? ? ? 1_555 F ZN . ZN ? ? A CYS 1376 A ZN 2001 1_555 ? ? ? ? ? ? ? 2.306 ? ? 
metalc3 metalc ? ? A CYS 1377 SG ? ? ? 1_555 F ZN . ZN ? ? A CYS 1377 A ZN 2001 1_555 ? ? ? ? ? ? ? 2.303 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 1108 ? A CYS 1108 ? 1_555 ZN ? F ZN . ? A ZN 2001 ? 1_555 SG ? A CYS 1376 ? A CYS 1376 ? 1_555 119.2 ? 
2 SG ? A CYS 1108 ? A CYS 1108 ? 1_555 ZN ? F ZN . ? A ZN 2001 ? 1_555 SG ? A CYS 1377 ? A CYS 1377 ? 1_555 99.2  ? 
3 SG ? A CYS 1376 ? A CYS 1376 ? 1_555 ZN ? F ZN . ? A ZN 2001 ? 1_555 SG ? A CYS 1377 ? A CYS 1377 ? 1_555 100.7 ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          HIS 
_struct_mon_prot_cis.label_seq_id           1202 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           HIS 
_struct_mon_prot_cis.auth_seq_id            1202 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    1203 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     1203 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       1.70 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 4 ? 
AA8 ? 2 ? 
AA9 ? 4 ? 
# 
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 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? 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 CYS A 65   ? THR A 69   ? CYS A 65   THR A 69   
AA1 2 PHE A 230  ? SER A 236  ? PHE A 230  SER A 236  
AA1 3 PHE A 188  ? PRO A 194  ? PHE A 188  PRO A 194  
AA1 4 GLU A 181  ? GLY A 184  ? GLU A 181  GLY A 184  
AA1 5 TRP A 173  ? PHE A 175  ? TRP A 173  PHE A 175  
AA2 1 ILE A 401  ? LEU A 402  ? ILE A 401  LEU A 402  
AA2 2 VAL C 477  ? SER C 479  ? VAL C 135  SER C 137  
AA2 3 ALA B 505  ? PHE B 507  ? ALA B 163  PHE B 165  
AA3 1 THR A 565  ? LYS A 568  ? THR A 565  LYS A 568  
AA3 2 PHE A 551  ? LEU A 555  ? PHE A 551  LEU A 555  
AA3 3 TYR A 676  ? VAL A 679  ? TYR A 676  VAL A 679  
AA3 4 TYR A 704  ? HIS A 705  ? TYR A 704  HIS A 705  
AA4 1 LYS A 737  ? VAL A 742  ? LYS A 737  VAL A 742  
AA4 2 ASN A 746  ? PRO A 756  ? ASN A 746  PRO A 756  
AA4 3 ALA A 625  ? ASP A 635  ? ALA A 625  ASP A 635  
AA4 4 VAL A 797  ? HIS A 798  ? VAL A 797  HIS A 798  
AA5 1 PHE A 801  ? TYR A 803  ? PHE A 801  TYR A 803  
AA5 2 GLN A 808  ? LEU A 810  ? GLN A 808  LEU A 810  
AA5 3 VAL A 813  ? GLN A 814  ? VAL A 813  GLN A 814  
AA6 1 PRO A 1028 ? MET A 1030 ? PRO A 1028 MET A 1030 
AA6 2 ARG A 1129 ? ILE A 1131 ? ARG A 1129 ILE A 1131 
AA7 1 PHE A 1142 ? LEU A 1149 ? PHE A 1142 LEU A 1149 
AA7 2 VAL A 1367 ? LEU A 1373 ? VAL A 1367 LEU A 1373 
AA7 3 TYR A 1189 ? LEU A 1194 ? TYR A 1189 LEU A 1194 
AA7 4 ALA A 1317 ? SER A 1320 ? ALA A 1317 SER A 1320 
AA8 1 GLN A 1200 ? LYS A 1201 ? GLN A 1200 LYS A 1201 
AA8 2 THR A 1211 ? ILE A 1212 ? THR A 1211 ILE A 1212 
AA9 1 VAL B 625  ? ARG B 627  ? VAL B 283  ARG B 285  
AA9 2 TRP B 655  ? SER B 660  ? TRP B 313  SER B 318  
AA9 3 THR B 666  ? LYS B 670  ? THR B 324  LYS B 328  
AA9 4 LEU B 642  ? ARG B 643  ? LEU B 300  ARG B 301  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N SER A 66   ? N SER A 66   O PHE A 230  ? O PHE A 230  
AA1 2 3 O SER A 233  ? O SER A 233  N PHE A 191  ? N PHE A 191  
AA1 3 4 O ILE A 190  ? O ILE A 190  N PHE A 183  ? N PHE A 183  
AA1 4 5 O GLY A 184  ? O GLY A 184  N TRP A 173  ? N TRP A 173  
AA2 1 2 N LEU A 402  ? N LEU A 402  O ILE C 478  ? O ILE C 136  
AA2 2 3 O VAL C 477  ? O VAL C 135  N PHE B 507  ? N PHE B 165  
AA3 1 2 O PHE A 566  ? O PHE A 566  N SER A 554  ? N SER A 554  
AA3 2 3 N PHE A 553  ? N PHE A 553  O HIS A 678  ? O HIS A 678  
AA3 3 4 N MET A 677  ? N MET A 677  O TYR A 704  ? O TYR A 704  
AA4 1 2 N LYS A 739  ? N LYS A 739  O THR A 750  ? O THR A 750  
AA4 2 3 O THR A 751  ? O THR A 751  N ALA A 630  ? N ALA A 630  
AA4 3 4 N SER A 631  ? N SER A 631  O HIS A 798  ? O HIS A 798  
AA5 1 2 N ILE A 802  ? N ILE A 802  O TYR A 809  ? O TYR A 809  
AA5 2 3 N LEU A 810  ? N LEU A 810  O VAL A 813  ? O VAL A 813  
AA6 1 2 N VAL A 1029 ? N VAL A 1029 O ILE A 1131 ? O ILE A 1131 
AA7 1 2 N GLU A 1143 ? N GLU A 1143 O MET A 1372 ? O MET A 1372 
AA7 2 3 O PHE A 1369 ? O PHE A 1369 N CYS A 1192 ? N CYS A 1192 
AA7 3 4 N ALA A 1193 ? N ALA A 1193 O ILE A 1318 ? O ILE A 1318 
AA8 1 2 N GLN A 1200 ? N GLN A 1200 O ILE A 1212 ? O ILE A 1212 
AA9 1 2 N ILE B 626  ? N ILE B 284  O VAL B 658  ? O VAL B 316  
AA9 2 3 N TYR B 659  ? N TYR B 317  O ARG B 667  ? O ARG B 325  
AA9 3 4 O ALA B 668  ? O ALA B 326  N ARG B 643  ? N ARG B 301  
# 
_pdbx_entry_details.entry_id                   9IP4 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
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 NH1 A ARG 1040 ? ? OE1 A GLU 1246 ? ? 2.07 
2 1 OG1 A THR 490  ? ? O   A LYS 517  ? ? 2.07 
3 1 OG  A SER 1191 ? ? OG  A SER 1320 ? ? 2.16 
4 1 OD2 A ASP 1260 ? ? NZ  A LYS 1263 ? ? 2.17 
5 1 OE2 B GLU 260  ? ? NH1 B ARG 268  ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CD A LYS 296 ? ? CE A LYS 296 ? ? NZ  A LYS 296 ? ? 87.82  111.70 -23.88 2.30 N 
2 1 CG A MET 743 ? ? SD A MET 743 ? ? CE  A MET 743 ? ? 117.97 100.20 17.77  1.60 N 
3 1 CA A GLU 794 ? ? CB A GLU 794 ? ? CG  A GLU 794 ? ? 129.17 113.40 15.77  2.20 N 
4 1 CB A LEU 828 ? ? CG A LEU 828 ? ? CD2 A LEU 828 ? ? 95.53  111.00 -15.47 1.70 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 14   ? ? 179.18  153.66  
2  1 PHE A 94   ? ? -118.82 51.06   
3  1 LEU A 97   ? ? 75.76   -11.24  
4  1 LEU A 98   ? ? 37.99   70.53   
5  1 ALA A 131  ? ? -59.36  -7.03   
6  1 LEU A 169  ? ? 72.09   -5.11   
7  1 LEU A 180  ? ? 56.19   70.11   
8  1 ILE A 185  ? ? -127.19 -169.04 
9  1 SER A 265  ? ? 72.68   -9.90   
10 1 ASP A 266  ? ? -107.70 -60.20  
11 1 LEU A 291  ? ? 56.75   -129.69 
12 1 THR A 311  ? ? -95.84  35.23   
13 1 SER A 474  ? ? -49.83  150.88  
14 1 LEU A 544  ? ? -57.89  3.30    
15 1 HIS A 615  ? ? -94.00  -64.86  
16 1 GLN A 817  ? ? -140.13 43.66   
17 1 PRO A 883  ? ? -58.70  174.94  
18 1 ASN A 887  ? ? 59.44   71.97   
19 1 THR A 1058 ? ? 57.95   2.25    
20 1 ALA A 1216 ? ? -158.86 78.01   
21 1 HIS A 1287 ? ? -129.74 -162.59 
22 1 TYR A 1288 ? ? 80.56   21.00   
23 1 THR A 1321 ? ? -98.73  31.18   
24 1 LEU A 1324 ? ? -91.33  47.97   
25 1 ASP A 1393 ? ? -114.00 77.45   
26 1 ARG B 140  ? ? 76.58   -10.33  
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9IP4 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9IP4 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.84 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               178297 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       '25 mM HEPES, 500 mM NaCl, 1 mM TCEP, 6 mM MgCl2' 
_em_buffer.pH            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Ternary complex of L-VP35 core region from Marburg virus' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1,2 
# 
_em_imaging.entry_id                        9IP4 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1000 
_em_imaging.nominal_defocus_max             1500 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
_em_imaging.objective_aperture              ? 
_em_imaging.microscope_serial_number        ? 
_em_imaging.microscope_version              ? 
# 
_em_vitrification.entry_id              9IP4 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9IP4 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
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 MET 1    ? A MET 1    
2    1 Y 1 A GLN 2    ? A GLN 2    
3    1 Y 1 A HIS 3    ? A HIS 3    
4    1 Y 1 A ASN 617  ? A ASN 617  
5    1 Y 1 A SER 618  ? A SER 618  
6    1 Y 1 A ALA 619  ? A ALA 619  
7    1 Y 1 A SER 620  ? A SER 620  
8    1 Y 1 A ILE 621  ? A ILE 621  
9    1 Y 1 A GLY 622  ? A GLY 622  
10   1 Y 1 A ARG 1063 ? A ARG 1063 
11   1 Y 1 A THR 1064 ? A THR 1064 
12   1 Y 1 A ILE 1065 ? A ILE 1065 
13   1 Y 1 A SER 1066 ? A SER 1066 
14   1 Y 1 A LEU 1067 ? A LEU 1067 
15   1 Y 1 A THR 1068 ? A THR 1068 
16   1 Y 1 A THR 1069 ? A THR 1069 
17   1 Y 1 A GLU 1070 ? A GLU 1070 
18   1 Y 1 A ASP 1162 ? A ASP 1162 
19   1 Y 1 A SER 1163 ? A SER 1163 
20   1 Y 1 A LYS 1164 ? A LYS 1164 
21   1 Y 1 A SER 1165 ? A SER 1165 
22   1 Y 1 A THR 1166 ? A THR 1166 
23   1 Y 1 A ILE 1167 ? A ILE 1167 
24   1 Y 1 A ASN 1168 ? A ASN 1168 
25   1 Y 1 A LEU 1169 ? A LEU 1169 
26   1 Y 1 A LEU 1170 ? A LEU 1170 
27   1 Y 1 A PRO 1171 ? A PRO 1171 
28   1 Y 1 A TYR 1172 ? A TYR 1172 
29   1 Y 1 A ASP 1173 ? A ASP 1173 
30   1 Y 1 A CYS 1174 ? A CYS 1174 
31   1 Y 1 A LYS 1175 ? A LYS 1175 
32   1 Y 1 A GLU 1176 ? A GLU 1176 
33   1 Y 1 A LEU 1177 ? A LEU 1177 
34   1 Y 1 A ARG 1178 ? A ARG 1178 
35   1 Y 1 A LEU 1179 ? A LEU 1179 
36   1 Y 1 A GLU 1180 ? A GLU 1180 
37   1 Y 1 A GLY 1181 ? A GLY 1181 
38   1 Y 1 A SER 1182 ? A SER 1182 
39   1 Y 1 A ASN 1183 ? A ASN 1183 
40   1 Y 1 A ASP 1184 ? A ASP 1184 
41   1 Y 1 A THR 1185 ? A THR 1185 
42   1 Y 1 A GLU 1186 ? A GLU 1186 
43   1 Y 1 A ARG 1222 ? A ARG 1222 
44   1 Y 1 A THR 1223 ? A THR 1223 
45   1 Y 1 A GLU 1224 ? A GLU 1224 
46   1 Y 1 A ASP 1225 ? A ASP 1225 
47   1 Y 1 A LYS 1226 ? A LYS 1226 
48   1 Y 1 A ILE 1227 ? A ILE 1227 
49   1 Y 1 A GLY 1228 ? A GLY 1228 
50   1 Y 1 A TYR 1229 ? A TYR 1229 
51   1 Y 1 A GLY 1329 ? A GLY 1329 
52   1 Y 1 A GLY 1330 ? A GLY 1330 
53   1 Y 1 A GLY 1417 ? A GLY 1417 
54   1 Y 1 A ARG 1418 ? A ARG 1418 
55   1 Y 1 A LEU 1419 ? A LEU 1419 
56   1 Y 1 A GLY 1420 ? A GLY 1420 
57   1 Y 1 A ARG 1421 ? A ARG 1421 
58   1 Y 1 A VAL 1422 ? A VAL 1422 
59   1 Y 1 A SER 1423 ? A SER 1423 
60   1 Y 1 A ARG 1424 ? A ARG 1424 
61   1 Y 1 A SER 1425 ? A SER 1425 
62   1 Y 1 A SER 1426 ? A SER 1426 
63   1 Y 1 A ARG 1427 ? A ARG 1427 
64   1 Y 1 A GLU 1428 ? A GLU 1428 
65   1 Y 1 A ASN 1429 ? A ASN 1429 
66   1 Y 1 A LEU 1430 ? A LEU 1430 
67   1 Y 1 A TYR 1431 ? A TYR 1431 
68   1 Y 1 A PHE 1432 ? A PHE 1432 
69   1 Y 1 A GLN 1433 ? A GLN 1433 
70   1 Y 1 A GLY 1434 ? A GLY 1434 
71   1 Y 1 A SER 1435 ? A SER 1435 
72   1 Y 1 A GLY 1436 ? A GLY 1436 
73   1 Y 1 A TRP 1437 ? A TRP 1437 
74   1 Y 1 A SER 1438 ? A SER 1438 
75   1 Y 1 A HIS 1439 ? A HIS 1439 
76   1 Y 1 A PRO 1440 ? A PRO 1440 
77   1 Y 1 A GLN 1441 ? A GLN 1441 
78   1 Y 1 A PHE 1442 ? A PHE 1442 
79   1 Y 1 A GLU 1443 ? A GLU 1443 
80   1 Y 1 A LYS 1444 ? A LYS 1444 
81   1 Y 1 A GLY 1445 ? A GLY 1445 
82   1 Y 1 A GLY 1446 ? A GLY 1446 
83   1 Y 1 A GLY 1447 ? A GLY 1447 
84   1 Y 1 A SER 1448 ? A SER 1448 
85   1 Y 1 A GLY 1449 ? A GLY 1449 
86   1 Y 1 A GLY 1450 ? A GLY 1450 
87   1 Y 1 A GLY 1451 ? A GLY 1451 
88   1 Y 1 A SER 1452 ? A SER 1452 
89   1 Y 1 A GLY 1453 ? A GLY 1453 
90   1 Y 1 A GLY 1454 ? A GLY 1454 
91   1 Y 1 A SER 1455 ? A SER 1455 
92   1 Y 1 A ALA 1456 ? A ALA 1456 
93   1 Y 1 A TRP 1457 ? A TRP 1457 
94   1 Y 1 A SER 1458 ? A SER 1458 
95   1 Y 1 A HIS 1459 ? A HIS 1459 
96   1 Y 1 A PRO 1460 ? A PRO 1460 
97   1 Y 1 A GLN 1461 ? A GLN 1461 
98   1 Y 1 A PHE 1462 ? A PHE 1462 
99   1 Y 1 A GLU 1463 ? A GLU 1463 
100  1 Y 1 A LYS 1464 ? A LYS 1464 
101  1 Y 1 A GLY 1465 ? A GLY 1465 
102  1 Y 1 A SER 1466 ? A SER 1466 
103  1 Y 1 A ALA 1467 ? A ALA 1467 
104  1 Y 1 A SER 1468 ? A SER 1468 
105  1 Y 1 A HIS 1469 ? A HIS 1469 
106  1 Y 1 A HIS 1470 ? A HIS 1470 
107  1 Y 1 A HIS 1471 ? A HIS 1471 
108  1 Y 1 A HIS 1472 ? A HIS 1472 
109  1 Y 1 A HIS 1473 ? A HIS 1473 
110  1 Y 1 A HIS 1474 ? A HIS 1474 
111  1 Y 1 A GLY 1475 ? A GLY 1475 
112  1 Y 1 A THR 1476 ? A THR 1476 
113  1 Y 1 A LYS 1477 ? A LYS 1477 
114  1 Y 1 A THR 1478 ? A THR 1478 
115  1 Y 1 A GLU 1479 ? A GLU 1479 
116  1 Y 1 A GLU 1480 ? A GLU 1480 
117  1 Y 1 A GLY 1481 ? A GLY 1481 
118  1 Y 1 A LYS 1482 ? A LYS 1482 
119  1 Y 1 A LEU 1483 ? A LEU 1483 
120  1 Y 1 A VAL 1484 ? A VAL 1484 
121  1 Y 1 A ILE 1485 ? A ILE 1485 
122  1 Y 1 A TRP 1486 ? A TRP 1486 
123  1 Y 1 A ILE 1487 ? A ILE 1487 
124  1 Y 1 A ASN 1488 ? A ASN 1488 
125  1 Y 1 A GLY 1489 ? A GLY 1489 
126  1 Y 1 A ASP 1490 ? A ASP 1490 
127  1 Y 1 A LYS 1491 ? A LYS 1491 
128  1 Y 1 A GLY 1492 ? A GLY 1492 
129  1 Y 1 A TYR 1493 ? A TYR 1493 
130  1 Y 1 A ASN 1494 ? A ASN 1494 
131  1 Y 1 A GLY 1495 ? A GLY 1495 
132  1 Y 1 A LEU 1496 ? A LEU 1496 
133  1 Y 1 A ALA 1497 ? A ALA 1497 
134  1 Y 1 A GLU 1498 ? A GLU 1498 
135  1 Y 1 A VAL 1499 ? A VAL 1499 
136  1 Y 1 A GLY 1500 ? A GLY 1500 
137  1 Y 1 A LYS 1501 ? A LYS 1501 
138  1 Y 1 A LYS 1502 ? A LYS 1502 
139  1 Y 1 A PHE 1503 ? A PHE 1503 
140  1 Y 1 A GLU 1504 ? A GLU 1504 
141  1 Y 1 A LYS 1505 ? A LYS 1505 
142  1 Y 1 A ASP 1506 ? A ASP 1506 
143  1 Y 1 A THR 1507 ? A THR 1507 
144  1 Y 1 A GLY 1508 ? A GLY 1508 
145  1 Y 1 A ILE 1509 ? A ILE 1509 
146  1 Y 1 A LYS 1510 ? A LYS 1510 
147  1 Y 1 A VAL 1511 ? A VAL 1511 
148  1 Y 1 A THR 1512 ? A THR 1512 
149  1 Y 1 A VAL 1513 ? A VAL 1513 
150  1 Y 1 A GLU 1514 ? A GLU 1514 
151  1 Y 1 A HIS 1515 ? A HIS 1515 
152  1 Y 1 A PRO 1516 ? A PRO 1516 
153  1 Y 1 A ASP 1517 ? A ASP 1517 
154  1 Y 1 A LYS 1518 ? A LYS 1518 
155  1 Y 1 A LEU 1519 ? A LEU 1519 
156  1 Y 1 A GLU 1520 ? A GLU 1520 
157  1 Y 1 A GLU 1521 ? A GLU 1521 
158  1 Y 1 A LYS 1522 ? A LYS 1522 
159  1 Y 1 A PHE 1523 ? A PHE 1523 
160  1 Y 1 A PRO 1524 ? A PRO 1524 
161  1 Y 1 A GLN 1525 ? A GLN 1525 
162  1 Y 1 A VAL 1526 ? A VAL 1526 
163  1 Y 1 A ALA 1527 ? A ALA 1527 
164  1 Y 1 A ALA 1528 ? A ALA 1528 
165  1 Y 1 A THR 1529 ? A THR 1529 
166  1 Y 1 A GLY 1530 ? A GLY 1530 
167  1 Y 1 A ASP 1531 ? A ASP 1531 
168  1 Y 1 A GLY 1532 ? A GLY 1532 
169  1 Y 1 A PRO 1533 ? A PRO 1533 
170  1 Y 1 A ASP 1534 ? A ASP 1534 
171  1 Y 1 A ILE 1535 ? A ILE 1535 
172  1 Y 1 A ILE 1536 ? A ILE 1536 
173  1 Y 1 A PHE 1537 ? A PHE 1537 
174  1 Y 1 A TRP 1538 ? A TRP 1538 
175  1 Y 1 A ALA 1539 ? A ALA 1539 
176  1 Y 1 A HIS 1540 ? A HIS 1540 
177  1 Y 1 A ASP 1541 ? A ASP 1541 
178  1 Y 1 A ARG 1542 ? A ARG 1542 
179  1 Y 1 A PHE 1543 ? A PHE 1543 
180  1 Y 1 A GLY 1544 ? A GLY 1544 
181  1 Y 1 A GLY 1545 ? A GLY 1545 
182  1 Y 1 A TYR 1546 ? A TYR 1546 
183  1 Y 1 A ALA 1547 ? A ALA 1547 
184  1 Y 1 A GLN 1548 ? A GLN 1548 
185  1 Y 1 A SER 1549 ? A SER 1549 
186  1 Y 1 A GLY 1550 ? A GLY 1550 
187  1 Y 1 A LEU 1551 ? A LEU 1551 
188  1 Y 1 A LEU 1552 ? A LEU 1552 
189  1 Y 1 A ALA 1553 ? A ALA 1553 
190  1 Y 1 A GLU 1554 ? A GLU 1554 
191  1 Y 1 A ILE 1555 ? A ILE 1555 
192  1 Y 1 A THR 1556 ? A THR 1556 
193  1 Y 1 A PRO 1557 ? A PRO 1557 
194  1 Y 1 A ASP 1558 ? A ASP 1558 
195  1 Y 1 A LYS 1559 ? A LYS 1559 
196  1 Y 1 A ALA 1560 ? A ALA 1560 
197  1 Y 1 A PHE 1561 ? A PHE 1561 
198  1 Y 1 A GLN 1562 ? A GLN 1562 
199  1 Y 1 A ASP 1563 ? A ASP 1563 
200  1 Y 1 A LYS 1564 ? A LYS 1564 
201  1 Y 1 A LEU 1565 ? A LEU 1565 
202  1 Y 1 A TYR 1566 ? A TYR 1566 
203  1 Y 1 A PRO 1567 ? A PRO 1567 
204  1 Y 1 A PHE 1568 ? A PHE 1568 
205  1 Y 1 A THR 1569 ? A THR 1569 
206  1 Y 1 A TRP 1570 ? A TRP 1570 
207  1 Y 1 A ASP 1571 ? A ASP 1571 
208  1 Y 1 A ALA 1572 ? A ALA 1572 
209  1 Y 1 A VAL 1573 ? A VAL 1573 
210  1 Y 1 A ARG 1574 ? A ARG 1574 
211  1 Y 1 A TYR 1575 ? A TYR 1575 
212  1 Y 1 A ASN 1576 ? A ASN 1576 
213  1 Y 1 A GLY 1577 ? A GLY 1577 
214  1 Y 1 A LYS 1578 ? A LYS 1578 
215  1 Y 1 A LEU 1579 ? A LEU 1579 
216  1 Y 1 A ILE 1580 ? A ILE 1580 
217  1 Y 1 A ALA 1581 ? A ALA 1581 
218  1 Y 1 A TYR 1582 ? A TYR 1582 
219  1 Y 1 A PRO 1583 ? A PRO 1583 
220  1 Y 1 A ILE 1584 ? A ILE 1584 
221  1 Y 1 A ALA 1585 ? A ALA 1585 
222  1 Y 1 A VAL 1586 ? A VAL 1586 
223  1 Y 1 A GLU 1587 ? A GLU 1587 
224  1 Y 1 A ALA 1588 ? A ALA 1588 
225  1 Y 1 A LEU 1589 ? A LEU 1589 
226  1 Y 1 A SER 1590 ? A SER 1590 
227  1 Y 1 A LEU 1591 ? A LEU 1591 
228  1 Y 1 A ILE 1592 ? A ILE 1592 
229  1 Y 1 A TYR 1593 ? A TYR 1593 
230  1 Y 1 A ASN 1594 ? A ASN 1594 
231  1 Y 1 A LYS 1595 ? A LYS 1595 
232  1 Y 1 A ASP 1596 ? A ASP 1596 
233  1 Y 1 A LEU 1597 ? A LEU 1597 
234  1 Y 1 A LEU 1598 ? A LEU 1598 
235  1 Y 1 A PRO 1599 ? A PRO 1599 
236  1 Y 1 A ASN 1600 ? A ASN 1600 
237  1 Y 1 A PRO 1601 ? A PRO 1601 
238  1 Y 1 A PRO 1602 ? A PRO 1602 
239  1 Y 1 A LYS 1603 ? A LYS 1603 
240  1 Y 1 A THR 1604 ? A THR 1604 
241  1 Y 1 A TRP 1605 ? A TRP 1605 
242  1 Y 1 A GLU 1606 ? A GLU 1606 
243  1 Y 1 A GLU 1607 ? A GLU 1607 
244  1 Y 1 A ILE 1608 ? A ILE 1608 
245  1 Y 1 A PRO 1609 ? A PRO 1609 
246  1 Y 1 A ALA 1610 ? A ALA 1610 
247  1 Y 1 A LEU 1611 ? A LEU 1611 
248  1 Y 1 A ASP 1612 ? A ASP 1612 
249  1 Y 1 A LYS 1613 ? A LYS 1613 
250  1 Y 1 A GLU 1614 ? A GLU 1614 
251  1 Y 1 A LEU 1615 ? A LEU 1615 
252  1 Y 1 A LYS 1616 ? A LYS 1616 
253  1 Y 1 A ALA 1617 ? A ALA 1617 
254  1 Y 1 A LYS 1618 ? A LYS 1618 
255  1 Y 1 A GLY 1619 ? A GLY 1619 
256  1 Y 1 A LYS 1620 ? A LYS 1620 
257  1 Y 1 A SER 1621 ? A SER 1621 
258  1 Y 1 A ALA 1622 ? A ALA 1622 
259  1 Y 1 A LEU 1623 ? A LEU 1623 
260  1 Y 1 A MET 1624 ? A MET 1624 
261  1 Y 1 A PHE 1625 ? A PHE 1625 
262  1 Y 1 A ASN 1626 ? A ASN 1626 
263  1 Y 1 A LEU 1627 ? A LEU 1627 
264  1 Y 1 A GLN 1628 ? A GLN 1628 
265  1 Y 1 A GLU 1629 ? A GLU 1629 
266  1 Y 1 A PRO 1630 ? A PRO 1630 
267  1 Y 1 A TYR 1631 ? A TYR 1631 
268  1 Y 1 A PHE 1632 ? A PHE 1632 
269  1 Y 1 A THR 1633 ? A THR 1633 
270  1 Y 1 A TRP 1634 ? A TRP 1634 
271  1 Y 1 A PRO 1635 ? A PRO 1635 
272  1 Y 1 A LEU 1636 ? A LEU 1636 
273  1 Y 1 A ILE 1637 ? A ILE 1637 
274  1 Y 1 A ALA 1638 ? A ALA 1638 
275  1 Y 1 A ALA 1639 ? A ALA 1639 
276  1 Y 1 A ASP 1640 ? A ASP 1640 
277  1 Y 1 A GLY 1641 ? A GLY 1641 
278  1 Y 1 A GLY 1642 ? A GLY 1642 
279  1 Y 1 A TYR 1643 ? A TYR 1643 
280  1 Y 1 A ALA 1644 ? A ALA 1644 
281  1 Y 1 A PHE 1645 ? A PHE 1645 
282  1 Y 1 A LYS 1646 ? A LYS 1646 
283  1 Y 1 A TYR 1647 ? A TYR 1647 
284  1 Y 1 A GLU 1648 ? A GLU 1648 
285  1 Y 1 A ASN 1649 ? A ASN 1649 
286  1 Y 1 A GLY 1650 ? A GLY 1650 
287  1 Y 1 A LYS 1651 ? A LYS 1651 
288  1 Y 1 A TYR 1652 ? A TYR 1652 
289  1 Y 1 A ASP 1653 ? A ASP 1653 
290  1 Y 1 A ILE 1654 ? A ILE 1654 
291  1 Y 1 A LYS 1655 ? A LYS 1655 
292  1 Y 1 A ASP 1656 ? A ASP 1656 
293  1 Y 1 A VAL 1657 ? A VAL 1657 
294  1 Y 1 A GLY 1658 ? A GLY 1658 
295  1 Y 1 A VAL 1659 ? A VAL 1659 
296  1 Y 1 A ASP 1660 ? A ASP 1660 
297  1 Y 1 A ASN 1661 ? A ASN 1661 
298  1 Y 1 A ALA 1662 ? A ALA 1662 
299  1 Y 1 A GLY 1663 ? A GLY 1663 
300  1 Y 1 A ALA 1664 ? A ALA 1664 
301  1 Y 1 A LYS 1665 ? A LYS 1665 
302  1 Y 1 A ALA 1666 ? A ALA 1666 
303  1 Y 1 A GLY 1667 ? A GLY 1667 
304  1 Y 1 A LEU 1668 ? A LEU 1668 
305  1 Y 1 A THR 1669 ? A THR 1669 
306  1 Y 1 A PHE 1670 ? A PHE 1670 
307  1 Y 1 A LEU 1671 ? A LEU 1671 
308  1 Y 1 A VAL 1672 ? A VAL 1672 
309  1 Y 1 A ASP 1673 ? A ASP 1673 
310  1 Y 1 A LEU 1674 ? A LEU 1674 
311  1 Y 1 A ILE 1675 ? A ILE 1675 
312  1 Y 1 A LYS 1676 ? A LYS 1676 
313  1 Y 1 A ASN 1677 ? A ASN 1677 
314  1 Y 1 A LYS 1678 ? A LYS 1678 
315  1 Y 1 A HIS 1679 ? A HIS 1679 
316  1 Y 1 A MET 1680 ? A MET 1680 
317  1 Y 1 A ASN 1681 ? A ASN 1681 
318  1 Y 1 A ALA 1682 ? A ALA 1682 
319  1 Y 1 A ASP 1683 ? A ASP 1683 
320  1 Y 1 A THR 1684 ? A THR 1684 
321  1 Y 1 A ASP 1685 ? A ASP 1685 
322  1 Y 1 A TYR 1686 ? A TYR 1686 
323  1 Y 1 A SER 1687 ? A SER 1687 
324  1 Y 1 A ILE 1688 ? A ILE 1688 
325  1 Y 1 A ALA 1689 ? A ALA 1689 
326  1 Y 1 A GLU 1690 ? A GLU 1690 
327  1 Y 1 A ALA 1691 ? A ALA 1691 
328  1 Y 1 A ALA 1692 ? A ALA 1692 
329  1 Y 1 A PHE 1693 ? A PHE 1693 
330  1 Y 1 A ASN 1694 ? A ASN 1694 
331  1 Y 1 A LYS 1695 ? A LYS 1695 
332  1 Y 1 A GLY 1696 ? A GLY 1696 
333  1 Y 1 A GLU 1697 ? A GLU 1697 
334  1 Y 1 A THR 1698 ? A THR 1698 
335  1 Y 1 A ALA 1699 ? A ALA 1699 
336  1 Y 1 A MET 1700 ? A MET 1700 
337  1 Y 1 A THR 1701 ? A THR 1701 
338  1 Y 1 A ILE 1702 ? A ILE 1702 
339  1 Y 1 A ASN 1703 ? A ASN 1703 
340  1 Y 1 A GLY 1704 ? A GLY 1704 
341  1 Y 1 A PRO 1705 ? A PRO 1705 
342  1 Y 1 A TRP 1706 ? A TRP 1706 
343  1 Y 1 A ALA 1707 ? A ALA 1707 
344  1 Y 1 A TRP 1708 ? A TRP 1708 
345  1 Y 1 A SER 1709 ? A SER 1709 
346  1 Y 1 A ASN 1710 ? A ASN 1710 
347  1 Y 1 A ILE 1711 ? A ILE 1711 
348  1 Y 1 A ASP 1712 ? A ASP 1712 
349  1 Y 1 A THR 1713 ? A THR 1713 
350  1 Y 1 A SER 1714 ? A SER 1714 
351  1 Y 1 A LYS 1715 ? A LYS 1715 
352  1 Y 1 A VAL 1716 ? A VAL 1716 
353  1 Y 1 A ASN 1717 ? A ASN 1717 
354  1 Y 1 A TYR 1718 ? A TYR 1718 
355  1 Y 1 A GLY 1719 ? A GLY 1719 
356  1 Y 1 A VAL 1720 ? A VAL 1720 
357  1 Y 1 A THR 1721 ? A THR 1721 
358  1 Y 1 A VAL 1722 ? A VAL 1722 
359  1 Y 1 A LEU 1723 ? A LEU 1723 
360  1 Y 1 A PRO 1724 ? A PRO 1724 
361  1 Y 1 A THR 1725 ? A THR 1725 
362  1 Y 1 A PHE 1726 ? A PHE 1726 
363  1 Y 1 A LYS 1727 ? A LYS 1727 
364  1 Y 1 A GLY 1728 ? A GLY 1728 
365  1 Y 1 A GLN 1729 ? A GLN 1729 
366  1 Y 1 A PRO 1730 ? A PRO 1730 
367  1 Y 1 A SER 1731 ? A SER 1731 
368  1 Y 1 A LYS 1732 ? A LYS 1732 
369  1 Y 1 A PRO 1733 ? A PRO 1733 
370  1 Y 1 A PHE 1734 ? A PHE 1734 
371  1 Y 1 A VAL 1735 ? A VAL 1735 
372  1 Y 1 A GLY 1736 ? A GLY 1736 
373  1 Y 1 A VAL 1737 ? A VAL 1737 
374  1 Y 1 A LEU 1738 ? A LEU 1738 
375  1 Y 1 A SER 1739 ? A SER 1739 
376  1 Y 1 A ALA 1740 ? A ALA 1740 
377  1 Y 1 A GLY 1741 ? A GLY 1741 
378  1 Y 1 A ILE 1742 ? A ILE 1742 
379  1 Y 1 A ASN 1743 ? A ASN 1743 
380  1 Y 1 A ALA 1744 ? A ALA 1744 
381  1 Y 1 A ALA 1745 ? A ALA 1745 
382  1 Y 1 A SER 1746 ? A SER 1746 
383  1 Y 1 A PRO 1747 ? A PRO 1747 
384  1 Y 1 A ASN 1748 ? A ASN 1748 
385  1 Y 1 A LYS 1749 ? A LYS 1749 
386  1 Y 1 A GLU 1750 ? A GLU 1750 
387  1 Y 1 A LEU 1751 ? A LEU 1751 
388  1 Y 1 A ALA 1752 ? A ALA 1752 
389  1 Y 1 A LYS 1753 ? A LYS 1753 
390  1 Y 1 A GLU 1754 ? A GLU 1754 
391  1 Y 1 A PHE 1755 ? A PHE 1755 
392  1 Y 1 A LEU 1756 ? A LEU 1756 
393  1 Y 1 A GLU 1757 ? A GLU 1757 
394  1 Y 1 A ASN 1758 ? A ASN 1758 
395  1 Y 1 A TYR 1759 ? A TYR 1759 
396  1 Y 1 A LEU 1760 ? A LEU 1760 
397  1 Y 1 A LEU 1761 ? A LEU 1761 
398  1 Y 1 A THR 1762 ? A THR 1762 
399  1 Y 1 A ASP 1763 ? A ASP 1763 
400  1 Y 1 A GLU 1764 ? A GLU 1764 
401  1 Y 1 A GLY 1765 ? A GLY 1765 
402  1 Y 1 A LEU 1766 ? A LEU 1766 
403  1 Y 1 A GLU 1767 ? A GLU 1767 
404  1 Y 1 A ALA 1768 ? A ALA 1768 
405  1 Y 1 A VAL 1769 ? A VAL 1769 
406  1 Y 1 A ASN 1770 ? A ASN 1770 
407  1 Y 1 A LYS 1771 ? A LYS 1771 
408  1 Y 1 A ASP 1772 ? A ASP 1772 
409  1 Y 1 A LYS 1773 ? A LYS 1773 
410  1 Y 1 A PRO 1774 ? A PRO 1774 
411  1 Y 1 A LEU 1775 ? A LEU 1775 
412  1 Y 1 A GLY 1776 ? A GLY 1776 
413  1 Y 1 A ALA 1777 ? A ALA 1777 
414  1 Y 1 A VAL 1778 ? A VAL 1778 
415  1 Y 1 A ALA 1779 ? A ALA 1779 
416  1 Y 1 A LEU 1780 ? A LEU 1780 
417  1 Y 1 A LYS 1781 ? A LYS 1781 
418  1 Y 1 A SER 1782 ? A SER 1782 
419  1 Y 1 A TYR 1783 ? A TYR 1783 
420  1 Y 1 A GLU 1784 ? A GLU 1784 
421  1 Y 1 A GLU 1785 ? A GLU 1785 
422  1 Y 1 A GLU 1786 ? A GLU 1786 
423  1 Y 1 A LEU 1787 ? A LEU 1787 
424  1 Y 1 A ALA 1788 ? A ALA 1788 
425  1 Y 1 A LYS 1789 ? A LYS 1789 
426  1 Y 1 A ASP 1790 ? A ASP 1790 
427  1 Y 1 A PRO 1791 ? A PRO 1791 
428  1 Y 1 A ARG 1792 ? A ARG 1792 
429  1 Y 1 A ILE 1793 ? A ILE 1793 
430  1 Y 1 A ALA 1794 ? A ALA 1794 
431  1 Y 1 A ALA 1795 ? A ALA 1795 
432  1 Y 1 A THR 1796 ? A THR 1796 
433  1 Y 1 A MET 1797 ? A MET 1797 
434  1 Y 1 A GLU 1798 ? A GLU 1798 
435  1 Y 1 A ASN 1799 ? A ASN 1799 
436  1 Y 1 A ALA 1800 ? A ALA 1800 
437  1 Y 1 A GLN 1801 ? A GLN 1801 
438  1 Y 1 A LYS 1802 ? A LYS 1802 
439  1 Y 1 A GLY 1803 ? A GLY 1803 
440  1 Y 1 A GLU 1804 ? A GLU 1804 
441  1 Y 1 A ILE 1805 ? A ILE 1805 
442  1 Y 1 A MET 1806 ? A MET 1806 
443  1 Y 1 A PRO 1807 ? A PRO 1807 
444  1 Y 1 A ASN 1808 ? A ASN 1808 
445  1 Y 1 A ILE 1809 ? A ILE 1809 
446  1 Y 1 A PRO 1810 ? A PRO 1810 
447  1 Y 1 A GLN 1811 ? A GLN 1811 
448  1 Y 1 A MET 1812 ? A MET 1812 
449  1 Y 1 A SER 1813 ? A SER 1813 
450  1 Y 1 A ALA 1814 ? A ALA 1814 
451  1 Y 1 A PHE 1815 ? A PHE 1815 
452  1 Y 1 A TRP 1816 ? A TRP 1816 
453  1 Y 1 A TYR 1817 ? A TYR 1817 
454  1 Y 1 A ALA 1818 ? A ALA 1818 
455  1 Y 1 A VAL 1819 ? A VAL 1819 
456  1 Y 1 A ARG 1820 ? A ARG 1820 
457  1 Y 1 A THR 1821 ? A THR 1821 
458  1 Y 1 A ALA 1822 ? A ALA 1822 
459  1 Y 1 A VAL 1823 ? A VAL 1823 
460  1 Y 1 A ILE 1824 ? A ILE 1824 
461  1 Y 1 A ASN 1825 ? A ASN 1825 
462  1 Y 1 A ALA 1826 ? A ALA 1826 
463  1 Y 1 A ALA 1827 ? A ALA 1827 
464  1 Y 1 A SER 1828 ? A SER 1828 
465  1 Y 1 A GLY 1829 ? A GLY 1829 
466  1 Y 1 A ARG 1830 ? A ARG 1830 
467  1 Y 1 A GLN 1831 ? A GLN 1831 
468  1 Y 1 A THR 1832 ? A THR 1832 
469  1 Y 1 A VAL 1833 ? A VAL 1833 
470  1 Y 1 A ASP 1834 ? A ASP 1834 
471  1 Y 1 A GLU 1835 ? A GLU 1835 
472  1 Y 1 A ALA 1836 ? A ALA 1836 
473  1 Y 1 A LEU 1837 ? A LEU 1837 
474  1 Y 1 A LYS 1838 ? A LYS 1838 
475  1 Y 1 A ASP 1839 ? A ASP 1839 
476  1 Y 1 A ALA 1840 ? A ALA 1840 
477  1 Y 1 A GLN 1841 ? A GLN 1841 
478  1 Y 1 A THR 1842 ? A THR 1842 
479  1 Y 1 A GLY 1843 ? A GLY 1843 
480  1 Y 1 A ASP 1844 ? A ASP 1844 
481  1 Y 1 A TYR 1845 ? A TYR 1845 
482  1 Y 1 A LYS 1846 ? A LYS 1846 
483  1 Y 1 A ASP 1847 ? A ASP 1847 
484  1 Y 1 A ASP 1848 ? A ASP 1848 
485  1 Y 1 A ASP 1849 ? A ASP 1849 
486  1 Y 1 A ASP 1850 ? A ASP 1850 
487  1 Y 1 A LYS 1851 ? A LYS 1851 
488  1 Y 1 B MET -341 ? B MET 1    
489  1 Y 1 B GLY -340 ? B GLY 2    
490  1 Y 1 B SER -339 ? B SER 3    
491  1 Y 1 B SER -338 ? B SER 4    
492  1 Y 1 B HIS -337 ? B HIS 5    
493  1 Y 1 B HIS -336 ? B HIS 6    
494  1 Y 1 B HIS -335 ? B HIS 7    
495  1 Y 1 B HIS -334 ? B HIS 8    
496  1 Y 1 B HIS -333 ? B HIS 9    
497  1 Y 1 B HIS -332 ? B HIS 10   
498  1 Y 1 B GLY -331 ? B GLY 11   
499  1 Y 1 B THR -330 ? B THR 12   
500  1 Y 1 B LYS -329 ? B LYS 13   
501  1 Y 1 B THR -328 ? B THR 14   
502  1 Y 1 B GLU -327 ? B GLU 15   
503  1 Y 1 B GLU -326 ? B GLU 16   
504  1 Y 1 B GLY -325 ? B GLY 17   
505  1 Y 1 B LYS -324 ? B LYS 18   
506  1 Y 1 B LEU -323 ? B LEU 19   
507  1 Y 1 B VAL -322 ? B VAL 20   
508  1 Y 1 B ILE -321 ? B ILE 21   
509  1 Y 1 B TRP -320 ? B TRP 22   
510  1 Y 1 B ILE -319 ? B ILE 23   
511  1 Y 1 B ASN -318 ? B ASN 24   
512  1 Y 1 B GLY -317 ? B GLY 25   
513  1 Y 1 B ASP -316 ? B ASP 26   
514  1 Y 1 B LYS -315 ? B LYS 27   
515  1 Y 1 B GLY -314 ? B GLY 28   
516  1 Y 1 B TYR -313 ? B TYR 29   
517  1 Y 1 B ASN -312 ? B ASN 30   
518  1 Y 1 B GLY -311 ? B GLY 31   
519  1 Y 1 B LEU -310 ? B LEU 32   
520  1 Y 1 B ALA -309 ? B ALA 33   
521  1 Y 1 B GLU -308 ? B GLU 34   
522  1 Y 1 B VAL -307 ? B VAL 35   
523  1 Y 1 B GLY -306 ? B GLY 36   
524  1 Y 1 B LYS -305 ? B LYS 37   
525  1 Y 1 B LYS -304 ? B LYS 38   
526  1 Y 1 B PHE -303 ? B PHE 39   
527  1 Y 1 B GLU -302 ? B GLU 40   
528  1 Y 1 B LYS -301 ? B LYS 41   
529  1 Y 1 B ASP -300 ? B ASP 42   
530  1 Y 1 B THR -299 ? B THR 43   
531  1 Y 1 B GLY -298 ? B GLY 44   
532  1 Y 1 B ILE -297 ? B ILE 45   
533  1 Y 1 B LYS -296 ? B LYS 46   
534  1 Y 1 B VAL -295 ? B VAL 47   
535  1 Y 1 B THR -294 ? B THR 48   
536  1 Y 1 B VAL -293 ? B VAL 49   
537  1 Y 1 B GLU -292 ? B GLU 50   
538  1 Y 1 B HIS -291 ? B HIS 51   
539  1 Y 1 B PRO -290 ? B PRO 52   
540  1 Y 1 B ASP -289 ? B ASP 53   
541  1 Y 1 B LYS -288 ? B LYS 54   
542  1 Y 1 B LEU -287 ? B LEU 55   
543  1 Y 1 B GLU -286 ? B GLU 56   
544  1 Y 1 B GLU -285 ? B GLU 57   
545  1 Y 1 B LYS -284 ? B LYS 58   
546  1 Y 1 B PHE -283 ? B PHE 59   
547  1 Y 1 B PRO -282 ? B PRO 60   
548  1 Y 1 B GLN -281 ? B GLN 61   
549  1 Y 1 B VAL -280 ? B VAL 62   
550  1 Y 1 B ALA -279 ? B ALA 63   
551  1 Y 1 B ALA -278 ? B ALA 64   
552  1 Y 1 B THR -277 ? B THR 65   
553  1 Y 1 B GLY -276 ? B GLY 66   
554  1 Y 1 B ASP -275 ? B ASP 67   
555  1 Y 1 B GLY -274 ? B GLY 68   
556  1 Y 1 B PRO -273 ? B PRO 69   
557  1 Y 1 B ASP -272 ? B ASP 70   
558  1 Y 1 B ILE -271 ? B ILE 71   
559  1 Y 1 B ILE -270 ? B ILE 72   
560  1 Y 1 B PHE -269 ? B PHE 73   
561  1 Y 1 B TRP -268 ? B TRP 74   
562  1 Y 1 B ALA -267 ? B ALA 75   
563  1 Y 1 B HIS -266 ? B HIS 76   
564  1 Y 1 B ASP -265 ? B ASP 77   
565  1 Y 1 B ARG -264 ? B ARG 78   
566  1 Y 1 B PHE -263 ? B PHE 79   
567  1 Y 1 B GLY -262 ? B GLY 80   
568  1 Y 1 B GLY -261 ? B GLY 81   
569  1 Y 1 B TYR -260 ? B TYR 82   
570  1 Y 1 B ALA -259 ? B ALA 83   
571  1 Y 1 B GLN -258 ? B GLN 84   
572  1 Y 1 B SER -257 ? B SER 85   
573  1 Y 1 B GLY -256 ? B GLY 86   
574  1 Y 1 B LEU -255 ? B LEU 87   
575  1 Y 1 B LEU -254 ? B LEU 88   
576  1 Y 1 B ALA -253 ? B ALA 89   
577  1 Y 1 B GLU -252 ? B GLU 90   
578  1 Y 1 B ILE -251 ? B ILE 91   
579  1 Y 1 B THR -250 ? B THR 92   
580  1 Y 1 B PRO -249 ? B PRO 93   
581  1 Y 1 B ASP -248 ? B ASP 94   
582  1 Y 1 B LYS -247 ? B LYS 95   
583  1 Y 1 B ALA -246 ? B ALA 96   
584  1 Y 1 B PHE -245 ? B PHE 97   
585  1 Y 1 B GLN -244 ? B GLN 98   
586  1 Y 1 B ASP -243 ? B ASP 99   
587  1 Y 1 B LYS -242 ? B LYS 100  
588  1 Y 1 B LEU -241 ? B LEU 101  
589  1 Y 1 B TYR -240 ? B TYR 102  
590  1 Y 1 B PRO -239 ? B PRO 103  
591  1 Y 1 B PHE -238 ? B PHE 104  
592  1 Y 1 B THR -237 ? B THR 105  
593  1 Y 1 B TRP -236 ? B TRP 106  
594  1 Y 1 B ASP -235 ? B ASP 107  
595  1 Y 1 B ALA -234 ? B ALA 108  
596  1 Y 1 B VAL -233 ? B VAL 109  
597  1 Y 1 B ARG -232 ? B ARG 110  
598  1 Y 1 B TYR -231 ? B TYR 111  
599  1 Y 1 B ASN -230 ? B ASN 112  
600  1 Y 1 B GLY -229 ? B GLY 113  
601  1 Y 1 B LYS -228 ? B LYS 114  
602  1 Y 1 B LEU -227 ? B LEU 115  
603  1 Y 1 B ILE -226 ? B ILE 116  
604  1 Y 1 B ALA -225 ? B ALA 117  
605  1 Y 1 B TYR -224 ? B TYR 118  
606  1 Y 1 B PRO -223 ? B PRO 119  
607  1 Y 1 B ILE -222 ? B ILE 120  
608  1 Y 1 B ALA -221 ? B ALA 121  
609  1 Y 1 B VAL -220 ? B VAL 122  
610  1 Y 1 B GLU -219 ? B GLU 123  
611  1 Y 1 B ALA -218 ? B ALA 124  
612  1 Y 1 B LEU -217 ? B LEU 125  
613  1 Y 1 B SER -216 ? B SER 126  
614  1 Y 1 B LEU -215 ? B LEU 127  
615  1 Y 1 B ILE -214 ? B ILE 128  
616  1 Y 1 B TYR -213 ? B TYR 129  
617  1 Y 1 B ASN -212 ? B ASN 130  
618  1 Y 1 B LYS -211 ? B LYS 131  
619  1 Y 1 B ASP -210 ? B ASP 132  
620  1 Y 1 B LEU -209 ? B LEU 133  
621  1 Y 1 B LEU -208 ? B LEU 134  
622  1 Y 1 B PRO -207 ? B PRO 135  
623  1 Y 1 B ASN -206 ? B ASN 136  
624  1 Y 1 B PRO -205 ? B PRO 137  
625  1 Y 1 B PRO -204 ? B PRO 138  
626  1 Y 1 B LYS -203 ? B LYS 139  
627  1 Y 1 B THR -202 ? B THR 140  
628  1 Y 1 B TRP -201 ? B TRP 141  
629  1 Y 1 B GLU -200 ? B GLU 142  
630  1 Y 1 B GLU -199 ? B GLU 143  
631  1 Y 1 B ILE -198 ? B ILE 144  
632  1 Y 1 B PRO -197 ? B PRO 145  
633  1 Y 1 B ALA -196 ? B ALA 146  
634  1 Y 1 B LEU -195 ? B LEU 147  
635  1 Y 1 B ASP -194 ? B ASP 148  
636  1 Y 1 B LYS -193 ? B LYS 149  
637  1 Y 1 B GLU -192 ? B GLU 150  
638  1 Y 1 B LEU -191 ? B LEU 151  
639  1 Y 1 B LYS -190 ? B LYS 152  
640  1 Y 1 B ALA -189 ? B ALA 153  
641  1 Y 1 B LYS -188 ? B LYS 154  
642  1 Y 1 B GLY -187 ? B GLY 155  
643  1 Y 1 B LYS -186 ? B LYS 156  
644  1 Y 1 B SER -185 ? B SER 157  
645  1 Y 1 B ALA -184 ? B ALA 158  
646  1 Y 1 B LEU -183 ? B LEU 159  
647  1 Y 1 B MET -182 ? B MET 160  
648  1 Y 1 B PHE -181 ? B PHE 161  
649  1 Y 1 B ASN -180 ? B ASN 162  
650  1 Y 1 B LEU -179 ? B LEU 163  
651  1 Y 1 B GLN -178 ? B GLN 164  
652  1 Y 1 B GLU -177 ? B GLU 165  
653  1 Y 1 B PRO -176 ? B PRO 166  
654  1 Y 1 B TYR -175 ? B TYR 167  
655  1 Y 1 B PHE -174 ? B PHE 168  
656  1 Y 1 B THR -173 ? B THR 169  
657  1 Y 1 B TRP -172 ? B TRP 170  
658  1 Y 1 B PRO -171 ? B PRO 171  
659  1 Y 1 B LEU -170 ? B LEU 172  
660  1 Y 1 B ILE -169 ? B ILE 173  
661  1 Y 1 B ALA -168 ? B ALA 174  
662  1 Y 1 B ALA -167 ? B ALA 175  
663  1 Y 1 B ASP -166 ? B ASP 176  
664  1 Y 1 B GLY -165 ? B GLY 177  
665  1 Y 1 B GLY -164 ? B GLY 178  
666  1 Y 1 B TYR -163 ? B TYR 179  
667  1 Y 1 B ALA -162 ? B ALA 180  
668  1 Y 1 B PHE -161 ? B PHE 181  
669  1 Y 1 B LYS -160 ? B LYS 182  
670  1 Y 1 B TYR -159 ? B TYR 183  
671  1 Y 1 B GLU -158 ? B GLU 184  
672  1 Y 1 B ASN -157 ? B ASN 185  
673  1 Y 1 B GLY -156 ? B GLY 186  
674  1 Y 1 B LYS -155 ? B LYS 187  
675  1 Y 1 B TYR -154 ? B TYR 188  
676  1 Y 1 B ASP -153 ? B ASP 189  
677  1 Y 1 B ILE -152 ? B ILE 190  
678  1 Y 1 B LYS -151 ? B LYS 191  
679  1 Y 1 B ASP -150 ? B ASP 192  
680  1 Y 1 B VAL -149 ? B VAL 193  
681  1 Y 1 B GLY -148 ? B GLY 194  
682  1 Y 1 B VAL -147 ? B VAL 195  
683  1 Y 1 B ASP -146 ? B ASP 196  
684  1 Y 1 B ASN -145 ? B ASN 197  
685  1 Y 1 B ALA -144 ? B ALA 198  
686  1 Y 1 B GLY -143 ? B GLY 199  
687  1 Y 1 B ALA -142 ? B ALA 200  
688  1 Y 1 B LYS -141 ? B LYS 201  
689  1 Y 1 B ALA -140 ? B ALA 202  
690  1 Y 1 B GLY -139 ? B GLY 203  
691  1 Y 1 B LEU -138 ? B LEU 204  
692  1 Y 1 B THR -137 ? B THR 205  
693  1 Y 1 B PHE -136 ? B PHE 206  
694  1 Y 1 B LEU -135 ? B LEU 207  
695  1 Y 1 B VAL -134 ? B VAL 208  
696  1 Y 1 B ASP -133 ? B ASP 209  
697  1 Y 1 B LEU -132 ? B LEU 210  
698  1 Y 1 B ILE -131 ? B ILE 211  
699  1 Y 1 B LYS -130 ? B LYS 212  
700  1 Y 1 B ASN -129 ? B ASN 213  
701  1 Y 1 B LYS -128 ? B LYS 214  
702  1 Y 1 B HIS -127 ? B HIS 215  
703  1 Y 1 B MET -126 ? B MET 216  
704  1 Y 1 B ASN -125 ? B ASN 217  
705  1 Y 1 B ALA -124 ? B ALA 218  
706  1 Y 1 B ASP -123 ? B ASP 219  
707  1 Y 1 B THR -122 ? B THR 220  
708  1 Y 1 B ASP -121 ? B ASP 221  
709  1 Y 1 B TYR -120 ? B TYR 222  
710  1 Y 1 B SER -119 ? B SER 223  
711  1 Y 1 B ILE -118 ? B ILE 224  
712  1 Y 1 B ALA -117 ? B ALA 225  
713  1 Y 1 B GLU -116 ? B GLU 226  
714  1 Y 1 B ALA -115 ? B ALA 227  
715  1 Y 1 B ALA -114 ? B ALA 228  
716  1 Y 1 B PHE -113 ? B PHE 229  
717  1 Y 1 B ASN -112 ? B ASN 230  
718  1 Y 1 B LYS -111 ? B LYS 231  
719  1 Y 1 B GLY -110 ? B GLY 232  
720  1 Y 1 B GLU -109 ? B GLU 233  
721  1 Y 1 B THR -108 ? B THR 234  
722  1 Y 1 B ALA -107 ? B ALA 235  
723  1 Y 1 B MET -106 ? B MET 236  
724  1 Y 1 B THR -105 ? B THR 237  
725  1 Y 1 B ILE -104 ? B ILE 238  
726  1 Y 1 B ASN -103 ? B ASN 239  
727  1 Y 1 B GLY -102 ? B GLY 240  
728  1 Y 1 B PRO -101 ? B PRO 241  
729  1 Y 1 B TRP -100 ? B TRP 242  
730  1 Y 1 B ALA -99  ? B ALA 243  
731  1 Y 1 B TRP -98  ? B TRP 244  
732  1 Y 1 B SER -97  ? B SER 245  
733  1 Y 1 B ASN -96  ? B ASN 246  
734  1 Y 1 B ILE -95  ? B ILE 247  
735  1 Y 1 B ASP -94  ? B ASP 248  
736  1 Y 1 B THR -93  ? B THR 249  
737  1 Y 1 B SER -92  ? B SER 250  
738  1 Y 1 B LYS -91  ? B LYS 251  
739  1 Y 1 B VAL -90  ? B VAL 252  
740  1 Y 1 B ASN -89  ? B ASN 253  
741  1 Y 1 B TYR -88  ? B TYR 254  
742  1 Y 1 B GLY -87  ? B GLY 255  
743  1 Y 1 B VAL -86  ? B VAL 256  
744  1 Y 1 B THR -85  ? B THR 257  
745  1 Y 1 B VAL -84  ? B VAL 258  
746  1 Y 1 B LEU -83  ? B LEU 259  
747  1 Y 1 B PRO -82  ? B PRO 260  
748  1 Y 1 B THR -81  ? B THR 261  
749  1 Y 1 B PHE -80  ? B PHE 262  
750  1 Y 1 B LYS -79  ? B LYS 263  
751  1 Y 1 B GLY -78  ? B GLY 264  
752  1 Y 1 B GLN -77  ? B GLN 265  
753  1 Y 1 B PRO -76  ? B PRO 266  
754  1 Y 1 B SER -75  ? B SER 267  
755  1 Y 1 B LYS -74  ? B LYS 268  
756  1 Y 1 B PRO -73  ? B PRO 269  
757  1 Y 1 B PHE -72  ? B PHE 270  
758  1 Y 1 B VAL -71  ? B VAL 271  
759  1 Y 1 B GLY -70  ? B GLY 272  
760  1 Y 1 B VAL -69  ? B VAL 273  
761  1 Y 1 B LEU -68  ? B LEU 274  
762  1 Y 1 B SER -67  ? B SER 275  
763  1 Y 1 B ALA -66  ? B ALA 276  
764  1 Y 1 B GLY -65  ? B GLY 277  
765  1 Y 1 B ILE -64  ? B ILE 278  
766  1 Y 1 B ASN -63  ? B ASN 279  
767  1 Y 1 B ALA -62  ? B ALA 280  
768  1 Y 1 B ALA -61  ? B ALA 281  
769  1 Y 1 B SER -60  ? B SER 282  
770  1 Y 1 B PRO -59  ? B PRO 283  
771  1 Y 1 B ASN -58  ? B ASN 284  
772  1 Y 1 B LYS -57  ? B LYS 285  
773  1 Y 1 B GLU -56  ? B GLU 286  
774  1 Y 1 B LEU -55  ? B LEU 287  
775  1 Y 1 B ALA -54  ? B ALA 288  
776  1 Y 1 B LYS -53  ? B LYS 289  
777  1 Y 1 B GLU -52  ? B GLU 290  
778  1 Y 1 B PHE -51  ? B PHE 291  
779  1 Y 1 B LEU -50  ? B LEU 292  
780  1 Y 1 B GLU -49  ? B GLU 293  
781  1 Y 1 B ASN -48  ? B ASN 294  
782  1 Y 1 B TYR -47  ? B TYR 295  
783  1 Y 1 B LEU -46  ? B LEU 296  
784  1 Y 1 B LEU -45  ? B LEU 297  
785  1 Y 1 B THR -44  ? B THR 298  
786  1 Y 1 B ASP -43  ? B ASP 299  
787  1 Y 1 B GLU -42  ? B GLU 300  
788  1 Y 1 B GLY -41  ? B GLY 301  
789  1 Y 1 B LEU -40  ? B LEU 302  
790  1 Y 1 B GLU -39  ? B GLU 303  
791  1 Y 1 B ALA -38  ? B ALA 304  
792  1 Y 1 B VAL -37  ? B VAL 305  
793  1 Y 1 B ASN -36  ? B ASN 306  
794  1 Y 1 B LYS -35  ? B LYS 307  
795  1 Y 1 B ASP -34  ? B ASP 308  
796  1 Y 1 B LYS -33  ? B LYS 309  
797  1 Y 1 B PRO -32  ? B PRO 310  
798  1 Y 1 B LEU -31  ? B LEU 311  
799  1 Y 1 B GLY -30  ? B GLY 312  
800  1 Y 1 B ALA -29  ? B ALA 313  
801  1 Y 1 B VAL -28  ? B VAL 314  
802  1 Y 1 B ALA -27  ? B ALA 315  
803  1 Y 1 B LEU -26  ? B LEU 316  
804  1 Y 1 B LYS -25  ? B LYS 317  
805  1 Y 1 B SER -24  ? B SER 318  
806  1 Y 1 B TYR -23  ? B TYR 319  
807  1 Y 1 B GLU -22  ? B GLU 320  
808  1 Y 1 B GLU -21  ? B GLU 321  
809  1 Y 1 B GLU -20  ? B GLU 322  
810  1 Y 1 B LEU -19  ? B LEU 323  
811  1 Y 1 B ALA -18  ? B ALA 324  
812  1 Y 1 B LYS -17  ? B LYS 325  
813  1 Y 1 B ASP -16  ? B ASP 326  
814  1 Y 1 B PRO -15  ? B PRO 327  
815  1 Y 1 B ARG -14  ? B ARG 328  
816  1 Y 1 B ILE -13  ? B ILE 329  
817  1 Y 1 B ALA -12  ? B ALA 330  
818  1 Y 1 B ALA -11  ? B ALA 331  
819  1 Y 1 B THR -10  ? B THR 332  
820  1 Y 1 B MET -9   ? B MET 333  
821  1 Y 1 B GLU -8   ? B GLU 334  
822  1 Y 1 B ASN -7   ? B ASN 335  
823  1 Y 1 B ALA -6   ? B ALA 336  
824  1 Y 1 B GLN -5   ? B GLN 337  
825  1 Y 1 B LYS -4   ? B LYS 338  
826  1 Y 1 B GLY -3   ? B GLY 339  
827  1 Y 1 B GLU -2   ? B GLU 340  
828  1 Y 1 B ILE -1   ? B ILE 341  
829  1 Y 1 B MET 0    ? B MET 342  
830  1 Y 1 B PRO 1    ? B PRO 343  
831  1 Y 1 B ASN 2    ? B ASN 344  
832  1 Y 1 B ILE 3    ? B ILE 345  
833  1 Y 1 B PRO 4    ? B PRO 346  
834  1 Y 1 B GLN 5    ? B GLN 347  
835  1 Y 1 B MET 6    ? B MET 348  
836  1 Y 1 B SER 7    ? B SER 349  
837  1 Y 1 B ALA 8    ? B ALA 350  
838  1 Y 1 B PHE 9    ? B PHE 351  
839  1 Y 1 B TRP 10   ? B TRP 352  
840  1 Y 1 B TYR 11   ? B TYR 353  
841  1 Y 1 B ALA 12   ? B ALA 354  
842  1 Y 1 B VAL 13   ? B VAL 355  
843  1 Y 1 B ARG 14   ? B ARG 356  
844  1 Y 1 B THR 15   ? B THR 357  
845  1 Y 1 B ALA 16   ? B ALA 358  
846  1 Y 1 B VAL 17   ? B VAL 359  
847  1 Y 1 B ILE 18   ? B ILE 360  
848  1 Y 1 B ASN 19   ? B ASN 361  
849  1 Y 1 B ALA 20   ? B ALA 362  
850  1 Y 1 B ALA 21   ? B ALA 363  
851  1 Y 1 B SER 22   ? B SER 364  
852  1 Y 1 B GLY 23   ? B GLY 365  
853  1 Y 1 B ARG 24   ? B ARG 366  
854  1 Y 1 B GLN 25   ? B GLN 367  
855  1 Y 1 B THR 26   ? B THR 368  
856  1 Y 1 B VAL 27   ? B VAL 369  
857  1 Y 1 B ASP 28   ? B ASP 370  
858  1 Y 1 B GLU 29   ? B GLU 371  
859  1 Y 1 B ALA 30   ? B ALA 372  
860  1 Y 1 B LEU 31   ? B LEU 373  
861  1 Y 1 B LYS 32   ? B LYS 374  
862  1 Y 1 B ASP 33   ? B ASP 375  
863  1 Y 1 B ALA 34   ? B ALA 376  
864  1 Y 1 B GLN 35   ? B GLN 377  
865  1 Y 1 B THR 36   ? B THR 378  
866  1 Y 1 B GLY 37   ? B GLY 379  
867  1 Y 1 B THR 38   ? B THR 380  
868  1 Y 1 B ASP 39   ? B ASP 381  
869  1 Y 1 B TYR 40   ? B TYR 382  
870  1 Y 1 B ASP 41   ? B ASP 383  
871  1 Y 1 B ILE 42   ? B ILE 384  
872  1 Y 1 B PRO 43   ? B PRO 385  
873  1 Y 1 B THR 44   ? B THR 386  
874  1 Y 1 B THR 45   ? B THR 387  
875  1 Y 1 B LEU 46   ? B LEU 388  
876  1 Y 1 B GLU 47   ? B GLU 389  
877  1 Y 1 B VAL 48   ? B VAL 390  
878  1 Y 1 B LEU 49   ? B LEU 391  
879  1 Y 1 B PHE 50   ? B PHE 392  
880  1 Y 1 B GLN 51   ? B GLN 393  
881  1 Y 1 B GLY 52   ? B GLY 394  
882  1 Y 1 B PRO 53   ? B PRO 395  
883  1 Y 1 B LEU 54   ? B LEU 396  
884  1 Y 1 B GLY 55   ? B GLY 397  
885  1 Y 1 B SER 56   ? B SER 398  
886  1 Y 1 B SER 57   ? B SER 399  
887  1 Y 1 B THR 58   ? B THR 400  
888  1 Y 1 B ASP 59   ? B ASP 401  
889  1 Y 1 B ASP 60   ? B ASP 402  
890  1 Y 1 B ILE 61   ? B ILE 403  
891  1 Y 1 B ILE 62   ? B ILE 404  
892  1 Y 1 B TRP 63   ? B TRP 405  
893  1 Y 1 B ASP 64   ? B ASP 406  
894  1 Y 1 B GLN 65   ? B GLN 407  
895  1 Y 1 B LEU 66   ? B LEU 408  
896  1 Y 1 B ILE 67   ? B ILE 409  
897  1 Y 1 B VAL 68   ? B VAL 410  
898  1 Y 1 B LYS 69   ? B LYS 411  
899  1 Y 1 B ARG 70   ? B ARG 412  
900  1 Y 1 B THR 71   ? B THR 413  
901  1 Y 1 B LEU 72   ? B LEU 414  
902  1 Y 1 B ALA 73   ? B ALA 415  
903  1 Y 1 B ASP 74   ? B ASP 416  
904  1 Y 1 B LEU 75   ? B LEU 417  
905  1 Y 1 B LEU 76   ? B LEU 418  
906  1 Y 1 B ILE 77   ? B ILE 419  
907  1 Y 1 B PRO 78   ? B PRO 420  
908  1 Y 1 B ILE 79   ? B ILE 421  
909  1 Y 1 B ASN 80   ? B ASN 422  
910  1 Y 1 B ARG 81   ? B ARG 423  
911  1 Y 1 B GLN 82   ? B GLN 424  
912  1 Y 1 B ILE 83   ? B ILE 425  
913  1 Y 1 B SER 84   ? B SER 426  
914  1 Y 1 B ASP 85   ? B ASP 427  
915  1 Y 1 B ILE 86   ? B ILE 428  
916  1 Y 1 B GLN 87   ? B GLN 429  
917  1 Y 1 B SER 88   ? B SER 430  
918  1 Y 1 B THR 89   ? B THR 431  
919  1 Y 1 B LEU 90   ? B LEU 432  
920  1 Y 1 B SER 91   ? B SER 433  
921  1 Y 1 B GLU 92   ? B GLU 434  
922  1 Y 1 B VAL 93   ? B VAL 435  
923  1 Y 1 B THR 94   ? B THR 436  
924  1 Y 1 B THR 95   ? B THR 437  
925  1 Y 1 B ARG 96   ? B ARG 438  
926  1 Y 1 B VAL 97   ? B VAL 439  
927  1 Y 1 B HIS 98   ? B HIS 440  
928  1 Y 1 B GLU 99   ? B GLU 441  
929  1 Y 1 B ILE 100  ? B ILE 442  
930  1 Y 1 B GLU 101  ? B GLU 443  
931  1 Y 1 B ARG 102  ? B ARG 444  
932  1 Y 1 B GLN 103  ? B GLN 445  
933  1 Y 1 B LEU 104  ? B LEU 446  
934  1 Y 1 B HIS 105  ? B HIS 447  
935  1 Y 1 B GLU 106  ? B GLU 448  
936  1 Y 1 B ILE 107  ? B ILE 449  
937  1 Y 1 B THR 108  ? B THR 450  
938  1 Y 1 B PRO 109  ? B PRO 451  
939  1 Y 1 B VAL 110  ? B VAL 452  
940  1 Y 1 B LEU 111  ? B LEU 453  
941  1 Y 1 B LYS 112  ? B LYS 454  
942  1 Y 1 C MET -341 ? C MET 1    
943  1 Y 1 C GLY -340 ? C GLY 2    
944  1 Y 1 C SER -339 ? C SER 3    
945  1 Y 1 C SER -338 ? C SER 4    
946  1 Y 1 C HIS -337 ? C HIS 5    
947  1 Y 1 C HIS -336 ? C HIS 6    
948  1 Y 1 C HIS -335 ? C HIS 7    
949  1 Y 1 C HIS -334 ? C HIS 8    
950  1 Y 1 C HIS -333 ? C HIS 9    
951  1 Y 1 C HIS -332 ? C HIS 10   
952  1 Y 1 C GLY -331 ? C GLY 11   
953  1 Y 1 C THR -330 ? C THR 12   
954  1 Y 1 C LYS -329 ? C LYS 13   
955  1 Y 1 C THR -328 ? C THR 14   
956  1 Y 1 C GLU -327 ? C GLU 15   
957  1 Y 1 C GLU -326 ? C GLU 16   
958  1 Y 1 C GLY -325 ? C GLY 17   
959  1 Y 1 C LYS -324 ? C LYS 18   
960  1 Y 1 C LEU -323 ? C LEU 19   
961  1 Y 1 C VAL -322 ? C VAL 20   
962  1 Y 1 C ILE -321 ? C ILE 21   
963  1 Y 1 C TRP -320 ? C TRP 22   
964  1 Y 1 C ILE -319 ? C ILE 23   
965  1 Y 1 C ASN -318 ? C ASN 24   
966  1 Y 1 C GLY -317 ? C GLY 25   
967  1 Y 1 C ASP -316 ? C ASP 26   
968  1 Y 1 C LYS -315 ? C LYS 27   
969  1 Y 1 C GLY -314 ? C GLY 28   
970  1 Y 1 C TYR -313 ? C TYR 29   
971  1 Y 1 C ASN -312 ? C ASN 30   
972  1 Y 1 C GLY -311 ? C GLY 31   
973  1 Y 1 C LEU -310 ? C LEU 32   
974  1 Y 1 C ALA -309 ? C ALA 33   
975  1 Y 1 C GLU -308 ? C GLU 34   
976  1 Y 1 C VAL -307 ? C VAL 35   
977  1 Y 1 C GLY -306 ? C GLY 36   
978  1 Y 1 C LYS -305 ? C LYS 37   
979  1 Y 1 C LYS -304 ? C LYS 38   
980  1 Y 1 C PHE -303 ? C PHE 39   
981  1 Y 1 C GLU -302 ? C GLU 40   
982  1 Y 1 C LYS -301 ? C LYS 41   
983  1 Y 1 C ASP -300 ? C ASP 42   
984  1 Y 1 C THR -299 ? C THR 43   
985  1 Y 1 C GLY -298 ? C GLY 44   
986  1 Y 1 C ILE -297 ? C ILE 45   
987  1 Y 1 C LYS -296 ? C LYS 46   
988  1 Y 1 C VAL -295 ? C VAL 47   
989  1 Y 1 C THR -294 ? C THR 48   
990  1 Y 1 C VAL -293 ? C VAL 49   
991  1 Y 1 C GLU -292 ? C GLU 50   
992  1 Y 1 C HIS -291 ? C HIS 51   
993  1 Y 1 C PRO -290 ? C PRO 52   
994  1 Y 1 C ASP -289 ? C ASP 53   
995  1 Y 1 C LYS -288 ? C LYS 54   
996  1 Y 1 C LEU -287 ? C LEU 55   
997  1 Y 1 C GLU -286 ? C GLU 56   
998  1 Y 1 C GLU -285 ? C GLU 57   
999  1 Y 1 C LYS -284 ? C LYS 58   
1000 1 Y 1 C PHE -283 ? C PHE 59   
1001 1 Y 1 C PRO -282 ? C PRO 60   
1002 1 Y 1 C GLN -281 ? C GLN 61   
1003 1 Y 1 C VAL -280 ? C VAL 62   
1004 1 Y 1 C ALA -279 ? C ALA 63   
1005 1 Y 1 C ALA -278 ? C ALA 64   
1006 1 Y 1 C THR -277 ? C THR 65   
1007 1 Y 1 C GLY -276 ? C GLY 66   
1008 1 Y 1 C ASP -275 ? C ASP 67   
1009 1 Y 1 C GLY -274 ? C GLY 68   
1010 1 Y 1 C PRO -273 ? C PRO 69   
1011 1 Y 1 C ASP -272 ? C ASP 70   
1012 1 Y 1 C ILE -271 ? C ILE 71   
1013 1 Y 1 C ILE -270 ? C ILE 72   
1014 1 Y 1 C PHE -269 ? C PHE 73   
1015 1 Y 1 C TRP -268 ? C TRP 74   
1016 1 Y 1 C ALA -267 ? C ALA 75   
1017 1 Y 1 C HIS -266 ? C HIS 76   
1018 1 Y 1 C ASP -265 ? C ASP 77   
1019 1 Y 1 C ARG -264 ? C ARG 78   
1020 1 Y 1 C PHE -263 ? C PHE 79   
1021 1 Y 1 C GLY -262 ? C GLY 80   
1022 1 Y 1 C GLY -261 ? C GLY 81   
1023 1 Y 1 C TYR -260 ? C TYR 82   
1024 1 Y 1 C ALA -259 ? C ALA 83   
1025 1 Y 1 C GLN -258 ? C GLN 84   
1026 1 Y 1 C SER -257 ? C SER 85   
1027 1 Y 1 C GLY -256 ? C GLY 86   
1028 1 Y 1 C LEU -255 ? C LEU 87   
1029 1 Y 1 C LEU -254 ? C LEU 88   
1030 1 Y 1 C ALA -253 ? C ALA 89   
1031 1 Y 1 C GLU -252 ? C GLU 90   
1032 1 Y 1 C ILE -251 ? C ILE 91   
1033 1 Y 1 C THR -250 ? C THR 92   
1034 1 Y 1 C PRO -249 ? C PRO 93   
1035 1 Y 1 C ASP -248 ? C ASP 94   
1036 1 Y 1 C LYS -247 ? C LYS 95   
1037 1 Y 1 C ALA -246 ? C ALA 96   
1038 1 Y 1 C PHE -245 ? C PHE 97   
1039 1 Y 1 C GLN -244 ? C GLN 98   
1040 1 Y 1 C ASP -243 ? C ASP 99   
1041 1 Y 1 C LYS -242 ? C LYS 100  
1042 1 Y 1 C LEU -241 ? C LEU 101  
1043 1 Y 1 C TYR -240 ? C TYR 102  
1044 1 Y 1 C PRO -239 ? C PRO 103  
1045 1 Y 1 C PHE -238 ? C PHE 104  
1046 1 Y 1 C THR -237 ? C THR 105  
1047 1 Y 1 C TRP -236 ? C TRP 106  
1048 1 Y 1 C ASP -235 ? C ASP 107  
1049 1 Y 1 C ALA -234 ? C ALA 108  
1050 1 Y 1 C VAL -233 ? C VAL 109  
1051 1 Y 1 C ARG -232 ? C ARG 110  
1052 1 Y 1 C TYR -231 ? C TYR 111  
1053 1 Y 1 C ASN -230 ? C ASN 112  
1054 1 Y 1 C GLY -229 ? C GLY 113  
1055 1 Y 1 C LYS -228 ? C LYS 114  
1056 1 Y 1 C LEU -227 ? C LEU 115  
1057 1 Y 1 C ILE -226 ? C ILE 116  
1058 1 Y 1 C ALA -225 ? C ALA 117  
1059 1 Y 1 C TYR -224 ? C TYR 118  
1060 1 Y 1 C PRO -223 ? C PRO 119  
1061 1 Y 1 C ILE -222 ? C ILE 120  
1062 1 Y 1 C ALA -221 ? C ALA 121  
1063 1 Y 1 C VAL -220 ? C VAL 122  
1064 1 Y 1 C GLU -219 ? C GLU 123  
1065 1 Y 1 C ALA -218 ? C ALA 124  
1066 1 Y 1 C LEU -217 ? C LEU 125  
1067 1 Y 1 C SER -216 ? C SER 126  
1068 1 Y 1 C LEU -215 ? C LEU 127  
1069 1 Y 1 C ILE -214 ? C ILE 128  
1070 1 Y 1 C TYR -213 ? C TYR 129  
1071 1 Y 1 C ASN -212 ? C ASN 130  
1072 1 Y 1 C LYS -211 ? C LYS 131  
1073 1 Y 1 C ASP -210 ? C ASP 132  
1074 1 Y 1 C LEU -209 ? C LEU 133  
1075 1 Y 1 C LEU -208 ? C LEU 134  
1076 1 Y 1 C PRO -207 ? C PRO 135  
1077 1 Y 1 C ASN -206 ? C ASN 136  
1078 1 Y 1 C PRO -205 ? C PRO 137  
1079 1 Y 1 C PRO -204 ? C PRO 138  
1080 1 Y 1 C LYS -203 ? C LYS 139  
1081 1 Y 1 C THR -202 ? C THR 140  
1082 1 Y 1 C TRP -201 ? C TRP 141  
1083 1 Y 1 C GLU -200 ? C GLU 142  
1084 1 Y 1 C GLU -199 ? C GLU 143  
1085 1 Y 1 C ILE -198 ? C ILE 144  
1086 1 Y 1 C PRO -197 ? C PRO 145  
1087 1 Y 1 C ALA -196 ? C ALA 146  
1088 1 Y 1 C LEU -195 ? C LEU 147  
1089 1 Y 1 C ASP -194 ? C ASP 148  
1090 1 Y 1 C LYS -193 ? C LYS 149  
1091 1 Y 1 C GLU -192 ? C GLU 150  
1092 1 Y 1 C LEU -191 ? C LEU 151  
1093 1 Y 1 C LYS -190 ? C LYS 152  
1094 1 Y 1 C ALA -189 ? C ALA 153  
1095 1 Y 1 C LYS -188 ? C LYS 154  
1096 1 Y 1 C GLY -187 ? C GLY 155  
1097 1 Y 1 C LYS -186 ? C LYS 156  
1098 1 Y 1 C SER -185 ? C SER 157  
1099 1 Y 1 C ALA -184 ? C ALA 158  
1100 1 Y 1 C LEU -183 ? C LEU 159  
1101 1 Y 1 C MET -182 ? C MET 160  
1102 1 Y 1 C PHE -181 ? C PHE 161  
1103 1 Y 1 C ASN -180 ? C ASN 162  
1104 1 Y 1 C LEU -179 ? C LEU 163  
1105 1 Y 1 C GLN -178 ? C GLN 164  
1106 1 Y 1 C GLU -177 ? C GLU 165  
1107 1 Y 1 C PRO -176 ? C PRO 166  
1108 1 Y 1 C TYR -175 ? C TYR 167  
1109 1 Y 1 C PHE -174 ? C PHE 168  
1110 1 Y 1 C THR -173 ? C THR 169  
1111 1 Y 1 C TRP -172 ? C TRP 170  
1112 1 Y 1 C PRO -171 ? C PRO 171  
1113 1 Y 1 C LEU -170 ? C LEU 172  
1114 1 Y 1 C ILE -169 ? C ILE 173  
1115 1 Y 1 C ALA -168 ? C ALA 174  
1116 1 Y 1 C ALA -167 ? C ALA 175  
1117 1 Y 1 C ASP -166 ? C ASP 176  
1118 1 Y 1 C GLY -165 ? C GLY 177  
1119 1 Y 1 C GLY -164 ? C GLY 178  
1120 1 Y 1 C TYR -163 ? C TYR 179  
1121 1 Y 1 C ALA -162 ? C ALA 180  
1122 1 Y 1 C PHE -161 ? C PHE 181  
1123 1 Y 1 C LYS -160 ? C LYS 182  
1124 1 Y 1 C TYR -159 ? C TYR 183  
1125 1 Y 1 C GLU -158 ? C GLU 184  
1126 1 Y 1 C ASN -157 ? C ASN 185  
1127 1 Y 1 C GLY -156 ? C GLY 186  
1128 1 Y 1 C LYS -155 ? C LYS 187  
1129 1 Y 1 C TYR -154 ? C TYR 188  
1130 1 Y 1 C ASP -153 ? C ASP 189  
1131 1 Y 1 C ILE -152 ? C ILE 190  
1132 1 Y 1 C LYS -151 ? C LYS 191  
1133 1 Y 1 C ASP -150 ? C ASP 192  
1134 1 Y 1 C VAL -149 ? C VAL 193  
1135 1 Y 1 C GLY -148 ? C GLY 194  
1136 1 Y 1 C VAL -147 ? C VAL 195  
1137 1 Y 1 C ASP -146 ? C ASP 196  
1138 1 Y 1 C ASN -145 ? C ASN 197  
1139 1 Y 1 C ALA -144 ? C ALA 198  
1140 1 Y 1 C GLY -143 ? C GLY 199  
1141 1 Y 1 C ALA -142 ? C ALA 200  
1142 1 Y 1 C LYS -141 ? C LYS 201  
1143 1 Y 1 C ALA -140 ? C ALA 202  
1144 1 Y 1 C GLY -139 ? C GLY 203  
1145 1 Y 1 C LEU -138 ? C LEU 204  
1146 1 Y 1 C THR -137 ? C THR 205  
1147 1 Y 1 C PHE -136 ? C PHE 206  
1148 1 Y 1 C LEU -135 ? C LEU 207  
1149 1 Y 1 C VAL -134 ? C VAL 208  
1150 1 Y 1 C ASP -133 ? C ASP 209  
1151 1 Y 1 C LEU -132 ? C LEU 210  
1152 1 Y 1 C ILE -131 ? C ILE 211  
1153 1 Y 1 C LYS -130 ? C LYS 212  
1154 1 Y 1 C ASN -129 ? C ASN 213  
1155 1 Y 1 C LYS -128 ? C LYS 214  
1156 1 Y 1 C HIS -127 ? C HIS 215  
1157 1 Y 1 C MET -126 ? C MET 216  
1158 1 Y 1 C ASN -125 ? C ASN 217  
1159 1 Y 1 C ALA -124 ? C ALA 218  
1160 1 Y 1 C ASP -123 ? C ASP 219  
1161 1 Y 1 C THR -122 ? C THR 220  
1162 1 Y 1 C ASP -121 ? C ASP 221  
1163 1 Y 1 C TYR -120 ? C TYR 222  
1164 1 Y 1 C SER -119 ? C SER 223  
1165 1 Y 1 C ILE -118 ? C ILE 224  
1166 1 Y 1 C ALA -117 ? C ALA 225  
1167 1 Y 1 C GLU -116 ? C GLU 226  
1168 1 Y 1 C ALA -115 ? C ALA 227  
1169 1 Y 1 C ALA -114 ? C ALA 228  
1170 1 Y 1 C PHE -113 ? C PHE 229  
1171 1 Y 1 C ASN -112 ? C ASN 230  
1172 1 Y 1 C LYS -111 ? C LYS 231  
1173 1 Y 1 C GLY -110 ? C GLY 232  
1174 1 Y 1 C GLU -109 ? C GLU 233  
1175 1 Y 1 C THR -108 ? C THR 234  
1176 1 Y 1 C ALA -107 ? C ALA 235  
1177 1 Y 1 C MET -106 ? C MET 236  
1178 1 Y 1 C THR -105 ? C THR 237  
1179 1 Y 1 C ILE -104 ? C ILE 238  
1180 1 Y 1 C ASN -103 ? C ASN 239  
1181 1 Y 1 C GLY -102 ? C GLY 240  
1182 1 Y 1 C PRO -101 ? C PRO 241  
1183 1 Y 1 C TRP -100 ? C TRP 242  
1184 1 Y 1 C ALA -99  ? C ALA 243  
1185 1 Y 1 C TRP -98  ? C TRP 244  
1186 1 Y 1 C SER -97  ? C SER 245  
1187 1 Y 1 C ASN -96  ? C ASN 246  
1188 1 Y 1 C ILE -95  ? C ILE 247  
1189 1 Y 1 C ASP -94  ? C ASP 248  
1190 1 Y 1 C THR -93  ? C THR 249  
1191 1 Y 1 C SER -92  ? C SER 250  
1192 1 Y 1 C LYS -91  ? C LYS 251  
1193 1 Y 1 C VAL -90  ? C VAL 252  
1194 1 Y 1 C ASN -89  ? C ASN 253  
1195 1 Y 1 C TYR -88  ? C TYR 254  
1196 1 Y 1 C GLY -87  ? C GLY 255  
1197 1 Y 1 C VAL -86  ? C VAL 256  
1198 1 Y 1 C THR -85  ? C THR 257  
1199 1 Y 1 C VAL -84  ? C VAL 258  
1200 1 Y 1 C LEU -83  ? C LEU 259  
1201 1 Y 1 C PRO -82  ? C PRO 260  
1202 1 Y 1 C THR -81  ? C THR 261  
1203 1 Y 1 C PHE -80  ? C PHE 262  
1204 1 Y 1 C LYS -79  ? C LYS 263  
1205 1 Y 1 C GLY -78  ? C GLY 264  
1206 1 Y 1 C GLN -77  ? C GLN 265  
1207 1 Y 1 C PRO -76  ? C PRO 266  
1208 1 Y 1 C SER -75  ? C SER 267  
1209 1 Y 1 C LYS -74  ? C LYS 268  
1210 1 Y 1 C PRO -73  ? C PRO 269  
1211 1 Y 1 C PHE -72  ? C PHE 270  
1212 1 Y 1 C VAL -71  ? C VAL 271  
1213 1 Y 1 C GLY -70  ? C GLY 272  
1214 1 Y 1 C VAL -69  ? C VAL 273  
1215 1 Y 1 C LEU -68  ? C LEU 274  
1216 1 Y 1 C SER -67  ? C SER 275  
1217 1 Y 1 C ALA -66  ? C ALA 276  
1218 1 Y 1 C GLY -65  ? C GLY 277  
1219 1 Y 1 C ILE -64  ? C ILE 278  
1220 1 Y 1 C ASN -63  ? C ASN 279  
1221 1 Y 1 C ALA -62  ? C ALA 280  
1222 1 Y 1 C ALA -61  ? C ALA 281  
1223 1 Y 1 C SER -60  ? C SER 282  
1224 1 Y 1 C PRO -59  ? C PRO 283  
1225 1 Y 1 C ASN -58  ? C ASN 284  
1226 1 Y 1 C LYS -57  ? C LYS 285  
1227 1 Y 1 C GLU -56  ? C GLU 286  
1228 1 Y 1 C LEU -55  ? C LEU 287  
1229 1 Y 1 C ALA -54  ? C ALA 288  
1230 1 Y 1 C LYS -53  ? C LYS 289  
1231 1 Y 1 C GLU -52  ? C GLU 290  
1232 1 Y 1 C PHE -51  ? C PHE 291  
1233 1 Y 1 C LEU -50  ? C LEU 292  
1234 1 Y 1 C GLU -49  ? C GLU 293  
1235 1 Y 1 C ASN -48  ? C ASN 294  
1236 1 Y 1 C TYR -47  ? C TYR 295  
1237 1 Y 1 C LEU -46  ? C LEU 296  
1238 1 Y 1 C LEU -45  ? C LEU 297  
1239 1 Y 1 C THR -44  ? C THR 298  
1240 1 Y 1 C ASP -43  ? C ASP 299  
1241 1 Y 1 C GLU -42  ? C GLU 300  
1242 1 Y 1 C GLY -41  ? C GLY 301  
1243 1 Y 1 C LEU -40  ? C LEU 302  
1244 1 Y 1 C GLU -39  ? C GLU 303  
1245 1 Y 1 C ALA -38  ? C ALA 304  
1246 1 Y 1 C VAL -37  ? C VAL 305  
1247 1 Y 1 C ASN -36  ? C ASN 306  
1248 1 Y 1 C LYS -35  ? C LYS 307  
1249 1 Y 1 C ASP -34  ? C ASP 308  
1250 1 Y 1 C LYS -33  ? C LYS 309  
1251 1 Y 1 C PRO -32  ? C PRO 310  
1252 1 Y 1 C LEU -31  ? C LEU 311  
1253 1 Y 1 C GLY -30  ? C GLY 312  
1254 1 Y 1 C ALA -29  ? C ALA 313  
1255 1 Y 1 C VAL -28  ? C VAL 314  
1256 1 Y 1 C ALA -27  ? C ALA 315  
1257 1 Y 1 C LEU -26  ? C LEU 316  
1258 1 Y 1 C LYS -25  ? C LYS 317  
1259 1 Y 1 C SER -24  ? C SER 318  
1260 1 Y 1 C TYR -23  ? C TYR 319  
1261 1 Y 1 C GLU -22  ? C GLU 320  
1262 1 Y 1 C GLU -21  ? C GLU 321  
1263 1 Y 1 C GLU -20  ? C GLU 322  
1264 1 Y 1 C LEU -19  ? C LEU 323  
1265 1 Y 1 C ALA -18  ? C ALA 324  
1266 1 Y 1 C LYS -17  ? C LYS 325  
1267 1 Y 1 C ASP -16  ? C ASP 326  
1268 1 Y 1 C PRO -15  ? C PRO 327  
1269 1 Y 1 C ARG -14  ? C ARG 328  
1270 1 Y 1 C ILE -13  ? C ILE 329  
1271 1 Y 1 C ALA -12  ? C ALA 330  
1272 1 Y 1 C ALA -11  ? C ALA 331  
1273 1 Y 1 C THR -10  ? C THR 332  
1274 1 Y 1 C MET -9   ? C MET 333  
1275 1 Y 1 C GLU -8   ? C GLU 334  
1276 1 Y 1 C ASN -7   ? C ASN 335  
1277 1 Y 1 C ALA -6   ? C ALA 336  
1278 1 Y 1 C GLN -5   ? C GLN 337  
1279 1 Y 1 C LYS -4   ? C LYS 338  
1280 1 Y 1 C GLY -3   ? C GLY 339  
1281 1 Y 1 C GLU -2   ? C GLU 340  
1282 1 Y 1 C ILE -1   ? C ILE 341  
1283 1 Y 1 C MET 0    ? C MET 342  
1284 1 Y 1 C PRO 1    ? C PRO 343  
1285 1 Y 1 C ASN 2    ? C ASN 344  
1286 1 Y 1 C ILE 3    ? C ILE 345  
1287 1 Y 1 C PRO 4    ? C PRO 346  
1288 1 Y 1 C GLN 5    ? C GLN 347  
1289 1 Y 1 C MET 6    ? C MET 348  
1290 1 Y 1 C SER 7    ? C SER 349  
1291 1 Y 1 C ALA 8    ? C ALA 350  
1292 1 Y 1 C PHE 9    ? C PHE 351  
1293 1 Y 1 C TRP 10   ? C TRP 352  
1294 1 Y 1 C TYR 11   ? C TYR 353  
1295 1 Y 1 C ALA 12   ? C ALA 354  
1296 1 Y 1 C VAL 13   ? C VAL 355  
1297 1 Y 1 C ARG 14   ? C ARG 356  
1298 1 Y 1 C THR 15   ? C THR 357  
1299 1 Y 1 C ALA 16   ? C ALA 358  
1300 1 Y 1 C VAL 17   ? C VAL 359  
1301 1 Y 1 C ILE 18   ? C ILE 360  
1302 1 Y 1 C ASN 19   ? C ASN 361  
1303 1 Y 1 C ALA 20   ? C ALA 362  
1304 1 Y 1 C ALA 21   ? C ALA 363  
1305 1 Y 1 C SER 22   ? C SER 364  
1306 1 Y 1 C GLY 23   ? C GLY 365  
1307 1 Y 1 C ARG 24   ? C ARG 366  
1308 1 Y 1 C GLN 25   ? C GLN 367  
1309 1 Y 1 C THR 26   ? C THR 368  
1310 1 Y 1 C VAL 27   ? C VAL 369  
1311 1 Y 1 C ASP 28   ? C ASP 370  
1312 1 Y 1 C GLU 29   ? C GLU 371  
1313 1 Y 1 C ALA 30   ? C ALA 372  
1314 1 Y 1 C LEU 31   ? C LEU 373  
1315 1 Y 1 C LYS 32   ? C LYS 374  
1316 1 Y 1 C ASP 33   ? C ASP 375  
1317 1 Y 1 C ALA 34   ? C ALA 376  
1318 1 Y 1 C GLN 35   ? C GLN 377  
1319 1 Y 1 C THR 36   ? C THR 378  
1320 1 Y 1 C GLY 37   ? C GLY 379  
1321 1 Y 1 C THR 38   ? C THR 380  
1322 1 Y 1 C ASP 39   ? C ASP 381  
1323 1 Y 1 C TYR 40   ? C TYR 382  
1324 1 Y 1 C ASP 41   ? C ASP 383  
1325 1 Y 1 C ILE 42   ? C ILE 384  
1326 1 Y 1 C PRO 43   ? C PRO 385  
1327 1 Y 1 C THR 44   ? C THR 386  
1328 1 Y 1 C THR 45   ? C THR 387  
1329 1 Y 1 C LEU 46   ? C LEU 388  
1330 1 Y 1 C GLU 47   ? C GLU 389  
1331 1 Y 1 C VAL 48   ? C VAL 390  
1332 1 Y 1 C LEU 49   ? C LEU 391  
1333 1 Y 1 C PHE 50   ? C PHE 392  
1334 1 Y 1 C GLN 51   ? C GLN 393  
1335 1 Y 1 C GLY 52   ? C GLY 394  
1336 1 Y 1 C PRO 53   ? C PRO 395  
1337 1 Y 1 C LEU 54   ? C LEU 396  
1338 1 Y 1 C GLY 55   ? C GLY 397  
1339 1 Y 1 C SER 56   ? C SER 398  
1340 1 Y 1 C SER 57   ? C SER 399  
1341 1 Y 1 C THR 58   ? C THR 400  
1342 1 Y 1 C ASP 59   ? C ASP 401  
1343 1 Y 1 C ASP 60   ? C ASP 402  
1344 1 Y 1 C ILE 61   ? C ILE 403  
1345 1 Y 1 C ILE 62   ? C ILE 404  
1346 1 Y 1 C TRP 63   ? C TRP 405  
1347 1 Y 1 C ASP 64   ? C ASP 406  
1348 1 Y 1 C GLN 65   ? C GLN 407  
1349 1 Y 1 C LEU 66   ? C LEU 408  
1350 1 Y 1 C ILE 67   ? C ILE 409  
1351 1 Y 1 C VAL 68   ? C VAL 410  
1352 1 Y 1 C LYS 69   ? C LYS 411  
1353 1 Y 1 C ARG 70   ? C ARG 412  
1354 1 Y 1 C THR 71   ? C THR 413  
1355 1 Y 1 C LEU 72   ? C LEU 414  
1356 1 Y 1 C ALA 73   ? C ALA 415  
1357 1 Y 1 C ASP 74   ? C ASP 416  
1358 1 Y 1 C LEU 75   ? C LEU 417  
1359 1 Y 1 C LEU 76   ? C LEU 418  
1360 1 Y 1 C ILE 77   ? C ILE 419  
1361 1 Y 1 C PRO 78   ? C PRO 420  
1362 1 Y 1 C ILE 79   ? C ILE 421  
1363 1 Y 1 C ASN 80   ? C ASN 422  
1364 1 Y 1 C ARG 81   ? C ARG 423  
1365 1 Y 1 C GLN 82   ? C GLN 424  
1366 1 Y 1 C ILE 83   ? C ILE 425  
1367 1 Y 1 C SER 84   ? C SER 426  
1368 1 Y 1 C ASP 85   ? C ASP 427  
1369 1 Y 1 C ILE 86   ? C ILE 428  
1370 1 Y 1 C GLN 87   ? C GLN 429  
1371 1 Y 1 C SER 88   ? C SER 430  
1372 1 Y 1 C THR 89   ? C THR 431  
1373 1 Y 1 C LEU 90   ? C LEU 432  
1374 1 Y 1 C SER 91   ? C SER 433  
1375 1 Y 1 C GLU 92   ? C GLU 434  
1376 1 Y 1 C VAL 93   ? C VAL 435  
1377 1 Y 1 C THR 94   ? C THR 436  
1378 1 Y 1 C THR 95   ? C THR 437  
1379 1 Y 1 C ARG 96   ? C ARG 438  
1380 1 Y 1 C VAL 97   ? C VAL 439  
1381 1 Y 1 C HIS 98   ? C HIS 440  
1382 1 Y 1 C GLU 99   ? C GLU 441  
1383 1 Y 1 C ILE 100  ? C ILE 442  
1384 1 Y 1 C GLU 101  ? C GLU 443  
1385 1 Y 1 C ARG 102  ? C ARG 444  
1386 1 Y 1 C GLN 103  ? C GLN 445  
1387 1 Y 1 C LEU 104  ? C LEU 446  
1388 1 Y 1 C HIS 105  ? C HIS 447  
1389 1 Y 1 C GLU 106  ? C GLU 448  
1390 1 Y 1 C ILE 107  ? C ILE 449  
1391 1 Y 1 C THR 108  ? C THR 450  
1392 1 Y 1 C PRO 109  ? C PRO 451  
1393 1 Y 1 C GLN 173  ? C GLN 515  
1394 1 Y 1 C ALA 174  ? C ALA 516  
1395 1 Y 1 C CYS 175  ? C CYS 517  
1396 1 Y 1 C SER 176  ? C SER 518  
1397 1 Y 1 C LYS 177  ? C LYS 519  
1398 1 Y 1 C GLY 178  ? C GLY 520  
1399 1 Y 1 C THR 179  ? C THR 521  
1400 1 Y 1 C MET 180  ? C MET 522  
1401 1 Y 1 C VAL 181  ? C VAL 523  
1402 1 Y 1 C LYS 182  ? C LYS 524  
1403 1 Y 1 C ASN 183  ? C ASN 525  
1404 1 Y 1 C ALA 184  ? C ALA 526  
1405 1 Y 1 C THR 185  ? C THR 527  
1406 1 Y 1 C THR 186  ? C THR 528  
1407 1 Y 1 C ASP 187  ? C ASP 529  
1408 1 Y 1 C ALA 188  ? C ALA 530  
1409 1 Y 1 C ALA 189  ? C ALA 531  
1410 1 Y 1 C ASP 190  ? C ASP 532  
1411 1 Y 1 C LYS 191  ? C LYS 533  
1412 1 Y 1 C MET 192  ? C MET 534  
1413 1 Y 1 C SER 193  ? C SER 535  
1414 1 Y 1 C LYS 194  ? C LYS 536  
1415 1 Y 1 C VAL 195  ? C VAL 537  
1416 1 Y 1 C LEU 196  ? C LEU 538  
1417 1 Y 1 C GLU 197  ? C GLU 539  
1418 1 Y 1 C LEU 198  ? C LEU 540  
1419 1 Y 1 C SER 199  ? C SER 541  
1420 1 Y 1 C GLU 200  ? C GLU 542  
1421 1 Y 1 C GLU 201  ? C GLU 543  
1422 1 Y 1 C THR 202  ? C THR 544  
1423 1 Y 1 C PHE 203  ? C PHE 545  
1424 1 Y 1 C SER 204  ? C SER 546  
1425 1 Y 1 C LYS 205  ? C LYS 547  
1426 1 Y 1 C PRO 206  ? C PRO 548  
1427 1 Y 1 C ASN 207  ? C ASN 549  
1428 1 Y 1 C LEU 208  ? C LEU 550  
1429 1 Y 1 C SER 209  ? C SER 551  
1430 1 Y 1 C ALA 210  ? C ALA 552  
1431 1 Y 1 C LYS 211  ? C LYS 553  
1432 1 Y 1 C ASP 212  ? C ASP 554  
1433 1 Y 1 C LEU 213  ? C LEU 555  
1434 1 Y 1 C ALA 214  ? C ALA 556  
1435 1 Y 1 C LEU 215  ? C LEU 557  
1436 1 Y 1 C LEU 216  ? C LEU 558  
1437 1 Y 1 C LEU 217  ? C LEU 559  
1438 1 Y 1 C PHE 218  ? C PHE 560  
1439 1 Y 1 C THR 219  ? C THR 561  
1440 1 Y 1 C HIS 220  ? C HIS 562  
1441 1 Y 1 C LEU 221  ? C LEU 563  
1442 1 Y 1 C PRO 222  ? C PRO 564  
1443 1 Y 1 C GLY 223  ? C GLY 565  
1444 1 Y 1 C ASN 224  ? C ASN 566  
1445 1 Y 1 C ASN 225  ? C ASN 567  
1446 1 Y 1 C THR 226  ? C THR 568  
1447 1 Y 1 C PRO 227  ? C PRO 569  
1448 1 Y 1 C PHE 228  ? C PHE 570  
1449 1 Y 1 C HIS 229  ? C HIS 571  
1450 1 Y 1 C ILE 230  ? C ILE 572  
1451 1 Y 1 C LEU 231  ? C LEU 573  
1452 1 Y 1 C ALA 232  ? C ALA 574  
1453 1 Y 1 C GLN 233  ? C GLN 575  
1454 1 Y 1 C VAL 234  ? C VAL 576  
1455 1 Y 1 C LEU 235  ? C LEU 577  
1456 1 Y 1 C SER 236  ? C SER 578  
1457 1 Y 1 C LYS 237  ? C LYS 579  
1458 1 Y 1 C ILE 238  ? C ILE 580  
1459 1 Y 1 C ALA 239  ? C ALA 581  
1460 1 Y 1 C TYR 240  ? C TYR 582  
1461 1 Y 1 C LYS 241  ? C LYS 583  
1462 1 Y 1 C SER 242  ? C SER 584  
1463 1 Y 1 C GLY 243  ? C GLY 585  
1464 1 Y 1 C LYS 244  ? C LYS 586  
1465 1 Y 1 C SER 245  ? C SER 587  
1466 1 Y 1 C GLY 246  ? C GLY 588  
1467 1 Y 1 C ALA 247  ? C ALA 589  
1468 1 Y 1 C PHE 248  ? C PHE 590  
1469 1 Y 1 C LEU 249  ? C LEU 591  
1470 1 Y 1 C ASP 250  ? C ASP 592  
1471 1 Y 1 C ALA 251  ? C ALA 593  
1472 1 Y 1 C PHE 252  ? C PHE 594  
1473 1 Y 1 C HIS 253  ? C HIS 595  
1474 1 Y 1 C GLN 254  ? C GLN 596  
1475 1 Y 1 C ILE 255  ? C ILE 597  
1476 1 Y 1 C LEU 256  ? C LEU 598  
1477 1 Y 1 C SER 257  ? C SER 599  
1478 1 Y 1 C GLU 258  ? C GLU 600  
1479 1 Y 1 C GLY 259  ? C GLY 601  
1480 1 Y 1 C GLU 260  ? C GLU 602  
1481 1 Y 1 C ASN 261  ? C ASN 603  
1482 1 Y 1 C ALA 262  ? C ALA 604  
1483 1 Y 1 C GLN 263  ? C GLN 605  
1484 1 Y 1 C ALA 264  ? C ALA 606  
1485 1 Y 1 C ALA 265  ? C ALA 607  
1486 1 Y 1 C LEU 266  ? C LEU 608  
1487 1 Y 1 C THR 267  ? C THR 609  
1488 1 Y 1 C ARG 268  ? C ARG 610  
1489 1 Y 1 C LEU 269  ? C LEU 611  
1490 1 Y 1 C SER 270  ? C SER 612  
1491 1 Y 1 C ARG 271  ? C ARG 613  
1492 1 Y 1 C THR 272  ? C THR 614  
1493 1 Y 1 C PHE 273  ? C PHE 615  
1494 1 Y 1 C ASP 274  ? C ASP 616  
1495 1 Y 1 C ALA 275  ? C ALA 617  
1496 1 Y 1 C PHE 276  ? C PHE 618  
1497 1 Y 1 C LEU 277  ? C LEU 619  
1498 1 Y 1 C GLY 278  ? C GLY 620  
1499 1 Y 1 C VAL 279  ? C VAL 621  
1500 1 Y 1 C VAL 280  ? C VAL 622  
1501 1 Y 1 C PRO 281  ? C PRO 623  
1502 1 Y 1 C PRO 282  ? C PRO 624  
1503 1 Y 1 C VAL 283  ? C VAL 625  
1504 1 Y 1 C ILE 284  ? C ILE 626  
1505 1 Y 1 C ARG 285  ? C ARG 627  
1506 1 Y 1 C VAL 286  ? C VAL 628  
1507 1 Y 1 C LYS 287  ? C LYS 629  
1508 1 Y 1 C ASN 288  ? C ASN 630  
1509 1 Y 1 C PHE 289  ? C PHE 631  
1510 1 Y 1 C GLN 290  ? C GLN 632  
1511 1 Y 1 C THR 291  ? C THR 633  
1512 1 Y 1 C VAL 292  ? C VAL 634  
1513 1 Y 1 C PRO 293  ? C PRO 635  
1514 1 Y 1 C ARG 294  ? C ARG 636  
1515 1 Y 1 C PRO 295  ? C PRO 637  
1516 1 Y 1 C CYS 296  ? C CYS 638  
1517 1 Y 1 C GLN 297  ? C GLN 639  
1518 1 Y 1 C LYS 298  ? C LYS 640  
1519 1 Y 1 C SER 299  ? C SER 641  
1520 1 Y 1 C LEU 300  ? C LEU 642  
1521 1 Y 1 C ARG 301  ? C ARG 643  
1522 1 Y 1 C ALA 302  ? C ALA 644  
1523 1 Y 1 C VAL 303  ? C VAL 645  
1524 1 Y 1 C PRO 304  ? C PRO 646  
1525 1 Y 1 C PRO 305  ? C PRO 647  
1526 1 Y 1 C ASN 306  ? C ASN 648  
1527 1 Y 1 C PRO 307  ? C PRO 649  
1528 1 Y 1 C THR 308  ? C THR 650  
1529 1 Y 1 C ILE 309  ? C ILE 651  
1530 1 Y 1 C ASP 310  ? C ASP 652  
1531 1 Y 1 C LYS 311  ? C LYS 653  
1532 1 Y 1 C GLY 312  ? C GLY 654  
1533 1 Y 1 C TRP 313  ? C TRP 655  
1534 1 Y 1 C VAL 314  ? C VAL 656  
1535 1 Y 1 C CYS 315  ? C CYS 657  
1536 1 Y 1 C VAL 316  ? C VAL 658  
1537 1 Y 1 C TYR 317  ? C TYR 659  
1538 1 Y 1 C SER 318  ? C SER 660  
1539 1 Y 1 C SER 319  ? C SER 661  
1540 1 Y 1 C GLU 320  ? C GLU 662  
1541 1 Y 1 C GLN 321  ? C GLN 663  
1542 1 Y 1 C GLY 322  ? C GLY 664  
1543 1 Y 1 C GLU 323  ? C GLU 665  
1544 1 Y 1 C THR 324  ? C THR 666  
1545 1 Y 1 C ARG 325  ? C ARG 667  
1546 1 Y 1 C ALA 326  ? C ALA 668  
1547 1 Y 1 C LEU 327  ? C LEU 669  
1548 1 Y 1 C LYS 328  ? C LYS 670  
1549 1 Y 1 C ILE 329  ? C ILE 671  
1550 1 Y 1 D MET -341 ? D MET 1    
1551 1 Y 1 D GLY -340 ? D GLY 2    
1552 1 Y 1 D SER -339 ? D SER 3    
1553 1 Y 1 D SER -338 ? D SER 4    
1554 1 Y 1 D HIS -337 ? D HIS 5    
1555 1 Y 1 D HIS -336 ? D HIS 6    
1556 1 Y 1 D HIS -335 ? D HIS 7    
1557 1 Y 1 D HIS -334 ? D HIS 8    
1558 1 Y 1 D HIS -333 ? D HIS 9    
1559 1 Y 1 D HIS -332 ? D HIS 10   
1560 1 Y 1 D GLY -331 ? D GLY 11   
1561 1 Y 1 D THR -330 ? D THR 12   
1562 1 Y 1 D LYS -329 ? D LYS 13   
1563 1 Y 1 D THR -328 ? D THR 14   
1564 1 Y 1 D GLU -327 ? D GLU 15   
1565 1 Y 1 D GLU -326 ? D GLU 16   
1566 1 Y 1 D GLY -325 ? D GLY 17   
1567 1 Y 1 D LYS -324 ? D LYS 18   
1568 1 Y 1 D LEU -323 ? D LEU 19   
1569 1 Y 1 D VAL -322 ? D VAL 20   
1570 1 Y 1 D ILE -321 ? D ILE 21   
1571 1 Y 1 D TRP -320 ? D TRP 22   
1572 1 Y 1 D ILE -319 ? D ILE 23   
1573 1 Y 1 D ASN -318 ? D ASN 24   
1574 1 Y 1 D GLY -317 ? D GLY 25   
1575 1 Y 1 D ASP -316 ? D ASP 26   
1576 1 Y 1 D LYS -315 ? D LYS 27   
1577 1 Y 1 D GLY -314 ? D GLY 28   
1578 1 Y 1 D TYR -313 ? D TYR 29   
1579 1 Y 1 D ASN -312 ? D ASN 30   
1580 1 Y 1 D GLY -311 ? D GLY 31   
1581 1 Y 1 D LEU -310 ? D LEU 32   
1582 1 Y 1 D ALA -309 ? D ALA 33   
1583 1 Y 1 D GLU -308 ? D GLU 34   
1584 1 Y 1 D VAL -307 ? D VAL 35   
1585 1 Y 1 D GLY -306 ? D GLY 36   
1586 1 Y 1 D LYS -305 ? D LYS 37   
1587 1 Y 1 D LYS -304 ? D LYS 38   
1588 1 Y 1 D PHE -303 ? D PHE 39   
1589 1 Y 1 D GLU -302 ? D GLU 40   
1590 1 Y 1 D LYS -301 ? D LYS 41   
1591 1 Y 1 D ASP -300 ? D ASP 42   
1592 1 Y 1 D THR -299 ? D THR 43   
1593 1 Y 1 D GLY -298 ? D GLY 44   
1594 1 Y 1 D ILE -297 ? D ILE 45   
1595 1 Y 1 D LYS -296 ? D LYS 46   
1596 1 Y 1 D VAL -295 ? D VAL 47   
1597 1 Y 1 D THR -294 ? D THR 48   
1598 1 Y 1 D VAL -293 ? D VAL 49   
1599 1 Y 1 D GLU -292 ? D GLU 50   
1600 1 Y 1 D HIS -291 ? D HIS 51   
1601 1 Y 1 D PRO -290 ? D PRO 52   
1602 1 Y 1 D ASP -289 ? D ASP 53   
1603 1 Y 1 D LYS -288 ? D LYS 54   
1604 1 Y 1 D LEU -287 ? D LEU 55   
1605 1 Y 1 D GLU -286 ? D GLU 56   
1606 1 Y 1 D GLU -285 ? D GLU 57   
1607 1 Y 1 D LYS -284 ? D LYS 58   
1608 1 Y 1 D PHE -283 ? D PHE 59   
1609 1 Y 1 D PRO -282 ? D PRO 60   
1610 1 Y 1 D GLN -281 ? D GLN 61   
1611 1 Y 1 D VAL -280 ? D VAL 62   
1612 1 Y 1 D ALA -279 ? D ALA 63   
1613 1 Y 1 D ALA -278 ? D ALA 64   
1614 1 Y 1 D THR -277 ? D THR 65   
1615 1 Y 1 D GLY -276 ? D GLY 66   
1616 1 Y 1 D ASP -275 ? D ASP 67   
1617 1 Y 1 D GLY -274 ? D GLY 68   
1618 1 Y 1 D PRO -273 ? D PRO 69   
1619 1 Y 1 D ASP -272 ? D ASP 70   
1620 1 Y 1 D ILE -271 ? D ILE 71   
1621 1 Y 1 D ILE -270 ? D ILE 72   
1622 1 Y 1 D PHE -269 ? D PHE 73   
1623 1 Y 1 D TRP -268 ? D TRP 74   
1624 1 Y 1 D ALA -267 ? D ALA 75   
1625 1 Y 1 D HIS -266 ? D HIS 76   
1626 1 Y 1 D ASP -265 ? D ASP 77   
1627 1 Y 1 D ARG -264 ? D ARG 78   
1628 1 Y 1 D PHE -263 ? D PHE 79   
1629 1 Y 1 D GLY -262 ? D GLY 80   
1630 1 Y 1 D GLY -261 ? D GLY 81   
1631 1 Y 1 D TYR -260 ? D TYR 82   
1632 1 Y 1 D ALA -259 ? D ALA 83   
1633 1 Y 1 D GLN -258 ? D GLN 84   
1634 1 Y 1 D SER -257 ? D SER 85   
1635 1 Y 1 D GLY -256 ? D GLY 86   
1636 1 Y 1 D LEU -255 ? D LEU 87   
1637 1 Y 1 D LEU -254 ? D LEU 88   
1638 1 Y 1 D ALA -253 ? D ALA 89   
1639 1 Y 1 D GLU -252 ? D GLU 90   
1640 1 Y 1 D ILE -251 ? D ILE 91   
1641 1 Y 1 D THR -250 ? D THR 92   
1642 1 Y 1 D PRO -249 ? D PRO 93   
1643 1 Y 1 D ASP -248 ? D ASP 94   
1644 1 Y 1 D LYS -247 ? D LYS 95   
1645 1 Y 1 D ALA -246 ? D ALA 96   
1646 1 Y 1 D PHE -245 ? D PHE 97   
1647 1 Y 1 D GLN -244 ? D GLN 98   
1648 1 Y 1 D ASP -243 ? D ASP 99   
1649 1 Y 1 D LYS -242 ? D LYS 100  
1650 1 Y 1 D LEU -241 ? D LEU 101  
1651 1 Y 1 D TYR -240 ? D TYR 102  
1652 1 Y 1 D PRO -239 ? D PRO 103  
1653 1 Y 1 D PHE -238 ? D PHE 104  
1654 1 Y 1 D THR -237 ? D THR 105  
1655 1 Y 1 D TRP -236 ? D TRP 106  
1656 1 Y 1 D ASP -235 ? D ASP 107  
1657 1 Y 1 D ALA -234 ? D ALA 108  
1658 1 Y 1 D VAL -233 ? D VAL 109  
1659 1 Y 1 D ARG -232 ? D ARG 110  
1660 1 Y 1 D TYR -231 ? D TYR 111  
1661 1 Y 1 D ASN -230 ? D ASN 112  
1662 1 Y 1 D GLY -229 ? D GLY 113  
1663 1 Y 1 D LYS -228 ? D LYS 114  
1664 1 Y 1 D LEU -227 ? D LEU 115  
1665 1 Y 1 D ILE -226 ? D ILE 116  
1666 1 Y 1 D ALA -225 ? D ALA 117  
1667 1 Y 1 D TYR -224 ? D TYR 118  
1668 1 Y 1 D PRO -223 ? D PRO 119  
1669 1 Y 1 D ILE -222 ? D ILE 120  
1670 1 Y 1 D ALA -221 ? D ALA 121  
1671 1 Y 1 D VAL -220 ? D VAL 122  
1672 1 Y 1 D GLU -219 ? D GLU 123  
1673 1 Y 1 D ALA -218 ? D ALA 124  
1674 1 Y 1 D LEU -217 ? D LEU 125  
1675 1 Y 1 D SER -216 ? D SER 126  
1676 1 Y 1 D LEU -215 ? D LEU 127  
1677 1 Y 1 D ILE -214 ? D ILE 128  
1678 1 Y 1 D TYR -213 ? D TYR 129  
1679 1 Y 1 D ASN -212 ? D ASN 130  
1680 1 Y 1 D LYS -211 ? D LYS 131  
1681 1 Y 1 D ASP -210 ? D ASP 132  
1682 1 Y 1 D LEU -209 ? D LEU 133  
1683 1 Y 1 D LEU -208 ? D LEU 134  
1684 1 Y 1 D PRO -207 ? D PRO 135  
1685 1 Y 1 D ASN -206 ? D ASN 136  
1686 1 Y 1 D PRO -205 ? D PRO 137  
1687 1 Y 1 D PRO -204 ? D PRO 138  
1688 1 Y 1 D LYS -203 ? D LYS 139  
1689 1 Y 1 D THR -202 ? D THR 140  
1690 1 Y 1 D TRP -201 ? D TRP 141  
1691 1 Y 1 D GLU -200 ? D GLU 142  
1692 1 Y 1 D GLU -199 ? D GLU 143  
1693 1 Y 1 D ILE -198 ? D ILE 144  
1694 1 Y 1 D PRO -197 ? D PRO 145  
1695 1 Y 1 D ALA -196 ? D ALA 146  
1696 1 Y 1 D LEU -195 ? D LEU 147  
1697 1 Y 1 D ASP -194 ? D ASP 148  
1698 1 Y 1 D LYS -193 ? D LYS 149  
1699 1 Y 1 D GLU -192 ? D GLU 150  
1700 1 Y 1 D LEU -191 ? D LEU 151  
1701 1 Y 1 D LYS -190 ? D LYS 152  
1702 1 Y 1 D ALA -189 ? D ALA 153  
1703 1 Y 1 D LYS -188 ? D LYS 154  
1704 1 Y 1 D GLY -187 ? D GLY 155  
1705 1 Y 1 D LYS -186 ? D LYS 156  
1706 1 Y 1 D SER -185 ? D SER 157  
1707 1 Y 1 D ALA -184 ? D ALA 158  
1708 1 Y 1 D LEU -183 ? D LEU 159  
1709 1 Y 1 D MET -182 ? D MET 160  
1710 1 Y 1 D PHE -181 ? D PHE 161  
1711 1 Y 1 D ASN -180 ? D ASN 162  
1712 1 Y 1 D LEU -179 ? D LEU 163  
1713 1 Y 1 D GLN -178 ? D GLN 164  
1714 1 Y 1 D GLU -177 ? D GLU 165  
1715 1 Y 1 D PRO -176 ? D PRO 166  
1716 1 Y 1 D TYR -175 ? D TYR 167  
1717 1 Y 1 D PHE -174 ? D PHE 168  
1718 1 Y 1 D THR -173 ? D THR 169  
1719 1 Y 1 D TRP -172 ? D TRP 170  
1720 1 Y 1 D PRO -171 ? D PRO 171  
1721 1 Y 1 D LEU -170 ? D LEU 172  
1722 1 Y 1 D ILE -169 ? D ILE 173  
1723 1 Y 1 D ALA -168 ? D ALA 174  
1724 1 Y 1 D ALA -167 ? D ALA 175  
1725 1 Y 1 D ASP -166 ? D ASP 176  
1726 1 Y 1 D GLY -165 ? D GLY 177  
1727 1 Y 1 D GLY -164 ? D GLY 178  
1728 1 Y 1 D TYR -163 ? D TYR 179  
1729 1 Y 1 D ALA -162 ? D ALA 180  
1730 1 Y 1 D PHE -161 ? D PHE 181  
1731 1 Y 1 D LYS -160 ? D LYS 182  
1732 1 Y 1 D TYR -159 ? D TYR 183  
1733 1 Y 1 D GLU -158 ? D GLU 184  
1734 1 Y 1 D ASN -157 ? D ASN 185  
1735 1 Y 1 D GLY -156 ? D GLY 186  
1736 1 Y 1 D LYS -155 ? D LYS 187  
1737 1 Y 1 D TYR -154 ? D TYR 188  
1738 1 Y 1 D ASP -153 ? D ASP 189  
1739 1 Y 1 D ILE -152 ? D ILE 190  
1740 1 Y 1 D LYS -151 ? D LYS 191  
1741 1 Y 1 D ASP -150 ? D ASP 192  
1742 1 Y 1 D VAL -149 ? D VAL 193  
1743 1 Y 1 D GLY -148 ? D GLY 194  
1744 1 Y 1 D VAL -147 ? D VAL 195  
1745 1 Y 1 D ASP -146 ? D ASP 196  
1746 1 Y 1 D ASN -145 ? D ASN 197  
1747 1 Y 1 D ALA -144 ? D ALA 198  
1748 1 Y 1 D GLY -143 ? D GLY 199  
1749 1 Y 1 D ALA -142 ? D ALA 200  
1750 1 Y 1 D LYS -141 ? D LYS 201  
1751 1 Y 1 D ALA -140 ? D ALA 202  
1752 1 Y 1 D GLY -139 ? D GLY 203  
1753 1 Y 1 D LEU -138 ? D LEU 204  
1754 1 Y 1 D THR -137 ? D THR 205  
1755 1 Y 1 D PHE -136 ? D PHE 206  
1756 1 Y 1 D LEU -135 ? D LEU 207  
1757 1 Y 1 D VAL -134 ? D VAL 208  
1758 1 Y 1 D ASP -133 ? D ASP 209  
1759 1 Y 1 D LEU -132 ? D LEU 210  
1760 1 Y 1 D ILE -131 ? D ILE 211  
1761 1 Y 1 D LYS -130 ? D LYS 212  
1762 1 Y 1 D ASN -129 ? D ASN 213  
1763 1 Y 1 D LYS -128 ? D LYS 214  
1764 1 Y 1 D HIS -127 ? D HIS 215  
1765 1 Y 1 D MET -126 ? D MET 216  
1766 1 Y 1 D ASN -125 ? D ASN 217  
1767 1 Y 1 D ALA -124 ? D ALA 218  
1768 1 Y 1 D ASP -123 ? D ASP 219  
1769 1 Y 1 D THR -122 ? D THR 220  
1770 1 Y 1 D ASP -121 ? D ASP 221  
1771 1 Y 1 D TYR -120 ? D TYR 222  
1772 1 Y 1 D SER -119 ? D SER 223  
1773 1 Y 1 D ILE -118 ? D ILE 224  
1774 1 Y 1 D ALA -117 ? D ALA 225  
1775 1 Y 1 D GLU -116 ? D GLU 226  
1776 1 Y 1 D ALA -115 ? D ALA 227  
1777 1 Y 1 D ALA -114 ? D ALA 228  
1778 1 Y 1 D PHE -113 ? D PHE 229  
1779 1 Y 1 D ASN -112 ? D ASN 230  
1780 1 Y 1 D LYS -111 ? D LYS 231  
1781 1 Y 1 D GLY -110 ? D GLY 232  
1782 1 Y 1 D GLU -109 ? D GLU 233  
1783 1 Y 1 D THR -108 ? D THR 234  
1784 1 Y 1 D ALA -107 ? D ALA 235  
1785 1 Y 1 D MET -106 ? D MET 236  
1786 1 Y 1 D THR -105 ? D THR 237  
1787 1 Y 1 D ILE -104 ? D ILE 238  
1788 1 Y 1 D ASN -103 ? D ASN 239  
1789 1 Y 1 D GLY -102 ? D GLY 240  
1790 1 Y 1 D PRO -101 ? D PRO 241  
1791 1 Y 1 D TRP -100 ? D TRP 242  
1792 1 Y 1 D ALA -99  ? D ALA 243  
1793 1 Y 1 D TRP -98  ? D TRP 244  
1794 1 Y 1 D SER -97  ? D SER 245  
1795 1 Y 1 D ASN -96  ? D ASN 246  
1796 1 Y 1 D ILE -95  ? D ILE 247  
1797 1 Y 1 D ASP -94  ? D ASP 248  
1798 1 Y 1 D THR -93  ? D THR 249  
1799 1 Y 1 D SER -92  ? D SER 250  
1800 1 Y 1 D LYS -91  ? D LYS 251  
1801 1 Y 1 D VAL -90  ? D VAL 252  
1802 1 Y 1 D ASN -89  ? D ASN 253  
1803 1 Y 1 D TYR -88  ? D TYR 254  
1804 1 Y 1 D GLY -87  ? D GLY 255  
1805 1 Y 1 D VAL -86  ? D VAL 256  
1806 1 Y 1 D THR -85  ? D THR 257  
1807 1 Y 1 D VAL -84  ? D VAL 258  
1808 1 Y 1 D LEU -83  ? D LEU 259  
1809 1 Y 1 D PRO -82  ? D PRO 260  
1810 1 Y 1 D THR -81  ? D THR 261  
1811 1 Y 1 D PHE -80  ? D PHE 262  
1812 1 Y 1 D LYS -79  ? D LYS 263  
1813 1 Y 1 D GLY -78  ? D GLY 264  
1814 1 Y 1 D GLN -77  ? D GLN 265  
1815 1 Y 1 D PRO -76  ? D PRO 266  
1816 1 Y 1 D SER -75  ? D SER 267  
1817 1 Y 1 D LYS -74  ? D LYS 268  
1818 1 Y 1 D PRO -73  ? D PRO 269  
1819 1 Y 1 D PHE -72  ? D PHE 270  
1820 1 Y 1 D VAL -71  ? D VAL 271  
1821 1 Y 1 D GLY -70  ? D GLY 272  
1822 1 Y 1 D VAL -69  ? D VAL 273  
1823 1 Y 1 D LEU -68  ? D LEU 274  
1824 1 Y 1 D SER -67  ? D SER 275  
1825 1 Y 1 D ALA -66  ? D ALA 276  
1826 1 Y 1 D GLY -65  ? D GLY 277  
1827 1 Y 1 D ILE -64  ? D ILE 278  
1828 1 Y 1 D ASN -63  ? D ASN 279  
1829 1 Y 1 D ALA -62  ? D ALA 280  
1830 1 Y 1 D ALA -61  ? D ALA 281  
1831 1 Y 1 D SER -60  ? D SER 282  
1832 1 Y 1 D PRO -59  ? D PRO 283  
1833 1 Y 1 D ASN -58  ? D ASN 284  
1834 1 Y 1 D LYS -57  ? D LYS 285  
1835 1 Y 1 D GLU -56  ? D GLU 286  
1836 1 Y 1 D LEU -55  ? D LEU 287  
1837 1 Y 1 D ALA -54  ? D ALA 288  
1838 1 Y 1 D LYS -53  ? D LYS 289  
1839 1 Y 1 D GLU -52  ? D GLU 290  
1840 1 Y 1 D PHE -51  ? D PHE 291  
1841 1 Y 1 D LEU -50  ? D LEU 292  
1842 1 Y 1 D GLU -49  ? D GLU 293  
1843 1 Y 1 D ASN -48  ? D ASN 294  
1844 1 Y 1 D TYR -47  ? D TYR 295  
1845 1 Y 1 D LEU -46  ? D LEU 296  
1846 1 Y 1 D LEU -45  ? D LEU 297  
1847 1 Y 1 D THR -44  ? D THR 298  
1848 1 Y 1 D ASP -43  ? D ASP 299  
1849 1 Y 1 D GLU -42  ? D GLU 300  
1850 1 Y 1 D GLY -41  ? D GLY 301  
1851 1 Y 1 D LEU -40  ? D LEU 302  
1852 1 Y 1 D GLU -39  ? D GLU 303  
1853 1 Y 1 D ALA -38  ? D ALA 304  
1854 1 Y 1 D VAL -37  ? D VAL 305  
1855 1 Y 1 D ASN -36  ? D ASN 306  
1856 1 Y 1 D LYS -35  ? D LYS 307  
1857 1 Y 1 D ASP -34  ? D ASP 308  
1858 1 Y 1 D LYS -33  ? D LYS 309  
1859 1 Y 1 D PRO -32  ? D PRO 310  
1860 1 Y 1 D LEU -31  ? D LEU 311  
1861 1 Y 1 D GLY -30  ? D GLY 312  
1862 1 Y 1 D ALA -29  ? D ALA 313  
1863 1 Y 1 D VAL -28  ? D VAL 314  
1864 1 Y 1 D ALA -27  ? D ALA 315  
1865 1 Y 1 D LEU -26  ? D LEU 316  
1866 1 Y 1 D LYS -25  ? D LYS 317  
1867 1 Y 1 D SER -24  ? D SER 318  
1868 1 Y 1 D TYR -23  ? D TYR 319  
1869 1 Y 1 D GLU -22  ? D GLU 320  
1870 1 Y 1 D GLU -21  ? D GLU 321  
1871 1 Y 1 D GLU -20  ? D GLU 322  
1872 1 Y 1 D LEU -19  ? D LEU 323  
1873 1 Y 1 D ALA -18  ? D ALA 324  
1874 1 Y 1 D LYS -17  ? D LYS 325  
1875 1 Y 1 D ASP -16  ? D ASP 326  
1876 1 Y 1 D PRO -15  ? D PRO 327  
1877 1 Y 1 D ARG -14  ? D ARG 328  
1878 1 Y 1 D ILE -13  ? D ILE 329  
1879 1 Y 1 D ALA -12  ? D ALA 330  
1880 1 Y 1 D ALA -11  ? D ALA 331  
1881 1 Y 1 D THR -10  ? D THR 332  
1882 1 Y 1 D MET -9   ? D MET 333  
1883 1 Y 1 D GLU -8   ? D GLU 334  
1884 1 Y 1 D ASN -7   ? D ASN 335  
1885 1 Y 1 D ALA -6   ? D ALA 336  
1886 1 Y 1 D GLN -5   ? D GLN 337  
1887 1 Y 1 D LYS -4   ? D LYS 338  
1888 1 Y 1 D GLY -3   ? D GLY 339  
1889 1 Y 1 D GLU -2   ? D GLU 340  
1890 1 Y 1 D ILE -1   ? D ILE 341  
1891 1 Y 1 D MET 0    ? D MET 342  
1892 1 Y 1 D PRO 1    ? D PRO 343  
1893 1 Y 1 D ASN 2    ? D ASN 344  
1894 1 Y 1 D ILE 3    ? D ILE 345  
1895 1 Y 1 D PRO 4    ? D PRO 346  
1896 1 Y 1 D GLN 5    ? D GLN 347  
1897 1 Y 1 D MET 6    ? D MET 348  
1898 1 Y 1 D SER 7    ? D SER 349  
1899 1 Y 1 D ALA 8    ? D ALA 350  
1900 1 Y 1 D PHE 9    ? D PHE 351  
1901 1 Y 1 D TRP 10   ? D TRP 352  
1902 1 Y 1 D TYR 11   ? D TYR 353  
1903 1 Y 1 D ALA 12   ? D ALA 354  
1904 1 Y 1 D VAL 13   ? D VAL 355  
1905 1 Y 1 D ARG 14   ? D ARG 356  
1906 1 Y 1 D THR 15   ? D THR 357  
1907 1 Y 1 D ALA 16   ? D ALA 358  
1908 1 Y 1 D VAL 17   ? D VAL 359  
1909 1 Y 1 D ILE 18   ? D ILE 360  
1910 1 Y 1 D ASN 19   ? D ASN 361  
1911 1 Y 1 D ALA 20   ? D ALA 362  
1912 1 Y 1 D ALA 21   ? D ALA 363  
1913 1 Y 1 D SER 22   ? D SER 364  
1914 1 Y 1 D GLY 23   ? D GLY 365  
1915 1 Y 1 D ARG 24   ? D ARG 366  
1916 1 Y 1 D GLN 25   ? D GLN 367  
1917 1 Y 1 D THR 26   ? D THR 368  
1918 1 Y 1 D VAL 27   ? D VAL 369  
1919 1 Y 1 D ASP 28   ? D ASP 370  
1920 1 Y 1 D GLU 29   ? D GLU 371  
1921 1 Y 1 D ALA 30   ? D ALA 372  
1922 1 Y 1 D LEU 31   ? D LEU 373  
1923 1 Y 1 D LYS 32   ? D LYS 374  
1924 1 Y 1 D ASP 33   ? D ASP 375  
1925 1 Y 1 D ALA 34   ? D ALA 376  
1926 1 Y 1 D GLN 35   ? D GLN 377  
1927 1 Y 1 D THR 36   ? D THR 378  
1928 1 Y 1 D GLY 37   ? D GLY 379  
1929 1 Y 1 D THR 38   ? D THR 380  
1930 1 Y 1 D ASP 39   ? D ASP 381  
1931 1 Y 1 D TYR 40   ? D TYR 382  
1932 1 Y 1 D ASP 41   ? D ASP 383  
1933 1 Y 1 D ILE 42   ? D ILE 384  
1934 1 Y 1 D PRO 43   ? D PRO 385  
1935 1 Y 1 D THR 44   ? D THR 386  
1936 1 Y 1 D THR 45   ? D THR 387  
1937 1 Y 1 D LEU 46   ? D LEU 388  
1938 1 Y 1 D GLU 47   ? D GLU 389  
1939 1 Y 1 D VAL 48   ? D VAL 390  
1940 1 Y 1 D LEU 49   ? D LEU 391  
1941 1 Y 1 D PHE 50   ? D PHE 392  
1942 1 Y 1 D GLN 51   ? D GLN 393  
1943 1 Y 1 D GLY 52   ? D GLY 394  
1944 1 Y 1 D PRO 53   ? D PRO 395  
1945 1 Y 1 D LEU 54   ? D LEU 396  
1946 1 Y 1 D GLY 55   ? D GLY 397  
1947 1 Y 1 D SER 56   ? D SER 398  
1948 1 Y 1 D SER 57   ? D SER 399  
1949 1 Y 1 D THR 58   ? D THR 400  
1950 1 Y 1 D ASP 59   ? D ASP 401  
1951 1 Y 1 D ASP 60   ? D ASP 402  
1952 1 Y 1 D ILE 61   ? D ILE 403  
1953 1 Y 1 D ILE 62   ? D ILE 404  
1954 1 Y 1 D TRP 63   ? D TRP 405  
1955 1 Y 1 D ASP 64   ? D ASP 406  
1956 1 Y 1 D GLN 65   ? D GLN 407  
1957 1 Y 1 D LEU 66   ? D LEU 408  
1958 1 Y 1 D ILE 67   ? D ILE 409  
1959 1 Y 1 D VAL 68   ? D VAL 410  
1960 1 Y 1 D LYS 69   ? D LYS 411  
1961 1 Y 1 D ARG 70   ? D ARG 412  
1962 1 Y 1 D THR 71   ? D THR 413  
1963 1 Y 1 D LEU 72   ? D LEU 414  
1964 1 Y 1 D ALA 73   ? D ALA 415  
1965 1 Y 1 D ASP 74   ? D ASP 416  
1966 1 Y 1 D LEU 75   ? D LEU 417  
1967 1 Y 1 D LEU 76   ? D LEU 418  
1968 1 Y 1 D ILE 77   ? D ILE 419  
1969 1 Y 1 D PRO 78   ? D PRO 420  
1970 1 Y 1 D ILE 79   ? D ILE 421  
1971 1 Y 1 D ASN 80   ? D ASN 422  
1972 1 Y 1 D ARG 81   ? D ARG 423  
1973 1 Y 1 D GLN 82   ? D GLN 424  
1974 1 Y 1 D ILE 83   ? D ILE 425  
1975 1 Y 1 D SER 84   ? D SER 426  
1976 1 Y 1 D ASP 85   ? D ASP 427  
1977 1 Y 1 D ILE 86   ? D ILE 428  
1978 1 Y 1 D GLN 87   ? D GLN 429  
1979 1 Y 1 D SER 88   ? D SER 430  
1980 1 Y 1 D THR 89   ? D THR 431  
1981 1 Y 1 D LEU 90   ? D LEU 432  
1982 1 Y 1 D SER 91   ? D SER 433  
1983 1 Y 1 D GLU 92   ? D GLU 434  
1984 1 Y 1 D VAL 93   ? D VAL 435  
1985 1 Y 1 D THR 94   ? D THR 436  
1986 1 Y 1 D THR 95   ? D THR 437  
1987 1 Y 1 D ARG 96   ? D ARG 438  
1988 1 Y 1 D VAL 97   ? D VAL 439  
1989 1 Y 1 D HIS 98   ? D HIS 440  
1990 1 Y 1 D GLU 99   ? D GLU 441  
1991 1 Y 1 D ILE 100  ? D ILE 442  
1992 1 Y 1 D GLU 101  ? D GLU 443  
1993 1 Y 1 D ARG 102  ? D ARG 444  
1994 1 Y 1 D GLN 103  ? D GLN 445  
1995 1 Y 1 D LEU 104  ? D LEU 446  
1996 1 Y 1 D HIS 105  ? D HIS 447  
1997 1 Y 1 D GLU 106  ? D GLU 448  
1998 1 Y 1 D GLY 139  ? D GLY 481  
1999 1 Y 1 D ARG 140  ? D ARG 482  
2000 1 Y 1 D THR 141  ? D THR 483  
2001 1 Y 1 D THR 142  ? D THR 484  
2002 1 Y 1 D ALA 143  ? D ALA 485  
2003 1 Y 1 D PRO 144  ? D PRO 486  
2004 1 Y 1 D ALA 145  ? D ALA 487  
2005 1 Y 1 D ALA 146  ? D ALA 488  
2006 1 Y 1 D ALA 147  ? D ALA 489  
2007 1 Y 1 D PHE 148  ? D PHE 490  
2008 1 Y 1 D ASP 149  ? D ASP 491  
2009 1 Y 1 D ALA 150  ? D ALA 492  
2010 1 Y 1 D TYR 151  ? D TYR 493  
2011 1 Y 1 D LEU 152  ? D LEU 494  
2012 1 Y 1 D ASN 153  ? D ASN 495  
2013 1 Y 1 D GLU 154  ? D GLU 496  
2014 1 Y 1 D HIS 155  ? D HIS 497  
2015 1 Y 1 D GLY 156  ? D GLY 498  
2016 1 Y 1 D VAL 157  ? D VAL 499  
2017 1 Y 1 D PRO 158  ? D PRO 500  
2018 1 Y 1 D PRO 159  ? D PRO 501  
2019 1 Y 1 D PRO 160  ? D PRO 502  
2020 1 Y 1 D GLN 161  ? D GLN 503  
2021 1 Y 1 D PRO 162  ? D PRO 504  
2022 1 Y 1 D ALA 163  ? D ALA 505  
2023 1 Y 1 D ILE 164  ? D ILE 506  
2024 1 Y 1 D PHE 165  ? D PHE 507  
2025 1 Y 1 D LYS 166  ? D LYS 508  
2026 1 Y 1 D ASP 167  ? D ASP 509  
2027 1 Y 1 D LEU 168  ? D LEU 510  
2028 1 Y 1 D GLY 169  ? D GLY 511  
2029 1 Y 1 D VAL 170  ? D VAL 512  
2030 1 Y 1 D ALA 171  ? D ALA 513  
2031 1 Y 1 D GLN 172  ? D GLN 514  
2032 1 Y 1 D GLN 173  ? D GLN 515  
2033 1 Y 1 D ALA 174  ? D ALA 516  
2034 1 Y 1 D CYS 175  ? D CYS 517  
2035 1 Y 1 D SER 176  ? D SER 518  
2036 1 Y 1 D LYS 177  ? D LYS 519  
2037 1 Y 1 D GLY 178  ? D GLY 520  
2038 1 Y 1 D THR 179  ? D THR 521  
2039 1 Y 1 D MET 180  ? D MET 522  
2040 1 Y 1 D VAL 181  ? D VAL 523  
2041 1 Y 1 D LYS 182  ? D LYS 524  
2042 1 Y 1 D ASN 183  ? D ASN 525  
2043 1 Y 1 D ALA 184  ? D ALA 526  
2044 1 Y 1 D THR 185  ? D THR 527  
2045 1 Y 1 D THR 186  ? D THR 528  
2046 1 Y 1 D ASP 187  ? D ASP 529  
2047 1 Y 1 D ALA 188  ? D ALA 530  
2048 1 Y 1 D ALA 189  ? D ALA 531  
2049 1 Y 1 D ASP 190  ? D ASP 532  
2050 1 Y 1 D LYS 191  ? D LYS 533  
2051 1 Y 1 D MET 192  ? D MET 534  
2052 1 Y 1 D SER 193  ? D SER 535  
2053 1 Y 1 D LYS 194  ? D LYS 536  
2054 1 Y 1 D VAL 195  ? D VAL 537  
2055 1 Y 1 D LEU 196  ? D LEU 538  
2056 1 Y 1 D GLU 197  ? D GLU 539  
2057 1 Y 1 D LEU 198  ? D LEU 540  
2058 1 Y 1 D SER 199  ? D SER 541  
2059 1 Y 1 D GLU 200  ? D GLU 542  
2060 1 Y 1 D GLU 201  ? D GLU 543  
2061 1 Y 1 D THR 202  ? D THR 544  
2062 1 Y 1 D PHE 203  ? D PHE 545  
2063 1 Y 1 D SER 204  ? D SER 546  
2064 1 Y 1 D LYS 205  ? D LYS 547  
2065 1 Y 1 D PRO 206  ? D PRO 548  
2066 1 Y 1 D ASN 207  ? D ASN 549  
2067 1 Y 1 D LEU 208  ? D LEU 550  
2068 1 Y 1 D SER 209  ? D SER 551  
2069 1 Y 1 D ALA 210  ? D ALA 552  
2070 1 Y 1 D LYS 211  ? D LYS 553  
2071 1 Y 1 D ASP 212  ? D ASP 554  
2072 1 Y 1 D LEU 213  ? D LEU 555  
2073 1 Y 1 D ALA 214  ? D ALA 556  
2074 1 Y 1 D LEU 215  ? D LEU 557  
2075 1 Y 1 D LEU 216  ? D LEU 558  
2076 1 Y 1 D LEU 217  ? D LEU 559  
2077 1 Y 1 D PHE 218  ? D PHE 560  
2078 1 Y 1 D THR 219  ? D THR 561  
2079 1 Y 1 D HIS 220  ? D HIS 562  
2080 1 Y 1 D LEU 221  ? D LEU 563  
2081 1 Y 1 D PRO 222  ? D PRO 564  
2082 1 Y 1 D GLY 223  ? D GLY 565  
2083 1 Y 1 D ASN 224  ? D ASN 566  
2084 1 Y 1 D ASN 225  ? D ASN 567  
2085 1 Y 1 D THR 226  ? D THR 568  
2086 1 Y 1 D PRO 227  ? D PRO 569  
2087 1 Y 1 D PHE 228  ? D PHE 570  
2088 1 Y 1 D HIS 229  ? D HIS 571  
2089 1 Y 1 D ILE 230  ? D ILE 572  
2090 1 Y 1 D LEU 231  ? D LEU 573  
2091 1 Y 1 D ALA 232  ? D ALA 574  
2092 1 Y 1 D GLN 233  ? D GLN 575  
2093 1 Y 1 D VAL 234  ? D VAL 576  
2094 1 Y 1 D LEU 235  ? D LEU 577  
2095 1 Y 1 D SER 236  ? D SER 578  
2096 1 Y 1 D LYS 237  ? D LYS 579  
2097 1 Y 1 D ILE 238  ? D ILE 580  
2098 1 Y 1 D ALA 239  ? D ALA 581  
2099 1 Y 1 D TYR 240  ? D TYR 582  
2100 1 Y 1 D LYS 241  ? D LYS 583  
2101 1 Y 1 D SER 242  ? D SER 584  
2102 1 Y 1 D GLY 243  ? D GLY 585  
2103 1 Y 1 D LYS 244  ? D LYS 586  
2104 1 Y 1 D SER 245  ? D SER 587  
2105 1 Y 1 D GLY 246  ? D GLY 588  
2106 1 Y 1 D ALA 247  ? D ALA 589  
2107 1 Y 1 D PHE 248  ? D PHE 590  
2108 1 Y 1 D LEU 249  ? D LEU 591  
2109 1 Y 1 D ASP 250  ? D ASP 592  
2110 1 Y 1 D ALA 251  ? D ALA 593  
2111 1 Y 1 D PHE 252  ? D PHE 594  
2112 1 Y 1 D HIS 253  ? D HIS 595  
2113 1 Y 1 D GLN 254  ? D GLN 596  
2114 1 Y 1 D ILE 255  ? D ILE 597  
2115 1 Y 1 D LEU 256  ? D LEU 598  
2116 1 Y 1 D SER 257  ? D SER 599  
2117 1 Y 1 D GLU 258  ? D GLU 600  
2118 1 Y 1 D GLY 259  ? D GLY 601  
2119 1 Y 1 D GLU 260  ? D GLU 602  
2120 1 Y 1 D ASN 261  ? D ASN 603  
2121 1 Y 1 D ALA 262  ? D ALA 604  
2122 1 Y 1 D GLN 263  ? D GLN 605  
2123 1 Y 1 D ALA 264  ? D ALA 606  
2124 1 Y 1 D ALA 265  ? D ALA 607  
2125 1 Y 1 D LEU 266  ? D LEU 608  
2126 1 Y 1 D THR 267  ? D THR 609  
2127 1 Y 1 D ARG 268  ? D ARG 610  
2128 1 Y 1 D LEU 269  ? D LEU 611  
2129 1 Y 1 D SER 270  ? D SER 612  
2130 1 Y 1 D ARG 271  ? D ARG 613  
2131 1 Y 1 D THR 272  ? D THR 614  
2132 1 Y 1 D PHE 273  ? D PHE 615  
2133 1 Y 1 D ASP 274  ? D ASP 616  
2134 1 Y 1 D ALA 275  ? D ALA 617  
2135 1 Y 1 D PHE 276  ? D PHE 618  
2136 1 Y 1 D LEU 277  ? D LEU 619  
2137 1 Y 1 D GLY 278  ? D GLY 620  
2138 1 Y 1 D VAL 279  ? D VAL 621  
2139 1 Y 1 D VAL 280  ? D VAL 622  
2140 1 Y 1 D PRO 281  ? D PRO 623  
2141 1 Y 1 D PRO 282  ? D PRO 624  
2142 1 Y 1 D VAL 283  ? D VAL 625  
2143 1 Y 1 D ILE 284  ? D ILE 626  
2144 1 Y 1 D ARG 285  ? D ARG 627  
2145 1 Y 1 D VAL 286  ? D VAL 628  
2146 1 Y 1 D LYS 287  ? D LYS 629  
2147 1 Y 1 D ASN 288  ? D ASN 630  
2148 1 Y 1 D PHE 289  ? D PHE 631  
2149 1 Y 1 D GLN 290  ? D GLN 632  
2150 1 Y 1 D THR 291  ? D THR 633  
2151 1 Y 1 D VAL 292  ? D VAL 634  
2152 1 Y 1 D PRO 293  ? D PRO 635  
2153 1 Y 1 D ARG 294  ? D ARG 636  
2154 1 Y 1 D PRO 295  ? D PRO 637  
2155 1 Y 1 D CYS 296  ? D CYS 638  
2156 1 Y 1 D GLN 297  ? D GLN 639  
2157 1 Y 1 D LYS 298  ? D LYS 640  
2158 1 Y 1 D SER 299  ? D SER 641  
2159 1 Y 1 D LEU 300  ? D LEU 642  
2160 1 Y 1 D ARG 301  ? D ARG 643  
2161 1 Y 1 D ALA 302  ? D ALA 644  
2162 1 Y 1 D VAL 303  ? D VAL 645  
2163 1 Y 1 D PRO 304  ? D PRO 646  
2164 1 Y 1 D PRO 305  ? D PRO 647  
2165 1 Y 1 D ASN 306  ? D ASN 648  
2166 1 Y 1 D PRO 307  ? D PRO 649  
2167 1 Y 1 D THR 308  ? D THR 650  
2168 1 Y 1 D ILE 309  ? D ILE 651  
2169 1 Y 1 D ASP 310  ? D ASP 652  
2170 1 Y 1 D LYS 311  ? D LYS 653  
2171 1 Y 1 D GLY 312  ? D GLY 654  
2172 1 Y 1 D TRP 313  ? D TRP 655  
2173 1 Y 1 D VAL 314  ? D VAL 656  
2174 1 Y 1 D CYS 315  ? D CYS 657  
2175 1 Y 1 D VAL 316  ? D VAL 658  
2176 1 Y 1 D TYR 317  ? D TYR 659  
2177 1 Y 1 D SER 318  ? D SER 660  
2178 1 Y 1 D SER 319  ? D SER 661  
2179 1 Y 1 D GLU 320  ? D GLU 662  
2180 1 Y 1 D GLN 321  ? D GLN 663  
2181 1 Y 1 D GLY 322  ? D GLY 664  
2182 1 Y 1 D GLU 323  ? D GLU 665  
2183 1 Y 1 D THR 324  ? D THR 666  
2184 1 Y 1 D ARG 325  ? D ARG 667  
2185 1 Y 1 D ALA 326  ? D ALA 668  
2186 1 Y 1 D LEU 327  ? D LEU 669  
2187 1 Y 1 D LYS 328  ? D LYS 670  
2188 1 Y 1 D ILE 329  ? D ILE 671  
2189 1 Y 1 E MET -341 ? E MET 1    
2190 1 Y 1 E GLY -340 ? E GLY 2    
2191 1 Y 1 E SER -339 ? E SER 3    
2192 1 Y 1 E SER -338 ? E SER 4    
2193 1 Y 1 E HIS -337 ? E HIS 5    
2194 1 Y 1 E HIS -336 ? E HIS 6    
2195 1 Y 1 E HIS -335 ? E HIS 7    
2196 1 Y 1 E HIS -334 ? E HIS 8    
2197 1 Y 1 E HIS -333 ? E HIS 9    
2198 1 Y 1 E HIS -332 ? E HIS 10   
2199 1 Y 1 E GLY -331 ? E GLY 11   
2200 1 Y 1 E THR -330 ? E THR 12   
2201 1 Y 1 E LYS -329 ? E LYS 13   
2202 1 Y 1 E THR -328 ? E THR 14   
2203 1 Y 1 E GLU -327 ? E GLU 15   
2204 1 Y 1 E GLU -326 ? E GLU 16   
2205 1 Y 1 E GLY -325 ? E GLY 17   
2206 1 Y 1 E LYS -324 ? E LYS 18   
2207 1 Y 1 E LEU -323 ? E LEU 19   
2208 1 Y 1 E VAL -322 ? E VAL 20   
2209 1 Y 1 E ILE -321 ? E ILE 21   
2210 1 Y 1 E TRP -320 ? E TRP 22   
2211 1 Y 1 E ILE -319 ? E ILE 23   
2212 1 Y 1 E ASN -318 ? E ASN 24   
2213 1 Y 1 E GLY -317 ? E GLY 25   
2214 1 Y 1 E ASP -316 ? E ASP 26   
2215 1 Y 1 E LYS -315 ? E LYS 27   
2216 1 Y 1 E GLY -314 ? E GLY 28   
2217 1 Y 1 E TYR -313 ? E TYR 29   
2218 1 Y 1 E ASN -312 ? E ASN 30   
2219 1 Y 1 E GLY -311 ? E GLY 31   
2220 1 Y 1 E LEU -310 ? E LEU 32   
2221 1 Y 1 E ALA -309 ? E ALA 33   
2222 1 Y 1 E GLU -308 ? E GLU 34   
2223 1 Y 1 E VAL -307 ? E VAL 35   
2224 1 Y 1 E GLY -306 ? E GLY 36   
2225 1 Y 1 E LYS -305 ? E LYS 37   
2226 1 Y 1 E LYS -304 ? E LYS 38   
2227 1 Y 1 E PHE -303 ? E PHE 39   
2228 1 Y 1 E GLU -302 ? E GLU 40   
2229 1 Y 1 E LYS -301 ? E LYS 41   
2230 1 Y 1 E ASP -300 ? E ASP 42   
2231 1 Y 1 E THR -299 ? E THR 43   
2232 1 Y 1 E GLY -298 ? E GLY 44   
2233 1 Y 1 E ILE -297 ? E ILE 45   
2234 1 Y 1 E LYS -296 ? E LYS 46   
2235 1 Y 1 E VAL -295 ? E VAL 47   
2236 1 Y 1 E THR -294 ? E THR 48   
2237 1 Y 1 E VAL -293 ? E VAL 49   
2238 1 Y 1 E GLU -292 ? E GLU 50   
2239 1 Y 1 E HIS -291 ? E HIS 51   
2240 1 Y 1 E PRO -290 ? E PRO 52   
2241 1 Y 1 E ASP -289 ? E ASP 53   
2242 1 Y 1 E LYS -288 ? E LYS 54   
2243 1 Y 1 E LEU -287 ? E LEU 55   
2244 1 Y 1 E GLU -286 ? E GLU 56   
2245 1 Y 1 E GLU -285 ? E GLU 57   
2246 1 Y 1 E LYS -284 ? E LYS 58   
2247 1 Y 1 E PHE -283 ? E PHE 59   
2248 1 Y 1 E PRO -282 ? E PRO 60   
2249 1 Y 1 E GLN -281 ? E GLN 61   
2250 1 Y 1 E VAL -280 ? E VAL 62   
2251 1 Y 1 E ALA -279 ? E ALA 63   
2252 1 Y 1 E ALA -278 ? E ALA 64   
2253 1 Y 1 E THR -277 ? E THR 65   
2254 1 Y 1 E GLY -276 ? E GLY 66   
2255 1 Y 1 E ASP -275 ? E ASP 67   
2256 1 Y 1 E GLY -274 ? E GLY 68   
2257 1 Y 1 E PRO -273 ? E PRO 69   
2258 1 Y 1 E ASP -272 ? E ASP 70   
2259 1 Y 1 E ILE -271 ? E ILE 71   
2260 1 Y 1 E ILE -270 ? E ILE 72   
2261 1 Y 1 E PHE -269 ? E PHE 73   
2262 1 Y 1 E TRP -268 ? E TRP 74   
2263 1 Y 1 E ALA -267 ? E ALA 75   
2264 1 Y 1 E HIS -266 ? E HIS 76   
2265 1 Y 1 E ASP -265 ? E ASP 77   
2266 1 Y 1 E ARG -264 ? E ARG 78   
2267 1 Y 1 E PHE -263 ? E PHE 79   
2268 1 Y 1 E GLY -262 ? E GLY 80   
2269 1 Y 1 E GLY -261 ? E GLY 81   
2270 1 Y 1 E TYR -260 ? E TYR 82   
2271 1 Y 1 E ALA -259 ? E ALA 83   
2272 1 Y 1 E GLN -258 ? E GLN 84   
2273 1 Y 1 E SER -257 ? E SER 85   
2274 1 Y 1 E GLY -256 ? E GLY 86   
2275 1 Y 1 E LEU -255 ? E LEU 87   
2276 1 Y 1 E LEU -254 ? E LEU 88   
2277 1 Y 1 E ALA -253 ? E ALA 89   
2278 1 Y 1 E GLU -252 ? E GLU 90   
2279 1 Y 1 E ILE -251 ? E ILE 91   
2280 1 Y 1 E THR -250 ? E THR 92   
2281 1 Y 1 E PRO -249 ? E PRO 93   
2282 1 Y 1 E ASP -248 ? E ASP 94   
2283 1 Y 1 E LYS -247 ? E LYS 95   
2284 1 Y 1 E ALA -246 ? E ALA 96   
2285 1 Y 1 E PHE -245 ? E PHE 97   
2286 1 Y 1 E GLN -244 ? E GLN 98   
2287 1 Y 1 E ASP -243 ? E ASP 99   
2288 1 Y 1 E LYS -242 ? E LYS 100  
2289 1 Y 1 E LEU -241 ? E LEU 101  
2290 1 Y 1 E TYR -240 ? E TYR 102  
2291 1 Y 1 E PRO -239 ? E PRO 103  
2292 1 Y 1 E PHE -238 ? E PHE 104  
2293 1 Y 1 E THR -237 ? E THR 105  
2294 1 Y 1 E TRP -236 ? E TRP 106  
2295 1 Y 1 E ASP -235 ? E ASP 107  
2296 1 Y 1 E ALA -234 ? E ALA 108  
2297 1 Y 1 E VAL -233 ? E VAL 109  
2298 1 Y 1 E ARG -232 ? E ARG 110  
2299 1 Y 1 E TYR -231 ? E TYR 111  
2300 1 Y 1 E ASN -230 ? E ASN 112  
2301 1 Y 1 E GLY -229 ? E GLY 113  
2302 1 Y 1 E LYS -228 ? E LYS 114  
2303 1 Y 1 E LEU -227 ? E LEU 115  
2304 1 Y 1 E ILE -226 ? E ILE 116  
2305 1 Y 1 E ALA -225 ? E ALA 117  
2306 1 Y 1 E TYR -224 ? E TYR 118  
2307 1 Y 1 E PRO -223 ? E PRO 119  
2308 1 Y 1 E ILE -222 ? E ILE 120  
2309 1 Y 1 E ALA -221 ? E ALA 121  
2310 1 Y 1 E VAL -220 ? E VAL 122  
2311 1 Y 1 E GLU -219 ? E GLU 123  
2312 1 Y 1 E ALA -218 ? E ALA 124  
2313 1 Y 1 E LEU -217 ? E LEU 125  
2314 1 Y 1 E SER -216 ? E SER 126  
2315 1 Y 1 E LEU -215 ? E LEU 127  
2316 1 Y 1 E ILE -214 ? E ILE 128  
2317 1 Y 1 E TYR -213 ? E TYR 129  
2318 1 Y 1 E ASN -212 ? E ASN 130  
2319 1 Y 1 E LYS -211 ? E LYS 131  
2320 1 Y 1 E ASP -210 ? E ASP 132  
2321 1 Y 1 E LEU -209 ? E LEU 133  
2322 1 Y 1 E LEU -208 ? E LEU 134  
2323 1 Y 1 E PRO -207 ? E PRO 135  
2324 1 Y 1 E ASN -206 ? E ASN 136  
2325 1 Y 1 E PRO -205 ? E PRO 137  
2326 1 Y 1 E PRO -204 ? E PRO 138  
2327 1 Y 1 E LYS -203 ? E LYS 139  
2328 1 Y 1 E THR -202 ? E THR 140  
2329 1 Y 1 E TRP -201 ? E TRP 141  
2330 1 Y 1 E GLU -200 ? E GLU 142  
2331 1 Y 1 E GLU -199 ? E GLU 143  
2332 1 Y 1 E ILE -198 ? E ILE 144  
2333 1 Y 1 E PRO -197 ? E PRO 145  
2334 1 Y 1 E ALA -196 ? E ALA 146  
2335 1 Y 1 E LEU -195 ? E LEU 147  
2336 1 Y 1 E ASP -194 ? E ASP 148  
2337 1 Y 1 E LYS -193 ? E LYS 149  
2338 1 Y 1 E GLU -192 ? E GLU 150  
2339 1 Y 1 E LEU -191 ? E LEU 151  
2340 1 Y 1 E LYS -190 ? E LYS 152  
2341 1 Y 1 E ALA -189 ? E ALA 153  
2342 1 Y 1 E LYS -188 ? E LYS 154  
2343 1 Y 1 E GLY -187 ? E GLY 155  
2344 1 Y 1 E LYS -186 ? E LYS 156  
2345 1 Y 1 E SER -185 ? E SER 157  
2346 1 Y 1 E ALA -184 ? E ALA 158  
2347 1 Y 1 E LEU -183 ? E LEU 159  
2348 1 Y 1 E MET -182 ? E MET 160  
2349 1 Y 1 E PHE -181 ? E PHE 161  
2350 1 Y 1 E ASN -180 ? E ASN 162  
2351 1 Y 1 E LEU -179 ? E LEU 163  
2352 1 Y 1 E GLN -178 ? E GLN 164  
2353 1 Y 1 E GLU -177 ? E GLU 165  
2354 1 Y 1 E PRO -176 ? E PRO 166  
2355 1 Y 1 E TYR -175 ? E TYR 167  
2356 1 Y 1 E PHE -174 ? E PHE 168  
2357 1 Y 1 E THR -173 ? E THR 169  
2358 1 Y 1 E TRP -172 ? E TRP 170  
2359 1 Y 1 E PRO -171 ? E PRO 171  
2360 1 Y 1 E LEU -170 ? E LEU 172  
2361 1 Y 1 E ILE -169 ? E ILE 173  
2362 1 Y 1 E ALA -168 ? E ALA 174  
2363 1 Y 1 E ALA -167 ? E ALA 175  
2364 1 Y 1 E ASP -166 ? E ASP 176  
2365 1 Y 1 E GLY -165 ? E GLY 177  
2366 1 Y 1 E GLY -164 ? E GLY 178  
2367 1 Y 1 E TYR -163 ? E TYR 179  
2368 1 Y 1 E ALA -162 ? E ALA 180  
2369 1 Y 1 E PHE -161 ? E PHE 181  
2370 1 Y 1 E LYS -160 ? E LYS 182  
2371 1 Y 1 E TYR -159 ? E TYR 183  
2372 1 Y 1 E GLU -158 ? E GLU 184  
2373 1 Y 1 E ASN -157 ? E ASN 185  
2374 1 Y 1 E GLY -156 ? E GLY 186  
2375 1 Y 1 E LYS -155 ? E LYS 187  
2376 1 Y 1 E TYR -154 ? E TYR 188  
2377 1 Y 1 E ASP -153 ? E ASP 189  
2378 1 Y 1 E ILE -152 ? E ILE 190  
2379 1 Y 1 E LYS -151 ? E LYS 191  
2380 1 Y 1 E ASP -150 ? E ASP 192  
2381 1 Y 1 E VAL -149 ? E VAL 193  
2382 1 Y 1 E GLY -148 ? E GLY 194  
2383 1 Y 1 E VAL -147 ? E VAL 195  
2384 1 Y 1 E ASP -146 ? E ASP 196  
2385 1 Y 1 E ASN -145 ? E ASN 197  
2386 1 Y 1 E ALA -144 ? E ALA 198  
2387 1 Y 1 E GLY -143 ? E GLY 199  
2388 1 Y 1 E ALA -142 ? E ALA 200  
2389 1 Y 1 E LYS -141 ? E LYS 201  
2390 1 Y 1 E ALA -140 ? E ALA 202  
2391 1 Y 1 E GLY -139 ? E GLY 203  
2392 1 Y 1 E LEU -138 ? E LEU 204  
2393 1 Y 1 E THR -137 ? E THR 205  
2394 1 Y 1 E PHE -136 ? E PHE 206  
2395 1 Y 1 E LEU -135 ? E LEU 207  
2396 1 Y 1 E VAL -134 ? E VAL 208  
2397 1 Y 1 E ASP -133 ? E ASP 209  
2398 1 Y 1 E LEU -132 ? E LEU 210  
2399 1 Y 1 E ILE -131 ? E ILE 211  
2400 1 Y 1 E LYS -130 ? E LYS 212  
2401 1 Y 1 E ASN -129 ? E ASN 213  
2402 1 Y 1 E LYS -128 ? E LYS 214  
2403 1 Y 1 E HIS -127 ? E HIS 215  
2404 1 Y 1 E MET -126 ? E MET 216  
2405 1 Y 1 E ASN -125 ? E ASN 217  
2406 1 Y 1 E ALA -124 ? E ALA 218  
2407 1 Y 1 E ASP -123 ? E ASP 219  
2408 1 Y 1 E THR -122 ? E THR 220  
2409 1 Y 1 E ASP -121 ? E ASP 221  
2410 1 Y 1 E TYR -120 ? E TYR 222  
2411 1 Y 1 E SER -119 ? E SER 223  
2412 1 Y 1 E ILE -118 ? E ILE 224  
2413 1 Y 1 E ALA -117 ? E ALA 225  
2414 1 Y 1 E GLU -116 ? E GLU 226  
2415 1 Y 1 E ALA -115 ? E ALA 227  
2416 1 Y 1 E ALA -114 ? E ALA 228  
2417 1 Y 1 E PHE -113 ? E PHE 229  
2418 1 Y 1 E ASN -112 ? E ASN 230  
2419 1 Y 1 E LYS -111 ? E LYS 231  
2420 1 Y 1 E GLY -110 ? E GLY 232  
2421 1 Y 1 E GLU -109 ? E GLU 233  
2422 1 Y 1 E THR -108 ? E THR 234  
2423 1 Y 1 E ALA -107 ? E ALA 235  
2424 1 Y 1 E MET -106 ? E MET 236  
2425 1 Y 1 E THR -105 ? E THR 237  
2426 1 Y 1 E ILE -104 ? E ILE 238  
2427 1 Y 1 E ASN -103 ? E ASN 239  
2428 1 Y 1 E GLY -102 ? E GLY 240  
2429 1 Y 1 E PRO -101 ? E PRO 241  
2430 1 Y 1 E TRP -100 ? E TRP 242  
2431 1 Y 1 E ALA -99  ? E ALA 243  
2432 1 Y 1 E TRP -98  ? E TRP 244  
2433 1 Y 1 E SER -97  ? E SER 245  
2434 1 Y 1 E ASN -96  ? E ASN 246  
2435 1 Y 1 E ILE -95  ? E ILE 247  
2436 1 Y 1 E ASP -94  ? E ASP 248  
2437 1 Y 1 E THR -93  ? E THR 249  
2438 1 Y 1 E SER -92  ? E SER 250  
2439 1 Y 1 E LYS -91  ? E LYS 251  
2440 1 Y 1 E VAL -90  ? E VAL 252  
2441 1 Y 1 E ASN -89  ? E ASN 253  
2442 1 Y 1 E TYR -88  ? E TYR 254  
2443 1 Y 1 E GLY -87  ? E GLY 255  
2444 1 Y 1 E VAL -86  ? E VAL 256  
2445 1 Y 1 E THR -85  ? E THR 257  
2446 1 Y 1 E VAL -84  ? E VAL 258  
2447 1 Y 1 E LEU -83  ? E LEU 259  
2448 1 Y 1 E PRO -82  ? E PRO 260  
2449 1 Y 1 E THR -81  ? E THR 261  
2450 1 Y 1 E PHE -80  ? E PHE 262  
2451 1 Y 1 E LYS -79  ? E LYS 263  
2452 1 Y 1 E GLY -78  ? E GLY 264  
2453 1 Y 1 E GLN -77  ? E GLN 265  
2454 1 Y 1 E PRO -76  ? E PRO 266  
2455 1 Y 1 E SER -75  ? E SER 267  
2456 1 Y 1 E LYS -74  ? E LYS 268  
2457 1 Y 1 E PRO -73  ? E PRO 269  
2458 1 Y 1 E PHE -72  ? E PHE 270  
2459 1 Y 1 E VAL -71  ? E VAL 271  
2460 1 Y 1 E GLY -70  ? E GLY 272  
2461 1 Y 1 E VAL -69  ? E VAL 273  
2462 1 Y 1 E LEU -68  ? E LEU 274  
2463 1 Y 1 E SER -67  ? E SER 275  
2464 1 Y 1 E ALA -66  ? E ALA 276  
2465 1 Y 1 E GLY -65  ? E GLY 277  
2466 1 Y 1 E ILE -64  ? E ILE 278  
2467 1 Y 1 E ASN -63  ? E ASN 279  
2468 1 Y 1 E ALA -62  ? E ALA 280  
2469 1 Y 1 E ALA -61  ? E ALA 281  
2470 1 Y 1 E SER -60  ? E SER 282  
2471 1 Y 1 E PRO -59  ? E PRO 283  
2472 1 Y 1 E ASN -58  ? E ASN 284  
2473 1 Y 1 E LYS -57  ? E LYS 285  
2474 1 Y 1 E GLU -56  ? E GLU 286  
2475 1 Y 1 E LEU -55  ? E LEU 287  
2476 1 Y 1 E ALA -54  ? E ALA 288  
2477 1 Y 1 E LYS -53  ? E LYS 289  
2478 1 Y 1 E GLU -52  ? E GLU 290  
2479 1 Y 1 E PHE -51  ? E PHE 291  
2480 1 Y 1 E LEU -50  ? E LEU 292  
2481 1 Y 1 E GLU -49  ? E GLU 293  
2482 1 Y 1 E ASN -48  ? E ASN 294  
2483 1 Y 1 E TYR -47  ? E TYR 295  
2484 1 Y 1 E LEU -46  ? E LEU 296  
2485 1 Y 1 E LEU -45  ? E LEU 297  
2486 1 Y 1 E THR -44  ? E THR 298  
2487 1 Y 1 E ASP -43  ? E ASP 299  
2488 1 Y 1 E GLU -42  ? E GLU 300  
2489 1 Y 1 E GLY -41  ? E GLY 301  
2490 1 Y 1 E LEU -40  ? E LEU 302  
2491 1 Y 1 E GLU -39  ? E GLU 303  
2492 1 Y 1 E ALA -38  ? E ALA 304  
2493 1 Y 1 E VAL -37  ? E VAL 305  
2494 1 Y 1 E ASN -36  ? E ASN 306  
2495 1 Y 1 E LYS -35  ? E LYS 307  
2496 1 Y 1 E ASP -34  ? E ASP 308  
2497 1 Y 1 E LYS -33  ? E LYS 309  
2498 1 Y 1 E PRO -32  ? E PRO 310  
2499 1 Y 1 E LEU -31  ? E LEU 311  
2500 1 Y 1 E GLY -30  ? E GLY 312  
2501 1 Y 1 E ALA -29  ? E ALA 313  
2502 1 Y 1 E VAL -28  ? E VAL 314  
2503 1 Y 1 E ALA -27  ? E ALA 315  
2504 1 Y 1 E LEU -26  ? E LEU 316  
2505 1 Y 1 E LYS -25  ? E LYS 317  
2506 1 Y 1 E SER -24  ? E SER 318  
2507 1 Y 1 E TYR -23  ? E TYR 319  
2508 1 Y 1 E GLU -22  ? E GLU 320  
2509 1 Y 1 E GLU -21  ? E GLU 321  
2510 1 Y 1 E GLU -20  ? E GLU 322  
2511 1 Y 1 E LEU -19  ? E LEU 323  
2512 1 Y 1 E ALA -18  ? E ALA 324  
2513 1 Y 1 E LYS -17  ? E LYS 325  
2514 1 Y 1 E ASP -16  ? E ASP 326  
2515 1 Y 1 E PRO -15  ? E PRO 327  
2516 1 Y 1 E ARG -14  ? E ARG 328  
2517 1 Y 1 E ILE -13  ? E ILE 329  
2518 1 Y 1 E ALA -12  ? E ALA 330  
2519 1 Y 1 E ALA -11  ? E ALA 331  
2520 1 Y 1 E THR -10  ? E THR 332  
2521 1 Y 1 E MET -9   ? E MET 333  
2522 1 Y 1 E GLU -8   ? E GLU 334  
2523 1 Y 1 E ASN -7   ? E ASN 335  
2524 1 Y 1 E ALA -6   ? E ALA 336  
2525 1 Y 1 E GLN -5   ? E GLN 337  
2526 1 Y 1 E LYS -4   ? E LYS 338  
2527 1 Y 1 E GLY -3   ? E GLY 339  
2528 1 Y 1 E GLU -2   ? E GLU 340  
2529 1 Y 1 E ILE -1   ? E ILE 341  
2530 1 Y 1 E MET 0    ? E MET 342  
2531 1 Y 1 E PRO 1    ? E PRO 343  
2532 1 Y 1 E ASN 2    ? E ASN 344  
2533 1 Y 1 E ILE 3    ? E ILE 345  
2534 1 Y 1 E PRO 4    ? E PRO 346  
2535 1 Y 1 E GLN 5    ? E GLN 347  
2536 1 Y 1 E MET 6    ? E MET 348  
2537 1 Y 1 E SER 7    ? E SER 349  
2538 1 Y 1 E ALA 8    ? E ALA 350  
2539 1 Y 1 E PHE 9    ? E PHE 351  
2540 1 Y 1 E TRP 10   ? E TRP 352  
2541 1 Y 1 E TYR 11   ? E TYR 353  
2542 1 Y 1 E ALA 12   ? E ALA 354  
2543 1 Y 1 E VAL 13   ? E VAL 355  
2544 1 Y 1 E ARG 14   ? E ARG 356  
2545 1 Y 1 E THR 15   ? E THR 357  
2546 1 Y 1 E ALA 16   ? E ALA 358  
2547 1 Y 1 E VAL 17   ? E VAL 359  
2548 1 Y 1 E ILE 18   ? E ILE 360  
2549 1 Y 1 E ASN 19   ? E ASN 361  
2550 1 Y 1 E ALA 20   ? E ALA 362  
2551 1 Y 1 E ALA 21   ? E ALA 363  
2552 1 Y 1 E SER 22   ? E SER 364  
2553 1 Y 1 E GLY 23   ? E GLY 365  
2554 1 Y 1 E ARG 24   ? E ARG 366  
2555 1 Y 1 E GLN 25   ? E GLN 367  
2556 1 Y 1 E THR 26   ? E THR 368  
2557 1 Y 1 E VAL 27   ? E VAL 369  
2558 1 Y 1 E ASP 28   ? E ASP 370  
2559 1 Y 1 E GLU 29   ? E GLU 371  
2560 1 Y 1 E ALA 30   ? E ALA 372  
2561 1 Y 1 E LEU 31   ? E LEU 373  
2562 1 Y 1 E LYS 32   ? E LYS 374  
2563 1 Y 1 E ASP 33   ? E ASP 375  
2564 1 Y 1 E ALA 34   ? E ALA 376  
2565 1 Y 1 E GLN 35   ? E GLN 377  
2566 1 Y 1 E THR 36   ? E THR 378  
2567 1 Y 1 E GLY 37   ? E GLY 379  
2568 1 Y 1 E THR 38   ? E THR 380  
2569 1 Y 1 E ASP 39   ? E ASP 381  
2570 1 Y 1 E TYR 40   ? E TYR 382  
2571 1 Y 1 E ASP 41   ? E ASP 383  
2572 1 Y 1 E ILE 42   ? E ILE 384  
2573 1 Y 1 E PRO 43   ? E PRO 385  
2574 1 Y 1 E THR 44   ? E THR 386  
2575 1 Y 1 E THR 45   ? E THR 387  
2576 1 Y 1 E LEU 46   ? E LEU 388  
2577 1 Y 1 E GLU 47   ? E GLU 389  
2578 1 Y 1 E VAL 48   ? E VAL 390  
2579 1 Y 1 E LEU 49   ? E LEU 391  
2580 1 Y 1 E PHE 50   ? E PHE 392  
2581 1 Y 1 E GLN 51   ? E GLN 393  
2582 1 Y 1 E GLY 52   ? E GLY 394  
2583 1 Y 1 E PRO 53   ? E PRO 395  
2584 1 Y 1 E LEU 54   ? E LEU 396  
2585 1 Y 1 E GLY 55   ? E GLY 397  
2586 1 Y 1 E SER 56   ? E SER 398  
2587 1 Y 1 E SER 57   ? E SER 399  
2588 1 Y 1 E THR 58   ? E THR 400  
2589 1 Y 1 E ASP 59   ? E ASP 401  
2590 1 Y 1 E ASP 60   ? E ASP 402  
2591 1 Y 1 E ILE 61   ? E ILE 403  
2592 1 Y 1 E ILE 62   ? E ILE 404  
2593 1 Y 1 E TRP 63   ? E TRP 405  
2594 1 Y 1 E ASP 64   ? E ASP 406  
2595 1 Y 1 E GLN 65   ? E GLN 407  
2596 1 Y 1 E LEU 66   ? E LEU 408  
2597 1 Y 1 E ILE 67   ? E ILE 409  
2598 1 Y 1 E VAL 68   ? E VAL 410  
2599 1 Y 1 E LYS 69   ? E LYS 411  
2600 1 Y 1 E ARG 70   ? E ARG 412  
2601 1 Y 1 E THR 71   ? E THR 413  
2602 1 Y 1 E LEU 72   ? E LEU 414  
2603 1 Y 1 E ALA 73   ? E ALA 415  
2604 1 Y 1 E ASP 74   ? E ASP 416  
2605 1 Y 1 E LEU 75   ? E LEU 417  
2606 1 Y 1 E LEU 76   ? E LEU 418  
2607 1 Y 1 E ILE 77   ? E ILE 419  
2608 1 Y 1 E PRO 78   ? E PRO 420  
2609 1 Y 1 E ILE 79   ? E ILE 421  
2610 1 Y 1 E ASN 80   ? E ASN 422  
2611 1 Y 1 E ARG 81   ? E ARG 423  
2612 1 Y 1 E GLN 82   ? E GLN 424  
2613 1 Y 1 E ILE 83   ? E ILE 425  
2614 1 Y 1 E SER 84   ? E SER 426  
2615 1 Y 1 E ASP 85   ? E ASP 427  
2616 1 Y 1 E ILE 86   ? E ILE 428  
2617 1 Y 1 E GLN 87   ? E GLN 429  
2618 1 Y 1 E SER 88   ? E SER 430  
2619 1 Y 1 E THR 89   ? E THR 431  
2620 1 Y 1 E LEU 90   ? E LEU 432  
2621 1 Y 1 E SER 91   ? E SER 433  
2622 1 Y 1 E GLU 92   ? E GLU 434  
2623 1 Y 1 E VAL 93   ? E VAL 435  
2624 1 Y 1 E THR 94   ? E THR 436  
2625 1 Y 1 E THR 95   ? E THR 437  
2626 1 Y 1 E ARG 96   ? E ARG 438  
2627 1 Y 1 E VAL 97   ? E VAL 439  
2628 1 Y 1 E HIS 98   ? E HIS 440  
2629 1 Y 1 E GLU 99   ? E GLU 441  
2630 1 Y 1 E ILE 100  ? E ILE 442  
2631 1 Y 1 E GLU 101  ? E GLU 443  
2632 1 Y 1 E ARG 102  ? E ARG 444  
2633 1 Y 1 E GLN 103  ? E GLN 445  
2634 1 Y 1 E LEU 104  ? E LEU 446  
2635 1 Y 1 E HIS 105  ? E HIS 447  
2636 1 Y 1 E GLU 106  ? E GLU 448  
2637 1 Y 1 E ILE 107  ? E ILE 449  
2638 1 Y 1 E THR 108  ? E THR 450  
2639 1 Y 1 E PRO 109  ? E PRO 451  
2640 1 Y 1 E ILE 136  ? E ILE 478  
2641 1 Y 1 E SER 137  ? E SER 479  
2642 1 Y 1 E THR 138  ? E THR 480  
2643 1 Y 1 E GLY 139  ? E GLY 481  
2644 1 Y 1 E ARG 140  ? E ARG 482  
2645 1 Y 1 E THR 141  ? E THR 483  
2646 1 Y 1 E THR 142  ? E THR 484  
2647 1 Y 1 E ALA 143  ? E ALA 485  
2648 1 Y 1 E PRO 144  ? E PRO 486  
2649 1 Y 1 E ALA 145  ? E ALA 487  
2650 1 Y 1 E ALA 146  ? E ALA 488  
2651 1 Y 1 E ALA 147  ? E ALA 489  
2652 1 Y 1 E PHE 148  ? E PHE 490  
2653 1 Y 1 E ASP 149  ? E ASP 491  
2654 1 Y 1 E ALA 150  ? E ALA 492  
2655 1 Y 1 E TYR 151  ? E TYR 493  
2656 1 Y 1 E LEU 152  ? E LEU 494  
2657 1 Y 1 E ASN 153  ? E ASN 495  
2658 1 Y 1 E GLU 154  ? E GLU 496  
2659 1 Y 1 E HIS 155  ? E HIS 497  
2660 1 Y 1 E GLY 156  ? E GLY 498  
2661 1 Y 1 E VAL 157  ? E VAL 499  
2662 1 Y 1 E PRO 158  ? E PRO 500  
2663 1 Y 1 E PRO 159  ? E PRO 501  
2664 1 Y 1 E PRO 160  ? E PRO 502  
2665 1 Y 1 E GLN 161  ? E GLN 503  
2666 1 Y 1 E PRO 162  ? E PRO 504  
2667 1 Y 1 E ALA 163  ? E ALA 505  
2668 1 Y 1 E ILE 164  ? E ILE 506  
2669 1 Y 1 E PHE 165  ? E PHE 507  
2670 1 Y 1 E LYS 166  ? E LYS 508  
2671 1 Y 1 E ASP 167  ? E ASP 509  
2672 1 Y 1 E LEU 168  ? E LEU 510  
2673 1 Y 1 E GLY 169  ? E GLY 511  
2674 1 Y 1 E VAL 170  ? E VAL 512  
2675 1 Y 1 E ALA 171  ? E ALA 513  
2676 1 Y 1 E GLN 172  ? E GLN 514  
2677 1 Y 1 E GLN 173  ? E GLN 515  
2678 1 Y 1 E ALA 174  ? E ALA 516  
2679 1 Y 1 E CYS 175  ? E CYS 517  
2680 1 Y 1 E SER 176  ? E SER 518  
2681 1 Y 1 E LYS 177  ? E LYS 519  
2682 1 Y 1 E GLY 178  ? E GLY 520  
2683 1 Y 1 E THR 179  ? E THR 521  
2684 1 Y 1 E MET 180  ? E MET 522  
2685 1 Y 1 E VAL 181  ? E VAL 523  
2686 1 Y 1 E LYS 182  ? E LYS 524  
2687 1 Y 1 E ASN 183  ? E ASN 525  
2688 1 Y 1 E ALA 184  ? E ALA 526  
2689 1 Y 1 E THR 185  ? E THR 527  
2690 1 Y 1 E THR 186  ? E THR 528  
2691 1 Y 1 E ASP 187  ? E ASP 529  
2692 1 Y 1 E ALA 188  ? E ALA 530  
2693 1 Y 1 E ALA 189  ? E ALA 531  
2694 1 Y 1 E ASP 190  ? E ASP 532  
2695 1 Y 1 E LYS 191  ? E LYS 533  
2696 1 Y 1 E MET 192  ? E MET 534  
2697 1 Y 1 E SER 193  ? E SER 535  
2698 1 Y 1 E LYS 194  ? E LYS 536  
2699 1 Y 1 E VAL 195  ? E VAL 537  
2700 1 Y 1 E LEU 196  ? E LEU 538  
2701 1 Y 1 E GLU 197  ? E GLU 539  
2702 1 Y 1 E LEU 198  ? E LEU 540  
2703 1 Y 1 E SER 199  ? E SER 541  
2704 1 Y 1 E GLU 200  ? E GLU 542  
2705 1 Y 1 E GLU 201  ? E GLU 543  
2706 1 Y 1 E THR 202  ? E THR 544  
2707 1 Y 1 E PHE 203  ? E PHE 545  
2708 1 Y 1 E SER 204  ? E SER 546  
2709 1 Y 1 E LYS 205  ? E LYS 547  
2710 1 Y 1 E PRO 206  ? E PRO 548  
2711 1 Y 1 E ASN 207  ? E ASN 549  
2712 1 Y 1 E LEU 208  ? E LEU 550  
2713 1 Y 1 E SER 209  ? E SER 551  
2714 1 Y 1 E ALA 210  ? E ALA 552  
2715 1 Y 1 E LYS 211  ? E LYS 553  
2716 1 Y 1 E ASP 212  ? E ASP 554  
2717 1 Y 1 E LEU 213  ? E LEU 555  
2718 1 Y 1 E ALA 214  ? E ALA 556  
2719 1 Y 1 E LEU 215  ? E LEU 557  
2720 1 Y 1 E LEU 216  ? E LEU 558  
2721 1 Y 1 E LEU 217  ? E LEU 559  
2722 1 Y 1 E PHE 218  ? E PHE 560  
2723 1 Y 1 E THR 219  ? E THR 561  
2724 1 Y 1 E HIS 220  ? E HIS 562  
2725 1 Y 1 E LEU 221  ? E LEU 563  
2726 1 Y 1 E PRO 222  ? E PRO 564  
2727 1 Y 1 E GLY 223  ? E GLY 565  
2728 1 Y 1 E ASN 224  ? E ASN 566  
2729 1 Y 1 E ASN 225  ? E ASN 567  
2730 1 Y 1 E THR 226  ? E THR 568  
2731 1 Y 1 E PRO 227  ? E PRO 569  
2732 1 Y 1 E PHE 228  ? E PHE 570  
2733 1 Y 1 E HIS 229  ? E HIS 571  
2734 1 Y 1 E ILE 230  ? E ILE 572  
2735 1 Y 1 E LEU 231  ? E LEU 573  
2736 1 Y 1 E ALA 232  ? E ALA 574  
2737 1 Y 1 E GLN 233  ? E GLN 575  
2738 1 Y 1 E VAL 234  ? E VAL 576  
2739 1 Y 1 E LEU 235  ? E LEU 577  
2740 1 Y 1 E SER 236  ? E SER 578  
2741 1 Y 1 E LYS 237  ? E LYS 579  
2742 1 Y 1 E ILE 238  ? E ILE 580  
2743 1 Y 1 E ALA 239  ? E ALA 581  
2744 1 Y 1 E TYR 240  ? E TYR 582  
2745 1 Y 1 E LYS 241  ? E LYS 583  
2746 1 Y 1 E SER 242  ? E SER 584  
2747 1 Y 1 E GLY 243  ? E GLY 585  
2748 1 Y 1 E LYS 244  ? E LYS 586  
2749 1 Y 1 E SER 245  ? E SER 587  
2750 1 Y 1 E GLY 246  ? E GLY 588  
2751 1 Y 1 E ALA 247  ? E ALA 589  
2752 1 Y 1 E PHE 248  ? E PHE 590  
2753 1 Y 1 E LEU 249  ? E LEU 591  
2754 1 Y 1 E ASP 250  ? E ASP 592  
2755 1 Y 1 E ALA 251  ? E ALA 593  
2756 1 Y 1 E PHE 252  ? E PHE 594  
2757 1 Y 1 E HIS 253  ? E HIS 595  
2758 1 Y 1 E GLN 254  ? E GLN 596  
2759 1 Y 1 E ILE 255  ? E ILE 597  
2760 1 Y 1 E LEU 256  ? E LEU 598  
2761 1 Y 1 E SER 257  ? E SER 599  
2762 1 Y 1 E GLU 258  ? E GLU 600  
2763 1 Y 1 E GLY 259  ? E GLY 601  
2764 1 Y 1 E GLU 260  ? E GLU 602  
2765 1 Y 1 E ASN 261  ? E ASN 603  
2766 1 Y 1 E ALA 262  ? E ALA 604  
2767 1 Y 1 E GLN 263  ? E GLN 605  
2768 1 Y 1 E ALA 264  ? E ALA 606  
2769 1 Y 1 E ALA 265  ? E ALA 607  
2770 1 Y 1 E LEU 266  ? E LEU 608  
2771 1 Y 1 E THR 267  ? E THR 609  
2772 1 Y 1 E ARG 268  ? E ARG 610  
2773 1 Y 1 E LEU 269  ? E LEU 611  
2774 1 Y 1 E SER 270  ? E SER 612  
2775 1 Y 1 E ARG 271  ? E ARG 613  
2776 1 Y 1 E THR 272  ? E THR 614  
2777 1 Y 1 E PHE 273  ? E PHE 615  
2778 1 Y 1 E ASP 274  ? E ASP 616  
2779 1 Y 1 E ALA 275  ? E ALA 617  
2780 1 Y 1 E PHE 276  ? E PHE 618  
2781 1 Y 1 E LEU 277  ? E LEU 619  
2782 1 Y 1 E GLY 278  ? E GLY 620  
2783 1 Y 1 E VAL 279  ? E VAL 621  
2784 1 Y 1 E VAL 280  ? E VAL 622  
2785 1 Y 1 E PRO 281  ? E PRO 623  
2786 1 Y 1 E PRO 282  ? E PRO 624  
2787 1 Y 1 E VAL 283  ? E VAL 625  
2788 1 Y 1 E ILE 284  ? E ILE 626  
2789 1 Y 1 E ARG 285  ? E ARG 627  
2790 1 Y 1 E VAL 286  ? E VAL 628  
2791 1 Y 1 E LYS 287  ? E LYS 629  
2792 1 Y 1 E ASN 288  ? E ASN 630  
2793 1 Y 1 E PHE 289  ? E PHE 631  
2794 1 Y 1 E GLN 290  ? E GLN 632  
2795 1 Y 1 E THR 291  ? E THR 633  
2796 1 Y 1 E VAL 292  ? E VAL 634  
2797 1 Y 1 E PRO 293  ? E PRO 635  
2798 1 Y 1 E ARG 294  ? E ARG 636  
2799 1 Y 1 E PRO 295  ? E PRO 637  
2800 1 Y 1 E CYS 296  ? E CYS 638  
2801 1 Y 1 E GLN 297  ? E GLN 639  
2802 1 Y 1 E LYS 298  ? E LYS 640  
2803 1 Y 1 E SER 299  ? E SER 641  
2804 1 Y 1 E LEU 300  ? E LEU 642  
2805 1 Y 1 E ARG 301  ? E ARG 643  
2806 1 Y 1 E ALA 302  ? E ALA 644  
2807 1 Y 1 E VAL 303  ? E VAL 645  
2808 1 Y 1 E PRO 304  ? E PRO 646  
2809 1 Y 1 E PRO 305  ? E PRO 647  
2810 1 Y 1 E ASN 306  ? E ASN 648  
2811 1 Y 1 E PRO 307  ? E PRO 649  
2812 1 Y 1 E THR 308  ? E THR 650  
2813 1 Y 1 E ILE 309  ? E ILE 651  
2814 1 Y 1 E ASP 310  ? E ASP 652  
2815 1 Y 1 E LYS 311  ? E LYS 653  
2816 1 Y 1 E GLY 312  ? E GLY 654  
2817 1 Y 1 E TRP 313  ? E TRP 655  
2818 1 Y 1 E VAL 314  ? E VAL 656  
2819 1 Y 1 E CYS 315  ? E CYS 657  
2820 1 Y 1 E VAL 316  ? E VAL 658  
2821 1 Y 1 E TYR 317  ? E TYR 659  
2822 1 Y 1 E SER 318  ? E SER 660  
2823 1 Y 1 E SER 319  ? E SER 661  
2824 1 Y 1 E GLU 320  ? E GLU 662  
2825 1 Y 1 E GLN 321  ? E GLN 663  
2826 1 Y 1 E GLY 322  ? E GLY 664  
2827 1 Y 1 E GLU 323  ? E GLU 665  
2828 1 Y 1 E THR 324  ? E THR 666  
2829 1 Y 1 E ARG 325  ? E ARG 667  
2830 1 Y 1 E ALA 326  ? E ALA 668  
2831 1 Y 1 E LEU 327  ? E LEU 669  
2832 1 Y 1 E LYS 328  ? E LYS 670  
2833 1 Y 1 E ILE 329  ? E ILE 671  
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
ILE N    N  N N 158 
ILE CA   C  N S 159 
ILE C    C  N N 160 
ILE O    O  N N 161 
ILE CB   C  N S 162 
ILE CG1  C  N N 163 
ILE CG2  C  N N 164 
ILE CD1  C  N N 165 
ILE OXT  O  N N 166 
ILE H    H  N N 167 
ILE H2   H  N N 168 
ILE HA   H  N N 169 
ILE HB   H  N N 170 
ILE HG12 H  N N 171 
ILE HG13 H  N N 172 
ILE HG21 H  N N 173 
ILE HG22 H  N N 174 
ILE HG23 H  N N 175 
ILE HD11 H  N N 176 
ILE HD12 H  N N 177 
ILE HD13 H  N N 178 
ILE HXT  H  N N 179 
LEU N    N  N N 180 
LEU CA   C  N S 181 
LEU C    C  N N 182 
LEU O    O  N N 183 
LEU CB   C  N N 184 
LEU CG   C  N N 185 
LEU CD1  C  N N 186 
LEU CD2  C  N N 187 
LEU OXT  O  N N 188 
LEU H    H  N N 189 
LEU H2   H  N N 190 
LEU HA   H  N N 191 
LEU HB2  H  N N 192 
LEU HB3  H  N N 193 
LEU HG   H  N N 194 
LEU HD11 H  N N 195 
LEU HD12 H  N N 196 
LEU HD13 H  N N 197 
LEU HD21 H  N N 198 
LEU HD22 H  N N 199 
LEU HD23 H  N N 200 
LEU HXT  H  N N 201 
LYS N    N  N N 202 
LYS CA   C  N S 203 
LYS C    C  N N 204 
LYS O    O  N N 205 
LYS CB   C  N N 206 
LYS CG   C  N N 207 
LYS CD   C  N N 208 
LYS CE   C  N N 209 
LYS NZ   N  N N 210 
LYS OXT  O  N N 211 
LYS H    H  N N 212 
LYS H2   H  N N 213 
LYS HA   H  N N 214 
LYS HB2  H  N N 215 
LYS HB3  H  N N 216 
LYS HG2  H  N N 217 
LYS HG3  H  N N 218 
LYS HD2  H  N N 219 
LYS HD3  H  N N 220 
LYS HE2  H  N N 221 
LYS HE3  H  N N 222 
LYS HZ1  H  N N 223 
LYS HZ2  H  N N 224 
LYS HZ3  H  N N 225 
LYS HXT  H  N N 226 
MET N    N  N N 227 
MET CA   C  N S 228 
MET C    C  N N 229 
MET O    O  N N 230 
MET CB   C  N N 231 
MET CG   C  N N 232 
MET SD   S  N N 233 
MET CE   C  N N 234 
MET OXT  O  N N 235 
MET H    H  N N 236 
MET H2   H  N N 237 
MET HA   H  N N 238 
MET HB2  H  N N 239 
MET HB3  H  N N 240 
MET HG2  H  N N 241 
MET HG3  H  N N 242 
MET HE1  H  N N 243 
MET HE2  H  N N 244 
MET HE3  H  N N 245 
MET HXT  H  N N 246 
PHE N    N  N N 247 
PHE CA   C  N S 248 
PHE C    C  N N 249 
PHE O    O  N N 250 
PHE CB   C  N N 251 
PHE CG   C  Y N 252 
PHE CD1  C  Y N 253 
PHE CD2  C  Y N 254 
PHE CE1  C  Y N 255 
PHE CE2  C  Y N 256 
PHE CZ   C  Y N 257 
PHE OXT  O  N N 258 
PHE H    H  N N 259 
PHE H2   H  N N 260 
PHE HA   H  N N 261 
PHE HB2  H  N N 262 
PHE HB3  H  N N 263 
PHE HD1  H  N N 264 
PHE HD2  H  N N 265 
PHE HE1  H  N N 266 
PHE HE2  H  N N 267 
PHE HZ   H  N N 268 
PHE HXT  H  N N 269 
PRO N    N  N N 270 
PRO CA   C  N S 271 
PRO C    C  N N 272 
PRO O    O  N N 273 
PRO CB   C  N N 274 
PRO CG   C  N N 275 
PRO CD   C  N N 276 
PRO OXT  O  N N 277 
PRO H    H  N N 278 
PRO HA   H  N N 279 
PRO HB2  H  N N 280 
PRO HB3  H  N N 281 
PRO HG2  H  N N 282 
PRO HG3  H  N N 283 
PRO HD2  H  N N 284 
PRO HD3  H  N N 285 
PRO HXT  H  N N 286 
SER N    N  N N 287 
SER CA   C  N S 288 
SER C    C  N N 289 
SER O    O  N N 290 
SER CB   C  N N 291 
SER OG   O  N N 292 
SER OXT  O  N N 293 
SER H    H  N N 294 
SER H2   H  N N 295 
SER HA   H  N N 296 
SER HB2  H  N N 297 
SER HB3  H  N N 298 
SER HG   H  N N 299 
SER HXT  H  N N 300 
THR N    N  N N 301 
THR CA   C  N S 302 
THR C    C  N N 303 
THR O    O  N N 304 
THR CB   C  N R 305 
THR OG1  O  N N 306 
THR CG2  C  N N 307 
THR OXT  O  N N 308 
THR H    H  N N 309 
THR H2   H  N N 310 
THR HA   H  N N 311 
THR HB   H  N N 312 
THR HG1  H  N N 313 
THR HG21 H  N N 314 
THR HG22 H  N N 315 
THR HG23 H  N N 316 
THR HXT  H  N N 317 
TRP N    N  N N 318 
TRP CA   C  N S 319 
TRP C    C  N N 320 
TRP O    O  N N 321 
TRP CB   C  N N 322 
TRP CG   C  Y N 323 
TRP CD1  C  Y N 324 
TRP CD2  C  Y N 325 
TRP NE1  N  Y N 326 
TRP CE2  C  Y N 327 
TRP CE3  C  Y N 328 
TRP CZ2  C  Y N 329 
TRP CZ3  C  Y N 330 
TRP CH2  C  Y N 331 
TRP OXT  O  N N 332 
TRP H    H  N N 333 
TRP H2   H  N N 334 
TRP HA   H  N N 335 
TRP HB2  H  N N 336 
TRP HB3  H  N N 337 
TRP HD1  H  N N 338 
TRP HE1  H  N N 339 
TRP HE3  H  N N 340 
TRP HZ2  H  N N 341 
TRP HZ3  H  N N 342 
TRP HH2  H  N N 343 
TRP HXT  H  N N 344 
TYR N    N  N N 345 
TYR CA   C  N S 346 
TYR C    C  N N 347 
TYR O    O  N N 348 
TYR CB   C  N N 349 
TYR CG   C  Y N 350 
TYR CD1  C  Y N 351 
TYR CD2  C  Y N 352 
TYR CE1  C  Y N 353 
TYR CE2  C  Y N 354 
TYR CZ   C  Y N 355 
TYR OH   O  N N 356 
TYR OXT  O  N N 357 
TYR H    H  N N 358 
TYR H2   H  N N 359 
TYR HA   H  N N 360 
TYR HB2  H  N N 361 
TYR HB3  H  N N 362 
TYR HD1  H  N N 363 
TYR HD2  H  N N 364 
TYR HE1  H  N N 365 
TYR HE2  H  N N 366 
TYR HH   H  N N 367 
TYR HXT  H  N N 368 
VAL N    N  N N 369 
VAL CA   C  N S 370 
VAL C    C  N N 371 
VAL O    O  N N 372 
VAL CB   C  N N 373 
VAL CG1  C  N N 374 
VAL CG2  C  N N 375 
VAL OXT  O  N N 376 
VAL H    H  N N 377 
VAL H2   H  N N 378 
VAL HA   H  N N 379 
VAL HB   H  N N 380 
VAL HG11 H  N N 381 
VAL HG12 H  N N 382 
VAL HG13 H  N N 383 
VAL HG21 H  N N 384 
VAL HG22 H  N N 385 
VAL HG23 H  N N 386 
VAL HXT  H  N N 387 
ZN  ZN   ZN N N 388 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-07-10 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           9IP4 
_em_admin.last_update        2025-04-16 
_em_admin.map_release_date   2025-04-09 
_em_admin.title              'Cryo-EM structure of the RNA-dependent RNA polymerase complex from Marburg virus' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.5 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          33727 
_em_entity_assembly_naturalsource.organism             'Marburg virus - Musoke, Kenya, 1980' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         52.52 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 ? ? 
MASKING                         ? 3  ? ? ? ? ? 
'CTF CORRECTION'                ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ? ? 
'MODEL FITTING'                 ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'              ? 8  ? ? ? ? ? 
OTHER                           ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ? ? 
CLASSIFICATION                  ? 12 1 ? ? ? ? 
RECONSTRUCTION                  ? 13 1 ? ? ? ? 
'VOLUME SELECTION'              ? 14 1 1 1 ? ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ? ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ? ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ? ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ? ? 
# 
_em_specimen.concentration           1.2 
_em_specimen.details                 'This sample is monodisperse.' 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           32371344 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9IP4 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
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   . PRO A 1 4    ? 83.481  105.840 91.075  1.00 144.69 ? 4    PRO A N   1 
ATOM   2     C  CA  . PRO A 1 4    ? 84.344  105.586 89.916  1.00 139.59 ? 4    PRO A CA  1 
ATOM   3     C  C   . PRO A 1 4    ? 85.762  106.115 90.112  1.00 144.05 ? 4    PRO A C   1 
ATOM   4     O  O   . PRO A 1 4    ? 86.728  105.412 89.810  1.00 137.96 ? 4    PRO A O   1 
ATOM   5     C  CB  . PRO A 1 4    ? 83.636  106.330 88.780  1.00 127.53 ? 4    PRO A CB  1 
ATOM   6     C  CG  . PRO A 1 4    ? 82.830  107.384 89.458  1.00 145.94 ? 4    PRO A CG  1 
ATOM   7     C  CD  . PRO A 1 4    ? 82.400  106.794 90.766  1.00 147.14 ? 4    PRO A CD  1 
ATOM   8     N  N   . THR A 1 5    ? 85.878  107.343 90.621  1.00 158.48 ? 5    THR A N   1 
ATOM   9     C  CA  . THR A 1 5    ? 87.196  107.942 90.805  1.00 161.59 ? 5    THR A CA  1 
ATOM   10    C  C   . THR A 1 5    ? 87.968  107.221 91.900  1.00 158.45 ? 5    THR A C   1 
ATOM   11    O  O   . THR A 1 5    ? 89.189  107.054 91.802  1.00 141.27 ? 5    THR A O   1 
ATOM   12    C  CB  . THR A 1 5    ? 87.061  109.427 91.136  1.00 160.81 ? 5    THR A CB  1 
ATOM   13    O  OG1 . THR A 1 5    ? 86.250  109.589 92.308  1.00 157.40 ? 5    THR A OG1 1 
ATOM   14    C  CG2 . THR A 1 5    ? 86.423  110.174 89.975  1.00 144.51 ? 5    THR A CG2 1 
ATOM   15    N  N   . GLN A 1 6    ? 87.275  106.793 92.947  1.00 159.75 ? 6    GLN A N   1 
ATOM   16    C  CA  . GLN A 1 6    ? 87.899  106.187 94.110  1.00 155.10 ? 6    GLN A CA  1 
ATOM   17    C  C   . GLN A 1 6    ? 87.480  104.728 94.204  1.00 144.85 ? 6    GLN A C   1 
ATOM   18    O  O   . GLN A 1 6    ? 86.333  104.376 93.908  1.00 140.44 ? 6    GLN A O   1 
ATOM   19    C  CB  . GLN A 1 6    ? 87.551  106.953 95.386  1.00 156.36 ? 6    GLN A CB  1 
ATOM   20    C  CG  . GLN A 1 6    ? 88.214  108.317 95.407  1.00 163.64 ? 6    GLN A CG  1 
ATOM   21    C  CD  . GLN A 1 6    ? 88.065  109.036 96.723  1.00 167.06 ? 6    GLN A CD  1 
ATOM   22    O  OE1 . GLN A 1 6    ? 87.637  108.457 97.721  1.00 166.03 ? 6    GLN A OE1 1 
ATOM   23    N  NE2 . GLN A 1 6    ? 88.444  110.307 96.740  1.00 164.46 ? 6    GLN A NE2 1 
ATOM   24    N  N   . TYR A 1 7    ? 88.416  103.893 94.625  1.00 125.88 ? 7    TYR A N   1 
ATOM   25    C  CA  . TYR A 1 7    ? 88.255  102.453 94.723  1.00 115.86 ? 7    TYR A CA  1 
ATOM   26    C  C   . TYR A 1 7    ? 88.855  101.995 96.038  1.00 112.62 ? 7    TYR A C   1 
ATOM   27    O  O   . TYR A 1 7    ? 89.597  102.746 96.681  1.00 108.48 ? 7    TYR A O   1 
ATOM   28    C  CB  . TYR A 1 7    ? 88.958  101.722 93.571  1.00 120.13 ? 7    TYR A CB  1 
ATOM   29    C  CG  . TYR A 1 7    ? 88.324  101.918 92.221  1.00 118.01 ? 7    TYR A CG  1 
ATOM   30    C  CD1 . TYR A 1 7    ? 86.963  101.728 92.040  1.00 119.44 ? 7    TYR A CD1 1 
ATOM   31    C  CD2 . TYR A 1 7    ? 89.091  102.269 91.119  1.00 105.82 ? 7    TYR A CD2 1 
ATOM   32    C  CE1 . TYR A 1 7    ? 86.379  101.901 90.803  1.00 128.35 ? 7    TYR A CE1 1 
ATOM   33    C  CE2 . TYR A 1 7    ? 88.517  102.442 89.877  1.00 97.61  ? 7    TYR A CE2 1 
ATOM   34    C  CZ  . TYR A 1 7    ? 87.160  102.257 89.723  1.00 107.78 ? 7    TYR A CZ  1 
ATOM   35    O  OH  . TYR A 1 7    ? 86.583  102.429 88.486  1.00 107.23 ? 7    TYR A OH  1 
ATOM   36    N  N   . PRO A 1 8    ? 88.531  100.780 96.482  1.00 98.13  ? 8    PRO A N   1 
ATOM   37    C  CA  . PRO A 1 8    ? 89.168  100.269 97.696  1.00 84.76  ? 8    PRO A CA  1 
ATOM   38    C  C   . PRO A 1 8    ? 90.675  100.276 97.514  1.00 89.02  ? 8    PRO A C   1 
ATOM   39    O  O   . PRO A 1 8    ? 91.191  100.153 96.400  1.00 88.88  ? 8    PRO A O   1 
ATOM   40    C  CB  . PRO A 1 8    ? 88.618  98.844  97.815  1.00 82.70  ? 8    PRO A CB  1 
ATOM   41    C  CG  . PRO A 1 8    ? 87.295  98.910  97.141  1.00 80.29  ? 8    PRO A CG  1 
ATOM   42    C  CD  . PRO A 1 8    ? 87.466  99.879  96.003  1.00 91.79  ? 8    PRO A CD  1 
ATOM   43    N  N   . ASP A 1 9    ? 91.381  100.437 98.625  1.00 97.68  ? 9    ASP A N   1 
ATOM   44    C  CA  . ASP A 1 9    ? 92.817  100.636 98.564  1.00 96.43  ? 9    ASP A CA  1 
ATOM   45    C  C   . ASP A 1 9    ? 93.484  99.382  98.015  1.00 97.83  ? 9    ASP A C   1 
ATOM   46    O  O   . ASP A 1 9    ? 93.094  98.258  98.339  1.00 92.13  ? 9    ASP A O   1 
ATOM   47    C  CB  . ASP A 1 9    ? 93.355  100.987 99.951  1.00 113.89 ? 9    ASP A CB  1 
ATOM   48    C  CG  . ASP A 1 9    ? 94.409  102.071 99.907  1.00 133.23 ? 9    ASP A CG  1 
ATOM   49    O  OD1 . ASP A 1 9    ? 95.059  102.216 98.856  1.00 121.46 ? 9    ASP A OD1 1 
ATOM   50    O  OD2 . ASP A 1 9    ? 94.576  102.791 100.913 1.00 137.00 ? 9    ASP A OD2 1 
ATOM   51    N  N   . ALA A 1 10   ? 94.495  99.581  97.166  1.00 101.80 ? 10   ALA A N   1 
ATOM   52    C  CA  . ALA A 1 10   ? 95.174  98.444  96.554  1.00 89.18  ? 10   ALA A CA  1 
ATOM   53    C  C   . ALA A 1 10   ? 96.024  97.706  97.577  1.00 99.01  ? 10   ALA A C   1 
ATOM   54    O  O   . ALA A 1 10   ? 96.120  96.474  97.542  1.00 85.54  ? 10   ALA A O   1 
ATOM   55    C  CB  . ALA A 1 10   ? 96.029  98.912  95.376  1.00 79.43  ? 10   ALA A CB  1 
ATOM   56    N  N   . ARG A 1 11   ? 96.640  98.438  98.496  1.00 112.00 ? 11   ARG A N   1 
ATOM   57    C  CA  . ARG A 1 11   ? 97.450  97.852  99.549  1.00 91.21  ? 11   ARG A CA  1 
ATOM   58    C  C   . ARG A 1 11   ? 96.797  98.141  100.892 1.00 92.07  ? 11   ARG A C   1 
ATOM   59    O  O   . ARG A 1 11   ? 95.914  98.994  101.015 1.00 102.30 ? 11   ARG A O   1 
ATOM   60    C  CB  . ARG A 1 11   ? 98.870  98.422  99.527  1.00 106.88 ? 11   ARG A CB  1 
ATOM   61    C  CG  . ARG A 1 11   ? 99.635  98.127  98.262  1.00 105.36 ? 11   ARG A CG  1 
ATOM   62    C  CD  . ARG A 1 11   ? 101.013 98.746  98.330  1.00 109.65 ? 11   ARG A CD  1 
ATOM   63    N  NE  . ARG A 1 11   ? 101.645 98.799  97.018  1.00 106.64 ? 11   ARG A NE  1 
ATOM   64    C  CZ  . ARG A 1 11   ? 102.883 99.228  96.806  1.00 103.37 ? 11   ARG A CZ  1 
ATOM   65    N  NH1 . ARG A 1 11   ? 103.631 99.630  97.825  1.00 98.15  ? 11   ARG A NH1 1 
ATOM   66    N  NH2 . ARG A 1 11   ? 103.378 99.247  95.576  1.00 94.19  ? 11   ARG A NH2 1 
ATOM   67    N  N   . LEU A 1 12   ? 97.244  97.414  101.910 1.00 96.71  ? 12   LEU A N   1 
ATOM   68    C  CA  . LEU A 1 12   ? 96.668  97.541  103.243 1.00 107.16 ? 12   LEU A CA  1 
ATOM   69    C  C   . LEU A 1 12   ? 97.194  98.822  103.876 1.00 108.83 ? 12   LEU A C   1 
ATOM   70    O  O   . LEU A 1 12   ? 98.389  98.933  104.165 1.00 111.31 ? 12   LEU A O   1 
ATOM   71    C  CB  . LEU A 1 12   ? 97.005  96.323  104.096 1.00 96.94  ? 12   LEU A CB  1 
ATOM   72    C  CG  . LEU A 1 12   ? 96.651  96.490  105.572 1.00 83.71  ? 12   LEU A CG  1 
ATOM   73    C  CD1 . LEU A 1 12   ? 95.158  96.283  105.776 1.00 82.89  ? 12   LEU A CD1 1 
ATOM   74    C  CD2 . LEU A 1 12   ? 97.459  95.536  106.439 1.00 85.80  ? 12   LEU A CD2 1 
ATOM   75    N  N   . SER A 1 13   ? 96.305  99.801  104.090 1.00 98.07  ? 13   SER A N   1 
ATOM   76    C  CA  . SER A 1 13   ? 96.627  100.971 104.908 1.00 94.99  ? 13   SER A CA  1 
ATOM   77    C  C   . SER A 1 13   ? 95.397  101.280 105.760 1.00 96.91  ? 13   SER A C   1 
ATOM   78    O  O   . SER A 1 13   ? 94.585  102.148 105.427 1.00 99.22  ? 13   SER A O   1 
ATOM   79    C  CB  . SER A 1 13   ? 97.036  102.164 104.046 1.00 99.43  ? 13   SER A CB  1 
ATOM   80    O  OG  . SER A 1 13   ? 96.037  102.466 103.086 1.00 100.93 ? 13   SER A OG  1 
ATOM   81    N  N   . SER A 1 14   ? 95.293  100.573 106.887 1.00 98.21  ? 14   SER A N   1 
ATOM   82    C  CA  . SER A 1 14   ? 94.298  100.772 107.934 1.00 103.75 ? 14   SER A CA  1 
ATOM   83    C  C   . SER A 1 14   ? 94.533  99.735  109.026 1.00 100.80 ? 14   SER A C   1 
ATOM   84    O  O   . SER A 1 14   ? 95.072  98.656  108.748 1.00 102.48 ? 14   SER A O   1 
ATOM   85    C  CB  . SER A 1 14   ? 92.876  100.650 107.381 1.00 100.29 ? 14   SER A CB  1 
ATOM   86    O  OG  . SER A 1 14   ? 92.613  99.332  106.931 1.00 96.01  ? 14   SER A OG  1 
ATOM   87    N  N   . PRO A 1 15   ? 94.147  100.011 110.269 1.00 90.55  ? 15   PRO A N   1 
ATOM   88    C  CA  . PRO A 1 15   ? 94.187  98.969  111.301 1.00 83.88  ? 15   PRO A CA  1 
ATOM   89    C  C   . PRO A 1 15   ? 93.168  97.869  111.039 1.00 80.50  ? 15   PRO A C   1 
ATOM   90    O  O   . PRO A 1 15   ? 92.158  98.059  110.358 1.00 82.93  ? 15   PRO A O   1 
ATOM   91    C  CB  . PRO A 1 15   ? 93.863  99.735  112.588 1.00 80.57  ? 15   PRO A CB  1 
ATOM   92    C  CG  . PRO A 1 15   ? 93.072  100.916 112.123 1.00 86.88  ? 15   PRO A CG  1 
ATOM   93    C  CD  . PRO A 1 15   ? 93.689  101.303 110.809 1.00 88.11  ? 15   PRO A CD  1 
ATOM   94    N  N   . ILE A 1 16   ? 93.458  96.695  111.594 1.00 82.03  ? 16   ILE A N   1 
ATOM   95    C  CA  . ILE A 1 16   ? 92.604  95.520  111.453 1.00 87.85  ? 16   ILE A CA  1 
ATOM   96    C  C   . ILE A 1 16   ? 91.648  95.460  112.642 1.00 88.00  ? 16   ILE A C   1 
ATOM   97    O  O   . ILE A 1 16   ? 92.066  95.204  113.774 1.00 84.06  ? 16   ILE A O   1 
ATOM   98    C  CB  . ILE A 1 16   ? 93.421  94.230  111.332 1.00 81.52  ? 16   ILE A CB  1 
ATOM   99    C  CG1 . ILE A 1 16   ? 94.141  94.180  109.986 1.00 72.80  ? 16   ILE A CG1 1 
ATOM   100   C  CG2 . ILE A 1 16   ? 92.516  93.013  111.473 1.00 71.10  ? 16   ILE A CG2 1 
ATOM   101   C  CD1 . ILE A 1 16   ? 95.110  93.030  109.859 1.00 73.02  ? 16   ILE A CD1 1 
ATOM   102   N  N   . ILE A 1 17   ? 90.366  95.715  112.387 1.00 87.14  ? 17   ILE A N   1 
ATOM   103   C  CA  . ILE A 1 17   ? 89.326  95.711  113.410 1.00 70.42  ? 17   ILE A CA  1 
ATOM   104   C  C   . ILE A 1 17   ? 88.286  94.681  112.988 1.00 77.90  ? 17   ILE A C   1 
ATOM   105   O  O   . ILE A 1 17   ? 87.849  94.675  111.831 1.00 86.64  ? 17   ILE A O   1 
ATOM   106   C  CB  . ILE A 1 17   ? 88.687  97.100  113.593 1.00 86.05  ? 17   ILE A CB  1 
ATOM   107   C  CG1 . ILE A 1 17   ? 89.766  98.174  113.755 1.00 78.78  ? 17   ILE A CG1 1 
ATOM   108   C  CG2 . ILE A 1 17   ? 87.769  97.109  114.806 1.00 94.21  ? 17   ILE A CG2 1 
ATOM   109   C  CD1 . ILE A 1 17   ? 90.602  98.031  115.008 1.00 78.75  ? 17   ILE A CD1 1 
ATOM   110   N  N   . LEU A 1 18   ? 87.897  93.806  113.920 1.00 80.57  ? 18   LEU A N   1 
ATOM   111   C  CA  . LEU A 1 18   ? 86.996  92.689  113.641 1.00 76.89  ? 18   LEU A CA  1 
ATOM   112   C  C   . LEU A 1 18   ? 85.727  92.711  114.492 1.00 84.03  ? 18   LEU A C   1 
ATOM   113   O  O   . LEU A 1 18   ? 85.189  91.656  114.831 1.00 78.87  ? 18   LEU A O   1 
ATOM   114   C  CB  . LEU A 1 18   ? 87.729  91.362  113.820 1.00 73.90  ? 18   LEU A CB  1 
ATOM   115   C  CG  . LEU A 1 18   ? 88.855  91.125  112.817 1.00 75.85  ? 18   LEU A CG  1 
ATOM   116   C  CD1 . LEU A 1 18   ? 89.651  89.885  113.181 1.00 74.58  ? 18   LEU A CD1 1 
ATOM   117   C  CD2 . LEU A 1 18   ? 88.260  90.998  111.424 1.00 95.83  ? 18   LEU A CD2 1 
ATOM   118   N  N   . ASP A 1 19   ? 85.239  93.898  114.850 1.00 85.61  ? 19   ASP A N   1 
ATOM   119   C  CA  . ASP A 1 19   ? 84.018  93.988  115.649 1.00 72.83  ? 19   ASP A CA  1 
ATOM   120   C  C   . ASP A 1 19   ? 82.781  93.510  114.883 1.00 86.86  ? 19   ASP A C   1 
ATOM   121   O  O   . ASP A 1 19   ? 82.033  92.658  115.375 1.00 90.30  ? 19   ASP A O   1 
ATOM   122   C  CB  . ASP A 1 19   ? 83.834  95.421  116.144 1.00 89.68  ? 19   ASP A CB  1 
ATOM   123   C  CG  . ASP A 1 19   ? 84.610  95.695  117.415 1.00 110.13 ? 19   ASP A CG  1 
ATOM   124   O  OD1 . ASP A 1 19   ? 84.167  95.240  118.490 1.00 105.04 ? 19   ASP A OD1 1 
ATOM   125   O  OD2 . ASP A 1 19   ? 85.670  96.350  117.340 1.00 112.05 ? 19   ASP A OD2 1 
ATOM   126   N  N   . GLN A 1 20   ? 82.557  94.033  113.672 1.00 66.53  ? 20   GLN A N   1 
ATOM   127   C  CA  . GLN A 1 20   ? 81.347  93.719  112.906 1.00 64.73  ? 20   GLN A CA  1 
ATOM   128   C  C   . GLN A 1 20   ? 81.231  92.237  112.560 1.00 77.72  ? 20   GLN A C   1 
ATOM   129   O  O   . GLN A 1 20   ? 80.128  91.750  112.250 1.00 86.16  ? 20   GLN A O   1 
ATOM   130   C  CB  . GLN A 1 20   ? 81.300  94.546  111.618 1.00 60.74  ? 20   GLN A CB  1 
ATOM   131   C  CG  . GLN A 1 20   ? 82.421  94.243  110.631 1.00 80.47  ? 20   GLN A CG  1 
ATOM   132   C  CD  . GLN A 1 20   ? 83.743  94.876  111.022 1.00 89.31  ? 20   GLN A CD  1 
ATOM   133   O  OE1 . GLN A 1 20   ? 83.816  95.645  111.980 1.00 82.36  ? 20   GLN A OE1 1 
ATOM   134   N  NE2 . GLN A 1 20   ? 84.798  94.543  110.287 1.00 84.59  ? 20   GLN A NE2 1 
ATOM   135   N  N   . CYS A 1 21   ? 82.347  91.511  112.593 1.00 74.00  ? 21   CYS A N   1 
ATOM   136   C  CA  . CYS A 1 21   ? 82.289  90.078  112.353 1.00 62.35  ? 21   CYS A CA  1 
ATOM   137   C  C   . CYS A 1 21   ? 81.396  89.386  113.377 1.00 77.42  ? 21   CYS A C   1 
ATOM   138   O  O   . CYS A 1 21   ? 80.708  88.412  113.047 1.00 86.21  ? 21   CYS A O   1 
ATOM   139   C  CB  . CYS A 1 21   ? 83.705  89.502  112.381 1.00 57.30  ? 21   CYS A CB  1 
ATOM   140   S  SG  . CYS A 1 21   ? 84.782  90.162  111.082 1.00 89.39  ? 21   CYS A SG  1 
ATOM   141   N  N   . ASP A 1 22   ? 81.442  89.828  114.641 1.00 75.68  ? 22   ASP A N   1 
ATOM   142   C  CA  . ASP A 1 22   ? 80.534  89.280  115.646 1.00 76.12  ? 22   ASP A CA  1 
ATOM   143   C  C   . ASP A 1 22   ? 79.067  89.443  115.255 1.00 80.84  ? 22   ASP A C   1 
ATOM   144   O  O   . ASP A 1 22   ? 78.255  88.529  115.473 1.00 78.20  ? 22   ASP A O   1 
ATOM   145   C  CB  . ASP A 1 22   ? 80.779  89.984  116.982 1.00 80.59  ? 22   ASP A CB  1 
ATOM   146   C  CG  . ASP A 1 22   ? 81.857  89.320  117.802 1.00 98.16  ? 22   ASP A CG  1 
ATOM   147   O  OD1 . ASP A 1 22   ? 82.734  88.666  117.205 1.00 95.03  ? 22   ASP A OD1 1 
ATOM   148   O  OD2 . ASP A 1 22   ? 81.837  89.468  119.042 1.00 95.37  ? 22   ASP A OD2 1 
ATOM   149   N  N   . LEU A 1 23   ? 78.735  90.533  114.553 1.00 70.97  ? 23   LEU A N   1 
ATOM   150   C  CA  . LEU A 1 23   ? 77.354  90.756  114.146 1.00 65.06  ? 23   LEU A CA  1 
ATOM   151   C  C   . LEU A 1 23   ? 76.992  89.883  112.967 1.00 66.00  ? 23   LEU A C   1 
ATOM   152   O  O   . LEU A 1 23   ? 75.870  89.354  112.891 1.00 71.40  ? 23   LEU A O   1 
ATOM   153   C  CB  . LEU A 1 23   ? 77.145  92.229  113.797 1.00 59.71  ? 23   LEU A CB  1 
ATOM   154   C  CG  . LEU A 1 23   ? 77.328  93.186  114.971 1.00 58.17  ? 23   LEU A CG  1 
ATOM   155   C  CD1 . LEU A 1 23   ? 77.472  94.612  114.473 1.00 61.19  ? 23   LEU A CD1 1 
ATOM   156   C  CD2 . LEU A 1 23   ? 76.165  93.060  115.940 1.00 66.24  ? 23   LEU A CD2 1 
ATOM   157   N  N   . LEU A 1 24   ? 77.978  89.594  112.127 1.00 61.63  ? 24   LEU A N   1 
ATOM   158   C  CA  . LEU A 1 24   ? 77.694  88.723  110.999 1.00 57.73  ? 24   LEU A CA  1 
ATOM   159   C  C   . LEU A 1 24   ? 77.466  87.310  111.514 1.00 73.13  ? 24   LEU A C   1 
ATOM   160   O  O   . LEU A 1 24   ? 76.513  86.630  111.107 1.00 85.76  ? 24   LEU A O   1 
ATOM   161   C  CB  . LEU A 1 24   ? 78.820  88.771  109.971 1.00 60.19  ? 24   LEU A CB  1 
ATOM   162   C  CG  . LEU A 1 24   ? 78.570  87.825  108.796 1.00 64.94  ? 24   LEU A CG  1 
ATOM   163   C  CD1 . LEU A 1 24   ? 77.260  88.185  108.106 1.00 56.22  ? 24   LEU A CD1 1 
ATOM   164   C  CD2 . LEU A 1 24   ? 79.724  87.880  107.811 1.00 85.73  ? 24   LEU A CD2 1 
ATOM   165   N  N   . ALA A 1 25   ? 78.342  86.850  112.410 1.00 66.43  ? 25   ALA A N   1 
ATOM   166   C  CA  . ALA A 1 25   ? 78.175  85.510  112.950 1.00 63.32  ? 25   ALA A CA  1 
ATOM   167   C  C   . ALA A 1 25   ? 76.826  85.369  113.649 1.00 78.06  ? 25   ALA A C   1 
ATOM   168   O  O   . ALA A 1 25   ? 76.143  84.355  113.469 1.00 83.23  ? 25   ALA A O   1 
ATOM   169   C  CB  . ALA A 1 25   ? 79.319  85.178  113.907 1.00 68.56  ? 25   ALA A CB  1 
ATOM   170   N  N   . ARG A 1 26   ? 76.413  86.366  114.457 1.00 72.71  ? 26   ARG A N   1 
ATOM   171   C  CA  . ARG A 1 26   ? 75.094  86.213  115.075 1.00 63.01  ? 26   ARG A CA  1 
ATOM   172   C  C   . ARG A 1 26   ? 73.987  86.195  114.032 1.00 62.59  ? 26   ARG A C   1 
ATOM   173   O  O   . ARG A 1 26   ? 72.929  85.600  114.266 1.00 65.05  ? 26   ARG A O   1 
ATOM   174   C  CB  . ARG A 1 26   ? 74.728  87.283  116.100 1.00 72.69  ? 26   ARG A CB  1 
ATOM   175   C  CG  . ARG A 1 26   ? 75.315  87.128  117.478 1.00 101.80 ? 26   ARG A CG  1 
ATOM   176   C  CD  . ARG A 1 26   ? 75.425  88.497  118.084 1.00 86.62  ? 26   ARG A CD  1 
ATOM   177   N  NE  . ARG A 1 26   ? 74.054  88.928  118.363 1.00 63.67  ? 26   ARG A NE  1 
ATOM   178   C  CZ  . ARG A 1 26   ? 73.612  90.180  118.325 1.00 75.72  ? 26   ARG A CZ  1 
ATOM   179   N  NH1 . ARG A 1 26   ? 72.316  90.427  118.467 1.00 78.31  ? 26   ARG A NH1 1 
ATOM   180   N  NH2 . ARG A 1 26   ? 74.444  91.174  118.064 1.00 81.88  ? 26   ARG A NH2 1 
ATOM   181   N  N   . SER A 1 27   ? 74.207  86.824  112.874 1.00 73.39  ? 27   SER A N   1 
ATOM   182   C  CA  . SER A 1 27   ? 73.141  86.809  111.884 1.00 69.18  ? 27   SER A CA  1 
ATOM   183   C  C   . SER A 1 27   ? 73.169  85.560  111.018 1.00 77.13  ? 27   SER A C   1 
ATOM   184   O  O   . SER A 1 27   ? 72.216  85.325  110.268 1.00 80.66  ? 27   SER A O   1 
ATOM   185   C  CB  . SER A 1 27   ? 73.228  88.050  110.992 1.00 59.69  ? 27   SER A CB  1 
ATOM   186   O  OG  . SER A 1 27   ? 74.537  88.209  110.478 1.00 61.53  ? 27   SER A OG  1 
ATOM   187   N  N   . LEU A 1 28   ? 74.214  84.745  111.123 1.00 77.85  ? 28   LEU A N   1 
ATOM   188   C  CA  . LEU A 1 28   ? 74.256  83.477  110.410 1.00 70.47  ? 28   LEU A CA  1 
ATOM   189   C  C   . LEU A 1 28   ? 74.012  82.279  111.317 1.00 87.04  ? 28   LEU A C   1 
ATOM   190   O  O   . LEU A 1 28   ? 74.013  81.143  110.834 1.00 93.05  ? 28   LEU A O   1 
ATOM   191   C  CB  . LEU A 1 28   ? 75.601  83.314  109.699 1.00 77.31  ? 28   LEU A CB  1 
ATOM   192   C  CG  . LEU A 1 28   ? 75.889  84.347  108.616 1.00 76.16  ? 28   LEU A CG  1 
ATOM   193   C  CD1 . LEU A 1 28   ? 77.331  84.245  108.161 1.00 73.94  ? 28   LEU A CD1 1 
ATOM   194   C  CD2 . LEU A 1 28   ? 74.939  84.124  107.450 1.00 80.38  ? 28   LEU A CD2 1 
ATOM   195   N  N   . GLY A 1 29   ? 73.782  82.505  112.607 1.00 85.03  ? 29   GLY A N   1 
ATOM   196   C  CA  . GLY A 1 29   ? 73.549  81.417  113.532 1.00 81.03  ? 29   GLY A CA  1 
ATOM   197   C  C   . GLY A 1 29   ? 74.797  80.767  114.083 1.00 77.54  ? 29   GLY A C   1 
ATOM   198   O  O   . GLY A 1 29   ? 74.694  79.726  114.742 1.00 88.38  ? 29   GLY A O   1 
ATOM   199   N  N   . LEU A 1 30   ? 75.970  81.347  113.847 1.00 77.01  ? 30   LEU A N   1 
ATOM   200   C  CA  . LEU A 1 30   ? 77.224  80.805  114.337 1.00 74.58  ? 30   LEU A CA  1 
ATOM   201   C  C   . LEU A 1 30   ? 77.629  81.507  115.632 1.00 67.74  ? 30   LEU A C   1 
ATOM   202   O  O   . LEU A 1 30   ? 76.985  82.455  116.087 1.00 77.86  ? 30   LEU A O   1 
ATOM   203   C  CB  . LEU A 1 30   ? 78.315  80.916  113.270 1.00 77.01  ? 30   LEU A CB  1 
ATOM   204   C  CG  . LEU A 1 30   ? 77.877  80.599  111.840 1.00 73.81  ? 30   LEU A CG  1 
ATOM   205   C  CD1 . LEU A 1 30   ? 78.962  80.974  110.845 1.00 60.60  ? 30   LEU A CD1 1 
ATOM   206   C  CD2 . LEU A 1 30   ? 77.529  79.119  111.723 1.00 65.95  ? 30   LEU A CD2 1 
ATOM   207   N  N   . TYR A 1 31   ? 78.720  81.035  116.224 1.00 65.34  ? 31   TYR A N   1 
ATOM   208   C  CA  . TYR A 1 31   ? 79.234  81.589  117.466 1.00 76.58  ? 31   TYR A CA  1 
ATOM   209   C  C   . TYR A 1 31   ? 80.602  82.224  117.258 1.00 79.48  ? 31   TYR A C   1 
ATOM   210   O  O   . TYR A 1 31   ? 81.459  81.668  116.564 1.00 82.44  ? 31   TYR A O   1 
ATOM   211   C  CB  . TYR A 1 31   ? 79.325  80.501  118.538 1.00 79.50  ? 31   TYR A CB  1 
ATOM   212   C  CG  . TYR A 1 31   ? 79.867  81.000  119.850 1.00 95.50  ? 31   TYR A CG  1 
ATOM   213   C  CD1 . TYR A 1 31   ? 81.188  80.772  120.206 1.00 101.76 ? 31   TYR A CD1 1 
ATOM   214   C  CD2 . TYR A 1 31   ? 79.064  81.709  120.729 1.00 103.55 ? 31   TYR A CD2 1 
ATOM   215   C  CE1 . TYR A 1 31   ? 81.694  81.231  121.402 1.00 103.32 ? 31   TYR A CE1 1 
ATOM   216   C  CE2 . TYR A 1 31   ? 79.561  82.174  121.931 1.00 131.64 ? 31   TYR A CE2 1 
ATOM   217   C  CZ  . TYR A 1 31   ? 80.877  81.931  122.262 1.00 118.66 ? 31   TYR A CZ  1 
ATOM   218   O  OH  . TYR A 1 31   ? 81.379  82.391  123.457 1.00 101.38 ? 31   TYR A OH  1 
ATOM   219   N  N   . SER A 1 32   ? 80.796  83.394  117.868 1.00 85.15  ? 32   SER A N   1 
ATOM   220   C  CA  . SER A 1 32   ? 82.044  84.137  117.768 1.00 68.96  ? 32   SER A CA  1 
ATOM   221   C  C   . SER A 1 32   ? 82.148  85.104  118.940 1.00 86.99  ? 32   SER A C   1 
ATOM   222   O  O   . SER A 1 32   ? 81.135  85.610  119.431 1.00 101.91 ? 32   SER A O   1 
ATOM   223   C  CB  . SER A 1 32   ? 82.142  84.895  116.442 1.00 75.88  ? 32   SER A CB  1 
ATOM   224   O  OG  . SER A 1 32   ? 83.272  85.747  116.433 1.00 88.59  ? 32   SER A OG  1 
ATOM   225   N  N   . HIS A 1 33   ? 83.379  85.345  119.390 1.00 81.69  ? 33   HIS A N   1 
ATOM   226   C  CA  . HIS A 1 33   ? 83.638  86.196  120.552 1.00 86.08  ? 33   HIS A CA  1 
ATOM   227   C  C   . HIS A 1 33   ? 84.839  87.105  120.287 1.00 76.00  ? 33   HIS A C   1 
ATOM   228   O  O   . HIS A 1 33   ? 85.756  87.219  121.102 1.00 78.32  ? 33   HIS A O   1 
ATOM   229   C  CB  . HIS A 1 33   ? 83.848  85.387  121.828 1.00 89.07  ? 33   HIS A CB  1 
ATOM   230   C  CG  . HIS A 1 33   ? 83.784  86.221  123.068 1.00 118.54 ? 33   HIS A CG  1 
ATOM   231   N  ND1 . HIS A 1 33   ? 82.702  87.023  123.364 1.00 115.96 ? 33   HIS A ND1 1 
ATOM   232   C  CD2 . HIS A 1 33   ? 84.679  86.414  124.066 1.00 127.22 ? 33   HIS A CD2 1 
ATOM   233   C  CE1 . HIS A 1 33   ? 82.924  87.657  124.501 1.00 113.73 ? 33   HIS A CE1 1 
ATOM   234   N  NE2 . HIS A 1 33   ? 84.117  87.306  124.947 1.00 125.74 ? 33   HIS A NE2 1 
ATOM   235   N  N   . TYR A 1 34   ? 84.847  87.758  119.122 1.00 72.20  ? 34   TYR A N   1 
ATOM   236   C  CA  . TYR A 1 34   ? 85.970  88.621  118.765 1.00 64.24  ? 34   TYR A CA  1 
ATOM   237   C  C   . TYR A 1 34   ? 86.089  89.815  119.704 1.00 75.95  ? 34   TYR A C   1 
ATOM   238   O  O   . TYR A 1 34   ? 87.199  90.202  120.092 1.00 82.50  ? 34   TYR A O   1 
ATOM   239   C  CB  . TYR A 1 34   ? 85.800  89.128  117.333 1.00 71.02  ? 34   TYR A CB  1 
ATOM   240   C  CG  . TYR A 1 34   ? 86.288  88.179  116.272 1.00 77.46  ? 34   TYR A CG  1 
ATOM   241   C  CD1 . TYR A 1 34   ? 87.625  87.836  116.173 1.00 71.70  ? 34   TYR A CD1 1 
ATOM   242   C  CD2 . TYR A 1 34   ? 85.401  87.632  115.357 1.00 69.06  ? 34   TYR A CD2 1 
ATOM   243   C  CE1 . TYR A 1 34   ? 88.066  86.963  115.194 1.00 63.67  ? 34   TYR A CE1 1 
ATOM   244   C  CE2 . TYR A 1 34   ? 85.829  86.760  114.379 1.00 56.96  ? 34   TYR A CE2 1 
ATOM   245   C  CZ  . TYR A 1 34   ? 87.160  86.429  114.299 1.00 59.56  ? 34   TYR A CZ  1 
ATOM   246   O  OH  . TYR A 1 34   ? 87.588  85.559  113.322 1.00 65.02  ? 34   TYR A OH  1 
ATOM   247   N  N   . SER A 1 35   ? 84.961  90.415  120.072 1.00 81.30  ? 35   SER A N   1 
ATOM   248   C  CA  . SER A 1 35   ? 84.936  91.709  120.738 1.00 73.27  ? 35   SER A CA  1 
ATOM   249   C  C   . SER A 1 35   ? 84.807  91.596  122.253 1.00 76.16  ? 35   SER A C   1 
ATOM   250   O  O   . SER A 1 35   ? 84.184  90.670  122.777 1.00 86.97  ? 35   SER A O   1 
ATOM   251   C  CB  . SER A 1 35   ? 83.771  92.544  120.207 1.00 84.15  ? 35   SER A CB  1 
ATOM   252   O  OG  . SER A 1 35   ? 82.534  92.014  120.658 1.00 78.82  ? 35   SER A OG  1 
ATOM   253   N  N   . HIS A 1 36   ? 85.402  92.566  122.949 1.00 83.21  ? 36   HIS A N   1 
ATOM   254   C  CA  . HIS A 1 36   ? 85.256  92.719  124.392 1.00 86.69  ? 36   HIS A CA  1 
ATOM   255   C  C   . HIS A 1 36   ? 84.104  93.642  124.770 1.00 86.50  ? 36   HIS A C   1 
ATOM   256   O  O   . HIS A 1 36   ? 83.848  93.829  125.964 1.00 83.79  ? 36   HIS A O   1 
ATOM   257   C  CB  . HIS A 1 36   ? 86.548  93.260  125.019 1.00 82.92  ? 36   HIS A CB  1 
ATOM   258   C  CG  . HIS A 1 36   ? 87.761  92.429  124.740 1.00 88.23  ? 36   HIS A CG  1 
ATOM   259   N  ND1 . HIS A 1 36   ? 89.040  92.865  125.016 1.00 90.44  ? 36   HIS A ND1 1 
ATOM   260   C  CD2 . HIS A 1 36   ? 87.891  91.174  124.248 1.00 94.23  ? 36   HIS A CD2 1 
ATOM   261   C  CE1 . HIS A 1 36   ? 89.905  91.926  124.685 1.00 97.17  ? 36   HIS A CE1 1 
ATOM   262   N  NE2 . HIS A 1 36   ? 89.234  90.888  124.217 1.00 94.89  ? 36   HIS A NE2 1 
ATOM   263   N  N   . ASN A 1 37   ? 83.410  94.218  123.795 1.00 84.75  ? 37   ASN A N   1 
ATOM   264   C  CA  . ASN A 1 37   ? 82.358  95.187  124.079 1.00 80.30  ? 37   ASN A CA  1 
ATOM   265   C  C   . ASN A 1 37   ? 81.056  94.457  124.391 1.00 81.25  ? 37   ASN A C   1 
ATOM   266   O  O   . ASN A 1 37   ? 80.571  93.693  123.548 1.00 85.33  ? 37   ASN A O   1 
ATOM   267   C  CB  . ASN A 1 37   ? 82.178  96.125  122.890 1.00 75.61  ? 37   ASN A CB  1 
ATOM   268   C  CG  . ASN A 1 37   ? 81.483  97.418  123.262 1.00 65.59  ? 37   ASN A CG  1 
ATOM   269   O  OD1 . ASN A 1 37   ? 80.523  97.426  124.030 1.00 76.62  ? 37   ASN A OD1 1 
ATOM   270   N  ND2 . ASN A 1 37   ? 81.969  98.527  122.714 1.00 64.38  ? 37   ASN A ND2 1 
ATOM   271   N  N   . PRO A 1 38   ? 80.461  94.652  125.573 1.00 75.77  ? 38   PRO A N   1 
ATOM   272   C  CA  . PRO A 1 38   ? 79.182  93.987  125.871 1.00 72.93  ? 38   PRO A CA  1 
ATOM   273   C  C   . PRO A 1 38   ? 77.984  94.560  125.130 1.00 88.46  ? 38   PRO A C   1 
ATOM   274   O  O   . PRO A 1 38   ? 76.904  93.958  125.193 1.00 97.19  ? 38   PRO A O   1 
ATOM   275   C  CB  . PRO A 1 38   ? 79.027  94.190  127.384 1.00 67.00  ? 38   PRO A CB  1 
ATOM   276   C  CG  . PRO A 1 38   ? 79.860  95.401  127.685 1.00 78.10  ? 38   PRO A CG  1 
ATOM   277   C  CD  . PRO A 1 38   ? 81.031  95.309  126.761 1.00 81.89  ? 38   PRO A CD  1 
ATOM   278   N  N   . LYS A 1 39   ? 78.126  95.691  124.433 1.00 87.82  ? 39   LYS A N   1 
ATOM   279   C  CA  . LYS A 1 39   ? 77.026  96.188  123.613 1.00 73.46  ? 39   LYS A CA  1 
ATOM   280   C  C   . LYS A 1 39   ? 76.715  95.248  122.457 1.00 77.40  ? 39   LYS A C   1 
ATOM   281   O  O   . LYS A 1 39   ? 75.553  95.130  122.051 1.00 85.98  ? 39   LYS A O   1 
ATOM   282   C  CB  . LYS A 1 39   ? 77.319  97.597  123.099 1.00 71.89  ? 39   LYS A CB  1 
ATOM   283   C  CG  . LYS A 1 39   ? 77.341  98.649  124.193 1.00 80.17  ? 39   LYS A CG  1 
ATOM   284   C  CD  . LYS A 1 39   ? 76.872  99.992  123.663 1.00 78.59  ? 39   LYS A CD  1 
ATOM   285   C  CE  . LYS A 1 39   ? 76.510  100.930 124.799 1.00 72.04  ? 39   LYS A CE  1 
ATOM   286   N  NZ  . LYS A 1 39   ? 75.090  100.756 125.219 1.00 85.05  ? 39   LYS A NZ  1 
ATOM   287   N  N   . LEU A 1 40   ? 77.730  94.564  121.931 1.00 84.30  ? 40   LEU A N   1 
ATOM   288   C  CA  . LEU A 1 40   ? 77.573  93.717  120.759 1.00 79.52  ? 40   LEU A CA  1 
ATOM   289   C  C   . LEU A 1 40   ? 76.994  92.347  121.077 1.00 83.99  ? 40   LEU A C   1 
ATOM   290   O  O   . LEU A 1 40   ? 76.679  91.601  120.144 1.00 87.71  ? 40   LEU A O   1 
ATOM   291   C  CB  . LEU A 1 40   ? 78.919  93.545  120.052 1.00 68.89  ? 40   LEU A CB  1 
ATOM   292   C  CG  . LEU A 1 40   ? 79.503  94.809  119.432 1.00 74.85  ? 40   LEU A CG  1 
ATOM   293   C  CD1 . LEU A 1 40   ? 80.983  94.631  119.150 1.00 73.41  ? 40   LEU A CD1 1 
ATOM   294   C  CD2 . LEU A 1 40   ? 78.746  95.110  118.149 1.00 80.87  ? 40   LEU A CD2 1 
ATOM   295   N  N   . ARG A 1 41   ? 76.852  91.990  122.353 1.00 80.37  ? 41   ARG A N   1 
ATOM   296   C  CA  . ARG A 1 41   ? 76.277  90.690  122.667 1.00 96.42  ? 41   ARG A CA  1 
ATOM   297   C  C   . ARG A 1 41   ? 74.765  90.660  122.481 1.00 101.37 ? 41   ARG A C   1 
ATOM   298   O  O   . ARG A 1 41   ? 74.214  89.605  122.147 1.00 101.73 ? 41   ARG A O   1 
ATOM   299   C  CB  . ARG A 1 41   ? 76.634  90.279  124.096 1.00 102.63 ? 41   ARG A CB  1 
ATOM   300   C  CG  . ARG A 1 41   ? 78.124  90.185  124.362 1.00 115.12 ? 41   ARG A CG  1 
ATOM   301   C  CD  . ARG A 1 41   ? 78.556  88.728  124.366 1.00 140.93 ? 41   ARG A CD  1 
ATOM   302   N  NE  . ARG A 1 41   ? 77.651  87.901  125.158 1.00 153.17 ? 41   ARG A NE  1 
ATOM   303   C  CZ  . ARG A 1 41   ? 77.493  86.591  124.988 1.00 160.37 ? 41   ARG A CZ  1 
ATOM   304   N  NH1 . ARG A 1 41   ? 78.178  85.953  124.051 1.00 162.39 ? 41   ARG A NH1 1 
ATOM   305   N  NH2 . ARG A 1 41   ? 76.646  85.920  125.759 1.00 152.55 ? 41   ARG A NH2 1 
ATOM   306   N  N   . ASN A 1 42   ? 74.070  91.786  122.676 1.00 97.61  ? 42   ASN A N   1 
ATOM   307   C  CA  . ASN A 1 42   ? 72.614  91.746  122.698 1.00 98.10  ? 42   ASN A CA  1 
ATOM   308   C  C   . ASN A 1 42   ? 71.938  92.856  121.896 1.00 100.13 ? 42   ASN A C   1 
ATOM   309   O  O   . ASN A 1 42   ? 70.706  92.956  121.933 1.00 107.65 ? 42   ASN A O   1 
ATOM   310   C  CB  . ASN A 1 42   ? 72.117  91.790  124.146 1.00 105.16 ? 42   ASN A CB  1 
ATOM   311   C  CG  . ASN A 1 42   ? 72.031  90.414  124.771 1.00 130.35 ? 42   ASN A CG  1 
ATOM   312   O  OD1 . ASN A 1 42   ? 72.673  90.139  125.784 1.00 124.46 ? 42   ASN A OD1 1 
ATOM   313   N  ND2 . ASN A 1 42   ? 71.246  89.534  124.160 1.00 132.06 ? 42   ASN A ND2 1 
ATOM   314   N  N   . CYS A 1 43   ? 72.689  93.686  121.178 1.00 88.10  ? 43   CYS A N   1 
ATOM   315   C  CA  . CYS A 1 43   ? 72.055  94.696  120.344 1.00 88.38  ? 43   CYS A CA  1 
ATOM   316   C  C   . CYS A 1 43   ? 71.303  94.033  119.188 1.00 93.23  ? 43   CYS A C   1 
ATOM   317   O  O   . CYS A 1 43   ? 71.435  92.832  118.931 1.00 93.08  ? 43   CYS A O   1 
ATOM   318   C  CB  . CYS A 1 43   ? 73.093  95.681  119.814 1.00 84.03  ? 43   CYS A CB  1 
ATOM   319   S  SG  . CYS A 1 43   ? 74.272  94.961  118.652 1.00 102.18 ? 43   CYS A SG  1 
ATOM   320   N  N   . ARG A 1 44   ? 70.508  94.830  118.475 1.00 88.26  ? 44   ARG A N   1 
ATOM   321   C  CA  . ARG A 1 44   ? 69.846  94.353  117.269 1.00 83.38  ? 44   ARG A CA  1 
ATOM   322   C  C   . ARG A 1 44   ? 70.749  94.612  116.070 1.00 87.83  ? 44   ARG A C   1 
ATOM   323   O  O   . ARG A 1 44   ? 71.419  95.646  115.992 1.00 92.58  ? 44   ARG A O   1 
ATOM   324   C  CB  . ARG A 1 44   ? 68.477  95.005  117.061 1.00 93.57  ? 44   ARG A CB  1 
ATOM   325   C  CG  . ARG A 1 44   ? 68.484  96.493  116.788 1.00 116.33 ? 44   ARG A CG  1 
ATOM   326   C  CD  . ARG A 1 44   ? 67.078  97.055  116.921 1.00 134.48 ? 44   ARG A CD  1 
ATOM   327   N  NE  . ARG A 1 44   ? 67.068  98.509  117.029 1.00 144.02 ? 44   ARG A NE  1 
ATOM   328   C  CZ  . ARG A 1 44   ? 67.160  99.177  118.173 1.00 145.12 ? 44   ARG A CZ  1 
ATOM   329   N  NH1 . ARG A 1 44   ? 67.265  98.523  119.321 1.00 139.14 ? 44   ARG A NH1 1 
ATOM   330   N  NH2 . ARG A 1 44   ? 67.142  100.503 118.169 1.00 139.08 ? 44   ARG A NH2 1 
ATOM   331   N  N   . ILE A 1 45   ? 70.776  93.661  115.146 1.00 79.87  ? 45   ILE A N   1 
ATOM   332   C  CA  . ILE A 1 45   ? 71.755  93.686  114.050 1.00 71.99  ? 45   ILE A CA  1 
ATOM   333   C  C   . ILE A 1 45   ? 71.439  94.841  113.105 1.00 85.83  ? 45   ILE A C   1 
ATOM   334   O  O   . ILE A 1 45   ? 70.267  95.032  112.735 1.00 96.27  ? 45   ILE A O   1 
ATOM   335   C  CB  . ILE A 1 45   ? 71.742  92.353  113.301 1.00 82.64  ? 45   ILE A CB  1 
ATOM   336   C  CG1 . ILE A 1 45   ? 71.890  91.187  114.275 1.00 67.59  ? 45   ILE A CG1 1 
ATOM   337   C  CG2 . ILE A 1 45   ? 72.867  92.306  112.280 1.00 87.56  ? 45   ILE A CG2 1 
ATOM   338   C  CD1 . ILE A 1 45   ? 73.169  91.211  115.057 1.00 85.19  ? 45   ILE A CD1 1 
ATOM   339   N  N   . PRO A 1 46   ? 72.429  95.644  112.708 1.00 78.46  ? 46   PRO A N   1 
ATOM   340   C  CA  . PRO A 1 46   ? 72.185  96.660  111.676 1.00 77.96  ? 46   PRO A CA  1 
ATOM   341   C  C   . PRO A 1 46   ? 71.678  96.009  110.396 1.00 78.83  ? 46   PRO A C   1 
ATOM   342   O  O   . PRO A 1 46   ? 72.096  94.908  110.033 1.00 86.81  ? 46   PRO A O   1 
ATOM   343   C  CB  . PRO A 1 46   ? 73.561  97.306  111.479 1.00 67.69  ? 46   PRO A CB  1 
ATOM   344   C  CG  . PRO A 1 46   ? 74.283  97.060  112.760 1.00 67.48  ? 46   PRO A CG  1 
ATOM   345   C  CD  . PRO A 1 46   ? 73.784  95.739  113.276 1.00 80.48  ? 46   PRO A CD  1 
ATOM   346   N  N   . HIS A 1 47   ? 70.758  96.698  109.717 1.00 79.55  ? 47   HIS A N   1 
ATOM   347   C  CA  . HIS A 1 47   ? 70.048  96.081  108.599 1.00 77.26  ? 47   HIS A CA  1 
ATOM   348   C  C   . HIS A 1 47   ? 70.974  95.723  107.440 1.00 83.18  ? 47   HIS A C   1 
ATOM   349   O  O   . HIS A 1 47   ? 70.829  94.653  106.832 1.00 94.66  ? 47   HIS A O   1 
ATOM   350   C  CB  . HIS A 1 47   ? 68.946  97.015  108.104 1.00 93.30  ? 47   HIS A CB  1 
ATOM   351   C  CG  . HIS A 1 47   ? 68.185  96.473  106.936 1.00 106.61 ? 47   HIS A CG  1 
ATOM   352   N  ND1 . HIS A 1 47   ? 67.450  95.308  106.999 1.00 110.23 ? 47   HIS A ND1 1 
ATOM   353   C  CD2 . HIS A 1 47   ? 68.074  96.921  105.664 1.00 109.72 ? 47   HIS A CD2 1 
ATOM   354   C  CE1 . HIS A 1 47   ? 66.906  95.071  105.820 1.00 122.61 ? 47   HIS A CE1 1 
ATOM   355   N  NE2 . HIS A 1 47   ? 67.269  96.034  104.991 1.00 113.10 ? 47   HIS A NE2 1 
ATOM   356   N  N   . HIS A 1 48   ? 71.942  96.589  107.129 1.00 87.51  ? 48   HIS A N   1 
ATOM   357   C  CA  . HIS A 1 48   ? 72.809  96.331  105.985 1.00 89.97  ? 48   HIS A CA  1 
ATOM   358   C  C   . HIS A 1 48   ? 73.732  95.137  106.183 1.00 85.29  ? 48   HIS A C   1 
ATOM   359   O  O   . HIS A 1 48   ? 74.345  94.696  105.209 1.00 84.00  ? 48   HIS A O   1 
ATOM   360   C  CB  . HIS A 1 48   ? 73.640  97.570  105.647 1.00 78.98  ? 48   HIS A CB  1 
ATOM   361   C  CG  . HIS A 1 48   ? 74.655  97.921  106.686 1.00 80.88  ? 48   HIS A CG  1 
ATOM   362   N  ND1 . HIS A 1 48   ? 74.323  98.523  107.880 1.00 89.01  ? 48   HIS A ND1 1 
ATOM   363   C  CD2 . HIS A 1 48   ? 75.998  97.749  106.711 1.00 83.47  ? 48   HIS A CD2 1 
ATOM   364   C  CE1 . HIS A 1 48   ? 75.417  98.709  108.595 1.00 93.06  ? 48   HIS A CE1 1 
ATOM   365   N  NE2 . HIS A 1 48   ? 76.447  98.247  107.909 1.00 89.90  ? 48   HIS A NE2 1 
ATOM   366   N  N   . ILE A 1 49   ? 73.874  94.631  107.406 1.00 85.95  ? 49   ILE A N   1 
ATOM   367   C  CA  . ILE A 1 49   ? 74.572  93.377  107.671 1.00 63.95  ? 49   ILE A CA  1 
ATOM   368   C  C   . ILE A 1 49   ? 73.593  92.218  107.797 1.00 63.70  ? 49   ILE A C   1 
ATOM   369   O  O   . ILE A 1 49   ? 73.847  91.121  107.299 1.00 83.11  ? 49   ILE A O   1 
ATOM   370   C  CB  . ILE A 1 49   ? 75.467  93.486  108.924 1.00 54.31  ? 49   ILE A CB  1 
ATOM   371   C  CG1 . ILE A 1 49   ? 76.635  94.438  108.665 1.00 78.92  ? 49   ILE A CG1 1 
ATOM   372   C  CG2 . ILE A 1 49   ? 76.005  92.115  109.325 1.00 54.78  ? 49   ILE A CG2 1 
ATOM   373   C  CD1 . ILE A 1 49   ? 77.551  94.615  109.855 1.00 66.92  ? 49   ILE A CD1 1 
ATOM   374   N  N   . TYR A 1 50   ? 72.456  92.470  108.445 1.00 68.23  ? 50   TYR A N   1 
ATOM   375   C  CA  . TYR A 1 50   ? 71.465  91.429  108.678 1.00 71.90  ? 50   TYR A CA  1 
ATOM   376   C  C   . TYR A 1 50   ? 70.873  90.920  107.371 1.00 80.68  ? 50   TYR A C   1 
ATOM   377   O  O   . TYR A 1 50   ? 70.454  89.759  107.284 1.00 87.52  ? 50   TYR A O   1 
ATOM   378   C  CB  . TYR A 1 50   ? 70.387  91.974  109.621 1.00 86.89  ? 50   TYR A CB  1 
ATOM   379   C  CG  . TYR A 1 50   ? 69.425  90.937  110.140 1.00 94.50  ? 50   TYR A CG  1 
ATOM   380   C  CD1 . TYR A 1 50   ? 68.421  90.443  109.330 1.00 107.33 ? 50   TYR A CD1 1 
ATOM   381   C  CD2 . TYR A 1 50   ? 69.550  90.418  111.423 1.00 100.85 ? 50   TYR A CD2 1 
ATOM   382   C  CE1 . TYR A 1 50   ? 67.555  89.500  109.775 1.00 112.15 ? 50   TYR A CE1 1 
ATOM   383   C  CE2 . TYR A 1 50   ? 68.679  89.450  111.882 1.00 108.84 ? 50   TYR A CE2 1 
ATOM   384   C  CZ  . TYR A 1 50   ? 67.684  88.992  111.043 1.00 107.60 ? 50   TYR A CZ  1 
ATOM   385   O  OH  . TYR A 1 50   ? 66.797  88.034  111.471 1.00 118.76 ? 50   TYR A OH  1 
ATOM   386   N  N   . ARG A 1 51   ? 70.887  91.748  106.322 1.00 85.11  ? 51   ARG A N   1 
ATOM   387   C  CA  . ARG A 1 51   ? 70.281  91.351  105.056 1.00 83.63  ? 51   ARG A CA  1 
ATOM   388   C  C   . ARG A 1 51   ? 71.098  90.320  104.279 1.00 78.34  ? 51   ARG A C   1 
ATOM   389   O  O   . ARG A 1 51   ? 70.553  89.663  103.385 1.00 83.69  ? 51   ARG A O   1 
ATOM   390   C  CB  . ARG A 1 51   ? 70.035  92.621  104.234 1.00 94.38  ? 51   ARG A CB  1 
ATOM   391   C  CG  . ARG A 1 51   ? 71.312  93.296  103.754 1.00 95.68  ? 51   ARG A CG  1 
ATOM   392   C  CD  . ARG A 1 51   ? 71.033  94.625  103.079 1.00 110.35 ? 51   ARG A CD  1 
ATOM   393   N  NE  . ARG A 1 51   ? 69.923  94.541  102.137 1.00 121.97 ? 51   ARG A NE  1 
ATOM   394   C  CZ  . ARG A 1 51   ? 70.113  94.421  100.826 1.00 132.00 ? 51   ARG A CZ  1 
ATOM   395   N  NH1 . ARG A 1 51   ? 71.344  94.381  100.354 1.00 128.50 ? 51   ARG A NH1 1 
ATOM   396   N  NH2 . ARG A 1 51   ? 69.074  94.354  99.997  1.00 126.87 ? 51   ARG A NH2 1 
ATOM   397   N  N   . LEU A 1 52   ? 72.382  90.130  104.611 1.00 84.12  ? 52   LEU A N   1 
ATOM   398   C  CA  . LEU A 1 52   ? 73.237  89.187  103.888 1.00 83.70  ? 52   LEU A CA  1 
ATOM   399   C  C   . LEU A 1 52   ? 72.877  87.724  104.118 1.00 82.56  ? 52   LEU A C   1 
ATOM   400   O  O   . LEU A 1 52   ? 73.311  86.868  103.338 1.00 89.53  ? 52   LEU A O   1 
ATOM   401   C  CB  . LEU A 1 52   ? 74.711  89.424  104.230 1.00 54.77  ? 52   LEU A CB  1 
ATOM   402   C  CG  . LEU A 1 52   ? 75.415  90.712  103.798 1.00 61.72  ? 52   LEU A CG  1 
ATOM   403   C  CD1 . LEU A 1 52   ? 74.844  91.939  104.401 1.00 98.71  ? 52   LEU A CD1 1 
ATOM   404   C  CD2 . LEU A 1 52   ? 76.834  90.579  104.295 1.00 64.96  ? 52   LEU A CD2 1 
ATOM   405   N  N   . ARG A 1 53   ? 72.100  87.399  105.150 1.00 76.17  ? 53   ARG A N   1 
ATOM   406   C  CA  . ARG A 1 53   ? 71.785  85.992  105.366 1.00 86.03  ? 53   ARG A CA  1 
ATOM   407   C  C   . ARG A 1 53   ? 70.830  85.431  104.320 1.00 101.31 ? 53   ARG A C   1 
ATOM   408   O  O   . ARG A 1 53   ? 70.605  84.216  104.309 1.00 103.12 ? 53   ARG A O   1 
ATOM   409   C  CB  . ARG A 1 53   ? 71.222  85.748  106.765 1.00 86.66  ? 53   ARG A CB  1 
ATOM   410   C  CG  . ARG A 1 53   ? 70.001  86.546  107.123 1.00 89.98  ? 53   ARG A CG  1 
ATOM   411   C  CD  . ARG A 1 53   ? 69.729  86.362  108.599 1.00 102.60 ? 53   ARG A CD  1 
ATOM   412   N  NE  . ARG A 1 53   ? 68.424  86.863  109.006 1.00 114.02 ? 53   ARG A NE  1 
ATOM   413   C  CZ  . ARG A 1 53   ? 67.249  86.394  108.593 1.00 128.62 ? 53   ARG A CZ  1 
ATOM   414   N  NH1 . ARG A 1 53   ? 66.131  86.941  109.049 1.00 138.82 ? 53   ARG A NH1 1 
ATOM   415   N  NH2 . ARG A 1 53   ? 67.178  85.393  107.728 1.00 134.44 ? 53   ARG A NH2 1 
ATOM   416   N  N   . ASN A 1 54   ? 70.267  86.266  103.449 1.00 94.29  ? 54   ASN A N   1 
ATOM   417   C  CA  . ASN A 1 54   ? 69.289  85.798  102.479 1.00 92.16  ? 54   ASN A CA  1 
ATOM   418   C  C   . ASN A 1 54   ? 69.909  85.323  101.169 1.00 104.00 ? 54   ASN A C   1 
ATOM   419   O  O   . ASN A 1 54   ? 69.191  84.755  100.338 1.00 111.28 ? 54   ASN A O   1 
ATOM   420   C  CB  . ASN A 1 54   ? 68.281  86.912  102.180 1.00 96.49  ? 54   ASN A CB  1 
ATOM   421   C  CG  . ASN A 1 54   ? 67.251  87.072  103.275 1.00 96.67  ? 54   ASN A CG  1 
ATOM   422   O  OD1 . ASN A 1 54   ? 66.829  86.096  103.893 1.00 96.32  ? 54   ASN A OD1 1 
ATOM   423   N  ND2 . ASN A 1 54   ? 66.845  88.310  103.529 1.00 79.52  ? 54   ASN A ND2 1 
ATOM   424   N  N   . SER A 1 55   ? 71.207  85.527  100.962 1.00 96.85  ? 55   SER A N   1 
ATOM   425   C  CA  . SER A 1 55   ? 71.831  85.130  99.705  1.00 99.79  ? 55   SER A CA  1 
ATOM   426   C  C   . SER A 1 55   ? 71.942  83.610  99.642  1.00 87.50  ? 55   SER A C   1 
ATOM   427   O  O   . SER A 1 55   ? 72.364  82.969  100.609 1.00 89.92  ? 55   SER A O   1 
ATOM   428   C  CB  . SER A 1 55   ? 73.209  85.774  99.561  1.00 88.93  ? 55   SER A CB  1 
ATOM   429   O  OG  . SER A 1 55   ? 74.133  85.205  100.468 1.00 84.85  ? 55   SER A OG  1 
ATOM   430   N  N   . THR A 1 56   ? 71.566  83.032  98.497  1.00 86.86  ? 56   THR A N   1 
ATOM   431   C  CA  . THR A 1 56   ? 71.576  81.577  98.363  1.00 86.80  ? 56   THR A CA  1 
ATOM   432   C  C   . THR A 1 56   ? 72.988  81.024  98.213  1.00 85.95  ? 56   THR A C   1 
ATOM   433   O  O   . THR A 1 56   ? 73.269  79.903  98.663  1.00 96.53  ? 56   THR A O   1 
ATOM   434   C  CB  . THR A 1 56   ? 70.734  81.164  97.157  1.00 92.21  ? 56   THR A CB  1 
ATOM   435   O  OG1 . THR A 1 56   ? 71.051  82.011  96.044  1.00 84.38  ? 56   THR A OG1 1 
ATOM   436   C  CG2 . THR A 1 56   ? 69.252  81.304  97.467  1.00 105.51 ? 56   THR A CG2 1 
ATOM   437   N  N   . ALA A 1 57   ? 73.898  81.814  97.639  1.00 83.32  ? 57   ALA A N   1 
ATOM   438   C  CA  . ALA A 1 57   ? 75.274  81.359  97.485  1.00 79.48  ? 57   ALA A CA  1 
ATOM   439   C  C   . ALA A 1 57   ? 75.945  81.188  98.838  1.00 85.38  ? 57   ALA A C   1 
ATOM   440   O  O   . ALA A 1 57   ? 76.671  80.211  99.060  1.00 93.71  ? 57   ALA A O   1 
ATOM   441   C  CB  . ALA A 1 57   ? 76.056  82.337  96.611  1.00 77.36  ? 57   ALA A CB  1 
ATOM   442   N  N   . LEU A 1 58   ? 75.687  82.109  99.767  1.00 80.85  ? 58   LEU A N   1 
ATOM   443   C  CA  . LEU A 1 58   ? 76.314  81.990  101.074 1.00 69.45  ? 58   LEU A CA  1 
ATOM   444   C  C   . LEU A 1 58   ? 75.717  80.832  101.861 1.00 68.37  ? 58   LEU A C   1 
ATOM   445   O  O   . LEU A 1 58   ? 76.403  80.237  102.699 1.00 78.18  ? 58   LEU A O   1 
ATOM   446   C  CB  . LEU A 1 58   ? 76.168  83.305  101.839 1.00 70.20  ? 58   LEU A CB  1 
ATOM   447   C  CG  . LEU A 1 58   ? 76.783  83.396  103.231 1.00 66.46  ? 58   LEU A CG  1 
ATOM   448   C  CD1 . LEU A 1 58   ? 78.236  82.962  103.178 1.00 74.50  ? 58   LEU A CD1 1 
ATOM   449   C  CD2 . LEU A 1 58   ? 76.661  84.819  103.745 1.00 69.06  ? 58   LEU A CD2 1 
ATOM   450   N  N   . LYS A 1 59   ? 74.457  80.483  101.595 1.00 82.14  ? 59   LYS A N   1 
ATOM   451   C  CA  . LYS A 1 59   ? 73.864  79.356  102.300 1.00 80.81  ? 59   LYS A CA  1 
ATOM   452   C  C   . LYS A 1 59   ? 74.374  78.030  101.759 1.00 83.77  ? 59   LYS A C   1 
ATOM   453   O  O   . LYS A 1 59   ? 74.515  77.069  102.525 1.00 91.72  ? 59   LYS A O   1 
ATOM   454   C  CB  . LYS A 1 59   ? 72.339  79.389  102.224 1.00 93.71  ? 59   LYS A CB  1 
ATOM   455   C  CG  . LYS A 1 59   ? 71.693  80.500  103.021 1.00 96.58  ? 59   LYS A CG  1 
ATOM   456   C  CD  . LYS A 1 59   ? 70.212  80.228  103.157 1.00 108.08 ? 59   LYS A CD  1 
ATOM   457   C  CE  . LYS A 1 59   ? 69.493  80.462  101.845 1.00 117.49 ? 59   LYS A CE  1 
ATOM   458   N  NZ  . LYS A 1 59   ? 68.026  80.278  101.996 1.00 127.16 ? 59   LYS A NZ  1 
ATOM   459   N  N   . THR A 1 60   ? 74.658  77.951  100.454 1.00 79.42  ? 60   THR A N   1 
ATOM   460   C  CA  . THR A 1 60   ? 75.270  76.725  99.956  1.00 77.11  ? 60   THR A CA  1 
ATOM   461   C  C   . THR A 1 60   ? 76.746  76.639  100.323 1.00 80.59  ? 60   THR A C   1 
ATOM   462   O  O   . THR A 1 60   ? 77.290  75.535  100.424 1.00 87.71  ? 60   THR A O   1 
ATOM   463   C  CB  . THR A 1 60   ? 75.115  76.618  98.436  1.00 84.71  ? 60   THR A CB  1 
ATOM   464   O  OG1 . THR A 1 60   ? 75.939  77.603  97.798  1.00 86.48  ? 60   THR A OG1 1 
ATOM   465   C  CG2 . THR A 1 60   ? 73.667  76.825  98.027  1.00 105.50 ? 60   THR A CG2 1 
ATOM   466   N  N   . PHE A 1 61   ? 77.408  77.781  100.531 1.00 79.04  ? 61   PHE A N   1 
ATOM   467   C  CA  . PHE A 1 61   ? 78.804  77.739  100.958 1.00 69.17  ? 61   PHE A CA  1 
ATOM   468   C  C   . PHE A 1 61   ? 78.964  77.264  102.403 1.00 73.09  ? 61   PHE A C   1 
ATOM   469   O  O   . PHE A 1 61   ? 79.987  76.655  102.741 1.00 79.75  ? 61   PHE A O   1 
ATOM   470   C  CB  . PHE A 1 61   ? 79.437  79.117  100.803 1.00 73.06  ? 61   PHE A CB  1 
ATOM   471   C  CG  . PHE A 1 61   ? 80.874  79.163  101.230 1.00 69.38  ? 61   PHE A CG  1 
ATOM   472   C  CD1 . PHE A 1 61   ? 81.227  79.654  102.477 1.00 72.87  ? 61   PHE A CD1 1 
ATOM   473   C  CD2 . PHE A 1 61   ? 81.876  78.729  100.379 1.00 70.45  ? 61   PHE A CD2 1 
ATOM   474   C  CE1 . PHE A 1 61   ? 82.549  79.691  102.876 1.00 58.00  ? 61   PHE A CE1 1 
ATOM   475   C  CE2 . PHE A 1 61   ? 83.202  78.769  100.770 1.00 67.67  ? 61   PHE A CE2 1 
ATOM   476   C  CZ  . PHE A 1 61   ? 83.538  79.250  102.020 1.00 68.05  ? 61   PHE A CZ  1 
ATOM   477   N  N   . LEU A 1 62   ? 77.959  77.505  103.248 1.00 77.08  ? 62   LEU A N   1 
ATOM   478   C  CA  . LEU A 1 62   ? 77.952  77.172  104.666 1.00 71.25  ? 62   LEU A CA  1 
ATOM   479   C  C   . LEU A 1 62   ? 77.258  75.848  104.895 1.00 77.50  ? 62   LEU A C   1 
ATOM   480   O  O   . LEU A 1 62   ? 76.911  75.527  106.037 1.00 80.54  ? 62   LEU A O   1 
ATOM   481   C  CB  . LEU A 1 62   ? 77.232  78.251  105.475 1.00 74.37  ? 62   LEU A CB  1 
ATOM   482   C  CG  . LEU A 1 62   ? 77.934  79.588  105.617 1.00 65.10  ? 62   LEU A CG  1 
ATOM   483   C  CD1 . LEU A 1 62   ? 77.010  80.517  106.373 1.00 71.89  ? 62   LEU A CD1 1 
ATOM   484   C  CD2 . LEU A 1 62   ? 79.253  79.391  106.340 1.00 63.98  ? 62   LEU A CD2 1 
ATOM   485   N  N   . GLN A 1 63   ? 77.105  75.068  103.837 1.00 79.27  ? 63   GLN A N   1 
ATOM   486   C  CA  . GLN A 1 63   ? 76.526  73.752  103.936 1.00 77.75  ? 63   GLN A CA  1 
ATOM   487   C  C   . GLN A 1 63   ? 77.551  72.785  104.522 1.00 82.62  ? 63   GLN A C   1 
ATOM   488   O  O   . GLN A 1 63   ? 78.744  72.879  104.226 1.00 91.52  ? 63   GLN A O   1 
ATOM   489   C  CB  . GLN A 1 63   ? 76.212  73.290  102.490 1.00 83.43  ? 63   GLN A CB  1 
ATOM   490   C  CG  . GLN A 1 63   ? 74.867  73.649  101.760 1.00 112.75 ? 63   GLN A CG  1 
ATOM   491   C  CD  . GLN A 1 63   ? 73.573  73.121  102.354 1.00 119.69 ? 63   GLN A CD  1 
ATOM   492   O  OE1 . GLN A 1 63   ? 72.771  73.906  102.878 1.00 121.29 ? 63   GLN A OE1 1 
ATOM   493   N  NE2 . GLN A 1 63   ? 73.367  71.803  102.300 1.00 123.69 ? 63   GLN A NE2 1 
ATOM   494   N  N   . ASN A 1 64   ? 77.089  71.877  105.379 1.00 93.44  ? 64   ASN A N   1 
ATOM   495   C  CA  . ASN A 1 64   ? 77.957  70.857  105.988 1.00 93.37  ? 64   ASN A CA  1 
ATOM   496   C  C   . ASN A 1 64   ? 79.056  71.457  106.879 1.00 83.29  ? 64   ASN A C   1 
ATOM   497   O  O   . ASN A 1 64   ? 80.167  70.889  106.972 1.00 88.08  ? 64   ASN A O   1 
ATOM   498   C  CB  . ASN A 1 64   ? 78.499  69.942  104.890 1.00 93.51  ? 64   ASN A CB  1 
ATOM   499   C  CG  . ASN A 1 64   ? 78.775  68.515  105.357 1.00 117.07 ? 64   ASN A CG  1 
ATOM   500   O  OD1 . ASN A 1 64   ? 78.284  68.073  106.403 1.00 117.66 ? 64   ASN A OD1 1 
ATOM   501   N  ND2 . ASN A 1 64   ? 79.477  67.767  104.525 1.00 108.44 ? 64   ASN A ND2 1 
ATOM   502   N  N   . CYS A 1 65   ? 78.795  72.574  107.543 1.00 94.15  ? 65   CYS A N   1 
ATOM   503   C  CA  . CYS A 1 65   ? 79.697  73.254  108.472 1.00 87.87  ? 65   CYS A CA  1 
ATOM   504   C  C   . CYS A 1 65   ? 79.198  73.212  109.916 1.00 91.83  ? 65   CYS A C   1 
ATOM   505   O  O   . CYS A 1 65   ? 78.016  72.991  110.184 1.00 97.65  ? 65   CYS A O   1 
ATOM   506   C  CB  . CYS A 1 65   ? 79.892  74.721  108.056 1.00 80.16  ? 65   CYS A CB  1 
ATOM   507   S  SG  . CYS A 1 65   ? 80.968  74.966  106.630 1.00 108.44 ? 65   CYS A SG  1 
ATOM   508   N  N   . SER A 1 66   ? 80.124  73.440  110.853 1.00 84.70  ? 66   SER A N   1 
ATOM   509   C  CA  . SER A 1 66   ? 79.820  73.399  112.278 1.00 84.73  ? 66   SER A CA  1 
ATOM   510   C  C   . SER A 1 66   ? 79.251  74.737  112.758 1.00 86.19  ? 66   SER A C   1 
ATOM   511   O  O   . SER A 1 66   ? 79.378  75.775  112.101 1.00 92.30  ? 66   SER A O   1 
ATOM   512   C  CB  . SER A 1 66   ? 81.066  73.047  113.088 1.00 83.56  ? 66   SER A CB  1 
ATOM   513   O  OG  . SER A 1 66   ? 80.819  73.148  114.481 1.00 94.49  ? 66   SER A OG  1 
ATOM   514   N  N   . ILE A 1 67   ? 78.616  74.698  113.934 1.00 77.56  ? 67   ILE A N   1 
ATOM   515   C  CA  . ILE A 1 67   ? 78.093  75.914  114.550 1.00 74.10  ? 67   ILE A CA  1 
ATOM   516   C  C   . ILE A 1 67   ? 79.208  76.807  115.084 1.00 72.56  ? 67   ILE A C   1 
ATOM   517   O  O   . ILE A 1 67   ? 79.078  78.037  115.089 1.00 77.44  ? 67   ILE A O   1 
ATOM   518   C  CB  . ILE A 1 67   ? 77.104  75.530  115.667 1.00 84.96  ? 67   ILE A CB  1 
ATOM   519   C  CG1 . ILE A 1 67   ? 75.947  74.711  115.096 1.00 93.63  ? 67   ILE A CG1 1 
ATOM   520   C  CG2 . ILE A 1 67   ? 76.569  76.765  116.380 1.00 89.46  ? 67   ILE A CG2 1 
ATOM   521   C  CD1 . ILE A 1 67   ? 75.134  75.444  114.061 1.00 102.58 ? 67   ILE A CD1 1 
ATOM   522   N  N   . LEU A 1 68   ? 80.323  76.223  115.507 1.00 75.48  ? 68   LEU A N   1 
ATOM   523   C  CA  . LEU A 1 68   ? 81.423  76.979  116.088 1.00 79.40  ? 68   LEU A CA  1 
ATOM   524   C  C   . LEU A 1 68   ? 82.371  77.511  115.021 1.00 81.01  ? 68   LEU A C   1 
ATOM   525   O  O   . LEU A 1 68   ? 82.531  76.921  113.950 1.00 82.99  ? 68   LEU A O   1 
ATOM   526   C  CB  . LEU A 1 68   ? 82.197  76.125  117.094 1.00 86.07  ? 68   LEU A CB  1 
ATOM   527   C  CG  . LEU A 1 68   ? 81.324  75.327  118.061 1.00 95.33  ? 68   LEU A CG  1 
ATOM   528   C  CD1 . LEU A 1 68   ? 82.163  74.317  118.822 1.00 103.98 ? 68   LEU A CD1 1 
ATOM   529   C  CD2 . LEU A 1 68   ? 80.610  76.272  119.020 1.00 91.23  ? 68   LEU A CD2 1 
ATOM   530   N  N   . THR A 1 69   ? 82.999  78.643  115.330 1.00 61.00  ? 69   THR A N   1 
ATOM   531   C  CA  . THR A 1 69   ? 84.036  79.217  114.492 1.00 63.02  ? 69   THR A CA  1 
ATOM   532   C  C   . THR A 1 69   ? 85.318  79.360  115.304 1.00 70.57  ? 69   THR A C   1 
ATOM   533   O  O   . THR A 1 69   ? 85.329  79.206  116.529 1.00 76.58  ? 69   THR A O   1 
ATOM   534   C  CB  . THR A 1 69   ? 83.614  80.585  113.932 1.00 59.15  ? 69   THR A CB  1 
ATOM   535   O  OG1 . THR A 1 69   ? 83.687  81.573  114.969 1.00 70.53  ? 69   THR A OG1 1 
ATOM   536   C  CG2 . THR A 1 69   ? 82.191  80.532  113.392 1.00 68.51  ? 69   THR A CG2 1 
ATOM   537   N  N   . VAL A 1 70   ? 86.407  79.663  114.604 1.00 66.13  ? 70   VAL A N   1 
ATOM   538   C  CA  . VAL A 1 70   ? 87.717  79.821  115.232 1.00 56.36  ? 70   VAL A CA  1 
ATOM   539   C  C   . VAL A 1 70   ? 88.285  81.185  114.858 1.00 65.06  ? 70   VAL A C   1 
ATOM   540   O  O   . VAL A 1 70   ? 87.905  81.749  113.821 1.00 75.07  ? 70   VAL A O   1 
ATOM   541   C  CB  . VAL A 1 70   ? 88.668  78.689  114.814 1.00 51.04  ? 70   VAL A CB  1 
ATOM   542   C  CG1 . VAL A 1 70   ? 88.111  77.337  115.243 1.00 61.09  ? 70   VAL A CG1 1 
ATOM   543   C  CG2 . VAL A 1 70   ? 88.895  78.717  113.308 1.00 50.49  ? 70   VAL A CG2 1 
ATOM   544   N  N   . PRO A 1 71   ? 89.171  81.764  115.667 1.00 59.21  ? 71   PRO A N   1 
ATOM   545   C  CA  . PRO A 1 71   ? 89.781  83.044  115.292 1.00 56.48  ? 71   PRO A CA  1 
ATOM   546   C  C   . PRO A 1 71   ? 90.667  82.889  114.064 1.00 75.26  ? 71   PRO A C   1 
ATOM   547   O  O   . PRO A 1 71   ? 90.915  81.790  113.563 1.00 88.90  ? 71   PRO A O   1 
ATOM   548   C  CB  . PRO A 1 71   ? 90.612  83.433  116.519 1.00 60.88  ? 71   PRO A CB  1 
ATOM   549   C  CG  . PRO A 1 71   ? 90.733  82.179  117.335 1.00 60.65  ? 71   PRO A CG  1 
ATOM   550   C  CD  . PRO A 1 71   ? 89.526  81.355  117.034 1.00 65.93  ? 71   PRO A CD  1 
ATOM   551   N  N   . PHE A 1 72   ? 91.147  84.031  113.577 1.00 75.96  ? 72   PHE A N   1 
ATOM   552   C  CA  . PHE A 1 72   ? 91.769  84.079  112.259 1.00 68.70  ? 72   PHE A CA  1 
ATOM   553   C  C   . PHE A 1 72   ? 93.211  83.571  112.279 1.00 73.48  ? 72   PHE A C   1 
ATOM   554   O  O   . PHE A 1 72   ? 93.668  82.907  111.329 1.00 86.33  ? 72   PHE A O   1 
ATOM   555   C  CB  . PHE A 1 72   ? 91.708  85.516  111.736 1.00 68.05  ? 72   PHE A CB  1 
ATOM   556   C  CG  . PHE A 1 72   ? 92.491  85.736  110.485 1.00 71.92  ? 72   PHE A CG  1 
ATOM   557   C  CD1 . PHE A 1 72   ? 92.163  85.069  109.320 1.00 68.80  ? 72   PHE A CD1 1 
ATOM   558   C  CD2 . PHE A 1 72   ? 93.564  86.610  110.476 1.00 77.12  ? 72   PHE A CD2 1 
ATOM   559   C  CE1 . PHE A 1 72   ? 92.892  85.271  108.164 1.00 75.07  ? 72   PHE A CE1 1 
ATOM   560   C  CE2 . PHE A 1 72   ? 94.298  86.816  109.325 1.00 69.12  ? 72   PHE A CE2 1 
ATOM   561   C  CZ  . PHE A 1 72   ? 93.961  86.145  108.167 1.00 64.16  ? 72   PHE A CZ  1 
ATOM   562   N  N   . HIS A 1 73   ? 93.926  83.818  113.378 1.00 52.36  ? 73   HIS A N   1 
ATOM   563   C  CA  . HIS A 1 73   ? 95.358  83.557  113.373 1.00 57.69  ? 73   HIS A CA  1 
ATOM   564   C  C   . HIS A 1 73   ? 95.659  82.085  113.619 1.00 72.21  ? 73   HIS A C   1 
ATOM   565   O  O   . HIS A 1 73   ? 96.597  81.537  113.030 1.00 87.90  ? 73   HIS A O   1 
ATOM   566   C  CB  . HIS A 1 73   ? 96.046  84.447  114.409 1.00 68.01  ? 73   HIS A CB  1 
ATOM   567   C  CG  . HIS A 1 73   ? 95.945  85.912  114.103 1.00 59.23  ? 73   HIS A CG  1 
ATOM   568   N  ND1 . HIS A 1 73   ? 96.704  86.519  113.124 1.00 56.39  ? 73   HIS A ND1 1 
ATOM   569   C  CD2 . HIS A 1 73   ? 95.175  86.888  114.641 1.00 65.02  ? 73   HIS A CD2 1 
ATOM   570   C  CE1 . HIS A 1 73   ? 96.405  87.804  113.072 1.00 59.98  ? 73   HIS A CE1 1 
ATOM   571   N  NE2 . HIS A 1 73   ? 95.481  88.054  113.983 1.00 68.59  ? 73   HIS A NE2 1 
ATOM   572   N  N   . SER A 1 74   ? 94.894  81.435  114.500 1.00 43.61  ? 74   SER A N   1 
ATOM   573   C  CA  . SER A 1 74   ? 95.023  79.994  114.694 1.00 58.41  ? 74   SER A CA  1 
ATOM   574   C  C   . SER A 1 74   ? 95.001  79.214  113.380 1.00 77.55  ? 74   SER A C   1 
ATOM   575   O  O   . SER A 1 74   ? 95.591  78.133  113.288 1.00 78.81  ? 74   SER A O   1 
ATOM   576   C  CB  . SER A 1 74   ? 93.896  79.499  115.604 1.00 48.42  ? 74   SER A CB  1 
ATOM   577   O  OG  . SER A 1 74   ? 92.630  79.689  114.992 1.00 62.54  ? 74   SER A OG  1 
ATOM   578   N  N   . ILE A 1 75   ? 94.338  79.755  112.359 1.00 74.15  ? 75   ILE A N   1 
ATOM   579   C  CA  . ILE A 1 75   ? 94.345  79.203  111.004 1.00 54.40  ? 75   ILE A CA  1 
ATOM   580   C  C   . ILE A 1 75   ? 95.448  79.760  110.101 1.00 66.10  ? 75   ILE A C   1 
ATOM   581   O  O   . ILE A 1 75   ? 95.892  79.065  109.177 1.00 78.38  ? 75   ILE A O   1 
ATOM   582   C  CB  . ILE A 1 75   ? 92.953  79.379  110.377 1.00 62.83  ? 75   ILE A CB  1 
ATOM   583   C  CG1 . ILE A 1 75   ? 91.933  78.632  111.225 1.00 80.00  ? 75   ILE A CG1 1 
ATOM   584   C  CG2 . ILE A 1 75   ? 92.901  78.766  108.997 1.00 79.75  ? 75   ILE A CG2 1 
ATOM   585   C  CD1 . ILE A 1 75   ? 92.396  77.242  111.643 1.00 92.32  ? 75   ILE A CD1 1 
ATOM   586   N  N   . TRP A 1 76   ? 95.891  80.997  110.335 1.00 64.19  ? 76   TRP A N   1 
ATOM   587   C  CA  . TRP A 1 76   ? 96.928  81.631  109.514 1.00 62.87  ? 76   TRP A CA  1 
ATOM   588   C  C   . TRP A 1 76   ? 98.036  80.710  108.976 1.00 64.72  ? 76   TRP A C   1 
ATOM   589   O  O   . TRP A 1 76   ? 98.353  80.754  107.774 1.00 86.49  ? 76   TRP A O   1 
ATOM   590   C  CB  . TRP A 1 76   ? 97.582  82.714  110.376 1.00 46.92  ? 76   TRP A CB  1 
ATOM   591   C  CG  . TRP A 1 76   ? 98.827  83.278  109.833 1.00 52.50  ? 76   TRP A CG  1 
ATOM   592   C  CD1 . TRP A 1 76   ? 100.101 82.868  110.095 1.00 59.42  ? 76   TRP A CD1 1 
ATOM   593   C  CD2 . TRP A 1 76   ? 98.936  84.423  108.993 1.00 70.30  ? 76   TRP A CD2 1 
ATOM   594   N  NE1 . TRP A 1 76   ? 100.997 83.663  109.423 1.00 62.03  ? 76   TRP A NE1 1 
ATOM   595   C  CE2 . TRP A 1 76   ? 100.304 84.630  108.743 1.00 68.75  ? 76   TRP A CE2 1 
ATOM   596   C  CE3 . TRP A 1 76   ? 98.004  85.285  108.409 1.00 61.03  ? 76   TRP A CE3 1 
ATOM   597   C  CZ2 . TRP A 1 76   ? 100.764 85.665  107.935 1.00 73.70  ? 76   TRP A CZ2 1 
ATOM   598   C  CZ3 . TRP A 1 76   ? 98.460  86.309  107.608 1.00 56.60  ? 76   TRP A CZ3 1 
ATOM   599   C  CH2 . TRP A 1 76   ? 99.828  86.492  107.377 1.00 63.76  ? 76   TRP A CH2 1 
ATOM   600   N  N   . ASP A 1 77   ? 98.609  79.859  109.833 1.00 65.17  ? 77   ASP A N   1 
ATOM   601   C  CA  . ASP A 1 77   ? 99.673  78.950  109.401 1.00 60.48  ? 77   ASP A CA  1 
ATOM   602   C  C   . ASP A 1 77   ? 99.197  78.017  108.292 1.00 56.19  ? 77   ASP A C   1 
ATOM   603   O  O   . ASP A 1 77   ? 99.834  77.898  107.231 1.00 68.57  ? 77   ASP A O   1 
ATOM   604   C  CB  . ASP A 1 77   ? 100.185 78.134  110.591 1.00 76.38  ? 77   ASP A CB  1 
ATOM   605   C  CG  . ASP A 1 77   ? 101.430 77.333  110.253 1.00 102.83 ? 77   ASP A CG  1 
ATOM   606   O  OD1 . ASP A 1 77   ? 102.057 77.618  109.211 1.00 103.70 ? 77   ASP A OD1 1 
ATOM   607   O  OD2 . ASP A 1 77   ? 101.772 76.403  111.015 1.00 109.74 ? 77   ASP A OD2 1 
ATOM   608   N  N   . HIS A 1 78   ? 98.067  77.346  108.530 1.00 65.71  ? 78   HIS A N   1 
ATOM   609   C  CA  . HIS A 1 78   ? 97.529  76.404  107.559 1.00 62.22  ? 78   HIS A CA  1 
ATOM   610   C  C   . HIS A 1 78   ? 97.115  77.111  106.280 1.00 63.77  ? 78   HIS A C   1 
ATOM   611   O  O   . HIS A 1 78   ? 97.285  76.566  105.183 1.00 76.77  ? 78   HIS A O   1 
ATOM   612   C  CB  . HIS A 1 78   ? 96.338  75.658  108.163 1.00 61.60  ? 78   HIS A CB  1 
ATOM   613   C  CG  . HIS A 1 78   ? 95.669  74.721  107.207 1.00 77.42  ? 78   HIS A CG  1 
ATOM   614   N  ND1 . HIS A 1 78   ? 94.687  75.135  106.333 1.00 75.26  ? 78   HIS A ND1 1 
ATOM   615   C  CD2 . HIS A 1 78   ? 95.842  73.398  106.981 1.00 97.42  ? 78   HIS A CD2 1 
ATOM   616   C  CE1 . HIS A 1 78   ? 94.282  74.106  105.611 1.00 81.06  ? 78   HIS A CE1 1 
ATOM   617   N  NE2 . HIS A 1 78   ? 94.967  73.040  105.985 1.00 90.19  ? 78   HIS A NE2 1 
ATOM   618   N  N   . ILE A 1 79   ? 96.597  78.334  106.400 1.00 61.47  ? 79   ILE A N   1 
ATOM   619   C  CA  . ILE A 1 79   ? 96.243  79.108  105.211 1.00 56.35  ? 79   ILE A CA  1 
ATOM   620   C  C   . ILE A 1 79   ? 97.465  79.283  104.320 1.00 59.73  ? 79   ILE A C   1 
ATOM   621   O  O   . ILE A 1 79   ? 97.430  79.008  103.108 1.00 74.39  ? 79   ILE A O   1 
ATOM   622   C  CB  . ILE A 1 79   ? 95.669  80.480  105.611 1.00 52.96  ? 79   ILE A CB  1 
ATOM   623   C  CG1 . ILE A 1 79   ? 94.273  80.353  106.215 1.00 68.48  ? 79   ILE A CG1 1 
ATOM   624   C  CG2 . ILE A 1 79   ? 95.652  81.427  104.412 1.00 64.85  ? 79   ILE A CG2 1 
ATOM   625   C  CD1 . ILE A 1 79   ? 93.854  81.583  107.005 1.00 78.15  ? 79   ILE A CD1 1 
ATOM   626   N  N   . LEU A 1 80   ? 98.565  79.753  104.915 1.00 63.75  ? 80   LEU A N   1 
ATOM   627   C  CA  . LEU A 1 80   ? 99.783  80.006  104.146 1.00 60.50  ? 80   LEU A CA  1 
ATOM   628   C  C   . LEU A 1 80   ? 100.303 78.733  103.482 1.00 61.62  ? 80   LEU A C   1 
ATOM   629   O  O   . LEU A 1 80   ? 100.568 78.713  102.269 1.00 70.57  ? 80   LEU A O   1 
ATOM   630   C  CB  . LEU A 1 80   ? 100.837 80.626  105.055 1.00 57.26  ? 80   LEU A CB  1 
ATOM   631   C  CG  . LEU A 1 80   ? 101.001 82.137  104.895 1.00 65.03  ? 80   LEU A CG  1 
ATOM   632   C  CD1 . LEU A 1 80   ? 99.690  82.841  105.214 1.00 55.09  ? 80   LEU A CD1 1 
ATOM   633   C  CD2 . LEU A 1 80   ? 102.105 82.626  105.809 1.00 90.21  ? 80   LEU A CD2 1 
ATOM   634   N  N   . THR A 1 81   ? 100.391 77.647  104.251 1.00 68.12  ? 81   THR A N   1 
ATOM   635   C  CA  . THR A 1 81   ? 100.915 76.407  103.695 1.00 58.61  ? 81   THR A CA  1 
ATOM   636   C  C   . THR A 1 81   ? 100.035 75.929  102.546 1.00 60.21  ? 81   THR A C   1 
ATOM   637   O  O   . THR A 1 81   ? 100.546 75.447  101.515 1.00 75.44  ? 81   THR A O   1 
ATOM   638   C  CB  . THR A 1 81   ? 101.044 75.332  104.802 1.00 68.91  ? 81   THR A CB  1 
ATOM   639   O  OG1 . THR A 1 81   ? 102.152 75.668  105.656 1.00 77.71  ? 81   THR A OG1 1 
ATOM   640   C  CG2 . THR A 1 81   ? 101.299 73.958  104.198 1.00 77.96  ? 81   THR A CG2 1 
ATOM   641   N  N   . SER A 1 82   ? 98.704  76.059  102.716 1.00 65.41  ? 82   SER A N   1 
ATOM   642   C  CA  . SER A 1 82   ? 97.771  75.503  101.748 1.00 57.50  ? 82   SER A CA  1 
ATOM   643   C  C   . SER A 1 82   ? 97.841  76.220  100.425 1.00 63.97  ? 82   SER A C   1 
ATOM   644   O  O   . SER A 1 82   ? 97.912  75.589  99.359  1.00 74.23  ? 82   SER A O   1 
ATOM   645   C  CB  . SER A 1 82   ? 96.327  75.627  102.268 1.00 56.38  ? 82   SER A CB  1 
ATOM   646   O  OG  . SER A 1 82   ? 95.446  75.013  101.360 1.00 74.90  ? 82   SER A OG  1 
ATOM   647   N  N   . ILE A 1 83   ? 97.850  77.544  100.479 1.00 65.26  ? 83   ILE A N   1 
ATOM   648   C  CA  . ILE A 1 83   ? 97.973  78.305  99.241  1.00 59.76  ? 83   ILE A CA  1 
ATOM   649   C  C   . ILE A 1 83   ? 99.310  78.036  98.576  1.00 71.95  ? 83   ILE A C   1 
ATOM   650   O  O   . ILE A 1 83   ? 99.375  77.780  97.361  1.00 84.93  ? 83   ILE A O   1 
ATOM   651   C  CB  . ILE A 1 83   ? 97.749  79.804  99.505  1.00 53.81  ? 83   ILE A CB  1 
ATOM   652   C  CG1 . ILE A 1 83   ? 96.271  80.057  99.807  1.00 63.56  ? 83   ILE A CG1 1 
ATOM   653   C  CG2 . ILE A 1 83   ? 98.164  80.605  98.295  1.00 54.85  ? 83   ILE A CG2 1 
ATOM   654   C  CD1 . ILE A 1 83   ? 95.953  81.500  100.108 1.00 62.47  ? 83   ILE A CD1 1 
ATOM   655   N  N   . GLN A 1 84   ? 100.371 77.926  99.387  1.00 74.08  ? 84   GLN A N   1 
ATOM   656   C  CA  . GLN A 1 84   ? 101.701 77.699  98.834  1.00 67.14  ? 84   GLN A CA  1 
ATOM   657   C  C   . GLN A 1 84   ? 101.780 76.392  98.062  1.00 67.98  ? 84   GLN A C   1 
ATOM   658   O  O   . GLN A 1 84   ? 102.371 76.343  96.978  1.00 58.35  ? 84   GLN A O   1 
ATOM   659   C  CB  . GLN A 1 84   ? 102.739 77.706  99.949  1.00 64.91  ? 84   GLN A CB  1 
ATOM   660   C  CG  . GLN A 1 84   ? 104.130 77.373  99.463  1.00 63.75  ? 84   GLN A CG  1 
ATOM   661   C  CD  . GLN A 1 84   ? 105.160 77.493  100.556 1.00 81.44  ? 84   GLN A CD  1 
ATOM   662   O  OE1 . GLN A 1 84   ? 104.946 78.182  101.553 1.00 69.13  ? 84   GLN A OE1 1 
ATOM   663   N  NE2 . GLN A 1 84   ? 106.284 76.811  100.384 1.00 93.72  ? 84   GLN A NE2 1 
ATOM   664   N  N   . TYR A 1 85   ? 101.177 75.329  98.583  1.00 82.22  ? 85   TYR A N   1 
ATOM   665   C  CA  . TYR A 1 85   ? 101.354 74.042  97.924  1.00 73.73  ? 85   TYR A CA  1 
ATOM   666   C  C   . TYR A 1 85   ? 100.247 73.726  96.935  1.00 73.29  ? 85   TYR A C   1 
ATOM   667   O  O   . TYR A 1 85   ? 100.400 72.790  96.143  1.00 78.39  ? 85   TYR A O   1 
ATOM   668   C  CB  . TYR A 1 85   ? 101.443 72.905  98.943  1.00 85.32  ? 85   TYR A CB  1 
ATOM   669   C  CG  . TYR A 1 85   ? 102.774 72.821  99.641  1.00 97.83  ? 85   TYR A CG  1 
ATOM   670   C  CD1 . TYR A 1 85   ? 103.921 72.479  98.940  1.00 100.00 ? 85   TYR A CD1 1 
ATOM   671   C  CD2 . TYR A 1 85   ? 102.884 73.073  100.999 1.00 102.95 ? 85   TYR A CD2 1 
ATOM   672   C  CE1 . TYR A 1 85   ? 105.142 72.397  99.569  1.00 121.45 ? 85   TYR A CE1 1 
ATOM   673   C  CE2 . TYR A 1 85   ? 104.102 72.992  101.639 1.00 117.83 ? 85   TYR A CE2 1 
ATOM   674   C  CZ  . TYR A 1 85   ? 105.229 72.653  100.920 1.00 132.46 ? 85   TYR A CZ  1 
ATOM   675   O  OH  . TYR A 1 85   ? 106.445 72.572  101.555 1.00 134.19 ? 85   TYR A OH  1 
ATOM   676   N  N   . ASP A 1 86   ? 99.143  74.472  96.950  1.00 76.91  ? 86   ASP A N   1 
ATOM   677   C  CA  . ASP A 1 86   ? 98.026  74.151  96.085  1.00 72.63  ? 86   ASP A CA  1 
ATOM   678   C  C   . ASP A 1 86   ? 97.844  75.122  94.924  1.00 75.28  ? 86   ASP A C   1 
ATOM   679   O  O   . ASP A 1 86   ? 97.033  74.843  94.036  1.00 74.40  ? 86   ASP A O   1 
ATOM   680   C  CB  . ASP A 1 86   ? 96.729  74.080  96.904  1.00 87.85  ? 86   ASP A CB  1 
ATOM   681   C  CG  . ASP A 1 86   ? 95.580  73.497  96.115  1.00 103.60 ? 86   ASP A CG  1 
ATOM   682   O  OD1 . ASP A 1 86   ? 94.490  74.104  96.101  1.00 107.79 ? 86   ASP A OD1 1 
ATOM   683   O  OD2 . ASP A 1 86   ? 95.775  72.429  95.496  1.00 98.01  ? 86   ASP A OD2 1 
ATOM   684   N  N   . ALA A 1 87   ? 98.589  76.232  94.875  1.00 79.18  ? 87   ALA A N   1 
ATOM   685   C  CA  . ALA A 1 87   ? 98.276  77.232  93.857  1.00 52.63  ? 87   ALA A CA  1 
ATOM   686   C  C   . ALA A 1 87   ? 98.629  76.791  92.436  1.00 63.94  ? 87   ALA A C   1 
ATOM   687   O  O   . ALA A 1 87   ? 98.135  77.399  91.481  1.00 73.94  ? 87   ALA A O   1 
ATOM   688   C  CB  . ALA A 1 87   ? 98.991  78.546  94.176  1.00 62.85  ? 87   ALA A CB  1 
ATOM   689   N  N   . ILE A 1 88   ? 99.447  75.747  92.263  1.00 77.83  ? 88   ILE A N   1 
ATOM   690   C  CA  . ILE A 1 88   ? 99.878  75.354  90.918  1.00 65.72  ? 88   ILE A CA  1 
ATOM   691   C  C   . ILE A 1 88   ? 98.839  74.566  90.130  1.00 67.61  ? 88   ILE A C   1 
ATOM   692   O  O   . ILE A 1 88   ? 98.958  74.459  88.903  1.00 71.29  ? 88   ILE A O   1 
ATOM   693   C  CB  . ILE A 1 88   ? 101.168 74.513  90.999  1.00 70.75  ? 88   ILE A CB  1 
ATOM   694   C  CG1 . ILE A 1 88   ? 101.849 74.421  89.630  1.00 84.31  ? 88   ILE A CG1 1 
ATOM   695   C  CG2 . ILE A 1 88   ? 100.860 73.113  91.523  1.00 73.26  ? 88   ILE A CG2 1 
ATOM   696   C  CD1 . ILE A 1 88   ? 103.101 73.576  89.621  1.00 95.80  ? 88   ILE A CD1 1 
ATOM   697   N  N   . ASN A 1 89   ? 97.795  74.052  90.774  1.00 74.65  ? 89   ASN A N   1 
ATOM   698   C  CA  . ASN A 1 89   ? 96.773  73.277  90.079  1.00 76.98  ? 89   ASN A CA  1 
ATOM   699   C  C   . ASN A 1 89   ? 95.642  74.136  89.534  1.00 83.53  ? 89   ASN A C   1 
ATOM   700   O  O   . ASN A 1 89   ? 94.676  73.592  88.990  1.00 83.06  ? 89   ASN A O   1 
ATOM   701   C  CB  . ASN A 1 89   ? 96.210  72.187  90.994  1.00 74.18  ? 89   ASN A CB  1 
ATOM   702   C  CG  . ASN A 1 89   ? 97.282  71.249  91.511  1.00 75.41  ? 89   ASN A CG  1 
ATOM   703   O  OD1 . ASN A 1 89   ? 98.055  70.683  90.735  1.00 76.45  ? 89   ASN A OD1 1 
ATOM   704   N  ND2 . ASN A 1 89   ? 97.332  71.074  92.825  1.00 80.53  ? 89   ASN A ND2 1 
ATOM   705   N  N   . HIS A 1 90   ? 95.743  75.456  89.650  1.00 83.05  ? 90   HIS A N   1 
ATOM   706   C  CA  . HIS A 1 90   ? 94.686  76.361  89.226  1.00 78.58  ? 90   HIS A CA  1 
ATOM   707   C  C   . HIS A 1 90   ? 95.209  77.391  88.236  1.00 86.99  ? 90   HIS A C   1 
ATOM   708   O  O   . HIS A 1 90   ? 94.782  78.545  88.235  1.00 92.69  ? 90   HIS A O   1 
ATOM   709   C  CB  . HIS A 1 90   ? 94.061  77.069  90.425  1.00 78.33  ? 90   HIS A CB  1 
ATOM   710   C  CG  . HIS A 1 90   ? 93.519  76.139  91.465  1.00 81.50  ? 90   HIS A CG  1 
ATOM   711   N  ND1 . HIS A 1 90   ? 92.329  75.460  91.308  1.00 84.69  ? 90   HIS A ND1 1 
ATOM   712   C  CD2 . HIS A 1 90   ? 93.998  75.785  92.681  1.00 81.23  ? 90   HIS A CD2 1 
ATOM   713   C  CE1 . HIS A 1 90   ? 92.102  74.723  92.380  1.00 87.53  ? 90   HIS A CE1 1 
ATOM   714   N  NE2 . HIS A 1 90   ? 93.100  74.902  93.228  1.00 88.60  ? 90   HIS A NE2 1 
ATOM   715   N  N   . VAL A 1 91   ? 96.104  76.969  87.338  1.00 86.34  ? 91   VAL A N   1 
ATOM   716   C  CA  . VAL A 1 91   ? 96.685  77.915  86.393  1.00 64.95  ? 91   VAL A CA  1 
ATOM   717   C  C   . VAL A 1 91   ? 95.637  78.344  85.377  1.00 76.92  ? 91   VAL A C   1 
ATOM   718   O  O   . VAL A 1 91   ? 95.672  79.474  84.878  1.00 81.09  ? 91   VAL A O   1 
ATOM   719   C  CB  . VAL A 1 91   ? 97.930  77.320  85.706  1.00 61.93  ? 91   VAL A CB  1 
ATOM   720   C  CG1 . VAL A 1 91   ? 98.563  78.339  84.765  1.00 66.30  ? 91   VAL A CG1 1 
ATOM   721   C  CG2 . VAL A 1 91   ? 98.943  76.864  86.744  1.00 80.58  ? 91   VAL A CG2 1 
ATOM   722   N  N   . ASP A 1 92   ? 94.673  77.470  85.072  1.00 82.61  ? 92   ASP A N   1 
ATOM   723   C  CA  . ASP A 1 92   ? 93.650  77.812  84.092  1.00 78.13  ? 92   ASP A CA  1 
ATOM   724   C  C   . ASP A 1 92   ? 92.798  78.988  84.546  1.00 75.18  ? 92   ASP A C   1 
ATOM   725   O  O   . ASP A 1 92   ? 92.206  79.672  83.706  1.00 88.44  ? 92   ASP A O   1 
ATOM   726   C  CB  . ASP A 1 92   ? 92.755  76.600  83.841  1.00 89.99  ? 92   ASP A CB  1 
ATOM   727   C  CG  . ASP A 1 92   ? 93.488  75.471  83.154  1.00 128.25 ? 92   ASP A CG  1 
ATOM   728   O  OD1 . ASP A 1 92   ? 92.889  74.390  82.979  1.00 143.08 ? 92   ASP A OD1 1 
ATOM   729   O  OD2 . ASP A 1 92   ? 94.673  75.659  82.806  1.00 113.99 ? 92   ASP A OD2 1 
ATOM   730   N  N   . ASP A 1 93   ? 92.724  79.237  85.854  1.00 73.73  ? 93   ASP A N   1 
ATOM   731   C  CA  . ASP A 1 93   ? 91.969  80.382  86.348  1.00 70.42  ? 93   ASP A CA  1 
ATOM   732   C  C   . ASP A 1 93   ? 92.668  81.679  85.972  1.00 66.52  ? 93   ASP A C   1 
ATOM   733   O  O   . ASP A 1 93   ? 92.017  82.678  85.644  1.00 68.31  ? 93   ASP A O   1 
ATOM   734   C  CB  . ASP A 1 93   ? 91.772  80.274  87.857  1.00 74.38  ? 93   ASP A CB  1 
ATOM   735   C  CG  . ASP A 1 93   ? 90.746  79.223  88.230  1.00 95.71  ? 93   ASP A CG  1 
ATOM   736   O  OD1 . ASP A 1 93   ? 89.715  79.131  87.534  1.00 101.87 ? 93   ASP A OD1 1 
ATOM   737   O  OD2 . ASP A 1 93   ? 90.970  78.486  89.214  1.00 101.30 ? 93   ASP A OD2 1 
ATOM   738   N  N   . PHE A 1 94   ? 93.998  81.671  86.004  1.00 59.37  ? 94   PHE A N   1 
ATOM   739   C  CA  . PHE A 1 94   ? 94.811  82.804  85.590  1.00 58.07  ? 94   PHE A CA  1 
ATOM   740   C  C   . PHE A 1 94   ? 95.699  82.405  84.418  1.00 63.06  ? 94   PHE A C   1 
ATOM   741   O  O   . PHE A 1 94   ? 96.922  82.567  84.466  1.00 61.76  ? 94   PHE A O   1 
ATOM   742   C  CB  . PHE A 1 94   ? 95.627  83.358  86.767  1.00 53.20  ? 94   PHE A CB  1 
ATOM   743   C  CG  . PHE A 1 94   ? 96.405  82.317  87.530  1.00 72.18  ? 94   PHE A CG  1 
ATOM   744   C  CD1 . PHE A 1 94   ? 97.746  82.096  87.262  1.00 93.29  ? 94   PHE A CD1 1 
ATOM   745   C  CD2 . PHE A 1 94   ? 95.801  81.578  88.533  1.00 82.95  ? 94   PHE A CD2 1 
ATOM   746   C  CE1 . PHE A 1 94   ? 98.463  81.147  87.964  1.00 75.49  ? 94   PHE A CE1 1 
ATOM   747   C  CE2 . PHE A 1 94   ? 96.517  80.630  89.243  1.00 70.44  ? 94   PHE A CE2 1 
ATOM   748   C  CZ  . PHE A 1 94   ? 97.847  80.413  88.954  1.00 60.71  ? 94   PHE A CZ  1 
ATOM   749   N  N   . LYS A 1 95   ? 95.087  81.816  83.385  1.00 77.91  ? 95   LYS A N   1 
ATOM   750   C  CA  . LYS A 1 95   ? 95.826  81.476  82.172  1.00 65.29  ? 95   LYS A CA  1 
ATOM   751   C  C   . LYS A 1 95   ? 96.372  82.730  81.507  1.00 71.71  ? 95   LYS A C   1 
ATOM   752   O  O   . LYS A 1 95   ? 97.507  82.738  81.013  1.00 78.35  ? 95   LYS A O   1 
ATOM   753   C  CB  . LYS A 1 95   ? 94.933  80.705  81.201  1.00 87.94  ? 95   LYS A CB  1 
ATOM   754   C  CG  . LYS A 1 95   ? 95.681  80.092  80.027  1.00 103.33 ? 95   LYS A CG  1 
ATOM   755   C  CD  . LYS A 1 95   ? 96.665  79.023  80.462  1.00 120.11 ? 95   LYS A CD  1 
ATOM   756   C  CE  . LYS A 1 95   ? 95.997  77.664  80.518  1.00 130.44 ? 95   LYS A CE  1 
ATOM   757   N  NZ  . LYS A 1 95   ? 96.929  76.612  81.002  1.00 114.81 ? 95   LYS A NZ  1 
ATOM   758   N  N   . TYR A 1 96   ? 95.581  83.802  81.486  1.00 66.92  ? 96   TYR A N   1 
ATOM   759   C  CA  . TYR A 1 96   ? 96.105  85.121  81.160  1.00 54.78  ? 96   TYR A CA  1 
ATOM   760   C  C   . TYR A 1 96   ? 97.108  85.504  82.244  1.00 68.12  ? 96   TYR A C   1 
ATOM   761   O  O   . TYR A 1 96   ? 97.290  84.748  83.201  1.00 79.66  ? 96   TYR A O   1 
ATOM   762   C  CB  . TYR A 1 96   ? 94.982  86.152  81.034  1.00 55.30  ? 96   TYR A CB  1 
ATOM   763   C  CG  . TYR A 1 96   ? 94.427  86.610  82.358  1.00 61.30  ? 96   TYR A CG  1 
ATOM   764   C  CD1 . TYR A 1 96   ? 94.715  87.873  82.849  1.00 68.11  ? 96   TYR A CD1 1 
ATOM   765   C  CD2 . TYR A 1 96   ? 93.604  85.787  83.113  1.00 68.45  ? 96   TYR A CD2 1 
ATOM   766   C  CE1 . TYR A 1 96   ? 94.211  88.303  84.061  1.00 56.44  ? 96   TYR A CE1 1 
ATOM   767   C  CE2 . TYR A 1 96   ? 93.092  86.209  84.327  1.00 69.21  ? 96   TYR A CE2 1 
ATOM   768   C  CZ  . TYR A 1 96   ? 93.399  87.468  84.795  1.00 51.68  ? 96   TYR A CZ  1 
ATOM   769   O  OH  . TYR A 1 96   ? 92.896  87.897  86.003  1.00 57.48  ? 96   TYR A OH  1 
ATOM   770   N  N   . LEU A 1 97   ? 97.750  86.664  82.126  1.00 58.41  ? 97   LEU A N   1 
ATOM   771   C  CA  . LEU A 1 97   ? 98.944  87.078  82.860  1.00 65.96  ? 97   LEU A CA  1 
ATOM   772   C  C   . LEU A 1 97   ? 100.186 86.385  82.314  1.00 74.86  ? 97   LEU A C   1 
ATOM   773   O  O   . LEU A 1 97   ? 101.294 86.792  82.663  1.00 76.58  ? 97   LEU A O   1 
ATOM   774   C  CB  . LEU A 1 97   ? 98.882  86.818  84.381  1.00 42.67  ? 97   LEU A CB  1 
ATOM   775   C  CG  . LEU A 1 97   ? 97.749  87.276  85.294  1.00 63.90  ? 97   LEU A CG  1 
ATOM   776   C  CD1 . LEU A 1 97   ? 98.039  86.802  86.710  1.00 52.19  ? 97   LEU A CD1 1 
ATOM   777   C  CD2 . LEU A 1 97   ? 97.627  88.787  85.259  1.00 74.75  ? 97   LEU A CD2 1 
ATOM   778   N  N   . LEU A 1 98   ? 100.040 85.368  81.452  1.00 66.53  ? 98   LEU A N   1 
ATOM   779   C  CA  . LEU A 1 98   ? 101.093 84.775  80.634  1.00 62.30  ? 98   LEU A CA  1 
ATOM   780   C  C   . LEU A 1 98   ? 102.424 84.689  81.375  1.00 65.78  ? 98   LEU A C   1 
ATOM   781   O  O   . LEU A 1 98   ? 103.362 85.426  81.048  1.00 77.85  ? 98   LEU A O   1 
ATOM   782   C  CB  . LEU A 1 98   ? 101.247 85.612  79.364  1.00 62.07  ? 98   LEU A CB  1 
ATOM   783   C  CG  . LEU A 1 98   ? 99.984  85.666  78.502  1.00 65.35  ? 98   LEU A CG  1 
ATOM   784   C  CD1 . LEU A 1 98   ? 100.137 86.691  77.393  1.00 63.26  ? 98   LEU A CD1 1 
ATOM   785   C  CD2 . LEU A 1 98   ? 99.680  84.290  77.929  1.00 91.11  ? 98   LEU A CD2 1 
ATOM   786   N  N   . PRO A 1 99   ? 102.539 83.808  82.378  1.00 63.08  ? 99   PRO A N   1 
ATOM   787   C  CA  . PRO A 1 99   ? 103.739 83.823  83.245  1.00 58.55  ? 99   PRO A CA  1 
ATOM   788   C  C   . PRO A 1 99   ? 105.055 83.650  82.496  1.00 72.72  ? 99   PRO A C   1 
ATOM   789   O  O   . PRO A 1 99   ? 106.055 84.324  82.809  1.00 72.41  ? 99   PRO A O   1 
ATOM   790   C  CB  . PRO A 1 99   ? 103.478 82.654  84.209  1.00 55.45  ? 99   PRO A CB  1 
ATOM   791   C  CG  . PRO A 1 99   ? 101.988 82.435  84.174  1.00 50.56  ? 99   PRO A CG  1 
ATOM   792   C  CD  . PRO A 1 99   ? 101.564 82.777  82.780  1.00 56.91  ? 99   PRO A CD  1 
ATOM   793   N  N   . SER A 1 100  ? 105.072 82.766  81.495  1.00 66.95  ? 100  SER A N   1 
ATOM   794   C  CA  . SER A 1 100  ? 106.298 82.525  80.743  1.00 63.67  ? 100  SER A CA  1 
ATOM   795   C  C   . SER A 1 100  ? 106.777 83.787  80.043  1.00 65.88  ? 100  SER A C   1 
ATOM   796   O  O   . SER A 1 100  ? 107.986 84.025  79.957  1.00 75.51  ? 100  SER A O   1 
ATOM   797   C  CB  . SER A 1 100  ? 106.075 81.405  79.724  1.00 73.81  ? 100  SER A CB  1 
ATOM   798   O  OG  . SER A 1 100  ? 105.113 81.781  78.750  1.00 74.60  ? 100  SER A OG  1 
ATOM   799   N  N   . GLU A 1 101  ? 105.853 84.627  79.573  1.00 56.23  ? 101  GLU A N   1 
ATOM   800   C  CA  . GLU A 1 101  ? 106.260 85.891  78.967  1.00 57.04  ? 101  GLU A CA  1 
ATOM   801   C  C   . GLU A 1 101  ? 106.845 86.851  79.996  1.00 62.47  ? 101  GLU A C   1 
ATOM   802   O  O   . GLU A 1 101  ? 107.771 87.608  79.679  1.00 72.95  ? 101  GLU A O   1 
ATOM   803   C  CB  . GLU A 1 101  ? 105.085 86.530  78.233  1.00 53.65  ? 101  GLU A CB  1 
ATOM   804   C  CG  . GLU A 1 101  ? 104.641 85.741  77.021  1.00 82.92  ? 101  GLU A CG  1 
ATOM   805   C  CD  . GLU A 1 101  ? 103.864 86.588  76.043  1.00 110.16 ? 101  GLU A CD  1 
ATOM   806   O  OE1 . GLU A 1 101  ? 103.595 87.766  76.359  1.00 97.58  ? 101  GLU A OE1 1 
ATOM   807   O  OE2 . GLU A 1 101  ? 103.527 86.078  74.953  1.00 110.80 ? 101  GLU A OE2 1 
ATOM   808   N  N   . LEU A 1 102  ? 106.319 86.852  81.225  1.00 57.66  ? 102  LEU A N   1 
ATOM   809   C  CA  . LEU A 1 102  ? 106.926 87.659  82.279  1.00 50.33  ? 102  LEU A CA  1 
ATOM   810   C  C   . LEU A 1 102  ? 108.378 87.266  82.492  1.00 63.76  ? 102  LEU A C   1 
ATOM   811   O  O   . LEU A 1 102  ? 109.280 88.120  82.515  1.00 73.70  ? 102  LEU A O   1 
ATOM   812   C  CB  . LEU A 1 102  ? 106.141 87.501  83.586  1.00 53.23  ? 102  LEU A CB  1 
ATOM   813   C  CG  . LEU A 1 102  ? 104.617 87.541  83.549  1.00 53.93  ? 102  LEU A CG  1 
ATOM   814   C  CD1 . LEU A 1 102  ? 104.065 87.324  84.947  1.00 55.50  ? 102  LEU A CD1 1 
ATOM   815   C  CD2 . LEU A 1 102  ? 104.171 88.885  83.012  1.00 67.65  ? 102  LEU A CD2 1 
ATOM   816   N  N   . VAL A 1 103  ? 108.629 85.963  82.618  1.00 61.82  ? 103  VAL A N   1 
ATOM   817   C  CA  . VAL A 1 103  ? 110.003 85.501  82.818  1.00 54.12  ? 103  VAL A CA  1 
ATOM   818   C  C   . VAL A 1 103  ? 110.867 85.854  81.612  1.00 66.43  ? 103  VAL A C   1 
ATOM   819   O  O   . VAL A 1 103  ? 112.018 86.300  81.753  1.00 74.20  ? 103  VAL A O   1 
ATOM   820   C  CB  . VAL A 1 103  ? 110.024 83.996  83.100  1.00 46.66  ? 103  VAL A CB  1 
ATOM   821   C  CG1 . VAL A 1 103  ? 111.449 83.442  83.065  1.00 66.62  ? 103  VAL A CG1 1 
ATOM   822   C  CG2 . VAL A 1 103  ? 109.374 83.687  84.454  1.00 46.08  ? 103  VAL A CG2 1 
ATOM   823   N  N   . LYS A 1 104  ? 110.310 85.695  80.410  1.00 59.58  ? 104  LYS A N   1 
ATOM   824   C  CA  . LYS A 1 104  ? 111.047 85.974  79.186  1.00 52.64  ? 104  LYS A CA  1 
ATOM   825   C  C   . LYS A 1 104  ? 111.478 87.438  79.116  1.00 52.68  ? 104  LYS A C   1 
ATOM   826   O  O   . LYS A 1 104  ? 112.641 87.759  78.828  1.00 64.72  ? 104  LYS A O   1 
ATOM   827   C  CB  . LYS A 1 104  ? 110.118 85.688  78.005  1.00 65.69  ? 104  LYS A CB  1 
ATOM   828   C  CG  . LYS A 1 104  ? 110.742 85.984  76.682  1.00 65.78  ? 104  LYS A CG  1 
ATOM   829   C  CD  . LYS A 1 104  ? 110.096 85.214  75.597  1.00 68.96  ? 104  LYS A CD  1 
ATOM   830   C  CE  . LYS A 1 104  ? 110.698 85.591  74.290  1.00 89.10  ? 104  LYS A CE  1 
ATOM   831   N  NZ  . LYS A 1 104  ? 112.077 85.102  74.384  1.00 84.81  ? 104  LYS A NZ  1 
ATOM   832   N  N   . TYR A 1 105  ? 110.550 88.344  79.418  1.00 49.82  ? 105  TYR A N   1 
ATOM   833   C  CA  . TYR A 1 105  ? 110.861 89.769  79.371  1.00 47.02  ? 105  TYR A CA  1 
ATOM   834   C  C   . TYR A 1 105  ? 111.902 90.148  80.424  1.00 62.57  ? 105  TYR A C   1 
ATOM   835   O  O   . TYR A 1 105  ? 112.825 90.932  80.149  1.00 79.34  ? 105  TYR A O   1 
ATOM   836   C  CB  . TYR A 1 105  ? 109.598 90.597  79.572  1.00 48.30  ? 105  TYR A CB  1 
ATOM   837   C  CG  . TYR A 1 105  ? 109.928 92.043  79.690  1.00 53.65  ? 105  TYR A CG  1 
ATOM   838   C  CD1 . TYR A 1 105  ? 110.468 92.728  78.615  1.00 54.47  ? 105  TYR A CD1 1 
ATOM   839   C  CD2 . TYR A 1 105  ? 109.769 92.718  80.889  1.00 59.19  ? 105  TYR A CD2 1 
ATOM   840   C  CE1 . TYR A 1 105  ? 110.799 94.067  78.712  1.00 50.90  ? 105  TYR A CE1 1 
ATOM   841   C  CE2 . TYR A 1 105  ? 110.103 94.058  80.998  1.00 47.87  ? 105  TYR A CE2 1 
ATOM   842   C  CZ  . TYR A 1 105  ? 110.617 94.727  79.907  1.00 51.97  ? 105  TYR A CZ  1 
ATOM   843   O  OH  . TYR A 1 105  ? 110.955 96.057  80.015  1.00 62.87  ? 105  TYR A OH  1 
ATOM   844   N  N   . ALA A 1 106  ? 111.781 89.598  81.637  1.00 53.61  ? 106  ALA A N   1 
ATOM   845   C  CA  . ALA A 1 106  ? 112.758 89.932  82.671  1.00 41.96  ? 106  ALA A CA  1 
ATOM   846   C  C   . ALA A 1 106  ? 114.164 89.475  82.285  1.00 64.65  ? 106  ALA A C   1 
ATOM   847   O  O   . ALA A 1 106  ? 115.145 90.218  82.465  1.00 68.75  ? 106  ALA A O   1 
ATOM   848   C  CB  . ALA A 1 106  ? 112.336 89.323  84.007  1.00 56.35  ? 106  ALA A CB  1 
ATOM   849   N  N   . ASN A 1 107  ? 114.277 88.263  81.726  1.00 64.28  ? 107  ASN A N   1 
ATOM   850   C  CA  . ASN A 1 107  ? 115.582 87.773  81.295  1.00 59.65  ? 107  ASN A CA  1 
ATOM   851   C  C   . ASN A 1 107  ? 116.167 88.651  80.196  1.00 65.58  ? 107  ASN A C   1 
ATOM   852   O  O   . ASN A 1 107  ? 117.358 89.008  80.231  1.00 70.32  ? 107  ASN A O   1 
ATOM   853   C  CB  . ASN A 1 107  ? 115.447 86.334  80.802  1.00 66.34  ? 107  ASN A CB  1 
ATOM   854   C  CG  . ASN A 1 107  ? 115.303 85.345  81.935  1.00 65.31  ? 107  ASN A CG  1 
ATOM   855   O  OD1 . ASN A 1 107  ? 115.497 85.687  83.098  1.00 71.72  ? 107  ASN A OD1 1 
ATOM   856   N  ND2 . ASN A 1 107  ? 114.955 84.108  81.599  1.00 77.25  ? 107  ASN A ND2 1 
ATOM   857   N  N   . TRP A 1 108  ? 115.335 89.020  79.216  1.00 64.57  ? 108  TRP A N   1 
ATOM   858   C  CA  . TRP A 1 108  ? 115.817 89.875  78.140  1.00 68.98  ? 108  TRP A CA  1 
ATOM   859   C  C   . TRP A 1 108  ? 116.300 91.215  78.676  1.00 58.72  ? 108  TRP A C   1 
ATOM   860   O  O   . TRP A 1 108  ? 117.316 91.750  78.213  1.00 69.04  ? 108  TRP A O   1 
ATOM   861   C  CB  . TRP A 1 108  ? 114.725 90.084  77.093  1.00 58.11  ? 108  TRP A CB  1 
ATOM   862   C  CG  . TRP A 1 108  ? 115.207 90.897  75.939  1.00 57.61  ? 108  TRP A CG  1 
ATOM   863   C  CD1 . TRP A 1 108  ? 115.794 90.437  74.800  1.00 62.70  ? 108  TRP A CD1 1 
ATOM   864   C  CD2 . TRP A 1 108  ? 115.163 92.325  75.820  1.00 65.12  ? 108  TRP A CD2 1 
ATOM   865   N  NE1 . TRP A 1 108  ? 116.115 91.488  73.975  1.00 58.91  ? 108  TRP A NE1 1 
ATOM   866   C  CE2 . TRP A 1 108  ? 115.737 92.659  74.580  1.00 60.64  ? 108  TRP A CE2 1 
ATOM   867   C  CE3 . TRP A 1 108  ? 114.692 93.353  76.643  1.00 72.85  ? 108  TRP A CE3 1 
ATOM   868   C  CZ2 . TRP A 1 108  ? 115.850 93.977  74.140  1.00 59.90  ? 108  TRP A CZ2 1 
ATOM   869   C  CZ3 . TRP A 1 108  ? 114.805 94.663  76.204  1.00 54.77  ? 108  TRP A CZ3 1 
ATOM   870   C  CH2 . TRP A 1 108  ? 115.380 94.961  74.965  1.00 45.48  ? 108  TRP A CH2 1 
ATOM   871   N  N   . ASP A 1 109  ? 115.585 91.772  79.656  1.00 53.28  ? 109  ASP A N   1 
ATOM   872   C  CA  . ASP A 1 109  ? 115.991 93.057  80.212  1.00 42.23  ? 109  ASP A CA  1 
ATOM   873   C  C   . ASP A 1 109  ? 117.328 92.971  80.943  1.00 76.86  ? 109  ASP A C   1 
ATOM   874   O  O   . ASP A 1 109  ? 118.165 93.878  80.816  1.00 86.29  ? 109  ASP A O   1 
ATOM   875   C  CB  . ASP A 1 109  ? 114.909 93.594  81.146  1.00 53.78  ? 109  ASP A CB  1 
ATOM   876   C  CG  . ASP A 1 109  ? 115.082 95.072  81.438  1.00 67.19  ? 109  ASP A CG  1 
ATOM   877   O  OD1 . ASP A 1 109  ? 114.245 95.642  82.168  1.00 81.37  ? 109  ASP A OD1 1 
ATOM   878   O  OD2 . ASP A 1 109  ? 116.043 95.673  80.915  1.00 66.07  ? 109  ASP A OD2 1 
ATOM   879   N  N   . ASN A 1 110  ? 117.564 91.900  81.712  1.00 78.19  ? 110  ASN A N   1 
ATOM   880   C  CA  . ASN A 1 110  ? 118.893 91.769  82.319  1.00 71.38  ? 110  ASN A CA  1 
ATOM   881   C  C   . ASN A 1 110  ? 119.993 91.652  81.270  1.00 68.93  ? 110  ASN A C   1 
ATOM   882   O  O   . ASN A 1 110  ? 121.065 92.254  81.423  1.00 67.98  ? 110  ASN A O   1 
ATOM   883   C  CB  . ASN A 1 110  ? 118.973 90.597  83.296  1.00 72.68  ? 110  ASN A CB  1 
ATOM   884   C  CG  . ASN A 1 110  ? 118.387 90.928  84.647  1.00 85.36  ? 110  ASN A CG  1 
ATOM   885   O  OD1 . ASN A 1 110  ? 118.560 92.038  85.153  1.00 78.44  ? 110  ASN A OD1 1 
ATOM   886   N  ND2 . ASN A 1 110  ? 117.750 89.954  85.271  1.00 105.98 ? 110  ASN A ND2 1 
ATOM   887   N  N   . GLU A 1 111  ? 119.764 90.874  80.207  1.00 72.45  ? 111  GLU A N   1 
ATOM   888   C  CA  . GLU A 1 111  ? 120.792 90.789  79.169  1.00 64.83  ? 111  GLU A CA  1 
ATOM   889   C  C   . GLU A 1 111  ? 121.058 92.151  78.542  1.00 66.38  ? 111  GLU A C   1 
ATOM   890   O  O   . GLU A 1 111  ? 122.219 92.523  78.295  1.00 69.67  ? 111  GLU A O   1 
ATOM   891   C  CB  . GLU A 1 111  ? 120.397 89.771  78.103  1.00 65.64  ? 111  GLU A CB  1 
ATOM   892   C  CG  . GLU A 1 111  ? 120.340 88.362  78.629  1.00 79.06  ? 111  GLU A CG  1 
ATOM   893   C  CD  . GLU A 1 111  ? 121.674 87.935  79.207  1.00 105.93 ? 111  GLU A CD  1 
ATOM   894   O  OE1 . GLU A 1 111  ? 122.533 87.451  78.441  1.00 107.32 ? 111  GLU A OE1 1 
ATOM   895   O  OE2 . GLU A 1 111  ? 121.865 88.085  80.433  1.00 105.25 ? 111  GLU A OE2 1 
ATOM   896   N  N   . PHE A 1 112  ? 119.994 92.917  78.297  1.00 64.09  ? 112  PHE A N   1 
ATOM   897   C  CA  . PHE A 1 112  ? 120.157 94.245  77.722  1.00 54.32  ? 112  PHE A CA  1 
ATOM   898   C  C   . PHE A 1 112  ? 120.998 95.131  78.627  1.00 55.04  ? 112  PHE A C   1 
ATOM   899   O  O   . PHE A 1 112  ? 121.911 95.826  78.163  1.00 77.79  ? 112  PHE A O   1 
ATOM   900   C  CB  . PHE A 1 112  ? 118.794 94.893  77.484  1.00 62.81  ? 112  PHE A CB  1 
ATOM   901   C  CG  . PHE A 1 112  ? 118.868 96.385  77.386  1.00 49.83  ? 112  PHE A CG  1 
ATOM   902   C  CD1 . PHE A 1 112  ? 119.592 96.981  76.368  1.00 60.93  ? 112  PHE A CD1 1 
ATOM   903   C  CD2 . PHE A 1 112  ? 118.263 97.191  78.334  1.00 60.80  ? 112  PHE A CD2 1 
ATOM   904   C  CE1 . PHE A 1 112  ? 119.688 98.353  76.277  1.00 71.85  ? 112  PHE A CE1 1 
ATOM   905   C  CE2 . PHE A 1 112  ? 118.356 98.570  78.249  1.00 63.30  ? 112  PHE A CE2 1 
ATOM   906   C  CZ  . PHE A 1 112  ? 119.070 99.150  77.219  1.00 62.73  ? 112  PHE A CZ  1 
ATOM   907   N  N   . LEU A 1 113  ? 120.692 95.133  79.925  1.00 51.97  ? 113  LEU A N   1 
ATOM   908   C  CA  . LEU A 1 113  ? 121.433 95.998  80.838  1.00 44.70  ? 113  LEU A CA  1 
ATOM   909   C  C   . LEU A 1 113  ? 122.896 95.573  80.945  1.00 72.24  ? 113  LEU A C   1 
ATOM   910   O  O   . LEU A 1 113  ? 123.787 96.420  81.052  1.00 72.71  ? 113  LEU A O   1 
ATOM   911   C  CB  . LEU A 1 113  ? 120.774 96.029  82.205  1.00 47.90  ? 113  LEU A CB  1 
ATOM   912   C  CG  . LEU A 1 113  ? 121.470 97.016  83.145  1.00 60.25  ? 113  LEU A CG  1 
ATOM   913   C  CD1 . LEU A 1 113  ? 121.186 98.427  82.664  1.00 50.77  ? 113  LEU A CD1 1 
ATOM   914   C  CD2 . LEU A 1 113  ? 121.001 96.836  84.579  1.00 60.75  ? 113  LEU A CD2 1 
ATOM   915   N  N   . LYS A 1 114  ? 123.159 94.267  80.882  1.00 71.96  ? 114  LYS A N   1 
ATOM   916   C  CA  . LYS A 1 114  ? 124.541 93.796  80.910  1.00 51.74  ? 114  LYS A CA  1 
ATOM   917   C  C   . LYS A 1 114  ? 125.312 94.306  79.695  1.00 64.07  ? 114  LYS A C   1 
ATOM   918   O  O   . LYS A 1 114  ? 126.447 94.794  79.816  1.00 69.66  ? 114  LYS A O   1 
ATOM   919   C  CB  . LYS A 1 114  ? 124.602 92.279  80.940  1.00 57.71  ? 114  LYS A CB  1 
ATOM   920   C  CG  . LYS A 1 114  ? 124.271 91.637  82.273  1.00 65.10  ? 114  LYS A CG  1 
ATOM   921   C  CD  . LYS A 1 114  ? 124.738 90.187  82.260  1.00 82.58  ? 114  LYS A CD  1 
ATOM   922   C  CE  . LYS A 1 114  ? 124.295 89.458  83.508  1.00 85.21  ? 114  LYS A CE  1 
ATOM   923   N  NZ  . LYS A 1 114  ? 122.898 88.976  83.346  1.00 79.26  ? 114  LYS A NZ  1 
ATOM   924   N  N   . ALA A 1 115  ? 124.701 94.223  78.503  1.00 68.96  ? 115  ALA A N   1 
ATOM   925   C  CA  . ALA A 1 115  ? 125.353 94.735  77.297  1.00 56.43  ? 115  ALA A CA  1 
ATOM   926   C  C   . ALA A 1 115  ? 125.592 96.239  77.398  1.00 63.16  ? 115  ALA A C   1 
ATOM   927   O  O   . ALA A 1 115  ? 126.668 96.741  77.032  1.00 71.24  ? 115  ALA A O   1 
ATOM   928   C  CB  . ALA A 1 115  ? 124.515 94.401  76.065  1.00 65.88  ? 115  ALA A CB  1 
ATOM   929   N  N   . TYR A 1 116  ? 124.595 96.963  77.904  1.00 63.53  ? 116  TYR A N   1 
ATOM   930   C  CA  . TYR A 1 116  ? 124.686 98.410  78.054  1.00 49.01  ? 116  TYR A CA  1 
ATOM   931   C  C   . TYR A 1 116  ? 125.857 98.791  78.950  1.00 63.16  ? 116  TYR A C   1 
ATOM   932   O  O   . TYR A 1 116  ? 126.674 99.657  78.605  1.00 82.04  ? 116  TYR A O   1 
ATOM   933   C  CB  . TYR A 1 116  ? 123.370 98.918  78.646  1.00 56.31  ? 116  TYR A CB  1 
ATOM   934   C  CG  . TYR A 1 116  ? 123.206 100.415 78.706  1.00 67.10  ? 116  TYR A CG  1 
ATOM   935   C  CD1 . TYR A 1 116  ? 123.636 101.139 79.809  1.00 63.54  ? 116  TYR A CD1 1 
ATOM   936   C  CD2 . TYR A 1 116  ? 122.571 101.099 77.682  1.00 79.22  ? 116  TYR A CD2 1 
ATOM   937   C  CE1 . TYR A 1 116  ? 123.468 102.509 79.872  1.00 64.73  ? 116  TYR A CE1 1 
ATOM   938   C  CE2 . TYR A 1 116  ? 122.398 102.468 77.736  1.00 71.59  ? 116  TYR A CE2 1 
ATOM   939   C  CZ  . TYR A 1 116  ? 122.847 103.168 78.832  1.00 69.64  ? 116  TYR A CZ  1 
ATOM   940   O  OH  . TYR A 1 116  ? 122.679 104.532 78.886  1.00 69.30  ? 116  TYR A OH  1 
ATOM   941   N  N   . LEU A 1 117  ? 125.964 98.132  80.104  1.00 69.02  ? 117  LEU A N   1 
ATOM   942   C  CA  . LEU A 1 117  ? 127.028 98.453  81.046  1.00 66.93  ? 117  LEU A CA  1 
ATOM   943   C  C   . LEU A 1 117  ? 128.391 98.024  80.520  1.00 73.57  ? 117  LEU A C   1 
ATOM   944   O  O   . LEU A 1 117  ? 129.389 98.710  80.769  1.00 69.45  ? 117  LEU A O   1 
ATOM   945   C  CB  . LEU A 1 117  ? 126.733 97.787  82.387  1.00 68.95  ? 117  LEU A CB  1 
ATOM   946   C  CG  . LEU A 1 117  ? 125.631 98.490  83.174  1.00 69.09  ? 117  LEU A CG  1 
ATOM   947   C  CD1 . LEU A 1 117  ? 125.319 97.744  84.458  1.00 56.88  ? 117  LEU A CD1 1 
ATOM   948   C  CD2 . LEU A 1 117  ? 126.054 99.922  83.470  1.00 58.63  ? 117  LEU A CD2 1 
ATOM   949   N  N   . ASN A 1 118  ? 128.456 96.909  79.787  1.00 78.00  ? 118  ASN A N   1 
ATOM   950   C  CA  . ASN A 1 118  ? 129.721 96.507  79.183  1.00 74.40  ? 118  ASN A CA  1 
ATOM   951   C  C   . ASN A 1 118  ? 130.204 97.534  78.170  1.00 80.25  ? 118  ASN A C   1 
ATOM   952   O  O   . ASN A 1 118  ? 131.404 97.821  78.091  1.00 83.92  ? 118  ASN A O   1 
ATOM   953   C  CB  . ASN A 1 118  ? 129.576 95.141  78.515  1.00 78.22  ? 118  ASN A CB  1 
ATOM   954   C  CG  . ASN A 1 118  ? 129.658 94.001  79.500  1.00 78.58  ? 118  ASN A CG  1 
ATOM   955   O  OD1 . ASN A 1 118  ? 130.153 94.165  80.614  1.00 84.14  ? 118  ASN A OD1 1 
ATOM   956   N  ND2 . ASN A 1 118  ? 129.176 92.833  79.095  1.00 77.25  ? 118  ASN A ND2 1 
ATOM   957   N  N   . LYS A 1 119  ? 129.285 98.108  77.390  1.00 84.23  ? 119  LYS A N   1 
ATOM   958   C  CA  . LYS A 1 119  ? 129.709 99.131  76.442  1.00 75.06  ? 119  LYS A CA  1 
ATOM   959   C  C   . LYS A 1 119  ? 130.123 100.415 77.150  1.00 69.23  ? 119  LYS A C   1 
ATOM   960   O  O   . LYS A 1 119  ? 131.123 101.041 76.779  1.00 75.55  ? 119  LYS A O   1 
ATOM   961   C  CB  . LYS A 1 119  ? 128.603 99.431  75.433  1.00 74.38  ? 119  LYS A CB  1 
ATOM   962   C  CG  . LYS A 1 119  ? 129.009 100.523 74.458  1.00 84.57  ? 119  LYS A CG  1 
ATOM   963   C  CD  . LYS A 1 119  ? 127.894 100.919 73.516  1.00 96.13  ? 119  LYS A CD  1 
ATOM   964   C  CE  . LYS A 1 119  ? 128.258 102.207 72.794  1.00 83.75  ? 119  LYS A CE  1 
ATOM   965   N  NZ  . LYS A 1 119  ? 127.213 102.620 71.824  1.00 84.37  ? 119  LYS A NZ  1 
ATOM   966   N  N   . ILE A 1 120  ? 129.369 100.821 78.176  1.00 69.73  ? 120  ILE A N   1 
ATOM   967   C  CA  . ILE A 1 120  ? 129.657 102.092 78.837  1.00 57.22  ? 120  ILE A CA  1 
ATOM   968   C  C   . ILE A 1 120  ? 130.978 102.029 79.597  1.00 67.36  ? 120  ILE A C   1 
ATOM   969   O  O   . ILE A 1 120  ? 131.836 102.906 79.450  1.00 72.83  ? 120  ILE A O   1 
ATOM   970   C  CB  . ILE A 1 120  ? 128.494 102.502 79.756  1.00 60.62  ? 120  ILE A CB  1 
ATOM   971   C  CG1 . ILE A 1 120  ? 127.302 102.948 78.911  1.00 56.32  ? 120  ILE A CG1 1 
ATOM   972   C  CG2 . ILE A 1 120  ? 128.916 103.646 80.665  1.00 56.57  ? 120  ILE A CG2 1 
ATOM   973   C  CD1 . ILE A 1 120  ? 127.656 103.970 77.850  1.00 70.38  ? 120  ILE A CD1 1 
ATOM   974   N  N   . LEU A 1 121  ? 131.171 100.986 80.411  1.00 73.63  ? 121  LEU A N   1 
ATOM   975   C  CA  . LEU A 1 121  ? 132.371 100.918 81.238  1.00 79.34  ? 121  LEU A CA  1 
ATOM   976   C  C   . LEU A 1 121  ? 133.646 100.655 80.451  1.00 76.50  ? 121  LEU A C   1 
ATOM   977   O  O   . LEU A 1 121  ? 134.736 100.825 81.007  1.00 75.41  ? 121  LEU A O   1 
ATOM   978   C  CB  . LEU A 1 121  ? 132.212 99.838  82.310  1.00 82.17  ? 121  LEU A CB  1 
ATOM   979   C  CG  . LEU A 1 121  ? 131.031 99.985  83.266  1.00 84.48  ? 121  LEU A CG  1 
ATOM   980   C  CD1 . LEU A 1 121  ? 130.977 98.804  84.216  1.00 83.11  ? 121  LEU A CD1 1 
ATOM   981   C  CD2 . LEU A 1 121  ? 131.169 101.286 84.041  1.00 69.97  ? 121  LEU A CD2 1 
ATOM   982   N  N   . GLY A 1 122  ? 133.554 100.248 79.189  1.00 78.36  ? 122  GLY A N   1 
ATOM   983   C  CA  . GLY A 1 122  ? 134.744 100.059 78.393  1.00 76.57  ? 122  GLY A CA  1 
ATOM   984   C  C   . GLY A 1 122  ? 135.433 98.725  78.553  1.00 79.15  ? 122  GLY A C   1 
ATOM   985   O  O   . GLY A 1 122  ? 136.406 98.462  77.833  1.00 90.00  ? 122  GLY A O   1 
ATOM   986   N  N   . LEU A 1 123  ? 134.978 97.872  79.464  1.00 76.26  ? 123  LEU A N   1 
ATOM   987   C  CA  . LEU A 1 123  ? 135.566 96.553  79.645  1.00 92.93  ? 123  LEU A CA  1 
ATOM   988   C  C   . LEU A 1 123  ? 134.566 95.506  79.187  1.00 95.83  ? 123  LEU A C   1 
ATOM   989   O  O   . LEU A 1 123  ? 133.435 95.458  79.683  1.00 104.06 ? 123  LEU A O   1 
ATOM   990   C  CB  . LEU A 1 123  ? 135.942 96.301  81.104  1.00 86.63  ? 123  LEU A CB  1 
ATOM   991   C  CG  . LEU A 1 123  ? 136.860 97.228  81.888  1.00 95.00  ? 123  LEU A CG  1 
ATOM   992   C  CD1 . LEU A 1 123  ? 136.499 97.150  83.363  1.00 82.54  ? 123  LEU A CD1 1 
ATOM   993   C  CD2 . LEU A 1 123  ? 138.313 96.850  81.666  1.00 98.91  ? 123  LEU A CD2 1 
ATOM   994   N  N   . ASP A 1 124  ? 134.991 94.667  78.253  1.00 92.58  ? 124  ASP A N   1 
ATOM   995   C  CA  . ASP A 1 124  ? 134.233 93.477  77.921  1.00 99.80  ? 124  ASP A CA  1 
ATOM   996   C  C   . ASP A 1 124  ? 134.393 92.445  79.031  1.00 111.51 ? 124  ASP A C   1 
ATOM   997   O  O   . ASP A 1 124  ? 135.383 92.445  79.768  1.00 113.91 ? 124  ASP A O   1 
ATOM   998   C  CB  . ASP A 1 124  ? 134.714 92.908  76.589  1.00 120.85 ? 124  ASP A CB  1 
ATOM   999   C  CG  . ASP A 1 124  ? 134.392 93.820  75.421  1.00 124.93 ? 124  ASP A CG  1 
ATOM   1000  O  OD1 . ASP A 1 124  ? 133.385 94.554  75.497  1.00 122.22 ? 124  ASP A OD1 1 
ATOM   1001  O  OD2 . ASP A 1 124  ? 135.157 93.817  74.435  1.00 126.74 ? 124  ASP A OD2 1 
ATOM   1002  N  N   . HIS A 1 125  ? 133.389 91.580  79.167  1.00 100.94 ? 125  HIS A N   1 
ATOM   1003  C  CA  . HIS A 1 125  ? 133.452 90.411  80.038  1.00 104.27 ? 125  HIS A CA  1 
ATOM   1004  C  C   . HIS A 1 125  ? 133.532 90.774  81.515  1.00 100.91 ? 125  HIS A C   1 
ATOM   1005  O  O   . HIS A 1 125  ? 134.043 89.983  82.314  1.00 107.03 ? 125  HIS A O   1 
ATOM   1006  C  CB  . HIS A 1 125  ? 134.639 89.511  79.678  1.00 116.30 ? 125  HIS A CB  1 
ATOM   1007  C  CG  . HIS A 1 125  ? 134.749 89.202  78.218  1.00 120.86 ? 125  HIS A CG  1 
ATOM   1008  N  ND1 . HIS A 1 125  ? 135.936 89.315  77.528  1.00 117.92 ? 125  HIS A ND1 1 
ATOM   1009  C  CD2 . HIS A 1 125  ? 133.827 88.787  77.318  1.00 128.96 ? 125  HIS A CD2 1 
ATOM   1010  C  CE1 . HIS A 1 125  ? 135.741 88.983  76.265  1.00 124.39 ? 125  HIS A CE1 1 
ATOM   1011  N  NE2 . HIS A 1 125  ? 134.470 88.658  76.111  1.00 137.86 ? 125  HIS A NE2 1 
ATOM   1012  N  N   . VAL A 1 126  ? 133.043 91.949  81.917  1.00 95.06  ? 126  VAL A N   1 
ATOM   1013  C  CA  . VAL A 1 126  ? 132.944 92.228  83.347  1.00 86.08  ? 126  VAL A CA  1 
ATOM   1014  C  C   . VAL A 1 126  ? 131.871 91.356  83.975  1.00 102.42 ? 126  VAL A C   1 
ATOM   1015  O  O   . VAL A 1 126  ? 132.034 90.850  85.092  1.00 107.20 ? 126  VAL A O   1 
ATOM   1016  C  CB  . VAL A 1 126  ? 132.664 93.720  83.600  1.00 68.79  ? 126  VAL A CB  1 
ATOM   1017  C  CG1 . VAL A 1 126  ? 132.622 94.006  85.098  1.00 71.23  ? 126  VAL A CG1 1 
ATOM   1018  C  CG2 . VAL A 1 126  ? 133.709 94.568  82.940  1.00 79.38  ? 126  VAL A CG2 1 
ATOM   1019  N  N   . PHE A 1 127  ? 130.771 91.147  83.264  1.00 99.68  ? 127  PHE A N   1 
ATOM   1020  C  CA  . PHE A 1 127  ? 129.645 90.374  83.762  1.00 97.61  ? 127  PHE A CA  1 
ATOM   1021  C  C   . PHE A 1 127  ? 129.527 89.102  82.937  1.00 117.01 ? 127  PHE A C   1 
ATOM   1022  O  O   . PHE A 1 127  ? 129.376 89.160  81.711  1.00 101.21 ? 127  PHE A O   1 
ATOM   1023  C  CB  . PHE A 1 127  ? 128.365 91.205  83.713  1.00 91.01  ? 127  PHE A CB  1 
ATOM   1024  C  CG  . PHE A 1 127  ? 128.486 92.518  84.434  1.00 85.06  ? 127  PHE A CG  1 
ATOM   1025  C  CD1 . PHE A 1 127  ? 128.500 92.564  85.818  1.00 94.31  ? 127  PHE A CD1 1 
ATOM   1026  C  CD2 . PHE A 1 127  ? 128.604 93.704  83.729  1.00 75.45  ? 127  PHE A CD2 1 
ATOM   1027  C  CE1 . PHE A 1 127  ? 128.623 93.770  86.487  1.00 67.24  ? 127  PHE A CE1 1 
ATOM   1028  C  CE2 . PHE A 1 127  ? 128.725 94.914  84.393  1.00 72.09  ? 127  PHE A CE2 1 
ATOM   1029  C  CZ  . PHE A 1 127  ? 128.734 94.946  85.773  1.00 57.71  ? 127  PHE A CZ  1 
ATOM   1030  N  N   . SER A 1 128  ? 129.591 87.962  83.614  1.00 131.13 ? 128  SER A N   1 
ATOM   1031  C  CA  . SER A 1 128  ? 129.663 86.642  83.013  1.00 134.12 ? 128  SER A CA  1 
ATOM   1032  C  C   . SER A 1 128  ? 128.313 85.953  83.160  1.00 135.27 ? 128  SER A C   1 
ATOM   1033  O  O   . SER A 1 128  ? 127.334 86.550  83.623  1.00 128.91 ? 128  SER A O   1 
ATOM   1034  C  CB  . SER A 1 128  ? 130.792 85.834  83.656  1.00 139.25 ? 128  SER A CB  1 
ATOM   1035  O  OG  . SER A 1 128  ? 130.356 85.227  84.861  1.00 126.29 ? 128  SER A OG  1 
ATOM   1036  N  N   . ALA A 1 129  ? 128.255 84.682  82.771  1.00 130.23 ? 129  ALA A N   1 
ATOM   1037  C  CA  . ALA A 1 129  ? 126.989 83.970  82.662  1.00 136.17 ? 129  ALA A CA  1 
ATOM   1038  C  C   . ALA A 1 129  ? 126.974 82.794  83.629  1.00 111.15 ? 129  ALA A C   1 
ATOM   1039  O  O   . ALA A 1 129  ? 127.682 81.802  83.426  1.00 97.24  ? 129  ALA A O   1 
ATOM   1040  C  CB  . ALA A 1 129  ? 126.760 83.492  81.228  1.00 135.64 ? 129  ALA A CB  1 
ATOM   1041  N  N   . SER A 1 130  ? 126.167 82.918  84.679  1.00 123.15 ? 130  SER A N   1 
ATOM   1042  C  CA  . SER A 1 130  ? 125.829 81.804  85.560  1.00 121.66 ? 130  SER A CA  1 
ATOM   1043  C  C   . SER A 1 130  ? 124.575 81.180  84.967  1.00 105.61 ? 130  SER A C   1 
ATOM   1044  O  O   . SER A 1 130  ? 123.454 81.607  85.244  1.00 93.10  ? 130  SER A O   1 
ATOM   1045  C  CB  . SER A 1 130  ? 125.608 82.278  86.990  1.00 106.73 ? 130  SER A CB  1 
ATOM   1046  O  OG  . SER A 1 130  ? 124.364 82.948  87.114  1.00 100.96 ? 130  SER A OG  1 
ATOM   1047  N  N   . ALA A 1 131  ? 124.766 80.150  84.138  1.00 120.38 ? 131  ALA A N   1 
ATOM   1048  C  CA  . ALA A 1 131  ? 123.671 79.586  83.354  1.00 120.45 ? 131  ALA A CA  1 
ATOM   1049  C  C   . ALA A 1 131  ? 122.526 79.064  84.211  1.00 114.99 ? 131  ALA A C   1 
ATOM   1050  O  O   . ALA A 1 131  ? 121.482 78.696  83.660  1.00 118.34 ? 131  ALA A O   1 
ATOM   1051  C  CB  . ALA A 1 131  ? 124.193 78.462  82.455  1.00 132.43 ? 131  ALA A CB  1 
ATOM   1052  N  N   . ARG A 1 132  ? 122.682 79.034  85.534  1.00 93.96  ? 132  ARG A N   1 
ATOM   1053  C  CA  . ARG A 1 132  ? 121.604 78.559  86.391  1.00 90.37  ? 132  ARG A CA  1 
ATOM   1054  C  C   . ARG A 1 132  ? 120.536 79.627  86.610  1.00 88.64  ? 132  ARG A C   1 
ATOM   1055  O  O   . ARG A 1 132  ? 119.347 79.303  86.691  1.00 96.95  ? 132  ARG A O   1 
ATOM   1056  C  CB  . ARG A 1 132  ? 122.173 78.077  87.722  1.00 98.56  ? 132  ARG A CB  1 
ATOM   1057  C  CG  . ARG A 1 132  ? 121.160 77.340  88.562  1.00 96.77  ? 132  ARG A CG  1 
ATOM   1058  C  CD  . ARG A 1 132  ? 121.840 76.437  89.562  1.00 104.95 ? 132  ARG A CD  1 
ATOM   1059  N  NE  . ARG A 1 132  ? 120.964 76.136  90.687  1.00 96.69  ? 132  ARG A NE  1 
ATOM   1060  C  CZ  . ARG A 1 132  ? 121.258 76.415  91.950  1.00 100.39 ? 132  ARG A CZ  1 
ATOM   1061  N  NH1 . ARG A 1 132  ? 120.401 76.111  92.914  1.00 107.50 ? 132  ARG A NH1 1 
ATOM   1062  N  NH2 . ARG A 1 132  ? 122.408 77.003  92.250  1.00 96.24  ? 132  ARG A NH2 1 
ATOM   1063  N  N   . SER A 1 133  ? 120.926 80.898  86.724  1.00 88.22  ? 133  SER A N   1 
ATOM   1064  C  CA  . SER A 1 133  ? 119.931 81.959  86.860  1.00 86.58  ? 133  SER A CA  1 
ATOM   1065  C  C   . SER A 1 133  ? 119.287 82.344  85.536  1.00 92.64  ? 133  SER A C   1 
ATOM   1066  O  O   . SER A 1 133  ? 118.190 82.910  85.533  1.00 88.74  ? 133  SER A O   1 
ATOM   1067  C  CB  . SER A 1 133  ? 120.561 83.209  87.475  1.00 60.39  ? 133  SER A CB  1 
ATOM   1068  O  OG  . SER A 1 133  ? 120.642 83.128  88.885  1.00 72.73  ? 133  SER A OG  1 
ATOM   1069  N  N   . GLN A 1 134  ? 119.927 82.026  84.410  1.00 97.19  ? 134  GLN A N   1 
ATOM   1070  C  CA  . GLN A 1 134  ? 119.478 82.471  83.100  1.00 74.94  ? 134  GLN A CA  1 
ATOM   1071  C  C   . GLN A 1 134  ? 118.506 81.520  82.419  1.00 81.85  ? 134  GLN A C   1 
ATOM   1072  O  O   . GLN A 1 134  ? 117.971 81.870  81.362  1.00 95.77  ? 134  GLN A O   1 
ATOM   1073  C  CB  . GLN A 1 134  ? 120.694 82.677  82.190  1.00 85.31  ? 134  GLN A CB  1 
ATOM   1074  C  CG  . GLN A 1 134  ? 121.740 83.553  82.822  1.00 99.29  ? 134  GLN A CG  1 
ATOM   1075  C  CD  . GLN A 1 134  ? 122.896 83.837  81.890  1.00 114.46 ? 134  GLN A CD  1 
ATOM   1076  O  OE1 . GLN A 1 134  ? 123.147 83.089  80.944  1.00 115.34 ? 134  GLN A OE1 1 
ATOM   1077  N  NE2 . GLN A 1 134  ? 123.611 84.922  82.153  1.00 99.23  ? 134  GLN A NE2 1 
ATOM   1078  N  N   . CYS A 1 135  ? 118.258 80.342  82.978  1.00 85.44  ? 135  CYS A N   1 
ATOM   1079  C  CA  . CYS A 1 135  ? 117.321 79.427  82.348  1.00 91.99  ? 135  CYS A CA  1 
ATOM   1080  C  C   . CYS A 1 135  ? 115.880 79.780  82.714  1.00 81.27  ? 135  CYS A C   1 
ATOM   1081  O  O   . CYS A 1 135  ? 115.604 80.325  83.793  1.00 88.52  ? 135  CYS A O   1 
ATOM   1082  C  CB  . CYS A 1 135  ? 117.660 77.988  82.736  1.00 98.54  ? 135  CYS A CB  1 
ATOM   1083  S  SG  . CYS A 1 135  ? 117.794 77.665  84.510  1.00 126.96 ? 135  CYS A SG  1 
ATOM   1084  N  N   . GLU A 1 136  ? 114.956 79.466  81.799  1.00 92.49  ? 136  GLU A N   1 
ATOM   1085  C  CA  . GLU A 1 136  ? 113.550 79.822  81.945  1.00 83.54  ? 136  GLU A CA  1 
ATOM   1086  C  C   . GLU A 1 136  ? 112.887 79.166  83.142  1.00 87.39  ? 136  GLU A C   1 
ATOM   1087  O  O   . GLU A 1 136  ? 111.852 79.656  83.614  1.00 92.34  ? 136  GLU A O   1 
ATOM   1088  C  CB  . GLU A 1 136  ? 112.785 79.437  80.675  1.00 91.56  ? 136  GLU A CB  1 
ATOM   1089  C  CG  . GLU A 1 136  ? 113.304 80.100  79.419  1.00 116.99 ? 136  GLU A CG  1 
ATOM   1090  C  CD  . GLU A 1 136  ? 112.581 81.386  79.089  1.00 123.40 ? 136  GLU A CD  1 
ATOM   1091  O  OE1 . GLU A 1 136  ? 111.337 81.414  79.194  1.00 111.50 ? 136  GLU A OE1 1 
ATOM   1092  O  OE2 . GLU A 1 136  ? 113.258 82.371  78.725  1.00 106.36 ? 136  GLU A OE2 1 
ATOM   1093  N  N   . ASP A 1 137  ? 113.445 78.071  83.640  1.00 87.91  ? 137  ASP A N   1 
ATOM   1094  C  CA  . ASP A 1 137  ? 112.793 77.237  84.635  1.00 76.38  ? 137  ASP A CA  1 
ATOM   1095  C  C   . ASP A 1 137  ? 113.312 77.536  86.035  1.00 86.40  ? 137  ASP A C   1 
ATOM   1096  O  O   . ASP A 1 137  ? 112.929 76.860  86.992  1.00 96.07  ? 137  ASP A O   1 
ATOM   1097  C  CB  . ASP A 1 137  ? 113.000 75.761  84.280  1.00 104.90 ? 137  ASP A CB  1 
ATOM   1098  C  CG  . ASP A 1 137  ? 112.137 74.829  85.105  1.00 125.91 ? 137  ASP A CG  1 
ATOM   1099  O  OD1 . ASP A 1 137  ? 112.435 73.617  85.132  1.00 118.39 ? 137  ASP A OD1 1 
ATOM   1100  O  OD2 . ASP A 1 137  ? 111.150 75.303  85.703  1.00 117.78 ? 137  ASP A OD2 1 
ATOM   1101  N  N   . PHE A 1 138  ? 114.173 78.545  86.173  1.00 82.19  ? 138  PHE A N   1 
ATOM   1102  C  CA  . PHE A 1 138  ? 114.792 78.816  87.467  1.00 66.35  ? 138  PHE A CA  1 
ATOM   1103  C  C   . PHE A 1 138  ? 113.756 79.231  88.505  1.00 67.52  ? 138  PHE A C   1 
ATOM   1104  O  O   . PHE A 1 138  ? 113.655 78.622  89.578  1.00 84.95  ? 138  PHE A O   1 
ATOM   1105  C  CB  . PHE A 1 138  ? 115.851 79.906  87.311  1.00 73.32  ? 138  PHE A CB  1 
ATOM   1106  C  CG  . PHE A 1 138  ? 116.563 80.238  88.586  1.00 65.82  ? 138  PHE A CG  1 
ATOM   1107  C  CD1 . PHE A 1 138  ? 117.399 79.312  89.181  1.00 87.69  ? 138  PHE A CD1 1 
ATOM   1108  C  CD2 . PHE A 1 138  ? 116.368 81.458  89.210  1.00 84.66  ? 138  PHE A CD2 1 
ATOM   1109  C  CE1 . PHE A 1 138  ? 118.052 79.605  90.362  1.00 80.99  ? 138  PHE A CE1 1 
ATOM   1110  C  CE2 . PHE A 1 138  ? 117.016 81.756  90.395  1.00 74.69  ? 138  PHE A CE2 1 
ATOM   1111  C  CZ  . PHE A 1 138  ? 117.858 80.828  90.971  1.00 54.45  ? 138  PHE A CZ  1 
ATOM   1112  N  N   . SER A 1 139  ? 112.956 80.247  88.189  1.00 72.41  ? 139  SER A N   1 
ATOM   1113  C  CA  . SER A 1 139  ? 112.039 80.840  89.157  1.00 63.56  ? 139  SER A CA  1 
ATOM   1114  C  C   . SER A 1 139  ? 110.799 79.980  89.408  1.00 67.92  ? 139  SER A C   1 
ATOM   1115  O  O   . SER A 1 139  ? 110.402 79.821  90.569  1.00 68.34  ? 139  SER A O   1 
ATOM   1116  C  CB  . SER A 1 139  ? 111.634 82.250  88.714  1.00 66.82  ? 139  SER A CB  1 
ATOM   1117  O  OG  . SER A 1 139  ? 111.098 82.992  89.796  1.00 71.57  ? 139  SER A OG  1 
ATOM   1118  N  N   . PRO A 1 140  ? 110.154 79.413  88.377  1.00 71.39  ? 140  PRO A N   1 
ATOM   1119  C  CA  . PRO A 1 140  ? 109.028 78.502  88.655  1.00 68.25  ? 140  PRO A CA  1 
ATOM   1120  C  C   . PRO A 1 140  ? 109.412 77.313  89.513  1.00 71.53  ? 140  PRO A C   1 
ATOM   1121  O  O   . PRO A 1 140  ? 108.595 76.838  90.312  1.00 82.80  ? 140  PRO A O   1 
ATOM   1122  C  CB  . PRO A 1 140  ? 108.593 78.047  87.256  1.00 76.66  ? 140  PRO A CB  1 
ATOM   1123  C  CG  . PRO A 1 140  ? 108.982 79.149  86.361  1.00 80.81  ? 140  PRO A CG  1 
ATOM   1124  C  CD  . PRO A 1 140  ? 110.236 79.741  86.938  1.00 76.95  ? 140  PRO A CD  1 
ATOM   1125  N  N   . LYS A 1 141  ? 110.637 76.819  89.371  1.00 75.51  ? 141  LYS A N   1 
ATOM   1126  C  CA  . LYS A 1 141  ? 111.045 75.572  89.999  1.00 78.99  ? 141  LYS A CA  1 
ATOM   1127  C  C   . LYS A 1 141  ? 111.717 75.759  91.355  1.00 80.51  ? 141  LYS A C   1 
ATOM   1128  O  O   . LYS A 1 141  ? 111.598 74.878  92.213  1.00 95.63  ? 141  LYS A O   1 
ATOM   1129  C  CB  . LYS A 1 141  ? 111.966 74.807  89.043  1.00 91.75  ? 141  LYS A CB  1 
ATOM   1130  C  CG  . LYS A 1 141  ? 112.360 73.413  89.477  1.00 117.88 ? 141  LYS A CG  1 
ATOM   1131  C  CD  . LYS A 1 141  ? 113.211 72.756  88.399  1.00 121.18 ? 141  LYS A CD  1 
ATOM   1132  C  CE  . LYS A 1 141  ? 114.614 73.335  88.370  1.00 121.24 ? 141  LYS A CE  1 
ATOM   1133  N  NZ  . LYS A 1 141  ? 115.392 72.946  89.576  1.00 124.02 ? 141  LYS A NZ  1 
ATOM   1134  N  N   . GLU A 1 142  ? 112.404 76.880  91.590  1.00 69.33  ? 142  GLU A N   1 
ATOM   1135  C  CA  . GLU A 1 142  ? 113.184 77.031  92.810  1.00 64.55  ? 142  GLU A CA  1 
ATOM   1136  C  C   . GLU A 1 142  ? 112.649 78.069  93.789  1.00 72.81  ? 142  GLU A C   1 
ATOM   1137  O  O   . GLU A 1 142  ? 113.146 78.131  94.920  1.00 75.96  ? 142  GLU A O   1 
ATOM   1138  C  CB  . GLU A 1 142  ? 114.640 77.356  92.457  1.00 56.64  ? 142  GLU A CB  1 
ATOM   1139  C  CG  . GLU A 1 142  ? 115.208 76.377  91.452  1.00 75.30  ? 142  GLU A CG  1 
ATOM   1140  C  CD  . GLU A 1 142  ? 116.713 76.356  91.446  1.00 89.91  ? 142  GLU A CD  1 
ATOM   1141  O  OE1 . GLU A 1 142  ? 117.314 76.875  92.408  1.00 87.57  ? 142  GLU A OE1 1 
ATOM   1142  O  OE2 . GLU A 1 142  ? 117.295 75.813  90.484  1.00 96.56  ? 142  GLU A OE2 1 
ATOM   1143  N  N   . ASN A 1 143  ? 111.671 78.887  93.402  1.00 72.42  ? 143  ASN A N   1 
ATOM   1144  C  CA  . ASN A 1 143  ? 111.101 79.860  94.326  1.00 53.89  ? 143  ASN A CA  1 
ATOM   1145  C  C   . ASN A 1 143  ? 109.792 79.313  94.871  1.00 69.12  ? 143  ASN A C   1 
ATOM   1146  O  O   . ASN A 1 143  ? 108.870 79.051  94.084  1.00 84.87  ? 143  ASN A O   1 
ATOM   1147  C  CB  . ASN A 1 143  ? 110.866 81.193  93.622  1.00 54.86  ? 143  ASN A CB  1 
ATOM   1148  C  CG  . ASN A 1 143  ? 110.651 82.341  94.591  1.00 46.74  ? 143  ASN A CG  1 
ATOM   1149  O  OD1 . ASN A 1 143  ? 110.027 82.179  95.639  1.00 56.92  ? 143  ASN A OD1 1 
ATOM   1150  N  ND2 . ASN A 1 143  ? 111.166 83.513  94.240  1.00 52.43  ? 143  ASN A ND2 1 
ATOM   1151  N  N   . PRO A 1 144  ? 109.656 79.119  96.186  1.00 54.08  ? 144  PRO A N   1 
ATOM   1152  C  CA  . PRO A 1 144  ? 108.442 78.485  96.723  1.00 50.43  ? 144  PRO A CA  1 
ATOM   1153  C  C   . PRO A 1 144  ? 107.202 79.370  96.761  1.00 53.27  ? 144  PRO A C   1 
ATOM   1154  O  O   . PRO A 1 144  ? 106.137 78.873  97.146  1.00 64.26  ? 144  PRO A O   1 
ATOM   1155  C  CB  . PRO A 1 144  ? 108.861 78.092  98.152  1.00 47.63  ? 144  PRO A CB  1 
ATOM   1156  C  CG  . PRO A 1 144  ? 110.046 78.947  98.470  1.00 53.41  ? 144  PRO A CG  1 
ATOM   1157  C  CD  . PRO A 1 144  ? 110.745 79.185  97.176  1.00 58.71  ? 144  PRO A CD  1 
ATOM   1158  N  N   . TYR A 1 145  ? 107.280 80.648  96.389  1.00 55.03  ? 145  TYR A N   1 
ATOM   1159  C  CA  . TYR A 1 145  ? 106.141 81.557  96.501  1.00 46.55  ? 145  TYR A CA  1 
ATOM   1160  C  C   . TYR A 1 145  ? 105.621 82.052  95.154  1.00 63.31  ? 145  TYR A C   1 
ATOM   1161  O  O   . TYR A 1 145  ? 104.790 82.963  95.120  1.00 74.62  ? 145  TYR A O   1 
ATOM   1162  C  CB  . TYR A 1 145  ? 106.510 82.765  97.362  1.00 50.92  ? 145  TYR A CB  1 
ATOM   1163  C  CG  . TYR A 1 145  ? 106.921 82.411  98.768  1.00 68.77  ? 145  TYR A CG  1 
ATOM   1164  C  CD1 . TYR A 1 145  ? 105.977 82.189  99.759  1.00 65.58  ? 145  TYR A CD1 1 
ATOM   1165  C  CD2 . TYR A 1 145  ? 108.262 82.321  99.110  1.00 77.08  ? 145  TYR A CD2 1 
ATOM   1166  C  CE1 . TYR A 1 145  ? 106.361 81.870  101.051 1.00 59.43  ? 145  TYR A CE1 1 
ATOM   1167  C  CE2 . TYR A 1 145  ? 108.655 82.004  100.394 1.00 64.94  ? 145  TYR A CE2 1 
ATOM   1168  C  CZ  . TYR A 1 145  ? 107.701 81.780  101.362 1.00 66.47  ? 145  TYR A CZ  1 
ATOM   1169  O  OH  . TYR A 1 145  ? 108.093 81.459  102.642 1.00 71.51  ? 145  TYR A OH  1 
ATOM   1170  N  N   . TYR A 1 146  ? 106.090 81.477  94.051  1.00 62.77  ? 146  TYR A N   1 
ATOM   1171  C  CA  . TYR A 1 146  ? 105.788 81.999  92.720  1.00 53.22  ? 146  TYR A CA  1 
ATOM   1172  C  C   . TYR A 1 146  ? 104.300 81.868  92.367  1.00 66.08  ? 146  TYR A C   1 
ATOM   1173  O  O   . TYR A 1 146  ? 103.591 82.873  92.162  1.00 82.19  ? 146  TYR A O   1 
ATOM   1174  C  CB  . TYR A 1 146  ? 106.687 81.261  91.725  1.00 53.36  ? 146  TYR A CB  1 
ATOM   1175  C  CG  . TYR A 1 146  ? 106.570 81.679  90.288  1.00 59.72  ? 146  TYR A CG  1 
ATOM   1176  C  CD1 . TYR A 1 146  ? 107.060 82.906  89.871  1.00 68.33  ? 146  TYR A CD1 1 
ATOM   1177  C  CD2 . TYR A 1 146  ? 106.021 80.834  89.339  1.00 71.54  ? 146  TYR A CD2 1 
ATOM   1178  C  CE1 . TYR A 1 146  ? 106.974 83.298  88.553  1.00 53.30  ? 146  TYR A CE1 1 
ATOM   1179  C  CE2 . TYR A 1 146  ? 105.931 81.217  88.014  1.00 57.62  ? 146  TYR A CE2 1 
ATOM   1180  C  CZ  . TYR A 1 146  ? 106.410 82.451  87.627  1.00 46.18  ? 146  TYR A CZ  1 
ATOM   1181  O  OH  . TYR A 1 146  ? 106.327 82.842  86.310  1.00 56.73  ? 146  TYR A OH  1 
ATOM   1182  N  N   . TRP A 1 147  ? 103.796 80.631  92.349  1.00 48.21  ? 147  TRP A N   1 
ATOM   1183  C  CA  . TRP A 1 147  ? 102.416 80.375  91.932  1.00 48.14  ? 147  TRP A CA  1 
ATOM   1184  C  C   . TRP A 1 147  ? 101.404 80.990  92.895  1.00 56.10  ? 147  TRP A C   1 
ATOM   1185  O  O   . TRP A 1 147  ? 100.368 81.512  92.454  1.00 78.10  ? 147  TRP A O   1 
ATOM   1186  C  CB  . TRP A 1 147  ? 102.179 78.871  91.786  1.00 71.81  ? 147  TRP A CB  1 
ATOM   1187  C  CG  . TRP A 1 147  ? 103.057 78.219  90.766  1.00 61.89  ? 147  TRP A CG  1 
ATOM   1188  C  CD1 . TRP A 1 147  ? 104.085 77.352  90.996  1.00 75.18  ? 147  TRP A CD1 1 
ATOM   1189  C  CD2 . TRP A 1 147  ? 102.976 78.380  89.345  1.00 61.63  ? 147  TRP A CD2 1 
ATOM   1190  N  NE1 . TRP A 1 147  ? 104.653 76.967  89.803  1.00 80.13  ? 147  TRP A NE1 1 
ATOM   1191  C  CE2 . TRP A 1 147  ? 103.989 77.585  88.776  1.00 73.64  ? 147  TRP A CE2 1 
ATOM   1192  C  CE3 . TRP A 1 147  ? 102.146 79.122  88.500  1.00 72.79  ? 147  TRP A CE3 1 
ATOM   1193  C  CZ2 . TRP A 1 147  ? 104.193 77.511  87.397  1.00 80.68  ? 147  TRP A CZ2 1 
ATOM   1194  C  CZ3 . TRP A 1 147  ? 102.350 79.048  87.134  1.00 67.76  ? 147  TRP A CZ3 1 
ATOM   1195  C  CH2 . TRP A 1 147  ? 103.364 78.249  86.596  1.00 78.44  ? 147  TRP A CH2 1 
ATOM   1196  N  N   . GLY A 1 148  ? 101.682 80.943  94.204  1.00 48.89  ? 148  GLY A N   1 
ATOM   1197  C  CA  . GLY A 1 148  ? 100.776 81.557  95.157  1.00 53.52  ? 148  GLY A CA  1 
ATOM   1198  C  C   . GLY A 1 148  ? 100.655 83.048  94.931  1.00 66.44  ? 148  GLY A C   1 
ATOM   1199  O  O   . GLY A 1 148  ? 99.568  83.620  95.030  1.00 74.99  ? 148  GLY A O   1 
ATOM   1200  N  N   . MET A 1 149  ? 101.782 83.688  94.608  1.00 51.75  ? 149  MET A N   1 
ATOM   1201  C  CA  . MET A 1 149  ? 101.809 85.112  94.330  1.00 37.94  ? 149  MET A CA  1 
ATOM   1202  C  C   . MET A 1 149  ? 100.931 85.450  93.137  1.00 51.83  ? 149  MET A C   1 
ATOM   1203  O  O   . MET A 1 149  ? 100.112 86.377  93.202  1.00 62.37  ? 149  MET A O   1 
ATOM   1204  C  CB  . MET A 1 149  ? 103.275 85.527  94.126  1.00 54.32  ? 149  MET A CB  1 
ATOM   1205  C  CG  . MET A 1 149  ? 103.535 86.958  93.879  1.00 55.95  ? 149  MET A CG  1 
ATOM   1206  S  SD  . MET A 1 149  ? 103.349 87.174  92.078  1.00 71.11  ? 149  MET A SD  1 
ATOM   1207  C  CE  . MET A 1 149  ? 104.772 86.221  91.490  1.00 56.90  ? 149  MET A CE  1 
ATOM   1208  N  N   . LEU A 1 150  ? 101.034 84.667  92.051  1.00 62.75  ? 150  LEU A N   1 
ATOM   1209  C  CA  . LEU A 1 150  ? 100.184 84.937  90.888  1.00 53.01  ? 150  LEU A CA  1 
ATOM   1210  C  C   . LEU A 1 150  ? 98.697  84.737  91.214  1.00 55.85  ? 150  LEU A C   1 
ATOM   1211  O  O   . LEU A 1 150  ? 97.842  85.578  90.863  1.00 75.85  ? 150  LEU A O   1 
ATOM   1212  C  CB  . LEU A 1 150  ? 100.592 84.026  89.727  1.00 52.39  ? 150  LEU A CB  1 
ATOM   1213  C  CG  . LEU A 1 150  ? 101.954 84.300  89.104  1.00 43.86  ? 150  LEU A CG  1 
ATOM   1214  C  CD1 . LEU A 1 150  ? 102.296 83.222  88.093  1.00 54.99  ? 150  LEU A CD1 1 
ATOM   1215  C  CD2 . LEU A 1 150  ? 101.964 85.679  88.457  1.00 41.50  ? 150  LEU A CD2 1 
ATOM   1216  N  N   . LEU A 1 151  ? 98.370  83.642  91.911  1.00 50.45  ? 151  LEU A N   1 
ATOM   1217  C  CA  . LEU A 1 151  ? 96.973  83.369  92.241  1.00 43.43  ? 151  LEU A CA  1 
ATOM   1218  C  C   . LEU A 1 151  ? 96.375  84.471  93.104  1.00 47.53  ? 151  LEU A C   1 
ATOM   1219  O  O   . LEU A 1 151  ? 95.233  84.898  92.881  1.00 67.77  ? 151  LEU A O   1 
ATOM   1220  C  CB  . LEU A 1 151  ? 96.855  82.013  92.935  1.00 49.78  ? 151  LEU A CB  1 
ATOM   1221  C  CG  . LEU A 1 151  ? 95.474  81.735  93.520  1.00 43.78  ? 151  LEU A CG  1 
ATOM   1222  C  CD1 . LEU A 1 151  ? 94.498  81.368  92.417  1.00 47.88  ? 151  LEU A CD1 1 
ATOM   1223  C  CD2 . LEU A 1 151  ? 95.549  80.630  94.562  1.00 50.59  ? 151  LEU A CD2 1 
ATOM   1224  N  N   . LEU A 1 152  ? 97.138  84.969  94.081  1.00 59.61  ? 152  LEU A N   1 
ATOM   1225  C  CA  . LEU A 1 152  ? 96.593  86.008  94.944  1.00 49.73  ? 152  LEU A CA  1 
ATOM   1226  C  C   . LEU A 1 152  ? 96.517  87.367  94.266  1.00 54.20  ? 152  LEU A C   1 
ATOM   1227  O  O   . LEU A 1 152  ? 95.642  88.161  94.614  1.00 65.43  ? 152  LEU A O   1 
ATOM   1228  C  CB  . LEU A 1 152  ? 97.393  86.105  96.237  1.00 45.53  ? 152  LEU A CB  1 
ATOM   1229  C  CG  . LEU A 1 152  ? 96.933  85.019  97.199  1.00 55.37  ? 152  LEU A CG  1 
ATOM   1230  C  CD1 . LEU A 1 152  ? 97.913  84.867  98.323  1.00 71.76  ? 152  LEU A CD1 1 
ATOM   1231  C  CD2 . LEU A 1 152  ? 95.548  85.378  97.724  1.00 62.28  ? 152  LEU A CD2 1 
ATOM   1232  N  N   . VAL A 1 153  ? 97.371  87.646  93.279  1.00 57.60  ? 153  VAL A N   1 
ATOM   1233  C  CA  . VAL A 1 153  ? 97.175  88.859  92.484  1.00 54.79  ? 153  VAL A CA  1 
ATOM   1234  C  C   . VAL A 1 153  ? 95.820  88.825  91.776  1.00 52.52  ? 153  VAL A C   1 
ATOM   1235  O  O   . VAL A 1 153  ? 95.003  89.764  91.880  1.00 74.95  ? 153  VAL A O   1 
ATOM   1236  C  CB  . VAL A 1 153  ? 98.331  89.031  91.481  1.00 48.95  ? 153  VAL A CB  1 
ATOM   1237  C  CG1 . VAL A 1 153  ? 97.937  89.993  90.369  1.00 51.96  ? 153  VAL A CG1 1 
ATOM   1238  C  CG2 . VAL A 1 153  ? 99.587  89.517  92.194  1.00 56.25  ? 153  VAL A CG2 1 
ATOM   1239  N  N   . HIS A 1 154  ? 95.528  87.699  91.117  1.00 47.84  ? 154  HIS A N   1 
ATOM   1240  C  CA  . HIS A 1 154  ? 94.228  87.535  90.461  1.00 48.03  ? 154  HIS A CA  1 
ATOM   1241  C  C   . HIS A 1 154  ? 93.064  87.677  91.452  1.00 56.61  ? 154  HIS A C   1 
ATOM   1242  O  O   . HIS A 1 154  ? 92.131  88.484  91.248  1.00 62.44  ? 154  HIS A O   1 
ATOM   1243  C  CB  . HIS A 1 154  ? 94.219  86.175  89.753  1.00 52.89  ? 154  HIS A CB  1 
ATOM   1244  C  CG  . HIS A 1 154  ? 92.856  85.652  89.423  1.00 45.21  ? 154  HIS A CG  1 
ATOM   1245  N  ND1 . HIS A 1 154  ? 92.066  86.199  88.435  1.00 54.89  ? 154  HIS A ND1 1 
ATOM   1246  C  CD2 . HIS A 1 154  ? 92.161  84.605  89.927  1.00 47.61  ? 154  HIS A CD2 1 
ATOM   1247  C  CE1 . HIS A 1 154  ? 90.933  85.524  88.359  1.00 65.29  ? 154  HIS A CE1 1 
ATOM   1248  N  NE2 . HIS A 1 154  ? 90.965  84.553  89.253  1.00 51.17  ? 154  HIS A NE2 1 
ATOM   1249  N  N   . LEU A 1 155  ? 93.117  86.923  92.553  1.00 55.56  ? 155  LEU A N   1 
ATOM   1250  C  CA  . LEU A 1 155  ? 92.015  86.948  93.509  1.00 40.00  ? 155  LEU A CA  1 
ATOM   1251  C  C   . LEU A 1 155  ? 91.846  88.312  94.168  1.00 53.96  ? 155  LEU A C   1 
ATOM   1252  O  O   . LEU A 1 155  ? 90.715  88.715  94.465  1.00 68.59  ? 155  LEU A O   1 
ATOM   1253  C  CB  . LEU A 1 155  ? 92.221  85.872  94.573  1.00 41.63  ? 155  LEU A CB  1 
ATOM   1254  C  CG  . LEU A 1 155  ? 92.003  84.436  94.106  1.00 50.87  ? 155  LEU A CG  1 
ATOM   1255  C  CD1 . LEU A 1 155  ? 92.112  83.488  95.286  1.00 57.16  ? 155  LEU A CD1 1 
ATOM   1256  C  CD2 . LEU A 1 155  ? 90.644  84.311  93.427  1.00 62.09  ? 155  LEU A CD2 1 
ATOM   1257  N  N   . SER A 1 156  ? 92.942  89.036  94.416  1.00 53.26  ? 156  SER A N   1 
ATOM   1258  C  CA  . SER A 1 156  ? 92.819  90.351  95.031  1.00 55.77  ? 156  SER A CA  1 
ATOM   1259  C  C   . SER A 1 156  ? 92.149  91.343  94.100  1.00 61.28  ? 156  SER A C   1 
ATOM   1260  O  O   . SER A 1 156  ? 91.381  92.200  94.562  1.00 73.43  ? 156  SER A O   1 
ATOM   1261  C  CB  . SER A 1 156  ? 94.195  90.880  95.428  1.00 59.23  ? 156  SER A CB  1 
ATOM   1262  O  OG  . SER A 1 156  ? 94.863  91.417  94.298  1.00 74.83  ? 156  SER A OG  1 
ATOM   1263  N  N   . GLN A 1 157  ? 92.396  91.238  92.790  1.00 57.43  ? 157  GLN A N   1 
ATOM   1264  C  CA  . GLN A 1 157  ? 91.645  92.113  91.892  1.00 60.59  ? 157  GLN A CA  1 
ATOM   1265  C  C   . GLN A 1 157  ? 90.151  91.807  91.963  1.00 69.27  ? 157  GLN A C   1 
ATOM   1266  O  O   . GLN A 1 157  ? 89.314  92.728  92.031  1.00 72.62  ? 157  GLN A O   1 
ATOM   1267  C  CB  . GLN A 1 157  ? 92.169  91.997  90.462  1.00 63.61  ? 157  GLN A CB  1 
ATOM   1268  C  CG  . GLN A 1 157  ? 93.260  93.016  90.182  1.00 71.25  ? 157  GLN A CG  1 
ATOM   1269  C  CD  . GLN A 1 157  ? 92.708  94.413  89.975  1.00 69.42  ? 157  GLN A CD  1 
ATOM   1270  O  OE1 . GLN A 1 157  ? 92.995  95.324  90.752  1.00 70.65  ? 157  GLN A OE1 1 
ATOM   1271  N  NE2 . GLN A 1 157  ? 91.913  94.590  88.929  1.00 78.37  ? 157  GLN A NE2 1 
ATOM   1272  N  N   . LEU A 1 158  ? 89.798  90.516  91.989  1.00 72.57  ? 158  LEU A N   1 
ATOM   1273  C  CA  . LEU A 1 158  ? 88.384  90.160  92.158  1.00 53.52  ? 158  LEU A CA  1 
ATOM   1274  C  C   . LEU A 1 158  ? 87.793  90.733  93.449  1.00 52.18  ? 158  LEU A C   1 
ATOM   1275  O  O   . LEU A 1 158  ? 86.671  91.266  93.454  1.00 56.49  ? 158  LEU A O   1 
ATOM   1276  C  CB  . LEU A 1 158  ? 88.211  88.645  92.120  1.00 48.37  ? 158  LEU A CB  1 
ATOM   1277  C  CG  . LEU A 1 158  ? 88.378  88.045  90.728  1.00 59.66  ? 158  LEU A CG  1 
ATOM   1278  C  CD1 . LEU A 1 158  ? 87.866  86.617  90.714  1.00 65.82  ? 158  LEU A CD1 1 
ATOM   1279  C  CD2 . LEU A 1 158  ? 87.638  88.902  89.707  1.00 69.15  ? 158  LEU A CD2 1 
ATOM   1280  N  N   . ALA A 1 159  ? 88.534  90.628  94.556  1.00 53.53  ? 159  ALA A N   1 
ATOM   1281  C  CA  . ALA A 1 159  ? 88.025  91.100  95.843  1.00 52.82  ? 159  ALA A CA  1 
ATOM   1282  C  C   . ALA A 1 159  ? 87.813  92.608  95.839  1.00 59.72  ? 159  ALA A C   1 
ATOM   1283  O  O   . ALA A 1 159  ? 86.828  93.107  96.403  1.00 75.97  ? 159  ALA A O   1 
ATOM   1284  C  CB  . ALA A 1 159  ? 88.984  90.696  96.962  1.00 63.05  ? 159  ALA A CB  1 
ATOM   1285  N  N   . ARG A 1 160  ? 88.735  93.352  95.224  1.00 69.11  ? 160  ARG A N   1 
ATOM   1286  C  CA  . ARG A 1 160  ? 88.552  94.796  95.118  1.00 52.80  ? 160  ARG A CA  1 
ATOM   1287  C  C   . ARG A 1 160  ? 87.283  95.123  94.348  1.00 54.72  ? 160  ARG A C   1 
ATOM   1288  O  O   . ARG A 1 160  ? 86.510  96.007  94.750  1.00 66.83  ? 160  ARG A O   1 
ATOM   1289  C  CB  . ARG A 1 160  ? 89.764  95.440  94.458  1.00 47.84  ? 160  ARG A CB  1 
ATOM   1290  C  CG  . ARG A 1 160  ? 90.996  95.453  95.325  1.00 50.72  ? 160  ARG A CG  1 
ATOM   1291  C  CD  . ARG A 1 160  ? 92.093  96.173  94.595  1.00 59.77  ? 160  ARG A CD  1 
ATOM   1292  N  NE  . ARG A 1 160  ? 91.768  97.587  94.451  1.00 58.72  ? 160  ARG A NE  1 
ATOM   1293  C  CZ  . ARG A 1 160  ? 92.205  98.347  93.455  1.00 59.96  ? 160  ARG A CZ  1 
ATOM   1294  N  NH1 . ARG A 1 160  ? 92.981  97.823  92.517  1.00 70.89  ? 160  ARG A NH1 1 
ATOM   1295  N  NH2 . ARG A 1 160  ? 91.864  99.625  93.391  1.00 75.78  ? 160  ARG A NH2 1 
ATOM   1296  N  N   . ARG A 1 161  ? 87.034  94.400  93.251  1.00 66.18  ? 161  ARG A N   1 
ATOM   1297  C  CA  . ARG A 1 161  ? 85.804  94.648  92.503  1.00 58.75  ? 161  ARG A CA  1 
ATOM   1298  C  C   . ARG A 1 161  ? 84.571  94.403  93.360  1.00 54.39  ? 161  ARG A C   1 
ATOM   1299  O  O   . ARG A 1 161  ? 83.633  95.210  93.355  1.00 74.07  ? 161  ARG A O   1 
ATOM   1300  C  CB  . ARG A 1 161  ? 85.721  93.753  91.271  1.00 78.46  ? 161  ARG A CB  1 
ATOM   1301  C  CG  . ARG A 1 161  ? 84.398  93.935  90.536  1.00 56.86  ? 161  ARG A CG  1 
ATOM   1302  C  CD  . ARG A 1 161  ? 84.307  93.099  89.284  1.00 73.83  ? 161  ARG A CD  1 
ATOM   1303  N  NE  . ARG A 1 161  ? 85.442  93.306  88.400  1.00 79.63  ? 161  ARG A NE  1 
ATOM   1304  C  CZ  . ARG A 1 161  ? 85.421  94.137  87.365  1.00 87.60  ? 161  ARG A CZ  1 
ATOM   1305  N  NH1 . ARG A 1 161  ? 84.326  94.835  87.096  1.00 83.20  ? 161  ARG A NH1 1 
ATOM   1306  N  NH2 . ARG A 1 161  ? 86.495  94.272  86.600  1.00 81.30  ? 161  ARG A NH2 1 
ATOM   1307  N  N   . ILE A 1 162  ? 84.557  93.303  94.112  1.00 71.81  ? 162  ILE A N   1 
ATOM   1308  C  CA  . ILE A 1 162  ? 83.354  92.977  94.876  1.00 59.45  ? 162  ILE A CA  1 
ATOM   1309  C  C   . ILE A 1 162  ? 83.122  93.981  96.000  1.00 54.95  ? 162  ILE A C   1 
ATOM   1310  O  O   . ILE A 1 162  ? 81.982  94.387  96.254  1.00 63.61  ? 162  ILE A O   1 
ATOM   1311  C  CB  . ILE A 1 162  ? 83.420  91.534  95.403  1.00 56.77  ? 162  ILE A CB  1 
ATOM   1312  C  CG1 . ILE A 1 162  ? 83.475  90.567  94.225  1.00 68.76  ? 162  ILE A CG1 1 
ATOM   1313  C  CG2 . ILE A 1 162  ? 82.206  91.220  96.264  1.00 60.23  ? 162  ILE A CG2 1 
ATOM   1314  C  CD1 . ILE A 1 162  ? 82.265  90.656  93.321  1.00 71.02  ? 162  ILE A CD1 1 
ATOM   1315  N  N   . LYS A 1 163  ? 84.184  94.404  96.689  1.00 67.52  ? 163  LYS A N   1 
ATOM   1316  C  CA  . LYS A 1 163  ? 83.996  95.383  97.759  1.00 59.50  ? 163  LYS A CA  1 
ATOM   1317  C  C   . LYS A 1 163  ? 83.578  96.750  97.222  1.00 74.88  ? 163  LYS A C   1 
ATOM   1318  O  O   . LYS A 1 163  ? 82.769  97.444  97.849  1.00 86.79  ? 163  LYS A O   1 
ATOM   1319  C  CB  . LYS A 1 163  ? 85.256  95.517  98.609  1.00 65.67  ? 163  LYS A CB  1 
ATOM   1320  C  CG  . LYS A 1 163  ? 85.122  96.621  99.646  1.00 72.90  ? 163  LYS A CG  1 
ATOM   1321  C  CD  . LYS A 1 163  ? 86.100  96.491  100.787 1.00 83.59  ? 163  LYS A CD  1 
ATOM   1322  C  CE  . LYS A 1 163  ? 85.643  97.344  101.958 1.00 63.11  ? 163  LYS A CE  1 
ATOM   1323  N  NZ  . LYS A 1 163  ? 86.271  98.690  101.926 1.00 82.54  ? 163  LYS A NZ  1 
ATOM   1324  N  N   . GLY A 1 164  ? 84.095  97.142  96.054  1.00 81.94  ? 164  GLY A N   1 
ATOM   1325  C  CA  . GLY A 1 164  ? 83.761  98.455  95.515  1.00 77.15  ? 164  GLY A CA  1 
ATOM   1326  C  C   . GLY A 1 164  ? 82.276  98.678  95.298  1.00 88.58  ? 164  GLY A C   1 
ATOM   1327  O  O   . GLY A 1 164  ? 81.754  99.757  95.590  1.00 110.82 ? 164  GLY A O   1 
ATOM   1328  N  N   . GLN A 1 165  ? 81.573  97.670  94.789  1.00 88.48  ? 165  GLN A N   1 
ATOM   1329  C  CA  . GLN A 1 165  ? 80.128  97.780  94.628  1.00 93.47  ? 165  GLN A CA  1 
ATOM   1330  C  C   . GLN A 1 165  ? 79.430  97.914  95.974  1.00 120.14 ? 165  GLN A C   1 
ATOM   1331  O  O   . GLN A 1 165  ? 79.809  97.272  96.958  1.00 125.92 ? 165  GLN A O   1 
ATOM   1332  C  CB  . GLN A 1 165  ? 79.585  96.566  93.882  1.00 88.60  ? 165  GLN A CB  1 
ATOM   1333  C  CG  . GLN A 1 165  ? 80.060  96.462  92.454  1.00 102.50 ? 165  GLN A CG  1 
ATOM   1334  C  CD  . GLN A 1 165  ? 79.884  95.069  91.911  1.00 115.20 ? 165  GLN A CD  1 
ATOM   1335  O  OE1 . GLN A 1 165  ? 79.625  94.134  92.664  1.00 99.33  ? 165  GLN A OE1 1 
ATOM   1336  N  NE2 . GLN A 1 165  ? 80.031  94.916  90.602  1.00 121.01 ? 165  GLN A NE2 1 
ATOM   1337  N  N   . ARG A 1 166  ? 78.399  98.756  96.010  1.00 141.34 ? 166  ARG A N   1 
ATOM   1338  C  CA  . ARG A 1 166  ? 77.782  99.186  97.259  1.00 158.90 ? 166  ARG A CA  1 
ATOM   1339  C  C   . ARG A 1 166  ? 76.896  98.123  97.896  1.00 170.01 ? 166  ARG A C   1 
ATOM   1340  O  O   . ARG A 1 166  ? 76.164  98.439  98.841  1.00 170.25 ? 166  ARG A O   1 
ATOM   1341  C  CB  . ARG A 1 166  ? 76.973  100.466 97.027  1.00 157.61 ? 166  ARG A CB  1 
ATOM   1342  C  CG  . ARG A 1 166  ? 77.800  101.613 96.470  1.00 150.39 ? 166  ARG A CG  1 
ATOM   1343  C  CD  . ARG A 1 166  ? 78.340  102.488 97.593  1.00 157.30 ? 166  ARG A CD  1 
ATOM   1344  N  NE  . ARG A 1 166  ? 79.238  101.748 98.475  1.00 152.37 ? 166  ARG A NE  1 
ATOM   1345  C  CZ  . ARG A 1 166  ? 80.563  101.824 98.435  1.00 152.33 ? 166  ARG A CZ  1 
ATOM   1346  N  NH1 . ARG A 1 166  ? 81.157  102.614 97.551  1.00 153.78 ? 166  ARG A NH1 1 
ATOM   1347  N  NH2 . ARG A 1 166  ? 81.297  101.109 99.277  1.00 145.22 ? 166  ARG A NH2 1 
ATOM   1348  N  N   . GLY A 1 167  ? 76.936  96.885  97.414  1.00 162.35 ? 167  GLY A N   1 
ATOM   1349  C  CA  . GLY A 1 167  ? 76.120  95.839  97.996  1.00 164.93 ? 167  GLY A CA  1 
ATOM   1350  C  C   . GLY A 1 167  ? 74.893  95.497  97.178  1.00 171.62 ? 167  GLY A C   1 
ATOM   1351  O  O   . GLY A 1 167  ? 73.896  96.223  97.210  1.00 163.98 ? 167  GLY A O   1 
ATOM   1352  N  N   . SER A 1 168  ? 74.956  94.389  96.441  1.00 167.37 ? 168  SER A N   1 
ATOM   1353  C  CA  . SER A 1 168  ? 73.872  93.978  95.563  1.00 161.58 ? 168  SER A CA  1 
ATOM   1354  C  C   . SER A 1 168  ? 73.260  92.635  95.932  1.00 157.65 ? 168  SER A C   1 
ATOM   1355  O  O   . SER A 1 168  ? 72.256  92.251  95.322  1.00 155.87 ? 168  SER A O   1 
ATOM   1356  C  CB  . SER A 1 168  ? 74.344  93.925  94.102  1.00 156.49 ? 168  SER A CB  1 
ATOM   1357  O  OG  . SER A 1 168  ? 73.344  93.359  93.270  1.00 147.43 ? 168  SER A OG  1 
ATOM   1358  N  N   . LEU A 1 169  ? 73.846  91.902  96.883  1.00 151.31 ? 169  LEU A N   1 
ATOM   1359  C  CA  . LEU A 1 169  ? 73.368  90.618  97.393  1.00 145.54 ? 169  LEU A CA  1 
ATOM   1360  C  C   . LEU A 1 169  ? 73.561  89.492  96.387  1.00 154.84 ? 169  LEU A C   1 
ATOM   1361  O  O   . LEU A 1 169  ? 73.301  88.328  96.717  1.00 147.27 ? 169  LEU A O   1 
ATOM   1362  C  CB  . LEU A 1 169  ? 71.895  90.659  97.828  1.00 147.48 ? 169  LEU A CB  1 
ATOM   1363  C  CG  . LEU A 1 169  ? 71.500  89.673  98.927  1.00 126.05 ? 169  LEU A CG  1 
ATOM   1364  C  CD1 . LEU A 1 169  ? 72.252  89.979  100.213 1.00 120.25 ? 169  LEU A CD1 1 
ATOM   1365  C  CD2 . LEU A 1 169  ? 69.997  89.691  99.153  1.00 118.04 ? 169  LEU A CD2 1 
ATOM   1366  N  N   . ARG A 1 170  ? 74.018  89.792  95.176  1.00 151.52 ? 170  ARG A N   1 
ATOM   1367  C  CA  . ARG A 1 170  ? 74.378  88.778  94.202  1.00 147.19 ? 170  ARG A CA  1 
ATOM   1368  C  C   . ARG A 1 170  ? 75.814  88.920  93.724  1.00 129.55 ? 170  ARG A C   1 
ATOM   1369  O  O   . ARG A 1 170  ? 76.272  88.091  92.928  1.00 124.96 ? 170  ARG A O   1 
ATOM   1370  C  CB  . ARG A 1 170  ? 73.426  88.831  93.000  1.00 144.94 ? 170  ARG A CB  1 
ATOM   1371  C  CG  . ARG A 1 170  ? 72.007  88.406  93.329  1.00 149.41 ? 170  ARG A CG  1 
ATOM   1372  C  CD  . ARG A 1 170  ? 71.164  88.296  92.074  1.00 172.25 ? 170  ARG A CD  1 
ATOM   1373  N  NE  . ARG A 1 170  ? 71.023  89.584  91.401  1.00 185.35 ? 170  ARG A NE  1 
ATOM   1374  C  CZ  . ARG A 1 170  ? 70.076  90.474  91.677  1.00 189.89 ? 170  ARG A CZ  1 
ATOM   1375  N  NH1 . ARG A 1 170  ? 69.182  90.222  92.623  1.00 182.50 ? 170  ARG A NH1 1 
ATOM   1376  N  NH2 . ARG A 1 170  ? 70.026  91.618  91.009  1.00 184.27 ? 170  ARG A NH2 1 
ATOM   1377  N  N   . SER A 1 171  ? 76.533  89.943  94.177  1.00 106.35 ? 171  SER A N   1 
ATOM   1378  C  CA  . SER A 1 171  ? 77.936  90.116  93.829  1.00 95.88  ? 171  SER A CA  1 
ATOM   1379  C  C   . SER A 1 171  ? 78.783  89.400  94.874  1.00 99.84  ? 171  SER A C   1 
ATOM   1380  O  O   . SER A 1 171  ? 78.834  89.813  96.038  1.00 95.50  ? 171  SER A O   1 
ATOM   1381  C  CB  . SER A 1 171  ? 78.293  91.597  93.760  1.00 102.94 ? 171  SER A CB  1 
ATOM   1382  O  OG  . SER A 1 171  ? 77.600  92.243  92.706  1.00 118.14 ? 171  SER A OG  1 
ATOM   1383  N  N   . ASN A 1 172  ? 79.447  88.329  94.454  1.00 94.27  ? 172  ASN A N   1 
ATOM   1384  C  CA  . ASN A 1 172  ? 80.329  87.569  95.323  1.00 68.81  ? 172  ASN A CA  1 
ATOM   1385  C  C   . ASN A 1 172  ? 81.334  86.843  94.446  1.00 72.56  ? 172  ASN A C   1 
ATOM   1386  O  O   . ASN A 1 172  ? 81.146  86.709  93.234  1.00 80.52  ? 172  ASN A O   1 
ATOM   1387  C  CB  . ASN A 1 172  ? 79.554  86.575  96.188  1.00 67.27  ? 172  ASN A CB  1 
ATOM   1388  C  CG  . ASN A 1 172  ? 78.636  85.695  95.370  1.00 82.18  ? 172  ASN A CG  1 
ATOM   1389  O  OD1 . ASN A 1 172  ? 78.122  86.109  94.332  1.00 94.71  ? 172  ASN A OD1 1 
ATOM   1390  N  ND2 . ASN A 1 172  ? 78.433  84.466  95.826  1.00 80.67  ? 172  ASN A ND2 1 
ATOM   1391  N  N   . TRP A 1 173  ? 82.400  86.367  95.074  1.00 64.41  ? 173  TRP A N   1 
ATOM   1392  C  CA  . TRP A 1 173  ? 83.373  85.526  94.403  1.00 64.12  ? 173  TRP A CA  1 
ATOM   1393  C  C   . TRP A 1 173  ? 83.710  84.376  95.338  1.00 62.84  ? 173  TRP A C   1 
ATOM   1394  O  O   . TRP A 1 173  ? 83.533  84.469  96.555  1.00 71.79  ? 173  TRP A O   1 
ATOM   1395  C  CB  . TRP A 1 173  ? 84.628  86.305  94.015  1.00 53.18  ? 173  TRP A CB  1 
ATOM   1396  C  CG  . TRP A 1 173  ? 85.325  86.851  95.188  1.00 52.52  ? 173  TRP A CG  1 
ATOM   1397  C  CD1 . TRP A 1 173  ? 85.115  88.054  95.787  1.00 69.13  ? 173  TRP A CD1 1 
ATOM   1398  C  CD2 . TRP A 1 173  ? 86.388  86.222  95.902  1.00 56.74  ? 173  TRP A CD2 1 
ATOM   1399  N  NE1 . TRP A 1 173  ? 85.971  88.204  96.853  1.00 70.20  ? 173  TRP A NE1 1 
ATOM   1400  C  CE2 . TRP A 1 173  ? 86.766  87.091  96.941  1.00 60.54  ? 173  TRP A CE2 1 
ATOM   1401  C  CE3 . TRP A 1 173  ? 87.052  84.999  95.768  1.00 52.13  ? 173  TRP A CE3 1 
ATOM   1402  C  CZ2 . TRP A 1 173  ? 87.781  86.778  97.841  1.00 63.22  ? 173  TRP A CZ2 1 
ATOM   1403  C  CZ3 . TRP A 1 173  ? 88.058  84.689  96.662  1.00 60.12  ? 173  TRP A CZ3 1 
ATOM   1404  C  CH2 . TRP A 1 173  ? 88.414  85.574  97.685  1.00 64.77  ? 173  TRP A CH2 1 
ATOM   1405  N  N   . LYS A 1 174  ? 84.200  83.282  94.764  1.00 58.25  ? 174  LYS A N   1 
ATOM   1406  C  CA  . LYS A 1 174  ? 84.598  82.147  95.579  1.00 62.44  ? 174  LYS A CA  1 
ATOM   1407  C  C   . LYS A 1 174  ? 85.736  81.403  94.900  1.00 66.26  ? 174  LYS A C   1 
ATOM   1408  O  O   . LYS A 1 174  ? 85.942  81.499  93.688  1.00 77.09  ? 174  LYS A O   1 
ATOM   1409  C  CB  . LYS A 1 174  ? 83.409  81.222  95.840  1.00 58.74  ? 174  LYS A CB  1 
ATOM   1410  C  CG  . LYS A 1 174  ? 82.886  80.566  94.587  1.00 73.77  ? 174  LYS A CG  1 
ATOM   1411  C  CD  . LYS A 1 174  ? 81.694  79.684  94.881  1.00 84.34  ? 174  LYS A CD  1 
ATOM   1412  C  CE  . LYS A 1 174  ? 80.942  79.377  93.601  1.00 108.05 ? 174  LYS A CE  1 
ATOM   1413  N  NZ  . LYS A 1 174  ? 81.668  78.377  92.776  1.00 111.17 ? 174  LYS A NZ  1 
ATOM   1414  N  N   . PHE A 1 175  ? 86.473  80.652  95.714  1.00 68.58  ? 175  PHE A N   1 
ATOM   1415  C  CA  . PHE A 1 175  ? 87.608  79.866  95.260  1.00 66.18  ? 175  PHE A CA  1 
ATOM   1416  C  C   . PHE A 1 175  ? 87.591  78.523  95.971  1.00 68.57  ? 175  PHE A C   1 
ATOM   1417  O  O   . PHE A 1 175  ? 87.517  78.470  97.202  1.00 69.10  ? 175  PHE A O   1 
ATOM   1418  C  CB  . PHE A 1 175  ? 88.907  80.641  95.531  1.00 67.64  ? 175  PHE A CB  1 
ATOM   1419  C  CG  . PHE A 1 175  ? 90.144  79.798  95.533  1.00 71.75  ? 175  PHE A CG  1 
ATOM   1420  C  CD1 . PHE A 1 175  ? 90.763  79.448  94.346  1.00 83.63  ? 175  PHE A CD1 1 
ATOM   1421  C  CD2 . PHE A 1 175  ? 90.722  79.400  96.727  1.00 77.22  ? 175  PHE A CD2 1 
ATOM   1422  C  CE1 . PHE A 1 175  ? 91.915  78.682  94.349  1.00 89.57  ? 175  PHE A CE1 1 
ATOM   1423  C  CE2 . PHE A 1 175  ? 91.874  78.636  96.737  1.00 67.01  ? 175  PHE A CE2 1 
ATOM   1424  C  CZ  . PHE A 1 175  ? 92.471  78.277  95.546  1.00 75.09  ? 175  PHE A CZ  1 
ATOM   1425  N  N   . ILE A 1 176  ? 87.653  77.443  95.195  1.00 70.61  ? 176  ILE A N   1 
ATOM   1426  C  CA  . ILE A 1 176  ? 87.556  76.084  95.716  1.00 68.03  ? 176  ILE A CA  1 
ATOM   1427  C  C   . ILE A 1 176  ? 88.879  75.381  95.461  1.00 72.02  ? 176  ILE A C   1 
ATOM   1428  O  O   . ILE A 1 176  ? 89.277  75.198  94.304  1.00 95.27  ? 176  ILE A O   1 
ATOM   1429  C  CB  . ILE A 1 176  ? 86.407  75.305  95.055  1.00 79.12  ? 176  ILE A CB  1 
ATOM   1430  C  CG1 . ILE A 1 176  ? 85.138  76.159  94.996  1.00 88.58  ? 176  ILE A CG1 1 
ATOM   1431  C  CG2 . ILE A 1 176  ? 86.157  73.990  95.787  1.00 84.35  ? 176  ILE A CG2 1 
ATOM   1432  C  CD1 . ILE A 1 176  ? 84.478  76.399  96.327  1.00 80.80  ? 176  ILE A CD1 1 
ATOM   1433  N  N   . GLY A 1 177  ? 89.551  74.972  96.531  1.00 67.49  ? 177  GLY A N   1 
ATOM   1434  C  CA  . GLY A 1 177  ? 90.799  74.256  96.372  1.00 74.96  ? 177  GLY A CA  1 
ATOM   1435  C  C   . GLY A 1 177  ? 90.720  72.878  96.991  1.00 86.06  ? 177  GLY A C   1 
ATOM   1436  O  O   . GLY A 1 177  ? 89.644  72.455  97.424  1.00 86.18  ? 177  GLY A O   1 
ATOM   1437  N  N   . THR A 1 178  ? 91.849  72.168  97.046  1.00 93.03  ? 178  THR A N   1 
ATOM   1438  C  CA  . THR A 1 178  ? 91.867  70.885  97.741  1.00 95.70  ? 178  THR A CA  1 
ATOM   1439  C  C   . THR A 1 178  ? 91.547  71.075  99.215  1.00 100.50 ? 178  THR A C   1 
ATOM   1440  O  O   . THR A 1 178  ? 90.743  70.333  99.790  1.00 109.42 ? 178  THR A O   1 
ATOM   1441  C  CB  . THR A 1 178  ? 93.222  70.201  97.562  1.00 102.93 ? 178  THR A CB  1 
ATOM   1442  O  OG1 . THR A 1 178  ? 93.378  69.805  96.193  1.00 100.08 ? 178  THR A OG1 1 
ATOM   1443  C  CG2 . THR A 1 178  ? 93.320  68.968  98.450  1.00 103.25 ? 178  THR A CG2 1 
ATOM   1444  N  N   . ASP A 1 179  ? 92.153  72.079  99.833  1.00 95.16  ? 179  ASP A N   1 
ATOM   1445  C  CA  . ASP A 1 179  ? 91.714  72.610  101.109 1.00 92.88  ? 179  ASP A CA  1 
ATOM   1446  C  C   . ASP A 1 179  ? 91.416  74.093  100.923 1.00 92.46  ? 179  ASP A C   1 
ATOM   1447  O  O   . ASP A 1 179  ? 91.528  74.631  99.819  1.00 104.87 ? 179  ASP A O   1 
ATOM   1448  C  CB  . ASP A 1 179  ? 92.787  72.398  102.179 1.00 85.23  ? 179  ASP A CB  1 
ATOM   1449  C  CG  . ASP A 1 179  ? 93.028  70.933  102.476 1.00 117.36 ? 179  ASP A CG  1 
ATOM   1450  O  OD1 . ASP A 1 179  ? 92.086  70.128  102.318 1.00 120.75 ? 179  ASP A OD1 1 
ATOM   1451  O  OD2 . ASP A 1 179  ? 94.166  70.582  102.853 1.00 118.19 ? 179  ASP A OD2 1 
ATOM   1452  N  N   . LEU A 1 180  ? 91.040  74.756  102.017 1.00 70.72  ? 180  LEU A N   1 
ATOM   1453  C  CA  . LEU A 1 180  ? 90.993  76.216  102.075 1.00 67.07  ? 180  LEU A CA  1 
ATOM   1454  C  C   . LEU A 1 180  ? 90.098  76.782  100.968 1.00 65.32  ? 180  LEU A C   1 
ATOM   1455  O  O   . LEU A 1 180  ? 90.553  77.371  99.983  1.00 73.58  ? 180  LEU A O   1 
ATOM   1456  C  CB  . LEU A 1 180  ? 92.404  76.807  102.011 1.00 56.21  ? 180  LEU A CB  1 
ATOM   1457  C  CG  . LEU A 1 180  ? 92.409  78.312  102.246 1.00 53.32  ? 180  LEU A CG  1 
ATOM   1458  C  CD1 . LEU A 1 180  ? 91.892  78.607  103.644 1.00 54.10  ? 180  LEU A CD1 1 
ATOM   1459  C  CD2 . LEU A 1 180  ? 93.797  78.878  102.045 1.00 66.01  ? 180  LEU A CD2 1 
ATOM   1460  N  N   . GLU A 1 181  ? 88.803  76.549  101.132 1.00 62.11  ? 181  GLU A N   1 
ATOM   1461  C  CA  . GLU A 1 181  ? 87.833  77.290  100.345 1.00 56.74  ? 181  GLU A CA  1 
ATOM   1462  C  C   . GLU A 1 181  ? 87.684  78.710  100.879 1.00 56.18  ? 181  GLU A C   1 
ATOM   1463  O  O   . GLU A 1 181  ? 87.826  78.968  102.078 1.00 67.85  ? 181  GLU A O   1 
ATOM   1464  C  CB  . GLU A 1 181  ? 86.492  76.559  100.359 1.00 75.38  ? 181  GLU A CB  1 
ATOM   1465  C  CG  . GLU A 1 181  ? 86.624  75.116  99.895  1.00 94.29  ? 181  GLU A CG  1 
ATOM   1466  C  CD  . GLU A 1 181  ? 85.296  74.407  99.764  1.00 112.94 ? 181  GLU A CD  1 
ATOM   1467  O  OE1 . GLU A 1 181  ? 84.802  73.883  100.782 1.00 107.35 ? 181  GLU A OE1 1 
ATOM   1468  O  OE2 . GLU A 1 181  ? 84.747  74.359  98.647  1.00 120.99 ? 181  GLU A OE2 1 
ATOM   1469  N  N   . LEU A 1 182  ? 87.382  79.632  99.969  1.00 58.60  ? 182  LEU A N   1 
ATOM   1470  C  CA  . LEU A 1 182  ? 87.217  81.040  100.290 1.00 50.43  ? 182  LEU A CA  1 
ATOM   1471  C  C   . LEU A 1 182  ? 85.895  81.542  99.740  1.00 63.91  ? 182  LEU A C   1 
ATOM   1472  O  O   . LEU A 1 182  ? 85.375  81.023  98.748  1.00 82.66  ? 182  LEU A O   1 
ATOM   1473  C  CB  . LEU A 1 182  ? 88.352  81.908  99.724  1.00 58.70  ? 182  LEU A CB  1 
ATOM   1474  C  CG  . LEU A 1 182  ? 89.779  81.617  100.173 1.00 55.25  ? 182  LEU A CG  1 
ATOM   1475  C  CD1 . LEU A 1 182  ? 90.764  82.484  99.409  1.00 45.30  ? 182  LEU A CD1 1 
ATOM   1476  C  CD2 . LEU A 1 182  ? 89.868  81.894  101.649 1.00 63.37  ? 182  LEU A CD2 1 
ATOM   1477  N  N   . PHE A 1 183  ? 85.360  82.569  100.389 1.00 50.04  ? 183  PHE A N   1 
ATOM   1478  C  CA  . PHE A 1 183  ? 84.122  83.175  99.932  1.00 46.71  ? 183  PHE A CA  1 
ATOM   1479  C  C   . PHE A 1 183  ? 84.143  84.648  100.300 1.00 43.92  ? 183  PHE A C   1 
ATOM   1480  O  O   . PHE A 1 183  ? 84.413  85.003  101.451 1.00 62.83  ? 183  PHE A O   1 
ATOM   1481  C  CB  . PHE A 1 183  ? 82.904  82.478  100.543 1.00 63.30  ? 183  PHE A CB  1 
ATOM   1482  C  CG  . PHE A 1 183  ? 81.597  82.921  99.955  1.00 62.20  ? 183  PHE A CG  1 
ATOM   1483  C  CD1 . PHE A 1 183  ? 80.869  83.946  100.537 1.00 55.68  ? 183  PHE A CD1 1 
ATOM   1484  C  CD2 . PHE A 1 183  ? 81.101  82.321  98.810  1.00 67.48  ? 183  PHE A CD2 1 
ATOM   1485  C  CE1 . PHE A 1 183  ? 79.666  84.357  99.990  1.00 60.68  ? 183  PHE A CE1 1 
ATOM   1486  C  CE2 . PHE A 1 183  ? 79.899  82.729  98.258  1.00 60.34  ? 183  PHE A CE2 1 
ATOM   1487  C  CZ  . PHE A 1 183  ? 79.182  83.748  98.849  1.00 60.13  ? 183  PHE A CZ  1 
ATOM   1488  N  N   . GLY A 1 184  ? 83.849  85.495  99.320  1.00 51.92  ? 184  GLY A N   1 
ATOM   1489  C  CA  . GLY A 1 184  ? 83.877  86.927  99.518  1.00 47.39  ? 184  GLY A CA  1 
ATOM   1490  C  C   . GLY A 1 184  ? 82.534  87.579  99.277  1.00 60.36  ? 184  GLY A C   1 
ATOM   1491  O  O   . GLY A 1 184  ? 81.928  87.411  98.214  1.00 76.59  ? 184  GLY A O   1 
ATOM   1492  N  N   . ILE A 1 185  ? 82.070  88.338  100.265 1.00 61.10  ? 185  ILE A N   1 
ATOM   1493  C  CA  . ILE A 1 185  ? 80.788  89.025  100.202 1.00 65.44  ? 185  ILE A CA  1 
ATOM   1494  C  C   . ILE A 1 185  ? 81.108  90.479  100.526 1.00 65.66  ? 185  ILE A C   1 
ATOM   1495  O  O   . ILE A 1 185  ? 82.287  90.851  100.555 1.00 70.86  ? 185  ILE A O   1 
ATOM   1496  C  CB  . ILE A 1 185  ? 79.754  88.391  101.157 1.00 54.24  ? 185  ILE A CB  1 
ATOM   1497  C  CG1 . ILE A 1 185  ? 78.322  88.784  100.766 1.00 48.44  ? 185  ILE A CG1 1 
ATOM   1498  C  CG2 . ILE A 1 185  ? 80.068  88.720  102.623 1.00 70.72  ? 185  ILE A CG2 1 
ATOM   1499  C  CD1 . ILE A 1 185  ? 77.847  88.171  99.454  1.00 61.33  ? 185  ILE A CD1 1 
ATOM   1500  N  N   . ALA A 1 186  ? 80.083  91.307  100.760 1.00 52.88  ? 186  ALA A N   1 
ATOM   1501  C  CA  . ALA A 1 186  ? 80.225  92.760  100.714 1.00 66.05  ? 186  ALA A CA  1 
ATOM   1502  C  C   . ALA A 1 186  ? 81.507  93.268  101.375 1.00 60.10  ? 186  ALA A C   1 
ATOM   1503  O  O   . ALA A 1 186  ? 82.373  93.843  100.708 1.00 81.97  ? 186  ALA A O   1 
ATOM   1504  C  CB  . ALA A 1 186  ? 79.000  93.412  101.363 1.00 87.55  ? 186  ALA A CB  1 
ATOM   1505  N  N   . ASP A 1 187  ? 81.664  93.039  102.679 1.00 68.20  ? 187  ASP A N   1 
ATOM   1506  C  CA  . ASP A 1 187  ? 82.827  93.538  103.408 1.00 68.52  ? 187  ASP A CA  1 
ATOM   1507  C  C   . ASP A 1 187  ? 83.626  92.424  104.071 1.00 73.18  ? 187  ASP A C   1 
ATOM   1508  O  O   . ASP A 1 187  ? 84.593  92.710  104.787 1.00 68.52  ? 187  ASP A O   1 
ATOM   1509  C  CB  . ASP A 1 187  ? 82.403  94.560  104.468 1.00 76.78  ? 187  ASP A CB  1 
ATOM   1510  C  CG  . ASP A 1 187  ? 81.562  95.686  103.897 1.00 98.26  ? 187  ASP A CG  1 
ATOM   1511  O  OD1 . ASP A 1 187  ? 81.535  95.856  102.662 1.00 99.72  ? 187  ASP A OD1 1 
ATOM   1512  O  OD2 . ASP A 1 187  ? 80.930  96.409  104.693 1.00 97.26  ? 187  ASP A OD2 1 
ATOM   1513  N  N   . PHE A 1 188  ? 83.259  91.168  103.843 1.00 71.39  ? 188  PHE A N   1 
ATOM   1514  C  CA  . PHE A 1 188  ? 83.759  90.060  104.636 1.00 56.17  ? 188  PHE A CA  1 
ATOM   1515  C  C   . PHE A 1 188  ? 84.368  89.007  103.726 1.00 68.97  ? 188  PHE A C   1 
ATOM   1516  O  O   . PHE A 1 188  ? 84.011  88.884  102.552 1.00 70.96  ? 188  PHE A O   1 
ATOM   1517  C  CB  . PHE A 1 188  ? 82.649  89.427  105.487 1.00 66.35  ? 188  PHE A CB  1 
ATOM   1518  C  CG  . PHE A 1 188  ? 81.848  90.421  106.272 1.00 75.03  ? 188  PHE A CG  1 
ATOM   1519  C  CD1 . PHE A 1 188  ? 80.698  90.977  105.742 1.00 81.19  ? 188  PHE A CD1 1 
ATOM   1520  C  CD2 . PHE A 1 188  ? 82.243  90.795  107.546 1.00 69.00  ? 188  PHE A CD2 1 
ATOM   1521  C  CE1 . PHE A 1 188  ? 79.959  91.896  106.461 1.00 75.97  ? 188  PHE A CE1 1 
ATOM   1522  C  CE2 . PHE A 1 188  ? 81.507  91.712  108.272 1.00 70.51  ? 188  PHE A CE2 1 
ATOM   1523  C  CZ  . PHE A 1 188  ? 80.365  92.263  107.728 1.00 82.44  ? 188  PHE A CZ  1 
ATOM   1524  N  N   . VAL A 1 189  ? 85.291  88.239  104.293 1.00 65.59  ? 189  VAL A N   1 
ATOM   1525  C  CA  . VAL A 1 189  ? 85.838  87.060  103.640 1.00 58.77  ? 189  VAL A CA  1 
ATOM   1526  C  C   . VAL A 1 189  ? 85.768  85.918  104.637 1.00 51.42  ? 189  VAL A C   1 
ATOM   1527  O  O   . VAL A 1 189  ? 86.070  86.094  105.824 1.00 67.60  ? 189  VAL A O   1 
ATOM   1528  C  CB  . VAL A 1 189  ? 87.285  87.278  103.151 1.00 67.51  ? 189  VAL A CB  1 
ATOM   1529  C  CG1 . VAL A 1 189  ? 87.748  86.085  102.327 1.00 68.27  ? 189  VAL A CG1 1 
ATOM   1530  C  CG2 . VAL A 1 189  ? 87.392  88.567  102.340 1.00 71.33  ? 189  VAL A CG2 1 
ATOM   1531  N  N   . ILE A 1 190  ? 85.366  84.749  104.156 1.00 48.34  ? 190  ILE A N   1 
ATOM   1532  C  CA  . ILE A 1 190  ? 85.139  83.581  104.993 1.00 53.80  ? 190  ILE A CA  1 
ATOM   1533  C  C   . ILE A 1 190  ? 86.099  82.477  104.573 1.00 69.50  ? 190  ILE A C   1 
ATOM   1534  O  O   . ILE A 1 190  ? 86.166  82.122  103.389 1.00 85.09  ? 190  ILE A O   1 
ATOM   1535  C  CB  . ILE A 1 190  ? 83.671  83.128  104.909 1.00 60.51  ? 190  ILE A CB  1 
ATOM   1536  C  CG1 . ILE A 1 190  ? 82.759  84.250  105.416 1.00 47.33  ? 190  ILE A CG1 1 
ATOM   1537  C  CG2 . ILE A 1 190  ? 83.455  81.855  105.678 1.00 57.34  ? 190  ILE A CG2 1 
ATOM   1538  C  CD1 . ILE A 1 190  ? 81.278  83.990  105.240 1.00 59.39  ? 190  ILE A CD1 1 
ATOM   1539  N  N   . PHE A 1 191  ? 86.829  81.930  105.544 1.00 56.17  ? 191  PHE A N   1 
ATOM   1540  C  CA  . PHE A 1 191  ? 87.784  80.853  105.318 1.00 45.72  ? 191  PHE A CA  1 
ATOM   1541  C  C   . PHE A 1 191  ? 87.200  79.553  105.850 1.00 49.55  ? 191  PHE A C   1 
ATOM   1542  O  O   . PHE A 1 191  ? 86.617  79.522  106.938 1.00 67.12  ? 191  PHE A O   1 
ATOM   1543  C  CB  . PHE A 1 191  ? 89.122  81.133  106.015 1.00 55.63  ? 191  PHE A CB  1 
ATOM   1544  C  CG  . PHE A 1 191  ? 89.760  82.439  105.624 1.00 50.40  ? 191  PHE A CG  1 
ATOM   1545  C  CD1 . PHE A 1 191  ? 89.309  83.635  106.154 1.00 54.34  ? 191  PHE A CD1 1 
ATOM   1546  C  CD2 . PHE A 1 191  ? 90.839  82.465  104.756 1.00 54.86  ? 191  PHE A CD2 1 
ATOM   1547  C  CE1 . PHE A 1 191  ? 89.897  84.836  105.800 1.00 54.05  ? 191  PHE A CE1 1 
ATOM   1548  C  CE2 . PHE A 1 191  ? 91.432  83.666  104.395 1.00 51.44  ? 191  PHE A CE2 1 
ATOM   1549  C  CZ  . PHE A 1 191  ? 90.961  84.851  104.922 1.00 50.48  ? 191  PHE A CZ  1 
ATOM   1550  N  N   . LYS A 1 192  ? 87.368  78.479  105.084 1.00 52.79  ? 192  LYS A N   1 
ATOM   1551  C  CA  . LYS A 1 192  ? 86.713  77.207  105.362 1.00 54.03  ? 192  LYS A CA  1 
ATOM   1552  C  C   . LYS A 1 192  ? 87.732  76.083  105.252 1.00 62.94  ? 192  LYS A C   1 
ATOM   1553  O  O   . LYS A 1 192  ? 88.296  75.862  104.176 1.00 82.32  ? 192  LYS A O   1 
ATOM   1554  C  CB  . LYS A 1 192  ? 85.547  76.997  104.398 1.00 54.30  ? 192  LYS A CB  1 
ATOM   1555  C  CG  . LYS A 1 192  ? 84.729  75.756  104.630 1.00 51.69  ? 192  LYS A CG  1 
ATOM   1556  C  CD  . LYS A 1 192  ? 84.008  75.417  103.345 1.00 69.30  ? 192  LYS A CD  1 
ATOM   1557  C  CE  . LYS A 1 192  ? 82.697  74.709  103.587 1.00 80.71  ? 192  LYS A CE  1 
ATOM   1558  N  NZ  . LYS A 1 192  ? 82.000  74.467  102.295 1.00 74.67  ? 192  LYS A NZ  1 
ATOM   1559  N  N   . VAL A 1 193  ? 87.957  75.369  106.352 1.00 60.14  ? 193  VAL A N   1 
ATOM   1560  C  CA  . VAL A 1 193  ? 88.982  74.327  106.396 1.00 63.39  ? 193  VAL A CA  1 
ATOM   1561  C  C   . VAL A 1 193  ? 88.424  73.025  106.967 1.00 73.38  ? 193  VAL A C   1 
ATOM   1562  O  O   . VAL A 1 193  ? 87.512  73.054  107.806 1.00 78.73  ? 193  VAL A O   1 
ATOM   1563  C  CB  . VAL A 1 193  ? 90.199  74.795  107.212 1.00 68.03  ? 193  VAL A CB  1 
ATOM   1564  C  CG1 . VAL A 1 193  ? 90.904  75.949  106.508 1.00 78.47  ? 193  VAL A CG1 1 
ATOM   1565  C  CG2 . VAL A 1 193  ? 89.772  75.212  108.616 1.00 74.55  ? 193  VAL A CG2 1 
ATOM   1566  N  N   . PRO A 1 194  ? 88.930  71.868  106.535 1.00 70.51  ? 194  PRO A N   1 
ATOM   1567  C  CA  . PRO A 1 194  ? 88.472  70.599  107.115 1.00 82.50  ? 194  PRO A CA  1 
ATOM   1568  C  C   . PRO A 1 194  ? 88.882  70.476  108.575 1.00 88.92  ? 194  PRO A C   1 
ATOM   1569  O  O   . PRO A 1 194  ? 89.931  70.967  108.996 1.00 99.69  ? 194  PRO A O   1 
ATOM   1570  C  CB  . PRO A 1 194  ? 89.160  69.536  106.249 1.00 74.35  ? 194  PRO A CB  1 
ATOM   1571  C  CG  . PRO A 1 194  ? 90.256  70.253  105.525 1.00 79.56  ? 194  PRO A CG  1 
ATOM   1572  C  CD  . PRO A 1 194  ? 89.808  71.669  105.371 1.00 80.19  ? 194  PRO A CD  1 
ATOM   1573  N  N   . VAL A 1 195  ? 88.028  69.803  109.350 1.00 85.09  ? 195  VAL A N   1 
ATOM   1574  C  CA  . VAL A 1 195  ? 88.246  69.666  110.789 1.00 85.05  ? 195  VAL A CA  1 
ATOM   1575  C  C   . VAL A 1 195  ? 89.444  68.769  111.090 1.00 105.95 ? 195  VAL A C   1 
ATOM   1576  O  O   . VAL A 1 195  ? 90.196  69.012  112.042 1.00 109.37 ? 195  VAL A O   1 
ATOM   1577  C  CB  . VAL A 1 195  ? 86.966  69.132  111.460 1.00 92.39  ? 195  VAL A CB  1 
ATOM   1578  C  CG1 . VAL A 1 195  ? 87.144  69.034  112.970 1.00 102.48 ? 195  VAL A CG1 1 
ATOM   1579  C  CG2 . VAL A 1 195  ? 85.766  70.001  111.100 1.00 104.57 ? 195  VAL A CG2 1 
ATOM   1580  N  N   . LYS A 1 196  ? 89.654  67.734  110.273 1.00 109.97 ? 196  LYS A N   1 
ATOM   1581  C  CA  . LYS A 1 196  ? 90.690  66.739  110.548 1.00 109.64 ? 196  LYS A CA  1 
ATOM   1582  C  C   . LYS A 1 196  ? 92.091  67.341  110.555 1.00 111.49 ? 196  LYS A C   1 
ATOM   1583  O  O   . LYS A 1 196  ? 92.935  66.956  111.373 1.00 116.56 ? 196  LYS A O   1 
ATOM   1584  C  CB  . LYS A 1 196  ? 90.603  65.595  109.535 1.00 116.62 ? 196  LYS A CB  1 
ATOM   1585  C  CG  . LYS A 1 196  ? 89.528  64.559  109.854 1.00 136.85 ? 196  LYS A CG  1 
ATOM   1586  C  CD  . LYS A 1 196  ? 88.124  65.084  109.603 1.00 140.94 ? 196  LYS A CD  1 
ATOM   1587  C  CE  . LYS A 1 196  ? 87.083  64.008  109.850 1.00 143.96 ? 196  LYS A CE  1 
ATOM   1588  N  NZ  . LYS A 1 196  ? 85.699  64.540  109.730 1.00 128.04 ? 196  LYS A NZ  1 
ATOM   1589  N  N   . THR A 1 197  ? 92.358  68.289  109.659 1.00 110.40 ? 197  THR A N   1 
ATOM   1590  C  CA  . THR A 1 197  ? 93.667  68.928  109.589 1.00 109.23 ? 197  THR A CA  1 
ATOM   1591  C  C   . THR A 1 197  ? 93.981  69.829  110.777 1.00 103.10 ? 197  THR A C   1 
ATOM   1592  O  O   . THR A 1 197  ? 95.135  70.253  110.908 1.00 104.66 ? 197  THR A O   1 
ATOM   1593  C  CB  . THR A 1 197  ? 93.779  69.751  108.305 1.00 104.94 ? 197  THR A CB  1 
ATOM   1594  O  OG1 . THR A 1 197  ? 92.882  70.866  108.376 1.00 96.68  ? 197  THR A OG1 1 
ATOM   1595  C  CG2 . THR A 1 197  ? 93.417  68.901  107.098 1.00 111.30 ? 197  THR A CG2 1 
ATOM   1596  N  N   . ILE A 1 198  ? 93.019  70.134  111.642 1.00 100.47 ? 198  ILE A N   1 
ATOM   1597  C  CA  . ILE A 1 198  ? 93.302  70.919  112.836 1.00 110.31 ? 198  ILE A CA  1 
ATOM   1598  C  C   . ILE A 1 198  ? 93.475  70.049  114.076 1.00 123.91 ? 198  ILE A C   1 
ATOM   1599  O  O   . ILE A 1 198  ? 94.368  70.303  114.885 1.00 115.08 ? 198  ILE A O   1 
ATOM   1600  C  CB  . ILE A 1 198  ? 92.190  71.969  113.046 1.00 105.74 ? 198  ILE A CB  1 
ATOM   1601  C  CG1 . ILE A 1 198  ? 92.110  72.888  111.829 1.00 104.55 ? 198  ILE A CG1 1 
ATOM   1602  C  CG2 . ILE A 1 198  ? 92.434  72.776  114.313 1.00 101.07 ? 198  ILE A CG2 1 
ATOM   1603  C  CD1 . ILE A 1 198  ? 93.388  73.653  111.568 1.00 101.60 ? 198  ILE A CD1 1 
ATOM   1604  N  N   . ILE A 1 199  ? 92.647  69.016  114.254 1.00 120.42 ? 199  ILE A N   1 
ATOM   1605  C  CA  . ILE A 1 199  ? 92.830  68.135  115.404 1.00 105.28 ? 199  ILE A CA  1 
ATOM   1606  C  C   . ILE A 1 199  ? 94.136  67.356  115.285 1.00 120.40 ? 199  ILE A C   1 
ATOM   1607  O  O   . ILE A 1 199  ? 94.965  67.364  116.202 1.00 129.63 ? 199  ILE A O   1 
ATOM   1608  C  CB  . ILE A 1 199  ? 91.623  67.195  115.565 1.00 107.26 ? 199  ILE A CB  1 
ATOM   1609  C  CG1 . ILE A 1 199  ? 90.353  68.014  115.784 1.00 94.99  ? 199  ILE A CG1 1 
ATOM   1610  C  CG2 . ILE A 1 199  ? 91.849  66.231  116.723 1.00 132.42 ? 199  ILE A CG2 1 
ATOM   1611  C  CD1 . ILE A 1 199  ? 90.224  68.560  117.187 1.00 98.56  ? 199  ILE A CD1 1 
ATOM   1612  N  N   . ARG A 1 200  ? 94.342  66.689  114.147 1.00 122.06 ? 200  ARG A N   1 
ATOM   1613  C  CA  . ARG A 1 200  ? 95.601  66.013  113.833 1.00 129.68 ? 200  ARG A CA  1 
ATOM   1614  C  C   . ARG A 1 200  ? 95.974  64.995  114.910 1.00 144.08 ? 200  ARG A C   1 
ATOM   1615  O  O   . ARG A 1 200  ? 97.074  65.026  115.468 1.00 147.63 ? 200  ARG A O   1 
ATOM   1616  C  CB  . ARG A 1 200  ? 96.737  67.011  113.612 1.00 135.07 ? 200  ARG A CB  1 
ATOM   1617  C  CG  . ARG A 1 200  ? 97.003  67.333  112.155 1.00 133.36 ? 200  ARG A CG  1 
ATOM   1618  C  CD  . ARG A 1 200  ? 98.220  68.217  112.063 1.00 142.50 ? 200  ARG A CD  1 
ATOM   1619  N  NE  . ARG A 1 200  ? 98.181  69.255  113.087 1.00 142.58 ? 200  ARG A NE  1 
ATOM   1620  C  CZ  . ARG A 1 200  ? 99.191  69.528  113.905 1.00 149.57 ? 200  ARG A CZ  1 
ATOM   1621  N  NH1 . ARG A 1 200  ? 100.319 68.835  113.821 1.00 151.54 ? 200  ARG A NH1 1 
ATOM   1622  N  NH2 . ARG A 1 200  ? 99.072  70.487  114.812 1.00 151.88 ? 200  ARG A NH2 1 
ATOM   1623  N  N   . ASN A 1 201  ? 95.043  64.087  115.204 1.00 143.99 ? 201  ASN A N   1 
ATOM   1624  C  CA  . ASN A 1 201  ? 95.273  63.008  116.165 1.00 142.30 ? 201  ASN A CA  1 
ATOM   1625  C  C   . ASN A 1 201  ? 95.671  63.559  117.537 1.00 134.36 ? 201  ASN A C   1 
ATOM   1626  O  O   . ASN A 1 201  ? 96.780  63.348  118.030 1.00 132.92 ? 201  ASN A O   1 
ATOM   1627  C  CB  . ASN A 1 201  ? 96.324  62.023  115.641 1.00 147.06 ? 201  ASN A CB  1 
ATOM   1628  C  CG  . ASN A 1 201  ? 95.820  61.196  114.478 1.00 157.91 ? 201  ASN A CG  1 
ATOM   1629  O  OD1 . ASN A 1 201  ? 94.682  60.731  114.478 1.00 152.93 ? 201  ASN A OD1 1 
ATOM   1630  N  ND2 . ASN A 1 201  ? 96.669  61.010  113.473 1.00 153.73 ? 201  ASN A ND2 1 
ATOM   1631  N  N   . ALA A 1 202  ? 94.736  64.286  118.144 1.00 130.71 ? 202  ALA A N   1 
ATOM   1632  C  CA  . ALA A 1 202  ? 94.910  64.840  119.478 1.00 121.38 ? 202  ALA A CA  1 
ATOM   1633  C  C   . ALA A 1 202  ? 93.653  64.547  120.286 1.00 122.77 ? 202  ALA A C   1 
ATOM   1634  O  O   . ALA A 1 202  ? 92.632  64.114  119.747 1.00 119.06 ? 202  ALA A O   1 
ATOM   1635  C  CB  . ALA A 1 202  ? 95.191  66.348  119.433 1.00 108.85 ? 202  ALA A CB  1 
ATOM   1636  N  N   . VAL A 1 203  ? 93.733  64.782  121.598 1.00 128.60 ? 203  VAL A N   1 
ATOM   1637  C  CA  . VAL A 1 203  ? 92.608  64.459  122.473 1.00 129.76 ? 203  VAL A CA  1 
ATOM   1638  C  C   . VAL A 1 203  ? 91.402  65.339  122.164 1.00 130.51 ? 203  VAL A C   1 
ATOM   1639  O  O   . VAL A 1 203  ? 90.275  64.848  122.039 1.00 125.39 ? 203  VAL A O   1 
ATOM   1640  C  CB  . VAL A 1 203  ? 93.027  64.573  123.950 1.00 131.76 ? 203  VAL A CB  1 
ATOM   1641  C  CG1 . VAL A 1 203  ? 91.832  64.330  124.859 1.00 122.42 ? 203  VAL A CG1 1 
ATOM   1642  C  CG2 . VAL A 1 203  ? 94.146  63.589  124.260 1.00 137.81 ? 203  VAL A CG2 1 
ATOM   1643  N  N   . SER A 1 204  ? 91.618  66.644  122.017 1.00 133.10 ? 204  SER A N   1 
ATOM   1644  C  CA  . SER A 1 204  ? 90.510  67.566  121.817 1.00 124.99 ? 204  SER A CA  1 
ATOM   1645  C  C   . SER A 1 204  ? 91.003  68.786  121.049 1.00 112.36 ? 204  SER A C   1 
ATOM   1646  O  O   . SER A 1 204  ? 92.196  68.936  120.774 1.00 113.15 ? 204  SER A O   1 
ATOM   1647  C  CB  . SER A 1 204  ? 89.883  67.972  123.155 1.00 115.50 ? 204  SER A CB  1 
ATOM   1648  O  OG  . SER A 1 204  ? 90.874  68.413  124.067 1.00 115.55 ? 204  SER A OG  1 
ATOM   1649  N  N   . LEU A 1 205  ? 90.059  69.667  120.708 1.00 97.61  ? 205  LEU A N   1 
ATOM   1650  C  CA  . LEU A 1 205  ? 90.401  70.875  119.966 1.00 101.57 ? 205  LEU A CA  1 
ATOM   1651  C  C   . LEU A 1 205  ? 91.291  71.813  120.775 1.00 100.73 ? 205  LEU A C   1 
ATOM   1652  O  O   . LEU A 1 205  ? 92.252  72.374  120.239 1.00 104.58 ? 205  LEU A O   1 
ATOM   1653  C  CB  . LEU A 1 205  ? 89.126  71.583  119.513 1.00 107.06 ? 205  LEU A CB  1 
ATOM   1654  C  CG  . LEU A 1 205  ? 89.329  72.709  118.501 1.00 108.48 ? 205  LEU A CG  1 
ATOM   1655  C  CD1 . LEU A 1 205  ? 89.919  72.168  117.212 1.00 101.95 ? 205  LEU A CD1 1 
ATOM   1656  C  CD2 . LEU A 1 205  ? 88.002  73.393  118.227 1.00 109.13 ? 205  LEU A CD2 1 
ATOM   1657  N  N   . GLN A 1 206  ? 90.997  71.997  122.067 1.00 98.67  ? 206  GLN A N   1 
ATOM   1658  C  CA  . GLN A 1 206  ? 91.833  72.882  122.873 1.00 91.61  ? 206  GLN A CA  1 
ATOM   1659  C  C   . GLN A 1 206  ? 93.206  72.276  123.127 1.00 107.42 ? 206  GLN A C   1 
ATOM   1660  O  O   . GLN A 1 206  ? 94.186  73.012  123.294 1.00 109.02 ? 206  GLN A O   1 
ATOM   1661  C  CB  . GLN A 1 206  ? 91.147  73.212  124.199 1.00 97.66  ? 206  GLN A CB  1 
ATOM   1662  C  CG  . GLN A 1 206  ? 89.772  73.835  124.053 1.00 85.88  ? 206  GLN A CG  1 
ATOM   1663  C  CD  . GLN A 1 206  ? 88.664  72.813  124.179 1.00 94.25  ? 206  GLN A CD  1 
ATOM   1664  O  OE1 . GLN A 1 206  ? 88.745  71.720  123.618 1.00 98.59  ? 206  GLN A OE1 1 
ATOM   1665  N  NE2 . GLN A 1 206  ? 87.619  73.163  124.921 1.00 97.25  ? 206  GLN A NE2 1 
ATOM   1666  N  N   . ALA A 1 207  ? 93.295  70.945  123.166 1.00 109.58 ? 207  ALA A N   1 
ATOM   1667  C  CA  . ALA A 1 207  ? 94.587  70.298  123.362 1.00 104.69 ? 207  ALA A CA  1 
ATOM   1668  C  C   . ALA A 1 207  ? 95.524  70.572  122.193 1.00 109.53 ? 207  ALA A C   1 
ATOM   1669  O  O   . ALA A 1 207  ? 96.723  70.806  122.386 1.00 113.44 ? 207  ALA A O   1 
ATOM   1670  C  CB  . ALA A 1 207  ? 94.394  68.793  123.559 1.00 103.98 ? 207  ALA A CB  1 
ATOM   1671  N  N   . SER A 1 208  ? 94.990  70.560  120.968 1.00 103.21 ? 208  SER A N   1 
ATOM   1672  C  CA  . SER A 1 208  ? 95.811  70.812  119.789 1.00 97.32  ? 208  SER A CA  1 
ATOM   1673  C  C   . SER A 1 208  ? 96.183  72.284  119.659 1.00 89.93  ? 208  SER A C   1 
ATOM   1674  O  O   . SER A 1 208  ? 97.320  72.612  119.299 1.00 91.31  ? 208  SER A O   1 
ATOM   1675  C  CB  . SER A 1 208  ? 95.083  70.339  118.531 1.00 104.67 ? 208  SER A CB  1 
ATOM   1676  O  OG  . SER A 1 208  ? 95.932  70.406  117.396 1.00 109.53 ? 208  SER A OG  1 
ATOM   1677  N  N   . LYS A 1 209  ? 95.246  73.187  119.948 1.00 94.10  ? 209  LYS A N   1 
ATOM   1678  C  CA  . LYS A 1 209  ? 95.490  74.627  119.868 1.00 90.41  ? 209  LYS A CA  1 
ATOM   1679  C  C   . LYS A 1 209  ? 95.136  75.237  121.218 1.00 98.05  ? 209  LYS A C   1 
ATOM   1680  O  O   . LYS A 1 209  ? 93.978  75.599  121.465 1.00 99.57  ? 209  LYS A O   1 
ATOM   1681  C  CB  . LYS A 1 209  ? 94.678  75.249  118.735 1.00 86.42  ? 209  LYS A CB  1 
ATOM   1682  C  CG  . LYS A 1 209  ? 94.733  74.435  117.446 1.00 101.52 ? 209  LYS A CG  1 
ATOM   1683  C  CD  . LYS A 1 209  ? 94.504  75.272  116.205 1.00 92.27  ? 209  LYS A CD  1 
ATOM   1684  C  CE  . LYS A 1 209  ? 95.756  76.049  115.852 1.00 89.15  ? 209  LYS A CE  1 
ATOM   1685  N  NZ  . LYS A 1 209  ? 96.726  75.176  115.132 1.00 93.18  ? 209  LYS A NZ  1 
ATOM   1686  N  N   . PRO A 1 210  ? 96.117  75.376  122.116 1.00 97.67  ? 210  PRO A N   1 
ATOM   1687  C  CA  . PRO A 1 210  ? 95.820  75.909  123.457 1.00 90.05  ? 210  PRO A CA  1 
ATOM   1688  C  C   . PRO A 1 210  ? 95.271  77.323  123.449 1.00 99.43  ? 210  PRO A C   1 
ATOM   1689  O  O   . PRO A 1 210  ? 94.554  77.704  124.383 1.00 98.61  ? 210  PRO A O   1 
ATOM   1690  C  CB  . PRO A 1 210  ? 97.179  75.841  124.169 1.00 95.65  ? 210  PRO A CB  1 
ATOM   1691  C  CG  . PRO A 1 210  ? 98.189  75.834  123.062 1.00 103.47 ? 210  PRO A CG  1 
ATOM   1692  C  CD  . PRO A 1 210  ? 97.549  75.077  121.940 1.00 108.66 ? 210  PRO A CD  1 
ATOM   1693  N  N   . GLY A 1 211  ? 95.587  78.115  122.425 1.00 90.08  ? 211  GLY A N   1 
ATOM   1694  C  CA  . GLY A 1 211  ? 95.076  79.470  122.347 1.00 77.41  ? 211  GLY A CA  1 
ATOM   1695  C  C   . GLY A 1 211  ? 93.567  79.555  122.270 1.00 96.88  ? 211  GLY A C   1 
ATOM   1696  O  O   . GLY A 1 211  ? 92.999  80.616  122.551 1.00 92.08  ? 211  GLY A O   1 
ATOM   1697  N  N   . LEU A 1 212  ? 92.896  78.459  121.902 1.00 98.35  ? 212  LEU A N   1 
ATOM   1698  C  CA  . LEU A 1 212  ? 91.439  78.449  121.889 1.00 83.18  ? 212  LEU A CA  1 
ATOM   1699  C  C   . LEU A 1 212  ? 90.807  78.423  123.276 1.00 89.85  ? 212  LEU A C   1 
ATOM   1700  O  O   . LEU A 1 212  ? 89.582  78.554  123.365 1.00 89.43  ? 212  LEU A O   1 
ATOM   1701  C  CB  . LEU A 1 212  ? 90.936  77.253  121.081 1.00 77.08  ? 212  LEU A CB  1 
ATOM   1702  C  CG  . LEU A 1 212  ? 91.212  77.348  119.584 1.00 74.87  ? 212  LEU A CG  1 
ATOM   1703  C  CD1 . LEU A 1 212  ? 90.501  76.234  118.834 1.00 79.10  ? 212  LEU A CD1 1 
ATOM   1704  C  CD2 . LEU A 1 212  ? 90.784  78.713  119.071 1.00 70.70  ? 212  LEU A CD2 1 
ATOM   1705  N  N   . ARG A 1 213  ? 91.580  78.254  124.352 1.00 98.65  ? 213  ARG A N   1 
ATOM   1706  C  CA  . ARG A 1 213  ? 90.956  78.269  125.672 1.00 97.75  ? 213  ARG A CA  1 
ATOM   1707  C  C   . ARG A 1 213  ? 90.379  79.631  126.021 1.00 92.85  ? 213  ARG A C   1 
ATOM   1708  O  O   . ARG A 1 213  ? 89.573  79.729  126.953 1.00 94.80  ? 213  ARG A O   1 
ATOM   1709  C  CB  . ARG A 1 213  ? 91.933  77.843  126.767 1.00 109.08 ? 213  ARG A CB  1 
ATOM   1710  C  CG  . ARG A 1 213  ? 91.818  76.382  127.147 1.00 111.08 ? 213  ARG A CG  1 
ATOM   1711  C  CD  . ARG A 1 213  ? 93.063  75.881  127.840 1.00 104.53 ? 213  ARG A CD  1 
ATOM   1712  N  NE  . ARG A 1 213  ? 93.243  74.449  127.643 1.00 113.98 ? 213  ARG A NE  1 
ATOM   1713  C  CZ  . ARG A 1 213  ? 94.392  73.809  127.833 1.00 134.81 ? 213  ARG A CZ  1 
ATOM   1714  N  NH1 . ARG A 1 213  ? 95.467  74.477  128.225 1.00 132.91 ? 213  ARG A NH1 1 
ATOM   1715  N  NH2 . ARG A 1 213  ? 94.463  72.502  127.629 1.00 134.36 ? 213  ARG A NH2 1 
ATOM   1716  N  N   . ILE A 1 214  ? 90.772  80.680  125.299 1.00 92.73  ? 214  ILE A N   1 
ATOM   1717  C  CA  . ILE A 1 214  ? 90.259  82.011  125.595 1.00 87.94  ? 214  ILE A CA  1 
ATOM   1718  C  C   . ILE A 1 214  ? 88.795  82.115  125.190 1.00 96.34  ? 214  ILE A C   1 
ATOM   1719  O  O   . ILE A 1 214  ? 87.991  82.757  125.875 1.00 102.18 ? 214  ILE A O   1 
ATOM   1720  C  CB  . ILE A 1 214  ? 91.125  83.082  124.908 1.00 84.64  ? 214  ILE A CB  1 
ATOM   1721  C  CG1 . ILE A 1 214  ? 92.594  82.891  125.291 1.00 87.67  ? 214  ILE A CG1 1 
ATOM   1722  C  CG2 . ILE A 1 214  ? 90.669  84.475  125.313 1.00 103.16 ? 214  ILE A CG2 1 
ATOM   1723  C  CD1 . ILE A 1 214  ? 93.527  83.921  124.693 1.00 102.54 ? 214  ILE A CD1 1 
ATOM   1724  N  N   . TRP A 1 215  ? 88.421  81.488  124.073 1.00 98.99  ? 215  TRP A N   1 
ATOM   1725  C  CA  . TRP A 1 215  ? 87.025  81.522  123.656 1.00 90.90  ? 215  TRP A CA  1 
ATOM   1726  C  C   . TRP A 1 215  ? 86.194  80.452  124.351 1.00 87.81  ? 215  TRP A C   1 
ATOM   1727  O  O   . TRP A 1 215  ? 85.084  80.733  124.819 1.00 96.70  ? 215  TRP A O   1 
ATOM   1728  C  CB  . TRP A 1 215  ? 86.919  81.331  122.146 1.00 97.68  ? 215  TRP A CB  1 
ATOM   1729  C  CG  . TRP A 1 215  ? 87.293  82.526  121.361 1.00 94.07  ? 215  TRP A CG  1 
ATOM   1730  C  CD1 . TRP A 1 215  ? 88.037  83.586  121.782 1.00 94.23  ? 215  TRP A CD1 1 
ATOM   1731  C  CD2 . TRP A 1 215  ? 86.900  82.814  120.018 1.00 81.29  ? 215  TRP A CD2 1 
ATOM   1732  N  NE1 . TRP A 1 215  ? 88.154  84.509  120.771 1.00 84.92  ? 215  TRP A NE1 1 
ATOM   1733  C  CE2 . TRP A 1 215  ? 87.460  84.058  119.679 1.00 80.84  ? 215  TRP A CE2 1 
ATOM   1734  C  CE3 . TRP A 1 215  ? 86.136  82.135  119.065 1.00 75.85  ? 215  TRP A CE3 1 
ATOM   1735  C  CZ2 . TRP A 1 215  ? 87.280  84.639  118.427 1.00 81.14  ? 215  TRP A CZ2 1 
ATOM   1736  C  CZ3 . TRP A 1 215  ? 85.958  82.712  117.825 1.00 69.55  ? 215  TRP A CZ3 1 
ATOM   1737  C  CH2 . TRP A 1 215  ? 86.527  83.951  117.516 1.00 76.45  ? 215  TRP A CH2 1 
ATOM   1738  N  N   . TYR A 1 216  ? 86.713  79.227  124.419 1.00 90.43  ? 216  TYR A N   1 
ATOM   1739  C  CA  . TYR A 1 216  ? 86.044  78.099  125.063 1.00 98.02  ? 216  TYR A CA  1 
ATOM   1740  C  C   . TYR A 1 216  ? 86.951  77.612  126.181 1.00 105.72 ? 216  TYR A C   1 
ATOM   1741  O  O   . TYR A 1 216  ? 87.943  76.921  125.930 1.00 115.31 ? 216  TYR A O   1 
ATOM   1742  C  CB  . TYR A 1 216  ? 85.759  76.963  124.099 1.00 102.78 ? 216  TYR A CB  1 
ATOM   1743  C  CG  . TYR A 1 216  ? 85.359  77.367  122.709 1.00 107.51 ? 216  TYR A CG  1 
ATOM   1744  C  CD1 . TYR A 1 216  ? 86.289  77.348  121.685 1.00 105.43 ? 216  TYR A CD1 1 
ATOM   1745  C  CD2 . TYR A 1 216  ? 84.058  77.748  122.408 1.00 115.97 ? 216  TYR A CD2 1 
ATOM   1746  C  CE1 . TYR A 1 216  ? 85.948  77.697  120.397 1.00 87.61  ? 216  TYR A CE1 1 
ATOM   1747  C  CE2 . TYR A 1 216  ? 83.703  78.105  121.113 1.00 97.50  ? 216  TYR A CE2 1 
ATOM   1748  C  CZ  . TYR A 1 216  ? 84.655  78.077  120.113 1.00 86.29  ? 216  TYR A CZ  1 
ATOM   1749  O  OH  . TYR A 1 216  ? 84.316  78.429  118.827 1.00 76.50  ? 216  TYR A OH  1 
ATOM   1750  N  N   . ARG A 1 217  ? 86.604  77.983  127.404 1.00 101.12 ? 217  ARG A N   1 
ATOM   1751  C  CA  . ARG A 1 217  ? 87.469  77.799  128.551 1.00 104.07 ? 217  ARG A CA  1 
ATOM   1752  C  C   . ARG A 1 217  ? 87.793  76.322  128.750 1.00 111.81 ? 217  ARG A C   1 
ATOM   1753  O  O   . ARG A 1 217  ? 88.922  75.898  128.486 1.00 109.49 ? 217  ARG A O   1 
ATOM   1754  C  CB  . ARG A 1 217  ? 86.788  78.467  129.742 1.00 117.51 ? 217  ARG A CB  1 
ATOM   1755  C  CG  . ARG A 1 217  ? 85.549  77.823  130.360 1.00 135.70 ? 217  ARG A CG  1 
ATOM   1756  C  CD  . ARG A 1 217  ? 84.912  78.898  131.199 1.00 137.45 ? 217  ARG A CD  1 
ATOM   1757  N  NE  . ARG A 1 217  ? 84.445  79.930  130.273 1.00 144.08 ? 217  ARG A NE  1 
ATOM   1758  C  CZ  . ARG A 1 217  ? 85.045  81.108  130.027 1.00 129.92 ? 217  ARG A CZ  1 
ATOM   1759  N  NH1 . ARG A 1 217  ? 84.473  81.930  129.151 1.00 125.49 ? 217  ARG A NH1 1 
ATOM   1760  N  NH2 . ARG A 1 217  ? 86.220  81.401  130.554 1.00 132.06 ? 217  ARG A NH2 1 
ATOM   1761  N  N   . ASP A 1 218  ? 86.810  75.528  129.161 1.00 122.98 ? 218  ASP A N   1 
ATOM   1762  C  CA  . ASP A 1 218  ? 86.960  74.079  129.234 1.00 123.27 ? 218  ASP A CA  1 
ATOM   1763  C  C   . ASP A 1 218  ? 85.567  73.485  129.023 1.00 125.20 ? 218  ASP A C   1 
ATOM   1764  O  O   . ASP A 1 218  ? 84.794  73.335  129.970 1.00 131.04 ? 218  ASP A O   1 
ATOM   1765  C  CB  . ASP A 1 218  ? 87.578  73.659  130.557 1.00 125.48 ? 218  ASP A CB  1 
ATOM   1766  C  CG  . ASP A 1 218  ? 89.089  73.676  130.511 1.00 126.76 ? 218  ASP A CG  1 
ATOM   1767  O  OD1 . ASP A 1 218  ? 89.659  73.126  129.545 1.00 125.50 ? 218  ASP A OD1 1 
ATOM   1768  O  OD2 . ASP A 1 218  ? 89.705  74.267  131.421 1.00 120.07 ? 218  ASP A OD2 1 
ATOM   1769  N  N   . GLN A 1 219  ? 85.259  73.162  127.770 1.00 114.75 ? 219  GLN A N   1 
ATOM   1770  C  CA  . GLN A 1 219  ? 83.953  72.642  127.404 1.00 111.80 ? 219  GLN A CA  1 
ATOM   1771  C  C   . GLN A 1 219  ? 84.124  71.442  126.487 1.00 116.08 ? 219  GLN A C   1 
ATOM   1772  O  O   . GLN A 1 219  ? 85.055  71.384  125.679 1.00 117.07 ? 219  GLN A O   1 
ATOM   1773  C  CB  . GLN A 1 219  ? 83.110  73.705  126.689 1.00 102.85 ? 219  GLN A CB  1 
ATOM   1774  C  CG  . GLN A 1 219  ? 83.028  75.033  127.417 1.00 109.24 ? 219  GLN A CG  1 
ATOM   1775  C  CD  . GLN A 1 219  ? 81.704  75.729  127.205 1.00 118.30 ? 219  GLN A CD  1 
ATOM   1776  O  OE1 . GLN A 1 219  ? 81.616  76.706  126.461 1.00 107.26 ? 219  GLN A OE1 1 
ATOM   1777  N  NE2 . GLN A 1 219  ? 80.661  75.228  127.856 1.00 145.54 ? 219  GLN A NE2 1 
ATOM   1778  N  N   . ASN A 1 220  ? 83.213  70.484  126.618 1.00 122.61 ? 220  ASN A N   1 
ATOM   1779  C  CA  . ASN A 1 220  ? 83.193  69.310  125.749 1.00 118.21 ? 220  ASN A CA  1 
ATOM   1780  C  C   . ASN A 1 220  ? 82.688  69.735  124.375 1.00 117.22 ? 220  ASN A C   1 
ATOM   1781  O  O   . ASN A 1 220  ? 81.480  69.845  124.152 1.00 124.71 ? 220  ASN A O   1 
ATOM   1782  C  CB  . ASN A 1 220  ? 82.324  68.212  126.348 1.00 127.06 ? 220  ASN A CB  1 
ATOM   1783  C  CG  . ASN A 1 220  ? 82.590  66.861  125.721 1.00 133.63 ? 220  ASN A CG  1 
ATOM   1784  O  OD1 . ASN A 1 220  ? 83.743  66.460  125.552 1.00 132.18 ? 220  ASN A OD1 1 
ATOM   1785  N  ND2 . ASN A 1 220  ? 81.527  66.153  125.362 1.00 139.88 ? 220  ASN A ND2 1 
ATOM   1786  N  N   . LEU A 1 221  ? 83.608  69.991  123.449 1.00 115.82 ? 221  LEU A N   1 
ATOM   1787  C  CA  . LEU A 1 221  ? 83.251  70.471  122.119 1.00 113.39 ? 221  LEU A CA  1 
ATOM   1788  C  C   . LEU A 1 221  ? 82.919  69.362  121.130 1.00 108.06 ? 221  LEU A C   1 
ATOM   1789  O  O   . LEU A 1 221  ? 82.512  69.670  120.005 1.00 110.75 ? 221  LEU A O   1 
ATOM   1790  C  CB  . LEU A 1 221  ? 84.385  71.322  121.546 1.00 104.56 ? 221  LEU A CB  1 
ATOM   1791  C  CG  . LEU A 1 221  ? 84.655  72.625  122.285 1.00 116.45 ? 221  LEU A CG  1 
ATOM   1792  C  CD1 . LEU A 1 221  ? 85.596  73.494  121.473 1.00 97.92  ? 221  LEU A CD1 1 
ATOM   1793  C  CD2 . LEU A 1 221  ? 83.340  73.343  122.550 1.00 120.27 ? 221  LEU A CD2 1 
ATOM   1794  N  N   . THR A 1 222  ? 83.072  68.097  121.505 1.00 113.67 ? 222  THR A N   1 
ATOM   1795  C  CA  . THR A 1 222  ? 82.838  67.041  120.525 1.00 116.61 ? 222  THR A CA  1 
ATOM   1796  C  C   . THR A 1 222  ? 81.382  66.903  120.063 1.00 121.67 ? 222  THR A C   1 
ATOM   1797  O  O   . THR A 1 222  ? 81.170  66.441  118.936 1.00 122.32 ? 222  THR A O   1 
ATOM   1798  C  CB  . THR A 1 222  ? 83.365  65.692  121.040 1.00 120.57 ? 222  THR A CB  1 
ATOM   1799  O  OG1 . THR A 1 222  ? 83.254  64.710  120.001 1.00 123.99 ? 222  THR A OG1 1 
ATOM   1800  C  CG2 . THR A 1 222  ? 82.612  65.207  122.266 1.00 133.85 ? 222  THR A CG2 1 
ATOM   1801  N  N   . PRO A 1 223  ? 80.352  67.281  120.840 1.00 115.22 ? 223  PRO A N   1 
ATOM   1802  C  CA  . PRO A 1 223  ? 78.989  67.223  120.279 1.00 119.57 ? 223  PRO A CA  1 
ATOM   1803  C  C   . PRO A 1 223  ? 78.767  68.117  119.067 1.00 120.51 ? 223  PRO A C   1 
ATOM   1804  O  O   . PRO A 1 223  ? 77.856  67.841  118.277 1.00 128.26 ? 223  PRO A O   1 
ATOM   1805  C  CB  . PRO A 1 223  ? 78.102  67.661  121.454 1.00 121.30 ? 223  PRO A CB  1 
ATOM   1806  C  CG  . PRO A 1 223  ? 78.885  67.341  122.654 1.00 114.72 ? 223  PRO A CG  1 
ATOM   1807  C  CD  . PRO A 1 223  ? 80.298  67.641  122.272 1.00 116.36 ? 223  PRO A CD  1 
ATOM   1808  N  N   . TYR A 1 224  ? 79.561  69.172  118.888 1.00 115.40 ? 224  TYR A N   1 
ATOM   1809  C  CA  . TYR A 1 224  ? 79.396  70.099  117.774 1.00 108.06 ? 224  TYR A CA  1 
ATOM   1810  C  C   . TYR A 1 224  ? 80.297  69.806  116.579 1.00 116.34 ? 224  TYR A C   1 
ATOM   1811  O  O   . TYR A 1 224  ? 80.181  70.493  115.560 1.00 119.34 ? 224  TYR A O   1 
ATOM   1812  C  CB  . TYR A 1 224  ? 79.616  71.542  118.242 1.00 98.50  ? 224  TYR A CB  1 
ATOM   1813  C  CG  . TYR A 1 224  ? 78.892  71.874  119.523 1.00 114.49 ? 224  TYR A CG  1 
ATOM   1814  C  CD1 . TYR A 1 224  ? 77.508  71.958  119.553 1.00 123.66 ? 224  TYR A CD1 1 
ATOM   1815  C  CD2 . TYR A 1 224  ? 79.590  72.127  120.696 1.00 127.38 ? 224  TYR A CD2 1 
ATOM   1816  C  CE1 . TYR A 1 224  ? 76.835  72.265  120.718 1.00 133.65 ? 224  TYR A CE1 1 
ATOM   1817  C  CE2 . TYR A 1 224  ? 78.925  72.439  121.866 1.00 130.96 ? 224  TYR A CE2 1 
ATOM   1818  C  CZ  . TYR A 1 224  ? 77.548  72.507  121.871 1.00 137.36 ? 224  TYR A CZ  1 
ATOM   1819  O  OH  . TYR A 1 224  ? 76.880  72.813  123.034 1.00 138.48 ? 224  TYR A OH  1 
ATOM   1820  N  N   . LEU A 1 225  ? 81.179  68.812  116.665 1.00 116.23 ? 225  LEU A N   1 
ATOM   1821  C  CA  . LEU A 1 225  ? 82.142  68.557  115.603 1.00 108.33 ? 225  LEU A CA  1 
ATOM   1822  C  C   . LEU A 1 225  ? 82.039  67.171  114.984 1.00 117.65 ? 225  LEU A C   1 
ATOM   1823  O  O   . LEU A 1 225  ? 82.761  66.889  114.020 1.00 123.75 ? 225  LEU A O   1 
ATOM   1824  C  CB  . LEU A 1 225  ? 83.573  68.777  116.115 1.00 114.08 ? 225  LEU A CB  1 
ATOM   1825  C  CG  . LEU A 1 225  ? 83.880  70.189  116.612 1.00 108.58 ? 225  LEU A CG  1 
ATOM   1826  C  CD1 . LEU A 1 225  ? 85.221  70.224  117.328 1.00 102.28 ? 225  LEU A CD1 1 
ATOM   1827  C  CD2 . LEU A 1 225  ? 83.853  71.174  115.450 1.00 101.27 ? 225  LEU A CD2 1 
ATOM   1828  N  N   . CYS A 1 226  ? 81.170  66.298  115.495 1.00 123.94 ? 226  CYS A N   1 
ATOM   1829  C  CA  . CYS A 1 226  ? 81.093  64.947  114.949 1.00 143.03 ? 226  CYS A CA  1 
ATOM   1830  C  C   . CYS A 1 226  ? 80.434  64.937  113.573 1.00 141.56 ? 226  CYS A C   1 
ATOM   1831  O  O   . CYS A 1 226  ? 80.923  64.276  112.650 1.00 135.53 ? 226  CYS A O   1 
ATOM   1832  C  CB  . CYS A 1 226  ? 80.327  64.032  115.905 1.00 147.06 ? 226  CYS A CB  1 
ATOM   1833  S  SG  . CYS A 1 226  ? 81.138  63.725  117.490 1.00 154.11 ? 226  CYS A SG  1 
ATOM   1834  N  N   . ASP A 1 227  ? 79.337  65.672  113.413 1.00 138.18 ? 227  ASP A N   1 
ATOM   1835  C  CA  . ASP A 1 227  ? 78.494  65.568  112.228 1.00 146.09 ? 227  ASP A CA  1 
ATOM   1836  C  C   . ASP A 1 227  ? 78.912  66.487  111.089 1.00 140.32 ? 227  ASP A C   1 
ATOM   1837  O  O   . ASP A 1 227  ? 78.327  66.405  110.004 1.00 141.07 ? 227  ASP A O   1 
ATOM   1838  C  CB  . ASP A 1 227  ? 77.039  65.860  112.596 1.00 150.14 ? 227  ASP A CB  1 
ATOM   1839  C  CG  . ASP A 1 227  ? 76.444  64.788  113.482 1.00 161.16 ? 227  ASP A CG  1 
ATOM   1840  O  OD1 . ASP A 1 227  ? 77.157  63.814  113.794 1.00 163.10 ? 227  ASP A OD1 1 
ATOM   1841  O  OD2 . ASP A 1 227  ? 75.261  64.917  113.866 1.00 163.75 ? 227  ASP A OD2 1 
ATOM   1842  N  N   . ASP A 1 228  ? 79.899  67.353  111.291 1.00 133.51 ? 228  ASP A N   1 
ATOM   1843  C  CA  . ASP A 1 228  ? 80.291  68.329  110.285 1.00 124.29 ? 228  ASP A CA  1 
ATOM   1844  C  C   . ASP A 1 228  ? 81.747  68.142  109.874 1.00 103.81 ? 228  ASP A C   1 
ATOM   1845  O  O   . ASP A 1 228  ? 82.619  67.964  110.729 1.00 109.75 ? 228  ASP A O   1 
ATOM   1846  C  CB  . ASP A 1 228  ? 80.073  69.757  110.810 1.00 127.89 ? 228  ASP A CB  1 
ATOM   1847  C  CG  . ASP A 1 228  ? 78.623  70.029  111.175 1.00 141.76 ? 228  ASP A CG  1 
ATOM   1848  O  OD1 . ASP A 1 228  ? 78.319  70.057  112.386 1.00 137.77 ? 228  ASP A OD1 1 
ATOM   1849  O  OD2 . ASP A 1 228  ? 77.787  70.195  110.263 1.00 136.41 ? 228  ASP A OD2 1 
ATOM   1850  N  N   . GLU A 1 229  ? 82.002  68.208  108.556 1.00 96.13  ? 229  GLU A N   1 
ATOM   1851  C  CA  . GLU A 1 229  ? 83.307  67.918  107.964 1.00 99.20  ? 229  GLU A CA  1 
ATOM   1852  C  C   . GLU A 1 229  ? 84.208  69.142  107.911 1.00 88.95  ? 229  GLU A C   1 
ATOM   1853  O  O   . GLU A 1 229  ? 85.433  68.985  107.856 1.00 94.80  ? 229  GLU A O   1 
ATOM   1854  C  CB  . GLU A 1 229  ? 83.121  67.435  106.508 1.00 113.30 ? 229  GLU A CB  1 
ATOM   1855  C  CG  . GLU A 1 229  ? 82.393  66.097  106.203 1.00 125.61 ? 229  GLU A CG  1 
ATOM   1856  C  CD  . GLU A 1 229  ? 83.210  64.866  106.587 1.00 145.49 ? 229  GLU A CD  1 
ATOM   1857  O  OE1 . GLU A 1 229  ? 82.902  64.204  107.601 1.00 133.70 ? 229  GLU A OE1 1 
ATOM   1858  O  OE2 . GLU A 1 229  ? 84.123  64.519  105.807 1.00 142.88 ? 229  GLU A OE2 1 
ATOM   1859  N  N   . PHE A 1 230  ? 83.639  70.344  107.990 1.00 82.21  ? 230  PHE A N   1 
ATOM   1860  C  CA  . PHE A 1 230  ? 84.379  71.591  107.851 1.00 73.79  ? 230  PHE A CA  1 
ATOM   1861  C  C   . PHE A 1 230  ? 84.170  72.487  109.067 1.00 73.43  ? 230  PHE A C   1 
ATOM   1862  O  O   . PHE A 1 230  ? 83.212  72.326  109.829 1.00 90.17  ? 230  PHE A O   1 
ATOM   1863  C  CB  . PHE A 1 230  ? 83.992  72.345  106.577 1.00 76.08  ? 230  PHE A CB  1 
ATOM   1864  C  CG  . PHE A 1 230  ? 84.336  71.609  105.316 1.00 77.51  ? 230  PHE A CG  1 
ATOM   1865  C  CD1 . PHE A 1 230  ? 83.435  70.729  104.749 1.00 91.49  ? 230  PHE A CD1 1 
ATOM   1866  C  CD2 . PHE A 1 230  ? 85.566  71.795  104.701 1.00 85.80  ? 230  PHE A CD2 1 
ATOM   1867  C  CE1 . PHE A 1 230  ? 83.748  70.043  103.589 1.00 92.32  ? 230  PHE A CE1 1 
ATOM   1868  C  CE2 . PHE A 1 230  ? 85.884  71.112  103.539 1.00 94.82  ? 230  PHE A CE2 1 
ATOM   1869  C  CZ  . PHE A 1 230  ? 84.974  70.236  102.983 1.00 97.21  ? 230  PHE A CZ  1 
ATOM   1870  N  N   . ILE A 1 231  ? 85.069  73.455  109.226 1.00 63.77  ? 231  ILE A N   1 
ATOM   1871  C  CA  . ILE A 1 231  ? 84.924  74.484  110.246 1.00 64.05  ? 231  ILE A CA  1 
ATOM   1872  C  C   . ILE A 1 231  ? 85.295  75.814  109.598 1.00 74.63  ? 231  ILE A C   1 
ATOM   1873  O  O   . ILE A 1 231  ? 86.060  75.862  108.630 1.00 94.49  ? 231  ILE A O   1 
ATOM   1874  C  CB  . ILE A 1 231  ? 85.773  74.192  111.500 1.00 65.45  ? 231  ILE A CB  1 
ATOM   1875  C  CG1 . ILE A 1 231  ? 85.205  74.937  112.707 1.00 79.64  ? 231  ILE A CG1 1 
ATOM   1876  C  CG2 . ILE A 1 231  ? 87.220  74.595  111.282 1.00 67.81  ? 231  ILE A CG2 1 
ATOM   1877  C  CD1 . ILE A 1 231  ? 85.757  74.459  114.031 1.00 90.30  ? 231  ILE A CD1 1 
ATOM   1878  N  N   . VAL A 1 232  ? 84.737  76.900  110.130 1.00 64.36  ? 232  VAL A N   1 
ATOM   1879  C  CA  . VAL A 1 232  ? 84.723  78.189  109.451 1.00 57.64  ? 232  VAL A CA  1 
ATOM   1880  C  C   . VAL A 1 232  ? 85.366  79.251  110.333 1.00 56.36  ? 232  VAL A C   1 
ATOM   1881  O  O   . VAL A 1 232  ? 85.292  79.190  111.563 1.00 78.32  ? 232  VAL A O   1 
ATOM   1882  C  CB  . VAL A 1 232  ? 83.272  78.572  109.074 1.00 64.88  ? 232  VAL A CB  1 
ATOM   1883  C  CG1 . VAL A 1 232  ? 83.197  79.963  108.497 1.00 57.18  ? 232  VAL A CG1 1 
ATOM   1884  C  CG2 . VAL A 1 232  ? 82.716  77.575  108.073 1.00 63.11  ? 232  VAL A CG2 1 
ATOM   1885  N  N   . SER A 1 233  ? 86.005  80.231  109.691 1.00 50.52  ? 233  SER A N   1 
ATOM   1886  C  CA  . SER A 1 233  ? 86.454  81.449  110.353 1.00 47.73  ? 233  SER A CA  1 
ATOM   1887  C  C   . SER A 1 233  ? 86.022  82.660  109.541 1.00 60.21  ? 233  SER A C   1 
ATOM   1888  O  O   . SER A 1 233  ? 86.247  82.708  108.328 1.00 74.45  ? 233  SER A O   1 
ATOM   1889  C  CB  . SER A 1 233  ? 87.976  81.459  110.529 1.00 54.03  ? 233  SER A CB  1 
ATOM   1890  O  OG  . SER A 1 233  ? 88.449  82.775  110.762 1.00 60.35  ? 233  SER A OG  1 
ATOM   1891  N  N   . VAL A 1 234  ? 85.413  83.636  110.213 1.00 63.31  ? 234  VAL A N   1 
ATOM   1892  C  CA  . VAL A 1 234  ? 84.938  84.864  109.583 1.00 54.69  ? 234  VAL A CA  1 
ATOM   1893  C  C   . VAL A 1 234  ? 85.951  85.978  109.809 1.00 67.45  ? 234  VAL A C   1 
ATOM   1894  O  O   . VAL A 1 234  ? 86.467  86.151  110.921 1.00 75.24  ? 234  VAL A O   1 
ATOM   1895  C  CB  . VAL A 1 234  ? 83.554  85.267  110.129 1.00 37.72  ? 234  VAL A CB  1 
ATOM   1896  C  CG1 . VAL A 1 234  ? 82.968  86.411  109.312 1.00 57.09  ? 234  VAL A CG1 1 
ATOM   1897  C  CG2 . VAL A 1 234  ? 82.612  84.068  110.127 1.00 51.56  ? 234  VAL A CG2 1 
ATOM   1898  N  N   . ALA A 1 235  ? 86.229  86.742  108.755 1.00 53.24  ? 235  ALA A N   1 
ATOM   1899  C  CA  . ALA A 1 235  ? 87.168  87.848  108.837 1.00 54.23  ? 235  ALA A CA  1 
ATOM   1900  C  C   . ALA A 1 235  ? 86.744  88.918  107.839 1.00 66.30  ? 235  ALA A C   1 
ATOM   1901  O  O   . ALA A 1 235  ? 85.747  88.773  107.126 1.00 73.67  ? 235  ALA A O   1 
ATOM   1902  C  CB  . ALA A 1 235  ? 88.603  87.378  108.581 1.00 68.29  ? 235  ALA A CB  1 
ATOM   1903  N  N   . SER A 1 236  ? 87.519  89.996  107.787 1.00 63.15  ? 236  SER A N   1 
ATOM   1904  C  CA  . SER A 1 236  ? 87.212  91.140  106.948 1.00 60.96  ? 236  SER A CA  1 
ATOM   1905  C  C   . SER A 1 236  ? 88.050  91.115  105.672 1.00 66.59  ? 236  SER A C   1 
ATOM   1906  O  O   . SER A 1 236  ? 88.898  90.246  105.458 1.00 81.47  ? 236  SER A O   1 
ATOM   1907  C  CB  . SER A 1 236  ? 87.430  92.442  107.723 1.00 69.81  ? 236  SER A CB  1 
ATOM   1908  O  OG  . SER A 1 236  ? 88.702  92.458  108.344 1.00 74.61  ? 236  SER A OG  1 
ATOM   1909  N  N   . TYR A 1 237  ? 87.797  92.104  104.814 1.00 65.61  ? 237  TYR A N   1 
ATOM   1910  C  CA  . TYR A 1 237  ? 88.546  92.272  103.573 1.00 63.27  ? 237  TYR A CA  1 
ATOM   1911  C  C   . TYR A 1 237  ? 90.004  92.666  103.822 1.00 61.91  ? 237  TYR A C   1 
ATOM   1912  O  O   . TYR A 1 237  ? 90.895  92.300  103.036 1.00 69.97  ? 237  TYR A O   1 
ATOM   1913  C  CB  . TYR A 1 237  ? 87.813  93.299  102.707 1.00 50.98  ? 237  TYR A CB  1 
ATOM   1914  C  CG  . TYR A 1 237  ? 88.646  93.989  101.659 1.00 63.11  ? 237  TYR A CG  1 
ATOM   1915  C  CD1 . TYR A 1 237  ? 88.782  93.460  100.386 1.00 61.38  ? 237  TYR A CD1 1 
ATOM   1916  C  CD2 . TYR A 1 237  ? 89.258  95.204  101.933 1.00 87.73  ? 237  TYR A CD2 1 
ATOM   1917  C  CE1 . TYR A 1 237  ? 89.537  94.108  99.425  1.00 67.85  ? 237  TYR A CE1 1 
ATOM   1918  C  CE2 . TYR A 1 237  ? 90.011  95.857  100.983 1.00 73.52  ? 237  TYR A CE2 1 
ATOM   1919  C  CZ  . TYR A 1 237  ? 90.146  95.308  99.729  1.00 61.66  ? 237  TYR A CZ  1 
ATOM   1920  O  OH  . TYR A 1 237  ? 90.902  95.958  98.780  1.00 70.62  ? 237  TYR A OH  1 
ATOM   1921  N  N   . GLU A 1 238  ? 90.273  93.376  104.921 1.00 64.71  ? 238  GLU A N   1 
ATOM   1922  C  CA  . GLU A 1 238  ? 91.643  93.789  105.208 1.00 64.50  ? 238  GLU A CA  1 
ATOM   1923  C  C   . GLU A 1 238  ? 92.533  92.599  105.532 1.00 71.37  ? 238  GLU A C   1 
ATOM   1924  O  O   . GLU A 1 238  ? 93.725  92.616  105.208 1.00 97.22  ? 238  GLU A O   1 
ATOM   1925  C  CB  . GLU A 1 238  ? 91.667  94.793  106.362 1.00 74.34  ? 238  GLU A CB  1 
ATOM   1926  C  CG  . GLU A 1 238  ? 91.368  96.220  105.945 1.00 90.00  ? 238  GLU A CG  1 
ATOM   1927  C  CD  . GLU A 1 238  ? 89.890  96.540  105.991 1.00 97.16  ? 238  GLU A CD  1 
ATOM   1928  O  OE1 . GLU A 1 238  ? 89.094  95.628  106.297 1.00 91.77  ? 238  GLU A OE1 1 
ATOM   1929  O  OE2 . GLU A 1 238  ? 89.524  97.700  105.711 1.00 91.28  ? 238  GLU A OE2 1 
ATOM   1930  N  N   . CYS A 1 239  ? 91.977  91.559  106.154 1.00 61.78  ? 239  CYS A N   1 
ATOM   1931  C  CA  . CYS A 1 239  ? 92.764  90.360  106.421 1.00 58.12  ? 239  CYS A CA  1 
ATOM   1932  C  C   . CYS A 1 239  ? 93.237  89.721  105.121 1.00 65.10  ? 239  CYS A C   1 
ATOM   1933  O  O   . CYS A 1 239  ? 94.406  89.323  104.992 1.00 76.31  ? 239  CYS A O   1 
ATOM   1934  C  CB  . CYS A 1 239  ? 91.927  89.369  107.232 1.00 62.37  ? 239  CYS A CB  1 
ATOM   1935  S  SG  . CYS A 1 239  ? 91.349  90.009  108.822 1.00 87.39  ? 239  CYS A SG  1 
ATOM   1936  N  N   . PHE A 1 240  ? 92.346  89.649  104.131 1.00 53.61  ? 240  PHE A N   1 
ATOM   1937  C  CA  . PHE A 1 240  ? 92.723  89.112  102.829 1.00 46.92  ? 240  PHE A CA  1 
ATOM   1938  C  C   . PHE A 1 240  ? 93.778  89.969  102.139 1.00 62.96  ? 240  PHE A C   1 
ATOM   1939  O  O   . PHE A 1 240  ? 94.740  89.436  101.559 1.00 74.09  ? 240  PHE A O   1 
ATOM   1940  C  CB  . PHE A 1 240  ? 91.490  88.981  101.943 1.00 51.47  ? 240  PHE A CB  1 
ATOM   1941  C  CG  . PHE A 1 240  ? 91.763  88.263  100.668 1.00 59.87  ? 240  PHE A CG  1 
ATOM   1942  C  CD1 . PHE A 1 240  ? 91.999  86.903  100.670 1.00 63.31  ? 240  PHE A CD1 1 
ATOM   1943  C  CD2 . PHE A 1 240  ? 91.822  88.952  99.470  1.00 61.80  ? 240  PHE A CD2 1 
ATOM   1944  C  CE1 . PHE A 1 240  ? 92.273  86.234  99.499  1.00 49.33  ? 240  PHE A CE1 1 
ATOM   1945  C  CE2 . PHE A 1 240  ? 92.094  88.289  98.292  1.00 69.88  ? 240  PHE A CE2 1 
ATOM   1946  C  CZ  . PHE A 1 240  ? 92.319  86.927  98.306  1.00 72.26  ? 240  PHE A CZ  1 
ATOM   1947  N  N   . ILE A 1 241  ? 93.619  91.297  102.176 1.00 63.14  ? 241  ILE A N   1 
ATOM   1948  C  CA  . ILE A 1 241  ? 94.635  92.145  101.555 1.00 53.23  ? 241  ILE A CA  1 
ATOM   1949  C  C   . ILE A 1 241  ? 95.982  91.960  102.242 1.00 60.44  ? 241  ILE A C   1 
ATOM   1950  O  O   . ILE A 1 241  ? 97.035  91.948  101.588 1.00 69.95  ? 241  ILE A O   1 
ATOM   1951  C  CB  . ILE A 1 241  ? 94.189  93.621  101.566 1.00 55.38  ? 241  ILE A CB  1 
ATOM   1952  C  CG1 . ILE A 1 241  ? 93.034  93.820  100.588 1.00 68.23  ? 241  ILE A CG1 1 
ATOM   1953  C  CG2 . ILE A 1 241  ? 95.346  94.539  101.199 1.00 80.74  ? 241  ILE A CG2 1 
ATOM   1954  C  CD1 . ILE A 1 241  ? 93.306  93.262  99.207  1.00 55.44  ? 241  ILE A CD1 1 
ATOM   1955  N  N   . MET A 1 242  ? 95.973  91.785  103.564 1.00 52.16  ? 242  MET A N   1 
ATOM   1956  C  CA  . MET A 1 242  ? 97.224  91.571  104.279 1.00 47.25  ? 242  MET A CA  1 
ATOM   1957  C  C   . MET A 1 242  ? 97.885  90.257  103.871 1.00 58.76  ? 242  MET A C   1 
ATOM   1958  O  O   . MET A 1 242  ? 99.113  90.194  103.721 1.00 74.16  ? 242  MET A O   1 
ATOM   1959  C  CB  . MET A 1 242  ? 96.980  91.613  105.788 1.00 54.16  ? 242  MET A CB  1 
ATOM   1960  C  CG  . MET A 1 242  ? 98.184  91.193  106.614 1.00 71.75  ? 242  MET A CG  1 
ATOM   1961  S  SD  . MET A 1 242  ? 97.900  91.346  108.385 1.00 81.27  ? 242  MET A SD  1 
ATOM   1962  C  CE  . MET A 1 242  ? 96.783  89.975  108.652 1.00 62.51  ? 242  MET A CE  1 
ATOM   1963  N  N   . ILE A 1 243  ? 97.087  89.202  103.662 1.00 61.87  ? 243  ILE A N   1 
ATOM   1964  C  CA  . ILE A 1 243  ? 97.642  87.936  103.174 1.00 52.30  ? 243  ILE A CA  1 
ATOM   1965  C  C   . ILE A 1 243  ? 98.308  88.122  101.811 1.00 52.46  ? 243  ILE A C   1 
ATOM   1966  O  O   . ILE A 1 243  ? 99.420  87.624  101.559 1.00 59.37  ? 243  ILE A O   1 
ATOM   1967  C  CB  . ILE A 1 243  ? 96.537  86.866  103.096 1.00 46.64  ? 243  ILE A CB  1 
ATOM   1968  C  CG1 . ILE A 1 243  ? 96.065  86.448  104.488 1.00 61.23  ? 243  ILE A CG1 1 
ATOM   1969  C  CG2 . ILE A 1 243  ? 97.024  85.646  102.315 1.00 50.99  ? 243  ILE A CG2 1 
ATOM   1970  C  CD1 . ILE A 1 243  ? 94.908  85.463  104.457 1.00 63.80  ? 243  ILE A CD1 1 
ATOM   1971  N  N   . LYS A 1 244  ? 97.627  88.835  100.907 1.00 60.53  ? 244  LYS A N   1 
ATOM   1972  C  CA  . LYS A 1 244  ? 98.190  89.067  99.577  1.00 57.99  ? 244  LYS A CA  1 
ATOM   1973  C  C   . LYS A 1 244  ? 99.510  89.829  99.669  1.00 61.93  ? 244  LYS A C   1 
ATOM   1974  O  O   . LYS A 1 244  ? 100.494 89.500  98.981  1.00 71.81  ? 244  LYS A O   1 
ATOM   1975  C  CB  . LYS A 1 244  ? 97.176  89.817  98.710  1.00 54.31  ? 244  LYS A CB  1 
ATOM   1976  C  CG  . LYS A 1 244  ? 97.557  89.969  97.245  1.00 72.23  ? 244  LYS A CG  1 
ATOM   1977  C  CD  . LYS A 1 244  ? 98.299  91.274  97.007  1.00 73.45  ? 244  LYS A CD  1 
ATOM   1978  C  CE  . LYS A 1 244  ? 97.376  92.466  97.167  1.00 68.87  ? 244  LYS A CE  1 
ATOM   1979  N  NZ  . LYS A 1 244  ? 98.101  93.752  96.980  1.00 74.88  ? 244  LYS A NZ  1 
ATOM   1980  N  N   . ASP A 1 245  ? 99.544  90.841  100.540 1.00 64.02  ? 245  ASP A N   1 
ATOM   1981  C  CA  . ASP A 1 245  ? 100.752 91.630  100.742 1.00 46.05  ? 245  ASP A CA  1 
ATOM   1982  C  C   . ASP A 1 245  ? 101.892 90.755  101.245 1.00 52.93  ? 245  ASP A C   1 
ATOM   1983  O  O   . ASP A 1 245  ? 103.044 90.897  100.805 1.00 78.79  ? 245  ASP A O   1 
ATOM   1984  C  CB  . ASP A 1 245  ? 100.458 92.739  101.752 1.00 82.37  ? 245  ASP A CB  1 
ATOM   1985  C  CG  . ASP A 1 245  ? 99.856  93.973  101.112 1.00 110.17 ? 245  ASP A CG  1 
ATOM   1986  O  OD1 . ASP A 1 245  ? 99.373  93.871  99.965  1.00 95.99  ? 245  ASP A OD1 1 
ATOM   1987  O  OD2 . ASP A 1 245  ? 99.845  95.038  101.765 1.00 112.41 ? 245  ASP A OD2 1 
ATOM   1988  N  N   . VAL A 1 246  ? 101.580 89.830  102.156 1.00 64.63  ? 246  VAL A N   1 
ATOM   1989  C  CA  . VAL A 1 246  ? 102.597 88.945  102.720 1.00 52.67  ? 246  VAL A CA  1 
ATOM   1990  C  C   . VAL A 1 246  ? 103.211 88.057  101.640 1.00 57.96  ? 246  VAL A C   1 
ATOM   1991  O  O   . VAL A 1 246  ? 104.441 87.924  101.548 1.00 69.60  ? 246  VAL A O   1 
ATOM   1992  C  CB  . VAL A 1 246  ? 101.994 88.111  103.866 1.00 44.36  ? 246  VAL A CB  1 
ATOM   1993  C  CG1 . VAL A 1 246  ? 102.865 86.899  104.170 1.00 56.75  ? 246  VAL A CG1 1 
ATOM   1994  C  CG2 . VAL A 1 246  ? 101.816 88.973  105.113 1.00 52.67  ? 246  VAL A CG2 1 
ATOM   1995  N  N   . PHE A 1 247  ? 102.370 87.448  100.792 1.00 53.54  ? 247  PHE A N   1 
ATOM   1996  C  CA  . PHE A 1 247  ? 102.928 86.655  99.690  1.00 44.18  ? 247  PHE A CA  1 
ATOM   1997  C  C   . PHE A 1 247  ? 103.808 87.462  98.745  1.00 51.31  ? 247  PHE A C   1 
ATOM   1998  O  O   . PHE A 1 247  ? 104.893 86.997  98.364  1.00 57.92  ? 247  PHE A O   1 
ATOM   1999  C  CB  . PHE A 1 247  ? 101.843 85.944  98.884  1.00 49.64  ? 247  PHE A CB  1 
ATOM   2000  C  CG  . PHE A 1 247  ? 101.477 84.601  99.421  1.00 55.71  ? 247  PHE A CG  1 
ATOM   2001  C  CD1 . PHE A 1 247  ? 102.161 83.486  98.961  1.00 57.76  ? 247  PHE A CD1 1 
ATOM   2002  C  CD2 . PHE A 1 247  ? 100.489 84.432  100.367 1.00 75.06  ? 247  PHE A CD2 1 
ATOM   2003  C  CE1 . PHE A 1 247  ? 101.864 82.227  99.422  1.00 50.35  ? 247  PHE A CE1 1 
ATOM   2004  C  CE2 . PHE A 1 247  ? 100.180 83.164  100.834 1.00 85.71  ? 247  PHE A CE2 1 
ATOM   2005  C  CZ  . PHE A 1 247  ? 100.873 82.062  100.360 1.00 64.59  ? 247  PHE A CZ  1 
ATOM   2006  N  N   . ILE A 1 248  ? 103.378 88.661  98.351  1.00 50.81  ? 248  ILE A N   1 
ATOM   2007  C  CA  . ILE A 1 248  ? 104.216 89.415  97.416  1.00 44.22  ? 248  ILE A CA  1 
ATOM   2008  C  C   . ILE A 1 248  ? 105.555 89.772  98.054  1.00 46.80  ? 248  ILE A C   1 
ATOM   2009  O  O   . ILE A 1 248  ? 106.619 89.635  97.427  1.00 60.10  ? 248  ILE A O   1 
ATOM   2010  C  CB  . ILE A 1 248  ? 103.479 90.656  96.884  1.00 48.68  ? 248  ILE A CB  1 
ATOM   2011  C  CG1 . ILE A 1 248  ? 102.367 90.218  95.932  1.00 53.06  ? 248  ILE A CG1 1 
ATOM   2012  C  CG2 . ILE A 1 248  ? 104.448 91.571  96.151  1.00 56.06  ? 248  ILE A CG2 1 
ATOM   2013  C  CD1 . ILE A 1 248  ? 101.561 91.357  95.363  1.00 77.81  ? 248  ILE A CD1 1 
ATOM   2014  N  N   . GLU A 1 249  ? 105.530 90.218  99.314  1.00 48.07  ? 249  GLU A N   1 
ATOM   2015  C  CA  . GLU A 1 249  ? 106.778 90.585  99.974  1.00 44.14  ? 249  GLU A CA  1 
ATOM   2016  C  C   . GLU A 1 249  ? 107.724 89.392  100.064 1.00 41.68  ? 249  GLU A C   1 
ATOM   2017  O  O   . GLU A 1 249  ? 108.924 89.515  99.774  1.00 48.05  ? 249  GLU A O   1 
ATOM   2018  C  CB  . GLU A 1 249  ? 106.482 91.150  101.362 1.00 58.51  ? 249  GLU A CB  1 
ATOM   2019  C  CG  . GLU A 1 249  ? 106.126 92.625  101.347 1.00 74.77  ? 249  GLU A CG  1 
ATOM   2020  C  CD  . GLU A 1 249  ? 105.629 93.121  102.686 1.00 76.87  ? 249  GLU A CD  1 
ATOM   2021  O  OE1 . GLU A 1 249  ? 106.337 93.931  103.320 1.00 81.97  ? 249  GLU A OE1 1 
ATOM   2022  O  OE2 . GLU A 1 249  ? 104.533 92.697  103.108 1.00 80.16  ? 249  GLU A OE2 1 
ATOM   2023  N  N   . ARG A 1 250  ? 107.198 88.223  100.439 1.00 48.24  ? 250  ARG A N   1 
ATOM   2024  C  CA  . ARG A 1 250  ? 108.060 87.055  100.592 1.00 47.95  ? 250  ARG A CA  1 
ATOM   2025  C  C   . ARG A 1 250  ? 108.634 86.593  99.258  1.00 52.31  ? 250  ARG A C   1 
ATOM   2026  O  O   . ARG A 1 250  ? 109.813 86.216  99.183  1.00 63.02  ? 250  ARG A O   1 
ATOM   2027  C  CB  . ARG A 1 250  ? 107.283 85.922  101.253 1.00 45.95  ? 250  ARG A CB  1 
ATOM   2028  C  CG  . ARG A 1 250  ? 106.980 86.203  102.696 1.00 52.70  ? 250  ARG A CG  1 
ATOM   2029  C  CD  . ARG A 1 250  ? 106.498 84.975  103.415 1.00 49.62  ? 250  ARG A CD  1 
ATOM   2030  N  NE  . ARG A 1 250  ? 106.024 85.323  104.745 1.00 46.35  ? 250  ARG A NE  1 
ATOM   2031  C  CZ  . ARG A 1 250  ? 105.701 84.435  105.676 1.00 51.83  ? 250  ARG A CZ  1 
ATOM   2032  N  NH1 . ARG A 1 250  ? 105.806 83.138  105.423 1.00 62.00  ? 250  ARG A NH1 1 
ATOM   2033  N  NH2 . ARG A 1 250  ? 105.281 84.844  106.864 1.00 51.17  ? 250  ARG A NH2 1 
ATOM   2034  N  N   . TYR A 1 251  ? 107.834 86.652  98.189  1.00 50.40  ? 251  TYR A N   1 
ATOM   2035  C  CA  . TYR A 1 251  ? 108.350 86.279  96.874  1.00 46.69  ? 251  TYR A CA  1 
ATOM   2036  C  C   . TYR A 1 251  ? 109.494 87.194  96.456  1.00 45.78  ? 251  TYR A C   1 
ATOM   2037  O  O   . TYR A 1 251  ? 110.556 86.724  96.019  1.00 52.04  ? 251  TYR A O   1 
ATOM   2038  C  CB  . TYR A 1 251  ? 107.240 86.315  95.824  1.00 48.26  ? 251  TYR A CB  1 
ATOM   2039  C  CG  . TYR A 1 251  ? 107.777 86.083  94.428  1.00 55.19  ? 251  TYR A CG  1 
ATOM   2040  C  CD1 . TYR A 1 251  ? 108.032 87.138  93.564  1.00 51.75  ? 251  TYR A CD1 1 
ATOM   2041  C  CD2 . TYR A 1 251  ? 108.054 84.796  93.986  1.00 70.46  ? 251  TYR A CD2 1 
ATOM   2042  C  CE1 . TYR A 1 251  ? 108.537 86.914  92.289  1.00 51.45  ? 251  TYR A CE1 1 
ATOM   2043  C  CE2 . TYR A 1 251  ? 108.557 84.564  92.720  1.00 57.72  ? 251  TYR A CE2 1 
ATOM   2044  C  CZ  . TYR A 1 251  ? 108.797 85.622  91.875  1.00 45.82  ? 251  TYR A CZ  1 
ATOM   2045  O  OH  . TYR A 1 251  ? 109.304 85.385  90.616  1.00 48.51  ? 251  TYR A OH  1 
ATOM   2046  N  N   . ASN A 1 252  ? 109.293 88.509  96.590  1.00 46.07  ? 252  ASN A N   1 
ATOM   2047  C  CA  . ASN A 1 252  ? 110.336 89.450  96.192  1.00 35.59  ? 252  ASN A CA  1 
ATOM   2048  C  C   . ASN A 1 252  ? 111.617 89.215  96.986  1.00 40.57  ? 252  ASN A C   1 
ATOM   2049  O  O   . ASN A 1 252  ? 112.719 89.167  96.413  1.00 52.38  ? 252  ASN A O   1 
ATOM   2050  C  CB  . ASN A 1 252  ? 109.839 90.883  96.400  1.00 47.44  ? 252  ASN A CB  1 
ATOM   2051  C  CG  . ASN A 1 252  ? 108.790 91.295  95.384  1.00 57.40  ? 252  ASN A CG  1 
ATOM   2052  O  OD1 . ASN A 1 252  ? 108.711 90.734  94.293  1.00 59.52  ? 252  ASN A OD1 1 
ATOM   2053  N  ND2 . ASN A 1 252  ? 107.967 92.273  95.747  1.00 53.76  ? 252  ASN A ND2 1 
ATOM   2054  N  N   . THR A 1 253  ? 111.486 89.033  98.305  1.00 41.08  ? 253  THR A N   1 
ATOM   2055  C  CA  . THR A 1 253  ? 112.656 88.859  99.161  1.00 41.71  ? 253  THR A CA  1 
ATOM   2056  C  C   . THR A 1 253  ? 113.433 87.597  98.797  1.00 37.83  ? 253  THR A C   1 
ATOM   2057  O  O   . THR A 1 253  ? 114.665 87.632  98.634  1.00 50.34  ? 253  THR A O   1 
ATOM   2058  C  CB  . THR A 1 253  ? 112.221 88.815  100.625 1.00 42.64  ? 253  THR A CB  1 
ATOM   2059  O  OG1 . THR A 1 253  ? 111.518 90.019  100.954 1.00 58.55  ? 253  THR A OG1 1 
ATOM   2060  C  CG2 . THR A 1 253  ? 113.430 88.680  101.536 1.00 53.38  ? 253  THR A CG2 1 
ATOM   2061  N  N   . TRP A 1 254  ? 112.721 86.472  98.634  1.00 40.44  ? 254  TRP A N   1 
ATOM   2062  C  CA  . TRP A 1 254  ? 113.395 85.226  98.285  1.00 38.92  ? 254  TRP A CA  1 
ATOM   2063  C  C   . TRP A 1 254  ? 114.103 85.333  96.945  1.00 43.21  ? 254  TRP A C   1 
ATOM   2064  O  O   . TRP A 1 254  ? 115.247 84.879  96.802  1.00 53.89  ? 254  TRP A O   1 
ATOM   2065  C  CB  . TRP A 1 254  ? 112.394 84.070  98.236  1.00 52.49  ? 254  TRP A CB  1 
ATOM   2066  C  CG  . TRP A 1 254  ? 113.048 82.714  98.189  1.00 59.78  ? 254  TRP A CG  1 
ATOM   2067  C  CD1 . TRP A 1 254  ? 113.670 82.148  97.115  1.00 65.61  ? 254  TRP A CD1 1 
ATOM   2068  C  CD2 . TRP A 1 254  ? 113.099 81.738  99.239  1.00 58.50  ? 254  TRP A CD2 1 
ATOM   2069  N  NE1 . TRP A 1 254  ? 114.134 80.896  97.440  1.00 64.07  ? 254  TRP A NE1 1 
ATOM   2070  C  CE2 . TRP A 1 254  ? 113.792 80.619  98.736  1.00 49.83  ? 254  TRP A CE2 1 
ATOM   2071  C  CE3 . TRP A 1 254  ? 112.638 81.706  100.559 1.00 71.60  ? 254  TRP A CE3 1 
ATOM   2072  C  CZ2 . TRP A 1 254  ? 114.035 79.482  99.504  1.00 67.69  ? 254  TRP A CZ2 1 
ATOM   2073  C  CZ3 . TRP A 1 254  ? 112.881 80.573  101.320 1.00 70.31  ? 254  TRP A CZ3 1 
ATOM   2074  C  CH2 . TRP A 1 254  ? 113.572 79.478  100.790 1.00 69.30  ? 254  TRP A CH2 1 
ATOM   2075  N  N   . GLU A 1 255  ? 113.440 85.920  95.946  1.00 47.61  ? 255  GLU A N   1 
ATOM   2076  C  CA  . GLU A 1 255  ? 114.059 85.996  94.628  1.00 48.97  ? 255  GLU A CA  1 
ATOM   2077  C  C   . GLU A 1 255  ? 115.329 86.839  94.654  1.00 49.17  ? 255  GLU A C   1 
ATOM   2078  O  O   . GLU A 1 255  ? 116.363 86.438  94.090  1.00 66.58  ? 255  GLU A O   1 
ATOM   2079  C  CB  . GLU A 1 255  ? 113.064 86.549  93.611  1.00 41.88  ? 255  GLU A CB  1 
ATOM   2080  C  CG  . GLU A 1 255  ? 113.542 86.393  92.188  1.00 56.13  ? 255  GLU A CG  1 
ATOM   2081  C  CD  . GLU A 1 255  ? 113.522 84.947  91.736  1.00 63.29  ? 255  GLU A CD  1 
ATOM   2082  O  OE1 . GLU A 1 255  ? 114.184 84.630  90.727  1.00 62.57  ? 255  GLU A OE1 1 
ATOM   2083  O  OE2 . GLU A 1 255  ? 112.845 84.126  92.389  1.00 53.69  ? 255  GLU A OE2 1 
ATOM   2084  N  N   . ILE A 1 256  ? 115.285 87.990  95.335  1.00 47.91  ? 256  ILE A N   1 
ATOM   2085  C  CA  . ILE A 1 256  ? 116.464 88.852  95.388  1.00 40.25  ? 256  ILE A CA  1 
ATOM   2086  C  C   . ILE A 1 256  ? 117.623 88.139  96.078  1.00 47.10  ? 256  ILE A C   1 
ATOM   2087  O  O   . ILE A 1 256  ? 118.760 88.134  95.578  1.00 51.78  ? 256  ILE A O   1 
ATOM   2088  C  CB  . ILE A 1 256  ? 116.126 90.175  96.098  1.00 47.73  ? 256  ILE A CB  1 
ATOM   2089  C  CG1 . ILE A 1 256  ? 115.197 91.032  95.235  1.00 51.32  ? 256  ILE A CG1 1 
ATOM   2090  C  CG2 . ILE A 1 256  ? 117.397 90.942  96.448  1.00 47.29  ? 256  ILE A CG2 1 
ATOM   2091  C  CD1 . ILE A 1 256  ? 114.825 92.357  95.871  1.00 45.29  ? 256  ILE A CD1 1 
ATOM   2092  N  N   . CYS A 1 257  ? 117.347 87.485  97.214  1.00 50.93  ? 257  CYS A N   1 
ATOM   2093  C  CA  . CYS A 1 257  ? 118.426 86.805  97.930  1.00 48.04  ? 257  CYS A CA  1 
ATOM   2094  C  C   . CYS A 1 257  ? 119.019 85.661  97.113  1.00 40.99  ? 257  CYS A C   1 
ATOM   2095  O  O   . CYS A 1 257  ? 120.246 85.502  97.057  1.00 64.25  ? 257  CYS A O   1 
ATOM   2096  C  CB  . CYS A 1 257  ? 117.929 86.312  99.288  1.00 42.18  ? 257  CYS A CB  1 
ATOM   2097  S  SG  . CYS A 1 257  ? 117.641 87.650  100.475 1.00 56.67  ? 257  CYS A SG  1 
ATOM   2098  N  N   . ALA A 1 258  ? 118.166 84.857  96.472  1.00 47.85  ? 258  ALA A N   1 
ATOM   2099  C  CA  . ALA A 1 258  ? 118.673 83.720  95.711  1.00 47.64  ? 258  ALA A CA  1 
ATOM   2100  C  C   . ALA A 1 258  ? 119.558 84.178  94.559  1.00 52.09  ? 258  ALA A C   1 
ATOM   2101  O  O   . ALA A 1 258  ? 120.647 83.621  94.335  1.00 60.86  ? 258  ALA A O   1 
ATOM   2102  C  CB  . ALA A 1 258  ? 117.508 82.878  95.191  1.00 56.68  ? 258  ALA A CB  1 
ATOM   2103  N  N   . ARG A 1 259  ? 119.130 85.216  93.834  1.00 56.90  ? 259  ARG A N   1 
ATOM   2104  C  CA  . ARG A 1 259  ? 119.948 85.659  92.711  1.00 49.58  ? 259  ARG A CA  1 
ATOM   2105  C  C   . ARG A 1 259  ? 121.258 86.272  93.190  1.00 51.55  ? 259  ARG A C   1 
ATOM   2106  O  O   . ARG A 1 259  ? 122.308 86.065  92.569  1.00 57.58  ? 259  ARG A O   1 
ATOM   2107  C  CB  . ARG A 1 259  ? 119.163 86.636  91.845  1.00 47.02  ? 259  ARG A CB  1 
ATOM   2108  C  CG  . ARG A 1 259  ? 117.996 85.945  91.197  1.00 60.90  ? 259  ARG A CG  1 
ATOM   2109  C  CD  . ARG A 1 259  ? 117.267 86.788  90.195  1.00 51.72  ? 259  ARG A CD  1 
ATOM   2110  N  NE  . ARG A 1 259  ? 116.315 85.939  89.492  1.00 58.98  ? 259  ARG A NE  1 
ATOM   2111  C  CZ  . ARG A 1 259  ? 116.539 85.381  88.309  1.00 64.19  ? 259  ARG A CZ  1 
ATOM   2112  N  NH1 . ARG A 1 259  ? 117.689 85.590  87.681  1.00 73.45  ? 259  ARG A NH1 1 
ATOM   2113  N  NH2 . ARG A 1 259  ? 115.612 84.616  87.753  1.00 61.15  ? 259  ARG A NH2 1 
ATOM   2114  N  N   . ALA A 1 260  ? 121.225 87.009  94.306  1.00 50.24  ? 260  ALA A N   1 
ATOM   2115  C  CA  . ALA A 1 260  ? 122.463 87.583  94.821  1.00 42.31  ? 260  ALA A CA  1 
ATOM   2116  C  C   . ALA A 1 260  ? 123.451 86.494  95.226  1.00 47.03  ? 260  ALA A C   1 
ATOM   2117  O  O   . ALA A 1 260  ? 124.655 86.610  94.966  1.00 60.46  ? 260  ALA A O   1 
ATOM   2118  C  CB  . ALA A 1 260  ? 122.164 88.502  95.998  1.00 48.65  ? 260  ALA A CB  1 
ATOM   2119  N  N   . TRP A 1 261  ? 122.961 85.424  95.858  1.00 67.51  ? 261  TRP A N   1 
ATOM   2120  C  CA  . TRP A 1 261  ? 123.853 84.352  96.290  1.00 51.55  ? 261  TRP A CA  1 
ATOM   2121  C  C   . TRP A 1 261  ? 124.359 83.505  95.135  1.00 52.32  ? 261  TRP A C   1 
ATOM   2122  O  O   . TRP A 1 261  ? 125.404 82.860  95.268  1.00 62.11  ? 261  TRP A O   1 
ATOM   2123  C  CB  . TRP A 1 261  ? 123.184 83.482  97.351  1.00 57.95  ? 261  TRP A CB  1 
ATOM   2124  C  CG  . TRP A 1 261  ? 123.402 84.057  98.704  1.00 62.03  ? 261  TRP A CG  1 
ATOM   2125  C  CD1 . TRP A 1 261  ? 122.529 84.802  99.436  1.00 52.20  ? 261  TRP A CD1 1 
ATOM   2126  C  CD2 . TRP A 1 261  ? 124.602 83.958  99.482  1.00 47.35  ? 261  TRP A CD2 1 
ATOM   2127  N  NE1 . TRP A 1 261  ? 123.108 85.166  100.630 1.00 51.81  ? 261  TRP A NE1 1 
ATOM   2128  C  CE2 . TRP A 1 261  ? 124.380 84.658  100.681 1.00 50.86  ? 261  TRP A CE2 1 
ATOM   2129  C  CE3 . TRP A 1 261  ? 125.838 83.336  99.282  1.00 57.30  ? 261  TRP A CE3 1 
ATOM   2130  C  CZ2 . TRP A 1 261  ? 125.350 84.755  101.679 1.00 55.09  ? 261  TRP A CZ2 1 
ATOM   2131  C  CZ3 . TRP A 1 261  ? 126.800 83.435  100.273 1.00 64.78  ? 261  TRP A CZ3 1 
ATOM   2132  C  CH2 . TRP A 1 261  ? 126.550 84.139  101.455 1.00 56.63  ? 261  TRP A CH2 1 
ATOM   2133  N  N   . LEU A 1 262  ? 123.645 83.485  94.011  1.00 66.13  ? 262  LEU A N   1 
ATOM   2134  C  CA  . LEU A 1 262  ? 124.239 82.909  92.808  1.00 57.85  ? 262  LEU A CA  1 
ATOM   2135  C  C   . LEU A 1 262  ? 125.253 83.846  92.163  1.00 59.58  ? 262  LEU A C   1 
ATOM   2136  O  O   . LEU A 1 262  ? 126.185 83.384  91.497  1.00 63.84  ? 262  LEU A O   1 
ATOM   2137  C  CB  . LEU A 1 262  ? 123.157 82.547  91.795  1.00 53.07  ? 262  LEU A CB  1 
ATOM   2138  C  CG  . LEU A 1 262  ? 122.527 81.178  92.020  1.00 69.09  ? 262  LEU A CG  1 
ATOM   2139  C  CD1 . LEU A 1 262  ? 121.397 80.956  91.040  1.00 81.67  ? 262  LEU A CD1 1 
ATOM   2140  C  CD2 . LEU A 1 262  ? 123.596 80.106  91.863  1.00 79.74  ? 262  LEU A CD2 1 
ATOM   2141  N  N   . GLU A 1 263  ? 125.094 85.155  92.363  1.00 75.47  ? 263  GLU A N   1 
ATOM   2142  C  CA  . GLU A 1 263  ? 125.996 86.127  91.752  1.00 59.88  ? 263  GLU A CA  1 
ATOM   2143  C  C   . GLU A 1 263  ? 127.378 86.140  92.403  1.00 63.16  ? 263  GLU A C   1 
ATOM   2144  O  O   . GLU A 1 263  ? 128.395 86.174  91.701  1.00 62.86  ? 263  GLU A O   1 
ATOM   2145  C  CB  . GLU A 1 263  ? 125.369 87.515  91.844  1.00 74.18  ? 263  GLU A CB  1 
ATOM   2146  C  CG  . GLU A 1 263  ? 125.846 88.513  90.818  1.00 82.93  ? 263  GLU A CG  1 
ATOM   2147  C  CD  . GLU A 1 263  ? 125.243 89.879  91.056  1.00 81.26  ? 263  GLU A CD  1 
ATOM   2148  O  OE1 . GLU A 1 263  ? 124.828 90.145  92.203  1.00 63.53  ? 263  GLU A OE1 1 
ATOM   2149  O  OE2 . GLU A 1 263  ? 125.175 90.680  90.102  1.00 85.35  ? 263  GLU A OE2 1 
ATOM   2150  N  N   . ASP A 1 264  ? 127.442 86.112  93.734  1.00 75.29  ? 264  ASP A N   1 
ATOM   2151  C  CA  . ASP A 1 264  ? 128.704 86.231  94.455  1.00 70.88  ? 264  ASP A CA  1 
ATOM   2152  C  C   . ASP A 1 264  ? 129.200 84.912  95.038  1.00 79.61  ? 264  ASP A C   1 
ATOM   2153  O  O   . ASP A 1 264  ? 130.345 84.523  94.789  1.00 93.91  ? 264  ASP A O   1 
ATOM   2154  C  CB  . ASP A 1 264  ? 128.574 87.290  95.560  1.00 76.30  ? 264  ASP A CB  1 
ATOM   2155  C  CG  . ASP A 1 264  ? 129.901 87.950  95.888  1.00 92.87  ? 264  ASP A CG  1 
ATOM   2156  O  OD1 . ASP A 1 264  ? 130.884 87.224  96.140  1.00 101.55 ? 264  ASP A OD1 1 
ATOM   2157  O  OD2 . ASP A 1 264  ? 129.964 89.198  95.882  1.00 81.22  ? 264  ASP A OD2 1 
ATOM   2158  N  N   . SER A 1 265  ? 128.381 84.240  95.847  1.00 73.48  ? 265  SER A N   1 
ATOM   2159  C  CA  . SER A 1 265  ? 128.629 82.884  96.339  1.00 74.23  ? 265  SER A CA  1 
ATOM   2160  C  C   . SER A 1 265  ? 129.730 82.811  97.396  1.00 83.63  ? 265  SER A C   1 
ATOM   2161  O  O   . SER A 1 265  ? 129.911 81.759  98.018  1.00 92.08  ? 265  SER A O   1 
ATOM   2162  C  CB  . SER A 1 265  ? 128.949 81.941  95.171  1.00 74.38  ? 265  SER A CB  1 
ATOM   2163  O  OG  . SER A 1 265  ? 130.317 82.024  94.814  1.00 89.14  ? 265  SER A OG  1 
ATOM   2164  N  N   . ASP A 1 266  ? 130.478 83.900  97.617  1.00 79.64  ? 266  ASP A N   1 
ATOM   2165  C  CA  . ASP A 1 266  ? 131.388 84.014  98.758  1.00 72.03  ? 266  ASP A CA  1 
ATOM   2166  C  C   . ASP A 1 266  ? 130.840 84.987  99.791  1.00 74.76  ? 266  ASP A C   1 
ATOM   2167  O  O   . ASP A 1 266  ? 130.598 84.615  100.937 1.00 78.35  ? 266  ASP A O   1 
ATOM   2168  C  CB  . ASP A 1 266  ? 132.806 84.441  98.347  1.00 78.29  ? 266  ASP A CB  1 
ATOM   2169  C  CG  . ASP A 1 266  ? 133.659 83.277  97.893  1.00 112.05 ? 266  ASP A CG  1 
ATOM   2170  O  OD1 . ASP A 1 266  ? 133.353 82.130  98.271  1.00 111.18 ? 266  ASP A OD1 1 
ATOM   2171  O  OD2 . ASP A 1 266  ? 134.649 83.514  97.165  1.00 120.78 ? 266  ASP A OD2 1 
ATOM   2172  N  N   . GLY A 1 267  ? 130.636 86.246  99.404  1.00 74.96  ? 267  GLY A N   1 
ATOM   2173  C  CA  . GLY A 1 267  ? 129.894 87.131  100.264 1.00 66.42  ? 267  GLY A CA  1 
ATOM   2174  C  C   . GLY A 1 267  ? 128.894 87.969  99.504  1.00 59.81  ? 267  GLY A C   1 
ATOM   2175  O  O   . GLY A 1 267  ? 129.265 88.808  98.678  1.00 71.04  ? 267  GLY A O   1 
ATOM   2176  N  N   . ALA A 1 268  ? 127.615 87.739  99.770  1.00 50.30  ? 268  ALA A N   1 
ATOM   2177  C  CA  . ALA A 1 268  ? 126.538 88.552  99.240  1.00 45.56  ? 268  ALA A CA  1 
ATOM   2178  C  C   . ALA A 1 268  ? 125.838 89.179  100.431 1.00 59.11  ? 268  ALA A C   1 
ATOM   2179  O  O   . ALA A 1 268  ? 125.609 88.512  101.445 1.00 78.31  ? 268  ALA A O   1 
ATOM   2180  C  CB  . ALA A 1 268  ? 125.561 87.722  98.396  1.00 64.45  ? 268  ALA A CB  1 
ATOM   2181  N  N   . ASP A 1 269  ? 125.490 90.458  100.315 1.00 57.28  ? 269  ASP A N   1 
ATOM   2182  C  CA  . ASP A 1 269  ? 124.920 91.199  101.442 1.00 46.61  ? 269  ASP A CA  1 
ATOM   2183  C  C   . ASP A 1 269  ? 123.439 90.873  101.622 1.00 52.97  ? 269  ASP A C   1 
ATOM   2184  O  O   . ASP A 1 269  ? 122.568 91.740  101.641 1.00 60.09  ? 269  ASP A O   1 
ATOM   2185  C  CB  . ASP A 1 269  ? 125.157 92.692  101.266 1.00 50.96  ? 269  ASP A CB  1 
ATOM   2186  C  CG  . ASP A 1 269  ? 126.615 93.017  101.046 1.00 71.51  ? 269  ASP A CG  1 
ATOM   2187  O  OD1 . ASP A 1 269  ? 127.443 92.088  101.166 1.00 64.88  ? 269  ASP A OD1 1 
ATOM   2188  O  OD2 . ASP A 1 269  ? 126.934 94.188  100.763 1.00 77.41  ? 269  ASP A OD2 1 
ATOM   2189  N  N   . TYR A 1 270  ? 123.167 89.576  101.755 1.00 51.96  ? 270  TYR A N   1 
ATOM   2190  C  CA  . TYR A 1 270  ? 121.817 89.104  101.901 1.00 53.31  ? 270  TYR A CA  1 
ATOM   2191  C  C   . TYR A 1 270  ? 121.872 87.846  102.746 1.00 58.26  ? 270  TYR A C   1 
ATOM   2192  O  O   . TYR A 1 270  ? 122.813 87.051  102.594 1.00 59.48  ? 270  TYR A O   1 
ATOM   2193  C  CB  . TYR A 1 270  ? 121.196 88.780  100.542 1.00 67.81  ? 270  TYR A CB  1 
ATOM   2194  C  CG  . TYR A 1 270  ? 120.770 89.991  99.754  1.00 52.02  ? 270  TYR A CG  1 
ATOM   2195  C  CD1 . TYR A 1 270  ? 119.724 90.793  100.176 1.00 75.16  ? 270  TYR A CD1 1 
ATOM   2196  C  CD2 . TYR A 1 270  ? 121.440 90.352  98.599  1.00 52.04  ? 270  TYR A CD2 1 
ATOM   2197  C  CE1 . TYR A 1 270  ? 119.342 91.908  99.448  1.00 68.42  ? 270  TYR A CE1 1 
ATOM   2198  C  CE2 . TYR A 1 270  ? 121.068 91.458  97.866  1.00 49.18  ? 270  TYR A CE2 1 
ATOM   2199  C  CZ  . TYR A 1 270  ? 120.021 92.237  98.294  1.00 42.16  ? 270  TYR A CZ  1 
ATOM   2200  O  OH  . TYR A 1 270  ? 119.653 93.345  97.563  1.00 49.10  ? 270  TYR A OH  1 
ATOM   2201  N  N   . PRO A 1 271  ? 120.901 87.632  103.630 1.00 48.87  ? 271  PRO A N   1 
ATOM   2202  C  CA  . PRO A 1 271  ? 120.912 86.420  104.433 1.00 47.36  ? 271  PRO A CA  1 
ATOM   2203  C  C   . PRO A 1 271  ? 120.807 85.204  103.531 1.00 63.14  ? 271  PRO A C   1 
ATOM   2204  O  O   . PRO A 1 271  ? 120.156 85.256  102.472 1.00 73.09  ? 271  PRO A O   1 
ATOM   2205  C  CB  . PRO A 1 271  ? 119.672 86.573  105.324 1.00 47.93  ? 271  PRO A CB  1 
ATOM   2206  C  CG  . PRO A 1 271  ? 118.808 87.572  104.618 1.00 43.75  ? 271  PRO A CG  1 
ATOM   2207  C  CD  . PRO A 1 271  ? 119.759 88.505  103.946 1.00 49.06  ? 271  PRO A CD  1 
ATOM   2208  N  N   . PRO A 1 272  ? 121.428 84.093  103.907 1.00 52.35  ? 272  PRO A N   1 
ATOM   2209  C  CA  . PRO A 1 272  ? 121.313 82.892  103.076 1.00 49.39  ? 272  PRO A CA  1 
ATOM   2210  C  C   . PRO A 1 272  ? 119.885 82.371  103.130 1.00 59.73  ? 272  PRO A C   1 
ATOM   2211  O  O   . PRO A 1 272  ? 119.066 82.802  103.942 1.00 73.09  ? 272  PRO A O   1 
ATOM   2212  C  CB  . PRO A 1 272  ? 122.308 81.912  103.707 1.00 54.01  ? 272  PRO A CB  1 
ATOM   2213  C  CG  . PRO A 1 272  ? 122.527 82.426  105.100 1.00 55.29  ? 272  PRO A CG  1 
ATOM   2214  C  CD  . PRO A 1 272  ? 122.371 83.914  105.024 1.00 46.31  ? 272  PRO A CD  1 
ATOM   2215  N  N   . LEU A 1 273  ? 119.587 81.417  102.250 1.00 69.26  ? 273  LEU A N   1 
ATOM   2216  C  CA  . LEU A 1 273  ? 118.217 80.930  102.128 1.00 63.19  ? 273  LEU A CA  1 
ATOM   2217  C  C   . LEU A 1 273  ? 117.814 80.008  103.271 1.00 65.97  ? 273  LEU A C   1 
ATOM   2218  O  O   . LEU A 1 273  ? 116.618 79.912  103.585 1.00 73.82  ? 273  LEU A O   1 
ATOM   2219  C  CB  . LEU A 1 273  ? 118.041 80.207  100.793 1.00 70.91  ? 273  LEU A CB  1 
ATOM   2220  C  CG  . LEU A 1 273  ? 118.260 81.080  99.557  1.00 57.54  ? 273  LEU A CG  1 
ATOM   2221  C  CD1 . LEU A 1 273  ? 118.058 80.259  98.294  1.00 72.05  ? 273  LEU A CD1 1 
ATOM   2222  C  CD2 . LEU A 1 273  ? 117.324 82.280  99.584  1.00 55.32  ? 273  LEU A CD2 1 
ATOM   2223  N  N   . ASP A 1 274  ? 118.786 79.366  103.918 1.00 68.01  ? 274  ASP A N   1 
ATOM   2224  C  CA  . ASP A 1 274  ? 118.501 78.544  105.089 1.00 73.96  ? 274  ASP A CA  1 
ATOM   2225  C  C   . ASP A 1 274  ? 117.853 79.374  106.191 1.00 78.50  ? 274  ASP A C   1 
ATOM   2226  O  O   . ASP A 1 274  ? 116.821 78.988  106.762 1.00 91.70  ? 274  ASP A O   1 
ATOM   2227  C  CB  . ASP A 1 274  ? 119.803 77.916  105.590 1.00 84.72  ? 274  ASP A CB  1 
ATOM   2228  C  CG  . ASP A 1 274  ? 120.369 76.895  104.623 1.00 116.36 ? 274  ASP A CG  1 
ATOM   2229  O  OD1 . ASP A 1 274  ? 119.578 76.258  103.899 1.00 104.93 ? 274  ASP A OD1 1 
ATOM   2230  O  OD2 . ASP A 1 274  ? 121.609 76.743  104.577 1.00 116.18 ? 274  ASP A OD2 1 
ATOM   2231  N  N   . VAL A 1 275  ? 118.443 80.536  106.484 1.00 59.12  ? 275  VAL A N   1 
ATOM   2232  C  CA  . VAL A 1 275  ? 117.929 81.410  107.532 1.00 41.34  ? 275  VAL A CA  1 
ATOM   2233  C  C   . VAL A 1 275  ? 116.522 81.893  107.196 1.00 62.98  ? 275  VAL A C   1 
ATOM   2234  O  O   . VAL A 1 275  ? 115.643 81.925  108.066 1.00 73.62  ? 275  VAL A O   1 
ATOM   2235  C  CB  . VAL A 1 275  ? 118.898 82.585  107.767 1.00 51.30  ? 275  VAL A CB  1 
ATOM   2236  C  CG1 . VAL A 1 275  ? 118.281 83.611  108.706 1.00 45.59  ? 275  VAL A CG1 1 
ATOM   2237  C  CG2 . VAL A 1 275  ? 120.227 82.079  108.326 1.00 62.25  ? 275  VAL A CG2 1 
ATOM   2238  N  N   . LEU A 1 276  ? 116.285 82.290  105.939 1.00 54.71  ? 276  LEU A N   1 
ATOM   2239  C  CA  . LEU A 1 276  ? 114.941 82.721  105.556 1.00 49.25  ? 276  LEU A CA  1 
ATOM   2240  C  C   . LEU A 1 276  ? 113.920 81.609  105.747 1.00 54.52  ? 276  LEU A C   1 
ATOM   2241  O  O   . LEU A 1 276  ? 112.844 81.835  106.315 1.00 70.45  ? 276  LEU A O   1 
ATOM   2242  C  CB  . LEU A 1 276  ? 114.911 83.211  104.110 1.00 56.67  ? 276  LEU A CB  1 
ATOM   2243  C  CG  . LEU A 1 276  ? 115.665 84.490  103.780 1.00 54.61  ? 276  LEU A CG  1 
ATOM   2244  C  CD1 . LEU A 1 276  ? 115.608 84.724  102.283 1.00 49.13  ? 276  LEU A CD1 1 
ATOM   2245  C  CD2 . LEU A 1 276  ? 115.036 85.648  104.539 1.00 55.26  ? 276  LEU A CD2 1 
ATOM   2246  N  N   . GLY A 1 277  ? 114.219 80.409  105.248 1.00 54.79  ? 277  GLY A N   1 
ATOM   2247  C  CA  . GLY A 1 277  ? 113.257 79.328  105.387 1.00 54.21  ? 277  GLY A CA  1 
ATOM   2248  C  C   . GLY A 1 277  ? 112.922 79.061  106.840 1.00 64.65  ? 277  GLY A C   1 
ATOM   2249  O  O   . GLY A 1 277  ? 111.743 78.968  107.224 1.00 71.04  ? 277  GLY A O   1 
ATOM   2250  N  N   . GLU A 1 278  ? 113.958 78.998  107.684 1.00 68.77  ? 278  GLU A N   1 
ATOM   2251  C  CA  . GLU A 1 278  ? 113.748 78.729  109.102 1.00 56.58  ? 278  GLU A CA  1 
ATOM   2252  C  C   . GLU A 1 278  ? 112.926 79.826  109.772 1.00 60.00  ? 278  GLU A C   1 
ATOM   2253  O  O   . GLU A 1 278  ? 111.954 79.536  110.483 1.00 75.64  ? 278  GLU A O   1 
ATOM   2254  C  CB  . GLU A 1 278  ? 115.097 78.553  109.797 1.00 69.03  ? 278  GLU A CB  1 
ATOM   2255  C  CG  . GLU A 1 278  ? 115.591 77.121  109.776 1.00 103.37 ? 278  GLU A CG  1 
ATOM   2256  C  CD  . GLU A 1 278  ? 116.920 76.954  110.473 1.00 125.80 ? 278  GLU A CD  1 
ATOM   2257  O  OE1 . GLU A 1 278  ? 117.900 77.601  110.048 1.00 111.45 ? 278  GLU A OE1 1 
ATOM   2258  O  OE2 . GLU A 1 278  ? 116.983 76.177  111.448 1.00 123.47 ? 278  GLU A OE2 1 
ATOM   2259  N  N   . LEU A 1 279  ? 113.296 81.096  109.559 1.00 47.89  ? 279  LEU A N   1 
ATOM   2260  C  CA  . LEU A 1 279  ? 112.567 82.177  110.217 1.00 42.72  ? 279  LEU A CA  1 
ATOM   2261  C  C   . LEU A 1 279  ? 111.122 82.231  109.755 1.00 51.63  ? 279  LEU A C   1 
ATOM   2262  O  O   . LEU A 1 279  ? 110.217 82.436  110.570 1.00 68.39  ? 279  LEU A O   1 
ATOM   2263  C  CB  . LEU A 1 279  ? 113.233 83.530  109.967 1.00 40.87  ? 279  LEU A CB  1 
ATOM   2264  C  CG  . LEU A 1 279  ? 114.600 83.831  110.560 1.00 63.44  ? 279  LEU A CG  1 
ATOM   2265  C  CD1 . LEU A 1 279  ? 115.057 85.184  110.061 1.00 63.92  ? 279  LEU A CD1 1 
ATOM   2266  C  CD2 . LEU A 1 279  ? 114.481 83.835  112.074 1.00 58.59  ? 279  LEU A CD2 1 
ATOM   2267  N  N   . TYR A 1 280  ? 110.882 82.058  108.455 1.00 49.91  ? 280  TYR A N   1 
ATOM   2268  C  CA  . TYR A 1 280  ? 109.516 82.114  107.955 1.00 39.19  ? 280  TYR A CA  1 
ATOM   2269  C  C   . TYR A 1 280  ? 108.652 81.040  108.602 1.00 50.25  ? 280  TYR A C   1 
ATOM   2270  O  O   . TYR A 1 280  ? 107.570 81.331  109.138 1.00 68.49  ? 280  TYR A O   1 
ATOM   2271  C  CB  . TYR A 1 280  ? 109.509 81.982  106.432 1.00 55.69  ? 280  TYR A CB  1 
ATOM   2272  C  CG  . TYR A 1 280  ? 109.901 83.259  105.721 1.00 60.95  ? 280  TYR A CG  1 
ATOM   2273  C  CD1 . TYR A 1 280  ? 109.790 84.486  106.359 1.00 58.28  ? 280  TYR A CD1 1 
ATOM   2274  C  CD2 . TYR A 1 280  ? 110.363 83.241  104.412 1.00 74.97  ? 280  TYR A CD2 1 
ATOM   2275  C  CE1 . TYR A 1 280  ? 110.142 85.662  105.718 1.00 45.62  ? 280  TYR A CE1 1 
ATOM   2276  C  CE2 . TYR A 1 280  ? 110.715 84.415  103.761 1.00 57.75  ? 280  TYR A CE2 1 
ATOM   2277  C  CZ  . TYR A 1 280  ? 110.602 85.620  104.419 1.00 44.14  ? 280  TYR A CZ  1 
ATOM   2278  O  OH  . TYR A 1 280  ? 110.949 86.787  103.778 1.00 43.43  ? 280  TYR A OH  1 
ATOM   2279  N  N   . ASN A 1 281  ? 109.141 79.791  108.613 1.00 51.95  ? 281  ASN A N   1 
ATOM   2280  C  CA  . ASN A 1 281  ? 108.330 78.718  109.179 1.00 52.80  ? 281  ASN A CA  1 
ATOM   2281  C  C   . ASN A 1 281  ? 108.086 78.927  110.671 1.00 53.55  ? 281  ASN A C   1 
ATOM   2282  O  O   . ASN A 1 281  ? 106.949 78.789  111.156 1.00 72.08  ? 281  ASN A O   1 
ATOM   2283  C  CB  . ASN A 1 281  ? 109.014 77.372  108.940 1.00 58.05  ? 281  ASN A CB  1 
ATOM   2284  C  CG  . ASN A 1 281  ? 108.994 76.956  107.483 1.00 85.31  ? 281  ASN A CG  1 
ATOM   2285  O  OD1 . ASN A 1 281  ? 108.222 77.484  106.684 1.00 73.62  ? 281  ASN A OD1 1 
ATOM   2286  N  ND2 . ASN A 1 281  ? 109.844 75.997  107.129 1.00 91.84  ? 281  ASN A ND2 1 
ATOM   2287  N  N   . GLN A 1 282  ? 109.134 79.289  111.412 1.00 53.05  ? 282  GLN A N   1 
ATOM   2288  C  CA  . GLN A 1 282  ? 108.985 79.417  112.857 1.00 46.69  ? 282  GLN A CA  1 
ATOM   2289  C  C   . GLN A 1 282  ? 108.110 80.605  113.235 1.00 47.87  ? 282  GLN A C   1 
ATOM   2290  O  O   . GLN A 1 282  ? 107.341 80.527  114.201 1.00 63.05  ? 282  GLN A O   1 
ATOM   2291  C  CB  . GLN A 1 282  ? 110.361 79.486  113.506 1.00 54.42  ? 282  GLN A CB  1 
ATOM   2292  C  CG  . GLN A 1 282  ? 110.949 78.097  113.659 1.00 61.63  ? 282  GLN A CG  1 
ATOM   2293  C  CD  . GLN A 1 282  ? 112.431 78.056  113.408 1.00 72.80  ? 282  GLN A CD  1 
ATOM   2294  O  OE1 . GLN A 1 282  ? 113.072 79.091  113.238 1.00 76.60  ? 282  GLN A OE1 1 
ATOM   2295  N  NE2 . GLN A 1 282  ? 112.986 76.852  113.351 1.00 87.14  ? 282  GLN A NE2 1 
ATOM   2296  N  N   . GLY A 1 283  ? 108.197 81.709  112.492 1.00 50.28  ? 283  GLY A N   1 
ATOM   2297  C  CA  . GLY A 1 283  ? 107.306 82.822  112.761 1.00 44.73  ? 283  GLY A CA  1 
ATOM   2298  C  C   . GLY A 1 283  ? 105.857 82.470  112.493 1.00 56.17  ? 283  GLY A C   1 
ATOM   2299  O  O   . GLY A 1 283  ? 104.961 82.856  113.256 1.00 70.16  ? 283  GLY A O   1 
ATOM   2300  N  N   . ASP A 1 284  ? 105.603 81.723  111.409 1.00 58.36  ? 284  ASP A N   1 
ATOM   2301  C  CA  . ASP A 1 284  ? 104.238 81.281  111.151 1.00 51.83  ? 284  ASP A CA  1 
ATOM   2302  C  C   . ASP A 1 284  ? 103.702 80.467  112.321 1.00 60.96  ? 284  ASP A C   1 
ATOM   2303  O  O   . ASP A 1 284  ? 102.577 80.692  112.795 1.00 70.67  ? 284  ASP A O   1 
ATOM   2304  C  CB  . ASP A 1 284  ? 104.182 80.451  109.866 1.00 73.14  ? 284  ASP A CB  1 
ATOM   2305  C  CG  . ASP A 1 284  ? 104.380 81.284  108.617 1.00 87.94  ? 284  ASP A CG  1 
ATOM   2306  O  OD1 . ASP A 1 284  ? 104.405 82.527  108.730 1.00 81.58  ? 284  ASP A OD1 1 
ATOM   2307  O  OD2 . ASP A 1 284  ? 104.500 80.696  107.521 1.00 75.03  ? 284  ASP A OD2 1 
ATOM   2308  N  N   . GLN A 1 285  ? 104.509 79.525  112.817 1.00 64.69  ? 285  GLN A N   1 
ATOM   2309  C  CA  . GLN A 1 285  ? 104.055 78.708  113.941 1.00 54.49  ? 285  GLN A CA  1 
ATOM   2310  C  C   . GLN A 1 285  ? 103.844 79.527  115.214 1.00 54.59  ? 285  GLN A C   1 
ATOM   2311  O  O   . GLN A 1 285  ? 102.887 79.281  115.961 1.00 66.49  ? 285  GLN A O   1 
ATOM   2312  C  CB  . GLN A 1 285  ? 105.031 77.563  114.194 1.00 59.76  ? 285  GLN A CB  1 
ATOM   2313  C  CG  . GLN A 1 285  ? 105.083 76.568  113.058 1.00 68.54  ? 285  GLN A CG  1 
ATOM   2314  C  CD  . GLN A 1 285  ? 105.895 75.346  113.402 1.00 75.19  ? 285  GLN A CD  1 
ATOM   2315  O  OE1 . GLN A 1 285  ? 107.100 75.428  113.636 1.00 79.62  ? 285  GLN A OE1 1 
ATOM   2316  N  NE2 . GLN A 1 285  ? 105.234 74.195  113.449 1.00 85.60  ? 285  GLN A NE2 1 
ATOM   2317  N  N   . ILE A 1 286  ? 104.735 80.486  115.494 1.00 59.91  ? 286  ILE A N   1 
ATOM   2318  C  CA  . ILE A 1 286  ? 104.571 81.321  116.686 1.00 49.05  ? 286  ILE A CA  1 
ATOM   2319  C  C   . ILE A 1 286  ? 103.256 82.085  116.639 1.00 41.11  ? 286  ILE A C   1 
ATOM   2320  O  O   . ILE A 1 286  ? 102.497 82.119  117.621 1.00 52.36  ? 286  ILE A O   1 
ATOM   2321  C  CB  . ILE A 1 286  ? 105.750 82.301  116.832 1.00 53.48  ? 286  ILE A CB  1 
ATOM   2322  C  CG1 . ILE A 1 286  ? 107.017 81.604  117.320 1.00 62.72  ? 286  ILE A CG1 1 
ATOM   2323  C  CG2 . ILE A 1 286  ? 105.384 83.431  117.796 1.00 55.78  ? 286  ILE A CG2 1 
ATOM   2324  C  CD1 . ILE A 1 286  ? 108.185 82.560  117.467 1.00 63.45  ? 286  ILE A CD1 1 
ATOM   2325  N  N   . ILE A 1 287  ? 102.946 82.682  115.482 1.00 52.18  ? 287  ILE A N   1 
ATOM   2326  C  CA  . ILE A 1 287  ? 101.692 83.424  115.361 1.00 51.71  ? 287  ILE A CA  1 
ATOM   2327  C  C   . ILE A 1 287  ? 100.492 82.503  115.503 1.00 55.54  ? 287  ILE A C   1 
ATOM   2328  O  O   . ILE A 1 287  ? 99.503  82.849  116.159 1.00 67.00  ? 287  ILE A O   1 
ATOM   2329  C  CB  . ILE A 1 287  ? 101.644 84.208  114.040 1.00 53.71  ? 287  ILE A CB  1 
ATOM   2330  C  CG1 . ILE A 1 287  ? 102.590 85.395  114.114 1.00 43.66  ? 287  ILE A CG1 1 
ATOM   2331  C  CG2 . ILE A 1 287  ? 100.240 84.742  113.788 1.00 49.83  ? 287  ILE A CG2 1 
ATOM   2332  C  CD1 . ILE A 1 287  ? 102.654 86.201  112.851 1.00 55.28  ? 287  ILE A CD1 1 
ATOM   2333  N  N   . ALA A 1 288  ? 100.555 81.316  114.904 1.00 62.07  ? 288  ALA A N   1 
ATOM   2334  C  CA  . ALA A 1 288  ? 99.415  80.413  115.002 1.00 52.00  ? 288  ALA A CA  1 
ATOM   2335  C  C   . ALA A 1 288  ? 99.165  79.958  116.436 1.00 58.76  ? 288  ALA A C   1 
ATOM   2336  O  O   . ALA A 1 288  ? 98.017  79.962  116.906 1.00 63.35  ? 288  ALA A O   1 
ATOM   2337  C  CB  . ALA A 1 288  ? 99.626  79.203  114.090 1.00 57.57  ? 288  ALA A CB  1 
ATOM   2338  N  N   . MET A 1 289  ? 100.222 79.566  117.151 1.00 70.14  ? 289  MET A N   1 
ATOM   2339  C  CA  . MET A 1 289  ? 100.052 79.122  118.534 1.00 65.18  ? 289  MET A CA  1 
ATOM   2340  C  C   . MET A 1 289  ? 99.667  80.238  119.514 1.00 53.55  ? 289  MET A C   1 
ATOM   2341  O  O   . MET A 1 289  ? 98.803  80.013  120.376 1.00 53.22  ? 289  MET A O   1 
ATOM   2342  C  CB  . MET A 1 289  ? 101.281 78.342  118.984 1.00 68.70  ? 289  MET A CB  1 
ATOM   2343  C  CG  . MET A 1 289  ? 101.226 77.908  120.439 1.00 79.43  ? 289  MET A CG  1 
ATOM   2344  S  SD  . MET A 1 289  ? 102.226 76.436  120.677 1.00 106.30 ? 289  MET A SD  1 
ATOM   2345  C  CE  . MET A 1 289  ? 101.306 75.300  119.642 1.00 91.95  ? 289  MET A CE  1 
ATOM   2346  N  N   . TYR A 1 290  ? 100.266 81.423  119.430 1.00 60.62  ? 290  TYR A N   1 
ATOM   2347  C  CA  . TYR A 1 290  ? 99.943  82.462  120.429 1.00 59.76  ? 290  TYR A CA  1 
ATOM   2348  C  C   . TYR A 1 290  ? 98.948  83.527  119.980 1.00 62.04  ? 290  TYR A C   1 
ATOM   2349  O  O   . TYR A 1 290  ? 98.643  84.423  120.767 1.00 62.85  ? 290  TYR A O   1 
ATOM   2350  C  CB  . TYR A 1 290  ? 101.218 83.160  120.922 1.00 63.21  ? 290  TYR A CB  1 
ATOM   2351  C  CG  . TYR A 1 290  ? 102.146 82.219  121.641 1.00 67.26  ? 290  TYR A CG  1 
ATOM   2352  C  CD1 . TYR A 1 290  ? 101.955 81.925  122.982 1.00 67.39  ? 290  TYR A CD1 1 
ATOM   2353  C  CD2 . TYR A 1 290  ? 103.207 81.619  120.983 1.00 68.73  ? 290  TYR A CD2 1 
ATOM   2354  C  CE1 . TYR A 1 290  ? 102.791 81.059  123.650 1.00 55.12  ? 290  TYR A CE1 1 
ATOM   2355  C  CE2 . TYR A 1 290  ? 104.051 80.750  121.644 1.00 56.50  ? 290  TYR A CE2 1 
ATOM   2356  C  CZ  . TYR A 1 290  ? 103.839 80.474  122.977 1.00 54.88  ? 290  TYR A CZ  1 
ATOM   2357  O  OH  . TYR A 1 290  ? 104.673 79.609  123.643 1.00 77.61  ? 290  TYR A OH  1 
ATOM   2358  N  N   . LEU A 1 291  ? 98.432  83.445  118.759 1.00 57.73  ? 291  LEU A N   1 
ATOM   2359  C  CA  . LEU A 1 291  ? 97.460  84.404  118.209 1.00 44.85  ? 291  LEU A CA  1 
ATOM   2360  C  C   . LEU A 1 291  ? 98.009  85.832  118.250 1.00 54.43  ? 291  LEU A C   1 
ATOM   2361  O  O   . LEU A 1 291  ? 99.149  86.053  117.812 1.00 66.29  ? 291  LEU A O   1 
ATOM   2362  C  CB  . LEU A 1 291  ? 96.146  84.187  118.957 1.00 57.49  ? 291  LEU A CB  1 
ATOM   2363  C  CG  . LEU A 1 291  ? 95.593  82.763  119.034 1.00 63.70  ? 291  LEU A CG  1 
ATOM   2364  C  CD1 . LEU A 1 291  ? 94.198  82.762  119.643 1.00 66.32  ? 291  LEU A CD1 1 
ATOM   2365  C  CD2 . LEU A 1 291  ? 95.574  82.134  117.653 1.00 64.65  ? 291  LEU A CD2 1 
ATOM   2366  N  N   . GLU A 1 292  ? 97.260  86.808  118.780 1.00 66.69  ? 292  GLU A N   1 
ATOM   2367  C  CA  . GLU A 1 292  ? 97.708  88.201  118.804 1.00 71.06  ? 292  GLU A CA  1 
ATOM   2368  C  C   . GLU A 1 292  ? 98.969  88.395  119.632 1.00 76.79  ? 292  GLU A C   1 
ATOM   2369  O  O   . GLU A 1 292  ? 99.822  89.219  119.284 1.00 77.96  ? 292  GLU A O   1 
ATOM   2370  C  CB  . GLU A 1 292  ? 96.606  89.110  119.351 1.00 72.83  ? 292  GLU A CB  1 
ATOM   2371  C  CG  . GLU A 1 292  ? 95.276  89.002  118.647 1.00 90.92  ? 292  GLU A CG  1 
ATOM   2372  C  CD  . GLU A 1 292  ? 94.412  87.922  119.256 1.00 102.52 ? 292  GLU A CD  1 
ATOM   2373  O  OE1 . GLU A 1 292  ? 94.575  87.652  120.467 1.00 83.80  ? 292  GLU A OE1 1 
ATOM   2374  O  OE2 . GLU A 1 292  ? 93.581  87.337  118.533 1.00 104.08 ? 292  GLU A OE2 1 
ATOM   2375  N  N   . ASP A 1 293  ? 99.097  87.666  120.742 1.00 73.88  ? 293  ASP A N   1 
ATOM   2376  C  CA  . ASP A 1 293  ? 100.267 87.853  121.591 1.00 72.90  ? 293  ASP A CA  1 
ATOM   2377  C  C   . ASP A 1 293  ? 101.558 87.531  120.853 1.00 73.06  ? 293  ASP A C   1 
ATOM   2378  O  O   . ASP A 1 293  ? 102.563 88.219  121.051 1.00 71.41  ? 293  ASP A O   1 
ATOM   2379  C  CB  . ASP A 1 293  ? 100.139 87.019  122.866 1.00 89.66  ? 293  ASP A CB  1 
ATOM   2380  C  CG  . ASP A 1 293  ? 98.818  87.237  123.570 1.00 103.68 ? 293  ASP A CG  1 
ATOM   2381  O  OD1 . ASP A 1 293  ? 98.515  88.394  123.931 1.00 100.75 ? 293  ASP A OD1 1 
ATOM   2382  O  OD2 . ASP A 1 293  ? 98.083  86.247  123.762 1.00 101.10 ? 293  ASP A OD2 1 
ATOM   2383  N  N   . GLY A 1 294  ? 101.560 86.489  120.017 1.00 66.29  ? 294  GLY A N   1 
ATOM   2384  C  CA  . GLY A 1 294  ? 102.761 86.116  119.281 1.00 54.88  ? 294  GLY A CA  1 
ATOM   2385  C  C   . GLY A 1 294  ? 103.558 87.300  118.774 1.00 56.76  ? 294  GLY A C   1 
ATOM   2386  O  O   . GLY A 1 294  ? 104.795 87.290  118.786 1.00 69.95  ? 294  GLY A O   1 
ATOM   2387  N  N   . PHE A 1 295  ? 102.836 88.318  118.287 1.00 54.20  ? 295  PHE A N   1 
ATOM   2388  C  CA  . PHE A 1 295  ? 103.458 89.555  117.825 1.00 47.79  ? 295  PHE A CA  1 
ATOM   2389  C  C   . PHE A 1 295  ? 104.308 90.211  118.907 1.00 59.36  ? 295  PHE A C   1 
ATOM   2390  O  O   . PHE A 1 295  ? 105.247 90.912  118.575 1.00 73.42  ? 295  PHE A O   1 
ATOM   2391  C  CB  . PHE A 1 295  ? 102.418 90.507  117.288 1.00 42.35  ? 295  PHE A CB  1 
ATOM   2392  C  CG  . PHE A 1 295  ? 101.814 90.038  116.017 1.00 56.01  ? 295  PHE A CG  1 
ATOM   2393  C  CD1 . PHE A 1 295  ? 102.528 90.133  114.849 1.00 50.75  ? 295  PHE A CD1 1 
ATOM   2394  C  CD2 . PHE A 1 295  ? 100.564 89.439  116.002 1.00 65.14  ? 295  PHE A CD2 1 
ATOM   2395  C  CE1 . PHE A 1 295  ? 102.018 89.667  113.662 1.00 56.34  ? 295  PHE A CE1 1 
ATOM   2396  C  CE2 . PHE A 1 295  ? 100.042 88.976  114.817 1.00 69.36  ? 295  PHE A CE2 1 
ATOM   2397  C  CZ  . PHE A 1 295  ? 100.764 89.089  113.648 1.00 64.53  ? 295  PHE A CZ  1 
ATOM   2398  N  N   . LYS A 1 296  ? 104.040 89.928  120.177 1.00 62.15  ? 296  LYS A N   1 
ATOM   2399  C  CA  . LYS A 1 296  ? 104.901 90.383  121.234 1.00 67.65  ? 296  LYS A CA  1 
ATOM   2400  C  C   . LYS A 1 296  ? 106.293 89.798  121.136 1.00 61.62  ? 296  LYS A C   1 
ATOM   2401  O  O   . LYS A 1 296  ? 107.288 90.494  121.354 1.00 70.42  ? 296  LYS A O   1 
ATOM   2402  C  CB  . LYS A 1 296  ? 104.293 90.035  122.572 1.00 81.09  ? 296  LYS A CB  1 
ATOM   2403  C  CG  . LYS A 1 296  ? 103.192 90.911  123.041 1.00 94.80  ? 296  LYS A CG  1 
ATOM   2404  C  CD  . LYS A 1 296  ? 102.675 90.346  124.344 1.00 107.89 ? 296  LYS A CD  1 
ATOM   2405  C  CE  . LYS A 1 296  ? 101.520 91.198  124.772 1.00 105.05 ? 296  LYS A CE  1 
ATOM   2406  N  NZ  . LYS A 1 296  ? 102.487 92.384  124.817 1.00 108.61 ? 296  LYS A NZ  1 
ATOM   2407  N  N   . LEU A 1 297  ? 106.388 88.521  120.770 1.00 54.77  ? 297  LEU A N   1 
ATOM   2408  C  CA  . LEU A 1 297  ? 107.673 87.875  120.576 1.00 51.17  ? 297  LEU A CA  1 
ATOM   2409  C  C   . LEU A 1 297  ? 108.304 88.294  119.258 1.00 58.35  ? 297  LEU A C   1 
ATOM   2410  O  O   . LEU A 1 297  ? 109.510 88.572  119.181 1.00 62.28  ? 297  LEU A O   1 
ATOM   2411  C  CB  . LEU A 1 297  ? 107.485 86.367  120.618 1.00 53.83  ? 297  LEU A CB  1 
ATOM   2412  C  CG  . LEU A 1 297  ? 106.990 85.888  121.978 1.00 43.35  ? 297  LEU A CG  1 
ATOM   2413  C  CD1 . LEU A 1 297  ? 106.702 84.400  121.927 1.00 42.67  ? 297  LEU A CD1 1 
ATOM   2414  C  CD2 . LEU A 1 297  ? 108.035 86.207  123.044 1.00 61.78  ? 297  LEU A CD2 1 
ATOM   2415  N  N   . ILE A 1 298  ? 107.489 88.342  118.207 1.00 58.82  ? 298  ILE A N   1 
ATOM   2416  C  CA  . ILE A 1 298  ? 107.974 88.674  116.875 1.00 56.40  ? 298  ILE A CA  1 
ATOM   2417  C  C   . ILE A 1 298  ? 108.444 90.117  116.787 1.00 61.73  ? 298  ILE A C   1 
ATOM   2418  O  O   . ILE A 1 298  ? 109.319 90.440  115.966 1.00 61.52  ? 298  ILE A O   1 
ATOM   2419  C  CB  . ILE A 1 298  ? 106.860 88.355  115.866 1.00 53.40  ? 298  ILE A CB  1 
ATOM   2420  C  CG1 . ILE A 1 298  ? 106.829 86.869  115.621 1.00 40.49  ? 298  ILE A CG1 1 
ATOM   2421  C  CG2 . ILE A 1 298  ? 107.180 88.916  114.512 1.00 38.74  ? 298  ILE A CG2 1 
ATOM   2422  C  CD1 . ILE A 1 298  ? 105.686 86.453  114.813 1.00 43.75  ? 298  ILE A CD1 1 
ATOM   2423  N  N   . LYS A 1 299  ? 107.938 90.980  117.664 1.00 64.35  ? 299  LYS A N   1 
ATOM   2424  C  CA  . LYS A 1 299  ? 108.319 92.384  117.707 1.00 49.21  ? 299  LYS A CA  1 
ATOM   2425  C  C   . LYS A 1 299  ? 109.787 92.554  118.056 1.00 60.42  ? 299  LYS A C   1 
ATOM   2426  O  O   . LYS A 1 299  ? 110.336 93.644  117.873 1.00 65.79  ? 299  LYS A O   1 
ATOM   2427  C  CB  . LYS A 1 299  ? 107.428 93.072  118.743 1.00 50.75  ? 299  LYS A CB  1 
ATOM   2428  C  CG  . LYS A 1 299  ? 107.638 94.551  118.935 1.00 74.51  ? 299  LYS A CG  1 
ATOM   2429  C  CD  . LYS A 1 299  ? 106.672 95.086  119.977 1.00 66.26  ? 299  LYS A CD  1 
ATOM   2430  C  CE  . LYS A 1 299  ? 106.840 96.580  120.143 1.00 78.77  ? 299  LYS A CE  1 
ATOM   2431  N  NZ  . LYS A 1 299  ? 106.604 97.271  118.848 1.00 91.44  ? 299  LYS A NZ  1 
ATOM   2432  N  N   . HIS A 1 300  ? 110.433 91.491  118.529 1.00 57.88  ? 300  HIS A N   1 
ATOM   2433  C  CA  . HIS A 1 300  ? 111.809 91.528  118.987 1.00 51.77  ? 300  HIS A CA  1 
ATOM   2434  C  C   . HIS A 1 300  ? 112.816 91.326  117.867 1.00 54.20  ? 300  HIS A C   1 
ATOM   2435  O  O   . HIS A 1 300  ? 114.022 91.344  118.133 1.00 65.39  ? 300  HIS A O   1 
ATOM   2436  C  CB  . HIS A 1 300  ? 112.029 90.465  120.065 1.00 53.43  ? 300  HIS A CB  1 
ATOM   2437  C  CG  . HIS A 1 300  ? 111.685 90.931  121.443 1.00 61.32  ? 300  HIS A CG  1 
ATOM   2438  N  ND1 . HIS A 1 300  ? 110.412 90.841  121.962 1.00 56.59  ? 300  HIS A ND1 1 
ATOM   2439  C  CD2 . HIS A 1 300  ? 112.443 91.516  122.400 1.00 58.80  ? 300  HIS A CD2 1 
ATOM   2440  C  CE1 . HIS A 1 300  ? 110.403 91.339  123.185 1.00 64.30  ? 300  HIS A CE1 1 
ATOM   2441  N  NE2 . HIS A 1 300  ? 111.622 91.755  123.474 1.00 65.89  ? 300  HIS A NE2 1 
ATOM   2442  N  N   . LEU A 1 301  ? 112.362 91.125  116.629 1.00 59.36  ? 301  LEU A N   1 
ATOM   2443  C  CA  . LEU A 1 301  ? 113.305 90.832  115.556 1.00 47.79  ? 301  LEU A CA  1 
ATOM   2444  C  C   . LEU A 1 301  ? 114.239 92.011  115.312 1.00 56.67  ? 301  LEU A C   1 
ATOM   2445  O  O   . LEU A 1 301  ? 115.442 91.823  115.100 1.00 66.00  ? 301  LEU A O   1 
ATOM   2446  C  CB  . LEU A 1 301  ? 112.552 90.446  114.282 1.00 64.10  ? 301  LEU A CB  1 
ATOM   2447  C  CG  . LEU A 1 301  ? 113.413 90.280  113.030 1.00 52.21  ? 301  LEU A CG  1 
ATOM   2448  C  CD1 . LEU A 1 301  ? 114.021 88.893  112.986 1.00 53.74  ? 301  LEU A CD1 1 
ATOM   2449  C  CD2 . LEU A 1 301  ? 112.581 90.535  111.783 1.00 72.67  ? 301  LEU A CD2 1 
ATOM   2450  N  N   . GLU A 1 302  ? 113.707 93.237  115.350 1.00 56.10  ? 302  GLU A N   1 
ATOM   2451  C  CA  . GLU A 1 302  ? 114.531 94.395  115.005 1.00 56.00  ? 302  GLU A CA  1 
ATOM   2452  C  C   . GLU A 1 302  ? 115.586 94.692  116.068 1.00 73.38  ? 302  GLU A C   1 
ATOM   2453  O  O   . GLU A 1 302  ? 116.777 94.790  115.716 1.00 78.73  ? 302  GLU A O   1 
ATOM   2454  C  CB  . GLU A 1 302  ? 113.643 95.615  114.737 1.00 78.17  ? 302  GLU A CB  1 
ATOM   2455  C  CG  . GLU A 1 302  ? 113.024 95.680  113.357 1.00 101.96 ? 302  GLU A CG  1 
ATOM   2456  C  CD  . GLU A 1 302  ? 112.239 96.960  113.152 1.00 116.73 ? 302  GLU A CD  1 
ATOM   2457  O  OE1 . GLU A 1 302  ? 111.813 97.225  112.010 1.00 107.05 ? 302  GLU A OE1 1 
ATOM   2458  O  OE2 . GLU A 1 302  ? 112.066 97.712  114.135 1.00 113.06 ? 302  GLU A OE2 1 
ATOM   2459  N  N   . PRO A 1 303  ? 115.244 94.844  117.358 1.00 60.08  ? 303  PRO A N   1 
ATOM   2460  C  CA  . PRO A 1 303  ? 116.303 95.059  118.357 1.00 47.67  ? 303  PRO A CA  1 
ATOM   2461  C  C   . PRO A 1 303  ? 117.321 93.941  118.429 1.00 58.75  ? 303  PRO A C   1 
ATOM   2462  O  O   . PRO A 1 303  ? 118.497 94.213  118.688 1.00 69.46  ? 303  PRO A O   1 
ATOM   2463  C  CB  . PRO A 1 303  ? 115.520 95.179  119.676 1.00 56.91  ? 303  PRO A CB  1 
ATOM   2464  C  CG  . PRO A 1 303  ? 114.192 94.547  119.393 1.00 64.35  ? 303  PRO A CG  1 
ATOM   2465  C  CD  . PRO A 1 303  ? 113.909 94.909  117.981 1.00 62.20  ? 303  PRO A CD  1 
ATOM   2466  N  N   . LEU A 1 304  ? 116.913 92.691  118.203 1.00 56.68  ? 304  LEU A N   1 
ATOM   2467  C  CA  . LEU A 1 304  ? 117.877 91.596  118.208 1.00 47.24  ? 304  LEU A CA  1 
ATOM   2468  C  C   . LEU A 1 304  ? 118.864 91.713  117.057 1.00 61.66  ? 304  LEU A C   1 
ATOM   2469  O  O   . LEU A 1 304  ? 120.068 91.487  117.239 1.00 74.30  ? 304  LEU A O   1 
ATOM   2470  C  CB  . LEU A 1 304  ? 117.143 90.262  118.144 1.00 47.47  ? 304  LEU A CB  1 
ATOM   2471  C  CG  . LEU A 1 304  ? 116.639 89.777  119.492 1.00 56.22  ? 304  LEU A CG  1 
ATOM   2472  C  CD1 . LEU A 1 304  ? 115.651 88.655  119.281 1.00 55.59  ? 304  LEU A CD1 1 
ATOM   2473  C  CD2 . LEU A 1 304  ? 117.825 89.316  120.332 1.00 51.88  ? 304  LEU A CD2 1 
ATOM   2474  N  N   . CYS A 1 305  ? 118.381 92.094  115.875 1.00 56.47  ? 305  CYS A N   1 
ATOM   2475  C  CA  . CYS A 1 305  ? 119.286 92.305  114.753 1.00 54.78  ? 305  CYS A CA  1 
ATOM   2476  C  C   . CYS A 1 305  ? 120.262 93.438  115.044 1.00 64.05  ? 305  CYS A C   1 
ATOM   2477  O  O   . CYS A 1 305  ? 121.469 93.313  114.781 1.00 55.04  ? 305  CYS A O   1 
ATOM   2478  C  CB  . CYS A 1 305  ? 118.475 92.598  113.489 1.00 57.97  ? 305  CYS A CB  1 
ATOM   2479  S  SG  . CYS A 1 305  ? 117.623 91.160  112.796 1.00 73.72  ? 305  CYS A SG  1 
ATOM   2480  N  N   . VAL A 1 306  ? 119.767 94.530  115.631 1.00 68.74  ? 306  VAL A N   1 
ATOM   2481  C  CA  . VAL A 1 306  ? 120.652 95.645  115.956 1.00 50.01  ? 306  VAL A CA  1 
ATOM   2482  C  C   . VAL A 1 306  ? 121.689 95.228  116.995 1.00 50.33  ? 306  VAL A C   1 
ATOM   2483  O  O   . VAL A 1 306  ? 122.876 95.558  116.878 1.00 62.19  ? 306  VAL A O   1 
ATOM   2484  C  CB  . VAL A 1 306  ? 119.830 96.859  116.432 1.00 49.53  ? 306  VAL A CB  1 
ATOM   2485  C  CG1 . VAL A 1 306  ? 120.736 97.895  117.082 1.00 53.34  ? 306  VAL A CG1 1 
ATOM   2486  C  CG2 . VAL A 1 306  ? 119.064 97.471  115.267 1.00 61.76  ? 306  VAL A CG2 1 
ATOM   2487  N  N   . SER A 1 307  ? 121.265 94.467  118.009 1.00 60.70  ? 307  SER A N   1 
ATOM   2488  C  CA  . SER A 1 307  ? 122.178 94.042  119.066 1.00 49.40  ? 307  SER A CA  1 
ATOM   2489  C  C   . SER A 1 307  ? 123.218 93.056  118.562 1.00 54.76  ? 307  SER A C   1 
ATOM   2490  O  O   . SER A 1 307  ? 124.334 93.011  119.090 1.00 71.34  ? 307  SER A O   1 
ATOM   2491  C  CB  . SER A 1 307  ? 121.387 93.406  120.207 1.00 55.49  ? 307  SER A CB  1 
ATOM   2492  O  OG  . SER A 1 307  ? 120.723 92.235  119.761 1.00 59.30  ? 307  SER A OG  1 
ATOM   2493  N  N   . CYS A 1 308  ? 122.876 92.274  117.538 1.00 59.81  ? 308  CYS A N   1 
ATOM   2494  C  CA  . CYS A 1 308  ? 123.861 91.393  116.922 1.00 49.01  ? 308  CYS A CA  1 
ATOM   2495  C  C   . CYS A 1 308  ? 124.851 92.163  116.059 1.00 59.56  ? 308  CYS A C   1 
ATOM   2496  O  O   . CYS A 1 308  ? 126.026 91.787  115.989 1.00 55.82  ? 308  CYS A O   1 
ATOM   2497  C  CB  . CYS A 1 308  ? 123.157 90.305  116.111 1.00 57.49  ? 308  CYS A CB  1 
ATOM   2498  S  SG  . CYS A 1 308  ? 122.241 89.128  117.134 1.00 69.06  ? 308  CYS A SG  1 
ATOM   2499  N  N   . ILE A 1 309  ? 124.404 93.234  115.397 1.00 74.90  ? 309  ILE A N   1 
ATOM   2500  C  CA  . ILE A 1 309  ? 125.331 94.056  114.617 1.00 59.99  ? 309  ILE A CA  1 
ATOM   2501  C  C   . ILE A 1 309  ? 126.404 94.668  115.518 1.00 48.22  ? 309  ILE A C   1 
ATOM   2502  O  O   . ILE A 1 309  ? 127.576 94.765  115.136 1.00 68.03  ? 309  ILE A O   1 
ATOM   2503  C  CB  . ILE A 1 309  ? 124.562 95.152  113.856 1.00 60.69  ? 309  ILE A CB  1 
ATOM   2504  C  CG1 . ILE A 1 309  ? 123.762 94.559  112.700 1.00 65.92  ? 309  ILE A CG1 1 
ATOM   2505  C  CG2 . ILE A 1 309  ? 125.519 96.205  113.309 1.00 47.22  ? 309  ILE A CG2 1 
ATOM   2506  C  CD1 . ILE A 1 309  ? 122.842 95.557  112.028 1.00 48.48  ? 309  ILE A CD1 1 
ATOM   2507  N  N   . GLN A 1 310  ? 126.028 95.056  116.738 1.00 60.05  ? 310  GLN A N   1 
ATOM   2508  C  CA  . GLN A 1 310  ? 126.893 95.820  117.634 1.00 58.14  ? 310  GLN A CA  1 
ATOM   2509  C  C   . GLN A 1 310  ? 128.091 95.059  118.177 1.00 57.40  ? 310  GLN A C   1 
ATOM   2510  O  O   . GLN A 1 310  ? 128.960 95.688  118.793 1.00 68.32  ? 310  GLN A O   1 
ATOM   2511  C  CB  . GLN A 1 310  ? 126.084 96.294  118.835 1.00 58.54  ? 310  GLN A CB  1 
ATOM   2512  C  CG  . GLN A 1 310  ? 125.068 97.347  118.538 1.00 65.53  ? 310  GLN A CG  1 
ATOM   2513  C  CD  . GLN A 1 310  ? 124.502 97.932  119.800 1.00 69.94  ? 310  GLN A CD  1 
ATOM   2514  O  OE1 . GLN A 1 310  ? 124.989 97.662  120.899 1.00 71.67  ? 310  GLN A OE1 1 
ATOM   2515  N  NE2 . GLN A 1 310  ? 123.408 98.661  119.664 1.00 79.26  ? 310  GLN A NE2 1 
ATOM   2516  N  N   . THR A 1 311  ? 128.181 93.745  117.981 1.00 53.91  ? 311  THR A N   1 
ATOM   2517  C  CA  . THR A 1 311  ? 129.206 92.941  118.637 1.00 51.76  ? 311  THR A CA  1 
ATOM   2518  C  C   . THR A 1 311  ? 130.438 92.713  117.766 1.00 66.96  ? 311  THR A C   1 
ATOM   2519  O  O   . THR A 1 311  ? 131.052 91.645  117.847 1.00 67.18  ? 311  THR A O   1 
ATOM   2520  C  CB  . THR A 1 311  ? 128.619 91.590  119.042 1.00 51.85  ? 311  THR A CB  1 
ATOM   2521  O  OG1 . THR A 1 311  ? 128.362 90.820  117.865 1.00 47.75  ? 311  THR A OG1 1 
ATOM   2522  C  CG2 . THR A 1 311  ? 127.308 91.788  119.781 1.00 59.41  ? 311  THR A CG2 1 
ATOM   2523  N  N   . HIS A 1 312  ? 130.829 93.690  116.954 1.00 64.48  ? 312  HIS A N   1 
ATOM   2524  C  CA  . HIS A 1 312  ? 131.817 93.413  115.918 1.00 64.55  ? 312  HIS A CA  1 
ATOM   2525  C  C   . HIS A 1 312  ? 133.140 94.158  116.034 1.00 80.61  ? 312  HIS A C   1 
ATOM   2526  O  O   . HIS A 1 312  ? 134.114 93.720  115.415 1.00 84.54  ? 312  HIS A O   1 
ATOM   2527  C  CB  . HIS A 1 312  ? 131.214 93.662  114.530 1.00 40.26  ? 312  HIS A CB  1 
ATOM   2528  C  CG  . HIS A 1 312  ? 130.542 92.449  113.967 1.00 62.21  ? 312  HIS A CG  1 
ATOM   2529  N  ND1 . HIS A 1 312  ? 131.237 91.447  113.324 1.00 72.88  ? 312  HIS A ND1 1 
ATOM   2530  C  CD2 . HIS A 1 312  ? 129.246 92.057  113.985 1.00 73.94  ? 312  HIS A CD2 1 
ATOM   2531  C  CE1 . HIS A 1 312  ? 130.397 90.500  112.952 1.00 76.56  ? 312  HIS A CE1 1 
ATOM   2532  N  NE2 . HIS A 1 312  ? 129.182 90.845  113.340 1.00 71.93  ? 312  HIS A NE2 1 
ATOM   2533  N  N   . GLY A 1 313  ? 133.222 95.247  116.791 1.00 73.98  ? 313  GLY A N   1 
ATOM   2534  C  CA  . GLY A 1 313  ? 134.462 95.994  116.888 1.00 79.42  ? 313  GLY A CA  1 
ATOM   2535  C  C   . GLY A 1 313  ? 135.482 95.343  117.797 1.00 95.44  ? 313  GLY A C   1 
ATOM   2536  O  O   . GLY A 1 313  ? 135.474 94.127  118.018 1.00 88.89  ? 313  GLY A O   1 
ATOM   2537  N  N   . ILE A 1 314  ? 136.383 96.170  118.329 1.00 93.51  ? 314  ILE A N   1 
ATOM   2538  C  CA  . ILE A 1 314  ? 137.359 95.712  119.311 1.00 85.70  ? 314  ILE A CA  1 
ATOM   2539  C  C   . ILE A 1 314  ? 136.637 95.323  120.591 1.00 97.23  ? 314  ILE A C   1 
ATOM   2540  O  O   . ILE A 1 314  ? 135.789 96.073  121.092 1.00 110.94 ? 314  ILE A O   1 
ATOM   2541  C  CB  . ILE A 1 314  ? 138.404 96.804  119.576 1.00 92.50  ? 314  ILE A CB  1 
ATOM   2542  C  CG1 . ILE A 1 314  ? 139.258 97.035  118.330 1.00 100.73 ? 314  ILE A CG1 1 
ATOM   2543  C  CG2 . ILE A 1 314  ? 139.289 96.429  120.756 1.00 107.20 ? 314  ILE A CG2 1 
ATOM   2544  C  CD1 . ILE A 1 314  ? 140.040 95.822  117.884 1.00 113.93 ? 314  ILE A CD1 1 
ATOM   2545  N  N   . PHE A 1 315  ? 136.972 94.155  121.140 1.00 85.98  ? 315  PHE A N   1 
ATOM   2546  C  CA  . PHE A 1 315  ? 136.184 93.630  122.244 1.00 75.63  ? 315  PHE A CA  1 
ATOM   2547  C  C   . PHE A 1 315  ? 136.250 94.543  123.462 1.00 75.81  ? 315  PHE A C   1 
ATOM   2548  O  O   . PHE A 1 315  ? 137.327 94.965  123.888 1.00 82.27  ? 315  PHE A O   1 
ATOM   2549  C  CB  . PHE A 1 315  ? 136.637 92.221  122.623 1.00 86.75  ? 315  PHE A CB  1 
ATOM   2550  C  CG  . PHE A 1 315  ? 135.895 91.661  123.807 1.00 81.03  ? 315  PHE A CG  1 
ATOM   2551  C  CD1 . PHE A 1 315  ? 134.559 91.308  123.707 1.00 81.00  ? 315  PHE A CD1 1 
ATOM   2552  C  CD2 . PHE A 1 315  ? 136.538 91.489  125.023 1.00 85.45  ? 315  PHE A CD2 1 
ATOM   2553  C  CE1 . PHE A 1 315  ? 133.875 90.808  124.802 1.00 72.55  ? 315  PHE A CE1 1 
ATOM   2554  C  CE2 . PHE A 1 315  ? 135.862 90.984  126.118 1.00 83.99  ? 315  PHE A CE2 1 
ATOM   2555  C  CZ  . PHE A 1 315  ? 134.529 90.642  126.007 1.00 69.12  ? 315  PHE A CZ  1 
ATOM   2556  N  N   . THR A 1 316  ? 135.080 94.802  124.042 1.00 78.20  ? 316  THR A N   1 
ATOM   2557  C  CA  . THR A 1 316  ? 134.897 95.493  125.296 1.00 72.75  ? 316  THR A CA  1 
ATOM   2558  C  C   . THR A 1 316  ? 133.631 94.867  125.881 1.00 73.53  ? 316  THR A C   1 
ATOM   2559  O  O   . THR A 1 316  ? 132.658 94.673  125.139 1.00 81.46  ? 316  THR A O   1 
ATOM   2560  C  CB  . THR A 1 316  ? 134.736 97.009  125.124 1.00 69.91  ? 316  THR A CB  1 
ATOM   2561  O  OG1 . THR A 1 316  ? 135.931 97.555  124.551 1.00 87.35  ? 316  THR A OG1 1 
ATOM   2562  C  CG2 . THR A 1 316  ? 134.453 97.693  126.451 1.00 73.85  ? 316  THR A CG2 1 
ATOM   2563  N  N   . PRO A 1 317  ? 133.628 94.534  127.163 1.00 65.17  ? 317  PRO A N   1 
ATOM   2564  C  CA  . PRO A 1 317  ? 132.482 93.780  127.748 1.00 61.72  ? 317  PRO A CA  1 
ATOM   2565  C  C   . PRO A 1 317  ? 131.124 94.448  127.513 1.00 68.01  ? 317  PRO A C   1 
ATOM   2566  O  O   . PRO A 1 317  ? 130.138 93.742  127.291 1.00 74.46  ? 317  PRO A O   1 
ATOM   2567  C  CB  . PRO A 1 317  ? 132.822 93.741  129.244 1.00 64.16  ? 317  PRO A CB  1 
ATOM   2568  C  CG  . PRO A 1 317  ? 134.293 93.805  129.283 1.00 74.06  ? 317  PRO A CG  1 
ATOM   2569  C  CD  . PRO A 1 317  ? 134.721 94.681  128.151 1.00 74.20  ? 317  PRO A CD  1 
ATOM   2570  N  N   . ARG A 1 318  ? 131.082 95.768  127.566 1.00 68.20  ? 318  ARG A N   1 
ATOM   2571  C  CA  . ARG A 1 318  ? 129.828 96.498  127.394 1.00 71.66  ? 318  ARG A CA  1 
ATOM   2572  C  C   . ARG A 1 318  ? 129.129 96.194  126.068 1.00 74.59  ? 318  ARG A C   1 
ATOM   2573  O  O   . ARG A 1 318  ? 127.904 96.307  125.972 1.00 85.35  ? 318  ARG A O   1 
ATOM   2574  C  CB  . ARG A 1 318  ? 130.087 97.997  127.534 1.00 45.92  ? 318  ARG A CB  1 
ATOM   2575  C  CG  . ARG A 1 318  ? 128.818 98.796  127.689 1.00 56.05  ? 318  ARG A CG  1 
ATOM   2576  C  CD  . ARG A 1 318  ? 129.087 100.277 127.665 1.00 61.14  ? 318  ARG A CD  1 
ATOM   2577  N  NE  . ARG A 1 318  ? 129.927 100.651 128.799 1.00 73.87  ? 318  ARG A NE  1 
ATOM   2578  C  CZ  . ARG A 1 318  ? 129.456 101.055 129.975 1.00 65.65  ? 318  ARG A CZ  1 
ATOM   2579  N  NH1 . ARG A 1 318  ? 128.148 101.125 130.177 1.00 61.35  ? 318  ARG A NH1 1 
ATOM   2580  N  NH2 . ARG A 1 318  ? 130.294 101.374 130.952 1.00 56.81  ? 318  ARG A NH2 1 
ATOM   2581  N  N   . LYS A 1 319  ? 129.882 95.796  125.039 1.00 67.88  ? 319  LYS A N   1 
ATOM   2582  C  CA  . LYS A 1 319  ? 129.277 95.545  123.734 1.00 65.46  ? 319  LYS A CA  1 
ATOM   2583  C  C   . LYS A 1 319  ? 128.263 94.408  123.721 1.00 64.41  ? 319  LYS A C   1 
ATOM   2584  O  O   . LYS A 1 319  ? 127.480 94.322  122.771 1.00 76.24  ? 319  LYS A O   1 
ATOM   2585  C  CB  . LYS A 1 319  ? 130.359 95.227  122.704 1.00 60.10  ? 319  LYS A CB  1 
ATOM   2586  C  CG  . LYS A 1 319  ? 131.212 96.398  122.298 1.00 71.18  ? 319  LYS A CG  1 
ATOM   2587  C  CD  . LYS A 1 319  ? 132.024 96.055  121.071 1.00 62.87  ? 319  LYS A CD  1 
ATOM   2588  C  CE  . LYS A 1 319  ? 133.005 97.159  120.773 1.00 69.54  ? 319  LYS A CE  1 
ATOM   2589  N  NZ  . LYS A 1 319  ? 132.310 98.415  120.403 1.00 84.64  ? 319  LYS A NZ  1 
ATOM   2590  N  N   . TYR A 1 320  ? 128.241 93.543  124.732 1.00 64.35  ? 320  TYR A N   1 
ATOM   2591  C  CA  . TYR A 1 320  ? 127.273 92.452  124.768 1.00 60.43  ? 320  TYR A CA  1 
ATOM   2592  C  C   . TYR A 1 320  ? 126.099 92.688  125.718 1.00 66.16  ? 320  TYR A C   1 
ATOM   2593  O  O   . TYR A 1 320  ? 125.164 91.873  125.746 1.00 64.43  ? 320  TYR A O   1 
ATOM   2594  C  CB  . TYR A 1 320  ? 128.004 91.170  125.171 1.00 64.71  ? 320  TYR A CB  1 
ATOM   2595  C  CG  . TYR A 1 320  ? 128.771 90.553  124.026 1.00 80.06  ? 320  TYR A CG  1 
ATOM   2596  C  CD1 . TYR A 1 320  ? 130.041 91.020  123.708 1.00 76.27  ? 320  TYR A CD1 1 
ATOM   2597  C  CD2 . TYR A 1 320  ? 128.236 89.535  123.252 1.00 79.35  ? 320  TYR A CD2 1 
ATOM   2598  C  CE1 . TYR A 1 320  ? 130.763 90.485  122.664 1.00 63.82  ? 320  TYR A CE1 1 
ATOM   2599  C  CE2 . TYR A 1 320  ? 128.957 88.990  122.197 1.00 66.39  ? 320  TYR A CE2 1 
ATOM   2600  C  CZ  . TYR A 1 320  ? 130.220 89.472  121.910 1.00 66.47  ? 320  TYR A CZ  1 
ATOM   2601  O  OH  . TYR A 1 320  ? 130.947 88.941  120.868 1.00 73.61  ? 320  TYR A OH  1 
ATOM   2602  N  N   . TRP A 1 321  ? 126.110 93.792  126.464 1.00 60.92  ? 321  TRP A N   1 
ATOM   2603  C  CA  . TRP A 1 321  ? 125.052 94.052  127.436 1.00 58.49  ? 321  TRP A CA  1 
ATOM   2604  C  C   . TRP A 1 321  ? 123.685 94.225  126.782 1.00 62.04  ? 321  TRP A C   1 
ATOM   2605  O  O   . TRP A 1 321  ? 122.676 93.742  127.309 1.00 71.03  ? 321  TRP A O   1 
ATOM   2606  C  CB  . TRP A 1 321  ? 125.408 95.271  128.287 1.00 60.88  ? 321  TRP A CB  1 
ATOM   2607  C  CG  . TRP A 1 321  ? 126.542 94.990  129.215 1.00 57.87  ? 321  TRP A CG  1 
ATOM   2608  C  CD1 . TRP A 1 321  ? 127.160 93.789  129.404 1.00 63.08  ? 321  TRP A CD1 1 
ATOM   2609  C  CD2 . TRP A 1 321  ? 127.144 95.900  130.139 1.00 66.08  ? 321  TRP A CD2 1 
ATOM   2610  N  NE1 . TRP A 1 321  ? 128.142 93.906  130.356 1.00 63.84  ? 321  TRP A NE1 1 
ATOM   2611  C  CE2 . TRP A 1 321  ? 128.148 95.191  130.829 1.00 73.60  ? 321  TRP A CE2 1 
ATOM   2612  C  CE3 . TRP A 1 321  ? 126.943 97.250  130.441 1.00 72.94  ? 321  TRP A CE3 1 
ATOM   2613  C  CZ2 . TRP A 1 321  ? 128.948 95.787  131.800 1.00 73.93  ? 321  TRP A CZ2 1 
ATOM   2614  C  CZ3 . TRP A 1 321  ? 127.740 97.839  131.406 1.00 68.43  ? 321  TRP A CZ3 1 
ATOM   2615  C  CH2 . TRP A 1 321  ? 128.729 97.108  132.074 1.00 54.17  ? 321  TRP A CH2 1 
ATOM   2616  N  N   . PHE A 1 322  ? 123.622 94.937  125.654 1.00 62.20  ? 322  PHE A N   1 
ATOM   2617  C  CA  . PHE A 1 322  ? 122.333 95.148  124.998 1.00 59.71  ? 322  PHE A CA  1 
ATOM   2618  C  C   . PHE A 1 322  ? 121.729 93.826  124.540 1.00 54.94  ? 322  PHE A C   1 
ATOM   2619  O  O   . PHE A 1 322  ? 120.522 93.586  124.705 1.00 76.57  ? 322  PHE A O   1 
ATOM   2620  C  CB  . PHE A 1 322  ? 122.498 96.122  123.834 1.00 64.42  ? 322  PHE A CB  1 
ATOM   2621  C  CG  . PHE A 1 322  ? 121.197 96.559  123.237 1.00 54.87  ? 322  PHE A CG  1 
ATOM   2622  C  CD1 . PHE A 1 322  ? 120.193 97.055  124.051 1.00 61.45  ? 322  PHE A CD1 1 
ATOM   2623  C  CD2 . PHE A 1 322  ? 120.979 96.504  121.872 1.00 59.13  ? 322  PHE A CD2 1 
ATOM   2624  C  CE1 . PHE A 1 322  ? 118.987 97.465  123.523 1.00 67.83  ? 322  PHE A CE1 1 
ATOM   2625  C  CE2 . PHE A 1 322  ? 119.771 96.918  121.334 1.00 60.55  ? 322  PHE A CE2 1 
ATOM   2626  C  CZ  . PHE A 1 322  ? 118.775 97.399  122.162 1.00 58.57  ? 322  PHE A CZ  1 
ATOM   2627  N  N   . GLN A 1 323  ? 122.561 92.950  123.979 1.00 47.00  ? 323  GLN A N   1 
ATOM   2628  C  CA  . GLN A 1 323  ? 122.082 91.640  123.557 1.00 57.91  ? 323  GLN A CA  1 
ATOM   2629  C  C   . GLN A 1 323  ? 121.592 90.848  124.760 1.00 72.45  ? 323  GLN A C   1 
ATOM   2630  O  O   . GLN A 1 323  ? 120.560 90.167  124.691 1.00 72.91  ? 323  GLN A O   1 
ATOM   2631  C  CB  . GLN A 1 323  ? 123.178 90.861  122.852 1.00 62.73  ? 323  GLN A CB  1 
ATOM   2632  C  CG  . GLN A 1 323  ? 122.741 89.486  122.370 1.00 56.54  ? 323  GLN A CG  1 
ATOM   2633  C  CD  . GLN A 1 323  ? 123.840 88.699  121.709 1.00 53.67  ? 323  GLN A CD  1 
ATOM   2634  O  OE1 . GLN A 1 323  ? 124.502 87.877  122.344 1.00 66.22  ? 323  GLN A OE1 1 
ATOM   2635  N  NE2 . GLN A 1 323  ? 124.034 88.933  120.422 1.00 59.32  ? 323  GLN A NE2 1 
ATOM   2636  N  N   . SER A 1 324  ? 122.324 90.928  125.876 1.00 62.72  ? 324  SER A N   1 
ATOM   2637  C  CA  . SER A 1 324  ? 121.911 90.216  127.079 1.00 51.70  ? 324  SER A CA  1 
ATOM   2638  C  C   . SER A 1 324  ? 120.540 90.701  127.549 1.00 61.55  ? 324  SER A C   1 
ATOM   2639  O  O   . SER A 1 324  ? 119.661 89.891  127.884 1.00 65.19  ? 324  SER A O   1 
ATOM   2640  C  CB  . SER A 1 324  ? 122.947 90.450  128.176 1.00 51.24  ? 324  SER A CB  1 
ATOM   2641  O  OG  . SER A 1 324  ? 124.242 90.044  127.770 1.00 58.08  ? 324  SER A OG  1 
ATOM   2642  N  N   . GLN A 1 325  ? 120.330 92.018  127.535 1.00 55.91  ? 325  GLN A N   1 
ATOM   2643  C  CA  . GLN A 1 325  ? 119.056 92.582  127.968 1.00 55.78  ? 325  GLN A CA  1 
ATOM   2644  C  C   . GLN A 1 325  ? 117.904 92.123  127.079 1.00 64.58  ? 325  GLN A C   1 
ATOM   2645  O  O   . GLN A 1 325  ? 116.818 91.766  127.562 1.00 73.76  ? 325  GLN A O   1 
ATOM   2646  C  CB  . GLN A 1 325  ? 119.144 94.104  128.012 1.00 58.38  ? 325  GLN A CB  1 
ATOM   2647  C  CG  . GLN A 1 325  ? 120.084 94.642  129.082 1.00 71.54  ? 325  GLN A CG  1 
ATOM   2648  C  CD  . GLN A 1 325  ? 119.517 94.563  130.483 1.00 87.88  ? 325  GLN A CD  1 
ATOM   2649  O  OE1 . GLN A 1 325  ? 118.702 93.696  130.792 1.00 83.13  ? 325  GLN A OE1 1 
ATOM   2650  N  NE2 . GLN A 1 325  ? 119.945 95.482  131.341 1.00 100.70 ? 325  GLN A NE2 1 
ATOM   2651  N  N   . MET A 1 326  ? 118.130 92.108  125.755 1.00 67.50  ? 326  MET A N   1 
ATOM   2652  C  CA  . MET A 1 326  ? 117.071 91.686  124.824 1.00 58.56  ? 326  MET A CA  1 
ATOM   2653  C  C   . MET A 1 326  ? 116.715 90.221  125.025 1.00 60.94  ? 326  MET A C   1 
ATOM   2654  O  O   . MET A 1 326  ? 115.534 89.853  125.018 1.00 76.08  ? 326  MET A O   1 
ATOM   2655  C  CB  . MET A 1 326  ? 117.491 91.951  123.382 1.00 43.35  ? 326  MET A CB  1 
ATOM   2656  C  CG  . MET A 1 326  ? 117.525 93.433  122.975 1.00 53.54  ? 326  MET A CG  1 
ATOM   2657  S  SD  . MET A 1 326  ? 116.044 94.467  123.172 1.00 79.58  ? 326  MET A SD  1 
ATOM   2658  C  CE  . MET A 1 326  ? 116.294 94.996  124.848 1.00 67.26  ? 326  MET A CE  1 
ATOM   2659  N  N   . ILE A 1 327  ? 117.728 89.365  125.238 1.00 57.38  ? 327  ILE A N   1 
ATOM   2660  C  CA  . ILE A 1 327  ? 117.441 87.945  125.452 1.00 69.05  ? 327  ILE A CA  1 
ATOM   2661  C  C   . ILE A 1 327  ? 116.618 87.758  126.721 1.00 71.21  ? 327  ILE A C   1 
ATOM   2662  O  O   . ILE A 1 327  ? 115.634 86.996  126.741 1.00 78.55  ? 327  ILE A O   1 
ATOM   2663  C  CB  . ILE A 1 327  ? 118.752 87.141  125.508 1.00 61.79  ? 327  ILE A CB  1 
ATOM   2664  C  CG1 . ILE A 1 327  ? 119.420 87.098  124.135 1.00 59.85  ? 327  ILE A CG1 1 
ATOM   2665  C  CG2 . ILE A 1 327  ? 118.468 85.711  125.979 1.00 55.31  ? 327  ILE A CG2 1 
ATOM   2666  C  CD1 . ILE A 1 327  ? 120.715 86.308  124.113 1.00 50.35  ? 327  ILE A CD1 1 
ATOM   2667  N  N   . LYS A 1 328  ? 116.985 88.472  127.788 1.00 64.15  ? 328  LYS A N   1 
ATOM   2668  C  CA  . LYS A 1 328  ? 116.221 88.347  129.021 1.00 53.37  ? 328  LYS A CA  1 
ATOM   2669  C  C   . LYS A 1 328  ? 114.786 88.824  128.826 1.00 65.37  ? 328  LYS A C   1 
ATOM   2670  O  O   . LYS A 1 328  ? 113.843 88.193  129.322 1.00 75.27  ? 328  LYS A O   1 
ATOM   2671  C  CB  . LYS A 1 328  ? 116.895 89.135  130.140 1.00 66.53  ? 328  LYS A CB  1 
ATOM   2672  C  CG  . LYS A 1 328  ? 116.048 89.214  131.385 1.00 78.24  ? 328  LYS A CG  1 
ATOM   2673  C  CD  . LYS A 1 328  ? 116.659 90.117  132.428 1.00 75.65  ? 328  LYS A CD  1 
ATOM   2674  C  CE  . LYS A 1 328  ? 115.722 90.255  133.612 1.00 94.94  ? 328  LYS A CE  1 
ATOM   2675  N  NZ  . LYS A 1 328  ? 116.329 91.067  134.695 1.00 109.62 ? 328  LYS A NZ  1 
ATOM   2676  N  N   . SER A 1 329  ? 114.598 89.926  128.094 1.00 62.62  ? 329  SER A N   1 
ATOM   2677  C  CA  . SER A 1 329  ? 113.245 90.424  127.850 1.00 58.81  ? 329  SER A CA  1 
ATOM   2678  C  C   . SER A 1 329  ? 112.419 89.423  127.052 1.00 58.56  ? 329  SER A C   1 
ATOM   2679  O  O   . SER A 1 329  ? 111.235 89.199  127.347 1.00 72.80  ? 329  SER A O   1 
ATOM   2680  C  CB  . SER A 1 329  ? 113.300 91.760  127.112 1.00 55.98  ? 329  SER A CB  1 
ATOM   2681  O  OG  . SER A 1 329  ? 112.007 92.154  126.677 1.00 66.78  ? 329  SER A OG  1 
ATOM   2682  N  N   . TYR A 1 330  ? 113.042 88.785  126.058 1.00 66.96  ? 330  TYR A N   1 
ATOM   2683  C  CA  . TYR A 1 330  ? 112.326 87.824  125.229 1.00 52.34  ? 330  TYR A CA  1 
ATOM   2684  C  C   . TYR A 1 330  ? 111.846 86.645  126.060 1.00 55.10  ? 330  TYR A C   1 
ATOM   2685  O  O   . TYR A 1 330  ? 110.683 86.222  125.945 1.00 73.71  ? 330  TYR A O   1 
ATOM   2686  C  CB  . TYR A 1 330  ? 113.249 87.353  124.101 1.00 52.82  ? 330  TYR A CB  1 
ATOM   2687  C  CG  . TYR A 1 330  ? 112.641 86.375  123.119 1.00 57.96  ? 330  TYR A CG  1 
ATOM   2688  C  CD1 . TYR A 1 330  ? 112.636 85.012  123.377 1.00 67.21  ? 330  TYR A CD1 1 
ATOM   2689  C  CD2 . TYR A 1 330  ? 112.111 86.812  121.912 1.00 63.17  ? 330  TYR A CD2 1 
ATOM   2690  C  CE1 . TYR A 1 330  ? 112.091 84.113  122.479 1.00 54.31  ? 330  TYR A CE1 1 
ATOM   2691  C  CE2 . TYR A 1 330  ? 111.567 85.919  121.005 1.00 58.52  ? 330  TYR A CE2 1 
ATOM   2692  C  CZ  . TYR A 1 330  ? 111.559 84.572  121.294 1.00 55.29  ? 330  TYR A CZ  1 
ATOM   2693  O  OH  . TYR A 1 330  ? 111.020 83.682  120.392 1.00 55.59  ? 330  TYR A OH  1 
ATOM   2694  N  N   . TYR A 1 331  ? 112.692 86.152  126.967 1.00 56.42  ? 331  TYR A N   1 
ATOM   2695  C  CA  . TYR A 1 331  ? 112.227 85.013  127.756 1.00 52.31  ? 331  TYR A CA  1 
ATOM   2696  C  C   . TYR A 1 331  ? 111.239 85.429  128.833 1.00 60.45  ? 331  TYR A C   1 
ATOM   2697  O  O   . TYR A 1 331  ? 110.365 84.628  129.197 1.00 74.04  ? 331  TYR A O   1 
ATOM   2698  C  CB  . TYR A 1 331  ? 113.405 84.244  128.353 1.00 58.21  ? 331  TYR A CB  1 
ATOM   2699  C  CG  . TYR A 1 331  ? 114.038 83.346  127.324 1.00 66.10  ? 331  TYR A CG  1 
ATOM   2700  C  CD1 . TYR A 1 331  ? 113.349 82.242  126.836 1.00 65.53  ? 331  TYR A CD1 1 
ATOM   2701  C  CD2 . TYR A 1 331  ? 115.310 83.590  126.839 1.00 68.47  ? 331  TYR A CD2 1 
ATOM   2702  C  CE1 . TYR A 1 331  ? 113.910 81.412  125.888 1.00 51.80  ? 331  TYR A CE1 1 
ATOM   2703  C  CE2 . TYR A 1 331  ? 115.884 82.761  125.890 1.00 66.55  ? 331  TYR A CE2 1 
ATOM   2704  C  CZ  . TYR A 1 331  ? 115.178 81.672  125.420 1.00 64.09  ? 331  TYR A CZ  1 
ATOM   2705  O  OH  . TYR A 1 331  ? 115.740 80.842  124.475 1.00 58.53  ? 331  TYR A OH  1 
ATOM   2706  N  N   . ASP A 1 332  ? 111.373 86.640  129.370 1.00 65.09  ? 332  ASP A N   1 
ATOM   2707  C  CA  . ASP A 1 332  ? 110.383 87.130  130.329 1.00 66.10  ? 332  ASP A CA  1 
ATOM   2708  C  C   . ASP A 1 332  ? 108.997 87.127  129.698 1.00 68.62  ? 332  ASP A C   1 
ATOM   2709  O  O   . ASP A 1 332  ? 108.026 86.600  130.267 1.00 74.91  ? 332  ASP A O   1 
ATOM   2710  C  CB  . ASP A 1 332  ? 110.780 88.540  130.767 1.00 66.31  ? 332  ASP A CB  1 
ATOM   2711  C  CG  . ASP A 1 332  ? 111.922 88.543  131.749 1.00 88.59  ? 332  ASP A CG  1 
ATOM   2712  O  OD1 . ASP A 1 332  ? 112.527 87.465  131.941 1.00 85.93  ? 332  ASP A OD1 1 
ATOM   2713  O  OD2 . ASP A 1 332  ? 112.218 89.606  132.328 1.00 100.29 ? 332  ASP A OD2 1 
ATOM   2714  N  N   . GLU A 1 333  ? 108.907 87.706  128.491 1.00 71.40  ? 333  GLU A N   1 
ATOM   2715  C  CA  . GLU A 1 333  ? 107.675 87.684  127.708 1.00 60.73  ? 333  GLU A CA  1 
ATOM   2716  C  C   . GLU A 1 333  ? 107.157 86.269  127.530 1.00 59.52  ? 333  GLU A C   1 
ATOM   2717  O  O   . GLU A 1 333  ? 105.966 85.990  127.706 1.00 71.21  ? 333  GLU A O   1 
ATOM   2718  C  CB  . GLU A 1 333  ? 107.927 88.317  126.333 1.00 59.53  ? 333  GLU A CB  1 
ATOM   2719  C  CG  . GLU A 1 333  ? 107.694 89.825  126.206 1.00 77.81  ? 333  GLU A CG  1 
ATOM   2720  C  CD  . GLU A 1 333  ? 106.314 90.246  126.676 1.00 108.97 ? 333  GLU A CD  1 
ATOM   2721  O  OE1 . GLU A 1 333  ? 105.434 89.371  126.835 1.00 109.61 ? 333  GLU A OE1 1 
ATOM   2722  O  OE2 . GLU A 1 333  ? 106.083 91.456  126.891 1.00 114.74 ? 333  GLU A OE2 1 
ATOM   2723  N  N   . LEU A 1 334  ? 108.058 85.362  127.129 1.00 57.16  ? 334  LEU A N   1 
ATOM   2724  C  CA  . LEU A 1 334  ? 107.639 83.989  126.898 1.00 59.00  ? 334  LEU A CA  1 
ATOM   2725  C  C   . LEU A 1 334  ? 107.033 83.386  128.160 1.00 78.27  ? 334  LEU A C   1 
ATOM   2726  O  O   . LEU A 1 334  ? 106.020 82.677  128.094 1.00 83.79  ? 334  LEU A O   1 
ATOM   2727  C  CB  . LEU A 1 334  ? 108.822 83.166  126.404 1.00 56.24  ? 334  LEU A CB  1 
ATOM   2728  C  CG  . LEU A 1 334  ? 108.431 81.841  125.770 1.00 49.52  ? 334  LEU A CG  1 
ATOM   2729  C  CD1 . LEU A 1 334  ? 107.195 82.026  124.901 1.00 62.74  ? 334  LEU A CD1 1 
ATOM   2730  C  CD2 . LEU A 1 334  ? 109.593 81.340  124.949 1.00 55.75  ? 334  LEU A CD2 1 
ATOM   2731  N  N   . HIS A 1 335  ? 107.676 83.602  129.312 1.00 83.64  ? 335  HIS A N   1 
ATOM   2732  C  CA  . HIS A 1 335  ? 107.189 83.043  130.571 1.00 77.04  ? 335  HIS A CA  1 
ATOM   2733  C  C   . HIS A 1 335  ? 105.804 83.567  130.919 1.00 77.73  ? 335  HIS A C   1 
ATOM   2734  O  O   . HIS A 1 335  ? 104.937 82.805  131.390 1.00 85.04  ? 335  HIS A O   1 
ATOM   2735  C  CB  . HIS A 1 335  ? 108.158 83.363  131.706 1.00 83.17  ? 335  HIS A CB  1 
ATOM   2736  C  CG  . HIS A 1 335  ? 107.741 82.784  133.020 1.00 102.72 ? 335  HIS A CG  1 
ATOM   2737  N  ND1 . HIS A 1 335  ? 108.194 81.567  133.478 1.00 119.30 ? 335  HIS A ND1 1 
ATOM   2738  C  CD2 . HIS A 1 335  ? 106.900 83.258  133.973 1.00 99.84  ? 335  HIS A CD2 1 
ATOM   2739  C  CE1 . HIS A 1 335  ? 107.651 81.315  134.656 1.00 124.07 ? 335  HIS A CE1 1 
ATOM   2740  N  NE2 . HIS A 1 335  ? 106.864 82.325  134.979 1.00 112.35 ? 335  HIS A NE2 1 
ATOM   2741  N  N   . ASP A 1 336  ? 105.528 84.823  130.558 1.00 82.59  ? 336  ASP A N   1 
ATOM   2742  C  CA  . ASP A 1 336  ? 104.189 85.341  130.817 1.00 75.43  ? 336  ASP A CA  1 
ATOM   2743  C  C   . ASP A 1 336  ? 103.193 84.613  129.936 1.00 73.94  ? 336  ASP A C   1 
ATOM   2744  O  O   . ASP A 1 336  ? 102.139 84.165  130.408 1.00 79.31  ? 336  ASP A O   1 
ATOM   2745  C  CB  . ASP A 1 336  ? 104.134 86.845  130.573 1.00 75.48  ? 336  ASP A CB  1 
ATOM   2746  C  CG  . ASP A 1 336  ? 105.052 87.614  131.492 1.00 97.86  ? 336  ASP A CG  1 
ATOM   2747  O  OD1 . ASP A 1 336  ? 105.508 88.709  131.100 1.00 100.04 ? 336  ASP A OD1 1 
ATOM   2748  O  OD2 . ASP A 1 336  ? 105.335 87.113  132.600 1.00 103.46 ? 336  ASP A OD2 1 
ATOM   2749  N  N   . LEU A 1 337  ? 103.500 84.507  128.646 1.00 79.94  ? 337  LEU A N   1 
ATOM   2750  C  CA  . LEU A 1 337  ? 102.525 83.914  127.743 1.00 68.58  ? 337  LEU A CA  1 
ATOM   2751  C  C   . LEU A 1 337  ? 102.270 82.469  128.157 1.00 66.79  ? 337  LEU A C   1 
ATOM   2752  O  O   . LEU A 1 337  ? 101.121 82.010  128.174 1.00 83.58  ? 337  LEU A O   1 
ATOM   2753  C  CB  . LEU A 1 337  ? 103.014 83.998  126.300 1.00 65.29  ? 337  LEU A CB  1 
ATOM   2754  C  CG  . LEU A 1 337  ? 103.221 85.428  125.802 1.00 61.83  ? 337  LEU A CG  1 
ATOM   2755  C  CD1 . LEU A 1 337  ? 103.588 85.429  124.332 1.00 59.67  ? 337  LEU A CD1 1 
ATOM   2756  C  CD2 . LEU A 1 337  ? 101.949 86.235  126.040 1.00 77.89  ? 337  LEU A CD2 1 
ATOM   2757  N  N   . ASN A 1 338  ? 103.339 81.735  128.498 1.00 65.28  ? 338  ASN A N   1 
ATOM   2758  C  CA  . ASN A 1 338  ? 103.193 80.339  128.905 1.00 75.64  ? 338  ASN A CA  1 
ATOM   2759  C  C   . ASN A 1 338  ? 102.378 80.167  130.185 1.00 88.85  ? 338  ASN A C   1 
ATOM   2760  O  O   . ASN A 1 338  ? 101.769 79.106  130.372 1.00 88.46  ? 338  ASN A O   1 
ATOM   2761  C  CB  . ASN A 1 338  ? 104.576 79.694  129.057 1.00 91.23  ? 338  ASN A CB  1 
ATOM   2762  C  CG  . ASN A 1 338  ? 105.236 79.390  127.717 1.00 98.33  ? 338  ASN A CG  1 
ATOM   2763  O  OD1 . ASN A 1 338  ? 104.764 79.828  126.663 1.00 101.78 ? 338  ASN A OD1 1 
ATOM   2764  N  ND2 . ASN A 1 338  ? 106.315 78.619  127.752 1.00 95.80  ? 338  ASN A ND2 1 
ATOM   2765  N  N   . LEU A 1 339  ? 102.324 81.169  131.073 1.00 85.65  ? 339  LEU A N   1 
ATOM   2766  C  CA  . LEU A 1 339  ? 101.392 80.971  132.186 1.00 79.94  ? 339  LEU A CA  1 
ATOM   2767  C  C   . LEU A 1 339  ? 99.999  81.477  131.908 1.00 78.12  ? 339  LEU A C   1 
ATOM   2768  O  O   . LEU A 1 339  ? 99.054  81.062  132.581 1.00 86.73  ? 339  LEU A O   1 
ATOM   2769  C  CB  . LEU A 1 339  ? 101.817 81.579  133.526 1.00 84.18  ? 339  LEU A CB  1 
ATOM   2770  C  CG  . LEU A 1 339  ? 102.817 80.771  134.328 1.00 104.41 ? 339  LEU A CG  1 
ATOM   2771  C  CD1 . LEU A 1 339  ? 103.041 81.476  135.667 1.00 105.89 ? 339  LEU A CD1 1 
ATOM   2772  C  CD2 . LEU A 1 339  ? 102.244 79.366  134.503 1.00 115.28 ? 339  LEU A CD2 1 
ATOM   2773  N  N   . LYS A 1 340  ? 99.843  82.394  130.966 1.00 84.29  ? 340  LYS A N   1 
ATOM   2774  C  CA  . LYS A 1 340  ? 98.493  82.833  130.713 1.00 85.96  ? 340  LYS A CA  1 
ATOM   2775  C  C   . LYS A 1 340  ? 97.709  81.775  129.951 1.00 84.82  ? 340  LYS A C   1 
ATOM   2776  O  O   . LYS A 1 340  ? 96.488  81.695  130.114 1.00 93.86  ? 340  LYS A O   1 
ATOM   2777  C  CB  . LYS A 1 340  ? 98.495  84.169  129.959 1.00 88.12  ? 340  LYS A CB  1 
ATOM   2778  C  CG  . LYS A 1 340  ? 97.101  84.713  129.663 1.00 89.93  ? 340  LYS A CG  1 
ATOM   2779  C  CD  . LYS A 1 340  ? 97.207  86.093  129.053 1.00 110.85 ? 340  LYS A CD  1 
ATOM   2780  C  CE  . LYS A 1 340  ? 97.800  86.021  127.658 1.00 119.38 ? 340  LYS A CE  1 
ATOM   2781  N  NZ  . LYS A 1 340  ? 96.890  85.311  126.719 1.00 115.28 ? 340  LYS A NZ  1 
ATOM   2782  N  N   . LEU A 1 341  ? 98.366  80.935  129.162 1.00 87.20  ? 341  LEU A N   1 
ATOM   2783  C  CA  . LEU A 1 341  ? 97.681  79.873  128.445 1.00 76.55  ? 341  LEU A CA  1 
ATOM   2784  C  C   . LEU A 1 341  ? 97.970  78.470  128.979 1.00 96.08  ? 341  LEU A C   1 
ATOM   2785  O  O   . LEU A 1 341  ? 97.488  77.498  128.384 1.00 102.56 ? 341  LEU A O   1 
ATOM   2786  C  CB  . LEU A 1 341  ? 98.034  79.950  126.956 1.00 68.46  ? 341  LEU A CB  1 
ATOM   2787  C  CG  . LEU A 1 341  ? 97.943  81.374  126.391 1.00 92.57  ? 341  LEU A CG  1 
ATOM   2788  C  CD1 . LEU A 1 341  ? 98.233  81.388  124.878 1.00 78.76  ? 341  LEU A CD1 1 
ATOM   2789  C  CD2 . LEU A 1 341  ? 96.623  82.127  126.727 1.00 112.87 ? 341  LEU A CD2 1 
ATOM   2790  N  N   . GLN A 1 342  ? 98.728  78.332  130.064 1.00 98.15  ? 342  GLN A N   1 
ATOM   2791  C  CA  . GLN A 1 342  ? 99.029  77.022  130.658 1.00 112.28 ? 342  GLN A CA  1 
ATOM   2792  C  C   . GLN A 1 342  ? 99.631  76.056  129.638 1.00 118.49 ? 342  GLN A C   1 
ATOM   2793  O  O   . GLN A 1 342  ? 99.181  74.921  129.488 1.00 116.16 ? 342  GLN A O   1 
ATOM   2794  C  CB  . GLN A 1 342  ? 97.758  76.423  131.265 1.00 117.00 ? 342  GLN A CB  1 
ATOM   2795  C  CG  . GLN A 1 342  ? 96.929  77.379  132.093 1.00 121.17 ? 342  GLN A CG  1 
ATOM   2796  C  CD  . GLN A 1 342  ? 95.494  76.901  132.237 1.00 126.33 ? 342  GLN A CD  1 
ATOM   2797  O  OE1 . GLN A 1 342  ? 95.226  75.699  132.203 1.00 120.65 ? 342  GLN A OE1 1 
ATOM   2798  N  NE2 . GLN A 1 342  ? 94.564  77.838  132.381 1.00 113.99 ? 342  GLN A NE2 1 
ATOM   2799  N  N   . ILE A 1 343  ? 100.646 76.520  128.917 1.00 118.02 ? 343  ILE A N   1 
ATOM   2800  C  CA  . ILE A 1 343  ? 101.284 75.712  127.880 1.00 123.55 ? 343  ILE A CA  1 
ATOM   2801  C  C   . ILE A 1 343  ? 102.432 74.920  128.494 1.00 131.60 ? 343  ILE A C   1 
ATOM   2802  O  O   . ILE A 1 343  ? 103.268 75.476  129.217 1.00 127.21 ? 343  ILE A O   1 
ATOM   2803  C  CB  . ILE A 1 343  ? 101.781 76.587  126.718 1.00 106.83 ? 343  ILE A CB  1 
ATOM   2804  C  CG1 . ILE A 1 343  ? 100.608 77.311  126.058 1.00 109.66 ? 343  ILE A CG1 1 
ATOM   2805  C  CG2 . ILE A 1 343  ? 102.505 75.736  125.685 1.00 114.35 ? 343  ILE A CG2 1 
ATOM   2806  C  CD1 . ILE A 1 343  ? 101.018 78.210  124.914 1.00 94.26  ? 343  ILE A CD1 1 
ATOM   2807  N  N   . SER A 1 344  ? 102.468 73.619  128.211 1.00 134.16 ? 344  SER A N   1 
ATOM   2808  C  CA  . SER A 1 344  ? 103.586 72.790  128.636 1.00 133.92 ? 344  SER A CA  1 
ATOM   2809  C  C   . SER A 1 344  ? 104.855 73.188  127.892 1.00 141.06 ? 344  SER A C   1 
ATOM   2810  O  O   . SER A 1 344  ? 104.812 73.741  126.789 1.00 143.71 ? 344  SER A O   1 
ATOM   2811  C  CB  . SER A 1 344  ? 103.274 71.315  128.393 1.00 135.23 ? 344  SER A CB  1 
ATOM   2812  O  OG  . SER A 1 344  ? 102.984 71.076  127.026 1.00 129.05 ? 344  SER A OG  1 
ATOM   2813  N  N   . ASP A 1 345  ? 106.000 72.893  128.513 1.00 140.82 ? 345  ASP A N   1 
ATOM   2814  C  CA  . ASP A 1 345  ? 107.285 73.290  127.942 1.00 136.26 ? 345  ASP A CA  1 
ATOM   2815  C  C   . ASP A 1 345  ? 107.556 72.602  126.609 1.00 132.46 ? 345  ASP A C   1 
ATOM   2816  O  O   . ASP A 1 345  ? 108.123 73.210  125.694 1.00 124.05 ? 345  ASP A O   1 
ATOM   2817  C  CB  . ASP A 1 345  ? 108.412 72.998  128.935 1.00 143.27 ? 345  ASP A CB  1 
ATOM   2818  C  CG  . ASP A 1 345  ? 108.551 71.520  129.242 1.00 144.73 ? 345  ASP A CG  1 
ATOM   2819  O  OD1 . ASP A 1 345  ? 107.812 71.019  130.115 1.00 134.89 ? 345  ASP A OD1 1 
ATOM   2820  O  OD2 . ASP A 1 345  ? 109.395 70.856  128.604 1.00 141.28 ? 345  ASP A OD2 1 
ATOM   2821  N  N   . ASN A 1 346  ? 107.164 71.332  126.478 1.00 138.86 ? 346  ASN A N   1 
ATOM   2822  C  CA  . ASN A 1 346  ? 107.418 70.598  125.243 1.00 134.32 ? 346  ASN A CA  1 
ATOM   2823  C  C   . ASN A 1 346  ? 106.589 71.096  124.068 1.00 125.69 ? 346  ASN A C   1 
ATOM   2824  O  O   . ASN A 1 346  ? 106.938 70.810  122.918 1.00 127.66 ? 346  ASN A O   1 
ATOM   2825  C  CB  . ASN A 1 346  ? 107.130 69.109  125.449 1.00 138.89 ? 346  ASN A CB  1 
ATOM   2826  C  CG  . ASN A 1 346  ? 108.241 68.393  126.186 1.00 148.25 ? 346  ASN A CG  1 
ATOM   2827  O  OD1 . ASN A 1 346  ? 109.342 68.919  126.338 1.00 147.64 ? 346  ASN A OD1 1 
ATOM   2828  N  ND2 . ASN A 1 346  ? 107.958 67.179  126.645 1.00 140.40 ? 346  ASN A ND2 1 
ATOM   2829  N  N   . LYS A 1 347  ? 105.503 71.825  124.322 1.00 125.16 ? 347  LYS A N   1 
ATOM   2830  C  CA  . LYS A 1 347  ? 104.677 72.324  123.227 1.00 132.30 ? 347  LYS A CA  1 
ATOM   2831  C  C   . LYS A 1 347  ? 105.277 73.554  122.549 1.00 123.01 ? 347  LYS A C   1 
ATOM   2832  O  O   . LYS A 1 347  ? 105.158 73.709  121.327 1.00 120.06 ? 347  LYS A O   1 
ATOM   2833  C  CB  . LYS A 1 347  ? 103.268 72.622  123.743 1.00 133.13 ? 347  LYS A CB  1 
ATOM   2834  C  CG  . LYS A 1 347  ? 102.333 73.210  122.706 1.00 134.93 ? 347  LYS A CG  1 
ATOM   2835  C  CD  . LYS A 1 347  ? 102.032 72.181  121.628 1.00 134.09 ? 347  LYS A CD  1 
ATOM   2836  C  CE  . LYS A 1 347  ? 101.100 71.095  122.141 1.00 133.96 ? 347  LYS A CE  1 
ATOM   2837  N  NZ  . LYS A 1 347  ? 99.730  71.607  122.410 1.00 113.60 ? 347  LYS A NZ  1 
ATOM   2838  N  N   . ALA A 1 348  ? 105.931 74.428  123.309 1.00 119.52 ? 348  ALA A N   1 
ATOM   2839  C  CA  . ALA A 1 348  ? 106.398 75.719  122.795 1.00 101.33 ? 348  ALA A CA  1 
ATOM   2840  C  C   . ALA A 1 348  ? 107.876 75.684  122.401 1.00 111.48 ? 348  ALA A C   1 
ATOM   2841  O  O   . ALA A 1 348  ? 108.719 76.364  122.989 1.00 107.79 ? 348  ALA A O   1 
ATOM   2842  C  CB  . ALA A 1 348  ? 106.133 76.814  123.823 1.00 97.44  ? 348  ALA A CB  1 
ATOM   2843  N  N   . GLU A 1 349  ? 108.193 74.885  121.384 1.00 98.65  ? 349  GLU A N   1 
ATOM   2844  C  CA  . GLU A 1 349  ? 109.550 74.840  120.850 1.00 82.20  ? 349  GLU A CA  1 
ATOM   2845  C  C   . GLU A 1 349  ? 109.809 75.880  119.767 1.00 84.22  ? 349  GLU A C   1 
ATOM   2846  O  O   . GLU A 1 349  ? 110.969 76.260  119.549 1.00 88.50  ? 349  GLU A O   1 
ATOM   2847  C  CB  . GLU A 1 349  ? 109.860 73.458  120.271 1.00 90.87  ? 349  GLU A CB  1 
ATOM   2848  C  CG  . GLU A 1 349  ? 110.587 72.529  121.217 1.00 124.05 ? 349  GLU A CG  1 
ATOM   2849  C  CD  . GLU A 1 349  ? 110.866 71.183  120.584 1.00 148.22 ? 349  GLU A CD  1 
ATOM   2850  O  OE1 . GLU A 1 349  ? 110.892 71.111  119.336 1.00 135.12 ? 349  GLU A OE1 1 
ATOM   2851  O  OE2 . GLU A 1 349  ? 111.062 70.201  121.330 1.00 148.74 ? 349  GLU A OE2 1 
ATOM   2852  N  N   . CYS A 1 350  ? 108.756 76.357  119.098 1.00 81.71  ? 350  CYS A N   1 
ATOM   2853  C  CA  . CYS A 1 350  ? 108.925 77.298  117.996 1.00 58.63  ? 350  CYS A CA  1 
ATOM   2854  C  C   . CYS A 1 350  ? 109.496 78.637  118.454 1.00 70.73  ? 350  CYS A C   1 
ATOM   2855  O  O   . CYS A 1 350  ? 110.306 79.238  117.740 1.00 81.22  ? 350  CYS A O   1 
ATOM   2856  C  CB  . CYS A 1 350  ? 107.586 77.497  117.286 1.00 67.27  ? 350  CYS A CB  1 
ATOM   2857  S  SG  . CYS A 1 350  ? 106.233 77.980  118.385 1.00 97.37  ? 350  CYS A SG  1 
ATOM   2858  N  N   . ALA A 1 351  ? 109.101 79.124  119.632 1.00 59.09  ? 351  ALA A N   1 
ATOM   2859  C  CA  . ALA A 1 351  ? 109.613 80.413  120.098 1.00 63.68  ? 351  ALA A CA  1 
ATOM   2860  C  C   . ALA A 1 351  ? 111.118 80.351  120.358 1.00 79.62  ? 351  ALA A C   1 
ATOM   2861  O  O   . ALA A 1 351  ? 111.886 81.237  119.937 1.00 85.88  ? 351  ALA A O   1 
ATOM   2862  C  CB  . ALA A 1 351  ? 108.859 80.841  121.357 1.00 54.03  ? 351  ALA A CB  1 
ATOM   2863  N  N   . GLN A 1 352  ? 111.558 79.288  121.034 1.00 63.45  ? 352  GLN A N   1 
ATOM   2864  C  CA  . GLN A 1 352  ? 112.980 79.099  121.276 1.00 49.12  ? 352  GLN A CA  1 
ATOM   2865  C  C   . GLN A 1 352  ? 113.740 78.911  119.971 1.00 72.15  ? 352  GLN A C   1 
ATOM   2866  O  O   . GLN A 1 352  ? 114.852 79.428  119.817 1.00 83.23  ? 352  GLN A O   1 
ATOM   2867  C  CB  . GLN A 1 352  ? 113.186 77.906  122.204 1.00 62.38  ? 352  GLN A CB  1 
ATOM   2868  C  CG  . GLN A 1 352  ? 112.659 78.144  123.606 1.00 70.37  ? 352  GLN A CG  1 
ATOM   2869  C  CD  . GLN A 1 352  ? 112.026 76.906  124.199 1.00 78.74  ? 352  GLN A CD  1 
ATOM   2870  O  OE1 . GLN A 1 352  ? 112.168 75.805  123.666 1.00 83.64  ? 352  GLN A OE1 1 
ATOM   2871  N  NE2 . GLN A 1 352  ? 111.298 77.081  125.295 1.00 79.99  ? 352  GLN A NE2 1 
ATOM   2872  N  N   . ASN A 1 353  ? 113.167 78.165  119.020 1.00 63.74  ? 353  ASN A N   1 
ATOM   2873  C  CA  . ASN A 1 353  ? 113.842 78.026  117.732 1.00 56.54  ? 353  ASN A CA  1 
ATOM   2874  C  C   . ASN A 1 353  ? 113.949 79.365  117.015 1.00 64.23  ? 353  ASN A C   1 
ATOM   2875  O  O   . ASN A 1 353  ? 114.939 79.617  116.330 1.00 71.27  ? 353  ASN A O   1 
ATOM   2876  C  CB  . ASN A 1 353  ? 113.135 76.993  116.863 1.00 61.21  ? 353  ASN A CB  1 
ATOM   2877  C  CG  . ASN A 1 353  ? 113.282 75.592  117.408 1.00 71.45  ? 353  ASN A CG  1 
ATOM   2878  O  OD1 . ASN A 1 353  ? 114.239 75.294  118.124 1.00 65.47  ? 353  ASN A OD1 1 
ATOM   2879  N  ND2 . ASN A 1 353  ? 112.346 74.719  117.064 1.00 99.23  ? 353  ASN A ND2 1 
ATOM   2880  N  N   . PHE A 1 354  ? 112.946 80.231  117.161 1.00 60.37  ? 354  PHE A N   1 
ATOM   2881  C  CA  . PHE A 1 354  ? 112.988 81.551  116.534 1.00 50.68  ? 354  PHE A CA  1 
ATOM   2882  C  C   . PHE A 1 354  ? 114.173 82.362  117.050 1.00 59.28  ? 354  PHE A C   1 
ATOM   2883  O  O   . PHE A 1 354  ? 115.031 82.828  116.267 1.00 69.74  ? 354  PHE A O   1 
ATOM   2884  C  CB  . PHE A 1 354  ? 111.660 82.257  116.808 1.00 47.04  ? 354  PHE A CB  1 
ATOM   2885  C  CG  . PHE A 1 354  ? 111.416 83.477  115.970 1.00 60.10  ? 354  PHE A CG  1 
ATOM   2886  C  CD1 . PHE A 1 354  ? 111.043 83.358  114.642 1.00 66.54  ? 354  PHE A CD1 1 
ATOM   2887  C  CD2 . PHE A 1 354  ? 111.512 84.743  116.522 1.00 68.71  ? 354  PHE A CD2 1 
ATOM   2888  C  CE1 . PHE A 1 354  ? 110.799 84.481  113.873 1.00 53.88  ? 354  PHE A CE1 1 
ATOM   2889  C  CE2 . PHE A 1 354  ? 111.270 85.871  115.757 1.00 49.37  ? 354  PHE A CE2 1 
ATOM   2890  C  CZ  . PHE A 1 354  ? 110.913 85.739  114.432 1.00 37.09  ? 354  PHE A CZ  1 
ATOM   2891  N  N   . ILE A 1 355  ? 114.270 82.480  118.384 1.00 54.38  ? 355  ILE A N   1 
ATOM   2892  C  CA  . ILE A 1 355  ? 115.376 83.247  118.955 1.00 46.87  ? 355  ILE A CA  1 
ATOM   2893  C  C   . ILE A 1 355  ? 116.730 82.605  118.621 1.00 61.53  ? 355  ILE A C   1 
ATOM   2894  O  O   . ILE A 1 355  ? 117.680 83.326  118.278 1.00 64.74  ? 355  ILE A O   1 
ATOM   2895  C  CB  . ILE A 1 355  ? 115.205 83.428  120.479 1.00 58.87  ? 355  ILE A CB  1 
ATOM   2896  C  CG1 . ILE A 1 355  ? 116.402 84.209  121.043 1.00 41.08  ? 355  ILE A CG1 1 
ATOM   2897  C  CG2 . ILE A 1 355  ? 115.072 82.087  121.192 1.00 79.64  ? 355  ILE A CG2 1 
ATOM   2898  C  CD1 . ILE A 1 355  ? 116.389 85.650  120.711 1.00 59.04  ? 355  ILE A CD1 1 
ATOM   2899  N  N   . LYS A 1 356  ? 116.823 81.253  118.677 1.00 55.15  ? 356  LYS A N   1 
ATOM   2900  C  CA  . LYS A 1 356  ? 118.081 80.605  118.398 1.00 45.59  ? 356  LYS A CA  1 
ATOM   2901  C  C   . LYS A 1 356  ? 118.467 80.789  116.930 1.00 50.25  ? 356  LYS A C   1 
ATOM   2902  O  O   . LYS A 1 356  ? 119.654 80.938  116.603 1.00 63.69  ? 356  LYS A O   1 
ATOM   2903  C  CB  . LYS A 1 356  ? 118.066 79.086  118.655 1.00 53.55  ? 356  LYS A CB  1 
ATOM   2904  C  CG  . LYS A 1 356  ? 118.000 78.663  120.177 1.00 49.74  ? 356  LYS A CG  1 
ATOM   2905  C  CD  . LYS A 1 356  ? 118.023 77.156  120.190 1.00 70.61  ? 356  LYS A CD  1 
ATOM   2906  C  CE  . LYS A 1 356  ? 117.837 76.597  121.574 1.00 85.71  ? 356  LYS A CE  1 
ATOM   2907  N  NZ  . LYS A 1 356  ? 116.604 76.914  122.292 1.00 82.50  ? 356  LYS A NZ  1 
ATOM   2908  N  N   . THR A 1 357  ? 117.502 80.751  116.017 1.00 60.70  ? 357  THR A N   1 
ATOM   2909  C  CA  . THR A 1 357  ? 117.832 80.951  114.604 1.00 66.56  ? 357  THR A CA  1 
ATOM   2910  C  C   . THR A 1 357  ? 118.420 82.334  114.373 1.00 58.22  ? 357  THR A C   1 
ATOM   2911  O  O   . THR A 1 357  ? 119.395 82.497  113.622 1.00 58.38  ? 357  THR A O   1 
ATOM   2912  C  CB  . THR A 1 357  ? 116.610 80.745  113.701 1.00 62.14  ? 357  THR A CB  1 
ATOM   2913  O  OG1 . THR A 1 357  ? 116.096 79.428  113.906 1.00 70.59  ? 357  THR A OG1 1 
ATOM   2914  C  CG2 . THR A 1 357  ? 116.979 80.920  112.237 1.00 61.32  ? 357  THR A CG2 1 
ATOM   2915  N  N   . ILE A 1 358  ? 117.856 83.349  115.032 1.00 72.20  ? 358  ILE A N   1 
ATOM   2916  C  CA  . ILE A 1 358  ? 118.417 84.692  114.860 1.00 62.46  ? 358  ILE A CA  1 
ATOM   2917  C  C   . ILE A 1 358  ? 119.833 84.769  115.432 1.00 71.22  ? 358  ILE A C   1 
ATOM   2918  O  O   . ILE A 1 358  ? 120.756 85.269  114.779 1.00 78.07  ? 358  ILE A O   1 
ATOM   2919  C  CB  . ILE A 1 358  ? 117.519 85.761  115.499 1.00 74.52  ? 358  ILE A CB  1 
ATOM   2920  C  CG1 . ILE A 1 358  ? 116.125 85.742  114.879 1.00 66.70  ? 358  ILE A CG1 1 
ATOM   2921  C  CG2 . ILE A 1 358  ? 118.156 87.145  115.346 1.00 50.77  ? 358  ILE A CG2 1 
ATOM   2922  C  CD1 . ILE A 1 358  ? 115.171 86.701  115.544 1.00 73.35  ? 358  ILE A CD1 1 
ATOM   2923  N  N   . VAL A 1 359  ? 120.034 84.258  116.648 1.00 70.19  ? 359  VAL A N   1 
ATOM   2924  C  CA  . VAL A 1 359  ? 121.307 84.498  117.327 1.00 64.98  ? 359  VAL A CA  1 
ATOM   2925  C  C   . VAL A 1 359  ? 122.419 83.637  116.744 1.00 62.34  ? 359  VAL A C   1 
ATOM   2926  O  O   . VAL A 1 359  ? 123.525 84.125  116.484 1.00 76.50  ? 359  VAL A O   1 
ATOM   2927  C  CB  . VAL A 1 359  ? 121.167 84.275  118.845 1.00 59.18  ? 359  VAL A CB  1 
ATOM   2928  C  CG1 . VAL A 1 359  ? 122.546 84.133  119.484 1.00 39.06  ? 359  VAL A CG1 1 
ATOM   2929  C  CG2 . VAL A 1 359  ? 120.427 85.432  119.480 1.00 61.04  ? 359  VAL A CG2 1 
ATOM   2930  N  N   . GLN A 1 360  ? 122.146 82.361  116.504 1.00 65.60  ? 360  GLN A N   1 
ATOM   2931  C  CA  . GLN A 1 360  ? 123.198 81.407  116.167 1.00 53.85  ? 360  GLN A CA  1 
ATOM   2932  C  C   . GLN A 1 360  ? 123.706 81.523  114.738 1.00 53.05  ? 360  GLN A C   1 
ATOM   2933  O  O   . GLN A 1 360  ? 124.762 80.951  114.432 1.00 61.92  ? 360  GLN A O   1 
ATOM   2934  C  CB  . GLN A 1 360  ? 122.657 80.008  116.400 1.00 51.00  ? 360  GLN A CB  1 
ATOM   2935  C  CG  . GLN A 1 360  ? 122.621 79.621  117.848 1.00 61.20  ? 360  GLN A CG  1 
ATOM   2936  C  CD  . GLN A 1 360  ? 122.302 78.171  118.048 1.00 64.63  ? 360  GLN A CD  1 
ATOM   2937  O  OE1 . GLN A 1 360  ? 121.587 77.816  118.977 1.00 60.17  ? 360  GLN A OE1 1 
ATOM   2938  N  NE2 . GLN A 1 360  ? 122.876 77.310  117.207 1.00 68.75  ? 360  GLN A NE2 1 
ATOM   2939  N  N   . ALA A 1 361  ? 123.006 82.230  113.858 1.00 61.16  ? 361  ALA A N   1 
ATOM   2940  C  CA  . ALA A 1 361  ? 123.526 82.492  112.517 1.00 60.69  ? 361  ALA A CA  1 
ATOM   2941  C  C   . ALA A 1 361  ? 124.598 83.567  112.625 1.00 73.62  ? 361  ALA A C   1 
ATOM   2942  O  O   . ALA A 1 361  ? 124.310 84.684  113.071 1.00 80.24  ? 361  ALA A O   1 
ATOM   2943  C  CB  . ALA A 1 361  ? 122.405 82.918  111.573 1.00 51.69  ? 361  ALA A CB  1 
ATOM   2944  N  N   . LYS A 1 362  ? 125.829 83.245  112.226 1.00 67.03  ? 362  LYS A N   1 
ATOM   2945  C  CA  . LYS A 1 362  ? 126.945 84.180  112.381 1.00 62.56  ? 362  LYS A CA  1 
ATOM   2946  C  C   . LYS A 1 362  ? 127.139 84.925  111.065 1.00 74.45  ? 362  LYS A C   1 
ATOM   2947  O  O   . LYS A 1 362  ? 128.022 84.626  110.266 1.00 86.61  ? 362  LYS A O   1 
ATOM   2948  C  CB  . LYS A 1 362  ? 128.213 83.443  112.799 1.00 76.48  ? 362  LYS A CB  1 
ATOM   2949  C  CG  . LYS A 1 362  ? 128.108 82.742  114.130 1.00 85.74  ? 362  LYS A CG  1 
ATOM   2950  C  CD  . LYS A 1 362  ? 128.075 83.773  115.240 1.00 84.77  ? 362  LYS A CD  1 
ATOM   2951  C  CE  . LYS A 1 362  ? 128.074 83.126  116.607 1.00 94.46  ? 362  LYS A CE  1 
ATOM   2952  N  NZ  . LYS A 1 362  ? 128.440 84.112  117.658 1.00 100.65 ? 362  LYS A NZ  1 
ATOM   2953  N  N   . LEU A 1 363  ? 126.293 85.925  110.859 1.00 68.52  ? 363  LEU A N   1 
ATOM   2954  C  CA  . LEU A 1 363  ? 126.323 86.694  109.632 1.00 60.58  ? 363  LEU A CA  1 
ATOM   2955  C  C   . LEU A 1 363  ? 127.220 87.916  109.806 1.00 61.26  ? 363  LEU A C   1 
ATOM   2956  O  O   . LEU A 1 363  ? 127.629 88.272  110.913 1.00 67.72  ? 363  LEU A O   1 
ATOM   2957  C  CB  . LEU A 1 363  ? 124.909 87.106  109.227 1.00 60.42  ? 363  LEU A CB  1 
ATOM   2958  C  CG  . LEU A 1 363  ? 123.876 85.977  109.284 1.00 59.80  ? 363  LEU A CG  1 
ATOM   2959  C  CD1 . LEU A 1 363  ? 122.482 86.495  108.934 1.00 47.13  ? 363  LEU A CD1 1 
ATOM   2960  C  CD2 . LEU A 1 363  ? 124.270 84.775  108.406 1.00 63.91  ? 363  LEU A CD2 1 
ATOM   2961  N  N   . THR A 1 364  ? 127.514 88.567  108.689 1.00 52.80  ? 364  THR A N   1 
ATOM   2962  C  CA  . THR A 1 364  ? 128.259 89.813  108.705 1.00 47.34  ? 364  THR A CA  1 
ATOM   2963  C  C   . THR A 1 364  ? 127.287 90.944  109.029 1.00 55.14  ? 364  THR A C   1 
ATOM   2964  O  O   . THR A 1 364  ? 126.069 90.762  108.965 1.00 65.19  ? 364  THR A O   1 
ATOM   2965  C  CB  . THR A 1 364  ? 128.968 90.004  107.366 1.00 51.02  ? 364  THR A CB  1 
ATOM   2966  O  OG1 . THR A 1 364  ? 128.001 90.257  106.340 1.00 67.83  ? 364  THR A OG1 1 
ATOM   2967  C  CG2 . THR A 1 364  ? 129.781 88.763  107.008 1.00 66.37  ? 364  THR A CG2 1 
ATOM   2968  N  N   . PRO A 1 365  ? 127.788 92.131  109.388 1.00 45.12  ? 365  PRO A N   1 
ATOM   2969  C  CA  . PRO A 1 365  ? 126.866 93.249  109.664 1.00 41.21  ? 365  PRO A CA  1 
ATOM   2970  C  C   . PRO A 1 365  ? 125.928 93.597  108.516 1.00 62.75  ? 365  PRO A C   1 
ATOM   2971  O  O   . PRO A 1 365  ? 124.783 93.991  108.772 1.00 63.05  ? 365  PRO A O   1 
ATOM   2972  C  CB  . PRO A 1 365  ? 127.809 94.417  109.995 1.00 37.14  ? 365  PRO A CB  1 
ATOM   2973  C  CG  . PRO A 1 365  ? 129.102 93.790  110.370 1.00 46.04  ? 365  PRO A CG  1 
ATOM   2974  C  CD  . PRO A 1 365  ? 129.197 92.497  109.633 1.00 50.09  ? 365  PRO A CD  1 
ATOM   2975  N  N   . GLN A 1 366  ? 126.367 93.469  107.263 1.00 62.16  ? 366  GLN A N   1 
ATOM   2976  C  CA  . GLN A 1 366  ? 125.490 93.787  106.138 1.00 51.93  ? 366  GLN A CA  1 
ATOM   2977  C  C   . GLN A 1 366  ? 124.288 92.852  106.083 1.00 58.39  ? 366  GLN A C   1 
ATOM   2978  O  O   . GLN A 1 366  ? 123.152 93.292  105.858 1.00 64.90  ? 366  GLN A O   1 
ATOM   2979  C  CB  . GLN A 1 366  ? 126.273 93.724  104.829 1.00 53.04  ? 366  GLN A CB  1 
ATOM   2980  C  CG  . GLN A 1 366  ? 127.224 94.884  104.651 1.00 57.91  ? 366  GLN A CG  1 
ATOM   2981  C  CD  . GLN A 1 366  ? 128.556 94.623  105.310 1.00 46.10  ? 366  GLN A CD  1 
ATOM   2982  O  OE1 . GLN A 1 366  ? 128.901 93.479  105.599 1.00 50.40  ? 366  GLN A OE1 1 
ATOM   2983  N  NE2 . GLN A 1 366  ? 129.301 95.686  105.580 1.00 49.80  ? 366  GLN A NE2 1 
ATOM   2984  N  N   . GLN A 1 367  ? 124.515 91.556  106.292 1.00 49.25  ? 367  GLN A N   1 
ATOM   2985  C  CA  . GLN A 1 367  ? 123.407 90.615  106.224 1.00 47.48  ? 367  GLN A CA  1 
ATOM   2986  C  C   . GLN A 1 367  ? 122.445 90.807  107.386 1.00 49.01  ? 367  GLN A C   1 
ATOM   2987  O  O   . GLN A 1 367  ? 121.230 90.664  107.208 1.00 62.00  ? 367  GLN A O   1 
ATOM   2988  C  CB  . GLN A 1 367  ? 123.958 89.194  106.193 1.00 44.92  ? 367  GLN A CB  1 
ATOM   2989  C  CG  . GLN A 1 367  ? 124.907 88.975  105.029 1.00 44.42  ? 367  GLN A CG  1 
ATOM   2990  C  CD  . GLN A 1 367  ? 125.618 87.649  105.094 1.00 49.60  ? 367  GLN A CD  1 
ATOM   2991  O  OE1 . GLN A 1 367  ? 125.453 86.888  106.044 1.00 69.32  ? 367  GLN A OE1 1 
ATOM   2992  N  NE2 . GLN A 1 367  ? 126.428 87.365  104.082 1.00 56.88  ? 367  GLN A NE2 1 
ATOM   2993  N  N   . TYR A 1 368  ? 122.954 91.175  108.563 1.00 49.62  ? 368  TYR A N   1 
ATOM   2994  C  CA  . TYR A 1 368  ? 122.059 91.500  109.669 1.00 42.35  ? 368  TYR A CA  1 
ATOM   2995  C  C   . TYR A 1 368  ? 121.258 92.759  109.375 1.00 49.21  ? 368  TYR A C   1 
ATOM   2996  O  O   . TYR A 1 368  ? 120.064 92.833  109.687 1.00 62.17  ? 368  TYR A O   1 
ATOM   2997  C  CB  . TYR A 1 368  ? 122.858 91.679  110.956 1.00 47.56  ? 368  TYR A CB  1 
ATOM   2998  C  CG  . TYR A 1 368  ? 123.101 90.399  111.704 1.00 57.88  ? 368  TYR A CG  1 
ATOM   2999  C  CD1 . TYR A 1 368  ? 122.045 89.591  112.089 1.00 66.85  ? 368  TYR A CD1 1 
ATOM   3000  C  CD2 . TYR A 1 368  ? 124.387 89.998  112.029 1.00 66.93  ? 368  TYR A CD2 1 
ATOM   3001  C  CE1 . TYR A 1 368  ? 122.261 88.415  112.774 1.00 61.35  ? 368  TYR A CE1 1 
ATOM   3002  C  CE2 . TYR A 1 368  ? 124.615 88.824  112.715 1.00 73.20  ? 368  TYR A CE2 1 
ATOM   3003  C  CZ  . TYR A 1 368  ? 123.547 88.035  113.086 1.00 64.10  ? 368  TYR A CZ  1 
ATOM   3004  O  OH  . TYR A 1 368  ? 123.770 86.864  113.771 1.00 66.57  ? 368  TYR A OH  1 
ATOM   3005  N  N   . CYS A 1 369  ? 121.901 93.761  108.770 1.00 62.62  ? 369  CYS A N   1 
ATOM   3006  C  CA  . CYS A 1 369  ? 121.197 94.997  108.456 1.00 60.77  ? 369  CYS A CA  1 
ATOM   3007  C  C   . CYS A 1 369  ? 120.113 94.766  107.415 1.00 60.21  ? 369  CYS A C   1 
ATOM   3008  O  O   . CYS A 1 369  ? 119.079 95.442  107.439 1.00 69.23  ? 369  CYS A O   1 
ATOM   3009  C  CB  . CYS A 1 369  ? 122.179 96.063  107.974 1.00 58.17  ? 369  CYS A CB  1 
ATOM   3010  S  SG  . CYS A 1 369  ? 121.493 97.732  107.995 1.00 89.52  ? 369  CYS A SG  1 
ATOM   3011  N  N   . GLU A 1 370  ? 120.327 93.819  106.500 1.00 66.57  ? 370  GLU A N   1 
ATOM   3012  C  CA  . GLU A 1 370  ? 119.271 93.483  105.550 1.00 64.04  ? 370  GLU A CA  1 
ATOM   3013  C  C   . GLU A 1 370  ? 118.165 92.678  106.221 1.00 61.17  ? 370  GLU A C   1 
ATOM   3014  O  O   . GLU A 1 370  ? 116.979 92.910  105.964 1.00 75.89  ? 370  GLU A O   1 
ATOM   3015  C  CB  . GLU A 1 370  ? 119.847 92.717  104.362 1.00 62.71  ? 370  GLU A CB  1 
ATOM   3016  C  CG  . GLU A 1 370  ? 120.693 93.565  103.431 1.00 67.39  ? 370  GLU A CG  1 
ATOM   3017  C  CD  . GLU A 1 370  ? 119.864 94.353  102.432 1.00 68.26  ? 370  GLU A CD  1 
ATOM   3018  O  OE1 . GLU A 1 370  ? 120.413 94.732  101.378 1.00 68.61  ? 370  GLU A OE1 1 
ATOM   3019  O  OE2 . GLU A 1 370  ? 118.669 94.599  102.695 1.00 77.45  ? 370  GLU A OE2 1 
ATOM   3020  N  N   . LEU A 1 371  ? 118.536 91.737  107.092 1.00 55.42  ? 371  LEU A N   1 
ATOM   3021  C  CA  . LEU A 1 371  ? 117.554 90.931  107.806 1.00 49.65  ? 371  LEU A CA  1 
ATOM   3022  C  C   . LEU A 1 371  ? 116.697 91.772  108.740 1.00 54.12  ? 371  LEU A C   1 
ATOM   3023  O  O   . LEU A 1 371  ? 115.574 91.375  109.071 1.00 55.63  ? 371  LEU A O   1 
ATOM   3024  C  CB  . LEU A 1 371  ? 118.290 89.845  108.590 1.00 51.80  ? 371  LEU A CB  1 
ATOM   3025  C  CG  . LEU A 1 371  ? 117.509 88.837  109.421 1.00 67.06  ? 371  LEU A CG  1 
ATOM   3026  C  CD1 . LEU A 1 371  ? 116.925 87.770  108.520 1.00 78.39  ? 371  LEU A CD1 1 
ATOM   3027  C  CD2 . LEU A 1 371  ? 118.440 88.227  110.457 1.00 60.11  ? 371  LEU A CD2 1 
ATOM   3028  N  N   . PHE A 1 372  ? 117.200 92.936  109.145 1.00 71.87  ? 372  PHE A N   1 
ATOM   3029  C  CA  . PHE A 1 372  ? 116.431 93.886  109.940 1.00 59.47  ? 372  PHE A CA  1 
ATOM   3030  C  C   . PHE A 1 372  ? 115.142 94.325  109.247 1.00 59.59  ? 372  PHE A C   1 
ATOM   3031  O  O   . PHE A 1 372  ? 114.213 94.784  109.920 1.00 64.62  ? 372  PHE A O   1 
ATOM   3032  C  CB  . PHE A 1 372  ? 117.331 95.088  110.253 1.00 66.63  ? 372  PHE A CB  1 
ATOM   3033  C  CG  . PHE A 1 372  ? 116.663 96.185  111.028 1.00 59.81  ? 372  PHE A CG  1 
ATOM   3034  C  CD1 . PHE A 1 372  ? 116.749 96.222  112.409 1.00 72.87  ? 372  PHE A CD1 1 
ATOM   3035  C  CD2 . PHE A 1 372  ? 115.989 97.203  110.376 1.00 81.46  ? 372  PHE A CD2 1 
ATOM   3036  C  CE1 . PHE A 1 372  ? 116.149 97.239  113.125 1.00 84.84  ? 372  PHE A CE1 1 
ATOM   3037  C  CE2 . PHE A 1 372  ? 115.382 98.220  111.088 1.00 87.42  ? 372  PHE A CE2 1 
ATOM   3038  C  CZ  . PHE A 1 372  ? 115.463 98.237  112.465 1.00 84.66  ? 372  PHE A CZ  1 
ATOM   3039  N  N   . SER A 1 373  ? 115.052 94.151  107.929 1.00 72.40  ? 373  SER A N   1 
ATOM   3040  C  CA  . SER A 1 373  ? 113.957 94.678  107.122 1.00 61.00  ? 373  SER A CA  1 
ATOM   3041  C  C   . SER A 1 373  ? 112.788 93.715  106.969 1.00 57.50  ? 373  SER A C   1 
ATOM   3042  O  O   . SER A 1 373  ? 111.835 94.034  106.251 1.00 64.15  ? 373  SER A O   1 
ATOM   3043  C  CB  . SER A 1 373  ? 114.471 95.082  105.735 1.00 60.15  ? 373  SER A CB  1 
ATOM   3044  O  OG  . SER A 1 373  ? 115.396 96.155  105.827 1.00 76.22  ? 373  SER A OG  1 
ATOM   3045  N  N   . LEU A 1 374  ? 112.818 92.551  107.621 1.00 57.75  ? 374  LEU A N   1 
ATOM   3046  C  CA  . LEU A 1 374  ? 111.731 91.591  107.492 1.00 60.78  ? 374  LEU A CA  1 
ATOM   3047  C  C   . LEU A 1 374  ? 110.703 91.719  108.601 1.00 61.23  ? 374  LEU A C   1 
ATOM   3048  O  O   . LEU A 1 374  ? 109.996 90.748  108.895 1.00 60.06  ? 374  LEU A O   1 
ATOM   3049  C  CB  . LEU A 1 374  ? 112.276 90.157  107.487 1.00 52.63  ? 374  LEU A CB  1 
ATOM   3050  C  CG  . LEU A 1 374  ? 113.457 89.754  106.614 1.00 54.10  ? 374  LEU A CG  1 
ATOM   3051  C  CD1 . LEU A 1 374  ? 113.555 88.237  106.602 1.00 43.73  ? 374  LEU A CD1 1 
ATOM   3052  C  CD2 . LEU A 1 374  ? 113.293 90.299  105.205 1.00 64.65  ? 374  LEU A CD2 1 
ATOM   3053  N  N   . GLN A 1 375  ? 110.599 92.892  109.225 1.00 54.01  ? 375  GLN A N   1 
ATOM   3054  C  CA  . GLN A 1 375  ? 109.772 92.996  110.419 1.00 62.27  ? 375  GLN A CA  1 
ATOM   3055  C  C   . GLN A 1 375  ? 108.290 92.837  110.119 1.00 65.26  ? 375  GLN A C   1 
ATOM   3056  O  O   . GLN A 1 375  ? 107.553 92.273  110.936 1.00 72.59  ? 375  GLN A O   1 
ATOM   3057  C  CB  . GLN A 1 375  ? 110.020 94.327  111.121 1.00 70.05  ? 375  GLN A CB  1 
ATOM   3058  C  CG  . GLN A 1 375  ? 109.190 94.479  112.372 1.00 68.45  ? 375  GLN A CG  1 
ATOM   3059  C  CD  . GLN A 1 375  ? 109.698 93.637  113.514 1.00 72.70  ? 375  GLN A CD  1 
ATOM   3060  O  OE1 . GLN A 1 375  ? 109.516 92.423  113.539 1.00 73.68  ? 375  GLN A OE1 1 
ATOM   3061  N  NE2 . GLN A 1 375  ? 110.351 94.283  114.472 1.00 91.40  ? 375  GLN A NE2 1 
ATOM   3062  N  N   . LYS A 1 376  ? 107.833 93.281  108.950 1.00 61.31  ? 376  LYS A N   1 
ATOM   3063  C  CA  . LYS A 1 376  ? 106.414 93.259  108.636 1.00 47.58  ? 376  LYS A CA  1 
ATOM   3064  C  C   . LYS A 1 376  ? 106.032 92.097  107.732 1.00 52.56  ? 376  LYS A C   1 
ATOM   3065  O  O   . LYS A 1 376  ? 104.960 92.127  107.114 1.00 59.24  ? 376  LYS A O   1 
ATOM   3066  C  CB  . LYS A 1 376  ? 106.009 94.592  108.010 1.00 56.73  ? 376  LYS A CB  1 
ATOM   3067  C  CG  . LYS A 1 376  ? 106.143 95.748  108.981 1.00 68.71  ? 376  LYS A CG  1 
ATOM   3068  C  CD  . LYS A 1 376  ? 105.817 97.070  108.330 1.00 77.40  ? 376  LYS A CD  1 
ATOM   3069  C  CE  . LYS A 1 376  ? 105.725 98.165  109.373 1.00 85.22  ? 376  LYS A CE  1 
ATOM   3070  N  NZ  . LYS A 1 376  ? 105.744 99.513  108.749 1.00 90.18  ? 376  LYS A NZ  1 
ATOM   3071  N  N   . HIS A 1 377  ? 106.871 91.069  107.646 1.00 57.48  ? 377  HIS A N   1 
ATOM   3072  C  CA  . HIS A 1 377  ? 106.617 89.954  106.747 1.00 43.49  ? 377  HIS A CA  1 
ATOM   3073  C  C   . HIS A 1 377  ? 105.755 88.869  107.375 1.00 44.62  ? 377  HIS A C   1 
ATOM   3074  O  O   . HIS A 1 377  ? 105.635 87.781  106.800 1.00 52.74  ? 377  HIS A O   1 
ATOM   3075  C  CB  . HIS A 1 377  ? 107.944 89.360  106.264 1.00 43.46  ? 377  HIS A CB  1 
ATOM   3076  C  CG  . HIS A 1 377  ? 108.665 90.232  105.283 1.00 58.62  ? 377  HIS A CG  1 
ATOM   3077  N  ND1 . HIS A 1 377  ? 109.505 89.727  104.313 1.00 62.69  ? 377  HIS A ND1 1 
ATOM   3078  C  CD2 . HIS A 1 377  ? 108.661 91.576  105.117 1.00 64.65  ? 377  HIS A CD2 1 
ATOM   3079  C  CE1 . HIS A 1 377  ? 109.992 90.724  103.595 1.00 64.73  ? 377  HIS A CE1 1 
ATOM   3080  N  NE2 . HIS A 1 377  ? 109.495 91.855  104.062 1.00 55.76  ? 377  HIS A NE2 1 
ATOM   3081  N  N   . TRP A 1 378  ? 105.161 89.131  108.536 1.00 50.77  ? 378  TRP A N   1 
ATOM   3082  C  CA  . TRP A 1 378  ? 104.251 88.188  109.165 1.00 52.15  ? 378  TRP A CA  1 
ATOM   3083  C  C   . TRP A 1 378  ? 102.848 88.749  109.356 1.00 56.50  ? 378  TRP A C   1 
ATOM   3084  O  O   . TRP A 1 378  ? 101.994 88.058  109.922 1.00 60.70  ? 378  TRP A O   1 
ATOM   3085  C  CB  . TRP A 1 378  ? 104.809 87.723  110.516 1.00 49.83  ? 378  TRP A CB  1 
ATOM   3086  C  CG  . TRP A 1 378  ? 105.973 86.790  110.389 1.00 53.31  ? 378  TRP A CG  1 
ATOM   3087  C  CD1 . TRP A 1 378  ? 105.922 85.441  110.195 1.00 62.36  ? 378  TRP A CD1 1 
ATOM   3088  C  CD2 . TRP A 1 378  ? 107.364 87.132  110.465 1.00 53.14  ? 378  TRP A CD2 1 
ATOM   3089  N  NE1 . TRP A 1 378  ? 107.194 84.925  110.134 1.00 51.95  ? 378  TRP A NE1 1 
ATOM   3090  C  CE2 . TRP A 1 378  ? 108.097 85.942  110.298 1.00 42.10  ? 378  TRP A CE2 1 
ATOM   3091  C  CE3 . TRP A 1 378  ? 108.060 88.331  110.653 1.00 62.62  ? 378  TRP A CE3 1 
ATOM   3092  C  CZ2 . TRP A 1 378  ? 109.489 85.914  110.311 1.00 43.29  ? 378  TRP A CZ2 1 
ATOM   3093  C  CZ3 . TRP A 1 378  ? 109.445 88.298  110.668 1.00 48.40  ? 378  TRP A CZ3 1 
ATOM   3094  C  CH2 . TRP A 1 378  ? 110.143 87.100  110.497 1.00 41.93  ? 378  TRP A CH2 1 
ATOM   3095  N  N   . GLY A 1 379  ? 102.579 89.964  108.896 1.00 51.10  ? 379  GLY A N   1 
ATOM   3096  C  CA  . GLY A 1 379  ? 101.276 90.572  109.073 1.00 54.89  ? 379  GLY A CA  1 
ATOM   3097  C  C   . GLY A 1 379  ? 101.245 91.513  110.263 1.00 76.96  ? 379  GLY A C   1 
ATOM   3098  O  O   . GLY A 1 379  ? 102.273 91.909  110.821 1.00 78.82  ? 379  GLY A O   1 
ATOM   3099  N  N   . HIS A 1 380  ? 100.030 91.876  110.651 1.00 63.53  ? 380  HIS A N   1 
ATOM   3100  C  CA  . HIS A 1 380  ? 99.794  92.837  111.716 1.00 57.64  ? 380  HIS A CA  1 
ATOM   3101  C  C   . HIS A 1 380  ? 98.687  92.327  112.625 1.00 64.76  ? 380  HIS A C   1 
ATOM   3102  O  O   . HIS A 1 380  ? 97.843  91.532  112.200 1.00 68.31  ? 380  HIS A O   1 
ATOM   3103  C  CB  . HIS A 1 380  ? 99.445  94.220  111.150 1.00 70.24  ? 380  HIS A CB  1 
ATOM   3104  C  CG  . HIS A 1 380  ? 100.467 94.750  110.191 1.00 64.28  ? 380  HIS A CG  1 
ATOM   3105  N  ND1 . HIS A 1 380  ? 101.540 95.513  110.601 1.00 65.90  ? 380  HIS A ND1 1 
ATOM   3106  C  CD2 . HIS A 1 380  ? 100.590 94.618  108.849 1.00 68.42  ? 380  HIS A CD2 1 
ATOM   3107  C  CE1 . HIS A 1 380  ? 102.276 95.833  109.553 1.00 75.79  ? 380  HIS A CE1 1 
ATOM   3108  N  NE2 . HIS A 1 380  ? 101.721 95.302  108.478 1.00 72.96  ? 380  HIS A NE2 1 
ATOM   3109  N  N   . PRO A 1 381  ? 98.670  92.758  113.884 1.00 64.44  ? 381  PRO A N   1 
ATOM   3110  C  CA  . PRO A 1 381  ? 97.710  92.213  114.850 1.00 55.87  ? 381  PRO A CA  1 
ATOM   3111  C  C   . PRO A 1 381  ? 96.345  92.889  114.788 1.00 71.65  ? 381  PRO A C   1 
ATOM   3112  O  O   . PRO A 1 381  ? 96.148  93.930  114.159 1.00 83.48  ? 381  PRO A O   1 
ATOM   3113  C  CB  . PRO A 1 381  ? 98.384  92.491  116.197 1.00 59.21  ? 381  PRO A CB  1 
ATOM   3114  C  CG  . PRO A 1 381  ? 99.196  93.720  115.953 1.00 56.40  ? 381  PRO A CG  1 
ATOM   3115  C  CD  . PRO A 1 381  ? 99.663  93.641  114.527 1.00 60.93  ? 381  PRO A CD  1 
ATOM   3116  N  N   . VAL A 1 382  ? 95.390  92.248  115.465 1.00 76.51  ? 382  VAL A N   1 
ATOM   3117  C  CA  . VAL A 1 382  ? 94.055  92.794  115.689 1.00 70.01  ? 382  VAL A CA  1 
ATOM   3118  C  C   . VAL A 1 382  ? 94.089  93.722  116.894 1.00 78.82  ? 382  VAL A C   1 
ATOM   3119  O  O   . VAL A 1 382  ? 94.731  93.426  117.910 1.00 91.33  ? 382  VAL A O   1 
ATOM   3120  C  CB  . VAL A 1 382  ? 93.031  91.662  115.883 1.00 53.57  ? 382  VAL A CB  1 
ATOM   3121  C  CG1 . VAL A 1 382  ? 91.624  92.229  115.992 1.00 69.64  ? 382  VAL A CG1 1 
ATOM   3122  C  CG2 . VAL A 1 382  ? 93.122  90.666  114.734 1.00 72.94  ? 382  VAL A CG2 1 
ATOM   3123  N  N   . LEU A 1 383  ? 93.401  94.855  116.790 1.00 66.35  ? 383  LEU A N   1 
ATOM   3124  C  CA  . LEU A 1 383  ? 93.438  95.883  117.818 1.00 70.10  ? 383  LEU A CA  1 
ATOM   3125  C  C   . LEU A 1 383  ? 92.121  95.950  118.578 1.00 79.41  ? 383  LEU A C   1 
ATOM   3126  O  O   . LEU A 1 383  ? 91.043  95.794  117.995 1.00 85.47  ? 383  LEU A O   1 
ATOM   3127  C  CB  . LEU A 1 383  ? 93.741  97.245  117.193 1.00 63.69  ? 383  LEU A CB  1 
ATOM   3128  C  CG  . LEU A 1 383  ? 95.019  97.243  116.360 1.00 58.40  ? 383  LEU A CG  1 
ATOM   3129  C  CD1 . LEU A 1 383  ? 95.300  98.623  115.795 1.00 74.24  ? 383  LEU A CD1 1 
ATOM   3130  C  CD2 . LEU A 1 383  ? 96.186  96.752  117.210 1.00 70.91  ? 383  LEU A CD2 1 
ATOM   3131  N  N   . TYR A 1 384  ? 92.223  96.176  119.887 1.00 70.45  ? 384  TYR A N   1 
ATOM   3132  C  CA  . TYR A 1 384  ? 91.077  96.372  120.765 1.00 65.88  ? 384  TYR A CA  1 
ATOM   3133  C  C   . TYR A 1 384  ? 91.244  97.725  121.436 1.00 84.22  ? 384  TYR A C   1 
ATOM   3134  O  O   . TYR A 1 384  ? 92.308  98.012  121.993 1.00 101.87 ? 384  TYR A O   1 
ATOM   3135  C  CB  . TYR A 1 384  ? 90.978  95.275  121.828 1.00 75.47  ? 384  TYR A CB  1 
ATOM   3136  C  CG  . TYR A 1 384  ? 91.045  93.870  121.283 1.00 83.36  ? 384  TYR A CG  1 
ATOM   3137  C  CD1 . TYR A 1 384  ? 89.935  93.270  120.706 1.00 103.02 ? 384  TYR A CD1 1 
ATOM   3138  C  CD2 . TYR A 1 384  ? 92.216  93.133  121.373 1.00 90.57  ? 384  TYR A CD2 1 
ATOM   3139  C  CE1 . TYR A 1 384  ? 90.000  91.979  120.212 1.00 92.30  ? 384  TYR A CE1 1 
ATOM   3140  C  CE2 . TYR A 1 384  ? 92.289  91.845  120.885 1.00 100.32 ? 384  TYR A CE2 1 
ATOM   3141  C  CZ  . TYR A 1 384  ? 91.179  91.272  120.307 1.00 92.48  ? 384  TYR A CZ  1 
ATOM   3142  O  OH  . TYR A 1 384  ? 91.249  89.986  119.820 1.00 82.56  ? 384  TYR A OH  1 
ATOM   3143  N  N   . ASN A 1 385  ? 90.203  98.555  121.384 1.00 73.44  ? 385  ASN A N   1 
ATOM   3144  C  CA  . ASN A 1 385  ? 90.358  99.927  121.860 1.00 77.18  ? 385  ASN A CA  1 
ATOM   3145  C  C   . ASN A 1 385  ? 90.463  100.014 123.381 1.00 81.42  ? 385  ASN A C   1 
ATOM   3146  O  O   . ASN A 1 385  ? 91.129  100.921 123.896 1.00 86.08  ? 385  ASN A O   1 
ATOM   3147  C  CB  . ASN A 1 385  ? 89.206  100.793 121.350 1.00 76.03  ? 385  ASN A CB  1 
ATOM   3148  C  CG  . ASN A 1 385  ? 87.859  100.114 121.485 1.00 93.15  ? 385  ASN A CG  1 
ATOM   3149  O  OD1 . ASN A 1 385  ? 87.699  99.170  122.257 1.00 101.76 ? 385  ASN A OD1 1 
ATOM   3150  N  ND2 . ASN A 1 385  ? 86.878  100.598 120.731 1.00 85.57  ? 385  ASN A ND2 1 
ATOM   3151  N  N   . ASP A 1 386  ? 89.855  99.078  124.120 1.00 70.78  ? 386  ASP A N   1 
ATOM   3152  C  CA  . ASP A 1 386  ? 90.005  99.099  125.575 1.00 77.59  ? 386  ASP A CA  1 
ATOM   3153  C  C   . ASP A 1 386  ? 91.424  98.731  125.998 1.00 83.53  ? 386  ASP A C   1 
ATOM   3154  O  O   . ASP A 1 386  ? 92.002  99.377  126.881 1.00 87.32  ? 386  ASP A O   1 
ATOM   3155  C  CB  . ASP A 1 386  ? 88.987  98.165  126.236 1.00 88.57  ? 386  ASP A CB  1 
ATOM   3156  C  CG  . ASP A 1 386  ? 89.115  96.724  125.771 1.00 94.21  ? 386  ASP A CG  1 
ATOM   3157  O  OD1 . ASP A 1 386  ? 89.937  96.449  124.875 1.00 95.59  ? 386  ASP A OD1 1 
ATOM   3158  O  OD2 . ASP A 1 386  ? 88.403  95.857  126.323 1.00 92.10  ? 386  ASP A OD2 1 
ATOM   3159  N  N   . VAL A 1 387  ? 91.996  97.693  125.382 1.00 84.32  ? 387  VAL A N   1 
ATOM   3160  C  CA  . VAL A 1 387  ? 93.385  97.334  125.653 1.00 72.54  ? 387  VAL A CA  1 
ATOM   3161  C  C   . VAL A 1 387  ? 94.308  98.470  125.237 1.00 69.75  ? 387  VAL A C   1 
ATOM   3162  O  O   . VAL A 1 387  ? 95.314  98.752  125.898 1.00 81.25  ? 387  VAL A O   1 
ATOM   3163  C  CB  . VAL A 1 387  ? 93.755  96.012  124.953 1.00 65.32  ? 387  VAL A CB  1 
ATOM   3164  C  CG1 . VAL A 1 387  ? 95.182  95.607  125.301 1.00 70.47  ? 387  VAL A CG1 1 
ATOM   3165  C  CG2 . VAL A 1 387  ? 92.782  94.908  125.348 1.00 76.02  ? 387  VAL A CG2 1 
ATOM   3166  N  N   . ALA A 1 388  ? 93.967  99.152  124.141 1.00 65.65  ? 388  ALA A N   1 
ATOM   3167  C  CA  . ALA A 1 388  ? 94.792  100.254 123.667 1.00 61.40  ? 388  ALA A CA  1 
ATOM   3168  C  C   . ALA A 1 388  ? 94.768  101.418 124.648 1.00 78.86  ? 388  ALA A C   1 
ATOM   3169  O  O   . ALA A 1 388  ? 95.810  102.024 124.923 1.00 93.04  ? 388  ALA A O   1 
ATOM   3170  C  CB  . ALA A 1 388  ? 94.320  100.703 122.283 1.00 56.58  ? 388  ALA A CB  1 
ATOM   3171  N  N   . LEU A 1 389  ? 93.600  101.739 125.199 1.00 71.51  ? 389  LEU A N   1 
ATOM   3172  C  CA  . LEU A 1 389  ? 93.481  102.893 126.078 1.00 68.61  ? 389  LEU A CA  1 
ATOM   3173  C  C   . LEU A 1 389  ? 93.787  102.601 127.540 1.00 82.11  ? 389  LEU A C   1 
ATOM   3174  O  O   . LEU A 1 389  ? 93.941  103.552 128.307 1.00 86.43  ? 389  LEU A O   1 
ATOM   3175  C  CB  . LEU A 1 389  ? 92.085  103.515 125.976 1.00 58.36  ? 389  LEU A CB  1 
ATOM   3176  C  CG  . LEU A 1 389  ? 91.825  104.200 124.641 1.00 68.51  ? 389  LEU A CG  1 
ATOM   3177  C  CD1 . LEU A 1 389  ? 90.412  104.711 124.586 1.00 63.38  ? 389  LEU A CD1 1 
ATOM   3178  C  CD2 . LEU A 1 389  ? 92.812  105.342 124.453 1.00 71.62  ? 389  LEU A CD2 1 
ATOM   3179  N  N   . ASP A 1 390  ? 93.892  101.338 127.958 1.00 87.83  ? 390  ASP A N   1 
ATOM   3180  C  CA  . ASP A 1 390  ? 94.342  101.077 129.325 1.00 78.45  ? 390  ASP A CA  1 
ATOM   3181  C  C   . ASP A 1 390  ? 95.737  101.647 129.565 1.00 85.26  ? 390  ASP A C   1 
ATOM   3182  O  O   . ASP A 1 390  ? 95.982  102.324 130.572 1.00 87.63  ? 390  ASP A O   1 
ATOM   3183  C  CB  . ASP A 1 390  ? 94.324  99.574  129.605 1.00 97.82  ? 390  ASP A CB  1 
ATOM   3184  C  CG  . ASP A 1 390  ? 92.973  99.090  130.076 1.00 124.19 ? 390  ASP A CG  1 
ATOM   3185  O  OD1 . ASP A 1 390  ? 92.065  99.931  130.236 1.00 120.42 ? 390  ASP A OD1 1 
ATOM   3186  O  OD2 . ASP A 1 390  ? 92.819  97.868  130.289 1.00 132.14 ? 390  ASP A OD2 1 
ATOM   3187  N  N   . LYS A 1 391  ? 96.659  101.402 128.631 1.00 82.37  ? 391  LYS A N   1 
ATOM   3188  C  CA  . LYS A 1 391  ? 98.021  101.903 128.777 1.00 75.11  ? 391  LYS A CA  1 
ATOM   3189  C  C   . LYS A 1 391  ? 98.048  103.425 128.782 1.00 74.80  ? 391  LYS A C   1 
ATOM   3190  O  O   . LYS A 1 391  ? 98.711  104.049 129.624 1.00 84.55  ? 391  LYS A O   1 
ATOM   3191  C  CB  . LYS A 1 391  ? 98.899  101.368 127.649 1.00 87.51  ? 391  LYS A CB  1 
ATOM   3192  C  CG  . LYS A 1 391  ? 100.375 101.600 127.882 1.00 103.44 ? 391  LYS A CG  1 
ATOM   3193  C  CD  . LYS A 1 391  ? 101.181 101.248 126.652 1.00 114.54 ? 391  LYS A CD  1 
ATOM   3194  C  CE  . LYS A 1 391  ? 102.657 101.483 126.894 1.00 116.51 ? 391  LYS A CE  1 
ATOM   3195  N  NZ  . LYS A 1 391  ? 103.267 102.220 125.753 1.00 111.51 ? 391  LYS A NZ  1 
ATOM   3196  N  N   . VAL A 1 392  ? 97.311  104.038 127.853 1.00 70.73  ? 392  VAL A N   1 
ATOM   3197  C  CA  . VAL A 1 392  ? 97.278  105.494 127.756 1.00 67.32  ? 392  VAL A CA  1 
ATOM   3198  C  C   . VAL A 1 392  ? 96.679  106.098 129.015 1.00 74.50  ? 392  VAL A C   1 
ATOM   3199  O  O   . VAL A 1 392  ? 97.186  107.096 129.537 1.00 76.69  ? 392  VAL A O   1 
ATOM   3200  C  CB  . VAL A 1 392  ? 96.506  105.928 126.495 1.00 66.39  ? 392  VAL A CB  1 
ATOM   3201  C  CG1 . VAL A 1 392  ? 96.336  107.443 126.466 1.00 70.63  ? 392  VAL A CG1 1 
ATOM   3202  C  CG2 . VAL A 1 392  ? 97.218  105.442 125.239 1.00 75.74  ? 392  VAL A CG2 1 
ATOM   3203  N  N   . LYS A 1 393  ? 95.584  105.522 129.514 1.00 72.00  ? 393  LYS A N   1 
ATOM   3204  C  CA  . LYS A 1 393  ? 94.963  106.046 130.722 1.00 53.26  ? 393  LYS A CA  1 
ATOM   3205  C  C   . LYS A 1 393  ? 95.911  105.953 131.908 1.00 64.13  ? 393  LYS A C   1 
ATOM   3206  O  O   . LYS A 1 393  ? 96.054  106.910 132.676 1.00 78.07  ? 393  LYS A O   1 
ATOM   3207  C  CB  . LYS A 1 393  ? 93.672  105.287 131.013 1.00 60.71  ? 393  LYS A CB  1 
ATOM   3208  C  CG  . LYS A 1 393  ? 93.124  105.534 132.402 1.00 65.89  ? 393  LYS A CG  1 
ATOM   3209  C  CD  . LYS A 1 393  ? 91.827  104.785 132.617 1.00 78.11  ? 393  LYS A CD  1 
ATOM   3210  C  CE  . LYS A 1 393  ? 91.172  105.196 133.920 1.00 83.74  ? 393  LYS A CE  1 
ATOM   3211  N  NZ  . LYS A 1 393  ? 89.789  104.661 134.012 1.00 74.13  ? 393  LYS A NZ  1 
ATOM   3212  N  N   . LYS A 1 394  ? 96.568  104.800 132.078 1.00 81.86  ? 394  LYS A N   1 
ATOM   3213  C  CA  . LYS A 1 394  ? 97.469  104.661 133.216 1.00 71.84  ? 394  LYS A CA  1 
ATOM   3214  C  C   . LYS A 1 394  ? 98.618  105.656 133.133 1.00 68.73  ? 394  LYS A C   1 
ATOM   3215  O  O   . LYS A 1 394  ? 98.994  106.269 134.138 1.00 70.83  ? 394  LYS A O   1 
ATOM   3216  C  CB  . LYS A 1 394  ? 98.025  103.239 133.298 1.00 76.47  ? 394  LYS A CB  1 
ATOM   3217  C  CG  . LYS A 1 394  ? 98.914  103.021 134.516 1.00 96.18  ? 394  LYS A CG  1 
ATOM   3218  C  CD  . LYS A 1 394  ? 99.348  101.576 134.662 1.00 109.88 ? 394  LYS A CD  1 
ATOM   3219  C  CE  . LYS A 1 394  ? 100.398 101.232 133.620 1.00 104.90 ? 394  LYS A CE  1 
ATOM   3220  N  NZ  . LYS A 1 394  ? 101.682 101.939 133.897 1.00 94.23  ? 394  LYS A NZ  1 
ATOM   3221  N  N   . HIS A 1 395  ? 99.182  105.839 131.936 1.00 76.24  ? 395  HIS A N   1 
ATOM   3222  C  CA  . HIS A 1 395  ? 100.328 106.729 131.797 1.00 67.15  ? 395  HIS A CA  1 
ATOM   3223  C  C   . HIS A 1 395  ? 99.952  108.207 131.841 1.00 62.89  ? 395  HIS A C   1 
ATOM   3224  O  O   . HIS A 1 395  ? 100.768 109.032 132.269 1.00 66.80  ? 395  HIS A O   1 
ATOM   3225  C  CB  . HIS A 1 395  ? 101.072 106.402 130.501 1.00 72.14  ? 395  HIS A CB  1 
ATOM   3226  C  CG  . HIS A 1 395  ? 101.977 105.214 130.621 1.00 84.77  ? 395  HIS A CG  1 
ATOM   3227  N  ND1 . HIS A 1 395  ? 102.544 104.833 131.819 1.00 93.78  ? 395  HIS A ND1 1 
ATOM   3228  C  CD2 . HIS A 1 395  ? 102.398 104.313 129.702 1.00 89.27  ? 395  HIS A CD2 1 
ATOM   3229  C  CE1 . HIS A 1 395  ? 103.280 103.752 131.630 1.00 89.44  ? 395  HIS A CE1 1 
ATOM   3230  N  NE2 . HIS A 1 395  ? 103.209 103.418 130.354 1.00 88.30  ? 395  HIS A NE2 1 
ATOM   3231  N  N   . ALA A 1 396  ? 98.741  108.566 131.414 1.00 68.51  ? 396  ALA A N   1 
ATOM   3232  C  CA  . ALA A 1 396  ? 98.340  109.966 131.343 1.00 58.39  ? 396  ALA A CA  1 
ATOM   3233  C  C   . ALA A 1 396  ? 97.609  110.470 132.580 1.00 60.21  ? 396  ALA A C   1 
ATOM   3234  O  O   . ALA A 1 396  ? 97.330  111.672 132.660 1.00 59.05  ? 396  ALA A O   1 
ATOM   3235  C  CB  . ALA A 1 396  ? 97.458  110.192 130.113 1.00 60.41  ? 396  ALA A CB  1 
ATOM   3236  N  N   . GLN A 1 397  ? 97.272  109.604 133.531 1.00 69.41  ? 397  GLN A N   1 
ATOM   3237  C  CA  . GLN A 1 397  ? 96.666  110.043 134.779 1.00 56.46  ? 397  GLN A CA  1 
ATOM   3238  C  C   . GLN A 1 397  ? 97.586  109.863 135.970 1.00 68.90  ? 397  GLN A C   1 
ATOM   3239  O  O   . GLN A 1 397  ? 97.202  110.219 137.090 1.00 70.18  ? 397  GLN A O   1 
ATOM   3240  C  CB  . GLN A 1 397  ? 95.356  109.300 135.050 1.00 63.77  ? 397  GLN A CB  1 
ATOM   3241  C  CG  . GLN A 1 397  ? 94.220  109.655 134.129 1.00 59.40  ? 397  GLN A CG  1 
ATOM   3242  C  CD  . GLN A 1 397  ? 92.910  109.106 134.636 1.00 67.03  ? 397  GLN A CD  1 
ATOM   3243  O  OE1 . GLN A 1 397  ? 92.876  108.059 135.280 1.00 76.39  ? 397  GLN A OE1 1 
ATOM   3244  N  NE2 . GLN A 1 397  ? 91.824  109.815 134.361 1.00 68.72  ? 397  GLN A NE2 1 
ATOM   3245  N  N   . SER A 1 398  ? 98.789  109.339 135.765 1.00 69.88  ? 398  SER A N   1 
ATOM   3246  C  CA  . SER A 1 398  ? 99.643  109.038 136.894 1.00 66.05  ? 398  SER A CA  1 
ATOM   3247  C  C   . SER A 1 398  ? 100.200 110.326 137.487 1.00 59.15  ? 398  SER A C   1 
ATOM   3248  O  O   . SER A 1 398  ? 100.263 111.371 136.835 1.00 67.21  ? 398  SER A O   1 
ATOM   3249  C  CB  . SER A 1 398  ? 100.778 108.102 136.474 1.00 56.36  ? 398  SER A CB  1 
ATOM   3250  O  OG  . SER A 1 398  ? 101.583 108.694 135.470 1.00 67.64  ? 398  SER A OG  1 
ATOM   3251  N  N   . THR A 1 399  ? 100.617 110.233 138.742 1.00 61.33  ? 399  THR A N   1 
ATOM   3252  C  CA  . THR A 1 399  ? 101.198 111.358 139.452 1.00 61.79  ? 399  THR A CA  1 
ATOM   3253  C  C   . THR A 1 399  ? 102.716 111.292 139.383 1.00 67.31  ? 399  THR A C   1 
ATOM   3254  O  O   . THR A 1 399  ? 103.305 110.207 139.387 1.00 82.42  ? 399  THR A O   1 
ATOM   3255  C  CB  . THR A 1 399  ? 100.732 111.393 140.911 1.00 62.63  ? 399  THR A CB  1 
ATOM   3256  O  OG1 . THR A 1 399  ? 101.243 112.569 141.548 1.00 67.76  ? 399  THR A OG1 1 
ATOM   3257  C  CG2 . THR A 1 399  ? 101.193 110.154 141.670 1.00 90.46  ? 399  THR A CG2 1 
ATOM   3258  N  N   . LYS A 1 400  ? 103.342 112.460 139.298 1.00 61.04  ? 400  LYS A N   1 
ATOM   3259  C  CA  . LYS A 1 400  ? 104.779 112.574 139.131 1.00 49.93  ? 400  LYS A CA  1 
ATOM   3260  C  C   . LYS A 1 400  ? 105.378 113.314 140.315 1.00 64.39  ? 400  LYS A C   1 
ATOM   3261  O  O   . LYS A 1 400  ? 104.725 114.150 140.946 1.00 72.22  ? 400  LYS A O   1 
ATOM   3262  C  CB  . LYS A 1 400  ? 105.144 113.303 137.832 1.00 54.12  ? 400  LYS A CB  1 
ATOM   3263  C  CG  . LYS A 1 400  ? 104.456 112.749 136.604 1.00 50.15  ? 400  LYS A CG  1 
ATOM   3264  C  CD  . LYS A 1 400  ? 105.128 111.460 136.171 1.00 54.74  ? 400  LYS A CD  1 
ATOM   3265  C  CE  . LYS A 1 400  ? 104.497 110.896 134.914 1.00 60.03  ? 400  LYS A CE  1 
ATOM   3266  N  NZ  . LYS A 1 400  ? 105.051 109.554 134.585 1.00 55.73  ? 400  LYS A NZ  1 
ATOM   3267  N  N   . ILE A 1 401  ? 106.632 112.994 140.604 1.00 66.05  ? 401  ILE A N   1 
ATOM   3268  C  CA  . ILE A 1 401  ? 107.408 113.672 141.629 1.00 58.24  ? 401  ILE A CA  1 
ATOM   3269  C  C   . ILE A 1 401  ? 108.460 114.499 140.912 1.00 69.38  ? 401  ILE A C   1 
ATOM   3270  O  O   . ILE A 1 401  ? 109.323 113.954 140.212 1.00 72.33  ? 401  ILE A O   1 
ATOM   3271  C  CB  . ILE A 1 401  ? 108.044 112.676 142.609 1.00 62.44  ? 401  ILE A CB  1 
ATOM   3272  C  CG1 . ILE A 1 401  ? 106.981 112.103 143.548 1.00 69.38  ? 401  ILE A CG1 1 
ATOM   3273  C  CG2 . ILE A 1 401  ? 109.134 113.335 143.413 1.00 65.71  ? 401  ILE A CG2 1 
ATOM   3274  C  CD1 . ILE A 1 401  ? 106.450 113.104 144.551 1.00 67.91  ? 401  ILE A CD1 1 
ATOM   3275  N  N   . LEU A 1 402  ? 108.392 115.814 141.086 1.00 57.12  ? 402  LEU A N   1 
ATOM   3276  C  CA  . LEU A 1 402  ? 109.260 116.744 140.375 1.00 46.31  ? 402  LEU A CA  1 
ATOM   3277  C  C   . LEU A 1 402  ? 110.119 117.529 141.360 1.00 59.71  ? 402  LEU A C   1 
ATOM   3278  O  O   . LEU A 1 402  ? 109.720 117.754 142.501 1.00 68.44  ? 402  LEU A O   1 
ATOM   3279  C  CB  . LEU A 1 402  ? 108.445 117.712 139.515 1.00 51.58  ? 402  LEU A CB  1 
ATOM   3280  C  CG  . LEU A 1 402  ? 107.331 117.055 138.709 1.00 58.30  ? 402  LEU A CG  1 
ATOM   3281  C  CD1 . LEU A 1 402  ? 106.500 118.117 138.019 1.00 43.46  ? 402  LEU A CD1 1 
ATOM   3282  C  CD2 . LEU A 1 402  ? 107.916 116.069 137.710 1.00 67.95  ? 402  LEU A CD2 1 
ATOM   3283  N  N   . LYS A 1 403  ? 111.300 117.952 140.898 1.00 48.55  ? 403  LYS A N   1 
ATOM   3284  C  CA  . LYS A 1 403  ? 112.228 118.731 141.690 1.00 43.45  ? 403  LYS A CA  1 
ATOM   3285  C  C   . LYS A 1 403  ? 112.308 120.140 141.140 1.00 62.27  ? 403  LYS A C   1 
ATOM   3286  O  O   . LYS A 1 403  ? 112.663 120.331 139.970 1.00 77.53  ? 403  LYS A O   1 
ATOM   3287  C  CB  . LYS A 1 403  ? 113.607 118.083 141.688 1.00 59.87  ? 403  LYS A CB  1 
ATOM   3288  C  CG  . LYS A 1 403  ? 114.519 118.611 142.756 1.00 55.37  ? 403  LYS A CG  1 
ATOM   3289  C  CD  . LYS A 1 403  ? 115.830 117.855 142.748 1.00 55.62  ? 403  LYS A CD  1 
ATOM   3290  C  CE  . LYS A 1 403  ? 116.777 118.300 143.842 1.00 60.33  ? 403  LYS A CE  1 
ATOM   3291  N  NZ  . LYS A 1 403  ? 116.261 117.904 145.173 1.00 86.97  ? 403  LYS A NZ  1 
ATOM   3292  N  N   . PRO A 1 404  ? 111.988 121.164 141.936 1.00 59.52  ? 404  PRO A N   1 
ATOM   3293  C  CA  . PRO A 1 404  ? 112.021 122.531 141.395 1.00 63.39  ? 404  PRO A CA  1 
ATOM   3294  C  C   . PRO A 1 404  ? 113.389 122.948 140.849 1.00 65.44  ? 404  PRO A C   1 
ATOM   3295  O  O   . PRO A 1 404  ? 113.450 123.746 139.911 1.00 72.62  ? 404  PRO A O   1 
ATOM   3296  C  CB  . PRO A 1 404  ? 111.565 123.381 142.591 1.00 57.06  ? 404  PRO A CB  1 
ATOM   3297  C  CG  . PRO A 1 404  ? 110.653 122.492 143.406 1.00 58.76  ? 404  PRO A CG  1 
ATOM   3298  C  CD  . PRO A 1 404  ? 111.250 121.083 143.208 1.00 69.25  ? 404  PRO A CD  1 
ATOM   3299  N  N   . LYS A 1 405  ? 114.504 122.481 141.440 1.00 58.99  ? 405  LYS A N   1 
ATOM   3300  C  CA  . LYS A 1 405  ? 115.810 122.975 140.996 1.00 50.43  ? 405  LYS A CA  1 
ATOM   3301  C  C   . LYS A 1 405  ? 116.096 122.594 139.546 1.00 55.70  ? 405  LYS A C   1 
ATOM   3302  O  O   . LYS A 1 405  ? 116.559 123.436 138.761 1.00 81.79  ? 405  LYS A O   1 
ATOM   3303  C  CB  . LYS A 1 405  ? 116.936 122.445 141.877 1.00 56.35  ? 405  LYS A CB  1 
ATOM   3304  C  CG  . LYS A 1 405  ? 118.244 123.174 141.623 1.00 69.46  ? 405  LYS A CG  1 
ATOM   3305  C  CD  . LYS A 1 405  ? 119.356 122.719 142.529 1.00 82.54  ? 405  LYS A CD  1 
ATOM   3306  C  CE  . LYS A 1 405  ? 120.458 123.755 142.529 1.00 85.46  ? 405  LYS A CE  1 
ATOM   3307  N  NZ  . LYS A 1 405  ? 121.523 123.433 143.508 1.00 94.84  ? 405  LYS A NZ  1 
ATOM   3308  N  N   . VAL A 1 406  ? 115.811 121.345 139.166 1.00 55.63  ? 406  VAL A N   1 
ATOM   3309  C  CA  . VAL A 1 406  ? 116.047 120.913 137.791 1.00 60.82  ? 406  VAL A CA  1 
ATOM   3310  C  C   . VAL A 1 406  ? 115.167 121.690 136.819 1.00 77.23  ? 406  VAL A C   1 
ATOM   3311  O  O   . VAL A 1 406  ? 115.636 122.153 135.770 1.00 82.39  ? 406  VAL A O   1 
ATOM   3312  C  CB  . VAL A 1 406  ? 115.804 119.401 137.656 1.00 59.39  ? 406  VAL A CB  1 
ATOM   3313  C  CG1 . VAL A 1 406  ? 115.929 118.968 136.199 1.00 60.02  ? 406  VAL A CG1 1 
ATOM   3314  C  CG2 . VAL A 1 406  ? 116.787 118.624 138.518 1.00 53.91  ? 406  VAL A CG2 1 
ATOM   3315  N  N   . MET A 1 407  ? 113.888 121.875 137.165 1.00 63.72  ? 407  MET A N   1 
ATOM   3316  C  CA  . MET A 1 407  ? 112.989 122.621 136.294 1.00 68.70  ? 407  MET A CA  1 
ATOM   3317  C  C   . MET A 1 407  ? 113.427 124.063 136.132 1.00 68.08  ? 407  MET A C   1 
ATOM   3318  O  O   . MET A 1 407  ? 113.454 124.603 135.017 1.00 73.63  ? 407  MET A O   1 
ATOM   3319  C  CB  . MET A 1 407  ? 111.578 122.558 136.885 1.00 62.72  ? 407  MET A CB  1 
ATOM   3320  C  CG  . MET A 1 407  ? 110.973 121.173 136.964 1.00 56.10  ? 407  MET A CG  1 
ATOM   3321  S  SD  . MET A 1 407  ? 109.265 121.144 137.572 1.00 75.50  ? 407  MET A SD  1 
ATOM   3322  C  CE  . MET A 1 407  ? 109.355 121.999 139.153 1.00 63.78  ? 407  MET A CE  1 
ATOM   3323  N  N   . PHE A 1 408  ? 113.815 124.694 137.240 1.00 59.83  ? 408  PHE A N   1 
ATOM   3324  C  CA  . PHE A 1 408  ? 114.324 126.061 137.222 1.00 53.90  ? 408  PHE A CA  1 
ATOM   3325  C  C   . PHE A 1 408  ? 115.534 126.201 136.308 1.00 56.22  ? 408  PHE A C   1 
ATOM   3326  O  O   . PHE A 1 408  ? 115.598 127.110 135.464 1.00 69.16  ? 408  PHE A O   1 
ATOM   3327  C  CB  . PHE A 1 408  ? 114.670 126.476 138.651 1.00 64.32  ? 408  PHE A CB  1 
ATOM   3328  C  CG  . PHE A 1 408  ? 115.170 127.874 138.766 1.00 65.74  ? 408  PHE A CG  1 
ATOM   3329  C  CD1 . PHE A 1 408  ? 114.320 128.944 138.564 1.00 69.78  ? 408  PHE A CD1 1 
ATOM   3330  C  CD2 . PHE A 1 408  ? 116.495 128.122 139.082 1.00 81.75  ? 408  PHE A CD2 1 
ATOM   3331  C  CE1 . PHE A 1 408  ? 114.784 130.241 138.664 1.00 81.40  ? 408  PHE A CE1 1 
ATOM   3332  C  CE2 . PHE A 1 408  ? 116.964 129.417 139.187 1.00 92.43  ? 408  PHE A CE2 1 
ATOM   3333  C  CZ  . PHE A 1 408  ? 116.108 130.476 138.977 1.00 84.41  ? 408  PHE A CZ  1 
ATOM   3334  N  N   . GLU A 1 409  ? 116.507 125.303 136.460 1.00 62.08  ? 409  GLU A N   1 
ATOM   3335  C  CA  . GLU A 1 409  ? 117.740 125.441 135.699 1.00 55.69  ? 409  GLU A CA  1 
ATOM   3336  C  C   . GLU A 1 409  ? 117.519 125.183 134.214 1.00 59.42  ? 409  GLU A C   1 
ATOM   3337  O  O   . GLU A 1 409  ? 118.097 125.881 133.370 1.00 76.11  ? 409  GLU A O   1 
ATOM   3338  C  CB  . GLU A 1 409  ? 118.808 124.522 136.286 1.00 62.73  ? 409  GLU A CB  1 
ATOM   3339  C  CG  . GLU A 1 409  ? 119.386 125.090 137.570 1.00 64.38  ? 409  GLU A CG  1 
ATOM   3340  C  CD  . GLU A 1 409  ? 120.498 124.248 138.140 1.00 94.78  ? 409  GLU A CD  1 
ATOM   3341  O  OE1 . GLU A 1 409  ? 120.560 123.044 137.818 1.00 95.37  ? 409  GLU A OE1 1 
ATOM   3342  O  OE2 . GLU A 1 409  ? 121.312 124.795 138.912 1.00 93.71  ? 409  GLU A OE2 1 
ATOM   3343  N  N   . THR A 1 410  ? 116.667 124.209 133.866 1.00 54.18  ? 410  THR A N   1 
ATOM   3344  C  CA  . THR A 1 410  ? 116.430 123.984 132.444 1.00 52.95  ? 410  THR A CA  1 
ATOM   3345  C  C   . THR A 1 410  ? 115.653 125.137 131.815 1.00 60.75  ? 410  THR A C   1 
ATOM   3346  O  O   . THR A 1 410  ? 115.897 125.484 130.653 1.00 74.70  ? 410  THR A O   1 
ATOM   3347  C  CB  . THR A 1 410  ? 115.707 122.649 132.209 1.00 44.83  ? 410  THR A CB  1 
ATOM   3348  O  OG1 . THR A 1 410  ? 115.448 122.490 130.810 1.00 61.49  ? 410  THR A OG1 1 
ATOM   3349  C  CG2 . THR A 1 410  ? 114.386 122.584 132.945 1.00 79.27  ? 410  THR A CG2 1 
ATOM   3350  N  N   . PHE A 1 411  ? 114.770 125.791 132.579 1.00 64.87  ? 411  PHE A N   1 
ATOM   3351  C  CA  . PHE A 1 411  ? 114.113 126.993 132.068 1.00 57.05  ? 411  PHE A CA  1 
ATOM   3352  C  C   . PHE A 1 411  ? 115.115 128.121 131.814 1.00 57.63  ? 411  PHE A C   1 
ATOM   3353  O  O   . PHE A 1 411  ? 115.065 128.804 130.772 1.00 70.75  ? 411  PHE A O   1 
ATOM   3354  C  CB  . PHE A 1 411  ? 113.039 127.444 133.062 1.00 49.31  ? 411  PHE A CB  1 
ATOM   3355  C  CG  . PHE A 1 411  ? 112.346 128.714 132.663 1.00 51.96  ? 411  PHE A CG  1 
ATOM   3356  C  CD1 . PHE A 1 411  ? 111.835 128.874 131.390 1.00 60.47  ? 411  PHE A CD1 1 
ATOM   3357  C  CD2 . PHE A 1 411  ? 112.212 129.756 133.571 1.00 52.03  ? 411  PHE A CD2 1 
ATOM   3358  C  CE1 . PHE A 1 411  ? 111.203 130.047 131.023 1.00 60.93  ? 411  PHE A CE1 1 
ATOM   3359  C  CE2 . PHE A 1 411  ? 111.581 130.931 133.211 1.00 56.73  ? 411  PHE A CE2 1 
ATOM   3360  C  CZ  . PHE A 1 411  ? 111.075 131.076 131.934 1.00 58.34  ? 411  PHE A CZ  1 
ATOM   3361  N  N   . CYS A 1 412  ? 116.030 128.338 132.763 1.00 61.77  ? 412  CYS A N   1 
ATOM   3362  C  CA  . CYS A 1 412  ? 117.036 129.377 132.562 1.00 57.19  ? 412  CYS A CA  1 
ATOM   3363  C  C   . CYS A 1 412  ? 117.908 129.085 131.341 1.00 63.40  ? 412  CYS A C   1 
ATOM   3364  O  O   . CYS A 1 412  ? 118.248 130.002 130.577 1.00 70.15  ? 412  CYS A O   1 
ATOM   3365  C  CB  . CYS A 1 412  ? 117.889 129.520 133.823 1.00 64.05  ? 412  CYS A CB  1 
ATOM   3366  S  SG  . CYS A 1 412  ? 116.952 130.053 135.276 1.00 73.10  ? 412  CYS A SG  1 
ATOM   3367  N  N   . VAL A 1 413  ? 118.253 127.815 131.126 1.00 60.64  ? 413  VAL A N   1 
ATOM   3368  C  CA  . VAL A 1 413  ? 119.034 127.444 129.946 1.00 57.54  ? 413  VAL A CA  1 
ATOM   3369  C  C   . VAL A 1 413  ? 118.244 127.708 128.667 1.00 72.45  ? 413  VAL A C   1 
ATOM   3370  O  O   . VAL A 1 413  ? 118.806 128.127 127.647 1.00 80.66  ? 413  VAL A O   1 
ATOM   3371  C  CB  . VAL A 1 413  ? 119.498 125.979 130.047 1.00 62.36  ? 413  VAL A CB  1 
ATOM   3372  C  CG1 . VAL A 1 413  ? 120.043 125.493 128.712 1.00 65.90  ? 413  VAL A CG1 1 
ATOM   3373  C  CG2 . VAL A 1 413  ? 120.572 125.856 131.119 1.00 62.05  ? 413  VAL A CG2 1 
ATOM   3374  N  N   . PHE A 1 414  ? 116.935 127.444 128.694 1.00 68.44  ? 414  PHE A N   1 
ATOM   3375  C  CA  . PHE A 1 414  ? 116.071 127.776 127.562 1.00 61.02  ? 414  PHE A CA  1 
ATOM   3376  C  C   . PHE A 1 414  ? 116.222 129.242 127.163 1.00 68.17  ? 414  PHE A C   1 
ATOM   3377  O  O   . PHE A 1 414  ? 116.507 129.576 125.995 1.00 72.48  ? 414  PHE A O   1 
ATOM   3378  C  CB  . PHE A 1 414  ? 114.622 127.480 127.961 1.00 74.54  ? 414  PHE A CB  1 
ATOM   3379  C  CG  . PHE A 1 414  ? 113.649 127.462 126.820 1.00 70.96  ? 414  PHE A CG  1 
ATOM   3380  C  CD1 . PHE A 1 414  ? 113.442 126.312 126.082 1.00 77.60  ? 414  PHE A CD1 1 
ATOM   3381  C  CD2 . PHE A 1 414  ? 112.922 128.598 126.502 1.00 70.88  ? 414  PHE A CD2 1 
ATOM   3382  C  CE1 . PHE A 1 414  ? 112.534 126.295 125.038 1.00 71.36  ? 414  PHE A CE1 1 
ATOM   3383  C  CE2 . PHE A 1 414  ? 112.017 128.590 125.459 1.00 65.72  ? 414  PHE A CE2 1 
ATOM   3384  C  CZ  . PHE A 1 414  ? 111.822 127.438 124.725 1.00 59.58  ? 414  PHE A CZ  1 
ATOM   3385  N  N   . LYS A 1 415  ? 116.068 130.131 128.148 1.00 67.02  ? 415  LYS A N   1 
ATOM   3386  C  CA  . LYS A 1 415  ? 116.173 131.561 127.862 1.00 56.78  ? 415  LYS A CA  1 
ATOM   3387  C  C   . LYS A 1 415  ? 117.564 131.932 127.356 1.00 62.23  ? 415  LYS A C   1 
ATOM   3388  O  O   . LYS A 1 415  ? 117.708 132.730 126.414 1.00 72.20  ? 415  LYS A O   1 
ATOM   3389  C  CB  . LYS A 1 415  ? 115.846 132.360 129.118 1.00 45.28  ? 415  LYS A CB  1 
ATOM   3390  C  CG  . LYS A 1 415  ? 114.418 132.230 129.576 1.00 55.95  ? 415  LYS A CG  1 
ATOM   3391  C  CD  . LYS A 1 415  ? 114.181 133.117 130.773 1.00 56.28  ? 415  LYS A CD  1 
ATOM   3392  C  CE  . LYS A 1 415  ? 114.190 134.572 130.359 1.00 64.86  ? 415  LYS A CE  1 
ATOM   3393  N  NZ  . LYS A 1 415  ? 113.352 135.397 131.264 1.00 76.43  ? 415  LYS A NZ  1 
ATOM   3394  N  N   . PHE A 1 416  ? 118.601 131.341 127.958 1.00 68.08  ? 416  PHE A N   1 
ATOM   3395  C  CA  . PHE A 1 416  ? 119.965 131.628 127.529 1.00 74.57  ? 416  PHE A CA  1 
ATOM   3396  C  C   . PHE A 1 416  ? 120.214 131.215 126.082 1.00 66.39  ? 416  PHE A C   1 
ATOM   3397  O  O   . PHE A 1 416  ? 120.876 131.942 125.332 1.00 76.45  ? 416  PHE A O   1 
ATOM   3398  C  CB  . PHE A 1 416  ? 120.954 130.930 128.461 1.00 82.45  ? 416  PHE A CB  1 
ATOM   3399  C  CG  . PHE A 1 416  ? 122.254 130.584 127.804 1.00 70.29  ? 416  PHE A CG  1 
ATOM   3400  C  CD1 . PHE A 1 416  ? 123.238 131.539 127.628 1.00 81.99  ? 416  PHE A CD1 1 
ATOM   3401  C  CD2 . PHE A 1 416  ? 122.493 129.290 127.368 1.00 73.26  ? 416  PHE A CD2 1 
ATOM   3402  C  CE1 . PHE A 1 416  ? 124.432 131.212 127.013 1.00 91.60  ? 416  PHE A CE1 1 
ATOM   3403  C  CE2 . PHE A 1 416  ? 123.686 128.958 126.757 1.00 71.13  ? 416  PHE A CE2 1 
ATOM   3404  C  CZ  . PHE A 1 416  ? 124.657 129.920 126.580 1.00 81.51  ? 416  PHE A CZ  1 
ATOM   3405  N  N   . ILE A 1 417  ? 119.708 130.048 125.676 1.00 64.78  ? 417  ILE A N   1 
ATOM   3406  C  CA  . ILE A 1 417  ? 119.907 129.592 124.302 1.00 52.89  ? 417  ILE A CA  1 
ATOM   3407  C  C   . ILE A 1 417  ? 119.249 130.549 123.317 1.00 63.02  ? 417  ILE A C   1 
ATOM   3408  O  O   . ILE A 1 417  ? 119.842 130.915 122.287 1.00 75.51  ? 417  ILE A O   1 
ATOM   3409  C  CB  . ILE A 1 417  ? 119.392 128.152 124.127 1.00 63.62  ? 417  ILE A CB  1 
ATOM   3410  C  CG1 . ILE A 1 417  ? 120.268 127.180 124.917 1.00 77.86  ? 417  ILE A CG1 1 
ATOM   3411  C  CG2 . ILE A 1 417  ? 119.388 127.764 122.652 1.00 72.68  ? 417  ILE A CG2 1 
ATOM   3412  C  CD1 . ILE A 1 417  ? 119.776 125.752 124.883 1.00 91.80  ? 417  ILE A CD1 1 
ATOM   3413  N  N   . VAL A 1 418  ? 118.015 130.977 123.617 1.00 73.34  ? 418  VAL A N   1 
ATOM   3414  C  CA  . VAL A 1 418  ? 117.344 131.917 122.715 1.00 72.14  ? 418  VAL A CA  1 
ATOM   3415  C  C   . VAL A 1 418  ? 118.157 133.203 122.580 1.00 68.11  ? 418  VAL A C   1 
ATOM   3416  O  O   . VAL A 1 418  ? 118.415 133.690 121.465 1.00 69.73  ? 418  VAL A O   1 
ATOM   3417  C  CB  . VAL A 1 418  ? 115.907 132.199 123.190 1.00 74.97  ? 418  VAL A CB  1 
ATOM   3418  C  CG1 . VAL A 1 418  ? 115.378 133.474 122.545 1.00 67.76  ? 418  VAL A CG1 1 
ATOM   3419  C  CG2 . VAL A 1 418  ? 114.998 131.026 122.848 1.00 63.98  ? 418  VAL A CG2 1 
ATOM   3420  N  N   . ALA A 1 419  ? 118.607 133.750 123.714 1.00 74.77  ? 419  ALA A N   1 
ATOM   3421  C  CA  . ALA A 1 419  ? 119.361 135.001 123.680 1.00 75.29  ? 419  ALA A CA  1 
ATOM   3422  C  C   . ALA A 1 419  ? 120.669 134.851 122.906 1.00 79.05  ? 419  ALA A C   1 
ATOM   3423  O  O   . ALA A 1 419  ? 121.047 135.741 122.129 1.00 90.27  ? 419  ALA A O   1 
ATOM   3424  C  CB  . ALA A 1 419  ? 119.633 135.485 125.104 1.00 82.41  ? 419  ALA A CB  1 
ATOM   3425  N  N   . LYS A 1 420  ? 121.371 133.732 123.103 1.00 75.85  ? 420  LYS A N   1 
ATOM   3426  C  CA  . LYS A 1 420  ? 122.643 133.529 122.418 1.00 64.40  ? 420  LYS A CA  1 
ATOM   3427  C  C   . LYS A 1 420  ? 122.461 133.422 120.910 1.00 67.88  ? 420  LYS A C   1 
ATOM   3428  O  O   . LYS A 1 420  ? 123.260 133.983 120.145 1.00 89.15  ? 420  LYS A O   1 
ATOM   3429  C  CB  . LYS A 1 420  ? 123.346 132.286 122.959 1.00 69.50  ? 420  LYS A CB  1 
ATOM   3430  C  CG  . LYS A 1 420  ? 124.500 131.835 122.089 1.00 71.05  ? 420  LYS A CG  1 
ATOM   3431  C  CD  . LYS A 1 420  ? 125.207 130.632 122.669 1.00 86.91  ? 420  LYS A CD  1 
ATOM   3432  C  CE  . LYS A 1 420  ? 126.279 130.135 121.717 1.00 98.22  ? 420  LYS A CE  1 
ATOM   3433  N  NZ  . LYS A 1 420  ? 127.073 129.040 122.329 1.00 98.98  ? 420  LYS A NZ  1 
ATOM   3434  N  N   . ASN A 1 421  ? 121.436 132.693 120.457 1.00 66.67  ? 421  ASN A N   1 
ATOM   3435  C  CA  . ASN A 1 421  ? 121.218 132.628 119.014 1.00 63.99  ? 421  ASN A CA  1 
ATOM   3436  C  C   . ASN A 1 421  ? 120.889 134.002 118.453 1.00 74.70  ? 421  ASN A C   1 
ATOM   3437  O  O   . ASN A 1 421  ? 121.368 134.369 117.372 1.00 83.21  ? 421  ASN A O   1 
ATOM   3438  C  CB  . ASN A 1 421  ? 120.110 131.642 118.652 1.00 79.34  ? 421  ASN A CB  1 
ATOM   3439  C  CG  . ASN A 1 421  ? 119.696 131.758 117.188 1.00 75.80  ? 421  ASN A CG  1 
ATOM   3440  O  OD1 . ASN A 1 421  ? 118.872 132.598 116.825 1.00 79.66  ? 421  ASN A OD1 1 
ATOM   3441  N  ND2 . ASN A 1 421  ? 120.307 130.943 116.338 1.00 73.97  ? 421  ASN A ND2 1 
ATOM   3442  N  N   . HIS A 1 422  ? 120.084 134.784 119.180 1.00 86.14  ? 422  HIS A N   1 
ATOM   3443  C  CA  . HIS A 1 422  ? 119.779 136.136 118.715 1.00 81.36  ? 422  HIS A CA  1 
ATOM   3444  C  C   . HIS A 1 422  ? 121.060 136.949 118.549 1.00 79.91  ? 422  HIS A C   1 
ATOM   3445  O  O   . HIS A 1 422  ? 121.253 137.625 117.528 1.00 93.18  ? 422  HIS A O   1 
ATOM   3446  C  CB  . HIS A 1 422  ? 118.811 136.833 119.672 1.00 84.31  ? 422  HIS A CB  1 
ATOM   3447  C  CG  . HIS A 1 422  ? 118.469 138.234 119.263 1.00 89.53  ? 422  HIS A CG  1 
ATOM   3448  N  ND1 . HIS A 1 422  ? 117.689 138.514 118.160 1.00 88.19  ? 422  HIS A ND1 1 
ATOM   3449  C  CD2 . HIS A 1 422  ? 118.805 139.430 119.799 1.00 98.11  ? 422  HIS A CD2 1 
ATOM   3450  C  CE1 . HIS A 1 422  ? 117.556 139.823 118.039 1.00 91.76  ? 422  HIS A CE1 1 
ATOM   3451  N  NE2 . HIS A 1 422  ? 118.223 140.402 119.022 1.00 89.64  ? 422  HIS A NE2 1 
ATOM   3452  N  N   . TYR A 1 423  ? 121.950 136.894 119.548 1.00 89.18  ? 423  TYR A N   1 
ATOM   3453  C  CA  . TYR A 1 423  ? 123.180 137.680 119.472 1.00 83.77  ? 423  TYR A CA  1 
ATOM   3454  C  C   . TYR A 1 423  ? 124.073 137.233 118.321 1.00 82.61  ? 423  TYR A C   1 
ATOM   3455  O  O   . TYR A 1 423  ? 124.600 138.071 117.580 1.00 91.40  ? 423  TYR A O   1 
ATOM   3456  C  CB  . TYR A 1 423  ? 123.958 137.585 120.786 1.00 89.88  ? 423  TYR A CB  1 
ATOM   3457  C  CG  . TYR A 1 423  ? 125.225 138.423 120.811 1.00 94.79  ? 423  TYR A CG  1 
ATOM   3458  C  CD1 . TYR A 1 423  ? 126.415 137.932 120.283 1.00 101.49 ? 423  TYR A CD1 1 
ATOM   3459  C  CD2 . TYR A 1 423  ? 125.238 139.691 121.375 1.00 112.37 ? 423  TYR A CD2 1 
ATOM   3460  C  CE1 . TYR A 1 423  ? 127.573 138.684 120.297 1.00 108.62 ? 423  TYR A CE1 1 
ATOM   3461  C  CE2 . TYR A 1 423  ? 126.398 140.450 121.398 1.00 128.85 ? 423  TYR A CE2 1 
ATOM   3462  C  CZ  . TYR A 1 423  ? 127.561 139.940 120.858 1.00 124.36 ? 423  TYR A CZ  1 
ATOM   3463  O  OH  . TYR A 1 423  ? 128.716 140.690 120.875 1.00 110.05 ? 423  TYR A OH  1 
ATOM   3464  N  N   . HIS A 1 424  ? 124.257 135.921 118.141 1.00 85.67  ? 424  HIS A N   1 
ATOM   3465  C  CA  . HIS A 1 424  ? 125.133 135.520 117.043 1.00 82.83  ? 424  HIS A CA  1 
ATOM   3466  C  C   . HIS A 1 424  ? 124.477 135.674 115.681 1.00 94.62  ? 424  HIS A C   1 
ATOM   3467  O  O   . HIS A 1 424  ? 125.177 135.593 114.666 1.00 101.55 ? 424  HIS A O   1 
ATOM   3468  C  CB  . HIS A 1 424  ? 125.637 134.084 117.208 1.00 77.28  ? 424  HIS A CB  1 
ATOM   3469  C  CG  . HIS A 1 424  ? 126.649 133.920 118.299 1.00 87.12  ? 424  HIS A CG  1 
ATOM   3470  N  ND1 . HIS A 1 424  ? 127.493 134.940 118.684 1.00 96.52  ? 424  HIS A ND1 1 
ATOM   3471  C  CD2 . HIS A 1 424  ? 126.989 132.846 119.049 1.00 97.88  ? 424  HIS A CD2 1 
ATOM   3472  C  CE1 . HIS A 1 424  ? 128.289 134.510 119.646 1.00 97.56  ? 424  HIS A CE1 1 
ATOM   3473  N  NE2 . HIS A 1 424  ? 128.005 133.242 119.885 1.00 95.20  ? 424  HIS A NE2 1 
ATOM   3474  N  N   . SER A 1 425  ? 123.168 135.901 115.631 1.00 97.51  ? 425  SER A N   1 
ATOM   3475  C  CA  . SER A 1 425  ? 122.548 136.157 114.340 1.00 98.77  ? 425  SER A CA  1 
ATOM   3476  C  C   . SER A 1 425  ? 122.611 137.634 113.969 1.00 94.55  ? 425  SER A C   1 
ATOM   3477  O  O   . SER A 1 425  ? 122.965 137.975 112.836 1.00 94.68  ? 425  SER A O   1 
ATOM   3478  C  CB  . SER A 1 425  ? 121.097 135.668 114.337 1.00 99.17  ? 425  SER A CB  1 
ATOM   3479  O  OG  . SER A 1 425  ? 120.479 135.940 113.091 1.00 95.34  ? 425  SER A OG  1 
ATOM   3480  N  N   . GLN A 1 426  ? 122.287 138.526 114.908 1.00 100.96 ? 426  GLN A N   1 
ATOM   3481  C  CA  . GLN A 1 426  ? 122.182 139.945 114.594 1.00 90.50  ? 426  GLN A CA  1 
ATOM   3482  C  C   . GLN A 1 426  ? 123.259 140.810 115.243 1.00 86.74  ? 426  GLN A C   1 
ATOM   3483  O  O   . GLN A 1 426  ? 123.145 142.041 115.212 1.00 87.91  ? 426  GLN A O   1 
ATOM   3484  C  CB  . GLN A 1 426  ? 120.798 140.444 115.002 1.00 89.90  ? 426  GLN A CB  1 
ATOM   3485  C  CG  . GLN A 1 426  ? 119.749 140.240 113.934 1.00 101.19 ? 426  GLN A CG  1 
ATOM   3486  C  CD  . GLN A 1 426  ? 118.350 140.312 114.496 1.00 110.72 ? 426  GLN A CD  1 
ATOM   3487  O  OE1 . GLN A 1 426  ? 117.782 139.299 114.905 1.00 114.74 ? 426  GLN A OE1 1 
ATOM   3488  N  NE2 . GLN A 1 426  ? 117.785 141.511 114.527 1.00 127.62 ? 426  GLN A NE2 1 
ATOM   3489  N  N   . GLY A 1 427  ? 124.293 140.212 115.824 1.00 94.06  ? 427  GLY A N   1 
ATOM   3490  C  CA  . GLY A 1 427  ? 125.435 140.970 116.302 1.00 98.83  ? 427  GLY A CA  1 
ATOM   3491  C  C   . GLY A 1 427  ? 125.197 141.981 117.409 1.00 103.15 ? 427  GLY A C   1 
ATOM   3492  O  O   . GLY A 1 427  ? 126.058 142.832 117.650 1.00 101.78 ? 427  GLY A O   1 
ATOM   3493  N  N   . SER A 1 428  ? 124.054 141.918 118.088 1.00 101.33 ? 428  SER A N   1 
ATOM   3494  C  CA  . SER A 1 428  ? 123.785 142.868 119.162 1.00 100.52 ? 428  SER A CA  1 
ATOM   3495  C  C   . SER A 1 428  ? 122.724 142.295 120.086 1.00 110.07 ? 428  SER A C   1 
ATOM   3496  O  O   . SER A 1 428  ? 121.970 141.392 119.715 1.00 105.68 ? 428  SER A O   1 
ATOM   3497  C  CB  . SER A 1 428  ? 123.343 144.232 118.617 1.00 99.75  ? 428  SER A CB  1 
ATOM   3498  O  OG  . SER A 1 428  ? 123.081 145.142 119.671 1.00 106.62 ? 428  SER A OG  1 
ATOM   3499  N  N   . TRP A 1 429  ? 122.674 142.842 121.299 1.00 109.52 ? 429  TRP A N   1 
ATOM   3500  C  CA  . TRP A 1 429  ? 121.645 142.450 122.248 1.00 109.99 ? 429  TRP A CA  1 
ATOM   3501  C  C   . TRP A 1 429  ? 120.285 142.964 121.793 1.00 111.98 ? 429  TRP A C   1 
ATOM   3502  O  O   . TRP A 1 429  ? 120.169 144.073 121.264 1.00 117.70 ? 429  TRP A O   1 
ATOM   3503  C  CB  . TRP A 1 429  ? 121.962 143.020 123.631 1.00 110.77 ? 429  TRP A CB  1 
ATOM   3504  C  CG  . TRP A 1 429  ? 122.960 142.229 124.413 1.00 105.99 ? 429  TRP A CG  1 
ATOM   3505  C  CD1 . TRP A 1 429  ? 124.318 142.303 124.307 1.00 109.32 ? 429  TRP A CD1 1 
ATOM   3506  C  CD2 . TRP A 1 429  ? 122.689 141.227 125.399 1.00 102.66 ? 429  TRP A CD2 1 
ATOM   3507  N  NE1 . TRP A 1 429  ? 124.910 141.423 125.178 1.00 109.10 ? 429  TRP A NE1 1 
ATOM   3508  C  CE2 . TRP A 1 429  ? 123.931 140.747 125.858 1.00 103.32 ? 429  TRP A CE2 1 
ATOM   3509  C  CE3 . TRP A 1 429  ? 121.518 140.690 125.942 1.00 108.60 ? 429  TRP A CE3 1 
ATOM   3510  C  CZ2 . TRP A 1 429  ? 124.037 139.758 126.833 1.00 101.26 ? 429  TRP A CZ2 1 
ATOM   3511  C  CZ3 . TRP A 1 429  ? 121.625 139.708 126.911 1.00 97.10  ? 429  TRP A CZ3 1 
ATOM   3512  C  CH2 . TRP A 1 429  ? 122.875 139.253 127.347 1.00 91.06  ? 429  TRP A CH2 1 
ATOM   3513  N  N   . TYR A 1 430  ? 119.247 142.160 122.011 1.00 100.74 ? 430  TYR A N   1 
ATOM   3514  C  CA  . TYR A 1 430  ? 117.887 142.669 121.915 1.00 95.28  ? 430  TYR A CA  1 
ATOM   3515  C  C   . TYR A 1 430  ? 117.605 143.671 123.038 1.00 96.31  ? 430  TYR A C   1 
ATOM   3516  O  O   . TYR A 1 430  ? 118.351 143.788 124.014 1.00 99.09  ? 430  TYR A O   1 
ATOM   3517  C  CB  . TYR A 1 430  ? 116.867 141.531 121.921 1.00 86.48  ? 430  TYR A CB  1 
ATOM   3518  C  CG  . TYR A 1 430  ? 117.025 140.540 123.046 1.00 88.95  ? 430  TYR A CG  1 
ATOM   3519  C  CD1 . TYR A 1 430  ? 117.557 139.283 122.815 1.00 88.85  ? 430  TYR A CD1 1 
ATOM   3520  C  CD2 . TYR A 1 430  ? 116.692 140.876 124.346 1.00 102.41 ? 430  TYR A CD2 1 
ATOM   3521  C  CE1 . TYR A 1 430  ? 117.705 138.370 123.838 1.00 86.86  ? 430  TYR A CE1 1 
ATOM   3522  C  CE2 . TYR A 1 430  ? 116.846 139.975 125.380 1.00 90.81  ? 430  TYR A CE2 1 
ATOM   3523  C  CZ  . TYR A 1 430  ? 117.352 138.722 125.121 1.00 78.71  ? 430  TYR A CZ  1 
ATOM   3524  O  OH  . TYR A 1 430  ? 117.514 137.823 126.148 1.00 81.57  ? 430  TYR A OH  1 
ATOM   3525  N  N   . LYS A 1 431  ? 116.499 144.395 122.885 1.00 95.44  ? 431  LYS A N   1 
ATOM   3526  C  CA  . LYS A 1 431  ? 116.186 145.559 123.713 1.00 111.67 ? 431  LYS A CA  1 
ATOM   3527  C  C   . LYS A 1 431  ? 115.568 145.104 125.031 1.00 112.75 ? 431  LYS A C   1 
ATOM   3528  O  O   . LYS A 1 431  ? 114.369 144.821 125.108 1.00 115.47 ? 431  LYS A O   1 
ATOM   3529  C  CB  . LYS A 1 431  ? 115.252 146.496 122.956 1.00 113.66 ? 431  LYS A CB  1 
ATOM   3530  C  CG  . LYS A 1 431  ? 114.853 147.739 123.720 1.00 131.66 ? 431  LYS A CG  1 
ATOM   3531  C  CD  . LYS A 1 431  ? 116.032 148.662 123.938 1.00 142.74 ? 431  LYS A CD  1 
ATOM   3532  C  CE  . LYS A 1 431  ? 115.581 149.963 124.574 1.00 154.62 ? 431  LYS A CE  1 
ATOM   3533  N  NZ  . LYS A 1 431  ? 115.072 149.740 125.955 1.00 146.17 ? 431  LYS A NZ  1 
ATOM   3534  N  N   . THR A 1 432  ? 116.394 145.032 126.074 1.00 107.47 ? 432  THR A N   1 
ATOM   3535  C  CA  . THR A 1 432  ? 115.952 144.612 127.398 1.00 108.65 ? 432  THR A CA  1 
ATOM   3536  C  C   . THR A 1 432  ? 115.072 145.675 128.055 1.00 111.54 ? 432  THR A C   1 
ATOM   3537  O  O   . THR A 1 432  ? 115.250 146.878 127.843 1.00 114.10 ? 432  THR A O   1 
ATOM   3538  C  CB  . THR A 1 432  ? 117.162 144.325 128.289 1.00 117.08 ? 432  THR A CB  1 
ATOM   3539  O  OG1 . THR A 1 432  ? 117.848 145.551 128.570 1.00 112.11 ? 432  THR A OG1 1 
ATOM   3540  C  CG2 . THR A 1 432  ? 118.122 143.374 127.587 1.00 111.80 ? 432  THR A CG2 1 
ATOM   3541  N  N   . THR A 1 433  ? 114.107 145.218 128.867 1.00 106.60 ? 433  THR A N   1 
ATOM   3542  C  CA  . THR A 1 433  ? 113.195 146.122 129.565 1.00 112.91 ? 433  THR A CA  1 
ATOM   3543  C  C   . THR A 1 433  ? 113.118 145.869 131.070 1.00 113.51 ? 433  THR A C   1 
ATOM   3544  O  O   . THR A 1 433  ? 112.283 146.484 131.743 1.00 112.32 ? 433  THR A O   1 
ATOM   3545  C  CB  . THR A 1 433  ? 111.779 146.029 128.978 1.00 111.64 ? 433  THR A CB  1 
ATOM   3546  O  OG1 . THR A 1 433  ? 111.124 144.865 129.498 1.00 111.61 ? 433  THR A OG1 1 
ATOM   3547  C  CG2 . THR A 1 433  ? 111.817 145.944 127.458 1.00 107.34 ? 433  THR A CG2 1 
ATOM   3548  N  N   . HIS A 1 434  ? 113.960 145.000 131.617 1.00 109.12 ? 434  HIS A N   1 
ATOM   3549  C  CA  . HIS A 1 434  ? 113.965 144.679 133.039 1.00 108.38 ? 434  HIS A CA  1 
ATOM   3550  C  C   . HIS A 1 434  ? 115.002 145.530 133.760 1.00 113.61 ? 434  HIS A C   1 
ATOM   3551  O  O   . HIS A 1 434  ? 115.933 146.060 133.148 1.00 124.92 ? 434  HIS A O   1 
ATOM   3552  C  CB  . HIS A 1 434  ? 114.276 143.203 133.285 1.00 105.85 ? 434  HIS A CB  1 
ATOM   3553  C  CG  . HIS A 1 434  ? 115.709 142.847 133.045 1.00 97.32  ? 434  HIS A CG  1 
ATOM   3554  N  ND1 . HIS A 1 434  ? 116.260 142.769 131.784 1.00 103.83 ? 434  HIS A ND1 1 
ATOM   3555  C  CD2 . HIS A 1 434  ? 116.712 142.572 133.912 1.00 98.76  ? 434  HIS A CD2 1 
ATOM   3556  C  CE1 . HIS A 1 434  ? 117.538 142.450 131.885 1.00 108.39 ? 434  HIS A CE1 1 
ATOM   3557  N  NE2 . HIS A 1 434  ? 117.837 142.325 133.165 1.00 101.20 ? 434  HIS A NE2 1 
ATOM   3558  N  N   . ASP A 1 435  ? 114.825 145.674 135.072 1.00 109.19 ? 435  ASP A N   1 
ATOM   3559  C  CA  . ASP A 1 435  ? 115.776 146.460 135.845 1.00 121.20 ? 435  ASP A CA  1 
ATOM   3560  C  C   . ASP A 1 435  ? 117.130 145.756 135.799 1.00 123.81 ? 435  ASP A C   1 
ATOM   3561  O  O   . ASP A 1 435  ? 117.238 144.563 136.098 1.00 119.93 ? 435  ASP A O   1 
ATOM   3562  C  CB  . ASP A 1 435  ? 115.284 146.615 137.288 1.00 118.15 ? 435  ASP A CB  1 
ATOM   3563  C  CG  . ASP A 1 435  ? 116.186 147.500 138.140 1.00 125.55 ? 435  ASP A CG  1 
ATOM   3564  O  OD1 . ASP A 1 435  ? 117.336 147.779 137.743 1.00 130.35 ? 435  ASP A OD1 1 
ATOM   3565  O  OD2 . ASP A 1 435  ? 115.735 147.919 139.227 1.00 120.74 ? 435  ASP A OD2 1 
ATOM   3566  N  N   . LEU A 1 436  ? 118.166 146.516 135.434 1.00 127.22 ? 436  LEU A N   1 
ATOM   3567  C  CA  . LEU A 1 436  ? 119.523 145.983 135.323 1.00 116.10 ? 436  LEU A CA  1 
ATOM   3568  C  C   . LEU A 1 436  ? 120.114 145.573 136.666 1.00 119.22 ? 436  LEU A C   1 
ATOM   3569  O  O   . LEU A 1 436  ? 120.943 144.657 136.722 1.00 118.10 ? 436  LEU A O   1 
ATOM   3570  C  CB  . LEU A 1 436  ? 120.431 147.005 134.635 1.00 117.91 ? 436  LEU A CB  1 
ATOM   3571  C  CG  . LEU A 1 436  ? 120.308 147.152 133.112 1.00 116.04 ? 436  LEU A CG  1 
ATOM   3572  C  CD1 . LEU A 1 436  ? 120.643 145.832 132.421 1.00 104.97 ? 436  LEU A CD1 1 
ATOM   3573  C  CD2 . LEU A 1 436  ? 118.947 147.688 132.659 1.00 111.75 ? 436  LEU A CD2 1 
ATOM   3574  N  N   . HIS A 1 437  ? 119.701 146.230 137.749 1.00 127.03 ? 437  HIS A N   1 
ATOM   3575  C  CA  . HIS A 1 437  ? 120.247 145.951 139.076 1.00 125.52 ? 437  HIS A CA  1 
ATOM   3576  C  C   . HIS A 1 437  ? 120.034 144.502 139.504 1.00 119.06 ? 437  HIS A C   1 
ATOM   3577  O  O   . HIS A 1 437  ? 120.882 143.938 140.205 1.00 122.87 ? 437  HIS A O   1 
ATOM   3578  C  CB  . HIS A 1 437  ? 119.667 146.933 140.091 1.00 130.49 ? 437  HIS A CB  1 
ATOM   3579  C  CG  . HIS A 1 437  ? 120.110 148.345 139.860 1.00 140.33 ? 437  HIS A CG  1 
ATOM   3580  N  ND1 . HIS A 1 437  ? 121.401 148.763 140.101 1.00 135.81 ? 437  HIS A ND1 1 
ATOM   3581  C  CD2 . HIS A 1 437  ? 119.445 149.428 139.392 1.00 145.38 ? 437  HIS A CD2 1 
ATOM   3582  C  CE1 . HIS A 1 437  ? 121.511 150.044 139.800 1.00 146.68 ? 437  HIS A CE1 1 
ATOM   3583  N  NE2 . HIS A 1 437  ? 120.338 150.472 139.367 1.00 153.78 ? 437  HIS A NE2 1 
ATOM   3584  N  N   . LEU A 1 438  ? 118.915 143.892 139.116 1.00 118.54 ? 438  LEU A N   1 
ATOM   3585  C  CA  . LEU A 1 438  ? 118.645 142.511 139.510 1.00 120.33 ? 438  LEU A CA  1 
ATOM   3586  C  C   . LEU A 1 438  ? 119.722 141.547 139.013 1.00 122.81 ? 438  LEU A C   1 
ATOM   3587  O  O   . LEU A 1 438  ? 120.099 140.617 139.734 1.00 120.68 ? 438  LEU A O   1 
ATOM   3588  C  CB  . LEU A 1 438  ? 117.266 142.079 139.009 1.00 123.90 ? 438  LEU A CB  1 
ATOM   3589  C  CG  . LEU A 1 438  ? 116.076 142.679 139.758 1.00 118.96 ? 438  LEU A CG  1 
ATOM   3590  C  CD1 . LEU A 1 438  ? 114.768 142.266 139.104 1.00 116.50 ? 438  LEU A CD1 1 
ATOM   3591  C  CD2 . LEU A 1 438  ? 116.109 142.259 141.222 1.00 118.31 ? 438  LEU A CD2 1 
ATOM   3592  N  N   . THR A 1 439  ? 120.241 141.744 137.797 1.00 115.54 ? 439  THR A N   1 
ATOM   3593  C  CA  . THR A 1 439  ? 121.283 140.847 137.297 1.00 103.63 ? 439  THR A CA  1 
ATOM   3594  C  C   . THR A 1 439  ? 122.607 141.591 137.131 1.00 107.95 ? 439  THR A C   1 
ATOM   3595  O  O   . THR A 1 439  ? 122.827 142.253 136.105 1.00 118.26 ? 439  THR A O   1 
ATOM   3596  C  CB  . THR A 1 439  ? 120.851 140.221 135.967 1.00 90.61  ? 439  THR A CB  1 
ATOM   3597  O  OG1 . THR A 1 439  ? 120.992 141.183 134.914 1.00 88.48  ? 439  THR A OG1 1 
ATOM   3598  C  CG2 . THR A 1 439  ? 119.394 139.778 136.034 1.00 86.66  ? 439  THR A CG2 1 
ATOM   3599  N  N   . PRO A 1 440  ? 123.522 141.492 138.104 1.00 94.00  ? 440  PRO A N   1 
ATOM   3600  C  CA  . PRO A 1 440  ? 124.818 142.191 137.992 1.00 93.17  ? 440  PRO A CA  1 
ATOM   3601  C  C   . PRO A 1 440  ? 125.755 141.661 136.913 1.00 101.50 ? 440  PRO A C   1 
ATOM   3602  O  O   . PRO A 1 440  ? 126.366 142.458 136.188 1.00 106.44 ? 440  PRO A O   1 
ATOM   3603  C  CB  . PRO A 1 440  ? 125.426 142.011 139.395 1.00 88.31  ? 440  PRO A CB  1 
ATOM   3604  C  CG  . PRO A 1 440  ? 124.268 141.648 140.287 1.00 95.96  ? 440  PRO A CG  1 
ATOM   3605  C  CD  . PRO A 1 440  ? 123.356 140.847 139.416 1.00 97.80  ? 440  PRO A CD  1 
ATOM   3606  N  N   . TYR A 1 441  ? 125.891 140.337 136.793 1.00 98.88  ? 441  TYR A N   1 
ATOM   3607  C  CA  . TYR A 1 441  ? 126.823 139.744 135.834 1.00 99.53  ? 441  TYR A CA  1 
ATOM   3608  C  C   . TYR A 1 441  ? 126.464 140.065 134.388 1.00 96.20  ? 441  TYR A C   1 
ATOM   3609  O  O   . TYR A 1 441  ? 127.339 140.393 133.579 1.00 110.83 ? 441  TYR A O   1 
ATOM   3610  C  CB  . TYR A 1 441  ? 126.876 138.228 136.037 1.00 100.55 ? 441  TYR A CB  1 
ATOM   3611  C  CG  . TYR A 1 441  ? 127.798 137.534 135.066 1.00 107.78 ? 441  TYR A CG  1 
ATOM   3612  C  CD1 . TYR A 1 441  ? 129.170 137.727 135.132 1.00 114.10 ? 441  TYR A CD1 1 
ATOM   3613  C  CD2 . TYR A 1 441  ? 127.299 136.701 134.076 1.00 107.75 ? 441  TYR A CD2 1 
ATOM   3614  C  CE1 . TYR A 1 441  ? 130.022 137.103 134.243 1.00 126.52 ? 441  TYR A CE1 1 
ATOM   3615  C  CE2 . TYR A 1 441  ? 128.145 136.070 133.181 1.00 113.11 ? 441  TYR A CE2 1 
ATOM   3616  C  CZ  . TYR A 1 441  ? 129.505 136.275 133.270 1.00 124.81 ? 441  TYR A CZ  1 
ATOM   3617  O  OH  . TYR A 1 441  ? 130.355 135.651 132.386 1.00 109.79 ? 441  TYR A OH  1 
ATOM   3618  N  N   . LEU A 1 442  ? 125.185 139.988 134.051 1.00 92.26  ? 442  LEU A N   1 
ATOM   3619  C  CA  . LEU A 1 442  ? 124.722 140.296 132.703 1.00 98.60  ? 442  LEU A CA  1 
ATOM   3620  C  C   . LEU A 1 442  ? 124.752 141.788 132.391 1.00 99.54  ? 442  LEU A C   1 
ATOM   3621  O  O   . LEU A 1 442  ? 124.828 142.166 131.216 1.00 105.20 ? 442  LEU A O   1 
ATOM   3622  C  CB  . LEU A 1 442  ? 123.305 139.759 132.483 1.00 95.89  ? 442  LEU A CB  1 
ATOM   3623  C  CG  . LEU A 1 442  ? 123.193 138.230 132.569 1.00 77.40  ? 442  LEU A CG  1 
ATOM   3624  C  CD1 . LEU A 1 442  ? 121.764 137.780 132.341 1.00 78.03  ? 442  LEU A CD1 1 
ATOM   3625  C  CD2 . LEU A 1 442  ? 124.144 137.592 131.551 1.00 84.78  ? 442  LEU A CD2 1 
ATOM   3626  N  N   . ARG A 1 443  ? 124.669 142.652 133.399 1.00 92.20  ? 443  ARG A N   1 
ATOM   3627  C  CA  . ARG A 1 443  ? 124.667 144.087 133.127 1.00 93.50  ? 443  ARG A CA  1 
ATOM   3628  C  C   . ARG A 1 443  ? 125.948 144.579 132.449 1.00 106.48 ? 443  ARG A C   1 
ATOM   3629  O  O   . ARG A 1 443  ? 125.883 145.285 131.428 1.00 108.87 ? 443  ARG A O   1 
ATOM   3630  C  CB  . ARG A 1 443  ? 124.419 144.841 134.438 1.00 95.44  ? 443  ARG A CB  1 
ATOM   3631  C  CG  . ARG A 1 443  ? 124.472 146.320 134.246 1.00 106.53 ? 443  ARG A CG  1 
ATOM   3632  C  CD  . ARG A 1 443  ? 124.485 146.991 135.548 1.00 123.83 ? 443  ARG A CD  1 
ATOM   3633  N  NE  . ARG A 1 443  ? 124.594 148.432 135.434 1.00 138.72 ? 443  ARG A NE  1 
ATOM   3634  C  CZ  . ARG A 1 443  ? 124.415 149.224 136.482 1.00 151.27 ? 443  ARG A CZ  1 
ATOM   3635  N  NH1 . ARG A 1 443  ? 124.125 148.677 137.659 1.00 148.76 ? 443  ARG A NH1 1 
ATOM   3636  N  NH2 . ARG A 1 443  ? 124.542 150.552 136.374 1.00 148.38 ? 443  ARG A NH2 1 
ATOM   3637  N  N   . GLN A 1 444  ? 127.100 144.240 132.982 1.00 113.98 ? 444  GLN A N   1 
ATOM   3638  C  CA  . GLN A 1 444  ? 128.306 144.743 132.336 1.00 113.80 ? 444  GLN A CA  1 
ATOM   3639  C  C   . GLN A 1 444  ? 128.680 144.011 131.048 1.00 110.20 ? 444  GLN A C   1 
ATOM   3640  O  O   . GLN A 1 444  ? 129.543 144.504 130.313 1.00 118.39 ? 444  GLN A O   1 
ATOM   3641  C  CB  . GLN A 1 444  ? 129.462 144.737 133.341 1.00 118.91 ? 444  GLN A CB  1 
ATOM   3642  C  CG  . GLN A 1 444  ? 129.845 143.390 133.928 1.00 128.97 ? 444  GLN A CG  1 
ATOM   3643  C  CD  . GLN A 1 444  ? 130.808 142.629 133.058 1.00 143.90 ? 444  GLN A CD  1 
ATOM   3644  O  OE1 . GLN A 1 444  ? 131.593 143.223 132.318 1.00 141.39 ? 444  GLN A OE1 1 
ATOM   3645  N  NE2 . GLN A 1 444  ? 130.817 141.315 133.202 1.00 132.16 ? 444  GLN A NE2 1 
ATOM   3646  N  N   . HIS A 1 445  ? 128.074 142.855 130.741 1.00 110.78 ? 445  HIS A N   1 
ATOM   3647  C  CA  . HIS A 1 445  ? 128.151 142.392 129.355 1.00 110.09 ? 445  HIS A CA  1 
ATOM   3648  C  C   . HIS A 1 445  ? 127.180 143.111 128.426 1.00 111.25 ? 445  HIS A C   1 
ATOM   3649  O  O   . HIS A 1 445  ? 127.491 143.289 127.241 1.00 116.88 ? 445  HIS A O   1 
ATOM   3650  C  CB  . HIS A 1 445  ? 127.919 140.882 129.248 1.00 107.44 ? 445  HIS A CB  1 
ATOM   3651  C  CG  . HIS A 1 445  ? 129.084 140.051 129.690 1.00 108.02 ? 445  HIS A CG  1 
ATOM   3652  N  ND1 . HIS A 1 445  ? 129.607 140.101 130.963 1.00 116.04 ? 445  HIS A ND1 1 
ATOM   3653  C  CD2 . HIS A 1 445  ? 129.850 139.167 129.005 1.00 107.74 ? 445  HIS A CD2 1 
ATOM   3654  C  CE1 . HIS A 1 445  ? 130.627 139.267 131.053 1.00 113.17 ? 445  HIS A CE1 1 
ATOM   3655  N  NE2 . HIS A 1 445  ? 130.798 138.691 129.877 1.00 107.03 ? 445  HIS A NE2 1 
ATOM   3656  N  N   . ILE A 1 446  ? 126.020 143.537 128.927 1.00 110.16 ? 446  ILE A N   1 
ATOM   3657  C  CA  . ILE A 1 446  ? 125.070 144.230 128.063 1.00 110.06 ? 446  ILE A CA  1 
ATOM   3658  C  C   . ILE A 1 446  ? 125.566 145.631 127.731 1.00 116.44 ? 446  ILE A C   1 
ATOM   3659  O  O   . ILE A 1 446  ? 125.503 146.067 126.576 1.00 119.21 ? 446  ILE A O   1 
ATOM   3660  C  CB  . ILE A 1 446  ? 123.667 144.256 128.696 1.00 100.51 ? 446  ILE A CB  1 
ATOM   3661  C  CG1 . ILE A 1 446  ? 123.067 142.849 128.708 1.00 95.59  ? 446  ILE A CG1 1 
ATOM   3662  C  CG2 . ILE A 1 446  ? 122.754 145.197 127.925 1.00 93.77  ? 446  ILE A CG2 1 
ATOM   3663  C  CD1 . ILE A 1 446  ? 121.817 142.726 129.548 1.00 91.71  ? 446  ILE A CD1 1 
ATOM   3664  N  N   . VAL A 1 447  ? 126.076 146.352 128.733 1.00 115.09 ? 447  VAL A N   1 
ATOM   3665  C  CA  . VAL A 1 447  ? 126.511 147.729 128.515 1.00 119.53 ? 447  VAL A CA  1 
ATOM   3666  C  C   . VAL A 1 447  ? 127.654 147.774 127.511 1.00 119.45 ? 447  VAL A C   1 
ATOM   3667  O  O   . VAL A 1 447  ? 127.745 148.703 126.699 1.00 122.44 ? 447  VAL A O   1 
ATOM   3668  C  CB  . VAL A 1 447  ? 126.896 148.385 129.857 1.00 116.99 ? 447  VAL A CB  1 
ATOM   3669  C  CG1 . VAL A 1 447  ? 127.516 149.758 129.632 1.00 123.16 ? 447  VAL A CG1 1 
ATOM   3670  C  CG2 . VAL A 1 447  ? 125.677 148.493 130.764 1.00 111.56 ? 447  VAL A CG2 1 
ATOM   3671  N  N   . SER A 1 448  ? 128.519 146.765 127.522 1.00 119.08 ? 448  SER A N   1 
ATOM   3672  C  CA  . SER A 1 448  ? 129.647 146.705 126.606 1.00 115.90 ? 448  SER A CA  1 
ATOM   3673  C  C   . SER A 1 448  ? 129.330 145.936 125.332 1.00 112.93 ? 448  SER A C   1 
ATOM   3674  O  O   . SER A 1 448  ? 130.219 145.773 124.489 1.00 117.77 ? 448  SER A O   1 
ATOM   3675  C  CB  . SER A 1 448  ? 130.861 146.080 127.303 1.00 107.17 ? 448  SER A CB  1 
ATOM   3676  O  OG  . SER A 1 448  ? 131.086 146.682 128.566 1.00 106.22 ? 448  SER A OG  1 
ATOM   3677  N  N   . ASN A 1 449  ? 128.091 145.468 125.169 1.00 109.83 ? 449  ASN A N   1 
ATOM   3678  C  CA  . ASN A 1 449  ? 127.660 144.755 123.966 1.00 113.11 ? 449  ASN A CA  1 
ATOM   3679  C  C   . ASN A 1 449  ? 128.563 143.560 123.675 1.00 122.49 ? 449  ASN A C   1 
ATOM   3680  O  O   . ASN A 1 449  ? 128.985 143.322 122.541 1.00 114.39 ? 449  ASN A O   1 
ATOM   3681  C  CB  . ASN A 1 449  ? 127.592 145.696 122.762 1.00 116.61 ? 449  ASN A CB  1 
ATOM   3682  C  CG  . ASN A 1 449  ? 126.674 145.176 121.673 1.00 122.23 ? 449  ASN A CG  1 
ATOM   3683  O  OD1 . ASN A 1 449  ? 127.120 144.536 120.722 1.00 114.98 ? 449  ASN A OD1 1 
ATOM   3684  N  ND2 . ASN A 1 449  ? 125.381 145.447 121.811 1.00 122.09 ? 449  ASN A ND2 1 
ATOM   3685  N  N   . SER A 1 450  ? 128.857 142.793 124.717 1.00 126.55 ? 450  SER A N   1 
ATOM   3686  C  CA  . SER A 1 450  ? 129.631 141.571 124.578 1.00 121.10 ? 450  SER A CA  1 
ATOM   3687  C  C   . SER A 1 450  ? 128.851 140.420 125.192 1.00 106.24 ? 450  SER A C   1 
ATOM   3688  O  O   . SER A 1 450  ? 128.006 140.612 126.070 1.00 103.34 ? 450  SER A O   1 
ATOM   3689  C  CB  . SER A 1 450  ? 131.008 141.694 125.244 1.00 128.42 ? 450  SER A CB  1 
ATOM   3690  O  OG  . SER A 1 450  ? 130.886 142.105 126.596 1.00 117.93 ? 450  SER A OG  1 
ATOM   3691  N  N   . PHE A 1 451  ? 129.148 139.212 124.722 1.00 98.81  ? 451  PHE A N   1 
ATOM   3692  C  CA  . PHE A 1 451  ? 128.397 138.059 125.179 1.00 92.40  ? 451  PHE A CA  1 
ATOM   3693  C  C   . PHE A 1 451  ? 129.271 137.170 126.043 1.00 96.93  ? 451  PHE A C   1 
ATOM   3694  O  O   . PHE A 1 451  ? 130.417 136.898 125.674 1.00 106.48 ? 451  PHE A O   1 
ATOM   3695  C  CB  . PHE A 1 451  ? 127.867 137.238 124.017 1.00 103.04 ? 451  PHE A CB  1 
ATOM   3696  C  CG  . PHE A 1 451  ? 126.656 136.436 124.353 1.00 114.28 ? 451  PHE A CG  1 
ATOM   3697  C  CD1 . PHE A 1 451  ? 126.671 135.057 124.326 1.00 113.85 ? 451  PHE A CD1 1 
ATOM   3698  C  CD2 . PHE A 1 451  ? 125.459 137.087 124.620 1.00 111.32 ? 451  PHE A CD2 1 
ATOM   3699  C  CE1 . PHE A 1 451  ? 125.536 134.338 124.634 1.00 94.77  ? 451  PHE A CE1 1 
ATOM   3700  C  CE2 . PHE A 1 451  ? 124.320 136.375 124.908 1.00 100.90 ? 451  PHE A CE2 1 
ATOM   3701  C  CZ  . PHE A 1 451  ? 124.359 135.000 124.919 1.00 92.08  ? 451  PHE A CZ  1 
ATOM   3702  N  N   . PRO A 1 452  ? 128.767 136.702 127.181 1.00 93.63  ? 452  PRO A N   1 
ATOM   3703  C  CA  . PRO A 1 452  ? 129.595 135.878 128.070 1.00 100.02 ? 452  PRO A CA  1 
ATOM   3704  C  C   . PRO A 1 452  ? 129.961 134.547 127.424 1.00 103.00 ? 452  PRO A C   1 
ATOM   3705  O  O   . PRO A 1 452  ? 129.238 134.016 126.573 1.00 96.96  ? 452  PRO A O   1 
ATOM   3706  C  CB  . PRO A 1 452  ? 128.706 135.666 129.295 1.00 108.90 ? 452  PRO A CB  1 
ATOM   3707  C  CG  . PRO A 1 452  ? 127.311 135.879 128.804 1.00 110.35 ? 452  PRO A CG  1 
ATOM   3708  C  CD  . PRO A 1 452  ? 127.402 136.894 127.704 1.00 102.55 ? 452  PRO A CD  1 
ATOM   3709  N  N   . SER A 1 453  ? 131.110 134.021 127.833 1.00 109.98 ? 453  SER A N   1 
ATOM   3710  C  CA  . SER A 1 453  ? 131.631 132.784 127.282 1.00 101.55 ? 453  SER A CA  1 
ATOM   3711  C  C   . SER A 1 453  ? 130.895 131.575 127.864 1.00 108.87 ? 453  SER A C   1 
ATOM   3712  O  O   . SER A 1 453  ? 130.206 131.659 128.883 1.00 118.60 ? 453  SER A O   1 
ATOM   3713  C  CB  . SER A 1 453  ? 133.127 132.661 127.576 1.00 115.66 ? 453  SER A CB  1 
ATOM   3714  O  OG  . SER A 1 453  ? 133.405 133.020 128.921 1.00 109.47 ? 453  SER A OG  1 
ATOM   3715  N  N   . GLN A 1 454  ? 131.045 130.443 127.168 1.00 102.59 ? 454  GLN A N   1 
ATOM   3716  C  CA  . GLN A 1 454  ? 130.391 129.180 127.511 1.00 96.79  ? 454  GLN A CA  1 
ATOM   3717  C  C   . GLN A 1 454  ? 130.851 128.642 128.866 1.00 94.73  ? 454  GLN A C   1 
ATOM   3718  O  O   . GLN A 1 454  ? 130.055 128.050 129.601 1.00 99.17  ? 454  GLN A O   1 
ATOM   3719  C  CB  . GLN A 1 454  ? 130.597 128.232 126.316 1.00 97.41  ? 454  GLN A CB  1 
ATOM   3720  C  CG  . GLN A 1 454  ? 130.050 126.802 126.287 1.00 102.63 ? 454  GLN A CG  1 
ATOM   3721  C  CD  . GLN A 1 454  ? 128.565 126.754 126.285 1.00 94.22  ? 454  GLN A CD  1 
ATOM   3722  O  OE1 . GLN A 1 454  ? 127.973 126.027 127.094 1.00 90.03  ? 454  GLN A OE1 1 
ATOM   3723  N  NE2 . GLN A 1 454  ? 127.971 127.794 125.691 1.00 95.83  ? 454  GLN A NE2 1 
ATOM   3724  N  N   . ALA A 1 455  ? 132.112 128.873 129.226 1.00 97.65  ? 455  ALA A N   1 
ATOM   3725  C  CA  . ALA A 1 455  ? 132.640 128.384 130.496 1.00 95.86  ? 455  ALA A CA  1 
ATOM   3726  C  C   . ALA A 1 455  ? 131.940 129.010 131.710 1.00 103.93 ? 455  ALA A C   1 
ATOM   3727  O  O   . ALA A 1 455  ? 131.657 128.317 132.696 1.00 105.16 ? 455  ALA A O   1 
ATOM   3728  C  CB  . ALA A 1 455  ? 134.146 128.651 130.555 1.00 105.89 ? 455  ALA A CB  1 
ATOM   3729  N  N   . GLU A 1 456  ? 131.632 130.306 131.662 1.00 103.67 ? 456  GLU A N   1 
ATOM   3730  C  CA  . GLU A 1 456  ? 131.044 130.987 132.816 1.00 108.04 ? 456  GLU A CA  1 
ATOM   3731  C  C   . GLU A 1 456  ? 129.518 130.991 132.882 1.00 95.65  ? 456  GLU A C   1 
ATOM   3732  O  O   . GLU A 1 456  ? 128.972 131.538 133.846 1.00 101.73 ? 456  GLU A O   1 
ATOM   3733  C  CB  . GLU A 1 456  ? 131.520 132.445 132.843 1.00 114.52 ? 456  GLU A CB  1 
ATOM   3734  C  CG  . GLU A 1 456  ? 132.976 132.642 133.226 1.00 144.84 ? 456  GLU A CG  1 
ATOM   3735  C  CD  . GLU A 1 456  ? 133.263 132.295 134.674 1.00 146.94 ? 456  GLU A CD  1 
ATOM   3736  O  OE1 . GLU A 1 456  ? 132.314 131.976 135.420 1.00 129.01 ? 456  GLU A OE1 1 
ATOM   3737  O  OE2 . GLU A 1 456  ? 134.446 132.352 135.068 1.00 138.50 ? 456  GLU A OE2 1 
ATOM   3738  N  N   . ILE A 1 457  ? 128.808 130.410 131.914 1.00 90.51  ? 457  ILE A N   1 
ATOM   3739  C  CA  . ILE A 1 457  ? 127.346 130.442 131.966 1.00 77.82  ? 457  ILE A CA  1 
ATOM   3740  C  C   . ILE A 1 457  ? 126.795 129.681 133.170 1.00 82.88  ? 457  ILE A C   1 
ATOM   3741  O  O   . ILE A 1 457  ? 125.861 130.145 133.835 1.00 93.20  ? 457  ILE A O   1 
ATOM   3742  C  CB  . ILE A 1 457  ? 126.754 129.907 130.647 1.00 79.41  ? 457  ILE A CB  1 
ATOM   3743  C  CG1 . ILE A 1 457  ? 126.960 130.935 129.540 1.00 100.89 ? 457  ILE A CG1 1 
ATOM   3744  C  CG2 . ILE A 1 457  ? 125.272 129.590 130.802 1.00 81.05  ? 457  ILE A CG2 1 
ATOM   3745  C  CD1 . ILE A 1 457  ? 126.264 132.253 129.808 1.00 98.73  ? 457  ILE A CD1 1 
ATOM   3746  N  N   . TYR A 1 458  ? 127.371 128.521 133.490 1.00 85.72  ? 458  TYR A N   1 
ATOM   3747  C  CA  . TYR A 1 458  ? 126.837 127.716 134.589 1.00 74.49  ? 458  TYR A CA  1 
ATOM   3748  C  C   . TYR A 1 458  ? 126.924 128.402 135.951 1.00 81.12  ? 458  TYR A C   1 
ATOM   3749  O  O   . TYR A 1 458  ? 126.010 128.276 136.770 1.00 84.00  ? 458  TYR A O   1 
ATOM   3750  C  CB  . TYR A 1 458  ? 127.518 126.355 134.645 1.00 80.28  ? 458  TYR A CB  1 
ATOM   3751  C  CG  . TYR A 1 458  ? 126.740 125.427 135.539 1.00 81.74  ? 458  TYR A CG  1 
ATOM   3752  C  CD1 . TYR A 1 458  ? 125.427 125.097 135.239 1.00 82.20  ? 458  TYR A CD1 1 
ATOM   3753  C  CD2 . TYR A 1 458  ? 127.296 124.915 136.700 1.00 85.60  ? 458  TYR A CD2 1 
ATOM   3754  C  CE1 . TYR A 1 458  ? 124.694 124.271 136.063 1.00 76.71  ? 458  TYR A CE1 1 
ATOM   3755  C  CE2 . TYR A 1 458  ? 126.571 124.082 137.530 1.00 85.17  ? 458  TYR A CE2 1 
ATOM   3756  C  CZ  . TYR A 1 458  ? 125.270 123.763 137.205 1.00 80.83  ? 458  TYR A CZ  1 
ATOM   3757  O  OH  . TYR A 1 458  ? 124.544 122.936 138.030 1.00 86.83  ? 458  TYR A OH  1 
ATOM   3758  N  N   . GLN A 1 459  ? 128.015 129.119 136.221 1.00 83.93  ? 459  GLN A N   1 
ATOM   3759  C  CA  . GLN A 1 459  ? 128.171 129.758 137.524 1.00 86.06  ? 459  GLN A CA  1 
ATOM   3760  C  C   . GLN A 1 459  ? 127.086 130.799 137.797 1.00 98.16  ? 459  GLN A C   1 
ATOM   3761  O  O   . GLN A 1 459  ? 126.607 130.927 138.928 1.00 101.68 ? 459  GLN A O   1 
ATOM   3762  C  CB  . GLN A 1 459  ? 129.555 130.395 137.622 1.00 104.09 ? 459  GLN A CB  1 
ATOM   3763  C  CG  . GLN A 1 459  ? 129.920 130.880 139.007 1.00 122.31 ? 459  GLN A CG  1 
ATOM   3764  C  CD  . GLN A 1 459  ? 131.327 131.427 139.078 1.00 128.52 ? 459  GLN A CD  1 
ATOM   3765  O  OE1 . GLN A 1 459  ? 132.029 131.491 138.070 1.00 118.31 ? 459  GLN A OE1 1 
ATOM   3766  N  NE2 . GLN A 1 459  ? 131.709 131.921 140.249 1.00 132.60 ? 459  GLN A NE2 1 
ATOM   3767  N  N   . HIS A 1 460  ? 126.687 131.572 136.776 1.00 97.88  ? 460  HIS A N   1 
ATOM   3768  C  CA  . HIS A 1 460  ? 125.692 132.631 136.920 1.00 83.42  ? 460  HIS A CA  1 
ATOM   3769  C  C   . HIS A 1 460  ? 124.369 132.306 136.225 1.00 86.06  ? 460  HIS A C   1 
ATOM   3770  O  O   . HIS A 1 460  ? 123.676 133.203 135.734 1.00 89.85  ? 460  HIS A O   1 
ATOM   3771  C  CB  . HIS A 1 460  ? 126.283 133.942 136.411 1.00 87.03  ? 460  HIS A CB  1 
ATOM   3772  C  CG  . HIS A 1 460  ? 127.597 134.279 137.046 1.00 101.01 ? 460  HIS A CG  1 
ATOM   3773  N  ND1 . HIS A 1 460  ? 127.707 134.721 138.348 1.00 102.82 ? 460  HIS A ND1 1 
ATOM   3774  C  CD2 . HIS A 1 460  ? 128.863 134.186 136.573 1.00 104.91 ? 460  HIS A CD2 1 
ATOM   3775  C  CE1 . HIS A 1 460  ? 128.982 134.908 138.640 1.00 111.75 ? 460  HIS A CE1 1 
ATOM   3776  N  NE2 . HIS A 1 460  ? 129.704 134.590 137.581 1.00 110.78 ? 460  HIS A NE2 1 
ATOM   3777  N  N   . LEU A 1 461  ? 124.007 131.023 136.178 1.00 86.16  ? 461  LEU A N   1 
ATOM   3778  C  CA  . LEU A 1 461  ? 122.799 130.588 135.480 1.00 73.14  ? 461  LEU A CA  1 
ATOM   3779  C  C   . LEU A 1 461  ? 121.509 131.212 136.016 1.00 73.24  ? 461  LEU A C   1 
ATOM   3780  O  O   . LEU A 1 461  ? 120.594 131.502 135.237 1.00 81.36  ? 461  LEU A O   1 
ATOM   3781  C  CB  . LEU A 1 461  ? 122.698 129.062 135.538 1.00 71.48  ? 461  LEU A CB  1 
ATOM   3782  C  CG  . LEU A 1 461  ? 121.561 128.450 134.722 1.00 55.56  ? 461  LEU A CG  1 
ATOM   3783  C  CD1 . LEU A 1 461  ? 121.674 128.858 133.264 1.00 60.32  ? 461  LEU A CD1 1 
ATOM   3784  C  CD2 . LEU A 1 461  ? 121.565 126.936 134.867 1.00 63.45  ? 461  LEU A CD2 1 
ATOM   3785  N  N   . TRP A 1 462  ? 121.403 131.427 137.331 1.00 82.31  ? 462  TRP A N   1 
ATOM   3786  C  CA  . TRP A 1 462  ? 120.153 131.961 137.881 1.00 81.56  ? 462  TRP A CA  1 
ATOM   3787  C  C   . TRP A 1 462  ? 119.788 133.339 137.322 1.00 89.36  ? 462  TRP A C   1 
ATOM   3788  O  O   . TRP A 1 462  ? 118.603 133.631 137.121 1.00 93.33  ? 462  TRP A O   1 
ATOM   3789  C  CB  . TRP A 1 462  ? 120.229 132.022 139.408 1.00 72.41  ? 462  TRP A CB  1 
ATOM   3790  C  CG  . TRP A 1 462  ? 121.306 132.923 139.929 1.00 100.10 ? 462  TRP A CG  1 
ATOM   3791  C  CD1 . TRP A 1 462  ? 122.591 132.582 140.230 1.00 107.43 ? 462  TRP A CD1 1 
ATOM   3792  C  CD2 . TRP A 1 462  ? 121.185 134.324 140.213 1.00 105.41 ? 462  TRP A CD2 1 
ATOM   3793  N  NE1 . TRP A 1 462  ? 123.280 133.684 140.681 1.00 105.60 ? 462  TRP A NE1 1 
ATOM   3794  C  CE2 . TRP A 1 462  ? 122.439 134.765 140.680 1.00 105.16 ? 462  TRP A CE2 1 
ATOM   3795  C  CE3 . TRP A 1 462  ? 120.139 135.247 140.116 1.00 102.70 ? 462  TRP A CE3 1 
ATOM   3796  C  CZ2 . TRP A 1 462  ? 122.674 136.089 141.051 1.00 98.19  ? 462  TRP A CZ2 1 
ATOM   3797  C  CZ3 . TRP A 1 462  ? 120.376 136.561 140.481 1.00 106.31 ? 462  TRP A CZ3 1 
ATOM   3798  C  CH2 . TRP A 1 462  ? 121.632 136.969 140.943 1.00 99.77  ? 462  TRP A CH2 1 
ATOM   3799  N  N   . GLU A 1 463  ? 120.778 134.206 137.084 1.00 91.00  ? 463  GLU A N   1 
ATOM   3800  C  CA  . GLU A 1 463  ? 120.502 135.566 136.609 1.00 72.82  ? 463  GLU A CA  1 
ATOM   3801  C  C   . GLU A 1 463  ? 119.622 135.655 135.362 1.00 75.59  ? 463  GLU A C   1 
ATOM   3802  O  O   . GLU A 1 463  ? 119.039 136.716 135.113 1.00 92.76  ? 463  GLU A O   1 
ATOM   3803  C  CB  . GLU A 1 463  ? 121.811 136.323 136.379 1.00 79.82  ? 463  GLU A CB  1 
ATOM   3804  C  CG  . GLU A 1 463  ? 122.661 136.400 137.631 1.00 100.92 ? 463  GLU A CG  1 
ATOM   3805  C  CD  . GLU A 1 463  ? 123.683 137.511 137.582 1.00 115.93 ? 463  GLU A CD  1 
ATOM   3806  O  OE1 . GLU A 1 463  ? 123.671 138.288 136.605 1.00 115.91 ? 463  GLU A OE1 1 
ATOM   3807  O  OE2 . GLU A 1 463  ? 124.490 137.617 138.530 1.00 114.38 ? 463  GLU A OE2 1 
ATOM   3808  N  N   . TRP A 1 464  ? 119.496 134.584 134.574 1.00 71.13  ? 464  TRP A N   1 
ATOM   3809  C  CA  . TRP A 1 464  ? 118.643 134.638 133.385 1.00 61.50  ? 464  TRP A CA  1 
ATOM   3810  C  C   . TRP A 1 464  ? 117.154 134.615 133.680 1.00 66.16  ? 464  TRP A C   1 
ATOM   3811  O  O   . TRP A 1 464  ? 116.360 134.817 132.757 1.00 73.22  ? 464  TRP A O   1 
ATOM   3812  C  CB  . TRP A 1 464  ? 118.955 133.508 132.408 1.00 64.71  ? 464  TRP A CB  1 
ATOM   3813  C  CG  . TRP A 1 464  ? 120.279 133.634 131.786 1.00 81.11  ? 464  TRP A CG  1 
ATOM   3814  C  CD1 . TRP A 1 464  ? 121.437 133.027 132.159 1.00 87.32  ? 464  TRP A CD1 1 
ATOM   3815  C  CD2 . TRP A 1 464  ? 120.598 134.476 130.676 1.00 90.40  ? 464  TRP A CD2 1 
ATOM   3816  N  NE1 . TRP A 1 464  ? 122.460 133.421 131.328 1.00 94.74  ? 464  TRP A NE1 1 
ATOM   3817  C  CE2 . TRP A 1 464  ? 121.969 134.314 130.411 1.00 92.08  ? 464  TRP A CE2 1 
ATOM   3818  C  CE3 . TRP A 1 464  ? 119.853 135.347 129.875 1.00 91.82  ? 464  TRP A CE3 1 
ATOM   3819  C  CZ2 . TRP A 1 464  ? 122.612 134.991 129.377 1.00 95.07  ? 464  TRP A CZ2 1 
ATOM   3820  C  CZ3 . TRP A 1 464  ? 120.490 136.016 128.851 1.00 78.81  ? 464  TRP A CZ3 1 
ATOM   3821  C  CH2 . TRP A 1 464  ? 121.856 135.836 128.610 1.00 88.21  ? 464  TRP A CH2 1 
ATOM   3822  N  N   . TYR A 1 465  ? 116.748 134.388 134.924 1.00 76.11  ? 465  TYR A N   1 
ATOM   3823  C  CA  . TYR A 1 465  ? 115.324 134.382 135.224 1.00 71.26  ? 465  TYR A CA  1 
ATOM   3824  C  C   . TYR A 1 465  ? 114.699 135.769 135.101 1.00 72.64  ? 465  TYR A C   1 
ATOM   3825  O  O   . TYR A 1 465  ? 113.531 135.883 134.711 1.00 92.10  ? 465  TYR A O   1 
ATOM   3826  C  CB  . TYR A 1 465  ? 115.095 133.812 136.623 1.00 85.08  ? 465  TYR A CB  1 
ATOM   3827  C  CG  . TYR A 1 465  ? 113.649 133.814 137.041 1.00 86.37  ? 465  TYR A CG  1 
ATOM   3828  C  CD1 . TYR A 1 465  ? 112.769 132.864 136.544 1.00 90.98  ? 465  TYR A CD1 1 
ATOM   3829  C  CD2 . TYR A 1 465  ? 113.159 134.762 137.926 1.00 91.31  ? 465  TYR A CD2 1 
ATOM   3830  C  CE1 . TYR A 1 465  ? 111.441 132.856 136.917 1.00 87.68  ? 465  TYR A CE1 1 
ATOM   3831  C  CE2 . TYR A 1 465  ? 111.829 134.763 138.306 1.00 92.25  ? 465  TYR A CE2 1 
ATOM   3832  C  CZ  . TYR A 1 465  ? 110.975 133.807 137.797 1.00 88.71  ? 465  TYR A CZ  1 
ATOM   3833  O  OH  . TYR A 1 465  ? 109.651 133.800 138.168 1.00 94.09  ? 465  TYR A OH  1 
ATOM   3834  N  N   . PHE A 1 466  ? 115.445 136.826 135.413 1.00 74.20  ? 466  PHE A N   1 
ATOM   3835  C  CA  . PHE A 1 466  ? 114.894 138.176 135.445 1.00 73.60  ? 466  PHE A CA  1 
ATOM   3836  C  C   . PHE A 1 466  ? 114.880 138.890 134.097 1.00 87.86  ? 466  PHE A C   1 
ATOM   3837  O  O   . PHE A 1 466  ? 114.246 139.945 133.989 1.00 101.58 ? 466  PHE A O   1 
ATOM   3838  C  CB  . PHE A 1 466  ? 115.667 139.031 136.450 1.00 85.15  ? 466  PHE A CB  1 
ATOM   3839  C  CG  . PHE A 1 466  ? 115.452 138.614 137.869 1.00 99.92  ? 466  PHE A CG  1 
ATOM   3840  C  CD1 . PHE A 1 466  ? 114.190 138.650 138.432 1.00 112.44 ? 466  PHE A CD1 1 
ATOM   3841  C  CD2 . PHE A 1 466  ? 116.516 138.184 138.643 1.00 105.97 ? 466  PHE A CD2 1 
ATOM   3842  C  CE1 . PHE A 1 466  ? 113.987 138.256 139.737 1.00 108.39 ? 466  PHE A CE1 1 
ATOM   3843  C  CE2 . PHE A 1 466  ? 116.323 137.793 139.952 1.00 109.89 ? 466  PHE A CE2 1 
ATOM   3844  C  CZ  . PHE A 1 466  ? 115.055 137.829 140.500 1.00 108.92 ? 466  PHE A CZ  1 
ATOM   3845  N  N   . VAL A 1 467  ? 115.548 138.360 133.074 1.00 87.16  ? 467  VAL A N   1 
ATOM   3846  C  CA  . VAL A 1 467  ? 115.702 139.093 131.820 1.00 87.53  ? 467  VAL A CA  1 
ATOM   3847  C  C   . VAL A 1 467  ? 114.353 139.195 131.117 1.00 98.44  ? 467  VAL A C   1 
ATOM   3848  O  O   . VAL A 1 467  ? 113.692 138.183 130.856 1.00 98.16  ? 467  VAL A O   1 
ATOM   3849  C  CB  . VAL A 1 467  ? 116.749 138.430 130.917 1.00 75.93  ? 467  VAL A CB  1 
ATOM   3850  C  CG1 . VAL A 1 467  ? 116.684 139.012 129.510 1.00 81.09  ? 467  VAL A CG1 1 
ATOM   3851  C  CG2 . VAL A 1 467  ? 118.145 138.607 131.505 1.00 84.74  ? 467  VAL A CG2 1 
ATOM   3852  N  N   . GLU A 1 468  ? 113.944 140.425 130.804 1.00 99.81  ? 468  GLU A N   1 
ATOM   3853  C  CA  . GLU A 1 468  ? 112.776 140.694 129.980 1.00 99.46  ? 468  GLU A CA  1 
ATOM   3854  C  C   . GLU A 1 468  ? 113.174 141.612 128.836 1.00 94.01  ? 468  GLU A C   1 
ATOM   3855  O  O   . GLU A 1 468  ? 114.144 142.366 128.927 1.00 99.20  ? 468  GLU A O   1 
ATOM   3856  C  CB  . GLU A 1 468  ? 111.650 141.355 130.779 1.00 108.46 ? 468  GLU A CB  1 
ATOM   3857  C  CG  . GLU A 1 468  ? 111.440 140.793 132.163 1.00 110.86 ? 468  GLU A CG  1 
ATOM   3858  C  CD  . GLU A 1 468  ? 110.444 141.610 132.951 1.00 117.14 ? 468  GLU A CD  1 
ATOM   3859  O  OE1 . GLU A 1 468  ? 110.003 141.146 134.022 1.00 124.16 ? 468  GLU A OE1 1 
ATOM   3860  O  OE2 . GLU A 1 468  ? 110.098 142.720 132.492 1.00 107.58 ? 468  GLU A OE2 1 
ATOM   3861  N  N   . HIS A 1 469  ? 112.406 141.548 127.752 1.00 90.33  ? 469  HIS A N   1 
ATOM   3862  C  CA  . HIS A 1 469  ? 112.751 142.297 126.554 1.00 88.61  ? 469  HIS A CA  1 
ATOM   3863  C  C   . HIS A 1 469  ? 111.510 142.552 125.709 1.00 99.97  ? 469  HIS A C   1 
ATOM   3864  O  O   . HIS A 1 469  ? 110.387 142.207 126.084 1.00 103.92 ? 469  HIS A O   1 
ATOM   3865  C  CB  . HIS A 1 469  ? 113.778 141.522 125.740 1.00 77.46  ? 469  HIS A CB  1 
ATOM   3866  C  CG  . HIS A 1 469  ? 113.343 140.125 125.430 1.00 85.47  ? 469  HIS A CG  1 
ATOM   3867  N  ND1 . HIS A 1 469  ? 112.763 139.769 124.231 1.00 85.35  ? 469  HIS A ND1 1 
ATOM   3868  C  CD2 . HIS A 1 469  ? 113.383 138.996 126.178 1.00 92.58  ? 469  HIS A CD2 1 
ATOM   3869  C  CE1 . HIS A 1 469  ? 112.473 138.480 124.253 1.00 73.30  ? 469  HIS A CE1 1 
ATOM   3870  N  NE2 . HIS A 1 469  ? 112.843 137.988 125.420 1.00 89.68  ? 469  HIS A NE2 1 
ATOM   3871  N  N   . GLU A 1 470  ? 111.745 143.157 124.547 1.00 103.41 ? 470  GLU A N   1 
ATOM   3872  C  CA  . GLU A 1 470  ? 110.736 143.462 123.549 1.00 100.72 ? 470  GLU A CA  1 
ATOM   3873  C  C   . GLU A 1 470  ? 110.342 142.215 122.764 1.00 90.80  ? 470  GLU A C   1 
ATOM   3874  O  O   . GLU A 1 470  ? 111.117 141.263 122.658 1.00 91.49  ? 470  GLU A O   1 
ATOM   3875  C  CB  . GLU A 1 470  ? 111.248 144.540 122.600 1.00 116.57 ? 470  GLU A CB  1 
ATOM   3876  C  CG  . GLU A 1 470  ? 111.486 145.876 123.268 1.00 136.69 ? 470  GLU A CG  1 
ATOM   3877  C  CD  . GLU A 1 470  ? 110.198 146.504 123.764 1.00 142.49 ? 470  GLU A CD  1 
ATOM   3878  O  OE1 . GLU A 1 470  ? 109.143 146.280 123.132 1.00 140.25 ? 470  GLU A OE1 1 
ATOM   3879  O  OE2 . GLU A 1 470  ? 110.238 147.220 124.785 1.00 139.40 ? 470  GLU A OE2 1 
ATOM   3880  N  N   . PRO A 1 471  ? 109.130 142.197 122.211 1.00 89.60  ? 471  PRO A N   1 
ATOM   3881  C  CA  . PRO A 1 471  ? 108.696 141.041 121.422 1.00 80.26  ? 471  PRO A CA  1 
ATOM   3882  C  C   . PRO A 1 471  ? 109.547 140.840 120.176 1.00 78.31  ? 471  PRO A C   1 
ATOM   3883  O  O   . PRO A 1 471  ? 110.117 141.783 119.622 1.00 87.59  ? 471  PRO A O   1 
ATOM   3884  C  CB  . PRO A 1 471  ? 107.250 141.391 121.047 1.00 82.40  ? 471  PRO A CB  1 
ATOM   3885  C  CG  . PRO A 1 471  ? 106.809 142.345 122.100 1.00 99.80  ? 471  PRO A CG  1 
ATOM   3886  C  CD  . PRO A 1 471  ? 108.030 143.151 122.441 1.00 97.62  ? 471  PRO A CD  1 
ATOM   3887  N  N   . LEU A 1 472  ? 109.647 139.586 119.760 1.00 73.85  ? 472  LEU A N   1 
ATOM   3888  C  CA  . LEU A 1 472  ? 110.304 139.169 118.528 1.00 69.89  ? 472  LEU A CA  1 
ATOM   3889  C  C   . LEU A 1 472  ? 109.238 138.549 117.634 1.00 76.31  ? 472  LEU A C   1 
ATOM   3890  O  O   . LEU A 1 472  ? 108.065 138.483 118.010 1.00 89.94  ? 472  LEU A O   1 
ATOM   3891  C  CB  . LEU A 1 472  ? 111.431 138.167 118.806 1.00 69.41  ? 472  LEU A CB  1 
ATOM   3892  C  CG  . LEU A 1 472  ? 112.682 138.518 119.612 1.00 77.69  ? 472  LEU A CG  1 
ATOM   3893  C  CD1 . LEU A 1 472  ? 112.351 138.783 121.053 1.00 72.98  ? 472  LEU A CD1 1 
ATOM   3894  C  CD2 . LEU A 1 472  ? 113.670 137.361 119.521 1.00 82.69  ? 472  LEU A CD2 1 
ATOM   3895  N  N   . PHE A 1 473  ? 109.645 138.092 116.449 1.00 78.21  ? 473  PHE A N   1 
ATOM   3896  C  CA  . PHE A 1 473  ? 108.831 137.199 115.620 1.00 93.62  ? 473  PHE A CA  1 
ATOM   3897  C  C   . PHE A 1 473  ? 107.378 137.674 115.506 1.00 113.35 ? 473  PHE A C   1 
ATOM   3898  O  O   . PHE A 1 473  ? 106.466 137.087 116.090 1.00 116.46 ? 473  PHE A O   1 
ATOM   3899  C  CB  . PHE A 1 473  ? 108.865 135.759 116.140 1.00 87.59  ? 473  PHE A CB  1 
ATOM   3900  C  CG  . PHE A 1 473  ? 110.203 135.316 116.650 1.00 91.43  ? 473  PHE A CG  1 
ATOM   3901  C  CD1 . PHE A 1 473  ? 110.375 134.975 117.981 1.00 99.21  ? 473  PHE A CD1 1 
ATOM   3902  C  CD2 . PHE A 1 473  ? 111.274 135.185 115.785 1.00 100.97 ? 473  PHE A CD2 1 
ATOM   3903  C  CE1 . PHE A 1 473  ? 111.607 134.549 118.446 1.00 92.66  ? 473  PHE A CE1 1 
ATOM   3904  C  CE2 . PHE A 1 473  ? 112.505 134.757 116.242 1.00 110.63 ? 473  PHE A CE2 1 
ATOM   3905  C  CZ  . PHE A 1 473  ? 112.672 134.438 117.574 1.00 97.17  ? 473  PHE A CZ  1 
ATOM   3906  N  N   . SER A 1 474  ? 107.189 138.783 114.790 1.00 123.14 ? 474  SER A N   1 
ATOM   3907  C  CA  . SER A 1 474  ? 105.838 139.286 114.570 1.00 121.70 ? 474  SER A CA  1 
ATOM   3908  C  C   . SER A 1 474  ? 104.945 138.153 114.072 1.00 118.04 ? 474  SER A C   1 
ATOM   3909  O  O   . SER A 1 474  ? 105.403 137.220 113.407 1.00 111.78 ? 474  SER A O   1 
ATOM   3910  C  CB  . SER A 1 474  ? 105.845 140.443 113.568 1.00 135.42 ? 474  SER A CB  1 
ATOM   3911  O  OG  . SER A 1 474  ? 106.356 140.030 112.313 1.00 144.32 ? 474  SER A OG  1 
ATOM   3912  N  N   . THR A 1 475  ? 103.653 138.245 114.385 1.00 126.03 ? 475  THR A N   1 
ATOM   3913  C  CA  . THR A 1 475  ? 102.753 137.109 114.227 1.00 132.30 ? 475  THR A CA  1 
ATOM   3914  C  C   . THR A 1 475  ? 101.966 137.109 112.928 1.00 131.86 ? 475  THR A C   1 
ATOM   3915  O  O   . THR A 1 475  ? 101.595 136.036 112.445 1.00 119.66 ? 475  THR A O   1 
ATOM   3916  C  CB  . THR A 1 475  ? 101.750 137.079 115.382 1.00 123.32 ? 475  THR A CB  1 
ATOM   3917  O  OG1 . THR A 1 475  ? 100.745 138.076 115.158 1.00 110.93 ? 475  THR A OG1 1 
ATOM   3918  C  CG2 . THR A 1 475  ? 102.448 137.387 116.693 1.00 122.93 ? 475  THR A CG2 1 
ATOM   3919  N  N   . LYS A 1 476  ? 101.712 138.274 112.345 1.00 141.63 ? 476  LYS A N   1 
ATOM   3920  C  CA  . LYS A 1 476  ? 100.790 138.383 111.217 1.00 143.79 ? 476  LYS A CA  1 
ATOM   3921  C  C   . LYS A 1 476  ? 101.331 137.817 109.913 1.00 137.73 ? 476  LYS A C   1 
ATOM   3922  O  O   . LYS A 1 476  ? 100.625 137.882 108.900 1.00 139.79 ? 476  LYS A O   1 
ATOM   3923  C  CB  . LYS A 1 476  ? 100.363 139.840 111.037 1.00 149.17 ? 476  LYS A CB  1 
ATOM   3924  C  CG  . LYS A 1 476  ? 101.488 140.858 111.054 1.00 152.55 ? 476  LYS A CG  1 
ATOM   3925  C  CD  . LYS A 1 476  ? 100.937 142.236 111.382 1.00 152.63 ? 476  LYS A CD  1 
ATOM   3926  C  CE  . LYS A 1 476  ? 102.041 143.270 111.473 1.00 165.54 ? 476  LYS A CE  1 
ATOM   3927  N  NZ  . LYS A 1 476  ? 103.049 142.896 112.505 1.00 159.38 ? 476  LYS A NZ  1 
ATOM   3928  N  N   . ILE A 1 477  ? 102.549 137.262 109.876 1.00 131.60 ? 477  ILE A N   1 
ATOM   3929  C  CA  . ILE A 1 477  ? 103.082 136.626 108.675 1.00 138.33 ? 477  ILE A CA  1 
ATOM   3930  C  C   . ILE A 1 477  ? 103.576 135.239 109.033 1.00 135.54 ? 477  ILE A C   1 
ATOM   3931  O  O   . ILE A 1 477  ? 104.334 135.072 109.988 1.00 136.72 ? 477  ILE A O   1 
ATOM   3932  C  CB  . ILE A 1 477  ? 104.224 137.440 108.035 1.00 145.27 ? 477  ILE A CB  1 
ATOM   3933  C  CG1 . ILE A 1 477  ? 103.733 138.811 107.576 1.00 146.99 ? 477  ILE A CG1 1 
ATOM   3934  C  CG2 . ILE A 1 477  ? 104.834 136.664 106.876 1.00 137.54 ? 477  ILE A CG2 1 
ATOM   3935  C  CD1 . ILE A 1 477  ? 103.840 139.884 108.633 1.00 136.19 ? 477  ILE A CD1 1 
ATOM   3936  N  N   . ILE A 1 478  ? 103.141 134.255 108.262 1.00 123.25 ? 478  ILE A N   1 
ATOM   3937  C  CA  . ILE A 1 478  ? 103.808 132.957 108.257 1.00 119.38 ? 478  ILE A CA  1 
ATOM   3938  C  C   . ILE A 1 478  ? 104.298 132.663 106.853 1.00 124.73 ? 478  ILE A C   1 
ATOM   3939  O  O   . ILE A 1 478  ? 103.791 133.208 105.867 1.00 124.75 ? 478  ILE A O   1 
ATOM   3940  C  CB  . ILE A 1 478  ? 103.033 131.699 108.548 1.00 106.73 ? 478  ILE A CB  1 
ATOM   3941  C  CG1 . ILE A 1 478  ? 102.095 131.499 107.402 1.00 114.44 ? 478  ILE A CG1 1 
ATOM   3942  C  CG2 . ILE A 1 478  ? 102.124 131.943 109.768 1.00 96.54  ? 478  ILE A CG2 1 
ATOM   3943  C  CD1 . ILE A 1 478  ? 101.427 130.200 107.594 1.00 121.63 ? 478  ILE A CD1 1 
ATOM   3944  N  N   . SER A 1 479  ? 105.350 131.849 106.759 1.00 124.56 ? 479  SER A N   1 
ATOM   3945  C  CA  . SER A 1 479  ? 106.006 131.624 105.472 1.00 130.21 ? 479  SER A CA  1 
ATOM   3946  C  C   . SER A 1 479  ? 105.114 130.848 104.482 1.00 129.25 ? 479  SER A C   1 
ATOM   3947  O  O   . SER A 1 479  ? 104.911 131.289 103.347 1.00 128.61 ? 479  SER A O   1 
ATOM   3948  C  CB  . SER A 1 479  ? 107.310 130.862 105.687 1.00 137.40 ? 479  SER A CB  1 
ATOM   3949  O  OG  . SER A 1 479  ? 107.056 129.483 105.923 1.00 128.06 ? 479  SER A OG  1 
ATOM   3950  N  N   . ASP A 1 480  ? 104.553 129.694 104.886 1.00 130.88 ? 480  ASP A N   1 
ATOM   3951  C  CA  . ASP A 1 480  ? 103.932 128.792 103.907 1.00 133.07 ? 480  ASP A CA  1 
ATOM   3952  C  C   . ASP A 1 480  ? 102.499 129.202 103.570 1.00 132.46 ? 480  ASP A C   1 
ATOM   3953  O  O   . ASP A 1 480  ? 102.185 129.513 102.413 1.00 124.29 ? 480  ASP A O   1 
ATOM   3954  C  CB  . ASP A 1 480  ? 103.969 127.347 104.428 1.00 135.75 ? 480  ASP A CB  1 
ATOM   3955  C  CG  . ASP A 1 480  ? 103.842 126.309 103.314 1.00 134.56 ? 480  ASP A CG  1 
ATOM   3956  O  OD1 . ASP A 1 480  ? 103.298 126.644 102.240 1.00 134.64 ? 480  ASP A OD1 1 
ATOM   3957  O  OD2 . ASP A 1 480  ? 104.299 125.160 103.509 1.00 120.57 ? 480  ASP A OD2 1 
ATOM   3958  N  N   . LEU A 1 481  ? 101.613 129.177 104.569 1.00 128.51 ? 481  LEU A N   1 
ATOM   3959  C  CA  . LEU A 1 481  ? 100.180 129.471 104.484 1.00 126.63 ? 481  LEU A CA  1 
ATOM   3960  C  C   . LEU A 1 481  ? 99.405  128.467 103.629 1.00 118.49 ? 481  LEU A C   1 
ATOM   3961  O  O   . LEU A 1 481  ? 98.203  128.653 103.389 1.00 106.51 ? 481  LEU A O   1 
ATOM   3962  C  CB  . LEU A 1 481  ? 99.959  130.915 104.006 1.00 121.70 ? 481  LEU A CB  1 
ATOM   3963  C  CG  . LEU A 1 481  ? 98.582  131.569 104.017 1.00 124.16 ? 481  LEU A CG  1 
ATOM   3964  C  CD1 . LEU A 1 481  ? 97.869  131.242 105.325 1.00 106.83 ? 481  LEU A CD1 1 
ATOM   3965  C  CD2 . LEU A 1 481  ? 98.745  133.066 103.859 1.00 134.63 ? 481  LEU A CD2 1 
ATOM   3966  N  N   . SER A 1 482  ? 100.045 127.386 103.192 1.00 121.52 ? 482  SER A N   1 
ATOM   3967  C  CA  . SER A 1 482  ? 99.378  126.318 102.459 1.00 114.91 ? 482  SER A CA  1 
ATOM   3968  C  C   . SER A 1 482  ? 99.252  125.041 103.290 1.00 111.42 ? 482  SER A C   1 
ATOM   3969  O  O   . SER A 1 482  ? 98.997  123.965 102.740 1.00 104.35 ? 482  SER A O   1 
ATOM   3970  C  CB  . SER A 1 482  ? 100.135 126.044 101.160 1.00 120.98 ? 482  SER A CB  1 
ATOM   3971  O  OG  . SER A 1 482  ? 101.433 125.547 101.427 1.00 124.62 ? 482  SER A OG  1 
ATOM   3972  N  N   . ILE A 1 483  ? 99.426  125.150 104.610 1.00 114.19 ? 483  ILE A N   1 
ATOM   3973  C  CA  . ILE A 1 483  ? 99.292  124.018 105.527 1.00 113.98 ? 483  ILE A CA  1 
ATOM   3974  C  C   . ILE A 1 483  ? 97.850  123.756 105.962 1.00 109.58 ? 483  ILE A C   1 
ATOM   3975  O  O   . ILE A 1 483  ? 97.539  122.643 106.406 1.00 114.76 ? 483  ILE A O   1 
ATOM   3976  C  CB  . ILE A 1 483  ? 100.172 124.249 106.759 1.00 114.11 ? 483  ILE A CB  1 
ATOM   3977  C  CG1 . ILE A 1 483  ? 99.933  125.658 107.289 1.00 105.24 ? 483  ILE A CG1 1 
ATOM   3978  C  CG2 . ILE A 1 483  ? 101.642 124.072 106.395 1.00 135.93 ? 483  ILE A CG2 1 
ATOM   3979  C  CD1 . ILE A 1 483  ? 100.797 126.031 108.431 1.00 102.66 ? 483  ILE A CD1 1 
ATOM   3980  N  N   . PHE A 1 484  ? 96.964  124.745 105.821 1.00 99.31  ? 484  PHE A N   1 
ATOM   3981  C  CA  . PHE A 1 484  ? 95.549  124.633 106.163 1.00 93.09  ? 484  PHE A CA  1 
ATOM   3982  C  C   . PHE A 1 484  ? 94.791  123.851 105.105 1.00 98.03  ? 484  PHE A C   1 
ATOM   3983  O  O   . PHE A 1 484  ? 93.858  123.102 105.431 1.00 100.40 ? 484  PHE A O   1 
ATOM   3984  C  CB  . PHE A 1 484  ? 94.956  126.046 106.275 1.00 78.33  ? 484  PHE A CB  1 
ATOM   3985  C  CG  . PHE A 1 484  ? 95.602  126.913 107.326 1.00 91.42  ? 484  PHE A CG  1 
ATOM   3986  C  CD1 . PHE A 1 484  ? 94.985  127.083 108.551 1.00 102.76 ? 484  PHE A CD1 1 
ATOM   3987  C  CD2 . PHE A 1 484  ? 96.903  127.369 107.183 1.00 105.16 ? 484  PHE A CD2 1 
ATOM   3988  C  CE1 . PHE A 1 484  ? 95.563  127.847 109.548 1.00 103.58 ? 484  PHE A CE1 1 
ATOM   3989  C  CE2 . PHE A 1 484  ? 97.511  128.100 108.192 1.00 98.46  ? 484  PHE A CE2 1 
ATOM   3990  C  CZ  . PHE A 1 484  ? 96.838  128.338 109.375 1.00 86.53  ? 484  PHE A CZ  1 
ATOM   3991  N  N   . ILE A 1 485  ? 95.230  123.976 103.852 1.00 107.46 ? 485  ILE A N   1 
ATOM   3992  C  CA  . ILE A 1 485  ? 94.597  123.326 102.714 1.00 99.93  ? 485  ILE A CA  1 
ATOM   3993  C  C   . ILE A 1 485  ? 94.825  121.823 102.772 1.00 105.50 ? 485  ILE A C   1 
ATOM   3994  O  O   . ILE A 1 485  ? 93.997  121.046 102.289 1.00 104.89 ? 485  ILE A O   1 
ATOM   3995  C  CB  . ILE A 1 485  ? 95.061  123.962 101.401 1.00 111.96 ? 485  ILE A CB  1 
ATOM   3996  C  CG1 . ILE A 1 485  ? 95.012  125.482 101.549 1.00 99.95  ? 485  ILE A CG1 1 
ATOM   3997  C  CG2 . ILE A 1 485  ? 94.145  123.542 100.281 1.00 100.50 ? 485  ILE A CG2 1 
ATOM   3998  C  CD1 . ILE A 1 485  ? 95.863  126.215 100.555 1.00 108.96 ? 485  ILE A CD1 1 
ATOM   3999  N  N   . LYS A 1 486  ? 95.921  121.385 103.395 1.00 110.28 ? 486  LYS A N   1 
ATOM   4000  C  CA  . LYS A 1 486  ? 96.302  119.982 103.362 1.00 119.08 ? 486  LYS A CA  1 
ATOM   4001  C  C   . LYS A 1 486  ? 95.248  119.117 104.012 1.00 126.35 ? 486  LYS A C   1 
ATOM   4002  O  O   . LYS A 1 486  ? 94.491  119.561 104.875 1.00 126.24 ? 486  LYS A O   1 
ATOM   4003  C  CB  . LYS A 1 486  ? 97.552  119.759 104.224 1.00 121.87 ? 486  LYS A CB  1 
ATOM   4004  C  CG  . LYS A 1 486  ? 98.336  118.456 104.038 1.00 133.41 ? 486  LYS A CG  1 
ATOM   4005  C  CD  . LYS A 1 486  ? 99.583  118.287 103.283 1.00 141.03 ? 486  LYS A CD  1 
ATOM   4006  C  CE  . LYS A 1 486  ? 99.914  116.781 103.316 1.00 133.62 ? 486  LYS A CE  1 
ATOM   4007  N  NZ  . LYS A 1 486  ? 101.107 116.483 102.493 1.00 127.56 ? 486  LYS A NZ  1 
ATOM   4008  N  N   . ASP A 1 487  ? 95.233  117.847 103.611 1.00 134.60 ? 487  ASP A N   1 
ATOM   4009  C  CA  . ASP A 1 487  ? 94.231  116.932 104.128 1.00 135.58 ? 487  ASP A CA  1 
ATOM   4010  C  C   . ASP A 1 487  ? 94.516  116.588 105.579 1.00 145.43 ? 487  ASP A C   1 
ATOM   4011  O  O   . ASP A 1 487  ? 95.667  116.376 105.962 1.00 138.60 ? 487  ASP A O   1 
ATOM   4012  C  CB  . ASP A 1 487  ? 94.171  115.667 103.274 1.00 139.33 ? 487  ASP A CB  1 
ATOM   4013  C  CG  . ASP A 1 487  ? 93.069  114.723 103.711 1.00 146.03 ? 487  ASP A CG  1 
ATOM   4014  O  OD1 . ASP A 1 487  ? 93.215  114.093 104.779 1.00 147.17 ? 487  ASP A OD1 1 
ATOM   4015  O  OD2 . ASP A 1 487  ? 92.053  114.618 102.990 1.00 138.56 ? 487  ASP A OD2 1 
ATOM   4016  N  N   . ARG A 1 488  ? 93.453  116.504 106.375 1.00 144.86 ? 488  ARG A N   1 
ATOM   4017  C  CA  . ARG A 1 488  ? 93.544  116.121 107.779 1.00 135.13 ? 488  ARG A CA  1 
ATOM   4018  C  C   . ARG A 1 488  ? 92.189  115.573 108.203 1.00 130.67 ? 488  ARG A C   1 
ATOM   4019  O  O   . ARG A 1 488  ? 91.161  115.869 107.588 1.00 129.12 ? 488  ARG A O   1 
ATOM   4020  C  CB  . ARG A 1 488  ? 93.977  117.287 108.676 1.00 124.33 ? 488  ARG A CB  1 
ATOM   4021  C  CG  . ARG A 1 488  ? 95.480  117.449 108.826 1.00 132.13 ? 488  ARG A CG  1 
ATOM   4022  C  CD  . ARG A 1 488  ? 95.814  118.417 109.944 1.00 147.21 ? 488  ARG A CD  1 
ATOM   4023  N  NE  . ARG A 1 488  ? 94.929  119.579 109.930 1.00 149.32 ? 488  ARG A NE  1 
ATOM   4024  C  CZ  . ARG A 1 488  ? 95.155  120.681 109.222 1.00 142.12 ? 488  ARG A CZ  1 
ATOM   4025  N  NH1 . ARG A 1 488  ? 94.293  121.688 109.269 1.00 117.21 ? 488  ARG A NH1 1 
ATOM   4026  N  NH2 . ARG A 1 488  ? 96.240  120.776 108.466 1.00 133.17 ? 488  ARG A NH2 1 
ATOM   4027  N  N   . ALA A 1 489  ? 92.203  114.756 109.251 1.00 124.38 ? 489  ALA A N   1 
ATOM   4028  C  CA  . ALA A 1 489  ? 90.991  114.184 109.824 1.00 114.04 ? 489  ALA A CA  1 
ATOM   4029  C  C   . ALA A 1 489  ? 90.612  114.972 111.072 1.00 108.54 ? 489  ALA A C   1 
ATOM   4030  O  O   . ALA A 1 489  ? 91.474  115.264 111.908 1.00 101.48 ? 489  ALA A O   1 
ATOM   4031  C  CB  . ALA A 1 489  ? 91.186  112.705 110.158 1.00 116.35 ? 489  ALA A CB  1 
ATOM   4032  N  N   . THR A 1 490  ? 89.331  115.318 111.198 1.00 98.78  ? 490  THR A N   1 
ATOM   4033  C  CA  . THR A 1 490  ? 88.852  116.119 112.315 1.00 85.93  ? 490  THR A CA  1 
ATOM   4034  C  C   . THR A 1 490  ? 87.697  115.409 113.011 1.00 93.74  ? 490  THR A C   1 
ATOM   4035  O  O   . THR A 1 490  ? 87.088  114.484 112.466 1.00 93.92  ? 490  THR A O   1 
ATOM   4036  C  CB  . THR A 1 490  ? 88.411  117.521 111.865 1.00 80.58  ? 490  THR A CB  1 
ATOM   4037  O  OG1 . THR A 1 490  ? 87.565  117.414 110.714 1.00 96.02  ? 490  THR A OG1 1 
ATOM   4038  C  CG2 . THR A 1 490  ? 89.625  118.377 111.521 1.00 89.58  ? 490  THR A CG2 1 
ATOM   4039  N  N   . ALA A 1 491  ? 87.398  115.859 114.227 1.00 83.06  ? 491  ALA A N   1 
ATOM   4040  C  CA  . ALA A 1 491  ? 86.263  115.368 114.993 1.00 66.81  ? 491  ALA A CA  1 
ATOM   4041  C  C   . ALA A 1 491  ? 85.047  116.277 114.828 1.00 82.66  ? 491  ALA A C   1 
ATOM   4042  O  O   . ALA A 1 491  ? 85.123  117.380 114.282 1.00 93.01  ? 491  ALA A O   1 
ATOM   4043  C  CB  . ALA A 1 491  ? 86.632  115.235 116.475 1.00 67.57  ? 491  ALA A CB  1 
ATOM   4044  N  N   . VAL A 1 492  ? 83.912  115.787 115.326 1.00 74.72  ? 492  VAL A N   1 
ATOM   4045  C  CA  . VAL A 1 492  ? 82.646  116.506 115.282 1.00 69.11  ? 492  VAL A CA  1 
ATOM   4046  C  C   . VAL A 1 492  ? 82.448  117.337 116.546 1.00 76.34  ? 492  VAL A C   1 
ATOM   4047  O  O   . VAL A 1 492  ? 83.086  117.116 117.580 1.00 92.58  ? 492  VAL A O   1 
ATOM   4048  C  CB  . VAL A 1 492  ? 81.481  115.520 115.076 1.00 64.87  ? 492  VAL A CB  1 
ATOM   4049  C  CG1 . VAL A 1 492  ? 81.532  114.934 113.675 1.00 84.02  ? 492  VAL A CG1 1 
ATOM   4050  C  CG2 . VAL A 1 492  ? 81.569  114.404 116.104 1.00 67.81  ? 492  VAL A CG2 1 
ATOM   4051  N  N   . ASN A 1 493  ? 81.532  118.303 116.459 1.00 74.35  ? 493  ASN A N   1 
ATOM   4052  C  CA  . ASN A 1 493  ? 81.217  119.175 117.580 1.00 76.56  ? 493  ASN A CA  1 
ATOM   4053  C  C   . ASN A 1 493  ? 80.505  118.404 118.689 1.00 87.42  ? 493  ASN A C   1 
ATOM   4054  O  O   . ASN A 1 493  ? 79.903  117.350 118.469 1.00 93.73  ? 493  ASN A O   1 
ATOM   4055  C  CB  . ASN A 1 493  ? 80.352  120.350 117.125 1.00 85.88  ? 493  ASN A CB  1 
ATOM   4056  C  CG  . ASN A 1 493  ? 81.162  121.449 116.465 1.00 89.96  ? 493  ASN A CG  1 
ATOM   4057  O  OD1 . ASN A 1 493  ? 82.359  121.293 116.221 1.00 85.11  ? 493  ASN A OD1 1 
ATOM   4058  N  ND2 . ASN A 1 493  ? 80.514  122.571 116.174 1.00 94.03  ? 493  ASN A ND2 1 
ATOM   4059  N  N   . GLN A 1 494  ? 80.584  118.954 119.904 1.00 74.74  ? 494  GLN A N   1 
ATOM   4060  C  CA  . GLN A 1 494  ? 80.112  118.233 121.080 1.00 68.94  ? 494  GLN A CA  1 
ATOM   4061  C  C   . GLN A 1 494  ? 78.596  118.051 121.124 1.00 79.39  ? 494  GLN A C   1 
ATOM   4062  O  O   . GLN A 1 494  ? 78.128  117.140 121.815 1.00 82.34  ? 494  GLN A O   1 
ATOM   4063  C  CB  . GLN A 1 494  ? 80.580  118.949 122.348 1.00 70.38  ? 494  GLN A CB  1 
ATOM   4064  C  CG  . GLN A 1 494  ? 80.602  118.057 123.578 1.00 73.50  ? 494  GLN A CG  1 
ATOM   4065  C  CD  . GLN A 1 494  ? 79.332  118.164 124.390 1.00 84.36  ? 494  GLN A CD  1 
ATOM   4066  O  OE1 . GLN A 1 494  ? 78.502  119.041 124.152 1.00 93.13  ? 494  GLN A OE1 1 
ATOM   4067  N  NE2 . GLN A 1 494  ? 79.166  117.264 125.353 1.00 89.62  ? 494  GLN A NE2 1 
ATOM   4068  N  N   . GLU A 1 495  ? 77.814  118.878 120.420 1.00 88.26  ? 495  GLU A N   1 
ATOM   4069  C  CA  . GLU A 1 495  ? 76.368  118.656 120.407 1.00 84.77  ? 495  GLU A CA  1 
ATOM   4070  C  C   . GLU A 1 495  ? 76.039  117.311 119.785 1.00 82.98  ? 495  GLU A C   1 
ATOM   4071  O  O   . GLU A 1 495  ? 75.142  116.597 120.251 1.00 84.43  ? 495  GLU A O   1 
ATOM   4072  C  CB  . GLU A 1 495  ? 75.642  119.757 119.636 1.00 89.28  ? 495  GLU A CB  1 
ATOM   4073  C  CG  . GLU A 1 495  ? 75.803  121.135 120.199 1.00 98.94  ? 495  GLU A CG  1 
ATOM   4074  C  CD  . GLU A 1 495  ? 77.038  121.802 119.662 1.00 99.78  ? 495  GLU A CD  1 
ATOM   4075  O  OE1 . GLU A 1 495  ? 77.736  122.461 120.450 1.00 94.41  ? 495  GLU A OE1 1 
ATOM   4076  O  OE2 . GLU A 1 495  ? 77.313  121.660 118.451 1.00 95.32  ? 495  GLU A OE2 1 
ATOM   4077  N  N   . CYS A 1 496  ? 76.764  116.950 118.733 1.00 75.29  ? 496  CYS A N   1 
ATOM   4078  C  CA  . CYS A 1 496  ? 76.599  115.692 118.015 1.00 67.55  ? 496  CYS A CA  1 
ATOM   4079  C  C   . CYS A 1 496  ? 77.921  114.940 118.073 1.00 87.24  ? 496  CYS A C   1 
ATOM   4080  O  O   . CYS A 1 496  ? 78.704  114.947 117.123 1.00 98.72  ? 496  CYS A O   1 
ATOM   4081  C  CB  . CYS A 1 496  ? 76.160  115.970 116.586 1.00 87.20  ? 496  CYS A CB  1 
ATOM   4082  S  SG  . CYS A 1 496  ? 77.180  117.206 115.749 1.00 94.54  ? 496  CYS A SG  1 
ATOM   4083  N  N   . TRP A 1 497  ? 78.161  114.273 119.196 1.00 84.50  ? 497  TRP A N   1 
ATOM   4084  C  CA  . TRP A 1 497  ? 79.333  113.424 119.341 1.00 66.93  ? 497  TRP A CA  1 
ATOM   4085  C  C   . TRP A 1 497  ? 78.992  111.945 119.246 1.00 68.86  ? 497  TRP A C   1 
ATOM   4086  O  O   . TRP A 1 497  ? 79.893  111.128 119.033 1.00 69.47  ? 497  TRP A O   1 
ATOM   4087  C  CB  . TRP A 1 497  ? 80.063  113.725 120.658 1.00 69.35  ? 497  TRP A CB  1 
ATOM   4088  C  CG  . TRP A 1 497  ? 79.397  113.184 121.881 1.00 80.60  ? 497  TRP A CG  1 
ATOM   4089  C  CD1 . TRP A 1 497  ? 78.440  113.799 122.633 1.00 81.16  ? 497  TRP A CD1 1 
ATOM   4090  C  CD2 . TRP A 1 497  ? 79.622  111.904 122.485 1.00 76.09  ? 497  TRP A CD2 1 
ATOM   4091  N  NE1 . TRP A 1 497  ? 78.065  112.988 123.676 1.00 75.95  ? 497  TRP A NE1 1 
ATOM   4092  C  CE2 . TRP A 1 497  ? 78.774  111.817 123.605 1.00 74.83  ? 497  TRP A CE2 1 
ATOM   4093  C  CE3 . TRP A 1 497  ? 80.460  110.825 122.187 1.00 80.08  ? 497  TRP A CE3 1 
ATOM   4094  C  CZ2 . TRP A 1 497  ? 78.739  110.693 124.429 1.00 73.16  ? 497  TRP A CZ2 1 
ATOM   4095  C  CZ3 . TRP A 1 497  ? 80.424  109.711 123.007 1.00 64.96  ? 497  TRP A CZ3 1 
ATOM   4096  C  CH2 . TRP A 1 497  ? 79.570  109.654 124.113 1.00 61.47  ? 497  TRP A CH2 1 
ATOM   4097  N  N   . ASP A 1 498  ? 77.721  111.586 119.409 1.00 73.83  ? 498  ASP A N   1 
ATOM   4098  C  CA  . ASP A 1 498  ? 77.282  110.213 119.208 1.00 67.76  ? 498  ASP A CA  1 
ATOM   4099  C  C   . ASP A 1 498  ? 77.185  109.834 117.743 1.00 84.09  ? 498  ASP A C   1 
ATOM   4100  O  O   . ASP A 1 498  ? 77.140  108.640 117.430 1.00 90.97  ? 498  ASP A O   1 
ATOM   4101  C  CB  . ASP A 1 498  ? 75.915  110.010 119.831 1.00 72.79  ? 498  ASP A CB  1 
ATOM   4102  C  CG  . ASP A 1 498  ? 75.923  110.250 121.290 1.00 74.13  ? 498  ASP A CG  1 
ATOM   4103  O  OD1 . ASP A 1 498  ? 76.877  109.848 121.987 1.00 85.71  ? 498  ASP A OD1 1 
ATOM   4104  O  OD2 . ASP A 1 498  ? 74.999  110.949 121.713 1.00 78.24  ? 498  ASP A OD2 1 
ATOM   4105  N  N   . SER A 1 499  ? 77.125  110.817 116.845 1.00 79.22  ? 499  SER A N   1 
ATOM   4106  C  CA  . SER A 1 499  ? 76.764  110.548 115.461 1.00 82.83  ? 499  SER A CA  1 
ATOM   4107  C  C   . SER A 1 499  ? 77.803  109.712 114.727 1.00 86.86  ? 499  SER A C   1 
ATOM   4108  O  O   . SER A 1 499  ? 77.524  109.251 113.615 1.00 91.03  ? 499  SER A O   1 
ATOM   4109  C  CB  . SER A 1 499  ? 76.542  111.868 114.717 1.00 88.92  ? 499  SER A CB  1 
ATOM   4110  O  OG  . SER A 1 499  ? 77.746  112.613 114.639 1.00 86.87  ? 499  SER A OG  1 
ATOM   4111  N  N   . VAL A 1 500  ? 78.978  109.495 115.317 1.00 73.57  ? 500  VAL A N   1 
ATOM   4112  C  CA  . VAL A 1 500  ? 80.025  108.704 114.680 1.00 69.26  ? 500  VAL A CA  1 
ATOM   4113  C  C   . VAL A 1 500  ? 79.822  107.216 114.938 1.00 72.35  ? 500  VAL A C   1 
ATOM   4114  O  O   . VAL A 1 500  ? 80.657  106.394 114.545 1.00 81.87  ? 500  VAL A O   1 
ATOM   4115  C  CB  . VAL A 1 500  ? 81.422  109.149 115.153 1.00 59.10  ? 500  VAL A CB  1 
ATOM   4116  C  CG1 . VAL A 1 500  ? 81.631  110.634 114.886 1.00 86.72  ? 500  VAL A CG1 1 
ATOM   4117  C  CG2 . VAL A 1 500  ? 81.615  108.827 116.630 1.00 69.83  ? 500  VAL A CG2 1 
ATOM   4118  N  N   . PHE A 1 501  ? 78.720  106.850 115.585 1.00 67.48  ? 501  PHE A N   1 
ATOM   4119  C  CA  . PHE A 1 501  ? 78.459  105.458 115.920 1.00 59.45  ? 501  PHE A CA  1 
ATOM   4120  C  C   . PHE A 1 501  ? 77.205  104.977 115.202 1.00 73.67  ? 501  PHE A C   1 
ATOM   4121  O  O   . PHE A 1 501  ? 76.458  105.758 114.607 1.00 79.49  ? 501  PHE A O   1 
ATOM   4122  C  CB  . PHE A 1 501  ? 78.302  105.263 117.433 1.00 61.92  ? 501  PHE A CB  1 
ATOM   4123  C  CG  . PHE A 1 501  ? 79.495  105.704 118.225 1.00 68.24  ? 501  PHE A CG  1 
ATOM   4124  C  CD1 . PHE A 1 501  ? 80.730  105.110 118.037 1.00 64.46  ? 501  PHE A CD1 1 
ATOM   4125  C  CD2 . PHE A 1 501  ? 79.376  106.703 119.176 1.00 77.79  ? 501  PHE A CD2 1 
ATOM   4126  C  CE1 . PHE A 1 501  ? 81.831  105.520 118.768 1.00 69.14  ? 501  PHE A CE1 1 
ATOM   4127  C  CE2 . PHE A 1 501  ? 80.472  107.113 119.913 1.00 63.19  ? 501  PHE A CE2 1 
ATOM   4128  C  CZ  . PHE A 1 501  ? 81.701  106.521 119.708 1.00 65.67  ? 501  PHE A CZ  1 
ATOM   4129  N  N   . ASP A 1 502  ? 76.980  103.669 115.272 1.00 63.55  ? 502  ASP A N   1 
ATOM   4130  C  CA  . ASP A 1 502  ? 75.816  103.069 114.641 1.00 81.64  ? 502  ASP A CA  1 
ATOM   4131  C  C   . ASP A 1 502  ? 74.592  103.194 115.536 1.00 81.61  ? 502  ASP A C   1 
ATOM   4132  O  O   . ASP A 1 502  ? 74.673  103.029 116.756 1.00 83.27  ? 502  ASP A O   1 
ATOM   4133  C  CB  . ASP A 1 502  ? 76.063  101.600 114.308 1.00 93.92  ? 502  ASP A CB  1 
ATOM   4134  C  CG  . ASP A 1 502  ? 74.959  101.010 113.449 1.00 117.34 ? 502  ASP A CG  1 
ATOM   4135  O  OD1 . ASP A 1 502  ? 73.842  100.797 113.970 1.00 103.51 ? 502  ASP A OD1 1 
ATOM   4136  O  OD2 . ASP A 1 502  ? 75.200  100.777 112.247 1.00 105.37 ? 502  ASP A OD2 1 
ATOM   4137  N  N   . ARG A 1 503  ? 73.450  103.487 114.910 1.00 86.06  ? 503  ARG A N   1 
ATOM   4138  C  CA  . ARG A 1 503  ? 72.218  103.700 115.658 1.00 81.58  ? 503  ARG A CA  1 
ATOM   4139  C  C   . ARG A 1 503  ? 71.754  102.426 116.353 1.00 86.29  ? 503  ARG A C   1 
ATOM   4140  O  O   . ARG A 1 503  ? 71.229  102.480 117.472 1.00 95.19  ? 503  ARG A O   1 
ATOM   4141  C  CB  . ARG A 1 503  ? 71.121  104.190 114.713 1.00 97.20  ? 503  ARG A CB  1 
ATOM   4142  C  CG  . ARG A 1 503  ? 71.329  105.565 114.118 1.00 103.55 ? 503  ARG A CG  1 
ATOM   4143  C  CD  . ARG A 1 503  ? 70.146  105.906 113.228 1.00 120.69 ? 503  ARG A CD  1 
ATOM   4144  N  NE  . ARG A 1 503  ? 70.306  107.185 112.550 1.00 135.27 ? 503  ARG A NE  1 
ATOM   4145  C  CZ  . ARG A 1 503  ? 69.914  108.346 113.059 1.00 141.05 ? 503  ARG A CZ  1 
ATOM   4146  N  NH1 . ARG A 1 503  ? 69.338  108.385 114.253 1.00 132.24 ? 503  ARG A NH1 1 
ATOM   4147  N  NH2 . ARG A 1 503  ? 70.095  109.468 112.376 1.00 150.44 ? 503  ARG A NH2 1 
ATOM   4148  N  N   . SER A 1 504  ? 71.923  101.272 115.704 1.00 80.10  ? 504  SER A N   1 
ATOM   4149  C  CA  . SER A 1 504  ? 71.429  100.025 116.279 1.00 74.15  ? 504  SER A CA  1 
ATOM   4150  C  C   . SER A 1 504  ? 72.315  99.510  117.413 1.00 81.36  ? 504  SER A C   1 
ATOM   4151  O  O   . SER A 1 504  ? 71.804  98.955  118.392 1.00 90.58  ? 504  SER A O   1 
ATOM   4152  C  CB  . SER A 1 504  ? 71.301  98.968  115.180 1.00 86.52  ? 504  SER A CB  1 
ATOM   4153  O  OG  . SER A 1 504  ? 70.224  99.268  114.307 1.00 97.37  ? 504  SER A OG  1 
ATOM   4154  N  N   . VAL A 1 505  ? 73.634  99.689  117.308 1.00 84.67  ? 505  VAL A N   1 
ATOM   4155  C  CA  . VAL A 1 505  ? 74.533  99.297  118.393 1.00 75.97  ? 505  VAL A CA  1 
ATOM   4156  C  C   . VAL A 1 505  ? 74.380  100.224 119.594 1.00 76.38  ? 505  VAL A C   1 
ATOM   4157  O  O   . VAL A 1 505  ? 74.423  99.779  120.747 1.00 84.57  ? 505  VAL A O   1 
ATOM   4158  C  CB  . VAL A 1 505  ? 75.989  99.236  117.898 1.00 70.55  ? 505  VAL A CB  1 
ATOM   4159  C  CG1 . VAL A 1 505  ? 76.898  98.716  119.001 1.00 71.56  ? 505  VAL A CG1 1 
ATOM   4160  C  CG2 . VAL A 1 505  ? 76.085  98.329  116.680 1.00 72.72  ? 505  VAL A CG2 1 
ATOM   4161  N  N   . LEU A 1 506  ? 74.202  101.523 119.347 1.00 78.82  ? 506  LEU A N   1 
ATOM   4162  C  CA  . LEU A 1 506  ? 74.048  102.476 120.442 1.00 73.08  ? 506  LEU A CA  1 
ATOM   4163  C  C   . LEU A 1 506  ? 72.829  102.139 121.290 1.00 84.49  ? 506  LEU A C   1 
ATOM   4164  O  O   . LEU A 1 506  ? 72.897  102.132 122.525 1.00 84.68  ? 506  LEU A O   1 
ATOM   4165  C  CB  . LEU A 1 506  ? 73.954  103.898 119.889 1.00 73.87  ? 506  LEU A CB  1 
ATOM   4166  C  CG  . LEU A 1 506  ? 75.284  104.652 119.831 1.00 67.70  ? 506  LEU A CG  1 
ATOM   4167  C  CD1 . LEU A 1 506  ? 75.093  106.035 119.229 1.00 75.66  ? 506  LEU A CD1 1 
ATOM   4168  C  CD2 . LEU A 1 506  ? 75.905  104.741 121.221 1.00 75.18  ? 506  LEU A CD2 1 
ATOM   4169  N  N   . GLY A 1 507  ? 71.701  101.863 120.644 1.00 90.10  ? 507  GLY A N   1 
ATOM   4170  C  CA  . GLY A 1 507  ? 70.459  101.596 121.332 1.00 91.81  ? 507  GLY A CA  1 
ATOM   4171  C  C   . GLY A 1 507  ? 69.491  102.753 121.360 1.00 85.70  ? 507  GLY A C   1 
ATOM   4172  O  O   . GLY A 1 507  ? 68.401  102.613 121.928 1.00 90.49  ? 507  GLY A O   1 
ATOM   4173  N  N   . TYR A 1 508  ? 69.854  103.888 120.774 1.00 83.59  ? 508  TYR A N   1 
ATOM   4174  C  CA  . TYR A 1 508  ? 68.967  105.038 120.711 1.00 97.62  ? 508  TYR A CA  1 
ATOM   4175  C  C   . TYR A 1 508  ? 69.359  105.857 119.492 1.00 106.11 ? 508  TYR A C   1 
ATOM   4176  O  O   . TYR A 1 508  ? 70.443  105.692 118.926 1.00 102.78 ? 508  TYR A O   1 
ATOM   4177  C  CB  . TYR A 1 508  ? 69.044  105.875 121.993 1.00 96.35  ? 508  TYR A CB  1 
ATOM   4178  C  CG  . TYR A 1 508  ? 70.411  106.475 122.232 1.00 109.83 ? 508  TYR A CG  1 
ATOM   4179  C  CD1 . TYR A 1 508  ? 70.734  107.733 121.743 1.00 115.82 ? 508  TYR A CD1 1 
ATOM   4180  C  CD2 . TYR A 1 508  ? 71.387  105.773 122.926 1.00 110.47 ? 508  TYR A CD2 1 
ATOM   4181  C  CE1 . TYR A 1 508  ? 71.984  108.281 121.946 1.00 98.94  ? 508  TYR A CE1 1 
ATOM   4182  C  CE2 . TYR A 1 508  ? 72.641  106.314 123.136 1.00 98.25  ? 508  TYR A CE2 1 
ATOM   4183  C  CZ  . TYR A 1 508  ? 72.934  107.568 122.644 1.00 88.04  ? 508  TYR A CZ  1 
ATOM   4184  O  OH  . TYR A 1 508  ? 74.180  108.114 122.850 1.00 76.32  ? 508  TYR A OH  1 
ATOM   4185  N  N   . ASN A 1 509  ? 68.467  106.759 119.092 1.00 107.42 ? 509  ASN A N   1 
ATOM   4186  C  CA  . ASN A 1 509  ? 68.742  107.627 117.961 1.00 114.54 ? 509  ASN A CA  1 
ATOM   4187  C  C   . ASN A 1 509  ? 69.209  108.985 118.454 1.00 113.92 ? 509  ASN A C   1 
ATOM   4188  O  O   . ASN A 1 509  ? 68.457  109.650 119.185 1.00 118.83 ? 509  ASN A O   1 
ATOM   4189  C  CB  . ASN A 1 509  ? 67.498  107.777 117.098 1.00 111.93 ? 509  ASN A CB  1 
ATOM   4190  C  CG  . ASN A 1 509  ? 67.018  106.454 116.539 1.00 115.84 ? 509  ASN A CG  1 
ATOM   4191  O  OD1 . ASN A 1 509  ? 66.264  105.728 117.187 1.00 113.87 ? 509  ASN A OD1 1 
ATOM   4192  N  ND2 . ASN A 1 509  ? 67.467  106.123 115.335 1.00 111.74 ? 509  ASN A ND2 1 
ATOM   4193  N  N   . PRO A 1 510  ? 70.413  109.433 118.111 1.00 106.75 ? 510  PRO A N   1 
ATOM   4194  C  CA  . PRO A 1 510  ? 70.865  110.744 118.579 1.00 110.73 ? 510  PRO A CA  1 
ATOM   4195  C  C   . PRO A 1 510  ? 69.962  111.834 118.031 1.00 142.53 ? 510  PRO A C   1 
ATOM   4196  O  O   . PRO A 1 510  ? 69.551  111.782 116.862 1.00 137.66 ? 510  PRO A O   1 
ATOM   4197  C  CB  . PRO A 1 510  ? 72.293  110.850 118.022 1.00 93.86  ? 510  PRO A CB  1 
ATOM   4198  C  CG  . PRO A 1 510  ? 72.723  109.426 117.835 1.00 94.58  ? 510  PRO A CG  1 
ATOM   4199  C  CD  . PRO A 1 510  ? 71.482  108.689 117.425 1.00 100.28 ? 510  PRO A CD  1 
ATOM   4200  N  N   . PRO A 1 511  ? 69.626  112.833 118.849 1.00 149.80 ? 511  PRO A N   1 
ATOM   4201  C  CA  . PRO A 1 511  ? 68.724  113.898 118.377 1.00 160.81 ? 511  PRO A CA  1 
ATOM   4202  C  C   . PRO A 1 511  ? 69.258  114.716 117.213 1.00 157.51 ? 511  PRO A C   1 
ATOM   4203  O  O   . PRO A 1 511  ? 68.494  115.057 116.301 1.00 149.28 ? 511  PRO A O   1 
ATOM   4204  C  CB  . PRO A 1 511  ? 68.530  114.765 119.630 1.00 155.67 ? 511  PRO A CB  1 
ATOM   4205  C  CG  . PRO A 1 511  ? 68.833  113.852 120.777 1.00 142.28 ? 511  PRO A CG  1 
ATOM   4206  C  CD  . PRO A 1 511  ? 69.925  112.954 120.284 1.00 132.77 ? 511  PRO A CD  1 
ATOM   4207  N  N   . VAL A 1 512  ? 70.550  115.034 117.210 1.00 153.08 ? 512  VAL A N   1 
ATOM   4208  C  CA  . VAL A 1 512  ? 71.163  115.854 116.171 1.00 165.45 ? 512  VAL A CA  1 
ATOM   4209  C  C   . VAL A 1 512  ? 72.169  115.038 115.365 1.00 160.47 ? 512  VAL A C   1 
ATOM   4210  O  O   . VAL A 1 512  ? 72.995  114.307 115.924 1.00 153.77 ? 512  VAL A O   1 
ATOM   4211  C  CB  . VAL A 1 512  ? 71.810  117.114 116.775 1.00 165.18 ? 512  VAL A CB  1 
ATOM   4212  C  CG1 . VAL A 1 512  ? 72.894  116.749 117.782 1.00 145.00 ? 512  VAL A CG1 1 
ATOM   4213  C  CG2 . VAL A 1 512  ? 72.366  118.010 115.677 1.00 157.23 ? 512  VAL A CG2 1 
ATOM   4214  N  N   . ARG A 1 513  ? 72.229  115.301 114.060 1.00 157.00 ? 513  ARG A N   1 
ATOM   4215  C  CA  . ARG A 1 513  ? 73.193  114.647 113.164 1.00 157.62 ? 513  ARG A CA  1 
ATOM   4216  C  C   . ARG A 1 513  ? 74.186  115.673 112.570 1.00 169.59 ? 513  ARG A C   1 
ATOM   4217  O  O   . ARG A 1 513  ? 73.772  116.717 112.071 1.00 167.95 ? 513  ARG A O   1 
ATOM   4218  C  CB  . ARG A 1 513  ? 72.463  113.891 112.054 1.00 147.08 ? 513  ARG A CB  1 
ATOM   4219  C  CG  . ARG A 1 513  ? 73.333  113.554 110.857 1.00 153.26 ? 513  ARG A CG  1 
ATOM   4220  C  CD  . ARG A 1 513  ? 74.475  112.625 111.232 1.00 157.37 ? 513  ARG A CD  1 
ATOM   4221  N  NE  . ARG A 1 513  ? 75.407  112.459 110.121 1.00 172.33 ? 513  ARG A NE  1 
ATOM   4222  C  CZ  . ARG A 1 513  ? 76.390  111.567 110.095 1.00 175.29 ? 513  ARG A CZ  1 
ATOM   4223  N  NH1 . ARG A 1 513  ? 77.188  111.490 109.040 1.00 166.68 ? 513  ARG A NH1 1 
ATOM   4224  N  NH2 . ARG A 1 513  ? 76.578  110.751 111.121 1.00 164.95 ? 513  ARG A NH2 1 
ATOM   4225  N  N   . PHE A 1 514  ? 75.485  115.366 112.616 1.00 160.76 ? 514  PHE A N   1 
ATOM   4226  C  CA  . PHE A 1 514  ? 76.552  116.274 112.146 1.00 159.35 ? 514  PHE A CA  1 
ATOM   4227  C  C   . PHE A 1 514  ? 76.597  116.626 110.653 1.00 160.49 ? 514  PHE A C   1 
ATOM   4228  O  O   . PHE A 1 514  ? 76.443  115.758 109.795 1.00 159.23 ? 514  PHE A O   1 
ATOM   4229  C  CB  . PHE A 1 514  ? 77.918  115.700 112.521 1.00 145.07 ? 514  PHE A CB  1 
ATOM   4230  C  CG  . PHE A 1 514  ? 78.454  114.729 111.512 1.00 161.51 ? 514  PHE A CG  1 
ATOM   4231  C  CD1 . PHE A 1 514  ? 78.355  113.365 111.720 1.00 157.06 ? 514  PHE A CD1 1 
ATOM   4232  C  CD2 . PHE A 1 514  ? 79.041  115.181 110.342 1.00 163.60 ? 514  PHE A CD2 1 
ATOM   4233  C  CE1 . PHE A 1 514  ? 78.840  112.469 110.785 1.00 154.39 ? 514  PHE A CE1 1 
ATOM   4234  C  CE2 . PHE A 1 514  ? 79.528  114.293 109.404 1.00 148.80 ? 514  PHE A CE2 1 
ATOM   4235  C  CZ  . PHE A 1 514  ? 79.427  112.935 109.626 1.00 148.78 ? 514  PHE A CZ  1 
ATOM   4236  N  N   . GLN A 1 515  ? 76.811  117.911 110.363 1.00 30.00  ? 515  GLN A N   1 
ATOM   4237  C  CA  . GLN A 1 515  ? 76.907  118.416 108.985 1.00 30.00  ? 515  GLN A CA  1 
ATOM   4238  C  C   . GLN A 1 515  ? 78.117  118.021 108.105 1.00 30.00  ? 515  GLN A C   1 
ATOM   4239  O  O   . GLN A 1 515  ? 77.930  117.628 106.952 1.00 30.00  ? 515  GLN A O   1 
ATOM   4240  C  CB  . GLN A 1 515  ? 76.792  119.943 109.000 1.00 30.00  ? 515  GLN A CB  1 
ATOM   4241  C  CG  . GLN A 1 515  ? 75.643  120.470 109.844 1.00 30.00  ? 515  GLN A CG  1 
ATOM   4242  C  CD  . GLN A 1 515  ? 75.699  121.974 110.028 1.00 30.00  ? 515  GLN A CD  1 
ATOM   4243  O  OE1 . GLN A 1 515  ? 76.687  122.617 109.674 1.00 30.00  ? 515  GLN A OE1 1 
ATOM   4244  N  NE2 . GLN A 1 515  ? 74.636  122.543 110.586 1.00 30.00  ? 515  GLN A NE2 1 
ATOM   4245  N  N   . SER A 1 516  ? 79.339  118.114 108.641 1.00 30.00  ? 516  SER A N   1 
ATOM   4246  C  CA  . SER A 1 516  ? 80.560  117.779 107.879 1.00 30.00  ? 516  SER A CA  1 
ATOM   4247  C  C   . SER A 1 516  ? 81.785  117.490 108.760 1.00 30.00  ? 516  SER A C   1 
ATOM   4248  O  O   . SER A 1 516  ? 81.813  117.878 109.928 1.00 30.00  ? 516  SER A O   1 
ATOM   4249  C  CB  . SER A 1 516  ? 80.893  118.874 106.860 1.00 30.00  ? 516  SER A CB  1 
ATOM   4250  O  OG  . SER A 1 516  ? 80.874  120.155 107.461 1.00 30.00  ? 516  SER A OG  1 
ATOM   4251  N  N   . LYS A 1 517  ? 82.762  116.757 108.208 1.00 138.89 ? 517  LYS A N   1 
ATOM   4252  C  CA  . LYS A 1 517  ? 83.983  116.388 108.953 1.00 144.25 ? 517  LYS A CA  1 
ATOM   4253  C  C   . LYS A 1 517  ? 85.418  116.635 108.397 1.00 151.91 ? 517  LYS A C   1 
ATOM   4254  O  O   . LYS A 1 517  ? 86.267  117.157 109.120 1.00 145.23 ? 517  LYS A O   1 
ATOM   4255  C  CB  . LYS A 1 517  ? 83.862  114.945 109.454 1.00 128.21 ? 517  LYS A CB  1 
ATOM   4256  C  CG  . LYS A 1 517  ? 83.344  113.967 108.417 1.00 132.90 ? 517  LYS A CG  1 
ATOM   4257  C  CD  . LYS A 1 517  ? 82.619  112.824 109.101 1.00 134.41 ? 517  LYS A CD  1 
ATOM   4258  C  CE  . LYS A 1 517  ? 83.332  112.424 110.380 1.00 128.56 ? 517  LYS A CE  1 
ATOM   4259  N  NZ  . LYS A 1 517  ? 82.504  111.512 111.215 1.00 130.57 ? 517  LYS A NZ  1 
ATOM   4260  N  N   . ARG A 1 518  ? 85.688  116.274 107.141 1.00 143.83 ? 518  ARG A N   1 
ATOM   4261  C  CA  . ARG A 1 518  ? 87.046  116.396 106.559 1.00 131.53 ? 518  ARG A CA  1 
ATOM   4262  C  C   . ARG A 1 518  ? 87.569  117.820 106.393 1.00 130.59 ? 518  ARG A C   1 
ATOM   4263  O  O   . ARG A 1 518  ? 86.779  118.747 106.251 1.00 138.98 ? 518  ARG A O   1 
ATOM   4264  C  CB  . ARG A 1 518  ? 87.161  115.623 105.246 1.00 142.50 ? 518  ARG A CB  1 
ATOM   4265  C  CG  . ARG A 1 518  ? 87.375  114.134 105.450 1.00 145.31 ? 518  ARG A CG  1 
ATOM   4266  C  CD  . ARG A 1 518  ? 88.134  113.507 104.293 1.00 134.77 ? 518  ARG A CD  1 
ATOM   4267  N  NE  . ARG A 1 518  ? 88.642  112.188 104.652 1.00 139.37 ? 518  ARG A NE  1 
ATOM   4268  C  CZ  . ARG A 1 518  ? 89.799  111.979 105.270 1.00 142.96 ? 518  ARG A CZ  1 
ATOM   4269  N  NH1 . ARG A 1 518  ? 90.577  113.004 105.592 1.00 134.73 ? 518  ARG A NH1 1 
ATOM   4270  N  NH2 . ARG A 1 518  ? 90.180  110.744 105.564 1.00 144.21 ? 518  ARG A NH2 1 
ATOM   4271  N  N   . VAL A 1 519  ? 88.892  118.008 106.406 1.00 128.90 ? 519  VAL A N   1 
ATOM   4272  C  CA  . VAL A 1 519  ? 89.394  119.382 106.338 1.00 131.99 ? 519  VAL A CA  1 
ATOM   4273  C  C   . VAL A 1 519  ? 89.093  120.027 104.986 1.00 139.38 ? 519  VAL A C   1 
ATOM   4274  O  O   . VAL A 1 519  ? 88.379  121.038 104.962 1.00 129.36 ? 519  VAL A O   1 
ATOM   4275  C  CB  . VAL A 1 519  ? 90.890  119.461 106.689 1.00 127.48 ? 519  VAL A CB  1 
ATOM   4276  C  CG1 . VAL A 1 519  ? 91.385  120.889 106.531 1.00 111.72 ? 519  VAL A CG1 1 
ATOM   4277  C  CG2 . VAL A 1 519  ? 91.094  119.019 108.115 1.00 133.88 ? 519  VAL A CG2 1 
ATOM   4278  N  N   . PRO A 1 520  ? 89.594  119.514 103.850 1.00 142.66 ? 520  PRO A N   1 
ATOM   4279  C  CA  . PRO A 1 520  ? 89.315  120.185 102.562 1.00 130.25 ? 520  PRO A CA  1 
ATOM   4280  C  C   . PRO A 1 520  ? 87.856  120.555 102.320 1.00 122.32 ? 520  PRO A C   1 
ATOM   4281  O  O   . PRO A 1 520  ? 87.599  121.571 101.661 1.00 115.29 ? 520  PRO A O   1 
ATOM   4282  C  CB  . PRO A 1 520  ? 89.798  119.163 101.518 1.00 129.38 ? 520  PRO A CB  1 
ATOM   4283  C  CG  . PRO A 1 520  ? 90.021  117.888 102.254 1.00 137.11 ? 520  PRO A CG  1 
ATOM   4284  C  CD  . PRO A 1 520  ? 90.349  118.263 103.649 1.00 140.98 ? 520  PRO A CD  1 
ATOM   4285  N  N   . GLU A 1 521  ? 86.892  119.785 102.827 1.00 130.73 ? 521  GLU A N   1 
ATOM   4286  C  CA  . GLU A 1 521  ? 85.491  120.150 102.638 1.00 117.51 ? 521  GLU A CA  1 
ATOM   4287  C  C   . GLU A 1 521  ? 84.999  121.207 103.623 1.00 101.07 ? 521  GLU A C   1 
ATOM   4288  O  O   . GLU A 1 521  ? 83.952  121.816 103.378 1.00 100.00 ? 521  GLU A O   1 
ATOM   4289  C  CB  . GLU A 1 521  ? 84.612  118.899 102.715 1.00 135.11 ? 521  GLU A CB  1 
ATOM   4290  C  CG  . GLU A 1 521  ? 84.661  118.050 101.446 1.00 148.97 ? 521  GLU A CG  1 
ATOM   4291  C  CD  . GLU A 1 521  ? 85.890  117.159 101.362 1.00 154.16 ? 521  GLU A CD  1 
ATOM   4292  O  OE1 . GLU A 1 521  ? 86.937  117.518 101.937 1.00 138.65 ? 521  GLU A OE1 1 
ATOM   4293  O  OE2 . GLU A 1 521  ? 85.813  116.104 100.699 1.00 159.09 ? 521  GLU A OE2 1 
ATOM   4294  N  N   . GLN A 1 522  ? 85.707  121.433 104.730 1.00 105.75 ? 522  GLN A N   1 
ATOM   4295  C  CA  . GLN A 1 522  ? 85.299  122.435 105.710 1.00 104.21 ? 522  GLN A CA  1 
ATOM   4296  C  C   . GLN A 1 522  ? 86.096  123.727 105.624 1.00 103.37 ? 522  GLN A C   1 
ATOM   4297  O  O   . GLN A 1 522  ? 85.624  124.763 106.105 1.00 97.05  ? 522  GLN A O   1 
ATOM   4298  C  CB  . GLN A 1 522  ? 85.407  121.887 107.135 1.00 96.00  ? 522  GLN A CB  1 
ATOM   4299  C  CG  . GLN A 1 522  ? 84.155  121.194 107.612 1.00 108.42 ? 522  GLN A CG  1 
ATOM   4300  C  CD  . GLN A 1 522  ? 84.384  120.409 108.876 1.00 101.70 ? 522  GLN A CD  1 
ATOM   4301  O  OE1 . GLN A 1 522  ? 85.400  119.732 109.026 1.00 107.65 ? 522  GLN A OE1 1 
ATOM   4302  N  NE2 . GLN A 1 522  ? 83.446  120.508 109.808 1.00 100.70 ? 522  GLN A NE2 1 
ATOM   4303  N  N   . PHE A 1 523  ? 87.283  123.686 105.024 1.00 99.60  ? 523  PHE A N   1 
ATOM   4304  C  CA  . PHE A 1 523  ? 88.007  124.912 104.713 1.00 95.10  ? 523  PHE A CA  1 
ATOM   4305  C  C   . PHE A 1 523  ? 87.293  125.702 103.623 1.00 97.76  ? 523  PHE A C   1 
ATOM   4306  O  O   . PHE A 1 523  ? 87.275  126.939 103.657 1.00 97.15  ? 523  PHE A O   1 
ATOM   4307  C  CB  . PHE A 1 523  ? 89.444  124.585 104.308 1.00 100.60 ? 523  PHE A CB  1 
ATOM   4308  C  CG  . PHE A 1 523  ? 90.253  125.790 103.932 1.00 96.51  ? 523  PHE A CG  1 
ATOM   4309  C  CD1 . PHE A 1 523  ? 90.398  126.162 102.606 1.00 97.42  ? 523  PHE A CD1 1 
ATOM   4310  C  CD2 . PHE A 1 523  ? 90.853  126.564 104.910 1.00 100.00 ? 523  PHE A CD2 1 
ATOM   4311  C  CE1 . PHE A 1 523  ? 91.136  127.278 102.263 1.00 96.91  ? 523  PHE A CE1 1 
ATOM   4312  C  CE2 . PHE A 1 523  ? 91.592  127.682 104.574 1.00 86.93  ? 523  PHE A CE2 1 
ATOM   4313  C  CZ  . PHE A 1 523  ? 91.733  128.039 103.249 1.00 88.22  ? 523  PHE A CZ  1 
ATOM   4314  N  N   . LEU A 1 524  ? 86.704  125.010 102.647 1.00 95.72  ? 524  LEU A N   1 
ATOM   4315  C  CA  . LEU A 1 524  ? 85.937  125.692 101.612 1.00 84.90  ? 524  LEU A CA  1 
ATOM   4316  C  C   . LEU A 1 524  ? 84.608  126.221 102.131 1.00 88.69  ? 524  LEU A C   1 
ATOM   4317  O  O   . LEU A 1 524  ? 84.068  127.172 101.558 1.00 100.72 ? 524  LEU A O   1 
ATOM   4318  C  CB  . LEU A 1 524  ? 85.657  124.740 100.448 1.00 87.26  ? 524  LEU A CB  1 
ATOM   4319  C  CG  . LEU A 1 524  ? 86.807  124.135 99.649  1.00 81.05  ? 524  LEU A CG  1 
ATOM   4320  C  CD1 . LEU A 1 524  ? 86.244  123.330 98.488  1.00 81.23  ? 524  LEU A CD1 1 
ATOM   4321  C  CD2 . LEU A 1 524  ? 87.743  125.222 99.151  1.00 80.93  ? 524  LEU A CD2 1 
ATOM   4322  N  N   . GLY A 1 525  ? 84.083  125.644 103.215 1.00 88.80  ? 525  GLY A N   1 
ATOM   4323  C  CA  . GLY A 1 525  ? 82.811  126.085 103.760 1.00 87.45  ? 525  GLY A CA  1 
ATOM   4324  C  C   . GLY A 1 525  ? 82.882  127.285 104.677 1.00 91.07  ? 525  GLY A C   1 
ATOM   4325  O  O   . GLY A 1 525  ? 81.872  127.975 104.848 1.00 94.30  ? 525  GLY A O   1 
ATOM   4326  N  N   . GLN A 1 526  ? 84.042  127.561 105.267 1.00 82.98  ? 526  GLN A N   1 
ATOM   4327  C  CA  . GLN A 1 526  ? 84.151  128.681 106.192 1.00 81.52  ? 526  GLN A CA  1 
ATOM   4328  C  C   . GLN A 1 526  ? 84.132  129.992 105.415 1.00 88.58  ? 526  GLN A C   1 
ATOM   4329  O  O   . GLN A 1 526  ? 84.958  130.209 104.524 1.00 103.22 ? 526  GLN A O   1 
ATOM   4330  C  CB  . GLN A 1 526  ? 85.422  128.559 107.026 1.00 84.70  ? 526  GLN A CB  1 
ATOM   4331  C  CG  . GLN A 1 526  ? 85.501  129.566 108.154 1.00 97.28  ? 526  GLN A CG  1 
ATOM   4332  C  CD  . GLN A 1 526  ? 86.678  129.311 109.065 1.00 99.09  ? 526  GLN A CD  1 
ATOM   4333  O  OE1 . GLN A 1 526  ? 87.621  128.611 108.696 1.00 89.79  ? 526  GLN A OE1 1 
ATOM   4334  N  NE2 . GLN A 1 526  ? 86.624  129.865 110.269 1.00 110.49 ? 526  GLN A NE2 1 
ATOM   4335  N  N   . ALA A 1 527  ? 83.191  130.871 105.766 1.00 92.94  ? 527  ALA A N   1 
ATOM   4336  C  CA  . ALA A 1 527  ? 82.889  132.030 104.935 1.00 98.16  ? 527  ALA A CA  1 
ATOM   4337  C  C   . ALA A 1 527  ? 83.912  133.156 105.053 1.00 96.42  ? 527  ALA A C   1 
ATOM   4338  O  O   . ALA A 1 527  ? 84.085  133.919 104.097 1.00 105.49 ? 527  ALA A O   1 
ATOM   4339  C  CB  . ALA A 1 527  ? 81.499  132.567 105.280 1.00 100.56 ? 527  ALA A CB  1 
ATOM   4340  N  N   . ASP A 1 528  ? 84.606  133.281 106.183 1.00 103.00 ? 528  ASP A N   1 
ATOM   4341  C  CA  . ASP A 1 528  ? 85.463  134.439 106.413 1.00 112.11 ? 528  ASP A CA  1 
ATOM   4342  C  C   . ASP A 1 528  ? 86.948  134.098 106.435 1.00 109.51 ? 528  ASP A C   1 
ATOM   4343  O  O   . ASP A 1 528  ? 87.700  134.591 105.588 1.00 116.14 ? 528  ASP A O   1 
ATOM   4344  C  CB  . ASP A 1 528  ? 85.036  135.125 107.721 1.00 119.03 ? 528  ASP A CB  1 
ATOM   4345  C  CG  . ASP A 1 528  ? 84.969  134.161 108.896 1.00 128.49 ? 528  ASP A CG  1 
ATOM   4346  O  OD1 . ASP A 1 528  ? 85.320  132.975 108.721 1.00 117.93 ? 528  ASP A OD1 1 
ATOM   4347  O  OD2 . ASP A 1 528  ? 84.551  134.587 109.993 1.00 134.52 ? 528  ASP A OD2 1 
ATOM   4348  N  N   . PHE A 1 529  ? 87.387  133.249 107.362 1.00 108.21 ? 529  PHE A N   1 
ATOM   4349  C  CA  . PHE A 1 529  ? 88.781  132.826 107.462 1.00 101.28 ? 529  PHE A CA  1 
ATOM   4350  C  C   . PHE A 1 529  ? 89.803  133.955 107.341 1.00 101.62 ? 529  PHE A C   1 
ATOM   4351  O  O   . PHE A 1 529  ? 90.479  134.077 106.316 1.00 93.33  ? 529  PHE A O   1 
ATOM   4352  C  CB  . PHE A 1 529  ? 89.112  131.743 106.432 1.00 98.30  ? 529  PHE A CB  1 
ATOM   4353  C  CG  . PHE A 1 529  ? 90.467  131.128 106.647 1.00 102.79 ? 529  PHE A CG  1 
ATOM   4354  C  CD1 . PHE A 1 529  ? 90.667  130.209 107.663 1.00 104.70 ? 529  PHE A CD1 1 
ATOM   4355  C  CD2 . PHE A 1 529  ? 91.546  131.485 105.855 1.00 107.74 ? 529  PHE A CD2 1 
ATOM   4356  C  CE1 . PHE A 1 529  ? 91.917  129.657 107.879 1.00 99.67  ? 529  PHE A CE1 1 
ATOM   4357  C  CE2 . PHE A 1 529  ? 92.794  130.941 106.066 1.00 112.49 ? 529  PHE A CE2 1 
ATOM   4358  C  CZ  . PHE A 1 529  ? 92.981  130.024 107.078 1.00 97.86  ? 529  PHE A CZ  1 
ATOM   4359  N  N   . SER A 1 530  ? 89.869  134.838 108.325 1.00 120.57 ? 530  SER A N   1 
ATOM   4360  C  CA  . SER A 1 530  ? 91.050  135.676 108.434 1.00 116.40 ? 530  SER A CA  1 
ATOM   4361  C  C   . SER A 1 530  ? 92.115  134.927 109.237 1.00 97.43  ? 530  SER A C   1 
ATOM   4362  O  O   . SER A 1 530  ? 91.871  133.856 109.794 1.00 104.46 ? 530  SER A O   1 
ATOM   4363  C  CB  . SER A 1 530  ? 90.719  137.022 109.080 1.00 125.32 ? 530  SER A CB  1 
ATOM   4364  O  OG  . SER A 1 530  ? 91.842  137.886 109.051 1.00 118.38 ? 530  SER A OG  1 
ATOM   4365  N  N   . LEU A 1 531  ? 93.321  135.484 109.266 1.00 93.73  ? 531  LEU A N   1 
ATOM   4366  C  CA  . LEU A 1 531  ? 94.355  134.937 110.136 1.00 87.72  ? 531  LEU A CA  1 
ATOM   4367  C  C   . LEU A 1 531  ? 94.362  135.663 111.474 1.00 89.03  ? 531  LEU A C   1 
ATOM   4368  O  O   . LEU A 1 531  ? 94.510  135.044 112.543 1.00 91.91  ? 531  LEU A O   1 
ATOM   4369  C  CB  . LEU A 1 531  ? 95.721  135.059 109.458 1.00 101.18 ? 531  LEU A CB  1 
ATOM   4370  C  CG  . LEU A 1 531  ? 96.870  134.250 110.052 1.00 94.97  ? 531  LEU A CG  1 
ATOM   4371  C  CD1 . LEU A 1 531  ? 96.595  132.767 109.887 1.00 103.54 ? 531  LEU A CD1 1 
ATOM   4372  C  CD2 . LEU A 1 531  ? 98.184  134.639 109.393 1.00 103.95 ? 531  LEU A CD2 1 
ATOM   4373  N  N   . ASN A 1 532  ? 94.114  136.972 111.418 1.00 88.63  ? 532  ASN A N   1 
ATOM   4374  C  CA  . ASN A 1 532  ? 93.873  137.738 112.628 1.00 82.19  ? 532  ASN A CA  1 
ATOM   4375  C  C   . ASN A 1 532  ? 92.644  137.239 113.368 1.00 92.51  ? 532  ASN A C   1 
ATOM   4376  O  O   . ASN A 1 532  ? 92.569  137.367 114.593 1.00 104.56 ? 532  ASN A O   1 
ATOM   4377  C  CB  . ASN A 1 532  ? 93.718  139.218 112.281 1.00 95.36  ? 532  ASN A CB  1 
ATOM   4378  C  CG  . ASN A 1 532  ? 93.293  140.049 113.470 1.00 119.85 ? 532  ASN A CG  1 
ATOM   4379  O  OD1 . ASN A 1 532  ? 92.111  140.352 113.641 1.00 121.96 ? 532  ASN A OD1 1 
ATOM   4380  N  ND2 . ASN A 1 532  ? 94.253  140.411 114.311 1.00 121.72 ? 532  ASN A ND2 1 
ATOM   4381  N  N   . GLN A 1 533  ? 91.684  136.631 112.665 1.00 89.02  ? 533  GLN A N   1 
ATOM   4382  C  CA  . GLN A 1 533  ? 90.521  136.143 113.392 1.00 90.75  ? 533  GLN A CA  1 
ATOM   4383  C  C   . GLN A 1 533  ? 90.828  134.854 114.148 1.00 89.51  ? 533  GLN A C   1 
ATOM   4384  O  O   . GLN A 1 533  ? 90.279  134.644 115.231 1.00 94.25  ? 533  GLN A O   1 
ATOM   4385  C  CB  . GLN A 1 533  ? 89.325  135.941 112.454 1.00 94.49  ? 533  GLN A CB  1 
ATOM   4386  C  CG  . GLN A 1 533  ? 89.426  134.759 111.518 1.00 104.06 ? 533  GLN A CG  1 
ATOM   4387  C  CD  . GLN A 1 533  ? 88.818  133.505 112.113 1.00 103.25 ? 533  GLN A CD  1 
ATOM   4388  O  OE1 . GLN A 1 533  ? 87.913  133.577 112.943 1.00 107.54 ? 533  GLN A OE1 1 
ATOM   4389  N  NE2 . GLN A 1 533  ? 89.319  132.349 111.697 1.00 96.44  ? 533  GLN A NE2 1 
ATOM   4390  N  N   . ILE A 1 534  ? 91.715  133.997 113.625 1.00 82.83  ? 534  ILE A N   1 
ATOM   4391  C  CA  . ILE A 1 534  ? 92.204  132.878 114.432 1.00 76.39  ? 534  ILE A CA  1 
ATOM   4392  C  C   . ILE A 1 534  ? 92.950  133.400 115.649 1.00 72.41  ? 534  ILE A C   1 
ATOM   4393  O  O   . ILE A 1 534  ? 92.792  132.881 116.767 1.00 79.99  ? 534  ILE A O   1 
ATOM   4394  C  CB  . ILE A 1 534  ? 93.091  131.926 113.606 1.00 65.47  ? 534  ILE A CB  1 
ATOM   4395  C  CG1 . ILE A 1 534  ? 92.337  131.371 112.400 1.00 84.84  ? 534  ILE A CG1 1 
ATOM   4396  C  CG2 . ILE A 1 534  ? 93.605  130.785 114.484 1.00 56.78  ? 534  ILE A CG2 1 
ATOM   4397  C  CD1 . ILE A 1 534  ? 93.195  130.501 111.504 1.00 80.67  ? 534  ILE A CD1 1 
ATOM   4398  N  N   . LEU A 1 535  ? 93.798  134.419 115.452 1.00 81.18  ? 535  LEU A N   1 
ATOM   4399  C  CA  . LEU A 1 535  ? 94.487  134.972 116.612 1.00 73.44  ? 535  LEU A CA  1 
ATOM   4400  C  C   . LEU A 1 535  ? 93.487  135.468 117.645 1.00 75.90  ? 535  LEU A C   1 
ATOM   4401  O  O   . LEU A 1 535  ? 93.621  135.166 118.833 1.00 85.69  ? 535  LEU A O   1 
ATOM   4402  C  CB  . LEU A 1 535  ? 95.434  136.096 116.198 1.00 92.13  ? 535  LEU A CB  1 
ATOM   4403  C  CG  . LEU A 1 535  ? 96.831  135.632 115.800 1.00 79.94  ? 535  LEU A CG  1 
ATOM   4404  C  CD1 . LEU A 1 535  ? 97.674  136.810 115.353 1.00 97.61  ? 535  LEU A CD1 1 
ATOM   4405  C  CD2 . LEU A 1 535  ? 97.477  134.923 116.984 1.00 81.99  ? 535  LEU A CD2 1 
ATOM   4406  N  N   . GLU A 1 536  ? 92.443  136.174 117.203 1.00 80.95  ? 536  GLU A N   1 
ATOM   4407  C  CA  . GLU A 1 536  ? 91.449  136.685 118.140 1.00 91.74  ? 536  GLU A CA  1 
ATOM   4408  C  C   . GLU A 1 536  ? 90.709  135.547 118.821 1.00 89.42  ? 536  GLU A C   1 
ATOM   4409  O  O   . GLU A 1 536  ? 90.336  135.655 119.995 1.00 91.72  ? 536  GLU A O   1 
ATOM   4410  C  CB  . GLU A 1 536  ? 90.470  137.616 117.429 1.00 108.35 ? 536  GLU A CB  1 
ATOM   4411  C  CG  . GLU A 1 536  ? 89.657  138.440 118.399 1.00 126.85 ? 536  GLU A CG  1 
ATOM   4412  C  CD  . GLU A 1 536  ? 90.478  139.543 119.027 1.00 138.27 ? 536  GLU A CD  1 
ATOM   4413  O  OE1 . GLU A 1 536  ? 91.457  139.987 118.393 1.00 125.77 ? 536  GLU A OE1 1 
ATOM   4414  O  OE2 . GLU A 1 536  ? 90.160  139.948 120.164 1.00 136.01 ? 536  GLU A OE2 1 
ATOM   4415  N  N   . PHE A 1 537  ? 90.480  134.456 118.090 1.00 82.17  ? 537  PHE A N   1 
ATOM   4416  C  CA  . PHE A 1 537  ? 89.787  133.302 118.646 1.00 77.64  ? 537  PHE A CA  1 
ATOM   4417  C  C   . PHE A 1 537  ? 90.585  132.740 119.815 1.00 79.62  ? 537  PHE A C   1 
ATOM   4418  O  O   . PHE A 1 537  ? 90.033  132.420 120.874 1.00 82.17  ? 537  PHE A O   1 
ATOM   4419  C  CB  . PHE A 1 537  ? 89.600  132.265 117.533 1.00 71.61  ? 537  PHE A CB  1 
ATOM   4420  C  CG  . PHE A 1 537  ? 88.840  131.039 117.943 1.00 68.52  ? 537  PHE A CG  1 
ATOM   4421  C  CD1 . PHE A 1 537  ? 87.466  131.084 118.107 1.00 86.44  ? 537  PHE A CD1 1 
ATOM   4422  C  CD2 . PHE A 1 537  ? 89.490  129.831 118.127 1.00 77.40  ? 537  PHE A CD2 1 
ATOM   4423  C  CE1 . PHE A 1 537  ? 86.758  129.953 118.469 1.00 82.65  ? 537  PHE A CE1 1 
ATOM   4424  C  CE2 . PHE A 1 537  ? 88.787  128.696 118.490 1.00 78.60  ? 537  PHE A CE2 1 
ATOM   4425  C  CZ  . PHE A 1 537  ? 87.420  128.759 118.661 1.00 65.01  ? 537  PHE A CZ  1 
ATOM   4426  N  N   . ALA A 1 538  ? 91.902  132.616 119.627 1.00 89.72  ? 538  ALA A N   1 
ATOM   4427  C  CA  . ALA A 1 538  ? 92.788  132.132 120.687 1.00 57.63  ? 538  ALA A CA  1 
ATOM   4428  C  C   . ALA A 1 538  ? 92.911  133.124 121.848 1.00 66.62  ? 538  ALA A C   1 
ATOM   4429  O  O   . ALA A 1 538  ? 92.893  132.719 123.017 1.00 74.31  ? 538  ALA A O   1 
ATOM   4430  C  CB  . ALA A 1 538  ? 94.165  131.807 120.111 1.00 58.56  ? 538  ALA A CB  1 
ATOM   4431  N  N   . GLU A 1 539  ? 93.023  134.427 121.549 1.00 85.74  ? 539  GLU A N   1 
ATOM   4432  C  CA  . GLU A 1 539  ? 93.199  135.438 122.596 1.00 81.28  ? 539  GLU A CA  1 
ATOM   4433  C  C   . GLU A 1 539  ? 92.009  135.505 123.542 1.00 83.68  ? 539  GLU A C   1 
ATOM   4434  O  O   . GLU A 1 539  ? 92.182  135.681 124.754 1.00 91.75  ? 539  GLU A O   1 
ATOM   4435  C  CB  . GLU A 1 539  ? 93.385  136.835 121.983 1.00 101.56 ? 539  GLU A CB  1 
ATOM   4436  C  CG  . GLU A 1 539  ? 94.444  137.039 120.912 1.00 111.86 ? 539  GLU A CG  1 
ATOM   4437  C  CD  . GLU A 1 539  ? 95.824  136.630 121.348 1.00 106.53 ? 539  GLU A CD  1 
ATOM   4438  O  OE1 . GLU A 1 539  ? 96.648  136.270 120.482 1.00 99.47  ? 539  GLU A OE1 1 
ATOM   4439  O  OE2 . GLU A 1 539  ? 96.113  136.757 122.550 1.00 99.89  ? 539  GLU A OE2 1 
ATOM   4440  N  N   . LYS A 1 540  ? 90.801  135.366 123.016 1.00 81.69  ? 540  LYS A N   1 
ATOM   4441  C  CA  . LYS A 1 540  ? 89.605  135.466 123.835 1.00 86.33  ? 540  LYS A CA  1 
ATOM   4442  C  C   . LYS A 1 540  ? 89.215  134.156 124.509 1.00 88.43  ? 540  LYS A C   1 
ATOM   4443  O  O   . LYS A 1 540  ? 88.240  134.138 125.266 1.00 91.84  ? 540  LYS A O   1 
ATOM   4444  C  CB  . LYS A 1 540  ? 88.444  135.953 122.960 1.00 108.39 ? 540  LYS A CB  1 
ATOM   4445  C  CG  . LYS A 1 540  ? 88.547  137.419 122.562 1.00 109.11 ? 540  LYS A CG  1 
ATOM   4446  C  CD  . LYS A 1 540  ? 88.467  138.355 123.744 1.00 114.06 ? 540  LYS A CD  1 
ATOM   4447  C  CE  . LYS A 1 540  ? 88.423  139.801 123.279 1.00 116.73 ? 540  LYS A CE  1 
ATOM   4448  N  NZ  . LYS A 1 540  ? 88.436  140.751 124.423 1.00 132.22 ? 540  LYS A NZ  1 
ATOM   4449  N  N   . LEU A 1 541  ? 89.952  133.066 124.260 1.00 80.95  ? 541  LEU A N   1 
ATOM   4450  C  CA  . LEU A 1 541  ? 89.651  131.748 124.834 1.00 72.61  ? 541  LEU A CA  1 
ATOM   4451  C  C   . LEU A 1 541  ? 88.237  131.321 124.463 1.00 67.86  ? 541  LEU A C   1 
ATOM   4452  O  O   . LEU A 1 541  ? 87.487  130.774 125.270 1.00 74.46  ? 541  LEU A O   1 
ATOM   4453  C  CB  . LEU A 1 541  ? 89.856  131.703 126.347 1.00 68.44  ? 541  LEU A CB  1 
ATOM   4454  C  CG  . LEU A 1 541  ? 91.209  132.042 126.972 1.00 77.60  ? 541  LEU A CG  1 
ATOM   4455  C  CD1 . LEU A 1 541  ? 91.398  133.532 127.190 1.00 107.93 ? 541  LEU A CD1 1 
ATOM   4456  C  CD2 . LEU A 1 541  ? 91.309  131.294 128.292 1.00 77.00  ? 541  LEU A CD2 1 
ATOM   4457  N  N   . GLU A 1 542  ? 87.868  131.593 123.206 1.00 67.25  ? 542  GLU A N   1 
ATOM   4458  C  CA  . GLU A 1 542  ? 86.546  131.241 122.703 1.00 77.50  ? 542  GLU A CA  1 
ATOM   4459  C  C   . GLU A 1 542  ? 86.332  129.734 122.682 1.00 78.87  ? 542  GLU A C   1 
ATOM   4460  O  O   . GLU A 1 542  ? 85.204  129.271 122.878 1.00 85.88  ? 542  GLU A O   1 
ATOM   4461  C  CB  . GLU A 1 542  ? 86.327  131.885 121.338 1.00 95.05  ? 542  GLU A CB  1 
ATOM   4462  C  CG  . GLU A 1 542  ? 86.252  133.402 121.457 1.00 102.20 ? 542  GLU A CG  1 
ATOM   4463  C  CD  . GLU A 1 542  ? 85.774  134.080 120.197 1.00 119.06 ? 542  GLU A CD  1 
ATOM   4464  O  OE1 . GLU A 1 542  ? 85.099  133.418 119.383 1.00 128.18 ? 542  GLU A OE1 1 
ATOM   4465  O  OE2 . GLU A 1 542  ? 86.063  135.285 120.029 1.00 113.67 ? 542  GLU A OE2 1 
ATOM   4466  N  N   . TYR A 1 543  ? 87.392  128.957 122.442 1.00 73.81  ? 543  TYR A N   1 
ATOM   4467  C  CA  . TYR A 1 543  ? 87.251  127.505 122.377 1.00 75.89  ? 543  TYR A CA  1 
ATOM   4468  C  C   . TYR A 1 543  ? 86.694  126.919 123.672 1.00 75.78  ? 543  TYR A C   1 
ATOM   4469  O  O   . TYR A 1 543  ? 85.961  125.925 123.624 1.00 83.35  ? 543  TYR A O   1 
ATOM   4470  C  CB  . TYR A 1 543  ? 88.581  126.847 121.996 1.00 69.48  ? 543  TYR A CB  1 
ATOM   4471  C  CG  . TYR A 1 543  ? 89.797  127.319 122.764 1.00 68.69  ? 543  TYR A CG  1 
ATOM   4472  C  CD1 . TYR A 1 543  ? 90.160  126.743 123.973 1.00 84.20  ? 543  TYR A CD1 1 
ATOM   4473  C  CD2 . TYR A 1 543  ? 90.603  128.327 122.253 1.00 63.90  ? 543  TYR A CD2 1 
ATOM   4474  C  CE1 . TYR A 1 543  ? 91.284  127.176 124.663 1.00 73.04  ? 543  TYR A CE1 1 
ATOM   4475  C  CE2 . TYR A 1 543  ? 91.724  128.764 122.932 1.00 80.56  ? 543  TYR A CE2 1 
ATOM   4476  C  CZ  . TYR A 1 543  ? 92.061  128.188 124.135 1.00 67.43  ? 543  TYR A CZ  1 
ATOM   4477  O  OH  . TYR A 1 543  ? 93.179  128.629 124.808 1.00 63.31  ? 543  TYR A OH  1 
ATOM   4478  N  N   . LEU A 1 544  ? 87.037  127.481 124.834 1.00 74.87  ? 544  LEU A N   1 
ATOM   4479  C  CA  . LEU A 1 544  ? 86.516  126.951 126.095 1.00 75.77  ? 544  LEU A CA  1 
ATOM   4480  C  C   . LEU A 1 544  ? 84.988  126.944 126.156 1.00 80.13  ? 544  LEU A C   1 
ATOM   4481  O  O   . LEU A 1 544  ? 84.410  126.565 127.182 1.00 78.40  ? 544  LEU A O   1 
ATOM   4482  C  CB  . LEU A 1 544  ? 87.059  127.750 127.283 1.00 62.73  ? 544  LEU A CB  1 
ATOM   4483  C  CG  . LEU A 1 544  ? 88.546  127.630 127.599 1.00 70.83  ? 544  LEU A CG  1 
ATOM   4484  C  CD1 . LEU A 1 544  ? 88.812  128.115 129.013 1.00 71.03  ? 544  LEU A CD1 1 
ATOM   4485  C  CD2 . LEU A 1 544  ? 88.983  126.182 127.439 1.00 65.15  ? 544  LEU A CD2 1 
ATOM   4486  N  N   . ALA A 1 545  ? 84.324  127.340 125.071 1.00 81.51  ? 545  ALA A N   1 
ATOM   4487  C  CA  . ALA A 1 545  ? 82.877  127.250 124.992 1.00 68.66  ? 545  ALA A CA  1 
ATOM   4488  C  C   . ALA A 1 545  ? 82.432  125.787 124.980 1.00 72.49  ? 545  ALA A C   1 
ATOM   4489  O  O   . ALA A 1 545  ? 83.185  124.906 124.556 1.00 82.98  ? 545  ALA A O   1 
ATOM   4490  C  CB  . ALA A 1 545  ? 82.373  127.962 123.738 1.00 75.93  ? 545  ALA A CB  1 
ATOM   4491  N  N   . PRO A 1 546  ? 81.209  125.503 125.440 1.00 74.30  ? 546  PRO A N   1 
ATOM   4492  C  CA  . PRO A 1 546  ? 80.779  124.096 125.554 1.00 80.11  ? 546  PRO A CA  1 
ATOM   4493  C  C   . PRO A 1 546  ? 80.708  123.356 124.227 1.00 73.89  ? 546  PRO A C   1 
ATOM   4494  O  O   . PRO A 1 546  ? 80.707  122.119 124.228 1.00 78.23  ? 546  PRO A O   1 
ATOM   4495  C  CB  . PRO A 1 546  ? 79.389  124.209 126.195 1.00 93.51  ? 546  PRO A CB  1 
ATOM   4496  C  CG  . PRO A 1 546  ? 79.376  125.550 126.862 1.00 99.70  ? 546  PRO A CG  1 
ATOM   4497  C  CD  . PRO A 1 546  ? 80.200  126.431 125.977 1.00 78.41  ? 546  PRO A CD  1 
ATOM   4498  N  N   . SER A 1 547  ? 80.639  124.067 123.101 1.00 79.25  ? 547  SER A N   1 
ATOM   4499  C  CA  . SER A 1 547  ? 80.496  123.413 121.804 1.00 82.25  ? 547  SER A CA  1 
ATOM   4500  C  C   . SER A 1 547  ? 81.779  122.745 121.323 1.00 80.95  ? 547  SER A C   1 
ATOM   4501  O  O   . SER A 1 547  ? 81.708  121.815 120.513 1.00 79.27  ? 547  SER A O   1 
ATOM   4502  C  CB  . SER A 1 547  ? 80.020  124.418 120.755 1.00 84.71  ? 547  SER A CB  1 
ATOM   4503  O  OG  . SER A 1 547  ? 80.192  123.898 119.447 1.00 89.52  ? 547  SER A OG  1 
ATOM   4504  N  N   . TYR A 1 548  ? 82.942  123.182 121.811 1.00 75.51  ? 548  TYR A N   1 
ATOM   4505  C  CA  . TYR A 1 548  ? 84.240  122.742 121.307 1.00 71.06  ? 548  TYR A CA  1 
ATOM   4506  C  C   . TYR A 1 548  ? 85.000  121.848 122.285 1.00 73.93  ? 548  TYR A C   1 
ATOM   4507  O  O   . TYR A 1 548  ? 86.231  121.884 122.332 1.00 73.50  ? 548  TYR A O   1 
ATOM   4508  C  CB  . TYR A 1 548  ? 85.099  123.944 120.919 1.00 64.91  ? 548  TYR A CB  1 
ATOM   4509  C  CG  . TYR A 1 548  ? 84.409  124.910 119.984 1.00 72.28  ? 548  TYR A CG  1 
ATOM   4510  C  CD1 . TYR A 1 548  ? 84.362  124.665 118.620 1.00 77.06  ? 548  TYR A CD1 1 
ATOM   4511  C  CD2 . TYR A 1 548  ? 83.816  126.069 120.461 1.00 76.88  ? 548  TYR A CD2 1 
ATOM   4512  C  CE1 . TYR A 1 548  ? 83.734  125.541 117.756 1.00 80.37  ? 548  TYR A CE1 1 
ATOM   4513  C  CE2 . TYR A 1 548  ? 83.185  126.955 119.603 1.00 78.20  ? 548  TYR A CE2 1 
ATOM   4514  C  CZ  . TYR A 1 548  ? 83.149  126.685 118.251 1.00 80.28  ? 548  TYR A CZ  1 
ATOM   4515  O  OH  . TYR A 1 548  ? 82.523  127.559 117.391 1.00 85.88  ? 548  TYR A OH  1 
ATOM   4516  N  N   . ARG A 1 549  ? 84.286  121.044 123.068 1.00 78.01  ? 549  ARG A N   1 
ATOM   4517  C  CA  . ARG A 1 549  ? 84.920  120.225 124.093 1.00 59.41  ? 549  ARG A CA  1 
ATOM   4518  C  C   . ARG A 1 549  ? 84.817  118.745 123.756 1.00 68.84  ? 549  ARG A C   1 
ATOM   4519  O  O   . ARG A 1 549  ? 84.452  117.925 124.605 1.00 77.03  ? 549  ARG A O   1 
ATOM   4520  C  CB  . ARG A 1 549  ? 84.318  120.507 125.467 1.00 53.82  ? 549  ARG A CB  1 
ATOM   4521  C  CG  . ARG A 1 549  ? 84.772  121.826 126.036 1.00 64.92  ? 549  ARG A CG  1 
ATOM   4522  C  CD  . ARG A 1 549  ? 84.347  121.982 127.475 1.00 59.58  ? 549  ARG A CD  1 
ATOM   4523  N  NE  . ARG A 1 549  ? 84.222  123.390 127.826 1.00 67.97  ? 549  ARG A NE  1 
ATOM   4524  C  CZ  . ARG A 1 549  ? 83.453  123.850 128.804 1.00 69.74  ? 549  ARG A CZ  1 
ATOM   4525  N  NH1 . ARG A 1 549  ? 82.734  123.011 129.537 1.00 70.93  ? 549  ARG A NH1 1 
ATOM   4526  N  NH2 . ARG A 1 549  ? 83.404  125.151 129.049 1.00 71.24  ? 549  ARG A NH2 1 
ATOM   4527  N  N   . ASN A 1 550  ? 85.119  118.401 122.509 1.00 63.59  ? 550  ASN A N   1 
ATOM   4528  C  CA  . ASN A 1 550  ? 85.131  117.023 122.047 1.00 58.02  ? 550  ASN A CA  1 
ATOM   4529  C  C   . ASN A 1 550  ? 86.514  116.653 121.536 1.00 68.17  ? 550  ASN A C   1 
ATOM   4530  O  O   . ASN A 1 550  ? 87.161  117.441 120.839 1.00 86.30  ? 550  ASN A O   1 
ATOM   4531  C  CB  . ASN A 1 550  ? 84.112  116.805 120.927 1.00 60.59  ? 550  ASN A CB  1 
ATOM   4532  C  CG  . ASN A 1 550  ? 83.784  115.343 120.720 1.00 70.57  ? 550  ASN A CG  1 
ATOM   4533  O  OD1 . ASN A 1 550  ? 83.630  114.588 121.678 1.00 78.19  ? 550  ASN A OD1 1 
ATOM   4534  N  ND2 . ASN A 1 550  ? 83.708  114.927 119.461 1.00 68.80  ? 550  ASN A ND2 1 
ATOM   4535  N  N   . PHE A 1 551  ? 86.969  115.456 121.894 1.00 60.77  ? 551  PHE A N   1 
ATOM   4536  C  CA  . PHE A 1 551  ? 88.247  114.962 121.410 1.00 58.28  ? 551  PHE A CA  1 
ATOM   4537  C  C   . PHE A 1 551  ? 88.097  113.459 121.216 1.00 74.69  ? 551  PHE A C   1 
ATOM   4538  O  O   . PHE A 1 551  ? 87.514  112.783 122.068 1.00 79.90  ? 551  PHE A O   1 
ATOM   4539  C  CB  . PHE A 1 551  ? 89.383  115.273 122.394 1.00 63.48  ? 551  PHE A CB  1 
ATOM   4540  C  CG  . PHE A 1 551  ? 90.710  114.751 121.951 1.00 92.66  ? 551  PHE A CG  1 
ATOM   4541  C  CD1 . PHE A 1 551  ? 91.077  113.437 122.152 1.00 88.72  ? 551  PHE A CD1 1 
ATOM   4542  C  CD2 . PHE A 1 551  ? 91.600  115.601 121.324 1.00 85.43  ? 551  PHE A CD2 1 
ATOM   4543  C  CE1 . PHE A 1 551  ? 92.298  112.979 121.716 1.00 90.23  ? 551  PHE A CE1 1 
ATOM   4544  C  CE2 . PHE A 1 551  ? 92.821  115.152 120.893 1.00 75.44  ? 551  PHE A CE2 1 
ATOM   4545  C  CZ  . PHE A 1 551  ? 93.166  113.839 121.079 1.00 86.61  ? 551  PHE A CZ  1 
ATOM   4546  N  N   . SER A 1 552  ? 88.622  112.928 120.108 1.00 59.98  ? 552  SER A N   1 
ATOM   4547  C  CA  . SER A 1 552  ? 88.500  111.502 119.843 1.00 50.36  ? 552  SER A CA  1 
ATOM   4548  C  C   . SER A 1 552  ? 89.780  110.937 119.242 1.00 56.14  ? 552  SER A C   1 
ATOM   4549  O  O   . SER A 1 552  ? 90.478  111.601 118.474 1.00 71.61  ? 552  SER A O   1 
ATOM   4550  C  CB  . SER A 1 552  ? 87.325  111.212 118.903 1.00 64.37  ? 552  SER A CB  1 
ATOM   4551  O  OG  . SER A 1 552  ? 87.648  111.533 117.562 1.00 76.57  ? 552  SER A OG  1 
ATOM   4552  N  N   . PHE A 1 553  ? 90.082  109.692 119.605 1.00 65.07  ? 553  PHE A N   1 
ATOM   4553  C  CA  . PHE A 1 553  ? 91.266  108.993 119.141 1.00 64.84  ? 553  PHE A CA  1 
ATOM   4554  C  C   . PHE A 1 553  ? 90.994  108.177 117.880 1.00 65.11  ? 553  PHE A C   1 
ATOM   4555  O  O   . PHE A 1 553  ? 89.849  107.927 117.495 1.00 64.97  ? 553  PHE A O   1 
ATOM   4556  C  CB  . PHE A 1 553  ? 91.828  108.039 120.183 1.00 66.20  ? 553  PHE A CB  1 
ATOM   4557  C  CG  . PHE A 1 553  ? 92.559  108.708 121.287 1.00 69.81  ? 553  PHE A CG  1 
ATOM   4558  C  CD1 . PHE A 1 553  ? 93.704  109.436 121.038 1.00 78.07  ? 553  PHE A CD1 1 
ATOM   4559  C  CD2 . PHE A 1 553  ? 92.195  108.465 122.595 1.00 69.89  ? 553  PHE A CD2 1 
ATOM   4560  C  CE1 . PHE A 1 553  ? 94.401  110.018 122.073 1.00 80.01  ? 553  PHE A CE1 1 
ATOM   4561  C  CE2 . PHE A 1 553  ? 92.894  109.017 123.631 1.00 66.35  ? 553  PHE A CE2 1 
ATOM   4562  C  CZ  . PHE A 1 553  ? 94.000  109.799 123.372 1.00 69.19  ? 553  PHE A CZ  1 
ATOM   4563  N  N   . SER A 1 554  ? 92.083  107.776 117.228 1.00 64.13  ? 554  SER A N   1 
ATOM   4564  C  CA  . SER A 1 554  ? 92.032  106.755 116.194 1.00 65.87  ? 554  SER A CA  1 
ATOM   4565  C  C   . SER A 1 554  ? 93.379  106.045 116.124 1.00 87.10  ? 554  SER A C   1 
ATOM   4566  O  O   . SER A 1 554  ? 94.425  106.624 116.437 1.00 93.65  ? 554  SER A O   1 
ATOM   4567  C  CB  . SER A 1 554  ? 91.659  107.342 114.837 1.00 87.23  ? 554  SER A CB  1 
ATOM   4568  O  OG  . SER A 1 554  ? 92.549  108.381 114.499 1.00 89.26  ? 554  SER A OG  1 
ATOM   4569  N  N   . LEU A 1 555  ? 93.338  104.782 115.715 1.00 76.55  ? 555  LEU A N   1 
ATOM   4570  C  CA  . LEU A 1 555  ? 94.484  103.892 115.786 1.00 77.63  ? 555  LEU A CA  1 
ATOM   4571  C  C   . LEU A 1 555  ? 95.273  103.902 114.478 1.00 91.61  ? 555  LEU A C   1 
ATOM   4572  O  O   . LEU A 1 555  ? 94.754  104.233 113.413 1.00 95.29  ? 555  LEU A O   1 
ATOM   4573  C  CB  . LEU A 1 555  ? 94.005  102.473 116.103 1.00 77.06  ? 555  LEU A CB  1 
ATOM   4574  C  CG  . LEU A 1 555  ? 93.217  102.378 117.411 1.00 77.79  ? 555  LEU A CG  1 
ATOM   4575  C  CD1 . LEU A 1 555  ? 92.557  101.016 117.557 1.00 79.30  ? 555  LEU A CD1 1 
ATOM   4576  C  CD2 . LEU A 1 555  ? 94.141  102.651 118.576 1.00 76.45  ? 555  LEU A CD2 1 
ATOM   4577  N  N   . LYS A 1 556  ? 96.550  103.527 114.572 1.00 76.25  ? 556  LYS A N   1 
ATOM   4578  C  CA  . LYS A 1 556  ? 97.438  103.611 113.426 1.00 81.50  ? 556  LYS A CA  1 
ATOM   4579  C  C   . LYS A 1 556  ? 97.467  102.291 112.668 1.00 86.30  ? 556  LYS A C   1 
ATOM   4580  O  O   . LYS A 1 556  ? 97.076  101.241 113.178 1.00 78.88  ? 556  LYS A O   1 
ATOM   4581  C  CB  . LYS A 1 556  ? 98.862  104.005 113.824 1.00 80.47  ? 556  LYS A CB  1 
ATOM   4582  C  CG  . LYS A 1 556  ? 99.025  105.459 114.205 1.00 88.19  ? 556  LYS A CG  1 
ATOM   4583  C  CD  . LYS A 1 556  ? 100.496 105.791 114.355 1.00 85.81  ? 556  LYS A CD  1 
ATOM   4584  C  CE  . LYS A 1 556  ? 100.701 107.229 114.778 1.00 95.43  ? 556  LYS A CE  1 
ATOM   4585  N  NZ  . LYS A 1 556  ? 102.149 107.554 114.851 1.00 102.22 ? 556  LYS A NZ  1 
ATOM   4586  N  N   . GLU A 1 557  ? 97.968  102.357 111.434 1.00 91.64  ? 557  GLU A N   1 
ATOM   4587  C  CA  . GLU A 1 557  ? 97.661  101.324 110.455 1.00 86.78  ? 557  GLU A CA  1 
ATOM   4588  C  C   . GLU A 1 557  ? 98.537  100.092 110.634 1.00 84.73  ? 557  GLU A C   1 
ATOM   4589  O  O   . GLU A 1 557  ? 98.037  99.005  110.942 1.00 94.16  ? 557  GLU A O   1 
ATOM   4590  C  CB  . GLU A 1 557  ? 97.819  101.863 109.027 1.00 93.22  ? 557  GLU A CB  1 
ATOM   4591  C  CG  . GLU A 1 557  ? 97.112  103.174 108.728 1.00 103.49 ? 557  GLU A CG  1 
ATOM   4592  C  CD  . GLU A 1 557  ? 97.927  104.385 109.138 1.00 118.65 ? 557  GLU A CD  1 
ATOM   4593  O  OE1 . GLU A 1 557  ? 98.991  104.206 109.767 1.00 111.68 ? 557  GLU A OE1 1 
ATOM   4594  O  OE2 . GLU A 1 557  ? 97.507  105.516 108.820 1.00 126.43 ? 557  GLU A OE2 1 
ATOM   4595  N  N   . LYS A 1 558  ? 99.849  100.240 110.458 1.00 76.85  ? 558  LYS A N   1 
ATOM   4596  C  CA  . LYS A 1 558  ? 100.721 99.084  110.263 1.00 76.33  ? 558  LYS A CA  1 
ATOM   4597  C  C   . LYS A 1 558  ? 101.865 99.070  111.275 1.00 87.55  ? 558  LYS A C   1 
ATOM   4598  O  O   . LYS A 1 558  ? 102.970 99.538  110.991 1.00 96.94  ? 558  LYS A O   1 
ATOM   4599  C  CB  . LYS A 1 558  ? 101.241 99.127  108.831 1.00 83.20  ? 558  LYS A CB  1 
ATOM   4600  C  CG  . LYS A 1 558  ? 100.170 98.821  107.797 1.00 91.16  ? 558  LYS A CG  1 
ATOM   4601  C  CD  . LYS A 1 558  ? 100.658 99.128  106.393 1.00 88.69  ? 558  LYS A CD  1 
ATOM   4602  C  CE  . LYS A 1 558  ? 101.828 98.251  106.011 1.00 98.48  ? 558  LYS A CE  1 
ATOM   4603  N  NZ  . LYS A 1 558  ? 101.398 96.833  105.881 1.00 96.49  ? 558  LYS A NZ  1 
ATOM   4604  N  N   . GLU A 1 559  ? 101.588 98.517  112.458 1.00 87.27  ? 559  GLU A N   1 
ATOM   4605  C  CA  . GLU A 1 559  ? 102.569 98.371  113.526 1.00 89.52  ? 559  GLU A CA  1 
ATOM   4606  C  C   . GLU A 1 559  ? 102.319 97.028  114.203 1.00 88.56  ? 559  GLU A C   1 
ATOM   4607  O  O   . GLU A 1 559  ? 101.368 96.314  113.870 1.00 87.21  ? 559  GLU A O   1 
ATOM   4608  C  CB  . GLU A 1 559  ? 102.497 99.526  114.532 1.00 102.06 ? 559  GLU A CB  1 
ATOM   4609  C  CG  . GLU A 1 559  ? 102.621 100.911 113.920 1.00 106.33 ? 559  GLU A CG  1 
ATOM   4610  C  CD  . GLU A 1 559  ? 102.353 102.009 114.924 1.00 105.86 ? 559  GLU A CD  1 
ATOM   4611  O  OE1 . GLU A 1 559  ? 103.086 103.020 114.912 1.00 112.60 ? 559  GLU A OE1 1 
ATOM   4612  O  OE2 . GLU A 1 559  ? 101.421 101.852 115.739 1.00 102.16 ? 559  GLU A OE2 1 
ATOM   4613  N  N   . LEU A 1 560  ? 103.170 96.680  115.174 1.00 88.78  ? 560  LEU A N   1 
ATOM   4614  C  CA  . LEU A 1 560  ? 103.066 95.396  115.863 1.00 76.24  ? 560  LEU A CA  1 
ATOM   4615  C  C   . LEU A 1 560  ? 102.820 95.525  117.364 1.00 78.31  ? 560  LEU A C   1 
ATOM   4616  O  O   . LEU A 1 560  ? 102.986 94.544  118.095 1.00 78.78  ? 560  LEU A O   1 
ATOM   4617  C  CB  . LEU A 1 560  ? 104.311 94.545  115.612 1.00 71.55  ? 560  LEU A CB  1 
ATOM   4618  C  CG  . LEU A 1 560  ? 104.757 94.347  114.164 1.00 62.97  ? 560  LEU A CG  1 
ATOM   4619  C  CD1 . LEU A 1 560  ? 105.806 93.255  114.108 1.00 64.15  ? 560  LEU A CD1 1 
ATOM   4620  C  CD2 . LEU A 1 560  ? 103.564 93.978  113.291 1.00 76.98  ? 560  LEU A CD2 1 
ATOM   4621  N  N   . ASN A 1 561  ? 102.418 96.695  117.847 1.00 81.35  ? 561  ASN A N   1 
ATOM   4622  C  CA  . ASN A 1 561  ? 102.182 96.871  119.270 1.00 78.66  ? 561  ASN A CA  1 
ATOM   4623  C  C   . ASN A 1 561  ? 100.684 96.778  119.551 1.00 87.09  ? 561  ASN A C   1 
ATOM   4624  O  O   . ASN A 1 561  ? 99.871  96.549  118.652 1.00 89.35  ? 561  ASN A O   1 
ATOM   4625  C  CB  . ASN A 1 561  ? 102.786 98.191  119.758 1.00 70.60  ? 561  ASN A CB  1 
ATOM   4626  C  CG  . ASN A 1 561  ? 102.537 99.338  118.801 1.00 81.90  ? 561  ASN A CG  1 
ATOM   4627  O  OD1 . ASN A 1 561  ? 101.518 99.380  118.113 1.00 90.05  ? 561  ASN A OD1 1 
ATOM   4628  N  ND2 . ASN A 1 561  ? 103.483 100.270 118.737 1.00 95.95  ? 561  ASN A ND2 1 
ATOM   4629  N  N   . ILE A 1 562  ? 100.310 96.985  120.817 1.00 90.21  ? 562  ILE A N   1 
ATOM   4630  C  CA  . ILE A 1 562  ? 98.908  96.869  121.204 1.00 78.96  ? 562  ILE A CA  1 
ATOM   4631  C  C   . ILE A 1 562  ? 98.068  98.027  120.698 1.00 86.36  ? 562  ILE A C   1 
ATOM   4632  O  O   . ILE A 1 562  ? 96.839  97.998  120.834 1.00 87.52  ? 562  ILE A O   1 
ATOM   4633  C  CB  . ILE A 1 562  ? 98.761  96.774  122.736 1.00 68.38  ? 562  ILE A CB  1 
ATOM   4634  C  CG1 . ILE A 1 562  ? 99.218  98.075  123.395 1.00 93.21  ? 562  ILE A CG1 1 
ATOM   4635  C  CG2 . ILE A 1 562  ? 99.557  95.594  123.275 1.00 80.27  ? 562  ILE A CG2 1 
ATOM   4636  C  CD1 . ILE A 1 562  ? 99.028  98.098  124.899 1.00 84.69  ? 562  ILE A CD1 1 
ATOM   4637  N  N   . GLY A 1 563  ? 98.695  99.042  120.121 1.00 88.70  ? 563  GLY A N   1 
ATOM   4638  C  CA  . GLY A 1 563  ? 97.960  100.126 119.512 1.00 76.78  ? 563  GLY A CA  1 
ATOM   4639  C  C   . GLY A 1 563  ? 98.490  101.490 119.884 1.00 83.38  ? 563  GLY A C   1 
ATOM   4640  O  O   . GLY A 1 563  ? 98.558  101.851 121.062 1.00 80.11  ? 563  GLY A O   1 
ATOM   4641  N  N   . ARG A 1 564  ? 98.860  102.264 118.872 1.00 78.23  ? 564  ARG A N   1 
ATOM   4642  C  CA  . ARG A 1 564  ? 99.264  103.646 119.049 1.00 76.93  ? 564  ARG A CA  1 
ATOM   4643  C  C   . ARG A 1 564  ? 98.195  104.557 118.476 1.00 90.44  ? 564  ARG A C   1 
ATOM   4644  O  O   . ARG A 1 564  ? 97.641  104.291 117.405 1.00 87.81  ? 564  ARG A O   1 
ATOM   4645  C  CB  . ARG A 1 564  ? 100.599 103.938 118.374 1.00 84.75  ? 564  ARG A CB  1 
ATOM   4646  C  CG  . ARG A 1 564  ? 101.787 103.255 118.996 1.00 92.49  ? 564  ARG A CG  1 
ATOM   4647  C  CD  . ARG A 1 564  ? 103.006 103.626 118.200 1.00 105.68 ? 564  ARG A CD  1 
ATOM   4648  N  NE  . ARG A 1 564  ? 103.293 105.051 118.324 1.00 106.32 ? 564  ARG A NE  1 
ATOM   4649  C  CZ  . ARG A 1 564  ? 104.203 105.690 117.599 1.00 125.99 ? 564  ARG A CZ  1 
ATOM   4650  N  NH1 . ARG A 1 564  ? 104.909 105.030 116.694 1.00 130.88 ? 564  ARG A NH1 1 
ATOM   4651  N  NH2 . ARG A 1 564  ? 104.399 106.991 117.772 1.00 132.85 ? 564  ARG A NH2 1 
ATOM   4652  N  N   . THR A 1 565  ? 97.914  105.634 119.194 1.00 91.95  ? 565  THR A N   1 
ATOM   4653  C  CA  . THR A 1 565  ? 96.800  106.506 118.875 1.00 85.78  ? 565  THR A CA  1 
ATOM   4654  C  C   . THR A 1 565  ? 97.318  107.830 118.333 1.00 92.11  ? 565  THR A C   1 
ATOM   4655  O  O   . THR A 1 565  ? 98.344  108.338 118.788 1.00 100.70 ? 565  THR A O   1 
ATOM   4656  C  CB  . THR A 1 565  ? 95.951  106.769 120.122 1.00 94.73  ? 565  THR A CB  1 
ATOM   4657  O  OG1 . THR A 1 565  ? 96.801  107.212 121.187 1.00 88.25  ? 565  THR A OG1 1 
ATOM   4658  C  CG2 . THR A 1 565  ? 95.248  105.497 120.566 1.00 81.81  ? 565  THR A CG2 1 
ATOM   4659  N  N   . PHE A 1 566  ? 96.606  108.380 117.357 1.00 84.90  ? 566  PHE A N   1 
ATOM   4660  C  CA  . PHE A 1 566  ? 96.727  109.783 117.001 1.00 84.77  ? 566  PHE A CA  1 
ATOM   4661  C  C   . PHE A 1 566  ? 95.360  110.432 117.156 1.00 76.34  ? 566  PHE A C   1 
ATOM   4662  O  O   . PHE A 1 566  ? 94.320  109.805 116.945 1.00 80.34  ? 566  PHE A O   1 
ATOM   4663  C  CB  . PHE A 1 566  ? 97.310  110.041 115.591 1.00 102.38 ? 566  PHE A CB  1 
ATOM   4664  C  CG  . PHE A 1 566  ? 96.479  109.509 114.462 1.00 101.75 ? 566  PHE A CG  1 
ATOM   4665  C  CD1 . PHE A 1 566  ? 96.727  108.238 113.966 1.00 102.59 ? 566  PHE A CD1 1 
ATOM   4666  C  CD2 . PHE A 1 566  ? 95.400  110.222 113.959 1.00 94.69  ? 566  PHE A CD2 1 
ATOM   4667  C  CE1 . PHE A 1 566  ? 95.970  107.716 112.936 1.00 99.53  ? 566  PHE A CE1 1 
ATOM   4668  C  CE2 . PHE A 1 566  ? 94.624  109.699 112.939 1.00 94.55  ? 566  PHE A CE2 1 
ATOM   4669  C  CZ  . PHE A 1 566  ? 94.908  108.444 112.429 1.00 106.03 ? 566  PHE A CZ  1 
ATOM   4670  N  N   . GLY A 1 567  ? 95.387  111.702 117.545 1.00 69.47  ? 567  GLY A N   1 
ATOM   4671  C  CA  . GLY A 1 567  ? 94.202  112.407 117.965 1.00 67.55  ? 567  GLY A CA  1 
ATOM   4672  C  C   . GLY A 1 567  ? 93.595  113.247 116.863 1.00 67.84  ? 567  GLY A C   1 
ATOM   4673  O  O   . GLY A 1 567  ? 94.256  113.619 115.897 1.00 83.11  ? 567  GLY A O   1 
ATOM   4674  N  N   . LYS A 1 568  ? 92.308  113.528 117.026 1.00 61.43  ? 568  LYS A N   1 
ATOM   4675  C  CA  . LYS A 1 568  ? 91.549  114.320 116.074 1.00 63.25  ? 568  LYS A CA  1 
ATOM   4676  C  C   . LYS A 1 568  ? 90.768  115.372 116.839 1.00 66.16  ? 568  LYS A C   1 
ATOM   4677  O  O   . LYS A 1 568  ? 90.079  115.055 117.814 1.00 74.34  ? 568  LYS A O   1 
ATOM   4678  C  CB  . LYS A 1 568  ? 90.592  113.443 115.267 1.00 66.18  ? 568  LYS A CB  1 
ATOM   4679  C  CG  . LYS A 1 568  ? 91.248  112.310 114.508 1.00 76.39  ? 568  LYS A CG  1 
ATOM   4680  C  CD  . LYS A 1 568  ? 90.188  111.496 113.794 1.00 73.63  ? 568  LYS A CD  1 
ATOM   4681  C  CE  . LYS A 1 568  ? 89.179  110.950 114.786 1.00 63.00  ? 568  LYS A CE  1 
ATOM   4682  N  NZ  . LYS A 1 568  ? 88.134  110.125 114.128 1.00 76.06  ? 568  LYS A NZ  1 
ATOM   4683  N  N   . LEU A 1 569  ? 90.866  116.608 116.386 1.00 62.88  ? 569  LEU A N   1 
ATOM   4684  C  CA  . LEU A 1 569  ? 90.271  117.761 117.032 1.00 59.59  ? 569  LEU A CA  1 
ATOM   4685  C  C   . LEU A 1 569  ? 89.137  118.339 116.206 1.00 73.48  ? 569  LEU A C   1 
ATOM   4686  O  O   . LEU A 1 569  ? 89.028  118.071 115.004 1.00 83.03  ? 569  LEU A O   1 
ATOM   4687  C  CB  . LEU A 1 569  ? 91.334  118.848 117.243 1.00 68.05  ? 569  LEU A CB  1 
ATOM   4688  C  CG  . LEU A 1 569  ? 92.453  118.530 118.222 1.00 72.87  ? 569  LEU A CG  1 
ATOM   4689  C  CD1 . LEU A 1 569  ? 93.554  119.566 118.113 1.00 80.32  ? 569  LEU A CD1 1 
ATOM   4690  C  CD2 . LEU A 1 569  ? 91.871  118.530 119.621 1.00 76.28  ? 569  LEU A CD2 1 
ATOM   4691  N  N   . PRO A 1 570  ? 88.254  119.124 116.822 1.00 69.29  ? 570  PRO A N   1 
ATOM   4692  C  CA  . PRO A 1 570  ? 87.265  119.858 116.031 1.00 74.15  ? 570  PRO A CA  1 
ATOM   4693  C  C   . PRO A 1 570  ? 87.988  120.782 115.065 1.00 85.95  ? 570  PRO A C   1 
ATOM   4694  O  O   . PRO A 1 570  ? 89.192  121.026 115.171 1.00 83.91  ? 570  PRO A O   1 
ATOM   4695  C  CB  . PRO A 1 570  ? 86.463  120.625 117.085 1.00 61.82  ? 570  PRO A CB  1 
ATOM   4696  C  CG  . PRO A 1 570  ? 86.585  119.777 118.314 1.00 61.12  ? 570  PRO A CG  1 
ATOM   4697  C  CD  . PRO A 1 570  ? 87.987  119.228 118.267 1.00 68.80  ? 570  PRO A CD  1 
ATOM   4698  N  N   . TYR A 1 571  ? 87.231  121.329 114.118 1.00 74.13  ? 571  TYR A N   1 
ATOM   4699  C  CA  . TYR A 1 571  ? 87.861  122.039 113.011 1.00 58.94  ? 571  TYR A CA  1 
ATOM   4700  C  C   . TYR A 1 571  ? 88.590  123.306 113.458 1.00 71.05  ? 571  TYR A C   1 
ATOM   4701  O  O   . TYR A 1 571  ? 89.749  123.534 113.078 1.00 94.19  ? 571  TYR A O   1 
ATOM   4702  C  CB  . TYR A 1 571  ? 86.806  122.367 111.960 1.00 73.29  ? 571  TYR A CB  1 
ATOM   4703  C  CG  . TYR A 1 571  ? 87.329  123.281 110.896 1.00 75.69  ? 571  TYR A CG  1 
ATOM   4704  C  CD1 . TYR A 1 571  ? 88.351  122.875 110.055 1.00 83.25  ? 571  TYR A CD1 1 
ATOM   4705  C  CD2 . TYR A 1 571  ? 86.808  124.555 110.733 1.00 86.12  ? 571  TYR A CD2 1 
ATOM   4706  C  CE1 . TYR A 1 571  ? 88.844  123.713 109.081 1.00 92.25  ? 571  TYR A CE1 1 
ATOM   4707  C  CE2 . TYR A 1 571  ? 87.292  125.401 109.759 1.00 86.61  ? 571  TYR A CE2 1 
ATOM   4708  C  CZ  . TYR A 1 571  ? 88.311  124.975 108.935 1.00 85.69  ? 571  TYR A CZ  1 
ATOM   4709  O  OH  . TYR A 1 571  ? 88.803  125.811 107.960 1.00 91.15  ? 571  TYR A OH  1 
ATOM   4710  N  N   . ARG A 1 572  ? 87.953  124.127 114.292 1.00 63.67  ? 572  ARG A N   1 
ATOM   4711  C  CA  . ARG A 1 572  ? 88.561  125.413 114.622 1.00 71.56  ? 572  ARG A CA  1 
ATOM   4712  C  C   . ARG A 1 572  ? 89.717  125.268 115.607 1.00 76.66  ? 572  ARG A C   1 
ATOM   4713  O  O   . ARG A 1 572  ? 90.723  125.989 115.500 1.00 83.74  ? 572  ARG A O   1 
ATOM   4714  C  CB  . ARG A 1 572  ? 87.487  126.366 115.137 1.00 60.12  ? 572  ARG A CB  1 
ATOM   4715  C  CG  . ARG A 1 572  ? 86.337  126.487 114.144 1.00 70.86  ? 572  ARG A CG  1 
ATOM   4716  C  CD  . ARG A 1 572  ? 85.210  127.357 114.645 1.00 92.25  ? 572  ARG A CD  1 
ATOM   4717  N  NE  . ARG A 1 572  ? 85.664  128.731 114.811 1.00 93.94  ? 572  ARG A NE  1 
ATOM   4718  C  CZ  . ARG A 1 572  ? 85.409  129.703 113.942 1.00 94.94  ? 572  ARG A CZ  1 
ATOM   4719  N  NH1 . ARG A 1 572  ? 84.708  129.447 112.846 1.00 98.10  ? 572  ARG A NH1 1 
ATOM   4720  N  NH2 . ARG A 1 572  ? 85.862  130.929 114.163 1.00 91.72  ? 572  ARG A NH2 1 
ATOM   4721  N  N   . VAL A 1 573  ? 89.621  124.321 116.543 1.00 68.15  ? 573  VAL A N   1 
ATOM   4722  C  CA  . VAL A 1 573  ? 90.775  124.031 117.385 1.00 62.22  ? 573  VAL A CA  1 
ATOM   4723  C  C   . VAL A 1 573  ? 91.920  123.482 116.545 1.00 74.22  ? 573  VAL A C   1 
ATOM   4724  O  O   . VAL A 1 573  ? 93.094  123.746 116.835 1.00 77.98  ? 573  VAL A O   1 
ATOM   4725  C  CB  . VAL A 1 573  ? 90.382  123.070 118.524 1.00 59.01  ? 573  VAL A CB  1 
ATOM   4726  C  CG1 . VAL A 1 573  ? 91.512  122.953 119.536 1.00 73.51  ? 573  VAL A CG1 1 
ATOM   4727  C  CG2 . VAL A 1 573  ? 89.105  123.549 119.205 1.00 57.04  ? 573  VAL A CG2 1 
ATOM   4728  N  N   . ARG A 1 574  ? 91.610  122.711 115.497 1.00 71.83  ? 574  ARG A N   1 
ATOM   4729  C  CA  . ARG A 1 574  ? 92.667  122.252 114.600 1.00 73.77  ? 574  ARG A CA  1 
ATOM   4730  C  C   . ARG A 1 574  ? 93.338  123.413 113.879 1.00 78.00  ? 574  ARG A C   1 
ATOM   4731  O  O   . ARG A 1 574  ? 94.561  123.407 113.684 1.00 84.29  ? 574  ARG A O   1 
ATOM   4732  C  CB  . ARG A 1 574  ? 92.117  121.232 113.602 1.00 69.76  ? 574  ARG A CB  1 
ATOM   4733  C  CG  . ARG A 1 574  ? 93.175  120.704 112.645 1.00 70.28  ? 574  ARG A CG  1 
ATOM   4734  C  CD  . ARG A 1 574  ? 94.277  119.946 113.364 1.00 107.57 ? 574  ARG A CD  1 
ATOM   4735  N  NE  . ARG A 1 574  ? 93.805  118.802 114.132 1.00 112.14 ? 574  ARG A NE  1 
ATOM   4736  C  CZ  . ARG A 1 574  ? 93.594  117.595 113.623 1.00 116.94 ? 574  ARG A CZ  1 
ATOM   4737  N  NH1 . ARG A 1 574  ? 93.816  117.365 112.336 1.00 134.44 ? 574  ARG A NH1 1 
ATOM   4738  N  NH2 . ARG A 1 574  ? 93.172  116.613 114.403 1.00 98.55  ? 574  ARG A NH2 1 
ATOM   4739  N  N   . ASN A 1 575  ? 92.560  124.424 113.486 1.00 71.36  ? 575  ASN A N   1 
ATOM   4740  C  CA  . ASN A 1 575  ? 93.174  125.614 112.905 1.00 64.94  ? 575  ASN A CA  1 
ATOM   4741  C  C   . ASN A 1 575  ? 94.113  126.287 113.899 1.00 64.28  ? 575  ASN A C   1 
ATOM   4742  O  O   . ASN A 1 575  ? 95.220  126.710 113.535 1.00 71.85  ? 575  ASN A O   1 
ATOM   4743  C  CB  . ASN A 1 575  ? 92.101  126.588 112.421 1.00 65.32  ? 575  ASN A CB  1 
ATOM   4744  C  CG  . ASN A 1 575  ? 91.619  126.263 111.026 1.00 82.50  ? 575  ASN A CG  1 
ATOM   4745  O  OD1 . ASN A 1 575  ? 90.467  125.886 110.823 1.00 83.41  ? 575  ASN A OD1 1 
ATOM   4746  N  ND2 . ASN A 1 575  ? 92.508  126.389 110.054 1.00 102.23 ? 575  ASN A ND2 1 
ATOM   4747  N  N   . VAL A 1 576  ? 93.683  126.397 115.160 1.00 66.65  ? 576  VAL A N   1 
ATOM   4748  C  CA  . VAL A 1 576  ? 94.535  127.008 116.181 1.00 58.83  ? 576  VAL A CA  1 
ATOM   4749  C  C   . VAL A 1 576  ? 95.834  126.226 116.345 1.00 64.53  ? 576  VAL A C   1 
ATOM   4750  O  O   . VAL A 1 576  ? 96.927  126.810 116.404 1.00 74.70  ? 576  VAL A O   1 
ATOM   4751  C  CB  . VAL A 1 576  ? 93.781  127.125 117.519 1.00 53.02  ? 576  VAL A CB  1 
ATOM   4752  C  CG1 . VAL A 1 576  ? 94.738  127.537 118.631 1.00 51.99  ? 576  VAL A CG1 1 
ATOM   4753  C  CG2 . VAL A 1 576  ? 92.650  128.131 117.405 1.00 63.37  ? 576  VAL A CG2 1 
ATOM   4754  N  N   . GLN A 1 577  ? 95.740  124.895 116.401 1.00 61.92  ? 577  GLN A N   1 
ATOM   4755  C  CA  . GLN A 1 577  ? 96.940  124.073 116.546 1.00 67.58  ? 577  GLN A CA  1 
ATOM   4756  C  C   . GLN A 1 577  ? 97.889  124.244 115.368 1.00 72.90  ? 577  GLN A C   1 
ATOM   4757  O  O   . GLN A 1 577  ? 99.106  124.398 115.550 1.00 87.98  ? 577  GLN A O   1 
ATOM   4758  C  CB  . GLN A 1 577  ? 96.567  122.598 116.659 1.00 60.33  ? 577  GLN A CB  1 
ATOM   4759  C  CG  . GLN A 1 577  ? 97.798  121.705 116.587 1.00 71.02  ? 577  GLN A CG  1 
ATOM   4760  C  CD  . GLN A 1 577  ? 97.520  120.367 115.943 1.00 82.13  ? 577  GLN A CD  1 
ATOM   4761  O  OE1 . GLN A 1 577  ? 96.370  119.960 115.795 1.00 83.66  ? 577  GLN A OE1 1 
ATOM   4762  N  NE2 . GLN A 1 577  ? 98.580  119.686 115.520 1.00 86.15  ? 577  GLN A NE2 1 
ATOM   4763  N  N   . THR A 1 578  ? 97.348  124.223 114.148 1.00 78.18  ? 578  THR A N   1 
ATOM   4764  C  CA  . THR A 1 578  ? 98.200  124.359 112.973 1.00 76.50  ? 578  THR A CA  1 
ATOM   4765  C  C   . THR A 1 578  ? 98.893  125.715 112.962 1.00 68.39  ? 578  THR A C   1 
ATOM   4766  O  O   . THR A 1 578  ? 100.092 125.803 112.670 1.00 70.23  ? 578  THR A O   1 
ATOM   4767  C  CB  . THR A 1 578  ? 97.392  124.140 111.692 1.00 70.64  ? 578  THR A CB  1 
ATOM   4768  O  OG1 . THR A 1 578  ? 96.925  122.786 111.656 1.00 76.75  ? 578  THR A OG1 1 
ATOM   4769  C  CG2 . THR A 1 578  ? 98.269  124.367 110.468 1.00 87.65  ? 578  THR A CG2 1 
ATOM   4770  N  N   . LEU A 1 579  ? 98.152  126.784 113.270 1.00 64.61  ? 579  LEU A N   1 
ATOM   4771  C  CA  . LEU A 1 579  ? 98.765  128.108 113.292 1.00 64.98  ? 579  LEU A CA  1 
ATOM   4772  C  C   . LEU A 1 579  ? 99.866  128.201 114.339 1.00 77.09  ? 579  LEU A C   1 
ATOM   4773  O  O   . LEU A 1 579  ? 100.950 128.735 114.060 1.00 84.50  ? 579  LEU A O   1 
ATOM   4774  C  CB  . LEU A 1 579  ? 97.703  129.169 113.562 1.00 65.33  ? 579  LEU A CB  1 
ATOM   4775  C  CG  . LEU A 1 579  ? 98.289  130.557 113.807 1.00 58.07  ? 579  LEU A CG  1 
ATOM   4776  C  CD1 . LEU A 1 579  ? 98.804  131.149 112.511 1.00 73.26  ? 579  LEU A CD1 1 
ATOM   4777  C  CD2 . LEU A 1 579  ? 97.276  131.475 114.476 1.00 60.19  ? 579  LEU A CD2 1 
ATOM   4778  N  N   . ALA A 1 580  ? 99.617  127.677 115.548 1.00 74.69  ? 580  ALA A N   1 
ATOM   4779  C  CA  . ALA A 1 580  ? 100.635 127.757 116.593 1.00 67.66  ? 580  ALA A CA  1 
ATOM   4780  C  C   . ALA A 1 580  ? 101.895 126.986 116.208 1.00 66.43  ? 580  ALA A C   1 
ATOM   4781  O  O   . ALA A 1 580  ? 103.013 127.503 116.334 1.00 72.02  ? 580  ALA A O   1 
ATOM   4782  C  CB  . ALA A 1 580  ? 100.077 127.239 117.917 1.00 58.80  ? 580  ALA A CB  1 
ATOM   4783  N  N   . GLU A 1 581  ? 101.744 125.772 115.686 1.00 67.37  ? 581  GLU A N   1 
ATOM   4784  C  CA  . GLU A 1 581  ? 102.931 125.012 115.303 1.00 64.58  ? 581  GLU A CA  1 
ATOM   4785  C  C   . GLU A 1 581  ? 103.676 125.663 114.128 1.00 75.76  ? 581  GLU A C   1 
ATOM   4786  O  O   . GLU A 1 581  ? 104.918 125.644 114.082 1.00 84.56  ? 581  GLU A O   1 
ATOM   4787  C  CB  . GLU A 1 581  ? 102.559 123.553 115.075 1.00 83.77  ? 581  GLU A CB  1 
ATOM   4788  C  CG  . GLU A 1 581  ? 103.609 122.827 114.352 1.00 114.01 ? 581  GLU A CG  1 
ATOM   4789  C  CD  . GLU A 1 581  ? 103.399 121.311 114.184 1.00 127.91 ? 581  GLU A CD  1 
ATOM   4790  O  OE1 . GLU A 1 581  ? 102.702 120.686 115.054 1.00 112.18 ? 581  GLU A OE1 1 
ATOM   4791  O  OE2 . GLU A 1 581  ? 103.763 120.871 113.011 1.00 128.39 ? 581  GLU A OE2 1 
ATOM   4792  N  N   . ALA A 1 582  ? 102.953 126.227 113.160 1.00 80.39  ? 582  ALA A N   1 
ATOM   4793  C  CA  . ALA A 1 582  ? 103.645 126.891 112.050 1.00 75.47  ? 582  ALA A CA  1 
ATOM   4794  C  C   . ALA A 1 582  ? 104.428 128.094 112.530 1.00 70.87  ? 582  ALA A C   1 
ATOM   4795  O  O   . ALA A 1 582  ? 105.577 128.307 112.111 1.00 83.35  ? 582  ALA A O   1 
ATOM   4796  C  CB  . ALA A 1 582  ? 102.677 127.327 110.963 1.00 76.51  ? 582  ALA A CB  1 
ATOM   4797  N  N   . LEU A 1 583  ? 103.815 128.889 113.411 1.00 71.92  ? 583  LEU A N   1 
ATOM   4798  C  CA  . LEU A 1 583  ? 104.472 130.057 113.980 1.00 66.42  ? 583  LEU A CA  1 
ATOM   4799  C  C   . LEU A 1 583  ? 105.742 129.661 114.697 1.00 71.12  ? 583  LEU A C   1 
ATOM   4800  O  O   . LEU A 1 583  ? 106.802 130.291 114.524 1.00 78.49  ? 583  LEU A O   1 
ATOM   4801  C  CB  . LEU A 1 583  ? 103.519 130.726 114.968 1.00 65.43  ? 583  LEU A CB  1 
ATOM   4802  C  CG  . LEU A 1 583  ? 102.510 131.704 114.380 1.00 79.48  ? 583  LEU A CG  1 
ATOM   4803  C  CD1 . LEU A 1 583  ? 101.868 132.610 115.453 1.00 77.52  ? 583  LEU A CD1 1 
ATOM   4804  C  CD2 . LEU A 1 583  ? 103.067 132.494 113.180 1.00 90.72  ? 583  LEU A CD2 1 
ATOM   4805  N  N   . LEU A 1 584  ? 105.656 128.583 115.474 1.00 79.46  ? 584  LEU A N   1 
ATOM   4806  C  CA  . LEU A 1 584  ? 106.823 128.109 116.220 1.00 71.22  ? 584  LEU A CA  1 
ATOM   4807  C  C   . LEU A 1 584  ? 107.912 127.606 115.289 1.00 72.66  ? 584  LEU A C   1 
ATOM   4808  O  O   . LEU A 1 584  ? 109.088 127.933 115.481 1.00 79.05  ? 584  LEU A O   1 
ATOM   4809  C  CB  . LEU A 1 584  ? 106.373 127.004 117.182 1.00 77.63  ? 584  LEU A CB  1 
ATOM   4810  C  CG  . LEU A 1 584  ? 107.193 126.893 118.465 1.00 72.45  ? 584  LEU A CG  1 
ATOM   4811  C  CD1 . LEU A 1 584  ? 107.022 128.194 119.225 1.00 65.77  ? 584  LEU A CD1 1 
ATOM   4812  C  CD2 . LEU A 1 584  ? 106.843 125.658 119.338 1.00 82.77  ? 584  LEU A CD2 1 
ATOM   4813  N  N   . ALA A 1 585  ? 107.526 126.851 114.262 1.00 81.11  ? 585  ALA A N   1 
ATOM   4814  C  CA  . ALA A 1 585  ? 108.522 126.272 113.353 1.00 93.07  ? 585  ALA A CA  1 
ATOM   4815  C  C   . ALA A 1 585  ? 109.235 127.325 112.518 1.00 91.04  ? 585  ALA A C   1 
ATOM   4816  O  O   . ALA A 1 585  ? 110.373 127.113 112.103 1.00 100.06 ? 585  ALA A O   1 
ATOM   4817  C  CB  . ALA A 1 585  ? 107.840 125.258 112.437 1.00 84.29  ? 585  ALA A CB  1 
ATOM   4818  N  N   . ASP A 1 586  ? 108.576 128.457 112.248 1.00 92.72  ? 586  ASP A N   1 
ATOM   4819  C  CA  . ASP A 1 586  ? 109.251 129.497 111.472 1.00 89.53  ? 586  ASP A CA  1 
ATOM   4820  C  C   . ASP A 1 586  ? 110.101 130.393 112.362 1.00 92.30  ? 586  ASP A C   1 
ATOM   4821  O  O   . ASP A 1 586  ? 111.282 130.622 112.077 1.00 103.71 ? 586  ASP A O   1 
ATOM   4822  C  CB  . ASP A 1 586  ? 108.244 130.318 110.666 1.00 110.29 ? 586  ASP A CB  1 
ATOM   4823  C  CG  . ASP A 1 586  ? 107.728 129.571 109.455 1.00 142.41 ? 586  ASP A CG  1 
ATOM   4824  O  OD1 . ASP A 1 586  ? 108.450 128.674 108.966 1.00 125.90 ? 586  ASP A OD1 1 
ATOM   4825  O  OD2 . ASP A 1 586  ? 106.618 129.887 108.982 1.00 139.75 ? 586  ASP A OD2 1 
ATOM   4826  N  N   . GLY A 1 587  ? 109.527 130.888 113.455 1.00 94.44  ? 587  GLY A N   1 
ATOM   4827  C  CA  . GLY A 1 587  ? 110.225 131.882 114.247 1.00 89.60  ? 587  GLY A CA  1 
ATOM   4828  C  C   . GLY A 1 587  ? 111.247 131.358 115.235 1.00 86.41  ? 587  GLY A C   1 
ATOM   4829  O  O   . GLY A 1 587  ? 112.442 131.641 115.102 1.00 88.19  ? 587  GLY A O   1 
ATOM   4830  N  N   . LEU A 1 588  ? 110.801 130.576 116.218 1.00 91.68  ? 588  LEU A N   1 
ATOM   4831  C  CA  . LEU A 1 588  ? 111.628 130.279 117.379 1.00 78.18  ? 588  LEU A CA  1 
ATOM   4832  C  C   . LEU A 1 588  ? 112.263 128.894 117.354 1.00 72.43  ? 588  LEU A C   1 
ATOM   4833  O  O   . LEU A 1 588  ? 113.304 128.701 117.993 1.00 81.88  ? 588  LEU A O   1 
ATOM   4834  C  CB  . LEU A 1 588  ? 110.799 130.445 118.660 1.00 86.76  ? 588  LEU A CB  1 
ATOM   4835  C  CG  . LEU A 1 588  ? 111.487 130.220 120.005 1.00 79.40  ? 588  LEU A CG  1 
ATOM   4836  C  CD1 . LEU A 1 588  ? 111.104 131.320 120.976 1.00 71.56  ? 588  LEU A CD1 1 
ATOM   4837  C  CD2 . LEU A 1 588  ? 111.110 128.855 120.566 1.00 87.82  ? 588  LEU A CD2 1 
ATOM   4838  N  N   . ALA A 1 589  ? 111.703 127.936 116.615 1.00 73.97  ? 589  ALA A N   1 
ATOM   4839  C  CA  . ALA A 1 589  ? 112.334 126.622 116.569 1.00 64.14  ? 589  ALA A CA  1 
ATOM   4840  C  C   . ALA A 1 589  ? 113.651 126.648 115.808 1.00 77.97  ? 589  ALA A C   1 
ATOM   4841  O  O   . ALA A 1 589  ? 114.382 125.652 115.826 1.00 88.82  ? 589  ALA A O   1 
ATOM   4842  C  CB  . ALA A 1 589  ? 111.386 125.597 115.940 1.00 86.48  ? 589  ALA A CB  1 
ATOM   4843  N  N   . LYS A 1 590  ? 113.971 127.768 115.155 1.00 91.86  ? 590  LYS A N   1 
ATOM   4844  C  CA  . LYS A 1 590  ? 115.218 127.886 114.413 1.00 100.28 ? 590  LYS A CA  1 
ATOM   4845  C  C   . LYS A 1 590  ? 116.421 128.051 115.330 1.00 86.04  ? 590  LYS A C   1 
ATOM   4846  O  O   . LYS A 1 590  ? 117.551 127.814 114.893 1.00 95.07  ? 590  LYS A O   1 
ATOM   4847  C  CB  . LYS A 1 590  ? 115.133 129.052 113.430 1.00 100.07 ? 590  LYS A CB  1 
ATOM   4848  C  CG  . LYS A 1 590  ? 114.389 128.695 112.157 1.00 103.91 ? 590  LYS A CG  1 
ATOM   4849  C  CD  . LYS A 1 590  ? 114.544 129.762 111.094 1.00 116.70 ? 590  LYS A CD  1 
ATOM   4850  C  CE  . LYS A 1 590  ? 113.827 129.349 109.821 1.00 122.54 ? 590  LYS A CE  1 
ATOM   4851  N  NZ  . LYS A 1 590  ? 114.077 127.917 109.492 1.00 119.47 ? 590  LYS A NZ  1 
ATOM   4852  N  N   . ALA A 1 591  ? 116.212 128.449 116.587 1.00 75.01  ? 591  ALA A N   1 
ATOM   4853  C  CA  . ALA A 1 591  ? 117.338 128.652 117.487 1.00 73.61  ? 591  ALA A CA  1 
ATOM   4854  C  C   . ALA A 1 591  ? 117.833 127.345 118.086 1.00 82.47  ? 591  ALA A C   1 
ATOM   4855  O  O   . ALA A 1 591  ? 118.851 127.344 118.788 1.00 71.31  ? 591  ALA A O   1 
ATOM   4856  C  CB  . ALA A 1 591  ? 116.958 129.624 118.606 1.00 57.20  ? 591  ALA A CB  1 
ATOM   4857  N  N   . PHE A 1 592  ? 117.140 126.243 117.826 1.00 93.75  ? 592  PHE A N   1 
ATOM   4858  C  CA  . PHE A 1 592  ? 117.463 124.940 118.403 1.00 94.29  ? 592  PHE A CA  1 
ATOM   4859  C  C   . PHE A 1 592  ? 117.838 123.972 117.293 1.00 106.31 ? 592  PHE A C   1 
ATOM   4860  O  O   . PHE A 1 592  ? 116.958 123.553 116.516 1.00 98.26  ? 592  PHE A O   1 
ATOM   4861  C  CB  . PHE A 1 592  ? 116.305 124.388 119.233 1.00 71.49  ? 592  PHE A CB  1 
ATOM   4862  C  CG  . PHE A 1 592  ? 115.977 125.226 120.429 1.00 67.52  ? 592  PHE A CG  1 
ATOM   4863  C  CD1 . PHE A 1 592  ? 115.082 126.277 120.336 1.00 83.25  ? 592  PHE A CD1 1 
ATOM   4864  C  CD2 . PHE A 1 592  ? 116.595 124.983 121.643 1.00 73.56  ? 592  PHE A CD2 1 
ATOM   4865  C  CE1 . PHE A 1 592  ? 114.793 127.057 121.441 1.00 70.17  ? 592  PHE A CE1 1 
ATOM   4866  C  CE2 . PHE A 1 592  ? 116.313 125.759 122.749 1.00 65.15  ? 592  PHE A CE2 1 
ATOM   4867  C  CZ  . PHE A 1 592  ? 115.410 126.797 122.647 1.00 68.64  ? 592  PHE A CZ  1 
ATOM   4868  N  N   . PRO A 1 593  ? 119.102 123.592 117.175 1.00 120.63 ? 593  PRO A N   1 
ATOM   4869  C  CA  . PRO A 1 593  ? 119.511 122.643 116.133 1.00 127.06 ? 593  PRO A CA  1 
ATOM   4870  C  C   . PRO A 1 593  ? 119.224 121.216 116.574 1.00 122.94 ? 593  PRO A C   1 
ATOM   4871  O  O   . PRO A 1 593  ? 119.883 120.681 117.470 1.00 114.46 ? 593  PRO A O   1 
ATOM   4872  C  CB  . PRO A 1 593  ? 121.016 122.916 115.994 1.00 136.47 ? 593  PRO A CB  1 
ATOM   4873  C  CG  . PRO A 1 593  ? 121.438 123.469 117.345 1.00 120.67 ? 593  PRO A CG  1 
ATOM   4874  C  CD  . PRO A 1 593  ? 120.203 123.904 118.103 1.00 106.83 ? 593  PRO A CD  1 
ATOM   4875  N  N   . SER A 1 594  ? 118.229 120.593 115.944 1.00 128.46 ? 594  SER A N   1 
ATOM   4876  C  CA  . SER A 1 594  ? 117.837 119.230 116.276 1.00 129.93 ? 594  SER A CA  1 
ATOM   4877  C  C   . SER A 1 594  ? 118.383 118.204 115.297 1.00 123.06 ? 594  SER A C   1 
ATOM   4878  O  O   . SER A 1 594  ? 118.105 117.009 115.452 1.00 114.56 ? 594  SER A O   1 
ATOM   4879  C  CB  . SER A 1 594  ? 116.310 119.123 116.325 1.00 136.77 ? 594  SER A CB  1 
ATOM   4880  O  OG  . SER A 1 594  ? 115.733 119.491 115.083 1.00 133.50 ? 594  SER A OG  1 
ATOM   4881  N  N   . ASN A 1 595  ? 119.155 118.638 114.308 1.00 119.44 ? 595  ASN A N   1 
ATOM   4882  C  CA  . ASN A 1 595  ? 119.753 117.758 113.310 1.00 120.94 ? 595  ASN A CA  1 
ATOM   4883  C  C   . ASN A 1 595  ? 121.185 118.184 113.052 1.00 131.83 ? 595  ASN A C   1 
ATOM   4884  O  O   . ASN A 1 595  ? 121.694 118.107 111.928 1.00 141.64 ? 595  ASN A O   1 
ATOM   4885  C  CB  . ASN A 1 595  ? 118.936 117.728 112.024 1.00 135.10 ? 595  ASN A CB  1 
ATOM   4886  C  CG  . ASN A 1 595  ? 117.800 116.716 112.083 1.00 137.53 ? 595  ASN A CG  1 
ATOM   4887  O  OD1 . ASN A 1 595  ? 117.818 115.796 112.908 1.00 126.74 ? 595  ASN A OD1 1 
ATOM   4888  N  ND2 . ASN A 1 595  ? 116.816 116.874 111.212 1.00 148.40 ? 595  ASN A ND2 1 
ATOM   4889  N  N   . MET A 1 596  ? 121.853 118.611 114.121 1.00 130.75 ? 596  MET A N   1 
ATOM   4890  C  CA  . MET A 1 596  ? 123.195 119.166 114.018 1.00 148.02 ? 596  MET A CA  1 
ATOM   4891  C  C   . MET A 1 596  ? 124.224 118.102 113.700 1.00 132.82 ? 596  MET A C   1 
ATOM   4892  O  O   . MET A 1 596  ? 125.383 118.406 113.442 1.00 125.72 ? 596  MET A O   1 
ATOM   4893  C  CB  . MET A 1 596  ? 123.547 119.881 115.307 1.00 131.78 ? 596  MET A CB  1 
ATOM   4894  C  CG  . MET A 1 596  ? 123.653 118.991 116.507 1.00 115.83 ? 596  MET A CG  1 
ATOM   4895  S  SD  . MET A 1 596  ? 124.080 120.167 117.791 1.00 141.48 ? 596  MET A SD  1 
ATOM   4896  C  CE  . MET A 1 596  ? 125.763 120.586 117.225 1.00 118.44 ? 596  MET A CE  1 
ATOM   4897  N  N   . MET A 1 597  ? 123.840 116.845 113.762 1.00 122.54 ? 597  MET A N   1 
ATOM   4898  C  CA  . MET A 1 597  ? 124.785 115.768 113.614 1.00 130.93 ? 597  MET A CA  1 
ATOM   4899  C  C   . MET A 1 597  ? 125.262 115.536 112.190 1.00 129.47 ? 597  MET A C   1 
ATOM   4900  O  O   . MET A 1 597  ? 124.547 115.708 111.203 1.00 125.57 ? 597  MET A O   1 
ATOM   4901  C  CB  . MET A 1 597  ? 124.116 114.484 114.078 1.00 137.81 ? 597  MET A CB  1 
ATOM   4902  C  CG  . MET A 1 597  ? 124.920 113.181 114.018 1.00 120.57 ? 597  MET A CG  1 
ATOM   4903  S  SD  . MET A 1 597  ? 126.451 112.766 114.819 1.00 114.37 ? 597  MET A SD  1 
ATOM   4904  C  CE  . MET A 1 597  ? 126.523 111.139 114.187 1.00 123.98 ? 597  MET A CE  1 
ATOM   4905  N  N   . VAL A 1 598  ? 126.527 115.124 112.119 1.00 136.79 ? 598  VAL A N   1 
ATOM   4906  C  CA  . VAL A 1 598  ? 127.081 114.400 110.988 1.00 140.45 ? 598  VAL A CA  1 
ATOM   4907  C  C   . VAL A 1 598  ? 127.904 113.255 111.582 1.00 150.13 ? 598  VAL A C   1 
ATOM   4908  O  O   . VAL A 1 598  ? 128.504 113.395 112.651 1.00 138.96 ? 598  VAL A O   1 
ATOM   4909  C  CB  . VAL A 1 598  ? 127.922 115.316 110.070 1.00 125.44 ? 598  VAL A CB  1 
ATOM   4910  C  CG1 . VAL A 1 598  ? 128.411 114.582 108.813 1.00 123.81 ? 598  VAL A CG1 1 
ATOM   4911  C  CG2 . VAL A 1 598  ? 127.165 116.588 109.676 1.00 114.89 ? 598  VAL A CG2 1 
ATOM   4912  N  N   . VAL A 1 599  ? 128.088 112.187 110.803 1.00 141.80 ? 599  VAL A N   1 
ATOM   4913  C  CA  . VAL A 1 599  ? 128.853 111.044 111.297 1.00 126.30 ? 599  VAL A CA  1 
ATOM   4914  C  C   . VAL A 1 599  ? 130.295 111.452 111.573 1.00 134.69 ? 599  VAL A C   1 
ATOM   4915  O  O   . VAL A 1 599  ? 130.997 111.955 110.687 1.00 141.11 ? 599  VAL A O   1 
ATOM   4916  C  CB  . VAL A 1 599  ? 128.771 109.868 110.314 1.00 119.12 ? 599  VAL A CB  1 
ATOM   4917  C  CG1 . VAL A 1 599  ? 129.685 108.748 110.757 1.00 107.60 ? 599  VAL A CG1 1 
ATOM   4918  C  CG2 . VAL A 1 599  ? 127.314 109.375 110.258 1.00 103.03 ? 599  VAL A CG2 1 
ATOM   4919  N  N   . THR A 1 600  ? 130.742 111.243 112.824 1.00 113.89 ? 600  THR A N   1 
ATOM   4920  C  CA  . THR A 1 600  ? 132.005 111.821 113.279 1.00 119.23 ? 600  THR A CA  1 
ATOM   4921  C  C   . THR A 1 600  ? 133.201 111.166 112.596 1.00 119.93 ? 600  THR A C   1 
ATOM   4922  O  O   . THR A 1 600  ? 134.232 111.821 112.395 1.00 127.34 ? 600  THR A O   1 
ATOM   4923  C  CB  . THR A 1 600  ? 132.129 111.682 114.802 1.00 111.70 ? 600  THR A CB  1 
ATOM   4924  O  OG1 . THR A 1 600  ? 132.269 110.303 115.159 1.00 118.25 ? 600  THR A OG1 1 
ATOM   4925  C  CG2 . THR A 1 600  ? 130.908 112.262 115.497 1.00 127.02 ? 600  THR A CG2 1 
ATOM   4926  N  N   . GLU A 1 601  ? 133.096 109.890 112.222 1.00 115.63 ? 601  GLU A N   1 
ATOM   4927  C  CA  . GLU A 1 601  ? 134.213 109.250 111.534 1.00 112.23 ? 601  GLU A CA  1 
ATOM   4928  C  C   . GLU A 1 601  ? 134.412 109.833 110.144 1.00 117.37 ? 601  GLU A C   1 
ATOM   4929  O  O   . GLU A 1 601  ? 135.486 109.667 109.555 1.00 114.35 ? 601  GLU A O   1 
ATOM   4930  C  CB  . GLU A 1 601  ? 134.006 107.738 111.429 1.00 102.14 ? 601  GLU A CB  1 
ATOM   4931  C  CG  . GLU A 1 601  ? 134.144 107.002 112.744 1.00 118.65 ? 601  GLU A CG  1 
ATOM   4932  C  CD  . GLU A 1 601  ? 132.819 106.849 113.457 1.00 129.86 ? 601  GLU A CD  1 
ATOM   4933  O  OE1 . GLU A 1 601  ? 132.734 106.013 114.378 1.00 111.74 ? 601  GLU A OE1 1 
ATOM   4934  O  OE2 . GLU A 1 601  ? 131.859 107.558 113.085 1.00 125.34 ? 601  GLU A OE2 1 
ATOM   4935  N  N   . ARG A 1 602  ? 133.397 110.514 109.618 1.00 121.59 ? 602  ARG A N   1 
ATOM   4936  C  CA  . ARG A 1 602  ? 133.451 111.138 108.306 1.00 117.63 ? 602  ARG A CA  1 
ATOM   4937  C  C   . ARG A 1 602  ? 133.718 112.635 108.364 1.00 124.10 ? 602  ARG A C   1 
ATOM   4938  O  O   . ARG A 1 602  ? 133.577 113.315 107.344 1.00 125.82 ? 602  ARG A O   1 
ATOM   4939  C  CB  . ARG A 1 602  ? 132.137 110.883 107.575 1.00 105.86 ? 602  ARG A CB  1 
ATOM   4940  C  CG  . ARG A 1 602  ? 131.936 109.435 107.246 1.00 96.76  ? 602  ARG A CG  1 
ATOM   4941  C  CD  . ARG A 1 602  ? 131.290 109.265 105.907 1.00 87.52  ? 602  ARG A CD  1 
ATOM   4942  N  NE  . ARG A 1 602  ? 130.986 107.865 105.670 1.00 63.18  ? 602  ARG A NE  1 
ATOM   4943  C  CZ  . ARG A 1 602  ? 130.235 107.430 104.672 1.00 68.11  ? 602  ARG A CZ  1 
ATOM   4944  N  NH1 . ARG A 1 602  ? 129.707 108.284 103.807 1.00 78.30  ? 602  ARG A NH1 1 
ATOM   4945  N  NH2 . ARG A 1 602  ? 130.008 106.140 104.544 1.00 75.20  ? 602  ARG A NH2 1 
ATOM   4946  N  N   . GLU A 1 603  ? 134.085 113.166 109.526 1.00 125.66 ? 603  GLU A N   1 
ATOM   4947  C  CA  . GLU A 1 603  ? 134.296 114.591 109.660 1.00 131.71 ? 603  GLU A CA  1 
ATOM   4948  C  C   . GLU A 1 603  ? 135.790 114.870 109.733 1.00 134.07 ? 603  GLU A C   1 
ATOM   4949  O  O   . GLU A 1 603  ? 136.578 114.048 110.231 1.00 133.24 ? 603  GLU A O   1 
ATOM   4950  C  CB  . GLU A 1 603  ? 133.595 115.127 110.913 1.00 120.86 ? 603  GLU A CB  1 
ATOM   4951  C  CG  . GLU A 1 603  ? 133.673 116.626 111.093 1.00 138.97 ? 603  GLU A CG  1 
ATOM   4952  C  CD  . GLU A 1 603  ? 132.918 117.365 110.002 1.00 151.75 ? 603  GLU A CD  1 
ATOM   4953  O  OE1 . GLU A 1 603  ? 131.971 116.778 109.437 1.00 139.68 ? 603  GLU A OE1 1 
ATOM   4954  O  OE2 . GLU A 1 603  ? 133.272 118.524 109.704 1.00 154.33 ? 603  GLU A OE2 1 
ATOM   4955  N  N   . GLN A 1 604  ? 136.180 116.032 109.207 1.00 132.99 ? 604  GLN A N   1 
ATOM   4956  C  CA  . GLN A 1 604  ? 137.591 116.420 109.186 1.00 139.10 ? 604  GLN A CA  1 
ATOM   4957  C  C   . GLN A 1 604  ? 138.148 116.629 110.595 1.00 144.89 ? 604  GLN A C   1 
ATOM   4958  O  O   . GLN A 1 604  ? 137.430 117.041 111.501 1.00 144.80 ? 604  GLN A O   1 
ATOM   4959  C  CB  . GLN A 1 604  ? 137.757 117.713 108.390 1.00 139.63 ? 604  GLN A CB  1 
ATOM   4960  C  CG  . GLN A 1 604  ? 139.180 118.014 107.931 1.00 149.93 ? 604  GLN A CG  1 
ATOM   4961  C  CD  . GLN A 1 604  ? 139.398 119.485 107.611 1.00 162.90 ? 604  GLN A CD  1 
ATOM   4962  O  OE1 . GLN A 1 604  ? 138.521 120.323 107.827 1.00 157.81 ? 604  GLN A OE1 1 
ATOM   4963  N  NE2 . GLN A 1 604  ? 140.583 119.806 107.104 1.00 166.55 ? 604  GLN A NE2 1 
ATOM   4964  N  N   . LYS A 1 605  ? 139.437 116.309 110.780 1.00 139.93 ? 605  LYS A N   1 
ATOM   4965  C  CA  . LYS A 1 605  ? 140.062 116.373 112.087 1.00 139.64 ? 605  LYS A CA  1 
ATOM   4966  C  C   . LYS A 1 605  ? 140.117 117.795 112.625 1.00 143.99 ? 605  LYS A C   1 
ATOM   4967  O  O   . LYS A 1 605  ? 139.925 118.012 113.816 1.00 142.49 ? 605  LYS A O   1 
ATOM   4968  C  CB  . LYS A 1 605  ? 141.455 115.754 111.985 1.00 143.31 ? 605  LYS A CB  1 
ATOM   4969  C  CG  . LYS A 1 605  ? 141.649 114.243 111.772 1.00 153.31 ? 605  LYS A CG  1 
ATOM   4970  C  CD  . LYS A 1 605  ? 143.187 114.267 111.791 1.00 163.74 ? 605  LYS A CD  1 
ATOM   4971  C  CE  . LYS A 1 605  ? 143.854 114.912 113.084 1.00 168.93 ? 605  LYS A CE  1 
ATOM   4972  N  NZ  . LYS A 1 605  ? 145.360 114.946 112.764 1.00 163.70 ? 605  LYS A NZ  1 
ATOM   4973  N  N   . GLU A 1 606  ? 140.407 118.793 111.770 1.00 149.58 ? 606  GLU A N   1 
ATOM   4974  C  CA  . GLU A 1 606  ? 140.468 120.166 112.291 1.00 151.16 ? 606  GLU A CA  1 
ATOM   4975  C  C   . GLU A 1 606  ? 139.112 120.601 112.842 1.00 142.32 ? 606  GLU A C   1 
ATOM   4976  O  O   . GLU A 1 606  ? 139.036 121.206 113.921 1.00 138.05 ? 606  GLU A O   1 
ATOM   4977  C  CB  . GLU A 1 606  ? 140.941 121.132 111.210 1.00 163.34 ? 606  GLU A CB  1 
ATOM   4978  C  CG  . GLU A 1 606  ? 142.440 121.156 111.037 1.00 165.89 ? 606  GLU A CG  1 
ATOM   4979  C  CD  . GLU A 1 606  ? 142.887 122.341 110.220 1.00 174.44 ? 606  GLU A CD  1 
ATOM   4980  O  OE1 . GLU A 1 606  ? 142.062 123.257 110.014 1.00 169.23 ? 606  GLU A OE1 1 
ATOM   4981  O  OE2 . GLU A 1 606  ? 144.055 122.356 109.782 1.00 176.91 ? 606  GLU A OE2 1 
ATOM   4982  N  N   . ALA A 1 607  ? 138.031 120.274 112.129 1.00 138.09 ? 607  ALA A N   1 
ATOM   4983  C  CA  . ALA A 1 607  ? 136.689 120.606 112.604 1.00 129.74 ? 607  ALA A CA  1 
ATOM   4984  C  C   . ALA A 1 607  ? 136.359 119.894 113.912 1.00 135.84 ? 607  ALA A C   1 
ATOM   4985  O  O   . ALA A 1 607  ? 135.762 120.491 114.815 1.00 141.29 ? 607  ALA A O   1 
ATOM   4986  C  CB  . ALA A 1 607  ? 135.659 120.260 111.531 1.00 129.04 ? 607  ALA A CB  1 
ATOM   4987  N  N   . LEU A 1 608  ? 136.740 118.620 114.033 1.00 135.44 ? 608  LEU A N   1 
ATOM   4988  C  CA  . LEU A 1 608  ? 136.501 117.883 115.271 1.00 124.37 ? 608  LEU A CA  1 
ATOM   4989  C  C   . LEU A 1 608  ? 137.266 118.498 116.435 1.00 131.82 ? 608  LEU A C   1 
ATOM   4990  O  O   . LEU A 1 608  ? 136.721 118.674 117.531 1.00 133.60 ? 608  LEU A O   1 
ATOM   4991  C  CB  . LEU A 1 608  ? 136.882 116.418 115.080 1.00 116.89 ? 608  LEU A CB  1 
ATOM   4992  C  CG  . LEU A 1 608  ? 135.735 115.582 114.519 1.00 128.44 ? 608  LEU A CG  1 
ATOM   4993  C  CD1 . LEU A 1 608  ? 136.147 114.129 114.376 1.00 138.35 ? 608  LEU A CD1 1 
ATOM   4994  C  CD2 . LEU A 1 608  ? 134.504 115.725 115.405 1.00 124.52 ? 608  LEU A CD2 1 
ATOM   4995  N  N   . LEU A 1 609  ? 138.538 118.831 116.209 1.00 140.77 ? 609  LEU A N   1 
ATOM   4996  C  CA  . LEU A 1 609  ? 139.351 119.444 117.253 1.00 131.88 ? 609  LEU A CA  1 
ATOM   4997  C  C   . LEU A 1 609  ? 138.762 120.779 117.678 1.00 127.74 ? 609  LEU A C   1 
ATOM   4998  O  O   . LEU A 1 609  ? 138.735 121.106 118.871 1.00 123.71 ? 609  LEU A O   1 
ATOM   4999  C  CB  . LEU A 1 609  ? 140.785 119.607 116.761 1.00 144.73 ? 609  LEU A CB  1 
ATOM   5000  C  CG  . LEU A 1 609  ? 141.484 118.268 116.555 1.00 141.87 ? 609  LEU A CG  1 
ATOM   5001  C  CD1 . LEU A 1 609  ? 142.830 118.473 115.918 1.00 161.11 ? 609  LEU A CD1 1 
ATOM   5002  C  CD2 . LEU A 1 609  ? 141.640 117.584 117.902 1.00 130.81 ? 609  LEU A CD2 1 
ATOM   5003  N  N   . HIS A 1 610  ? 138.280 121.563 116.714 1.00 135.33 ? 610  HIS A N   1 
ATOM   5004  C  CA  . HIS A 1 610  ? 137.695 122.855 117.039 1.00 141.02 ? 610  HIS A CA  1 
ATOM   5005  C  C   . HIS A 1 610  ? 136.391 122.685 117.810 1.00 141.83 ? 610  HIS A C   1 
ATOM   5006  O  O   . HIS A 1 610  ? 136.101 123.461 118.728 1.00 140.98 ? 610  HIS A O   1 
ATOM   5007  C  CB  . HIS A 1 610  ? 137.464 123.649 115.754 1.00 144.15 ? 610  HIS A CB  1 
ATOM   5008  C  CG  . HIS A 1 610  ? 137.017 125.057 115.984 1.00 158.75 ? 610  HIS A CG  1 
ATOM   5009  N  ND1 . HIS A 1 610  ? 137.801 125.993 116.624 1.00 167.63 ? 610  HIS A ND1 1 
ATOM   5010  C  CD2 . HIS A 1 610  ? 135.864 125.689 115.660 1.00 159.45 ? 610  HIS A CD2 1 
ATOM   5011  C  CE1 . HIS A 1 610  ? 137.150 127.141 116.684 1.00 171.40 ? 610  HIS A CE1 1 
ATOM   5012  N  NE2 . HIS A 1 610  ? 135.973 126.983 116.106 1.00 163.33 ? 610  HIS A NE2 1 
ATOM   5013  N  N   . GLN A 1 611  ? 135.594 121.673 117.458 1.00 139.68 ? 611  GLN A N   1 
ATOM   5014  C  CA  . GLN A 1 611  ? 134.294 121.504 118.094 1.00 131.40 ? 611  GLN A CA  1 
ATOM   5015  C  C   . GLN A 1 611  ? 134.411 120.887 119.480 1.00 127.03 ? 611  GLN A C   1 
ATOM   5016  O  O   . GLN A 1 611  ? 133.620 121.220 120.369 1.00 129.39 ? 611  GLN A O   1 
ATOM   5017  C  CB  . GLN A 1 611  ? 133.384 120.630 117.233 1.00 132.63 ? 611  GLN A CB  1 
ATOM   5018  C  CG  . GLN A 1 611  ? 132.847 121.301 115.990 1.00 141.51 ? 611  GLN A CG  1 
ATOM   5019  C  CD  . GLN A 1 611  ? 132.138 120.322 115.081 1.00 139.91 ? 611  GLN A CD  1 
ATOM   5020  O  OE1 . GLN A 1 611  ? 132.272 119.107 115.236 1.00 131.00 ? 611  GLN A OE1 1 
ATOM   5021  N  NE2 . GLN A 1 611  ? 131.376 120.842 114.129 1.00 150.50 ? 611  GLN A NE2 1 
ATOM   5022  N  N   . ALA A 1 612  ? 135.386 120.005 119.684 1.00 133.56 ? 612  ALA A N   1 
ATOM   5023  C  CA  . ALA A 1 612  ? 135.497 119.233 120.915 1.00 125.37 ? 612  ALA A CA  1 
ATOM   5024  C  C   . ALA A 1 612  ? 136.335 119.920 121.982 1.00 112.81 ? 612  ALA A C   1 
ATOM   5025  O  O   . ALA A 1 612  ? 136.541 119.339 123.052 1.00 107.99 ? 612  ALA A O   1 
ATOM   5026  C  CB  . ALA A 1 612  ? 136.083 117.848 120.617 1.00 117.94 ? 612  ALA A CB  1 
ATOM   5027  N  N   . SER A 1 613  ? 136.810 121.137 121.733 1.00 131.32 ? 613  SER A N   1 
ATOM   5028  C  CA  . SER A 1 613  ? 137.632 121.847 122.702 1.00 148.85 ? 613  SER A CA  1 
ATOM   5029  C  C   . SER A 1 613  ? 136.722 122.685 123.587 1.00 149.16 ? 613  SER A C   1 
ATOM   5030  O  O   . SER A 1 613  ? 135.948 123.510 123.089 1.00 148.06 ? 613  SER A O   1 
ATOM   5031  C  CB  . SER A 1 613  ? 138.663 122.732 122.002 1.00 162.96 ? 613  SER A CB  1 
ATOM   5032  O  OG  . SER A 1 613  ? 138.035 123.816 121.338 1.00 167.40 ? 613  SER A OG  1 
ATOM   5033  N  N   . TRP A 1 614  ? 136.809 122.462 124.900 1.00 155.61 ? 614  TRP A N   1 
ATOM   5034  C  CA  . TRP A 1 614  ? 135.874 123.097 125.820 1.00 167.54 ? 614  TRP A CA  1 
ATOM   5035  C  C   . TRP A 1 614  ? 136.031 124.612 125.813 1.00 174.05 ? 614  TRP A C   1 
ATOM   5036  O  O   . TRP A 1 614  ? 135.037 125.348 125.787 1.00 167.45 ? 614  TRP A O   1 
ATOM   5037  C  CB  . TRP A 1 614  ? 136.092 122.535 127.228 1.00 171.00 ? 614  TRP A CB  1 
ATOM   5038  C  CG  . TRP A 1 614  ? 135.245 123.156 128.297 1.00 168.88 ? 614  TRP A CG  1 
ATOM   5039  C  CD1 . TRP A 1 614  ? 135.688 123.800 129.415 1.00 160.73 ? 614  TRP A CD1 1 
ATOM   5040  C  CD2 . TRP A 1 614  ? 133.815 123.184 128.362 1.00 156.43 ? 614  TRP A CD2 1 
ATOM   5041  N  NE1 . TRP A 1 614  ? 134.623 124.234 130.166 1.00 150.98 ? 614  TRP A NE1 1 
ATOM   5042  C  CE2 . TRP A 1 614  ? 133.462 123.866 129.540 1.00 151.86 ? 614  TRP A CE2 1 
ATOM   5043  C  CE3 . TRP A 1 614  ? 132.800 122.698 127.537 1.00 146.99 ? 614  TRP A CE3 1 
ATOM   5044  C  CZ2 . TRP A 1 614  ? 132.135 124.078 129.911 1.00 144.76 ? 614  TRP A CZ2 1 
ATOM   5045  C  CZ3 . TRP A 1 614  ? 131.484 122.910 127.904 1.00 127.78 ? 614  TRP A CZ3 1 
ATOM   5046  C  CH2 . TRP A 1 614  ? 131.164 123.592 129.081 1.00 129.26 ? 614  TRP A CH2 1 
ATOM   5047  N  N   . HIS A 1 615  ? 137.272 125.094 125.816 1.00 172.45 ? 615  HIS A N   1 
ATOM   5048  C  CA  . HIS A 1 615  ? 137.546 126.533 125.902 1.00 178.70 ? 615  HIS A CA  1 
ATOM   5049  C  C   . HIS A 1 615  ? 137.719 127.170 124.525 1.00 186.65 ? 615  HIS A C   1 
ATOM   5050  O  O   . HIS A 1 615  ? 136.898 127.989 124.103 1.00 192.01 ? 615  HIS A O   1 
ATOM   5051  C  CB  . HIS A 1 615  ? 138.765 126.757 126.798 1.00 181.89 ? 615  HIS A CB  1 
ATOM   5052  C  CG  . HIS A 1 615  ? 138.605 126.173 128.166 1.00 182.83 ? 615  HIS A CG  1 
ATOM   5053  N  ND1 . HIS A 1 615  ? 139.120 124.942 128.515 1.00 179.52 ? 615  HIS A ND1 1 
ATOM   5054  C  CD2 . HIS A 1 615  ? 137.956 126.632 129.262 1.00 180.46 ? 615  HIS A CD2 1 
ATOM   5055  C  CE1 . HIS A 1 615  ? 138.813 124.678 129.772 1.00 174.51 ? 615  HIS A CE1 1 
ATOM   5056  N  NE2 . HIS A 1 615  ? 138.106 125.687 130.248 1.00 174.70 ? 615  HIS A NE2 1 
ATOM   5057  N  N   . HIS A 1 616  ? 138.765 126.767 123.806 1.00 186.21 ? 616  HIS A N   1 
ATOM   5058  C  CA  . HIS A 1 616  ? 139.092 127.306 122.485 1.00 189.75 ? 616  HIS A CA  1 
ATOM   5059  C  C   . HIS A 1 616  ? 140.057 126.375 121.757 1.00 183.26 ? 616  HIS A C   1 
ATOM   5060  O  O   . HIS A 1 616  ? 141.275 126.535 121.846 1.00 171.72 ? 616  HIS A O   1 
ATOM   5061  C  CB  . HIS A 1 616  ? 139.725 128.703 122.589 1.00 193.35 ? 616  HIS A CB  1 
ATOM   5062  C  CG  . HIS A 1 616  ? 138.750 129.802 122.877 1.00 201.73 ? 616  HIS A CG  1 
ATOM   5063  N  ND1 . HIS A 1 616  ? 138.441 130.207 124.158 1.00 203.42 ? 616  HIS A ND1 1 
ATOM   5064  C  CD2 . HIS A 1 616  ? 138.021 130.588 122.050 1.00 197.82 ? 616  HIS A CD2 1 
ATOM   5065  C  CE1 . HIS A 1 616  ? 137.560 131.191 124.107 1.00 196.73 ? 616  HIS A CE1 1 
ATOM   5066  N  NE2 . HIS A 1 616  ? 137.289 131.441 122.839 1.00 195.41 ? 616  HIS A NE2 1 
ATOM   5067  N  N   . GLU A 1 623  ? 148.876 120.128 117.457 1.00 215.85 ? 623  GLU A N   1 
ATOM   5068  C  CA  . GLU A 1 623  ? 147.819 120.209 118.459 1.00 218.32 ? 623  GLU A CA  1 
ATOM   5069  C  C   . GLU A 1 623  ? 147.898 119.034 119.429 1.00 218.07 ? 623  GLU A C   1 
ATOM   5070  O  O   . GLU A 1 623  ? 147.285 119.065 120.495 1.00 213.00 ? 623  GLU A O   1 
ATOM   5071  C  CB  . GLU A 1 623  ? 146.446 120.243 117.783 1.00 213.41 ? 623  GLU A CB  1 
ATOM   5072  C  CG  . GLU A 1 623  ? 146.015 118.937 117.097 1.00 210.90 ? 623  GLU A CG  1 
ATOM   5073  C  CD  . GLU A 1 623  ? 146.987 118.398 116.047 1.00 212.75 ? 623  GLU A CD  1 
ATOM   5074  O  OE1 . GLU A 1 623  ? 147.950 119.099 115.669 1.00 214.36 ? 623  GLU A OE1 1 
ATOM   5075  O  OE2 . GLU A 1 623  ? 146.787 117.249 115.602 1.00 203.96 ? 623  GLU A OE2 1 
ATOM   5076  N  N   . ASN A 1 624  ? 148.534 117.956 118.965 1.00 212.37 ? 624  ASN A N   1 
ATOM   5077  C  CA  . ASN A 1 624  ? 148.799 116.724 119.726 1.00 209.23 ? 624  ASN A CA  1 
ATOM   5078  C  C   . ASN A 1 624  ? 147.560 116.160 120.432 1.00 204.98 ? 624  ASN A C   1 
ATOM   5079  O  O   . ASN A 1 624  ? 147.634 115.708 121.577 1.00 195.68 ? 624  ASN A O   1 
ATOM   5080  C  CB  . ASN A 1 624  ? 149.998 116.860 120.692 1.00 209.38 ? 624  ASN A CB  1 
ATOM   5081  C  CG  . ASN A 1 624  ? 149.732 117.717 121.932 1.00 212.66 ? 624  ASN A CG  1 
ATOM   5082  O  OD1 . ASN A 1 624  ? 149.328 118.869 121.859 1.00 208.76 ? 624  ASN A OD1 1 
ATOM   5083  N  ND2 . ASN A 1 624  ? 149.996 117.132 123.097 1.00 212.77 ? 624  ASN A ND2 1 
ATOM   5084  N  N   . ALA A 1 625  ? 146.408 116.157 119.756 1.00 191.84 ? 625  ALA A N   1 
ATOM   5085  C  CA  . ALA A 1 625  ? 145.203 115.628 120.384 1.00 163.23 ? 625  ALA A CA  1 
ATOM   5086  C  C   . ALA A 1 625  ? 144.439 114.695 119.452 1.00 143.73 ? 625  ALA A C   1 
ATOM   5087  O  O   . ALA A 1 625  ? 144.447 114.857 118.230 1.00 151.52 ? 625  ALA A O   1 
ATOM   5088  C  CB  . ALA A 1 625  ? 144.275 116.763 120.840 1.00 159.60 ? 625  ALA A CB  1 
ATOM   5089  N  N   . ILE A 1 626  ? 143.778 113.709 120.062 1.00 136.61 ? 626  ILE A N   1 
ATOM   5090  C  CA  . ILE A 1 626  ? 142.973 112.700 119.375 1.00 124.76 ? 626  ILE A CA  1 
ATOM   5091  C  C   . ILE A 1 626  ? 141.545 112.775 119.904 1.00 122.83 ? 626  ILE A C   1 
ATOM   5092  O  O   . ILE A 1 626  ? 141.337 112.846 121.121 1.00 122.97 ? 626  ILE A O   1 
ATOM   5093  C  CB  . ILE A 1 626  ? 143.547 111.284 119.559 1.00 116.05 ? 626  ILE A CB  1 
ATOM   5094  C  CG1 . ILE A 1 626  ? 145.054 111.272 119.309 1.00 141.03 ? 626  ILE A CG1 1 
ATOM   5095  C  CG2 . ILE A 1 626  ? 142.854 110.303 118.624 1.00 108.23 ? 626  ILE A CG2 1 
ATOM   5096  C  CD1 . ILE A 1 626  ? 145.697 109.924 119.554 1.00 154.67 ? 626  ILE A CD1 1 
ATOM   5097  N  N   . VAL A 1 627  ? 140.566 112.755 119.000 1.00 119.07 ? 627  VAL A N   1 
ATOM   5098  C  CA  . VAL A 1 627  ? 139.151 112.825 119.365 1.00 110.05 ? 627  VAL A CA  1 
ATOM   5099  C  C   . VAL A 1 627  ? 138.492 111.487 119.053 1.00 105.19 ? 627  VAL A C   1 
ATOM   5100  O  O   . VAL A 1 627  ? 138.623 110.968 117.938 1.00 104.08 ? 627  VAL A O   1 
ATOM   5101  C  CB  . VAL A 1 627  ? 138.430 113.963 118.623 1.00 106.26 ? 627  VAL A CB  1 
ATOM   5102  C  CG1 . VAL A 1 627  ? 136.975 114.043 119.067 1.00 101.20 ? 627  VAL A CG1 1 
ATOM   5103  C  CG2 . VAL A 1 627  ? 139.134 115.278 118.860 1.00 120.53 ? 627  VAL A CG2 1 
ATOM   5104  N  N   . ARG A 1 628  ? 137.791 110.930 120.042 1.00 96.37  ? 628  ARG A N   1 
ATOM   5105  C  CA  . ARG A 1 628  ? 137.090 109.658 119.900 1.00 86.14  ? 628  ARG A CA  1 
ATOM   5106  C  C   . ARG A 1 628  ? 135.659 109.803 120.401 1.00 80.39  ? 628  ARG A C   1 
ATOM   5107  O  O   . ARG A 1 628  ? 135.440 110.324 121.499 1.00 83.74  ? 628  ARG A O   1 
ATOM   5108  C  CB  . ARG A 1 628  ? 137.812 108.561 120.678 1.00 91.18  ? 628  ARG A CB  1 
ATOM   5109  C  CG  . ARG A 1 628  ? 137.215 107.190 120.509 1.00 109.30 ? 628  ARG A CG  1 
ATOM   5110  C  CD  . ARG A 1 628  ? 137.474 106.706 119.098 1.00 94.03  ? 628  ARG A CD  1 
ATOM   5111  N  NE  . ARG A 1 628  ? 138.886 106.389 118.921 1.00 93.34  ? 628  ARG A NE  1 
ATOM   5112  C  CZ  . ARG A 1 628  ? 139.413 105.193 119.152 1.00 115.92 ? 628  ARG A CZ  1 
ATOM   5113  N  NH1 . ARG A 1 628  ? 140.710 104.989 118.966 1.00 122.80 ? 628  ARG A NH1 1 
ATOM   5114  N  NH2 . ARG A 1 628  ? 138.642 104.202 119.576 1.00 114.33 ? 628  ARG A NH2 1 
ATOM   5115  N  N   . GLY A 1 629  ? 134.686 109.346 119.609 1.00 78.78  ? 629  GLY A N   1 
ATOM   5116  C  CA  . GLY A 1 629  ? 133.293 109.480 120.005 1.00 85.58  ? 629  GLY A CA  1 
ATOM   5117  C  C   . GLY A 1 629  ? 132.585 108.201 120.419 1.00 75.11  ? 629  GLY A C   1 
ATOM   5118  O  O   . GLY A 1 629  ? 133.009 107.100 120.053 1.00 80.83  ? 629  GLY A O   1 
ATOM   5119  N  N   . ALA A 1 630  ? 131.491 108.339 121.174 1.00 66.85  ? 630  ALA A N   1 
ATOM   5120  C  CA  . ALA A 1 630  ? 130.632 107.222 121.550 1.00 64.59  ? 630  ALA A CA  1 
ATOM   5121  C  C   . ALA A 1 630  ? 129.210 107.730 121.752 1.00 75.30  ? 630  ALA A C   1 
ATOM   5122  O  O   . ALA A 1 630  ? 129.008 108.838 122.254 1.00 91.00  ? 630  ALA A O   1 
ATOM   5123  C  CB  . ALA A 1 630  ? 131.136 106.525 122.819 1.00 77.76  ? 630  ALA A CB  1 
ATOM   5124  N  N   . SER A 1 631  ? 128.228 106.913 121.369 1.00 68.59  ? 631  SER A N   1 
ATOM   5125  C  CA  . SER A 1 631  ? 126.841 107.342 121.261 1.00 65.61  ? 631  SER A CA  1 
ATOM   5126  C  C   . SER A 1 631  ? 125.926 106.403 122.036 1.00 63.72  ? 631  SER A C   1 
ATOM   5127  O  O   . SER A 1 631  ? 126.270 105.249 122.302 1.00 84.70  ? 631  SER A O   1 
ATOM   5128  C  CB  . SER A 1 631  ? 126.383 107.381 119.798 1.00 84.59  ? 631  SER A CB  1 
ATOM   5129  O  OG  . SER A 1 631  ? 126.809 106.216 119.109 1.00 68.10  ? 631  SER A OG  1 
ATOM   5130  N  N   . PHE A 1 632  ? 124.744 106.905 122.399 1.00 61.85  ? 632  PHE A N   1 
ATOM   5131  C  CA  . PHE A 1 632  ? 123.707 106.032 122.931 1.00 68.75  ? 632  PHE A CA  1 
ATOM   5132  C  C   . PHE A 1 632  ? 122.367 106.506 122.386 1.00 66.77  ? 632  PHE A C   1 
ATOM   5133  O  O   . PHE A 1 632  ? 122.222 107.649 121.947 1.00 76.17  ? 632  PHE A O   1 
ATOM   5134  C  CB  . PHE A 1 632  ? 123.691 106.012 124.469 1.00 84.13  ? 632  PHE A CB  1 
ATOM   5135  C  CG  . PHE A 1 632  ? 123.227 107.290 125.102 1.00 78.55  ? 632  PHE A CG  1 
ATOM   5136  C  CD1 . PHE A 1 632  ? 124.102 108.339 125.319 1.00 80.68  ? 632  PHE A CD1 1 
ATOM   5137  C  CD2 . PHE A 1 632  ? 121.916 107.417 125.532 1.00 82.65  ? 632  PHE A CD2 1 
ATOM   5138  C  CE1 . PHE A 1 632  ? 123.663 109.509 125.919 1.00 89.36  ? 632  PHE A CE1 1 
ATOM   5139  C  CE2 . PHE A 1 632  ? 121.474 108.578 126.132 1.00 82.67  ? 632  PHE A CE2 1 
ATOM   5140  C  CZ  . PHE A 1 632  ? 122.347 109.625 126.326 1.00 93.02  ? 632  PHE A CZ  1 
ATOM   5141  N  N   . VAL A 1 633  ? 121.375 105.618 122.433 1.00 61.15  ? 633  VAL A N   1 
ATOM   5142  C  CA  . VAL A 1 633  ? 120.089 105.850 121.785 1.00 68.72  ? 633  VAL A CA  1 
ATOM   5143  C  C   . VAL A 1 633  ? 118.965 105.745 122.804 1.00 82.06  ? 633  VAL A C   1 
ATOM   5144  O  O   . VAL A 1 633  ? 118.899 104.780 123.573 1.00 88.48  ? 633  VAL A O   1 
ATOM   5145  C  CB  . VAL A 1 633  ? 119.861 104.874 120.616 1.00 86.78  ? 633  VAL A CB  1 
ATOM   5146  C  CG1 . VAL A 1 633  ? 118.640 105.290 119.813 1.00 100.20 ? 633  VAL A CG1 1 
ATOM   5147  C  CG2 . VAL A 1 633  ? 121.087 104.852 119.713 1.00 80.07  ? 633  VAL A CG2 1 
ATOM   5148  N  N   . THR A 1 634  ? 118.077 106.733 122.787 1.00 96.86  ? 634  THR A N   1 
ATOM   5149  C  CA  . THR A 1 634  ? 116.884 106.783 123.614 1.00 97.93  ? 634  THR A CA  1 
ATOM   5150  C  C   . THR A 1 634  ? 115.662 106.891 122.714 1.00 108.65 ? 634  THR A C   1 
ATOM   5151  O  O   . THR A 1 634  ? 115.763 107.257 121.540 1.00 115.38 ? 634  THR A O   1 
ATOM   5152  C  CB  . THR A 1 634  ? 116.916 107.962 124.595 1.00 108.90 ? 634  THR A CB  1 
ATOM   5153  O  OG1 . THR A 1 634  ? 116.959 109.192 123.862 1.00 110.02 ? 634  THR A OG1 1 
ATOM   5154  C  CG2 . THR A 1 634  ? 118.129 107.866 125.501 1.00 106.11 ? 634  THR A CG2 1 
ATOM   5155  N  N   . ASP A 1 635  ? 114.505 106.556 123.269 1.00 116.59 ? 635  ASP A N   1 
ATOM   5156  C  CA  . ASP A 1 635  ? 113.256 106.546 122.523 1.00 122.85 ? 635  ASP A CA  1 
ATOM   5157  C  C   . ASP A 1 635  ? 112.469 107.788 122.936 1.00 118.07 ? 635  ASP A C   1 
ATOM   5158  O  O   . ASP A 1 635  ? 112.267 108.032 124.129 1.00 115.56 ? 635  ASP A O   1 
ATOM   5159  C  CB  . ASP A 1 635  ? 112.469 105.258 122.797 1.00 116.78 ? 635  ASP A CB  1 
ATOM   5160  C  CG  . ASP A 1 635  ? 111.050 105.284 122.234 1.00 124.88 ? 635  ASP A CG  1 
ATOM   5161  O  OD1 . ASP A 1 635  ? 110.340 104.268 122.391 1.00 128.64 ? 635  ASP A OD1 1 
ATOM   5162  O  OD2 . ASP A 1 635  ? 110.657 106.270 121.582 1.00 125.68 ? 635  ASP A OD2 1 
ATOM   5163  N  N   . LEU A 1 636  ? 112.026 108.562 121.945 1.00 111.40 ? 636  LEU A N   1 
ATOM   5164  C  CA  . LEU A 1 636  ? 111.223 109.764 122.152 1.00 109.42 ? 636  LEU A CA  1 
ATOM   5165  C  C   . LEU A 1 636  ? 109.725 109.514 122.095 1.00 121.00 ? 636  LEU A C   1 
ATOM   5166  O  O   . LEU A 1 636  ? 108.950 110.441 122.349 1.00 115.49 ? 636  LEU A O   1 
ATOM   5167  C  CB  . LEU A 1 636  ? 111.569 110.839 121.122 1.00 102.98 ? 636  LEU A CB  1 
ATOM   5168  C  CG  . LEU A 1 636  ? 112.929 111.516 121.200 1.00 110.39 ? 636  LEU A CG  1 
ATOM   5169  C  CD1 . LEU A 1 636  ? 113.316 111.982 119.812 1.00 120.86 ? 636  LEU A CD1 1 
ATOM   5170  C  CD2 . LEU A 1 636  ? 112.876 112.679 122.179 1.00 117.76 ? 636  LEU A CD2 1 
ATOM   5171  N  N   . GLU A 1 637  ? 109.298 108.294 121.781 1.00 124.79 ? 637  GLU A N   1 
ATOM   5172  C  CA  . GLU A 1 637  ? 107.871 108.023 121.654 1.00 129.41 ? 637  GLU A CA  1 
ATOM   5173  C  C   . GLU A 1 637  ? 107.171 108.135 123.002 1.00 129.03 ? 637  GLU A C   1 
ATOM   5174  O  O   . GLU A 1 637  ? 106.030 108.603 123.076 1.00 124.75 ? 637  GLU A O   1 
ATOM   5175  C  CB  . GLU A 1 637  ? 107.669 106.643 121.018 1.00 131.12 ? 637  GLU A CB  1 
ATOM   5176  C  CG  . GLU A 1 637  ? 106.240 106.282 120.658 1.00 142.06 ? 637  GLU A CG  1 
ATOM   5177  C  CD  . GLU A 1 637  ? 105.480 105.657 121.816 1.00 139.49 ? 637  GLU A CD  1 
ATOM   5178  O  OE1 . GLU A 1 637  ? 106.046 105.544 122.924 1.00 127.27 ? 637  GLU A OE1 1 
ATOM   5179  O  OE2 . GLU A 1 637  ? 104.308 105.277 121.617 1.00 132.75 ? 637  GLU A OE2 1 
ATOM   5180  N  N   . LYS A 1 638  ? 107.834 107.721 124.077 1.00 123.18 ? 638  LYS A N   1 
ATOM   5181  C  CA  . LYS A 1 638  ? 107.226 107.697 125.401 1.00 113.10 ? 638  LYS A CA  1 
ATOM   5182  C  C   . LYS A 1 638  ? 107.229 109.067 126.090 1.00 92.26  ? 638  LYS A C   1 
ATOM   5183  O  O   . LYS A 1 638  ? 106.832 109.155 127.256 1.00 104.02 ? 638  LYS A O   1 
ATOM   5184  C  CB  . LYS A 1 638  ? 107.930 106.656 126.273 1.00 141.78 ? 638  LYS A CB  1 
ATOM   5185  C  CG  . LYS A 1 638  ? 109.430 106.852 126.393 1.00 139.71 ? 638  LYS A CG  1 
ATOM   5186  C  CD  . LYS A 1 638  ? 110.027 105.874 127.393 1.00 142.33 ? 638  LYS A CD  1 
ATOM   5187  C  CE  . LYS A 1 638  ? 109.097 105.646 128.573 1.00 156.78 ? 638  LYS A CE  1 
ATOM   5188  N  NZ  . LYS A 1 638  ? 109.761 104.882 129.663 1.00 143.58 ? 638  LYS A NZ  1 
ATOM   5189  N  N   . TYR A 1 639  ? 107.639 110.132 125.388 1.00 88.21  ? 639  TYR A N   1 
ATOM   5190  C  CA  . TYR A 1 639  ? 107.648 111.481 125.953 1.00 89.68  ? 639  TYR A CA  1 
ATOM   5191  C  C   . TYR A 1 639  ? 106.271 112.119 126.035 1.00 89.24  ? 639  TYR A C   1 
ATOM   5192  O  O   . TYR A 1 639  ? 106.006 112.882 126.971 1.00 83.65  ? 639  TYR A O   1 
ATOM   5193  C  CB  . TYR A 1 639  ? 108.510 112.432 125.119 1.00 106.22 ? 639  TYR A CB  1 
ATOM   5194  C  CG  . TYR A 1 639  ? 109.986 112.484 125.409 1.00 129.29 ? 639  TYR A CG  1 
ATOM   5195  C  CD1 . TYR A 1 639  ? 110.762 111.340 125.501 1.00 140.99 ? 639  TYR A CD1 1 
ATOM   5196  C  CD2 . TYR A 1 639  ? 110.607 113.715 125.581 1.00 114.09 ? 639  TYR A CD2 1 
ATOM   5197  C  CE1 . TYR A 1 639  ? 112.121 111.427 125.765 1.00 148.78 ? 639  TYR A CE1 1 
ATOM   5198  C  CE2 . TYR A 1 639  ? 111.949 113.813 125.843 1.00 115.24 ? 639  TYR A CE2 1 
ATOM   5199  C  CZ  . TYR A 1 639  ? 112.705 112.671 125.934 1.00 139.34 ? 639  TYR A CZ  1 
ATOM   5200  O  OH  . TYR A 1 639  ? 114.050 112.782 126.199 1.00 124.10 ? 639  TYR A OH  1 
ATOM   5201  N  N   . ASN A 1 640  ? 105.392 111.827 125.076 1.00 86.94  ? 640  ASN A N   1 
ATOM   5202  C  CA  . ASN A 1 640  ? 104.196 112.641 124.881 1.00 59.58  ? 640  ASN A CA  1 
ATOM   5203  C  C   . ASN A 1 640  ? 103.317 112.656 126.124 1.00 69.67  ? 640  ASN A C   1 
ATOM   5204  O  O   . ASN A 1 640  ? 102.875 113.719 126.575 1.00 74.18  ? 640  ASN A O   1 
ATOM   5205  C  CB  . ASN A 1 640  ? 103.404 112.100 123.690 1.00 76.25  ? 640  ASN A CB  1 
ATOM   5206  C  CG  . ASN A 1 640  ? 104.279 111.822 122.485 1.00 95.19  ? 640  ASN A CG  1 
ATOM   5207  O  OD1 . ASN A 1 640  ? 105.095 112.651 122.087 1.00 103.27 ? 640  ASN A OD1 1 
ATOM   5208  N  ND2 . ASN A 1 640  ? 104.125 110.634 121.908 1.00 93.14  ? 640  ASN A ND2 1 
ATOM   5209  N  N   . LEU A 1 641  ? 103.070 111.486 126.702 1.00 71.14  ? 641  LEU A N   1 
ATOM   5210  C  CA  . LEU A 1 641  ? 102.150 111.365 127.822 1.00 56.15  ? 641  LEU A CA  1 
ATOM   5211  C  C   . LEU A 1 641  ? 102.726 111.815 129.161 1.00 61.34  ? 641  LEU A C   1 
ATOM   5212  O  O   . LEU A 1 641  ? 101.958 111.959 130.119 1.00 57.63  ? 641  LEU A O   1 
ATOM   5213  C  CB  . LEU A 1 641  ? 101.705 109.908 127.930 1.00 57.73  ? 641  LEU A CB  1 
ATOM   5214  C  CG  . LEU A 1 641  ? 100.962 109.403 126.696 1.00 52.37  ? 641  LEU A CG  1 
ATOM   5215  C  CD1 . LEU A 1 641  ? 100.684 107.912 126.815 1.00 70.50  ? 641  LEU A CD1 1 
ATOM   5216  C  CD2 . LEU A 1 641  ? 99.680  110.192 126.464 1.00 51.93  ? 641  LEU A CD2 1 
ATOM   5217  N  N   . ALA A 1 642  ? 104.029 112.065 129.258 1.00 62.61  ? 642  ALA A N   1 
ATOM   5218  C  CA  . ALA A 1 642  ? 104.642 112.369 130.547 1.00 56.08  ? 642  ALA A CA  1 
ATOM   5219  C  C   . ALA A 1 642  ? 104.715 113.858 130.865 1.00 64.31  ? 642  ALA A C   1 
ATOM   5220  O  O   . ALA A 1 642  ? 105.156 114.214 131.964 1.00 70.46  ? 642  ALA A O   1 
ATOM   5221  C  CB  . ALA A 1 642  ? 106.047 111.762 130.613 1.00 69.22  ? 642  ALA A CB  1 
ATOM   5222  N  N   . PHE A 1 643  ? 104.285 114.730 129.961 1.00 67.80  ? 643  PHE A N   1 
ATOM   5223  C  CA  . PHE A 1 643  ? 104.389 116.166 130.208 1.00 59.38  ? 643  PHE A CA  1 
ATOM   5224  C  C   . PHE A 1 643  ? 103.251 116.638 131.101 1.00 59.36  ? 643  PHE A C   1 
ATOM   5225  O  O   . PHE A 1 643  ? 102.083 116.308 130.866 1.00 75.01  ? 643  PHE A O   1 
ATOM   5226  C  CB  . PHE A 1 643  ? 104.403 116.919 128.879 1.00 57.08  ? 643  PHE A CB  1 
ATOM   5227  C  CG  . PHE A 1 643  ? 105.761 116.964 128.236 1.00 73.55  ? 643  PHE A CG  1 
ATOM   5228  C  CD1 . PHE A 1 643  ? 106.788 117.685 128.820 1.00 72.63  ? 643  PHE A CD1 1 
ATOM   5229  C  CD2 . PHE A 1 643  ? 106.033 116.222 127.098 1.00 73.99  ? 643  PHE A CD2 1 
ATOM   5230  C  CE1 . PHE A 1 643  ? 108.050 117.714 128.251 1.00 73.61  ? 643  PHE A CE1 1 
ATOM   5231  C  CE2 . PHE A 1 643  ? 107.295 116.241 126.527 1.00 67.54  ? 643  PHE A CE2 1 
ATOM   5232  C  CZ  . PHE A 1 643  ? 108.304 116.986 127.105 1.00 59.04  ? 643  PHE A CZ  1 
ATOM   5233  N  N   . ARG A 1 644  ? 103.595 117.428 132.114 1.00 55.60  ? 644  ARG A N   1 
ATOM   5234  C  CA  . ARG A 1 644  ? 102.643 117.993 133.056 1.00 52.65  ? 644  ARG A CA  1 
ATOM   5235  C  C   . ARG A 1 644  ? 102.720 119.511 133.013 1.00 56.71  ? 644  ARG A C   1 
ATOM   5236  O  O   . ARG A 1 644  ? 103.739 120.094 132.632 1.00 69.28  ? 644  ARG A O   1 
ATOM   5237  C  CB  . ARG A 1 644  ? 102.904 117.507 134.489 1.00 64.06  ? 644  ARG A CB  1 
ATOM   5238  C  CG  . ARG A 1 644  ? 102.628 116.030 134.743 1.00 63.83  ? 644  ARG A CG  1 
ATOM   5239  C  CD  . ARG A 1 644  ? 101.237 115.596 134.300 1.00 57.07  ? 644  ARG A CD  1 
ATOM   5240  N  NE  . ARG A 1 644  ? 100.960 114.220 134.711 1.00 50.90  ? 644  ARG A NE  1 
ATOM   5241  C  CZ  . ARG A 1 644  ? 100.988 113.167 133.901 1.00 46.11  ? 644  ARG A CZ  1 
ATOM   5242  N  NH1 . ARG A 1 644  ? 101.284 113.313 132.617 1.00 61.07  ? 644  ARG A NH1 1 
ATOM   5243  N  NH2 . ARG A 1 644  ? 100.721 111.960 134.379 1.00 49.85  ? 644  ARG A NH2 1 
ATOM   5244  N  N   . TYR A 1 645  ? 101.618 120.148 133.416 1.00 57.49  ? 645  TYR A N   1 
ATOM   5245  C  CA  . TYR A 1 645  ? 101.540 121.605 133.361 1.00 57.52  ? 645  TYR A CA  1 
ATOM   5246  C  C   . TYR A 1 645  ? 102.534 122.276 134.300 1.00 67.97  ? 645  TYR A C   1 
ATOM   5247  O  O   . TYR A 1 645  ? 103.142 123.291 133.939 1.00 73.89  ? 645  TYR A O   1 
ATOM   5248  C  CB  . TYR A 1 645  ? 100.122 122.060 133.695 1.00 62.49  ? 645  TYR A CB  1 
ATOM   5249  C  CG  . TYR A 1 645  ? 99.857  123.490 133.298 1.00 56.54  ? 645  TYR A CG  1 
ATOM   5250  C  CD1 . TYR A 1 645  ? 100.117 123.937 132.012 1.00 58.36  ? 645  TYR A CD1 1 
ATOM   5251  C  CD2 . TYR A 1 645  ? 99.376  124.403 134.223 1.00 60.41  ? 645  TYR A CD2 1 
ATOM   5252  C  CE1 . TYR A 1 645  ? 99.883  125.253 131.653 1.00 49.77  ? 645  TYR A CE1 1 
ATOM   5253  C  CE2 . TYR A 1 645  ? 99.141  125.720 133.875 1.00 54.62  ? 645  TYR A CE2 1 
ATOM   5254  C  CZ  . TYR A 1 645  ? 99.397  126.140 132.589 1.00 50.00  ? 645  TYR A CZ  1 
ATOM   5255  O  OH  . TYR A 1 645  ? 99.166  127.453 132.240 1.00 67.07  ? 645  TYR A OH  1 
ATOM   5256  N  N   . GLU A 1 646  ? 102.748 121.700 135.489 1.00 69.75  ? 646  GLU A N   1 
ATOM   5257  C  CA  . GLU A 1 646  ? 103.671 122.294 136.455 1.00 62.52  ? 646  GLU A CA  1 
ATOM   5258  C  C   . GLU A 1 646  ? 105.045 122.495 135.845 1.00 68.11  ? 646  GLU A C   1 
ATOM   5259  O  O   . GLU A 1 646  ? 105.791 123.392 136.253 1.00 73.39  ? 646  GLU A O   1 
ATOM   5260  C  CB  . GLU A 1 646  ? 103.778 121.407 137.691 1.00 62.34  ? 646  GLU A CB  1 
ATOM   5261  C  CG  . GLU A 1 646  ? 102.563 121.460 138.581 1.00 78.66  ? 646  GLU A CG  1 
ATOM   5262  C  CD  . GLU A 1 646  ? 101.562 120.386 138.217 1.00 81.82  ? 646  GLU A CD  1 
ATOM   5263  O  OE1 . GLU A 1 646  ? 101.528 119.981 137.036 1.00 84.86  ? 646  GLU A OE1 1 
ATOM   5264  O  OE2 . GLU A 1 646  ? 100.808 119.946 139.108 1.00 90.39  ? 646  GLU A OE2 1 
ATOM   5265  N  N   . PHE A 1 647  ? 105.389 121.663 134.872 1.00 68.74  ? 647  PHE A N   1 
ATOM   5266  C  CA  . PHE A 1 647  ? 106.669 121.752 134.195 1.00 62.07  ? 647  PHE A CA  1 
ATOM   5267  C  C   . PHE A 1 647  ? 106.646 122.783 133.068 1.00 72.62  ? 647  PHE A C   1 
ATOM   5268  O  O   . PHE A 1 647  ? 107.584 123.576 132.934 1.00 63.17  ? 647  PHE A O   1 
ATOM   5269  C  CB  . PHE A 1 647  ? 107.031 120.361 133.675 1.00 61.26  ? 647  PHE A CB  1 
ATOM   5270  C  CG  . PHE A 1 647  ? 108.350 120.287 132.987 1.00 71.60  ? 647  PHE A CG  1 
ATOM   5271  C  CD1 . PHE A 1 647  ? 109.452 120.954 133.490 1.00 80.67  ? 647  PHE A CD1 1 
ATOM   5272  C  CD2 . PHE A 1 647  ? 108.494 119.525 131.841 1.00 67.56  ? 647  PHE A CD2 1 
ATOM   5273  C  CE1 . PHE A 1 647  ? 110.671 120.876 132.851 1.00 77.98  ? 647  PHE A CE1 1 
ATOM   5274  C  CE2 . PHE A 1 647  ? 109.709 119.441 131.198 1.00 78.33  ? 647  PHE A CE2 1 
ATOM   5275  C  CZ  . PHE A 1 647  ? 110.800 120.118 131.702 1.00 74.51  ? 647  PHE A CZ  1 
ATOM   5276  N  N   . THR A 1 648  ? 105.581 122.802 132.260 1.00 64.85  ? 648  THR A N   1 
ATOM   5277  C  CA  . THR A 1 648  ? 105.567 123.549 131.005 1.00 55.16  ? 648  THR A CA  1 
ATOM   5278  C  C   . THR A 1 648  ? 104.934 124.937 131.093 1.00 55.95  ? 648  THR A C   1 
ATOM   5279  O  O   . THR A 1 648  ? 104.913 125.653 130.077 1.00 71.78  ? 648  THR A O   1 
ATOM   5280  C  CB  . THR A 1 648  ? 104.835 122.734 129.936 1.00 40.80  ? 648  THR A CB  1 
ATOM   5281  O  OG1 . THR A 1 648  ? 103.529 122.390 130.415 1.00 54.68  ? 648  THR A OG1 1 
ATOM   5282  C  CG2 . THR A 1 648  ? 105.598 121.454 129.633 1.00 50.10  ? 648  THR A CG2 1 
ATOM   5283  N  N   . ARG A 1 649  ? 104.424 125.338 132.264 1.00 52.34  ? 649  ARG A N   1 
ATOM   5284  C  CA  . ARG A 1 649  ? 103.859 126.679 132.411 1.00 50.28  ? 649  ARG A CA  1 
ATOM   5285  C  C   . ARG A 1 649  ? 104.820 127.745 131.913 1.00 73.91  ? 649  ARG A C   1 
ATOM   5286  O  O   . ARG A 1 649  ? 104.454 128.619 131.117 1.00 89.80  ? 649  ARG A O   1 
ATOM   5287  C  CB  . ARG A 1 649  ? 103.540 126.977 133.875 1.00 62.65  ? 649  ARG A CB  1 
ATOM   5288  C  CG  . ARG A 1 649  ? 102.527 126.123 134.569 1.00 77.08  ? 649  ARG A CG  1 
ATOM   5289  C  CD  . ARG A 1 649  ? 102.466 126.577 136.009 1.00 80.63  ? 649  ARG A CD  1 
ATOM   5290  N  NE  . ARG A 1 649  ? 101.740 127.835 136.129 1.00 75.68  ? 649  ARG A NE  1 
ATOM   5291  C  CZ  . ARG A 1 649  ? 100.553 127.957 136.708 1.00 83.04  ? 649  ARG A CZ  1 
ATOM   5292  N  NH1 . ARG A 1 649  ? 99.960  126.895 137.231 1.00 80.83  ? 649  ARG A NH1 1 
ATOM   5293  N  NH2 . ARG A 1 649  ? 99.962  129.143 136.770 1.00 82.96  ? 649  ARG A NH2 1 
ATOM   5294  N  N   . HIS A 1 650  ? 106.065 127.678 132.385 1.00 62.02  ? 650  HIS A N   1 
ATOM   5295  C  CA  . HIS A 1 650  ? 107.013 128.760 132.173 1.00 52.69  ? 650  HIS A CA  1 
ATOM   5296  C  C   . HIS A 1 650  ? 107.458 128.835 130.720 1.00 63.86  ? 650  HIS A C   1 
ATOM   5297  O  O   . HIS A 1 650  ? 107.578 129.930 130.158 1.00 77.04  ? 650  HIS A O   1 
ATOM   5298  C  CB  . HIS A 1 650  ? 108.204 128.553 133.104 1.00 78.95  ? 650  HIS A CB  1 
ATOM   5299  C  CG  . HIS A 1 650  ? 107.820 128.482 134.549 1.00 75.52  ? 650  HIS A CG  1 
ATOM   5300  N  ND1 . HIS A 1 650  ? 107.762 129.591 135.366 1.00 75.06  ? 650  HIS A ND1 1 
ATOM   5301  C  CD2 . HIS A 1 650  ? 107.453 127.429 135.319 1.00 67.52  ? 650  HIS A CD2 1 
ATOM   5302  C  CE1 . HIS A 1 650  ? 107.385 129.223 136.576 1.00 91.14  ? 650  HIS A CE1 1 
ATOM   5303  N  NE2 . HIS A 1 650  ? 107.192 127.916 136.575 1.00 83.91  ? 650  HIS A NE2 1 
ATOM   5304  N  N   . PHE A 1 651  ? 107.685 127.681 130.091 1.00 58.04  ? 651  PHE A N   1 
ATOM   5305  C  CA  . PHE A 1 651  ? 108.048 127.669 128.679 1.00 48.02  ? 651  PHE A CA  1 
ATOM   5306  C  C   . PHE A 1 651  ? 106.920 128.218 127.817 1.00 67.39  ? 651  PHE A C   1 
ATOM   5307  O  O   . PHE A 1 651  ? 107.157 129.016 126.897 1.00 71.08  ? 651  PHE A O   1 
ATOM   5308  C  CB  . PHE A 1 651  ? 108.415 126.250 128.249 1.00 49.46  ? 651  PHE A CB  1 
ATOM   5309  C  CG  . PHE A 1 651  ? 109.484 125.622 129.097 1.00 65.26  ? 651  PHE A CG  1 
ATOM   5310  C  CD1 . PHE A 1 651  ? 109.154 124.878 130.218 1.00 74.42  ? 651  PHE A CD1 1 
ATOM   5311  C  CD2 . PHE A 1 651  ? 110.820 125.791 128.780 1.00 75.23  ? 651  PHE A CD2 1 
ATOM   5312  C  CE1 . PHE A 1 651  ? 110.140 124.308 131.003 1.00 77.26  ? 651  PHE A CE1 1 
ATOM   5313  C  CE2 . PHE A 1 651  ? 111.810 125.224 129.561 1.00 66.74  ? 651  PHE A CE2 1 
ATOM   5314  C  CZ  . PHE A 1 651  ? 111.470 124.482 130.673 1.00 66.83  ? 651  PHE A CZ  1 
ATOM   5315  N  N   . ILE A 1 652  ? 105.677 127.832 128.122 1.00 62.78  ? 652  ILE A N   1 
ATOM   5316  C  CA  . ILE A 1 652  ? 104.546 128.343 127.356 1.00 45.10  ? 652  ILE A CA  1 
ATOM   5317  C  C   . ILE A 1 652  ? 104.421 129.854 127.523 1.00 52.46  ? 652  ILE A C   1 
ATOM   5318  O  O   . ILE A 1 652  ? 104.215 130.590 126.547 1.00 72.96  ? 652  ILE A O   1 
ATOM   5319  C  CB  . ILE A 1 652  ? 103.257 127.618 127.778 1.00 49.98  ? 652  ILE A CB  1 
ATOM   5320  C  CG1 . ILE A 1 652  ? 103.245 126.194 127.222 1.00 54.53  ? 652  ILE A CG1 1 
ATOM   5321  C  CG2 . ILE A 1 652  ? 102.054 128.376 127.263 1.00 79.20  ? 652  ILE A CG2 1 
ATOM   5322  C  CD1 . ILE A 1 652  ? 102.188 125.307 127.843 1.00 75.55  ? 652  ILE A CD1 1 
ATOM   5323  N  N   . ASP A 1 653  ? 104.570 130.341 128.758 1.00 63.20  ? 653  ASP A N   1 
ATOM   5324  C  CA  . ASP A 1 653  ? 104.435 131.772 129.013 1.00 65.86  ? 653  ASP A CA  1 
ATOM   5325  C  C   . ASP A 1 653  ? 105.537 132.545 128.295 1.00 70.94  ? 653  ASP A C   1 
ATOM   5326  O  O   . ASP A 1 653  ? 105.284 133.603 127.700 1.00 78.36  ? 653  ASP A O   1 
ATOM   5327  C  CB  . ASP A 1 653  ? 104.460 132.019 130.530 1.00 79.86  ? 653  ASP A CB  1 
ATOM   5328  C  CG  . ASP A 1 653  ? 104.560 133.503 130.925 1.00 104.01 ? 653  ASP A CG  1 
ATOM   5329  O  OD1 . ASP A 1 653  ? 104.634 134.407 130.069 1.00 97.79  ? 653  ASP A OD1 1 
ATOM   5330  O  OD2 . ASP A 1 653  ? 104.563 133.768 132.144 1.00 109.19 ? 653  ASP A OD2 1 
ATOM   5331  N  N   . TYR A 1 654  ? 106.767 132.025 128.323 1.00 76.03  ? 654  TYR A N   1 
ATOM   5332  C  CA  . TYR A 1 654  ? 107.856 132.702 127.632 1.00 62.81  ? 654  TYR A CA  1 
ATOM   5333  C  C   . TYR A 1 654  ? 107.635 132.744 126.126 1.00 70.13  ? 654  TYR A C   1 
ATOM   5334  O  O   . TYR A 1 654  ? 107.949 133.750 125.480 1.00 86.64  ? 654  TYR A O   1 
ATOM   5335  C  CB  . TYR A 1 654  ? 109.191 132.039 127.959 1.00 73.02  ? 654  TYR A CB  1 
ATOM   5336  C  CG  . TYR A 1 654  ? 110.332 132.778 127.318 1.00 80.03  ? 654  TYR A CG  1 
ATOM   5337  C  CD1 . TYR A 1 654  ? 110.661 134.065 127.711 1.00 78.23  ? 654  TYR A CD1 1 
ATOM   5338  C  CD2 . TYR A 1 654  ? 111.072 132.192 126.303 1.00 77.43  ? 654  TYR A CD2 1 
ATOM   5339  C  CE1 . TYR A 1 654  ? 111.698 134.751 127.110 1.00 74.72  ? 654  TYR A CE1 1 
ATOM   5340  C  CE2 . TYR A 1 654  ? 112.113 132.865 125.700 1.00 72.74  ? 654  TYR A CE2 1 
ATOM   5341  C  CZ  . TYR A 1 654  ? 112.424 134.144 126.106 1.00 74.08  ? 654  TYR A CZ  1 
ATOM   5342  O  OH  . TYR A 1 654  ? 113.459 134.820 125.502 1.00 81.21  ? 654  TYR A OH  1 
ATOM   5343  N  N   . CYS A 1 655  ? 107.094 131.671 125.543 1.00 61.16  ? 655  CYS A N   1 
ATOM   5344  C  CA  . CYS A 1 655  ? 106.760 131.730 124.122 1.00 61.89  ? 655  CYS A CA  1 
ATOM   5345  C  C   . CYS A 1 655  ? 105.706 132.802 123.859 1.00 80.75  ? 655  CYS A C   1 
ATOM   5346  O  O   . CYS A 1 655  ? 105.816 133.581 122.894 1.00 86.82  ? 655  CYS A O   1 
ATOM   5347  C  CB  . CYS A 1 655  ? 106.291 130.360 123.636 1.00 59.82  ? 655  CYS A CB  1 
ATOM   5348  S  SG  . CYS A 1 655  ? 107.600 129.112 123.609 1.00 75.25  ? 655  CYS A SG  1 
ATOM   5349  N  N   . ASN A 1 656  ? 104.697 132.881 124.735 1.00 80.89  ? 656  ASN A N   1 
ATOM   5350  C  CA  . ASN A 1 656  ? 103.664 133.903 124.593 1.00 66.70  ? 656  ASN A CA  1 
ATOM   5351  C  C   . ASN A 1 656  ? 104.278 135.297 124.576 1.00 65.45  ? 656  ASN A C   1 
ATOM   5352  O  O   . ASN A 1 656  ? 103.940 136.127 123.724 1.00 75.95  ? 656  ASN A O   1 
ATOM   5353  C  CB  . ASN A 1 656  ? 102.650 133.795 125.736 1.00 70.94  ? 656  ASN A CB  1 
ATOM   5354  C  CG  . ASN A 1 656  ? 101.627 132.703 125.518 1.00 70.33  ? 656  ASN A CG  1 
ATOM   5355  O  OD1 . ASN A 1 656  ? 101.384 132.280 124.390 1.00 65.23  ? 656  ASN A OD1 1 
ATOM   5356  N  ND2 . ASN A 1 656  ? 101.006 132.249 126.600 1.00 70.27  ? 656  ASN A ND2 1 
ATOM   5357  N  N   . ARG A 1 657  ? 105.190 135.569 125.512 1.00 71.89  ? 657  ARG A N   1 
ATOM   5358  C  CA  . ARG A 1 657  ? 105.844 136.876 125.526 1.00 78.09  ? 657  ARG A CA  1 
ATOM   5359  C  C   . ARG A 1 657  ? 106.681 137.098 124.274 1.00 73.98  ? 657  ARG A C   1 
ATOM   5360  O  O   . ARG A 1 657  ? 106.701 138.205 123.724 1.00 78.02  ? 657  ARG A O   1 
ATOM   5361  C  CB  . ARG A 1 657  ? 106.704 137.059 126.773 1.00 77.34  ? 657  ARG A CB  1 
ATOM   5362  C  CG  . ARG A 1 657  ? 105.918 137.168 128.053 1.00 85.75  ? 657  ARG A CG  1 
ATOM   5363  C  CD  . ARG A 1 657  ? 106.856 137.358 129.218 1.00 109.12 ? 657  ARG A CD  1 
ATOM   5364  N  NE  . ARG A 1 657  ? 106.133 137.448 130.479 1.00 127.97 ? 657  ARG A NE  1 
ATOM   5365  C  CZ  . ARG A 1 657  ? 106.720 137.559 131.664 1.00 137.47 ? 657  ARG A CZ  1 
ATOM   5366  N  NH1 . ARG A 1 657  ? 108.043 137.597 131.749 1.00 137.20 ? 657  ARG A NH1 1 
ATOM   5367  N  NH2 . ARG A 1 657  ? 105.985 137.637 132.764 1.00 131.49 ? 657  ARG A NH2 1 
ATOM   5368  N  N   . CYS A 1 658  ? 107.390 136.063 123.815 1.00 73.40  ? 658  CYS A N   1 
ATOM   5369  C  CA  . CYS A 1 658  ? 108.251 136.234 122.650 1.00 65.06  ? 658  CYS A CA  1 
ATOM   5370  C  C   . CYS A 1 658  ? 107.449 136.612 121.417 1.00 70.06  ? 658  CYS A C   1 
ATOM   5371  O  O   . CYS A 1 658  ? 107.954 137.334 120.550 1.00 81.62  ? 658  CYS A O   1 
ATOM   5372  C  CB  . CYS A 1 658  ? 109.059 134.963 122.384 1.00 63.86  ? 658  CYS A CB  1 
ATOM   5373  S  SG  . CYS A 1 658  ? 110.538 134.800 123.399 1.00 103.24 ? 658  CYS A SG  1 
ATOM   5374  N  N   . TYR A 1 659  ? 106.195 136.172 121.331 1.00 73.30  ? 659  TYR A N   1 
ATOM   5375  C  CA  . TYR A 1 659  ? 105.377 136.538 120.181 1.00 68.94  ? 659  TYR A CA  1 
ATOM   5376  C  C   . TYR A 1 659  ? 104.443 137.712 120.443 1.00 74.27  ? 659  TYR A C   1 
ATOM   5377  O  O   . TYR A 1 659  ? 103.701 138.105 119.538 1.00 75.03  ? 659  TYR A O   1 
ATOM   5378  C  CB  . TYR A 1 659  ? 104.553 135.335 119.717 1.00 67.85  ? 659  TYR A CB  1 
ATOM   5379  C  CG  . TYR A 1 659  ? 105.331 134.326 118.907 1.00 67.92  ? 659  TYR A CG  1 
ATOM   5380  C  CD1 . TYR A 1 659  ? 106.067 133.325 119.524 1.00 77.28  ? 659  TYR A CD1 1 
ATOM   5381  C  CD2 . TYR A 1 659  ? 105.298 134.354 117.522 1.00 73.04  ? 659  TYR A CD2 1 
ATOM   5382  C  CE1 . TYR A 1 659  ? 106.772 132.397 118.779 1.00 71.60  ? 659  TYR A CE1 1 
ATOM   5383  C  CE2 . TYR A 1 659  ? 105.996 133.429 116.769 1.00 73.52  ? 659  TYR A CE2 1 
ATOM   5384  C  CZ  . TYR A 1 659  ? 106.730 132.452 117.402 1.00 70.11  ? 659  TYR A CZ  1 
ATOM   5385  O  OH  . TYR A 1 659  ? 107.428 131.529 116.656 1.00 70.01  ? 659  TYR A OH  1 
ATOM   5386  N  N   . GLY A 1 660  ? 104.456 138.288 121.645 1.00 79.96  ? 660  GLY A N   1 
ATOM   5387  C  CA  . GLY A 1 660  ? 103.579 139.394 121.960 1.00 74.27  ? 660  GLY A CA  1 
ATOM   5388  C  C   . GLY A 1 660  ? 102.146 139.002 122.238 1.00 79.65  ? 660  GLY A C   1 
ATOM   5389  O  O   . GLY A 1 660  ? 101.432 139.748 122.918 1.00 82.87  ? 660  GLY A O   1 
ATOM   5390  N  N   . VAL A 1 661  ? 101.707 137.849 121.736 1.00 83.32  ? 661  VAL A N   1 
ATOM   5391  C  CA  . VAL A 1 661  ? 100.349 137.357 121.926 1.00 85.23  ? 661  VAL A CA  1 
ATOM   5392  C  C   . VAL A 1 661  ? 100.183 136.909 123.367 1.00 72.70  ? 661  VAL A C   1 
ATOM   5393  O  O   . VAL A 1 661  ? 101.151 136.852 124.135 1.00 74.44  ? 661  VAL A O   1 
ATOM   5394  C  CB  . VAL A 1 661  ? 100.015 136.213 120.953 1.00 84.42  ? 661  VAL A CB  1 
ATOM   5395  C  CG1 . VAL A 1 661  ? 100.284 136.635 119.520 1.00 100.68 ? 661  VAL A CG1 1 
ATOM   5396  C  CG2 . VAL A 1 661  ? 100.820 134.974 121.306 1.00 78.21  ? 661  VAL A CG2 1 
ATOM   5397  N  N   . LYS A 1 662  ? 98.952  136.597 123.745 1.00 75.56  ? 662  LYS A N   1 
ATOM   5398  C  CA  . LYS A 1 662  ? 98.654  136.137 125.089 1.00 80.82  ? 662  LYS A CA  1 
ATOM   5399  C  C   . LYS A 1 662  ? 97.672  134.978 125.027 1.00 89.44  ? 662  LYS A C   1 
ATOM   5400  O  O   . LYS A 1 662  ? 96.736  134.991 124.227 1.00 88.79  ? 662  LYS A O   1 
ATOM   5401  C  CB  . LYS A 1 662  ? 98.091  137.308 125.898 1.00 82.70  ? 662  LYS A CB  1 
ATOM   5402  C  CG  . LYS A 1 662  ? 97.739  137.038 127.333 1.00 105.01 ? 662  LYS A CG  1 
ATOM   5403  C  CD  . LYS A 1 662  ? 97.349  138.351 127.982 1.00 125.84 ? 662  LYS A CD  1 
ATOM   5404  C  CE  . LYS A 1 662  ? 96.018  138.835 127.431 1.00 128.17 ? 662  LYS A CE  1 
ATOM   5405  N  NZ  . LYS A 1 662  ? 94.888  137.960 127.835 1.00 133.32 ? 662  LYS A NZ  1 
ATOM   5406  N  N   . ASN A 1 663  ? 97.909  133.960 125.852 1.00 86.09  ? 663  ASN A N   1 
ATOM   5407  C  CA  . ASN A 1 663  ? 97.083  132.757 125.941 1.00 78.84  ? 663  ASN A CA  1 
ATOM   5408  C  C   . ASN A 1 663  ? 97.092  131.904 124.676 1.00 70.62  ? 663  ASN A C   1 
ATOM   5409  O  O   . ASN A 1 663  ? 96.292  130.966 124.576 1.00 71.87  ? 663  ASN A O   1 
ATOM   5410  C  CB  . ASN A 1 663  ? 95.630  133.098 126.293 1.00 71.58  ? 663  ASN A CB  1 
ATOM   5411  C  CG  . ASN A 1 663  ? 95.512  133.889 127.579 1.00 80.44  ? 663  ASN A CG  1 
ATOM   5412  O  OD1 . ASN A 1 663  ? 96.254  133.662 128.533 1.00 74.83  ? 663  ASN A OD1 1 
ATOM   5413  N  ND2 . ASN A 1 663  ? 94.576  134.833 127.608 1.00 82.08  ? 663  ASN A ND2 1 
ATOM   5414  N  N   . LEU A 1 664  ? 97.955  132.194 123.698 1.00 59.41  ? 664  LEU A N   1 
ATOM   5415  C  CA  . LEU A 1 664  ? 97.911  131.427 122.455 1.00 61.57  ? 664  LEU A CA  1 
ATOM   5416  C  C   . LEU A 1 664  ? 98.471  130.018 122.632 1.00 68.01  ? 664  LEU A C   1 
ATOM   5417  O  O   . LEU A 1 664  ? 97.870  129.046 122.162 1.00 66.63  ? 664  LEU A O   1 
ATOM   5418  C  CB  . LEU A 1 664  ? 98.659  132.163 121.344 1.00 74.61  ? 664  LEU A CB  1 
ATOM   5419  C  CG  . LEU A 1 664  ? 98.923  131.328 120.086 1.00 71.64  ? 664  LEU A CG  1 
ATOM   5420  C  CD1 . LEU A 1 664  ? 97.614  130.850 119.468 1.00 66.20  ? 664  LEU A CD1 1 
ATOM   5421  C  CD2 . LEU A 1 664  ? 99.738  132.114 119.073 1.00 78.98  ? 664  LEU A CD2 1 
ATOM   5422  N  N   . PHE A 1 665  ? 99.604  129.880 123.316 1.00 70.41  ? 665  PHE A N   1 
ATOM   5423  C  CA  . PHE A 1 665  ? 100.285 128.594 123.413 1.00 64.21  ? 665  PHE A CA  1 
ATOM   5424  C  C   . PHE A 1 665  ? 99.797  127.746 124.578 1.00 65.04  ? 665  PHE A C   1 
ATOM   5425  O  O   . PHE A 1 665  ? 100.336 126.657 124.802 1.00 63.68  ? 665  PHE A O   1 
ATOM   5426  C  CB  . PHE A 1 665  ? 101.800 128.793 123.536 1.00 62.04  ? 665  PHE A CB  1 
ATOM   5427  C  CG  . PHE A 1 665  ? 102.432 129.388 122.315 1.00 73.25  ? 665  PHE A CG  1 
ATOM   5428  C  CD1 . PHE A 1 665  ? 102.662 128.611 121.194 1.00 80.66  ? 665  PHE A CD1 1 
ATOM   5429  C  CD2 . PHE A 1 665  ? 102.811 130.719 122.291 1.00 69.88  ? 665  PHE A CD2 1 
ATOM   5430  C  CE1 . PHE A 1 665  ? 103.245 129.152 120.065 1.00 71.07  ? 665  PHE A CE1 1 
ATOM   5431  C  CE2 . PHE A 1 665  ? 103.396 131.267 121.166 1.00 81.95  ? 665  PHE A CE2 1 
ATOM   5432  C  CZ  . PHE A 1 665  ? 103.613 130.482 120.052 1.00 80.00  ? 665  PHE A CZ  1 
ATOM   5433  N  N   . ASP A 1 666  ? 98.797  128.216 125.320 1.00 67.25  ? 666  ASP A N   1 
ATOM   5434  C  CA  . ASP A 1 666  ? 98.239  127.479 126.443 1.00 49.71  ? 666  ASP A CA  1 
ATOM   5435  C  C   . ASP A 1 666  ? 97.076  126.579 126.053 1.00 62.24  ? 666  ASP A C   1 
ATOM   5436  O  O   . ASP A 1 666  ? 96.483  125.947 126.932 1.00 72.16  ? 666  ASP A O   1 
ATOM   5437  C  CB  . ASP A 1 666  ? 97.756  128.471 127.508 1.00 70.30  ? 666  ASP A CB  1 
ATOM   5438  C  CG  . ASP A 1 666  ? 98.887  129.043 128.331 1.00 86.35  ? 666  ASP A CG  1 
ATOM   5439  O  OD1 . ASP A 1 666  ? 99.081  130.276 128.298 1.00 76.68  ? 666  ASP A OD1 1 
ATOM   5440  O  OD2 . ASP A 1 666  ? 99.564  128.265 129.033 1.00 99.23  ? 666  ASP A OD2 1 
ATOM   5441  N  N   . TRP A 1 667  ? 96.734  126.503 124.761 1.00 68.86  ? 667  TRP A N   1 
ATOM   5442  C  CA  . TRP A 1 667  ? 95.464  125.890 124.356 1.00 55.64  ? 667  TRP A CA  1 
ATOM   5443  C  C   . TRP A 1 667  ? 95.376  124.409 124.740 1.00 56.02  ? 667  TRP A C   1 
ATOM   5444  O  O   . TRP A 1 667  ? 94.328  123.951 125.208 1.00 75.16  ? 667  TRP A O   1 
ATOM   5445  C  CB  . TRP A 1 667  ? 95.248  126.077 122.870 1.00 62.46  ? 667  TRP A CB  1 
ATOM   5446  C  CG  . TRP A 1 667  ? 96.228  125.333 122.011 1.00 57.98  ? 667  TRP A CG  1 
ATOM   5447  C  CD1 . TRP A 1 667  ? 97.437  125.779 121.567 1.00 62.30  ? 667  TRP A CD1 1 
ATOM   5448  C  CD2 . TRP A 1 667  ? 96.072  124.008 121.488 1.00 67.31  ? 667  TRP A CD2 1 
ATOM   5449  N  NE1 . TRP A 1 667  ? 98.048  124.812 120.803 1.00 64.54  ? 667  TRP A NE1 1 
ATOM   5450  C  CE2 . TRP A 1 667  ? 97.230  123.714 120.741 1.00 63.18  ? 667  TRP A CE2 1 
ATOM   5451  C  CE3 . TRP A 1 667  ? 95.067  123.039 121.583 1.00 67.04  ? 667  TRP A CE3 1 
ATOM   5452  C  CZ2 . TRP A 1 667  ? 97.410  122.495 120.092 1.00 61.93  ? 667  TRP A CZ2 1 
ATOM   5453  C  CZ3 . TRP A 1 667  ? 95.249  121.829 120.939 1.00 66.24  ? 667  TRP A CZ3 1 
ATOM   5454  C  CH2 . TRP A 1 667  ? 96.409  121.568 120.203 1.00 71.21  ? 667  TRP A CH2 1 
ATOM   5455  N  N   . MET A 1 668  ? 96.465  123.653 124.603 1.00 61.38  ? 668  MET A N   1 
ATOM   5456  C  CA  . MET A 1 668  ? 96.404  122.216 124.884 1.00 60.47  ? 668  MET A CA  1 
ATOM   5457  C  C   . MET A 1 668  ? 96.180  121.947 126.363 1.00 63.86  ? 668  MET A C   1 
ATOM   5458  O  O   . MET A 1 668  ? 95.279  121.183 126.732 1.00 66.97  ? 668  MET A O   1 
ATOM   5459  C  CB  . MET A 1 668  ? 97.667  121.521 124.362 1.00 67.09  ? 668  MET A CB  1 
ATOM   5460  C  CG  . MET A 1 668  ? 97.712  119.960 124.374 1.00 45.14  ? 668  MET A CG  1 
ATOM   5461  S  SD  . MET A 1 668  ? 99.508  119.536 124.407 1.00 77.07  ? 668  MET A SD  1 
ATOM   5462  C  CE  . MET A 1 668  ? 99.883  118.892 126.062 1.00 68.72  ? 668  MET A CE  1 
ATOM   5463  N  N   . HIS A 1 669  ? 96.953  122.598 127.229 1.00 70.00  ? 669  HIS A N   1 
ATOM   5464  C  CA  . HIS A 1 669  ? 96.803  122.349 128.658 1.00 59.43  ? 669  HIS A CA  1 
ATOM   5465  C  C   . HIS A 1 669  ? 95.498  122.928 129.203 1.00 62.19  ? 669  HIS A C   1 
ATOM   5466  O  O   . HIS A 1 669  ? 94.965  122.431 130.205 1.00 69.35  ? 669  HIS A O   1 
ATOM   5467  C  CB  . HIS A 1 669  ? 98.018  122.887 129.413 1.00 65.98  ? 669  HIS A CB  1 
ATOM   5468  C  CG  . HIS A 1 669  ? 99.220  122.006 129.290 1.00 64.87  ? 669  HIS A CG  1 
ATOM   5469  N  ND1 . HIS A 1 669  ? 99.223  120.697 129.723 1.00 63.75  ? 669  HIS A ND1 1 
ATOM   5470  C  CD2 . HIS A 1 669  ? 100.427 122.216 128.714 1.00 60.04  ? 669  HIS A CD2 1 
ATOM   5471  C  CE1 . HIS A 1 669  ? 100.396 120.153 129.456 1.00 58.07  ? 669  HIS A CE1 1 
ATOM   5472  N  NE2 . HIS A 1 669  ? 101.143 121.052 128.842 1.00 61.38  ? 669  HIS A NE2 1 
ATOM   5473  N  N   . PHE A 1 670  ? 94.968  123.972 128.568 1.00 64.37  ? 670  PHE A N   1 
ATOM   5474  C  CA  . PHE A 1 670  ? 93.686  124.510 129.011 1.00 58.96  ? 670  PHE A CA  1 
ATOM   5475  C  C   . PHE A 1 670  ? 92.513  123.652 128.558 1.00 53.62  ? 670  PHE A C   1 
ATOM   5476  O  O   . PHE A 1 670  ? 91.521  123.533 129.287 1.00 57.08  ? 670  PHE A O   1 
ATOM   5477  C  CB  . PHE A 1 670  ? 93.469  125.932 128.490 1.00 66.36  ? 670  PHE A CB  1 
ATOM   5478  C  CG  . PHE A 1 670  ? 94.268  126.976 129.205 1.00 73.28  ? 670  PHE A CG  1 
ATOM   5479  C  CD1 . PHE A 1 670  ? 94.167  128.309 128.842 1.00 73.70  ? 670  PHE A CD1 1 
ATOM   5480  C  CD2 . PHE A 1 670  ? 95.128  126.630 130.231 1.00 71.21  ? 670  PHE A CD2 1 
ATOM   5481  C  CE1 . PHE A 1 670  ? 94.901  129.278 129.499 1.00 73.51  ? 670  PHE A CE1 1 
ATOM   5482  C  CE2 . PHE A 1 670  ? 95.868  127.592 130.887 1.00 85.41  ? 670  PHE A CE2 1 
ATOM   5483  C  CZ  . PHE A 1 670  ? 95.755  128.919 130.521 1.00 74.79  ? 670  PHE A CZ  1 
ATOM   5484  N  N   . LEU A 1 671  ? 92.600  123.043 127.378 1.00 57.51  ? 671  LEU A N   1 
ATOM   5485  C  CA  . LEU A 1 671  ? 91.447  122.378 126.783 1.00 56.81  ? 671  LEU A CA  1 
ATOM   5486  C  C   . LEU A 1 671  ? 91.385  120.878 127.028 1.00 65.48  ? 671  LEU A C   1 
ATOM   5487  O  O   . LEU A 1 671  ? 90.308  120.361 127.345 1.00 83.53  ? 671  LEU A O   1 
ATOM   5488  C  CB  . LEU A 1 671  ? 91.409  122.628 125.275 1.00 60.07  ? 671  LEU A CB  1 
ATOM   5489  C  CG  . LEU A 1 671  ? 90.188  121.974 124.626 1.00 61.29  ? 671  LEU A CG  1 
ATOM   5490  C  CD1 . LEU A 1 671  ? 88.901  122.621 125.122 1.00 60.94  ? 671  LEU A CD1 1 
ATOM   5491  C  CD2 . LEU A 1 671  ? 90.281  122.012 123.109 1.00 69.91  ? 671  LEU A CD2 1 
ATOM   5492  N  N   . ILE A 1 672  ? 92.503  120.158 126.911 1.00 56.46  ? 672  ILE A N   1 
ATOM   5493  C  CA  . ILE A 1 672  ? 92.453  118.692 126.934 1.00 59.00  ? 672  ILE A CA  1 
ATOM   5494  C  C   . ILE A 1 672  ? 91.852  118.129 128.219 1.00 61.96  ? 672  ILE A C   1 
ATOM   5495  O  O   . ILE A 1 672  ? 91.046  117.191 128.135 1.00 70.05  ? 672  ILE A O   1 
ATOM   5496  C  CB  . ILE A 1 672  ? 93.818  118.104 126.588 1.00 78.55  ? 672  ILE A CB  1 
ATOM   5497  C  CG1 . ILE A 1 672  ? 94.157  118.433 125.134 1.00 78.34  ? 672  ILE A CG1 1 
ATOM   5498  C  CG2 . ILE A 1 672  ? 93.817  116.594 126.757 1.00 83.01  ? 672  ILE A CG2 1 
ATOM   5499  C  CD1 . ILE A 1 672  ? 93.079  118.008 124.155 1.00 73.25  ? 672  ILE A CD1 1 
ATOM   5500  N  N   . PRO A 1 673  ? 92.177  118.631 129.432 1.00 62.04  ? 673  PRO A N   1 
ATOM   5501  C  CA  . PRO A 1 673  ? 91.558  118.040 130.632 1.00 61.18  ? 673  PRO A CA  1 
ATOM   5502  C  C   . PRO A 1 673  ? 90.044  118.215 130.740 1.00 66.53  ? 673  PRO A C   1 
ATOM   5503  O  O   . PRO A 1 673  ? 89.438  117.676 131.669 1.00 72.53  ? 673  PRO A O   1 
ATOM   5504  C  CB  . PRO A 1 673  ? 92.271  118.763 131.784 1.00 52.32  ? 673  PRO A CB  1 
ATOM   5505  C  CG  . PRO A 1 673  ? 93.565  119.218 131.210 1.00 51.37  ? 673  PRO A CG  1 
ATOM   5506  C  CD  . PRO A 1 673  ? 93.255  119.573 129.789 1.00 68.25  ? 673  PRO A CD  1 
ATOM   5507  N  N   . LEU A 1 674  ? 89.415  118.938 129.814 1.00 69.52  ? 674  LEU A N   1 
ATOM   5508  C  CA  . LEU A 1 674  ? 87.974  119.168 129.864 1.00 55.01  ? 674  LEU A CA  1 
ATOM   5509  C  C   . LEU A 1 674  ? 87.201  118.284 128.900 1.00 68.90  ? 674  LEU A C   1 
ATOM   5510  O  O   . LEU A 1 674  ? 85.979  118.394 128.822 1.00 77.91  ? 674  LEU A O   1 
ATOM   5511  C  CB  . LEU A 1 674  ? 87.630  120.630 129.582 1.00 49.01  ? 674  LEU A CB  1 
ATOM   5512  C  CG  . LEU A 1 674  ? 88.331  121.711 130.387 1.00 59.34  ? 674  LEU A CG  1 
ATOM   5513  C  CD1 . LEU A 1 674  ? 87.856  123.071 129.912 1.00 68.58  ? 674  LEU A CD1 1 
ATOM   5514  C  CD2 . LEU A 1 674  ? 88.022  121.518 131.863 1.00 58.77  ? 674  LEU A CD2 1 
ATOM   5515  N  N   . CYS A 1 675  ? 87.877  117.400 128.182 1.00 69.12  ? 675  CYS A N   1 
ATOM   5516  C  CA  . CYS A 1 675  ? 87.237  116.616 127.147 1.00 67.65  ? 675  CYS A CA  1 
ATOM   5517  C  C   . CYS A 1 675  ? 86.943  115.217 127.658 1.00 68.08  ? 675  CYS A C   1 
ATOM   5518  O  O   . CYS A 1 675  ? 87.385  114.798 128.729 1.00 75.13  ? 675  CYS A O   1 
ATOM   5519  C  CB  . CYS A 1 675  ? 88.098  116.570 125.883 1.00 59.66  ? 675  CYS A CB  1 
ATOM   5520  S  SG  . CYS A 1 675  ? 88.529  118.203 125.246 1.00 75.12  ? 675  CYS A SG  1 
ATOM   5521  N  N   . TYR A 1 676  ? 86.174  114.478 126.866 1.00 58.13  ? 676  TYR A N   1 
ATOM   5522  C  CA  . TYR A 1 676  ? 85.810  113.098 127.175 1.00 47.30  ? 676  TYR A CA  1 
ATOM   5523  C  C   . TYR A 1 676  ? 86.563  112.187 126.205 1.00 54.07  ? 676  TYR A C   1 
ATOM   5524  O  O   . TYR A 1 676  ? 86.253  112.165 125.010 1.00 60.49  ? 676  TYR A O   1 
ATOM   5525  C  CB  . TYR A 1 676  ? 84.294  112.923 127.056 1.00 66.51  ? 676  TYR A CB  1 
ATOM   5526  C  CG  . TYR A 1 676  ? 83.814  111.572 127.508 1.00 58.00  ? 676  TYR A CG  1 
ATOM   5527  C  CD1 . TYR A 1 676  ? 83.966  111.164 128.825 1.00 68.55  ? 676  TYR A CD1 1 
ATOM   5528  C  CD2 . TYR A 1 676  ? 83.186  110.710 126.625 1.00 51.25  ? 676  TYR A CD2 1 
ATOM   5529  C  CE1 . TYR A 1 676  ? 83.523  109.920 129.248 1.00 66.74  ? 676  TYR A CE1 1 
ATOM   5530  C  CE2 . TYR A 1 676  ? 82.738  109.469 127.038 1.00 46.44  ? 676  TYR A CE2 1 
ATOM   5531  C  CZ  . TYR A 1 676  ? 82.907  109.079 128.348 1.00 54.32  ? 676  TYR A CZ  1 
ATOM   5532  O  OH  . TYR A 1 676  ? 82.461  107.841 128.758 1.00 72.52  ? 676  TYR A OH  1 
ATOM   5533  N  N   . MET A 1 677  ? 87.546  111.445 126.716 1.00 51.13  ? 677  MET A N   1 
ATOM   5534  C  CA  . MET A 1 677  ? 88.463  110.721 125.848 1.00 51.05  ? 677  MET A CA  1 
ATOM   5535  C  C   . MET A 1 677  ? 87.871  109.377 125.446 1.00 55.55  ? 677  MET A C   1 
ATOM   5536  O  O   . MET A 1 677  ? 87.480  108.586 126.302 1.00 60.27  ? 677  MET A O   1 
ATOM   5537  C  CB  . MET A 1 677  ? 89.798  110.462 126.559 1.00 65.34  ? 677  MET A CB  1 
ATOM   5538  C  CG  . MET A 1 677  ? 90.437  111.676 127.174 1.00 58.39  ? 677  MET A CG  1 
ATOM   5539  S  SD  . MET A 1 677  ? 90.699  112.803 125.833 1.00 60.57  ? 677  MET A SD  1 
ATOM   5540  C  CE  . MET A 1 677  ? 91.832  111.809 124.919 1.00 69.45  ? 677  MET A CE  1 
ATOM   5541  N  N   . HIS A 1 678  ? 87.838  109.119 124.136 1.00 53.57  ? 678  HIS A N   1 
ATOM   5542  C  CA  . HIS A 1 678  ? 87.246  107.894 123.616 1.00 61.28  ? 678  HIS A CA  1 
ATOM   5543  C  C   . HIS A 1 678  ? 87.824  107.628 122.234 1.00 65.14  ? 678  HIS A C   1 
ATOM   5544  O  O   . HIS A 1 678  ? 88.475  108.490 121.630 1.00 73.49  ? 678  HIS A O   1 
ATOM   5545  C  CB  . HIS A 1 678  ? 85.723  107.983 123.554 1.00 54.16  ? 678  HIS A CB  1 
ATOM   5546  C  CG  . HIS A 1 678  ? 85.222  109.008 122.586 1.00 60.53  ? 678  HIS A CG  1 
ATOM   5547  N  ND1 . HIS A 1 678  ? 85.305  110.363 122.828 1.00 66.89  ? 678  HIS A ND1 1 
ATOM   5548  C  CD2 . HIS A 1 678  ? 84.634  108.876 121.372 1.00 66.66  ? 678  HIS A CD2 1 
ATOM   5549  C  CE1 . HIS A 1 678  ? 84.788  111.021 121.806 1.00 59.76  ? 678  HIS A CE1 1 
ATOM   5550  N  NE2 . HIS A 1 678  ? 84.374  110.143 120.910 1.00 69.40  ? 678  HIS A NE2 1 
ATOM   5551  N  N   . VAL A 1 679  ? 87.580  106.417 121.736 1.00 61.91  ? 679  VAL A N   1 
ATOM   5552  C  CA  . VAL A 1 679  ? 87.970  106.029 120.387 1.00 60.74  ? 679  VAL A CA  1 
ATOM   5553  C  C   . VAL A 1 679  ? 86.731  106.087 119.505 1.00 68.29  ? 679  VAL A C   1 
ATOM   5554  O  O   . VAL A 1 679  ? 85.665  105.579 119.880 1.00 74.75  ? 679  VAL A O   1 
ATOM   5555  C  CB  . VAL A 1 679  ? 88.600  104.629 120.355 1.00 65.01  ? 679  VAL A CB  1 
ATOM   5556  C  CG1 . VAL A 1 679  ? 88.943  104.234 118.924 1.00 75.05  ? 679  VAL A CG1 1 
ATOM   5557  C  CG2 . VAL A 1 679  ? 89.854  104.599 121.193 1.00 75.99  ? 679  VAL A CG2 1 
ATOM   5558  N  N   . SER A 1 680  ? 86.865  106.712 118.340 1.00 68.51  ? 680  SER A N   1 
ATOM   5559  C  CA  . SER A 1 680  ? 85.739  106.890 117.430 1.00 69.63  ? 680  SER A CA  1 
ATOM   5560  C  C   . SER A 1 680  ? 85.674  105.705 116.467 1.00 77.38  ? 680  SER A C   1 
ATOM   5561  O  O   . SER A 1 680  ? 85.816  105.828 115.251 1.00 72.10  ? 680  SER A O   1 
ATOM   5562  C  CB  . SER A 1 680  ? 85.865  108.212 116.686 1.00 73.59  ? 680  SER A CB  1 
ATOM   5563  O  OG  . SER A 1 680  ? 87.140  108.332 116.074 1.00 76.86  ? 680  SER A OG  1 
ATOM   5564  N  N   . ASP A 1 681  ? 85.445  104.530 117.052 1.00 89.31  ? 681  ASP A N   1 
ATOM   5565  C  CA  . ASP A 1 681  ? 85.242  103.313 116.280 1.00 86.72  ? 681  ASP A CA  1 
ATOM   5566  C  C   . ASP A 1 681  ? 83.767  103.205 115.939 1.00 82.85  ? 681  ASP A C   1 
ATOM   5567  O  O   . ASP A 1 681  ? 82.910  103.363 116.814 1.00 90.58  ? 681  ASP A O   1 
ATOM   5568  C  CB  . ASP A 1 681  ? 85.700  102.091 117.078 1.00 97.61  ? 681  ASP A CB  1 
ATOM   5569  C  CG  . ASP A 1 681  ? 87.144  101.723 116.799 1.00 132.78 ? 681  ASP A CG  1 
ATOM   5570  O  OD1 . ASP A 1 681  ? 87.664  102.106 115.730 1.00 135.82 ? 681  ASP A OD1 1 
ATOM   5571  O  OD2 . ASP A 1 681  ? 87.762  101.057 117.655 1.00 117.27 ? 681  ASP A OD2 1 
ATOM   5572  N  N   . PHE A 1 682  ? 83.475  102.939 114.668 1.00 73.12  ? 682  PHE A N   1 
ATOM   5573  C  CA  . PHE A 1 682  ? 82.091  103.010 114.217 1.00 70.61  ? 682  PHE A CA  1 
ATOM   5574  C  C   . PHE A 1 682  ? 81.222  101.970 114.921 1.00 74.48  ? 682  PHE A C   1 
ATOM   5575  O  O   . PHE A 1 682  ? 80.034  102.216 115.166 1.00 79.73  ? 682  PHE A O   1 
ATOM   5576  C  CB  . PHE A 1 682  ? 82.032  102.847 112.696 1.00 71.95  ? 682  PHE A CB  1 
ATOM   5577  C  CG  . PHE A 1 682  ? 80.711  103.243 112.090 1.00 72.49  ? 682  PHE A CG  1 
ATOM   5578  C  CD1 . PHE A 1 682  ? 79.583  102.449 112.198 1.00 79.37  ? 682  PHE A CD1 1 
ATOM   5579  C  CD2 . PHE A 1 682  ? 80.611  104.444 111.403 1.00 91.56  ? 682  PHE A CD2 1 
ATOM   5580  C  CE1 . PHE A 1 682  ? 78.381  102.849 111.638 1.00 78.92  ? 682  PHE A CE1 1 
ATOM   5581  C  CE2 . PHE A 1 682  ? 79.417  104.846 110.837 1.00 87.81  ? 682  PHE A CE2 1 
ATOM   5582  C  CZ  . PHE A 1 682  ? 78.300  104.048 110.955 1.00 77.07  ? 682  PHE A CZ  1 
ATOM   5583  N  N   . TYR A 1 683  ? 81.803  100.820 115.277 1.00 78.16  ? 683  TYR A N   1 
ATOM   5584  C  CA  . TYR A 1 683  ? 81.077  99.689  115.851 1.00 71.15  ? 683  TYR A CA  1 
ATOM   5585  C  C   . TYR A 1 683  ? 81.439  99.390  117.303 1.00 77.43  ? 683  TYR A C   1 
ATOM   5586  O  O   . TYR A 1 683  ? 81.148  98.292  117.787 1.00 81.27  ? 683  TYR A O   1 
ATOM   5587  C  CB  . TYR A 1 683  ? 81.308  98.437  115.005 1.00 64.28  ? 683  TYR A CB  1 
ATOM   5588  C  CG  . TYR A 1 683  ? 80.660  98.512  113.653 1.00 69.02  ? 683  TYR A CG  1 
ATOM   5589  C  CD1 . TYR A 1 683  ? 79.283  98.438  113.516 1.00 68.79  ? 683  TYR A CD1 1 
ATOM   5590  C  CD2 . TYR A 1 683  ? 81.426  98.668  112.508 1.00 77.02  ? 683  TYR A CD2 1 
ATOM   5591  C  CE1 . TYR A 1 683  ? 78.685  98.514  112.275 1.00 76.78  ? 683  TYR A CE1 1 
ATOM   5592  C  CE2 . TYR A 1 683  ? 80.840  98.744  111.264 1.00 84.53  ? 683  TYR A CE2 1 
ATOM   5593  C  CZ  . TYR A 1 683  ? 79.469  98.666  111.151 1.00 84.76  ? 683  TYR A CZ  1 
ATOM   5594  O  OH  . TYR A 1 683  ? 78.882  98.742  109.909 1.00 91.10  ? 683  TYR A OH  1 
ATOM   5595  N  N   . SER A 1 684  ? 82.064  100.321 118.015 1.00 78.00  ? 684  SER A N   1 
ATOM   5596  C  CA  . SER A 1 684  ? 82.423  100.107 119.419 1.00 65.13  ? 684  SER A CA  1 
ATOM   5597  C  C   . SER A 1 684  ? 82.228  101.383 120.223 1.00 71.44  ? 684  SER A C   1 
ATOM   5598  O  O   . SER A 1 684  ? 83.188  102.098 120.531 1.00 82.10  ? 684  SER A O   1 
ATOM   5599  C  CB  . SER A 1 684  ? 83.863  99.604  119.540 1.00 70.16  ? 684  SER A CB  1 
ATOM   5600  O  OG  . SER A 1 684  ? 83.972  98.252  119.126 1.00 88.07  ? 684  SER A OG  1 
ATOM   5601  N  N   . PRO A 1 685  ? 80.987  101.700 120.588 1.00 62.40  ? 685  PRO A N   1 
ATOM   5602  C  CA  . PRO A 1 685  ? 80.749  102.833 121.489 1.00 60.91  ? 685  PRO A CA  1 
ATOM   5603  C  C   . PRO A 1 685  ? 81.245  102.530 122.891 1.00 60.52  ? 685  PRO A C   1 
ATOM   5604  O  O   . PRO A 1 685  ? 81.612  101.385 123.199 1.00 74.24  ? 685  PRO A O   1 
ATOM   5605  C  CB  . PRO A 1 685  ? 79.218  102.987 121.465 1.00 73.24  ? 685  PRO A CB  1 
ATOM   5606  C  CG  . PRO A 1 685  ? 78.702  101.666 120.995 1.00 71.68  ? 685  PRO A CG  1 
ATOM   5607  C  CD  . PRO A 1 685  ? 79.733  101.143 120.051 1.00 58.58  ? 685  PRO A CD  1 
ATOM   5608  N  N   . PRO A 1 686  ? 81.287  103.538 123.766 1.00 61.68  ? 686  PRO A N   1 
ATOM   5609  C  CA  . PRO A 1 686  ? 81.636  103.295 125.173 1.00 63.26  ? 686  PRO A CA  1 
ATOM   5610  C  C   . PRO A 1 686  ? 80.701  102.290 125.834 1.00 79.89  ? 686  PRO A C   1 
ATOM   5611  O  O   . PRO A 1 686  ? 79.507  102.237 125.536 1.00 92.77  ? 686  PRO A O   1 
ATOM   5612  C  CB  . PRO A 1 686  ? 81.514  104.681 125.807 1.00 63.17  ? 686  PRO A CB  1 
ATOM   5613  C  CG  . PRO A 1 686  ? 81.818  105.622 124.687 1.00 57.50  ? 686  PRO A CG  1 
ATOM   5614  C  CD  . PRO A 1 686  ? 81.281  104.977 123.439 1.00 63.85  ? 686  PRO A CD  1 
ATOM   5615  N  N   . HIS A 1 687  ? 81.272  101.477 126.730 1.00 74.74  ? 687  HIS A N   1 
ATOM   5616  C  CA  . HIS A 1 687  ? 80.567  100.320 127.281 1.00 82.09  ? 687  HIS A CA  1 
ATOM   5617  C  C   . HIS A 1 687  ? 79.256  100.697 127.966 1.00 87.44  ? 687  HIS A C   1 
ATOM   5618  O  O   . HIS A 1 687  ? 78.307  99.904  127.961 1.00 90.63  ? 687  HIS A O   1 
ATOM   5619  C  CB  . HIS A 1 687  ? 81.457  99.607  128.300 1.00 99.32  ? 687  HIS A CB  1 
ATOM   5620  C  CG  . HIS A 1 687  ? 82.553  98.782  127.700 1.00 90.06  ? 687  HIS A CG  1 
ATOM   5621  N  ND1 . HIS A 1 687  ? 83.299  99.194  126.618 1.00 88.62  ? 687  HIS A ND1 1 
ATOM   5622  C  CD2 . HIS A 1 687  ? 83.056  97.578  128.068 1.00 92.85  ? 687  HIS A CD2 1 
ATOM   5623  C  CE1 . HIS A 1 687  ? 84.195  98.266  126.327 1.00 86.31  ? 687  HIS A CE1 1 
ATOM   5624  N  NE2 . HIS A 1 687  ? 84.068  97.278  127.192 1.00 88.65  ? 687  HIS A NE2 1 
ATOM   5625  N  N   . CYS A 1 688  ? 79.176  101.892 128.553 1.00 91.80  ? 688  CYS A N   1 
ATOM   5626  C  CA  . CYS A 1 688  ? 78.130  102.187 129.528 1.00 98.50  ? 688  CYS A CA  1 
ATOM   5627  C  C   . CYS A 1 688  ? 77.216  103.355 129.171 1.00 106.37 ? 688  CYS A C   1 
ATOM   5628  O  O   . CYS A 1 688  ? 76.397  103.754 130.007 1.00 110.03 ? 688  CYS A O   1 
ATOM   5629  C  CB  . CYS A 1 688  ? 78.778  102.449 130.888 1.00 113.98 ? 688  CYS A CB  1 
ATOM   5630  S  SG  . CYS A 1 688  ? 79.840  103.910 130.879 1.00 121.61 ? 688  CYS A SG  1 
ATOM   5631  N  N   . VAL A 1 689  ? 77.308  103.909 127.966 1.00 103.77 ? 689  VAL A N   1 
ATOM   5632  C  CA  . VAL A 1 689  ? 76.541  105.105 127.623 1.00 106.93 ? 689  VAL A CA  1 
ATOM   5633  C  C   . VAL A 1 689  ? 75.113  104.711 127.260 1.00 105.01 ? 689  VAL A C   1 
ATOM   5634  O  O   . VAL A 1 689  ? 74.893  103.789 126.466 1.00 108.09 ? 689  VAL A O   1 
ATOM   5635  C  CB  . VAL A 1 689  ? 77.221  105.889 126.487 1.00 93.83  ? 689  VAL A CB  1 
ATOM   5636  C  CG1 . VAL A 1 689  ? 77.466  105.003 125.273 1.00 101.68 ? 689  VAL A CG1 1 
ATOM   5637  C  CG2 . VAL A 1 689  ? 76.385  107.110 126.109 1.00 89.29  ? 689  VAL A CG2 1 
ATOM   5638  N  N   . THR A 1 690  ? 74.128  105.394 127.858 1.00 99.03  ? 690  THR A N   1 
ATOM   5639  C  CA  . THR A 1 690  ? 72.735  105.159 127.483 1.00 105.74 ? 690  THR A CA  1 
ATOM   5640  C  C   . THR A 1 690  ? 72.058  106.474 127.101 1.00 107.70 ? 690  THR A C   1 
ATOM   5641  O  O   . THR A 1 690  ? 72.727  107.509 127.010 1.00 107.89 ? 690  THR A O   1 
ATOM   5642  C  CB  . THR A 1 690  ? 71.961  104.472 128.621 1.00 109.99 ? 690  THR A CB  1 
ATOM   5643  O  OG1 . THR A 1 690  ? 71.685  105.417 129.662 1.00 109.08 ? 690  THR A OG1 1 
ATOM   5644  C  CG2 . THR A 1 690  ? 72.756  103.305 129.205 1.00 118.74 ? 690  THR A CG2 1 
ATOM   5645  N  N   . GLU A 1 691  ? 70.735  106.451 126.898 1.00 102.42 ? 691  GLU A N   1 
ATOM   5646  C  CA  . GLU A 1 691  ? 70.043  107.627 126.379 1.00 98.42  ? 691  GLU A CA  1 
ATOM   5647  C  C   . GLU A 1 691  ? 69.996  108.747 127.408 1.00 108.56 ? 691  GLU A C   1 
ATOM   5648  O  O   . GLU A 1 691  ? 70.338  109.895 127.107 1.00 113.30 ? 691  GLU A O   1 
ATOM   5649  C  CB  . GLU A 1 691  ? 68.621  107.240 125.950 1.00 110.32 ? 691  GLU A CB  1 
ATOM   5650  C  CG  . GLU A 1 691  ? 67.802  108.417 125.519 1.00 126.74 ? 691  GLU A CG  1 
ATOM   5651  C  CD  . GLU A 1 691  ? 66.762  108.040 124.507 1.00 141.39 ? 691  GLU A CD  1 
ATOM   5652  O  OE1 . GLU A 1 691  ? 66.768  108.634 123.411 1.00 138.27 ? 691  GLU A OE1 1 
ATOM   5653  O  OE2 . GLU A 1 691  ? 65.950  107.135 124.798 1.00 139.35 ? 691  GLU A OE2 1 
ATOM   5654  N  N   . ASP A 1 692  ? 69.573  108.419 128.625 1.00 111.53 ? 692  ASP A N   1 
ATOM   5655  C  CA  . ASP A 1 692  ? 69.519  109.400 129.697 1.00 108.93 ? 692  ASP A CA  1 
ATOM   5656  C  C   . ASP A 1 692  ? 70.899  109.695 130.261 1.00 99.01  ? 692  ASP A C   1 
ATOM   5657  O  O   . ASP A 1 692  ? 71.159  110.809 130.747 1.00 96.58  ? 692  ASP A O   1 
ATOM   5658  C  CB  . ASP A 1 692  ? 68.591  108.880 130.787 1.00 114.76 ? 692  ASP A CB  1 
ATOM   5659  C  CG  . ASP A 1 692  ? 68.904  107.473 131.184 1.00 117.17 ? 692  ASP A CG  1 
ATOM   5660  O  OD1 . ASP A 1 692  ? 69.806  106.862 130.554 1.00 105.30 ? 692  ASP A OD1 1 
ATOM   5661  O  OD2 . ASP A 1 692  ? 68.418  107.033 132.250 1.00 129.39 ? 692  ASP A OD2 1 
ATOM   5662  N  N   . ASN A 1 693  ? 71.829  108.732 130.200 1.00 108.39 ? 693  ASN A N   1 
ATOM   5663  C  CA  . ASN A 1 693  ? 73.214  108.851 130.649 1.00 98.43  ? 693  ASN A CA  1 
ATOM   5664  C  C   . ASN A 1 693  ? 74.060  109.696 129.682 1.00 97.08  ? 693  ASN A C   1 
ATOM   5665  O  O   . ASN A 1 693  ? 75.200  110.048 129.981 1.00 102.44 ? 693  ASN A O   1 
ATOM   5666  C  CB  . ASN A 1 693  ? 73.765  107.424 130.788 1.00 106.40 ? 693  ASN A CB  1 
ATOM   5667  C  CG  . ASN A 1 693  ? 75.179  107.355 131.310 1.00 106.21 ? 693  ASN A CG  1 
ATOM   5668  O  OD1 . ASN A 1 693  ? 75.798  108.352 131.678 1.00 112.97 ? 693  ASN A OD1 1 
ATOM   5669  N  ND2 . ASN A 1 693  ? 75.700  106.138 131.353 1.00 104.11 ? 693  ASN A ND2 1 
ATOM   5670  N  N   . ARG A 1 694  ? 73.486  110.089 128.555 1.00 106.87 ? 694  ARG A N   1 
ATOM   5671  C  CA  . ARG A 1 694  ? 74.277  110.534 127.419 1.00 91.85  ? 694  ARG A CA  1 
ATOM   5672  C  C   . ARG A 1 694  ? 74.964  111.872 127.670 1.00 87.78  ? 694  ARG A C   1 
ATOM   5673  O  O   . ARG A 1 694  ? 76.075  112.102 127.177 1.00 85.51  ? 694  ARG A O   1 
ATOM   5674  C  CB  . ARG A 1 694  ? 73.401  110.573 126.181 1.00 115.27 ? 694  ARG A CB  1 
ATOM   5675  C  CG  . ARG A 1 694  ? 74.148  110.862 124.930 1.00 109.73 ? 694  ARG A CG  1 
ATOM   5676  C  CD  . ARG A 1 694  ? 73.240  111.256 123.803 1.00 95.01  ? 694  ARG A CD  1 
ATOM   5677  N  NE  . ARG A 1 694  ? 72.834  112.667 123.727 1.00 96.75  ? 694  ARG A NE  1 
ATOM   5678  C  CZ  . ARG A 1 694  ? 73.317  113.526 122.827 1.00 94.78  ? 694  ARG A CZ  1 
ATOM   5679  N  NH1 . ARG A 1 694  ? 74.220  113.121 121.948 1.00 104.22 ? 694  ARG A NH1 1 
ATOM   5680  N  NH2 . ARG A 1 694  ? 72.905  114.788 122.795 1.00 112.06 ? 694  ARG A NH2 1 
ATOM   5681  N  N   . ASN A 1 695  ? 74.328  112.774 128.425 1.00 104.75 ? 695  ASN A N   1 
ATOM   5682  C  CA  . ASN A 1 695  ? 74.879  114.116 128.596 1.00 108.49 ? 695  ASN A CA  1 
ATOM   5683  C  C   . ASN A 1 695  ? 76.141  114.118 129.450 1.00 118.12 ? 695  ASN A C   1 
ATOM   5684  O  O   . ASN A 1 695  ? 77.102  114.832 129.135 1.00 118.58 ? 695  ASN A O   1 
ATOM   5685  C  CB  . ASN A 1 695  ? 73.832  115.034 129.233 1.00 108.65 ? 695  ASN A CB  1 
ATOM   5686  C  CG  . ASN A 1 695  ? 72.815  115.526 128.239 1.00 123.75 ? 695  ASN A CG  1 
ATOM   5687  O  OD1 . ASN A 1 695  ? 73.104  116.376 127.399 1.00 120.51 ? 695  ASN A OD1 1 
ATOM   5688  N  ND2 . ASN A 1 695  ? 71.615  114.963 128.304 1.00 130.11 ? 695  ASN A ND2 1 
ATOM   5689  N  N   . ASN A 1 696  ? 76.175  113.329 130.517 1.00 113.77 ? 696  ASN A N   1 
ATOM   5690  C  CA  . ASN A 1 696  ? 77.348  113.226 131.382 1.00 109.09 ? 696  ASN A CA  1 
ATOM   5691  C  C   . ASN A 1 696  ? 77.648  111.749 131.587 1.00 105.63 ? 696  ASN A C   1 
ATOM   5692  O  O   . ASN A 1 696  ? 77.301  111.167 132.623 1.00 108.39 ? 696  ASN A O   1 
ATOM   5693  C  CB  . ASN A 1 696  ? 77.119  113.952 132.711 1.00 112.13 ? 696  ASN A CB  1 
ATOM   5694  C  CG  . ASN A 1 696  ? 78.386  114.076 133.533 1.00 123.19 ? 696  ASN A CG  1 
ATOM   5695  O  OD1 . ASN A 1 696  ? 78.679  113.231 134.381 1.00 122.79 ? 696  ASN A OD1 1 
ATOM   5696  N  ND2 . ASN A 1 696  ? 79.147  115.134 133.285 1.00 121.43 ? 696  ASN A ND2 1 
ATOM   5697  N  N   . PRO A 1 697  ? 78.301  111.110 130.617 1.00 86.52  ? 697  PRO A N   1 
ATOM   5698  C  CA  . PRO A 1 697  ? 78.551  109.672 130.722 1.00 84.07  ? 697  PRO A CA  1 
ATOM   5699  C  C   . PRO A 1 697  ? 79.663  109.382 131.713 1.00 88.91  ? 697  PRO A C   1 
ATOM   5700  O  O   . PRO A 1 697  ? 80.536  110.230 131.954 1.00 96.76  ? 697  PRO A O   1 
ATOM   5701  C  CB  . PRO A 1 697  ? 78.958  109.280 129.295 1.00 82.36  ? 697  PRO A CB  1 
ATOM   5702  C  CG  . PRO A 1 697  ? 79.555  110.523 128.724 1.00 78.20  ? 697  PRO A CG  1 
ATOM   5703  C  CD  . PRO A 1 697  ? 78.882  111.694 129.395 1.00 75.90  ? 697  PRO A CD  1 
ATOM   5704  N  N   . PRO A 1 698  ? 79.660  108.193 132.309 1.00 83.98  ? 698  PRO A N   1 
ATOM   5705  C  CA  . PRO A 1 698  ? 80.675  107.859 133.312 1.00 88.31  ? 698  PRO A CA  1 
ATOM   5706  C  C   . PRO A 1 698  ? 81.910  107.218 132.706 1.00 79.41  ? 698  PRO A C   1 
ATOM   5707  O  O   . PRO A 1 698  ? 82.025  107.080 131.484 1.00 82.77  ? 698  PRO A O   1 
ATOM   5708  C  CB  . PRO A 1 698  ? 79.928  106.892 134.235 1.00 100.50 ? 698  PRO A CB  1 
ATOM   5709  C  CG  . PRO A 1 698  ? 79.015  106.168 133.304 1.00 94.96  ? 698  PRO A CG  1 
ATOM   5710  C  CD  . PRO A 1 698  ? 78.619  107.154 132.224 1.00 88.74  ? 698  PRO A CD  1 
ATOM   5711  N  N   . ASP A 1 699  ? 82.846  106.841 133.569 1.00 76.35  ? 699  ASP A N   1 
ATOM   5712  C  CA  . ASP A 1 699  ? 84.044  106.130 133.152 1.00 73.04  ? 699  ASP A CA  1 
ATOM   5713  C  C   . ASP A 1 699  ? 83.748  104.651 132.948 1.00 83.02  ? 699  ASP A C   1 
ATOM   5714  O  O   . ASP A 1 699  ? 82.944  104.054 133.669 1.00 93.66  ? 699  ASP A O   1 
ATOM   5715  C  CB  . ASP A 1 699  ? 85.159  106.296 134.183 1.00 89.39  ? 699  ASP A CB  1 
ATOM   5716  C  CG  . ASP A 1 699  ? 85.655  107.719 134.277 1.00 96.23  ? 699  ASP A CG  1 
ATOM   5717  O  OD1 . ASP A 1 699  ? 85.029  108.610 133.664 1.00 93.35  ? 699  ASP A OD1 1 
ATOM   5718  O  OD2 . ASP A 1 699  ? 86.678  107.947 134.954 1.00 95.51  ? 699  ASP A OD2 1 
ATOM   5719  N  N   . CYS A 1 700  ? 84.408  104.066 131.957 1.00 74.05  ? 700  CYS A N   1 
ATOM   5720  C  CA  . CYS A 1 700  ? 84.292  102.645 131.668 1.00 78.99  ? 700  CYS A CA  1 
ATOM   5721  C  C   . CYS A 1 700  ? 85.632  102.198 131.093 1.00 77.46  ? 700  CYS A C   1 
ATOM   5722  O  O   . CYS A 1 700  ? 86.636  102.908 131.212 1.00 81.25  ? 700  CYS A O   1 
ATOM   5723  C  CB  . CYS A 1 700  ? 83.091  102.368 130.745 1.00 72.57  ? 700  CYS A CB  1 
ATOM   5724  S  SG  . CYS A 1 700  ? 83.131  103.207 129.147 1.00 114.62 ? 700  CYS A SG  1 
ATOM   5725  N  N   . ALA A 1 701  ? 85.658  101.024 130.463 1.00 77.68  ? 701  ALA A N   1 
ATOM   5726  C  CA  . ALA A 1 701  ? 86.914  100.532 129.910 1.00 84.49  ? 701  ALA A CA  1 
ATOM   5727  C  C   . ALA A 1 701  ? 87.372  101.355 128.711 1.00 86.35  ? 701  ALA A C   1 
ATOM   5728  O  O   . ALA A 1 701  ? 88.570  101.622 128.561 1.00 76.89  ? 701  ALA A O   1 
ATOM   5729  C  CB  . ALA A 1 701  ? 86.772  99.059  129.523 1.00 78.82  ? 701  ALA A CB  1 
ATOM   5730  N  N   . ASN A 1 702  ? 86.439  101.788 127.860 1.00 85.55  ? 702  ASN A N   1 
ATOM   5731  C  CA  . ASN A 1 702  ? 86.819  102.589 126.700 1.00 67.33  ? 702  ASN A CA  1 
ATOM   5732  C  C   . ASN A 1 702  ? 87.215  104.010 127.083 1.00 75.17  ? 702  ASN A C   1 
ATOM   5733  O  O   . ASN A 1 702  ? 88.249  104.514 126.634 1.00 75.51  ? 702  ASN A O   1 
ATOM   5734  C  CB  . ASN A 1 702  ? 85.687  102.627 125.674 1.00 59.40  ? 702  ASN A CB  1 
ATOM   5735  C  CG  . ASN A 1 702  ? 85.517  101.317 124.945 1.00 64.33  ? 702  ASN A CG  1 
ATOM   5736  O  OD1 . ASN A 1 702  ? 84.434  100.739 124.939 1.00 79.85  ? 702  ASN A OD1 1 
ATOM   5737  N  ND2 . ASN A 1 702  ? 86.593  100.830 124.341 1.00 77.83  ? 702  ASN A ND2 1 
ATOM   5738  N  N   . ALA A 1 703  ? 86.435  104.668 127.933 1.00 66.71  ? 703  ALA A N   1 
ATOM   5739  C  CA  . ALA A 1 703  ? 86.520  106.116 128.027 1.00 49.11  ? 703  ALA A CA  1 
ATOM   5740  C  C   . ALA A 1 703  ? 86.730  106.553 129.468 1.00 69.33  ? 703  ALA A C   1 
ATOM   5741  O  O   . ALA A 1 703  ? 86.454  105.814 130.415 1.00 87.12  ? 703  ALA A O   1 
ATOM   5742  C  CB  . ALA A 1 703  ? 85.259  106.775 127.455 1.00 61.41  ? 703  ALA A CB  1 
ATOM   5743  N  N   . TYR A 1 704  ? 87.243  107.773 129.612 1.00 52.12  ? 704  TYR A N   1 
ATOM   5744  C  CA  . TYR A 1 704  ? 87.583  108.326 130.915 1.00 60.17  ? 704  TYR A CA  1 
ATOM   5745  C  C   . TYR A 1 704  ? 87.648  109.844 130.813 1.00 67.01  ? 704  TYR A C   1 
ATOM   5746  O  O   . TYR A 1 704  ? 87.589  110.420 129.724 1.00 74.10  ? 704  TYR A O   1 
ATOM   5747  C  CB  . TYR A 1 704  ? 88.906  107.746 131.419 1.00 80.15  ? 704  TYR A CB  1 
ATOM   5748  C  CG  . TYR A 1 704  ? 90.093  108.132 130.564 1.00 66.50  ? 704  TYR A CG  1 
ATOM   5749  C  CD1 . TYR A 1 704  ? 90.404  107.428 129.408 1.00 67.00  ? 704  TYR A CD1 1 
ATOM   5750  C  CD2 . TYR A 1 704  ? 90.908  109.197 130.918 1.00 68.58  ? 704  TYR A CD2 1 
ATOM   5751  C  CE1 . TYR A 1 704  ? 91.489  107.782 128.622 1.00 56.97  ? 704  TYR A CE1 1 
ATOM   5752  C  CE2 . TYR A 1 704  ? 91.995  109.556 130.141 1.00 65.01  ? 704  TYR A CE2 1 
ATOM   5753  C  CZ  . TYR A 1 704  ? 92.282  108.847 128.995 1.00 56.79  ? 704  TYR A CZ  1 
ATOM   5754  O  OH  . TYR A 1 704  ? 93.364  109.202 128.221 1.00 60.60  ? 704  TYR A OH  1 
ATOM   5755  N  N   . HIS A 1 705  ? 87.766  110.485 131.974 1.00 76.74  ? 705  HIS A N   1 
ATOM   5756  C  CA  . HIS A 1 705  ? 87.903  111.929 132.092 1.00 62.02  ? 705  HIS A CA  1 
ATOM   5757  C  C   . HIS A 1 705  ? 89.305  112.274 132.580 1.00 67.90  ? 705  HIS A C   1 
ATOM   5758  O  O   . HIS A 1 705  ? 90.043  111.420 133.077 1.00 83.09  ? 705  HIS A O   1 
ATOM   5759  C  CB  . HIS A 1 705  ? 86.872  112.526 133.058 1.00 64.64  ? 705  HIS A CB  1 
ATOM   5760  C  CG  . HIS A 1 705  ? 85.473  112.562 132.525 1.00 75.59  ? 705  HIS A CG  1 
ATOM   5761  N  ND1 . HIS A 1 705  ? 84.497  111.677 132.929 1.00 80.24  ? 705  HIS A ND1 1 
ATOM   5762  C  CD2 . HIS A 1 705  ? 84.879  113.399 131.640 1.00 78.42  ? 705  HIS A CD2 1 
ATOM   5763  C  CE1 . HIS A 1 705  ? 83.367  111.957 132.307 1.00 73.06  ? 705  HIS A CE1 1 
ATOM   5764  N  NE2 . HIS A 1 705  ? 83.571  112.998 131.519 1.00 73.92  ? 705  HIS A NE2 1 
ATOM   5765  N  N   . TYR A 1 706  ? 89.663  113.549 132.424 1.00 64.67  ? 706  TYR A N   1 
ATOM   5766  C  CA  . TYR A 1 706  ? 90.862  114.140 133.023 1.00 71.50  ? 706  TYR A CA  1 
ATOM   5767  C  C   . TYR A 1 706  ? 92.139  113.508 132.468 1.00 65.11  ? 706  TYR A C   1 
ATOM   5768  O  O   . TYR A 1 706  ? 92.963  112.955 133.199 1.00 73.92  ? 706  TYR A O   1 
ATOM   5769  C  CB  . TYR A 1 706  ? 90.839  114.050 134.552 1.00 59.35  ? 706  TYR A CB  1 
ATOM   5770  C  CG  . TYR A 1 706  ? 89.565  114.531 135.193 1.00 72.89  ? 706  TYR A CG  1 
ATOM   5771  C  CD1 . TYR A 1 706  ? 89.065  115.795 134.916 1.00 68.22  ? 706  TYR A CD1 1 
ATOM   5772  C  CD2 . TYR A 1 706  ? 88.877  113.737 136.096 1.00 89.28  ? 706  TYR A CD2 1 
ATOM   5773  C  CE1 . TYR A 1 706  ? 87.905  116.248 135.509 1.00 68.07  ? 706  TYR A CE1 1 
ATOM   5774  C  CE2 . TYR A 1 706  ? 87.716  114.180 136.694 1.00 86.46  ? 706  TYR A CE2 1 
ATOM   5775  C  CZ  . TYR A 1 706  ? 87.235  115.438 136.397 1.00 83.23  ? 706  TYR A CZ  1 
ATOM   5776  O  OH  . TYR A 1 706  ? 86.075  115.884 136.990 1.00 100.47 ? 706  TYR A OH  1 
ATOM   5777  N  N   . HIS A 1 707  ? 92.291  113.601 131.152 1.00 59.32  ? 707  HIS A N   1 
ATOM   5778  C  CA  . HIS A 1 707  ? 93.586  113.341 130.545 1.00 52.24  ? 707  HIS A CA  1 
ATOM   5779  C  C   . HIS A 1 707  ? 94.519  114.465 130.977 1.00 59.53  ? 707  HIS A C   1 
ATOM   5780  O  O   . HIS A 1 707  ? 94.183  115.644 130.836 1.00 76.31  ? 707  HIS A O   1 
ATOM   5781  C  CB  . HIS A 1 707  ? 93.450  113.277 129.026 1.00 71.22  ? 707  HIS A CB  1 
ATOM   5782  C  CG  . HIS A 1 707  ? 94.627  112.665 128.333 1.00 65.96  ? 707  HIS A CG  1 
ATOM   5783  N  ND1 . HIS A 1 707  ? 94.653  111.343 127.944 1.00 70.24  ? 707  HIS A ND1 1 
ATOM   5784  C  CD2 . HIS A 1 707  ? 95.818  113.191 127.963 1.00 73.22  ? 707  HIS A CD2 1 
ATOM   5785  C  CE1 . HIS A 1 707  ? 95.807  111.083 127.356 1.00 70.42  ? 707  HIS A CE1 1 
ATOM   5786  N  NE2 . HIS A 1 707  ? 96.533  112.187 127.360 1.00 74.21  ? 707  HIS A NE2 1 
ATOM   5787  N  N   . LEU A 1 708  ? 95.693  114.116 131.506 1.00 63.81  ? 708  LEU A N   1 
ATOM   5788  C  CA  . LEU A 1 708  ? 96.575  115.134 132.059 1.00 61.50  ? 708  LEU A CA  1 
ATOM   5789  C  C   . LEU A 1 708  ? 97.855  115.371 131.276 1.00 70.18  ? 708  LEU A C   1 
ATOM   5790  O  O   . LEU A 1 708  ? 98.514  116.392 131.512 1.00 60.34  ? 708  LEU A O   1 
ATOM   5791  C  CB  . LEU A 1 708  ? 96.940  114.774 133.508 1.00 52.15  ? 708  LEU A CB  1 
ATOM   5792  C  CG  . LEU A 1 708  ? 95.778  114.869 134.496 1.00 57.20  ? 708  LEU A CG  1 
ATOM   5793  C  CD1 . LEU A 1 708  ? 96.248  114.573 135.914 1.00 50.92  ? 708  LEU A CD1 1 
ATOM   5794  C  CD2 . LEU A 1 708  ? 95.108  116.236 134.409 1.00 57.31  ? 708  LEU A CD2 1 
ATOM   5795  N  N   . GLY A 1 709  ? 98.225  114.495 130.352 1.00 72.52  ? 709  GLY A N   1 
ATOM   5796  C  CA  . GLY A 1 709  ? 99.443  114.658 129.597 1.00 68.08  ? 709  GLY A CA  1 
ATOM   5797  C  C   . GLY A 1 709  ? 99.220  115.279 128.232 1.00 70.15  ? 709  GLY A C   1 
ATOM   5798  O  O   . GLY A 1 709  ? 98.199  115.914 127.962 1.00 76.03  ? 709  GLY A O   1 
ATOM   5799  N  N   . GLY A 1 710  ? 100.198 115.088 127.351 1.00 69.39  ? 710  GLY A N   1 
ATOM   5800  C  CA  . GLY A 1 710  ? 100.095 115.513 125.972 1.00 61.96  ? 710  GLY A CA  1 
ATOM   5801  C  C   . GLY A 1 710  ? 99.618  114.424 125.049 1.00 75.24  ? 710  GLY A C   1 
ATOM   5802  O  O   . GLY A 1 710  ? 99.318  113.295 125.456 1.00 86.42  ? 710  GLY A O   1 
ATOM   5803  N  N   . ILE A 1 711  ? 99.536  114.772 123.757 1.00 72.43  ? 711  ILE A N   1 
ATOM   5804  C  CA  . ILE A 1 711  ? 99.184  113.791 122.729 1.00 78.05  ? 711  ILE A CA  1 
ATOM   5805  C  C   . ILE A 1 711  ? 100.163 113.845 121.564 1.00 89.28  ? 711  ILE A C   1 
ATOM   5806  O  O   . ILE A 1 711  ? 100.933 114.793 121.393 1.00 90.58  ? 711  ILE A O   1 
ATOM   5807  C  CB  . ILE A 1 711  ? 97.688  113.748 122.285 1.00 79.74  ? 711  ILE A CB  1 
ATOM   5808  C  CG1 . ILE A 1 711  ? 96.825  113.432 123.493 1.00 83.02  ? 711  ILE A CG1 1 
ATOM   5809  C  CG2 . ILE A 1 711  ? 97.309  112.838 121.155 1.00 95.18  ? 711  ILE A CG2 1 
ATOM   5810  C  CD1 . ILE A 1 711  ? 95.417  113.898 123.375 1.00 81.07  ? 711  ILE A CD1 1 
ATOM   5811  N  N   . GLU A 1 712  ? 100.160 112.752 120.800 1.00 88.32  ? 712  GLU A N   1 
ATOM   5812  C  CA  . GLU A 1 712  ? 101.351 112.404 120.035 1.00 96.32  ? 712  GLU A CA  1 
ATOM   5813  C  C   . GLU A 1 712  ? 101.912 113.558 119.203 1.00 93.06  ? 712  GLU A C   1 
ATOM   5814  O  O   . GLU A 1 712  ? 103.138 113.734 119.144 1.00 103.83 ? 712  GLU A O   1 
ATOM   5815  C  CB  . GLU A 1 712  ? 101.158 111.079 119.267 1.00 111.69 ? 712  GLU A CB  1 
ATOM   5816  C  CG  . GLU A 1 712  ? 102.534 110.589 118.731 1.00 133.32 ? 712  GLU A CG  1 
ATOM   5817  C  CD  . GLU A 1 712  ? 102.650 110.771 117.216 1.00 145.52 ? 712  GLU A CD  1 
ATOM   5818  O  OE1 . GLU A 1 712  ? 102.565 109.685 116.643 1.00 132.37 ? 712  GLU A OE1 1 
ATOM   5819  O  OE2 . GLU A 1 712  ? 102.661 111.936 116.691 1.00 146.90 ? 712  GLU A OE2 1 
ATOM   5820  N  N   . GLY A 1 713  ? 101.074 114.304 118.500 1.00 83.84  ? 713  GLY A N   1 
ATOM   5821  C  CA  . GLY A 1 713  ? 101.668 115.309 117.619 1.00 91.24  ? 713  GLY A CA  1 
ATOM   5822  C  C   . GLY A 1 713  ? 101.187 116.731 117.850 1.00 76.86  ? 713  GLY A C   1 
ATOM   5823  O  O   . GLY A 1 713  ? 101.337 117.565 116.961 1.00 80.80  ? 713  GLY A O   1 
ATOM   5824  N  N   . LEU A 1 714  ? 100.651 117.033 119.037 1.00 75.06  ? 714  LEU A N   1 
ATOM   5825  C  CA  . LEU A 1 714  ? 100.017 118.335 119.192 1.00 75.29  ? 714  LEU A CA  1 
ATOM   5826  C  C   . LEU A 1 714  ? 101.019 119.481 119.344 1.00 76.02  ? 714  LEU A C   1 
ATOM   5827  O  O   . LEU A 1 714  ? 100.770 120.599 118.872 1.00 80.46  ? 714  LEU A O   1 
ATOM   5828  C  CB  . LEU A 1 714  ? 99.050  118.336 120.382 1.00 80.49  ? 714  LEU A CB  1 
ATOM   5829  C  CG  . LEU A 1 714  ? 97.896  117.344 120.199 1.00 74.36  ? 714  LEU A CG  1 
ATOM   5830  C  CD1 . LEU A 1 714  ? 96.752  117.578 121.226 1.00 71.37  ? 714  LEU A CD1 1 
ATOM   5831  C  CD2 . LEU A 1 714  ? 97.379  117.144 118.736 1.00 76.17  ? 714  LEU A CD2 1 
ATOM   5832  N  N   . GLN A 1 715  ? 102.135 119.255 120.026 1.00 75.64  ? 715  GLN A N   1 
ATOM   5833  C  CA  . GLN A 1 715  ? 103.074 120.336 120.294 1.00 70.63  ? 715  GLN A CA  1 
ATOM   5834  C  C   . GLN A 1 715  ? 104.503 119.866 120.100 1.00 74.10  ? 715  GLN A C   1 
ATOM   5835  O  O   . GLN A 1 715  ? 105.370 120.055 120.952 1.00 73.67  ? 715  GLN A O   1 
ATOM   5836  C  CB  . GLN A 1 715  ? 102.889 120.907 121.693 1.00 62.03  ? 715  GLN A CB  1 
ATOM   5837  C  CG  . GLN A 1 715  ? 101.722 121.868 121.796 1.00 69.02  ? 715  GLN A CG  1 
ATOM   5838  C  CD  . GLN A 1 715  ? 101.803 122.735 123.037 1.00 74.76  ? 715  GLN A CD  1 
ATOM   5839  O  OE1 . GLN A 1 715  ? 101.337 123.874 123.020 1.00 67.43  ? 715  GLN A OE1 1 
ATOM   5840  N  NE2 . GLN A 1 715  ? 102.428 122.222 124.083 1.00 78.15  ? 715  GLN A NE2 1 
ATOM   5841  N  N   . GLN A 1 716  ? 104.753 119.210 118.960 1.00 72.44  ? 716  GLN A N   1 
ATOM   5842  C  CA  . GLN A 1 716  ? 106.029 118.538 118.750 1.00 61.63  ? 716  GLN A CA  1 
ATOM   5843  C  C   . GLN A 1 716  ? 107.187 119.524 118.824 1.00 64.00  ? 716  GLN A C   1 
ATOM   5844  O  O   . GLN A 1 716  ? 108.242 119.214 119.398 1.00 74.06  ? 716  GLN A O   1 
ATOM   5845  C  CB  . GLN A 1 716  ? 106.013 117.856 117.384 1.00 79.58  ? 716  GLN A CB  1 
ATOM   5846  C  CG  . GLN A 1 716  ? 107.166 116.913 117.127 1.00 93.96  ? 716  GLN A CG  1 
ATOM   5847  C  CD  . GLN A 1 716  ? 107.623 116.968 115.680 1.00 107.18 ? 716  GLN A CD  1 
ATOM   5848  O  OE1 . GLN A 1 716  ? 107.075 117.720 114.872 1.00 91.27  ? 716  GLN A OE1 1 
ATOM   5849  N  NE2 . GLN A 1 716  ? 108.646 116.189 115.349 1.00 113.34 ? 716  GLN A NE2 1 
ATOM   5850  N  N   . LYS A 1 717  ? 106.999 120.722 118.274 1.00 63.46  ? 717  LYS A N   1 
ATOM   5851  C  CA  . LYS A 1 717  ? 108.081 121.690 118.207 1.00 76.44  ? 717  LYS A CA  1 
ATOM   5852  C  C   . LYS A 1 717  ? 108.526 122.116 119.602 1.00 74.25  ? 717  LYS A C   1 
ATOM   5853  O  O   . LYS A 1 717  ? 109.727 122.129 119.912 1.00 90.86  ? 717  LYS A O   1 
ATOM   5854  C  CB  . LYS A 1 717  ? 107.634 122.891 117.375 1.00 70.53  ? 717  LYS A CB  1 
ATOM   5855  C  CG  . LYS A 1 717  ? 107.419 122.531 115.923 1.00 77.13  ? 717  LYS A CG  1 
ATOM   5856  C  CD  . LYS A 1 717  ? 108.742 122.438 115.202 1.00 87.59  ? 717  LYS A CD  1 
ATOM   5857  C  CE  . LYS A 1 717  ? 108.545 122.064 113.749 1.00 98.76  ? 717  LYS A CE  1 
ATOM   5858  N  NZ  . LYS A 1 717  ? 107.803 120.780 113.618 1.00 96.45  ? 717  LYS A NZ  1 
ATOM   5859  N  N   . LEU A 1 718  ? 107.566 122.445 120.470 1.00 63.17  ? 718  LEU A N   1 
ATOM   5860  C  CA  . LEU A 1 718  ? 107.908 122.877 121.821 1.00 58.33  ? 718  LEU A CA  1 
ATOM   5861  C  C   . LEU A 1 718  ? 108.588 121.770 122.619 1.00 74.44  ? 718  LEU A C   1 
ATOM   5862  O  O   . LEU A 1 718  ? 109.545 122.027 123.361 1.00 83.79  ? 718  LEU A O   1 
ATOM   5863  C  CB  . LEU A 1 718  ? 106.652 123.354 122.547 1.00 55.38  ? 718  LEU A CB  1 
ATOM   5864  C  CG  . LEU A 1 718  ? 106.938 123.918 123.938 1.00 62.42  ? 718  LEU A CG  1 
ATOM   5865  C  CD1 . LEU A 1 718  ? 107.714 125.216 123.819 1.00 54.54  ? 718  LEU A CD1 1 
ATOM   5866  C  CD2 . LEU A 1 718  ? 105.651 124.120 124.722 1.00 62.73  ? 718  LEU A CD2 1 
ATOM   5867  N  N   . TRP A 1 719  ? 108.113 120.531 122.481 1.00 65.48  ? 719  TRP A N   1 
ATOM   5868  C  CA  . TRP A 1 719  ? 108.715 119.442 123.240 1.00 54.05  ? 719  TRP A CA  1 
ATOM   5869  C  C   . TRP A 1 719  ? 110.138 119.156 122.777 1.00 61.07  ? 719  TRP A C   1 
ATOM   5870  O  O   . TRP A 1 719  ? 111.029 118.909 123.603 1.00 72.14  ? 719  TRP A O   1 
ATOM   5871  C  CB  . TRP A 1 719  ? 107.847 118.193 123.125 1.00 72.98  ? 719  TRP A CB  1 
ATOM   5872  C  CG  . TRP A 1 719  ? 106.486 118.396 123.693 1.00 74.83  ? 719  TRP A CG  1 
ATOM   5873  C  CD1 . TRP A 1 719  ? 106.128 119.296 124.654 1.00 73.05  ? 719  TRP A CD1 1 
ATOM   5874  C  CD2 . TRP A 1 719  ? 105.294 117.691 123.337 1.00 70.46  ? 719  TRP A CD2 1 
ATOM   5875  N  NE1 . TRP A 1 719  ? 104.783 119.195 124.916 1.00 65.18  ? 719  TRP A NE1 1 
ATOM   5876  C  CE2 . TRP A 1 719  ? 104.249 118.215 124.121 1.00 62.73  ? 719  TRP A CE2 1 
ATOM   5877  C  CE3 . TRP A 1 719  ? 105.009 116.665 122.432 1.00 75.68  ? 719  TRP A CE3 1 
ATOM   5878  C  CZ2 . TRP A 1 719  ? 102.941 117.749 124.027 1.00 66.10  ? 719  TRP A CZ2 1 
ATOM   5879  C  CZ3 . TRP A 1 719  ? 103.710 116.205 122.341 1.00 72.09  ? 719  TRP A CZ3 1 
ATOM   5880  C  CH2 . TRP A 1 719  ? 102.693 116.745 123.132 1.00 66.88  ? 719  TRP A CH2 1 
ATOM   5881  N  N   . THR A 1 720  ? 110.381 119.205 121.464 1.00 65.93  ? 720  THR A N   1 
ATOM   5882  C  CA  . THR A 1 720  ? 111.746 119.028 120.976 1.00 67.31  ? 720  THR A CA  1 
ATOM   5883  C  C   . THR A 1 720  ? 112.656 120.155 121.453 1.00 60.84  ? 720  THR A C   1 
ATOM   5884  O  O   . THR A 1 720  ? 113.821 119.919 121.809 1.00 75.74  ? 720  THR A O   1 
ATOM   5885  C  CB  . THR A 1 720  ? 111.756 118.932 119.449 1.00 69.11  ? 720  THR A CB  1 
ATOM   5886  O  OG1 . THR A 1 720  ? 111.079 120.063 118.887 1.00 86.07  ? 720  THR A OG1 1 
ATOM   5887  C  CG2 . THR A 1 720  ? 111.067 117.651 118.989 1.00 72.94  ? 720  THR A CG2 1 
ATOM   5888  N  N   . CYS A 1 721  ? 112.135 121.385 121.500 1.00 58.62  ? 721  CYS A N   1 
ATOM   5889  C  CA  . CYS A 1 721  ? 112.932 122.495 122.015 1.00 56.97  ? 721  CYS A CA  1 
ATOM   5890  C  C   . CYS A 1 721  ? 113.301 122.293 123.484 1.00 68.09  ? 721  CYS A C   1 
ATOM   5891  O  O   . CYS A 1 721  ? 114.452 122.529 123.884 1.00 80.14  ? 721  CYS A O   1 
ATOM   5892  C  CB  . CYS A 1 721  ? 112.166 123.805 121.826 1.00 65.45  ? 721  CYS A CB  1 
ATOM   5893  S  SG  . CYS A 1 721  ? 112.020 124.350 120.103 1.00 97.56  ? 721  CYS A SG  1 
ATOM   5894  N  N   . ILE A 1 722  ? 112.347 121.833 124.299 1.00 74.63  ? 722  ILE A N   1 
ATOM   5895  C  CA  . ILE A 1 722  ? 112.646 121.568 125.707 1.00 63.08  ? 722  ILE A CA  1 
ATOM   5896  C  C   . ILE A 1 722  ? 113.681 120.454 125.846 1.00 69.81  ? 722  ILE A C   1 
ATOM   5897  O  O   . ILE A 1 722  ? 114.575 120.516 126.705 1.00 78.33  ? 722  ILE A O   1 
ATOM   5898  C  CB  . ILE A 1 722  ? 111.355 121.233 126.478 1.00 49.20  ? 722  ILE A CB  1 
ATOM   5899  C  CG1 . ILE A 1 722  ? 110.405 122.430 126.495 1.00 68.06  ? 722  ILE A CG1 1 
ATOM   5900  C  CG2 . ILE A 1 722  ? 111.680 120.816 127.907 1.00 62.27  ? 722  ILE A CG2 1 
ATOM   5901  C  CD1 . ILE A 1 722  ? 109.079 122.144 127.170 1.00 57.79  ? 722  ILE A CD1 1 
ATOM   5902  N  N   . SER A 1 723  ? 113.579 119.416 125.008 1.00 63.72  ? 723  SER A N   1 
ATOM   5903  C  CA  . SER A 1 723  ? 114.557 118.333 125.074 1.00 55.32  ? 723  SER A CA  1 
ATOM   5904  C  C   . SER A 1 723  ? 115.961 118.843 124.766 1.00 61.78  ? 723  SER A C   1 
ATOM   5905  O  O   . SER A 1 723  ? 116.935 118.479 125.447 1.00 75.00  ? 723  SER A O   1 
ATOM   5906  C  CB  . SER A 1 723  ? 114.163 117.213 124.108 1.00 56.47  ? 723  SER A CB  1 
ATOM   5907  O  OG  . SER A 1 723  ? 115.101 116.151 124.137 1.00 82.77  ? 723  SER A OG  1 
ATOM   5908  N  N   . CYS A 1 724  ? 116.080 119.706 123.753 1.00 59.55  ? 724  CYS A N   1 
ATOM   5909  C  CA  . CYS A 1 724  ? 117.377 120.290 123.432 1.00 58.54  ? 724  CYS A CA  1 
ATOM   5910  C  C   . CYS A 1 724  ? 117.910 121.136 124.583 1.00 69.92  ? 724  CYS A C   1 
ATOM   5911  O  O   . CYS A 1 724  ? 119.112 121.107 124.887 1.00 72.32  ? 724  CYS A O   1 
ATOM   5912  C  CB  . CYS A 1 724  ? 117.281 121.118 122.147 1.00 59.67  ? 724  CYS A CB  1 
ATOM   5913  S  SG  . CYS A 1 724  ? 116.858 120.167 120.660 1.00 110.76 ? 724  CYS A SG  1 
ATOM   5914  N  N   . ALA A 1 725  ? 117.024 121.875 125.262 1.00 72.23  ? 725  ALA A N   1 
ATOM   5915  C  CA  . ALA A 1 725  ? 117.469 122.659 126.420 1.00 60.91  ? 725  ALA A CA  1 
ATOM   5916  C  C   . ALA A 1 725  ? 118.013 121.783 127.550 1.00 71.41  ? 725  ALA A C   1 
ATOM   5917  O  O   . ALA A 1 725  ? 119.055 122.098 128.136 1.00 82.30  ? 725  ALA A O   1 
ATOM   5918  C  CB  . ALA A 1 725  ? 116.331 123.528 126.924 1.00 68.41  ? 725  ALA A CB  1 
ATOM   5919  N  N   . GLN A 1 726  ? 117.352 120.670 127.856 1.00 62.93  ? 726  GLN A N   1 
ATOM   5920  C  CA  . GLN A 1 726  ? 117.900 119.808 128.903 1.00 56.32  ? 726  GLN A CA  1 
ATOM   5921  C  C   . GLN A 1 726  ? 119.239 119.188 128.480 1.00 58.89  ? 726  GLN A C   1 
ATOM   5922  O  O   . GLN A 1 726  ? 120.149 119.029 129.312 1.00 66.62  ? 726  GLN A O   1 
ATOM   5923  C  CB  . GLN A 1 726  ? 116.906 118.738 129.342 1.00 58.19  ? 726  GLN A CB  1 
ATOM   5924  C  CG  . GLN A 1 726  ? 115.425 119.071 129.284 1.00 74.48  ? 726  GLN A CG  1 
ATOM   5925  C  CD  . GLN A 1 726  ? 114.579 117.844 129.593 1.00 70.10  ? 726  GLN A CD  1 
ATOM   5926  O  OE1 . GLN A 1 726  ? 114.974 116.713 129.262 1.00 58.17  ? 726  GLN A OE1 1 
ATOM   5927  N  NE2 . GLN A 1 726  ? 113.598 118.037 130.446 1.00 66.17  ? 726  GLN A NE2 1 
ATOM   5928  N  N   . ILE A 1 727  ? 119.363 118.791 127.211 1.00 63.02  ? 727  ILE A N   1 
ATOM   5929  C  CA  . ILE A 1 727  ? 120.632 118.218 126.781 1.00 55.68  ? 727  ILE A CA  1 
ATOM   5930  C  C   . ILE A 1 727  ? 121.750 119.243 126.949 1.00 59.32  ? 727  ILE A C   1 
ATOM   5931  O  O   . ILE A 1 727  ? 122.860 118.916 127.399 1.00 73.02  ? 727  ILE A O   1 
ATOM   5932  C  CB  . ILE A 1 727  ? 120.539 117.703 125.333 1.00 54.74  ? 727  ILE A CB  1 
ATOM   5933  C  CG1 . ILE A 1 727  ? 119.779 116.379 125.286 1.00 58.97  ? 727  ILE A CG1 1 
ATOM   5934  C  CG2 . ILE A 1 727  ? 121.942 117.503 124.742 1.00 46.33  ? 727  ILE A CG2 1 
ATOM   5935  C  CD1 . ILE A 1 727  ? 119.091 116.120 123.966 1.00 81.01  ? 727  ILE A CD1 1 
ATOM   5936  N  N   . THR A 1 728  ? 121.465 120.509 126.621 1.00 60.73  ? 728  THR A N   1 
ATOM   5937  C  CA  . THR A 1 728  ? 122.453 121.565 126.825 1.00 55.47  ? 728  THR A CA  1 
ATOM   5938  C  C   . THR A 1 728  ? 122.780 121.744 128.308 1.00 61.47  ? 728  THR A C   1 
ATOM   5939  O  O   . THR A 1 728  ? 123.930 122.024 128.671 1.00 71.42  ? 728  THR A O   1 
ATOM   5940  C  CB  . THR A 1 728  ? 121.954 122.876 126.214 1.00 63.18  ? 728  THR A CB  1 
ATOM   5941  O  OG1 . THR A 1 728  ? 121.751 122.691 124.809 1.00 67.56  ? 728  THR A OG1 1 
ATOM   5942  C  CG2 . THR A 1 728  ? 122.980 123.984 126.407 1.00 63.47  ? 728  THR A CG2 1 
ATOM   5943  N  N   . LEU A 1 729  ? 121.780 121.598 129.183 1.00 67.84  ? 729  LEU A N   1 
ATOM   5944  C  CA  . LEU A 1 729  ? 122.066 121.700 130.614 1.00 62.92  ? 729  LEU A CA  1 
ATOM   5945  C  C   . LEU A 1 729  ? 123.031 120.598 131.046 1.00 69.92  ? 729  LEU A C   1 
ATOM   5946  O  O   . LEU A 1 729  ? 123.962 120.838 131.826 1.00 82.05  ? 729  LEU A O   1 
ATOM   5947  C  CB  . LEU A 1 729  ? 120.779 121.649 131.435 1.00 55.77  ? 729  LEU A CB  1 
ATOM   5948  C  CG  . LEU A 1 729  ? 121.043 121.468 132.930 1.00 58.90  ? 729  LEU A CG  1 
ATOM   5949  C  CD1 . LEU A 1 729  ? 121.700 122.721 133.495 1.00 49.34  ? 729  LEU A CD1 1 
ATOM   5950  C  CD2 . LEU A 1 729  ? 119.764 121.147 133.684 1.00 61.08  ? 729  LEU A CD2 1 
ATOM   5951  N  N   . VAL A 1 730  ? 122.817 119.379 130.544 1.00 68.39  ? 730  VAL A N   1 
ATOM   5952  C  CA  . VAL A 1 730  ? 123.733 118.279 130.850 1.00 64.77  ? 730  VAL A CA  1 
ATOM   5953  C  C   . VAL A 1 730  ? 125.134 118.608 130.342 1.00 65.27  ? 730  VAL A C   1 
ATOM   5954  O  O   . VAL A 1 730  ? 126.145 118.320 130.995 1.00 66.74  ? 730  VAL A O   1 
ATOM   5955  C  CB  . VAL A 1 730  ? 123.219 116.951 130.272 1.00 57.81  ? 730  VAL A CB  1 
ATOM   5956  C  CG1 . VAL A 1 730  ? 124.340 115.927 130.196 1.00 57.39  ? 730  VAL A CG1 1 
ATOM   5957  C  CG2 . VAL A 1 730  ? 122.109 116.405 131.126 1.00 74.22  ? 730  VAL A CG2 1 
ATOM   5958  N  N   . GLU A 1 731  ? 125.212 119.231 129.161 1.00 72.31  ? 731  GLU A N   1 
ATOM   5959  C  CA  . GLU A 1 731  ? 126.512 119.623 128.619 1.00 62.53  ? 731  GLU A CA  1 
ATOM   5960  C  C   . GLU A 1 731  ? 127.227 120.613 129.529 1.00 72.62  ? 731  GLU A C   1 
ATOM   5961  O  O   . GLU A 1 731  ? 128.442 120.508 129.741 1.00 86.42  ? 731  GLU A O   1 
ATOM   5962  C  CB  . GLU A 1 731  ? 126.337 120.232 127.232 1.00 69.09  ? 731  GLU A CB  1 
ATOM   5963  C  CG  . GLU A 1 731  ? 127.642 120.513 126.535 1.00 76.24  ? 731  GLU A CG  1 
ATOM   5964  C  CD  . GLU A 1 731  ? 127.480 121.496 125.409 1.00 105.12 ? 731  GLU A CD  1 
ATOM   5965  O  OE1 . GLU A 1 731  ? 127.927 122.651 125.562 1.00 109.11 ? 731  GLU A OE1 1 
ATOM   5966  O  OE2 . GLU A 1 731  ? 126.899 121.113 124.374 1.00 98.07  ? 731  GLU A OE2 1 
ATOM   5967  N  N   . LEU A 1 732  ? 126.493 121.582 130.073 1.00 75.43  ? 732  LEU A N   1 
ATOM   5968  C  CA  . LEU A 1 732  ? 127.091 122.496 131.045 1.00 61.51  ? 732  LEU A CA  1 
ATOM   5969  C  C   . LEU A 1 732  ? 127.541 121.774 132.311 1.00 61.71  ? 732  LEU A C   1 
ATOM   5970  O  O   . LEU A 1 732  ? 128.574 122.117 132.897 1.00 67.56  ? 732  LEU A O   1 
ATOM   5971  C  CB  . LEU A 1 732  ? 126.111 123.610 131.402 1.00 70.35  ? 732  LEU A CB  1 
ATOM   5972  C  CG  . LEU A 1 732  ? 126.269 124.895 130.593 1.00 77.75  ? 732  LEU A CG  1 
ATOM   5973  C  CD1 . LEU A 1 732  ? 125.986 124.637 129.122 1.00 85.90  ? 732  LEU A CD1 1 
ATOM   5974  C  CD2 . LEU A 1 732  ? 125.363 125.981 131.146 1.00 90.32  ? 732  LEU A CD2 1 
ATOM   5975  N  N   . LYS A 1 733  ? 126.780 120.771 132.751 1.00 69.37  ? 733  LYS A N   1 
ATOM   5976  C  CA  . LYS A 1 733  ? 127.126 120.111 134.008 1.00 66.22  ? 733  LYS A CA  1 
ATOM   5977  C  C   . LYS A 1 733  ? 128.353 119.212 133.881 1.00 84.14  ? 733  LYS A C   1 
ATOM   5978  O  O   . LYS A 1 733  ? 129.229 119.230 134.754 1.00 86.42  ? 733  LYS A O   1 
ATOM   5979  C  CB  . LYS A 1 733  ? 125.942 119.297 134.519 1.00 74.46  ? 733  LYS A CB  1 
ATOM   5980  C  CG  . LYS A 1 733  ? 125.148 119.980 135.602 1.00 81.69  ? 733  LYS A CG  1 
ATOM   5981  C  CD  . LYS A 1 733  ? 123.894 119.193 135.906 1.00 75.82  ? 733  LYS A CD  1 
ATOM   5982  C  CE  . LYS A 1 733  ? 123.250 119.666 137.190 1.00 99.53  ? 733  LYS A CE  1 
ATOM   5983  N  NZ  . LYS A 1 733  ? 121.774 119.497 137.138 1.00 102.18 ? 733  LYS A NZ  1 
ATOM   5984  N  N   . THR A 1 734  ? 128.444 118.425 132.808 1.00 84.31  ? 734  THR A N   1 
ATOM   5985  C  CA  . THR A 1 734  ? 129.528 117.455 132.685 1.00 71.94  ? 734  THR A CA  1 
ATOM   5986  C  C   . THR A 1 734  ? 130.758 117.979 131.950 1.00 71.74  ? 734  THR A C   1 
ATOM   5987  O  O   . THR A 1 734  ? 131.801 117.314 131.982 1.00 81.73  ? 734  THR A O   1 
ATOM   5988  C  CB  . THR A 1 734  ? 129.025 116.189 131.986 1.00 70.24  ? 734  THR A CB  1 
ATOM   5989  O  OG1 . THR A 1 734  ? 128.597 116.512 130.658 1.00 81.37  ? 734  THR A OG1 1 
ATOM   5990  C  CG2 . THR A 1 734  ? 127.860 115.583 132.759 1.00 67.13  ? 734  THR A CG2 1 
ATOM   5991  N  N   . LYS A 1 735  ? 130.666 119.138 131.298 1.00 79.68  ? 735  LYS A N   1 
ATOM   5992  C  CA  . LYS A 1 735  ? 131.784 119.737 130.561 1.00 83.70  ? 735  LYS A CA  1 
ATOM   5993  C  C   . LYS A 1 735  ? 132.303 118.819 129.452 1.00 77.63  ? 735  LYS A C   1 
ATOM   5994  O  O   . LYS A 1 735  ? 133.510 118.714 129.226 1.00 81.41  ? 735  LYS A O   1 
ATOM   5995  C  CB  . LYS A 1 735  ? 132.918 120.116 131.517 1.00 77.32  ? 735  LYS A CB  1 
ATOM   5996  C  CG  . LYS A 1 735  ? 132.500 121.040 132.645 1.00 88.62  ? 735  LYS A CG  1 
ATOM   5997  C  CD  . LYS A 1 735  ? 133.644 121.257 133.622 1.00 104.22 ? 735  LYS A CD  1 
ATOM   5998  C  CE  . LYS A 1 735  ? 133.194 122.062 134.830 1.00 116.37 ? 735  LYS A CE  1 
ATOM   5999  N  NZ  . LYS A 1 735  ? 132.101 121.383 135.582 1.00 105.72 ? 735  LYS A NZ  1 
ATOM   6000  N  N   . LEU A 1 736  ? 131.388 118.134 128.765 1.00 75.26  ? 736  LEU A N   1 
ATOM   6001  C  CA  . LEU A 1 736  ? 131.716 117.303 127.611 1.00 75.59  ? 736  LEU A CA  1 
ATOM   6002  C  C   . LEU A 1 736  ? 130.872 117.718 126.414 1.00 86.26  ? 736  LEU A C   1 
ATOM   6003  O  O   . LEU A 1 736  ? 129.712 118.095 126.578 1.00 99.66  ? 736  LEU A O   1 
ATOM   6004  C  CB  . LEU A 1 736  ? 131.482 115.817 127.904 1.00 76.33  ? 736  LEU A CB  1 
ATOM   6005  C  CG  . LEU A 1 736  ? 132.417 115.118 128.889 1.00 78.08  ? 736  LEU A CG  1 
ATOM   6006  C  CD1 . LEU A 1 736  ? 131.668 114.015 129.616 1.00 84.70  ? 736  LEU A CD1 1 
ATOM   6007  C  CD2 . LEU A 1 736  ? 133.631 114.558 128.161 1.00 86.67  ? 736  LEU A CD2 1 
ATOM   6008  N  N   . LYS A 1 737  ? 131.471 117.724 125.224 1.00 75.63  ? 737  LYS A N   1 
ATOM   6009  C  CA  . LYS A 1 737  ? 130.763 118.134 124.014 1.00 78.94  ? 737  LYS A CA  1 
ATOM   6010  C  C   . LYS A 1 737  ? 129.817 117.045 123.513 1.00 87.82  ? 737  LYS A C   1 
ATOM   6011  O  O   . LYS A 1 737  ? 130.213 115.882 123.385 1.00 95.41  ? 737  LYS A O   1 
ATOM   6012  C  CB  . LYS A 1 737  ? 131.750 118.481 122.898 1.00 85.02  ? 737  LYS A CB  1 
ATOM   6013  C  CG  . LYS A 1 737  ? 132.276 119.898 122.882 1.00 117.77 ? 737  LYS A CG  1 
ATOM   6014  C  CD  . LYS A 1 737  ? 131.122 120.885 122.911 1.00 108.66 ? 737  LYS A CD  1 
ATOM   6015  C  CE  . LYS A 1 737  ? 131.583 122.250 123.352 1.00 120.25 ? 737  LYS A CE  1 
ATOM   6016  N  NZ  . LYS A 1 737  ? 132.037 122.209 124.747 1.00 109.53 ? 737  LYS A NZ  1 
ATOM   6017  N  N   . LEU A 1 738  ? 128.567 117.418 123.227 1.00 73.35  ? 738  LEU A N   1 
ATOM   6018  C  CA  . LEU A 1 738  ? 127.556 116.468 122.777 1.00 68.69  ? 738  LEU A CA  1 
ATOM   6019  C  C   . LEU A 1 738  ? 126.960 116.945 121.461 1.00 73.66  ? 738  LEU A C   1 
ATOM   6020  O  O   . LEU A 1 738  ? 126.867 118.148 121.199 1.00 80.63  ? 738  LEU A O   1 
ATOM   6021  C  CB  . LEU A 1 738  ? 126.412 116.218 123.780 1.00 74.27  ? 738  LEU A CB  1 
ATOM   6022  C  CG  . LEU A 1 738  ? 126.638 115.865 125.251 1.00 80.98  ? 738  LEU A CG  1 
ATOM   6023  C  CD1 . LEU A 1 738  ? 127.057 117.053 126.035 1.00 75.61  ? 738  LEU A CD1 1 
ATOM   6024  C  CD2 . LEU A 1 738  ? 125.383 115.255 125.848 1.00 91.97  ? 738  LEU A CD2 1 
ATOM   6025  N  N   . LYS A 1 739  ? 126.540 115.983 120.641 1.00 73.17  ? 739  LYS A N   1 
ATOM   6026  C  CA  . LYS A 1 739  ? 125.877 116.254 119.369 1.00 77.02  ? 739  LYS A CA  1 
ATOM   6027  C  C   . LYS A 1 739  ? 124.681 115.326 119.239 1.00 72.10  ? 739  LYS A C   1 
ATOM   6028  O  O   . LYS A 1 739  ? 124.841 114.104 119.237 1.00 85.80  ? 739  LYS A O   1 
ATOM   6029  C  CB  . LYS A 1 739  ? 126.826 116.063 118.183 1.00 76.23  ? 739  LYS A CB  1 
ATOM   6030  C  CG  . LYS A 1 739  ? 128.004 117.015 118.148 1.00 96.98  ? 739  LYS A CG  1 
ATOM   6031  C  CD  . LYS A 1 739  ? 128.965 116.596 117.056 1.00 100.93 ? 739  LYS A CD  1 
ATOM   6032  C  CE  . LYS A 1 739  ? 128.304 116.721 115.694 1.00 113.22 ? 739  LYS A CE  1 
ATOM   6033  N  NZ  . LYS A 1 739  ? 129.175 116.216 114.598 1.00 117.03 ? 739  LYS A NZ  1 
ATOM   6034  N  N   . SER A 1 740  ? 123.492 115.902 119.116 1.00 71.51  ? 740  SER A N   1 
ATOM   6035  C  CA  . SER A 1 740  ? 122.249 115.151 119.099 1.00 72.69  ? 740  SER A CA  1 
ATOM   6036  C  C   . SER A 1 740  ? 121.566 115.294 117.747 1.00 92.68  ? 740  SER A C   1 
ATOM   6037  O  O   . SER A 1 740  ? 121.661 116.325 117.084 1.00 111.80 ? 740  SER A O   1 
ATOM   6038  C  CB  . SER A 1 740  ? 121.291 115.615 120.199 1.00 80.43  ? 740  SER A CB  1 
ATOM   6039  O  OG  . SER A 1 740  ? 120.885 116.957 119.988 1.00 85.69  ? 740  SER A OG  1 
ATOM   6040  N  N   . SER A 1 741  ? 120.856 114.246 117.360 1.00 82.98  ? 741  SER A N   1 
ATOM   6041  C  CA  . SER A 1 741  ? 120.124 114.226 116.110 1.00 87.07  ? 741  SER A CA  1 
ATOM   6042  C  C   . SER A 1 741  ? 118.797 113.562 116.387 1.00 92.81  ? 741  SER A C   1 
ATOM   6043  O  O   . SER A 1 741  ? 118.720 112.598 117.152 1.00 99.75  ? 741  SER A O   1 
ATOM   6044  C  CB  . SER A 1 741  ? 120.877 113.460 115.002 1.00 86.05  ? 741  SER A CB  1 
ATOM   6045  O  OG  . SER A 1 741  ? 120.088 113.308 113.829 1.00 102.45 ? 741  SER A OG  1 
ATOM   6046  N  N   . VAL A 1 742  ? 117.761 114.016 115.708 1.00 100.74 ? 742  VAL A N   1 
ATOM   6047  C  CA  . VAL A 1 742  ? 116.432 113.506 115.971 1.00 104.72 ? 742  VAL A CA  1 
ATOM   6048  C  C   . VAL A 1 742  ? 116.005 112.887 114.669 1.00 117.87 ? 742  VAL A C   1 
ATOM   6049  O  O   . VAL A 1 742  ? 115.915 113.560 113.646 1.00 122.59 ? 742  VAL A O   1 
ATOM   6050  C  CB  . VAL A 1 742  ? 115.462 114.620 116.397 1.00 112.41 ? 742  VAL A CB  1 
ATOM   6051  C  CG1 . VAL A 1 742  ? 114.046 114.057 116.548 1.00 97.29  ? 742  VAL A CG1 1 
ATOM   6052  C  CG2 . VAL A 1 742  ? 115.905 115.112 117.748 1.00 118.48 ? 742  VAL A CG2 1 
ATOM   6053  N  N   . MET A 1 743  ? 115.720 111.647 114.709 1.00 109.11 ? 743  MET A N   1 
ATOM   6054  C  CA  . MET A 1 743  ? 115.041 111.052 113.568 1.00 119.08 ? 743  MET A CA  1 
ATOM   6055  C  C   . MET A 1 743  ? 113.534 111.134 113.757 1.00 136.79 ? 743  MET A C   1 
ATOM   6056  O  O   . MET A 1 743  ? 113.031 111.974 114.510 1.00 131.12 ? 743  MET A O   1 
ATOM   6057  C  CB  . MET A 1 743  ? 115.572 109.677 113.268 1.00 112.90 ? 743  MET A CB  1 
ATOM   6058  C  CG  . MET A 1 743  ? 115.093 109.020 112.020 1.00 161.16 ? 743  MET A CG  1 
ATOM   6059  S  SD  . MET A 1 743  ? 116.017 107.436 111.680 1.00 148.51 ? 743  MET A SD  1 
ATOM   6060  C  CE  . MET A 1 743  ? 117.747 107.451 111.841 1.00 127.41 ? 743  MET A CE  1 
ATOM   6061  N  N   . GLY A 1 744  ? 112.760 110.329 113.031 1.00 136.23 ? 744  GLY A N   1 
ATOM   6062  C  CA  . GLY A 1 744  ? 111.317 110.355 113.278 1.00 124.03 ? 744  GLY A CA  1 
ATOM   6063  C  C   . GLY A 1 744  ? 110.915 109.967 114.690 1.00 128.05 ? 744  GLY A C   1 
ATOM   6064  O  O   . GLY A 1 744  ? 110.078 110.640 115.304 1.00 133.13 ? 744  GLY A O   1 
ATOM   6065  N  N   . ASP A 1 745  ? 111.522 108.949 115.226 1.00 122.45 ? 745  ASP A N   1 
ATOM   6066  C  CA  . ASP A 1 745  ? 111.222 108.441 116.542 1.00 129.67 ? 745  ASP A CA  1 
ATOM   6067  C  C   . ASP A 1 745  ? 112.446 108.489 117.442 1.00 128.38 ? 745  ASP A C   1 
ATOM   6068  O  O   . ASP A 1 745  ? 112.344 108.916 118.590 1.00 128.81 ? 745  ASP A O   1 
ATOM   6069  C  CB  . ASP A 1 745  ? 110.689 107.012 116.415 1.00 129.16 ? 745  ASP A CB  1 
ATOM   6070  C  CG  . ASP A 1 745  ? 110.302 106.373 117.742 1.00 137.30 ? 745  ASP A CG  1 
ATOM   6071  O  OD1 . ASP A 1 745  ? 110.784 106.787 118.815 1.00 132.34 ? 745  ASP A OD1 1 
ATOM   6072  O  OD2 . ASP A 1 745  ? 109.489 105.428 117.717 1.00 136.95 ? 745  ASP A OD2 1 
ATOM   6073  N  N   . ASN A 1 746  ? 113.621 108.121 116.930 1.00 125.13 ? 746  ASN A N   1 
ATOM   6074  C  CA  . ASN A 1 746  ? 114.788 107.984 117.788 1.00 108.27 ? 746  ASN A CA  1 
ATOM   6075  C  C   . ASN A 1 746  ? 115.590 109.277 117.837 1.00 112.44 ? 746  ASN A C   1 
ATOM   6076  O  O   . ASN A 1 746  ? 115.595 110.064 116.890 1.00 121.07 ? 746  ASN A O   1 
ATOM   6077  C  CB  . ASN A 1 746  ? 115.683 106.837 117.314 1.00 102.18 ? 746  ASN A CB  1 
ATOM   6078  C  CG  . ASN A 1 746  ? 115.038 105.474 117.507 1.00 116.50 ? 746  ASN A CG  1 
ATOM   6079  O  OD1 . ASN A 1 746  ? 114.316 105.243 118.477 1.00 126.48 ? 746  ASN A OD1 1 
ATOM   6080  N  ND2 . ASN A 1 746  ? 115.274 104.572 116.560 1.00 103.79 ? 746  ASN A ND2 1 
ATOM   6081  N  N   . GLN A 1 747  ? 116.288 109.487 118.952 1.00 82.59  ? 747  GLN A N   1 
ATOM   6082  C  CA  . GLN A 1 747  ? 117.254 110.576 119.075 1.00 87.55  ? 747  GLN A CA  1 
ATOM   6083  C  C   . GLN A 1 747  ? 118.579 109.990 119.547 1.00 74.63  ? 747  GLN A C   1 
ATOM   6084  O  O   . GLN A 1 747  ? 118.624 109.290 120.561 1.00 78.13  ? 747  GLN A O   1 
ATOM   6085  C  CB  . GLN A 1 747  ? 116.760 111.724 119.960 1.00 91.82  ? 747  GLN A CB  1 
ATOM   6086  C  CG  . GLN A 1 747  ? 117.029 111.692 121.428 1.00 104.45 ? 747  GLN A CG  1 
ATOM   6087  C  CD  . GLN A 1 747  ? 116.737 113.051 122.030 1.00 111.68 ? 747  GLN A CD  1 
ATOM   6088  O  OE1 . GLN A 1 747  ? 116.681 114.058 121.320 1.00 103.99 ? 747  GLN A OE1 1 
ATOM   6089  N  NE2 . GLN A 1 747  ? 116.556 113.089 123.342 1.00 117.90 ? 747  GLN A NE2 1 
ATOM   6090  N  N   . CYS A 1 748  ? 119.635 110.237 118.782 1.00 70.98  ? 748  CYS A N   1 
ATOM   6091  C  CA  . CYS A 1 748  ? 120.959 109.706 119.046 1.00 66.07  ? 748  CYS A CA  1 
ATOM   6092  C  C   . CYS A 1 748  ? 121.865 110.823 119.552 1.00 68.25  ? 748  CYS A C   1 
ATOM   6093  O  O   . CYS A 1 748  ? 121.950 111.887 118.941 1.00 76.95  ? 748  CYS A O   1 
ATOM   6094  C  CB  . CYS A 1 748  ? 121.532 109.110 117.762 1.00 79.02  ? 748  CYS A CB  1 
ATOM   6095  S  SG  . CYS A 1 748  ? 120.512 107.802 117.010 1.00 112.04 ? 748  CYS A SG  1 
ATOM   6096  N  N   . ILE A 1 749  ? 122.547 110.570 120.673 1.00 62.15  ? 749  ILE A N   1 
ATOM   6097  C  CA  . ILE A 1 749  ? 123.429 111.554 121.282 1.00 62.53  ? 749  ILE A CA  1 
ATOM   6098  C  C   . ILE A 1 749  ? 124.850 111.006 121.296 1.00 60.33  ? 749  ILE A C   1 
ATOM   6099  O  O   . ILE A 1 749  ? 125.092 109.891 121.770 1.00 78.35  ? 749  ILE A O   1 
ATOM   6100  C  CB  . ILE A 1 749  ? 122.964 111.927 122.700 1.00 49.86  ? 749  ILE A CB  1 
ATOM   6101  C  CG1 . ILE A 1 749  ? 121.509 112.394 122.686 1.00 60.91  ? 749  ILE A CG1 1 
ATOM   6102  C  CG2 . ILE A 1 749  ? 123.851 113.028 123.279 1.00 66.41  ? 749  ILE A CG2 1 
ATOM   6103  C  CD1 . ILE A 1 749  ? 120.957 112.780 124.048 1.00 68.04  ? 749  ILE A CD1 1 
ATOM   6104  N  N   . THR A 1 750  ? 125.791 111.819 120.817 1.00 62.45  ? 750  THR A N   1 
ATOM   6105  C  CA  . THR A 1 750  ? 127.195 111.449 120.703 1.00 66.01  ? 750  THR A CA  1 
ATOM   6106  C  C   . THR A 1 750  ? 128.060 112.331 121.600 1.00 74.92  ? 750  THR A C   1 
ATOM   6107  O  O   . THR A 1 750  ? 127.951 113.559 121.559 1.00 83.21  ? 750  THR A O   1 
ATOM   6108  C  CB  . THR A 1 750  ? 127.666 111.554 119.249 1.00 76.52  ? 750  THR A CB  1 
ATOM   6109  O  OG1 . THR A 1 750  ? 126.915 110.641 118.440 1.00 83.80  ? 750  THR A OG1 1 
ATOM   6110  C  CG2 . THR A 1 750  ? 129.145 111.211 119.139 1.00 78.42  ? 750  THR A CG2 1 
ATOM   6111  N  N   . THR A 1 751  ? 128.930 111.699 122.386 1.00 77.57  ? 751  THR A N   1 
ATOM   6112  C  CA  . THR A 1 751  ? 129.856 112.389 123.277 1.00 77.53  ? 751  THR A CA  1 
ATOM   6113  C  C   . THR A 1 751  ? 131.276 112.299 122.727 1.00 80.19  ? 751  THR A C   1 
ATOM   6114  O  O   . THR A 1 751  ? 131.744 111.210 122.380 1.00 82.08  ? 751  THR A O   1 
ATOM   6115  C  CB  . THR A 1 751  ? 129.804 111.811 124.693 1.00 69.52  ? 751  THR A CB  1 
ATOM   6116  O  OG1 . THR A 1 751  ? 128.441 111.738 125.129 1.00 80.58  ? 751  THR A OG1 1 
ATOM   6117  C  CG2 . THR A 1 751  ? 130.587 112.691 125.656 1.00 74.59  ? 751  THR A CG2 1 
ATOM   6118  N  N   . LEU A 1 752  ? 131.954 113.442 122.660 1.00 76.02  ? 752  LEU A N   1 
ATOM   6119  C  CA  . LEU A 1 752  ? 133.293 113.556 122.095 1.00 79.95  ? 752  LEU A CA  1 
ATOM   6120  C  C   . LEU A 1 752  ? 134.308 113.740 123.217 1.00 90.48  ? 752  LEU A C   1 
ATOM   6121  O  O   . LEU A 1 752  ? 134.134 114.607 124.079 1.00 88.23  ? 752  LEU A O   1 
ATOM   6122  C  CB  . LEU A 1 752  ? 133.358 114.736 121.123 1.00 83.52  ? 752  LEU A CB  1 
ATOM   6123  C  CG  . LEU A 1 752  ? 132.425 114.619 119.917 1.00 84.43  ? 752  LEU A CG  1 
ATOM   6124  C  CD1 . LEU A 1 752  ? 132.386 115.925 119.139 1.00 86.74  ? 752  LEU A CD1 1 
ATOM   6125  C  CD2 . LEU A 1 752  ? 132.842 113.462 119.021 1.00 87.45  ? 752  LEU A CD2 1 
ATOM   6126  N  N   . SER A 1 753  ? 135.368 112.928 123.199 1.00 80.25  ? 753  SER A N   1 
ATOM   6127  C  CA  . SER A 1 753  ? 136.397 112.949 124.230 1.00 76.29  ? 753  SER A CA  1 
ATOM   6128  C  C   . SER A 1 753  ? 137.785 113.062 123.610 1.00 93.39  ? 753  SER A C   1 
ATOM   6129  O  O   . SER A 1 753  ? 138.046 112.540 122.524 1.00 102.50 ? 753  SER A O   1 
ATOM   6130  C  CB  . SER A 1 753  ? 136.324 111.690 125.104 1.00 89.10  ? 753  SER A CB  1 
ATOM   6131  O  OG  . SER A 1 753  ? 136.465 110.518 124.320 1.00 99.54  ? 753  SER A OG  1 
ATOM   6132  N  N   . LEU A 1 754  ? 138.674 113.749 124.328 1.00 95.95  ? 754  LEU A N   1 
ATOM   6133  C  CA  . LEU A 1 754  ? 140.016 114.080 123.863 1.00 102.79 ? 754  LEU A CA  1 
ATOM   6134  C  C   . LEU A 1 754  ? 141.076 113.253 124.582 1.00 106.98 ? 754  LEU A C   1 
ATOM   6135  O  O   . LEU A 1 754  ? 141.013 113.077 125.803 1.00 114.68 ? 754  LEU A O   1 
ATOM   6136  C  CB  . LEU A 1 754  ? 140.301 115.566 124.088 1.00 100.63 ? 754  LEU A CB  1 
ATOM   6137  C  CG  . LEU A 1 754  ? 139.356 116.547 123.400 1.00 99.15  ? 754  LEU A CG  1 
ATOM   6138  C  CD1 . LEU A 1 754  ? 139.312 117.856 124.166 1.00 104.46 ? 754  LEU A CD1 1 
ATOM   6139  C  CD2 . LEU A 1 754  ? 139.801 116.783 121.973 1.00 113.18 ? 754  LEU A CD2 1 
ATOM   6140  N  N   . PHE A 1 755  ? 142.050 112.753 123.829 1.00 110.13 ? 755  PHE A N   1 
ATOM   6141  C  CA  . PHE A 1 755  ? 143.108 111.910 124.361 1.00 117.26 ? 755  PHE A CA  1 
ATOM   6142  C  C   . PHE A 1 755  ? 144.467 112.405 123.892 1.00 134.66 ? 755  PHE A C   1 
ATOM   6143  O  O   . PHE A 1 755  ? 144.574 113.063 122.850 1.00 143.16 ? 755  PHE A O   1 
ATOM   6144  C  CB  . PHE A 1 755  ? 142.950 110.445 123.928 1.00 122.41 ? 755  PHE A CB  1 
ATOM   6145  C  CG  . PHE A 1 755  ? 141.721 109.778 124.458 1.00 110.30 ? 755  PHE A CG  1 
ATOM   6146  C  CD1 . PHE A 1 755  ? 141.714 109.228 125.728 1.00 113.05 ? 755  PHE A CD1 1 
ATOM   6147  C  CD2 . PHE A 1 755  ? 140.589 109.660 123.673 1.00 108.79 ? 755  PHE A CD2 1 
ATOM   6148  C  CE1 . PHE A 1 755  ? 140.587 108.602 126.219 1.00 120.89 ? 755  PHE A CE1 1 
ATOM   6149  C  CE2 . PHE A 1 755  ? 139.459 109.032 124.156 1.00 109.26 ? 755  PHE A CE2 1 
ATOM   6150  C  CZ  . PHE A 1 755  ? 139.459 108.502 125.431 1.00 107.99 ? 755  PHE A CZ  1 
ATOM   6151  N  N   . PRO A 1 756  ? 145.528 112.102 124.639 1.00 138.79 ? 756  PRO A N   1 
ATOM   6152  C  CA  . PRO A 1 756  ? 146.883 112.384 124.154 1.00 146.96 ? 756  PRO A CA  1 
ATOM   6153  C  C   . PRO A 1 756  ? 147.249 111.454 123.004 1.00 160.55 ? 756  PRO A C   1 
ATOM   6154  O  O   . PRO A 1 756  ? 146.597 110.439 122.750 1.00 155.64 ? 756  PRO A O   1 
ATOM   6155  C  CB  . PRO A 1 756  ? 147.762 112.148 125.385 1.00 144.65 ? 756  PRO A CB  1 
ATOM   6156  C  CG  . PRO A 1 756  ? 146.969 111.211 126.235 1.00 137.38 ? 756  PRO A CG  1 
ATOM   6157  C  CD  . PRO A 1 756  ? 145.534 111.601 126.024 1.00 128.98 ? 756  PRO A CD  1 
ATOM   6158  N  N   . ILE A 1 757  ? 148.319 111.823 122.295 1.00 161.55 ? 757  ILE A N   1 
ATOM   6159  C  CA  . ILE A 1 757  ? 148.730 111.072 121.109 1.00 169.83 ? 757  ILE A CA  1 
ATOM   6160  C  C   . ILE A 1 757  ? 149.142 109.646 121.459 1.00 167.17 ? 757  ILE A C   1 
ATOM   6161  O  O   . ILE A 1 757  ? 148.764 108.690 120.771 1.00 156.16 ? 757  ILE A O   1 
ATOM   6162  C  CB  . ILE A 1 757  ? 149.860 111.816 120.375 1.00 169.12 ? 757  ILE A CB  1 
ATOM   6163  C  CG1 . ILE A 1 757  ? 149.394 113.208 119.963 1.00 170.73 ? 757  ILE A CG1 1 
ATOM   6164  C  CG2 . ILE A 1 757  ? 150.315 111.031 119.155 1.00 169.62 ? 757  ILE A CG2 1 
ATOM   6165  C  CD1 . ILE A 1 757  ? 148.220 113.179 119.011 1.00 172.23 ? 757  ILE A CD1 1 
ATOM   6166  N  N   . ASP A 1 758  ? 149.915 109.475 122.533 1.00 170.04 ? 758  ASP A N   1 
ATOM   6167  C  CA  . ASP A 1 758  ? 150.432 108.156 122.909 1.00 166.50 ? 758  ASP A CA  1 
ATOM   6168  C  C   . ASP A 1 758  ? 149.465 107.452 123.858 1.00 170.02 ? 758  ASP A C   1 
ATOM   6169  O  O   . ASP A 1 758  ? 149.623 107.454 125.081 1.00 169.32 ? 758  ASP A O   1 
ATOM   6170  C  CB  . ASP A 1 758  ? 151.823 108.285 123.516 1.00 172.28 ? 758  ASP A CB  1 
ATOM   6171  C  CG  . ASP A 1 758  ? 151.887 109.324 124.616 1.00 178.40 ? 758  ASP A CG  1 
ATOM   6172  O  OD1 . ASP A 1 758  ? 150.881 110.034 124.822 1.00 174.08 ? 758  ASP A OD1 1 
ATOM   6173  O  OD2 . ASP A 1 758  ? 152.942 109.430 125.275 1.00 176.30 ? 758  ASP A OD2 1 
ATOM   6174  N  N   . ALA A 1 759  ? 148.445 106.820 123.274 1.00 156.10 ? 759  ALA A N   1 
ATOM   6175  C  CA  . ALA A 1 759  ? 147.468 106.091 124.066 1.00 137.45 ? 759  ALA A CA  1 
ATOM   6176  C  C   . ALA A 1 759  ? 147.128 104.788 123.351 1.00 131.65 ? 759  ALA A C   1 
ATOM   6177  O  O   . ALA A 1 759  ? 146.887 104.800 122.129 1.00 133.02 ? 759  ALA A O   1 
ATOM   6178  C  CB  . ALA A 1 759  ? 146.202 106.918 124.302 1.00 130.74 ? 759  ALA A CB  1 
ATOM   6179  N  N   . PRO A 1 760  ? 147.105 103.661 124.063 1.00 128.01 ? 760  PRO A N   1 
ATOM   6180  C  CA  . PRO A 1 760  ? 146.711 102.400 123.427 1.00 123.66 ? 760  PRO A CA  1 
ATOM   6181  C  C   . PRO A 1 760  ? 145.264 102.458 122.964 1.00 122.52 ? 760  PRO A C   1 
ATOM   6182  O  O   . PRO A 1 760  ? 144.429 103.148 123.551 1.00 126.13 ? 760  PRO A O   1 
ATOM   6183  C  CB  . PRO A 1 760  ? 146.910 101.358 124.535 1.00 131.64 ? 760  PRO A CB  1 
ATOM   6184  C  CG  . PRO A 1 760  ? 147.792 102.024 125.551 1.00 136.95 ? 760  PRO A CG  1 
ATOM   6185  C  CD  . PRO A 1 760  ? 147.473 103.481 125.476 1.00 128.94 ? 760  PRO A CD  1 
ATOM   6186  N  N   . ASN A 1 761  ? 144.970 101.716 121.894 1.00 120.42 ? 761  ASN A N   1 
ATOM   6187  C  CA  . ASN A 1 761  ? 143.634 101.765 121.306 1.00 124.52 ? 761  ASN A CA  1 
ATOM   6188  C  C   . ASN A 1 761  ? 142.579 101.210 122.256 1.00 121.93 ? 761  ASN A C   1 
ATOM   6189  O  O   . ASN A 1 761  ? 141.462 101.741 122.335 1.00 128.86 ? 761  ASN A O   1 
ATOM   6190  C  CB  . ASN A 1 761  ? 143.618 100.989 119.990 1.00 124.68 ? 761  ASN A CB  1 
ATOM   6191  C  CG  . ASN A 1 761  ? 142.500 101.429 119.071 1.00 126.11 ? 761  ASN A CG  1 
ATOM   6192  O  OD1 . ASN A 1 761  ? 141.672 102.260 119.439 1.00 124.08 ? 761  ASN A OD1 1 
ATOM   6193  N  ND2 . ASN A 1 761  ? 142.460 100.860 117.872 1.00 132.96 ? 761  ASN A ND2 1 
ATOM   6194  N  N   . ASP A 1 762  ? 142.917 100.151 122.993 1.00 116.41 ? 762  ASP A N   1 
ATOM   6195  C  CA  . ASP A 1 762  ? 141.969 99.568  123.936 1.00 120.90 ? 762  ASP A CA  1 
ATOM   6196  C  C   . ASP A 1 762  ? 141.605 100.560 125.036 1.00 125.30 ? 762  ASP A C   1 
ATOM   6197  O  O   . ASP A 1 762  ? 140.438 100.656 125.444 1.00 128.38 ? 762  ASP A O   1 
ATOM   6198  C  CB  . ASP A 1 762  ? 142.565 98.288  124.527 1.00 127.15 ? 762  ASP A CB  1 
ATOM   6199  C  CG  . ASP A 1 762  ? 141.517 97.371  125.124 1.00 141.29 ? 762  ASP A CG  1 
ATOM   6200  O  OD1 . ASP A 1 762  ? 141.779 96.152  125.208 1.00 143.08 ? 762  ASP A OD1 1 
ATOM   6201  O  OD2 . ASP A 1 762  ? 140.431 97.858  125.498 1.00 141.02 ? 762  ASP A OD2 1 
ATOM   6202  N  N   . TYR A 1 763  ? 142.594 101.319 125.514 1.00 117.20 ? 763  TYR A N   1 
ATOM   6203  C  CA  . TYR A 1 763  ? 142.343 102.324 126.543 1.00 109.55 ? 763  TYR A CA  1 
ATOM   6204  C  C   . TYR A 1 763  ? 141.379 103.397 126.052 1.00 109.84 ? 763  TYR A C   1 
ATOM   6205  O  O   . TYR A 1 763  ? 140.453 103.796 126.772 1.00 114.95 ? 763  TYR A O   1 
ATOM   6206  C  CB  . TYR A 1 763  ? 143.663 102.948 126.993 1.00 111.37 ? 763  TYR A CB  1 
ATOM   6207  C  CG  . TYR A 1 763  ? 143.466 104.027 128.024 1.00 119.26 ? 763  TYR A CG  1 
ATOM   6208  C  CD1 . TYR A 1 763  ? 143.163 103.707 129.338 1.00 122.08 ? 763  TYR A CD1 1 
ATOM   6209  C  CD2 . TYR A 1 763  ? 143.566 105.368 127.681 1.00 119.49 ? 763  TYR A CD2 1 
ATOM   6210  C  CE1 . TYR A 1 763  ? 142.970 104.690 130.285 1.00 128.54 ? 763  TYR A CE1 1 
ATOM   6211  C  CE2 . TYR A 1 763  ? 143.375 106.360 128.621 1.00 120.93 ? 763  TYR A CE2 1 
ATOM   6212  C  CZ  . TYR A 1 763  ? 143.078 106.015 129.923 1.00 127.84 ? 763  TYR A CZ  1 
ATOM   6213  O  OH  . TYR A 1 763  ? 142.886 106.998 130.866 1.00 120.58 ? 763  TYR A OH  1 
ATOM   6214  N  N   . GLN A 1 764  ? 141.582 103.879 124.823 1.00 108.11 ? 764  GLN A N   1 
ATOM   6215  C  CA  . GLN A 1 764  ? 140.677 104.874 124.256 1.00 107.94 ? 764  GLN A CA  1 
ATOM   6216  C  C   . GLN A 1 764  ? 139.274 104.309 124.116 1.00 106.67 ? 764  GLN A C   1 
ATOM   6217  O  O   . GLN A 1 764  ? 138.282 104.985 124.438 1.00 110.18 ? 764  GLN A O   1 
ATOM   6218  C  CB  . GLN A 1 764  ? 141.181 105.322 122.884 1.00 106.47 ? 764  GLN A CB  1 
ATOM   6219  C  CG  . GLN A 1 764  ? 142.629 105.746 122.825 1.00 119.70 ? 764  GLN A CG  1 
ATOM   6220  C  CD  . GLN A 1 764  ? 143.041 106.120 121.416 1.00 117.61 ? 764  GLN A CD  1 
ATOM   6221  O  OE1 . GLN A 1 764  ? 142.246 106.022 120.481 1.00 106.61 ? 764  GLN A OE1 1 
ATOM   6222  N  NE2 . GLN A 1 764  ? 144.288 106.541 121.254 1.00 135.56 ? 764  GLN A NE2 1 
ATOM   6223  N  N   . GLU A 1 765  ? 139.173 103.067 123.638 1.00 106.22 ? 765  GLU A N   1 
ATOM   6224  C  CA  . GLU A 1 765  ? 137.865 102.446 123.470 1.00 95.02  ? 765  GLU A CA  1 
ATOM   6225  C  C   . GLU A 1 765  ? 137.119 102.351 124.791 1.00 94.98  ? 765  GLU A C   1 
ATOM   6226  O  O   . GLU A 1 765  ? 135.910 102.600 124.847 1.00 102.13 ? 765  GLU A O   1 
ATOM   6227  C  CB  . GLU A 1 765  ? 138.021 101.055 122.850 1.00 105.84 ? 765  GLU A CB  1 
ATOM   6228  C  CG  . GLU A 1 765  ? 136.695 100.359 122.560 1.00 130.56 ? 765  GLU A CG  1 
ATOM   6229  C  CD  . GLU A 1 765  ? 135.931 100.968 121.390 1.00 143.25 ? 765  GLU A CD  1 
ATOM   6230  O  OE1 . GLU A 1 765  ? 136.003 102.195 121.161 1.00 127.27 ? 765  GLU A OE1 1 
ATOM   6231  O  OE2 . GLU A 1 765  ? 135.226 100.205 120.699 1.00 132.79 ? 765  GLU A OE2 1 
ATOM   6232  N  N   . ASN A 1 766  ? 137.821 101.995 125.867 1.00 100.18 ? 766  ASN A N   1 
ATOM   6233  C  CA  . ASN A 1 766  ? 137.165 101.907 127.172 1.00 91.17  ? 766  ASN A CA  1 
ATOM   6234  C  C   . ASN A 1 766  ? 136.776 103.280 127.721 1.00 94.60  ? 766  ASN A C   1 
ATOM   6235  O  O   . ASN A 1 766  ? 135.659 103.464 128.232 1.00 99.94  ? 766  ASN A O   1 
ATOM   6236  C  CB  . ASN A 1 766  ? 138.075 101.178 128.159 1.00 102.00 ? 766  ASN A CB  1 
ATOM   6237  C  CG  . ASN A 1 766  ? 137.314 100.619 129.341 1.00 113.90 ? 766  ASN A CG  1 
ATOM   6238  O  OD1 . ASN A 1 766  ? 136.134 100.288 129.231 1.00 116.16 ? 766  ASN A OD1 1 
ATOM   6239  N  ND2 . ASN A 1 766  ? 137.982 100.521 130.484 1.00 107.57 ? 766  ASN A ND2 1 
ATOM   6240  N  N   . GLU A 1 767  ? 137.671 104.266 127.607 1.00 89.08  ? 767  GLU A N   1 
ATOM   6241  C  CA  . GLU A 1 767  ? 137.403 105.564 128.223 1.00 81.67  ? 767  GLU A CA  1 
ATOM   6242  C  C   . GLU A 1 767  ? 136.290 106.328 127.515 1.00 81.04  ? 767  GLU A C   1 
ATOM   6243  O  O   . GLU A 1 767  ? 135.510 107.035 128.176 1.00 95.12  ? 767  GLU A O   1 
ATOM   6244  C  CB  . GLU A 1 767  ? 138.680 106.398 128.273 1.00 102.53 ? 767  GLU A CB  1 
ATOM   6245  C  CG  . GLU A 1 767  ? 139.528 106.080 129.490 1.00 114.96 ? 767  GLU A CG  1 
ATOM   6246  C  CD  . GLU A 1 767  ? 138.813 106.396 130.788 1.00 126.00 ? 767  GLU A CD  1 
ATOM   6247  O  OE1 . GLU A 1 767  ? 138.021 107.361 130.818 1.00 113.20 ? 767  GLU A OE1 1 
ATOM   6248  O  OE2 . GLU A 1 767  ? 139.031 105.666 131.778 1.00 126.35 ? 767  GLU A OE2 1 
ATOM   6249  N  N   . ALA A 1 768  ? 136.187 106.205 126.189 1.00 81.92  ? 768  ALA A N   1 
ATOM   6250  C  CA  . ALA A 1 768  ? 135.111 106.897 125.487 1.00 78.80  ? 768  ALA A CA  1 
ATOM   6251  C  C   . ALA A 1 768  ? 133.747 106.411 125.966 1.00 89.96  ? 768  ALA A C   1 
ATOM   6252  O  O   . ALA A 1 768  ? 132.840 107.217 126.229 1.00 99.06  ? 768  ALA A O   1 
ATOM   6253  C  CB  . ALA A 1 768  ? 135.258 106.694 123.979 1.00 80.75  ? 768  ALA A CB  1 
ATOM   6254  N  N   . GLU A 1 769  ? 133.598 105.094 126.124 1.00 78.73  ? 769  GLU A N   1 
ATOM   6255  C  CA  . GLU A 1 769  ? 132.347 104.549 126.632 1.00 65.64  ? 769  GLU A CA  1 
ATOM   6256  C  C   . GLU A 1 769  ? 132.102 104.938 128.084 1.00 70.99  ? 769  GLU A C   1 
ATOM   6257  O  O   . GLU A 1 769  ? 130.949 105.162 128.468 1.00 74.64  ? 769  GLU A O   1 
ATOM   6258  C  CB  . GLU A 1 769  ? 132.344 103.034 126.464 1.00 63.98  ? 769  GLU A CB  1 
ATOM   6259  C  CG  . GLU A 1 769  ? 132.184 102.618 125.016 1.00 64.83  ? 769  GLU A CG  1 
ATOM   6260  C  CD  . GLU A 1 769  ? 132.296 101.128 124.822 1.00 80.95  ? 769  GLU A CD  1 
ATOM   6261  O  OE1 . GLU A 1 769  ? 132.782 100.444 125.746 1.00 84.23  ? 769  GLU A OE1 1 
ATOM   6262  O  OE2 . GLU A 1 769  ? 131.909 100.641 123.740 1.00 76.88  ? 769  GLU A OE2 1 
ATOM   6263  N  N   . LEU A 1 770  ? 133.153 105.034 128.906 1.00 71.77  ? 770  LEU A N   1 
ATOM   6264  C  CA  . LEU A 1 770  ? 132.930 105.496 130.277 1.00 72.07  ? 770  LEU A CA  1 
ATOM   6265  C  C   . LEU A 1 770  ? 132.366 106.916 130.304 1.00 72.46  ? 770  LEU A C   1 
ATOM   6266  O  O   . LEU A 1 770  ? 131.432 107.213 131.067 1.00 81.04  ? 770  LEU A O   1 
ATOM   6267  C  CB  . LEU A 1 770  ? 134.220 105.425 131.092 1.00 81.70  ? 770  LEU A CB  1 
ATOM   6268  C  CG  . LEU A 1 770  ? 134.442 104.133 131.876 1.00 87.54  ? 770  LEU A CG  1 
ATOM   6269  C  CD1 . LEU A 1 770  ? 135.668 104.259 132.766 1.00 108.40 ? 770  LEU A CD1 1 
ATOM   6270  C  CD2 . LEU A 1 770  ? 133.201 103.807 132.700 1.00 88.11  ? 770  LEU A CD2 1 
ATOM   6271  N  N   . ASN A 1 771  ? 132.920 107.810 129.478 1.00 66.23  ? 771  ASN A N   1 
ATOM   6272  C  CA  . ASN A 1 771  ? 132.412 109.181 129.448 1.00 53.18  ? 771  ASN A CA  1 
ATOM   6273  C  C   . ASN A 1 771  ? 130.969 109.232 128.946 1.00 71.16  ? 771  ASN A C   1 
ATOM   6274  O  O   . ASN A 1 771  ? 130.121 109.951 129.507 1.00 85.93  ? 771  ASN A O   1 
ATOM   6275  C  CB  . ASN A 1 771  ? 133.313 110.046 128.567 1.00 58.10  ? 771  ASN A CB  1 
ATOM   6276  C  CG  . ASN A 1 771  ? 134.600 110.440 129.261 1.00 79.59  ? 771  ASN A CG  1 
ATOM   6277  O  OD1 . ASN A 1 771  ? 134.685 110.426 130.489 1.00 83.01  ? 771  ASN A OD1 1 
ATOM   6278  N  ND2 . ASN A 1 771  ? 135.612 110.794 128.477 1.00 84.65  ? 771  ASN A ND2 1 
ATOM   6279  N  N   . ALA A 1 772  ? 130.668 108.453 127.901 1.00 60.68  ? 772  ALA A N   1 
ATOM   6280  C  CA  . ALA A 1 772  ? 129.296 108.391 127.407 1.00 47.60  ? 772  ALA A CA  1 
ATOM   6281  C  C   . ALA A 1 772  ? 128.338 107.885 128.481 1.00 68.12  ? 772  ALA A C   1 
ATOM   6282  O  O   . ALA A 1 772  ? 127.208 108.377 128.597 1.00 76.81  ? 772  ALA A O   1 
ATOM   6283  C  CB  . ALA A 1 772  ? 129.225 107.513 126.158 1.00 64.44  ? 772  ALA A CB  1 
ATOM   6284  N  N   . ALA A 1 773  ? 128.775 106.914 129.292 1.00 75.24  ? 773  ALA A N   1 
ATOM   6285  C  CA  . ALA A 1 773  ? 127.918 106.416 130.365 1.00 65.23  ? 773  ALA A CA  1 
ATOM   6286  C  C   . ALA A 1 773  ? 127.697 107.467 131.449 1.00 69.26  ? 773  ALA A C   1 
ATOM   6287  O  O   . ALA A 1 773  ? 126.595 107.561 132.010 1.00 81.50  ? 773  ALA A O   1 
ATOM   6288  C  CB  . ALA A 1 773  ? 128.516 105.144 130.962 1.00 75.74  ? 773  ALA A CB  1 
ATOM   6289  N  N   . ARG A 1 774  ? 128.722 108.271 131.758 1.00 62.57  ? 774  ARG A N   1 
ATOM   6290  C  CA  . ARG A 1 774  ? 128.507 109.357 132.714 1.00 54.49  ? 774  ARG A CA  1 
ATOM   6291  C  C   . ARG A 1 774  ? 127.412 110.289 132.218 1.00 54.45  ? 774  ARG A C   1 
ATOM   6292  O  O   . ARG A 1 774  ? 126.486 110.653 132.963 1.00 63.31  ? 774  ARG A O   1 
ATOM   6293  C  CB  . ARG A 1 774  ? 129.781 110.174 132.948 1.00 71.61  ? 774  ARG A CB  1 
ATOM   6294  C  CG  . ARG A 1 774  ? 130.849 109.578 133.833 1.00 89.62  ? 774  ARG A CG  1 
ATOM   6295  C  CD  . ARG A 1 774  ? 132.145 110.336 133.597 1.00 100.68 ? 774  ARG A CD  1 
ATOM   6296  N  NE  . ARG A 1 774  ? 133.239 109.862 134.434 1.00 112.30 ? 774  ARG A NE  1 
ATOM   6297  C  CZ  . ARG A 1 774  ? 134.404 109.441 133.958 1.00 114.82 ? 774  ARG A CZ  1 
ATOM   6298  N  NH1 . ARG A 1 774  ? 134.631 109.463 132.652 1.00 109.80 ? 774  ARG A NH1 1 
ATOM   6299  N  NH2 . ARG A 1 774  ? 135.350 109.025 134.787 1.00 119.48 ? 774  ARG A NH2 1 
ATOM   6300  N  N   . VAL A 1 775  ? 127.506 110.676 130.942 1.00 61.86  ? 775  VAL A N   1 
ATOM   6301  C  CA  . VAL A 1 775  ? 126.506 111.565 130.354 1.00 61.86  ? 775  VAL A CA  1 
ATOM   6302  C  C   . VAL A 1 775  ? 125.118 110.930 130.383 1.00 63.39  ? 775  VAL A C   1 
ATOM   6303  O  O   . VAL A 1 775  ? 124.120 111.600 130.685 1.00 71.11  ? 775  VAL A O   1 
ATOM   6304  C  CB  . VAL A 1 775  ? 126.923 111.959 128.925 1.00 68.97  ? 775  VAL A CB  1 
ATOM   6305  C  CG1 . VAL A 1 775  ? 125.754 112.590 128.184 1.00 59.86  ? 775  VAL A CG1 1 
ATOM   6306  C  CG2 . VAL A 1 775  ? 128.110 112.915 128.964 1.00 75.01  ? 775  VAL A CG2 1 
ATOM   6307  N  N   . ALA A 1 776  ? 125.028 109.634 130.071 1.00 69.56  ? 776  ALA A N   1 
ATOM   6308  C  CA  . ALA A 1 776  ? 123.725 108.970 130.060 1.00 51.81  ? 776  ALA A CA  1 
ATOM   6309  C  C   . ALA A 1 776  ? 123.091 108.952 131.447 1.00 56.89  ? 776  ALA A C   1 
ATOM   6310  O  O   . ALA A 1 776  ? 121.886 109.202 131.589 1.00 75.77  ? 776  ALA A O   1 
ATOM   6311  C  CB  . ALA A 1 776  ? 123.864 107.550 129.515 1.00 69.36  ? 776  ALA A CB  1 
ATOM   6312  N  N   . VAL A 1 777  ? 123.887 108.688 132.487 1.00 70.35  ? 777  VAL A N   1 
ATOM   6313  C  CA  . VAL A 1 777  ? 123.349 108.693 133.848 1.00 62.05  ? 777  VAL A CA  1 
ATOM   6314  C  C   . VAL A 1 777  ? 122.862 110.089 134.223 1.00 61.87  ? 777  VAL A C   1 
ATOM   6315  O  O   . VAL A 1 777  ? 121.776 110.260 134.805 1.00 69.51  ? 777  VAL A O   1 
ATOM   6316  C  CB  . VAL A 1 777  ? 124.399 108.171 134.847 1.00 61.31  ? 777  VAL A CB  1 
ATOM   6317  C  CG1 . VAL A 1 777  ? 124.002 108.527 136.277 1.00 66.45  ? 777  VAL A CG1 1 
ATOM   6318  C  CG2 . VAL A 1 777  ? 124.562 106.664 134.706 1.00 81.10  ? 777  VAL A CG2 1 
ATOM   6319  N  N   . GLU A 1 778  ? 123.658 111.112 133.893 1.00 63.91  ? 778  GLU A N   1 
ATOM   6320  C  CA  . GLU A 1 778  ? 123.254 112.474 134.227 1.00 58.20  ? 778  GLU A CA  1 
ATOM   6321  C  C   . GLU A 1 778  ? 121.952 112.857 133.534 1.00 55.58  ? 778  GLU A C   1 
ATOM   6322  O  O   . GLU A 1 778  ? 121.063 113.459 134.152 1.00 66.95  ? 778  GLU A O   1 
ATOM   6323  C  CB  . GLU A 1 778  ? 124.365 113.457 133.862 1.00 67.88  ? 778  GLU A CB  1 
ATOM   6324  C  CG  . GLU A 1 778  ? 124.195 114.792 134.541 1.00 71.56  ? 778  GLU A CG  1 
ATOM   6325  C  CD  . GLU A 1 778  ? 124.101 114.641 136.045 1.00 99.04  ? 778  GLU A CD  1 
ATOM   6326  O  OE1 . GLU A 1 778  ? 124.866 113.832 136.611 1.00 95.51  ? 778  GLU A OE1 1 
ATOM   6327  O  OE2 . GLU A 1 778  ? 123.240 115.305 136.658 1.00 105.84 ? 778  GLU A OE2 1 
ATOM   6328  N  N   . LEU A 1 779  ? 121.812 112.502 132.254 1.00 53.53  ? 779  LEU A N   1 
ATOM   6329  C  CA  . LEU A 1 779  ? 120.574 112.808 131.544 1.00 46.58  ? 779  LEU A CA  1 
ATOM   6330  C  C   . LEU A 1 779  ? 119.391 112.040 132.124 1.00 57.71  ? 779  LEU A C   1 
ATOM   6331  O  O   . LEU A 1 779  ? 118.274 112.571 132.198 1.00 70.52  ? 779  LEU A O   1 
ATOM   6332  C  CB  . LEU A 1 779  ? 120.733 112.514 130.055 1.00 50.24  ? 779  LEU A CB  1 
ATOM   6333  C  CG  . LEU A 1 779  ? 119.481 112.872 129.257 1.00 52.30  ? 779  LEU A CG  1 
ATOM   6334  C  CD1 . LEU A 1 779  ? 119.407 114.377 129.065 1.00 61.03  ? 779  LEU A CD1 1 
ATOM   6335  C  CD2 . LEU A 1 779  ? 119.470 112.152 127.920 1.00 59.41  ? 779  LEU A CD2 1 
ATOM   6336  N  N   . ALA A 1 780  ? 119.614 110.789 132.539 1.00 59.65  ? 780  ALA A N   1 
ATOM   6337  C  CA  . ALA A 1 780  ? 118.536 110.018 133.149 1.00 46.65  ? 780  ALA A CA  1 
ATOM   6338  C  C   . ALA A 1 780  ? 118.013 110.700 134.406 1.00 48.39  ? 780  ALA A C   1 
ATOM   6339  O  O   . ALA A 1 780  ? 116.798 110.834 134.586 1.00 62.60  ? 780  ALA A O   1 
ATOM   6340  C  CB  . ALA A 1 780  ? 119.016 108.601 133.466 1.00 51.62  ? 780  ALA A CB  1 
ATOM   6341  N  N   . ILE A 1 781  ? 118.917 111.191 135.259 1.00 59.81  ? 781  ILE A N   1 
ATOM   6342  C  CA  . ILE A 1 781  ? 118.481 111.905 136.464 1.00 54.88  ? 781  ILE A CA  1 
ATOM   6343  C  C   . ILE A 1 781  ? 117.761 113.203 136.102 1.00 49.07  ? 781  ILE A C   1 
ATOM   6344  O  O   . ILE A 1 781  ? 116.698 113.528 136.663 1.00 55.25  ? 781  ILE A O   1 
ATOM   6345  C  CB  . ILE A 1 781  ? 119.676 112.172 137.396 1.00 58.23  ? 781  ILE A CB  1 
ATOM   6346  C  CG1 . ILE A 1 781  ? 120.222 110.861 137.961 1.00 65.00  ? 781  ILE A CG1 1 
ATOM   6347  C  CG2 . ILE A 1 781  ? 119.273 113.114 138.528 1.00 66.05  ? 781  ILE A CG2 1 
ATOM   6348  C  CD1 . ILE A 1 781  ? 121.520 111.020 138.720 1.00 57.95  ? 781  ILE A CD1 1 
ATOM   6349  N  N   . THR A 1 782  ? 118.327 113.963 135.157 1.00 56.29  ? 782  THR A N   1 
ATOM   6350  C  CA  . THR A 1 782  ? 117.752 115.259 134.806 1.00 52.51  ? 782  THR A CA  1 
ATOM   6351  C  C   . THR A 1 782  ? 116.334 115.116 134.266 1.00 50.57  ? 782  THR A C   1 
ATOM   6352  O  O   . THR A 1 782  ? 115.446 115.895 134.631 1.00 69.53  ? 782  THR A O   1 
ATOM   6353  C  CB  . THR A 1 782  ? 118.648 115.974 133.789 1.00 60.50  ? 782  THR A CB  1 
ATOM   6354  O  OG1 . THR A 1 782  ? 119.823 116.466 134.447 1.00 62.70  ? 782  THR A OG1 1 
ATOM   6355  C  CG2 . THR A 1 782  ? 117.918 117.148 133.141 1.00 51.83  ? 782  THR A CG2 1 
ATOM   6356  N  N   . THR A 1 783  ? 116.089 114.120 133.413 1.00 52.36  ? 783  THR A N   1 
ATOM   6357  C  CA  . THR A 1 783  ? 114.724 113.913 132.934 1.00 54.01  ? 783  THR A CA  1 
ATOM   6358  C  C   . THR A 1 783  ? 113.829 113.253 133.981 1.00 68.42  ? 783  THR A C   1 
ATOM   6359  O  O   . THR A 1 783  ? 112.618 113.512 133.996 1.00 70.34  ? 783  THR A O   1 
ATOM   6360  C  CB  . THR A 1 783  ? 114.721 113.089 131.643 1.00 52.00  ? 783  THR A CB  1 
ATOM   6361  O  OG1 . THR A 1 783  ? 115.321 111.812 131.878 1.00 88.57  ? 783  THR A OG1 1 
ATOM   6362  C  CG2 . THR A 1 783  ? 115.494 113.816 130.545 1.00 66.30  ? 783  THR A CG2 1 
ATOM   6363  N  N   . GLY A 1 784  ? 114.386 112.427 134.875 1.00 66.17  ? 784  GLY A N   1 
ATOM   6364  C  CA  . GLY A 1 784  ? 113.556 111.799 135.898 1.00 53.03  ? 784  GLY A CA  1 
ATOM   6365  C  C   . GLY A 1 784  ? 112.936 112.814 136.836 1.00 49.35  ? 784  GLY A C   1 
ATOM   6366  O  O   . GLY A 1 784  ? 111.761 112.707 137.192 1.00 65.97  ? 784  GLY A O   1 
ATOM   6367  N  N   . TYR A 1 785  ? 113.714 113.818 137.226 1.00 57.41  ? 785  TYR A N   1 
ATOM   6368  C  CA  . TYR A 1 785  ? 113.177 115.002 137.931 1.00 48.89  ? 785  TYR A CA  1 
ATOM   6369  C  C   . TYR A 1 785  ? 112.364 115.918 137.092 1.00 56.59  ? 785  TYR A C   1 
ATOM   6370  O  O   . TYR A 1 785  ? 112.092 117.022 137.572 1.00 59.68  ? 785  TYR A O   1 
ATOM   6371  C  CB  . TYR A 1 785  ? 114.317 115.745 138.623 1.00 67.66  ? 785  TYR A CB  1 
ATOM   6372  C  CG  . TYR A 1 785  ? 114.655 115.161 139.971 1.00 76.39  ? 785  TYR A CG  1 
ATOM   6373  C  CD1 . TYR A 1 785  ? 113.698 114.435 140.672 1.00 74.98  ? 785  TYR A CD1 1 
ATOM   6374  C  CD2 . TYR A 1 785  ? 115.928 115.253 140.510 1.00 82.57  ? 785  TYR A CD2 1 
ATOM   6375  C  CE1 . TYR A 1 785  ? 113.964 113.908 141.918 1.00 65.24  ? 785  TYR A CE1 1 
ATOM   6376  C  CE2 . TYR A 1 785  ? 116.219 114.695 141.748 1.00 87.62  ? 785  TYR A CE2 1 
ATOM   6377  C  CZ  . TYR A 1 785  ? 115.229 114.026 142.447 1.00 84.41  ? 785  TYR A CZ  1 
ATOM   6378  O  OH  . TYR A 1 785  ? 115.505 113.474 143.678 1.00 85.68  ? 785  TYR A OH  1 
ATOM   6379  N  N   . SER A 1 786  ? 111.938 115.537 135.893 1.00 64.69  ? 786  SER A N   1 
ATOM   6380  C  CA  . SER A 1 786  ? 110.953 116.310 135.147 1.00 46.41  ? 786  SER A CA  1 
ATOM   6381  C  C   . SER A 1 786  ? 109.707 115.486 134.849 1.00 56.48  ? 786  SER A C   1 
ATOM   6382  O  O   . SER A 1 786  ? 108.796 115.976 134.175 1.00 60.95  ? 786  SER A O   1 
ATOM   6383  C  CB  . SER A 1 786  ? 111.566 116.860 133.856 1.00 63.05  ? 786  SER A CB  1 
ATOM   6384  O  OG  . SER A 1 786  ? 112.734 117.611 134.139 1.00 80.11  ? 786  SER A OG  1 
ATOM   6385  N  N   . GLY A 1 787  ? 109.636 114.260 135.366 1.00 66.75  ? 787  GLY A N   1 
ATOM   6386  C  CA  . GLY A 1 787  ? 108.514 113.381 135.131 1.00 57.98  ? 787  GLY A CA  1 
ATOM   6387  C  C   . GLY A 1 787  ? 108.672 112.456 133.948 1.00 62.71  ? 787  GLY A C   1 
ATOM   6388  O  O   . GLY A 1 787  ? 107.781 111.633 133.701 1.00 75.28  ? 787  GLY A O   1 
ATOM   6389  N  N   . ILE A 1 788  ? 109.777 112.554 133.215 1.00 65.33  ? 788  ILE A N   1 
ATOM   6390  C  CA  . ILE A 1 788  ? 110.010 111.746 132.026 1.00 72.10  ? 788  ILE A CA  1 
ATOM   6391  C  C   . ILE A 1 788  ? 111.059 110.710 132.389 1.00 87.23  ? 788  ILE A C   1 
ATOM   6392  O  O   . ILE A 1 788  ? 112.179 111.057 132.783 1.00 75.33  ? 788  ILE A O   1 
ATOM   6393  C  CB  . ILE A 1 788  ? 110.468 112.595 130.831 1.00 74.40  ? 788  ILE A CB  1 
ATOM   6394  C  CG1 . ILE A 1 788  ? 109.416 113.650 130.490 1.00 71.54  ? 788  ILE A CG1 1 
ATOM   6395  C  CG2 . ILE A 1 788  ? 110.726 111.708 129.619 1.00 89.96  ? 788  ILE A CG2 1 
ATOM   6396  C  CD1 . ILE A 1 788  ? 109.985 114.876 129.806 1.00 64.82  ? 788  ILE A CD1 1 
ATOM   6397  N  N   . PHE A 1 789  ? 110.708 109.442 132.243 1.00 90.13  ? 789  PHE A N   1 
ATOM   6398  C  CA  . PHE A 1 789  ? 111.536 108.347 132.723 1.00 87.91  ? 789  PHE A CA  1 
ATOM   6399  C  C   . PHE A 1 789  ? 112.185 107.670 131.528 1.00 95.36  ? 789  PHE A C   1 
ATOM   6400  O  O   . PHE A 1 789  ? 111.515 106.978 130.754 1.00 106.06 ? 789  PHE A O   1 
ATOM   6401  C  CB  . PHE A 1 789  ? 110.723 107.362 133.557 1.00 87.11  ? 789  PHE A CB  1 
ATOM   6402  C  CG  . PHE A 1 789  ? 110.453 107.846 134.949 1.00 75.10  ? 789  PHE A CG  1 
ATOM   6403  C  CD1 . PHE A 1 789  ? 111.430 107.762 135.927 1.00 67.20  ? 789  PHE A CD1 1 
ATOM   6404  C  CD2 . PHE A 1 789  ? 109.225 108.392 135.281 1.00 76.79  ? 789  PHE A CD2 1 
ATOM   6405  C  CE1 . PHE A 1 789  ? 111.187 108.215 137.211 1.00 68.77  ? 789  PHE A CE1 1 
ATOM   6406  C  CE2 . PHE A 1 789  ? 108.976 108.844 136.562 1.00 72.31  ? 789  PHE A CE2 1 
ATOM   6407  C  CZ  . PHE A 1 789  ? 109.957 108.755 137.528 1.00 71.15  ? 789  PHE A CZ  1 
ATOM   6408  N  N   . LEU A 1 790  ? 113.492 107.861 131.395 1.00 84.88  ? 790  LEU A N   1 
ATOM   6409  C  CA  . LEU A 1 790  ? 114.263 107.033 130.487 1.00 92.24  ? 790  LEU A CA  1 
ATOM   6410  C  C   . LEU A 1 790  ? 114.325 105.628 131.051 1.00 100.79 ? 790  LEU A C   1 
ATOM   6411  O  O   . LEU A 1 790  ? 114.493 105.434 132.258 1.00 86.89  ? 790  LEU A O   1 
ATOM   6412  C  CB  . LEU A 1 790  ? 115.682 107.575 130.328 1.00 99.70  ? 790  LEU A CB  1 
ATOM   6413  C  CG  . LEU A 1 790  ? 115.906 108.917 129.646 1.00 100.40 ? 790  LEU A CG  1 
ATOM   6414  C  CD1 . LEU A 1 790  ? 117.366 109.026 129.246 1.00 89.66  ? 790  LEU A CD1 1 
ATOM   6415  C  CD2 . LEU A 1 790  ? 115.004 109.035 128.432 1.00 103.86 ? 790  LEU A CD2 1 
ATOM   6416  N  N   . LYS A 1 791  ? 114.181 104.635 130.183 1.00 104.88 ? 791  LYS A N   1 
ATOM   6417  C  CA  . LYS A 1 791  ? 114.223 103.284 130.701 1.00 95.24  ? 791  LYS A CA  1 
ATOM   6418  C  C   . LYS A 1 791  ? 115.576 102.691 130.359 1.00 86.13  ? 791  LYS A C   1 
ATOM   6419  O  O   . LYS A 1 791  ? 115.846 102.415 129.182 1.00 90.61  ? 791  LYS A O   1 
ATOM   6420  C  CB  . LYS A 1 791  ? 113.106 102.443 130.086 1.00 89.24  ? 791  LYS A CB  1 
ATOM   6421  C  CG  . LYS A 1 791  ? 112.667 101.256 130.921 1.00 111.08 ? 791  LYS A CG  1 
ATOM   6422  C  CD  . LYS A 1 791  ? 111.351 100.701 130.397 1.00 131.49 ? 791  LYS A CD  1 
ATOM   6423  C  CE  . LYS A 1 791  ? 111.092 99.294  130.912 1.00 132.07 ? 791  LYS A CE  1 
ATOM   6424  N  NZ  . LYS A 1 791  ? 112.197 98.359  130.554 1.00 103.98 ? 791  LYS A NZ  1 
ATOM   6425  N  N   . PRO A 1 792  ? 116.458 102.502 131.340 1.00 79.00  ? 792  PRO A N   1 
ATOM   6426  C  CA  . PRO A 1 792  ? 117.840 102.085 131.039 1.00 80.02  ? 792  PRO A CA  1 
ATOM   6427  C  C   . PRO A 1 792  ? 117.951 100.695 130.436 1.00 87.40  ? 792  PRO A C   1 
ATOM   6428  O  O   . PRO A 1 792  ? 119.006 100.343 129.878 1.00 85.25  ? 792  PRO A O   1 
ATOM   6429  C  CB  . PRO A 1 792  ? 118.543 102.186 132.405 1.00 57.73  ? 792  PRO A CB  1 
ATOM   6430  C  CG  . PRO A 1 792  ? 117.450 102.234 133.416 1.00 65.12  ? 792  PRO A CG  1 
ATOM   6431  C  CD  . PRO A 1 792  ? 116.286 102.889 132.752 1.00 73.00  ? 792  PRO A CD  1 
ATOM   6432  N  N   . GLU A 1 793  ? 116.869 99.921  130.514 1.00 94.75  ? 793  GLU A N   1 
ATOM   6433  C  CA  . GLU A 1 793  ? 116.862 98.537  130.071 1.00 79.01  ? 793  GLU A CA  1 
ATOM   6434  C  C   . GLU A 1 793  ? 116.966 98.433  128.548 1.00 80.52  ? 793  GLU A C   1 
ATOM   6435  O  O   . GLU A 1 793  ? 117.717 97.603  128.018 1.00 78.98  ? 793  GLU A O   1 
ATOM   6436  C  CB  . GLU A 1 793  ? 115.550 98.018  130.666 1.00 104.52 ? 793  GLU A CB  1 
ATOM   6437  C  CG  . GLU A 1 793  ? 115.623 98.528  132.130 1.00 114.24 ? 793  GLU A CG  1 
ATOM   6438  C  CD  . GLU A 1 793  ? 116.479 97.724  133.074 1.00 119.03 ? 793  GLU A CD  1 
ATOM   6439  O  OE1 . GLU A 1 793  ? 116.105 96.553  133.336 1.00 123.36 ? 793  GLU A OE1 1 
ATOM   6440  O  OE2 . GLU A 1 793  ? 117.644 98.211  133.279 1.00 115.64 ? 793  GLU A OE2 1 
ATOM   6441  N  N   . GLU A 1 794  ? 116.297 99.334  127.837 1.00 87.51  ? 794  GLU A N   1 
ATOM   6442  C  CA  . GLU A 1 794  ? 116.321 99.461  126.372 1.00 94.83  ? 794  GLU A CA  1 
ATOM   6443  C  C   . GLU A 1 794  ? 117.343 100.465 125.836 1.00 90.96  ? 794  GLU A C   1 
ATOM   6444  O  O   . GLU A 1 794  ? 117.357 100.734 124.624 1.00 84.08  ? 794  GLU A O   1 
ATOM   6445  C  CB  . GLU A 1 794  ? 114.979 99.805  125.746 1.00 107.77 ? 794  GLU A CB  1 
ATOM   6446  C  CG  . GLU A 1 794  ? 113.710 98.955  125.652 1.00 114.15 ? 794  GLU A CG  1 
ATOM   6447  C  CD  . GLU A 1 794  ? 112.585 99.237  126.608 1.00 132.08 ? 794  GLU A CD  1 
ATOM   6448  O  OE1 . GLU A 1 794  ? 112.813 99.587  127.785 1.00 124.84 ? 794  GLU A OE1 1 
ATOM   6449  O  OE2 . GLU A 1 794  ? 111.472 99.481  126.005 1.00 133.00 ? 794  GLU A OE2 1 
ATOM   6450  N  N   . THR A 1 795  ? 118.219 101.018 126.669 1.00 84.76  ? 795  THR A N   1 
ATOM   6451  C  CA  . THR A 1 795  ? 119.222 101.961 126.180 1.00 72.38  ? 795  THR A CA  1 
ATOM   6452  C  C   . THR A 1 795  ? 120.585 101.275 126.133 1.00 94.03  ? 795  THR A C   1 
ATOM   6453  O  O   . THR A 1 795  ? 120.959 100.554 127.058 1.00 107.97 ? 795  THR A O   1 
ATOM   6454  C  CB  . THR A 1 795  ? 119.277 103.236 127.040 1.00 80.33  ? 795  THR A CB  1 
ATOM   6455  O  OG1 . THR A 1 795  ? 117.980 103.822 127.111 1.00 85.78  ? 795  THR A OG1 1 
ATOM   6456  C  CG2 . THR A 1 795  ? 120.246 104.273 126.432 1.00 83.42  ? 795  THR A CG2 1 
ATOM   6457  N  N   . PHE A 1 796  ? 121.337 101.513 125.060 1.00 79.53  ? 796  PHE A N   1 
ATOM   6458  C  CA  . PHE A 1 796  ? 122.676 100.940 124.946 1.00 78.05  ? 796  PHE A CA  1 
ATOM   6459  C  C   . PHE A 1 796  ? 123.676 102.052 124.689 1.00 61.56  ? 796  PHE A C   1 
ATOM   6460  O  O   . PHE A 1 796  ? 123.334 103.080 124.110 1.00 71.55  ? 796  PHE A O   1 
ATOM   6461  C  CB  . PHE A 1 796  ? 122.814 99.935  123.788 1.00 88.38  ? 796  PHE A CB  1 
ATOM   6462  C  CG  . PHE A 1 796  ? 122.541 100.542 122.431 1.00 73.45  ? 796  PHE A CG  1 
ATOM   6463  C  CD1 . PHE A 1 796  ? 121.254 100.673 121.938 1.00 82.90  ? 796  PHE A CD1 1 
ATOM   6464  C  CD2 . PHE A 1 796  ? 123.602 100.987 121.653 1.00 78.92  ? 796  PHE A CD2 1 
ATOM   6465  C  CE1 . PHE A 1 796  ? 121.035 101.234 120.689 1.00 76.89  ? 796  PHE A CE1 1 
ATOM   6466  C  CE2 . PHE A 1 796  ? 123.387 101.552 120.409 1.00 76.73  ? 796  PHE A CE2 1 
ATOM   6467  C  CZ  . PHE A 1 796  ? 122.103 101.667 119.925 1.00 78.69  ? 796  PHE A CZ  1 
ATOM   6468  N  N   . VAL A 1 797  ? 124.921 101.812 125.083 1.00 62.61  ? 797  VAL A N   1 
ATOM   6469  C  CA  . VAL A 1 797  ? 126.027 102.719 124.813 1.00 61.85  ? 797  VAL A CA  1 
ATOM   6470  C  C   . VAL A 1 797  ? 127.036 101.958 123.969 1.00 66.39  ? 797  VAL A C   1 
ATOM   6471  O  O   . VAL A 1 797  ? 127.485 100.872 124.357 1.00 84.25  ? 797  VAL A O   1 
ATOM   6472  C  CB  . VAL A 1 797  ? 126.675 103.238 126.107 1.00 58.50  ? 797  VAL A CB  1 
ATOM   6473  C  CG1 . VAL A 1 797  ? 127.970 103.973 125.800 1.00 49.68  ? 797  VAL A CG1 1 
ATOM   6474  C  CG2 . VAL A 1 797  ? 125.704 104.133 126.868 1.00 60.36  ? 797  VAL A CG2 1 
ATOM   6475  N  N   . HIS A 1 798  ? 127.391 102.523 122.817 1.00 61.83  ? 798  HIS A N   1 
ATOM   6476  C  CA  . HIS A 1 798  ? 128.237 101.833 121.860 1.00 54.26  ? 798  HIS A CA  1 
ATOM   6477  C  C   . HIS A 1 798  ? 129.187 102.852 121.247 1.00 62.42  ? 798  HIS A C   1 
ATOM   6478  O  O   . HIS A 1 798  ? 128.918 104.055 121.238 1.00 75.00  ? 798  HIS A O   1 
ATOM   6479  C  CB  . HIS A 1 798  ? 127.404 101.145 120.770 1.00 74.14  ? 798  HIS A CB  1 
ATOM   6480  C  CG  . HIS A 1 798  ? 128.087 99.972  120.136 1.00 73.13  ? 798  HIS A CG  1 
ATOM   6481  N  ND1 . HIS A 1 798  ? 128.726 100.044 118.916 1.00 73.26  ? 798  HIS A ND1 1 
ATOM   6482  C  CD2 . HIS A 1 798  ? 128.197 98.686  120.543 1.00 62.23  ? 798  HIS A CD2 1 
ATOM   6483  C  CE1 . HIS A 1 798  ? 129.221 98.857  118.613 1.00 71.88  ? 798  HIS A CE1 1 
ATOM   6484  N  NE2 . HIS A 1 798  ? 128.911 98.015  119.582 1.00 63.10  ? 798  HIS A NE2 1 
ATOM   6485  N  N   . SER A 1 799  ? 130.311 102.357 120.729 1.00 64.54  ? 799  SER A N   1 
ATOM   6486  C  CA  . SER A 1 799  ? 131.308 103.229 120.125 1.00 64.65  ? 799  SER A CA  1 
ATOM   6487  C  C   . SER A 1 799  ? 131.137 103.400 118.621 1.00 78.77  ? 799  SER A C   1 
ATOM   6488  O  O   . SER A 1 799  ? 131.692 104.349 118.057 1.00 72.86  ? 799  SER A O   1 
ATOM   6489  C  CB  . SER A 1 799  ? 132.717 102.692 120.404 1.00 62.98  ? 799  SER A CB  1 
ATOM   6490  O  OG  . SER A 1 799  ? 133.057 102.808 121.776 1.00 91.04  ? 799  SER A OG  1 
ATOM   6491  N  N   . GLY A 1 800  ? 130.377 102.529 117.964 1.00 91.87  ? 800  GLY A N   1 
ATOM   6492  C  CA  . GLY A 1 800  ? 130.285 102.577 116.519 1.00 65.89  ? 800  GLY A CA  1 
ATOM   6493  C  C   . GLY A 1 800  ? 128.919 102.734 115.885 1.00 58.40  ? 800  GLY A C   1 
ATOM   6494  O  O   . GLY A 1 800  ? 128.812 103.278 114.782 1.00 75.88  ? 800  GLY A O   1 
ATOM   6495  N  N   . PHE A 1 801  ? 127.863 102.281 116.551 1.00 52.89  ? 801  PHE A N   1 
ATOM   6496  C  CA  . PHE A 1 801  ? 126.559 102.199 115.910 1.00 60.08  ? 801  PHE A CA  1 
ATOM   6497  C  C   . PHE A 1 801  ? 125.800 103.517 116.034 1.00 62.87  ? 801  PHE A C   1 
ATOM   6498  O  O   . PHE A 1 801  ? 125.735 104.109 117.114 1.00 76.53  ? 801  PHE A O   1 
ATOM   6499  C  CB  . PHE A 1 801  ? 125.757 101.059 116.540 1.00 53.26  ? 801  PHE A CB  1 
ATOM   6500  C  CG  . PHE A 1 801  ? 124.501 100.727 115.805 1.00 57.65  ? 801  PHE A CG  1 
ATOM   6501  C  CD1 . PHE A 1 801  ? 123.276 101.201 116.238 1.00 65.71  ? 801  PHE A CD1 1 
ATOM   6502  C  CD2 . PHE A 1 801  ? 124.548 99.935  114.672 1.00 52.49  ? 801  PHE A CD2 1 
ATOM   6503  C  CE1 . PHE A 1 801  ? 122.119 100.889 115.550 1.00 73.92  ? 801  PHE A CE1 1 
ATOM   6504  C  CE2 . PHE A 1 801  ? 123.397 99.620  113.980 1.00 57.27  ? 801  PHE A CE2 1 
ATOM   6505  C  CZ  . PHE A 1 801  ? 122.181 100.098 114.419 1.00 67.90  ? 801  PHE A CZ  1 
ATOM   6506  N  N   . ILE A 1 802  ? 125.206 103.959 114.920 1.00 65.65  ? 802  ILE A N   1 
ATOM   6507  C  CA  . ILE A 1 802  ? 124.541 105.263 114.834 1.00 60.67  ? 802  ILE A CA  1 
ATOM   6508  C  C   . ILE A 1 802  ? 123.390 105.181 113.830 1.00 74.99  ? 802  ILE A C   1 
ATOM   6509  O  O   . ILE A 1 802  ? 123.487 104.481 112.818 1.00 83.16  ? 802  ILE A O   1 
ATOM   6510  C  CB  . ILE A 1 802  ? 125.546 106.365 114.421 1.00 61.80  ? 802  ILE A CB  1 
ATOM   6511  C  CG1 . ILE A 1 802  ? 126.535 106.676 115.547 1.00 81.85  ? 802  ILE A CG1 1 
ATOM   6512  C  CG2 . ILE A 1 802  ? 124.833 107.656 114.043 1.00 90.32  ? 802  ILE A CG2 1 
ATOM   6513  C  CD1 . ILE A 1 802  ? 127.622 107.653 115.151 1.00 103.21 ? 802  ILE A CD1 1 
ATOM   6514  N  N   . TYR A 1 803  ? 122.294 105.893 114.117 1.00 78.24  ? 803  TYR A N   1 
ATOM   6515  C  CA  . TYR A 1 803  ? 121.312 106.305 113.120 1.00 83.65  ? 803  TYR A CA  1 
ATOM   6516  C  C   . TYR A 1 803  ? 121.528 107.776 112.751 1.00 87.11  ? 803  TYR A C   1 
ATOM   6517  O  O   . TYR A 1 803  ? 121.491 108.641 113.633 1.00 96.89  ? 803  TYR A O   1 
ATOM   6518  C  CB  . TYR A 1 803  ? 119.900 106.120 113.659 1.00 90.69  ? 803  TYR A CB  1 
ATOM   6519  C  CG  . TYR A 1 803  ? 119.532 104.760 114.155 1.00 90.11  ? 803  TYR A CG  1 
ATOM   6520  C  CD1 . TYR A 1 803  ? 119.115 103.780 113.271 1.00 92.81  ? 803  TYR A CD1 1 
ATOM   6521  C  CD2 . TYR A 1 803  ? 119.529 104.478 115.501 1.00 93.16  ? 803  TYR A CD2 1 
ATOM   6522  C  CE1 . TYR A 1 803  ? 118.759 102.532 113.714 1.00 98.55  ? 803  TYR A CE1 1 
ATOM   6523  C  CE2 . TYR A 1 803  ? 119.176 103.244 115.960 1.00 86.27  ? 803  TYR A CE2 1 
ATOM   6524  C  CZ  . TYR A 1 803  ? 118.790 102.269 115.066 1.00 90.46  ? 803  TYR A CZ  1 
ATOM   6525  O  OH  . TYR A 1 803  ? 118.436 101.024 115.530 1.00 96.06  ? 803  TYR A OH  1 
ATOM   6526  N  N   . PHE A 1 804  ? 121.738 108.067 111.453 1.00 76.44  ? 804  PHE A N   1 
ATOM   6527  C  CA  . PHE A 1 804  ? 121.933 109.452 111.018 1.00 83.97  ? 804  PHE A CA  1 
ATOM   6528  C  C   . PHE A 1 804  ? 120.838 109.996 110.099 1.00 98.24  ? 804  PHE A C   1 
ATOM   6529  O  O   . PHE A 1 804  ? 120.164 110.962 110.461 1.00 106.46 ? 804  PHE A O   1 
ATOM   6530  C  CB  . PHE A 1 804  ? 123.289 109.632 110.324 1.00 88.11  ? 804  PHE A CB  1 
ATOM   6531  C  CG  . PHE A 1 804  ? 123.460 110.969 109.718 1.00 103.23 ? 804  PHE A CG  1 
ATOM   6532  C  CD1 . PHE A 1 804  ? 123.177 112.101 110.458 1.00 115.00 ? 804  PHE A CD1 1 
ATOM   6533  C  CD2 . PHE A 1 804  ? 123.821 111.102 108.396 1.00 110.22 ? 804  PHE A CD2 1 
ATOM   6534  C  CE1 . PHE A 1 804  ? 123.289 113.363 109.901 1.00 123.27 ? 804  PHE A CE1 1 
ATOM   6535  C  CE2 . PHE A 1 804  ? 123.944 112.358 107.836 1.00 117.11 ? 804  PHE A CE2 1 
ATOM   6536  C  CZ  . PHE A 1 804  ? 123.680 113.489 108.584 1.00 113.26 ? 804  PHE A CZ  1 
ATOM   6537  N  N   . GLY A 1 805  ? 120.609 109.427 108.929 1.00 98.87  ? 805  GLY A N   1 
ATOM   6538  C  CA  . GLY A 1 805  ? 119.542 109.913 108.057 1.00 95.22  ? 805  GLY A CA  1 
ATOM   6539  C  C   . GLY A 1 805  ? 118.343 109.061 108.306 1.00 102.00 ? 805  GLY A C   1 
ATOM   6540  O  O   . GLY A 1 805  ? 117.656 109.336 109.301 1.00 107.34 ? 805  GLY A O   1 
ATOM   6541  N  N   . LYS A 1 806  ? 117.906 108.252 107.343 1.00 95.21  ? 806  LYS A N   1 
ATOM   6542  C  CA  . LYS A 1 806  ? 117.094 107.091 107.691 1.00 106.13 ? 806  LYS A CA  1 
ATOM   6543  C  C   . LYS A 1 806  ? 117.900 105.810 107.592 1.00 97.42  ? 806  LYS A C   1 
ATOM   6544  O  O   . LYS A 1 806  ? 117.347 104.749 107.315 1.00 105.73 ? 806  LYS A O   1 
ATOM   6545  C  CB  . LYS A 1 806  ? 115.816 107.008 106.859 1.00 131.17 ? 806  LYS A CB  1 
ATOM   6546  C  CG  . LYS A 1 806  ? 114.802 108.098 107.138 1.00 138.68 ? 806  LYS A CG  1 
ATOM   6547  C  CD  . LYS A 1 806  ? 113.530 107.875 106.306 1.00 124.90 ? 806  LYS A CD  1 
ATOM   6548  C  CE  . LYS A 1 806  ? 112.529 108.996 106.514 1.00 125.18 ? 806  LYS A CE  1 
ATOM   6549  N  NZ  . LYS A 1 806  ? 112.003 108.995 107.901 1.00 117.94 ? 806  LYS A NZ  1 
ATOM   6550  N  N   . LYS A 1 807  ? 119.200 105.914 107.809 1.00 97.28  ? 807  LYS A N   1 
ATOM   6551  C  CA  . LYS A 1 807  ? 120.180 104.880 107.563 1.00 89.32  ? 807  LYS A CA  1 
ATOM   6552  C  C   . LYS A 1 807  ? 120.963 104.569 108.831 1.00 86.54  ? 807  LYS A C   1 
ATOM   6553  O  O   . LYS A 1 807  ? 120.916 105.295 109.828 1.00 89.34  ? 807  LYS A O   1 
ATOM   6554  C  CB  . LYS A 1 807  ? 121.137 105.367 106.474 1.00 69.89  ? 807  LYS A CB  1 
ATOM   6555  C  CG  . LYS A 1 807  ? 120.409 105.858 105.225 1.00 74.33  ? 807  LYS A CG  1 
ATOM   6556  C  CD  . LYS A 1 807  ? 121.374 106.081 104.072 1.00 84.75  ? 807  LYS A CD  1 
ATOM   6557  C  CE  . LYS A 1 807  ? 121.986 107.478 104.171 1.00 84.37  ? 807  LYS A CE  1 
ATOM   6558  N  NZ  . LYS A 1 807  ? 121.210 108.482 103.390 1.00 107.65 ? 807  LYS A NZ  1 
ATOM   6559  N  N   . GLN A 1 808  ? 121.690 103.456 108.778 1.00 70.01  ? 808  GLN A N   1 
ATOM   6560  C  CA  . GLN A 1 808  ? 122.468 102.970 109.906 1.00 67.51  ? 808  GLN A CA  1 
ATOM   6561  C  C   . GLN A 1 808  ? 123.942 102.918 109.528 1.00 63.17  ? 808  GLN A C   1 
ATOM   6562  O  O   . GLN A 1 808  ? 124.298 102.519 108.414 1.00 76.24  ? 808  GLN A O   1 
ATOM   6563  C  CB  . GLN A 1 808  ? 121.990 101.582 110.315 1.00 81.72  ? 808  GLN A CB  1 
ATOM   6564  C  CG  . GLN A 1 808  ? 120.484 101.406 110.198 1.00 87.85  ? 808  GLN A CG  1 
ATOM   6565  C  CD  . GLN A 1 808  ? 120.013 100.064 110.716 1.00 70.30  ? 808  GLN A CD  1 
ATOM   6566  O  OE1 . GLN A 1 808  ? 120.751 99.082  110.685 1.00 60.60  ? 808  GLN A OE1 1 
ATOM   6567  N  NE2 . GLN A 1 808  ? 118.767 100.008 111.167 1.00 75.52  ? 808  GLN A NE2 1 
ATOM   6568  N  N   . TYR A 1 809  ? 124.796 103.330 110.461 1.00 50.37  ? 809  TYR A N   1 
ATOM   6569  C  CA  . TYR A 1 809  ? 126.237 103.329 110.262 1.00 49.60  ? 809  TYR A CA  1 
ATOM   6570  C  C   . TYR A 1 809  ? 126.909 102.527 111.365 1.00 52.27  ? 809  TYR A C   1 
ATOM   6571  O  O   . TYR A 1 809  ? 126.484 102.567 112.525 1.00 69.94  ? 809  TYR A O   1 
ATOM   6572  C  CB  . TYR A 1 809  ? 126.809 104.754 110.269 1.00 66.46  ? 809  TYR A CB  1 
ATOM   6573  C  CG  . TYR A 1 809  ? 126.320 105.650 109.154 1.00 63.27  ? 809  TYR A CG  1 
ATOM   6574  C  CD1 . TYR A 1 809  ? 125.065 106.237 109.204 1.00 77.57  ? 809  TYR A CD1 1 
ATOM   6575  C  CD2 . TYR A 1 809  ? 127.132 105.940 108.065 1.00 70.77  ? 809  TYR A CD2 1 
ATOM   6576  C  CE1 . TYR A 1 809  ? 124.619 107.065 108.190 1.00 82.43  ? 809  TYR A CE1 1 
ATOM   6577  C  CE2 . TYR A 1 809  ? 126.695 106.770 107.047 1.00 61.95  ? 809  TYR A CE2 1 
ATOM   6578  C  CZ  . TYR A 1 809  ? 125.438 107.330 107.113 1.00 66.10  ? 809  TYR A CZ  1 
ATOM   6579  O  OH  . TYR A 1 809  ? 124.999 108.158 106.103 1.00 77.08  ? 809  TYR A OH  1 
ATOM   6580  N  N   . LEU A 1 810  ? 127.956 101.795 110.999 1.00 56.82  ? 810  LEU A N   1 
ATOM   6581  C  CA  . LEU A 1 810  ? 128.796 101.068 111.949 1.00 48.18  ? 810  LEU A CA  1 
ATOM   6582  C  C   . LEU A 1 810  ? 130.236 101.530 111.754 1.00 60.09  ? 810  LEU A C   1 
ATOM   6583  O  O   . LEU A 1 810  ? 130.893 101.130 110.788 1.00 75.31  ? 810  LEU A O   1 
ATOM   6584  C  CB  . LEU A 1 810  ? 128.653 99.561  111.786 1.00 62.85  ? 810  LEU A CB  1 
ATOM   6585  C  CG  . LEU A 1 810  ? 129.556 98.766  112.726 1.00 59.77  ? 810  LEU A CG  1 
ATOM   6586  C  CD1 . LEU A 1 810  ? 129.115 98.943  114.171 1.00 64.09  ? 810  LEU A CD1 1 
ATOM   6587  C  CD2 . LEU A 1 810  ? 129.533 97.297  112.338 1.00 74.27  ? 810  LEU A CD2 1 
ATOM   6588  N  N   . ASN A 1 811  ? 130.717 102.384 112.661 1.00 70.65  ? 811  ASN A N   1 
ATOM   6589  C  CA  . ASN A 1 811  ? 132.075 102.931 112.603 1.00 63.72  ? 811  ASN A CA  1 
ATOM   6590  C  C   . ASN A 1 811  ? 132.294 103.765 111.345 1.00 62.32  ? 811  ASN A C   1 
ATOM   6591  O  O   . ASN A 1 811  ? 133.394 103.790 110.788 1.00 79.38  ? 811  ASN A O   1 
ATOM   6592  C  CB  . ASN A 1 811  ? 133.130 101.822 112.693 1.00 64.26  ? 811  ASN A CB  1 
ATOM   6593  C  CG  . ASN A 1 811  ? 133.514 101.488 114.120 1.00 68.91  ? 811  ASN A CG  1 
ATOM   6594  O  OD1 . ASN A 1 811  ? 133.904 102.363 114.894 1.00 68.97  ? 811  ASN A OD1 1 
ATOM   6595  N  ND2 . ASN A 1 811  ? 133.416 100.212 114.474 1.00 65.99  ? 811  ASN A ND2 1 
ATOM   6596  N  N   . GLY A 1 812  ? 131.250 104.448 110.878 1.00 72.13  ? 812  GLY A N   1 
ATOM   6597  C  CA  . GLY A 1 812  ? 131.344 105.276 109.697 1.00 76.71  ? 812  GLY A CA  1 
ATOM   6598  C  C   . GLY A 1 812  ? 131.083 104.552 108.394 1.00 75.83  ? 812  GLY A C   1 
ATOM   6599  O  O   . GLY A 1 812  ? 131.034 105.201 107.341 1.00 87.96  ? 812  GLY A O   1 
ATOM   6600  N  N   . VAL A 1 813  ? 130.896 103.237 108.433 1.00 61.19  ? 813  VAL A N   1 
ATOM   6601  C  CA  . VAL A 1 813  ? 130.637 102.445 107.236 1.00 45.94  ? 813  VAL A CA  1 
ATOM   6602  C  C   . VAL A 1 813  ? 129.130 102.295 107.109 1.00 62.65  ? 813  VAL A C   1 
ATOM   6603  O  O   . VAL A 1 813  ? 128.475 101.738 107.997 1.00 74.22  ? 813  VAL A O   1 
ATOM   6604  C  CB  . VAL A 1 813  ? 131.328 101.074 107.298 1.00 38.72  ? 813  VAL A CB  1 
ATOM   6605  C  CG1 . VAL A 1 813  ? 131.126 100.319 105.984 1.00 55.68  ? 813  VAL A CG1 1 
ATOM   6606  C  CG2 . VAL A 1 813  ? 132.810 101.235 107.604 1.00 44.30  ? 813  VAL A CG2 1 
ATOM   6607  N  N   . GLN A 1 814  ? 128.578 102.788 106.008 1.00 68.58  ? 814  GLN A N   1 
ATOM   6608  C  CA  . GLN A 1 814  ? 127.139 102.728 105.832 1.00 62.74  ? 814  GLN A CA  1 
ATOM   6609  C  C   . GLN A 1 814  ? 126.719 101.304 105.502 1.00 56.39  ? 814  GLN A C   1 
ATOM   6610  O  O   . GLN A 1 814  ? 127.396 100.595 104.753 1.00 63.55  ? 814  GLN A O   1 
ATOM   6611  C  CB  . GLN A 1 814  ? 126.719 103.680 104.713 1.00 38.46  ? 814  GLN A CB  1 
ATOM   6612  C  CG  . GLN A 1 814  ? 125.234 103.933 104.613 1.00 50.16  ? 814  GLN A CG  1 
ATOM   6613  C  CD  . GLN A 1 814  ? 124.841 104.418 103.235 1.00 60.87  ? 814  GLN A CD  1 
ATOM   6614  O  OE1 . GLN A 1 814  ? 125.554 105.210 102.619 1.00 59.85  ? 814  GLN A OE1 1 
ATOM   6615  N  NE2 . GLN A 1 814  ? 123.707 103.941 102.740 1.00 66.94  ? 814  GLN A NE2 1 
ATOM   6616  N  N   . LEU A 1 815  ? 125.587 100.892 106.061 1.00 46.71  ? 815  LEU A N   1 
ATOM   6617  C  CA  . LEU A 1 815  ? 125.148 99.529  105.857 1.00 43.02  ? 815  LEU A CA  1 
ATOM   6618  C  C   . LEU A 1 815  ? 123.909 99.493  104.970 1.00 63.35  ? 815  LEU A C   1 
ATOM   6619  O  O   . LEU A 1 815  ? 123.091 100.418 104.995 1.00 63.92  ? 815  LEU A O   1 
ATOM   6620  C  CB  . LEU A 1 815  ? 124.843 98.865  107.207 1.00 52.00  ? 815  LEU A CB  1 
ATOM   6621  C  CG  . LEU A 1 815  ? 125.946 99.024  108.258 1.00 55.46  ? 815  LEU A CG  1 
ATOM   6622  C  CD1 . LEU A 1 815  ? 125.410 98.738  109.653 1.00 68.35  ? 815  LEU A CD1 1 
ATOM   6623  C  CD2 . LEU A 1 815  ? 127.143 98.132  107.939 1.00 53.74  ? 815  LEU A CD2 1 
ATOM   6624  N  N   . PRO A 1 816  ? 123.732 98.433  104.188 1.00 56.04  ? 816  PRO A N   1 
ATOM   6625  C  CA  . PRO A 1 816  ? 122.639 98.416  103.212 1.00 56.73  ? 816  PRO A CA  1 
ATOM   6626  C  C   . PRO A 1 816  ? 121.282 98.151  103.844 1.00 67.89  ? 816  PRO A C   1 
ATOM   6627  O  O   . PRO A 1 816  ? 121.149 97.416  104.826 1.00 79.15  ? 816  PRO A O   1 
ATOM   6628  C  CB  . PRO A 1 816  ? 123.036 97.273  102.271 1.00 61.23  ? 816  PRO A CB  1 
ATOM   6629  C  CG  . PRO A 1 816  ? 123.874 96.370  103.116 1.00 55.41  ? 816  PRO A CG  1 
ATOM   6630  C  CD  . PRO A 1 816  ? 124.629 97.272  104.044 1.00 51.25  ? 816  PRO A CD  1 
ATOM   6631  N  N   . GLN A 1 817  ? 120.265 98.774  103.250 1.00 64.03  ? 817  GLN A N   1 
ATOM   6632  C  CA  . GLN A 1 817  ? 118.877 98.670  103.689 1.00 52.92  ? 817  GLN A CA  1 
ATOM   6633  C  C   . GLN A 1 817  ? 117.958 98.582  102.473 1.00 71.45  ? 817  GLN A C   1 
ATOM   6634  O  O   . GLN A 1 817  ? 116.910 99.233  102.414 1.00 79.97  ? 817  GLN A O   1 
ATOM   6635  C  CB  . GLN A 1 817  ? 118.492 99.846  104.590 1.00 67.95  ? 817  GLN A CB  1 
ATOM   6636  C  CG  . GLN A 1 817  ? 117.207 99.636  105.378 1.00 94.37  ? 817  GLN A CG  1 
ATOM   6637  C  CD  . GLN A 1 817  ? 117.414 98.736  106.578 1.00 99.51  ? 817  GLN A CD  1 
ATOM   6638  O  OE1 . GLN A 1 817  ? 116.615 97.840  106.845 1.00 91.03  ? 817  GLN A OE1 1 
ATOM   6639  N  NE2 . GLN A 1 817  ? 118.491 98.978  107.316 1.00 99.60  ? 817  GLN A NE2 1 
ATOM   6640  N  N   . SER A 1 818  ? 118.337 97.777  101.477 1.00 58.27  ? 818  SER A N   1 
ATOM   6641  C  CA  . SER A 1 818  ? 117.634 97.827  100.196 1.00 57.14  ? 818  SER A CA  1 
ATOM   6642  C  C   . SER A 1 818  ? 116.277 97.134  100.253 1.00 65.05  ? 818  SER A C   1 
ATOM   6643  O  O   . SER A 1 818  ? 115.318 97.592  99.614  1.00 74.50  ? 818  SER A O   1 
ATOM   6644  C  CB  . SER A 1 818  ? 118.486 97.197  99.097  1.00 56.16  ? 818  SER A CB  1 
ATOM   6645  O  OG  . SER A 1 818  ? 117.699 96.913  97.952  1.00 66.86  ? 818  SER A OG  1 
ATOM   6646  N  N   . LEU A 1 819  ? 116.172 96.037  101.008 1.00 67.58  ? 819  LEU A N   1 
ATOM   6647  C  CA  . LEU A 1 819  ? 114.920 95.295  101.028 1.00 49.64  ? 819  LEU A CA  1 
ATOM   6648  C  C   . LEU A 1 819  ? 113.771 96.120  101.585 1.00 62.33  ? 819  LEU A C   1 
ATOM   6649  O  O   . LEU A 1 819  ? 112.621 95.907  101.196 1.00 77.98  ? 819  LEU A O   1 
ATOM   6650  C  CB  . LEU A 1 819  ? 115.087 94.010  101.838 1.00 53.48  ? 819  LEU A CB  1 
ATOM   6651  C  CG  . LEU A 1 819  ? 115.749 92.869  101.080 1.00 61.15  ? 819  LEU A CG  1 
ATOM   6652  C  CD1 . LEU A 1 819  ? 115.944 91.662  101.986 1.00 53.18  ? 819  LEU A CD1 1 
ATOM   6653  C  CD2 . LEU A 1 819  ? 114.929 92.504  99.852  1.00 51.04  ? 819  LEU A CD2 1 
ATOM   6654  N  N   . LYS A 1 820  ? 114.053 97.045  102.506 1.00 62.83  ? 820  LYS A N   1 
ATOM   6655  C  CA  . LYS A 1 820  ? 112.983 97.856  103.080 1.00 67.11  ? 820  LYS A CA  1 
ATOM   6656  C  C   . LYS A 1 820  ? 112.145 98.544  102.007 1.00 64.24  ? 820  LYS A C   1 
ATOM   6657  O  O   . LYS A 1 820  ? 110.915 98.594  102.108 1.00 70.89  ? 820  LYS A O   1 
ATOM   6658  C  CB  . LYS A 1 820  ? 113.569 98.902  104.026 1.00 63.05  ? 820  LYS A CB  1 
ATOM   6659  C  CG  . LYS A 1 820  ? 112.533 99.873  104.570 1.00 74.54  ? 820  LYS A CG  1 
ATOM   6660  C  CD  . LYS A 1 820  ? 113.093 100.819 105.591 1.00 90.76  ? 820  LYS A CD  1 
ATOM   6661  C  CE  . LYS A 1 820  ? 112.400 102.165 105.444 1.00 108.88 ? 820  LYS A CE  1 
ATOM   6662  N  NZ  . LYS A 1 820  ? 111.023 102.083 104.837 1.00 109.97 ? 820  LYS A NZ  1 
ATOM   6663  N  N   . THR A 1 821  ? 112.785 99.071  100.957 1.00 67.14  ? 821  THR A N   1 
ATOM   6664  C  CA  . THR A 1 821  ? 112.054 99.734  99.890  1.00 64.06  ? 821  THR A CA  1 
ATOM   6665  C  C   . THR A 1 821  ? 111.771 98.835  98.699  1.00 55.41  ? 821  THR A C   1 
ATOM   6666  O  O   . THR A 1 821  ? 110.766 99.052  98.012  1.00 68.35  ? 821  THR A O   1 
ATOM   6667  C  CB  . THR A 1 821  ? 112.813 100.973 99.404  1.00 72.72  ? 821  THR A CB  1 
ATOM   6668  O  OG1 . THR A 1 821  ? 112.058 101.635 98.380  1.00 72.95  ? 821  THR A OG1 1 
ATOM   6669  C  CG2 . THR A 1 821  ? 114.175 100.590 98.847  1.00 70.57  ? 821  THR A CG2 1 
ATOM   6670  N  N   . MET A 1 822  ? 112.601 97.822  98.440  1.00 63.80  ? 822  MET A N   1 
ATOM   6671  C  CA  . MET A 1 822  ? 112.394 96.999  97.259  1.00 62.37  ? 822  MET A CA  1 
ATOM   6672  C  C   . MET A 1 822  ? 111.466 95.810  97.486  1.00 63.17  ? 822  MET A C   1 
ATOM   6673  O  O   . MET A 1 822  ? 111.049 95.177  96.511  1.00 70.97  ? 822  MET A O   1 
ATOM   6674  C  CB  . MET A 1 822  ? 113.751 96.513  96.729  1.00 67.88  ? 822  MET A CB  1 
ATOM   6675  C  CG  . MET A 1 822  ? 113.703 96.011  95.302  1.00 67.25  ? 822  MET A CG  1 
ATOM   6676  S  SD  . MET A 1 822  ? 113.623 97.392  94.145  1.00 93.49  ? 822  MET A SD  1 
ATOM   6677  C  CE  . MET A 1 822  ? 112.027 97.095  93.387  1.00 75.57  ? 822  MET A CE  1 
ATOM   6678  N  N   . ALA A 1 823  ? 111.087 95.517  98.729  1.00 72.65  ? 823  ALA A N   1 
ATOM   6679  C  CA  . ALA A 1 823  ? 110.183 94.400  98.975  1.00 55.28  ? 823  ALA A CA  1 
ATOM   6680  C  C   . ALA A 1 823  ? 108.721 94.794  98.816  1.00 68.76  ? 823  ALA A C   1 
ATOM   6681  O  O   . ALA A 1 823  ? 107.855 93.912  98.769  1.00 72.77  ? 823  ALA A O   1 
ATOM   6682  C  CB  . ALA A 1 823  ? 110.413 93.814  100.371 1.00 60.30  ? 823  ALA A CB  1 
ATOM   6683  N  N   . ARG A 1 824  ? 108.434 96.089  98.710  1.00 76.26  ? 824  ARG A N   1 
ATOM   6684  C  CA  . ARG A 1 824  ? 107.082 96.595  98.541  1.00 64.68  ? 824  ARG A CA  1 
ATOM   6685  C  C   . ARG A 1 824  ? 106.744 96.848  97.080  1.00 71.70  ? 824  ARG A C   1 
ATOM   6686  O  O   . ARG A 1 824  ? 105.675 97.388  96.785  1.00 78.30  ? 824  ARG A O   1 
ATOM   6687  C  CB  . ARG A 1 824  ? 106.900 97.888  99.332  1.00 65.23  ? 824  ARG A CB  1 
ATOM   6688  C  CG  . ARG A 1 824  ? 106.849 97.718  100.829 1.00 67.03  ? 824  ARG A CG  1 
ATOM   6689  C  CD  . ARG A 1 824  ? 106.867 99.082  101.484 1.00 81.07  ? 824  ARG A CD  1 
ATOM   6690  N  NE  . ARG A 1 824  ? 105.733 99.900  101.051 1.00 100.59 ? 824  ARG A NE  1 
ATOM   6691  C  CZ  . ARG A 1 824  ? 104.453 99.619  101.283 1.00 112.10 ? 824  ARG A CZ  1 
ATOM   6692  N  NH1 . ARG A 1 824  ? 104.104 98.539  101.969 1.00 102.98 ? 824  ARG A NH1 1 
ATOM   6693  N  NH2 . ARG A 1 824  ? 103.511 100.436 100.829 1.00 107.83 ? 824  ARG A NH2 1 
ATOM   6694  N  N   . CYS A 1 825  ? 107.640 96.484  96.169  1.00 72.47  ? 825  CYS A N   1 
ATOM   6695  C  CA  . CYS A 1 825  ? 107.364 96.613  94.746  1.00 63.70  ? 825  CYS A CA  1 
ATOM   6696  C  C   . CYS A 1 825  ? 106.167 95.749  94.370  1.00 63.91  ? 825  CYS A C   1 
ATOM   6697  O  O   . CYS A 1 825  ? 106.051 94.600  94.801  1.00 64.59  ? 825  CYS A O   1 
ATOM   6698  C  CB  . CYS A 1 825  ? 108.591 96.203  93.935  1.00 49.41  ? 825  CYS A CB  1 
ATOM   6699  S  SG  . CYS A 1 825  ? 108.632 96.846  92.251  1.00 92.70  ? 825  CYS A SG  1 
ATOM   6700  N  N   . GLY A 1 826  ? 105.265 96.314  93.572  1.00 62.27  ? 826  GLY A N   1 
ATOM   6701  C  CA  . GLY A 1 826  ? 104.063 95.619  93.183  1.00 53.59  ? 826  GLY A CA  1 
ATOM   6702  C  C   . GLY A 1 826  ? 103.501 96.085  91.854  1.00 66.46  ? 826  GLY A C   1 
ATOM   6703  O  O   . GLY A 1 826  ? 103.965 97.066  91.260  1.00 65.38  ? 826  GLY A O   1 
ATOM   6704  N  N   . PRO A 1 827  ? 102.476 95.385  91.360  1.00 56.62  ? 827  PRO A N   1 
ATOM   6705  C  CA  . PRO A 1 827  ? 101.900 95.765  90.060  1.00 56.48  ? 827  PRO A CA  1 
ATOM   6706  C  C   . PRO A 1 827  ? 101.065 97.040  90.099  1.00 71.36  ? 827  PRO A C   1 
ATOM   6707  O  O   . PRO A 1 827  ? 100.995 97.759  89.091  1.00 74.03  ? 827  PRO A O   1 
ATOM   6708  C  CB  . PRO A 1 827  ? 101.062 94.531  89.678  1.00 39.92  ? 827  PRO A CB  1 
ATOM   6709  C  CG  . PRO A 1 827  ? 101.527 93.412  90.610  1.00 43.53  ? 827  PRO A CG  1 
ATOM   6710  C  CD  . PRO A 1 827  ? 101.950 94.104  91.862  1.00 51.15  ? 827  PRO A CD  1 
ATOM   6711  N  N   . LEU A 1 828  ? 100.418 97.325  91.229  1.00 63.33  ? 828  LEU A N   1 
ATOM   6712  C  CA  . LEU A 1 828  ? 99.513  98.453  91.403  1.00 51.67  ? 828  LEU A CA  1 
ATOM   6713  C  C   . LEU A 1 828  ? 99.946  99.348  92.547  1.00 76.31  ? 828  LEU A C   1 
ATOM   6714  O  O   . LEU A 1 828  ? 100.569 98.913  93.526  1.00 85.24  ? 828  LEU A O   1 
ATOM   6715  C  CB  . LEU A 1 828  ? 98.056  98.007  91.628  1.00 65.31  ? 828  LEU A CB  1 
ATOM   6716  C  CG  . LEU A 1 828  ? 97.287  97.393  90.469  1.00 59.20  ? 828  LEU A CG  1 
ATOM   6717  C  CD1 . LEU A 1 828  ? 96.024  96.686  90.873  1.00 67.07  ? 828  LEU A CD1 1 
ATOM   6718  C  CD2 . LEU A 1 828  ? 96.730  98.712  89.947  1.00 69.95  ? 828  LEU A CD2 1 
ATOM   6719  N  N   . SER A 1 829  ? 99.589  100.615 92.389  1.00 76.93  ? 829  SER A N   1 
ATOM   6720  C  CA  . SER A 1 829  ? 99.783  101.671 93.354  1.00 85.03  ? 829  SER A CA  1 
ATOM   6721  C  C   . SER A 1 829  ? 98.465  102.406 93.493  1.00 94.37  ? 829  SER A C   1 
ATOM   6722  O  O   . SER A 1 829  ? 97.477  102.081 92.831  1.00 90.17  ? 829  SER A O   1 
ATOM   6723  C  CB  . SER A 1 829  ? 100.917 102.603 92.906  1.00 95.09  ? 829  SER A CB  1 
ATOM   6724  O  OG  . SER A 1 829  ? 102.114 101.853 92.788  1.00 102.75 ? 829  SER A OG  1 
ATOM   6725  N  N   . ASP A 1 830  ? 98.464  103.405 94.360  1.00 112.98 ? 830  ASP A N   1 
ATOM   6726  C  CA  . ASP A 1 830  ? 97.248  104.133 94.683  1.00 121.31 ? 830  ASP A CA  1 
ATOM   6727  C  C   . ASP A 1 830  ? 97.165  105.308 93.722  1.00 115.84 ? 830  ASP A C   1 
ATOM   6728  O  O   . ASP A 1 830  ? 97.710  106.383 93.972  1.00 124.33 ? 830  ASP A O   1 
ATOM   6729  C  CB  . ASP A 1 830  ? 97.293  104.579 96.135  1.00 139.25 ? 830  ASP A CB  1 
ATOM   6730  C  CG  . ASP A 1 830  ? 97.228  103.413 97.095  1.00 142.98 ? 830  ASP A CG  1 
ATOM   6731  O  OD1 . ASP A 1 830  ? 96.631  102.379 96.734  1.00 133.53 ? 830  ASP A OD1 1 
ATOM   6732  O  OD2 . ASP A 1 830  ? 97.788  103.527 98.206  1.00 137.64 ? 830  ASP A OD2 1 
ATOM   6733  N  N   . SER A 1 831  ? 96.475  105.102 92.600  1.00 110.40 ? 831  SER A N   1 
ATOM   6734  C  CA  . SER A 1 831  ? 96.330  106.174 91.625  1.00 119.03 ? 831  SER A CA  1 
ATOM   6735  C  C   . SER A 1 831  ? 94.873  106.359 91.231  1.00 111.70 ? 831  SER A C   1 
ATOM   6736  O  O   . SER A 1 831  ? 93.978  105.748 91.826  1.00 104.64 ? 831  SER A O   1 
ATOM   6737  C  CB  . SER A 1 831  ? 97.185  105.885 90.388  1.00 102.61 ? 831  SER A CB  1 
ATOM   6738  O  OG  . SER A 1 831  ? 96.987  104.558 89.926  1.00 95.22  ? 831  SER A OG  1 
ATOM   6739  N  N   . ILE A 1 832  ? 94.627  107.187 90.221  1.00 108.64 ? 832  ILE A N   1 
ATOM   6740  C  CA  . ILE A 1 832  ? 93.269  107.535 89.822  1.00 113.08 ? 832  ILE A CA  1 
ATOM   6741  C  C   . ILE A 1 832  ? 92.834  106.601 88.704  1.00 99.30  ? 832  ILE A C   1 
ATOM   6742  O  O   . ILE A 1 832  ? 93.491  106.526 87.661  1.00 104.51 ? 832  ILE A O   1 
ATOM   6743  C  CB  . ILE A 1 832  ? 93.185  108.999 89.366  1.00 114.26 ? 832  ILE A CB  1 
ATOM   6744  C  CG1 . ILE A 1 832  ? 93.696  109.934 90.460  1.00 136.09 ? 832  ILE A CG1 1 
ATOM   6745  C  CG2 . ILE A 1 832  ? 91.755  109.350 88.974  1.00 106.44 ? 832  ILE A CG2 1 
ATOM   6746  C  CD1 . ILE A 1 832  ? 93.866  111.364 89.997  1.00 135.78 ? 832  ILE A CD1 1 
ATOM   6747  N  N   . PHE A 1 833  ? 91.734  105.883 88.924  1.00 94.91  ? 833  PHE A N   1 
ATOM   6748  C  CA  . PHE A 1 833  ? 91.137  105.026 87.901  1.00 93.79  ? 833  PHE A CA  1 
ATOM   6749  C  C   . PHE A 1 833  ? 92.104  103.943 87.430  1.00 96.83  ? 833  PHE A C   1 
ATOM   6750  O  O   . PHE A 1 833  ? 92.036  103.498 86.282  1.00 95.75  ? 833  PHE A O   1 
ATOM   6751  C  CB  . PHE A 1 833  ? 90.631  105.849 86.713  1.00 84.20  ? 833  PHE A CB  1 
ATOM   6752  C  CG  . PHE A 1 833  ? 89.558  105.164 85.921  1.00 87.66  ? 833  PHE A CG  1 
ATOM   6753  C  CD1 . PHE A 1 833  ? 88.303  104.961 86.465  1.00 100.45 ? 833  PHE A CD1 1 
ATOM   6754  C  CD2 . PHE A 1 833  ? 89.806  104.720 84.633  1.00 85.82  ? 833  PHE A CD2 1 
ATOM   6755  C  CE1 . PHE A 1 833  ? 87.312  104.327 85.740  1.00 86.46  ? 833  PHE A CE1 1 
ATOM   6756  C  CE2 . PHE A 1 833  ? 88.821  104.086 83.903  1.00 91.10  ? 833  PHE A CE2 1 
ATOM   6757  C  CZ  . PHE A 1 833  ? 87.572  103.889 84.457  1.00 78.51  ? 833  PHE A CZ  1 
ATOM   6758  N  N   . ASP A 1 834  ? 93.013  103.520 88.307  1.00 92.74  ? 834  ASP A N   1 
ATOM   6759  C  CA  . ASP A 1 834  ? 93.970  102.460 88.000  1.00 79.41  ? 834  ASP A CA  1 
ATOM   6760  C  C   . ASP A 1 834  ? 94.787  102.823 86.758  1.00 71.72  ? 834  ASP A C   1 
ATOM   6761  O  O   . ASP A 1 834  ? 94.751  102.142 85.732  1.00 82.81  ? 834  ASP A O   1 
ATOM   6762  C  CB  . ASP A 1 834  ? 93.254  101.119 87.819  1.00 80.10  ? 834  ASP A CB  1 
ATOM   6763  C  CG  . ASP A 1 834  ? 93.109  100.362 89.115  1.00 99.35  ? 834  ASP A CG  1 
ATOM   6764  O  OD1 . ASP A 1 834  ? 93.605  100.855 90.147  1.00 98.14  ? 834  ASP A OD1 1 
ATOM   6765  O  OD2 . ASP A 1 834  ? 92.485  99.280  89.104  1.00 94.34  ? 834  ASP A OD2 1 
ATOM   6766  N  N   . ASP A 1 835  ? 95.527  103.923 86.867  1.00 79.18  ? 835  ASP A N   1 
ATOM   6767  C  CA  . ASP A 1 835  ? 96.293  104.410 85.732  1.00 74.64  ? 835  ASP A CA  1 
ATOM   6768  C  C   . ASP A 1 835  ? 97.547  103.563 85.572  1.00 80.22  ? 835  ASP A C   1 
ATOM   6769  O  O   . ASP A 1 835  ? 98.182  103.174 86.556  1.00 92.86  ? 835  ASP A O   1 
ATOM   6770  C  CB  . ASP A 1 835  ? 96.655  105.885 85.912  1.00 84.30  ? 835  ASP A CB  1 
ATOM   6771  C  CG  . ASP A 1 835  ? 97.156  106.516 84.629  1.00 93.38  ? 835  ASP A CG  1 
ATOM   6772  O  OD1 . ASP A 1 835  ? 96.741  106.057 83.544  1.00 84.68  ? 835  ASP A OD1 1 
ATOM   6773  O  OD2 . ASP A 1 835  ? 97.957  107.472 84.701  1.00 100.50 ? 835  ASP A OD2 1 
ATOM   6774  N  N   . LEU A 1 836  ? 97.906  103.279 84.319  1.00 61.18  ? 836  LEU A N   1 
ATOM   6775  C  CA  . LEU A 1 836  ? 99.095  102.470 84.072  1.00 57.52  ? 836  LEU A CA  1 
ATOM   6776  C  C   . LEU A 1 836  ? 100.378 103.245 84.358  1.00 60.34  ? 836  LEU A C   1 
ATOM   6777  O  O   . LEU A 1 836  ? 101.314 102.704 84.968  1.00 74.78  ? 836  LEU A O   1 
ATOM   6778  C  CB  . LEU A 1 836  ? 99.074  101.940 82.640  1.00 54.98  ? 836  LEU A CB  1 
ATOM   6779  C  CG  . LEU A 1 836  ? 100.045 100.785 82.410  1.00 50.10  ? 836  LEU A CG  1 
ATOM   6780  C  CD1 . LEU A 1 836  ? 99.822  99.723  83.470  1.00 64.40  ? 836  LEU A CD1 1 
ATOM   6781  C  CD2 . LEU A 1 836  ? 99.852  100.198 81.024  1.00 42.70  ? 836  LEU A CD2 1 
ATOM   6782  N  N   . GLN A 1 837  ? 100.444 104.513 83.938  1.00 57.70  ? 837  GLN A N   1 
ATOM   6783  C  CA  . GLN A 1 837  ? 101.634 105.300 84.242  1.00 63.89  ? 837  GLN A CA  1 
ATOM   6784  C  C   . GLN A 1 837  ? 101.825 105.490 85.737  1.00 80.65  ? 837  GLN A C   1 
ATOM   6785  O  O   . GLN A 1 837  ? 102.963 105.546 86.201  1.00 83.38  ? 837  GLN A O   1 
ATOM   6786  C  CB  . GLN A 1 837  ? 101.592 106.677 83.588  1.00 64.42  ? 837  GLN A CB  1 
ATOM   6787  C  CG  . GLN A 1 837  ? 101.778 106.719 82.101  1.00 65.31  ? 837  GLN A CG  1 
ATOM   6788  C  CD  . GLN A 1 837  ? 101.821 108.149 81.618  1.00 87.25  ? 837  GLN A CD  1 
ATOM   6789  O  OE1 . GLN A 1 837  ? 101.622 109.079 82.400  1.00 77.49  ? 837  GLN A OE1 1 
ATOM   6790  N  NE2 . GLN A 1 837  ? 102.109 108.339 80.338  1.00 93.28  ? 837  GLN A NE2 1 
ATOM   6791  N  N   . GLY A 1 838  ? 100.742 105.623 86.503  1.00 69.73  ? 838  GLY A N   1 
ATOM   6792  C  CA  . GLY A 1 838  ? 100.900 105.747 87.944  1.00 72.50  ? 838  GLY A CA  1 
ATOM   6793  C  C   . GLY A 1 838  ? 101.633 104.559 88.534  1.00 82.38  ? 838  GLY A C   1 
ATOM   6794  O  O   . GLY A 1 838  ? 102.600 104.710 89.293  1.00 88.55  ? 838  GLY A O   1 
ATOM   6795  N  N   . SER A 1 839  ? 101.227 103.355 88.123  1.00 63.44  ? 839  SER A N   1 
ATOM   6796  C  CA  . SER A 1 839  ? 101.853 102.131 88.606  1.00 55.52  ? 839  SER A CA  1 
ATOM   6797  C  C   . SER A 1 839  ? 103.315 102.058 88.181  1.00 66.53  ? 839  SER A C   1 
ATOM   6798  O  O   . SER A 1 839  ? 104.208 101.803 89.008  1.00 80.73  ? 839  SER A O   1 
ATOM   6799  C  CB  . SER A 1 839  ? 101.074 100.921 88.081  1.00 50.68  ? 839  SER A CB  1 
ATOM   6800  O  OG  . SER A 1 839  ? 99.741  100.906 88.570  1.00 70.03  ? 839  SER A OG  1 
ATOM   6801  N  N   . LEU A 1 840  ? 103.584 102.290 86.893  1.00 49.97  ? 840  LEU A N   1 
ATOM   6802  C  CA  . LEU A 1 840  ? 104.957 102.172 86.408  1.00 48.77  ? 840  LEU A CA  1 
ATOM   6803  C  C   . LEU A 1 840  ? 105.862 103.233 87.029  1.00 56.86  ? 840  LEU A C   1 
ATOM   6804  O  O   . LEU A 1 840  ? 107.030 102.958 87.328  1.00 64.50  ? 840  LEU A O   1 
ATOM   6805  C  CB  . LEU A 1 840  ? 104.980 102.226 84.883  1.00 52.55  ? 840  LEU A CB  1 
ATOM   6806  C  CG  . LEU A 1 840  ? 104.147 101.089 84.284  1.00 43.71  ? 840  LEU A CG  1 
ATOM   6807  C  CD1 . LEU A 1 840  ? 104.251 101.061 82.770  1.00 53.29  ? 840  LEU A CD1 1 
ATOM   6808  C  CD2 . LEU A 1 840  ? 104.603 99.758  84.882  1.00 59.27  ? 840  LEU A CD2 1 
ATOM   6809  N  N   . ALA A 1 841  ? 105.350 104.449 87.228  1.00 53.27  ? 841  ALA A N   1 
ATOM   6810  C  CA  . ALA A 1 841  ? 106.149 105.496 87.849  1.00 61.34  ? 841  ALA A CA  1 
ATOM   6811  C  C   . ALA A 1 841  ? 106.475 105.141 89.293  1.00 70.20  ? 841  ALA A C   1 
ATOM   6812  O  O   . ALA A 1 841  ? 107.600 105.376 89.760  1.00 75.61  ? 841  ALA A O   1 
ATOM   6813  C  CB  . ALA A 1 841  ? 105.410 106.832 87.774  1.00 66.77  ? 841  ALA A CB  1 
ATOM   6814  N  N   . SER A 1 842  ? 105.507 104.563 90.013  1.00 65.71  ? 842  SER A N   1 
ATOM   6815  C  CA  . SER A 1 842  ? 105.788 104.125 91.375  1.00 57.55  ? 842  SER A CA  1 
ATOM   6816  C  C   . SER A 1 842  ? 106.911 103.095 91.383  1.00 64.52  ? 842  SER A C   1 
ATOM   6817  O  O   . SER A 1 842  ? 107.846 103.176 92.196  1.00 79.46  ? 842  SER A O   1 
ATOM   6818  C  CB  . SER A 1 842  ? 104.523 103.541 92.005  1.00 67.90  ? 842  SER A CB  1 
ATOM   6819  O  OG  . SER A 1 842  ? 103.634 104.554 92.446  1.00 87.90  ? 842  SER A OG  1 
ATOM   6820  N  N   . ILE A 1 843  ? 106.842 102.127 90.461  1.00 62.39  ? 843  ILE A N   1 
ATOM   6821  C  CA  . ILE A 1 843  ? 107.895 101.115 90.366  1.00 56.42  ? 843  ILE A CA  1 
ATOM   6822  C  C   . ILE A 1 843  ? 109.247 101.760 90.077  1.00 68.29  ? 843  ILE A C   1 
ATOM   6823  O  O   . ILE A 1 843  ? 110.265 101.400 90.680  1.00 73.52  ? 843  ILE A O   1 
ATOM   6824  C  CB  . ILE A 1 843  ? 107.531 100.053 89.310  1.00 38.24  ? 843  ILE A CB  1 
ATOM   6825  C  CG1 . ILE A 1 843  ? 106.364 99.196  89.804  1.00 43.17  ? 843  ILE A CG1 1 
ATOM   6826  C  CG2 . ILE A 1 843  ? 108.734 99.169  88.998  1.00 45.82  ? 843  ILE A CG2 1 
ATOM   6827  C  CD1 . ILE A 1 843  ? 105.576 98.526  88.700  1.00 48.51  ? 843  ILE A CD1 1 
ATOM   6828  N  N   . GLY A 1 844  ? 109.281 102.726 89.154  1.00 64.19  ? 844  GLY A N   1 
ATOM   6829  C  CA  . GLY A 1 844  ? 110.547 103.354 88.797  1.00 47.25  ? 844  GLY A CA  1 
ATOM   6830  C  C   . GLY A 1 844  ? 111.202 104.082 89.957  1.00 62.83  ? 844  GLY A C   1 
ATOM   6831  O  O   . GLY A 1 844  ? 112.410 103.944 90.200  1.00 78.93  ? 844  GLY A O   1 
ATOM   6832  N  N   . THR A 1 845  ? 110.412 104.867 90.698  1.00 55.35  ? 845  THR A N   1 
ATOM   6833  C  CA  . THR A 1 845  ? 110.980 105.585 91.839  1.00 54.54  ? 845  THR A CA  1 
ATOM   6834  C  C   . THR A 1 845  ? 111.452 104.619 92.923  1.00 65.64  ? 845  THR A C   1 
ATOM   6835  O  O   . THR A 1 845  ? 112.539 104.800 93.506  1.00 76.00  ? 845  THR A O   1 
ATOM   6836  C  CB  . THR A 1 845  ? 109.960 106.571 92.412  1.00 58.84  ? 845  THR A CB  1 
ATOM   6837  O  OG1 . THR A 1 845  ? 108.948 105.856 93.132  1.00 71.10  ? 845  THR A OG1 1 
ATOM   6838  C  CG2 . THR A 1 845  ? 109.318 107.402 91.309  1.00 70.22  ? 845  THR A CG2 1 
ATOM   6839  N  N   . SER A 1 846  ? 110.650 103.587 93.211  1.00 65.85  ? 846  SER A N   1 
ATOM   6840  C  CA  . SER A 1 846  ? 111.078 102.602 94.196  1.00 67.23  ? 846  SER A CA  1 
ATOM   6841  C  C   . SER A 1 846  ? 112.382 101.942 93.775  1.00 64.11  ? 846  SER A C   1 
ATOM   6842  O  O   . SER A 1 846  ? 113.265 101.702 94.608  1.00 82.43  ? 846  SER A O   1 
ATOM   6843  C  CB  . SER A 1 846  ? 109.991 101.543 94.388  1.00 66.90  ? 846  SER A CB  1 
ATOM   6844  O  OG  . SER A 1 846  ? 109.839 100.754 93.220  1.00 72.49  ? 846  SER A OG  1 
ATOM   6845  N  N   . PHE A 1 847  ? 112.536 101.680 92.474  1.00 68.56  ? 847  PHE A N   1 
ATOM   6846  C  CA  . PHE A 1 847  ? 113.769 101.082 91.977  1.00 69.49  ? 847  PHE A CA  1 
ATOM   6847  C  C   . PHE A 1 847  ? 114.966 101.999 92.191  1.00 56.98  ? 847  PHE A C   1 
ATOM   6848  O  O   . PHE A 1 847  ? 116.048 101.534 92.574  1.00 64.76  ? 847  PHE A O   1 
ATOM   6849  C  CB  . PHE A 1 847  ? 113.630 100.709 90.500  1.00 74.51  ? 847  PHE A CB  1 
ATOM   6850  C  CG  . PHE A 1 847  ? 114.924 100.280 89.864  1.00 54.67  ? 847  PHE A CG  1 
ATOM   6851  C  CD1 . PHE A 1 847  ? 115.543 99.108  90.268  1.00 55.87  ? 847  PHE A CD1 1 
ATOM   6852  C  CD2 . PHE A 1 847  ? 115.518 101.034 88.865  1.00 74.91  ? 847  PHE A CD2 1 
ATOM   6853  C  CE1 . PHE A 1 847  ? 116.732 98.695  89.690  1.00 61.06  ? 847  PHE A CE1 1 
ATOM   6854  C  CE2 . PHE A 1 847  ? 116.712 100.626 88.284  1.00 52.29  ? 847  PHE A CE2 1 
ATOM   6855  C  CZ  . PHE A 1 847  ? 117.318 99.456  88.700  1.00 48.40  ? 847  PHE A CZ  1 
ATOM   6856  N  N   . GLU A 1 848  ? 114.812 103.301 91.920  1.00 55.22  ? 848  GLU A N   1 
ATOM   6857  C  CA  . GLU A 1 848  ? 115.995 104.154 92.042  1.00 59.16  ? 848  GLU A CA  1 
ATOM   6858  C  C   . GLU A 1 848  ? 116.431 104.278 93.499  1.00 72.19  ? 848  GLU A C   1 
ATOM   6859  O  O   . GLU A 1 848  ? 117.634 104.221 93.801  1.00 81.99  ? 848  GLU A O   1 
ATOM   6860  C  CB  . GLU A 1 848  ? 115.759 105.547 91.448  1.00 59.79  ? 848  GLU A CB  1 
ATOM   6861  C  CG  . GLU A 1 848  ? 114.710 106.400 92.142  1.00 95.67  ? 848  GLU A CG  1 
ATOM   6862  C  CD  . GLU A 1 848  ? 114.703 107.825 91.631  1.00 97.46  ? 848  GLU A CD  1 
ATOM   6863  O  OE1 . GLU A 1 848  ? 115.773 108.292 91.195  1.00 84.25  ? 848  GLU A OE1 1 
ATOM   6864  O  OE2 . GLU A 1 848  ? 113.647 108.488 91.693  1.00 95.82  ? 848  GLU A OE2 1 
ATOM   6865  N  N   . ARG A 1 849  ? 115.473 104.373 94.430  1.00 63.62  ? 849  ARG A N   1 
ATOM   6866  C  CA  . ARG A 1 849  ? 115.866 104.351 95.842  1.00 65.39  ? 849  ARG A CA  1 
ATOM   6867  C  C   . ARG A 1 849  ? 116.517 103.021 96.224  1.00 66.90  ? 849  ARG A C   1 
ATOM   6868  O  O   . ARG A 1 849  ? 117.573 102.994 96.886  1.00 66.97  ? 849  ARG A O   1 
ATOM   6869  C  CB  . ARG A 1 849  ? 114.655 104.626 96.731  1.00 66.60  ? 849  ARG A CB  1 
ATOM   6870  C  CG  . ARG A 1 849  ? 113.761 105.739 96.227  1.00 85.88  ? 849  ARG A CG  1 
ATOM   6871  C  CD  . ARG A 1 849  ? 112.810 106.214 97.302  1.00 87.57  ? 849  ARG A CD  1 
ATOM   6872  N  NE  . ARG A 1 849  ? 112.197 107.486 96.939  1.00 100.73 ? 849  ARG A NE  1 
ATOM   6873  C  CZ  . ARG A 1 849  ? 110.888 107.699 96.936  1.00 102.36 ? 849  ARG A CZ  1 
ATOM   6874  N  NH1 . ARG A 1 849  ? 110.059 106.720 97.274  1.00 92.31  ? 849  ARG A NH1 1 
ATOM   6875  N  NH2 . ARG A 1 849  ? 110.404 108.883 96.590  1.00 96.94  ? 849  ARG A NH2 1 
ATOM   6876  N  N   . GLY A 1 850  ? 115.918 101.907 95.789  1.00 74.37  ? 850  GLY A N   1 
ATOM   6877  C  CA  . GLY A 1 850  ? 116.468 100.604 96.114  1.00 59.45  ? 850  GLY A CA  1 
ATOM   6878  C  C   . GLY A 1 850  ? 117.905 100.445 95.665  1.00 59.98  ? 850  GLY A C   1 
ATOM   6879  O  O   . GLY A 1 850  ? 118.742 99.926  96.407  1.00 78.02  ? 850  GLY A O   1 
ATOM   6880  N  N   . THR A 1 851  ? 118.216 100.897 94.446  1.00 65.73  ? 851  THR A N   1 
ATOM   6881  C  CA  . THR A 1 851  ? 119.607 100.849 94.009  1.00 68.25  ? 851  THR A CA  1 
ATOM   6882  C  C   . THR A 1 851  ? 120.475 101.788 94.824  1.00 65.10  ? 851  THR A C   1 
ATOM   6883  O  O   . THR A 1 851  ? 121.643 101.474 95.085  1.00 61.28  ? 851  THR A O   1 
ATOM   6884  C  CB  . THR A 1 851  ? 119.744 101.191 92.526  1.00 70.51  ? 851  THR A CB  1 
ATOM   6885  O  OG1 . THR A 1 851  ? 119.263 102.519 92.285  1.00 84.16  ? 851  THR A OG1 1 
ATOM   6886  C  CG2 . THR A 1 851  ? 118.983 100.205 91.678  1.00 86.51  ? 851  THR A CG2 1 
ATOM   6887  N  N   . SER A 1 852  ? 119.940 102.943 95.235  1.00 71.33  ? 852  SER A N   1 
ATOM   6888  C  CA  . SER A 1 852  ? 120.752 103.812 96.076  1.00 56.03  ? 852  SER A CA  1 
ATOM   6889  C  C   . SER A 1 852  ? 121.136 103.151 97.391  1.00 59.21  ? 852  SER A C   1 
ATOM   6890  O  O   . SER A 1 852  ? 122.128 103.559 98.003  1.00 62.60  ? 852  SER A O   1 
ATOM   6891  C  CB  . SER A 1 852  ? 120.016 105.119 96.372  1.00 68.03  ? 852  SER A CB  1 
ATOM   6892  O  OG  . SER A 1 852  ? 120.600 105.787 97.479  1.00 58.13  ? 852  SER A OG  1 
ATOM   6893  N  N   . GLU A 1 853  ? 120.392 102.134 97.836  1.00 73.62  ? 853  GLU A N   1 
ATOM   6894  C  CA  . GLU A 1 853  ? 120.679 101.539 99.138  1.00 52.59  ? 853  GLU A CA  1 
ATOM   6895  C  C   . GLU A 1 853  ? 121.322 100.145 99.084  1.00 56.75  ? 853  GLU A C   1 
ATOM   6896  O  O   . GLU A 1 853  ? 121.187 99.377  100.041 1.00 62.27  ? 853  GLU A O   1 
ATOM   6897  C  CB  . GLU A 1 853  ? 119.414 101.507 99.988  1.00 60.76  ? 853  GLU A CB  1 
ATOM   6898  C  CG  . GLU A 1 853  ? 118.649 102.817 99.954  1.00 89.91  ? 853  GLU A CG  1 
ATOM   6899  C  CD  . GLU A 1 853  ? 117.269 102.709 100.557 1.00 93.99  ? 853  GLU A CD  1 
ATOM   6900  O  OE1 . GLU A 1 853  ? 116.795 101.571 100.753 1.00 92.20  ? 853  GLU A OE1 1 
ATOM   6901  O  OE2 . GLU A 1 853  ? 116.651 103.762 100.820 1.00 97.60  ? 853  GLU A OE2 1 
ATOM   6902  N  N   . THR A 1 854  ? 122.067 99.814  98.033  1.00 69.55  ? 854  THR A N   1 
ATOM   6903  C  CA  . THR A 1 854  ? 122.701 98.501  97.994  1.00 63.11  ? 854  THR A CA  1 
ATOM   6904  C  C   . THR A 1 854  ? 123.862 98.536  97.010  1.00 70.88  ? 854  THR A C   1 
ATOM   6905  O  O   . THR A 1 854  ? 124.157 99.564  96.397  1.00 86.18  ? 854  THR A O   1 
ATOM   6906  C  CB  . THR A 1 854  ? 121.742 97.363  97.655  1.00 63.03  ? 854  THR A CB  1 
ATOM   6907  O  OG1 . THR A 1 854  ? 122.428 96.108  97.747  1.00 67.87  ? 854  THR A OG1 1 
ATOM   6908  C  CG2 . THR A 1 854  ? 121.213 97.508  96.244  1.00 67.10  ? 854  THR A CG2 1 
ATOM   6909  N  N   . ARG A 1 855  ? 124.507 97.375  96.847  1.00 59.64  ? 855  ARG A N   1 
ATOM   6910  C  CA  . ARG A 1 855  ? 125.597 97.224  95.906  1.00 69.88  ? 855  ARG A CA  1 
ATOM   6911  C  C   . ARG A 1 855  ? 125.340 96.150  94.849  1.00 67.65  ? 855  ARG A C   1 
ATOM   6912  O  O   . ARG A 1 855  ? 126.173 95.975  93.954  1.00 69.15  ? 855  ARG A O   1 
ATOM   6913  C  CB  . ARG A 1 855  ? 126.816 96.865  96.753  1.00 61.39  ? 855  ARG A CB  1 
ATOM   6914  C  CG  . ARG A 1 855  ? 126.828 95.390  96.973  1.00 81.24  ? 855  ARG A CG  1 
ATOM   6915  C  CD  . ARG A 1 855  ? 128.052 94.842  97.632  1.00 70.24  ? 855  ARG A CD  1 
ATOM   6916  N  NE  . ARG A 1 855  ? 128.168 93.420  97.362  1.00 65.65  ? 855  ARG A NE  1 
ATOM   6917  C  CZ  . ARG A 1 855  ? 128.790 92.537  98.129  1.00 62.86  ? 855  ARG A CZ  1 
ATOM   6918  N  NH1 . ARG A 1 855  ? 129.346 92.918  99.282  1.00 74.06  ? 855  ARG A NH1 1 
ATOM   6919  N  NH2 . ARG A 1 855  ? 128.878 91.277  97.719  1.00 66.79  ? 855  ARG A NH2 1 
ATOM   6920  N  N   . HIS A 1 856  ? 124.202 95.436  94.905  1.00 70.37  ? 856  HIS A N   1 
ATOM   6921  C  CA  . HIS A 1 856  ? 123.808 94.467  93.896  1.00 55.69  ? 856  HIS A CA  1 
ATOM   6922  C  C   . HIS A 1 856  ? 122.739 95.086  93.000  1.00 68.84  ? 856  HIS A C   1 
ATOM   6923  O  O   . HIS A 1 856  ? 121.700 95.542  93.489  1.00 80.70  ? 856  HIS A O   1 
ATOM   6924  C  CB  . HIS A 1 856  ? 123.270 93.183  94.528  1.00 65.17  ? 856  HIS A CB  1 
ATOM   6925  C  CG  . HIS A 1 856  ? 124.244 92.467  95.411  1.00 59.78  ? 856  HIS A CG  1 
ATOM   6926  N  ND1 . HIS A 1 856  ? 125.087 91.481  94.943  1.00 57.37  ? 856  HIS A ND1 1 
ATOM   6927  C  CD2 . HIS A 1 856  ? 124.507 92.593  96.731  1.00 56.28  ? 856  HIS A CD2 1 
ATOM   6928  C  CE1 . HIS A 1 856  ? 125.828 91.033  95.939  1.00 56.52  ? 856  HIS A CE1 1 
ATOM   6929  N  NE2 . HIS A 1 856  ? 125.497 91.692  97.034  1.00 60.34  ? 856  HIS A NE2 1 
ATOM   6930  N  N   . ILE A 1 857  ? 122.980 95.078  91.693  1.00 62.37  ? 857  ILE A N   1 
ATOM   6931  C  CA  . ILE A 1 857  ? 122.124 95.775  90.738  1.00 50.27  ? 857  ILE A CA  1 
ATOM   6932  C  C   . ILE A 1 857  ? 121.093 94.846  90.113  1.00 51.34  ? 857  ILE A C   1 
ATOM   6933  O  O   . ILE A 1 857  ? 119.897 95.138  90.111  1.00 68.04  ? 857  ILE A O   1 
ATOM   6934  C  CB  . ILE A 1 857  ? 122.985 96.454  89.649  1.00 65.24  ? 857  ILE A CB  1 
ATOM   6935  C  CG1 . ILE A 1 857  ? 123.848 97.557  90.251  1.00 67.63  ? 857  ILE A CG1 1 
ATOM   6936  C  CG2 . ILE A 1 857  ? 122.100 97.017  88.549  1.00 66.83  ? 857  ILE A CG2 1 
ATOM   6937  C  CD1 . ILE A 1 857  ? 125.069 97.896  89.416  1.00 47.92  ? 857  ILE A CD1 1 
ATOM   6938  N  N   . PHE A 1 858  ? 121.537 93.712  89.584  1.00 49.15  ? 858  PHE A N   1 
ATOM   6939  C  CA  . PHE A 1 858  ? 120.715 92.883  88.709  1.00 58.97  ? 858  PHE A CA  1 
ATOM   6940  C  C   . PHE A 1 858  ? 119.579 92.151  89.429  1.00 68.81  ? 858  PHE A C   1 
ATOM   6941  O  O   . PHE A 1 858  ? 118.480 92.028  88.862  1.00 79.85  ? 858  PHE A O   1 
ATOM   6942  C  CB  . PHE A 1 858  ? 121.625 91.892  87.980  1.00 64.84  ? 858  PHE A CB  1 
ATOM   6943  C  CG  . PHE A 1 858  ? 122.673 92.565  87.143  1.00 59.78  ? 858  PHE A CG  1 
ATOM   6944  C  CD1 . PHE A 1 858  ? 122.358 93.109  85.913  1.00 69.68  ? 858  PHE A CD1 1 
ATOM   6945  C  CD2 . PHE A 1 858  ? 123.977 92.665  87.602  1.00 57.15  ? 858  PHE A CD2 1 
ATOM   6946  C  CE1 . PHE A 1 858  ? 123.324 93.743  85.152  1.00 57.24  ? 858  PHE A CE1 1 
ATOM   6947  C  CE2 . PHE A 1 858  ? 124.948 93.293  86.844  1.00 70.58  ? 858  PHE A CE2 1 
ATOM   6948  C  CZ  . PHE A 1 858  ? 124.621 93.833  85.619  1.00 53.95  ? 858  PHE A CZ  1 
ATOM   6949  N  N   . PRO A 1 859  ? 119.784 91.663  90.665  1.00 53.83  ? 859  PRO A N   1 
ATOM   6950  C  CA  . PRO A 1 859  ? 118.651 91.053  91.388  1.00 43.93  ? 859  PRO A CA  1 
ATOM   6951  C  C   . PRO A 1 859  ? 117.440 91.961  91.546  1.00 58.28  ? 859  PRO A C   1 
ATOM   6952  O  O   . PRO A 1 859  ? 116.304 91.477  91.471  1.00 55.94  ? 859  PRO A O   1 
ATOM   6953  C  CB  . PRO A 1 859  ? 119.271 90.699  92.746  1.00 52.68  ? 859  PRO A CB  1 
ATOM   6954  C  CG  . PRO A 1 859  ? 120.684 90.397  92.431  1.00 48.68  ? 859  PRO A CG  1 
ATOM   6955  C  CD  . PRO A 1 859  ? 121.070 91.344  91.323  1.00 60.39  ? 859  PRO A CD  1 
ATOM   6956  N  N   . SER A 1 860  ? 117.639 93.265  91.759  1.00 60.85  ? 860  SER A N   1 
ATOM   6957  C  CA  . SER A 1 860  ? 116.504 94.178  91.872  1.00 51.92  ? 860  SER A CA  1 
ATOM   6958  C  C   . SER A 1 860  ? 115.921 94.536  90.506  1.00 55.03  ? 860  SER A C   1 
ATOM   6959  O  O   . SER A 1 860  ? 114.699 94.714  90.366  1.00 67.46  ? 860  SER A O   1 
ATOM   6960  C  CB  . SER A 1 860  ? 116.940 95.449  92.602  1.00 56.13  ? 860  SER A CB  1 
ATOM   6961  O  OG  . SER A 1 860  ? 117.495 95.154  93.873  1.00 51.43  ? 860  SER A OG  1 
ATOM   6962  N  N   . ARG A 1 861  ? 116.785 94.639  89.496  1.00 55.56  ? 861  ARG A N   1 
ATOM   6963  C  CA  . ARG A 1 861  ? 116.333 94.956  88.147  1.00 54.56  ? 861  ARG A CA  1 
ATOM   6964  C  C   . ARG A 1 861  ? 115.398 93.882  87.616  1.00 57.33  ? 861  ARG A C   1 
ATOM   6965  O  O   . ARG A 1 861  ? 114.399 94.183  86.940  1.00 72.34  ? 861  ARG A O   1 
ATOM   6966  C  CB  . ARG A 1 861  ? 117.544 95.113  87.232  1.00 48.16  ? 861  ARG A CB  1 
ATOM   6967  C  CG  . ARG A 1 861  ? 117.187 95.441  85.814  1.00 51.42  ? 861  ARG A CG  1 
ATOM   6968  C  CD  . ARG A 1 861  ? 116.810 96.893  85.706  1.00 52.73  ? 861  ARG A CD  1 
ATOM   6969  N  NE  . ARG A 1 861  ? 116.512 97.268  84.333  1.00 49.83  ? 861  ARG A NE  1 
ATOM   6970  C  CZ  . ARG A 1 861  ? 116.655 98.498  83.858  1.00 57.88  ? 861  ARG A CZ  1 
ATOM   6971  N  NH1 . ARG A 1 861  ? 117.091 99.468  84.651  1.00 52.84  ? 861  ARG A NH1 1 
ATOM   6972  N  NH2 . ARG A 1 861  ? 116.365 98.759  82.592  1.00 54.51  ? 861  ARG A NH2 1 
ATOM   6973  N  N   . TRP A 1 862  ? 115.708 92.619  87.917  1.00 54.88  ? 862  TRP A N   1 
ATOM   6974  C  CA  . TRP A 1 862  ? 114.835 91.531  87.500  1.00 45.13  ? 862  TRP A CA  1 
ATOM   6975  C  C   . TRP A 1 862  ? 113.430 91.714  88.060  1.00 48.31  ? 862  TRP A C   1 
ATOM   6976  O  O   . TRP A 1 862  ? 112.436 91.560  87.337  1.00 72.27  ? 862  TRP A O   1 
ATOM   6977  C  CB  . TRP A 1 862  ? 115.428 90.197  87.950  1.00 53.11  ? 862  TRP A CB  1 
ATOM   6978  C  CG  . TRP A 1 862  ? 114.878 89.038  87.209  1.00 52.06  ? 862  TRP A CG  1 
ATOM   6979  C  CD1 . TRP A 1 862  ? 115.380 88.485  86.072  1.00 58.50  ? 862  TRP A CD1 1 
ATOM   6980  C  CD2 . TRP A 1 862  ? 113.705 88.287  87.538  1.00 57.59  ? 862  TRP A CD2 1 
ATOM   6981  N  NE1 . TRP A 1 862  ? 114.598 87.433  85.671  1.00 64.66  ? 862  TRP A NE1 1 
ATOM   6982  C  CE2 . TRP A 1 862  ? 113.561 87.290  86.555  1.00 57.50  ? 862  TRP A CE2 1 
ATOM   6983  C  CE3 . TRP A 1 862  ? 112.765 88.360  88.569  1.00 62.06  ? 862  TRP A CE3 1 
ATOM   6984  C  CZ2 . TRP A 1 862  ? 112.516 86.372  86.571  1.00 50.90  ? 862  TRP A CZ2 1 
ATOM   6985  C  CZ3 . TRP A 1 862  ? 111.725 87.444  88.583  1.00 64.62  ? 862  TRP A CZ3 1 
ATOM   6986  C  CH2 . TRP A 1 862  ? 111.609 86.466  87.591  1.00 53.47  ? 862  TRP A CH2 1 
ATOM   6987  N  N   . ILE A 1 863  ? 113.333 92.073  89.343  1.00 60.67  ? 863  ILE A N   1 
ATOM   6988  C  CA  . ILE A 1 863  ? 112.033 92.253  89.983  1.00 54.57  ? 863  ILE A CA  1 
ATOM   6989  C  C   . ILE A 1 863  ? 111.273 93.409  89.347  1.00 58.45  ? 863  ILE A C   1 
ATOM   6990  O  O   . ILE A 1 863  ? 110.064 93.311  89.079  1.00 68.32  ? 863  ILE A O   1 
ATOM   6991  C  CB  . ILE A 1 863  ? 112.221 92.460  91.498  1.00 43.75  ? 863  ILE A CB  1 
ATOM   6992  C  CG1 . ILE A 1 863  ? 112.586 91.134  92.160  1.00 54.11  ? 863  ILE A CG1 1 
ATOM   6993  C  CG2 . ILE A 1 863  ? 110.965 93.034  92.136  1.00 65.88  ? 863  ILE A CG2 1 
ATOM   6994  C  CD1 . ILE A 1 863  ? 111.516 90.080  92.017  1.00 54.65  ? 863  ILE A CD1 1 
ATOM   6995  N  N   . ALA A 1 864  ? 111.967 94.523  89.088  1.00 55.34  ? 864  ALA A N   1 
ATOM   6996  C  CA  . ALA A 1 864  ? 111.287 95.672  88.493  1.00 41.05  ? 864  ALA A CA  1 
ATOM   6997  C  C   . ALA A 1 864  ? 110.714 95.345  87.114  1.00 51.19  ? 864  ALA A C   1 
ATOM   6998  O  O   . ALA A 1 864  ? 109.549 95.661  86.826  1.00 59.19  ? 864  ALA A O   1 
ATOM   6999  C  CB  . ALA A 1 864  ? 112.248 96.859  88.405  1.00 54.32  ? 864  ALA A CB  1 
ATOM   7000  N  N   . SER A 1 865  ? 111.501 94.672  86.265  1.00 46.77  ? 865  SER A N   1 
ATOM   7001  C  CA  . SER A 1 865  ? 111.003 94.311  84.936  1.00 43.06  ? 865  SER A CA  1 
ATOM   7002  C  C   . SER A 1 865  ? 109.845 93.318  85.019  1.00 57.66  ? 865  SER A C   1 
ATOM   7003  O  O   . SER A 1 865  ? 108.841 93.441  84.288  1.00 65.29  ? 865  SER A O   1 
ATOM   7004  C  CB  . SER A 1 865  ? 112.143 93.732  84.099  1.00 51.02  ? 865  SER A CB  1 
ATOM   7005  O  OG  . SER A 1 865  ? 113.289 94.565  84.154  1.00 59.90  ? 865  SER A OG  1 
ATOM   7006  N  N   . PHE A 1 866  ? 109.970 92.327  85.910  1.00 48.60  ? 866  PHE A N   1 
ATOM   7007  C  CA  . PHE A 1 866  ? 108.907 91.352  86.108  1.00 39.12  ? 866  PHE A CA  1 
ATOM   7008  C  C   . PHE A 1 866  ? 107.591 92.042  86.432  1.00 42.93  ? 866  PHE A C   1 
ATOM   7009  O  O   . PHE A 1 866  ? 106.556 91.774  85.803  1.00 54.19  ? 866  PHE A O   1 
ATOM   7010  C  CB  . PHE A 1 866  ? 109.318 90.399  87.234  1.00 51.08  ? 866  PHE A CB  1 
ATOM   7011  C  CG  . PHE A 1 866  ? 108.337 89.296  87.500  1.00 40.89  ? 866  PHE A CG  1 
ATOM   7012  C  CD1 . PHE A 1 866  ? 108.425 88.096  86.819  1.00 49.23  ? 866  PHE A CD1 1 
ATOM   7013  C  CD2 . PHE A 1 866  ? 107.342 89.453  88.450  1.00 44.85  ? 866  PHE A CD2 1 
ATOM   7014  C  CE1 . PHE A 1 866  ? 107.526 87.075  87.069  1.00 49.64  ? 866  PHE A CE1 1 
ATOM   7015  C  CE2 . PHE A 1 866  ? 106.439 88.436  88.703  1.00 54.03  ? 866  PHE A CE2 1 
ATOM   7016  C  CZ  . PHE A 1 866  ? 106.532 87.246  88.012  1.00 46.49  ? 866  PHE A CZ  1 
ATOM   7017  N  N   . HIS A 1 867  ? 107.623 92.971  87.389  1.00 54.30  ? 867  HIS A N   1 
ATOM   7018  C  CA  . HIS A 1 867  ? 106.377 93.596  87.812  1.00 36.62  ? 867  HIS A CA  1 
ATOM   7019  C  C   . HIS A 1 867  ? 105.847 94.578  86.774  1.00 40.21  ? 867  HIS A C   1 
ATOM   7020  O  O   . HIS A 1 867  ? 104.630 94.768  86.681  1.00 53.57  ? 867  HIS A O   1 
ATOM   7021  C  CB  . HIS A 1 867  ? 106.565 94.259  89.175  1.00 40.99  ? 867  HIS A CB  1 
ATOM   7022  C  CG  . HIS A 1 867  ? 106.627 93.276  90.305  1.00 56.13  ? 867  HIS A CG  1 
ATOM   7023  N  ND1 . HIS A 1 867  ? 105.639 92.340  90.528  1.00 60.11  ? 867  HIS A ND1 1 
ATOM   7024  C  CD2 . HIS A 1 867  ? 107.564 93.071  91.261  1.00 62.53  ? 867  HIS A CD2 1 
ATOM   7025  C  CE1 . HIS A 1 867  ? 105.962 91.606  91.577  1.00 41.25  ? 867  HIS A CE1 1 
ATOM   7026  N  NE2 . HIS A 1 867  ? 107.123 92.028  92.041  1.00 56.69  ? 867  HIS A NE2 1 
ATOM   7027  N  N   . SER A 1 868  ? 106.720 95.179  85.958  1.00 52.84  ? 868  SER A N   1 
ATOM   7028  C  CA  . SER A 1 868  ? 106.230 96.020  84.866  1.00 44.38  ? 868  SER A CA  1 
ATOM   7029  C  C   . SER A 1 868  ? 105.392 95.216  83.869  1.00 43.48  ? 868  SER A C   1 
ATOM   7030  O  O   . SER A 1 868  ? 104.247 95.586  83.547  1.00 54.38  ? 868  SER A O   1 
ATOM   7031  C  CB  . SER A 1 868  ? 107.409 96.697  84.164  1.00 43.92  ? 868  SER A CB  1 
ATOM   7032  O  OG  . SER A 1 868  ? 108.194 97.442  85.080  1.00 37.40  ? 868  SER A OG  1 
ATOM   7033  N  N   . MET A 1 869  ? 105.938 94.093  83.383  1.00 48.75  ? 869  MET A N   1 
ATOM   7034  C  CA  . MET A 1 869  ? 105.155 93.289  82.442  1.00 38.97  ? 869  MET A CA  1 
ATOM   7035  C  C   . MET A 1 869  ? 103.896 92.732  83.096  1.00 48.39  ? 869  MET A C   1 
ATOM   7036  O  O   . MET A 1 869  ? 102.825 92.660  82.462  1.00 66.45  ? 869  MET A O   1 
ATOM   7037  C  CB  . MET A 1 869  ? 105.999 92.148  81.873  1.00 56.49  ? 869  MET A CB  1 
ATOM   7038  C  CG  . MET A 1 869  ? 105.300 91.382  80.756  1.00 54.06  ? 869  MET A CG  1 
ATOM   7039  S  SD  . MET A 1 869  ? 104.772 92.395  79.365  1.00 62.15  ? 869  MET A SD  1 
ATOM   7040  C  CE  . MET A 1 869  ? 106.103 92.095  78.208  1.00 49.39  ? 869  MET A CE  1 
ATOM   7041  N  N   . LEU A 1 870  ? 103.997 92.350  84.373  1.00 53.97  ? 870  LEU A N   1 
ATOM   7042  C  CA  . LEU A 1 870  ? 102.816 91.866  85.075  1.00 59.30  ? 870  LEU A CA  1 
ATOM   7043  C  C   . LEU A 1 870  ? 101.734 92.936  85.140  1.00 52.21  ? 870  LEU A C   1 
ATOM   7044  O  O   . LEU A 1 870  ? 100.545 92.639  84.970  1.00 59.50  ? 870  LEU A O   1 
ATOM   7045  C  CB  . LEU A 1 870  ? 103.206 91.400  86.475  1.00 54.88  ? 870  LEU A CB  1 
ATOM   7046  C  CG  . LEU A 1 870  ? 102.049 90.905  87.332  1.00 45.92  ? 870  LEU A CG  1 
ATOM   7047  C  CD1 . LEU A 1 870  ? 101.259 89.851  86.572  1.00 64.68  ? 870  LEU A CD1 1 
ATOM   7048  C  CD2 . LEU A 1 870  ? 102.586 90.346  88.635  1.00 49.67  ? 870  LEU A CD2 1 
ATOM   7049  N  N   . ALA A 1 871  ? 102.128 94.189  85.392  1.00 56.09  ? 871  ALA A N   1 
ATOM   7050  C  CA  . ALA A 1 871  ? 101.153 95.269  85.446  1.00 55.45  ? 871  ALA A CA  1 
ATOM   7051  C  C   . ALA A 1 871  ? 100.435 95.412  84.115  1.00 50.49  ? 871  ALA A C   1 
ATOM   7052  O  O   . ALA A 1 871  ? 99.203  95.545  84.076  1.00 58.20  ? 871  ALA A O   1 
ATOM   7053  C  CB  . ALA A 1 871  ? 101.837 96.581  85.832  1.00 53.29  ? 871  ALA A CB  1 
ATOM   7054  N  N   . ILE A 1 872  ? 101.192 95.362  83.010  1.00 61.30  ? 872  ILE A N   1 
ATOM   7055  C  CA  . ILE A 1 872  ? 100.553 95.496  81.698  1.00 47.74  ? 872  ILE A CA  1 
ATOM   7056  C  C   . ILE A 1 872  ? 99.494  94.417  81.503  1.00 50.46  ? 872  ILE A C   1 
ATOM   7057  O  O   . ILE A 1 872  ? 98.343  94.713  81.163  1.00 66.43  ? 872  ILE A O   1 
ATOM   7058  C  CB  . ILE A 1 872  ? 101.588 95.471  80.559  1.00 46.71  ? 872  ILE A CB  1 
ATOM   7059  C  CG1 . ILE A 1 872  ? 102.429 96.746  80.570  1.00 54.04  ? 872  ILE A CG1 1 
ATOM   7060  C  CG2 . ILE A 1 872  ? 100.882 95.338  79.211  1.00 54.08  ? 872  ILE A CG2 1 
ATOM   7061  C  CD1 . ILE A 1 872  ? 103.314 96.904  79.348  1.00 60.59  ? 872  ILE A CD1 1 
ATOM   7062  N  N   . ASN A 1 873  ? 99.857  93.150  81.740  1.00 53.26  ? 873  ASN A N   1 
ATOM   7063  C  CA  . ASN A 1 873  ? 98.903  92.065  81.478  1.00 48.59  ? 873  ASN A CA  1 
ATOM   7064  C  C   . ASN A 1 873  ? 97.681  92.149  82.394  1.00 57.93  ? 873  ASN A C   1 
ATOM   7065  O  O   . ASN A 1 873  ? 96.521  92.078  81.936  1.00 70.71  ? 873  ASN A O   1 
ATOM   7066  C  CB  . ASN A 1 873  ? 99.600  90.713  81.633  1.00 41.45  ? 873  ASN A CB  1 
ATOM   7067  C  CG  . ASN A 1 873  ? 100.544 90.414  80.488  1.00 62.37  ? 873  ASN A CG  1 
ATOM   7068  O  OD1 . ASN A 1 873  ? 100.380 90.932  79.384  1.00 62.96  ? 873  ASN A OD1 1 
ATOM   7069  N  ND2 . ASN A 1 873  ? 101.547 89.582  80.747  1.00 57.90  ? 873  ASN A ND2 1 
ATOM   7070  N  N   . LEU A 1 874  ? 97.927  92.347  83.694  1.00 53.28  ? 874  LEU A N   1 
ATOM   7071  C  CA  . LEU A 1 874  ? 96.845  92.398  84.668  1.00 46.69  ? 874  LEU A CA  1 
ATOM   7072  C  C   . LEU A 1 874  ? 95.855  93.500  84.331  1.00 56.37  ? 874  LEU A C   1 
ATOM   7073  O  O   . LEU A 1 874  ? 94.641  93.268  84.305  1.00 65.70  ? 874  LEU A O   1 
ATOM   7074  C  CB  . LEU A 1 874  ? 97.423  92.602  86.068  1.00 52.58  ? 874  LEU A CB  1 
ATOM   7075  C  CG  . LEU A 1 874  ? 96.384  92.904  87.143  1.00 59.14  ? 874  LEU A CG  1 
ATOM   7076  C  CD1 . LEU A 1 874  ? 95.548  91.668  87.429  1.00 61.90  ? 874  LEU A CD1 1 
ATOM   7077  C  CD2 . LEU A 1 874  ? 97.063  93.414  88.403  1.00 55.74  ? 874  LEU A CD2 1 
ATOM   7078  N  N   . LEU A 1 875  ? 96.349  94.711  84.068  1.00 66.93  ? 875  LEU A N   1 
ATOM   7079  C  CA  . LEU A 1 875  ? 95.425  95.785  83.733  1.00 50.28  ? 875  LEU A CA  1 
ATOM   7080  C  C   . LEU A 1 875  ? 94.798  95.576  82.363  1.00 54.17  ? 875  LEU A C   1 
ATOM   7081  O  O   . LEU A 1 875  ? 93.689  96.060  82.115  1.00 63.10  ? 875  LEU A O   1 
ATOM   7082  C  CB  . LEU A 1 875  ? 96.126  97.137  83.799  1.00 52.22  ? 875  LEU A CB  1 
ATOM   7083  C  CG  . LEU A 1 875  ? 96.011  97.781  85.175  1.00 53.07  ? 875  LEU A CG  1 
ATOM   7084  C  CD1 . LEU A 1 875  ? 96.560  99.193  85.140  1.00 71.83  ? 875  LEU A CD1 1 
ATOM   7085  C  CD2 . LEU A 1 875  ? 94.557  97.767  85.642  1.00 62.82  ? 875  LEU A CD2 1 
ATOM   7086  N  N   . ASN A 1 876  ? 95.482  94.859  81.467  1.00 57.46  ? 876  ASN A N   1 
ATOM   7087  C  CA  . ASN A 1 876  ? 94.910  94.607  80.152  1.00 57.08  ? 876  ASN A CA  1 
ATOM   7088  C  C   . ASN A 1 876  ? 93.616  93.821  80.253  1.00 58.45  ? 876  ASN A C   1 
ATOM   7089  O  O   . ASN A 1 876  ? 92.630  94.153  79.585  1.00 69.94  ? 876  ASN A O   1 
ATOM   7090  C  CB  . ASN A 1 876  ? 95.900  93.835  79.279  1.00 65.73  ? 876  ASN A CB  1 
ATOM   7091  C  CG  . ASN A 1 876  ? 95.368  93.580  77.873  1.00 66.35  ? 876  ASN A CG  1 
ATOM   7092  O  OD1 . ASN A 1 876  ? 94.361  94.155  77.460  1.00 75.04  ? 876  ASN A OD1 1 
ATOM   7093  N  ND2 . ASN A 1 876  ? 96.021  92.679  77.151  1.00 82.74  ? 876  ASN A ND2 1 
ATOM   7094  N  N   . GLN A 1 877  ? 93.577  92.794  81.097  1.00 69.08  ? 877  GLN A N   1 
ATOM   7095  C  CA  . GLN A 1 877  ? 92.382  91.963  81.061  1.00 61.87  ? 877  GLN A CA  1 
ATOM   7096  C  C   . GLN A 1 877  ? 91.556  91.975  82.345  1.00 57.35  ? 877  GLN A C   1 
ATOM   7097  O  O   . GLN A 1 877  ? 90.533  91.283  82.410  1.00 52.38  ? 877  GLN A O   1 
ATOM   7098  C  CB  . GLN A 1 877  ? 92.762  90.533  80.658  1.00 72.38  ? 877  GLN A CB  1 
ATOM   7099  C  CG  . GLN A 1 877  ? 91.597  89.694  80.166  1.00 72.03  ? 877  GLN A CG  1 
ATOM   7100  C  CD  . GLN A 1 877  ? 92.055  88.552  79.295  1.00 90.76  ? 877  GLN A CD  1 
ATOM   7101  O  OE1 . GLN A 1 877  ? 93.240  88.436  78.982  1.00 81.49  ? 877  GLN A OE1 1 
ATOM   7102  N  NE2 . GLN A 1 877  ? 91.117  87.716  78.873  1.00 111.41 ? 877  GLN A NE2 1 
ATOM   7103  N  N   . ASN A 1 878  ? 91.923  92.766  83.347  1.00 66.52  ? 878  ASN A N   1 
ATOM   7104  C  CA  . ASN A 1 878  ? 91.141  92.812  84.579  1.00 49.12  ? 878  ASN A CA  1 
ATOM   7105  C  C   . ASN A 1 878  ? 91.025  94.239  85.109  1.00 57.71  ? 878  ASN A C   1 
ATOM   7106  O  O   . ASN A 1 878  ? 91.198  94.498  86.301  1.00 60.72  ? 878  ASN A O   1 
ATOM   7107  C  CB  . ASN A 1 878  ? 91.736  91.888  85.638  1.00 64.08  ? 878  ASN A CB  1 
ATOM   7108  C  CG  . ASN A 1 878  ? 90.692  91.377  86.609  1.00 83.00  ? 878  ASN A CG  1 
ATOM   7109  O  OD1 . ASN A 1 878  ? 89.650  92.002  86.801  1.00 76.94  ? 878  ASN A OD1 1 
ATOM   7110  N  ND2 . ASN A 1 878  ? 90.966  90.235  87.228  1.00 79.09  ? 878  ASN A ND2 1 
ATOM   7111  N  N   . HIS A 1 879  ? 90.721  95.189  84.228  1.00 59.45  ? 879  HIS A N   1 
ATOM   7112  C  CA  . HIS A 1 879  ? 90.598  96.573  84.668  1.00 50.61  ? 879  HIS A CA  1 
ATOM   7113  C  C   . HIS A 1 879  ? 89.318  96.740  85.475  1.00 65.92  ? 879  HIS A C   1 
ATOM   7114  O  O   . HIS A 1 879  ? 88.265  96.202  85.120  1.00 79.99  ? 879  HIS A O   1 
ATOM   7115  C  CB  . HIS A 1 879  ? 90.596  97.521  83.467  1.00 62.03  ? 879  HIS A CB  1 
ATOM   7116  C  CG  . HIS A 1 879  ? 91.033  98.917  83.795  1.00 66.55  ? 879  HIS A CG  1 
ATOM   7117  N  ND1 . HIS A 1 879  ? 90.460  99.658  84.808  1.00 72.28  ? 879  HIS A ND1 1 
ATOM   7118  C  CD2 . HIS A 1 879  ? 91.981  99.708  83.240  1.00 64.66  ? 879  HIS A CD2 1 
ATOM   7119  C  CE1 . HIS A 1 879  ? 91.043  100.842 84.866  1.00 67.69  ? 879  HIS A CE1 1 
ATOM   7120  N  NE2 . HIS A 1 879  ? 91.968  100.898 83.924  1.00 61.46  ? 879  HIS A NE2 1 
ATOM   7121  N  N   . LEU A 1 880  ? 89.410  97.489  86.579  1.00 71.25  ? 880  LEU A N   1 
ATOM   7122  C  CA  . LEU A 1 880  ? 88.246  97.680  87.438  1.00 78.67  ? 880  LEU A CA  1 
ATOM   7123  C  C   . LEU A 1 880  ? 87.247  98.670  86.861  1.00 85.89  ? 880  LEU A C   1 
ATOM   7124  O  O   . LEU A 1 880  ? 86.053  98.588  87.173  1.00 94.92  ? 880  LEU A O   1 
ATOM   7125  C  CB  . LEU A 1 880  ? 88.679  98.154  88.825  1.00 81.69  ? 880  LEU A CB  1 
ATOM   7126  C  CG  . LEU A 1 880  ? 89.348  97.139  89.744  1.00 76.40  ? 880  LEU A CG  1 
ATOM   7127  C  CD1 . LEU A 1 880  ? 89.552  97.756  91.116  1.00 95.69  ? 880  LEU A CD1 1 
ATOM   7128  C  CD2 . LEU A 1 880  ? 88.482  95.892  89.839  1.00 69.92  ? 880  LEU A CD2 1 
ATOM   7129  N  N   . GLY A 1 881  ? 87.696  99.596  86.020  1.00 80.49  ? 881  GLY A N   1 
ATOM   7130  C  CA  . GLY A 1 881  ? 86.776  100.581 85.502  1.00 75.93  ? 881  GLY A CA  1 
ATOM   7131  C  C   . GLY A 1 881  ? 85.881  100.109 84.384  1.00 77.42  ? 881  GLY A C   1 
ATOM   7132  O  O   . GLY A 1 881  ? 85.051  100.883 83.902  1.00 86.48  ? 881  GLY A O   1 
ATOM   7133  N  N   . PHE A 1 882  ? 86.010  98.855  83.966  1.00 68.62  ? 882  PHE A N   1 
ATOM   7134  C  CA  . PHE A 1 882  ? 85.193  98.342  82.877  1.00 64.01  ? 882  PHE A CA  1 
ATOM   7135  C  C   . PHE A 1 882  ? 84.360  97.160  83.355  1.00 78.91  ? 882  PHE A C   1 
ATOM   7136  O  O   . PHE A 1 882  ? 84.522  96.716  84.500  1.00 87.60  ? 882  PHE A O   1 
ATOM   7137  C  CB  . PHE A 1 882  ? 86.098  97.936  81.711  1.00 68.37  ? 882  PHE A CB  1 
ATOM   7138  C  CG  . PHE A 1 882  ? 86.806  99.091  81.066  1.00 79.95  ? 882  PHE A CG  1 
ATOM   7139  C  CD1 . PHE A 1 882  ? 87.984  99.584  81.603  1.00 73.78  ? 882  PHE A CD1 1 
ATOM   7140  C  CD2 . PHE A 1 882  ? 86.294  99.690  79.927  1.00 85.40  ? 882  PHE A CD2 1 
ATOM   7141  C  CE1 . PHE A 1 882  ? 88.641  100.649 81.016  1.00 69.40  ? 882  PHE A CE1 1 
ATOM   7142  C  CE2 . PHE A 1 882  ? 86.948  100.757 79.334  1.00 78.61  ? 882  PHE A CE2 1 
ATOM   7143  C  CZ  . PHE A 1 882  ? 88.123  101.237 79.881  1.00 72.56  ? 882  PHE A CZ  1 
ATOM   7144  N  N   . PRO A 1 883  ? 83.458  96.625  82.528  1.00 82.02  ? 883  PRO A N   1 
ATOM   7145  C  CA  . PRO A 1 883  ? 82.765  95.385  82.897  1.00 80.55  ? 883  PRO A CA  1 
ATOM   7146  C  C   . PRO A 1 883  ? 83.755  94.252  83.136  1.00 99.37  ? 883  PRO A C   1 
ATOM   7147  O  O   . PRO A 1 883  ? 84.962  94.378  82.921  1.00 105.38 ? 883  PRO A O   1 
ATOM   7148  C  CB  . PRO A 1 883  ? 81.858  95.112  81.695  1.00 92.06  ? 883  PRO A CB  1 
ATOM   7149  C  CG  . PRO A 1 883  ? 81.580  96.467  81.136  1.00 94.13  ? 883  PRO A CG  1 
ATOM   7150  C  CD  . PRO A 1 883  ? 82.814  97.292  81.380  1.00 90.39  ? 883  PRO A CD  1 
ATOM   7151  N  N   . LEU A 1 884  ? 83.215  93.115  83.579  1.00 98.83  ? 884  LEU A N   1 
ATOM   7152  C  CA  . LEU A 1 884  ? 84.056  92.078  84.172  1.00 110.59 ? 884  LEU A CA  1 
ATOM   7153  C  C   . LEU A 1 884  ? 85.048  91.510  83.160  1.00 119.82 ? 884  LEU A C   1 
ATOM   7154  O  O   . LEU A 1 884  ? 86.250  91.422  83.439  1.00 115.30 ? 884  LEU A O   1 
ATOM   7155  C  CB  . LEU A 1 884  ? 83.179  90.979  84.774  1.00 106.02 ? 884  LEU A CB  1 
ATOM   7156  C  CG  . LEU A 1 884  ? 83.865  89.914  85.637  1.00 99.00  ? 884  LEU A CG  1 
ATOM   7157  C  CD1 . LEU A 1 884  ? 82.879  89.360  86.649  1.00 108.70 ? 884  LEU A CD1 1 
ATOM   7158  C  CD2 . LEU A 1 884  ? 84.432  88.773  84.797  1.00 114.96 ? 884  LEU A CD2 1 
ATOM   7159  N  N   . GLY A 1 885  ? 84.571  91.121  81.980  1.00 108.53 ? 885  GLY A N   1 
ATOM   7160  C  CA  . GLY A 1 885  ? 85.479  90.701  80.928  1.00 93.48  ? 885  GLY A CA  1 
ATOM   7161  C  C   . GLY A 1 885  ? 85.484  91.642  79.744  1.00 95.91  ? 885  GLY A C   1 
ATOM   7162  O  O   . GLY A 1 885  ? 84.503  91.701  78.996  1.00 101.88 ? 885  GLY A O   1 
ATOM   7163  N  N   . PHE A 1 886  ? 86.575  92.380  79.547  1.00 88.26  ? 886  PHE A N   1 
ATOM   7164  C  CA  . PHE A 1 886  ? 86.443  93.408  78.523  1.00 90.76  ? 886  PHE A CA  1 
ATOM   7165  C  C   . PHE A 1 886  ? 87.498  93.357  77.423  1.00 99.32  ? 886  PHE A C   1 
ATOM   7166  O  O   . PHE A 1 886  ? 87.166  93.639  76.269  1.00 101.33 ? 886  PHE A O   1 
ATOM   7167  C  CB  . PHE A 1 886  ? 86.456  94.779  79.206  1.00 80.14  ? 886  PHE A CB  1 
ATOM   7168  C  CG  . PHE A 1 886  ? 86.272  95.918  78.261  1.00 87.59  ? 886  PHE A CG  1 
ATOM   7169  C  CD1 . PHE A 1 886  ? 85.079  96.078  77.579  1.00 86.98  ? 886  PHE A CD1 1 
ATOM   7170  C  CD2 . PHE A 1 886  ? 87.287  96.835  78.056  1.00 89.57  ? 886  PHE A CD2 1 
ATOM   7171  C  CE1 . PHE A 1 886  ? 84.904  97.126  76.701  1.00 98.45  ? 886  PHE A CE1 1 
ATOM   7172  C  CE2 . PHE A 1 886  ? 87.118  97.888  77.181  1.00 83.40  ? 886  PHE A CE2 1 
ATOM   7173  C  CZ  . PHE A 1 886  ? 85.924  98.034  76.503  1.00 102.83 ? 886  PHE A CZ  1 
ATOM   7174  N  N   . ASN A 1 887  ? 88.750  93.017  77.741  1.00 80.21  ? 887  ASN A N   1 
ATOM   7175  C  CA  . ASN A 1 887  ? 89.811  92.872  76.737  1.00 66.39  ? 887  ASN A CA  1 
ATOM   7176  C  C   . ASN A 1 887  ? 90.032  94.179  75.964  1.00 72.73  ? 887  ASN A C   1 
ATOM   7177  O  O   . ASN A 1 887  ? 89.650  94.314  74.799  1.00 80.57  ? 887  ASN A O   1 
ATOM   7178  C  CB  . ASN A 1 887  ? 89.495  91.712  75.786  1.00 84.53  ? 887  ASN A CB  1 
ATOM   7179  C  CG  . ASN A 1 887  ? 90.067  90.394  76.265  1.00 92.67  ? 887  ASN A CG  1 
ATOM   7180  O  OD1 . ASN A 1 887  ? 89.327  89.487  76.646  1.00 95.68  ? 887  ASN A OD1 1 
ATOM   7181  N  ND2 . ASN A 1 887  ? 91.390  90.282  76.254  1.00 99.03  ? 887  ASN A ND2 1 
ATOM   7182  N  N   . ILE A 1 888  ? 90.627  95.158  76.659  1.00 70.47  ? 888  ILE A N   1 
ATOM   7183  C  CA  . ILE A 1 888  ? 90.905  96.468  76.062  1.00 66.93  ? 888  ILE A CA  1 
ATOM   7184  C  C   . ILE A 1 888  ? 91.541  96.342  74.680  1.00 69.84  ? 888  ILE A C   1 
ATOM   7185  O  O   . ILE A 1 888  ? 91.172  97.062  73.743  1.00 83.83  ? 888  ILE A O   1 
ATOM   7186  C  CB  . ILE A 1 888  ? 91.800  97.308  76.993  1.00 53.22  ? 888  ILE A CB  1 
ATOM   7187  C  CG1 . ILE A 1 888  ? 91.230  97.360  78.409  1.00 57.62  ? 888  ILE A CG1 1 
ATOM   7188  C  CG2 . ILE A 1 888  ? 91.952  98.721  76.444  1.00 55.66  ? 888  ILE A CG2 1 
ATOM   7189  C  CD1 . ILE A 1 888  ? 92.047  98.221  79.352  1.00 56.45  ? 888  ILE A CD1 1 
ATOM   7190  N  N   . ASP A 1 889  ? 92.506  95.430  74.531  1.00 74.27  ? 889  ASP A N   1 
ATOM   7191  C  CA  . ASP A 1 889  ? 93.240  95.336  73.270  1.00 67.92  ? 889  ASP A CA  1 
ATOM   7192  C  C   . ASP A 1 889  ? 92.340  94.896  72.121  1.00 76.25  ? 889  ASP A C   1 
ATOM   7193  O  O   . ASP A 1 889  ? 92.506  95.362  70.993  1.00 87.55  ? 889  ASP A O   1 
ATOM   7194  C  CB  . ASP A 1 889  ? 94.440  94.398  73.411  1.00 76.62  ? 889  ASP A CB  1 
ATOM   7195  C  CG  . ASP A 1 889  ? 94.042  92.968  73.709  1.00 99.63  ? 889  ASP A CG  1 
ATOM   7196  O  OD1 . ASP A 1 889  ? 92.850  92.715  73.978  1.00 99.06  ? 889  ASP A OD1 1 
ATOM   7197  O  OD2 . ASP A 1 889  ? 94.926  92.086  73.667  1.00 102.96 ? 889  ASP A OD2 1 
ATOM   7198  N  N   . ILE A 1 890  ? 91.403  93.981  72.371  1.00 81.00  ? 890  ILE A N   1 
ATOM   7199  C  CA  . ILE A 1 890  ? 90.489  93.579  71.306  1.00 82.33  ? 890  ILE A CA  1 
ATOM   7200  C  C   . ILE A 1 890  ? 89.544  94.721  70.949  1.00 85.57  ? 890  ILE A C   1 
ATOM   7201  O  O   . ILE A 1 890  ? 89.223  94.934  69.774  1.00 93.09  ? 890  ILE A O   1 
ATOM   7202  C  CB  . ILE A 1 890  ? 89.714  92.310  71.708  1.00 83.05  ? 890  ILE A CB  1 
ATOM   7203  C  CG1 . ILE A 1 890  ? 90.579  91.064  71.519  1.00 97.22  ? 890  ILE A CG1 1 
ATOM   7204  C  CG2 . ILE A 1 890  ? 88.420  92.182  70.907  1.00 79.87  ? 890  ILE A CG2 1 
ATOM   7205  C  CD1 . ILE A 1 890  ? 89.945  89.801  72.063  1.00 97.68  ? 890  ILE A CD1 1 
ATOM   7206  N  N   . SER A 1 891  ? 89.075  95.465  71.939  1.00 79.48  ? 891  SER A N   1 
ATOM   7207  C  CA  . SER A 1 891  ? 88.228  96.595  71.607  1.00 83.49  ? 891  SER A CA  1 
ATOM   7208  C  C   . SER A 1 891  ? 89.018  97.645  70.821  1.00 92.25  ? 891  SER A C   1 
ATOM   7209  O  O   . SER A 1 891  ? 88.539  98.170  69.819  1.00 102.37 ? 891  SER A O   1 
ATOM   7210  C  CB  . SER A 1 891  ? 87.664  97.230  72.870  1.00 76.40  ? 891  SER A CB  1 
ATOM   7211  O  OG  . SER A 1 891  ? 88.605  98.116  73.442  1.00 84.68  ? 891  SER A OG  1 
ATOM   7212  N  N   . CYS A 1 892  ? 90.227  97.951  71.290  1.00 88.68  ? 892  CYS A N   1 
ATOM   7213  C  CA  . CYS A 1 892  ? 91.094  98.948  70.649  1.00 84.57  ? 892  CYS A CA  1 
ATOM   7214  C  C   . CYS A 1 892  ? 91.697  98.664  69.266  1.00 92.73  ? 892  CYS A C   1 
ATOM   7215  O  O   . CYS A 1 892  ? 91.668  99.525  68.393  1.00 96.06  ? 892  CYS A O   1 
ATOM   7216  C  CB  . CYS A 1 892  ? 92.228  99.343  71.599  1.00 69.78  ? 892  CYS A CB  1 
ATOM   7217  S  SG  . CYS A 1 892  ? 91.808  100.615 72.805  1.00 76.50  ? 892  CYS A SG  1 
ATOM   7218  N  N   . PHE A 1 893  ? 92.241  97.466  69.065  1.00 97.47  ? 893  PHE A N   1 
ATOM   7219  C  CA  . PHE A 1 893  ? 92.879  97.134  67.789  1.00 90.31  ? 893  PHE A CA  1 
ATOM   7220  C  C   . PHE A 1 893  ? 92.229  95.984  67.037  1.00 100.47 ? 893  PHE A C   1 
ATOM   7221  O  O   . PHE A 1 893  ? 92.686  95.633  65.948  1.00 103.68 ? 893  PHE A O   1 
ATOM   7222  C  CB  . PHE A 1 893  ? 94.357  96.800  68.003  1.00 96.13  ? 893  PHE A CB  1 
ATOM   7223  C  CG  . PHE A 1 893  ? 95.039  97.667  69.020  1.00 97.22  ? 893  PHE A CG  1 
ATOM   7224  C  CD1 . PHE A 1 893  ? 95.231  97.215  70.311  1.00 99.57  ? 893  PHE A CD1 1 
ATOM   7225  C  CD2 . PHE A 1 893  ? 95.492  98.927  68.686  1.00 99.87  ? 893  PHE A CD2 1 
ATOM   7226  C  CE1 . PHE A 1 893  ? 95.857  98.004  71.252  1.00 84.86  ? 893  PHE A CE1 1 
ATOM   7227  C  CE2 . PHE A 1 893  ? 96.119  99.721  69.621  1.00 87.67  ? 893  PHE A CE2 1 
ATOM   7228  C  CZ  . PHE A 1 893  ? 96.302  99.259  70.907  1.00 71.68  ? 893  PHE A CZ  1 
ATOM   7229  N  N   . LYS A 1 894  ? 91.239  95.363  67.680  1.00 96.90  ? 894  LYS A N   1 
ATOM   7230  C  CA  . LYS A 1 894  ? 90.441  94.223  67.185  1.00 98.94  ? 894  LYS A CA  1 
ATOM   7231  C  C   . LYS A 1 894  ? 91.182  92.874  67.144  1.00 104.60 ? 894  LYS A C   1 
ATOM   7232  O  O   . LYS A 1 894  ? 90.683  91.904  66.575  1.00 104.42 ? 894  LYS A O   1 
ATOM   7233  C  CB  . LYS A 1 894  ? 89.689  94.519  65.872  1.00 100.91 ? 894  LYS A CB  1 
ATOM   7234  C  CG  . LYS A 1 894  ? 89.056  95.900  65.822  1.00 113.37 ? 894  LYS A CG  1 
ATOM   7235  C  CD  . LYS A 1 894  ? 88.325  96.130  64.511  1.00 124.76 ? 894  LYS A CD  1 
ATOM   7236  C  CE  . LYS A 1 894  ? 87.100  95.236  64.393  1.00 126.80 ? 894  LYS A CE  1 
ATOM   7237  N  NZ  . LYS A 1 894  ? 86.084  95.538  65.438  1.00 113.42 ? 894  LYS A NZ  1 
ATOM   7238  N  N   . LYS A 1 895  ? 92.367  92.824  67.747  1.00 107.63 ? 895  LYS A N   1 
ATOM   7239  C  CA  . LYS A 1 895  ? 93.159  91.600  67.825  1.00 107.29 ? 895  LYS A CA  1 
ATOM   7240  C  C   . LYS A 1 895  ? 94.074  91.665  69.042  1.00 104.71 ? 895  LYS A C   1 
ATOM   7241  O  O   . LYS A 1 895  ? 94.465  92.748  69.467  1.00 105.96 ? 895  LYS A O   1 
ATOM   7242  C  CB  . LYS A 1 895  ? 93.972  91.388  66.549  1.00 114.35 ? 895  LYS A CB  1 
ATOM   7243  C  CG  . LYS A 1 895  ? 94.863  92.557  66.170  1.00 115.55 ? 895  LYS A CG  1 
ATOM   7244  C  CD  . LYS A 1 895  ? 95.701  92.226  64.946  1.00 122.86 ? 895  LYS A CD  1 
ATOM   7245  C  CE  . LYS A 1 895  ? 96.408  93.459  64.411  1.00 124.23 ? 895  LYS A CE  1 
ATOM   7246  N  NZ  . LYS A 1 895  ? 97.218  94.148  65.454  1.00 123.31 ? 895  LYS A NZ  1 
ATOM   7247  N  N   . PRO A 1 896  ? 94.441  90.502  69.592  1.00 95.42  ? 896  PRO A N   1 
ATOM   7248  C  CA  . PRO A 1 896  ? 95.311  90.436  70.771  1.00 95.42  ? 896  PRO A CA  1 
ATOM   7249  C  C   . PRO A 1 896  ? 96.736  90.919  70.508  1.00 97.46  ? 896  PRO A C   1 
ATOM   7250  O  O   . PRO A 1 896  ? 97.275  90.685  69.431  1.00 108.26 ? 896  PRO A O   1 
ATOM   7251  C  CB  . PRO A 1 896  ? 95.312  88.946  71.122  1.00 88.45  ? 896  PRO A CB  1 
ATOM   7252  C  CG  . PRO A 1 896  ? 94.963  88.256  69.850  1.00 98.62  ? 896  PRO A CG  1 
ATOM   7253  C  CD  . PRO A 1 896  ? 94.008  89.169  69.145  1.00 94.05  ? 896  PRO A CD  1 
ATOM   7254  N  N   . LEU A 1 897  ? 97.327  91.590  71.493  1.00 88.10  ? 897  LEU A N   1 
ATOM   7255  C  CA  . LEU A 1 897  ? 98.692  92.098  71.393  1.00 90.85  ? 897  LEU A CA  1 
ATOM   7256  C  C   . LEU A 1 897  ? 99.712  90.968  71.414  1.00 94.92  ? 897  LEU A C   1 
ATOM   7257  O  O   . LEU A 1 897  ? 99.469  89.916  72.000  1.00 108.55 ? 897  LEU A O   1 
ATOM   7258  C  CB  . LEU A 1 897  ? 98.997  93.049  72.550  1.00 79.24  ? 897  LEU A CB  1 
ATOM   7259  C  CG  . LEU A 1 897  ? 98.406  94.455  72.528  1.00 76.26  ? 897  LEU A CG  1 
ATOM   7260  C  CD1 . LEU A 1 897  ? 98.770  95.198  73.803  1.00 63.31  ? 897  LEU A CD1 1 
ATOM   7261  C  CD2 . LEU A 1 897  ? 98.901  95.211  71.309  1.00 94.14  ? 897  LEU A CD2 1 
ATOM   7262  N  N   . THR A 1 898  ? 100.848 91.187  70.761  1.00 87.25  ? 898  THR A N   1 
ATOM   7263  C  CA  . THR A 1 898  ? 101.914 90.203  70.731  1.00 85.36  ? 898  THR A CA  1 
ATOM   7264  C  C   . THR A 1 898  ? 103.007 90.642  71.700  1.00 85.14  ? 898  THR A C   1 
ATOM   7265  O  O   . THR A 1 898  ? 102.979 91.745  72.248  1.00 87.51  ? 898  THR A O   1 
ATOM   7266  C  CB  . THR A 1 898  ? 102.472 90.044  69.314  1.00 98.62  ? 898  THR A CB  1 
ATOM   7267  O  OG1 . THR A 1 898  ? 102.765 91.339  68.772  1.00 107.76 ? 898  THR A OG1 1 
ATOM   7268  C  CG2 . THR A 1 898  ? 101.458 89.350  68.421  1.00 98.88  ? 898  THR A CG2 1 
ATOM   7269  N  N   . PHE A 1 899  ? 103.972 89.750  71.903  1.00 78.02  ? 899  PHE A N   1 
ATOM   7270  C  CA  . PHE A 1 899  ? 105.079 90.035  72.809  1.00 70.51  ? 899  PHE A CA  1 
ATOM   7271  C  C   . PHE A 1 899  ? 105.940 91.200  72.327  1.00 81.73  ? 899  PHE A C   1 
ATOM   7272  O  O   . PHE A 1 899  ? 106.356 92.051  73.127  1.00 82.55  ? 899  PHE A O   1 
ATOM   7273  C  CB  . PHE A 1 899  ? 105.927 88.783  73.002  1.00 64.96  ? 899  PHE A CB  1 
ATOM   7274  C  CG  . PHE A 1 899  ? 107.067 88.979  73.941  1.00 71.89  ? 899  PHE A CG  1 
ATOM   7275  C  CD1 . PHE A 1 899  ? 106.863 89.015  75.308  1.00 75.56  ? 899  PHE A CD1 1 
ATOM   7276  C  CD2 . PHE A 1 899  ? 108.352 89.128  73.453  1.00 87.49  ? 899  PHE A CD2 1 
ATOM   7277  C  CE1 . PHE A 1 899  ? 107.923 89.208  76.172  1.00 77.70  ? 899  PHE A CE1 1 
ATOM   7278  C  CE2 . PHE A 1 899  ? 109.414 89.314  74.311  1.00 79.59  ? 899  PHE A CE2 1 
ATOM   7279  C  CZ  . PHE A 1 899  ? 109.201 89.354  75.671  1.00 71.42  ? 899  PHE A CZ  1 
ATOM   7280  N  N   . SER A 1 900  ? 106.205 91.264  71.020  1.00 80.02  ? 900  SER A N   1 
ATOM   7281  C  CA  . SER A 1 900  ? 107.100 92.289  70.491  1.00 68.41  ? 900  SER A CA  1 
ATOM   7282  C  C   . SER A 1 900  ? 106.528 93.689  70.671  1.00 76.64  ? 900  SER A C   1 
ATOM   7283  O  O   . SER A 1 900  ? 107.270 94.633  70.968  1.00 86.62  ? 900  SER A O   1 
ATOM   7284  C  CB  . SER A 1 900  ? 107.381 92.019  69.014  1.00 76.83  ? 900  SER A CB  1 
ATOM   7285  O  OG  . SER A 1 900  ? 106.264 92.366  68.213  1.00 87.76  ? 900  SER A OG  1 
ATOM   7286  N  N   . GLU A 1 901  ? 105.218 93.848  70.485  1.00 76.91  ? 901  GLU A N   1 
ATOM   7287  C  CA  . GLU A 1 901  ? 104.604 95.160  70.653  1.00 75.26  ? 901  GLU A CA  1 
ATOM   7288  C  C   . GLU A 1 901  ? 104.713 95.654  72.093  1.00 69.68  ? 901  GLU A C   1 
ATOM   7289  O  O   . GLU A 1 901  ? 105.057 96.820  72.330  1.00 71.55  ? 901  GLU A O   1 
ATOM   7290  C  CB  . GLU A 1 901  ? 103.147 95.099  70.203  1.00 84.90  ? 901  GLU A CB  1 
ATOM   7291  C  CG  . GLU A 1 901  ? 102.997 94.620  68.770  1.00 99.28  ? 901  GLU A CG  1 
ATOM   7292  C  CD  . GLU A 1 901  ? 101.556 94.556  68.323  1.00 120.20 ? 901  GLU A CD  1 
ATOM   7293  O  OE1 . GLU A 1 901  ? 100.938 95.628  68.159  1.00 123.53 ? 901  GLU A OE1 1 
ATOM   7294  O  OE2 . GLU A 1 901  ? 101.042 93.433  68.136  1.00 114.31 ? 901  GLU A OE2 1 
ATOM   7295  N  N   . LYS A 1 902  ? 104.445 94.780  73.068  1.00 75.54  ? 902  LYS A N   1 
ATOM   7296  C  CA  . LYS A 1 902  ? 104.605 95.178  74.464  1.00 64.30  ? 902  LYS A CA  1 
ATOM   7297  C  C   . LYS A 1 902  ? 106.054 95.512  74.773  1.00 62.61  ? 902  LYS A C   1 
ATOM   7298  O  O   . LYS A 1 902  ? 106.338 96.474  75.499  1.00 65.07  ? 902  LYS A O   1 
ATOM   7299  C  CB  . LYS A 1 902  ? 104.125 94.073  75.406  1.00 62.99  ? 902  LYS A CB  1 
ATOM   7300  C  CG  . LYS A 1 902  ? 102.680 93.667  75.263  1.00 59.77  ? 902  LYS A CG  1 
ATOM   7301  C  CD  . LYS A 1 902  ? 102.436 92.421  76.093  1.00 59.65  ? 902  LYS A CD  1 
ATOM   7302  C  CE  . LYS A 1 902  ? 100.985 91.995  76.063  1.00 62.99  ? 902  LYS A CE  1 
ATOM   7303  N  NZ  . LYS A 1 902  ? 100.878 90.514  75.969  1.00 68.58  ? 902  LYS A NZ  1 
ATOM   7304  N  N   . LEU A 1 903  ? 106.986 94.728  74.229  1.00 65.61  ? 903  LEU A N   1 
ATOM   7305  C  CA  . LEU A 1 903  ? 108.399 95.016  74.448  1.00 65.20  ? 903  LEU A CA  1 
ATOM   7306  C  C   . LEU A 1 903  ? 108.764 96.398  73.922  1.00 70.96  ? 903  LEU A C   1 
ATOM   7307  O  O   . LEU A 1 903  ? 109.388 97.201  74.627  1.00 76.23  ? 903  LEU A O   1 
ATOM   7308  C  CB  . LEU A 1 903  ? 109.242 93.935  73.773  1.00 59.84  ? 903  LEU A CB  1 
ATOM   7309  C  CG  . LEU A 1 903  ? 110.703 93.775  74.174  1.00 53.89  ? 903  LEU A CG  1 
ATOM   7310  C  CD1 . LEU A 1 903  ? 111.107 92.323  74.073  1.00 71.81  ? 903  LEU A CD1 1 
ATOM   7311  C  CD2 . LEU A 1 903  ? 111.565 94.618  73.247  1.00 70.11  ? 903  LEU A CD2 1 
ATOM   7312  N  N   . ILE A 1 904  ? 108.344 96.706  72.692  1.00 68.99  ? 904  ILE A N   1 
ATOM   7313  C  CA  . ILE A 1 904  ? 108.688 97.990  72.088  1.00 59.91  ? 904  ILE A CA  1 
ATOM   7314  C  C   . ILE A 1 904  ? 108.044 99.135  72.859  1.00 64.43  ? 904  ILE A C   1 
ATOM   7315  O  O   . ILE A 1 904  ? 108.647 100.206 73.013  1.00 68.06  ? 904  ILE A O   1 
ATOM   7316  C  CB  . ILE A 1 904  ? 108.304 98.000  70.597  1.00 63.57  ? 904  ILE A CB  1 
ATOM   7317  C  CG1 . ILE A 1 904  ? 109.334 97.207  69.792  1.00 63.58  ? 904  ILE A CG1 1 
ATOM   7318  C  CG2 . ILE A 1 904  ? 108.218 99.425  70.064  1.00 56.42  ? 904  ILE A CG2 1 
ATOM   7319  C  CD1 . ILE A 1 904  ? 109.060 97.172  68.307  1.00 88.63  ? 904  ILE A CD1 1 
ATOM   7320  N  N   . ALA A 1 905  ? 106.834 98.927  73.386  1.00 71.67  ? 905  ALA A N   1 
ATOM   7321  C  CA  . ALA A 1 905  ? 106.226 99.952  74.232  1.00 62.76  ? 905  ALA A CA  1 
ATOM   7322  C  C   . ALA A 1 905  ? 107.039 100.166 75.503  1.00 54.47  ? 905  ALA A C   1 
ATOM   7323  O  O   . ALA A 1 905  ? 107.239 101.308 75.935  1.00 54.84  ? 905  ALA A O   1 
ATOM   7324  C  CB  . ALA A 1 905  ? 104.783 99.568  74.569  1.00 63.64  ? 905  ALA A CB  1 
ATOM   7325  N  N   . LEU A 1 906  ? 107.527 99.083  76.109  1.00 60.76  ? 906  LEU A N   1 
ATOM   7326  C  CA  . LEU A 1 906  ? 108.300 99.182  77.343  1.00 50.09  ? 906  LEU A CA  1 
ATOM   7327  C  C   . LEU A 1 906  ? 109.727 99.671  77.125  1.00 66.91  ? 906  LEU A C   1 
ATOM   7328  O  O   . LEU A 1 906  ? 110.409 99.991  78.102  1.00 70.51  ? 906  LEU A O   1 
ATOM   7329  C  CB  . LEU A 1 906  ? 108.336 97.833  78.058  1.00 47.23  ? 906  LEU A CB  1 
ATOM   7330  C  CG  . LEU A 1 906  ? 107.061 97.443  78.800  1.00 39.64  ? 906  LEU A CG  1 
ATOM   7331  C  CD1 . LEU A 1 906  ? 107.006 95.939  79.010  1.00 47.87  ? 906  LEU A CD1 1 
ATOM   7332  C  CD2 . LEU A 1 906  ? 106.982 98.186  80.130  1.00 49.19  ? 906  LEU A CD2 1 
ATOM   7333  N  N   . ILE A 1 907  ? 110.186 99.747  75.880  1.00 66.85  ? 907  ILE A N   1 
ATOM   7334  C  CA  . ILE A 1 907  ? 111.499 100.314 75.595  1.00 56.37  ? 907  ILE A CA  1 
ATOM   7335  C  C   . ILE A 1 907  ? 111.460 101.839 75.405  1.00 68.00  ? 907  ILE A C   1 
ATOM   7336  O  O   . ILE A 1 907  ? 112.409 102.516 75.799  1.00 64.73  ? 907  ILE A O   1 
ATOM   7337  C  CB  . ILE A 1 907  ? 112.100 99.639  74.354  1.00 56.77  ? 907  ILE A CB  1 
ATOM   7338  C  CG1 . ILE A 1 907  ? 112.258 98.147  74.584  1.00 64.69  ? 907  ILE A CG1 1 
ATOM   7339  C  CG2 . ILE A 1 907  ? 113.445 100.243 73.999  1.00 57.07  ? 907  ILE A CG2 1 
ATOM   7340  C  CD1 . ILE A 1 907  ? 113.166 97.821  75.745  1.00 97.82  ? 907  ILE A CD1 1 
ATOM   7341  N  N   . THR A 1 908  ? 110.377 102.393 74.854  1.00 75.71  ? 908  THR A N   1 
ATOM   7342  C  CA  . THR A 1 908  ? 110.342 103.797 74.503  1.00 64.88  ? 908  THR A CA  1 
ATOM   7343  C  C   . THR A 1 908  ? 110.287 104.686 75.743  1.00 67.53  ? 908  THR A C   1 
ATOM   7344  O  O   . THR A 1 908  ? 109.427 104.493 76.623  1.00 82.39  ? 908  THR A O   1 
ATOM   7345  C  CB  . THR A 1 908  ? 109.152 104.097 73.611  1.00 57.96  ? 908  THR A CB  1 
ATOM   7346  O  OG1 . THR A 1 908  ? 109.154 103.151 72.524  1.00 56.85  ? 908  THR A OG1 1 
ATOM   7347  C  CG2 . THR A 1 908  ? 109.252 105.503 73.086  1.00 62.14  ? 908  THR A CG2 1 
ATOM   7348  N  N   . PRO A 1 909  ? 111.191 105.648 75.875  1.00 46.04  ? 909  PRO A N   1 
ATOM   7349  C  CA  . PRO A 1 909  ? 111.195 106.509 77.072  1.00 47.65  ? 909  PRO A CA  1 
ATOM   7350  C  C   . PRO A 1 909  ? 109.921 107.328 77.175  1.00 55.48  ? 909  PRO A C   1 
ATOM   7351  O  O   . PRO A 1 909  ? 109.230 107.572 76.183  1.00 67.69  ? 909  PRO A O   1 
ATOM   7352  C  CB  . PRO A 1 909  ? 112.442 107.398 76.863  1.00 53.22  ? 909  PRO A CB  1 
ATOM   7353  C  CG  . PRO A 1 909  ? 113.331 106.654 75.912  1.00 53.52  ? 909  PRO A CG  1 
ATOM   7354  C  CD  . PRO A 1 909  ? 112.370 105.876 75.017  1.00 64.09  ? 909  PRO A CD  1 
ATOM   7355  N  N   . GLN A 1 910  ? 109.619 107.757 78.388  1.00 57.73  ? 910  GLN A N   1 
ATOM   7356  C  CA  . GLN A 1 910  ? 108.359 108.418 78.655  1.00 60.52  ? 910  GLN A CA  1 
ATOM   7357  C  C   . GLN A 1 910  ? 108.260 109.782 77.981  1.00 62.24  ? 910  GLN A C   1 
ATOM   7358  O  O   . GLN A 1 910  ? 107.167 110.197 77.579  1.00 72.65  ? 910  GLN A O   1 
ATOM   7359  C  CB  . GLN A 1 910  ? 108.157 108.571 80.163  1.00 74.21  ? 910  GLN A CB  1 
ATOM   7360  C  CG  . GLN A 1 910  ? 106.772 109.025 80.553  1.00 74.88  ? 910  GLN A CG  1 
ATOM   7361  C  CD  . GLN A 1 910  ? 106.753 110.495 80.896  1.00 80.14  ? 910  GLN A CD  1 
ATOM   7362  O  OE1 . GLN A 1 910  ? 107.787 111.155 80.870  1.00 77.31  ? 910  GLN A OE1 1 
ATOM   7363  N  NE2 . GLN A 1 910  ? 105.573 111.019 81.209  1.00 88.08  ? 910  GLN A NE2 1 
ATOM   7364  N  N   . VAL A 1 911  ? 109.380 110.489 77.842  1.00 64.69  ? 911  VAL A N   1 
ATOM   7365  C  CA  . VAL A 1 911  ? 109.356 111.799 77.191  1.00 62.43  ? 911  VAL A CA  1 
ATOM   7366  C  C   . VAL A 1 911  ? 108.902 111.689 75.738  1.00 60.17  ? 911  VAL A C   1 
ATOM   7367  O  O   . VAL A 1 911  ? 108.324 112.633 75.184  1.00 64.62  ? 911  VAL A O   1 
ATOM   7368  C  CB  . VAL A 1 911  ? 110.743 112.476 77.288  1.00 64.78  ? 911  VAL A CB  1 
ATOM   7369  C  CG1 . VAL A 1 911  ? 111.797 111.644 76.563  1.00 67.73  ? 911  VAL A CG1 1 
ATOM   7370  C  CG2 . VAL A 1 911  ? 110.699 113.890 76.724  1.00 56.07  ? 911  VAL A CG2 1 
ATOM   7371  N  N   . LEU A 1 912  ? 109.110 110.534 75.111  1.00 65.62  ? 912  LEU A N   1 
ATOM   7372  C  CA  . LEU A 1 912  ? 108.704 110.330 73.728  1.00 58.14  ? 912  LEU A CA  1 
ATOM   7373  C  C   . LEU A 1 912  ? 107.331 109.695 73.587  1.00 66.19  ? 912  LEU A C   1 
ATOM   7374  O  O   . LEU A 1 912  ? 106.901 109.427 72.460  1.00 69.66  ? 912  LEU A O   1 
ATOM   7375  C  CB  . LEU A 1 912  ? 109.737 109.467 72.998  1.00 53.30  ? 912  LEU A CB  1 
ATOM   7376  C  CG  . LEU A 1 912  ? 111.096 110.126 72.771  1.00 72.92  ? 912  LEU A CG  1 
ATOM   7377  C  CD1 . LEU A 1 912  ? 112.181 109.071 72.624  1.00 56.92  ? 912  LEU A CD1 1 
ATOM   7378  C  CD2 . LEU A 1 912  ? 111.041 111.031 71.549  1.00 84.64  ? 912  LEU A CD2 1 
ATOM   7379  N  N   . GLY A 1 913  ? 106.633 109.445 74.686  1.00 67.91  ? 913  GLY A N   1 
ATOM   7380  C  CA  . GLY A 1 913  ? 105.303 108.891 74.597  1.00 73.90  ? 913  GLY A CA  1 
ATOM   7381  C  C   . GLY A 1 913  ? 105.280 107.389 74.712  1.00 72.91  ? 913  GLY A C   1 
ATOM   7382  O  O   . GLY A 1 913  ? 104.442 106.739 74.080  1.00 68.76  ? 913  GLY A O   1 
ATOM   7383  N  N   . GLY A 1 914  ? 106.179 106.816 75.504  1.00 72.25  ? 914  GLY A N   1 
ATOM   7384  C  CA  . GLY A 1 914  ? 106.268 105.379 75.646  1.00 62.16  ? 914  GLY A CA  1 
ATOM   7385  C  C   . GLY A 1 914  ? 106.011 105.008 77.088  1.00 73.49  ? 914  GLY A C   1 
ATOM   7386  O  O   . GLY A 1 914  ? 105.369 105.774 77.811  1.00 73.00  ? 914  GLY A O   1 
ATOM   7387  N  N   . LEU A 1 915  ? 106.502 103.852 77.529  1.00 56.56  ? 915  LEU A N   1 
ATOM   7388  C  CA  . LEU A 1 915  ? 106.208 103.404 78.883  1.00 51.75  ? 915  LEU A CA  1 
ATOM   7389  C  C   . LEU A 1 915  ? 107.462 102.986 79.637  1.00 53.30  ? 915  LEU A C   1 
ATOM   7390  O  O   . LEU A 1 915  ? 107.394 102.146 80.538  1.00 63.59  ? 915  LEU A O   1 
ATOM   7391  C  CB  . LEU A 1 915  ? 105.209 102.248 78.855  1.00 62.53  ? 915  LEU A CB  1 
ATOM   7392  C  CG  . LEU A 1 915  ? 103.757 102.612 78.572  1.00 44.08  ? 915  LEU A CG  1 
ATOM   7393  C  CD1 . LEU A 1 915  ? 102.964 101.348 78.297  1.00 54.05  ? 915  LEU A CD1 1 
ATOM   7394  C  CD2 . LEU A 1 915  ? 103.175 103.378 79.750  1.00 51.33  ? 915  LEU A CD2 1 
ATOM   7395  N  N   . SER A 1 916  ? 108.611 103.568 79.314  1.00 54.72  ? 916  SER A N   1 
ATOM   7396  C  CA  . SER A 1 916  ? 109.853 103.197 79.977  1.00 60.55  ? 916  SER A CA  1 
ATOM   7397  C  C   . SER A 1 916  ? 110.152 104.205 81.077  1.00 63.67  ? 916  SER A C   1 
ATOM   7398  O  O   . SER A 1 916  ? 110.378 105.389 80.802  1.00 64.81  ? 916  SER A O   1 
ATOM   7399  C  CB  . SER A 1 916  ? 111.013 103.125 78.985  1.00 54.53  ? 916  SER A CB  1 
ATOM   7400  O  OG  . SER A 1 916  ? 112.240 102.912 79.661  1.00 62.89  ? 916  SER A OG  1 
ATOM   7401  N  N   . PHE A 1 917  ? 110.160 103.721 82.317  1.00 67.43  ? 917  PHE A N   1 
ATOM   7402  C  CA  . PHE A 1 917  ? 110.447 104.536 83.493  1.00 63.00  ? 917  PHE A CA  1 
ATOM   7403  C  C   . PHE A 1 917  ? 111.683 104.036 84.218  1.00 74.80  ? 917  PHE A C   1 
ATOM   7404  O  O   . PHE A 1 917  ? 111.993 104.524 85.311  1.00 81.60  ? 917  PHE A O   1 
ATOM   7405  C  CB  . PHE A 1 917  ? 109.249 104.549 84.446  1.00 62.07  ? 917  PHE A CB  1 
ATOM   7406  C  CG  . PHE A 1 917  ? 108.068 105.301 83.922  1.00 76.54  ? 917  PHE A CG  1 
ATOM   7407  C  CD1 . PHE A 1 917  ? 107.136 104.682 83.107  1.00 62.12  ? 917  PHE A CD1 1 
ATOM   7408  C  CD2 . PHE A 1 917  ? 107.885 106.634 84.251  1.00 76.60  ? 917  PHE A CD2 1 
ATOM   7409  C  CE1 . PHE A 1 917  ? 106.044 105.380 82.626  1.00 61.70  ? 917  PHE A CE1 1 
ATOM   7410  C  CE2 . PHE A 1 917  ? 106.795 107.337 83.775  1.00 69.06  ? 917  PHE A CE2 1 
ATOM   7411  C  CZ  . PHE A 1 917  ? 105.873 106.709 82.962  1.00 69.29  ? 917  PHE A CZ  1 
ATOM   7412  N  N   . LEU A 1 918  ? 112.405 103.092 83.623  1.00 67.98  ? 918  LEU A N   1 
ATOM   7413  C  CA  . LEU A 1 918  ? 113.621 102.559 84.210  1.00 56.99  ? 918  LEU A CA  1 
ATOM   7414  C  C   . LEU A 1 918  ? 114.758 102.975 83.293  1.00 60.12  ? 918  LEU A C   1 
ATOM   7415  O  O   . LEU A 1 918  ? 115.203 102.225 82.433  1.00 56.85  ? 918  LEU A O   1 
ATOM   7416  C  CB  . LEU A 1 918  ? 113.504 101.055 84.284  1.00 60.10  ? 918  LEU A CB  1 
ATOM   7417  C  CG  . LEU A 1 918  ? 112.326 100.449 85.045  1.00 55.06  ? 918  LEU A CG  1 
ATOM   7418  C  CD1 . LEU A 1 918  ? 112.186 98.994  84.611  1.00 59.03  ? 918  LEU A CD1 1 
ATOM   7419  C  CD2 . LEU A 1 918  ? 112.465 100.570 86.558  1.00 51.68  ? 918  LEU A CD2 1 
ATOM   7420  N  N   . ASN A 1 919  ? 115.237 104.195 83.498  1.00 66.40  ? 919  ASN A N   1 
ATOM   7421  C  CA  . ASN A 1 919  ? 116.349 104.673 82.703  1.00 70.19  ? 919  ASN A CA  1 
ATOM   7422  C  C   . ASN A 1 919  ? 117.647 104.166 83.313  1.00 66.75  ? 919  ASN A C   1 
ATOM   7423  O  O   . ASN A 1 919  ? 117.897 104.412 84.502  1.00 69.81  ? 919  ASN A O   1 
ATOM   7424  C  CB  . ASN A 1 919  ? 116.337 106.201 82.638  1.00 78.17  ? 919  ASN A CB  1 
ATOM   7425  C  CG  . ASN A 1 919  ? 117.231 106.749 81.541  1.00 72.19  ? 919  ASN A CG  1 
ATOM   7426  O  OD1 . ASN A 1 919  ? 117.774 105.996 80.733  1.00 69.96  ? 919  ASN A OD1 1 
ATOM   7427  N  ND2 . ASN A 1 919  ? 117.376 108.068 81.496  1.00 71.61  ? 919  ASN A ND2 1 
ATOM   7428  N  N   . PRO A 1 920  ? 118.489 103.449 82.561  1.00 61.39  ? 920  PRO A N   1 
ATOM   7429  C  CA  . PRO A 1 920  ? 119.750 102.973 83.154  1.00 55.81  ? 920  PRO A CA  1 
ATOM   7430  C  C   . PRO A 1 920  ? 120.642 104.097 83.647  1.00 56.93  ? 920  PRO A C   1 
ATOM   7431  O  O   . PRO A 1 920  ? 121.414 103.889 84.590  1.00 62.71  ? 920  PRO A O   1 
ATOM   7432  C  CB  . PRO A 1 920  ? 120.396 102.188 82.001  1.00 69.26  ? 920  PRO A CB  1 
ATOM   7433  C  CG  . PRO A 1 920  ? 119.242 101.786 81.132  1.00 67.62  ? 920  PRO A CG  1 
ATOM   7434  C  CD  . PRO A 1 920  ? 118.300 102.951 81.192  1.00 67.50  ? 920  PRO A CD  1 
ATOM   7435  N  N   . GLU A 1 921  ? 120.568 105.279 83.035  1.00 70.05  ? 921  GLU A N   1 
ATOM   7436  C  CA  . GLU A 1 921  ? 121.396 106.391 83.484  1.00 61.19  ? 921  GLU A CA  1 
ATOM   7437  C  C   . GLU A 1 921  ? 121.077 106.804 84.917  1.00 60.03  ? 921  GLU A C   1 
ATOM   7438  O  O   . GLU A 1 921  ? 121.924 107.409 85.582  1.00 73.19  ? 921  GLU A O   1 
ATOM   7439  C  CB  . GLU A 1 921  ? 121.229 107.584 82.538  1.00 61.86  ? 921  GLU A CB  1 
ATOM   7440  C  CG  . GLU A 1 921  ? 121.977 108.828 82.979  1.00 76.86  ? 921  GLU A CG  1 
ATOM   7441  C  CD  . GLU A 1 921  ? 122.360 109.720 81.827  1.00 97.33  ? 921  GLU A CD  1 
ATOM   7442  O  OE1 . GLU A 1 921  ? 122.008 109.387 80.678  1.00 99.39  ? 921  GLU A OE1 1 
ATOM   7443  O  OE2 . GLU A 1 921  ? 123.023 110.750 82.071  1.00 86.63  ? 921  GLU A OE2 1 
ATOM   7444  N  N   . LYS A 1 922  ? 119.907 106.433 85.435  1.00 60.88  ? 922  LYS A N   1 
ATOM   7445  C  CA  . LYS A 1 922  ? 119.554 106.757 86.811  1.00 66.00  ? 922  LYS A CA  1 
ATOM   7446  C  C   . LYS A 1 922  ? 120.259 105.879 87.833  1.00 68.97  ? 922  LYS A C   1 
ATOM   7447  O  O   . LYS A 1 922  ? 120.122 106.129 89.035  1.00 71.86  ? 922  LYS A O   1 
ATOM   7448  C  CB  . LYS A 1 922  ? 118.043 106.675 87.020  1.00 72.01  ? 922  LYS A CB  1 
ATOM   7449  C  CG  . LYS A 1 922  ? 117.324 107.952 86.647  1.00 72.55  ? 922  LYS A CG  1 
ATOM   7450  C  CD  . LYS A 1 922  ? 115.825 107.775 86.654  1.00 80.27  ? 922  LYS A CD  1 
ATOM   7451  C  CE  . LYS A 1 922  ? 115.156 109.051 86.199  1.00 94.29  ? 922  LYS A CE  1 
ATOM   7452  N  NZ  . LYS A 1 922  ? 115.561 110.186 87.072  1.00 75.20  ? 922  LYS A NZ  1 
ATOM   7453  N  N   . LEU A 1 923  ? 121.015 104.874 87.394  1.00 68.92  ? 923  LEU A N   1 
ATOM   7454  C  CA  . LEU A 1 923  ? 121.907 104.179 88.309  1.00 62.09  ? 923  LEU A CA  1 
ATOM   7455  C  C   . LEU A 1 923  ? 123.042 105.072 88.769  1.00 66.41  ? 923  LEU A C   1 
ATOM   7456  O  O   . LEU A 1 923  ? 123.683 104.780 89.783  1.00 83.36  ? 923  LEU A O   1 
ATOM   7457  C  CB  . LEU A 1 923  ? 122.490 102.933 87.641  1.00 59.78  ? 923  LEU A CB  1 
ATOM   7458  C  CG  . LEU A 1 923  ? 121.501 101.888 87.143  1.00 64.27  ? 923  LEU A CG  1 
ATOM   7459  C  CD1 . LEU A 1 923  ? 122.241 100.798 86.389  1.00 53.83  ? 923  LEU A CD1 1 
ATOM   7460  C  CD2 . LEU A 1 923  ? 120.738 101.311 88.325  1.00 77.12  ? 923  LEU A CD2 1 
ATOM   7461  N  N   . PHE A 1 924  ? 123.310 106.149 88.037  1.00 62.49  ? 924  PHE A N   1 
ATOM   7462  C  CA  . PHE A 1 924  ? 124.420 107.043 88.329  1.00 57.25  ? 924  PHE A CA  1 
ATOM   7463  C  C   . PHE A 1 924  ? 124.024 108.259 89.156  1.00 73.52  ? 924  PHE A C   1 
ATOM   7464  O  O   . PHE A 1 924  ? 124.763 108.640 90.073  1.00 77.14  ? 924  PHE A O   1 
ATOM   7465  C  CB  . PHE A 1 924  ? 125.044 107.498 87.010  1.00 58.39  ? 924  PHE A CB  1 
ATOM   7466  C  CG  . PHE A 1 924  ? 125.597 106.370 86.184  1.00 65.22  ? 924  PHE A CG  1 
ATOM   7467  C  CD1 . PHE A 1 924  ? 124.799 105.696 85.276  1.00 76.25  ? 924  PHE A CD1 1 
ATOM   7468  C  CD2 . PHE A 1 924  ? 126.924 105.997 86.301  1.00 64.87  ? 924  PHE A CD2 1 
ATOM   7469  C  CE1 . PHE A 1 924  ? 125.306 104.655 84.520  1.00 66.48  ? 924  PHE A CE1 1 
ATOM   7470  C  CE2 . PHE A 1 924  ? 127.440 104.960 85.545  1.00 62.32  ? 924  PHE A CE2 1 
ATOM   7471  C  CZ  . PHE A 1 924  ? 126.629 104.289 84.653  1.00 47.52  ? 924  PHE A CZ  1 
ATOM   7472  N  N   . TYR A 1 925  ? 122.881 108.874 88.869  1.00 75.13  ? 925  TYR A N   1 
ATOM   7473  C  CA  . TYR A 1 925  ? 122.444 110.078 89.573  1.00 68.59  ? 925  TYR A CA  1 
ATOM   7474  C  C   . TYR A 1 925  ? 120.981 110.352 89.266  1.00 61.84  ? 925  TYR A C   1 
ATOM   7475  O  O   . TYR A 1 925  ? 120.508 110.070 88.159  1.00 68.27  ? 925  TYR A O   1 
ATOM   7476  C  CB  . TYR A 1 925  ? 123.354 111.251 89.217  1.00 72.28  ? 925  TYR A CB  1 
ATOM   7477  C  CG  . TYR A 1 925  ? 123.764 111.247 87.757  1.00 75.60  ? 925  TYR A CG  1 
ATOM   7478  C  CD1 . TYR A 1 925  ? 125.039 110.865 87.382  1.00 80.47  ? 925  TYR A CD1 1 
ATOM   7479  C  CD2 . TYR A 1 925  ? 122.876 111.648 86.762  1.00 86.46  ? 925  TYR A CD2 1 
ATOM   7480  C  CE1 . TYR A 1 925  ? 125.431 110.852 86.061  1.00 83.03  ? 925  TYR A CE1 1 
ATOM   7481  C  CE2 . TYR A 1 925  ? 123.265 111.641 85.429  1.00 82.36  ? 925  TYR A CE2 1 
ATOM   7482  C  CZ  . TYR A 1 925  ? 124.545 111.243 85.089  1.00 74.90  ? 925  TYR A CZ  1 
ATOM   7483  O  OH  . TYR A 1 925  ? 124.957 111.219 83.778  1.00 71.56  ? 925  TYR A OH  1 
ATOM   7484  N  N   . ARG A 1 926  ? 120.254 110.899 90.249  1.00 67.49  ? 926  ARG A N   1 
ATOM   7485  C  CA  . ARG A 1 926  ? 118.808 111.058 90.086  1.00 64.15  ? 926  ARG A CA  1 
ATOM   7486  C  C   . ARG A 1 926  ? 118.471 112.234 89.173  1.00 84.00  ? 926  ARG A C   1 
ATOM   7487  O  O   . ARG A 1 926  ? 117.651 112.096 88.265  1.00 86.65  ? 926  ARG A O   1 
ATOM   7488  C  CB  . ARG A 1 926  ? 118.139 111.223 91.451  1.00 77.42  ? 926  ARG A CB  1 
ATOM   7489  C  CG  . ARG A 1 926  ? 118.060 109.942 92.272  1.00 77.94  ? 926  ARG A CG  1 
ATOM   7490  C  CD  . ARG A 1 926  ? 117.232 110.170 93.523  1.00 94.39  ? 926  ARG A CD  1 
ATOM   7491  N  NE  . ARG A 1 926  ? 117.662 109.358 94.658  1.00 96.71  ? 926  ARG A NE  1 
ATOM   7492  C  CZ  . ARG A 1 926  ? 116.836 108.711 95.471  1.00 99.56  ? 926  ARG A CZ  1 
ATOM   7493  N  NH1 . ARG A 1 926  ? 115.526 108.768 95.269  1.00 110.08 ? 926  ARG A NH1 1 
ATOM   7494  N  NH2 . ARG A 1 926  ? 117.316 108.016 96.492  1.00 92.11  ? 926  ARG A NH2 1 
ATOM   7495  N  N   . ASN A 1 927  ? 119.072 113.409 89.402  1.00 79.44  ? 927  ASN A N   1 
ATOM   7496  C  CA  . ASN A 1 927  ? 118.705 114.591 88.621  1.00 75.73  ? 927  ASN A CA  1 
ATOM   7497  C  C   . ASN A 1 927  ? 119.447 114.554 87.296  1.00 76.11  ? 927  ASN A C   1 
ATOM   7498  O  O   . ASN A 1 927  ? 120.685 114.653 87.260  1.00 86.69  ? 927  ASN A O   1 
ATOM   7499  C  CB  . ASN A 1 927  ? 119.011 115.893 89.352  1.00 98.57  ? 927  ASN A CB  1 
ATOM   7500  C  CG  . ASN A 1 927  ? 117.991 116.242 90.408  1.00 121.53 ? 927  ASN A CG  1 
ATOM   7501  O  OD1 . ASN A 1 927  ? 118.336 116.455 91.568  1.00 119.44 ? 927  ASN A OD1 1 
ATOM   7502  N  ND2 . ASN A 1 927  ? 116.730 116.377 89.995  1.00 119.91 ? 927  ASN A ND2 1 
ATOM   7503  N  N   . ILE A 1 928  ? 118.702 114.404 86.212  1.00 73.13  ? 928  ILE A N   1 
ATOM   7504  C  CA  . ILE A 1 928  ? 119.265 114.361 84.871  1.00 70.11  ? 928  ILE A CA  1 
ATOM   7505  C  C   . ILE A 1 928  ? 119.008 115.711 84.224  1.00 85.20  ? 928  ILE A C   1 
ATOM   7506  O  O   . ILE A 1 928  ? 117.884 116.231 84.280  1.00 88.39  ? 928  ILE A O   1 
ATOM   7507  C  CB  . ILE A 1 928  ? 118.644 113.220 84.047  1.00 71.37  ? 928  ILE A CB  1 
ATOM   7508  C  CG1 . ILE A 1 928  ? 118.935 111.869 84.700  1.00 77.53  ? 928  ILE A CG1 1 
ATOM   7509  C  CG2 . ILE A 1 928  ? 119.189 113.241 82.630  1.00 71.14  ? 928  ILE A CG2 1 
ATOM   7510  C  CD1 . ILE A 1 928  ? 118.634 110.677 83.811  1.00 73.91  ? 928  ILE A CD1 1 
ATOM   7511  N  N   . SER A 1 929  ? 120.047 116.278 83.613  1.00 82.20  ? 929  SER A N   1 
ATOM   7512  C  CA  . SER A 1 929  ? 119.959 117.629 83.074  1.00 72.23  ? 929  SER A CA  1 
ATOM   7513  C  C   . SER A 1 929  ? 118.914 117.711 81.967  1.00 78.83  ? 929  SER A C   1 
ATOM   7514  O  O   . SER A 1 929  ? 118.019 118.564 81.999  1.00 86.24  ? 929  SER A O   1 
ATOM   7515  C  CB  . SER A 1 929  ? 121.331 118.077 82.572  1.00 78.43  ? 929  SER A CB  1 
ATOM   7516  O  OG  . SER A 1 929  ? 122.330 117.831 83.550  1.00 87.45  ? 929  SER A OG  1 
ATOM   7517  N  N   . ASP A 1 930  ? 119.007 116.825 80.979  1.00 79.92  ? 930  ASP A N   1 
ATOM   7518  C  CA  . ASP A 1 930  ? 118.082 116.811 79.846  1.00 77.05  ? 930  ASP A CA  1 
ATOM   7519  C  C   . ASP A 1 930  ? 117.576 115.390 79.627  1.00 75.22  ? 930  ASP A C   1 
ATOM   7520  O  O   . ASP A 1 930  ? 118.362 114.514 79.213  1.00 78.29  ? 930  ASP A O   1 
ATOM   7521  C  CB  . ASP A 1 930  ? 118.770 117.345 78.594  1.00 77.24  ? 930  ASP A CB  1 
ATOM   7522  C  CG  . ASP A 1 930  ? 117.820 117.494 77.424  1.00 88.62  ? 930  ASP A CG  1 
ATOM   7523  O  OD1 . ASP A 1 930  ? 116.593 117.504 77.653  1.00 87.65  ? 930  ASP A OD1 1 
ATOM   7524  O  OD2 . ASP A 1 930  ? 118.298 117.597 76.275  1.00 87.65  ? 930  ASP A OD2 1 
ATOM   7525  N  N   . PRO A 1 931  ? 116.294 115.119 79.886  1.00 61.00  ? 931  PRO A N   1 
ATOM   7526  C  CA  . PRO A 1 931  ? 115.773 113.753 79.694  1.00 63.88  ? 931  PRO A CA  1 
ATOM   7527  C  C   . PRO A 1 931  ? 115.623 113.319 78.239  1.00 78.32  ? 931  PRO A C   1 
ATOM   7528  O  O   . PRO A 1 931  ? 115.662 112.109 77.970  1.00 81.73  ? 931  PRO A O   1 
ATOM   7529  C  CB  . PRO A 1 931  ? 114.405 113.804 80.390  1.00 80.86  ? 931  PRO A CB  1 
ATOM   7530  C  CG  . PRO A 1 931  ? 114.475 115.001 81.310  1.00 78.76  ? 931  PRO A CG  1 
ATOM   7531  C  CD  . PRO A 1 931  ? 115.328 115.987 80.580  1.00 60.56  ? 931  PRO A CD  1 
ATOM   7532  N  N   . LEU A 1 932  ? 115.507 114.251 77.292  1.00 68.25  ? 932  LEU A N   1 
ATOM   7533  C  CA  . LEU A 1 932  ? 115.285 113.863 75.899  1.00 68.42  ? 932  LEU A CA  1 
ATOM   7534  C  C   . LEU A 1 932  ? 116.518 113.215 75.282  1.00 70.96  ? 932  LEU A C   1 
ATOM   7535  O  O   . LEU A 1 932  ? 116.419 112.172 74.622  1.00 77.21  ? 932  LEU A O   1 
ATOM   7536  C  CB  . LEU A 1 932  ? 114.840 115.068 75.072  1.00 69.25  ? 932  LEU A CB  1 
ATOM   7537  C  CG  . LEU A 1 932  ? 114.383 114.638 73.675  1.00 68.19  ? 932  LEU A CG  1 
ATOM   7538  C  CD1 . LEU A 1 932  ? 113.322 113.548 73.786  1.00 79.29  ? 932  LEU A CD1 1 
ATOM   7539  C  CD2 . LEU A 1 932  ? 113.859 115.818 72.877  1.00 64.76  ? 932  LEU A CD2 1 
ATOM   7540  N  N   . THR A 1 933  ? 117.690 113.819 75.478  1.00 72.35  ? 933  THR A N   1 
ATOM   7541  C  CA  . THR A 1 933  ? 118.904 113.281 74.875  1.00 65.49  ? 933  THR A CA  1 
ATOM   7542  C  C   . THR A 1 933  ? 119.274 111.933 75.482  1.00 70.96  ? 933  THR A C   1 
ATOM   7543  O  O   . THR A 1 933  ? 119.664 111.004 74.760  1.00 77.88  ? 933  THR A O   1 
ATOM   7544  C  CB  . THR A 1 933  ? 120.048 114.278 75.045  1.00 73.85  ? 933  THR A CB  1 
ATOM   7545  O  OG1 . THR A 1 933  ? 120.027 114.799 76.380  1.00 79.10  ? 933  THR A OG1 1 
ATOM   7546  C  CG2 . THR A 1 933  ? 119.887 115.435 74.069  1.00 82.11  ? 933  THR A CG2 1 
ATOM   7547  N  N   . SER A 1 934  ? 119.140 111.795 76.803  1.00 67.67  ? 934  SER A N   1 
ATOM   7548  C  CA  . SER A 1 934  ? 119.421 110.510 77.429  1.00 60.14  ? 934  SER A CA  1 
ATOM   7549  C  C   . SER A 1 934  ? 118.417 109.460 76.973  1.00 71.42  ? 934  SER A C   1 
ATOM   7550  O  O   . SER A 1 934  ? 118.779 108.294 76.764  1.00 86.94  ? 934  SER A O   1 
ATOM   7551  C  CB  . SER A 1 934  ? 119.406 110.644 78.952  1.00 56.30  ? 934  SER A CB  1 
ATOM   7552  O  OG  . SER A 1 934  ? 118.102 110.446 79.471  1.00 78.64  ? 934  SER A OG  1 
ATOM   7553  N  N   . GLY A 1 935  ? 117.152 109.856 76.805  1.00 55.59  ? 935  GLY A N   1 
ATOM   7554  C  CA  . GLY A 1 935  ? 116.162 108.921 76.298  1.00 57.96  ? 935  GLY A CA  1 
ATOM   7555  C  C   . GLY A 1 935  ? 116.471 108.441 74.891  1.00 74.15  ? 935  GLY A C   1 
ATOM   7556  O  O   . GLY A 1 935  ? 116.327 107.254 74.585  1.00 73.80  ? 935  GLY A O   1 
ATOM   7557  N  N   . LEU A 1 936  ? 116.920 109.353 74.023  1.00 63.44  ? 936  LEU A N   1 
ATOM   7558  C  CA  . LEU A 1 936  ? 117.313 108.960 72.671  1.00 56.01  ? 936  LEU A CA  1 
ATOM   7559  C  C   . LEU A 1 936  ? 118.518 108.028 72.687  1.00 62.59  ? 936  LEU A C   1 
ATOM   7560  O  O   . LEU A 1 936  ? 118.560 107.041 71.940  1.00 77.22  ? 936  LEU A O   1 
ATOM   7561  C  CB  . LEU A 1 936  ? 117.622 110.201 71.834  1.00 55.56  ? 936  LEU A CB  1 
ATOM   7562  C  CG  . LEU A 1 936  ? 116.451 111.108 71.472  1.00 57.10  ? 936  LEU A CG  1 
ATOM   7563  C  CD1 . LEU A 1 936  ? 116.959 112.474 71.044  1.00 62.00  ? 936  LEU A CD1 1 
ATOM   7564  C  CD2 . LEU A 1 936  ? 115.628 110.467 70.363  1.00 61.83  ? 936  LEU A CD2 1 
ATOM   7565  N  N   . PHE A 1 937  ? 119.499 108.321 73.541  1.00 60.23  ? 937  PHE A N   1 
ATOM   7566  C  CA  . PHE A 1 937  ? 120.658 107.445 73.680  1.00 58.61  ? 937  PHE A CA  1 
ATOM   7567  C  C   . PHE A 1 937  ? 120.243 106.039 74.101  1.00 62.52  ? 937  PHE A C   1 
ATOM   7568  O  O   . PHE A 1 937  ? 120.666 105.037 73.499  1.00 70.18  ? 937  PHE A O   1 
ATOM   7569  C  CB  . PHE A 1 937  ? 121.631 108.053 74.692  1.00 75.86  ? 937  PHE A CB  1 
ATOM   7570  C  CG  . PHE A 1 937  ? 122.905 107.280 74.849  1.00 74.13  ? 937  PHE A CG  1 
ATOM   7571  C  CD1 . PHE A 1 937  ? 123.832 107.228 73.824  1.00 77.25  ? 937  PHE A CD1 1 
ATOM   7572  C  CD2 . PHE A 1 937  ? 123.178 106.613 76.031  1.00 74.39  ? 937  PHE A CD2 1 
ATOM   7573  C  CE1 . PHE A 1 937  ? 125.004 106.511 73.970  1.00 76.60  ? 937  PHE A CE1 1 
ATOM   7574  C  CE2 . PHE A 1 937  ? 124.350 105.897 76.185  1.00 66.25  ? 937  PHE A CE2 1 
ATOM   7575  C  CZ  . PHE A 1 937  ? 125.264 105.847 75.153  1.00 74.30  ? 937  PHE A CZ  1 
ATOM   7576  N  N   . GLN A 1 938  ? 119.387 105.952 75.121  1.00 55.66  ? 938  GLN A N   1 
ATOM   7577  C  CA  . GLN A 1 938  ? 118.935 104.653 75.601  1.00 55.13  ? 938  GLN A CA  1 
ATOM   7578  C  C   . GLN A 1 938  ? 118.157 103.903 74.526  1.00 63.49  ? 938  GLN A C   1 
ATOM   7579  O  O   . GLN A 1 938  ? 118.347 102.693 74.348  1.00 81.13  ? 938  GLN A O   1 
ATOM   7580  C  CB  . GLN A 1 938  ? 118.096 104.827 76.865  1.00 62.79  ? 938  GLN A CB  1 
ATOM   7581  C  CG  . GLN A 1 938  ? 117.321 103.589 77.268  1.00 72.66  ? 938  GLN A CG  1 
ATOM   7582  C  CD  . GLN A 1 938  ? 116.103 103.917 78.104  1.00 79.57  ? 938  GLN A CD  1 
ATOM   7583  O  OE1 . GLN A 1 938  ? 115.983 105.016 78.644  1.00 74.60  ? 938  GLN A OE1 1 
ATOM   7584  N  NE2 . GLN A 1 938  ? 115.187 102.963 78.210  1.00 61.92  ? 938  GLN A NE2 1 
ATOM   7585  N  N   . LEU A 1 939  ? 117.267 104.594 73.808  1.00 59.25  ? 939  LEU A N   1 
ATOM   7586  C  CA  . LEU A 1 939  ? 116.492 103.907 72.779  1.00 60.36  ? 939  LEU A CA  1 
ATOM   7587  C  C   . LEU A 1 939  ? 117.392 103.382 71.667  1.00 68.93  ? 939  LEU A C   1 
ATOM   7588  O  O   . LEU A 1 939  ? 117.190 102.264 71.174  1.00 72.42  ? 939  LEU A O   1 
ATOM   7589  C  CB  . LEU A 1 939  ? 115.407 104.819 72.209  1.00 64.77  ? 939  LEU A CB  1 
ATOM   7590  C  CG  . LEU A 1 939  ? 114.590 104.094 71.136  1.00 52.96  ? 939  LEU A CG  1 
ATOM   7591  C  CD1 . LEU A 1 939  ? 113.803 102.961 71.756  1.00 56.54  ? 939  LEU A CD1 1 
ATOM   7592  C  CD2 . LEU A 1 939  ? 113.654 105.050 70.419  1.00 52.25  ? 939  LEU A CD2 1 
ATOM   7593  N  N   . LYS A 1 940  ? 118.385 104.174 71.247  1.00 70.23  ? 940  LYS A N   1 
ATOM   7594  C  CA  . LYS A 1 940  ? 119.292 103.697 70.205  1.00 59.53  ? 940  LYS A CA  1 
ATOM   7595  C  C   . LYS A 1 940  ? 120.049 102.455 70.658  1.00 80.02  ? 940  LYS A C   1 
ATOM   7596  O  O   . LYS A 1 940  ? 120.175 101.481 69.901  1.00 83.90  ? 940  LYS A O   1 
ATOM   7597  C  CB  . LYS A 1 940  ? 120.275 104.793 69.807  1.00 57.63  ? 940  LYS A CB  1 
ATOM   7598  C  CG  . LYS A 1 940  ? 121.201 104.373 68.677  1.00 79.44  ? 940  LYS A CG  1 
ATOM   7599  C  CD  . LYS A 1 940  ? 122.124 105.499 68.263  1.00 98.70  ? 940  LYS A CD  1 
ATOM   7600  C  CE  . LYS A 1 940  ? 121.488 106.338 67.178  1.00 99.66  ? 940  LYS A CE  1 
ATOM   7601  N  NZ  . LYS A 1 940  ? 121.620 105.682 65.850  1.00 89.99  ? 940  LYS A NZ  1 
ATOM   7602  N  N   . ASN A 1 941  ? 120.545 102.463 71.901  1.00 81.48  ? 941  ASN A N   1 
ATOM   7603  C  CA  . ASN A 1 941  ? 121.261 101.291 72.400  1.00 68.62  ? 941  ASN A CA  1 
ATOM   7604  C  C   . ASN A 1 941  ? 120.351 100.071 72.454  1.00 67.98  ? 941  ASN A C   1 
ATOM   7605  O  O   . ASN A 1 941  ? 120.756 98.963  72.072  1.00 80.34  ? 941  ASN A O   1 
ATOM   7606  C  CB  . ASN A 1 941  ? 121.862 101.578 73.775  1.00 53.20  ? 941  ASN A CB  1 
ATOM   7607  C  CG  . ASN A 1 941  ? 123.119 102.404 73.689  1.00 83.71  ? 941  ASN A CG  1 
ATOM   7608  O  OD1 . ASN A 1 941  ? 124.094 102.003 73.053  1.00 94.69  ? 941  ASN A OD1 1 
ATOM   7609  N  ND2 . ASN A 1 941  ? 123.104 103.574 74.312  1.00 93.04  ? 941  ASN A ND2 1 
ATOM   7610  N  N   . ALA A 1 942  ? 119.119 100.250 72.934  1.00 63.34  ? 942  ALA A N   1 
ATOM   7611  C  CA  . ALA A 1 942  ? 118.220 99.110  73.050  1.00 61.66  ? 942  ALA A CA  1 
ATOM   7612  C  C   . ALA A 1 942  ? 117.883 98.540  71.678  1.00 77.72  ? 942  ALA A C   1 
ATOM   7613  O  O   . ALA A 1 942  ? 117.825 97.316  71.505  1.00 84.28  ? 942  ALA A O   1 
ATOM   7614  C  CB  . ALA A 1 942  ? 116.956 99.517  73.810  1.00 49.68  ? 942  ALA A CB  1 
ATOM   7615  N  N   . LEU A 1 943  ? 117.664 99.403  70.681  1.00 70.51  ? 943  LEU A N   1 
ATOM   7616  C  CA  . LEU A 1 943  ? 117.379 98.875  69.348  1.00 70.61  ? 943  LEU A CA  1 
ATOM   7617  C  C   . LEU A 1 943  ? 118.586 98.201  68.721  1.00 80.20  ? 943  LEU A C   1 
ATOM   7618  O  O   . LEU A 1 943  ? 118.429 97.243  67.960  1.00 82.50  ? 943  LEU A O   1 
ATOM   7619  C  CB  . LEU A 1 943  ? 116.875 99.970  68.410  1.00 68.02  ? 943  LEU A CB  1 
ATOM   7620  C  CG  . LEU A 1 943  ? 115.413 100.327 68.666  1.00 60.75  ? 943  LEU A CG  1 
ATOM   7621  C  CD1 . LEU A 1 943  ? 114.945 101.429 67.710  1.00 80.06  ? 943  LEU A CD1 1 
ATOM   7622  C  CD2 . LEU A 1 943  ? 114.476 99.094  68.686  1.00 66.56  ? 943  LEU A CD2 1 
ATOM   7623  N  N   . GLU A 1 944  ? 119.798 98.677  69.023  1.00 81.30  ? 944  GLU A N   1 
ATOM   7624  C  CA  . GLU A 1 944  ? 120.970 97.980  68.507  1.00 87.87  ? 944  GLU A CA  1 
ATOM   7625  C  C   . GLU A 1 944  ? 121.108 96.604  69.134  1.00 77.94  ? 944  GLU A C   1 
ATOM   7626  O  O   . GLU A 1 944  ? 121.488 95.643  68.456  1.00 81.55  ? 944  GLU A O   1 
ATOM   7627  C  CB  . GLU A 1 944  ? 122.239 98.797  68.735  1.00 89.85  ? 944  GLU A CB  1 
ATOM   7628  C  CG  . GLU A 1 944  ? 122.351 100.024 67.858  1.00 113.91 ? 944  GLU A CG  1 
ATOM   7629  C  CD  . GLU A 1 944  ? 123.519 100.902 68.244  1.00 123.85 ? 944  GLU A CD  1 
ATOM   7630  O  OE1 . GLU A 1 944  ? 123.982 100.807 69.400  1.00 114.62 ? 944  GLU A OE1 1 
ATOM   7631  O  OE2 . GLU A 1 944  ? 123.984 101.680 67.384  1.00 111.08 ? 944  GLU A OE2 1 
ATOM   7632  N  N   . PHE A 1 945  ? 120.797 96.488  70.424  1.00 77.59  ? 945  PHE A N   1 
ATOM   7633  C  CA  . PHE A 1 945  ? 120.827 95.172  71.054  1.00 65.59  ? 945  PHE A CA  1 
ATOM   7634  C  C   . PHE A 1 945  ? 119.747 94.251  70.492  1.00 70.06  ? 945  PHE A C   1 
ATOM   7635  O  O   . PHE A 1 945  ? 119.995 93.060  70.274  1.00 82.96  ? 945  PHE A O   1 
ATOM   7636  C  CB  . PHE A 1 945  ? 120.661 95.296  72.565  1.00 66.27  ? 945  PHE A CB  1 
ATOM   7637  C  CG  . PHE A 1 945  ? 120.696 93.976  73.273  1.00 67.25  ? 945  PHE A CG  1 
ATOM   7638  C  CD1 . PHE A 1 945  ? 119.546 93.431  73.818  1.00 77.22  ? 945  PHE A CD1 1 
ATOM   7639  C  CD2 . PHE A 1 945  ? 121.883 93.274  73.386  1.00 78.03  ? 945  PHE A CD2 1 
ATOM   7640  C  CE1 . PHE A 1 945  ? 119.580 92.207  74.465  1.00 69.74  ? 945  PHE A CE1 1 
ATOM   7641  C  CE2 . PHE A 1 945  ? 121.925 92.054  74.032  1.00 82.27  ? 945  PHE A CE2 1 
ATOM   7642  C  CZ  . PHE A 1 945  ? 120.773 91.520  74.571  1.00 66.09  ? 945  PHE A CZ  1 
ATOM   7643  N  N   . LEU A 1 946  ? 118.547 94.781  70.250  1.00 78.29  ? 946  LEU A N   1 
ATOM   7644  C  CA  . LEU A 1 946  ? 117.446 93.968  69.739  1.00 84.61  ? 946  LEU A CA  1 
ATOM   7645  C  C   . LEU A 1 946  ? 117.584 93.588  68.265  1.00 99.88  ? 946  LEU A C   1 
ATOM   7646  O  O   . LEU A 1 946  ? 116.801 92.758  67.789  1.00 92.53  ? 946  LEU A O   1 
ATOM   7647  C  CB  . LEU A 1 946  ? 116.122 94.697  69.990  1.00 73.10  ? 946  LEU A CB  1 
ATOM   7648  C  CG  . LEU A 1 946  ? 114.850 93.880  69.768  1.00 87.64  ? 946  LEU A CG  1 
ATOM   7649  C  CD1 . LEU A 1 946  ? 114.709 92.861  70.884  1.00 99.93  ? 946  LEU A CD1 1 
ATOM   7650  C  CD2 . LEU A 1 946  ? 113.638 94.788  69.714  1.00 93.56  ? 946  LEU A CD2 1 
ATOM   7651  N  N   . GLU A 1 947  ? 118.549 94.155  67.541  1.00 99.27  ? 947  GLU A N   1 
ATOM   7652  C  CA  . GLU A 1 947  ? 118.869 93.899  66.131  1.00 92.81  ? 947  GLU A CA  1 
ATOM   7653  C  C   . GLU A 1 947  ? 117.898 94.592  65.178  1.00 98.39  ? 947  GLU A C   1 
ATOM   7654  O  O   . GLU A 1 947  ? 118.049 94.445  63.957  1.00 102.71 ? 947  GLU A O   1 
ATOM   7655  C  CB  . GLU A 1 947  ? 118.893 92.401  65.779  1.00 99.52  ? 947  GLU A CB  1 
ATOM   7656  C  CG  . GLU A 1 947  ? 119.983 91.604  66.467  1.00 112.26 ? 947  GLU A CG  1 
ATOM   7657  C  CD  . GLU A 1 947  ? 121.368 92.008  66.023  1.00 123.26 ? 947  GLU A CD  1 
ATOM   7658  O  OE1 . GLU A 1 947  ? 121.519 92.412  64.851  1.00 132.55 ? 947  GLU A OE1 1 
ATOM   7659  O  OE2 . GLU A 1 947  ? 122.303 91.924  66.844  1.00 122.75 ? 947  GLU A OE2 1 
ATOM   7660  N  N   . LYS A 1 948  ? 116.913 95.327  65.679  1.00 95.22  ? 948  LYS A N   1 
ATOM   7661  C  CA  . LYS A 1 948  ? 115.975 96.076  64.841  1.00 86.61  ? 948  LYS A CA  1 
ATOM   7662  C  C   . LYS A 1 948  ? 116.395 97.542  64.768  1.00 87.25  ? 948  LYS A C   1 
ATOM   7663  O  O   . LYS A 1 948  ? 115.696 98.452  65.213  1.00 92.17  ? 948  LYS A O   1 
ATOM   7664  C  CB  . LYS A 1 948  ? 114.553 95.924  65.368  1.00 84.04  ? 948  LYS A CB  1 
ATOM   7665  C  CG  . LYS A 1 948  ? 114.009 94.520  65.221  1.00 97.00  ? 948  LYS A CG  1 
ATOM   7666  C  CD  . LYS A 1 948  ? 112.572 94.442  65.682  1.00 90.69  ? 948  LYS A CD  1 
ATOM   7667  C  CE  . LYS A 1 948  ? 112.144 93.002  65.860  1.00 108.42 ? 948  LYS A CE  1 
ATOM   7668  N  NZ  . LYS A 1 948  ? 110.881 92.902  66.635  1.00 119.28 ? 948  LYS A NZ  1 
ATOM   7669  N  N   . GLU A 1 949  ? 117.570 97.756  64.177  1.00 97.23  ? 949  GLU A N   1 
ATOM   7670  C  CA  . GLU A 1 949  ? 118.164 99.084  64.108  1.00 96.90  ? 949  GLU A CA  1 
ATOM   7671  C  C   . GLU A 1 949  ? 117.446 100.025 63.150  1.00 92.12  ? 949  GLU A C   1 
ATOM   7672  O  O   . GLU A 1 949  ? 117.679 101.237 63.217  1.00 91.70  ? 949  GLU A O   1 
ATOM   7673  C  CB  . GLU A 1 949  ? 119.624 98.952  63.681  1.00 110.30 ? 949  GLU A CB  1 
ATOM   7674  C  CG  . GLU A 1 949  ? 120.607 98.808  64.819  1.00 120.90 ? 949  GLU A CG  1 
ATOM   7675  C  CD  . GLU A 1 949  ? 121.995 98.479  64.320  1.00 137.92 ? 949  GLU A CD  1 
ATOM   7676  O  OE1 . GLU A 1 949  ? 122.101 97.746  63.314  1.00 140.04 ? 949  GLU A OE1 1 
ATOM   7677  O  OE2 . GLU A 1 949  ? 122.977 98.953  64.925  1.00 139.82 ? 949  GLU A OE2 1 
ATOM   7678  N  N   . GLU A 1 950  ? 116.580 99.512  62.277  1.00 97.97  ? 950  GLU A N   1 
ATOM   7679  C  CA  . GLU A 1 950  ? 115.888 100.352 61.308  1.00 94.28  ? 950  GLU A CA  1 
ATOM   7680  C  C   . GLU A 1 950  ? 114.629 101.015 61.859  1.00 91.81  ? 950  GLU A C   1 
ATOM   7681  O  O   . GLU A 1 950  ? 114.040 101.849 61.164  1.00 91.94  ? 950  GLU A O   1 
ATOM   7682  C  CB  . GLU A 1 950  ? 115.534 99.531  60.064  1.00 103.57 ? 950  GLU A CB  1 
ATOM   7683  C  CG  . GLU A 1 950  ? 114.503 98.450  60.313  1.00 108.07 ? 950  GLU A CG  1 
ATOM   7684  C  CD  . GLU A 1 950  ? 115.142 97.114  60.630  1.00 104.99 ? 950  GLU A CD  1 
ATOM   7685  O  OE1 . GLU A 1 950  ? 114.402 96.136  60.861  1.00 107.86 ? 950  GLU A OE1 1 
ATOM   7686  O  OE2 . GLU A 1 950  ? 116.389 97.042  60.646  1.00 101.62 ? 950  GLU A OE2 1 
ATOM   7687  N  N   . LEU A 1 951  ? 114.207 100.686 63.079  1.00 86.58  ? 951  LEU A N   1 
ATOM   7688  C  CA  . LEU A 1 951  ? 112.995 101.257 63.657  1.00 81.10  ? 951  LEU A CA  1 
ATOM   7689  C  C   . LEU A 1 951  ? 113.220 102.566 64.401  1.00 82.98  ? 951  LEU A C   1 
ATOM   7690  O  O   . LEU A 1 951  ? 112.254 103.123 64.930  1.00 86.41  ? 951  LEU A O   1 
ATOM   7691  C  CB  . LEU A 1 951  ? 112.322 100.271 64.610  1.00 70.35  ? 951  LEU A CB  1 
ATOM   7692  C  CG  . LEU A 1 951  ? 111.658 99.050  63.988  1.00 88.99  ? 951  LEU A CG  1 
ATOM   7693  C  CD1 . LEU A 1 951  ? 110.904 98.285  65.060  1.00 76.31  ? 951  LEU A CD1 1 
ATOM   7694  C  CD2 . LEU A 1 951  ? 110.726 99.490  62.869  1.00 92.64  ? 951  LEU A CD2 1 
ATOM   7695  N  N   . PHE A 1 952  ? 114.459 103.046 64.497  1.00 72.90  ? 952  PHE A N   1 
ATOM   7696  C  CA  . PHE A 1 952  ? 114.728 104.216 65.324  1.00 60.00  ? 952  PHE A CA  1 
ATOM   7697  C  C   . PHE A 1 952  ? 113.963 105.436 64.826  1.00 70.37  ? 952  PHE A C   1 
ATOM   7698  O  O   . PHE A 1 952  ? 113.207 106.074 65.579  1.00 84.26  ? 952  PHE A O   1 
ATOM   7699  C  CB  . PHE A 1 952  ? 116.231 104.492 65.345  1.00 66.00  ? 952  PHE A CB  1 
ATOM   7700  C  CG  . PHE A 1 952  ? 116.628 105.608 66.263  1.00 68.56  ? 952  PHE A CG  1 
ATOM   7701  C  CD1 . PHE A 1 952  ? 116.312 105.565 67.608  1.00 76.99  ? 952  PHE A CD1 1 
ATOM   7702  C  CD2 . PHE A 1 952  ? 117.320 106.704 65.776  1.00 86.44  ? 952  PHE A CD2 1 
ATOM   7703  C  CE1 . PHE A 1 952  ? 116.674 106.598 68.453  1.00 74.60  ? 952  PHE A CE1 1 
ATOM   7704  C  CE2 . PHE A 1 952  ? 117.687 107.740 66.616  1.00 77.46  ? 952  PHE A CE2 1 
ATOM   7705  C  CZ  . PHE A 1 952  ? 117.363 107.686 67.955  1.00 61.62  ? 952  PHE A CZ  1 
ATOM   7706  N  N   . TYR A 1 953  ? 114.117 105.761 63.542  1.00 72.27  ? 953  TYR A N   1 
ATOM   7707  C  CA  . TYR A 1 953  ? 113.480 106.964 63.025  1.00 70.61  ? 953  TYR A CA  1 
ATOM   7708  C  C   . TYR A 1 953  ? 111.983 106.792 62.864  1.00 69.22  ? 953  TYR A C   1 
ATOM   7709  O  O   . TYR A 1 953  ? 111.265 107.791 62.770  1.00 79.52  ? 953  TYR A O   1 
ATOM   7710  C  CB  . TYR A 1 953  ? 114.123 107.364 61.699  1.00 64.88  ? 953  TYR A CB  1 
ATOM   7711  C  CG  . TYR A 1 953  ? 115.596 107.585 61.880  1.00 88.14  ? 953  TYR A CG  1 
ATOM   7712  C  CD1 . TYR A 1 953  ? 116.070 108.644 62.633  1.00 94.96  ? 953  TYR A CD1 1 
ATOM   7713  C  CD2 . TYR A 1 953  ? 116.518 106.740 61.275  1.00 90.65  ? 953  TYR A CD2 1 
ATOM   7714  C  CE1 . TYR A 1 953  ? 117.421 108.846 62.810  1.00 92.32  ? 953  TYR A CE1 1 
ATOM   7715  C  CE2 . TYR A 1 953  ? 117.871 106.937 61.438  1.00 104.94 ? 953  TYR A CE2 1 
ATOM   7716  C  CZ  . TYR A 1 953  ? 118.317 107.992 62.204  1.00 106.00 ? 953  TYR A CZ  1 
ATOM   7717  O  OH  . TYR A 1 953  ? 119.666 108.192 62.378  1.00 106.26 ? 953  TYR A OH  1 
ATOM   7718  N  N   . ILE A 1 954  ? 111.499 105.549 62.838  1.00 66.76  ? 954  ILE A N   1 
ATOM   7719  C  CA  . ILE A 1 954  ? 110.057 105.334 62.841  1.00 63.59  ? 954  ILE A CA  1 
ATOM   7720  C  C   . ILE A 1 954  ? 109.482 105.570 64.232  1.00 69.27  ? 954  ILE A C   1 
ATOM   7721  O  O   . ILE A 1 954  ? 108.426 106.190 64.380  1.00 83.18  ? 954  ILE A O   1 
ATOM   7722  C  CB  . ILE A 1 954  ? 109.741 103.930 62.306  1.00 69.18  ? 954  ILE A CB  1 
ATOM   7723  C  CG1 . ILE A 1 954  ? 110.056 103.860 60.809  1.00 77.45  ? 954  ILE A CG1 1 
ATOM   7724  C  CG2 . ILE A 1 954  ? 108.281 103.580 62.544  1.00 68.43  ? 954  ILE A CG2 1 
ATOM   7725  C  CD1 . ILE A 1 954  ? 109.958 102.472 60.219  1.00 91.66  ? 954  ILE A CD1 1 
ATOM   7726  N  N   . LEU A 1 955  ? 110.170 105.108 65.283  1.00 72.21  ? 955  LEU A N   1 
ATOM   7727  C  CA  . LEU A 1 955  ? 109.618 105.247 66.632  1.00 75.48  ? 955  LEU A CA  1 
ATOM   7728  C  C   . LEU A 1 955  ? 109.742 106.649 67.191  1.00 69.29  ? 955  LEU A C   1 
ATOM   7729  O  O   . LEU A 1 955  ? 108.900 107.063 67.985  1.00 73.42  ? 955  LEU A O   1 
ATOM   7730  C  CB  . LEU A 1 955  ? 110.255 104.266 67.612  1.00 57.87  ? 955  LEU A CB  1 
ATOM   7731  C  CG  . LEU A 1 955  ? 109.919 102.799 67.393  1.00 58.02  ? 955  LEU A CG  1 
ATOM   7732  C  CD1 . LEU A 1 955  ? 110.589 101.948 68.453  1.00 55.32  ? 955  LEU A CD1 1 
ATOM   7733  C  CD2 . LEU A 1 955  ? 108.411 102.662 67.477  1.00 80.84  ? 955  LEU A CD2 1 
ATOM   7734  N  N   . ILE A 1 956  ? 110.770 107.415 66.802  1.00 73.16  ? 956  ILE A N   1 
ATOM   7735  C  CA  . ILE A 1 956  ? 110.891 108.726 67.429  1.00 62.71  ? 956  ILE A CA  1 
ATOM   7736  C  C   . ILE A 1 956  ? 110.052 109.788 66.732  1.00 79.94  ? 956  ILE A C   1 
ATOM   7737  O  O   . ILE A 1 956  ? 109.760 110.826 67.344  1.00 89.54  ? 956  ILE A O   1 
ATOM   7738  C  CB  . ILE A 1 956  ? 112.346 109.213 67.456  1.00 60.30  ? 956  ILE A CB  1 
ATOM   7739  C  CG1 . ILE A 1 956  ? 112.863 109.387 66.027  1.00 77.64  ? 956  ILE A CG1 1 
ATOM   7740  C  CG2 . ILE A 1 956  ? 113.223 108.217 68.198  1.00 80.46  ? 956  ILE A CG2 1 
ATOM   7741  C  CD1 . ILE A 1 956  ? 114.271 109.922 65.948  1.00 89.12  ? 956  ILE A CD1 1 
ATOM   7742  N  N   . SER A 1 957  ? 109.632 109.552 65.491  1.00 79.50  ? 957  SER A N   1 
ATOM   7743  C  CA  . SER A 1 957  ? 108.931 110.562 64.697  1.00 82.69  ? 957  SER A CA  1 
ATOM   7744  C  C   . SER A 1 957  ? 107.427 110.297 64.707  1.00 95.92  ? 957  SER A C   1 
ATOM   7745  O  O   . SER A 1 957  ? 106.893 109.610 63.835  1.00 95.88  ? 957  SER A O   1 
ATOM   7746  C  CB  . SER A 1 957  ? 109.487 110.573 63.276  1.00 87.63  ? 957  SER A CB  1 
ATOM   7747  O  OG  . SER A 1 957  ? 109.210 109.358 62.600  1.00 94.98  ? 957  SER A OG  1 
ATOM   7748  N  N   . LYS A 1 958  ? 106.734 110.863 65.691  1.00 100.73 ? 958  LYS A N   1 
ATOM   7749  C  CA  . LYS A 1 958  ? 105.293 110.703 65.815  1.00 103.90 ? 958  LYS A CA  1 
ATOM   7750  C  C   . LYS A 1 958  ? 104.579 112.024 65.557  1.00 112.58 ? 958  LYS A C   1 
ATOM   7751  O  O   . LYS A 1 958  ? 105.167 113.105 65.655  1.00 113.17 ? 958  LYS A O   1 
ATOM   7752  C  CB  . LYS A 1 958  ? 104.912 110.142 67.188  1.00 94.35  ? 958  LYS A CB  1 
ATOM   7753  C  CG  . LYS A 1 958  ? 105.281 108.678 67.339  1.00 99.67  ? 958  LYS A CG  1 
ATOM   7754  C  CD  . LYS A 1 958  ? 105.069 108.178 68.752  1.00 87.89  ? 958  LYS A CD  1 
ATOM   7755  C  CE  . LYS A 1 958  ? 105.422 106.704 68.853  1.00 78.67  ? 958  LYS A CE  1 
ATOM   7756  N  NZ  . LYS A 1 958  ? 105.313 106.201 70.246  1.00 73.52  ? 958  LYS A NZ  1 
ATOM   7757  N  N   . LYS A 1 959  ? 103.293 111.923 65.239  1.00 110.42 ? 959  LYS A N   1 
ATOM   7758  C  CA  . LYS A 1 959  ? 102.518 113.101 64.865  1.00 104.69 ? 959  LYS A CA  1 
ATOM   7759  C  C   . LYS A 1 959  ? 102.319 114.005 66.076  1.00 101.07 ? 959  LYS A C   1 
ATOM   7760  O  O   . LYS A 1 959  ? 101.836 113.543 67.115  1.00 109.20 ? 959  LYS A O   1 
ATOM   7761  C  CB  . LYS A 1 959  ? 101.162 112.693 64.294  1.00 121.76 ? 959  LYS A CB  1 
ATOM   7762  C  CG  . LYS A 1 959  ? 101.120 112.611 62.784  1.00 117.41 ? 959  LYS A CG  1 
ATOM   7763  C  CD  . LYS A 1 959  ? 99.922  111.820 62.302  1.00 124.61 ? 959  LYS A CD  1 
ATOM   7764  C  CE  . LYS A 1 959  ? 99.967  111.620 60.797  1.00 131.76 ? 959  LYS A CE  1 
ATOM   7765  N  NZ  . LYS A 1 959  ? 99.102  110.493 60.364  1.00 139.00 ? 959  LYS A NZ  1 
ATOM   7766  N  N   . PRO A 1 960  ? 102.670 115.287 65.984  1.00 91.04  ? 960  PRO A N   1 
ATOM   7767  C  CA  . PRO A 1 960  ? 102.411 116.197 67.103  1.00 96.65  ? 960  PRO A CA  1 
ATOM   7768  C  C   . PRO A 1 960  ? 100.922 116.394 67.317  1.00 101.97 ? 960  PRO A C   1 
ATOM   7769  O  O   . PRO A 1 960  ? 100.114 116.290 66.390  1.00 97.51  ? 960  PRO A O   1 
ATOM   7770  C  CB  . PRO A 1 960  ? 103.084 117.504 66.666  1.00 95.31  ? 960  PRO A CB  1 
ATOM   7771  C  CG  . PRO A 1 960  ? 103.169 117.415 65.182  1.00 94.26  ? 960  PRO A CG  1 
ATOM   7772  C  CD  . PRO A 1 960  ? 103.325 115.964 64.853  1.00 93.07  ? 960  PRO A CD  1 
ATOM   7773  N  N   . GLY A 1 961  ? 100.564 116.679 68.557  1.00 101.55 ? 961  GLY A N   1 
ATOM   7774  C  CA  . GLY A 1 961  ? 99.181  116.868 68.941  1.00 105.18 ? 961  GLY A CA  1 
ATOM   7775  C  C   . GLY A 1 961  ? 98.765  118.316 68.835  1.00 117.75 ? 961  GLY A C   1 
ATOM   7776  O  O   . GLY A 1 961  ? 99.321  119.095 68.054  1.00 112.79 ? 961  GLY A O   1 
ATOM   7777  N  N   . LEU A 1 962  ? 97.772  118.684 69.636  1.00 121.88 ? 962  LEU A N   1 
ATOM   7778  C  CA  . LEU A 1 962  ? 97.241  120.043 69.673  1.00 116.80 ? 962  LEU A CA  1 
ATOM   7779  C  C   . LEU A 1 962  ? 97.390  120.549 71.104  1.00 111.79 ? 962  LEU A C   1 
ATOM   7780  O  O   . LEU A 1 962  ? 96.610  120.177 71.985  1.00 113.24 ? 962  LEU A O   1 
ATOM   7781  C  CB  . LEU A 1 962  ? 95.788  120.074 69.211  1.00 121.45 ? 962  LEU A CB  1 
ATOM   7782  C  CG  . LEU A 1 962  ? 95.539  119.436 67.842  1.00 124.53 ? 962  LEU A CG  1 
ATOM   7783  C  CD1 . LEU A 1 962  ? 94.138  118.848 67.773  1.00 116.17 ? 962  LEU A CD1 1 
ATOM   7784  C  CD2 . LEU A 1 962  ? 95.767  120.442 66.721  1.00 110.65 ? 962  LEU A CD2 1 
ATOM   7785  N  N   . ALA A 1 963  ? 98.386  121.400 71.333  1.00 104.38 ? 963  ALA A N   1 
ATOM   7786  C  CA  . ALA A 1 963  ? 98.660  121.927 72.659  1.00 110.53 ? 963  ALA A CA  1 
ATOM   7787  C  C   . ALA A 1 963  ? 98.818  123.438 72.586  1.00 119.49 ? 963  ALA A C   1 
ATOM   7788  O  O   . ALA A 1 963  ? 99.325  123.981 71.601  1.00 104.23 ? 963  ALA A O   1 
ATOM   7789  C  CB  . ALA A 1 963  ? 99.919  121.297 73.267  1.00 104.42 ? 963  ALA A CB  1 
ATOM   7790  N  N   . ASP A 1 964  ? 98.376  124.109 73.644  1.00 120.15 ? 964  ASP A N   1 
ATOM   7791  C  CA  . ASP A 1 964  ? 98.437  125.557 73.720  1.00 110.56 ? 964  ASP A CA  1 
ATOM   7792  C  C   . ASP A 1 964  ? 99.805  125.983 74.252  1.00 95.39  ? 964  ASP A C   1 
ATOM   7793  O  O   . ASP A 1 964  ? 100.717 125.165 74.406  1.00 98.97  ? 964  ASP A O   1 
ATOM   7794  C  CB  . ASP A 1 964  ? 97.288  126.072 74.584  1.00 116.77 ? 964  ASP A CB  1 
ATOM   7795  C  CG  . ASP A 1 964  ? 95.936  125.869 73.927  1.00 132.40 ? 964  ASP A CG  1 
ATOM   7796  O  OD1 . ASP A 1 964  ? 95.871  125.871 72.679  1.00 129.54 ? 964  ASP A OD1 1 
ATOM   7797  O  OD2 . ASP A 1 964  ? 94.939  125.691 74.659  1.00 131.38 ? 964  ASP A OD2 1 
ATOM   7798  N  N   . ALA A 1 965  ? 99.963  127.275 74.543  1.00 89.99  ? 965  ALA A N   1 
ATOM   7799  C  CA  . ALA A 1 965  ? 101.202 127.744 75.153  1.00 74.26  ? 965  ALA A CA  1 
ATOM   7800  C  C   . ALA A 1 965  ? 101.295 127.407 76.636  1.00 80.04  ? 965  ALA A C   1 
ATOM   7801  O  O   . ALA A 1 965  ? 102.402 127.206 77.150  1.00 86.82  ? 965  ALA A O   1 
ATOM   7802  C  CB  . ALA A 1 965  ? 101.344 129.255 74.950  1.00 80.19  ? 965  ALA A CB  1 
ATOM   7803  N  N   . SER A 1 966  ? 100.161 127.335 77.340  1.00 83.31  ? 966  SER A N   1 
ATOM   7804  C  CA  . SER A 1 966  ? 100.208 127.043 78.770  1.00 82.49  ? 966  SER A CA  1 
ATOM   7805  C  C   . SER A 1 966  ? 100.696 125.628 79.045  1.00 89.09  ? 966  SER A C   1 
ATOM   7806  O  O   . SER A 1 966  ? 101.416 125.398 80.026  1.00 89.55  ? 966  SER A O   1 
ATOM   7807  C  CB  . SER A 1 966  ? 98.826  127.250 79.391  1.00 87.47  ? 966  SER A CB  1 
ATOM   7808  O  OG  . SER A 1 966  ? 97.843  126.483 78.717  1.00 93.65  ? 966  SER A OG  1 
ATOM   7809  N  N   . ASP A 1 967  ? 100.346 124.678 78.175  1.00 93.96  ? 967  ASP A N   1 
ATOM   7810  C  CA  . ASP A 1 967  ? 100.857 123.321 78.313  1.00 84.92  ? 967  ASP A CA  1 
ATOM   7811  C  C   . ASP A 1 967  ? 102.367 123.284 78.154  1.00 70.78  ? 967  ASP A C   1 
ATOM   7812  O  O   . ASP A 1 967  ? 103.064 122.577 78.890  1.00 81.81  ? 967  ASP A O   1 
ATOM   7813  C  CB  . ASP A 1 967  ? 100.203 122.406 77.276  1.00 107.54 ? 967  ASP A CB  1 
ATOM   7814  C  CG  . ASP A 1 967  ? 98.692  122.434 77.341  1.00 125.13 ? 967  ASP A CG  1 
ATOM   7815  O  OD1 . ASP A 1 967  ? 98.139  122.229 78.441  1.00 121.55 ? 967  ASP A OD1 1 
ATOM   7816  O  OD2 . ASP A 1 967  ? 98.057  122.659 76.289  1.00 117.96 ? 967  ASP A OD2 1 
ATOM   7817  N  N   . PHE A 1 968  ? 102.889 124.054 77.201  1.00 69.67  ? 968  PHE A N   1 
ATOM   7818  C  CA  . PHE A 1 968  ? 104.326 124.081 76.978  1.00 74.82  ? 968  PHE A CA  1 
ATOM   7819  C  C   . PHE A 1 968  ? 105.053 124.809 78.109  1.00 76.58  ? 968  PHE A C   1 
ATOM   7820  O  O   . PHE A 1 968  ? 106.182 124.444 78.453  1.00 84.56  ? 968  PHE A O   1 
ATOM   7821  C  CB  . PHE A 1 968  ? 104.596 124.727 75.616  1.00 71.76  ? 968  PHE A CB  1 
ATOM   7822  C  CG  . PHE A 1 968  ? 106.044 124.790 75.229  1.00 76.22  ? 968  PHE A CG  1 
ATOM   7823  C  CD1 . PHE A 1 968  ? 106.945 123.847 75.698  1.00 79.79  ? 968  PHE A CD1 1 
ATOM   7824  C  CD2 . PHE A 1 968  ? 106.502 125.775 74.372  1.00 80.54  ? 968  PHE A CD2 1 
ATOM   7825  C  CE1 . PHE A 1 968  ? 108.272 123.894 75.337  1.00 87.68  ? 968  PHE A CE1 1 
ATOM   7826  C  CE2 . PHE A 1 968  ? 107.834 125.828 74.006  1.00 80.78  ? 968  PHE A CE2 1 
ATOM   7827  C  CZ  . PHE A 1 968  ? 108.719 124.886 74.490  1.00 79.60  ? 968  PHE A CZ  1 
ATOM   7828  N  N   . VAL A 1 969  ? 104.413 125.807 78.730  1.00 75.07  ? 969  VAL A N   1 
ATOM   7829  C  CA  . VAL A 1 969  ? 105.035 126.482 79.870  1.00 56.53  ? 969  VAL A CA  1 
ATOM   7830  C  C   . VAL A 1 969  ? 105.057 125.566 81.086  1.00 66.88  ? 969  VAL A C   1 
ATOM   7831  O  O   . VAL A 1 969  ? 106.018 125.563 81.865  1.00 76.46  ? 969  VAL A O   1 
ATOM   7832  C  CB  . VAL A 1 969  ? 104.327 127.809 80.171  1.00 76.58  ? 969  VAL A CB  1 
ATOM   7833  C  CG1 . VAL A 1 969  ? 104.892 128.446 81.435  1.00 61.55  ? 969  VAL A CG1 1 
ATOM   7834  C  CG2 . VAL A 1 969  ? 104.499 128.768 79.004  1.00 83.49  ? 969  VAL A CG2 1 
ATOM   7835  N  N   . MET A 1 970  ? 104.009 124.757 81.265  1.00 79.41  ? 970  MET A N   1 
ATOM   7836  C  CA  . MET A 1 970  ? 103.998 123.847 82.398  1.00 85.81  ? 970  MET A CA  1 
ATOM   7837  C  C   . MET A 1 970  ? 104.942 122.672 82.216  1.00 89.58  ? 970  MET A C   1 
ATOM   7838  O  O   . MET A 1 970  ? 105.360 122.079 83.210  1.00 87.48  ? 970  MET A O   1 
ATOM   7839  C  CB  . MET A 1 970  ? 102.591 123.297 82.670  1.00 97.57  ? 970  MET A CB  1 
ATOM   7840  C  CG  . MET A 1 970  ? 101.576 124.299 83.167  1.00 95.83  ? 970  MET A CG  1 
ATOM   7841  S  SD  . MET A 1 970  ? 99.995  123.467 83.417  1.00 125.91 ? 970  MET A SD  1 
ATOM   7842  C  CE  . MET A 1 970  ? 100.491 122.094 84.456  1.00 100.59 ? 970  MET A CE  1 
ATOM   7843  N  N   . ASN A 1 971  ? 105.312 122.322 80.976  1.00 89.67  ? 971  ASN A N   1 
ATOM   7844  C  CA  . ASN A 1 971  ? 106.133 121.151 80.765  1.00 79.70  ? 971  ASN A CA  1 
ATOM   7845  C  C   . ASN A 1 971  ? 107.287 121.629 79.877  1.00 72.67  ? 971  ASN A C   1 
ATOM   7846  O  O   . ASN A 1 971  ? 107.280 121.397 78.662  1.00 70.03  ? 971  ASN A O   1 
ATOM   7847  C  CB  . ASN A 1 971  ? 105.343 120.032 80.092  1.00 84.53  ? 971  ASN A CB  1 
ATOM   7848  C  CG  . ASN A 1 971  ? 105.725 118.686 80.653  1.00 120.00 ? 971  ASN A CG  1 
ATOM   7849  O  OD1 . ASN A 1 971  ? 106.083 118.650 81.839  1.00 111.95 ? 971  ASN A OD1 1 
ATOM   7850  N  ND2 . ASN A 1 971  ? 105.759 117.641 79.834  1.00 129.52 ? 971  ASN A ND2 1 
ATOM   7851  N  N   . PRO A 1 972  ? 108.281 122.329 80.446  1.00 71.59  ? 972  PRO A N   1 
ATOM   7852  C  CA  . PRO A 1 972  ? 109.296 122.993 79.606  1.00 71.96  ? 972  PRO A CA  1 
ATOM   7853  C  C   . PRO A 1 972  ? 110.132 122.073 78.725  1.00 83.60  ? 972  PRO A C   1 
ATOM   7854  O  O   . PRO A 1 972  ? 110.477 122.460 77.600  1.00 77.74  ? 972  PRO A O   1 
ATOM   7855  C  CB  . PRO A 1 972  ? 110.203 123.679 80.632  1.00 66.84  ? 972  PRO A CB  1 
ATOM   7856  C  CG  . PRO A 1 972  ? 109.396 123.797 81.839  1.00 70.35  ? 972  PRO A CG  1 
ATOM   7857  C  CD  . PRO A 1 972  ? 108.504 122.596 81.874  1.00 76.44  ? 972  PRO A CD  1 
ATOM   7858  N  N   . LEU A 1 973  ? 110.481 120.893 79.207  1.00 78.85  ? 973  LEU A N   1 
ATOM   7859  C  CA  . LEU A 1 973  ? 111.483 120.048 78.580  1.00 73.50  ? 973  LEU A CA  1 
ATOM   7860  C  C   . LEU A 1 973  ? 110.879 118.906 77.777  1.00 69.72  ? 973  LEU A C   1 
ATOM   7861  O  O   . LEU A 1 973  ? 111.623 118.079 77.241  1.00 72.09  ? 973  LEU A O   1 
ATOM   7862  C  CB  . LEU A 1 973  ? 112.428 119.482 79.646  1.00 77.17  ? 973  LEU A CB  1 
ATOM   7863  C  CG  . LEU A 1 973  ? 113.315 120.518 80.335  1.00 68.92  ? 973  LEU A CG  1 
ATOM   7864  C  CD1 . LEU A 1 973  ? 114.043 119.904 81.520  1.00 65.22  ? 973  LEU A CD1 1 
ATOM   7865  C  CD2 . LEU A 1 973  ? 114.304 121.100 79.333  1.00 78.21  ? 973  LEU A CD2 1 
ATOM   7866  N  N   . GLY A 1 974  ? 109.553 118.848 77.665  1.00 65.17  ? 974  GLY A N   1 
ATOM   7867  C  CA  . GLY A 1 974  ? 108.881 117.767 76.984  1.00 66.03  ? 974  GLY A CA  1 
ATOM   7868  C  C   . GLY A 1 974  ? 108.553 118.074 75.533  1.00 60.03  ? 974  GLY A C   1 
ATOM   7869  O  O   . GLY A 1 974  ? 108.930 119.105 74.971  1.00 62.46  ? 974  GLY A O   1 
ATOM   7870  N  N   . LEU A 1 975  ? 107.838 117.136 74.924  1.00 79.95  ? 975  LEU A N   1 
ATOM   7871  C  CA  . LEU A 1 975  ? 107.358 117.200 73.553  1.00 82.25  ? 975  LEU A CA  1 
ATOM   7872  C  C   . LEU A 1 975  ? 105.843 117.336 73.501  1.00 79.01  ? 975  LEU A C   1 
ATOM   7873  O  O   . LEU A 1 975  ? 105.135 117.171 74.498  1.00 78.44  ? 975  LEU A O   1 
ATOM   7874  C  CB  . LEU A 1 975  ? 107.786 115.950 72.776  1.00 82.68  ? 975  LEU A CB  1 
ATOM   7875  C  CG  . LEU A 1 975  ? 109.250 115.841 72.371  1.00 56.23  ? 975  LEU A CG  1 
ATOM   7876  C  CD1 . LEU A 1 975  ? 109.427 114.676 71.415  1.00 68.32  ? 975  LEU A CD1 1 
ATOM   7877  C  CD2 . LEU A 1 975  ? 109.698 117.142 71.721  1.00 75.99  ? 975  LEU A CD2 1 
ATOM   7878  N  N   . ASN A 1 976  ? 105.355 117.641 72.300  1.00 77.11  ? 976  ASN A N   1 
ATOM   7879  C  CA  . ASN A 1 976  ? 103.921 117.769 72.053  1.00 71.80  ? 976  ASN A CA  1 
ATOM   7880  C  C   . ASN A 1 976  ? 103.386 116.453 71.496  1.00 81.52  ? 976  ASN A C   1 
ATOM   7881  O  O   . ASN A 1 976  ? 102.975 116.341 70.340  1.00 89.75  ? 976  ASN A O   1 
ATOM   7882  C  CB  . ASN A 1 976  ? 103.643 118.919 71.090  1.00 82.91  ? 976  ASN A CB  1 
ATOM   7883  C  CG  . ASN A 1 976  ? 102.162 119.216 70.955  1.00 78.99  ? 976  ASN A CG  1 
ATOM   7884  O  OD1 . ASN A 1 976  ? 101.349 118.732 71.742  1.00 92.25  ? 976  ASN A OD1 1 
ATOM   7885  N  ND2 . ASN A 1 976  ? 101.800 119.976 69.929  1.00 82.89  ? 976  ASN A ND2 1 
ATOM   7886  N  N   . VAL A 1 977  ? 103.399 115.441 72.355  1.00 76.03  ? 977  VAL A N   1 
ATOM   7887  C  CA  . VAL A 1 977  ? 102.889 114.117 72.030  1.00 83.69  ? 977  VAL A CA  1 
ATOM   7888  C  C   . VAL A 1 977  ? 101.728 113.826 72.968  1.00 94.60  ? 977  VAL A C   1 
ATOM   7889  O  O   . VAL A 1 977  ? 101.831 114.092 74.167  1.00 95.15  ? 977  VAL A O   1 
ATOM   7890  C  CB  . VAL A 1 977  ? 103.969 113.026 72.146  1.00 70.97  ? 977  VAL A CB  1 
ATOM   7891  C  CG1 . VAL A 1 977  ? 104.928 113.112 70.968  1.00 68.96  ? 977  VAL A CG1 1 
ATOM   7892  C  CG2 . VAL A 1 977  ? 104.750 113.182 73.443  1.00 75.50  ? 977  VAL A CG2 1 
ATOM   7893  N  N   . PRO A 1 978  ? 100.601 113.318 72.468  1.00 87.66  ? 978  PRO A N   1 
ATOM   7894  C  CA  . PRO A 1 978  ? 99.461  113.046 73.358  1.00 89.93  ? 978  PRO A CA  1 
ATOM   7895  C  C   . PRO A 1 978  ? 99.730  111.976 74.404  1.00 91.95  ? 978  PRO A C   1 
ATOM   7896  O  O   . PRO A 1 978  ? 99.137  112.022 75.488  1.00 95.27  ? 978  PRO A O   1 
ATOM   7897  C  CB  . PRO A 1 978  ? 98.350  112.621 72.386  1.00 89.78  ? 978  PRO A CB  1 
ATOM   7898  C  CG  . PRO A 1 978  ? 99.062  112.193 71.137  1.00 98.98  ? 978  PRO A CG  1 
ATOM   7899  C  CD  . PRO A 1 978  ? 100.290 113.041 71.054  1.00 88.54  ? 978  PRO A CD  1 
ATOM   7900  N  N   . GLY A 1 979  ? 100.612 111.011 74.117  1.00 81.14  ? 979  GLY A N   1 
ATOM   7901  C  CA  . GLY A 1 979  ? 100.803 109.877 75.010  1.00 82.92  ? 979  GLY A CA  1 
ATOM   7902  C  C   . GLY A 1 979  ? 101.612 110.153 76.259  1.00 97.43  ? 979  GLY A C   1 
ATOM   7903  O  O   . GLY A 1 979  ? 101.517 109.380 77.221  1.00 90.70  ? 979  GLY A O   1 
ATOM   7904  N  N   . SER A 1 980  ? 102.394 111.235 76.273  1.00 95.09  ? 980  SER A N   1 
ATOM   7905  C  CA  . SER A 1 980  ? 103.233 111.546 77.422  1.00 82.36  ? 980  SER A CA  1 
ATOM   7906  C  C   . SER A 1 980  ? 102.532 112.409 78.454  1.00 88.40  ? 980  SER A C   1 
ATOM   7907  O  O   . SER A 1 980  ? 103.145 112.765 79.466  1.00 97.64  ? 980  SER A O   1 
ATOM   7908  C  CB  . SER A 1 980  ? 104.509 112.284 76.985  1.00 83.11  ? 980  SER A CB  1 
ATOM   7909  O  OG  . SER A 1 980  ? 104.179 113.587 76.559  1.00 81.60  ? 980  SER A OG  1 
ATOM   7910  N  N   . LYS A 1 981  ? 101.277 112.751 78.244  1.00 94.16  ? 981  LYS A N   1 
ATOM   7911  C  CA  . LYS A 1 981  ? 100.592 113.692 79.117  1.00 95.63  ? 981  LYS A CA  1 
ATOM   7912  C  C   . LYS A 1 981  ? 99.975  112.898 80.263  1.00 96.06  ? 981  LYS A C   1 
ATOM   7913  O  O   . LYS A 1 981  ? 99.467  111.781 80.068  1.00 100.13 ? 981  LYS A O   1 
ATOM   7914  C  CB  . LYS A 1 981  ? 99.460  114.372 78.406  1.00 99.93  ? 981  LYS A CB  1 
ATOM   7915  C  CG  . LYS A 1 981  ? 98.752  115.460 79.170  1.00 110.82 ? 981  LYS A CG  1 
ATOM   7916  C  CD  . LYS A 1 981  ? 97.736  115.949 78.135  1.00 120.87 ? 981  LYS A CD  1 
ATOM   7917  C  CE  . LYS A 1 981  ? 98.438  116.672 76.952  1.00 121.18 ? 981  LYS A CE  1 
ATOM   7918  N  NZ  . LYS A 1 981  ? 97.271  117.074 76.026  1.00 117.65 ? 981  LYS A NZ  1 
ATOM   7919  N  N   . GLU A 1 982  ? 100.025 113.459 81.465  1.00 106.17 ? 982  GLU A N   1 
ATOM   7920  C  CA  . GLU A 1 982  ? 99.516  112.757 82.635  1.00 112.94 ? 982  GLU A CA  1 
ATOM   7921  C  C   . GLU A 1 982  ? 97.995  112.880 82.722  1.00 119.71 ? 982  GLU A C   1 
ATOM   7922  O  O   . GLU A 1 982  ? 97.377  113.723 82.070  1.00 119.22 ? 982  GLU A O   1 
ATOM   7923  C  CB  . GLU A 1 982  ? 100.163 113.315 83.905  1.00 118.49 ? 982  GLU A CB  1 
ATOM   7924  C  CG  . GLU A 1 982  ? 101.653 113.117 83.958  1.00 117.04 ? 982  GLU A CG  1 
ATOM   7925  C  CD  . GLU A 1 982  ? 102.259 113.608 85.253  1.00 143.45 ? 982  GLU A CD  1 
ATOM   7926  O  OE1 . GLU A 1 982  ? 101.507 114.133 86.101  1.00 139.56 ? 982  GLU A OE1 1 
ATOM   7927  O  OE2 . GLU A 1 982  ? 103.489 113.480 85.418  1.00 148.51 ? 982  GLU A OE2 1 
ATOM   7928  N  N   . ILE A 1 983  ? 97.395  112.006 83.535  1.00 109.92 ? 983  ILE A N   1 
ATOM   7929  C  CA  . ILE A 1 983  ? 95.932  111.906 83.575  1.00 106.66 ? 983  ILE A CA  1 
ATOM   7930  C  C   . ILE A 1 983  ? 95.290  113.032 84.388  1.00 114.54 ? 983  ILE A C   1 
ATOM   7931  O  O   . ILE A 1 983  ? 94.138  113.405 84.131  1.00 115.10 ? 983  ILE A O   1 
ATOM   7932  C  CB  . ILE A 1 983  ? 95.490  110.531 84.115  1.00 94.78  ? 983  ILE A CB  1 
ATOM   7933  C  CG1 . ILE A 1 983  ? 94.024  110.268 83.752  1.00 95.23  ? 983  ILE A CG1 1 
ATOM   7934  C  CG2 . ILE A 1 983  ? 95.687  110.446 85.632  1.00 102.04 ? 983  ILE A CG2 1 
ATOM   7935  C  CD1 . ILE A 1 983  ? 93.592  108.832 83.927  1.00 108.45 ? 983  ILE A CD1 1 
ATOM   7936  N  N   . ILE A 1 984  ? 96.005  113.595 85.364  1.00 114.18 ? 984  ILE A N   1 
ATOM   7937  C  CA  . ILE A 1 984  ? 95.420  114.627 86.216  1.00 122.07 ? 984  ILE A CA  1 
ATOM   7938  C  C   . ILE A 1 984  ? 95.013  115.851 85.401  1.00 115.23 ? 984  ILE A C   1 
ATOM   7939  O  O   . ILE A 1 984  ? 94.043  116.549 85.742  1.00 116.85 ? 984  ILE A O   1 
ATOM   7940  C  CB  . ILE A 1 984  ? 96.403  114.992 87.346  1.00 130.48 ? 984  ILE A CB  1 
ATOM   7941  C  CG1 . ILE A 1 984  ? 95.691  115.826 88.404  1.00 145.21 ? 984  ILE A CG1 1 
ATOM   7942  C  CG2 . ILE A 1 984  ? 97.633  115.719 86.802  1.00 117.62 ? 984  ILE A CG2 1 
ATOM   7943  C  CD1 . ILE A 1 984  ? 94.606  115.068 89.138  1.00 149.87 ? 984  ILE A CD1 1 
ATOM   7944  N  N   . THR A 1 985  ? 95.738  116.126 84.313  1.00 102.75 ? 985  THR A N   1 
ATOM   7945  C  CA  . THR A 1 985  ? 95.435  117.260 83.451  1.00 111.95 ? 985  THR A CA  1 
ATOM   7946  C  C   . THR A 1 985  ? 94.067  117.149 82.792  1.00 105.20 ? 985  THR A C   1 
ATOM   7947  O  O   . THR A 1 985  ? 93.550  118.156 82.297  1.00 105.65 ? 985  THR A O   1 
ATOM   7948  C  CB  . THR A 1 985  ? 96.516  117.389 82.376  1.00 113.19 ? 985  THR A CB  1 
ATOM   7949  O  OG1 . THR A 1 985  ? 96.350  116.349 81.404  1.00 114.15 ? 985  THR A OG1 1 
ATOM   7950  C  CG2 . THR A 1 985  ? 97.901  117.260 82.998  1.00 102.71 ? 985  THR A CG2 1 
ATOM   7951  N  N   . PHE A 1 986  ? 93.463  115.959 82.778  1.00 104.31 ? 986  PHE A N   1 
ATOM   7952  C  CA  . PHE A 1 986  ? 92.117  115.814 82.239  1.00 112.43 ? 986  PHE A CA  1 
ATOM   7953  C  C   . PHE A 1 986  ? 91.029  116.053 83.280  1.00 103.17 ? 986  PHE A C   1 
ATOM   7954  O  O   . PHE A 1 986  ? 89.882  116.320 82.904  1.00 92.84  ? 986  PHE A O   1 
ATOM   7955  C  CB  . PHE A 1 986  ? 91.943  114.415 81.635  1.00 130.93 ? 986  PHE A CB  1 
ATOM   7956  C  CG  . PHE A 1 986  ? 92.968  114.073 80.587  1.00 129.70 ? 986  PHE A CG  1 
ATOM   7957  C  CD1 . PHE A 1 986  ? 94.125  113.390 80.929  1.00 114.66 ? 986  PHE A CD1 1 
ATOM   7958  C  CD2 . PHE A 1 986  ? 92.780  114.435 79.262  1.00 127.95 ? 986  PHE A CD2 1 
ATOM   7959  C  CE1 . PHE A 1 986  ? 95.072  113.073 79.974  1.00 103.61 ? 986  PHE A CE1 1 
ATOM   7960  C  CE2 . PHE A 1 986  ? 93.727  114.120 78.301  1.00 110.92 ? 986  PHE A CE2 1 
ATOM   7961  C  CZ  . PHE A 1 986  ? 94.873  113.439 78.658  1.00 95.50  ? 986  PHE A CZ  1 
ATOM   7962  N  N   . LEU A 1 987  ? 91.361  115.974 84.570  1.00 106.38 ? 987  LEU A N   1 
ATOM   7963  C  CA  . LEU A 1 987  ? 90.403  116.195 85.648  1.00 107.30 ? 987  LEU A CA  1 
ATOM   7964  C  C   . LEU A 1 987  ? 90.501  117.587 86.251  1.00 105.37 ? 987  LEU A C   1 
ATOM   7965  O  O   . LEU A 1 987  ? 89.582  118.004 86.975  1.00 107.00 ? 987  LEU A O   1 
ATOM   7966  C  CB  . LEU A 1 987  ? 90.594  115.158 86.760  1.00 114.15 ? 987  LEU A CB  1 
ATOM   7967  C  CG  . LEU A 1 987  ? 90.705  113.703 86.315  1.00 114.46 ? 987  LEU A CG  1 
ATOM   7968  C  CD1 . LEU A 1 987  ? 90.661  112.793 87.526  1.00 118.24 ? 987  LEU A CD1 1 
ATOM   7969  C  CD2 . LEU A 1 987  ? 89.576  113.366 85.351  1.00 110.06 ? 987  LEU A CD2 1 
ATOM   7970  N  N   . ARG A 1 988  ? 91.619  118.276 86.014  1.00 101.88 ? 988  ARG A N   1 
ATOM   7971  C  CA  . ARG A 1 988  ? 91.832  119.583 86.622  1.00 97.44  ? 988  ARG A CA  1 
ATOM   7972  C  C   . ARG A 1 988  ? 90.681  120.536 86.300  1.00 103.76 ? 988  ARG A C   1 
ATOM   7973  O  O   . ARG A 1 988  ? 90.238  121.301 87.168  1.00 107.27 ? 988  ARG A O   1 
ATOM   7974  C  CB  . ARG A 1 988  ? 93.172  120.147 86.150  1.00 93.53  ? 988  ARG A CB  1 
ATOM   7975  C  CG  . ARG A 1 988  ? 94.009  120.771 87.251  1.00 88.75  ? 988  ARG A CG  1 
ATOM   7976  C  CD  . ARG A 1 988  ? 95.153  121.588 86.675  1.00 110.38 ? 988  ARG A CD  1 
ATOM   7977  N  NE  . ARG A 1 988  ? 96.129  120.746 85.985  1.00 115.81 ? 988  ARG A NE  1 
ATOM   7978  C  CZ  . ARG A 1 988  ? 97.148  120.134 86.579  1.00 110.30 ? 988  ARG A CZ  1 
ATOM   7979  N  NH1 . ARG A 1 988  ? 97.333  120.262 87.887  1.00 117.28 ? 988  ARG A NH1 1 
ATOM   7980  N  NH2 . ARG A 1 988  ? 97.984  119.390 85.867  1.00 98.18  ? 988  ARG A NH2 1 
ATOM   7981  N  N   . GLN A 1 989  ? 90.240  120.557 85.037  1.00 100.87 ? 989  GLN A N   1 
ATOM   7982  C  CA  . GLN A 1 989  ? 89.147  121.439 84.630  1.00 110.92 ? 989  GLN A CA  1 
ATOM   7983  C  C   . GLN A 1 989  ? 87.867  121.177 85.422  1.00 114.49 ? 989  GLN A C   1 
ATOM   7984  O  O   . GLN A 1 989  ? 87.184  122.122 85.854  1.00 125.38 ? 989  GLN A O   1 
ATOM   7985  C  CB  . GLN A 1 989  ? 88.882  121.256 83.136  1.00 120.34 ? 989  GLN A CB  1 
ATOM   7986  C  CG  . GLN A 1 989  ? 87.624  121.937 82.642  1.00 127.70 ? 989  GLN A CG  1 
ATOM   7987  C  CD  . GLN A 1 989  ? 87.868  123.358 82.198  1.00 140.93 ? 989  GLN A CD  1 
ATOM   7988  O  OE1 . GLN A 1 989  ? 88.676  124.075 82.787  1.00 140.12 ? 989  GLN A OE1 1 
ATOM   7989  N  NE2 . GLN A 1 989  ? 87.159  123.782 81.159  1.00 140.88 ? 989  GLN A NE2 1 
ATOM   7990  N  N   . THR A 1 990  ? 87.595  119.907 85.737  1.00 102.90 ? 990  THR A N   1 
ATOM   7991  C  CA  . THR A 1 990  ? 86.420  119.596 86.543  1.00 104.10 ? 990  THR A CA  1 
ATOM   7992  C  C   . THR A 1 990  ? 86.616  120.098 87.960  1.00 109.42 ? 990  THR A C   1 
ATOM   7993  O  O   . THR A 1 990  ? 85.675  120.620 88.579  1.00 112.39 ? 990  THR A O   1 
ATOM   7994  C  CB  . THR A 1 990  ? 86.137  118.093 86.538  1.00 95.95  ? 990  THR A CB  1 
ATOM   7995  O  OG1 . THR A 1 990  ? 87.076  117.424 87.387  1.00 101.33 ? 990  THR A OG1 1 
ATOM   7996  C  CG2 . THR A 1 990  ? 86.244  117.528 85.127  1.00 117.32 ? 990  THR A CG2 1 
ATOM   7997  N  N   . VAL A 1 991  ? 87.809  119.876 88.514  1.00 99.82  ? 991  VAL A N   1 
ATOM   7998  C  CA  . VAL A 1 991  ? 88.049  120.292 89.890  1.00 89.50  ? 991  VAL A CA  1 
ATOM   7999  C  C   . VAL A 1 991  ? 87.815  121.792 90.014  1.00 92.02  ? 991  VAL A C   1 
ATOM   8000  O  O   . VAL A 1 991  ? 87.133  122.263 90.933  1.00 101.88 ? 991  VAL A O   1 
ATOM   8001  C  CB  . VAL A 1 991  ? 89.472  119.904 90.335  1.00 87.56  ? 991  VAL A CB  1 
ATOM   8002  C  CG1 . VAL A 1 991  ? 89.746  120.423 91.739  1.00 84.03  ? 991  VAL A CG1 1 
ATOM   8003  C  CG2 . VAL A 1 991  ? 89.656  118.395 90.277  1.00 112.12 ? 991  VAL A CG2 1 
ATOM   8004  N  N   . ARG A 1 992  ? 88.427  122.567 89.109  1.00 88.95  ? 992  ARG A N   1 
ATOM   8005  C  CA  . ARG A 1 992  ? 88.214  124.012 89.091  1.00 90.57  ? 992  ARG A CA  1 
ATOM   8006  C  C   . ARG A 1 992  ? 86.734  124.376 89.025  1.00 89.96  ? 992  ARG A C   1 
ATOM   8007  O  O   . ARG A 1 992  ? 86.269  125.284 89.736  1.00 100.85 ? 992  ARG A O   1 
ATOM   8008  C  CB  . ARG A 1 992  ? 88.958  124.639 87.915  1.00 95.90  ? 992  ARG A CB  1 
ATOM   8009  C  CG  . ARG A 1 992  ? 88.845  126.149 87.872  1.00 108.92 ? 992  ARG A CG  1 
ATOM   8010  C  CD  . ARG A 1 992  ? 89.643  126.704 86.724  1.00 125.75 ? 992  ARG A CD  1 
ATOM   8011  N  NE  . ARG A 1 992  ? 91.069  126.493 86.941  1.00 135.88 ? 992  ARG A NE  1 
ATOM   8012  C  CZ  . ARG A 1 992  ? 92.002  126.714 86.025  1.00 140.64 ? 992  ARG A CZ  1 
ATOM   8013  N  NH1 . ARG A 1 992  ? 91.660  127.151 84.821  1.00 144.15 ? 992  ARG A NH1 1 
ATOM   8014  N  NH2 . ARG A 1 992  ? 93.278  126.492 86.311  1.00 136.75 ? 992  ARG A NH2 1 
ATOM   8015  N  N   . GLU A 1 993  ? 85.970  123.676 88.174  1.00 100.72 ? 993  GLU A N   1 
ATOM   8016  C  CA  . GLU A 1 993  ? 84.550  123.996 88.089  1.00 107.94 ? 993  GLU A CA  1 
ATOM   8017  C  C   . GLU A 1 993  ? 83.853  123.774 89.425  1.00 102.07 ? 993  GLU A C   1 
ATOM   8018  O  O   . GLU A 1 993  ? 83.075  124.622 89.876  1.00 102.97 ? 993  GLU A O   1 
ATOM   8019  C  CB  . GLU A 1 993  ? 83.869  123.195 86.980  1.00 122.33 ? 993  GLU A CB  1 
ATOM   8020  C  CG  . GLU A 1 993  ? 84.204  123.688 85.583  1.00 126.79 ? 993  GLU A CG  1 
ATOM   8021  C  CD  . GLU A 1 993  ? 83.644  122.794 84.499  1.00 145.73 ? 993  GLU A CD  1 
ATOM   8022  O  OE1 . GLU A 1 993  ? 82.801  121.928 84.819  1.00 137.83 ? 993  GLU A OE1 1 
ATOM   8023  O  OE2 . GLU A 1 993  ? 84.036  122.964 83.325  1.00 142.12 ? 993  GLU A OE2 1 
ATOM   8024  N  N   . ASN A 1 994  ? 84.114  122.634 90.076  1.00 96.12  ? 994  ASN A N   1 
ATOM   8025  C  CA  . ASN A 1 994  ? 83.485  122.409 91.376  1.00 98.32  ? 994  ASN A CA  1 
ATOM   8026  C  C   . ASN A 1 994  ? 83.912  123.455 92.399  1.00 101.32 ? 994  ASN A C   1 
ATOM   8027  O  O   . ASN A 1 994  ? 83.123  123.823 93.282  1.00 108.62 ? 994  ASN A O   1 
ATOM   8028  C  CB  . ASN A 1 994  ? 83.821  121.011 91.897  1.00 106.21 ? 994  ASN A CB  1 
ATOM   8029  C  CG  . ASN A 1 994  ? 83.009  119.927 91.225  1.00 118.18 ? 994  ASN A CG  1 
ATOM   8030  O  OD1 . ASN A 1 994  ? 81.982  119.492 91.747  1.00 131.48 ? 994  ASN A OD1 1 
ATOM   8031  N  ND2 . ASN A 1 994  ? 83.466  119.478 90.064  1.00 120.29 ? 994  ASN A ND2 1 
ATOM   8032  N  N   . ILE A 1 995  ? 85.158  123.932 92.302  1.00 99.20  ? 995  ILE A N   1 
ATOM   8033  C  CA  . ILE A 1 995  ? 85.631  124.961 93.225  1.00 89.09  ? 995  ILE A CA  1 
ATOM   8034  C  C   . ILE A 1 995  ? 84.824  126.234 93.046  1.00 86.00  ? 995  ILE A C   1 
ATOM   8035  O  O   . ILE A 1 995  ? 84.509  126.927 94.021  1.00 87.30  ? 995  ILE A O   1 
ATOM   8036  C  CB  . ILE A 1 995  ? 87.141  125.218 93.049  1.00 91.72  ? 995  ILE A CB  1 
ATOM   8037  C  CG1 . ILE A 1 995  ? 87.947  124.120 93.737  1.00 91.72  ? 995  ILE A CG1 1 
ATOM   8038  C  CG2 . ILE A 1 995  ? 87.529  126.569 93.640  1.00 74.58  ? 995  ILE A CG2 1 
ATOM   8039  C  CD1 . ILE A 1 995  ? 89.430  124.387 93.752  1.00 100.36 ? 995  ILE A CD1 1 
ATOM   8040  N  N   . THR A 1 996  ? 84.421  126.529 91.812  1.00 90.48  ? 996  THR A N   1 
ATOM   8041  C  CA  . THR A 1 996  ? 83.677  127.763 91.584  1.00 90.35  ? 996  THR A CA  1 
ATOM   8042  C  C   . THR A 1 996  ? 82.186  127.595 91.886  1.00 90.99  ? 996  THR A C   1 
ATOM   8043  O  O   . THR A 1 996  ? 81.415  128.551 91.754  1.00 89.46  ? 996  THR A O   1 
ATOM   8044  C  CB  . THR A 1 996  ? 83.917  128.228 90.134  1.00 102.65 ? 996  THR A CB  1 
ATOM   8045  O  OG1 . THR A 1 996  ? 85.327  128.358 89.915  1.00 96.52  ? 996  THR A OG1 1 
ATOM   8046  C  CG2 . THR A 1 996  ? 83.283  129.590 89.838  1.00 104.88 ? 996  THR A CG2 1 
ATOM   8047  N  N   . ILE A 1 997  ? 81.778  126.427 92.374  1.00 103.99 ? 997  ILE A N   1 
ATOM   8048  C  CA  . ILE A 1 997  ? 80.389  126.146 92.712  1.00 107.47 ? 997  ILE A CA  1 
ATOM   8049  C  C   . ILE A 1 997  ? 80.199  126.012 94.219  1.00 100.49 ? 997  ILE A C   1 
ATOM   8050  O  O   . ILE A 1 997  ? 79.289  126.612 94.795  1.00 93.52  ? 997  ILE A O   1 
ATOM   8051  C  CB  . ILE A 1 997  ? 79.877  124.886 91.978  1.00 112.34 ? 997  ILE A CB  1 
ATOM   8052  C  CG1 . ILE A 1 997  ? 79.884  125.110 90.466  1.00 118.01 ? 997  ILE A CG1 1 
ATOM   8053  C  CG2 . ILE A 1 997  ? 78.476  124.523 92.458  1.00 103.60 ? 997  ILE A CG2 1 
ATOM   8054  C  CD1 . ILE A 1 997  ? 79.646  123.851 89.667  1.00 118.87 ? 997  ILE A CD1 1 
ATOM   8055  N  N   . THR A 1 998  ? 81.064  125.241 94.875  1.00 105.58 ? 998  THR A N   1 
ATOM   8056  C  CA  . THR A 1 998  ? 80.857  124.845 96.263  1.00 100.72 ? 998  THR A CA  1 
ATOM   8057  C  C   . THR A 1 998  ? 81.684  125.645 97.265  1.00 98.74  ? 998  THR A C   1 
ATOM   8058  O  O   . THR A 1 998  ? 81.791  125.232 98.424  1.00 105.33 ? 998  THR A O   1 
ATOM   8059  C  CB  . THR A 1 998  ? 81.171  123.358 96.430  1.00 117.74 ? 998  THR A CB  1 
ATOM   8060  O  OG1 . THR A 1 998  ? 82.553  123.127 96.129  1.00 105.20 ? 998  THR A OG1 1 
ATOM   8061  C  CG2 . THR A 1 998  ? 80.318  122.528 95.484  1.00 125.30 ? 998  THR A CG2 1 
ATOM   8062  N  N   . SER A 1 999  ? 82.266  126.769 96.864  1.00 98.47  ? 999  SER A N   1 
ATOM   8063  C  CA  . SER A 1 999  ? 83.151  127.527 97.739  1.00 95.63  ? 999  SER A CA  1 
ATOM   8064  C  C   . SER A 1 999  ? 82.472  128.799 98.229  1.00 99.97  ? 999  SER A C   1 
ATOM   8065  O  O   . SER A 1 999  ? 81.888  129.545 97.436  1.00 101.02 ? 999  SER A O   1 
ATOM   8066  C  CB  . SER A 1 999  ? 84.459  127.883 97.030  1.00 92.76  ? 999  SER A CB  1 
ATOM   8067  O  OG  . SER A 1 999  ? 85.260  128.724 97.841  1.00 83.75  ? 999  SER A OG  1 
ATOM   8068  N  N   . GLN A 1 1000 ? 82.557  129.035 99.537  1.00 95.05  ? 1000 GLN A N   1 
ATOM   8069  C  CA  . GLN A 1 1000 ? 82.189  130.306 100.137 1.00 89.09  ? 1000 GLN A CA  1 
ATOM   8070  C  C   . GLN A 1 1000 ? 83.373  131.016 100.764 1.00 93.35  ? 1000 GLN A C   1 
ATOM   8071  O  O   . GLN A 1 1000 ? 83.218  132.158 101.215 1.00 100.47 ? 1000 GLN A O   1 
ATOM   8072  C  CB  . GLN A 1 1000 ? 81.096  130.130 101.201 1.00 89.00  ? 1000 GLN A CB  1 
ATOM   8073  C  CG  . GLN A 1 1000 ? 79.746  129.756 100.638 1.00 108.11 ? 1000 GLN A CG  1 
ATOM   8074  C  CD  . GLN A 1 1000 ? 79.065  128.687 101.455 1.00 115.40 ? 1000 GLN A CD  1 
ATOM   8075  O  OE1 . GLN A 1 1000 ? 79.630  128.175 102.420 1.00 110.69 ? 1000 GLN A OE1 1 
ATOM   8076  N  NE2 . GLN A 1 1000 ? 77.841  128.344 101.077 1.00 125.71 ? 1000 GLN A NE2 1 
ATOM   8077  N  N   . ASN A 1 1001 ? 84.536  130.371 100.829 1.00 87.89  ? 1001 ASN A N   1 
ATOM   8078  C  CA  . ASN A 1 1001 ? 85.698  130.995 101.440 1.00 90.96  ? 1001 ASN A CA  1 
ATOM   8079  C  C   . ASN A 1 1001 ? 86.054  132.243 100.650 1.00 96.50  ? 1001 ASN A C   1 
ATOM   8080  O  O   . ASN A 1 1001 ? 86.087  132.225 99.416  1.00 101.24 ? 1001 ASN A O   1 
ATOM   8081  C  CB  . ASN A 1 1001 ? 86.879  130.024 101.474 1.00 85.47  ? 1001 ASN A CB  1 
ATOM   8082  C  CG  . ASN A 1 1001 ? 87.975  130.469 102.427 1.00 92.89  ? 1001 ASN A CG  1 
ATOM   8083  O  OD1 . ASN A 1 1001 ? 88.232  131.663 102.584 1.00 92.21  ? 1001 ASN A OD1 1 
ATOM   8084  N  ND2 . ASN A 1 1001 ? 88.625  129.506 103.071 1.00 89.55  ? 1001 ASN A ND2 1 
ATOM   8085  N  N   . ARG A 1 1002 ? 86.327  133.332 101.366 1.00 92.38  ? 1002 ARG A N   1 
ATOM   8086  C  CA  . ARG A 1 1002 ? 86.623  134.588 100.689 1.00 88.51  ? 1002 ARG A CA  1 
ATOM   8087  C  C   . ARG A 1 1002 ? 87.988  134.539 100.019 1.00 88.60  ? 1002 ARG A C   1 
ATOM   8088  O  O   . ARG A 1 1002 ? 88.164  135.083 98.923  1.00 93.80  ? 1002 ARG A O   1 
ATOM   8089  C  CB  . ARG A 1 1002 ? 86.544  135.744 101.685 1.00 115.51 ? 1002 ARG A CB  1 
ATOM   8090  C  CG  . ARG A 1 1002 ? 86.661  137.114 101.055 1.00 129.83 ? 1002 ARG A CG  1 
ATOM   8091  C  CD  . ARG A 1 1002 ? 86.905  138.172 102.113 1.00 145.57 ? 1002 ARG A CD  1 
ATOM   8092  N  NE  . ARG A 1 1002 ? 87.796  137.684 103.162 1.00 138.94 ? 1002 ARG A NE  1 
ATOM   8093  C  CZ  . ARG A 1 1002 ? 89.091  137.971 103.234 1.00 128.91 ? 1002 ARG A CZ  1 
ATOM   8094  N  NH1 . ARG A 1 1002 ? 89.649  138.750 102.318 1.00 125.40 ? 1002 ARG A NH1 1 
ATOM   8095  N  NH2 . ARG A 1 1002 ? 89.828  137.484 104.222 1.00 113.57 ? 1002 ARG A NH2 1 
ATOM   8096  N  N   . ILE A 1 1003 ? 88.964  133.891 100.658 1.00 89.25  ? 1003 ILE A N   1 
ATOM   8097  C  CA  . ILE A 1 1003 ? 90.299  133.792 100.071 1.00 84.65  ? 1003 ILE A CA  1 
ATOM   8098  C  C   . ILE A 1 1003 ? 90.239  133.031 98.751  1.00 93.38  ? 1003 ILE A C   1 
ATOM   8099  O  O   . ILE A 1 1003 ? 90.800  133.464 97.736  1.00 92.88  ? 1003 ILE A O   1 
ATOM   8100  C  CB  . ILE A 1 1003 ? 91.272  133.124 101.060 1.00 81.90  ? 1003 ILE A CB  1 
ATOM   8101  C  CG1 . ILE A 1 1003 ? 91.429  133.981 102.314 1.00 98.15  ? 1003 ILE A CG1 1 
ATOM   8102  C  CG2 . ILE A 1 1003 ? 92.625  132.862 100.404 1.00 92.83  ? 1003 ILE A CG2 1 
ATOM   8103  C  CD1 . ILE A 1 1003 ? 92.144  135.289 102.071 1.00 100.13 ? 1003 ILE A CD1 1 
ATOM   8104  N  N   . ILE A 1 1004 ? 89.536  131.896 98.743  1.00 97.05  ? 1004 ILE A N   1 
ATOM   8105  C  CA  . ILE A 1 1004 ? 89.441  131.085 97.532  1.00 76.41  ? 1004 ILE A CA  1 
ATOM   8106  C  C   . ILE A 1 1004 ? 88.653  131.819 96.454  1.00 80.55  ? 1004 ILE A C   1 
ATOM   8107  O  O   . ILE A 1 1004 ? 89.043  131.826 95.280  1.00 92.29  ? 1004 ILE A O   1 
ATOM   8108  C  CB  . ILE A 1 1004 ? 88.829  129.711 97.858  1.00 80.01  ? 1004 ILE A CB  1 
ATOM   8109  C  CG1 . ILE A 1 1004 ? 89.793  128.916 98.736  1.00 79.19  ? 1004 ILE A CG1 1 
ATOM   8110  C  CG2 . ILE A 1 1004 ? 88.537  128.935 96.583  1.00 86.25  ? 1004 ILE A CG2 1 
ATOM   8111  C  CD1 . ILE A 1 1004 ? 91.118  128.624 98.068  1.00 75.14  ? 1004 ILE A CD1 1 
ATOM   8112  N  N   . ASN A 1 1005 ? 87.531  132.444 96.827  1.00 73.07  ? 1005 ASN A N   1 
ATOM   8113  C  CA  . ASN A 1 1005 ? 86.727  133.158 95.840  1.00 76.93  ? 1005 ASN A CA  1 
ATOM   8114  C  C   . ASN A 1 1005 ? 87.491  134.334 95.248  1.00 85.82  ? 1005 ASN A C   1 
ATOM   8115  O  O   . ASN A 1 1005 ? 87.303  134.669 94.072  1.00 87.75  ? 1005 ASN A O   1 
ATOM   8116  C  CB  . ASN A 1 1005 ? 85.418  133.643 96.465  1.00 88.27  ? 1005 ASN A CB  1 
ATOM   8117  C  CG  . ASN A 1 1005 ? 84.500  132.503 96.857  1.00 100.55 ? 1005 ASN A CG  1 
ATOM   8118  O  OD1 . ASN A 1 1005 ? 84.711  131.357 96.463  1.00 101.57 ? 1005 ASN A OD1 1 
ATOM   8119  N  ND2 . ASN A 1 1005 ? 83.466  132.816 97.629  1.00 99.52  ? 1005 ASN A ND2 1 
ATOM   8120  N  N   . SER A 1 1006 ? 88.363  134.966 96.039  1.00 89.74  ? 1006 SER A N   1 
ATOM   8121  C  CA  . SER A 1 1006 ? 89.158  136.068 95.516  1.00 89.23  ? 1006 SER A CA  1 
ATOM   8122  C  C   . SER A 1 1006 ? 90.301  135.579 94.647  1.00 82.52  ? 1006 SER A C   1 
ATOM   8123  O  O   . SER A 1 1006 ? 90.676  136.248 93.681  1.00 86.73  ? 1006 SER A O   1 
ATOM   8124  C  CB  . SER A 1 1006 ? 89.726  136.898 96.669  1.00 95.46  ? 1006 SER A CB  1 
ATOM   8125  O  OG  . SER A 1 1006 ? 90.844  137.657 96.240  1.00 94.19  ? 1006 SER A OG  1 
ATOM   8126  N  N   . LEU A 1 1007 ? 90.874  134.424 94.978  1.00 81.83  ? 1007 LEU A N   1 
ATOM   8127  C  CA  . LEU A 1 1007 ? 91.936  133.876 94.150  1.00 80.42  ? 1007 LEU A CA  1 
ATOM   8128  C  C   . LEU A 1 1007 ? 91.388  133.328 92.841  1.00 79.36  ? 1007 LEU A C   1 
ATOM   8129  O  O   . LEU A 1 1007 ? 91.947  133.591 91.768  1.00 88.28  ? 1007 LEU A O   1 
ATOM   8130  C  CB  . LEU A 1 1007 ? 92.698  132.781 94.891  1.00 83.62  ? 1007 LEU A CB  1 
ATOM   8131  C  CG  . LEU A 1 1007 ? 93.918  132.209 94.153  1.00 67.27  ? 1007 LEU A CG  1 
ATOM   8132  C  CD1 . LEU A 1 1007 ? 94.867  133.317 93.714  1.00 65.90  ? 1007 LEU A CD1 1 
ATOM   8133  C  CD2 . LEU A 1 1007 ? 94.639  131.175 95.007  1.00 72.11  ? 1007 LEU A CD2 1 
ATOM   8134  N  N   . PHE A 1 1008 ? 90.288  132.584 92.888  1.00 80.85  ? 1008 PHE A N   1 
ATOM   8135  C  CA  . PHE A 1 1008 ? 89.759  132.061 91.640  1.00 74.34  ? 1008 PHE A CA  1 
ATOM   8136  C  C   . PHE A 1 1008 ? 88.645  132.973 91.128  1.00 85.80  ? 1008 PHE A C   1 
ATOM   8137  O  O   . PHE A 1 1008 ? 87.488  132.559 91.030  1.00 89.06  ? 1008 PHE A O   1 
ATOM   8138  C  CB  . PHE A 1 1008 ? 89.216  130.639 91.803  1.00 72.90  ? 1008 PHE A CB  1 
ATOM   8139  C  CG  . PHE A 1 1008 ? 90.257  129.616 92.188  1.00 87.57  ? 1008 PHE A CG  1 
ATOM   8140  C  CD1 . PHE A 1 1008 ? 91.390  130.013 92.871  1.00 83.94  ? 1008 PHE A CD1 1 
ATOM   8141  C  CD2 . PHE A 1 1008 ? 90.279  128.370 91.585  1.00 107.90 ? 1008 PHE A CD2 1 
ATOM   8142  C  CE1 . PHE A 1 1008 ? 92.363  129.130 93.236  1.00 94.14  ? 1008 PHE A CE1 1 
ATOM   8143  C  CE2 . PHE A 1 1008 ? 91.306  127.479 91.878  1.00 97.56  ? 1008 PHE A CE2 1 
ATOM   8144  C  CZ  . PHE A 1 1008 ? 92.348  127.867 92.706  1.00 89.54  ? 1008 PHE A CZ  1 
ATOM   8145  N  N   . HIS A 1 1009 ? 88.975  134.213 90.793  1.00 84.89  ? 1009 HIS A N   1 
ATOM   8146  C  CA  . HIS A 1 1009 ? 87.929  135.142 90.377  1.00 85.29  ? 1009 HIS A CA  1 
ATOM   8147  C  C   . HIS A 1 1009 ? 87.438  134.800 88.961  1.00 92.62  ? 1009 HIS A C   1 
ATOM   8148  O  O   . HIS A 1 1009 ? 87.829  133.797 88.362  1.00 99.13  ? 1009 HIS A O   1 
ATOM   8149  C  CB  . HIS A 1 1009 ? 88.403  136.584 90.467  1.00 92.85  ? 1009 HIS A CB  1 
ATOM   8150  C  CG  . HIS A 1 1009 ? 89.668  136.846 89.714  1.00 96.35  ? 1009 HIS A CG  1 
ATOM   8151  N  ND1 . HIS A 1 1009 ? 89.683  137.398 88.450  1.00 102.26 ? 1009 HIS A ND1 1 
ATOM   8152  C  CD2 . HIS A 1 1009 ? 90.965  136.635 90.045  1.00 90.07  ? 1009 HIS A CD2 1 
ATOM   8153  C  CE1 . HIS A 1 1009 ? 90.933  137.515 88.035  1.00 100.59 ? 1009 HIS A CE1 1 
ATOM   8154  N  NE2 . HIS A 1 1009 ? 91.731  137.059 88.985  1.00 92.61  ? 1009 HIS A NE2 1 
ATOM   8155  N  N   . ILE A 1 1010 ? 86.530  135.633 88.443  1.00 99.22  ? 1010 ILE A N   1 
ATOM   8156  C  CA  . ILE A 1 1010 ? 85.788  135.287 87.234  1.00 107.56 ? 1010 ILE A CA  1 
ATOM   8157  C  C   . ILE A 1 1010 ? 86.689  135.240 86.006  1.00 106.74 ? 1010 ILE A C   1 
ATOM   8158  O  O   . ILE A 1 1010 ? 86.493  134.411 85.112  1.00 97.66  ? 1010 ILE A O   1 
ATOM   8159  C  CB  . ILE A 1 1010 ? 84.602  136.240 87.001  1.00 112.69 ? 1010 ILE A CB  1 
ATOM   8160  C  CG1 . ILE A 1 1010 ? 83.771  135.806 85.773  1.00 113.60 ? 1010 ILE A CG1 1 
ATOM   8161  C  CG2 . ILE A 1 1010 ? 85.055  137.708 86.962  1.00 119.75 ? 1010 ILE A CG2 1 
ATOM   8162  C  CD1 . ILE A 1 1010 ? 83.204  134.394 85.881  1.00 117.29 ? 1010 ILE A CD1 1 
ATOM   8163  N  N   . GLY A 1 1011 ? 87.715  136.090 85.931  1.00 102.08 ? 1011 GLY A N   1 
ATOM   8164  C  CA  . GLY A 1 1011 ? 88.487  136.124 84.719  1.00 95.05  ? 1011 GLY A CA  1 
ATOM   8165  C  C   . GLY A 1 1011 ? 89.902  135.613 84.840  1.00 105.08 ? 1011 GLY A C   1 
ATOM   8166  O  O   . GLY A 1 1011 ? 90.837  136.201 84.285  1.00 110.15 ? 1011 GLY A O   1 
ATOM   8167  N  N   . SER A 1 1012 ? 90.076  134.512 85.578  1.00 97.91  ? 1012 SER A N   1 
ATOM   8168  C  CA  . SER A 1 1012 ? 91.405  133.946 85.769  1.00 85.25  ? 1012 SER A CA  1 
ATOM   8169  C  C   . SER A 1 1012 ? 91.893  133.188 84.538  1.00 101.25 ? 1012 SER A C   1 
ATOM   8170  O  O   . SER A 1 1012 ? 93.098  133.189 84.256  1.00 112.20 ? 1012 SER A O   1 
ATOM   8171  C  CB  . SER A 1 1012 ? 91.416  133.011 86.979  1.00 75.12  ? 1012 SER A CB  1 
ATOM   8172  O  OG  . SER A 1 1012 ? 90.337  132.091 86.942  1.00 95.58  ? 1012 SER A OG  1 
ATOM   8173  N  N   . ASP A 1 1013 ? 90.984  132.546 83.797  1.00 97.18  ? 1013 ASP A N   1 
ATOM   8174  C  CA  . ASP A 1 1013 ? 91.382  131.801 82.603  1.00 101.94 ? 1013 ASP A CA  1 
ATOM   8175  C  C   . ASP A 1 1013 ? 91.997  132.721 81.558  1.00 101.06 ? 1013 ASP A C   1 
ATOM   8176  O  O   . ASP A 1 1013 ? 92.996  132.369 80.912  1.00 107.78 ? 1013 ASP A O   1 
ATOM   8177  C  CB  . ASP A 1 1013 ? 90.176  131.064 82.018  1.00 118.17 ? 1013 ASP A CB  1 
ATOM   8178  C  CG  . ASP A 1 1013 ? 89.698  129.928 82.900  1.00 131.72 ? 1013 ASP A CG  1 
ATOM   8179  O  OD1 . ASP A 1 1013 ? 90.534  129.344 83.621  1.00 131.77 ? 1013 ASP A OD1 1 
ATOM   8180  O  OD2 . ASP A 1 1013 ? 88.489  129.615 82.867  1.00 123.78 ? 1013 ASP A OD2 1 
ATOM   8181  N  N   . LEU A 1 1014 ? 91.416  133.908 81.380  1.00 90.09  ? 1014 LEU A N   1 
ATOM   8182  C  CA  . LEU A 1 1014 ? 91.980  134.864 80.438  1.00 84.58  ? 1014 LEU A CA  1 
ATOM   8183  C  C   . LEU A 1 1014 ? 93.373  135.300 80.873  1.00 92.33  ? 1014 LEU A C   1 
ATOM   8184  O  O   . LEU A 1 1014 ? 94.267  135.465 80.035  1.00 102.23 ? 1014 LEU A O   1 
ATOM   8185  C  CB  . LEU A 1 1014 ? 91.053  136.068 80.285  1.00 87.73  ? 1014 LEU A CB  1 
ATOM   8186  C  CG  . LEU A 1 1014 ? 91.305  136.840 78.992  1.00 100.77 ? 1014 LEU A CG  1 
ATOM   8187  C  CD1 . LEU A 1 1014 ? 90.861  136.002 77.805  1.00 103.98 ? 1014 LEU A CD1 1 
ATOM   8188  C  CD2 . LEU A 1 1014 ? 90.580  138.174 79.010  1.00 114.36 ? 1014 LEU A CD2 1 
ATOM   8189  N  N   . GLU A 1 1015 ? 93.578  135.495 82.179  1.00 88.67  ? 1015 GLU A N   1 
ATOM   8190  C  CA  . GLU A 1 1015 ? 94.910  135.835 82.668  1.00 87.00  ? 1015 GLU A CA  1 
ATOM   8191  C  C   . GLU A 1 1015 ? 95.911  134.725 82.381  1.00 89.76  ? 1015 GLU A C   1 
ATOM   8192  O  O   . GLU A 1 1015 ? 97.044  135.000 81.972  1.00 96.15  ? 1015 GLU A O   1 
ATOM   8193  C  CB  . GLU A 1 1015 ? 94.889  136.142 84.161  1.00 81.96  ? 1015 GLU A CB  1 
ATOM   8194  C  CG  . GLU A 1 1015 ? 94.281  137.474 84.512  1.00 102.90 ? 1015 GLU A CG  1 
ATOM   8195  C  CD  . GLU A 1 1015 ? 94.543  137.845 85.952  1.00 117.63 ? 1015 GLU A CD  1 
ATOM   8196  O  OE1 . GLU A 1 1015 ? 95.141  137.021 86.676  1.00 101.48 ? 1015 GLU A OE1 1 
ATOM   8197  O  OE2 . GLU A 1 1015 ? 94.168  138.964 86.357  1.00 125.81 ? 1015 GLU A OE2 1 
ATOM   8198  N  N   . ASP A 1 1016 ? 95.528  133.468 82.618  1.00 87.08  ? 1016 ASP A N   1 
ATOM   8199  C  CA  . ASP A 1 1016 ? 96.450  132.373 82.329  1.00 86.23  ? 1016 ASP A CA  1 
ATOM   8200  C  C   . ASP A 1 1016 ? 96.819  132.361 80.853  1.00 81.00  ? 1016 ASP A C   1 
ATOM   8201  O  O   . ASP A 1 1016 ? 98.002  132.260 80.492  1.00 89.17  ? 1016 ASP A O   1 
ATOM   8202  C  CB  . ASP A 1 1016 ? 95.837  131.032 82.734  1.00 102.25 ? 1016 ASP A CB  1 
ATOM   8203  C  CG  . ASP A 1 1016 ? 95.670  130.893 84.233  1.00 113.90 ? 1016 ASP A CG  1 
ATOM   8204  O  OD1 . ASP A 1 1016 ? 96.221  131.734 84.971  1.00 104.77 ? 1016 ASP A OD1 1 
ATOM   8205  O  OD2 . ASP A 1 1016 ? 94.996  129.936 84.672  1.00 105.14 ? 1016 ASP A OD2 1 
ATOM   8206  N  N   . GLN A 1 1017 ? 95.818  132.503 79.982  1.00 74.30  ? 1017 GLN A N   1 
ATOM   8207  C  CA  . GLN A 1 1017 ? 96.086  132.499 78.549  1.00 77.45  ? 1017 GLN A CA  1 
ATOM   8208  C  C   . GLN A 1 1017 ? 97.020  133.638 78.153  1.00 86.71  ? 1017 GLN A C   1 
ATOM   8209  O  O   . GLN A 1 1017 ? 98.014  133.425 77.446  1.00 91.56  ? 1017 GLN A O   1 
ATOM   8210  C  CB  . GLN A 1 1017 ? 94.769  132.605 77.780  1.00 101.72 ? 1017 GLN A CB  1 
ATOM   8211  C  CG  . GLN A 1 1017 ? 94.929  132.675 76.275  1.00 117.56 ? 1017 GLN A CG  1 
ATOM   8212  C  CD  . GLN A 1 1017 ? 93.600  132.636 75.552  1.00 123.55 ? 1017 GLN A CD  1 
ATOM   8213  O  OE1 . GLN A 1 1017 ? 92.577  132.268 76.127  1.00 120.01 ? 1017 GLN A OE1 1 
ATOM   8214  N  NE2 . GLN A 1 1017 ? 93.606  133.032 74.284  1.00 118.99 ? 1017 GLN A NE2 1 
ATOM   8215  N  N   . ARG A 1 1018 ? 96.751  134.849 78.654  1.00 85.26  ? 1018 ARG A N   1 
ATOM   8216  C  CA  . ARG A 1 1018 ? 97.560  136.000 78.264  1.00 79.32  ? 1018 ARG A CA  1 
ATOM   8217  C  C   . ARG A 1 1018 ? 98.984  135.922 78.798  1.00 77.35  ? 1018 ARG A C   1 
ATOM   8218  O  O   . ARG A 1 1018 ? 99.938  136.206 78.064  1.00 87.53  ? 1018 ARG A O   1 
ATOM   8219  C  CB  . ARG A 1 1018 ? 96.901  137.293 78.750  1.00 83.97  ? 1018 ARG A CB  1 
ATOM   8220  C  CG  . ARG A 1 1018 ? 95.633  137.680 78.026  1.00 98.39  ? 1018 ARG A CG  1 
ATOM   8221  C  CD  . ARG A 1 1018 ? 95.959  138.669 76.916  1.00 114.39 ? 1018 ARG A CD  1 
ATOM   8222  N  NE  . ARG A 1 1018 ? 94.823  138.962 76.045  1.00 129.73 ? 1018 ARG A NE  1 
ATOM   8223  C  CZ  . ARG A 1 1018 ? 94.206  138.073 75.272  1.00 132.82 ? 1018 ARG A CZ  1 
ATOM   8224  N  NH1 . ARG A 1 1018 ? 94.614  136.811 75.226  1.00 120.51 ? 1018 ARG A NH1 1 
ATOM   8225  N  NH2 . ARG A 1 1018 ? 93.182  138.456 74.522  1.00 132.85 ? 1018 ARG A NH2 1 
ATOM   8226  N  N   . VAL A 1 1019 ? 99.158  135.519 80.060  1.00 78.22  ? 1019 VAL A N   1 
ATOM   8227  C  CA  . VAL A 1 1019 ? 100.504 135.426 80.615  1.00 71.93  ? 1019 VAL A CA  1 
ATOM   8228  C  C   . VAL A 1 1019 ? 101.318 134.347 79.913  1.00 81.29  ? 1019 VAL A C   1 
ATOM   8229  O  O   . VAL A 1 1019 ? 102.484 134.569 79.549  1.00 89.48  ? 1019 VAL A O   1 
ATOM   8230  C  CB  . VAL A 1 1019 ? 100.444 135.195 82.136  1.00 63.18  ? 1019 VAL A CB  1 
ATOM   8231  C  CG1 . VAL A 1 1019 ? 101.836 134.917 82.683  1.00 59.83  ? 1019 VAL A CG1 1 
ATOM   8232  C  CG2 . VAL A 1 1019 ? 99.840  136.409 82.832  1.00 79.67  ? 1019 VAL A CG2 1 
ATOM   8233  N  N   . CYS A 1 1020 ? 100.720 133.171 79.682  1.00 85.27  ? 1020 CYS A N   1 
ATOM   8234  C  CA  . CYS A 1 1020 ? 101.470 132.120 79.005  1.00 70.18  ? 1020 CYS A CA  1 
ATOM   8235  C  C   . CYS A 1 1020 ? 101.818 132.515 77.576  1.00 72.51  ? 1020 CYS A C   1 
ATOM   8236  O  O   . CYS A 1 1020 ? 102.918 132.216 77.099  1.00 82.36  ? 1020 CYS A O   1 
ATOM   8237  C  CB  . CYS A 1 1020 ? 100.684 130.810 79.042  1.00 84.91  ? 1020 CYS A CB  1 
ATOM   8238  S  SG  . CYS A 1 1020 ? 100.670 130.033 80.679  1.00 91.36  ? 1020 CYS A SG  1 
ATOM   8239  N  N   . GLU A 1 1021 ? 100.907 133.201 76.878  1.00 84.16  ? 1021 GLU A N   1 
ATOM   8240  C  CA  . GLU A 1 1021 ? 101.229 133.639 75.526  1.00 82.40  ? 1021 GLU A CA  1 
ATOM   8241  C  C   . GLU A 1 1021 ? 102.320 134.702 75.527  1.00 78.20  ? 1021 GLU A C   1 
ATOM   8242  O  O   . GLU A 1 1021 ? 103.150 134.737 74.613  1.00 88.83  ? 1021 GLU A O   1 
ATOM   8243  C  CB  . GLU A 1 1021 ? 99.978  134.154 74.815  1.00 105.00 ? 1021 GLU A CB  1 
ATOM   8244  C  CG  . GLU A 1 1021 ? 99.014  133.052 74.423  1.00 105.64 ? 1021 GLU A CG  1 
ATOM   8245  C  CD  . GLU A 1 1021 ? 97.723  133.588 73.849  1.00 119.85 ? 1021 GLU A CD  1 
ATOM   8246  O  OE1 . GLU A 1 1021 ? 96.825  132.776 73.546  1.00 117.97 ? 1021 GLU A OE1 1 
ATOM   8247  O  OE2 . GLU A 1 1021 ? 97.612  134.822 73.690  1.00 121.99 ? 1021 GLU A OE2 1 
ATOM   8248  N  N   . TRP A 1 1022 ? 102.340 135.566 76.546  1.00 79.15  ? 1022 TRP A N   1 
ATOM   8249  C  CA  . TRP A 1 1022 ? 103.339 136.626 76.596  1.00 88.58  ? 1022 TRP A CA  1 
ATOM   8250  C  C   . TRP A 1 1022 ? 104.734 136.094 76.909  1.00 89.08  ? 1022 TRP A C   1 
ATOM   8251  O  O   . TRP A 1 1022 ? 105.722 136.568 76.336  1.00 90.35  ? 1022 TRP A O   1 
ATOM   8252  C  CB  . TRP A 1 1022 ? 102.936 137.663 77.641  1.00 90.10  ? 1022 TRP A CB  1 
ATOM   8253  C  CG  . TRP A 1 1022 ? 103.929 138.760 77.768  1.00 93.26  ? 1022 TRP A CG  1 
ATOM   8254  C  CD1 . TRP A 1 1022 ? 104.108 139.808 76.917  1.00 101.38 ? 1022 TRP A CD1 1 
ATOM   8255  C  CD2 . TRP A 1 1022 ? 104.934 138.886 78.780  1.00 86.07  ? 1022 TRP A CD2 1 
ATOM   8256  N  NE1 . TRP A 1 1022 ? 105.142 140.599 77.355  1.00 94.62  ? 1022 TRP A NE1 1 
ATOM   8257  C  CE2 . TRP A 1 1022 ? 105.669 140.052 78.495  1.00 87.76  ? 1022 TRP A CE2 1 
ATOM   8258  C  CE3 . TRP A 1 1022 ? 105.276 138.131 79.908  1.00 84.04  ? 1022 TRP A CE3 1 
ATOM   8259  C  CZ2 . TRP A 1 1022 ? 106.724 140.483 79.296  1.00 92.49  ? 1022 TRP A CZ2 1 
ATOM   8260  C  CZ3 . TRP A 1 1022 ? 106.325 138.563 80.701  1.00 78.44  ? 1022 TRP A CZ3 1 
ATOM   8261  C  CH2 . TRP A 1 1022 ? 107.037 139.726 80.392  1.00 89.03  ? 1022 TRP A CH2 1 
ATOM   8262  N  N   . LEU A 1 1023 ? 104.841 135.113 77.809  1.00 83.84  ? 1023 LEU A N   1 
ATOM   8263  C  CA  . LEU A 1 1023 ? 106.166 134.633 78.205  1.00 70.86  ? 1023 LEU A CA  1 
ATOM   8264  C  C   . LEU A 1 1023 ? 106.937 133.963 77.070  1.00 75.95  ? 1023 LEU A C   1 
ATOM   8265  O  O   . LEU A 1 1023 ? 108.165 133.852 77.159  1.00 77.97  ? 1023 LEU A O   1 
ATOM   8266  C  CB  . LEU A 1 1023 ? 106.059 133.689 79.403  1.00 67.42  ? 1023 LEU A CB  1 
ATOM   8267  C  CG  . LEU A 1 1023 ? 105.858 134.427 80.728  1.00 69.81  ? 1023 LEU A CG  1 
ATOM   8268  C  CD1 . LEU A 1 1023 ? 105.435 133.470 81.829  1.00 68.07  ? 1023 LEU A CD1 1 
ATOM   8269  C  CD2 . LEU A 1 1023 ? 107.135 135.172 81.110  1.00 70.52  ? 1023 LEU A CD2 1 
ATOM   8270  N  N   . LEU A 1 1024 ? 106.259 133.525 76.009  1.00 82.06  ? 1024 LEU A N   1 
ATOM   8271  C  CA  . LEU A 1 1024 ? 106.900 132.875 74.870  1.00 78.91  ? 1024 LEU A CA  1 
ATOM   8272  C  C   . LEU A 1 1024 ? 106.980 133.777 73.640  1.00 82.78  ? 1024 LEU A C   1 
ATOM   8273  O  O   . LEU A 1 1024 ? 107.007 133.284 72.509  1.00 96.63  ? 1024 LEU A O   1 
ATOM   8274  C  CB  . LEU A 1 1024 ? 106.162 131.586 74.512  1.00 86.02  ? 1024 LEU A CB  1 
ATOM   8275  C  CG  . LEU A 1 1024 ? 105.928 130.523 75.584  1.00 84.12  ? 1024 LEU A CG  1 
ATOM   8276  C  CD1 . LEU A 1 1024 ? 105.095 129.397 75.000  1.00 80.40  ? 1024 LEU A CD1 1 
ATOM   8277  C  CD2 . LEU A 1 1024 ? 107.255 129.990 76.102  1.00 69.14  ? 1024 LEU A CD2 1 
ATOM   8278  N  N   . SER A 1 1025 ? 107.021 135.095 73.835  1.00 81.19  ? 1025 SER A N   1 
ATOM   8279  C  CA  . SER A 1 1025 ? 107.030 136.039 72.724  1.00 85.47  ? 1025 SER A CA  1 
ATOM   8280  C  C   . SER A 1 1025 ? 108.380 136.710 72.497  1.00 95.92  ? 1025 SER A C   1 
ATOM   8281  O  O   . SER A 1 1025 ? 108.485 137.565 71.611  1.00 103.29 ? 1025 SER A O   1 
ATOM   8282  C  CB  . SER A 1 1025 ? 105.957 137.113 72.937  1.00 81.31  ? 1025 SER A CB  1 
ATOM   8283  O  OG  . SER A 1 1025 ? 106.060 137.687 74.228  1.00 88.17  ? 1025 SER A OG  1 
ATOM   8284  N  N   . SER A 1 1026 ? 109.416 136.334 73.242  1.00 95.32  ? 1026 SER A N   1 
ATOM   8285  C  CA  . SER A 1 1026 ? 110.746 136.874 73.000  1.00 95.98  ? 1026 SER A CA  1 
ATOM   8286  C  C   . SER A 1 1026 ? 111.292 136.330 71.684  1.00 100.51 ? 1026 SER A C   1 
ATOM   8287  O  O   . SER A 1 1026 ? 110.882 135.268 71.211  1.00 99.92  ? 1026 SER A O   1 
ATOM   8288  C  CB  . SER A 1 1026 ? 111.692 136.524 74.149  1.00 94.54  ? 1026 SER A CB  1 
ATOM   8289  O  OG  . SER A 1 1026 ? 111.853 135.121 74.270  1.00 96.28  ? 1026 SER A OG  1 
ATOM   8290  N  N   . ASN A 1 1027 ? 112.243 137.063 71.092  1.00 100.49 ? 1027 ASN A N   1 
ATOM   8291  C  CA  . ASN A 1 1027 ? 112.728 136.673 69.770  1.00 104.14 ? 1027 ASN A CA  1 
ATOM   8292  C  C   . ASN A 1 1027 ? 113.432 135.321 69.796  1.00 113.88 ? 1027 ASN A C   1 
ATOM   8293  O  O   . ASN A 1 1027 ? 113.080 134.458 68.973  1.00 118.38 ? 1027 ASN A O   1 
ATOM   8294  C  CB  . ASN A 1 1027 ? 113.614 137.785 69.192  1.00 105.01 ? 1027 ASN A CB  1 
ATOM   8295  C  CG  . ASN A 1 1027 ? 113.968 137.550 67.736  1.00 120.70 ? 1027 ASN A CG  1 
ATOM   8296  O  OD1 . ASN A 1 1027 ? 113.447 136.636 67.096  1.00 108.71 ? 1027 ASN A OD1 1 
ATOM   8297  N  ND2 . ASN A 1 1027 ? 114.868 138.369 67.209  1.00 129.06 ? 1027 ASN A ND2 1 
ATOM   8298  N  N   . PRO A 1 1028 ? 114.420 135.053 70.674  1.00 105.37 ? 1028 PRO A N   1 
ATOM   8299  C  CA  . PRO A 1 1028 ? 114.727 133.650 70.966  1.00 91.70  ? 1028 PRO A CA  1 
ATOM   8300  C  C   . PRO A 1 1028 ? 113.942 133.193 72.189  1.00 95.10  ? 1028 PRO A C   1 
ATOM   8301  O  O   . PRO A 1 1028 ? 113.989 133.849 73.229  1.00 102.55 ? 1028 PRO A O   1 
ATOM   8302  C  CB  . PRO A 1 1028 ? 116.244 133.658 71.205  1.00 84.30  ? 1028 PRO A CB  1 
ATOM   8303  C  CG  . PRO A 1 1028 ? 116.606 135.089 71.512  1.00 100.49 ? 1028 PRO A CG  1 
ATOM   8304  C  CD  . PRO A 1 1028 ? 115.403 135.963 71.284  1.00 96.95  ? 1028 PRO A CD  1 
ATOM   8305  N  N   . VAL A 1 1029 ? 113.206 132.103 72.091  1.00 77.61  ? 1029 VAL A N   1 
ATOM   8306  C  CA  . VAL A 1 1029 ? 112.376 131.631 73.192  1.00 65.31  ? 1029 VAL A CA  1 
ATOM   8307  C  C   . VAL A 1 1029 ? 113.220 130.819 74.163  1.00 81.93  ? 1029 VAL A C   1 
ATOM   8308  O  O   . VAL A 1 1029 ? 114.073 130.014 73.748  1.00 88.95  ? 1029 VAL A O   1 
ATOM   8309  C  CB  . VAL A 1 1029 ? 111.188 130.814 72.667  1.00 68.02  ? 1029 VAL A CB  1 
ATOM   8310  C  CG1 . VAL A 1 1029 ? 110.234 130.462 73.783  1.00 69.76  ? 1029 VAL A CG1 1 
ATOM   8311  C  CG2 . VAL A 1 1029 ? 110.458 131.565 71.569  1.00 70.20  ? 1029 VAL A CG2 1 
ATOM   8312  N  N   . MET A 1 1030 ? 113.006 131.031 75.467  1.00 72.56  ? 1030 MET A N   1 
ATOM   8313  C  CA  . MET A 1 1030 ? 113.688 130.225 76.471  1.00 80.81  ? 1030 MET A CA  1 
ATOM   8314  C  C   . MET A 1 1030 ? 112.639 129.656 77.397  1.00 86.92  ? 1030 MET A C   1 
ATOM   8315  O  O   . MET A 1 1030 ? 112.049 130.410 78.188  1.00 97.66  ? 1030 MET A O   1 
ATOM   8316  C  CB  . MET A 1 1030 ? 114.700 131.014 77.255  1.00 82.51  ? 1030 MET A CB  1 
ATOM   8317  C  CG  . MET A 1 1030 ? 115.462 130.192 78.240  1.00 85.11  ? 1030 MET A CG  1 
ATOM   8318  S  SD  . MET A 1 1030 ? 116.556 131.423 78.941  1.00 87.39  ? 1030 MET A SD  1 
ATOM   8319  C  CE  . MET A 1 1030 ? 117.734 131.596 77.539  1.00 94.70  ? 1030 MET A CE  1 
ATOM   8320  N  N   . SER A 1 1031 ? 112.410 128.344 77.322  1.00 74.70  ? 1031 SER A N   1 
ATOM   8321  C  CA  . SER A 1 1031 ? 111.312 127.734 78.058  1.00 76.00  ? 1031 SER A CA  1 
ATOM   8322  C  C   . SER A 1 1031 ? 111.593 127.596 79.554  1.00 84.20  ? 1031 SER A C   1 
ATOM   8323  O  O   . SER A 1 1031 ? 110.661 127.680 80.367  1.00 89.08  ? 1031 SER A O   1 
ATOM   8324  C  CB  . SER A 1 1031 ? 110.994 126.362 77.460  1.00 76.69  ? 1031 SER A CB  1 
ATOM   8325  O  OG  . SER A 1 1031 ? 112.167 125.573 77.395  1.00 91.21  ? 1031 SER A OG  1 
ATOM   8326  N  N   . ARG A 1 1032 ? 112.852 127.388 79.945  1.00 81.00  ? 1032 ARG A N   1 
ATOM   8327  C  CA  . ARG A 1 1032 ? 113.174 127.309 81.368  1.00 85.72  ? 1032 ARG A CA  1 
ATOM   8328  C  C   . ARG A 1 1032 ? 112.879 128.616 82.084  1.00 87.88  ? 1032 ARG A C   1 
ATOM   8329  O  O   . ARG A 1 1032 ? 112.339 128.615 83.198  1.00 97.58  ? 1032 ARG A O   1 
ATOM   8330  C  CB  . ARG A 1 1032 ? 114.632 126.905 81.565  1.00 93.93  ? 1032 ARG A CB  1 
ATOM   8331  C  CG  . ARG A 1 1032 ? 114.986 125.618 80.868  1.00 96.62  ? 1032 ARG A CG  1 
ATOM   8332  C  CD  . ARG A 1 1032 ? 115.939 124.807 81.713  1.00 94.77  ? 1032 ARG A CD  1 
ATOM   8333  N  NE  . ARG A 1 1032 ? 116.648 123.803 80.934  1.00 96.15  ? 1032 ARG A NE  1 
ATOM   8334  C  CZ  . ARG A 1 1032 ? 117.143 122.684 81.450  1.00 104.02 ? 1032 ARG A CZ  1 
ATOM   8335  N  NH1 . ARG A 1 1032 ? 117.001 122.429 82.744  1.00 107.17 ? 1032 ARG A NH1 1 
ATOM   8336  N  NH2 . ARG A 1 1032 ? 117.772 121.815 80.672  1.00 93.70  ? 1032 ARG A NH2 1 
ATOM   8337  N  N   . PHE A 1 1033 ? 113.227 129.741 81.461  1.00 83.61  ? 1033 PHE A N   1 
ATOM   8338  C  CA  . PHE A 1 1033 ? 112.917 131.034 82.051  1.00 78.50  ? 1033 PHE A CA  1 
ATOM   8339  C  C   . PHE A 1 1033 ? 111.409 131.221 82.192  1.00 78.90  ? 1033 PHE A C   1 
ATOM   8340  O  O   . PHE A 1 1033 ? 110.927 131.716 83.220  1.00 80.93  ? 1033 PHE A O   1 
ATOM   8341  C  CB  . PHE A 1 1033 ? 113.537 132.133 81.187  1.00 83.69  ? 1033 PHE A CB  1 
ATOM   8342  C  CG  . PHE A 1 1033 ? 112.930 133.484 81.384  1.00 78.82  ? 1033 PHE A CG  1 
ATOM   8343  C  CD1 . PHE A 1 1033 ? 113.213 134.224 82.517  1.00 86.96  ? 1033 PHE A CD1 1 
ATOM   8344  C  CD2 . PHE A 1 1033 ? 112.078 134.018 80.432  1.00 77.43  ? 1033 PHE A CD2 1 
ATOM   8345  C  CE1 . PHE A 1 1033 ? 112.656 135.475 82.698  1.00 91.54  ? 1033 PHE A CE1 1 
ATOM   8346  C  CE2 . PHE A 1 1033 ? 111.514 135.264 80.609  1.00 84.45  ? 1033 PHE A CE2 1 
ATOM   8347  C  CZ  . PHE A 1 1033 ? 111.804 135.994 81.744  1.00 98.43  ? 1033 PHE A CZ  1 
ATOM   8348  N  N   . ALA A 1 1034 ? 110.648 130.810 81.173  1.00 74.26  ? 1034 ALA A N   1 
ATOM   8349  C  CA  . ALA A 1 1034 ? 109.194 130.927 81.230  1.00 58.19  ? 1034 ALA A CA  1 
ATOM   8350  C  C   . ALA A 1 1034 ? 108.609 130.095 82.366  1.00 66.64  ? 1034 ALA A C   1 
ATOM   8351  O  O   . ALA A 1 1034 ? 107.721 130.557 83.090  1.00 82.96  ? 1034 ALA A O   1 
ATOM   8352  C  CB  . ALA A 1 1034 ? 108.581 130.516 79.892  1.00 64.04  ? 1034 ALA A CB  1 
ATOM   8353  N  N   . ALA A 1 1035 ? 109.095 128.860 82.539  1.00 69.06  ? 1035 ALA A N   1 
ATOM   8354  C  CA  . ALA A 1 1035 ? 108.601 128.024 83.629  1.00 67.79  ? 1035 ALA A CA  1 
ATOM   8355  C  C   . ALA A 1 1035 ? 108.956 128.609 84.987  1.00 78.46  ? 1035 ALA A C   1 
ATOM   8356  O  O   . ALA A 1 1035 ? 108.130 128.604 85.908  1.00 82.43  ? 1035 ALA A O   1 
ATOM   8357  C  CB  . ALA A 1 1035 ? 109.171 126.619 83.511  1.00 65.56  ? 1035 ALA A CB  1 
ATOM   8358  N  N   . ASP A 1 1036 ? 110.188 129.099 85.134  1.00 78.85  ? 1036 ASP A N   1 
ATOM   8359  C  CA  . ASP A 1 1036 ? 110.605 129.688 86.402  1.00 72.20  ? 1036 ASP A CA  1 
ATOM   8360  C  C   . ASP A 1 1036 ? 109.749 130.899 86.751  1.00 78.10  ? 1036 ASP A C   1 
ATOM   8361  O  O   . ASP A 1 1036 ? 109.367 131.084 87.912  1.00 85.31  ? 1036 ASP A O   1 
ATOM   8362  C  CB  . ASP A 1 1036 ? 112.089 130.047 86.356  1.00 93.47  ? 1036 ASP A CB  1 
ATOM   8363  C  CG  . ASP A 1 1036 ? 112.980 128.832 86.538  1.00 110.45 ? 1036 ASP A CG  1 
ATOM   8364  O  OD1 . ASP A 1 1036 ? 112.439 127.709 86.602  1.00 96.15  ? 1036 ASP A OD1 1 
ATOM   8365  O  OD2 . ASP A 1 1036 ? 114.215 128.997 86.627  1.00 115.66 ? 1036 ASP A OD2 1 
ATOM   8366  N  N   . ILE A 1 1037 ? 109.426 131.727 85.755  1.00 70.65  ? 1037 ILE A N   1 
ATOM   8367  C  CA  . ILE A 1 1037 ? 108.596 132.903 86.006  1.00 67.28  ? 1037 ILE A CA  1 
ATOM   8368  C  C   . ILE A 1 1037 ? 107.166 132.498 86.333  1.00 72.02  ? 1037 ILE A C   1 
ATOM   8369  O  O   . ILE A 1 1037 ? 106.551 133.037 87.261  1.00 80.96  ? 1037 ILE A O   1 
ATOM   8370  C  CB  . ILE A 1 1037 ? 108.646 133.859 84.802  1.00 71.45  ? 1037 ILE A CB  1 
ATOM   8371  C  CG1 . ILE A 1 1037 ? 110.038 134.468 84.684  1.00 88.80  ? 1037 ILE A CG1 1 
ATOM   8372  C  CG2 . ILE A 1 1037 ? 107.592 134.952 84.937  1.00 73.75  ? 1037 ILE A CG2 1 
ATOM   8373  C  CD1 . ILE A 1 1037 ? 110.458 135.249 85.910  1.00 97.75  ? 1037 ILE A CD1 1 
ATOM   8374  N  N   . PHE A 1 1038 ? 106.616 131.537 85.589  1.00 74.94  ? 1038 PHE A N   1 
ATOM   8375  C  CA  . PHE A 1 1038 ? 105.225 131.143 85.787  1.00 65.44  ? 1038 PHE A CA  1 
ATOM   8376  C  C   . PHE A 1 1038 ? 104.966 130.609 87.188  1.00 64.90  ? 1038 PHE A C   1 
ATOM   8377  O  O   . PHE A 1 1038 ? 103.866 130.784 87.723  1.00 76.56  ? 1038 PHE A O   1 
ATOM   8378  C  CB  . PHE A 1 1038 ? 104.839 130.083 84.758  1.00 79.01  ? 1038 PHE A CB  1 
ATOM   8379  C  CG  . PHE A 1 1038 ? 103.406 129.661 84.836  1.00 78.06  ? 1038 PHE A CG  1 
ATOM   8380  C  CD1 . PHE A 1 1038 ? 103.069 128.460 85.439  1.00 77.35  ? 1038 PHE A CD1 1 
ATOM   8381  C  CD2 . PHE A 1 1038 ? 102.395 130.457 84.326  1.00 72.23  ? 1038 PHE A CD2 1 
ATOM   8382  C  CE1 . PHE A 1 1038 ? 101.753 128.057 85.534  1.00 81.06  ? 1038 PHE A CE1 1 
ATOM   8383  C  CE2 . PHE A 1 1038 ? 101.075 130.057 84.414  1.00 81.19  ? 1038 PHE A CE2 1 
ATOM   8384  C  CZ  . PHE A 1 1038 ? 100.754 128.855 85.020  1.00 84.14  ? 1038 PHE A CZ  1 
ATOM   8385  N  N   . SER A 1 1039 ? 105.963 129.978 87.811  1.00 71.92  ? 1039 SER A N   1 
ATOM   8386  C  CA  . SER A 1 1039 ? 105.776 129.445 89.153  1.00 74.24  ? 1039 SER A CA  1 
ATOM   8387  C  C   . SER A 1 1039 ? 105.577 130.530 90.206  1.00 78.75  ? 1039 SER A C   1 
ATOM   8388  O  O   . SER A 1 1039 ? 105.124 130.217 91.314  1.00 90.97  ? 1039 SER A O   1 
ATOM   8389  C  CB  . SER A 1 1039 ? 106.971 128.570 89.536  1.00 79.95  ? 1039 SER A CB  1 
ATOM   8390  O  OG  . SER A 1 1039 ? 107.056 127.430 88.699  1.00 77.94  ? 1039 SER A OG  1 
ATOM   8391  N  N   . ARG A 1 1040 ? 105.902 131.789 89.907  1.00 78.86  ? 1040 ARG A N   1 
ATOM   8392  C  CA  . ARG A 1 1040 ? 105.873 132.823 90.931  1.00 81.32  ? 1040 ARG A CA  1 
ATOM   8393  C  C   . ARG A 1 1040 ? 104.769 133.852 90.741  1.00 80.80  ? 1040 ARG A C   1 
ATOM   8394  O  O   . ARG A 1 1040 ? 104.539 134.658 91.649  1.00 81.22  ? 1040 ARG A O   1 
ATOM   8395  C  CB  . ARG A 1 1040 ? 107.228 133.534 90.984  1.00 86.99  ? 1040 ARG A CB  1 
ATOM   8396  C  CG  . ARG A 1 1040 ? 108.289 132.617 91.525  1.00 87.54  ? 1040 ARG A CG  1 
ATOM   8397  C  CD  . ARG A 1 1040 ? 109.507 132.626 90.630  1.00 86.36  ? 1040 ARG A CD  1 
ATOM   8398  N  NE  . ARG A 1 1040 ? 110.245 131.372 90.714  1.00 87.50  ? 1040 ARG A NE  1 
ATOM   8399  C  CZ  . ARG A 1 1040 ? 110.958 130.998 91.765  1.00 97.60  ? 1040 ARG A CZ  1 
ATOM   8400  N  NH1 . ARG A 1 1040 ? 111.013 131.776 92.833  1.00 98.56  ? 1040 ARG A NH1 1 
ATOM   8401  N  NH2 . ARG A 1 1040 ? 111.601 129.839 91.757  1.00 100.75 ? 1040 ARG A NH2 1 
ATOM   8402  N  N   . THR A 1 1041 ? 104.082 133.845 89.605  1.00 79.05  ? 1041 THR A N   1 
ATOM   8403  C  CA  . THR A 1 1041 ? 102.923 134.697 89.397  1.00 75.00  ? 1041 THR A CA  1 
ATOM   8404  C  C   . THR A 1 1041 ? 101.743 134.109 90.159  1.00 92.16  ? 1041 THR A C   1 
ATOM   8405  O  O   . THR A 1 1041 ? 101.806 132.973 90.633  1.00 96.59  ? 1041 THR A O   1 
ATOM   8406  C  CB  . THR A 1 1041 ? 102.627 134.811 87.903  1.00 75.35  ? 1041 THR A CB  1 
ATOM   8407  O  OG1 . THR A 1 1041 ? 102.624 133.505 87.313  1.00 89.49  ? 1041 THR A OG1 1 
ATOM   8408  C  CG2 . THR A 1 1041 ? 103.681 135.669 87.210  1.00 84.41  ? 1041 THR A CG2 1 
ATOM   8409  N  N   . PRO A 1 1042 ? 100.646 134.858 90.316  1.00 84.99  ? 1042 PRO A N   1 
ATOM   8410  C  CA  . PRO A 1 1042 ? 99.478  134.277 91.001  1.00 66.71  ? 1042 PRO A CA  1 
ATOM   8411  C  C   . PRO A 1 1042 ? 98.953  133.030 90.315  1.00 82.54  ? 1042 PRO A C   1 
ATOM   8412  O  O   . PRO A 1 1042 ? 98.275  132.220 90.959  1.00 90.55  ? 1042 PRO A O   1 
ATOM   8413  C  CB  . PRO A 1 1042 ? 98.438  135.409 90.964  1.00 61.55  ? 1042 PRO A CB  1 
ATOM   8414  C  CG  . PRO A 1 1042 ? 99.018  136.479 90.065  1.00 69.85  ? 1042 PRO A CG  1 
ATOM   8415  C  CD  . PRO A 1 1042 ? 100.495 136.310 90.117  1.00 82.53  ? 1042 PRO A CD  1 
ATOM   8416  N  N   . SER A 1 1043 ? 99.266  132.842 89.032  1.00 77.32  ? 1043 SER A N   1 
ATOM   8417  C  CA  . SER A 1 1043 ? 98.930  131.600 88.346  1.00 79.73  ? 1043 SER A CA  1 
ATOM   8418  C  C   . SER A 1 1043 ? 99.669  130.407 88.948  1.00 80.79  ? 1043 SER A C   1 
ATOM   8419  O  O   . SER A 1 1043 ? 99.101  129.312 89.069  1.00 91.05  ? 1043 SER A O   1 
ATOM   8420  C  CB  . SER A 1 1043 ? 99.239  131.734 86.855  1.00 77.93  ? 1043 SER A CB  1 
ATOM   8421  O  OG  . SER A 1 1043 ? 98.384  132.685 86.241  1.00 64.06  ? 1043 SER A OG  1 
ATOM   8422  N  N   . GLY A 1 1044 ? 100.931 130.595 89.343  1.00 76.33  ? 1044 GLY A N   1 
ATOM   8423  C  CA  . GLY A 1 1044 ? 101.643 129.512 90.004  1.00 77.35  ? 1044 GLY A CA  1 
ATOM   8424  C  C   . GLY A 1 1044 ? 101.025 129.141 91.337  1.00 90.69  ? 1044 GLY A C   1 
ATOM   8425  O  O   . GLY A 1 1044 ? 100.914 127.960 91.676  1.00 91.85  ? 1044 GLY A O   1 
ATOM   8426  N  N   . LYS A 1 1045 ? 100.614 130.146 92.112  1.00 87.69  ? 1045 LYS A N   1 
ATOM   8427  C  CA  . LYS A 1 1045 ? 99.921  129.877 93.369  1.00 90.14  ? 1045 LYS A CA  1 
ATOM   8428  C  C   . LYS A 1 1045 ? 98.603  129.156 93.119  1.00 82.69  ? 1045 LYS A C   1 
ATOM   8429  O  O   . LYS A 1 1045 ? 98.216  128.259 93.877  1.00 93.50  ? 1045 LYS A O   1 
ATOM   8430  C  CB  . LYS A 1 1045 ? 99.669  131.171 94.132  1.00 78.74  ? 1045 LYS A CB  1 
ATOM   8431  C  CG  . LYS A 1 1045 ? 100.905 132.009 94.351  1.00 93.16  ? 1045 LYS A CG  1 
ATOM   8432  C  CD  . LYS A 1 1045 ? 101.940 131.226 95.130  1.00 111.23 ? 1045 LYS A CD  1 
ATOM   8433  C  CE  . LYS A 1 1045 ? 101.447 130.867 96.520  1.00 118.97 ? 1045 LYS A CE  1 
ATOM   8434  N  NZ  . LYS A 1 1045 ? 102.435 130.007 97.227  1.00 124.95 ? 1045 LYS A NZ  1 
ATOM   8435  N  N   . ARG A 1 1046 ? 97.903  129.543 92.053  1.00 73.17  ? 1046 ARG A N   1 
ATOM   8436  C  CA  . ARG A 1 1046 ? 96.637  128.916 91.722  1.00 72.66  ? 1046 ARG A CA  1 
ATOM   8437  C  C   . ARG A 1 1046 ? 96.845  127.442 91.394  1.00 75.28  ? 1046 ARG A C   1 
ATOM   8438  O  O   . ARG A 1 1046 ? 96.078  126.576 91.840  1.00 89.72  ? 1046 ARG A O   1 
ATOM   8439  C  CB  . ARG A 1 1046 ? 96.010  129.667 90.547  1.00 73.20  ? 1046 ARG A CB  1 
ATOM   8440  C  CG  . ARG A 1 1046 ? 94.591  129.325 90.227  1.00 77.87  ? 1046 ARG A CG  1 
ATOM   8441  C  CD  . ARG A 1 1046 ? 94.092  130.208 89.100  1.00 82.87  ? 1046 ARG A CD  1 
ATOM   8442  N  NE  . ARG A 1 1046 ? 94.168  131.632 89.429  1.00 65.80  ? 1046 ARG A NE  1 
ATOM   8443  C  CZ  . ARG A 1 1046 ? 94.534  132.549 88.535  1.00 76.15  ? 1046 ARG A CZ  1 
ATOM   8444  N  NH1 . ARG A 1 1046 ? 94.806  132.176 87.297  1.00 82.09  ? 1046 ARG A NH1 1 
ATOM   8445  N  NH2 . ARG A 1 1046 ? 94.610  133.834 88.881  1.00 67.68  ? 1046 ARG A NH2 1 
ATOM   8446  N  N   . LEU A 1 1047 ? 97.909  127.141 90.642  1.00 76.08  ? 1047 LEU A N   1 
ATOM   8447  C  CA  . LEU A 1 1047 ? 98.250  125.756 90.340  1.00 84.17  ? 1047 LEU A CA  1 
ATOM   8448  C  C   . LEU A 1 1047 ? 98.631  124.984 91.599  1.00 84.82  ? 1047 LEU A C   1 
ATOM   8449  O  O   . LEU A 1 1047 ? 98.272  123.809 91.750  1.00 90.32  ? 1047 LEU A O   1 
ATOM   8450  C  CB  . LEU A 1 1047 ? 99.389  125.701 89.319  1.00 94.78  ? 1047 LEU A CB  1 
ATOM   8451  C  CG  . LEU A 1 1047 ? 99.524  124.389 88.545  1.00 91.91  ? 1047 LEU A CG  1 
ATOM   8452  C  CD1 . LEU A 1 1047 ? 98.258  124.113 87.753  1.00 87.26  ? 1047 LEU A CD1 1 
ATOM   8453  C  CD2 . LEU A 1 1047 ? 100.740 124.417 87.622  1.00 101.17 ? 1047 LEU A CD2 1 
ATOM   8454  N  N   . GLN A 1 1048 ? 99.370  125.619 92.510  1.00 78.42  ? 1048 GLN A N   1 
ATOM   8455  C  CA  . GLN A 1 1048 ? 99.724  124.948 93.757  1.00 80.21  ? 1048 GLN A CA  1 
ATOM   8456  C  C   . GLN A 1 1048 ? 98.476  124.594 94.562  1.00 83.59  ? 1048 GLN A C   1 
ATOM   8457  O  O   . GLN A 1 1048 ? 98.382  123.499 95.133  1.00 95.85  ? 1048 GLN A O   1 
ATOM   8458  C  CB  . GLN A 1 1048 ? 100.672 125.812 94.584  1.00 82.50  ? 1048 GLN A CB  1 
ATOM   8459  C  CG  . GLN A 1 1048 ? 102.122 125.707 94.165  1.00 93.16  ? 1048 GLN A CG  1 
ATOM   8460  C  CD  . GLN A 1 1048 ? 103.037 126.511 95.063  1.00 117.08 ? 1048 GLN A CD  1 
ATOM   8461  O  OE1 . GLN A 1 1048 ? 102.995 126.376 96.288  1.00 113.62 ? 1048 GLN A OE1 1 
ATOM   8462  N  NE2 . GLN A 1 1048 ? 103.871 127.350 94.464  1.00 111.25 ? 1048 GLN A NE2 1 
ATOM   8463  N  N   . VAL A 1 1049 ? 97.524  125.527 94.651  1.00 82.34  ? 1049 VAL A N   1 
ATOM   8464  C  CA  . VAL A 1 1049 ? 96.309  125.256 95.414  1.00 71.52  ? 1049 VAL A CA  1 
ATOM   8465  C  C   . VAL A 1 1049 ? 95.519  124.132 94.756  1.00 74.85  ? 1049 VAL A C   1 
ATOM   8466  O  O   . VAL A 1 1049 ? 94.958  123.258 95.432  1.00 87.36  ? 1049 VAL A O   1 
ATOM   8467  C  CB  . VAL A 1 1049 ? 95.461  126.528 95.572  1.00 66.73  ? 1049 VAL A CB  1 
ATOM   8468  C  CG1 . VAL A 1 1049 ? 94.080  126.185 96.106  1.00 71.15  ? 1049 VAL A CG1 1 
ATOM   8469  C  CG2 . VAL A 1 1049 ? 96.128  127.490 96.511  1.00 84.26  ? 1049 VAL A CG2 1 
ATOM   8470  N  N   . LEU A 1 1050 ? 95.452  124.135 93.418  1.00 77.12  ? 1050 LEU A N   1 
ATOM   8471  C  CA  . LEU A 1 1050 ? 94.837  123.006 92.721  1.00 72.87  ? 1050 LEU A CA  1 
ATOM   8472  C  C   . LEU A 1 1050 ? 95.506  121.693 93.109  1.00 80.61  ? 1050 LEU A C   1 
ATOM   8473  O  O   . LEU A 1 1050 ? 94.828  120.713 93.436  1.00 94.28  ? 1050 LEU A O   1 
ATOM   8474  C  CB  . LEU A 1 1050 ? 94.898  123.228 91.213  1.00 78.68  ? 1050 LEU A CB  1 
ATOM   8475  C  CG  . LEU A 1 1050 ? 93.604  123.854 90.704  1.00 78.90  ? 1050 LEU A CG  1 
ATOM   8476  C  CD1 . LEU A 1 1050 ? 93.725  124.206 89.236  1.00 102.31 ? 1050 LEU A CD1 1 
ATOM   8477  C  CD2 . LEU A 1 1050 ? 92.428  122.912 90.956  1.00 78.43  ? 1050 LEU A CD2 1 
ATOM   8478  N  N   . GLY A 1 1051 ? 96.841  121.672 93.123  1.00 83.46  ? 1051 GLY A N   1 
ATOM   8479  C  CA  . GLY A 1 1051 ? 97.547  120.449 93.478  1.00 87.40  ? 1051 GLY A CA  1 
ATOM   8480  C  C   . GLY A 1 1051 ? 97.236  119.982 94.888  1.00 89.16  ? 1051 GLY A C   1 
ATOM   8481  O  O   . GLY A 1 1051 ? 97.111  118.782 95.143  1.00 91.38  ? 1051 GLY A O   1 
ATOM   8482  N  N   . TYR A 1 1052 ? 97.116  120.923 95.828  1.00 94.33  ? 1052 TYR A N   1 
ATOM   8483  C  CA  . TYR A 1 1052 ? 96.728  120.541 97.184  1.00 87.19  ? 1052 TYR A CA  1 
ATOM   8484  C  C   . TYR A 1 1052 ? 95.323  119.958 97.201  1.00 88.44  ? 1052 TYR A C   1 
ATOM   8485  O  O   . TYR A 1 1052 ? 95.062  118.966 97.894  1.00 91.80  ? 1052 TYR A O   1 
ATOM   8486  C  CB  . TYR A 1 1052 ? 96.849  121.729 98.133  1.00 77.84  ? 1052 TYR A CB  1 
ATOM   8487  C  CG  . TYR A 1 1052 ? 98.278  122.165 98.280  1.00 91.74  ? 1052 TYR A CG  1 
ATOM   8488  C  CD1 . TYR A 1 1052 ? 99.306  121.235 98.203  1.00 106.19 ? 1052 TYR A CD1 1 
ATOM   8489  C  CD2 . TYR A 1 1052 ? 98.609  123.493 98.483  1.00 96.33  ? 1052 TYR A CD2 1 
ATOM   8490  C  CE1 . TYR A 1 1052 ? 100.621 121.613 98.326  1.00 125.01 ? 1052 TYR A CE1 1 
ATOM   8491  C  CE2 . TYR A 1 1052 ? 99.925  123.881 98.606  1.00 104.97 ? 1052 TYR A CE2 1 
ATOM   8492  C  CZ  . TYR A 1 1052 ? 100.927 122.938 98.531  1.00 119.20 ? 1052 TYR A CZ  1 
ATOM   8493  O  OH  . TYR A 1 1052 ? 102.242 123.323 98.655  1.00 122.78 ? 1052 TYR A OH  1 
ATOM   8494  N  N   . LEU A 1 1053 ? 94.408  120.556 96.441  1.00 98.08  ? 1053 LEU A N   1 
ATOM   8495  C  CA  . LEU A 1 1053 ? 93.001  120.189 96.534  1.00 91.85  ? 1053 LEU A CA  1 
ATOM   8496  C  C   . LEU A 1 1053 ? 92.646  118.975 95.690  1.00 100.57 ? 1053 LEU A C   1 
ATOM   8497  O  O   . LEU A 1 1053 ? 91.514  118.490 95.786  1.00 112.03 ? 1053 LEU A O   1 
ATOM   8498  C  CB  . LEU A 1 1053 ? 92.115  121.366 96.135  1.00 84.73  ? 1053 LEU A CB  1 
ATOM   8499  C  CG  . LEU A 1 1053 ? 92.069  122.472 97.183  1.00 88.86  ? 1053 LEU A CG  1 
ATOM   8500  C  CD1 . LEU A 1 1053 ? 91.184  123.606 96.719  1.00 77.47  ? 1053 LEU A CD1 1 
ATOM   8501  C  CD2 . LEU A 1 1053 ? 91.544  121.886 98.484  1.00 101.06 ? 1053 LEU A CD2 1 
ATOM   8502  N  N   . GLU A 1 1054 ? 93.571  118.477 94.866  1.00 110.38 ? 1054 GLU A N   1 
ATOM   8503  C  CA  . GLU A 1 1054 ? 93.224  117.371 93.978  1.00 110.91 ? 1054 GLU A CA  1 
ATOM   8504  C  C   . GLU A 1 1054 ? 92.927  116.106 94.771  1.00 123.43 ? 1054 GLU A C   1 
ATOM   8505  O  O   . GLU A 1 1054 ? 91.968  115.388 94.467  1.00 132.61 ? 1054 GLU A O   1 
ATOM   8506  C  CB  . GLU A 1 1054 ? 94.347  117.127 92.974  1.00 114.27 ? 1054 GLU A CB  1 
ATOM   8507  C  CG  . GLU A 1 1054 ? 94.437  118.177 91.889  1.00 121.91 ? 1054 GLU A CG  1 
ATOM   8508  C  CD  . GLU A 1 1054 ? 95.602  117.952 90.958  1.00 124.14 ? 1054 GLU A CD  1 
ATOM   8509  O  OE1 . GLU A 1 1054 ? 96.430  117.063 91.249  1.00 126.65 ? 1054 GLU A OE1 1 
ATOM   8510  O  OE2 . GLU A 1 1054 ? 95.690  118.660 89.932  1.00 113.96 ? 1054 GLU A OE2 1 
ATOM   8511  N  N   . GLY A 1 1055 ? 93.729  115.818 95.791  1.00 121.32 ? 1055 GLY A N   1 
ATOM   8512  C  CA  . GLY A 1 1055 ? 93.583  114.573 96.517  1.00 126.19 ? 1055 GLY A CA  1 
ATOM   8513  C  C   . GLY A 1 1055 ? 92.397  114.584 97.460  1.00 133.14 ? 1055 GLY A C   1 
ATOM   8514  O  O   . GLY A 1 1055 ? 92.575  114.534 98.681  1.00 133.53 ? 1055 GLY A O   1 
ATOM   8515  N  N   . THR A 1 1056 ? 91.178  114.647 96.917  1.00 132.92 ? 1056 THR A N   1 
ATOM   8516  C  CA  . THR A 1 1056 ? 89.967  114.695 97.730  1.00 141.02 ? 1056 THR A CA  1 
ATOM   8517  C  C   . THR A 1 1056 ? 88.897  113.805 97.107  1.00 148.85 ? 1056 THR A C   1 
ATOM   8518  O  O   . THR A 1 1056 ? 89.090  113.209 96.041  1.00 148.68 ? 1056 THR A O   1 
ATOM   8519  C  CB  . THR A 1 1056 ? 89.432  116.128 97.888  1.00 133.07 ? 1056 THR A CB  1 
ATOM   8520  O  OG1 . THR A 1 1056 ? 89.038  116.643 96.609  1.00 131.88 ? 1056 THR A OG1 1 
ATOM   8521  C  CG2 . THR A 1 1056 ? 90.470  117.050 98.520  1.00 126.75 ? 1056 THR A CG2 1 
ATOM   8522  N  N   . ARG A 1 1057 ? 87.751  113.739 97.783  1.00 153.12 ? 1057 ARG A N   1 
ATOM   8523  C  CA  . ARG A 1 1057 ? 86.564  113.030 97.327  1.00 154.88 ? 1057 ARG A CA  1 
ATOM   8524  C  C   . ARG A 1 1057 ? 85.400  114.001 97.178  1.00 164.30 ? 1057 ARG A C   1 
ATOM   8525  O  O   . ARG A 1 1057 ? 85.403  115.081 97.774  1.00 158.61 ? 1057 ARG A O   1 
ATOM   8526  C  CB  . ARG A 1 1057 ? 86.190  111.908 98.313  1.00 160.74 ? 1057 ARG A CB  1 
ATOM   8527  C  CG  . ARG A 1 1057 ? 85.354  110.768 97.733  1.00 171.61 ? 1057 ARG A CG  1 
ATOM   8528  C  CD  . ARG A 1 1057 ? 83.858  111.007 97.846  1.00 180.84 ? 1057 ARG A CD  1 
ATOM   8529  N  NE  . ARG A 1 1057 ? 83.101  110.006 97.102  1.00 176.31 ? 1057 ARG A NE  1 
ATOM   8530  C  CZ  . ARG A 1 1057 ? 81.774  109.975 97.026  1.00 165.08 ? 1057 ARG A CZ  1 
ATOM   8531  N  NH1 . ARG A 1 1057 ? 81.051  110.894 97.650  1.00 161.19 ? 1057 ARG A NH1 1 
ATOM   8532  N  NH2 . ARG A 1 1057 ? 81.171  109.024 96.327  1.00 161.99 ? 1057 ARG A NH2 1 
ATOM   8533  N  N   . THR A 1 1058 ? 84.465  113.644 96.287  1.00 167.78 ? 1058 THR A N   1 
ATOM   8534  C  CA  . THR A 1 1058 ? 83.217  114.343 95.946  1.00 171.70 ? 1058 THR A CA  1 
ATOM   8535  C  C   . THR A 1 1058 ? 83.487  115.763 95.462  1.00 159.37 ? 1058 THR A C   1 
ATOM   8536  O  O   . THR A 1 1058 ? 82.557  116.519 95.161  1.00 150.42 ? 1058 THR A O   1 
ATOM   8537  C  CB  . THR A 1 1058 ? 82.191  114.347 97.095  1.00 177.20 ? 1058 THR A CB  1 
ATOM   8538  O  OG1 . THR A 1 1058 ? 80.935  114.809 96.586  1.00 174.30 ? 1058 THR A OG1 1 
ATOM   8539  C  CG2 . THR A 1 1058 ? 82.569  115.300 98.216  1.00 168.74 ? 1058 THR A CG2 1 
ATOM   8540  N  N   . LEU A 1 1059 ? 84.763  116.121 95.380  1.00 161.76 ? 1059 LEU A N   1 
ATOM   8541  C  CA  . LEU A 1 1059 ? 85.233  117.340 94.745  1.00 162.48 ? 1059 LEU A CA  1 
ATOM   8542  C  C   . LEU A 1 1059 ? 85.879  117.018 93.410  1.00 150.70 ? 1059 LEU A C   1 
ATOM   8543  O  O   . LEU A 1 1059 ? 85.528  117.603 92.381  1.00 140.75 ? 1059 LEU A O   1 
ATOM   8544  C  CB  . LEU A 1 1059 ? 86.229  118.059 95.668  1.00 156.06 ? 1059 LEU A CB  1 
ATOM   8545  C  CG  . LEU A 1 1059 ? 86.904  119.328 95.155  1.00 130.89 ? 1059 LEU A CG  1 
ATOM   8546  C  CD1 . LEU A 1 1059 ? 85.867  120.405 94.900  1.00 113.76 ? 1059 LEU A CD1 1 
ATOM   8547  C  CD2 . LEU A 1 1059 ? 87.947  119.803 96.155  1.00 111.35 ? 1059 LEU A CD2 1 
ATOM   8548  N  N   . LEU A 1 1060 ? 86.819  116.075 93.417  1.00 149.94 ? 1060 LEU A N   1 
ATOM   8549  C  CA  . LEU A 1 1060 ? 87.345  115.531 92.175  1.00 152.73 ? 1060 LEU A CA  1 
ATOM   8550  C  C   . LEU A 1 1060 ? 86.307  114.646 91.492  1.00 160.06 ? 1060 LEU A C   1 
ATOM   8551  O  O   . LEU A 1 1060 ? 86.195  114.643 90.261  1.00 154.13 ? 1060 LEU A O   1 
ATOM   8552  C  CB  . LEU A 1 1060 ? 88.622  114.745 92.478  1.00 151.34 ? 1060 LEU A CB  1 
ATOM   8553  C  CG  . LEU A 1 1060 ? 89.383  113.985 91.395  1.00 152.52 ? 1060 LEU A CG  1 
ATOM   8554  C  CD1 . LEU A 1 1060 ? 90.871  114.081 91.663  1.00 146.96 ? 1060 LEU A CD1 1 
ATOM   8555  C  CD2 . LEU A 1 1060 ? 88.949  112.529 91.377  1.00 157.63 ? 1060 LEU A CD2 1 
ATOM   8556  N  N   . ALA A 1 1061 ? 85.537  113.890 92.283  1.00 162.47 ? 1061 ALA A N   1 
ATOM   8557  C  CA  . ALA A 1 1061 ? 84.653  112.868 91.728  1.00 163.00 ? 1061 ALA A CA  1 
ATOM   8558  C  C   . ALA A 1 1061 ? 83.528  113.476 90.895  1.00 161.58 ? 1061 ALA A C   1 
ATOM   8559  O  O   . ALA A 1 1061 ? 83.280  113.046 89.763  1.00 157.76 ? 1061 ALA A O   1 
ATOM   8560  C  CB  . ALA A 1 1061 ? 84.080  112.007 92.854  1.00 159.87 ? 1061 ALA A CB  1 
ATOM   8561  N  N   . SER A 1 1062 ? 82.839  114.478 91.435  1.00 155.25 ? 1062 SER A N   1 
ATOM   8562  C  CA  . SER A 1 1062 ? 81.662  115.034 90.768  1.00 145.17 ? 1062 SER A CA  1 
ATOM   8563  C  C   . SER A 1 1062 ? 82.038  115.857 89.541  1.00 141.77 ? 1062 SER A C   1 
ATOM   8564  O  O   . SER A 1 1062 ? 81.174  116.231 88.748  1.00 135.54 ? 1062 SER A O   1 
ATOM   8565  C  CB  . SER A 1 1062 ? 80.844  115.888 91.740  1.00 143.77 ? 1062 SER A CB  1 
ATOM   8566  O  OG  . SER A 1 1062 ? 79.646  116.339 91.129  1.00 131.79 ? 1062 SER A OG  1 
ATOM   8567  N  N   . GLY A 1 1071 ? 77.438  107.457 85.422  1.00 110.10 ? 1071 GLY A N   1 
ATOM   8568  C  CA  . GLY A 1 1071 ? 76.922  108.572 84.650  1.00 113.09 ? 1071 GLY A CA  1 
ATOM   8569  C  C   . GLY A 1 1071 ? 77.771  108.894 83.437  1.00 118.41 ? 1071 GLY A C   1 
ATOM   8570  O  O   . GLY A 1 1071 ? 78.189  107.992 82.715  1.00 113.25 ? 1071 GLY A O   1 
ATOM   8571  N  N   . THR A 1 1072 ? 78.025  110.184 83.211  1.00 118.01 ? 1072 THR A N   1 
ATOM   8572  C  CA  . THR A 1 1072 ? 78.881  110.615 82.112  1.00 110.78 ? 1072 THR A CA  1 
ATOM   8573  C  C   . THR A 1 1072 ? 80.349  110.765 82.497  1.00 107.70 ? 1072 THR A C   1 
ATOM   8574  O  O   . THR A 1 1072 ? 81.212  110.687 81.615  1.00 116.95 ? 1072 THR A O   1 
ATOM   8575  C  CB  . THR A 1 1072 ? 78.380  111.949 81.538  1.00 112.00 ? 1072 THR A CB  1 
ATOM   8576  O  OG1 . THR A 1 1072 ? 79.055  112.228 80.306  1.00 105.29 ? 1072 THR A OG1 1 
ATOM   8577  C  CG2 . THR A 1 1072 ? 78.626  113.093 82.518  1.00 114.29 ? 1072 THR A CG2 1 
ATOM   8578  N  N   . MET A 1 1073 ? 80.655  110.956 83.785  1.00 97.37  ? 1073 MET A N   1 
ATOM   8579  C  CA  . MET A 1 1073 ? 82.048  110.981 84.225  1.00 92.00  ? 1073 MET A CA  1 
ATOM   8580  C  C   . MET A 1 1073 ? 82.734  109.646 83.981  1.00 102.42 ? 1073 MET A C   1 
ATOM   8581  O  O   . MET A 1 1073 ? 83.881  109.594 83.503  1.00 107.78 ? 1073 MET A O   1 
ATOM   8582  C  CB  . MET A 1 1073 ? 82.099  111.337 85.712  1.00 86.98  ? 1073 MET A CB  1 
ATOM   8583  C  CG  . MET A 1 1073 ? 83.493  111.499 86.267  1.00 92.38  ? 1073 MET A CG  1 
ATOM   8584  S  SD  . MET A 1 1073 ? 84.403  112.827 85.470  1.00 132.01 ? 1073 MET A SD  1 
ATOM   8585  C  CE  . MET A 1 1073 ? 86.006  112.627 86.241  1.00 109.66 ? 1073 MET A CE  1 
ATOM   8586  N  N   . LEU A 1 1074 ? 82.025  108.553 84.255  1.00 93.75  ? 1074 LEU A N   1 
ATOM   8587  C  CA  . LEU A 1 1074 ? 82.574  107.233 83.991  1.00 84.81  ? 1074 LEU A CA  1 
ATOM   8588  C  C   . LEU A 1 1074 ? 82.823  107.026 82.511  1.00 88.98  ? 1074 LEU A C   1 
ATOM   8589  O  O   . LEU A 1 1074 ? 83.863  106.473 82.120  1.00 103.54 ? 1074 LEU A O   1 
ATOM   8590  C  CB  . LEU A 1 1074 ? 81.610  106.154 84.516  1.00 89.78  ? 1074 LEU A CB  1 
ATOM   8591  C  CG  . LEU A 1 1074 ? 82.217  104.758 84.572  1.00 84.07  ? 1074 LEU A CG  1 
ATOM   8592  C  CD1 . LEU A 1 1074 ? 83.365  104.740 85.546  1.00 91.91  ? 1074 LEU A CD1 1 
ATOM   8593  C  CD2 . LEU A 1 1074 ? 81.164  103.731 84.953  1.00 99.24  ? 1074 LEU A CD2 1 
ATOM   8594  N  N   . MET A 1 1075 ? 81.873  107.441 81.676  1.00 81.69  ? 1075 MET A N   1 
ATOM   8595  C  CA  . MET A 1 1075 ? 82.061  107.257 80.248  1.00 82.58  ? 1075 MET A CA  1 
ATOM   8596  C  C   . MET A 1 1075 ? 83.240  108.076 79.726  1.00 85.32  ? 1075 MET A C   1 
ATOM   8597  O  O   . MET A 1 1075 ? 84.013  107.597 78.880  1.00 95.25  ? 1075 MET A O   1 
ATOM   8598  C  CB  . MET A 1 1075 ? 80.785  107.624 79.512  1.00 98.12  ? 1075 MET A CB  1 
ATOM   8599  C  CG  . MET A 1 1075 ? 79.604  106.940 80.131  1.00 105.11 ? 1075 MET A CG  1 
ATOM   8600  S  SD  . MET A 1 1075 ? 79.583  105.163 79.853  1.00 120.10 ? 1075 MET A SD  1 
ATOM   8601  C  CE  . MET A 1 1075 ? 79.726  105.035 78.080  1.00 124.87 ? 1075 MET A CE  1 
ATOM   8602  N  N   . LYS A 1 1076 ? 83.381  109.306 80.213  1.00 76.71  ? 1076 LYS A N   1 
ATOM   8603  C  CA  . LYS A 1 1076 ? 84.513  110.146 79.852  1.00 77.05  ? 1076 LYS A CA  1 
ATOM   8604  C  C   . LYS A 1 1076 ? 85.835  109.468 80.197  1.00 81.17  ? 1076 LYS A C   1 
ATOM   8605  O  O   . LYS A 1 1076 ? 86.763  109.418 79.375  1.00 89.62  ? 1076 LYS A O   1 
ATOM   8606  C  CB  . LYS A 1 1076 ? 84.383  111.495 80.563  1.00 91.29  ? 1076 LYS A CB  1 
ATOM   8607  C  CG  . LYS A 1 1076 ? 85.572  112.421 80.432  1.00 107.04 ? 1076 LYS A CG  1 
ATOM   8608  C  CD  . LYS A 1 1076 ? 85.326  113.711 81.203  1.00 119.42 ? 1076 LYS A CD  1 
ATOM   8609  C  CE  . LYS A 1 1076 ? 86.583  114.560 81.292  1.00 124.01 ? 1076 LYS A CE  1 
ATOM   8610  N  NZ  . LYS A 1 1076 ? 87.569  113.996 82.253  1.00 118.11 ? 1076 LYS A NZ  1 
ATOM   8611  N  N   . LEU A 1 1077 ? 85.928  108.912 81.410  1.00 72.99  ? 1077 LEU A N   1 
ATOM   8612  C  CA  . LEU A 1 1077 ? 87.174  108.266 81.822  1.00 68.59  ? 1077 LEU A CA  1 
ATOM   8613  C  C   . LEU A 1 1077 ? 87.466  107.031 80.973  1.00 66.23  ? 1077 LEU A C   1 
ATOM   8614  O  O   . LEU A 1 1077 ? 88.621  106.788 80.596  1.00 71.06  ? 1077 LEU A O   1 
ATOM   8615  C  CB  . LEU A 1 1077 ? 87.105  107.894 83.302  1.00 77.24  ? 1077 LEU A CB  1 
ATOM   8616  C  CG  . LEU A 1 1077 ? 87.303  109.035 84.296  1.00 73.38  ? 1077 LEU A CG  1 
ATOM   8617  C  CD1 . LEU A 1 1077 ? 87.011  108.561 85.710  1.00 83.56  ? 1077 LEU A CD1 1 
ATOM   8618  C  CD2 . LEU A 1 1077 ? 88.722  109.575 84.187  1.00 79.45  ? 1077 LEU A CD2 1 
ATOM   8619  N  N   . ARG A 1 1078 ? 86.430  106.256 80.646  1.00 72.01  ? 1078 ARG A N   1 
ATOM   8620  C  CA  . ARG A 1 1078 ? 86.633  105.068 79.821  1.00 62.14  ? 1078 ARG A CA  1 
ATOM   8621  C  C   . ARG A 1 1078 ? 87.153  105.439 78.437  1.00 69.89  ? 1078 ARG A C   1 
ATOM   8622  O  O   . ARG A 1 1078 ? 88.073  104.792 77.906  1.00 78.29  ? 1078 ARG A O   1 
ATOM   8623  C  CB  . ARG A 1 1078 ? 85.323  104.297 79.701  1.00 65.53  ? 1078 ARG A CB  1 
ATOM   8624  C  CG  . ARG A 1 1078 ? 84.891  103.637 80.984  1.00 71.43  ? 1078 ARG A CG  1 
ATOM   8625  C  CD  . ARG A 1 1078 ? 83.681  102.771 80.748  1.00 65.00  ? 1078 ARG A CD  1 
ATOM   8626  N  NE  . ARG A 1 1078 ? 83.238  102.130 81.977  1.00 72.60  ? 1078 ARG A NE  1 
ATOM   8627  C  CZ  . ARG A 1 1078 ? 82.089  101.479 82.098  1.00 80.67  ? 1078 ARG A CZ  1 
ATOM   8628  N  NH1 . ARG A 1 1078 ? 81.268  101.384 81.060  1.00 88.44  ? 1078 ARG A NH1 1 
ATOM   8629  N  NH2 . ARG A 1 1078 ? 81.760  100.921 83.254  1.00 74.82  ? 1078 ARG A NH2 1 
ATOM   8630  N  N   . GLU A 1 1079 ? 86.579  106.485 77.838  1.00 72.49  ? 1079 GLU A N   1 
ATOM   8631  C  CA  . GLU A 1 1079 ? 87.038  106.901 76.518  1.00 68.28  ? 1079 GLU A CA  1 
ATOM   8632  C  C   . GLU A 1 1079 ? 88.476  107.407 76.567  1.00 78.04  ? 1079 GLU A C   1 
ATOM   8633  O  O   . GLU A 1 1079 ? 89.277  107.114 75.664  1.00 88.11  ? 1079 GLU A O   1 
ATOM   8634  C  CB  . GLU A 1 1079 ? 86.107  107.964 75.942  1.00 73.78  ? 1079 GLU A CB  1 
ATOM   8635  C  CG  . GLU A 1 1079 ? 86.442  108.293 74.508  1.00 102.06 ? 1079 GLU A CG  1 
ATOM   8636  C  CD  . GLU A 1 1079 ? 86.257  107.095 73.597  1.00 111.05 ? 1079 GLU A CD  1 
ATOM   8637  O  OE1 . GLU A 1 1079 ? 85.418  106.225 73.915  1.00 106.81 ? 1079 GLU A OE1 1 
ATOM   8638  O  OE2 . GLU A 1 1079 ? 86.975  107.004 72.580  1.00 102.70 ? 1079 GLU A OE2 1 
ATOM   8639  N  N   . LEU A 1 1080 ? 88.831  108.149 77.623  1.00 77.44  ? 1080 LEU A N   1 
ATOM   8640  C  CA  . LEU A 1 1080 ? 90.218  108.587 77.762  1.00 61.88  ? 1080 LEU A CA  1 
ATOM   8641  C  C   . LEU A 1 1080 ? 91.161  107.394 77.826  1.00 64.02  ? 1080 LEU A C   1 
ATOM   8642  O  O   . LEU A 1 1080 ? 92.229  107.400 77.195  1.00 77.12  ? 1080 LEU A O   1 
ATOM   8643  C  CB  . LEU A 1 1080 ? 90.386  109.454 79.009  1.00 66.21  ? 1080 LEU A CB  1 
ATOM   8644  C  CG  . LEU A 1 1080 ? 89.747  110.837 78.990  1.00 104.69 ? 1080 LEU A CG  1 
ATOM   8645  C  CD1 . LEU A 1 1080 ? 90.127  111.592 80.253  1.00 100.65 ? 1080 LEU A CD1 1 
ATOM   8646  C  CD2 . LEU A 1 1080 ? 90.182  111.595 77.746  1.00 120.20 ? 1080 LEU A CD2 1 
ATOM   8647  N  N   . THR A 1 1081 ? 90.792  106.369 78.598  1.00 66.03  ? 1081 THR A N   1 
ATOM   8648  C  CA  . THR A 1 1081 ? 91.664  105.206 78.740  1.00 55.51  ? 1081 THR A CA  1 
ATOM   8649  C  C   . THR A 1 1081 ? 91.864  104.494 77.405  1.00 57.21  ? 1081 THR A C   1 
ATOM   8650  O  O   . THR A 1 1081 ? 92.995  104.113 77.057  1.00 69.00  ? 1081 THR A O   1 
ATOM   8651  C  CB  . THR A 1 1081 ? 91.089  104.242 79.779  1.00 61.68  ? 1081 THR A CB  1 
ATOM   8652  O  OG1 . THR A 1 1081 ? 90.970  104.914 81.040  1.00 76.68  ? 1081 THR A OG1 1 
ATOM   8653  C  CG2 . THR A 1 1081 ? 91.991  103.028 79.941  1.00 59.47  ? 1081 THR A CG2 1 
ATOM   8654  N  N   . ARG A 1 1082 ? 90.785  104.315 76.635  1.00 53.33  ? 1082 ARG A N   1 
ATOM   8655  C  CA  . ARG A 1 1082 ? 90.946  103.661 75.338  1.00 49.97  ? 1082 ARG A CA  1 
ATOM   8656  C  C   . ARG A 1 1082 ? 91.841  104.478 74.408  1.00 58.52  ? 1082 ARG A C   1 
ATOM   8657  O  O   . ARG A 1 1082 ? 92.700  103.917 73.707  1.00 72.33  ? 1082 ARG A O   1 
ATOM   8658  C  CB  . ARG A 1 1082 ? 89.581  103.419 74.688  1.00 69.64  ? 1082 ARG A CB  1 
ATOM   8659  C  CG  . ARG A 1 1082 ? 88.746  102.335 75.354  1.00 72.31  ? 1082 ARG A CG  1 
ATOM   8660  C  CD  . ARG A 1 1082 ? 87.330  102.278 74.786  1.00 87.35  ? 1082 ARG A CD  1 
ATOM   8661  N  NE  . ARG A 1 1082 ? 87.281  101.665 73.460  1.00 77.16  ? 1082 ARG A NE  1 
ATOM   8662  C  CZ  . ARG A 1 1082 ? 87.280  102.342 72.317  1.00 88.20  ? 1082 ARG A CZ  1 
ATOM   8663  N  NH1 . ARG A 1 1082 ? 87.322  103.668 72.323  1.00 93.94  ? 1082 ARG A NH1 1 
ATOM   8664  N  NH2 . ARG A 1 1082 ? 87.233  101.694 71.160  1.00 85.40  ? 1082 ARG A NH2 1 
ATOM   8665  N  N   . ASN A 1 1083 ? 91.677  105.806 74.405  1.00 65.28  ? 1083 ASN A N   1 
ATOM   8666  C  CA  . ASN A 1 1083 ? 92.533  106.640 73.562  1.00 64.79  ? 1083 ASN A CA  1 
ATOM   8667  C  C   . ASN A 1 1083 ? 94.004  106.519 73.955  1.00 62.83  ? 1083 ASN A C   1 
ATOM   8668  O  O   . ASN A 1 1083 ? 94.884  106.405 73.087  1.00 66.63  ? 1083 ASN A O   1 
ATOM   8669  C  CB  . ASN A 1 1083 ? 92.082  108.099 73.636  1.00 77.49  ? 1083 ASN A CB  1 
ATOM   8670  C  CG  . ASN A 1 1083 ? 90.964  108.411 72.665  1.00 86.23  ? 1083 ASN A CG  1 
ATOM   8671  O  OD1 . ASN A 1 1083 ? 90.598  107.580 71.836  1.00 81.62  ? 1083 ASN A OD1 1 
ATOM   8672  N  ND2 . ASN A 1 1083 ? 90.422  109.621 72.753  1.00 87.87  ? 1083 ASN A ND2 1 
ATOM   8673  N  N   . ARG A 1 1084 ? 94.288  106.527 75.261  1.00 58.78  ? 1084 ARG A N   1 
ATOM   8674  C  CA  . ARG A 1 1084 ? 95.675  106.420 75.706  1.00 41.84  ? 1084 ARG A CA  1 
ATOM   8675  C  C   . ARG A 1 1084 ? 96.295  105.087 75.307  1.00 53.64  ? 1084 ARG A C   1 
ATOM   8676  O  O   . ARG A 1 1084 ? 97.463  105.035 74.900  1.00 71.87  ? 1084 ARG A O   1 
ATOM   8677  C  CB  . ARG A 1 1084 ? 95.770  106.629 77.213  1.00 46.16  ? 1084 ARG A CB  1 
ATOM   8678  C  CG  . ARG A 1 1084 ? 96.006  108.074 77.598  1.00 52.96  ? 1084 ARG A CG  1 
ATOM   8679  C  CD  . ARG A 1 1084 ? 95.368  108.398 78.928  1.00 53.22  ? 1084 ARG A CD  1 
ATOM   8680  N  NE  . ARG A 1 1084 ? 96.235  107.991 80.029  1.00 59.49  ? 1084 ARG A NE  1 
ATOM   8681  C  CZ  . ARG A 1 1084 ? 97.295  108.681 80.437  1.00 74.33  ? 1084 ARG A CZ  1 
ATOM   8682  N  NH1 . ARG A 1 1084 ? 97.627  109.813 79.832  1.00 77.09  ? 1084 ARG A NH1 1 
ATOM   8683  N  NH2 . ARG A 1 1084 ? 98.030  108.233 81.445  1.00 80.57  ? 1084 ARG A NH2 1 
ATOM   8684  N  N   . TRP A 1 1085 ? 95.538  103.994 75.430  1.00 53.23  ? 1085 TRP A N   1 
ATOM   8685  C  CA  . TRP A 1 1085 ? 96.097  102.701 75.040  1.00 49.45  ? 1085 TRP A CA  1 
ATOM   8686  C  C   . TRP A 1 1085 ? 96.375  102.647 73.543  1.00 46.25  ? 1085 TRP A C   1 
ATOM   8687  O  O   . TRP A 1 1085 ? 97.429  102.140 73.114  1.00 68.61  ? 1085 TRP A O   1 
ATOM   8688  C  CB  . TRP A 1 1085 ? 95.169  101.570 75.478  1.00 46.44  ? 1085 TRP A CB  1 
ATOM   8689  C  CG  . TRP A 1 1085 ? 95.384  101.191 76.906  1.00 51.71  ? 1085 TRP A CG  1 
ATOM   8690  C  CD1 . TRP A 1 1085 ? 95.184  101.976 78.004  1.00 55.08  ? 1085 TRP A CD1 1 
ATOM   8691  C  CD2 . TRP A 1 1085 ? 95.851  99.929  77.394  1.00 52.00  ? 1085 TRP A CD2 1 
ATOM   8692  N  NE1 . TRP A 1 1085 ? 95.501  101.279 79.146  1.00 48.52  ? 1085 TRP A NE1 1 
ATOM   8693  C  CE2 . TRP A 1 1085 ? 95.911  100.019 78.798  1.00 47.43  ? 1085 TRP A CE2 1 
ATOM   8694  C  CE3 . TRP A 1 1085 ? 96.222  98.728  76.778  1.00 58.01  ? 1085 TRP A CE3 1 
ATOM   8695  C  CZ2 . TRP A 1 1085 ? 96.327  98.955  79.597  1.00 44.40  ? 1085 TRP A CZ2 1 
ATOM   8696  C  CZ3 . TRP A 1 1085 ? 96.636  97.675  77.574  1.00 55.63  ? 1085 TRP A CZ3 1 
ATOM   8697  C  CH2 . TRP A 1 1085 ? 96.685  97.794  78.967  1.00 52.23  ? 1085 TRP A CH2 1 
ATOM   8698  N  N   . LYS A 1 1086 ? 95.463  103.206 72.734  1.00 58.17  ? 1086 LYS A N   1 
ATOM   8699  C  CA  . LYS A 1 1086 ? 95.711  103.266 71.297  1.00 51.78  ? 1086 LYS A CA  1 
ATOM   8700  C  C   . LYS A 1 1086 ? 96.991  104.025 70.995  1.00 58.00  ? 1086 LYS A C   1 
ATOM   8701  O  O   . LYS A 1 1086 ? 97.776  103.613 70.132  1.00 66.60  ? 1086 LYS A O   1 
ATOM   8702  C  CB  . LYS A 1 1086 ? 94.543  103.922 70.563  1.00 58.14  ? 1086 LYS A CB  1 
ATOM   8703  C  CG  . LYS A 1 1086 ? 93.267  103.122 70.513  1.00 73.93  ? 1086 LYS A CG  1 
ATOM   8704  C  CD  . LYS A 1 1086 ? 92.203  103.923 69.791  1.00 77.88  ? 1086 LYS A CD  1 
ATOM   8705  C  CE  . LYS A 1 1086 ? 90.880  103.192 69.764  1.00 99.13  ? 1086 LYS A CE  1 
ATOM   8706  N  NZ  . LYS A 1 1086 ? 89.835  104.004 69.088  1.00 88.34  ? 1086 LYS A NZ  1 
ATOM   8707  N  N   . SER A 1 1087 ? 97.226  105.135 71.695  1.00 65.39  ? 1087 SER A N   1 
ATOM   8708  C  CA  . SER A 1 1087 ? 98.440  105.901 71.424  1.00 56.30  ? 1087 SER A CA  1 
ATOM   8709  C  C   . SER A 1 1087 ? 99.700  105.176 71.896  1.00 52.19  ? 1087 SER A C   1 
ATOM   8710  O  O   . SER A 1 1087 ? 100.746 105.286 71.247  1.00 63.24  ? 1087 SER A O   1 
ATOM   8711  C  CB  . SER A 1 1087 ? 98.359  107.283 72.071  1.00 51.76  ? 1087 SER A CB  1 
ATOM   8712  O  OG  . SER A 1 1087 ? 98.820  107.248 73.409  1.00 68.48  ? 1087 SER A OG  1 
ATOM   8713  N  N   . TRP A 1 1088 ? 99.628  104.431 73.006  1.00 60.92  ? 1088 TRP A N   1 
ATOM   8714  C  CA  . TRP A 1 1088 ? 100.827 103.766 73.524  1.00 53.01  ? 1088 TRP A CA  1 
ATOM   8715  C  C   . TRP A 1 1088 ? 101.271 102.577 72.675  1.00 50.56  ? 1088 TRP A C   1 
ATOM   8716  O  O   . TRP A 1 1088 ? 102.464 102.431 72.386  1.00 54.32  ? 1088 TRP A O   1 
ATOM   8717  C  CB  . TRP A 1 1088 ? 100.627 103.314 74.966  1.00 49.06  ? 1088 TRP A CB  1 
ATOM   8718  C  CG  . TRP A 1 1088 ? 100.649 104.428 75.939  1.00 60.83  ? 1088 TRP A CG  1 
ATOM   8719  C  CD1 . TRP A 1 1088 ? 101.366 105.583 75.845  1.00 60.62  ? 1088 TRP A CD1 1 
ATOM   8720  C  CD2 . TRP A 1 1088 ? 100.009 104.454 77.216  1.00 54.53  ? 1088 TRP A CD2 1 
ATOM   8721  N  NE1 . TRP A 1 1088 ? 101.162 106.357 76.961  1.00 53.24  ? 1088 TRP A NE1 1 
ATOM   8722  C  CE2 . TRP A 1 1088 ? 100.339 105.682 77.821  1.00 58.19  ? 1088 TRP A CE2 1 
ATOM   8723  C  CE3 . TRP A 1 1088 ? 99.169  103.570 77.896  1.00 54.01  ? 1088 TRP A CE3 1 
ATOM   8724  C  CZ2 . TRP A 1 1088 ? 99.857  106.045 79.075  1.00 71.28  ? 1088 TRP A CZ2 1 
ATOM   8725  C  CZ3 . TRP A 1 1088 ? 98.694  103.931 79.140  1.00 49.93  ? 1088 TRP A CZ3 1 
ATOM   8726  C  CH2 . TRP A 1 1088 ? 99.037  105.158 79.717  1.00 61.50  ? 1088 TRP A CH2 1 
ATOM   8727  N  N   . PHE A 1 1089 ? 100.337 101.718 72.262  1.00 64.15  ? 1089 PHE A N   1 
ATOM   8728  C  CA  . PHE A 1 1089 ? 100.661 100.399 71.698  1.00 61.18  ? 1089 PHE A CA  1 
ATOM   8729  C  C   . PHE A 1 1089 ? 100.578 100.326 70.181  1.00 72.72  ? 1089 PHE A C   1 
ATOM   8730  O  O   . PHE A 1 1089 ? 100.674 99.232  69.613  1.00 76.91  ? 1089 PHE A O   1 
ATOM   8731  C  CB  . PHE A 1 1089 ? 99.742  99.342  72.328  1.00 68.50  ? 1089 PHE A CB  1 
ATOM   8732  C  CG  . PHE A 1 1089 ? 100.071 99.045  73.760  1.00 74.62  ? 1089 PHE A CG  1 
ATOM   8733  C  CD1 . PHE A 1 1089 ? 101.185 98.270  74.052  1.00 72.02  ? 1089 PHE A CD1 1 
ATOM   8734  C  CD2 . PHE A 1 1089 ? 99.417  99.678  74.800  1.00 85.31  ? 1089 PHE A CD2 1 
ATOM   8735  C  CE1 . PHE A 1 1089 ? 101.549 98.000  75.355  1.00 79.49  ? 1089 PHE A CE1 1 
ATOM   8736  C  CE2 . PHE A 1 1089 ? 99.794  99.435  76.118  1.00 73.18  ? 1089 PHE A CE2 1 
ATOM   8737  C  CZ  . PHE A 1 1089 ? 100.863 98.594  76.389  1.00 68.66  ? 1089 PHE A CZ  1 
ATOM   8738  N  N   . SER A 1 1090 ? 100.452 101.462 69.504  1.00 72.39  ? 1090 SER A N   1 
ATOM   8739  C  CA  . SER A 1 1090 ? 100.536 101.511 68.049  1.00 73.05  ? 1090 SER A CA  1 
ATOM   8740  C  C   . SER A 1 1090 ? 101.554 102.555 67.619  1.00 88.94  ? 1090 SER A C   1 
ATOM   8741  O  O   . SER A 1 1090 ? 101.439 103.725 67.999  1.00 91.81  ? 1090 SER A O   1 
ATOM   8742  C  CB  . SER A 1 1090 ? 99.164  101.795 67.423  1.00 87.15  ? 1090 SER A CB  1 
ATOM   8743  O  OG  . SER A 1 1090 ? 98.358  100.632 67.448  1.00 97.88  ? 1090 SER A OG  1 
ATOM   8744  N  N   . TYR A 1 1091 ? 102.544 102.138 66.824  1.00 91.88  ? 1091 TYR A N   1 
ATOM   8745  C  CA  . TYR A 1 1091 ? 103.571 103.046 66.326  1.00 102.37 ? 1091 TYR A CA  1 
ATOM   8746  C  C   . TYR A 1 1091 ? 103.490 103.272 64.821  1.00 102.26 ? 1091 TYR A C   1 
ATOM   8747  O  O   . TYR A 1 1091 ? 104.121 104.207 64.322  1.00 105.52 ? 1091 TYR A O   1 
ATOM   8748  C  CB  . TYR A 1 1091 ? 105.005 102.592 66.675  1.00 95.54  ? 1091 TYR A CB  1 
ATOM   8749  C  CG  . TYR A 1 1091 ? 105.459 101.290 66.036  1.00 98.02  ? 1091 TYR A CG  1 
ATOM   8750  C  CD1 . TYR A 1 1091 ? 105.306 100.082 66.701  1.00 101.72 ? 1091 TYR A CD1 1 
ATOM   8751  C  CD2 . TYR A 1 1091 ? 105.946 101.259 64.730  1.00 93.74  ? 1091 TYR A CD2 1 
ATOM   8752  C  CE1 . TYR A 1 1091 ? 105.703 98.882  66.119  1.00 83.78  ? 1091 TYR A CE1 1 
ATOM   8753  C  CE2 . TYR A 1 1091 ? 106.327 100.067 64.133  1.00 105.70 ? 1091 TYR A CE2 1 
ATOM   8754  C  CZ  . TYR A 1 1091 ? 106.204 98.883  64.825  1.00 102.27 ? 1091 TYR A CZ  1 
ATOM   8755  O  OH  . TYR A 1 1091 ? 106.592 97.708  64.216  1.00 96.50  ? 1091 TYR A OH  1 
ATOM   8756  N  N   . ILE A 1 1092 ? 102.736 102.451 64.090  1.00 98.78  ? 1092 ILE A N   1 
ATOM   8757  C  CA  . ILE A 1 1092 ? 102.529 102.751 62.676  1.00 102.02 ? 1092 ILE A CA  1 
ATOM   8758  C  C   . ILE A 1 1092 ? 101.447 103.812 62.511  1.00 111.94 ? 1092 ILE A C   1 
ATOM   8759  O  O   . ILE A 1 1092 ? 101.466 104.577 61.542  1.00 113.85 ? 1092 ILE A O   1 
ATOM   8760  C  CB  . ILE A 1 1092 ? 102.171 101.471 61.896  1.00 101.47 ? 1092 ILE A CB  1 
ATOM   8761  C  CG1 . ILE A 1 1092 ? 103.218 100.383 62.114  1.00 105.56 ? 1092 ILE A CG1 1 
ATOM   8762  C  CG2 . ILE A 1 1092 ? 102.044 101.759 60.407  1.00 104.12 ? 1092 ILE A CG2 1 
ATOM   8763  C  CD1 . ILE A 1 1092 ? 104.489 100.612 61.324  1.00 105.85 ? 1092 ILE A CD1 1 
ATOM   8764  N  N   . ASP A 1 1093 ? 100.517 103.903 63.466  1.00 113.07 ? 1093 ASP A N   1 
ATOM   8765  C  CA  . ASP A 1 1093 ? 99.473  104.920 63.393  1.00 120.35 ? 1093 ASP A CA  1 
ATOM   8766  C  C   . ASP A 1 1093 ? 100.043 106.329 63.524  1.00 113.29 ? 1093 ASP A C   1 
ATOM   8767  O  O   . ASP A 1 1093 ? 99.620  107.242 62.806  1.00 113.97 ? 1093 ASP A O   1 
ATOM   8768  C  CB  . ASP A 1 1093 ? 98.428  104.667 64.477  1.00 116.81 ? 1093 ASP A CB  1 
ATOM   8769  C  CG  . ASP A 1 1093 ? 97.296  103.787 63.996  1.00 119.91 ? 1093 ASP A CG  1 
ATOM   8770  O  OD1 . ASP A 1 1093 ? 97.305  103.410 62.806  1.00 118.77 ? 1093 ASP A OD1 1 
ATOM   8771  O  OD2 . ASP A 1 1093 ? 96.397  103.475 64.804  1.00 125.00 ? 1093 ASP A OD2 1 
ATOM   8772  N  N   . ALA A 1 1094 ? 101.001 106.528 64.425  1.00 104.02 ? 1094 ALA A N   1 
ATOM   8773  C  CA  . ALA A 1 1094 ? 101.610 107.839 64.648  1.00 108.18 ? 1094 ALA A CA  1 
ATOM   8774  C  C   . ALA A 1 1094 ? 102.912 107.920 63.860  1.00 117.77 ? 1094 ALA A C   1 
ATOM   8775  O  O   . ALA A 1 1094 ? 103.932 107.356 64.265  1.00 120.31 ? 1094 ALA A O   1 
ATOM   8776  C  CB  . ALA A 1 1094 ? 101.843 108.080 66.135  1.00 88.24  ? 1094 ALA A CB  1 
ATOM   8777  N  N   . LEU A 1 1095 ? 102.875 108.625 62.729  1.00 111.40 ? 1095 LEU A N   1 
ATOM   8778  C  CA  . LEU A 1 1095 ? 104.061 108.824 61.909  1.00 102.18 ? 1095 LEU A CA  1 
ATOM   8779  C  C   . LEU A 1 1095 ? 103.949 110.120 61.119  1.00 116.46 ? 1095 LEU A C   1 
ATOM   8780  O  O   . LEU A 1 1095 ? 102.864 110.492 60.668  1.00 126.50 ? 1095 LEU A O   1 
ATOM   8781  C  CB  . LEU A 1 1095 ? 104.269 107.656 60.939  1.00 109.88 ? 1095 LEU A CB  1 
ATOM   8782  C  CG  . LEU A 1 1095 ? 105.200 106.534 61.391  1.00 102.12 ? 1095 LEU A CG  1 
ATOM   8783  C  CD1 . LEU A 1 1095 ? 105.184 105.395 60.387  1.00 97.98  ? 1095 LEU A CD1 1 
ATOM   8784  C  CD2 . LEU A 1 1095 ? 106.610 107.080 61.564  1.00 103.68 ? 1095 LEU A CD2 1 
ATOM   8785  N  N   . ASP A 1 1096 ? 105.087 110.789 60.951  1.00 115.08 ? 1096 ASP A N   1 
ATOM   8786  C  CA  . ASP A 1 1096 ? 105.252 111.913 60.030  1.00 127.46 ? 1096 ASP A CA  1 
ATOM   8787  C  C   . ASP A 1 1096 ? 106.365 111.549 59.057  1.00 130.37 ? 1096 ASP A C   1 
ATOM   8788  O  O   . ASP A 1 1096 ? 107.548 111.644 59.401  1.00 139.93 ? 1096 ASP A O   1 
ATOM   8789  C  CB  . ASP A 1 1096 ? 105.567 113.204 60.773  1.00 122.85 ? 1096 ASP A CB  1 
ATOM   8790  C  CG  . ASP A 1 1096 ? 104.358 113.792 61.447  1.00 127.81 ? 1096 ASP A CG  1 
ATOM   8791  O  OD1 . ASP A 1 1096 ? 103.254 113.681 60.876  1.00 135.40 ? 1096 ASP A OD1 1 
ATOM   8792  O  OD2 . ASP A 1 1096 ? 104.512 114.367 62.540  1.00 123.69 ? 1096 ASP A OD2 1 
ATOM   8793  N  N   . ASP A 1 1097 ? 105.990 111.123 57.848  1.00 120.96 ? 1097 ASP A N   1 
ATOM   8794  C  CA  . ASP A 1 1097 ? 107.001 110.693 56.888  1.00 138.59 ? 1097 ASP A CA  1 
ATOM   8795  C  C   . ASP A 1 1097 ? 107.966 111.821 56.555  1.00 139.13 ? 1097 ASP A C   1 
ATOM   8796  O  O   . ASP A 1 1097 ? 109.165 111.580 56.360  1.00 138.00 ? 1097 ASP A O   1 
ATOM   8797  C  CB  . ASP A 1 1097 ? 106.316 110.184 55.620  1.00 148.60 ? 1097 ASP A CB  1 
ATOM   8798  C  CG  . ASP A 1 1097 ? 105.517 108.919 55.859  1.00 149.25 ? 1097 ASP A CG  1 
ATOM   8799  O  OD1 . ASP A 1 1097 ? 105.887 108.146 56.766  1.00 143.38 ? 1097 ASP A OD1 1 
ATOM   8800  O  OD2 . ASP A 1 1097 ? 104.512 108.703 55.148  1.00 155.37 ? 1097 ASP A OD2 1 
ATOM   8801  N  N   . ASP A 1 1098 ? 107.471 113.059 56.516  1.00 140.34 ? 1098 ASP A N   1 
ATOM   8802  C  CA  . ASP A 1 1098 ? 108.350 114.202 56.302  1.00 141.85 ? 1098 ASP A CA  1 
ATOM   8803  C  C   . ASP A 1 1098 ? 109.348 114.354 57.441  1.00 133.70 ? 1098 ASP A C   1 
ATOM   8804  O  O   . ASP A 1 1098 ? 110.538 114.600 57.208  1.00 133.63 ? 1098 ASP A O   1 
ATOM   8805  C  CB  . ASP A 1 1098 ? 107.529 115.487 56.157  1.00 153.03 ? 1098 ASP A CB  1 
ATOM   8806  C  CG  . ASP A 1 1098 ? 106.491 115.397 55.062  1.00 174.04 ? 1098 ASP A CG  1 
ATOM   8807  O  OD1 . ASP A 1 1098 ? 106.772 114.758 54.028  1.00 168.78 ? 1098 ASP A OD1 1 
ATOM   8808  O  OD2 . ASP A 1 1098 ? 105.394 115.973 55.233  1.00 178.83 ? 1098 ASP A OD2 1 
ATOM   8809  N  N   . LEU A 1 1099 ? 108.879 114.204 58.680  1.00 126.17 ? 1099 LEU A N   1 
ATOM   8810  C  CA  . LEU A 1 1099 ? 109.758 114.364 59.832  1.00 115.19 ? 1099 LEU A CA  1 
ATOM   8811  C  C   . LEU A 1 1099 ? 110.841 113.277 59.817  1.00 112.85 ? 1099 LEU A C   1 
ATOM   8812  O  O   . LEU A 1 1099 ? 112.006 113.541 60.127  1.00 116.10 ? 1099 LEU A O   1 
ATOM   8813  C  CB  . LEU A 1 1099 ? 108.967 114.188 61.119  1.00 108.38 ? 1099 LEU A CB  1 
ATOM   8814  C  CG  . LEU A 1 1099 ? 109.644 114.397 62.476  1.00 100.19 ? 1099 LEU A CG  1 
ATOM   8815  C  CD1 . LEU A 1 1099 ? 110.284 115.821 62.556  1.00 98.42  ? 1099 LEU A CD1 1 
ATOM   8816  C  CD2 . LEU A 1 1099 ? 108.913 113.952 63.662  1.00 99.95  ? 1099 LEU A CD2 1 
ATOM   8817  N  N   . SER A 1 1100 ? 110.459 112.025 59.500  1.00 111.42 ? 1100 SER A N   1 
ATOM   8818  C  CA  . SER A 1 1100 ? 111.439 110.936 59.433  1.00 112.88 ? 1100 SER A CA  1 
ATOM   8819  C  C   . SER A 1 1100 ? 112.459 111.163 58.323  1.00 127.46 ? 1100 SER A C   1 
ATOM   8820  O  O   . SER A 1 1100 ? 113.673 110.996 58.533  1.00 126.37 ? 1100 SER A O   1 
ATOM   8821  C  CB  . SER A 1 1100 ? 110.716 109.598 59.222  1.00 106.68 ? 1100 SER A CB  1 
ATOM   8822  O  OG  . SER A 1 1100 ? 111.624 108.524 59.031  1.00 125.30 ? 1100 SER A OG  1 
ATOM   8823  N  N   . GLU A 1 1101 ? 111.988 111.612 57.154  1.00 130.65 ? 1101 GLU A N   1 
ATOM   8824  C  CA  . GLU A 1 1101 ? 112.893 111.908 56.051  1.00 132.54 ? 1101 GLU A CA  1 
ATOM   8825  C  C   . GLU A 1 1101 ? 113.873 113.009 56.427  1.00 127.55 ? 1101 GLU A C   1 
ATOM   8826  O  O   . GLU A 1 1101 ? 115.047 112.969 56.040  1.00 130.53 ? 1101 GLU A O   1 
ATOM   8827  C  CB  . GLU A 1 1101 ? 112.085 112.312 54.816  1.00 143.16 ? 1101 GLU A CB  1 
ATOM   8828  C  CG  . GLU A 1 1101 ? 112.931 112.625 53.607  1.00 161.21 ? 1101 GLU A CG  1 
ATOM   8829  C  CD  . GLU A 1 1101 ? 113.691 111.421 53.111  1.00 171.46 ? 1101 GLU A CD  1 
ATOM   8830  O  OE1 . GLU A 1 1101 ? 113.231 110.286 53.348  1.00 161.47 ? 1101 GLU A OE1 1 
ATOM   8831  O  OE2 . GLU A 1 1101 ? 114.760 111.609 52.492  1.00 169.13 ? 1101 GLU A OE2 1 
ATOM   8832  N  N   . SER A 1 1102 ? 113.396 114.004 57.179  1.00 121.23 ? 1102 SER A N   1 
ATOM   8833  C  CA  . SER A 1 1102 ? 114.243 115.104 57.618  1.00 118.12 ? 1102 SER A CA  1 
ATOM   8834  C  C   . SER A 1 1102 ? 115.236 114.687 58.709  1.00 114.01 ? 1102 SER A C   1 
ATOM   8835  O  O   . SER A 1 1102 ? 116.390 115.112 58.688  1.00 120.06 ? 1102 SER A O   1 
ATOM   8836  C  CB  . SER A 1 1102 ? 113.354 116.269 58.025  1.00 122.71 ? 1102 SER A CB  1 
ATOM   8837  O  OG  . SER A 1 1102 ? 112.505 115.916 59.088  1.00 125.72 ? 1102 SER A OG  1 
ATOM   8838  N  N   . LEU A 1 1103 ? 114.829 113.807 59.631  1.00 116.76 ? 1103 LEU A N   1 
ATOM   8839  C  CA  . LEU A 1 1103 ? 115.672 113.421 60.752  1.00 110.96 ? 1103 LEU A CA  1 
ATOM   8840  C  C   . LEU A 1 1103 ? 116.754 112.482 60.289  1.00 114.12 ? 1103 LEU A C   1 
ATOM   8841  O  O   . LEU A 1 1103 ? 117.796 112.354 60.944  1.00 114.63 ? 1103 LEU A O   1 
ATOM   8842  C  CB  . LEU A 1 1103 ? 114.894 112.786 61.904  1.00 106.75 ? 1103 LEU A CB  1 
ATOM   8843  C  CG  . LEU A 1 1103 ? 114.417 113.936 62.795  1.00 108.97 ? 1103 LEU A CG  1 
ATOM   8844  C  CD1 . LEU A 1 1103 ? 113.636 113.416 63.957  1.00 97.44  ? 1103 LEU A CD1 1 
ATOM   8845  C  CD2 . LEU A 1 1103 ? 115.647 114.745 63.250  1.00 88.70  ? 1103 LEU A CD2 1 
ATOM   8846  N  N   . GLU A 1 1104 ? 116.522 111.791 59.170  1.00 118.89 ? 1104 GLU A N   1 
ATOM   8847  C  CA  . GLU A 1 1104 ? 117.401 110.721 58.754  1.00 118.19 ? 1104 GLU A CA  1 
ATOM   8848  C  C   . GLU A 1 1104 ? 118.839 111.109 58.492  1.00 127.21 ? 1104 GLU A C   1 
ATOM   8849  O  O   . GLU A 1 1104 ? 119.696 110.266 58.736  1.00 125.22 ? 1104 GLU A O   1 
ATOM   8850  C  CB  . GLU A 1 1104 ? 116.862 110.348 57.377  1.00 140.76 ? 1104 GLU A CB  1 
ATOM   8851  C  CG  . GLU A 1 1104 ? 117.663 109.224 56.741  1.00 153.40 ? 1104 GLU A CG  1 
ATOM   8852  C  CD  . GLU A 1 1104 ? 118.882 109.751 56.022  1.00 156.77 ? 1104 GLU A CD  1 
ATOM   8853  O  OE1 . GLU A 1 1104 ? 118.723 110.939 55.634  1.00 150.32 ? 1104 GLU A OE1 1 
ATOM   8854  O  OE2 . GLU A 1 1104 ? 119.918 109.065 56.042  1.00 160.70 ? 1104 GLU A OE2 1 
ATOM   8855  N  N   . LYS A 1 1105 ? 119.109 112.383 58.270  1.00 130.84 ? 1105 LYS A N   1 
ATOM   8856  C  CA  . LYS A 1 1105 ? 120.441 112.862 57.946  1.00 130.13 ? 1105 LYS A CA  1 
ATOM   8857  C  C   . LYS A 1 1105 ? 121.382 113.050 59.137  1.00 120.84 ? 1105 LYS A C   1 
ATOM   8858  O  O   . LYS A 1 1105 ? 122.604 112.919 58.981  1.00 122.57 ? 1105 LYS A O   1 
ATOM   8859  C  CB  . LYS A 1 1105 ? 120.337 114.121 57.097  1.00 139.00 ? 1105 LYS A CB  1 
ATOM   8860  C  CG  . LYS A 1 1105 ? 119.321 115.124 57.549  1.00 143.49 ? 1105 LYS A CG  1 
ATOM   8861  C  CD  . LYS A 1 1105 ? 119.401 116.311 56.606  1.00 147.90 ? 1105 LYS A CD  1 
ATOM   8862  C  CE  . LYS A 1 1105 ? 120.681 117.081 56.837  1.00 151.74 ? 1105 LYS A CE  1 
ATOM   8863  N  NZ  . LYS A 1 1105 ? 120.659 117.899 58.067  1.00 143.20 ? 1105 LYS A NZ  1 
ATOM   8864  N  N   . PHE A 1 1106 ? 120.860 113.339 60.316  1.00 111.53 ? 1106 PHE A N   1 
ATOM   8865  C  CA  . PHE A 1 1106 ? 121.651 113.668 61.488  1.00 109.24 ? 1106 PHE A CA  1 
ATOM   8866  C  C   . PHE A 1 1106 ? 122.278 112.429 62.100  1.00 106.37 ? 1106 PHE A C   1 
ATOM   8867  O  O   . PHE A 1 1106 ? 121.785 111.308 61.960  1.00 107.21 ? 1106 PHE A O   1 
ATOM   8868  C  CB  . PHE A 1 1106 ? 120.729 114.332 62.519  1.00 106.67 ? 1106 PHE A CB  1 
ATOM   8869  C  CG  . PHE A 1 1106 ? 120.164 115.685 62.120  1.00 112.94 ? 1106 PHE A CG  1 
ATOM   8870  C  CD1 . PHE A 1 1106 ? 120.999 116.739 61.764  1.00 112.83 ? 1106 PHE A CD1 1 
ATOM   8871  C  CD2 . PHE A 1 1106 ? 118.839 115.770 61.722  1.00 114.51 ? 1106 PHE A CD2 1 
ATOM   8872  C  CE1 . PHE A 1 1106 ? 120.470 117.968 61.393  1.00 117.04 ? 1106 PHE A CE1 1 
ATOM   8873  C  CE2 . PHE A 1 1106 ? 118.309 116.962 61.258  1.00 116.80 ? 1106 PHE A CE2 1 
ATOM   8874  C  CZ  . PHE A 1 1106 ? 119.127 118.064 61.094  1.00 122.44 ? 1106 PHE A CZ  1 
ATOM   8875  N  N   . THR A 1 1107 ? 123.390 112.658 62.797  1.00 105.91 ? 1107 THR A N   1 
ATOM   8876  C  CA  . THR A 1 1107 ? 124.098 111.576 63.454  1.00 111.55 ? 1107 THR A CA  1 
ATOM   8877  C  C   . THR A 1 1107 ? 124.335 111.842 64.935  1.00 116.80 ? 1107 THR A C   1 
ATOM   8878  O  O   . THR A 1 1107 ? 124.341 110.899 65.730  1.00 112.62 ? 1107 THR A O   1 
ATOM   8879  C  CB  . THR A 1 1107 ? 125.429 111.311 62.746  1.00 125.87 ? 1107 THR A CB  1 
ATOM   8880  O  OG1 . THR A 1 1107 ? 126.059 110.166 63.331  1.00 121.68 ? 1107 THR A OG1 1 
ATOM   8881  C  CG2 . THR A 1 1107 ? 126.363 112.518 62.836  1.00 115.27 ? 1107 THR A CG2 1 
ATOM   8882  N  N   . CYS A 1 1108 ? 124.534 113.097 65.330  1.00 102.49 ? 1108 CYS A N   1 
ATOM   8883  C  CA  . CYS A 1 1108 ? 124.657 113.387 66.750  1.00 80.73  ? 1108 CYS A CA  1 
ATOM   8884  C  C   . CYS A 1 1108 ? 123.268 113.440 67.372  1.00 75.92  ? 1108 CYS A C   1 
ATOM   8885  O  O   . CYS A 1 1108 ? 122.287 113.802 66.716  1.00 94.54  ? 1108 CYS A O   1 
ATOM   8886  C  CB  . CYS A 1 1108 ? 125.405 114.698 66.990  1.00 88.09  ? 1108 CYS A CB  1 
ATOM   8887  S  SG  . CYS A 1 1108 ? 125.921 114.930 68.716  1.00 119.43 ? 1108 CYS A SG  1 
ATOM   8888  N  N   . THR A 1 1109 ? 123.186 113.087 68.655  1.00 71.07  ? 1109 THR A N   1 
ATOM   8889  C  CA  . THR A 1 1109 ? 121.889 113.075 69.320  1.00 75.82  ? 1109 THR A CA  1 
ATOM   8890  C  C   . THR A 1 1109 ? 121.398 114.479 69.656  1.00 83.06  ? 1109 THR A C   1 
ATOM   8891  O  O   . THR A 1 1109 ? 120.181 114.691 69.766  1.00 95.44  ? 1109 THR A O   1 
ATOM   8892  C  CB  . THR A 1 1109 ? 121.939 112.216 70.589  1.00 67.57  ? 1109 THR A CB  1 
ATOM   8893  O  OG1 . THR A 1 1109 ? 120.605 111.861 70.974  1.00 79.16  ? 1109 THR A OG1 1 
ATOM   8894  C  CG2 . THR A 1 1109 ? 122.601 112.970 71.739  1.00 92.66  ? 1109 THR A CG2 1 
ATOM   8895  N  N   . VAL A 1 1110 ? 122.308 115.451 69.744  1.00 77.73  ? 1110 VAL A N   1 
ATOM   8896  C  CA  . VAL A 1 1110 ? 121.914 116.824 70.041  1.00 73.74  ? 1110 VAL A CA  1 
ATOM   8897  C  C   . VAL A 1 1110 ? 121.161 117.418 68.860  1.00 86.63  ? 1110 VAL A C   1 
ATOM   8898  O  O   . VAL A 1 1110 ? 120.154 118.114 69.038  1.00 95.29  ? 1110 VAL A O   1 
ATOM   8899  C  CB  . VAL A 1 1110 ? 123.141 117.673 70.424  1.00 80.58  ? 1110 VAL A CB  1 
ATOM   8900  C  CG1 . VAL A 1 1110 ? 122.845 119.157 70.244  1.00 90.00  ? 1110 VAL A CG1 1 
ATOM   8901  C  CG2 . VAL A 1 1110 ? 123.548 117.397 71.863  1.00 83.40  ? 1110 VAL A CG2 1 
ATOM   8902  N  N   . ASP A 1 1111 ? 121.633 117.160 67.638  1.00 86.14  ? 1111 ASP A N   1 
ATOM   8903  C  CA  . ASP A 1 1111 ? 120.927 117.655 66.462  1.00 87.61  ? 1111 ASP A CA  1 
ATOM   8904  C  C   . ASP A 1 1111 ? 119.528 117.059 66.380  1.00 76.26  ? 1111 ASP A C   1 
ATOM   8905  O  O   . ASP A 1 1111 ? 118.562 117.761 66.049  1.00 82.72  ? 1111 ASP A O   1 
ATOM   8906  C  CB  . ASP A 1 1111 ? 121.718 117.316 65.198  1.00 83.90  ? 1111 ASP A CB  1 
ATOM   8907  C  CG  . ASP A 1 1111 ? 123.143 117.821 65.250  1.00 116.98 ? 1111 ASP A CG  1 
ATOM   8908  O  OD1 . ASP A 1 1111 ? 123.416 118.745 66.044  1.00 112.34 ? 1111 ASP A OD1 1 
ATOM   8909  O  OD2 . ASP A 1 1111 ? 123.990 117.288 64.504  1.00 121.79 ? 1111 ASP A OD2 1 
ATOM   8910  N  N   . VAL A 1 1112 ? 119.399 115.764 66.684  1.00 64.33  ? 1112 VAL A N   1 
ATOM   8911  C  CA  . VAL A 1 1112 ? 118.089 115.123 66.647  1.00 54.24  ? 1112 VAL A CA  1 
ATOM   8912  C  C   . VAL A 1 1112 ? 117.159 115.771 67.663  1.00 56.60  ? 1112 VAL A C   1 
ATOM   8913  O  O   . VAL A 1 1112 ? 115.997 116.078 67.360  1.00 74.23  ? 1112 VAL A O   1 
ATOM   8914  C  CB  . VAL A 1 1112 ? 118.227 113.608 66.892  1.00 56.58  ? 1112 VAL A CB  1 
ATOM   8915  C  CG1 . VAL A 1 1112 ? 116.855 112.963 67.059  1.00 60.97  ? 1112 VAL A CG1 1 
ATOM   8916  C  CG2 . VAL A 1 1112 ? 119.003 112.943 65.761  1.00 70.35  ? 1112 VAL A CG2 1 
ATOM   8917  N  N   . ALA A 1 1113 ? 117.662 116.018 68.878  1.00 53.56  ? 1113 ALA A N   1 
ATOM   8918  C  CA  . ALA A 1 1113 ? 116.829 116.649 69.899  1.00 51.67  ? 1113 ALA A CA  1 
ATOM   8919  C  C   . ALA A 1 1113 ? 116.422 118.065 69.500  1.00 64.53  ? 1113 ALA A C   1 
ATOM   8920  O  O   . ALA A 1 1113 ? 115.267 118.467 69.696  1.00 79.25  ? 1113 ALA A O   1 
ATOM   8921  C  CB  . ALA A 1 1113 ? 117.564 116.661 71.239  1.00 62.34  ? 1113 ALA A CB  1 
ATOM   8922  N  N   . ASN A 1 1114 ? 117.355 118.831 68.926  1.00 69.57  ? 1114 ASN A N   1 
ATOM   8923  C  CA  . ASN A 1 1114 ? 117.051 120.198 68.511  1.00 71.44  ? 1114 ASN A CA  1 
ATOM   8924  C  C   . ASN A 1 1114 ? 115.970 120.213 67.441  1.00 69.57  ? 1114 ASN A C   1 
ATOM   8925  O  O   . ASN A 1 1114 ? 115.008 120.992 67.515  1.00 71.46  ? 1114 ASN A O   1 
ATOM   8926  C  CB  . ASN A 1 1114 ? 118.318 120.879 67.991  1.00 76.65  ? 1114 ASN A CB  1 
ATOM   8927  C  CG  . ASN A 1 1114 ? 119.105 121.561 69.086  1.00 78.34  ? 1114 ASN A CG  1 
ATOM   8928  O  OD1 . ASN A 1 1114 ? 118.576 121.850 70.157  1.00 75.19  ? 1114 ASN A OD1 1 
ATOM   8929  N  ND2 . ASN A 1 1114 ? 120.380 121.824 68.823  1.00 76.42  ? 1114 ASN A ND2 1 
ATOM   8930  N  N   . PHE A 1 1115 ? 116.106 119.337 66.442  1.00 70.96  ? 1115 PHE A N   1 
ATOM   8931  C  CA  . PHE A 1 1115 ? 115.125 119.291 65.366  1.00 62.64  ? 1115 PHE A CA  1 
ATOM   8932  C  C   . PHE A 1 1115 ? 113.761 118.861 65.885  1.00 73.03  ? 1115 PHE A C   1 
ATOM   8933  O  O   . PHE A 1 1115 ? 112.732 119.416 65.481  1.00 87.56  ? 1115 PHE A O   1 
ATOM   8934  C  CB  . PHE A 1 1115 ? 115.598 118.351 64.259  1.00 78.77  ? 1115 PHE A CB  1 
ATOM   8935  C  CG  . PHE A 1 1115 ? 114.892 118.561 62.953  1.00 91.16  ? 1115 PHE A CG  1 
ATOM   8936  C  CD1 . PHE A 1 1115 ? 113.652 117.990 62.725  1.00 101.29 ? 1115 PHE A CD1 1 
ATOM   8937  C  CD2 . PHE A 1 1115 ? 115.461 119.336 61.958  1.00 108.22 ? 1115 PHE A CD2 1 
ATOM   8938  C  CE1 . PHE A 1 1115 ? 112.991 118.185 61.531  1.00 105.58 ? 1115 PHE A CE1 1 
ATOM   8939  C  CE2 . PHE A 1 1115 ? 114.805 119.534 60.757  1.00 120.53 ? 1115 PHE A CE2 1 
ATOM   8940  C  CZ  . PHE A 1 1115 ? 113.568 118.957 60.544  1.00 103.24 ? 1115 PHE A CZ  1 
ATOM   8941  N  N   . LEU A 1 1116 ? 113.731 117.877 66.789  1.00 69.49  ? 1116 LEU A N   1 
ATOM   8942  C  CA  . LEU A 1 1116 ? 112.455 117.439 67.345  1.00 61.36  ? 1116 LEU A CA  1 
ATOM   8943  C  C   . LEU A 1 1116 ? 111.771 118.545 68.134  1.00 70.10  ? 1116 LEU A C   1 
ATOM   8944  O  O   . LEU A 1 1116 ? 110.561 118.761 67.988  1.00 78.34  ? 1116 LEU A O   1 
ATOM   8945  C  CB  . LEU A 1 1116 ? 112.664 116.218 68.236  1.00 58.33  ? 1116 LEU A CB  1 
ATOM   8946  C  CG  . LEU A 1 1116 ? 112.620 114.860 67.549  1.00 67.30  ? 1116 LEU A CG  1 
ATOM   8947  C  CD1 . LEU A 1 1116 ? 112.927 113.764 68.553  1.00 67.14  ? 1116 LEU A CD1 1 
ATOM   8948  C  CD2 . LEU A 1 1116 ? 111.241 114.665 66.944  1.00 76.20  ? 1116 LEU A CD2 1 
ATOM   8949  N  N   . ARG A 1 1117 ? 112.522 119.268 68.967  1.00 73.55  ? 1117 ARG A N   1 
ATOM   8950  C  CA  . ARG A 1 1117 ? 111.900 120.345 69.730  1.00 62.88  ? 1117 ARG A CA  1 
ATOM   8951  C  C   . ARG A 1 1117 ? 111.403 121.462 68.824  1.00 68.81  ? 1117 ARG A C   1 
ATOM   8952  O  O   . ARG A 1 1117 ? 110.323 122.018 69.055  1.00 76.94  ? 1117 ARG A O   1 
ATOM   8953  C  CB  . ARG A 1 1117 ? 112.876 120.893 70.765  1.00 63.67  ? 1117 ARG A CB  1 
ATOM   8954  C  CG  . ARG A 1 1117 ? 112.704 120.258 72.122  1.00 64.49  ? 1117 ARG A CG  1 
ATOM   8955  C  CD  . ARG A 1 1117 ? 113.902 120.515 72.999  1.00 60.46  ? 1117 ARG A CD  1 
ATOM   8956  N  NE  . ARG A 1 1117 ? 113.757 119.852 74.286  1.00 71.76  ? 1117 ARG A NE  1 
ATOM   8957  C  CZ  . ARG A 1 1117 ? 114.735 119.187 74.890  1.00 85.30  ? 1117 ARG A CZ  1 
ATOM   8958  N  NH1 . ARG A 1 1117 ? 115.930 119.107 74.320  1.00 77.56  ? 1117 ARG A NH1 1 
ATOM   8959  N  NH2 . ARG A 1 1117 ? 114.520 118.604 76.060  1.00 70.85  ? 1117 ARG A NH2 1 
ATOM   8960  N  N   . ALA A 1 1118 ? 112.170 121.802 67.785  1.00 78.71  ? 1118 ALA A N   1 
ATOM   8961  C  CA  . ALA A 1 1118 ? 111.730 122.846 66.867  1.00 76.94  ? 1118 ALA A CA  1 
ATOM   8962  C  C   . ALA A 1 1118 ? 110.473 122.439 66.106  1.00 73.42  ? 1118 ALA A C   1 
ATOM   8963  O  O   . ALA A 1 1118 ? 109.539 123.236 65.965  1.00 86.22  ? 1118 ALA A O   1 
ATOM   8964  C  CB  . ALA A 1 1118 ? 112.855 123.195 65.894  1.00 98.14  ? 1118 ALA A CB  1 
ATOM   8965  N  N   . TYR A 1 1119 ? 110.425 121.194 65.625  1.00 76.26  ? 1119 TYR A N   1 
ATOM   8966  C  CA  . TYR A 1 1119 ? 109.294 120.758 64.811  1.00 74.71  ? 1119 TYR A CA  1 
ATOM   8967  C  C   . TYR A 1 1119 ? 108.036 120.543 65.647  1.00 69.78  ? 1119 TYR A C   1 
ATOM   8968  O  O   . TYR A 1 1119 ? 106.926 120.832 65.186  1.00 79.08  ? 1119 TYR A O   1 
ATOM   8969  C  CB  . TYR A 1 1119 ? 109.651 119.480 64.055  1.00 84.52  ? 1119 TYR A CB  1 
ATOM   8970  C  CG  . TYR A 1 1119 ? 108.527 118.960 63.184  1.00 82.99  ? 1119 TYR A CG  1 
ATOM   8971  C  CD1 . TYR A 1 1119 ? 107.574 118.082 63.682  1.00 88.72  ? 1119 TYR A CD1 1 
ATOM   8972  C  CD2 . TYR A 1 1119 ? 108.428 119.350 61.857  1.00 93.36  ? 1119 TYR A CD2 1 
ATOM   8973  C  CE1 . TYR A 1 1119 ? 106.547 117.615 62.882  1.00 103.50 ? 1119 TYR A CE1 1 
ATOM   8974  C  CE2 . TYR A 1 1119 ? 107.410 118.887 61.050  1.00 93.99  ? 1119 TYR A CE2 1 
ATOM   8975  C  CZ  . TYR A 1 1119 ? 106.471 118.020 61.565  1.00 107.96 ? 1119 TYR A CZ  1 
ATOM   8976  O  OH  . TYR A 1 1119 ? 105.454 117.559 60.761  1.00 109.16 ? 1119 TYR A OH  1 
ATOM   8977  N  N   . SER A 1 1120 ? 108.182 120.043 66.878  1.00 73.26  ? 1120 SER A N   1 
ATOM   8978  C  CA  . SER A 1 1120 ? 107.003 119.650 67.643  1.00 67.13  ? 1120 SER A CA  1 
ATOM   8979  C  C   . SER A 1 1120 ? 106.178 120.853 68.085  1.00 78.55  ? 1120 SER A C   1 
ATOM   8980  O  O   . SER A 1 1120 ? 104.946 120.769 68.136  1.00 91.08  ? 1120 SER A O   1 
ATOM   8981  C  CB  . SER A 1 1120 ? 107.420 118.814 68.854  1.00 62.14  ? 1120 SER A CB  1 
ATOM   8982  O  OG  . SER A 1 1120 ? 106.296 118.227 69.487  1.00 73.18  ? 1120 SER A OG  1 
ATOM   8983  N  N   . TRP A 1 1121 ? 106.825 121.974 68.400  1.00 77.99  ? 1121 TRP A N   1 
ATOM   8984  C  CA  . TRP A 1 1121 ? 106.149 123.162 68.908  1.00 65.51  ? 1121 TRP A CA  1 
ATOM   8985  C  C   . TRP A 1 1121 ? 106.154 124.283 67.871  1.00 78.08  ? 1121 TRP A C   1 
ATOM   8986  O  O   . TRP A 1 1121 ? 106.261 125.461 68.209  1.00 85.45  ? 1121 TRP A O   1 
ATOM   8987  C  CB  . TRP A 1 1121 ? 106.785 123.648 70.210  1.00 59.27  ? 1121 TRP A CB  1 
ATOM   8988  C  CG  . TRP A 1 1121 ? 106.712 122.659 71.330  1.00 78.85  ? 1121 TRP A CG  1 
ATOM   8989  C  CD1 . TRP A 1 1121 ? 107.743 121.924 71.836  1.00 75.50  ? 1121 TRP A CD1 1 
ATOM   8990  C  CD2 . TRP A 1 1121 ? 105.539 122.259 72.051  1.00 97.65  ? 1121 TRP A CD2 1 
ATOM   8991  N  NE1 . TRP A 1 1121 ? 107.293 121.112 72.850  1.00 77.37  ? 1121 TRP A NE1 1 
ATOM   8992  C  CE2 . TRP A 1 1121 ? 105.942 121.295 72.996  1.00 90.38  ? 1121 TRP A CE2 1 
ATOM   8993  C  CE3 . TRP A 1 1121 ? 104.195 122.627 71.995  1.00 98.55  ? 1121 TRP A CE3 1 
ATOM   8994  C  CZ2 . TRP A 1 1121 ? 105.045 120.696 73.879  1.00 84.55  ? 1121 TRP A CZ2 1 
ATOM   8995  C  CZ3 . TRP A 1 1121 ? 103.305 122.032 72.872  1.00 83.18  ? 1121 TRP A CZ3 1 
ATOM   8996  C  CH2 . TRP A 1 1121 ? 103.735 121.078 73.801  1.00 73.91  ? 1121 TRP A CH2 1 
ATOM   8997  N  N   . SER A 1 1122 ? 106.043 123.916 66.591  1.00 75.41  ? 1122 SER A N   1 
ATOM   8998  C  CA  . SER A 1 1122 ? 106.158 124.905 65.521  1.00 76.17  ? 1122 SER A CA  1 
ATOM   8999  C  C   . SER A 1 1122 ? 105.031 125.931 65.569  1.00 94.36  ? 1122 SER A C   1 
ATOM   9000  O  O   . SER A 1 1122 ? 105.260 127.122 65.323  1.00 102.25 ? 1122 SER A O   1 
ATOM   9001  C  CB  . SER A 1 1122 ? 106.177 124.203 64.163  1.00 78.20  ? 1122 SER A CB  1 
ATOM   9002  O  OG  . SER A 1 1122 ? 105.176 123.203 64.098  1.00 88.25  ? 1122 SER A OG  1 
ATOM   9003  N  N   . ASP A 1 1123 ? 103.809 125.497 65.892  1.00 96.70  ? 1123 ASP A N   1 
ATOM   9004  C  CA  . ASP A 1 1123 ? 102.688 126.432 65.917  1.00 103.96 ? 1123 ASP A CA  1 
ATOM   9005  C  C   . ASP A 1 1123 ? 102.883 127.485 66.997  1.00 87.29  ? 1123 ASP A C   1 
ATOM   9006  O  O   . ASP A 1 1123 ? 102.583 128.666 66.787  1.00 94.40  ? 1123 ASP A O   1 
ATOM   9007  C  CB  . ASP A 1 1123 ? 101.369 125.689 66.125  1.00 114.91 ? 1123 ASP A CB  1 
ATOM   9008  C  CG  . ASP A 1 1123 ? 100.903 124.966 64.877  1.00 129.39 ? 1123 ASP A CG  1 
ATOM   9009  O  OD1 . ASP A 1 1123 ? 99.956  124.158 64.973  1.00 129.05 ? 1123 ASP A OD1 1 
ATOM   9010  O  OD2 . ASP A 1 1123 ? 101.482 125.212 63.798  1.00 120.36 ? 1123 ASP A OD2 1 
ATOM   9011  N  N   . VAL A 1 1124 ? 103.387 127.075 68.161  1.00 83.12  ? 1124 VAL A N   1 
ATOM   9012  C  CA  . VAL A 1 1124 ? 103.623 128.026 69.241  1.00 77.48  ? 1124 VAL A CA  1 
ATOM   9013  C  C   . VAL A 1 1124 ? 104.798 128.936 68.904  1.00 85.14  ? 1124 VAL A C   1 
ATOM   9014  O  O   . VAL A 1 1124 ? 104.757 130.144 69.166  1.00 97.08  ? 1124 VAL A O   1 
ATOM   9015  C  CB  . VAL A 1 1124 ? 103.838 127.277 70.570  1.00 86.60  ? 1124 VAL A CB  1 
ATOM   9016  C  CG1 . VAL A 1 1124 ? 104.465 128.190 71.613  1.00 88.10  ? 1124 VAL A CG1 1 
ATOM   9017  C  CG2 . VAL A 1 1124 ? 102.517 126.710 71.079  1.00 82.41  ? 1124 VAL A CG2 1 
ATOM   9018  N  N   . LEU A 1 1125 ? 105.855 128.387 68.297  1.00 85.96  ? 1125 LEU A N   1 
ATOM   9019  C  CA  . LEU A 1 1125 ? 107.065 129.179 68.108  1.00 94.27  ? 1125 LEU A CA  1 
ATOM   9020  C  C   . LEU A 1 1125 ? 106.921 130.210 66.994  1.00 105.53 ? 1125 LEU A C   1 
ATOM   9021  O  O   . LEU A 1 1125 ? 107.554 131.269 67.062  1.00 108.64 ? 1125 LEU A O   1 
ATOM   9022  C  CB  . LEU A 1 1125 ? 108.255 128.262 67.821  1.00 96.57  ? 1125 LEU A CB  1 
ATOM   9023  C  CG  . LEU A 1 1125 ? 108.786 127.461 69.011  1.00 96.68  ? 1125 LEU A CG  1 
ATOM   9024  C  CD1 . LEU A 1 1125 ? 110.002 126.645 68.604  1.00 87.00  ? 1125 LEU A CD1 1 
ATOM   9025  C  CD2 . LEU A 1 1125 ? 109.114 128.390 70.173  1.00 85.21  ? 1125 LEU A CD2 1 
ATOM   9026  N  N   . LYS A 1 1126 ? 106.098 129.932 65.978  1.00 104.67 ? 1126 LYS A N   1 
ATOM   9027  C  CA  . LYS A 1 1126 ? 105.818 130.893 64.905  1.00 106.56 ? 1126 LYS A CA  1 
ATOM   9028  C  C   . LYS A 1 1126 ? 107.088 131.369 64.199  1.00 98.97  ? 1126 LYS A C   1 
ATOM   9029  O  O   . LYS A 1 1126 ? 107.236 132.551 63.883  1.00 100.74 ? 1126 LYS A O   1 
ATOM   9030  C  CB  . LYS A 1 1126 ? 104.993 132.075 65.415  1.00 106.94 ? 1126 LYS A CB  1 
ATOM   9031  C  CG  . LYS A 1 1126 ? 103.698 131.651 66.079  1.00 112.91 ? 1126 LYS A CG  1 
ATOM   9032  C  CD  . LYS A 1 1126 ? 103.044 132.785 66.836  1.00 117.02 ? 1126 LYS A CD  1 
ATOM   9033  C  CE  . LYS A 1 1126 ? 101.749 132.316 67.473  1.00 117.85 ? 1126 LYS A CE  1 
ATOM   9034  N  NZ  . LYS A 1 1126 ? 100.726 132.007 66.434  1.00 105.29 ? 1126 LYS A NZ  1 
ATOM   9035  N  N   . GLY A 1 1127 ? 108.022 130.450 63.966  1.00 95.34  ? 1127 GLY A N   1 
ATOM   9036  C  CA  . GLY A 1 1127 ? 109.225 130.749 63.225  1.00 95.90  ? 1127 GLY A CA  1 
ATOM   9037  C  C   . GLY A 1 1127 ? 110.403 131.198 64.061  1.00 101.27 ? 1127 GLY A C   1 
ATOM   9038  O  O   . GLY A 1 1127 ? 111.533 131.198 63.560  1.00 95.35  ? 1127 GLY A O   1 
ATOM   9039  N  N   . LYS A 1 1128 ? 110.180 131.592 65.310  1.00 96.83  ? 1128 LYS A N   1 
ATOM   9040  C  CA  . LYS A 1 1128 ? 111.308 131.927 66.158  1.00 91.57  ? 1128 LYS A CA  1 
ATOM   9041  C  C   . LYS A 1 1128 ? 112.015 130.643 66.582  1.00 99.25  ? 1128 LYS A C   1 
ATOM   9042  O  O   . LYS A 1 1128 ? 111.489 129.535 66.446  1.00 103.08 ? 1128 LYS A O   1 
ATOM   9043  C  CB  . LYS A 1 1128 ? 110.845 132.721 67.377  1.00 93.16  ? 1128 LYS A CB  1 
ATOM   9044  C  CG  . LYS A 1 1128 ? 110.265 134.079 67.037  1.00 102.64 ? 1128 LYS A CG  1 
ATOM   9045  C  CD  . LYS A 1 1128 ? 109.942 134.856 68.291  1.00 96.51  ? 1128 LYS A CD  1 
ATOM   9046  C  CE  . LYS A 1 1128 ? 108.785 134.209 69.028  1.00 93.60  ? 1128 LYS A CE  1 
ATOM   9047  N  NZ  . LYS A 1 1128 ? 107.551 134.190 68.200  1.00 99.68  ? 1128 LYS A NZ  1 
ATOM   9048  N  N   . ARG A 1 1129 ? 113.227 130.791 67.101  1.00 92.72  ? 1129 ARG A N   1 
ATOM   9049  C  CA  . ARG A 1 1129 ? 114.070 129.647 67.406  1.00 93.79  ? 1129 ARG A CA  1 
ATOM   9050  C  C   . ARG A 1 1129 ? 114.254 129.496 68.911  1.00 88.79  ? 1129 ARG A C   1 
ATOM   9051  O  O   . ARG A 1 1129 ? 114.324 130.487 69.647  1.00 92.73  ? 1129 ARG A O   1 
ATOM   9052  C  CB  . ARG A 1 1129 ? 115.410 129.785 66.679  1.00 107.76 ? 1129 ARG A CB  1 
ATOM   9053  C  CG  . ARG A 1 1129 ? 116.406 130.695 67.351  1.00 115.16 ? 1129 ARG A CG  1 
ATOM   9054  C  CD  . ARG A 1 1129 ? 117.695 130.740 66.562  1.00 122.90 ? 1129 ARG A CD  1 
ATOM   9055  N  NE  . ARG A 1 1129 ? 118.825 131.102 67.406  1.00 134.22 ? 1129 ARG A NE  1 
ATOM   9056  C  CZ  . ARG A 1 1129 ? 119.113 132.349 67.763  1.00 128.66 ? 1129 ARG A CZ  1 
ATOM   9057  N  NH1 . ARG A 1 1129 ? 120.162 132.585 68.531  1.00 132.24 ? 1129 ARG A NH1 1 
ATOM   9058  N  NH2 . ARG A 1 1129 ? 118.351 133.357 67.355  1.00 120.05 ? 1129 ARG A NH2 1 
ATOM   9059  N  N   . LEU A 1 1130 ? 114.311 128.244 69.359  1.00 76.85  ? 1130 LEU A N   1 
ATOM   9060  C  CA  . LEU A 1 1130 ? 114.324 127.902 70.774  1.00 74.78  ? 1130 LEU A CA  1 
ATOM   9061  C  C   . LEU A 1 1130 ? 115.751 127.673 71.258  1.00 84.75  ? 1130 LEU A C   1 
ATOM   9062  O  O   . LEU A 1 1130 ? 116.562 127.055 70.563  1.00 105.68 ? 1130 LEU A O   1 
ATOM   9063  C  CB  . LEU A 1 1130 ? 113.466 126.657 71.017  1.00 70.94  ? 1130 LEU A CB  1 
ATOM   9064  C  CG  . LEU A 1 1130 ? 113.352 126.096 72.431  1.00 79.59  ? 1130 LEU A CG  1 
ATOM   9065  C  CD1 . LEU A 1 1130 ? 112.579 127.055 73.319  1.00 95.59  ? 1130 LEU A CD1 1 
ATOM   9066  C  CD2 . LEU A 1 1130 ? 112.670 124.736 72.386  1.00 72.87  ? 1130 LEU A CD2 1 
ATOM   9067  N  N   . ILE A 1 1131 ? 116.053 128.176 72.459  1.00 72.25  ? 1131 ILE A N   1 
ATOM   9068  C  CA  . ILE A 1 1131 ? 117.374 128.046 73.060  1.00 74.08  ? 1131 ILE A CA  1 
ATOM   9069  C  C   . ILE A 1 1131 ? 117.243 127.641 74.522  1.00 73.24  ? 1131 ILE A C   1 
ATOM   9070  O  O   . ILE A 1 1131 ? 116.183 127.768 75.137  1.00 87.50  ? 1131 ILE A O   1 
ATOM   9071  C  CB  . ILE A 1 1131 ? 118.207 129.343 72.970  1.00 70.52  ? 1131 ILE A CB  1 
ATOM   9072  C  CG1 . ILE A 1 1131 ? 117.574 130.442 73.823  1.00 78.34  ? 1131 ILE A CG1 1 
ATOM   9073  C  CG2 . ILE A 1 1131 ? 118.347 129.802 71.524  1.00 91.02  ? 1131 ILE A CG2 1 
ATOM   9074  C  CD1 . ILE A 1 1131 ? 118.442 131.673 73.962  1.00 91.95  ? 1131 ILE A CD1 1 
ATOM   9075  N  N   . GLY A 1 1132 ? 118.345 127.133 75.072  1.00 78.27  ? 1132 GLY A N   1 
ATOM   9076  C  CA  . GLY A 1 1132 ? 118.425 126.867 76.494  1.00 83.30  ? 1132 GLY A CA  1 
ATOM   9077  C  C   . GLY A 1 1132 ? 117.788 125.591 76.991  1.00 92.16  ? 1132 GLY A C   1 
ATOM   9078  O  O   . GLY A 1 1132 ? 117.608 125.447 78.205  1.00 95.63  ? 1132 GLY A O   1 
ATOM   9079  N  N   . ALA A 1 1133 ? 117.451 124.658 76.111  1.00 87.76  ? 1133 ALA A N   1 
ATOM   9080  C  CA  . ALA A 1 1133 ? 116.803 123.424 76.533  1.00 93.65  ? 1133 ALA A CA  1 
ATOM   9081  C  C   . ALA A 1 1133 ? 117.670 122.192 76.343  1.00 92.86  ? 1133 ALA A C   1 
ATOM   9082  O  O   . ALA A 1 1133 ? 117.683 121.315 77.211  1.00 99.98  ? 1133 ALA A O   1 
ATOM   9083  C  CB  . ALA A 1 1133 ? 115.486 123.230 75.771  1.00 80.38  ? 1133 ALA A CB  1 
ATOM   9084  N  N   . THR A 1 1134 ? 118.406 122.107 75.241  1.00 78.68  ? 1134 THR A N   1 
ATOM   9085  C  CA  . THR A 1 1134 ? 119.149 120.904 74.901  1.00 83.69  ? 1134 THR A CA  1 
ATOM   9086  C  C   . THR A 1 1134 ? 120.547 120.925 75.505  1.00 85.80  ? 1134 THR A C   1 
ATOM   9087  O  O   . THR A 1 1134 ? 121.304 121.883 75.316  1.00 88.60  ? 1134 THR A O   1 
ATOM   9088  C  CB  . THR A 1 1134 ? 119.241 120.743 73.382  1.00 88.79  ? 1134 THR A CB  1 
ATOM   9089  O  OG1 . THR A 1 1134 ? 117.934 120.498 72.848  1.00 87.47  ? 1134 THR A OG1 1 
ATOM   9090  C  CG2 . THR A 1 1134 ? 120.158 119.582 73.019  1.00 97.92  ? 1134 THR A CG2 1 
ATOM   9091  N  N   . LEU A 1 1135 ? 120.880 119.861 76.229  1.00 78.91  ? 1135 LEU A N   1 
ATOM   9092  C  CA  . LEU A 1 1135 ? 122.203 119.621 76.777  1.00 74.99  ? 1135 LEU A CA  1 
ATOM   9093  C  C   . LEU A 1 1135 ? 122.598 118.191 76.448  1.00 81.58  ? 1135 LEU A C   1 
ATOM   9094  O  O   . LEU A 1 1135 ? 121.744 117.299 76.413  1.00 80.91  ? 1135 LEU A O   1 
ATOM   9095  C  CB  . LEU A 1 1135 ? 122.247 119.837 78.297  1.00 75.81  ? 1135 LEU A CB  1 
ATOM   9096  C  CG  . LEU A 1 1135 ? 122.023 121.256 78.819  1.00 72.43  ? 1135 LEU A CG  1 
ATOM   9097  C  CD1 . LEU A 1 1135 ? 121.506 121.221 80.246  1.00 86.15  ? 1135 LEU A CD1 1 
ATOM   9098  C  CD2 . LEU A 1 1135 ? 123.324 122.048 78.738  1.00 99.94  ? 1135 LEU A CD2 1 
ATOM   9099  N  N   . PRO A 1 1136 ? 123.881 117.941 76.209  1.00 73.97  ? 1136 PRO A N   1 
ATOM   9100  C  CA  . PRO A 1 1136 ? 124.301 116.597 75.807  1.00 69.75  ? 1136 PRO A CA  1 
ATOM   9101  C  C   . PRO A 1 1136 ? 124.164 115.588 76.935  1.00 72.04  ? 1136 PRO A C   1 
ATOM   9102  O  O   . PRO A 1 1136 ? 124.186 115.912 78.124  1.00 73.29  ? 1136 PRO A O   1 
ATOM   9103  C  CB  . PRO A 1 1136 ? 125.769 116.786 75.409  1.00 81.54  ? 1136 PRO A CB  1 
ATOM   9104  C  CG  . PRO A 1 1136 ? 126.209 117.994 76.166  1.00 90.93  ? 1136 PRO A CG  1 
ATOM   9105  C  CD  . PRO A 1 1136 ? 125.008 118.891 76.230  1.00 84.32  ? 1136 PRO A CD  1 
ATOM   9106  N  N   . CYS A 1 1137 ? 124.016 114.333 76.526  1.00 73.06  ? 1137 CYS A N   1 
ATOM   9107  C  CA  . CYS A 1 1137 ? 124.033 113.214 77.456  1.00 70.87  ? 1137 CYS A CA  1 
ATOM   9108  C  C   . CYS A 1 1137 ? 125.466 112.920 77.863  1.00 77.17  ? 1137 CYS A C   1 
ATOM   9109  O  O   . CYS A 1 1137 ? 126.359 112.846 77.012  1.00 82.43  ? 1137 CYS A O   1 
ATOM   9110  C  CB  . CYS A 1 1137 ? 123.404 111.970 76.841  1.00 74.77  ? 1137 CYS A CB  1 
ATOM   9111  S  SG  . CYS A 1 1137 ? 123.300 110.561 77.977  1.00 84.32  ? 1137 CYS A SG  1 
ATOM   9112  N  N   . LEU A 1 1138 ? 125.685 112.767 79.167  1.00 73.94  ? 1138 LEU A N   1 
ATOM   9113  C  CA  . LEU A 1 1138 ? 127.035 112.528 79.660  1.00 68.89  ? 1138 LEU A CA  1 
ATOM   9114  C  C   . LEU A 1 1138 ? 127.602 111.211 79.145  1.00 66.41  ? 1138 LEU A C   1 
ATOM   9115  O  O   . LEU A 1 1138 ? 128.784 111.136 78.782  1.00 75.58  ? 1138 LEU A O   1 
ATOM   9116  C  CB  . LEU A 1 1138 ? 127.044 112.544 81.193  1.00 54.07  ? 1138 LEU A CB  1 
ATOM   9117  C  CG  . LEU A 1 1138 ? 127.169 113.896 81.885  1.00 53.81  ? 1138 LEU A CG  1 
ATOM   9118  C  CD1 . LEU A 1 1138 ? 127.048 113.703 83.386  1.00 75.10  ? 1138 LEU A CD1 1 
ATOM   9119  C  CD2 . LEU A 1 1138 ? 128.497 114.527 81.523  1.00 57.79  ? 1138 LEU A CD2 1 
ATOM   9120  N  N   . LEU A 1 1139 ? 126.782 110.159 79.095  1.00 69.10  ? 1139 LEU A N   1 
ATOM   9121  C  CA  . LEU A 1 1139 ? 127.303 108.859 78.676  1.00 58.05  ? 1139 LEU A CA  1 
ATOM   9122  C  C   . LEU A 1 1139 ? 127.707 108.826 77.206  1.00 70.40  ? 1139 LEU A C   1 
ATOM   9123  O  O   . LEU A 1 1139 ? 128.377 107.882 76.791  1.00 73.85  ? 1139 LEU A O   1 
ATOM   9124  C  CB  . LEU A 1 1139 ? 126.293 107.765 78.997  1.00 57.09  ? 1139 LEU A CB  1 
ATOM   9125  C  CG  . LEU A 1 1139 ? 125.965 107.802 80.498  1.00 57.64  ? 1139 LEU A CG  1 
ATOM   9126  C  CD1 . LEU A 1 1139 ? 125.041 106.634 80.929  1.00 76.08  ? 1139 LEU A CD1 1 
ATOM   9127  C  CD2 . LEU A 1 1139 ? 127.164 108.049 81.489  1.00 66.23  ? 1139 LEU A CD2 1 
ATOM   9128  N  N   . GLU A 1 1140 ? 127.320 109.813 76.414  1.00 64.88  ? 1140 GLU A N   1 
ATOM   9129  C  CA  . GLU A 1 1140 ? 127.793 109.947 75.039  1.00 62.09  ? 1140 GLU A CA  1 
ATOM   9130  C  C   . GLU A 1 1140 ? 128.920 110.942 74.884  1.00 69.59  ? 1140 GLU A C   1 
ATOM   9131  O  O   . GLU A 1 1140 ? 129.687 110.843 73.922  1.00 77.87  ? 1140 GLU A O   1 
ATOM   9132  C  CB  . GLU A 1 1140 ? 126.669 110.352 74.089  1.00 73.06  ? 1140 GLU A CB  1 
ATOM   9133  C  CG  . GLU A 1 1140 ? 127.010 110.080 72.640  1.00 95.07  ? 1140 GLU A CG  1 
ATOM   9134  C  CD  . GLU A 1 1140 ? 125.830 110.053 71.704  1.00 96.96  ? 1140 GLU A CD  1 
ATOM   9135  O  OE1 . GLU A 1 1140 ? 126.057 109.790 70.506  1.00 89.42  ? 1140 GLU A OE1 1 
ATOM   9136  O  OE2 . GLU A 1 1140 ? 124.676 110.210 72.156  1.00 84.19  ? 1140 GLU A OE2 1 
ATOM   9137  N  N   . GLN A 1 1141 ? 129.069 111.849 75.837  1.00 66.07  ? 1141 GLN A N   1 
ATOM   9138  C  CA  . GLN A 1 1141 ? 130.103 112.853 75.722  1.00 68.74  ? 1141 GLN A CA  1 
ATOM   9139  C  C   . GLN A 1 1141 ? 131.450 112.357 76.222  1.00 76.36  ? 1141 GLN A C   1 
ATOM   9140  O  O   . GLN A 1 1141 ? 132.487 112.744 75.670  1.00 84.29  ? 1141 GLN A O   1 
ATOM   9141  C  CB  . GLN A 1 1141 ? 129.692 114.094 76.497  1.00 75.20  ? 1141 GLN A CB  1 
ATOM   9142  C  CG  . GLN A 1 1141 ? 130.451 115.326 76.109  1.00 78.58  ? 1141 GLN A CG  1 
ATOM   9143  C  CD  . GLN A 1 1141 ? 129.947 116.538 76.840  1.00 71.40  ? 1141 GLN A CD  1 
ATOM   9144  O  OE1 . GLN A 1 1141 ? 130.229 117.669 76.455  1.00 85.56  ? 1141 GLN A OE1 1 
ATOM   9145  N  NE2 . GLN A 1 1141 ? 129.206 116.312 77.919  1.00 58.83  ? 1141 GLN A NE2 1 
ATOM   9146  N  N   . PHE A 1 1142 ? 131.458 111.492 77.231  1.00 75.79  ? 1142 PHE A N   1 
ATOM   9147  C  CA  . PHE A 1 1142 ? 132.684 110.976 77.816  1.00 61.93  ? 1142 PHE A CA  1 
ATOM   9148  C  C   . PHE A 1 1142 ? 132.777 109.474 77.607  1.00 77.99  ? 1142 PHE A C   1 
ATOM   9149  O  O   . PHE A 1 1142 ? 131.781 108.756 77.738  1.00 88.66  ? 1142 PHE A O   1 
ATOM   9150  C  CB  . PHE A 1 1142 ? 132.732 111.250 79.318  1.00 64.37  ? 1142 PHE A CB  1 
ATOM   9151  C  CG  . PHE A 1 1142 ? 132.849 112.698 79.670  1.00 64.42  ? 1142 PHE A CG  1 
ATOM   9152  C  CD1 . PHE A 1 1142 ? 134.080 113.324 79.731  1.00 87.27  ? 1142 PHE A CD1 1 
ATOM   9153  C  CD2 . PHE A 1 1142 ? 131.713 113.429 79.968  1.00 64.89  ? 1142 PHE A CD2 1 
ATOM   9154  C  CE1 . PHE A 1 1142 ? 134.171 114.666 80.066  1.00 83.34  ? 1142 PHE A CE1 1 
ATOM   9155  C  CE2 . PHE A 1 1142 ? 131.797 114.763 80.304  1.00 78.27  ? 1142 PHE A CE2 1 
ATOM   9156  C  CZ  . PHE A 1 1142 ? 133.025 115.384 80.353  1.00 81.19  ? 1142 PHE A CZ  1 
ATOM   9157  N  N   . GLU A 1 1143 ? 133.980 108.998 77.311  1.00 77.52  ? 1143 GLU A N   1 
ATOM   9158  C  CA  . GLU A 1 1143 ? 134.229 107.571 77.216  1.00 95.24  ? 1143 GLU A CA  1 
ATOM   9159  C  C   . GLU A 1 1143 ? 135.281 107.166 78.236  1.00 102.99 ? 1143 GLU A C   1 
ATOM   9160  O  O   . GLU A 1 1143 ? 136.163 107.953 78.597  1.00 94.78  ? 1143 GLU A O   1 
ATOM   9161  C  CB  . GLU A 1 1143 ? 134.687 107.158 75.819  1.00 93.22  ? 1143 GLU A CB  1 
ATOM   9162  C  CG  . GLU A 1 1143 ? 136.054 107.673 75.435  1.00 114.20 ? 1143 GLU A CG  1 
ATOM   9163  C  CD  . GLU A 1 1143 ? 136.460 107.216 74.054  1.00 139.29 ? 1143 GLU A CD  1 
ATOM   9164  O  OE1 . GLU A 1 1143 ? 135.654 106.517 73.404  1.00 138.39 ? 1143 GLU A OE1 1 
ATOM   9165  O  OE2 . GLU A 1 1143 ? 137.585 107.542 73.625  1.00 145.56 ? 1143 GLU A OE2 1 
ATOM   9166  N  N   . VAL A 1 1144 ? 135.173 105.927 78.699  1.00 108.52 ? 1144 VAL A N   1 
ATOM   9167  C  CA  . VAL A 1 1144 ? 136.048 105.402 79.739  1.00 86.06  ? 1144 VAL A CA  1 
ATOM   9168  C  C   . VAL A 1 1144 ? 137.231 104.707 79.082  1.00 82.30  ? 1144 VAL A C   1 
ATOM   9169  O  O   . VAL A 1 1144 ? 137.056 103.807 78.254  1.00 88.37  ? 1144 VAL A O   1 
ATOM   9170  C  CB  . VAL A 1 1144 ? 135.292 104.439 80.665  1.00 70.02  ? 1144 VAL A CB  1 
ATOM   9171  C  CG1 . VAL A 1 1144 ? 136.227 103.895 81.736  1.00 75.45  ? 1144 VAL A CG1 1 
ATOM   9172  C  CG2 . VAL A 1 1144 ? 134.098 105.140 81.298  1.00 89.35  ? 1144 VAL A CG2 1 
ATOM   9173  N  N   . LYS A 1 1145 ? 138.434 105.134 79.446  1.00 82.60  ? 1145 LYS A N   1 
ATOM   9174  C  CA  . LYS A 1 1145 ? 139.669 104.545 78.952  1.00 86.75  ? 1145 LYS A CA  1 
ATOM   9175  C  C   . LYS A 1 1145 ? 140.479 104.104 80.161  1.00 93.25  ? 1145 LYS A C   1 
ATOM   9176  O  O   . LYS A 1 1145 ? 140.740 104.909 81.062  1.00 93.78  ? 1145 LYS A O   1 
ATOM   9177  C  CB  . LYS A 1 1145 ? 140.450 105.545 78.095  1.00 88.43  ? 1145 LYS A CB  1 
ATOM   9178  C  CG  . LYS A 1 1145 ? 141.813 105.066 77.629  1.00 111.20 ? 1145 LYS A CG  1 
ATOM   9179  C  CD  . LYS A 1 1145 ? 142.460 106.109 76.730  1.00 120.72 ? 1145 LYS A CD  1 
ATOM   9180  C  CE  . LYS A 1 1145 ? 143.759 105.607 76.127  1.00 132.20 ? 1145 LYS A CE  1 
ATOM   9181  N  NZ  . LYS A 1 1145 ? 143.538 104.435 75.235  1.00 137.66 ? 1145 LYS A NZ  1 
ATOM   9182  N  N   . TRP A 1 1146 ? 140.879 102.836 80.178  1.00 78.42  ? 1146 TRP A N   1 
ATOM   9183  C  CA  . TRP A 1 1146 ? 141.525 102.252 81.346  1.00 72.57  ? 1146 TRP A CA  1 
ATOM   9184  C  C   . TRP A 1 1146 ? 143.032 102.411 81.226  1.00 90.38  ? 1146 TRP A C   1 
ATOM   9185  O  O   . TRP A 1 1146 ? 143.633 101.980 80.237  1.00 104.68 ? 1146 TRP A O   1 
ATOM   9186  C  CB  . TRP A 1 1146 ? 141.147 100.781 81.508  1.00 72.14  ? 1146 TRP A CB  1 
ATOM   9187  C  CG  . TRP A 1 1146 ? 139.717 100.620 81.870  1.00 75.69  ? 1146 TRP A CG  1 
ATOM   9188  C  CD1 . TRP A 1 1146 ? 138.671 100.450 81.016  1.00 85.04  ? 1146 TRP A CD1 1 
ATOM   9189  C  CD2 . TRP A 1 1146 ? 139.158 100.673 83.187  1.00 70.36  ? 1146 TRP A CD2 1 
ATOM   9190  N  NE1 . TRP A 1 1146 ? 137.495 100.371 81.722  1.00 78.20  ? 1146 TRP A NE1 1 
ATOM   9191  C  CE2 . TRP A 1 1146 ? 137.767 100.503 83.057  1.00 65.64  ? 1146 TRP A CE2 1 
ATOM   9192  C  CE3 . TRP A 1 1146 ? 139.701 100.836 84.466  1.00 75.45  ? 1146 TRP A CE3 1 
ATOM   9193  C  CZ2 . TRP A 1 1146 ? 136.911 100.493 84.157  1.00 73.26  ? 1146 TRP A CZ2 1 
ATOM   9194  C  CZ3 . TRP A 1 1146 ? 138.848 100.824 85.557  1.00 81.97  ? 1146 TRP A CZ3 1 
ATOM   9195  C  CH2 . TRP A 1 1146 ? 137.469 100.653 85.395  1.00 66.10  ? 1146 TRP A CH2 1 
ATOM   9196  N  N   . ILE A 1 1147 ? 143.636 103.016 82.242  1.00 81.74  ? 1147 ILE A N   1 
ATOM   9197  C  CA  . ILE A 1 1147 ? 145.055 103.332 82.220  1.00 86.54  ? 1147 ILE A CA  1 
ATOM   9198  C  C   . ILE A 1 1147 ? 145.881 102.275 82.931  1.00 89.57  ? 1147 ILE A C   1 
ATOM   9199  O  O   . ILE A 1 1147 ? 146.855 101.764 82.376  1.00 91.54  ? 1147 ILE A O   1 
ATOM   9200  C  CB  . ILE A 1 1147 ? 145.294 104.728 82.838  1.00 83.94  ? 1147 ILE A CB  1 
ATOM   9201  C  CG1 . ILE A 1 1147 ? 144.593 105.797 82.005  1.00 89.73  ? 1147 ILE A CG1 1 
ATOM   9202  C  CG2 . ILE A 1 1147 ? 146.784 105.015 82.947  1.00 91.93  ? 1147 ILE A CG2 1 
ATOM   9203  C  CD1 . ILE A 1 1147 ? 144.949 105.750 80.538  1.00 95.30  ? 1147 ILE A CD1 1 
ATOM   9204  N  N   . ASN A 1 1148 ? 145.508 101.913 84.154  1.00 87.99  ? 1148 ASN A N   1 
ATOM   9205  C  CA  . ASN A 1 1148 ? 146.281 100.922 84.888  1.00 92.37  ? 1148 ASN A CA  1 
ATOM   9206  C  C   . ASN A 1 1148 ? 145.367 100.060 85.746  1.00 88.52  ? 1148 ASN A C   1 
ATOM   9207  O  O   . ASN A 1 1148 ? 144.520 100.579 86.479  1.00 91.86  ? 1148 ASN A O   1 
ATOM   9208  C  CB  . ASN A 1 1148 ? 147.345 101.619 85.747  1.00 86.29  ? 1148 ASN A CB  1 
ATOM   9209  C  CG  . ASN A 1 1148 ? 148.109 100.662 86.628  1.00 108.05 ? 1148 ASN A CG  1 
ATOM   9210  O  OD1 . ASN A 1 1148 ? 148.859 99.816  86.143  1.00 112.94 ? 1148 ASN A OD1 1 
ATOM   9211  N  ND2 . ASN A 1 1148 ? 147.938 100.801 87.938  1.00 107.94 ? 1148 ASN A ND2 1 
ATOM   9212  N  N   . LEU A 1 1149 ? 145.548 98.746  85.643  1.00 84.67  ? 1149 LEU A N   1 
ATOM   9213  C  CA  . LEU A 1 1149 ? 144.837 97.762  86.443  1.00 77.08  ? 1149 LEU A CA  1 
ATOM   9214  C  C   . LEU A 1 1149 ? 145.854 96.811  87.052  1.00 98.13  ? 1149 LEU A C   1 
ATOM   9215  O  O   . LEU A 1 1149 ? 146.818 96.417  86.386  1.00 106.21 ? 1149 LEU A O   1 
ATOM   9216  C  CB  . LEU A 1 1149 ? 143.823 96.972  85.607  1.00 80.54  ? 1149 LEU A CB  1 
ATOM   9217  C  CG  . LEU A 1 1149 ? 142.417 97.547  85.440  1.00 67.82  ? 1149 LEU A CG  1 
ATOM   9218  C  CD1 . LEU A 1 1149 ? 141.694 96.838  84.307  1.00 75.50  ? 1149 LEU A CD1 1 
ATOM   9219  C  CD2 . LEU A 1 1149 ? 141.628 97.426  86.736  1.00 78.99  ? 1149 LEU A CD2 1 
ATOM   9220  N  N   . SER A 1 1150 ? 145.640 96.439  88.310  1.00 90.59  ? 1150 SER A N   1 
ATOM   9221  C  CA  . SER A 1 1150 ? 146.575 95.539  88.963  1.00 96.24  ? 1150 SER A CA  1 
ATOM   9222  C  C   . SER A 1 1150 ? 146.476 94.141  88.355  1.00 97.97  ? 1150 SER A C   1 
ATOM   9223  O  O   . SER A 1 1150 ? 145.602 93.844  87.536  1.00 101.34 ? 1150 SER A O   1 
ATOM   9224  C  CB  . SER A 1 1150 ? 146.314 95.487  90.466  1.00 93.31  ? 1150 SER A CB  1 
ATOM   9225  O  OG  . SER A 1 1150 ? 147.157 94.534  91.090  1.00 107.53 ? 1150 SER A OG  1 
ATOM   9226  N  N   . GLU A 1 1151 ? 147.390 93.268  88.782  1.00 101.96 ? 1151 GLU A N   1 
ATOM   9227  C  CA  . GLU A 1 1151 ? 147.491 91.944  88.181  1.00 102.38 ? 1151 GLU A CA  1 
ATOM   9228  C  C   . GLU A 1 1151 ? 146.378 91.016  88.646  1.00 98.66  ? 1151 GLU A C   1 
ATOM   9229  O  O   . GLU A 1 1151 ? 145.954 90.135  87.890  1.00 105.56 ? 1151 GLU A O   1 
ATOM   9230  C  CB  . GLU A 1 1151 ? 148.852 91.324  88.498  1.00 119.80 ? 1151 GLU A CB  1 
ATOM   9231  C  CG  . GLU A 1 1151 ? 149.243 90.213  87.545  1.00 138.43 ? 1151 GLU A CG  1 
ATOM   9232  C  CD  . GLU A 1 1151 ? 149.025 90.594  86.096  1.00 140.25 ? 1151 GLU A CD  1 
ATOM   9233  O  OE1 . GLU A 1 1151 ? 148.370 89.819  85.369  1.00 134.81 ? 1151 GLU A OE1 1 
ATOM   9234  O  OE2 . GLU A 1 1151 ? 149.513 91.667  85.682  1.00 138.20 ? 1151 GLU A OE2 1 
ATOM   9235  N  N   . ASP A 1 1152 ? 145.892 91.201  89.871  1.00 101.68 ? 1152 ASP A N   1 
ATOM   9236  C  CA  . ASP A 1 1152 ? 144.840 90.351  90.411  1.00 99.04  ? 1152 ASP A CA  1 
ATOM   9237  C  C   . ASP A 1 1152 ? 143.471 90.668  89.824  1.00 92.51  ? 1152 ASP A C   1 
ATOM   9238  O  O   . ASP A 1 1152 ? 142.580 89.813  89.870  1.00 85.26  ? 1152 ASP A O   1 
ATOM   9239  C  CB  . ASP A 1 1152 ? 144.810 90.468  91.936  1.00 130.89 ? 1152 ASP A CB  1 
ATOM   9240  C  CG  . ASP A 1 1152 ? 144.755 91.905  92.408  1.00 123.76 ? 1152 ASP A CG  1 
ATOM   9241  O  OD1 . ASP A 1 1152 ? 145.654 92.689  92.033  1.00 115.66 ? 1152 ASP A OD1 1 
ATOM   9242  O  OD2 . ASP A 1 1152 ? 143.818 92.252  93.157  1.00 104.73 ? 1152 ASP A OD2 1 
ATOM   9243  N  N   . LEU A 1 1153 ? 143.286 91.868  89.272  1.00 99.91  ? 1153 LEU A N   1 
ATOM   9244  C  CA  . LEU A 1 1153 ? 142.030 92.231  88.625  1.00 88.84  ? 1153 LEU A CA  1 
ATOM   9245  C  C   . LEU A 1 1153 ? 141.985 91.875  87.147  1.00 92.75  ? 1153 LEU A C   1 
ATOM   9246  O  O   . LEU A 1 1153 ? 140.893 91.678  86.602  1.00 101.30 ? 1153 LEU A O   1 
ATOM   9247  C  CB  . LEU A 1 1153 ? 141.782 93.732  88.780  1.00 64.24  ? 1153 LEU A CB  1 
ATOM   9248  C  CG  . LEU A 1 1153 ? 141.667 94.230  90.216  1.00 72.34  ? 1153 LEU A CG  1 
ATOM   9249  C  CD1 . LEU A 1 1153 ? 141.873 95.723  90.261  1.00 85.80  ? 1153 LEU A CD1 1 
ATOM   9250  C  CD2 . LEU A 1 1153 ? 140.298 93.860  90.763  1.00 84.14  ? 1153 LEU A CD2 1 
ATOM   9251  N  N   . ARG A 1 1154 ? 143.139 91.775  86.487  1.00 89.38  ? 1154 ARG A N   1 
ATOM   9252  C  CA  . ARG A 1 1154 ? 143.148 91.372  85.085  1.00 83.87  ? 1154 ARG A CA  1 
ATOM   9253  C  C   . ARG A 1 1154 ? 142.633 89.952  84.918  1.00 97.86  ? 1154 ARG A C   1 
ATOM   9254  O  O   . ARG A 1 1154 ? 141.931 89.646  83.946  1.00 117.12 ? 1154 ARG A O   1 
ATOM   9255  C  CB  . ARG A 1 1154 ? 144.551 91.500  84.501  1.00 103.38 ? 1154 ARG A CB  1 
ATOM   9256  C  CG  . ARG A 1 1154 ? 144.982 92.924  84.270  1.00 108.39 ? 1154 ARG A CG  1 
ATOM   9257  C  CD  . ARG A 1 1154 ? 146.457 92.999  83.970  1.00 109.63 ? 1154 ARG A CD  1 
ATOM   9258  N  NE  . ARG A 1 1154 ? 146.770 94.251  83.298  1.00 118.92 ? 1154 ARG A NE  1 
ATOM   9259  C  CZ  . ARG A 1 1154 ? 146.769 94.390  81.976  1.00 140.82 ? 1154 ARG A CZ  1 
ATOM   9260  N  NH1 . ARG A 1 1154 ? 146.468 93.355  81.204  1.00 139.64 ? 1154 ARG A NH1 1 
ATOM   9261  N  NH2 . ARG A 1 1154 ? 147.060 95.560  81.428  1.00 149.00 ? 1154 ARG A NH2 1 
ATOM   9262  N  N   . GLU A 1 1155 ? 142.963 89.072  85.861  1.00 98.15  ? 1155 GLU A N   1 
ATOM   9263  C  CA  . GLU A 1 1155 ? 142.451 87.709  85.809  1.00 105.10 ? 1155 GLU A CA  1 
ATOM   9264  C  C   . GLU A 1 1155 ? 140.942 87.678  86.006  1.00 103.57 ? 1155 GLU A C   1 
ATOM   9265  O  O   . GLU A 1 1155 ? 140.247 86.875  85.374  1.00 103.42 ? 1155 GLU A O   1 
ATOM   9266  C  CB  . GLU A 1 1155 ? 143.151 86.852  86.862  1.00 122.06 ? 1155 GLU A CB  1 
ATOM   9267  C  CG  . GLU A 1 1155 ? 144.624 87.179  87.034  1.00 135.54 ? 1155 GLU A CG  1 
ATOM   9268  C  CD  . GLU A 1 1155 ? 145.406 86.033  87.637  1.00 150.30 ? 1155 GLU A CD  1 
ATOM   9269  O  OE1 . GLU A 1 1155 ? 144.773 85.088  88.153  1.00 151.66 ? 1155 GLU A OE1 1 
ATOM   9270  O  OE2 . GLU A 1 1155 ? 146.653 86.077  87.595  1.00 142.82 ? 1155 GLU A OE2 1 
ATOM   9271  N  N   . GLN A 1 1156 ? 140.412 88.545  86.873  1.00 98.06  ? 1156 GLN A N   1 
ATOM   9272  C  CA  . GLN A 1 1156 ? 138.975 88.529  87.116  1.00 87.93  ? 1156 GLN A CA  1 
ATOM   9273  C  C   . GLN A 1 1156 ? 138.184 89.114  85.953  1.00 93.57  ? 1156 GLN A C   1 
ATOM   9274  O  O   . GLN A 1 1156 ? 137.055 88.678  85.699  1.00 105.04 ? 1156 GLN A O   1 
ATOM   9275  C  CB  . GLN A 1 1156 ? 138.655 89.302  88.393  1.00 80.33  ? 1156 GLN A CB  1 
ATOM   9276  C  CG  . GLN A 1 1156 ? 139.412 88.828  89.614  1.00 87.07  ? 1156 GLN A CG  1 
ATOM   9277  C  CD  . GLN A 1 1156 ? 138.881 89.446  90.887  1.00 79.34  ? 1156 GLN A CD  1 
ATOM   9278  O  OE1 . GLN A 1 1156 ? 137.681 89.690  91.018  1.00 80.77  ? 1156 GLN A OE1 1 
ATOM   9279  N  NE2 . GLN A 1 1156 ? 139.772 89.711  91.834  1.00 86.24  ? 1156 GLN A NE2 1 
ATOM   9280  N  N   . PHE A 1 1157 ? 138.739 90.090  85.237  1.00 95.12  ? 1157 PHE A N   1 
ATOM   9281  C  CA  . PHE A 1 1157 ? 138.042 90.663  84.091  1.00 94.93  ? 1157 PHE A CA  1 
ATOM   9282  C  C   . PHE A 1 1157 ? 138.331 89.936  82.784  1.00 111.59 ? 1157 PHE A C   1 
ATOM   9283  O  O   . PHE A 1 1157 ? 137.832 90.361  81.736  1.00 109.32 ? 1157 PHE A O   1 
ATOM   9284  C  CB  . PHE A 1 1157 ? 138.391 92.148  83.943  1.00 88.21  ? 1157 PHE A CB  1 
ATOM   9285  C  CG  . PHE A 1 1157 ? 137.945 92.989  85.105  1.00 81.23  ? 1157 PHE A CG  1 
ATOM   9286  C  CD1 . PHE A 1 1157 ? 136.876 92.591  85.891  1.00 84.66  ? 1157 PHE A CD1 1 
ATOM   9287  C  CD2 . PHE A 1 1157 ? 138.575 94.187  85.396  1.00 83.43  ? 1157 PHE A CD2 1 
ATOM   9288  C  CE1 . PHE A 1 1157 ? 136.459 93.359  86.960  1.00 82.87  ? 1157 PHE A CE1 1 
ATOM   9289  C  CE2 . PHE A 1 1157 ? 138.158 94.963  86.464  1.00 71.71  ? 1157 PHE A CE2 1 
ATOM   9290  C  CZ  . PHE A 1 1157 ? 137.099 94.547  87.246  1.00 65.79  ? 1157 PHE A CZ  1 
ATOM   9291  N  N   . ASN A 1 1158 ? 139.118 88.861  82.822  1.00 117.96 ? 1158 ASN A N   1 
ATOM   9292  C  CA  . ASN A 1 1158 ? 139.349 87.992  81.667  1.00 119.38 ? 1158 ASN A CA  1 
ATOM   9293  C  C   . ASN A 1 1158 ? 139.908 88.774  80.482  1.00 113.40 ? 1158 ASN A C   1 
ATOM   9294  O  O   . ASN A 1 1158 ? 139.523 88.549  79.333  1.00 122.82 ? 1158 ASN A O   1 
ATOM   9295  C  CB  . ASN A 1 1158 ? 138.064 87.265  81.260  1.00 121.76 ? 1158 ASN A CB  1 
ATOM   9296  C  CG  . ASN A 1 1158 ? 137.602 86.267  82.298  1.00 134.99 ? 1158 ASN A CG  1 
ATOM   9297  O  OD1 . ASN A 1 1158 ? 138.408 85.577  82.920  1.00 135.33 ? 1158 ASN A OD1 1 
ATOM   9298  N  ND2 . ASN A 1 1158 ? 136.290 86.184  82.491  1.00 126.62 ? 1158 ASN A ND2 1 
ATOM   9299  N  N   . LEU A 1 1159 ? 140.822 89.700  80.752  1.00 109.40 ? 1159 LEU A N   1 
ATOM   9300  C  CA  . LEU A 1 1159 ? 141.453 90.487  79.703  1.00 128.63 ? 1159 LEU A CA  1 
ATOM   9301  C  C   . LEU A 1 1159 ? 142.945 90.196  79.654  1.00 145.89 ? 1159 LEU A C   1 
ATOM   9302  O  O   . LEU A 1 1159 ? 143.584 89.985  80.691  1.00 126.48 ? 1159 LEU A O   1 
ATOM   9303  C  CB  . LEU A 1 1159 ? 141.202 91.996  79.882  1.00 121.00 ? 1159 LEU A CB  1 
ATOM   9304  C  CG  . LEU A 1 1159 ? 141.666 92.790  81.104  1.00 112.06 ? 1159 LEU A CG  1 
ATOM   9305  C  CD1 . LEU A 1 1159 ? 143.118 93.223  80.977  1.00 127.58 ? 1159 LEU A CD1 1 
ATOM   9306  C  CD2 . LEU A 1 1159 ? 140.769 94.006  81.278  1.00 96.69  ? 1159 LEU A CD2 1 
ATOM   9307  N  N   . SER A 1 1160 ? 143.489 90.179  78.444  1.00 167.38 ? 1160 SER A N   1 
ATOM   9308  C  CA  . SER A 1 1160 ? 144.905 89.942  78.211  1.00 179.09 ? 1160 SER A CA  1 
ATOM   9309  C  C   . SER A 1 1160 ? 145.473 91.132  77.454  1.00 187.87 ? 1160 SER A C   1 
ATOM   9310  O  O   . SER A 1 1160 ? 144.819 91.682  76.562  1.00 176.77 ? 1160 SER A O   1 
ATOM   9311  C  CB  . SER A 1 1160 ? 145.133 88.649  77.423  1.00 164.64 ? 1160 SER A CB  1 
ATOM   9312  O  OG  . SER A 1 1160 ? 144.460 88.686  76.177  1.00 154.32 ? 1160 SER A OG  1 
ATOM   9313  N  N   . SER A 1 1161 ? 146.687 91.531  77.815  1.00 188.95 ? 1161 SER A N   1 
ATOM   9314  C  CA  . SER A 1 1161 ? 147.340 92.658  77.161  1.00 190.72 ? 1161 SER A CA  1 
ATOM   9315  C  C   . SER A 1 1161 ? 148.459 92.189  76.239  1.00 183.65 ? 1161 SER A C   1 
ATOM   9316  O  O   . SER A 1 1161 ? 148.372 92.335  75.019  1.00 172.98 ? 1161 SER A O   1 
ATOM   9317  C  CB  . SER A 1 1161 ? 147.888 93.637  78.202  1.00 180.88 ? 1161 SER A CB  1 
ATOM   9318  O  OG  . SER A 1 1161 ? 148.880 93.025  79.005  1.00 175.90 ? 1161 SER A OG  1 
ATOM   9319  N  N   . LEU A 1 1187 ? 145.256 117.171 74.853  1.00 121.52 ? 1187 LEU A N   1 
ATOM   9320  C  CA  . LEU A 1 1187 ? 144.140 116.321 75.254  1.00 130.31 ? 1187 LEU A CA  1 
ATOM   9321  C  C   . LEU A 1 1187 ? 143.504 116.831 76.542  1.00 128.44 ? 1187 LEU A C   1 
ATOM   9322  O  O   . LEU A 1 1187 ? 144.189 117.343 77.428  1.00 125.31 ? 1187 LEU A O   1 
ATOM   9323  C  CB  . LEU A 1 1187 ? 144.593 114.871 75.408  1.00 124.44 ? 1187 LEU A CB  1 
ATOM   9324  C  CG  . LEU A 1 1187 ? 144.691 114.151 74.062  1.00 129.07 ? 1187 LEU A CG  1 
ATOM   9325  C  CD1 . LEU A 1 1187 ? 145.478 112.855 74.183  1.00 119.09 ? 1187 LEU A CD1 1 
ATOM   9326  C  CD2 . LEU A 1 1187 ? 143.303 113.904 73.480  1.00 106.85 ? 1187 LEU A CD2 1 
ATOM   9327  N  N   . ASN A 1 1188 ? 142.186 116.677 76.642  1.00 119.44 ? 1188 ASN A N   1 
ATOM   9328  C  CA  . ASN A 1 1188 ? 141.419 117.126 77.795  1.00 115.81 ? 1188 ASN A CA  1 
ATOM   9329  C  C   . ASN A 1 1188 ? 140.684 115.951 78.422  1.00 108.58 ? 1188 ASN A C   1 
ATOM   9330  O  O   . ASN A 1 1188 ? 139.968 115.221 77.729  1.00 100.91 ? 1188 ASN A O   1 
ATOM   9331  C  CB  . ASN A 1 1188 ? 140.426 118.210 77.387  1.00 119.03 ? 1188 ASN A CB  1 
ATOM   9332  C  CG  . ASN A 1 1188 ? 141.072 119.300 76.566  1.00 125.97 ? 1188 ASN A CG  1 
ATOM   9333  O  OD1 . ASN A 1 1188 ? 142.114 119.833 76.937  1.00 132.70 ? 1188 ASN A OD1 1 
ATOM   9334  N  ND2 . ASN A 1 1188 ? 140.462 119.630 75.436  1.00 126.79 ? 1188 ASN A ND2 1 
ATOM   9335  N  N   . TYR A 1 1189 ? 140.874 115.766 79.727  1.00 107.86 ? 1189 TYR A N   1 
ATOM   9336  C  CA  . TYR A 1 1189 ? 140.264 114.640 80.415  1.00 95.92  ? 1189 TYR A CA  1 
ATOM   9337  C  C   . TYR A 1 1189 ? 140.211 114.871 81.913  1.00 103.01 ? 1189 TYR A C   1 
ATOM   9338  O  O   . TYR A 1 1189 ? 140.946 115.691 82.468  1.00 106.84 ? 1189 TYR A O   1 
ATOM   9339  C  CB  . TYR A 1 1189 ? 141.033 113.355 80.156  1.00 99.56  ? 1189 TYR A CB  1 
ATOM   9340  C  CG  . TYR A 1 1189 ? 142.499 113.417 80.523  1.00 112.99 ? 1189 TYR A CG  1 
ATOM   9341  C  CD1 . TYR A 1 1189 ? 143.466 113.644 79.554  1.00 124.19 ? 1189 TYR A CD1 1 
ATOM   9342  C  CD2 . TYR A 1 1189 ? 142.919 113.218 81.832  1.00 110.23 ? 1189 TYR A CD2 1 
ATOM   9343  C  CE1 . TYR A 1 1189 ? 144.807 113.693 79.883  1.00 117.99 ? 1189 TYR A CE1 1 
ATOM   9344  C  CE2 . TYR A 1 1189 ? 144.256 113.265 82.168  1.00 106.91 ? 1189 TYR A CE2 1 
ATOM   9345  C  CZ  . TYR A 1 1189 ? 145.195 113.501 81.192  1.00 109.23 ? 1189 TYR A CZ  1 
ATOM   9346  O  OH  . TYR A 1 1189 ? 146.526 113.548 81.532  1.00 111.01 ? 1189 TYR A OH  1 
ATOM   9347  N  N   . VAL A 1 1190 ? 139.333 114.114 82.557  1.00 98.53  ? 1190 VAL A N   1 
ATOM   9348  C  CA  . VAL A 1 1190 ? 139.303 114.001 84.007  1.00 94.54  ? 1190 VAL A CA  1 
ATOM   9349  C  C   . VAL A 1 1190 ? 139.998 112.695 84.368  1.00 94.70  ? 1190 VAL A C   1 
ATOM   9350  O  O   . VAL A 1 1190 ? 139.836 111.680 83.678  1.00 92.21  ? 1190 VAL A O   1 
ATOM   9351  C  CB  . VAL A 1 1190 ? 137.857 114.043 84.537  1.00 88.60  ? 1190 VAL A CB  1 
ATOM   9352  C  CG1 . VAL A 1 1190 ? 137.836 113.926 86.053  1.00 101.11 ? 1190 VAL A CG1 1 
ATOM   9353  C  CG2 . VAL A 1 1190 ? 137.167 115.323 84.075  1.00 105.24 ? 1190 VAL A CG2 1 
ATOM   9354  N  N   . SER A 1 1191 ? 140.768 112.714 85.451  1.00 85.62  ? 1191 SER A N   1 
ATOM   9355  C  CA  . SER A 1 1191 ? 141.554 111.566 85.884  1.00 84.04  ? 1191 SER A CA  1 
ATOM   9356  C  C   . SER A 1 1191 ? 141.023 111.057 87.214  1.00 82.68  ? 1191 SER A C   1 
ATOM   9357  O  O   . SER A 1 1191 ? 140.802 111.844 88.140  1.00 95.51  ? 1191 SER A O   1 
ATOM   9358  C  CB  . SER A 1 1191 ? 143.033 111.930 86.015  1.00 100.76 ? 1191 SER A CB  1 
ATOM   9359  O  OG  . SER A 1 1191 ? 143.213 113.005 86.918  1.00 104.75 ? 1191 SER A OG  1 
ATOM   9360  N  N   . CYS A 1 1192 ? 140.827 109.746 87.308  1.00 71.92  ? 1192 CYS A N   1 
ATOM   9361  C  CA  . CYS A 1 1192 ? 140.283 109.140 88.510  1.00 76.80  ? 1192 CYS A CA  1 
ATOM   9362  C  C   . CYS A 1 1192 ? 141.153 107.961 88.916  1.00 91.82  ? 1192 CYS A C   1 
ATOM   9363  O  O   . CYS A 1 1192 ? 141.657 107.223 88.063  1.00 95.60  ? 1192 CYS A O   1 
ATOM   9364  C  CB  . CYS A 1 1192 ? 138.838 108.678 88.284  1.00 65.26  ? 1192 CYS A CB  1 
ATOM   9365  S  SG  . CYS A 1 1192 ? 137.784 109.916 87.487  1.00 100.45 ? 1192 CYS A SG  1 
ATOM   9366  N  N   . ALA A 1 1193 ? 141.318 107.784 90.224  1.00 77.77  ? 1193 ALA A N   1 
ATOM   9367  C  CA  . ALA A 1 1193 ? 142.149 106.721 90.761  1.00 73.09  ? 1193 ALA A CA  1 
ATOM   9368  C  C   . ALA A 1 1193 ? 141.524 106.243 92.062  1.00 76.63  ? 1193 ALA A C   1 
ATOM   9369  O  O   . ALA A 1 1193 ? 140.593 106.856 92.589  1.00 86.67  ? 1193 ALA A O   1 
ATOM   9370  C  CB  . ALA A 1 1193 ? 143.594 107.187 90.973  1.00 68.63  ? 1193 ALA A CB  1 
ATOM   9371  N  N   . LEU A 1 1194 ? 142.056 105.146 92.589  1.00 71.97  ? 1194 LEU A N   1 
ATOM   9372  C  CA  . LEU A 1 1194 ? 141.567 104.561 93.829  1.00 74.40  ? 1194 LEU A CA  1 
ATOM   9373  C  C   . LEU A 1 1194 ? 142.586 104.775 94.941  1.00 72.23  ? 1194 LEU A C   1 
ATOM   9374  O  O   . LEU A 1 1194 ? 143.777 104.498 94.760  1.00 74.61  ? 1194 LEU A O   1 
ATOM   9375  C  CB  . LEU A 1 1194 ? 141.262 103.074 93.644  1.00 82.43  ? 1194 LEU A CB  1 
ATOM   9376  C  CG  . LEU A 1 1194 ? 140.785 102.370 94.908  1.00 68.40  ? 1194 LEU A CG  1 
ATOM   9377  C  CD1 . LEU A 1 1194 ? 139.396 102.870 95.259  1.00 75.59  ? 1194 LEU A CD1 1 
ATOM   9378  C  CD2 . LEU A 1 1194 ? 140.770 100.864 94.704  1.00 54.68  ? 1194 LEU A CD2 1 
ATOM   9379  N  N   . ASP A 1 1195 ? 142.114 105.264 96.087  1.00 67.61  ? 1195 ASP A N   1 
ATOM   9380  C  CA  . ASP A 1 1195 ? 142.988 105.533 97.221  1.00 74.92  ? 1195 ASP A CA  1 
ATOM   9381  C  C   . ASP A 1 1195 ? 143.375 104.239 97.927  1.00 87.68  ? 1195 ASP A C   1 
ATOM   9382  O  O   . ASP A 1 1195 ? 142.514 103.435 98.295  1.00 84.55  ? 1195 ASP A O   1 
ATOM   9383  C  CB  . ASP A 1 1195 ? 142.305 106.479 98.208  1.00 76.75  ? 1195 ASP A CB  1 
ATOM   9384  C  CG  . ASP A 1 1195 ? 143.273 107.065 99.215  1.00 99.33  ? 1195 ASP A CG  1 
ATOM   9385  O  OD1 . ASP A 1 1195 ? 144.498 106.935 99.007  1.00 100.90 ? 1195 ASP A OD1 1 
ATOM   9386  O  OD2 . ASP A 1 1195 ? 142.815 107.646 100.220 1.00 99.26  ? 1195 ASP A OD2 1 
ATOM   9387  N  N   . ARG A 1 1196 ? 144.682 104.044 98.101  1.00 93.00  ? 1196 ARG A N   1 
ATOM   9388  C  CA  . ARG A 1 1196 ? 145.213 102.816 98.673  1.00 92.32  ? 1196 ARG A CA  1 
ATOM   9389  C  C   . ARG A 1 1196 ? 145.063 102.733 100.188 1.00 97.35  ? 1196 ARG A C   1 
ATOM   9390  O  O   . ARG A 1 1196 ? 145.051 101.625 100.735 1.00 103.81 ? 1196 ARG A O   1 
ATOM   9391  C  CB  . ARG A 1 1196 ? 146.690 102.696 98.291  1.00 99.63  ? 1196 ARG A CB  1 
ATOM   9392  C  CG  . ARG A 1 1196 ? 147.367 101.409 98.695  1.00 123.84 ? 1196 ARG A CG  1 
ATOM   9393  C  CD  . ARG A 1 1196 ? 148.801 101.407 98.212  1.00 129.80 ? 1196 ARG A CD  1 
ATOM   9394  N  NE  . ARG A 1 1196 ? 148.856 101.395 96.755  1.00 120.50 ? 1196 ARG A NE  1 
ATOM   9395  C  CZ  . ARG A 1 1196 ? 148.783 100.292 96.019  1.00 123.95 ? 1196 ARG A CZ  1 
ATOM   9396  N  NH1 . ARG A 1 1196 ? 148.642 99.113  96.608  1.00 114.26 ? 1196 ARG A NH1 1 
ATOM   9397  N  NH2 . ARG A 1 1196 ? 148.840 100.367 94.697  1.00 122.87 ? 1196 ARG A NH2 1 
ATOM   9398  N  N   . LYS A 1 1197 ? 144.928 103.864 100.876 1.00 94.31  ? 1197 LYS A N   1 
ATOM   9399  C  CA  . LYS A 1 1197 ? 144.892 103.881 102.333 1.00 86.33  ? 1197 LYS A CA  1 
ATOM   9400  C  C   . LYS A 1 1197 ? 143.476 103.632 102.843 1.00 86.84  ? 1197 LYS A C   1 
ATOM   9401  O  O   . LYS A 1 1197 ? 142.528 104.287 102.398 1.00 93.33  ? 1197 LYS A O   1 
ATOM   9402  C  CB  . LYS A 1 1197 ? 145.434 105.209 102.861 1.00 92.78  ? 1197 LYS A CB  1 
ATOM   9403  C  CG  . LYS A 1 1197 ? 145.343 105.346 104.361 1.00 98.64  ? 1197 LYS A CG  1 
ATOM   9404  C  CD  . LYS A 1 1197 ? 145.450 106.787 104.801 1.00 113.32 ? 1197 LYS A CD  1 
ATOM   9405  C  CE  . LYS A 1 1197 ? 145.182 106.891 106.286 1.00 124.73 ? 1197 LYS A CE  1 
ATOM   9406  N  NZ  . LYS A 1 1197 ? 145.859 105.779 107.005 1.00 115.59 ? 1197 LYS A NZ  1 
ATOM   9407  N  N   . VAL A 1 1198 ? 143.338 102.700 103.787 1.00 91.67  ? 1198 VAL A N   1 
ATOM   9408  C  CA  . VAL A 1 1198 ? 142.048 102.334 104.366 1.00 77.79  ? 1198 VAL A CA  1 
ATOM   9409  C  C   . VAL A 1 1198 ? 142.015 102.740 105.834 1.00 77.11  ? 1198 VAL A C   1 
ATOM   9410  O  O   . VAL A 1 1198 ? 142.978 102.504 106.576 1.00 91.14  ? 1198 VAL A O   1 
ATOM   9411  C  CB  . VAL A 1 1198 ? 141.773 100.826 104.214 1.00 56.65  ? 1198 VAL A CB  1 
ATOM   9412  C  CG1 . VAL A 1 1198 ? 140.379 100.485 104.720 1.00 55.74  ? 1198 VAL A CG1 1 
ATOM   9413  C  CG2 . VAL A 1 1198 ? 141.938 100.399 102.761 1.00 80.96  ? 1198 VAL A CG2 1 
ATOM   9414  N  N   . VAL A 1 1199 ? 140.910 103.354 106.249 1.00 67.53  ? 1199 VAL A N   1 
ATOM   9415  C  CA  . VAL A 1 1199 ? 140.721 103.819 107.622 1.00 62.10  ? 1199 VAL A CA  1 
ATOM   9416  C  C   . VAL A 1 1199 ? 139.951 102.804 108.462 1.00 79.21  ? 1199 VAL A C   1 
ATOM   9417  O  O   . VAL A 1 1199 ? 140.393 102.419 109.543 1.00 89.43  ? 1199 VAL A O   1 
ATOM   9418  C  CB  . VAL A 1 1199 ? 140.020 105.195 107.625 1.00 59.15  ? 1199 VAL A CB  1 
ATOM   9419  C  CG1 . VAL A 1 1199 ? 139.526 105.543 109.023 1.00 58.94  ? 1199 VAL A CG1 1 
ATOM   9420  C  CG2 . VAL A 1 1199 ? 140.961 106.273 107.103 1.00 68.60  ? 1199 VAL A CG2 1 
ATOM   9421  N  N   . GLN A 1 1200 ? 138.792 102.357 107.974 1.00 68.77  ? 1200 GLN A N   1 
ATOM   9422  C  CA  . GLN A 1 1200 ? 137.963 101.373 108.659 1.00 53.89  ? 1200 GLN A CA  1 
ATOM   9423  C  C   . GLN A 1 1200 ? 137.509 100.296 107.685 1.00 56.65  ? 1200 GLN A C   1 
ATOM   9424  O  O   . GLN A 1 1200 ? 137.513 100.487 106.467 1.00 70.86  ? 1200 GLN A O   1 
ATOM   9425  C  CB  . GLN A 1 1200 ? 136.733 102.013 109.318 1.00 56.18  ? 1200 GLN A CB  1 
ATOM   9426  C  CG  . GLN A 1 1200 ? 137.056 103.096 110.325 1.00 80.95  ? 1200 GLN A CG  1 
ATOM   9427  C  CD  . GLN A 1 1200 ? 137.348 102.527 111.698 1.00 79.97  ? 1200 GLN A CD  1 
ATOM   9428  O  OE1 . GLN A 1 1200 ? 137.183 101.329 111.931 1.00 74.13  ? 1200 GLN A OE1 1 
ATOM   9429  N  NE2 . GLN A 1 1200 ? 137.783 103.381 112.616 1.00 80.17  ? 1200 GLN A NE2 1 
ATOM   9430  N  N   . LYS A 1 1201 ? 137.115 99.152  108.242 1.00 57.29  ? 1201 LYS A N   1 
ATOM   9431  C  CA  . LYS A 1 1201 ? 136.635 98.039  107.435 1.00 54.11  ? 1201 LYS A CA  1 
ATOM   9432  C  C   . LYS A 1 1201 ? 135.801 97.107  108.303 1.00 61.10  ? 1201 LYS A C   1 
ATOM   9433  O  O   . LYS A 1 1201 ? 136.131 96.870  109.468 1.00 75.90  ? 1201 LYS A O   1 
ATOM   9434  C  CB  . LYS A 1 1201 ? 137.799 97.274  106.798 1.00 59.40  ? 1201 LYS A CB  1 
ATOM   9435  C  CG  . LYS A 1 1201 ? 138.745 96.673  107.810 1.00 75.29  ? 1201 LYS A CG  1 
ATOM   9436  C  CD  . LYS A 1 1201 ? 140.162 96.621  107.292 1.00 90.89  ? 1201 LYS A CD  1 
ATOM   9437  C  CE  . LYS A 1 1201 ? 141.092 96.186  108.402 1.00 105.27 ? 1201 LYS A CE  1 
ATOM   9438  N  NZ  . LYS A 1 1201 ? 140.861 97.004  109.625 1.00 98.23  ? 1201 LYS A NZ  1 
ATOM   9439  N  N   . HIS A 1 1202 ? 134.713 96.593  107.728 1.00 58.64  ? 1202 HIS A N   1 
ATOM   9440  C  CA  . HIS A 1 1202 ? 133.826 95.645  108.391 1.00 60.23  ? 1202 HIS A CA  1 
ATOM   9441  C  C   . HIS A 1 1202 ? 133.147 94.751  107.360 1.00 58.72  ? 1202 HIS A C   1 
ATOM   9442  O  O   . HIS A 1 1202 ? 132.351 95.245  106.552 1.00 58.04  ? 1202 HIS A O   1 
ATOM   9443  C  CB  . HIS A 1 1202 ? 132.763 96.366  109.224 1.00 52.54  ? 1202 HIS A CB  1 
ATOM   9444  C  CG  . HIS A 1 1202 ? 133.294 97.009  110.469 1.00 63.23  ? 1202 HIS A CG  1 
ATOM   9445  N  ND1 . HIS A 1 1202 ? 133.677 96.281  111.576 1.00 63.75  ? 1202 HIS A ND1 1 
ATOM   9446  C  CD2 . HIS A 1 1202 ? 133.480 98.311  110.792 1.00 69.63  ? 1202 HIS A CD2 1 
ATOM   9447  C  CE1 . HIS A 1 1202 ? 134.092 97.105  112.520 1.00 66.17  ? 1202 HIS A CE1 1 
ATOM   9448  N  NE2 . HIS A 1 1202 ? 133.982 98.343  112.070 1.00 63.86  ? 1202 HIS A NE2 1 
ATOM   9449  N  N   . PRO A 1 1203 ? 133.414 93.433  107.349 1.00 53.15  ? 1203 PRO A N   1 
ATOM   9450  C  CA  . PRO A 1 1203 ? 134.277 92.634  108.229 1.00 57.37  ? 1203 PRO A CA  1 
ATOM   9451  C  C   . PRO A 1 1203 ? 135.740 92.535  107.786 1.00 73.37  ? 1203 PRO A C   1 
ATOM   9452  O  O   . PRO A 1 1203 ? 136.609 92.231  108.606 1.00 87.04  ? 1203 PRO A O   1 
ATOM   9453  C  CB  . PRO A 1 1203 ? 133.622 91.254  108.181 1.00 58.70  ? 1203 PRO A CB  1 
ATOM   9454  C  CG  . PRO A 1 1203 ? 133.055 91.180  106.809 1.00 51.77  ? 1203 PRO A CG  1 
ATOM   9455  C  CD  . PRO A 1 1203 ? 132.609 92.576  106.459 1.00 63.09  ? 1203 PRO A CD  1 
ATOM   9456  N  N   . SER A 1 1204 ? 136.009 92.774  106.506 1.00 68.01  ? 1204 SER A N   1 
ATOM   9457  C  CA  . SER A 1 1204 ? 137.366 92.666  105.991 1.00 70.10  ? 1204 SER A CA  1 
ATOM   9458  C  C   . SER A 1 1204 ? 137.542 93.664  104.852 1.00 66.52  ? 1204 SER A C   1 
ATOM   9459  O  O   . SER A 1 1204 ? 136.696 94.536  104.628 1.00 78.74  ? 1204 SER A O   1 
ATOM   9460  C  CB  . SER A 1 1204 ? 137.658 91.230  105.536 1.00 69.87  ? 1204 SER A CB  1 
ATOM   9461  O  OG  . SER A 1 1204 ? 136.895 90.887  104.389 1.00 66.84  ? 1204 SER A OG  1 
ATOM   9462  N  N   . VAL A 1 1205 ? 138.652 93.525  104.127 1.00 73.80  ? 1205 VAL A N   1 
ATOM   9463  C  CA  . VAL A 1 1205 ? 139.019 94.449  103.062 1.00 62.66  ? 1205 VAL A CA  1 
ATOM   9464  C  C   . VAL A 1 1205 ? 138.731 93.862  101.682 1.00 68.31  ? 1205 VAL A C   1 
ATOM   9465  O  O   . VAL A 1 1205 ? 139.144 94.432  100.667 1.00 83.34  ? 1205 VAL A O   1 
ATOM   9466  C  CB  . VAL A 1 1205 ? 140.498 94.861  103.199 1.00 68.91  ? 1205 VAL A CB  1 
ATOM   9467  C  CG1 . VAL A 1 1205 ? 141.426 93.726  102.757 1.00 83.72  ? 1205 VAL A CG1 1 
ATOM   9468  C  CG2 . VAL A 1 1205 ? 140.795 96.175  102.470 1.00 76.11  ? 1205 VAL A CG2 1 
ATOM   9469  N  N   . ASN A 1 1206 ? 137.981 92.763  101.617 1.00 70.47  ? 1206 ASN A N   1 
ATOM   9470  C  CA  . ASN A 1 1206 ? 137.830 92.019  100.375 1.00 60.37  ? 1206 ASN A CA  1 
ATOM   9471  C  C   . ASN A 1 1206 ? 136.807 92.623  99.424  1.00 57.99  ? 1206 ASN A C   1 
ATOM   9472  O  O   . ASN A 1 1206 ? 136.796 92.251  98.247  1.00 74.38  ? 1206 ASN A O   1 
ATOM   9473  C  CB  . ASN A 1 1206 ? 137.448 90.566  100.670 1.00 63.58  ? 1206 ASN A CB  1 
ATOM   9474  C  CG  . ASN A 1 1206 ? 138.599 89.767  101.243 1.00 72.57  ? 1206 ASN A CG  1 
ATOM   9475  O  OD1 . ASN A 1 1206 ? 138.513 89.240  102.351 1.00 74.04  ? 1206 ASN A OD1 1 
ATOM   9476  N  ND2 . ASN A 1 1206 ? 139.690 89.681  100.491 1.00 70.32  ? 1206 ASN A ND2 1 
ATOM   9477  N  N   . ARG A 1 1207 ? 135.963 93.547  99.882  1.00 56.00  ? 1207 ARG A N   1 
ATOM   9478  C  CA  . ARG A 1 1207 ? 135.066 94.249  98.979  1.00 54.80  ? 1207 ARG A CA  1 
ATOM   9479  C  C   . ARG A 1 1207 ? 135.241 95.747  99.169  1.00 69.95  ? 1207 ARG A C   1 
ATOM   9480  O  O   . ARG A 1 1207 ? 135.508 96.225  100.276 1.00 76.91  ? 1207 ARG A O   1 
ATOM   9481  C  CB  . ARG A 1 1207 ? 133.601 93.886  99.233  1.00 55.84  ? 1207 ARG A CB  1 
ATOM   9482  C  CG  . ARG A 1 1207 ? 133.270 92.425  99.012  1.00 69.26  ? 1207 ARG A CG  1 
ATOM   9483  C  CD  . ARG A 1 1207 ? 133.540 91.940  97.607  1.00 69.30  ? 1207 ARG A CD  1 
ATOM   9484  N  NE  . ARG A 1 1207 ? 133.026 90.584  97.446  1.00 67.17  ? 1207 ARG A NE  1 
ATOM   9485  C  CZ  . ARG A 1 1207 ? 133.673 89.488  97.831  1.00 72.21  ? 1207 ARG A CZ  1 
ATOM   9486  N  NH1 . ARG A 1 1207 ? 134.868 89.580  98.401  1.00 76.03  ? 1207 ARG A NH1 1 
ATOM   9487  N  NH2 . ARG A 1 1207 ? 133.123 88.297  97.649  1.00 81.13  ? 1207 ARG A NH2 1 
ATOM   9488  N  N   . LEU A 1 1208 ? 135.074 96.488  98.074  1.00 67.87  ? 1208 LEU A N   1 
ATOM   9489  C  CA  . LEU A 1 1208 ? 135.255 97.934  98.131  1.00 62.58  ? 1208 LEU A CA  1 
ATOM   9490  C  C   . LEU A 1 1208 ? 134.172 98.611  98.961  1.00 56.65  ? 1208 LEU A C   1 
ATOM   9491  O  O   . LEU A 1 1208 ? 134.431 99.648  99.584  1.00 66.30  ? 1208 LEU A O   1 
ATOM   9492  C  CB  . LEU A 1 1208 ? 135.309 98.512  96.716  1.00 67.31  ? 1208 LEU A CB  1 
ATOM   9493  C  CG  . LEU A 1 1208 ? 135.402 100.035 96.626  1.00 65.13  ? 1208 LEU A CG  1 
ATOM   9494  C  CD1 . LEU A 1 1208 ? 136.775 100.507 97.073  1.00 69.43  ? 1208 LEU A CD1 1 
ATOM   9495  C  CD2 . LEU A 1 1208 ? 135.119 100.486 95.205  1.00 72.43  ? 1208 LEU A CD2 1 
ATOM   9496  N  N   . ALA A 1 1209 ? 132.975 98.033  99.020  1.00 52.90  ? 1209 ALA A N   1 
ATOM   9497  C  CA  . ALA A 1 1209 ? 131.876 98.652  99.751  1.00 45.90  ? 1209 ALA A CA  1 
ATOM   9498  C  C   . ALA A 1 1209 ? 131.891 98.333  101.241 1.00 58.71  ? 1209 ALA A C   1 
ATOM   9499  O  O   . ALA A 1 1209 ? 130.994 98.782  101.962 1.00 80.59  ? 1209 ALA A O   1 
ATOM   9500  C  CB  . ALA A 1 1209 ? 130.536 98.222  99.146  1.00 50.24  ? 1209 ALA A CB  1 
ATOM   9501  N  N   . TRP A 1 1210 ? 132.872 97.570  101.715 1.00 70.42  ? 1210 TRP A N   1 
ATOM   9502  C  CA  . TRP A 1 1210 ? 133.020 97.259  103.131 1.00 59.74  ? 1210 TRP A CA  1 
ATOM   9503  C  C   . TRP A 1 1210 ? 133.968 98.205  103.862 1.00 66.06  ? 1210 TRP A C   1 
ATOM   9504  O  O   . TRP A 1 1210 ? 134.179 98.034  105.067 1.00 75.81  ? 1210 TRP A O   1 
ATOM   9505  C  CB  . TRP A 1 1210 ? 133.515 95.821  103.291 1.00 54.38  ? 1210 TRP A CB  1 
ATOM   9506  C  CG  . TRP A 1 1210 ? 132.514 94.806  102.852 1.00 62.88  ? 1210 TRP A CG  1 
ATOM   9507  C  CD1 . TRP A 1 1210 ? 131.230 95.041  102.456 1.00 66.99  ? 1210 TRP A CD1 1 
ATOM   9508  C  CD2 . TRP A 1 1210 ? 132.723 93.396  102.724 1.00 49.64  ? 1210 TRP A CD2 1 
ATOM   9509  N  NE1 . TRP A 1 1210 ? 130.619 93.860  102.108 1.00 63.22  ? 1210 TRP A NE1 1 
ATOM   9510  C  CE2 . TRP A 1 1210 ? 131.516 92.835  102.264 1.00 54.88  ? 1210 TRP A CE2 1 
ATOM   9511  C  CE3 . TRP A 1 1210 ? 133.810 92.552  102.964 1.00 60.06  ? 1210 TRP A CE3 1 
ATOM   9512  C  CZ2 . TRP A 1 1210 ? 131.367 91.470  102.038 1.00 52.66  ? 1210 TRP A CZ2 1 
ATOM   9513  C  CZ3 . TRP A 1 1210 ? 133.659 91.197  102.739 1.00 53.03  ? 1210 TRP A CZ3 1 
ATOM   9514  C  CH2 . TRP A 1 1210 ? 132.449 90.668  102.282 1.00 53.41  ? 1210 TRP A CH2 1 
ATOM   9515  N  N   . THR A 1 1211 ? 134.535 99.194  103.173 1.00 60.88  ? 1211 THR A N   1 
ATOM   9516  C  CA  . THR A 1 1211 ? 135.609 100.017 103.711 1.00 53.35  ? 1211 THR A CA  1 
ATOM   9517  C  C   . THR A 1 1211 ? 135.308 101.490 103.474 1.00 54.95  ? 1211 THR A C   1 
ATOM   9518  O  O   . THR A 1 1211 ? 134.464 101.846 102.648 1.00 69.35  ? 1211 THR A O   1 
ATOM   9519  C  CB  . THR A 1 1211 ? 136.961 99.666  103.070 1.00 62.30  ? 1211 THR A CB  1 
ATOM   9520  O  OG1 . THR A 1 1211 ? 136.931 100.018 101.680 1.00 62.68  ? 1211 THR A OG1 1 
ATOM   9521  C  CG2 . THR A 1 1211 ? 137.248 98.176  103.192 1.00 79.45  ? 1211 THR A CG2 1 
ATOM   9522  N  N   . ILE A 1 1212 ? 136.016 102.353 104.208 1.00 46.74  ? 1212 ILE A N   1 
ATOM   9523  C  CA  . ILE A 1 1212 ? 135.990 103.789 103.960 1.00 48.42  ? 1212 ILE A CA  1 
ATOM   9524  C  C   . ILE A 1 1212 ? 137.419 104.321 103.986 1.00 56.09  ? 1212 ILE A C   1 
ATOM   9525  O  O   . ILE A 1 1212 ? 138.354 103.647 104.418 1.00 70.84  ? 1212 ILE A O   1 
ATOM   9526  C  CB  . ILE A 1 1212 ? 135.119 104.554 104.978 1.00 39.67  ? 1212 ILE A CB  1 
ATOM   9527  C  CG1 . ILE A 1 1212 ? 135.571 104.273 106.408 1.00 58.69  ? 1212 ILE A CG1 1 
ATOM   9528  C  CG2 . ILE A 1 1212 ? 133.653 104.166 104.824 1.00 60.07  ? 1212 ILE A CG2 1 
ATOM   9529  C  CD1 . ILE A 1 1212 ? 135.106 105.329 107.398 1.00 52.23  ? 1212 ILE A CD1 1 
ATOM   9530  N  N   . GLY A 1 1213 ? 137.571 105.563 103.523 1.00 69.61  ? 1213 GLY A N   1 
ATOM   9531  C  CA  . GLY A 1 1213 ? 138.870 106.204 103.444 1.00 62.86  ? 1213 GLY A CA  1 
ATOM   9532  C  C   . GLY A 1 1213 ? 138.887 107.641 103.931 1.00 69.99  ? 1213 GLY A C   1 
ATOM   9533  O  O   . GLY A 1 1213 ? 138.150 107.998 104.854 1.00 74.78  ? 1213 GLY A O   1 
ATOM   9534  N  N   . ASN A 1 1214 ? 139.719 108.478 103.308 1.00 77.40  ? 1214 ASN A N   1 
ATOM   9535  C  CA  . ASN A 1 1214 ? 139.945 109.843 103.765 1.00 77.39  ? 1214 ASN A CA  1 
ATOM   9536  C  C   . ASN A 1 1214 ? 139.296 110.905 102.893 1.00 85.54  ? 1214 ASN A C   1 
ATOM   9537  O  O   . ASN A 1 1214 ? 139.016 112.001 103.381 1.00 85.49  ? 1214 ASN A O   1 
ATOM   9538  C  CB  . ASN A 1 1214 ? 141.452 110.135 103.813 1.00 86.63  ? 1214 ASN A CB  1 
ATOM   9539  C  CG  . ASN A 1 1214 ? 142.065 109.843 105.161 1.00 106.15 ? 1214 ASN A CG  1 
ATOM   9540  O  OD1 . ASN A 1 1214 ? 142.911 108.956 105.289 1.00 103.86 ? 1214 ASN A OD1 1 
ATOM   9541  N  ND2 . ASN A 1 1214 ? 141.644 110.581 106.178 1.00 109.52 ? 1214 ASN A ND2 1 
ATOM   9542  N  N   . ARG A 1 1215 ? 139.052 110.604 101.622 1.00 87.06  ? 1215 ARG A N   1 
ATOM   9543  C  CA  . ARG A 1 1215 ? 138.725 111.625 100.638 1.00 83.17  ? 1215 ARG A CA  1 
ATOM   9544  C  C   . ARG A 1 1215 ? 137.324 112.194 100.869 1.00 91.08  ? 1215 ARG A C   1 
ATOM   9545  O  O   . ARG A 1 1215 ? 136.528 111.682 101.661 1.00 87.93  ? 1215 ARG A O   1 
ATOM   9546  C  CB  . ARG A 1 1215 ? 138.865 111.061 99.226  1.00 77.70  ? 1215 ARG A CB  1 
ATOM   9547  C  CG  . ARG A 1 1215 ? 140.252 110.500 98.956  1.00 76.12  ? 1215 ARG A CG  1 
ATOM   9548  C  CD  . ARG A 1 1215 ? 141.324 111.437 99.498  1.00 87.99  ? 1215 ARG A CD  1 
ATOM   9549  N  NE  . ARG A 1 1215 ? 142.669 111.034 99.108  1.00 88.58  ? 1215 ARG A NE  1 
ATOM   9550  C  CZ  . ARG A 1 1215 ? 143.457 111.752 98.315  1.00 97.00  ? 1215 ARG A CZ  1 
ATOM   9551  N  NH1 . ARG A 1 1215 ? 143.031 112.910 97.827  1.00 90.71  ? 1215 ARG A NH1 1 
ATOM   9552  N  NH2 . ARG A 1 1215 ? 144.670 111.314 98.008  1.00 93.28  ? 1215 ARG A NH2 1 
ATOM   9553  N  N   . ALA A 1 1216 ? 137.035 113.286 100.155 1.00 91.73  ? 1216 ALA A N   1 
ATOM   9554  C  CA  . ALA A 1 1216 ? 135.735 113.942 100.175 1.00 85.24  ? 1216 ALA A CA  1 
ATOM   9555  C  C   . ALA A 1 1216 ? 135.577 114.785 98.914  1.00 96.11  ? 1216 ALA A C   1 
ATOM   9556  O  O   . ALA A 1 1216 ? 135.727 116.013 98.958  1.00 111.86 ? 1216 ALA A O   1 
ATOM   9557  C  CB  . ALA A 1 1216 ? 135.584 114.805 101.430 1.00 83.36  ? 1216 ALA A CB  1 
ATOM   9558  N  N   . PRO A 1 1217 ? 135.270 114.159 97.773  1.00 84.99  ? 1217 PRO A N   1 
ATOM   9559  C  CA  . PRO A 1 1217 ? 135.242 114.902 96.502  1.00 87.20  ? 1217 PRO A CA  1 
ATOM   9560  C  C   . PRO A 1 1217 ? 134.036 115.815 96.328  1.00 98.83  ? 1217 PRO A C   1 
ATOM   9561  O  O   . PRO A 1 1217 ? 134.079 116.703 95.469  1.00 101.38 ? 1217 PRO A O   1 
ATOM   9562  C  CB  . PRO A 1 1217 ? 135.245 113.789 95.447  1.00 70.29  ? 1217 PRO A CB  1 
ATOM   9563  C  CG  . PRO A 1 1217 ? 134.609 112.621 96.135  1.00 73.58  ? 1217 PRO A CG  1 
ATOM   9564  C  CD  . PRO A 1 1217 ? 134.961 112.728 97.595  1.00 69.78  ? 1217 PRO A CD  1 
ATOM   9565  N  N   . TYR A 1 1218 ? 132.968 115.631 97.105  1.00 105.12 ? 1218 TYR A N   1 
ATOM   9566  C  CA  . TYR A 1 1218 ? 131.771 116.455 96.964  1.00 104.66 ? 1218 TYR A CA  1 
ATOM   9567  C  C   . TYR A 1 1218 ? 131.893 117.822 97.620  1.00 128.54 ? 1218 TYR A C   1 
ATOM   9568  O  O   . TYR A 1 1218 ? 131.196 118.754 97.203  1.00 135.40 ? 1218 TYR A O   1 
ATOM   9569  C  CB  . TYR A 1 1218 ? 130.553 115.726 97.529  1.00 90.11  ? 1218 TYR A CB  1 
ATOM   9570  C  CG  . TYR A 1 1218 ? 130.282 114.427 96.820  1.00 88.24  ? 1218 TYR A CG  1 
ATOM   9571  C  CD1 . TYR A 1 1218 ? 130.536 114.296 95.463  1.00 89.66  ? 1218 TYR A CD1 1 
ATOM   9572  C  CD2 . TYR A 1 1218 ? 129.769 113.334 97.499  1.00 89.69  ? 1218 TYR A CD2 1 
ATOM   9573  C  CE1 . TYR A 1 1218 ? 130.295 113.111 94.802  1.00 88.74  ? 1218 TYR A CE1 1 
ATOM   9574  C  CE2 . TYR A 1 1218 ? 129.523 112.142 96.845  1.00 90.96  ? 1218 TYR A CE2 1 
ATOM   9575  C  CZ  . TYR A 1 1218 ? 129.788 112.037 95.497  1.00 79.66  ? 1218 TYR A CZ  1 
ATOM   9576  O  OH  . TYR A 1 1218 ? 129.544 110.852 94.841  1.00 68.90  ? 1218 TYR A OH  1 
ATOM   9577  N  N   . ILE A 1 1219 ? 132.758 117.966 98.623  1.00 129.55 ? 1219 ILE A N   1 
ATOM   9578  C  CA  . ILE A 1 1219 ? 132.917 119.253 99.293  1.00 146.69 ? 1219 ILE A CA  1 
ATOM   9579  C  C   . ILE A 1 1219 ? 133.457 120.294 98.320  1.00 154.15 ? 1219 ILE A C   1 
ATOM   9580  O  O   . ILE A 1 1219 ? 133.079 121.471 98.374  1.00 159.73 ? 1219 ILE A O   1 
ATOM   9581  C  CB  . ILE A 1 1219 ? 133.818 119.098 100.532 1.00 149.94 ? 1219 ILE A CB  1 
ATOM   9582  C  CG1 . ILE A 1 1219 ? 133.042 118.426 101.667 1.00 158.77 ? 1219 ILE A CG1 1 
ATOM   9583  C  CG2 . ILE A 1 1219 ? 134.357 120.446 100.988 1.00 164.94 ? 1219 ILE A CG2 1 
ATOM   9584  C  CD1 . ILE A 1 1219 ? 133.877 118.139 102.894 1.00 160.08 ? 1219 ILE A CD1 1 
ATOM   9585  N  N   . GLY A 1 1220 ? 134.328 119.875 97.400  1.00 155.45 ? 1220 GLY A N   1 
ATOM   9586  C  CA  . GLY A 1 1220 ? 134.840 120.804 96.405  1.00 161.73 ? 1220 GLY A CA  1 
ATOM   9587  C  C   . GLY A 1 1220 ? 133.738 121.451 95.586  1.00 164.98 ? 1220 GLY A C   1 
ATOM   9588  O  O   . GLY A 1 1220 ? 133.794 122.647 95.289  1.00 166.59 ? 1220 GLY A O   1 
ATOM   9589  N  N   . SER A 1 1221 ? 132.722 120.677 95.214  1.00 164.29 ? 1221 SER A N   1 
ATOM   9590  C  CA  . SER A 1 1221 ? 131.594 121.221 94.463  1.00 171.98 ? 1221 SER A CA  1 
ATOM   9591  C  C   . SER A 1 1221 ? 130.409 121.483 95.390  1.00 160.58 ? 1221 SER A C   1 
ATOM   9592  O  O   . SER A 1 1221 ? 129.725 122.500 95.268  1.00 156.64 ? 1221 SER A O   1 
ATOM   9593  C  CB  . SER A 1 1221 ? 131.177 120.269 93.342  1.00 156.47 ? 1221 SER A CB  1 
ATOM   9594  O  OG  . SER A 1 1221 ? 130.555 119.110 93.865  1.00 149.60 ? 1221 SER A OG  1 
ATOM   9595  N  N   . PRO A 1 1230 ? 125.016 140.818 98.690  1.00 196.16 ? 1230 PRO A N   1 
ATOM   9596  C  CA  . PRO A 1 1230 ? 123.683 141.215 99.155  1.00 194.44 ? 1230 PRO A CA  1 
ATOM   9597  C  C   . PRO A 1 1230 ? 123.752 142.374 100.144 1.00 191.76 ? 1230 PRO A C   1 
ATOM   9598  O  O   . PRO A 1 1230 ? 123.934 142.144 101.340 1.00 190.04 ? 1230 PRO A O   1 
ATOM   9599  C  CB  . PRO A 1 1230 ? 123.154 139.947 99.827  1.00 198.30 ? 1230 PRO A CB  1 
ATOM   9600  C  CG  . PRO A 1 1230 ? 124.381 139.220 100.271 1.00 197.75 ? 1230 PRO A CG  1 
ATOM   9601  C  CD  . PRO A 1 1230 ? 125.448 139.531 99.262  1.00 186.97 ? 1230 PRO A CD  1 
ATOM   9602  N  N   . PRO A 1 1231 ? 123.613 143.606 99.647  1.00 192.56 ? 1231 PRO A N   1 
ATOM   9603  C  CA  . PRO A 1 1231 ? 123.690 144.766 100.550 1.00 197.40 ? 1231 PRO A CA  1 
ATOM   9604  C  C   . PRO A 1 1231 ? 122.638 144.765 101.644 1.00 196.37 ? 1231 PRO A C   1 
ATOM   9605  O  O   . PRO A 1 1231 ? 122.920 145.232 102.756 1.00 192.93 ? 1231 PRO A O   1 
ATOM   9606  C  CB  . PRO A 1 1231 ? 123.516 145.964 99.602  1.00 193.01 ? 1231 PRO A CB  1 
ATOM   9607  C  CG  . PRO A 1 1231 ? 122.941 145.394 98.339  1.00 185.09 ? 1231 PRO A CG  1 
ATOM   9608  C  CD  . PRO A 1 1231 ? 123.461 144.001 98.238  1.00 188.14 ? 1231 PRO A CD  1 
ATOM   9609  N  N   . LEU A 1 1232 ? 121.441 144.245 101.379 1.00 193.92 ? 1232 LEU A N   1 
ATOM   9610  C  CA  . LEU A 1 1232 ? 120.375 144.221 102.368 1.00 194.76 ? 1232 LEU A CA  1 
ATOM   9611  C  C   . LEU A 1 1232 ? 119.791 142.821 102.493 1.00 188.10 ? 1232 LEU A C   1 
ATOM   9612  O  O   . LEU A 1 1232 ? 119.886 141.996 101.580 1.00 186.32 ? 1232 LEU A O   1 
ATOM   9613  C  CB  . LEU A 1 1232 ? 119.270 145.228 102.015 1.00 188.01 ? 1232 LEU A CB  1 
ATOM   9614  C  CG  . LEU A 1 1232 ? 119.719 146.692 102.033 1.00 181.95 ? 1232 LEU A CG  1 
ATOM   9615  C  CD1 . LEU A 1 1232 ? 118.557 147.624 101.744 1.00 172.57 ? 1232 LEU A CD1 1 
ATOM   9616  C  CD2 . LEU A 1 1232 ? 120.359 147.035 103.370 1.00 180.46 ? 1232 LEU A CD2 1 
ATOM   9617  N  N   . ARG A 1 1233 ? 119.178 142.568 103.649 1.00 181.89 ? 1233 ARG A N   1 
ATOM   9618  C  CA  . ARG A 1 1233 ? 118.567 141.280 103.950 1.00 179.37 ? 1233 ARG A CA  1 
ATOM   9619  C  C   . ARG A 1 1233 ? 117.568 141.492 105.078 1.00 186.38 ? 1233 ARG A C   1 
ATOM   9620  O  O   . ARG A 1 1233 ? 117.922 142.063 106.112 1.00 189.87 ? 1233 ARG A O   1 
ATOM   9621  C  CB  . ARG A 1 1233 ? 119.638 140.254 104.343 1.00 183.17 ? 1233 ARG A CB  1 
ATOM   9622  C  CG  . ARG A 1 1233 ? 119.126 138.857 104.644 1.00 185.65 ? 1233 ARG A CG  1 
ATOM   9623  C  CD  . ARG A 1 1233 ? 120.193 138.050 105.369 1.00 190.11 ? 1233 ARG A CD  1 
ATOM   9624  N  NE  . ARG A 1 1233 ? 119.683 136.785 105.887 1.00 200.05 ? 1233 ARG A NE  1 
ATOM   9625  C  CZ  . ARG A 1 1233 ? 120.326 136.026 106.768 1.00 199.61 ? 1233 ARG A CZ  1 
ATOM   9626  N  NH1 . ARG A 1 1233 ? 119.787 134.890 107.185 1.00 193.48 ? 1233 ARG A NH1 1 
ATOM   9627  N  NH2 . ARG A 1 1233 ? 121.508 136.406 107.235 1.00 189.51 ? 1233 ARG A NH2 1 
ATOM   9628  N  N   . VAL A 1 1234 ? 116.331 141.035 104.883 1.00 185.39 ? 1234 VAL A N   1 
ATOM   9629  C  CA  . VAL A 1 1234 ? 115.263 141.287 105.846 1.00 187.93 ? 1234 VAL A CA  1 
ATOM   9630  C  C   . VAL A 1 1234 ? 115.208 140.153 106.859 1.00 183.83 ? 1234 VAL A C   1 
ATOM   9631  O  O   . VAL A 1 1234 ? 115.427 138.984 106.518 1.00 175.78 ? 1234 VAL A O   1 
ATOM   9632  C  CB  . VAL A 1 1234 ? 113.912 141.455 105.122 1.00 175.89 ? 1234 VAL A CB  1 
ATOM   9633  C  CG1 . VAL A 1 1234 ? 112.790 141.718 106.118 1.00 166.31 ? 1234 VAL A CG1 1 
ATOM   9634  C  CG2 . VAL A 1 1234 ? 113.993 142.582 104.103 1.00 180.20 ? 1234 VAL A CG2 1 
ATOM   9635  N  N   . ASN A 1 1235 ? 114.927 140.504 108.119 1.00 181.02 ? 1235 ASN A N   1 
ATOM   9636  C  CA  . ASN A 1 1235 ? 114.869 139.501 109.179 1.00 184.75 ? 1235 ASN A CA  1 
ATOM   9637  C  C   . ASN A 1 1235 ? 113.807 138.450 108.881 1.00 181.68 ? 1235 ASN A C   1 
ATOM   9638  O  O   . ASN A 1 1235 ? 114.086 137.246 108.893 1.00 179.31 ? 1235 ASN A O   1 
ATOM   9639  C  CB  . ASN A 1 1235 ? 114.594 140.172 110.525 1.00 178.04 ? 1235 ASN A CB  1 
ATOM   9640  C  CG  . ASN A 1 1235 ? 115.780 140.963 111.035 1.00 164.78 ? 1235 ASN A CG  1 
ATOM   9641  O  OD1 . ASN A 1 1235 ? 116.930 140.623 110.762 1.00 160.85 ? 1235 ASN A OD1 1 
ATOM   9642  N  ND2 . ASN A 1 1235 ? 115.506 142.017 111.794 1.00 166.94 ? 1235 ASN A ND2 1 
ATOM   9643  N  N   . CYS A 1 1236 ? 112.580 138.892 108.600 1.00 178.28 ? 1236 CYS A N   1 
ATOM   9644  C  CA  . CYS A 1 1236 ? 111.451 137.994 108.367 1.00 175.46 ? 1236 CYS A CA  1 
ATOM   9645  C  C   . CYS A 1 1236 ? 110.842 138.318 107.009 1.00 169.66 ? 1236 CYS A C   1 
ATOM   9646  O  O   . CYS A 1 1236 ? 109.892 139.113 106.915 1.00 160.01 ? 1236 CYS A O   1 
ATOM   9647  C  CB  . CYS A 1 1236 ? 110.413 138.121 109.479 1.00 176.73 ? 1236 CYS A CB  1 
ATOM   9648  S  SG  . CYS A 1 1236 ? 110.875 137.311 111.027 1.00 211.93 ? 1236 CYS A SG  1 
ATOM   9649  N  N   . PRO A 1 1237 ? 111.353 137.727 105.934 1.00 168.10 ? 1237 PRO A N   1 
ATOM   9650  C  CA  . PRO A 1 1237 ? 110.744 137.937 104.617 1.00 158.89 ? 1237 PRO A CA  1 
ATOM   9651  C  C   . PRO A 1 1237 ? 109.647 136.923 104.337 1.00 150.69 ? 1237 PRO A C   1 
ATOM   9652  O  O   . PRO A 1 1237 ? 109.855 135.718 104.515 1.00 145.61 ? 1237 PRO A O   1 
ATOM   9653  C  CB  . PRO A 1 1237 ? 111.930 137.784 103.657 1.00 157.78 ? 1237 PRO A CB  1 
ATOM   9654  C  CG  . PRO A 1 1237 ? 112.924 136.912 104.397 1.00 163.73 ? 1237 PRO A CG  1 
ATOM   9655  C  CD  . PRO A 1 1237 ? 112.542 136.863 105.860 1.00 168.16 ? 1237 PRO A CD  1 
ATOM   9656  N  N   . SER A 1 1238 ? 108.478 137.390 103.912 1.00 139.16 ? 1238 SER A N   1 
ATOM   9657  C  CA  . SER A 1 1238 ? 107.410 136.463 103.581 1.00 135.76 ? 1238 SER A CA  1 
ATOM   9658  C  C   . SER A 1 1238 ? 107.744 135.723 102.287 1.00 135.60 ? 1238 SER A C   1 
ATOM   9659  O  O   . SER A 1 1238 ? 108.694 136.058 101.572 1.00 135.40 ? 1238 SER A O   1 
ATOM   9660  C  CB  . SER A 1 1238 ? 106.080 137.203 103.447 1.00 127.14 ? 1238 SER A CB  1 
ATOM   9661  O  OG  . SER A 1 1238 ? 106.239 138.406 102.714 1.00 129.88 ? 1238 SER A OG  1 
ATOM   9662  N  N   . ALA A 1 1239 ? 106.943 134.698 101.986 1.00 129.90 ? 1239 ALA A N   1 
ATOM   9663  C  CA  . ALA A 1 1239 ? 107.157 133.934 100.762 1.00 133.44 ? 1239 ALA A CA  1 
ATOM   9664  C  C   . ALA A 1 1239 ? 106.963 134.812 99.533  1.00 125.41 ? 1239 ALA A C   1 
ATOM   9665  O  O   . ALA A 1 1239 ? 107.688 134.677 98.537  1.00 121.60 ? 1239 ALA A O   1 
ATOM   9666  C  CB  . ALA A 1 1239 ? 106.220 132.729 100.720 1.00 138.75 ? 1239 ALA A CB  1 
ATOM   9667  N  N   . ALA A 1 1240 ? 105.986 135.720 99.589  1.00 117.60 ? 1240 ALA A N   1 
ATOM   9668  C  CA  . ALA A 1 1240 ? 105.724 136.603 98.459  1.00 107.72 ? 1240 ALA A CA  1 
ATOM   9669  C  C   . ALA A 1 1240 ? 106.937 137.469 98.149  1.00 115.71 ? 1240 ALA A C   1 
ATOM   9670  O  O   . ALA A 1 1240 ? 107.312 137.631 96.981  1.00 110.14 ? 1240 ALA A O   1 
ATOM   9671  C  CB  . ALA A 1 1240 ? 104.501 137.473 98.747  1.00 91.95  ? 1240 ALA A CB  1 
ATOM   9672  N  N   . LEU A 1 1241 ? 107.568 138.030 99.184  1.00 115.73 ? 1241 LEU A N   1 
ATOM   9673  C  CA  . LEU A 1 1241 ? 108.753 138.851 98.965  1.00 105.22 ? 1241 LEU A CA  1 
ATOM   9674  C  C   . LEU A 1 1241 ? 109.914 138.025 98.412  1.00 106.36 ? 1241 LEU A C   1 
ATOM   9675  O  O   . LEU A 1 1241 ? 110.623 138.479 97.505  1.00 110.49 ? 1241 LEU A O   1 
ATOM   9676  C  CB  . LEU A 1 1241 ? 109.143 139.541 100.274 1.00 100.14 ? 1241 LEU A CB  1 
ATOM   9677  C  CG  . LEU A 1 1241 ? 110.391 140.422 100.313 1.00 115.53 ? 1241 LEU A CG  1 
ATOM   9678  C  CD1 . LEU A 1 1241 ? 110.479 141.283 99.064  1.00 112.25 ? 1241 LEU A CD1 1 
ATOM   9679  C  CD2 . LEU A 1 1241 ? 110.367 141.290 101.559 1.00 124.28 ? 1241 LEU A CD2 1 
ATOM   9680  N  N   . LYS A 1 1242 ? 110.119 136.810 98.932  1.00 103.78 ? 1242 LYS A N   1 
ATOM   9681  C  CA  . LYS A 1 1242 ? 111.182 135.954 98.410  1.00 108.02 ? 1242 LYS A CA  1 
ATOM   9682  C  C   . LYS A 1 1242 ? 110.978 135.670 96.924  1.00 121.02 ? 1242 LYS A C   1 
ATOM   9683  O  O   . LYS A 1 1242 ? 111.915 135.775 96.118  1.00 122.57 ? 1242 LYS A O   1 
ATOM   9684  C  CB  . LYS A 1 1242 ? 111.255 134.642 99.196  1.00 115.35 ? 1242 LYS A CB  1 
ATOM   9685  C  CG  . LYS A 1 1242 ? 111.692 134.768 100.648 1.00 129.73 ? 1242 LYS A CG  1 
ATOM   9686  C  CD  . LYS A 1 1242 ? 111.746 133.391 101.304 1.00 139.68 ? 1242 LYS A CD  1 
ATOM   9687  C  CE  . LYS A 1 1242 ? 112.277 133.452 102.727 1.00 141.52 ? 1242 LYS A CE  1 
ATOM   9688  N  NZ  . LYS A 1 1242 ? 111.355 134.174 103.641 1.00 136.14 ? 1242 LYS A NZ  1 
ATOM   9689  N  N   . GLU A 1 1243 ? 109.747 135.323 96.542  1.00 115.15 ? 1243 GLU A N   1 
ATOM   9690  C  CA  . GLU A 1 1243 ? 109.473 134.990 95.149  1.00 107.38 ? 1243 GLU A CA  1 
ATOM   9691  C  C   . GLU A 1 1243 ? 109.584 136.216 94.249  1.00 107.93 ? 1243 GLU A C   1 
ATOM   9692  O  O   . GLU A 1 1243 ? 110.056 136.114 93.107  1.00 110.46 ? 1243 GLU A O   1 
ATOM   9693  C  CB  . GLU A 1 1243 ? 108.094 134.342 95.039  1.00 102.47 ? 1243 GLU A CB  1 
ATOM   9694  C  CG  . GLU A 1 1243 ? 108.000 133.023 95.794  1.00 127.84 ? 1243 GLU A CG  1 
ATOM   9695  C  CD  . GLU A 1 1243 ? 106.573 132.572 96.021  1.00 131.98 ? 1243 GLU A CD  1 
ATOM   9696  O  OE1 . GLU A 1 1243 ? 105.681 133.013 95.269  1.00 123.65 ? 1243 GLU A OE1 1 
ATOM   9697  O  OE2 . GLU A 1 1243 ? 106.346 131.773 96.956  1.00 125.05 ? 1243 GLU A OE2 1 
ATOM   9698  N  N   . ALA A 1 1244 ? 109.158 137.384 94.740  1.00 102.37 ? 1244 ALA A N   1 
ATOM   9699  C  CA  . ALA A 1 1244 ? 109.320 138.604 93.958  1.00 101.18 ? 1244 ALA A CA  1 
ATOM   9700  C  C   . ALA A 1 1244 ? 110.795 138.900 93.721  1.00 104.98 ? 1244 ALA A C   1 
ATOM   9701  O  O   . ALA A 1 1244 ? 111.191 139.294 92.614  1.00 101.76 ? 1244 ALA A O   1 
ATOM   9702  C  CB  . ALA A 1 1244 ? 108.639 139.777 94.662  1.00 98.47  ? 1244 ALA A CB  1 
ATOM   9703  N  N   . ILE A 1 1245 ? 111.626 138.713 94.750  1.00 105.76 ? 1245 ILE A N   1 
ATOM   9704  C  CA  . ILE A 1 1245 ? 113.058 138.942 94.588  1.00 101.28 ? 1245 ILE A CA  1 
ATOM   9705  C  C   . ILE A 1 1245 ? 113.632 137.970 93.560  1.00 109.60 ? 1245 ILE A C   1 
ATOM   9706  O  O   . ILE A 1 1245 ? 114.456 138.353 92.721  1.00 118.81 ? 1245 ILE A O   1 
ATOM   9707  C  CB  . ILE A 1 1245 ? 113.784 138.847 95.945  1.00 104.22 ? 1245 ILE A CB  1 
ATOM   9708  C  CG1 . ILE A 1 1245 ? 113.318 139.963 96.882  1.00 108.82 ? 1245 ILE A CG1 1 
ATOM   9709  C  CG2 . ILE A 1 1245 ? 115.294 138.953 95.759  1.00 116.71 ? 1245 ILE A CG2 1 
ATOM   9710  C  CD1 . ILE A 1 1245 ? 113.445 141.358 96.303  1.00 110.76 ? 1245 ILE A CD1 1 
ATOM   9711  N  N   . GLU A 1 1246 ? 113.213 136.699 93.605  1.00 109.79 ? 1246 GLU A N   1 
ATOM   9712  C  CA  . GLU A 1 1246 ? 113.729 135.730 92.635  1.00 110.90 ? 1246 GLU A CA  1 
ATOM   9713  C  C   . GLU A 1 1246 ? 113.335 136.109 91.202  1.00 104.39 ? 1246 GLU A C   1 
ATOM   9714  O  O   . GLU A 1 1246 ? 114.156 136.011 90.278  1.00 107.42 ? 1246 GLU A O   1 
ATOM   9715  C  CB  . GLU A 1 1246 ? 113.295 134.323 93.019  1.00 124.14 ? 1246 GLU A CB  1 
ATOM   9716  C  CG  . GLU A 1 1246 ? 113.933 133.871 94.354  1.00 137.80 ? 1246 GLU A CG  1 
ATOM   9717  C  CD  . GLU A 1 1246 ? 113.368 132.570 94.893  1.00 145.82 ? 1246 GLU A CD  1 
ATOM   9718  O  OE1 . GLU A 1 1246 ? 112.571 131.941 94.180  1.00 128.48 ? 1246 GLU A OE1 1 
ATOM   9719  O  OE2 . GLU A 1 1246 ? 113.722 132.177 96.027  1.00 143.88 ? 1246 GLU A OE2 1 
ATOM   9720  N  N   . MET A 1 1247 ? 112.084 136.547 90.990  1.00 101.57 ? 1247 MET A N   1 
ATOM   9721  C  CA  . MET A 1 1247 ? 111.652 136.960 89.638  1.00 96.69  ? 1247 MET A CA  1 
ATOM   9722  C  C   . MET A 1 1247 ? 112.449 138.174 89.171  1.00 109.38 ? 1247 MET A C   1 
ATOM   9723  O  O   . MET A 1 1247 ? 112.896 138.213 88.024  1.00 113.04 ? 1247 MET A O   1 
ATOM   9724  C  CB  . MET A 1 1247 ? 110.167 137.235 89.583  1.00 93.28  ? 1247 MET A CB  1 
ATOM   9725  C  CG  . MET A 1 1247 ? 109.283 135.972 89.390  1.00 100.57 ? 1247 MET A CG  1 
ATOM   9726  S  SD  . MET A 1 1247 ? 107.641 136.556 88.918  1.00 103.44 ? 1247 MET A SD  1 
ATOM   9727  C  CE  . MET A 1 1247 ? 107.353 137.453 90.520  1.00 78.83  ? 1247 MET A CE  1 
ATOM   9728  N  N   . VAL A 1 1248 ? 112.643 139.181 90.042  1.00 113.60 ? 1248 VAL A N   1 
ATOM   9729  C  CA  . VAL A 1 1248 ? 113.414 140.340 89.615  1.00 103.46 ? 1248 VAL A CA  1 
ATOM   9730  C  C   . VAL A 1 1248 ? 114.834 139.924 89.246  1.00 107.62 ? 1248 VAL A C   1 
ATOM   9731  O  O   . VAL A 1 1248 ? 115.363 140.343 88.208  1.00 101.39 ? 1248 VAL A O   1 
ATOM   9732  C  CB  . VAL A 1 1248 ? 113.383 141.428 90.697  1.00 105.95 ? 1248 VAL A CB  1 
ATOM   9733  C  CG1 . VAL A 1 1248 ? 114.348 142.553 90.334  1.00 115.46 ? 1248 VAL A CG1 1 
ATOM   9734  C  CG2 . VAL A 1 1248 ? 111.968 141.961 90.851  1.00 117.20 ? 1248 VAL A CG2 1 
ATOM   9735  N  N   . SER A 1 1249 ? 115.461 139.080 90.068  1.00 115.40 ? 1249 SER A N   1 
ATOM   9736  C  CA  . SER A 1 1249 ? 116.824 138.639 89.783  1.00 114.84 ? 1249 SER A CA  1 
ATOM   9737  C  C   . SER A 1 1249 ? 116.911 137.930 88.435  1.00 112.57 ? 1249 SER A C   1 
ATOM   9738  O  O   . SER A 1 1249 ? 117.751 138.278 87.593  1.00 120.11 ? 1249 SER A O   1 
ATOM   9739  C  CB  . SER A 1 1249 ? 117.324 137.720 90.899  1.00 114.81 ? 1249 SER A CB  1 
ATOM   9740  O  OG  . SER A 1 1249 ? 118.489 137.020 90.493  1.00 111.65 ? 1249 SER A OG  1 
ATOM   9741  N  N   . ARG A 1 1250 ? 116.037 136.943 88.201  1.00 100.56 ? 1250 ARG A N   1 
ATOM   9742  C  CA  . ARG A 1 1250 ? 116.108 136.193 86.947  1.00 94.07  ? 1250 ARG A CA  1 
ATOM   9743  C  C   . ARG A 1 1250 ? 115.877 137.100 85.744  1.00 95.39  ? 1250 ARG A C   1 
ATOM   9744  O  O   . ARG A 1 1250 ? 116.637 137.058 84.764  1.00 108.16 ? 1250 ARG A O   1 
ATOM   9745  C  CB  . ARG A 1 1250 ? 115.080 135.059 86.947  1.00 99.92  ? 1250 ARG A CB  1 
ATOM   9746  C  CG  . ARG A 1 1250 ? 115.465 133.824 87.739  1.00 108.92 ? 1250 ARG A CG  1 
ATOM   9747  C  CD  . ARG A 1 1250 ? 114.224 133.019 88.097  1.00 87.26  ? 1250 ARG A CD  1 
ATOM   9748  N  NE  . ARG A 1 1250 ? 114.551 131.736 88.709  1.00 94.64  ? 1250 ARG A NE  1 
ATOM   9749  C  CZ  . ARG A 1 1250 ? 114.921 131.583 89.976  1.00 100.47 ? 1250 ARG A CZ  1 
ATOM   9750  N  NH1 . ARG A 1 1250 ? 115.199 130.374 90.443  1.00 98.18  ? 1250 ARG A NH1 1 
ATOM   9751  N  NH2 . ARG A 1 1250 ? 115.009 132.635 90.777  1.00 100.66 ? 1250 ARG A NH2 1 
ATOM   9752  N  N   . LEU A 1 1251 ? 114.846 137.947 85.807  1.00 96.25  ? 1251 LEU A N   1 
ATOM   9753  C  CA  . LEU A 1 1251 ? 114.517 138.743 84.631  1.00 96.61  ? 1251 LEU A CA  1 
ATOM   9754  C  C   . LEU A 1 1251 ? 115.574 139.811 84.371  1.00 107.65 ? 1251 LEU A C   1 
ATOM   9755  O  O   . LEU A 1 1251 ? 115.857 140.121 83.208  1.00 112.17 ? 1251 LEU A O   1 
ATOM   9756  C  CB  . LEU A 1 1251 ? 113.119 139.351 84.771  1.00 97.54  ? 1251 LEU A CB  1 
ATOM   9757  C  CG  . LEU A 1 1251 ? 112.535 140.008 83.512  1.00 89.53  ? 1251 LEU A CG  1 
ATOM   9758  C  CD1 . LEU A 1 1251 ? 111.022 139.952 83.561  1.00 93.62  ? 1251 LEU A CD1 1 
ATOM   9759  C  CD2 . LEU A 1 1251 ? 112.982 141.459 83.337  1.00 114.88 ? 1251 LEU A CD2 1 
ATOM   9760  N  N   . LEU A 1 1252 ? 116.176 140.375 85.424  1.00 110.05 ? 1252 LEU A N   1 
ATOM   9761  C  CA  . LEU A 1 1252 ? 117.282 141.303 85.214  1.00 115.47 ? 1252 LEU A CA  1 
ATOM   9762  C  C   . LEU A 1 1252 ? 118.465 140.588 84.589  1.00 110.11 ? 1252 LEU A C   1 
ATOM   9763  O  O   . LEU A 1 1252 ? 119.146 141.136 83.715  1.00 114.34 ? 1252 LEU A O   1 
ATOM   9764  C  CB  . LEU A 1 1252 ? 117.700 141.953 86.533  1.00 120.13 ? 1252 LEU A CB  1 
ATOM   9765  C  CG  . LEU A 1 1252 ? 116.839 143.081 87.096  1.00 130.74 ? 1252 LEU A CG  1 
ATOM   9766  C  CD1 . LEU A 1 1252 ? 117.644 143.878 88.113  1.00 126.98 ? 1252 LEU A CD1 1 
ATOM   9767  C  CD2 . LEU A 1 1252 ? 116.328 143.981 85.983  1.00 136.22 ? 1252 LEU A CD2 1 
ATOM   9768  N  N   . TRP A 1 1253 ? 118.722 139.357 85.021  1.00 113.51 ? 1253 TRP A N   1 
ATOM   9769  C  CA  . TRP A 1 1253 ? 119.909 138.670 84.545  1.00 125.32 ? 1253 TRP A CA  1 
ATOM   9770  C  C   . TRP A 1 1253 ? 119.752 138.246 83.084  1.00 122.54 ? 1253 TRP A C   1 
ATOM   9771  O  O   . TRP A 1 1253 ? 120.747 138.158 82.358  1.00 130.76 ? 1253 TRP A O   1 
ATOM   9772  C  CB  . TRP A 1 1253 ? 120.179 137.459 85.434  1.00 140.73 ? 1253 TRP A CB  1 
ATOM   9773  C  CG  . TRP A 1 1253 ? 121.457 136.790 85.128  1.00 148.80 ? 1253 TRP A CG  1 
ATOM   9774  C  CD1 . TRP A 1 1253 ? 122.703 137.213 85.476  1.00 152.89 ? 1253 TRP A CD1 1 
ATOM   9775  C  CD2 . TRP A 1 1253 ? 121.635 135.611 84.342  1.00 146.95 ? 1253 TRP A CD2 1 
ATOM   9776  N  NE1 . TRP A 1 1253 ? 123.649 136.352 84.983  1.00 157.90 ? 1253 TRP A NE1 1 
ATOM   9777  C  CE2 . TRP A 1 1253 ? 123.018 135.361 84.278  1.00 155.29 ? 1253 TRP A CE2 1 
ATOM   9778  C  CE3 . TRP A 1 1253 ? 120.760 134.736 83.696  1.00 146.52 ? 1253 TRP A CE3 1 
ATOM   9779  C  CZ2 . TRP A 1 1253 ? 123.544 134.276 83.593  1.00 161.68 ? 1253 TRP A CZ2 1 
ATOM   9780  C  CZ3 . TRP A 1 1253 ? 121.284 133.660 83.019  1.00 154.54 ? 1253 TRP A CZ3 1 
ATOM   9781  C  CH2 . TRP A 1 1253 ? 122.663 133.435 82.975  1.00 163.53 ? 1253 TRP A CH2 1 
ATOM   9782  N  N   . VAL A 1 1254 ? 118.519 137.965 82.644  1.00 113.19 ? 1254 VAL A N   1 
ATOM   9783  C  CA  . VAL A 1 1254 ? 118.283 137.515 81.270  1.00 108.50 ? 1254 VAL A CA  1 
ATOM   9784  C  C   . VAL A 1 1254 ? 118.360 138.656 80.253  1.00 115.46 ? 1254 VAL A C   1 
ATOM   9785  O  O   . VAL A 1 1254 ? 118.889 138.488 79.151  1.00 120.74 ? 1254 VAL A O   1 
ATOM   9786  C  CB  . VAL A 1 1254 ? 116.927 136.794 81.171  1.00 104.68 ? 1254 VAL A CB  1 
ATOM   9787  C  CG1 . VAL A 1 1254 ? 116.600 136.485 79.729  1.00 96.24  ? 1254 VAL A CG1 1 
ATOM   9788  C  CG2 . VAL A 1 1254 ? 117.003 135.495 81.883  1.00 116.94 ? 1254 VAL A CG2 1 
ATOM   9789  N  N   . THR A 1 1255 ? 117.859 139.843 80.588  1.00 122.62 ? 1255 THR A N   1 
ATOM   9790  C  CA  . THR A 1 1255 ? 117.772 140.883 79.578  1.00 123.01 ? 1255 THR A CA  1 
ATOM   9791  C  C   . THR A 1 1255 ? 119.097 141.655 79.487  1.00 134.80 ? 1255 THR A C   1 
ATOM   9792  O  O   . THR A 1 1255 ? 120.052 141.392 80.220  1.00 133.01 ? 1255 THR A O   1 
ATOM   9793  C  CB  . THR A 1 1255 ? 116.574 141.780 79.897  1.00 116.13 ? 1255 THR A CB  1 
ATOM   9794  O  OG1 . THR A 1 1255 ? 115.455 140.934 80.182  1.00 111.19 ? 1255 THR A OG1 1 
ATOM   9795  C  CG2 . THR A 1 1255 ? 116.158 142.543 78.657  1.00 124.90 ? 1255 THR A CG2 1 
ATOM   9796  N  N   . GLN A 1 1256 ? 119.163 142.613 78.560  1.00 141.65 ? 1256 GLN A N   1 
ATOM   9797  C  CA  . GLN A 1 1256 ? 120.360 143.405 78.333  1.00 153.24 ? 1256 GLN A CA  1 
ATOM   9798  C  C   . GLN A 1 1256 ? 120.352 144.653 79.200  1.00 157.17 ? 1256 GLN A C   1 
ATOM   9799  O  O   . GLN A 1 1256 ? 119.299 145.153 79.600  1.00 154.06 ? 1256 GLN A O   1 
ATOM   9800  C  CB  . GLN A 1 1256 ? 120.453 143.818 76.864  1.00 151.93 ? 1256 GLN A CB  1 
ATOM   9801  C  CG  . GLN A 1 1256 ? 121.842 144.221 76.401  1.00 158.53 ? 1256 GLN A CG  1 
ATOM   9802  C  CD  . GLN A 1 1256 ? 121.944 144.299 74.894  1.00 159.09 ? 1256 GLN A CD  1 
ATOM   9803  O  OE1 . GLN A 1 1256 ? 120.935 144.405 74.198  1.00 153.76 ? 1256 GLN A OE1 1 
ATOM   9804  N  NE2 . GLN A 1 1256 ? 123.168 144.258 74.380  1.00 159.44 ? 1256 GLN A NE2 1 
ATOM   9805  N  N   . GLY A 1 1257 ? 121.557 145.150 79.481  1.00 160.90 ? 1257 GLY A N   1 
ATOM   9806  C  CA  . GLY A 1 1257 ? 121.690 146.348 80.289  1.00 162.97 ? 1257 GLY A CA  1 
ATOM   9807  C  C   . GLY A 1 1257 ? 121.102 147.579 79.629  1.00 169.25 ? 1257 GLY A C   1 
ATOM   9808  O  O   . GLY A 1 1257 ? 120.409 148.369 80.275  1.00 161.63 ? 1257 GLY A O   1 
ATOM   9809  N  N   . THR A 1 1258 ? 121.359 147.754 78.332  1.00 179.10 ? 1258 THR A N   1 
ATOM   9810  C  CA  . THR A 1 1258 ? 120.815 148.896 77.598  1.00 181.12 ? 1258 THR A CA  1 
ATOM   9811  C  C   . THR A 1 1258 ? 119.430 148.544 77.067  1.00 174.74 ? 1258 THR A C   1 
ATOM   9812  O  O   . THR A 1 1258 ? 119.229 148.235 75.891  1.00 171.25 ? 1258 THR A O   1 
ATOM   9813  C  CB  . THR A 1 1258 ? 121.753 149.301 76.469  1.00 180.04 ? 1258 THR A CB  1 
ATOM   9814  O  OG1 . THR A 1 1258 ? 121.889 148.212 75.548  1.00 169.51 ? 1258 THR A OG1 1 
ATOM   9815  C  CG2 . THR A 1 1258 ? 123.126 149.657 77.021  1.00 178.14 ? 1258 THR A CG2 1 
ATOM   9816  N  N   . ALA A 1 1259 ? 118.458 148.597 77.970  1.00 169.66 ? 1259 ALA A N   1 
ATOM   9817  C  CA  . ALA A 1 1259 ? 117.072 148.295 77.657  1.00 173.60 ? 1259 ALA A CA  1 
ATOM   9818  C  C   . ALA A 1 1259 ? 116.210 149.175 78.551  1.00 176.07 ? 1259 ALA A C   1 
ATOM   9819  O  O   . ALA A 1 1259 ? 116.707 150.102 79.199  1.00 167.92 ? 1259 ALA A O   1 
ATOM   9820  C  CB  . ALA A 1 1259 ? 116.779 146.801 77.841  1.00 155.94 ? 1259 ALA A CB  1 
ATOM   9821  N  N   . ASP A 1 1260 ? 114.911 148.890 78.599  1.00 172.41 ? 1260 ASP A N   1 
ATOM   9822  C  CA  . ASP A 1 1260 ? 114.047 149.745 79.397  1.00 167.30 ? 1260 ASP A CA  1 
ATOM   9823  C  C   . ASP A 1 1260 ? 113.315 148.861 80.402  1.00 160.41 ? 1260 ASP A C   1 
ATOM   9824  O  O   . ASP A 1 1260 ? 112.082 148.864 80.494  1.00 156.23 ? 1260 ASP A O   1 
ATOM   9825  C  CB  . ASP A 1 1260 ? 113.110 150.553 78.507  1.00 164.97 ? 1260 ASP A CB  1 
ATOM   9826  C  CG  . ASP A 1 1260 ? 112.454 151.684 79.250  1.00 167.01 ? 1260 ASP A CG  1 
ATOM   9827  O  OD1 . ASP A 1 1260 ? 112.704 151.827 80.466  1.00 165.31 ? 1260 ASP A OD1 1 
ATOM   9828  O  OD2 . ASP A 1 1260 ? 111.709 152.457 78.614  1.00 168.20 ? 1260 ASP A OD2 1 
ATOM   9829  N  N   . ARG A 1 1261 ? 114.116 148.095 81.143  1.00 157.27 ? 1261 ARG A N   1 
ATOM   9830  C  CA  . ARG A 1 1261 ? 113.676 147.010 82.018  1.00 156.93 ? 1261 ARG A CA  1 
ATOM   9831  C  C   . ARG A 1 1261 ? 112.534 147.373 82.965  1.00 156.98 ? 1261 ARG A C   1 
ATOM   9832  O  O   . ARG A 1 1261 ? 111.679 146.526 83.259  1.00 141.17 ? 1261 ARG A O   1 
ATOM   9833  C  CB  . ARG A 1 1261 ? 114.873 146.512 82.829  1.00 160.04 ? 1261 ARG A CB  1 
ATOM   9834  C  CG  . ARG A 1 1261 ? 115.960 145.845 81.998  1.00 144.16 ? 1261 ARG A CG  1 
ATOM   9835  C  CD  . ARG A 1 1261 ? 117.173 145.543 82.861  1.00 138.99 ? 1261 ARG A CD  1 
ATOM   9836  N  NE  . ARG A 1 1261 ? 118.199 144.775 82.162  1.00 146.52 ? 1261 ARG A NE  1 
ATOM   9837  C  CZ  . ARG A 1 1261 ? 119.355 144.416 82.711  1.00 146.91 ? 1261 ARG A CZ  1 
ATOM   9838  N  NH1 . ARG A 1 1261 ? 119.629 144.761 83.961  1.00 144.09 ? 1261 ARG A NH1 1 
ATOM   9839  N  NH2 . ARG A 1 1261 ? 120.237 143.713 82.018  1.00 136.46 ? 1261 ARG A NH2 1 
ATOM   9840  N  N   . GLU A 1 1262 ? 112.503 148.614 83.457  1.00 161.00 ? 1262 GLU A N   1 
ATOM   9841  C  CA  . GLU A 1 1262 ? 111.531 148.989 84.482  1.00 154.45 ? 1262 GLU A CA  1 
ATOM   9842  C  C   . GLU A 1 1262 ? 110.081 148.813 84.030  1.00 140.24 ? 1262 GLU A C   1 
ATOM   9843  O  O   . GLU A 1 1262 ? 109.263 148.265 84.783  1.00 136.02 ? 1262 GLU A O   1 
ATOM   9844  C  CB  . GLU A 1 1262 ? 111.796 150.432 84.913  1.00 153.15 ? 1262 GLU A CB  1 
ATOM   9845  C  CG  . GLU A 1 1262 ? 110.803 150.979 85.909  1.00 158.60 ? 1262 GLU A CG  1 
ATOM   9846  C  CD  . GLU A 1 1262 ? 111.214 152.326 86.460  1.00 165.33 ? 1262 GLU A CD  1 
ATOM   9847  O  OE1 . GLU A 1 1262 ? 112.173 152.920 85.924  1.00 167.89 ? 1262 GLU A OE1 1 
ATOM   9848  O  OE2 . GLU A 1 1262 ? 110.584 152.786 87.434  1.00 162.18 ? 1262 GLU A OE2 1 
ATOM   9849  N  N   . LYS A 1 1263 ? 109.726 149.258 82.815  1.00 140.16 ? 1263 LYS A N   1 
ATOM   9850  C  CA  . LYS A 1 1263 ? 108.322 149.100 82.423  1.00 145.71 ? 1263 LYS A CA  1 
ATOM   9851  C  C   . LYS A 1 1263 ? 107.942 147.637 82.286  1.00 144.39 ? 1263 LYS A C   1 
ATOM   9852  O  O   . LYS A 1 1263 ? 106.754 147.308 82.345  1.00 138.81 ? 1263 LYS A O   1 
ATOM   9853  C  CB  . LYS A 1 1263 ? 107.914 149.854 81.151  1.00 154.80 ? 1263 LYS A CB  1 
ATOM   9854  C  CG  . LYS A 1 1263 ? 108.534 149.438 79.847  1.00 153.28 ? 1263 LYS A CG  1 
ATOM   9855  C  CD  . LYS A 1 1263 ? 107.979 150.345 78.743  1.00 159.43 ? 1263 LYS A CD  1 
ATOM   9856  C  CE  . LYS A 1 1263 ? 108.303 151.814 78.921  1.00 170.84 ? 1263 LYS A CE  1 
ATOM   9857  N  NZ  . LYS A 1 1263 ? 109.679 152.103 79.302  1.00 174.49 ? 1263 LYS A NZ  1 
ATOM   9858  N  N   . LEU A 1 1264 ? 108.921 146.761 82.091  1.00 137.93 ? 1264 LEU A N   1 
ATOM   9859  C  CA  . LEU A 1 1264 ? 108.631 145.339 82.074  1.00 132.32 ? 1264 LEU A CA  1 
ATOM   9860  C  C   . LEU A 1 1264 ? 108.481 144.812 83.492  1.00 128.96 ? 1264 LEU A C   1 
ATOM   9861  O  O   . LEU A 1 1264 ? 107.681 143.899 83.730  1.00 120.39 ? 1264 LEU A O   1 
ATOM   9862  C  CB  . LEU A 1 1264 ? 109.752 144.582 81.362  1.00 126.11 ? 1264 LEU A CB  1 
ATOM   9863  C  CG  . LEU A 1 1264 ? 110.150 145.070 79.970  1.00 131.17 ? 1264 LEU A CG  1 
ATOM   9864  C  CD1 . LEU A 1 1264 ? 111.375 144.311 79.477  1.00 126.11 ? 1264 LEU A CD1 1 
ATOM   9865  C  CD2 . LEU A 1 1264 ? 108.991 144.939 78.996  1.00 140.71 ? 1264 LEU A CD2 1 
ATOM   9866  N  N   . LEU A 1 1265 ? 109.231 145.377 84.442  1.00 131.90 ? 1265 LEU A N   1 
ATOM   9867  C  CA  . LEU A 1 1265 ? 109.185 144.888 85.817  1.00 123.30 ? 1265 LEU A CA  1 
ATOM   9868  C  C   . LEU A 1 1265 ? 107.942 145.321 86.598  1.00 118.83 ? 1265 LEU A C   1 
ATOM   9869  O  O   . LEU A 1 1265 ? 107.462 144.541 87.429  1.00 111.29 ? 1265 LEU A O   1 
ATOM   9870  C  CB  . LEU A 1 1265 ? 110.443 145.317 86.571  1.00 134.13 ? 1265 LEU A CB  1 
ATOM   9871  C  CG  . LEU A 1 1265 ? 111.680 144.476 86.260  1.00 138.83 ? 1265 LEU A CG  1 
ATOM   9872  C  CD1 . LEU A 1 1265 ? 112.735 144.673 87.333  1.00 144.95 ? 1265 LEU A CD1 1 
ATOM   9873  C  CD2 . LEU A 1 1265 ? 111.293 143.007 86.153  1.00 117.83 ? 1265 LEU A CD2 1 
ATOM   9874  N  N   . ILE A 1 1266 ? 107.398 146.530 86.379  1.00 122.61 ? 1266 ILE A N   1 
ATOM   9875  C  CA  . ILE A 1 1266 ? 106.266 146.995 87.213  1.00 112.51 ? 1266 ILE A CA  1 
ATOM   9876  C  C   . ILE A 1 1266 ? 105.049 146.066 87.171  1.00 106.28 ? 1266 ILE A C   1 
ATOM   9877  O  O   . ILE A 1 1266 ? 104.529 145.715 88.240  1.00 107.30 ? 1266 ILE A O   1 
ATOM   9878  C  CB  . ILE A 1 1266 ? 105.878 148.435 86.912  1.00 120.74 ? 1266 ILE A CB  1 
ATOM   9879  C  CG1 . ILE A 1 1266 ? 106.970 149.480 87.156  1.00 132.42 ? 1266 ILE A CG1 1 
ATOM   9880  C  CG2 . ILE A 1 1266 ? 104.640 148.840 87.706  1.00 121.74 ? 1266 ILE A CG2 1 
ATOM   9881  C  CD1 . ILE A 1 1266 ? 107.488 150.099 85.923  1.00 137.06 ? 1266 ILE A CD1 1 
ATOM   9882  N  N   . PRO A 1 1267 ? 104.534 145.661 86.000  1.00 107.03 ? 1267 PRO A N   1 
ATOM   9883  C  CA  . PRO A 1 1267 ? 103.326 144.812 86.010  1.00 101.22 ? 1267 PRO A CA  1 
ATOM   9884  C  C   . PRO A 1 1267 ? 103.478 143.499 86.758  1.00 104.81 ? 1267 PRO A C   1 
ATOM   9885  O  O   . PRO A 1 1267 ? 102.512 143.050 87.388  1.00 105.44 ? 1267 PRO A O   1 
ATOM   9886  C  CB  . PRO A 1 1267 ? 103.049 144.579 84.515  1.00 92.14  ? 1267 PRO A CB  1 
ATOM   9887  C  CG  . PRO A 1 1267 ? 104.343 144.858 83.832  1.00 113.40 ? 1267 PRO A CG  1 
ATOM   9888  C  CD  . PRO A 1 1267 ? 104.965 145.961 84.624  1.00 116.48 ? 1267 PRO A CD  1 
ATOM   9889  N  N   . LEU A 1 1268 ? 104.650 142.867 86.721  1.00 108.82 ? 1268 LEU A N   1 
ATOM   9890  C  CA  . LEU A 1 1268 ? 104.829 141.635 87.484  1.00 107.10 ? 1268 LEU A CA  1 
ATOM   9891  C  C   . LEU A 1 1268 ? 104.937 141.911 88.979  1.00 102.94 ? 1268 LEU A C   1 
ATOM   9892  O  O   . LEU A 1 1268 ? 104.316 141.212 89.789  1.00 100.78 ? 1268 LEU A O   1 
ATOM   9893  C  CB  . LEU A 1 1268 ? 106.062 140.881 86.992  1.00 101.43 ? 1268 LEU A CB  1 
ATOM   9894  C  CG  . LEU A 1 1268 ? 105.925 140.278 85.596  1.00 110.88 ? 1268 LEU A CG  1 
ATOM   9895  C  CD1 . LEU A 1 1268 ? 107.229 139.623 85.171  1.00 106.58 ? 1268 LEU A CD1 1 
ATOM   9896  C  CD2 . LEU A 1 1268 ? 104.779 139.276 85.582  1.00 95.36  ? 1268 LEU A CD2 1 
ATOM   9897  N  N   . LEU A 1 1269 ? 105.706 142.929 89.364  1.00 108.64 ? 1269 LEU A N   1 
ATOM   9898  C  CA  . LEU A 1 1269 ? 105.961 143.164 90.782  1.00 105.93 ? 1269 LEU A CA  1 
ATOM   9899  C  C   . LEU A 1 1269 ? 104.743 143.730 91.506  1.00 107.58 ? 1269 LEU A C   1 
ATOM   9900  O  O   . LEU A 1 1269 ? 104.568 143.471 92.702  1.00 109.22 ? 1269 LEU A O   1 
ATOM   9901  C  CB  . LEU A 1 1269 ? 107.180 144.076 90.943  1.00 107.25 ? 1269 LEU A CB  1 
ATOM   9902  C  CG  . LEU A 1 1269 ? 107.748 144.317 92.344  1.00 105.85 ? 1269 LEU A CG  1 
ATOM   9903  C  CD1 . LEU A 1 1269 ? 109.223 144.628 92.239  1.00 109.92 ? 1269 LEU A CD1 1 
ATOM   9904  C  CD2 . LEU A 1 1269 ? 107.042 145.477 93.035  1.00 125.59 ? 1269 LEU A CD2 1 
ATOM   9905  N  N   . ASN A 1 1270 ? 103.890 144.493 90.818  1.00 106.73 ? 1270 ASN A N   1 
ATOM   9906  C  CA  . ASN A 1 1270 ? 102.721 145.055 91.490  1.00 110.33 ? 1270 ASN A CA  1 
ATOM   9907  C  C   . ASN A 1 1270 ? 101.718 144.002 91.945  1.00 115.70 ? 1270 ASN A C   1 
ATOM   9908  O  O   . ASN A 1 1270 ? 100.839 144.323 92.753  1.00 115.80 ? 1270 ASN A O   1 
ATOM   9909  C  CB  . ASN A 1 1270 ? 102.010 146.068 90.589  1.00 112.17 ? 1270 ASN A CB  1 
ATOM   9910  C  CG  . ASN A 1 1270 ? 102.633 147.446 90.661  1.00 125.90 ? 1270 ASN A CG  1 
ATOM   9911  O  OD1 . ASN A 1 1270 ? 103.492 147.707 91.503  1.00 127.41 ? 1270 ASN A OD1 1 
ATOM   9912  N  ND2 . ASN A 1 1270 ? 102.175 148.347 89.801  1.00 127.58 ? 1270 ASN A ND2 1 
ATOM   9913  N  N   . SER A 1 1271 ? 101.822 142.768 91.459  1.00 103.64 ? 1271 SER A N   1 
ATOM   9914  C  CA  . SER A 1 1271 ? 100.870 141.726 91.813  1.00 92.05  ? 1271 SER A CA  1 
ATOM   9915  C  C   . SER A 1 1271 ? 101.250 140.963 93.074  1.00 96.92  ? 1271 SER A C   1 
ATOM   9916  O  O   . SER A 1 1271 ? 100.458 140.136 93.539  1.00 102.26 ? 1271 SER A O   1 
ATOM   9917  C  CB  . SER A 1 1271 ? 100.726 140.730 90.657  1.00 93.60  ? 1271 SER A CB  1 
ATOM   9918  O  OG  . SER A 1 1271 ? 101.992 140.229 90.260  1.00 92.78  ? 1271 SER A OG  1 
ATOM   9919  N  N   . ARG A 1 1272 ? 102.425 141.221 93.644  1.00 101.22 ? 1272 ARG A N   1 
ATOM   9920  C  CA  . ARG A 1 1272 ? 102.891 140.461 94.797  1.00 95.10  ? 1272 ARG A CA  1 
ATOM   9921  C  C   . ARG A 1 1272 ? 103.125 141.324 96.026  1.00 98.18  ? 1272 ARG A C   1 
ATOM   9922  O  O   . ARG A 1 1272 ? 102.660 140.974 97.118  1.00 105.31 ? 1272 ARG A O   1 
ATOM   9923  C  CB  . ARG A 1 1272 ? 104.179 139.715 94.417  1.00 96.00  ? 1272 ARG A CB  1 
ATOM   9924  C  CG  . ARG A 1 1272 ? 103.992 138.761 93.244  1.00 99.71  ? 1272 ARG A CG  1 
ATOM   9925  C  CD  . ARG A 1 1272 ? 103.069 137.604 93.588  1.00 80.52  ? 1272 ARG A CD  1 
ATOM   9926  N  NE  . ARG A 1 1272 ? 103.789 136.529 94.261  1.00 79.65  ? 1272 ARG A NE  1 
ATOM   9927  C  CZ  . ARG A 1 1272 ? 103.245 135.691 95.139  1.00 89.58  ? 1272 ARG A CZ  1 
ATOM   9928  N  NH1 . ARG A 1 1272 ? 101.967 135.802 95.468  1.00 97.07  ? 1272 ARG A NH1 1 
ATOM   9929  N  NH2 . ARG A 1 1272 ? 103.987 134.744 95.694  1.00 101.48 ? 1272 ARG A NH2 1 
ATOM   9930  N  N   . VAL A 1 1273 ? 103.829 142.446 95.886  1.00 101.37 ? 1273 VAL A N   1 
ATOM   9931  C  CA  . VAL A 1 1273 ? 104.226 143.278 97.009  1.00 111.46 ? 1273 VAL A CA  1 
ATOM   9932  C  C   . VAL A 1 1273 ? 103.836 144.723 96.713  1.00 116.68 ? 1273 VAL A C   1 
ATOM   9933  O  O   . VAL A 1 1273 ? 103.355 145.051 95.630  1.00 116.70 ? 1273 VAL A O   1 
ATOM   9934  C  CB  . VAL A 1 1273 ? 105.733 143.163 97.323  1.00 118.16 ? 1273 VAL A CB  1 
ATOM   9935  C  CG1 . VAL A 1 1273 ? 106.105 141.726 97.673  1.00 115.07 ? 1273 VAL A CG1 1 
ATOM   9936  C  CG2 . VAL A 1 1273 ? 106.564 143.668 96.153  1.00 122.36 ? 1273 VAL A CG2 1 
ATOM   9937  N  N   . ASN A 1 1274 ? 104.056 145.589 97.700  1.00 116.87 ? 1274 ASN A N   1 
ATOM   9938  C  CA  . ASN A 1 1274 ? 103.677 146.992 97.628  1.00 118.20 ? 1274 ASN A CA  1 
ATOM   9939  C  C   . ASN A 1 1274 ? 104.864 147.918 97.386  1.00 123.18 ? 1274 ASN A C   1 
ATOM   9940  O  O   . ASN A 1 1274 ? 104.674 149.136 97.301  1.00 123.26 ? 1274 ASN A O   1 
ATOM   9941  C  CB  . ASN A 1 1274 ? 102.954 147.393 98.921  1.00 111.73 ? 1274 ASN A CB  1 
ATOM   9942  C  CG  . ASN A 1 1274 ? 102.011 148.565 98.730  1.00 117.65 ? 1274 ASN A CG  1 
ATOM   9943  O  OD1 . ASN A 1 1274 ? 102.011 149.219 97.688  1.00 118.82 ? 1274 ASN A OD1 1 
ATOM   9944  N  ND2 . ASN A 1 1274 ? 101.191 148.833 99.740  1.00 122.31 ? 1274 ASN A ND2 1 
ATOM   9945  N  N   . LEU A 1 1275 ? 106.076 147.379 97.276  1.00 120.24 ? 1275 LEU A N   1 
ATOM   9946  C  CA  . LEU A 1 1275 ? 107.237 148.221 97.043  1.00 132.70 ? 1275 LEU A CA  1 
ATOM   9947  C  C   . LEU A 1 1275 ? 107.239 148.868 95.660  1.00 140.34 ? 1275 LEU A C   1 
ATOM   9948  O  O   . LEU A 1 1275 ? 106.659 148.352 94.703  1.00 132.36 ? 1275 LEU A O   1 
ATOM   9949  C  CB  . LEU A 1 1275 ? 108.553 147.468 97.233  1.00 131.50 ? 1275 LEU A CB  1 
ATOM   9950  C  CG  . LEU A 1 1275 ? 108.753 147.044 98.682  1.00 137.18 ? 1275 LEU A CG  1 
ATOM   9951  C  CD1 . LEU A 1 1275 ? 110.159 146.467 98.905  1.00 132.79 ? 1275 LEU A CD1 1 
ATOM   9952  C  CD2 . LEU A 1 1275 ? 108.339 148.124 99.642  1.00 137.00 ? 1275 LEU A CD2 1 
ATOM   9953  N  N   . ASP A 1 1276 ? 107.892 150.030 95.578  1.00 149.71 ? 1276 ASP A N   1 
ATOM   9954  C  CA  . ASP A 1 1276 ? 108.222 150.624 94.291  1.00 155.98 ? 1276 ASP A CA  1 
ATOM   9955  C  C   . ASP A 1 1276 ? 109.424 149.911 93.668  1.00 166.82 ? 1276 ASP A C   1 
ATOM   9956  O  O   . ASP A 1 1276 ? 110.049 149.036 94.273  1.00 156.77 ? 1276 ASP A O   1 
ATOM   9957  C  CB  . ASP A 1 1276 ? 108.498 152.122 94.439  1.00 160.43 ? 1276 ASP A CB  1 
ATOM   9958  C  CG  . ASP A 1 1276 ? 109.674 152.420 95.355  1.00 166.57 ? 1276 ASP A CG  1 
ATOM   9959  O  OD1 . ASP A 1 1276 ? 110.211 151.477 95.969  1.00 159.29 ? 1276 ASP A OD1 1 
ATOM   9960  O  OD2 . ASP A 1 1276 ? 110.075 153.600 95.450  1.00 163.36 ? 1276 ASP A OD2 1 
ATOM   9961  N  N   . TYR A 1 1277 ? 109.749 150.308 92.433  1.00 167.27 ? 1277 TYR A N   1 
ATOM   9962  C  CA  . TYR A 1 1277 ? 110.809 149.637 91.684  1.00 169.40 ? 1277 TYR A CA  1 
ATOM   9963  C  C   . TYR A 1 1277 ? 112.188 149.833 92.307  1.00 166.20 ? 1277 TYR A C   1 
ATOM   9964  O  O   . TYR A 1 1277 ? 112.954 148.872 92.451  1.00 161.25 ? 1277 TYR A O   1 
ATOM   9965  C  CB  . TYR A 1 1277 ? 110.808 150.155 90.248  1.00 174.14 ? 1277 TYR A CB  1 
ATOM   9966  C  CG  . TYR A 1 1277 ? 112.004 149.729 89.431  1.00 180.96 ? 1277 TYR A CG  1 
ATOM   9967  C  CD1 . TYR A 1 1277 ? 112.325 148.390 89.266  1.00 166.82 ? 1277 TYR A CD1 1 
ATOM   9968  C  CD2 . TYR A 1 1277 ? 112.821 150.677 88.826  1.00 175.43 ? 1277 TYR A CD2 1 
ATOM   9969  C  CE1 . TYR A 1 1277 ? 113.424 148.007 88.517  1.00 166.46 ? 1277 TYR A CE1 1 
ATOM   9970  C  CE2 . TYR A 1 1277 ? 113.918 150.304 88.074  1.00 172.61 ? 1277 TYR A CE2 1 
ATOM   9971  C  CZ  . TYR A 1 1277 ? 114.217 148.968 87.924  1.00 173.09 ? 1277 TYR A CZ  1 
ATOM   9972  O  OH  . TYR A 1 1277 ? 115.309 148.591 87.177  1.00 159.80 ? 1277 TYR A OH  1 
ATOM   9973  N  N   . GLN A 1 1278 ? 112.521 151.067 92.685  1.00 162.60 ? 1278 GLN A N   1 
ATOM   9974  C  CA  . GLN A 1 1278 ? 113.903 151.371 93.054  1.00 164.67 ? 1278 GLN A CA  1 
ATOM   9975  C  C   . GLN A 1 1278 ? 114.314 150.697 94.352  1.00 160.14 ? 1278 GLN A C   1 
ATOM   9976  O  O   . GLN A 1 1278 ? 115.449 150.219 94.478  1.00 152.89 ? 1278 GLN A O   1 
ATOM   9977  C  CB  . GLN A 1 1278 ? 114.122 152.874 93.155  1.00 172.48 ? 1278 GLN A CB  1 
ATOM   9978  C  CG  . GLN A 1 1278 ? 115.572 153.208 93.460  1.00 182.69 ? 1278 GLN A CG  1 
ATOM   9979  C  CD  . GLN A 1 1278 ? 116.502 152.722 92.367  1.00 173.17 ? 1278 GLN A CD  1 
ATOM   9980  O  OE1 . GLN A 1 1278 ? 117.206 151.727 92.530  1.00 158.33 ? 1278 GLN A OE1 1 
ATOM   9981  N  NE2 . GLN A 1 1278 ? 116.501 153.422 91.236  1.00 171.79 ? 1278 GLN A NE2 1 
ATOM   9982  N  N   . THR A 1 1279 ? 113.406 150.638 95.322  1.00 155.28 ? 1279 THR A N   1 
ATOM   9983  C  CA  . THR A 1 1279 ? 113.743 150.067 96.618  1.00 158.33 ? 1279 THR A CA  1 
ATOM   9984  C  C   . THR A 1 1279 ? 114.129 148.593 96.495  1.00 154.18 ? 1279 THR A C   1 
ATOM   9985  O  O   . THR A 1 1279 ? 115.001 148.117 97.242  1.00 155.71 ? 1279 THR A O   1 
ATOM   9986  C  CB  . THR A 1 1279 ? 112.563 150.241 97.571  1.00 151.70 ? 1279 THR A CB  1 
ATOM   9987  O  OG1 . THR A 1 1279 ? 112.171 151.624 97.605  1.00 149.02 ? 1279 THR A OG1 1 
ATOM   9988  C  CG2 . THR A 1 1279 ? 112.983 149.860 98.955  1.00 147.96 ? 1279 THR A CG2 1 
ATOM   9989  N  N   . VAL A 1 1280 ? 113.522 147.879 95.552  1.00 147.90 ? 1280 VAL A N   1 
ATOM   9990  C  CA  . VAL A 1 1280 ? 113.753 146.440 95.389  1.00 147.73 ? 1280 VAL A CA  1 
ATOM   9991  C  C   . VAL A 1 1280 ? 115.208 146.152 95.033  1.00 158.75 ? 1280 VAL A C   1 
ATOM   9992  O  O   . VAL A 1 1280 ? 115.810 145.202 95.542  1.00 161.69 ? 1280 VAL A O   1 
ATOM   9993  C  CB  . VAL A 1 1280 ? 112.784 145.873 94.334  1.00 132.88 ? 1280 VAL A CB  1 
ATOM   9994  C  CG1 . VAL A 1 1280 ? 113.298 144.551 93.782  1.00 128.03 ? 1280 VAL A CG1 1 
ATOM   9995  C  CG2 . VAL A 1 1280 ? 111.396 145.701 94.934  1.00 129.51 ? 1280 VAL A CG2 1 
ATOM   9996  N  N   . LEU A 1 1281 ? 115.798 146.977 94.158  1.00 156.97 ? 1281 LEU A N   1 
ATOM   9997  C  CA  . LEU A 1 1281 ? 117.161 146.735 93.689  1.00 159.99 ? 1281 LEU A CA  1 
ATOM   9998  C  C   . LEU A 1 1281 ? 118.174 146.698 94.823  1.00 161.55 ? 1281 LEU A C   1 
ATOM   9999  O  O   . LEU A 1 1281 ? 119.262 146.136 94.654  1.00 159.29 ? 1281 LEU A O   1 
ATOM   10000 C  CB  . LEU A 1 1281 ? 117.566 147.828 92.698  1.00 164.03 ? 1281 LEU A CB  1 
ATOM   10001 C  CG  . LEU A 1 1281 ? 116.668 148.052 91.484  1.00 163.34 ? 1281 LEU A CG  1 
ATOM   10002 C  CD1 . LEU A 1 1281 ? 117.363 148.954 90.478  1.00 155.27 ? 1281 LEU A CD1 1 
ATOM   10003 C  CD2 . LEU A 1 1281 ? 116.289 146.726 90.845  1.00 152.51 ? 1281 LEU A CD2 1 
ATOM   10004 N  N   . ASN A 1 1282 ? 117.833 147.272 95.973  1.00 160.39 ? 1282 ASN A N   1 
ATOM   10005 C  CA  . ASN A 1 1282 ? 118.717 147.315 97.128  1.00 165.62 ? 1282 ASN A CA  1 
ATOM   10006 C  C   . ASN A 1 1282 ? 118.942 145.947 97.760  1.00 166.51 ? 1282 ASN A C   1 
ATOM   10007 O  O   . ASN A 1 1282 ? 119.843 145.813 98.593  1.00 170.92 ? 1282 ASN A O   1 
ATOM   10008 C  CB  . ASN A 1 1282 ? 118.142 148.278 98.168  1.00 163.75 ? 1282 ASN A CB  1 
ATOM   10009 C  CG  . ASN A 1 1282 ? 118.173 149.720 97.702  1.00 160.41 ? 1282 ASN A CG  1 
ATOM   10010 O  OD1 . ASN A 1 1282 ? 117.426 150.111 96.804  1.00 150.13 ? 1282 ASN A OD1 1 
ATOM   10011 N  ND2 . ASN A 1 1282 ? 119.048 150.519 98.301  1.00 160.99 ? 1282 ASN A ND2 1 
ATOM   10012 N  N   . PHE A 1 1283 ? 118.147 144.940 97.397  1.00 160.69 ? 1283 PHE A N   1 
ATOM   10013 C  CA  . PHE A 1 1283 ? 118.298 143.585 97.914  1.00 169.13 ? 1283 PHE A CA  1 
ATOM   10014 C  C   . PHE A 1 1283 ? 118.890 142.593 96.922  1.00 167.35 ? 1283 PHE A C   1 
ATOM   10015 O  O   . PHE A 1 1283 ? 119.090 141.429 97.285  1.00 168.12 ? 1283 PHE A O   1 
ATOM   10016 C  CB  . PHE A 1 1283 ? 116.941 143.064 98.411  1.00 168.08 ? 1283 PHE A CB  1 
ATOM   10017 C  CG  . PHE A 1 1283 ? 116.207 144.032 99.301  1.00 174.99 ? 1283 PHE A CG  1 
ATOM   10018 C  CD1 . PHE A 1 1283 ? 116.123 143.803 100.662 1.00 182.70 ? 1283 PHE A CD1 1 
ATOM   10019 C  CD2 . PHE A 1 1283 ? 115.580 145.154 98.777  1.00 174.63 ? 1283 PHE A CD2 1 
ATOM   10020 C  CE1 . PHE A 1 1283 ? 115.453 144.685 101.487 1.00 186.99 ? 1283 PHE A CE1 1 
ATOM   10021 C  CE2 . PHE A 1 1283 ? 114.911 146.039 99.596  1.00 171.82 ? 1283 PHE A CE2 1 
ATOM   10022 C  CZ  . PHE A 1 1283 ? 114.845 145.803 100.953 1.00 179.92 ? 1283 PHE A CZ  1 
ATOM   10023 N  N   . LEU A 1 1284 ? 119.170 143.003 95.696  1.00 166.10 ? 1284 LEU A N   1 
ATOM   10024 C  CA  . LEU A 1 1284 ? 119.737 142.034 94.766  1.00 174.92 ? 1284 LEU A CA  1 
ATOM   10025 C  C   . LEU A 1 1284 ? 121.208 141.769 95.091  1.00 189.73 ? 1284 LEU A C   1 
ATOM   10026 O  O   . LEU A 1 1284 ? 121.957 142.699 95.403  1.00 185.49 ? 1284 LEU A O   1 
ATOM   10027 C  CB  . LEU A 1 1284 ? 119.593 142.510 93.322  1.00 167.84 ? 1284 LEU A CB  1 
ATOM   10028 C  CG  . LEU A 1 1284 ? 118.234 142.223 92.673  1.00 158.66 ? 1284 LEU A CG  1 
ATOM   10029 C  CD1 . LEU A 1 1284 ? 118.028 140.721 92.591  1.00 140.56 ? 1284 LEU A CD1 1 
ATOM   10030 C  CD2 . LEU A 1 1284 ? 117.064 142.892 93.388  1.00 155.58 ? 1284 LEU A CD2 1 
ATOM   10031 N  N   . PRO A 1 1285 ? 121.640 140.502 95.026  1.00 197.91 ? 1285 PRO A N   1 
ATOM   10032 C  CA  . PRO A 1 1285 ? 123.062 140.176 95.223  1.00 204.00 ? 1285 PRO A CA  1 
ATOM   10033 C  C   . PRO A 1 1285 ? 123.948 140.630 94.074  1.00 205.56 ? 1285 PRO A C   1 
ATOM   10034 O  O   . PRO A 1 1285 ? 123.499 141.352 93.180  1.00 199.75 ? 1285 PRO A O   1 
ATOM   10035 C  CB  . PRO A 1 1285 ? 123.058 138.647 95.350  1.00 196.02 ? 1285 PRO A CB  1 
ATOM   10036 C  CG  . PRO A 1 1285 ? 121.817 138.212 94.646  1.00 187.38 ? 1285 PRO A CG  1 
ATOM   10037 C  CD  . PRO A 1 1285 ? 120.808 139.296 94.876  1.00 189.55 ? 1285 PRO A CD  1 
ATOM   10038 N  N   . THR A 1 1286 ? 125.221 140.245 94.114  1.00 213.02 ? 1286 THR A N   1 
ATOM   10039 C  CA  . THR A 1 1286 ? 126.163 140.631 93.072  1.00 220.20 ? 1286 THR A CA  1 
ATOM   10040 C  C   . THR A 1 1286 ? 125.839 139.950 91.744  1.00 219.30 ? 1286 THR A C   1 
ATOM   10041 O  O   . THR A 1 1286 ? 125.517 138.760 91.695  1.00 212.71 ? 1286 THR A O   1 
ATOM   10042 C  CB  . THR A 1 1286 ? 127.589 140.283 93.502  1.00 212.67 ? 1286 THR A CB  1 
ATOM   10043 O  OG1 . THR A 1 1286 ? 127.854 140.856 94.789  1.00 206.13 ? 1286 THR A OG1 1 
ATOM   10044 C  CG2 . THR A 1 1286 ? 128.602 140.819 92.500  1.00 206.52 ? 1286 THR A CG2 1 
ATOM   10045 N  N   . HIS A 1 1287 ? 125.929 140.724 90.667  1.00 219.71 ? 1287 HIS A N   1 
ATOM   10046 C  CA  . HIS A 1 1287 ? 125.644 140.257 89.313  1.00 223.71 ? 1287 HIS A CA  1 
ATOM   10047 C  C   . HIS A 1 1287 ? 126.805 140.644 88.400  1.00 223.80 ? 1287 HIS A C   1 
ATOM   10048 O  O   . HIS A 1 1287 ? 127.928 140.909 88.850  1.00 215.82 ? 1287 HIS A O   1 
ATOM   10049 C  CB  . HIS A 1 1287 ? 124.313 140.806 88.780  1.00 221.87 ? 1287 HIS A CB  1 
ATOM   10050 C  CG  . HIS A 1 1287 ? 123.109 140.297 89.508  1.00 218.86 ? 1287 HIS A CG  1 
ATOM   10051 N  ND1 . HIS A 1 1287 ? 122.432 139.163 89.116  1.00 206.03 ? 1287 HIS A ND1 1 
ATOM   10052 C  CD2 . HIS A 1 1287 ? 122.443 140.780 90.582  1.00 214.19 ? 1287 HIS A CD2 1 
ATOM   10053 C  CE1 . HIS A 1 1287 ? 121.412 138.958 89.930  1.00 197.18 ? 1287 HIS A CE1 1 
ATOM   10054 N  NE2 . HIS A 1 1287 ? 121.396 139.925 90.829  1.00 204.53 ? 1287 HIS A NE2 1 
ATOM   10055 N  N   . TYR A 1 1288 ? 126.535 140.612 87.091  1.00 225.33 ? 1288 TYR A N   1 
ATOM   10056 C  CA  . TYR A 1 1288 ? 127.389 141.084 85.998  1.00 226.56 ? 1288 TYR A CA  1 
ATOM   10057 C  C   . TYR A 1 1288 ? 128.484 140.102 85.599  1.00 217.56 ? 1288 TYR A C   1 
ATOM   10058 O  O   . TYR A 1 1288 ? 129.481 140.511 84.995  1.00 210.10 ? 1288 TYR A O   1 
ATOM   10059 C  CB  . TYR A 1 1288 ? 128.020 142.446 86.324  1.00 228.45 ? 1288 TYR A CB  1 
ATOM   10060 C  CG  . TYR A 1 1288 ? 127.050 143.422 86.964  1.00 231.04 ? 1288 TYR A CG  1 
ATOM   10061 C  CD1 . TYR A 1 1288 ? 125.961 143.917 86.260  1.00 224.72 ? 1288 TYR A CD1 1 
ATOM   10062 C  CD2 . TYR A 1 1288 ? 127.224 143.839 88.280  1.00 226.28 ? 1288 TYR A CD2 1 
ATOM   10063 C  CE1 . TYR A 1 1288 ? 125.072 144.799 86.850  1.00 224.07 ? 1288 TYR A CE1 1 
ATOM   10064 C  CE2 . TYR A 1 1288 ? 126.342 144.717 88.876  1.00 222.92 ? 1288 TYR A CE2 1 
ATOM   10065 C  CZ  . TYR A 1 1288 ? 125.268 145.195 88.157  1.00 224.71 ? 1288 TYR A CZ  1 
ATOM   10066 O  OH  . TYR A 1 1288 ? 124.388 146.073 88.747  1.00 213.69 ? 1288 TYR A OH  1 
ATOM   10067 N  N   . SER A 1 1289 ? 128.337 138.817 85.917  1.00 210.08 ? 1289 SER A N   1 
ATOM   10068 C  CA  . SER A 1 1289 ? 129.265 137.794 85.443  1.00 200.49 ? 1289 SER A CA  1 
ATOM   10069 C  C   . SER A 1 1289 ? 128.466 136.573 85.013  1.00 197.51 ? 1289 SER A C   1 
ATOM   10070 O  O   . SER A 1 1289 ? 127.704 136.022 85.815  1.00 193.72 ? 1289 SER A O   1 
ATOM   10071 C  CB  . SER A 1 1289 ? 130.283 137.421 86.524  1.00 191.22 ? 1289 SER A CB  1 
ATOM   10072 O  OG  . SER A 1 1289 ? 131.158 136.404 86.067  1.00 184.94 ? 1289 SER A OG  1 
ATOM   10073 N  N   . GLY A 1 1290 ? 128.631 136.149 83.772  1.00 191.76 ? 1290 GLY A N   1 
ATOM   10074 C  CA  . GLY A 1 1290 ? 127.999 134.922 83.322  1.00 182.41 ? 1290 GLY A CA  1 
ATOM   10075 C  C   . GLY A 1 1290 ? 127.745 134.934 81.830  1.00 170.10 ? 1290 GLY A C   1 
ATOM   10076 O  O   . GLY A 1 1290 ? 127.827 135.962 81.160  1.00 163.59 ? 1290 GLY A O   1 
ATOM   10077 N  N   . ASN A 1 1291 ? 127.422 133.746 81.315  1.00 174.54 ? 1291 ASN A N   1 
ATOM   10078 C  CA  . ASN A 1 1291 ? 127.065 133.541 79.916  1.00 176.10 ? 1291 ASN A CA  1 
ATOM   10079 C  C   . ASN A 1 1291 ? 125.659 132.956 79.884  1.00 179.53 ? 1291 ASN A C   1 
ATOM   10080 O  O   . ASN A 1 1291 ? 125.453 131.814 80.305  1.00 170.32 ? 1291 ASN A O   1 
ATOM   10081 C  CB  . ASN A 1 1291 ? 128.070 132.610 79.226  1.00 176.09 ? 1291 ASN A CB  1 
ATOM   10082 C  CG  . ASN A 1 1291 ? 127.685 132.268 77.788  1.00 172.42 ? 1291 ASN A CG  1 
ATOM   10083 O  OD1 . ASN A 1 1291 ? 126.630 132.661 77.292  1.00 169.72 ? 1291 ASN A OD1 1 
ATOM   10084 N  ND2 . ASN A 1 1291 ? 128.553 131.523 77.115  1.00 172.55 ? 1291 ASN A ND2 1 
ATOM   10085 N  N   . ILE A 1 1292 ? 124.715 133.718 79.324  1.00 188.79 ? 1292 ILE A N   1 
ATOM   10086 C  CA  . ILE A 1 1292 ? 123.297 133.556 79.655  1.00 190.58 ? 1292 ILE A CA  1 
ATOM   10087 C  C   . ILE A 1 1292 ? 122.819 132.132 79.393  1.00 178.87 ? 1292 ILE A C   1 
ATOM   10088 O  O   . ILE A 1 1292 ? 122.252 131.480 80.279  1.00 168.06 ? 1292 ILE A O   1 
ATOM   10089 C  CB  . ILE A 1 1292 ? 122.442 134.579 78.882  1.00 190.73 ? 1292 ILE A CB  1 
ATOM   10090 C  CG1 . ILE A 1 1292 ? 122.875 136.010 79.208  1.00 185.02 ? 1292 ILE A CG1 1 
ATOM   10091 C  CG2 . ILE A 1 1292 ? 120.962 134.364 79.169  1.00 164.28 ? 1292 ILE A CG2 1 
ATOM   10092 C  CD1 . ILE A 1 1292 ? 123.947 136.550 78.298  1.00 167.61 ? 1292 ILE A CD1 1 
ATOM   10093 N  N   . VAL A 1 1293 ? 123.097 131.611 78.196  1.00 181.52 ? 1293 VAL A N   1 
ATOM   10094 C  CA  . VAL A 1 1293 ? 122.640 130.269 77.841  1.00 186.53 ? 1293 VAL A CA  1 
ATOM   10095 C  C   . VAL A 1 1293 ? 123.280 129.233 78.754  1.00 188.02 ? 1293 VAL A C   1 
ATOM   10096 O  O   . VAL A 1 1293 ? 122.593 128.385 79.336  1.00 175.68 ? 1293 VAL A O   1 
ATOM   10097 C  CB  . VAL A 1 1293 ? 122.927 129.978 76.358  1.00 185.94 ? 1293 VAL A CB  1 
ATOM   10098 C  CG1 . VAL A 1 1293 ? 122.453 128.580 75.990  1.00 179.66 ? 1293 VAL A CG1 1 
ATOM   10099 C  CG2 . VAL A 1 1293 ? 122.260 131.025 75.475  1.00 169.22 ? 1293 VAL A CG2 1 
ATOM   10100 N  N   . HIS A 1 1294 ? 124.602 129.291 78.905  1.00 182.51 ? 1294 HIS A N   1 
ATOM   10101 C  CA  . HIS A 1 1294 ? 125.273 128.305 79.743  1.00 179.20 ? 1294 HIS A CA  1 
ATOM   10102 C  C   . HIS A 1 1294 ? 125.013 128.578 81.217  1.00 174.24 ? 1294 HIS A C   1 
ATOM   10103 O  O   . HIS A 1 1294 ? 124.728 127.652 81.984  1.00 172.69 ? 1294 HIS A O   1 
ATOM   10104 C  CB  . HIS A 1 1294 ? 126.776 128.279 79.480  1.00 184.27 ? 1294 HIS A CB  1 
ATOM   10105 C  CG  . HIS A 1 1294 ? 127.531 127.453 80.476  1.00 191.20 ? 1294 HIS A CG  1 
ATOM   10106 N  ND1 . HIS A 1 1294 ? 127.592 126.078 80.408  1.00 176.23 ? 1294 HIS A ND1 1 
ATOM   10107 C  CD2 . HIS A 1 1294 ? 128.225 127.807 81.583  1.00 181.79 ? 1294 HIS A CD2 1 
ATOM   10108 C  CE1 . HIS A 1 1294 ? 128.305 125.621 81.422  1.00 166.76 ? 1294 HIS A CE1 1 
ATOM   10109 N  NE2 . HIS A 1 1294 ? 128.702 126.650 82.149  1.00 167.44 ? 1294 HIS A NE2 1 
ATOM   10110 N  N   . ARG A 1 1295 ? 125.099 129.843 81.632  1.00 162.78 ? 1295 ARG A N   1 
ATOM   10111 C  CA  . ARG A 1 1295 ? 125.091 130.161 83.052  1.00 169.58 ? 1295 ARG A CA  1 
ATOM   10112 C  C   . ARG A 1 1295 ? 123.686 130.132 83.646  1.00 167.94 ? 1295 ARG A C   1 
ATOM   10113 O  O   . ARG A 1 1295 ? 123.554 130.059 84.871  1.00 160.15 ? 1295 ARG A O   1 
ATOM   10114 C  CB  . ARG A 1 1295 ? 125.748 131.532 83.279  1.00 173.34 ? 1295 ARG A CB  1 
ATOM   10115 C  CG  . ARG A 1 1295 ? 125.807 132.020 84.721  1.00 180.58 ? 1295 ARG A CG  1 
ATOM   10116 C  CD  . ARG A 1 1295 ? 126.729 131.154 85.560  1.00 179.19 ? 1295 ARG A CD  1 
ATOM   10117 N  NE  . ARG A 1 1295 ? 128.123 131.273 85.146  1.00 168.04 ? 1295 ARG A NE  1 
ATOM   10118 C  CZ  . ARG A 1 1295 ? 129.096 130.469 85.561  1.00 171.05 ? 1295 ARG A CZ  1 
ATOM   10119 N  NH1 . ARG A 1 1295 ? 128.829 129.485 86.408  1.00 170.56 ? 1295 ARG A NH1 1 
ATOM   10120 N  NH2 . ARG A 1 1295 ? 130.338 130.651 85.136  1.00 175.12 ? 1295 ARG A NH2 1 
ATOM   10121 N  N   . TYR A 1 1296 ? 122.638 130.044 82.824  1.00 150.60 ? 1296 TYR A N   1 
ATOM   10122 C  CA  . TYR A 1 1296 ? 121.309 129.889 83.407  1.00 145.71 ? 1296 TYR A CA  1 
ATOM   10123 C  C   . TYR A 1 1296 ? 121.131 128.513 84.033  1.00 145.77 ? 1296 TYR A C   1 
ATOM   10124 O  O   . TYR A 1 1296 ? 120.626 128.399 85.158  1.00 143.09 ? 1296 TYR A O   1 
ATOM   10125 C  CB  . TYR A 1 1296 ? 120.231 130.116 82.348  1.00 142.71 ? 1296 TYR A CB  1 
ATOM   10126 C  CG  . TYR A 1 1296 ? 118.849 130.274 82.940  1.00 140.12 ? 1296 TYR A CG  1 
ATOM   10127 C  CD1 . TYR A 1 1296 ? 118.070 129.157 83.219  1.00 130.69 ? 1296 TYR A CD1 1 
ATOM   10128 C  CD2 . TYR A 1 1296 ? 118.325 131.525 83.231  1.00 123.83 ? 1296 TYR A CD2 1 
ATOM   10129 C  CE1 . TYR A 1 1296 ? 116.811 129.278 83.767  1.00 107.27 ? 1296 TYR A CE1 1 
ATOM   10130 C  CE2 . TYR A 1 1296 ? 117.061 131.657 83.781  1.00 106.76 ? 1296 TYR A CE2 1 
ATOM   10131 C  CZ  . TYR A 1 1296 ? 116.309 130.529 84.046  1.00 105.75 ? 1296 TYR A CZ  1 
ATOM   10132 O  OH  . TYR A 1 1296 ? 115.051 130.651 84.591  1.00 99.93  ? 1296 TYR A OH  1 
ATOM   10133 N  N   . ASN A 1 1297 ? 121.564 127.460 83.337  1.00 143.26 ? 1297 ASN A N   1 
ATOM   10134 C  CA  . ASN A 1 1297 ? 121.335 126.107 83.830  1.00 138.51 ? 1297 ASN A CA  1 
ATOM   10135 C  C   . ASN A 1 1297 ? 122.054 125.869 85.151  1.00 140.14 ? 1297 ASN A C   1 
ATOM   10136 O  O   . ASN A 1 1297 ? 121.500 125.245 86.063  1.00 142.57 ? 1297 ASN A O   1 
ATOM   10137 C  CB  . ASN A 1 1297 ? 121.761 125.087 82.778  1.00 143.39 ? 1297 ASN A CB  1 
ATOM   10138 C  CG  . ASN A 1 1297 ? 120.941 125.196 81.508  1.00 144.25 ? 1297 ASN A CG  1 
ATOM   10139 O  OD1 . ASN A 1 1297 ? 121.462 125.534 80.445  1.00 142.24 ? 1297 ASN A OD1 1 
ATOM   10140 N  ND2 . ASN A 1 1297 ? 119.643 124.938 81.620  1.00 141.06 ? 1297 ASN A ND2 1 
ATOM   10141 N  N   . ASP A 1 1298 ? 123.285 126.366 85.282  1.00 136.85 ? 1298 ASP A N   1 
ATOM   10142 C  CA  . ASP A 1 1298 ? 124.034 126.107 86.503  1.00 146.40 ? 1298 ASP A CA  1 
ATOM   10143 C  C   . ASP A 1 1298 ? 123.689 127.110 87.598  1.00 152.80 ? 1298 ASP A C   1 
ATOM   10144 O  O   . ASP A 1 1298 ? 123.754 126.762 88.783  1.00 153.21 ? 1298 ASP A O   1 
ATOM   10145 C  CB  . ASP A 1 1298 ? 125.543 126.075 86.219  1.00 155.33 ? 1298 ASP A CB  1 
ATOM   10146 C  CG  . ASP A 1 1298 ? 126.065 127.370 85.639  1.00 165.23 ? 1298 ASP A CG  1 
ATOM   10147 O  OD1 . ASP A 1 1298 ? 125.304 128.346 85.582  1.00 162.80 ? 1298 ASP A OD1 1 
ATOM   10148 O  OD2 . ASP A 1 1298 ? 127.245 127.410 85.228  1.00 165.92 ? 1298 ASP A OD2 1 
ATOM   10149 N  N   . GLN A 1 1299 ? 123.323 128.350 87.244  1.00 142.35 ? 1299 GLN A N   1 
ATOM   10150 C  CA  . GLN A 1 1299 ? 122.982 129.326 88.270  1.00 143.06 ? 1299 GLN A CA  1 
ATOM   10151 C  C   . GLN A 1 1299 ? 121.626 129.026 88.896  1.00 140.47 ? 1299 GLN A C   1 
ATOM   10152 O  O   . GLN A 1 1299 ? 121.481 129.058 90.123  1.00 134.65 ? 1299 GLN A O   1 
ATOM   10153 C  CB  . GLN A 1 1299 ? 122.998 130.736 87.678  1.00 138.31 ? 1299 GLN A CB  1 
ATOM   10154 C  CG  . GLN A 1 1299 ? 122.542 131.807 88.655  1.00 146.67 ? 1299 GLN A CG  1 
ATOM   10155 C  CD  . GLN A 1 1299 ? 123.472 131.950 89.839  1.00 151.95 ? 1299 GLN A CD  1 
ATOM   10156 O  OE1 . GLN A 1 1299 ? 123.175 131.476 90.936  1.00 137.54 ? 1299 GLN A OE1 1 
ATOM   10157 N  NE2 . GLN A 1 1299 ? 124.603 132.613 89.629  1.00 157.67 ? 1299 GLN A NE2 1 
ATOM   10158 N  N   . TYR A 1 1300 ? 120.616 128.723 88.074  1.00 126.24 ? 1300 TYR A N   1 
ATOM   10159 C  CA  . TYR A 1 1300 ? 119.257 128.561 88.580  1.00 116.55 ? 1300 TYR A CA  1 
ATOM   10160 C  C   . TYR A 1 1300 ? 118.679 127.165 88.410  1.00 125.86 ? 1300 TYR A C   1 
ATOM   10161 O  O   . TYR A 1 1300 ? 117.497 126.965 88.716  1.00 127.78 ? 1300 TYR A O   1 
ATOM   10162 C  CB  . TYR A 1 1300 ? 118.318 129.572 87.920  1.00 115.08 ? 1300 TYR A CB  1 
ATOM   10163 C  CG  . TYR A 1 1300 ? 118.716 130.996 88.181  1.00 115.37 ? 1300 TYR A CG  1 
ATOM   10164 C  CD1 . TYR A 1 1300 ? 118.742 131.495 89.474  1.00 121.56 ? 1300 TYR A CD1 1 
ATOM   10165 C  CD2 . TYR A 1 1300 ? 119.059 131.845 87.141  1.00 110.10 ? 1300 TYR A CD2 1 
ATOM   10166 C  CE1 . TYR A 1 1300 ? 119.105 132.799 89.727  1.00 121.34 ? 1300 TYR A CE1 1 
ATOM   10167 C  CE2 . TYR A 1 1300 ? 119.423 133.154 87.383  1.00 115.06 ? 1300 TYR A CE2 1 
ATOM   10168 C  CZ  . TYR A 1 1300 ? 119.444 133.626 88.679  1.00 125.59 ? 1300 TYR A CZ  1 
ATOM   10169 O  OH  . TYR A 1 1300 ? 119.806 134.929 88.928  1.00 130.28 ? 1300 TYR A OH  1 
ATOM   10170 N  N   . GLY A 1 1301 ? 119.454 126.189 87.953  1.00 133.70 ? 1301 GLY A N   1 
ATOM   10171 C  CA  . GLY A 1 1301 ? 118.893 124.871 87.785  1.00 131.09 ? 1301 GLY A CA  1 
ATOM   10172 C  C   . GLY A 1 1301 ? 118.881 124.110 89.093  1.00 137.58 ? 1301 GLY A C   1 
ATOM   10173 O  O   . GLY A 1 1301 ? 119.323 124.587 90.136  1.00 137.32 ? 1301 GLY A O   1 
ATOM   10174 N  N   . GLN A 1 1302 ? 118.363 122.891 89.023  1.00 138.95 ? 1302 GLN A N   1 
ATOM   10175 C  CA  . GLN A 1 1302 ? 118.288 122.010 90.178  1.00 144.23 ? 1302 GLN A CA  1 
ATOM   10176 C  C   . GLN A 1 1302 ? 119.153 120.797 89.880  1.00 136.00 ? 1302 GLN A C   1 
ATOM   10177 O  O   . GLN A 1 1302 ? 118.889 120.066 88.920  1.00 131.74 ? 1302 GLN A O   1 
ATOM   10178 C  CB  . GLN A 1 1302 ? 116.844 121.614 90.495  1.00 148.08 ? 1302 GLN A CB  1 
ATOM   10179 C  CG  . GLN A 1 1302 ? 116.720 120.565 91.583  1.00 150.94 ? 1302 GLN A CG  1 
ATOM   10180 C  CD  . GLN A 1 1302 ? 115.583 119.600 91.335  1.00 157.98 ? 1302 GLN A CD  1 
ATOM   10181 O  OE1 . GLN A 1 1302 ? 115.372 119.145 90.210  1.00 151.54 ? 1302 GLN A OE1 1 
ATOM   10182 N  NE2 . GLN A 1 1302 ? 114.835 119.288 92.386  1.00 157.20 ? 1302 GLN A NE2 1 
ATOM   10183 N  N   . HIS A 1 1303 ? 120.179 120.585 90.690  1.00 139.57 ? 1303 HIS A N   1 
ATOM   10184 C  CA  . HIS A 1 1303 ? 121.171 119.552 90.435  1.00 135.59 ? 1303 HIS A CA  1 
ATOM   10185 C  C   . HIS A 1 1303 ? 121.150 118.472 91.506  1.00 131.71 ? 1303 HIS A C   1 
ATOM   10186 O  O   . HIS A 1 1303 ? 120.507 118.590 92.554  1.00 125.47 ? 1303 HIS A O   1 
ATOM   10187 C  CB  . HIS A 1 1303 ? 122.584 120.146 90.360  1.00 134.56 ? 1303 HIS A CB  1 
ATOM   10188 C  CG  . HIS A 1 1303 ? 122.754 121.205 89.317  1.00 138.04 ? 1303 HIS A CG  1 
ATOM   10189 N  ND1 . HIS A 1 1303 ? 123.713 122.190 89.413  1.00 145.29 ? 1303 HIS A ND1 1 
ATOM   10190 C  CD2 . HIS A 1 1303 ? 122.109 121.419 88.145  1.00 147.92 ? 1303 HIS A CD2 1 
ATOM   10191 C  CE1 . HIS A 1 1303 ? 123.643 122.974 88.353  1.00 146.04 ? 1303 HIS A CE1 1 
ATOM   10192 N  NE2 . HIS A 1 1303 ? 122.678 122.529 87.569  1.00 143.59 ? 1303 HIS A NE2 1 
ATOM   10193 N  N   . SER A 1 1304 ? 121.873 117.406 91.199  1.00 121.76 ? 1304 SER A N   1 
ATOM   10194 C  CA  . SER A 1 1304 ? 122.130 116.299 92.104  1.00 114.23 ? 1304 SER A CA  1 
ATOM   10195 C  C   . SER A 1 1304 ? 123.516 116.541 92.688  1.00 101.42 ? 1304 SER A C   1 
ATOM   10196 O  O   . SER A 1 1304 ? 124.469 116.782 91.943  1.00 100.12 ? 1304 SER A O   1 
ATOM   10197 C  CB  . SER A 1 1304 ? 122.067 114.964 91.361  1.00 105.35 ? 1304 SER A CB  1 
ATOM   10198 O  OG  . SER A 1 1304 ? 123.026 114.931 90.311  1.00 95.80  ? 1304 SER A OG  1 
ATOM   10199 N  N   . PHE A 1 1305 ? 123.629 116.462 94.012  1.00 101.15 ? 1305 PHE A N   1 
ATOM   10200 C  CA  . PHE A 1 1305 ? 124.874 116.780 94.716  1.00 104.18 ? 1305 PHE A CA  1 
ATOM   10201 C  C   . PHE A 1 1305 ? 125.747 115.562 94.928  1.00 96.16  ? 1305 PHE A C   1 
ATOM   10202 O  O   . PHE A 1 1305 ? 126.841 115.705 95.511  1.00 96.46  ? 1305 PHE A O   1 
ATOM   10203 C  CB  . PHE A 1 1305 ? 124.557 117.454 96.050  1.00 119.29 ? 1305 PHE A CB  1 
ATOM   10204 C  CG  . PHE A 1 1305 ? 123.939 118.799 95.904  1.00 130.83 ? 1305 PHE A CG  1 
ATOM   10205 C  CD1 . PHE A 1 1305 ? 123.237 119.376 96.941  1.00 138.94 ? 1305 PHE A CD1 1 
ATOM   10206 C  CD2 . PHE A 1 1305 ? 124.078 119.496 94.717  1.00 121.73 ? 1305 PHE A CD2 1 
ATOM   10207 C  CE1 . PHE A 1 1305 ? 122.680 120.636 96.795  1.00 140.38 ? 1305 PHE A CE1 1 
ATOM   10208 C  CE2 . PHE A 1 1305 ? 123.525 120.750 94.562  1.00 125.69 ? 1305 PHE A CE2 1 
ATOM   10209 C  CZ  . PHE A 1 1305 ? 122.824 121.322 95.602  1.00 141.40 ? 1305 PHE A CZ  1 
ATOM   10210 N  N   . MET A 1 1306 ? 125.270 114.396 94.486  1.00 97.93  ? 1306 MET A N   1 
ATOM   10211 C  CA  . MET A 1 1306 ? 125.995 113.163 94.717  1.00 84.64  ? 1306 MET A CA  1 
ATOM   10212 C  C   . MET A 1 1306 ? 125.462 112.044 93.796  1.00 77.04  ? 1306 MET A C   1 
ATOM   10213 O  O   . MET A 1 1306 ? 124.340 112.099 93.234  1.00 77.34  ? 1306 MET A O   1 
ATOM   10214 C  CB  . MET A 1 1306 ? 125.887 112.834 96.195  1.00 87.44  ? 1306 MET A CB  1 
ATOM   10215 C  CG  . MET A 1 1306 ? 124.521 112.536 96.751  1.00 103.33 ? 1306 MET A CG  1 
ATOM   10216 S  SD  . MET A 1 1306 ? 125.023 112.418 98.484  1.00 141.23 ? 1306 MET A SD  1 
ATOM   10217 C  CE  . MET A 1 1306 ? 125.424 114.119 98.928  1.00 105.55 ? 1306 MET A CE  1 
ATOM   10218 N  N   . ALA A 1 1307 ? 126.279 111.002 93.643  1.00 67.51  ? 1307 ALA A N   1 
ATOM   10219 C  CA  . ALA A 1 1307 ? 125.917 109.831 92.871  1.00 54.06  ? 1307 ALA A CA  1 
ATOM   10220 C  C   . ALA A 1 1307 ? 124.931 108.954 93.617  1.00 68.88  ? 1307 ALA A C   1 
ATOM   10221 O  O   . ALA A 1 1307 ? 124.897 108.898 94.845  1.00 81.72  ? 1307 ALA A O   1 
ATOM   10222 C  CB  . ALA A 1 1307 ? 127.172 109.020 92.512  1.00 46.14  ? 1307 ALA A CB  1 
ATOM   10223 N  N   . ASN A 1 1308 ? 124.115 108.245 92.832  1.00 67.34  ? 1308 ASN A N   1 
ATOM   10224 C  CA  . ASN A 1 1308 ? 123.059 107.421 93.391  1.00 57.73  ? 1308 ASN A CA  1 
ATOM   10225 C  C   . ASN A 1 1308 ? 123.582 106.055 93.832  1.00 64.60  ? 1308 ASN A C   1 
ATOM   10226 O  O   . ASN A 1 1308 ? 123.030 105.019 93.436  1.00 80.00  ? 1308 ASN A O   1 
ATOM   10227 C  CB  . ASN A 1 1308 ? 121.940 107.248 92.367  1.00 56.40  ? 1308 ASN A CB  1 
ATOM   10228 C  CG  . ASN A 1 1308 ? 120.622 106.905 93.006  1.00 65.90  ? 1308 ASN A CG  1 
ATOM   10229 O  OD1 . ASN A 1 1308 ? 120.359 107.285 94.146  1.00 78.54  ? 1308 ASN A OD1 1 
ATOM   10230 N  ND2 . ASN A 1 1308 ? 119.789 106.169 92.286  1.00 63.39  ? 1308 ASN A ND2 1 
ATOM   10231 N  N   . ARG A 1 1309 ? 124.637 106.039 94.646  1.00 63.69  ? 1309 ARG A N   1 
ATOM   10232 C  CA  . ARG A 1 1309 ? 125.254 104.818 95.148  1.00 62.95  ? 1309 ARG A CA  1 
ATOM   10233 C  C   . ARG A 1 1309 ? 125.355 104.925 96.666  1.00 69.46  ? 1309 ARG A C   1 
ATOM   10234 O  O   . ARG A 1 1309 ? 125.034 105.960 97.252  1.00 85.13  ? 1309 ARG A O   1 
ATOM   10235 C  CB  . ARG A 1 1309 ? 126.646 104.622 94.526  1.00 64.45  ? 1309 ARG A CB  1 
ATOM   10236 C  CG  . ARG A 1 1309 ? 126.719 104.845 93.026  1.00 68.91  ? 1309 ARG A CG  1 
ATOM   10237 C  CD  . ARG A 1 1309 ? 125.819 103.878 92.303  1.00 59.68  ? 1309 ARG A CD  1 
ATOM   10238 N  NE  . ARG A 1 1309 ? 126.257 102.506 92.519  1.00 67.75  ? 1309 ARG A NE  1 
ATOM   10239 C  CZ  . ARG A 1 1309 ? 125.437 101.462 92.544  1.00 77.10  ? 1309 ARG A CZ  1 
ATOM   10240 N  NH1 . ARG A 1 1309 ? 124.136 101.632 92.362  1.00 75.60  ? 1309 ARG A NH1 1 
ATOM   10241 N  NH2 . ARG A 1 1309 ? 125.920 100.246 92.756  1.00 62.72  ? 1309 ARG A NH2 1 
ATOM   10242 N  N   . MET A 1 1310 ? 125.801 103.861 97.323  1.00 60.08  ? 1310 MET A N   1 
ATOM   10243 C  CA  . MET A 1 1310 ? 126.137 104.010 98.729  1.00 67.59  ? 1310 MET A CA  1 
ATOM   10244 C  C   . MET A 1 1310 ? 127.355 104.899 98.858  1.00 66.76  ? 1310 MET A C   1 
ATOM   10245 O  O   . MET A 1 1310 ? 128.234 104.919 97.993  1.00 74.71  ? 1310 MET A O   1 
ATOM   10246 C  CB  . MET A 1 1310 ? 126.390 102.666 99.406  1.00 73.52  ? 1310 MET A CB  1 
ATOM   10247 C  CG  . MET A 1 1310 ? 125.112 101.880 99.713  1.00 69.79  ? 1310 MET A CG  1 
ATOM   10248 S  SD  . MET A 1 1310 ? 125.459 100.380 100.644 1.00 62.36  ? 1310 MET A SD  1 
ATOM   10249 C  CE  . MET A 1 1310 ? 126.246 99.450  99.328  1.00 58.83  ? 1310 MET A CE  1 
ATOM   10250 N  N   . SER A 1 1311 ? 127.394 105.632 99.946  1.00 57.02  ? 1311 SER A N   1 
ATOM   10251 C  CA  . SER A 1 1311 ? 128.338 106.714 100.103 1.00 59.17  ? 1311 SER A CA  1 
ATOM   10252 C  C   . SER A 1 1311 ? 129.694 106.245 100.599 1.00 65.18  ? 1311 SER A C   1 
ATOM   10253 O  O   . SER A 1 1311 ? 130.516 107.091 100.941 1.00 76.80  ? 1311 SER A O   1 
ATOM   10254 C  CB  . SER A 1 1311 ? 127.759 107.738 101.078 1.00 62.86  ? 1311 SER A CB  1 
ATOM   10255 O  OG  . SER A 1 1311 ? 127.501 107.139 102.339 1.00 64.70  ? 1311 SER A OG  1 
ATOM   10256 N  N   . ASN A 1 1312 ? 129.962 104.937 100.657 1.00 61.75  ? 1312 ASN A N   1 
ATOM   10257 C  CA  . ASN A 1 1312 ? 131.298 104.567 101.123 1.00 59.17  ? 1312 ASN A CA  1 
ATOM   10258 C  C   . ASN A 1 1312 ? 132.356 104.773 100.044 1.00 63.59  ? 1312 ASN A C   1 
ATOM   10259 O  O   . ASN A 1 1312 ? 133.511 105.078 100.355 1.00 66.83  ? 1312 ASN A O   1 
ATOM   10260 C  CB  . ASN A 1 1312 ? 131.414 103.112 101.594 1.00 41.20  ? 1312 ASN A CB  1 
ATOM   10261 C  CG  . ASN A 1 1312 ? 130.443 102.758 102.687 1.00 44.72  ? 1312 ASN A CG  1 
ATOM   10262 O  OD1 . ASN A 1 1312 ? 129.912 101.650 102.682 1.00 57.80  ? 1312 ASN A OD1 1 
ATOM   10263 N  ND2 . ASN A 1 1312 ? 129.951 103.777 103.393 1.00 76.89  ? 1312 ASN A ND2 1 
ATOM   10264 N  N   . THR A 1 1313 ? 131.978 104.599 98.767  1.00 71.66  ? 1313 THR A N   1 
ATOM   10265 C  CA  . THR A 1 1313 ? 132.959 104.664 97.682  1.00 70.26  ? 1313 THR A CA  1 
ATOM   10266 C  C   . THR A 1 1313 ? 133.545 106.059 97.516  1.00 59.24  ? 1313 THR A C   1 
ATOM   10267 O  O   . THR A 1 1313 ? 134.733 106.194 97.200  1.00 62.30  ? 1313 THR A O   1 
ATOM   10268 C  CB  . THR A 1 1313 ? 132.325 104.195 96.365  1.00 70.32  ? 1313 THR A CB  1 
ATOM   10269 O  OG1 . THR A 1 1313 ? 131.854 102.849 96.502  1.00 67.25  ? 1313 THR A OG1 1 
ATOM   10270 C  CG2 . THR A 1 1313 ? 133.347 104.228 95.220  1.00 69.56  ? 1313 THR A CG2 1 
ATOM   10271 N  N   . SER A 1 1314 ? 132.747 107.107 97.730  1.00 56.84  ? 1314 SER A N   1 
ATOM   10272 C  CA  . SER A 1 1314 ? 133.250 108.458 97.507  1.00 52.46  ? 1314 SER A CA  1 
ATOM   10273 C  C   . SER A 1 1314 ? 134.441 108.764 98.405  1.00 71.68  ? 1314 SER A C   1 
ATOM   10274 O  O   . SER A 1 1314 ? 135.311 109.560 98.036  1.00 88.28  ? 1314 SER A O   1 
ATOM   10275 C  CB  . SER A 1 1314 ? 132.133 109.472 97.754  1.00 56.17  ? 1314 SER A CB  1 
ATOM   10276 O  OG  . SER A 1 1314 ? 131.617 109.349 99.070  1.00 62.77  ? 1314 SER A OG  1 
ATOM   10277 N  N   . THR A 1 1315 ? 134.505 108.133 99.580  1.00 71.18  ? 1315 THR A N   1 
ATOM   10278 C  CA  . THR A 1 1315 ? 135.581 108.378 100.534 1.00 67.23  ? 1315 THR A CA  1 
ATOM   10279 C  C   . THR A 1 1315 ? 136.925 107.798 100.108 1.00 62.60  ? 1315 THR A C   1 
ATOM   10280 O  O   . THR A 1 1315 ? 137.928 108.064 100.780 1.00 73.00  ? 1315 THR A O   1 
ATOM   10281 C  CB  . THR A 1 1315 ? 135.193 107.805 101.898 1.00 60.47  ? 1315 THR A CB  1 
ATOM   10282 O  OG1 . THR A 1 1315 ? 135.028 106.386 101.788 1.00 65.24  ? 1315 THR A OG1 1 
ATOM   10283 C  CG2 . THR A 1 1315 ? 133.881 108.413 102.376 1.00 62.31  ? 1315 THR A CG2 1 
ATOM   10284 N  N   . ARG A 1 1316 ? 136.987 107.024 99.019  1.00 65.18  ? 1316 ARG A N   1 
ATOM   10285 C  CA  . ARG A 1 1316 ? 138.250 106.465 98.540  1.00 58.21  ? 1316 ARG A CA  1 
ATOM   10286 C  C   . ARG A 1 1316 ? 138.549 106.821 97.087  1.00 77.57  ? 1316 ARG A C   1 
ATOM   10287 O  O   . ARG A 1 1316 ? 139.407 106.187 96.463  1.00 79.68  ? 1316 ARG A O   1 
ATOM   10288 C  CB  . ARG A 1 1316 ? 138.267 104.946 98.724  1.00 60.65  ? 1316 ARG A CB  1 
ATOM   10289 C  CG  . ARG A 1 1316 ? 138.452 104.508 100.167 1.00 74.37  ? 1316 ARG A CG  1 
ATOM   10290 C  CD  . ARG A 1 1316 ? 138.540 102.999 100.263 1.00 54.78  ? 1316 ARG A CD  1 
ATOM   10291 N  NE  . ARG A 1 1316 ? 139.792 102.496 99.706  1.00 46.98  ? 1316 ARG A NE  1 
ATOM   10292 C  CZ  . ARG A 1 1316 ? 140.069 101.208 99.542  1.00 55.32  ? 1316 ARG A CZ  1 
ATOM   10293 N  NH1 . ARG A 1 1316 ? 139.181 100.288 99.895  1.00 49.56  ? 1316 ARG A NH1 1 
ATOM   10294 N  NH2 . ARG A 1 1316 ? 141.236 100.837 99.033  1.00 64.02  ? 1316 ARG A NH2 1 
ATOM   10295 N  N   . ALA A 1 1317 ? 137.878 107.829 96.535  1.00 75.14  ? 1317 ALA A N   1 
ATOM   10296 C  CA  . ALA A 1 1317 ? 138.042 108.201 95.135  1.00 61.74  ? 1317 ALA A CA  1 
ATOM   10297 C  C   . ALA A 1 1317 ? 138.882 109.463 95.053  1.00 67.50  ? 1317 ALA A C   1 
ATOM   10298 O  O   . ALA A 1 1317 ? 138.620 110.436 95.759  1.00 74.31  ? 1317 ALA A O   1 
ATOM   10299 C  CB  . ALA A 1 1317 ? 136.678 108.419 94.470  1.00 60.10  ? 1317 ALA A CB  1 
ATOM   10300 N  N   . ILE A 1 1318 ? 139.896 109.440 94.198  1.00 65.41  ? 1318 ILE A N   1 
ATOM   10301 C  CA  . ILE A 1 1318 ? 140.717 110.627 93.957  1.00 64.66  ? 1318 ILE A CA  1 
ATOM   10302 C  C   . ILE A 1 1318 ? 140.403 111.212 92.587  1.00 72.30  ? 1318 ILE A C   1 
ATOM   10303 O  O   . ILE A 1 1318 ? 140.962 110.788 91.583  1.00 74.34  ? 1318 ILE A O   1 
ATOM   10304 C  CB  . ILE A 1 1318 ? 142.214 110.291 94.075  1.00 65.81  ? 1318 ILE A CB  1 
ATOM   10305 C  CG1 . ILE A 1 1318 ? 142.501 109.458 95.316  1.00 75.65  ? 1318 ILE A CG1 1 
ATOM   10306 C  CG2 . ILE A 1 1318 ? 143.004 111.573 94.225  1.00 94.75  ? 1318 ILE A CG2 1 
ATOM   10307 C  CD1 . ILE A 1 1318 ? 143.879 108.841 95.313  1.00 81.99  ? 1318 ILE A CD1 1 
ATOM   10308 N  N   . ILE A 1 1319 ? 139.502 112.201 92.551  1.00 69.91  ? 1319 ILE A N   1 
ATOM   10309 C  CA  . ILE A 1 1319 ? 139.086 112.835 91.299  1.00 68.32  ? 1319 ILE A CA  1 
ATOM   10310 C  C   . ILE A 1 1319 ? 139.845 114.144 91.141  1.00 86.79  ? 1319 ILE A C   1 
ATOM   10311 O  O   . ILE A 1 1319 ? 139.952 114.926 92.095  1.00 99.56  ? 1319 ILE A O   1 
ATOM   10312 C  CB  . ILE A 1 1319 ? 137.570 113.091 91.277  1.00 62.94  ? 1319 ILE A CB  1 
ATOM   10313 C  CG1 . ILE A 1 1319 ? 136.800 111.856 91.755  1.00 63.78  ? 1319 ILE A CG1 1 
ATOM   10314 C  CG2 . ILE A 1 1319 ? 137.112 113.510 89.890  1.00 75.56  ? 1319 ILE A CG2 1 
ATOM   10315 C  CD1 . ILE A 1 1319 ? 136.954 110.656 90.856  1.00 73.28  ? 1319 ILE A CD1 1 
ATOM   10316 N  N   . SER A 1 1320 ? 140.381 114.382 89.944  1.00 86.49  ? 1320 SER A N   1 
ATOM   10317 C  CA  . SER A 1 1320 ? 141.180 115.571 89.655  1.00 95.33  ? 1320 SER A CA  1 
ATOM   10318 C  C   . SER A 1 1320 ? 140.719 116.136 88.319  1.00 102.54 ? 1320 SER A C   1 
ATOM   10319 O  O   . SER A 1 1320 ? 140.982 115.539 87.272  1.00 105.07 ? 1320 SER A O   1 
ATOM   10320 C  CB  . SER A 1 1320 ? 142.671 115.238 89.627  1.00 104.85 ? 1320 SER A CB  1 
ATOM   10321 O  OG  . SER A 1 1320 ? 143.015 114.510 88.460  1.00 103.09 ? 1320 SER A OG  1 
ATOM   10322 N  N   . THR A 1 1321 ? 140.031 117.278 88.354  1.00 111.07 ? 1321 THR A N   1 
ATOM   10323 C  CA  . THR A 1 1321 ? 139.553 117.939 87.147  1.00 113.06 ? 1321 THR A CA  1 
ATOM   10324 C  C   . THR A 1 1321 ? 140.462 119.082 86.698  1.00 121.59 ? 1321 THR A C   1 
ATOM   10325 O  O   . THR A 1 1321 ? 139.977 120.074 86.146  1.00 125.28 ? 1321 THR A O   1 
ATOM   10326 C  CB  . THR A 1 1321 ? 138.129 118.454 87.349  1.00 112.89 ? 1321 THR A CB  1 
ATOM   10327 O  OG1 . THR A 1 1321 ? 138.121 119.458 88.372  1.00 118.39 ? 1321 THR A OG1 1 
ATOM   10328 C  CG2 . THR A 1 1321 ? 137.202 117.317 87.758  1.00 111.55 ? 1321 THR A CG2 1 
ATOM   10329 N  N   . ASN A 1 1322 ? 141.765 118.989 86.950  1.00 123.95 ? 1322 ASN A N   1 
ATOM   10330 C  CA  . ASN A 1 1322 ? 142.683 120.029 86.504  1.00 114.98 ? 1322 ASN A CA  1 
ATOM   10331 C  C   . ASN A 1 1322 ? 143.316 119.744 85.151  1.00 105.92 ? 1322 ASN A C   1 
ATOM   10332 O  O   . ASN A 1 1322 ? 143.964 120.636 84.592  1.00 117.22 ? 1322 ASN A O   1 
ATOM   10333 C  CB  . ASN A 1 1322 ? 143.795 120.250 87.535  1.00 127.70 ? 1322 ASN A CB  1 
ATOM   10334 C  CG  . ASN A 1 1322 ? 143.326 121.043 88.734  1.00 136.28 ? 1322 ASN A CG  1 
ATOM   10335 O  OD1 . ASN A 1 1322 ? 142.193 121.524 88.771  1.00 133.79 ? 1322 ASN A OD1 1 
ATOM   10336 N  ND2 . ASN A 1 1322 ? 144.206 121.207 89.715  1.00 131.13 ? 1322 ASN A ND2 1 
ATOM   10337 N  N   . THR A 1 1323 ? 143.139 118.546 84.602  1.00 104.22 ? 1323 THR A N   1 
ATOM   10338 C  CA  . THR A 1 1323 ? 143.894 118.130 83.430  1.00 115.11 ? 1323 THR A CA  1 
ATOM   10339 C  C   . THR A 1 1323 ? 143.107 118.223 82.132  1.00 126.57 ? 1323 THR A C   1 
ATOM   10340 O  O   . THR A 1 1323 ? 143.635 117.846 81.082  1.00 128.40 ? 1323 THR A O   1 
ATOM   10341 C  CB  . THR A 1 1323 ? 144.392 116.694 83.614  1.00 109.02 ? 1323 THR A CB  1 
ATOM   10342 O  OG1 . THR A 1 1323 ? 143.269 115.815 83.749  1.00 109.53 ? 1323 THR A OG1 1 
ATOM   10343 C  CG2 . THR A 1 1323 ? 145.249 116.589 84.865  1.00 104.31 ? 1323 THR A CG2 1 
ATOM   10344 N  N   . LEU A 1 1324 ? 141.876 118.724 82.161  1.00 123.78 ? 1324 LEU A N   1 
ATOM   10345 C  CA  . LEU A 1 1324 ? 141.110 118.818 80.920  1.00 128.40 ? 1324 LEU A CA  1 
ATOM   10346 C  C   . LEU A 1 1324 ? 141.321 120.172 80.242  1.00 143.46 ? 1324 LEU A C   1 
ATOM   10347 O  O   . LEU A 1 1324 ? 140.392 120.845 79.798  1.00 142.06 ? 1324 LEU A O   1 
ATOM   10348 C  CB  . LEU A 1 1324 ? 139.633 118.520 81.168  1.00 120.87 ? 1324 LEU A CB  1 
ATOM   10349 C  CG  . LEU A 1 1324 ? 138.646 119.447 81.877  1.00 124.71 ? 1324 LEU A CG  1 
ATOM   10350 C  CD1 . LEU A 1 1324 ? 137.227 118.983 81.587  1.00 95.16  ? 1324 LEU A CD1 1 
ATOM   10351 C  CD2 . LEU A 1 1324 ? 138.894 119.450 83.362  1.00 126.54 ? 1324 LEU A CD2 1 
ATOM   10352 N  N   . GLY A 1 1325 ? 142.598 120.546 80.140  1.00 147.77 ? 1325 GLY A N   1 
ATOM   10353 C  CA  . GLY A 1 1325 ? 143.012 121.620 79.254  1.00 149.84 ? 1325 GLY A CA  1 
ATOM   10354 C  C   . GLY A 1 1325 ? 142.334 122.949 79.518  1.00 156.64 ? 1325 GLY A C   1 
ATOM   10355 O  O   . GLY A 1 1325 ? 142.217 123.406 80.661  1.00 153.03 ? 1325 GLY A O   1 
ATOM   10356 N  N   . LYS A 1 1326 ? 141.872 123.574 78.437  1.00 150.23 ? 1326 LYS A N   1 
ATOM   10357 C  CA  . LYS A 1 1326 ? 141.316 124.920 78.452  1.00 155.23 ? 1326 LYS A CA  1 
ATOM   10358 C  C   . LYS A 1 1326 ? 139.911 124.994 79.037  1.00 162.60 ? 1326 LYS A C   1 
ATOM   10359 O  O   . LYS A 1 1326 ? 139.268 126.042 78.918  1.00 169.12 ? 1326 LYS A O   1 
ATOM   10360 C  CB  . LYS A 1 1326 ? 141.307 125.487 77.031  1.00 160.81 ? 1326 LYS A CB  1 
ATOM   10361 C  CG  . LYS A 1 1326 ? 140.397 124.720 76.085  1.00 148.20 ? 1326 LYS A CG  1 
ATOM   10362 C  CD  . LYS A 1 1326 ? 140.459 125.276 74.677  1.00 146.84 ? 1326 LYS A CD  1 
ATOM   10363 C  CE  . LYS A 1 1326 ? 139.524 124.515 73.752  1.00 152.83 ? 1326 LYS A CE  1 
ATOM   10364 N  NZ  . LYS A 1 1326 ? 139.980 123.113 73.550  1.00 145.91 ? 1326 LYS A NZ  1 
ATOM   10365 N  N   . TYR A 1 1327 ? 139.417 123.926 79.660  1.00 151.87 ? 1327 TYR A N   1 
ATOM   10366 C  CA  . TYR A 1 1327 ? 138.106 123.933 80.291  1.00 151.24 ? 1327 TYR A CA  1 
ATOM   10367 C  C   . TYR A 1 1327 ? 138.181 123.938 81.810  1.00 157.14 ? 1327 TYR A C   1 
ATOM   10368 O  O   . TYR A 1 1327 ? 137.137 123.986 82.469  1.00 154.15 ? 1327 TYR A O   1 
ATOM   10369 C  CB  . TYR A 1 1327 ? 137.265 122.744 79.809  1.00 141.51 ? 1327 TYR A CB  1 
ATOM   10370 C  CG  . TYR A 1 1327 ? 137.196 122.621 78.305  1.00 142.50 ? 1327 TYR A CG  1 
ATOM   10371 C  CD1 . TYR A 1 1327 ? 136.252 123.338 77.581  1.00 146.40 ? 1327 TYR A CD1 1 
ATOM   10372 C  CD2 . TYR A 1 1327 ? 138.061 121.789 77.607  1.00 138.56 ? 1327 TYR A CD2 1 
ATOM   10373 C  CE1 . TYR A 1 1327 ? 136.175 123.238 76.207  1.00 134.11 ? 1327 TYR A CE1 1 
ATOM   10374 C  CE2 . TYR A 1 1327 ? 137.990 121.681 76.228  1.00 139.00 ? 1327 TYR A CE2 1 
ATOM   10375 C  CZ  . TYR A 1 1327 ? 137.045 122.408 75.535  1.00 129.10 ? 1327 TYR A CZ  1 
ATOM   10376 O  OH  . TYR A 1 1327 ? 136.967 122.309 74.164  1.00 124.64 ? 1327 TYR A OH  1 
ATOM   10377 N  N   . ALA A 1 1328 ? 139.381 123.882 82.383  1.00 159.13 ? 1328 ALA A N   1 
ATOM   10378 C  CA  . ALA A 1 1328 ? 139.544 123.881 83.831  1.00 160.19 ? 1328 ALA A CA  1 
ATOM   10379 C  C   . ALA A 1 1328 ? 139.053 125.193 84.435  1.00 149.35 ? 1328 ALA A C   1 
ATOM   10380 O  O   . ALA A 1 1328 ? 139.704 126.230 84.308  1.00 141.52 ? 1328 ALA A O   1 
ATOM   10381 C  CB  . ALA A 1 1328 ? 141.000 123.638 84.202  1.00 148.05 ? 1328 ALA A CB  1 
ATOM   10382 N  N   . GLY A 1 1331 ? 138.067 131.465 82.833  1.00 147.21 ? 1331 GLY A N   1 
ATOM   10383 C  CA  . GLY A 1 1331 ? 136.848 131.075 82.151  1.00 164.15 ? 1331 GLY A CA  1 
ATOM   10384 C  C   . GLY A 1 1331 ? 136.944 131.188 80.643  1.00 176.80 ? 1331 GLY A C   1 
ATOM   10385 O  O   . GLY A 1 1331 ? 136.000 131.625 79.985  1.00 170.04 ? 1331 GLY A O   1 
ATOM   10386 N  N   . GLN A 1 1332 ? 138.088 130.789 80.092  1.00 184.29 ? 1332 GLN A N   1 
ATOM   10387 C  CA  . GLN A 1 1332 ? 138.306 130.845 78.650  1.00 188.89 ? 1332 GLN A CA  1 
ATOM   10388 C  C   . GLN A 1 1332 ? 137.664 129.620 78.004  1.00 187.72 ? 1332 GLN A C   1 
ATOM   10389 O  O   . GLN A 1 1332 ? 138.117 128.489 78.211  1.00 182.05 ? 1332 GLN A O   1 
ATOM   10390 C  CB  . GLN A 1 1332 ? 139.800 130.917 78.342  1.00 192.52 ? 1332 GLN A CB  1 
ATOM   10391 C  CG  . GLN A 1 1332 ? 140.634 129.817 78.999  1.00 185.69 ? 1332 GLN A CG  1 
ATOM   10392 C  CD  . GLN A 1 1332 ? 142.120 129.971 78.758  1.00 185.44 ? 1332 GLN A CD  1 
ATOM   10393 O  OE1 . GLN A 1 1332 ? 142.606 131.064 78.474  1.00 191.46 ? 1332 GLN A OE1 1 
ATOM   10394 N  NE2 . GLN A 1 1332 ? 142.852 128.867 78.863  1.00 167.53 ? 1332 GLN A NE2 1 
ATOM   10395 N  N   . ALA A 1 1333 ? 136.572 129.837 77.267  1.00 179.29 ? 1333 ALA A N   1 
ATOM   10396 C  CA  . ALA A 1 1333 ? 135.877 128.766 76.556  1.00 175.51 ? 1333 ALA A CA  1 
ATOM   10397 C  C   . ALA A 1 1333 ? 135.306 127.724 77.515  1.00 174.45 ? 1333 ALA A C   1 
ATOM   10398 O  O   . ALA A 1 1333 ? 134.725 126.726 77.074  1.00 172.35 ? 1333 ALA A O   1 
ATOM   10399 C  CB  . ALA A 1 1333 ? 136.803 128.104 75.530  1.00 164.40 ? 1333 ALA A CB  1 
ATOM   10400 N  N   . ALA A 1 1334 ? 135.468 127.938 78.822  1.00 175.08 ? 1334 ALA A N   1 
ATOM   10401 C  CA  . ALA A 1 1334 ? 134.877 127.077 79.840  1.00 172.31 ? 1334 ALA A CA  1 
ATOM   10402 C  C   . ALA A 1 1334 ? 133.492 127.554 80.264  1.00 182.17 ? 1334 ALA A C   1 
ATOM   10403 O  O   . ALA A 1 1334 ? 132.559 126.751 80.361  1.00 173.90 ? 1334 ALA A O   1 
ATOM   10404 C  CB  . ALA A 1 1334 ? 135.806 126.996 81.058  1.00 161.80 ? 1334 ALA A CB  1 
ATOM   10405 N  N   . ILE A 1 1335 ? 133.342 128.858 80.509  1.00 185.82 ? 1335 ILE A N   1 
ATOM   10406 C  CA  . ILE A 1 1335 ? 132.027 129.458 80.706  1.00 191.83 ? 1335 ILE A CA  1 
ATOM   10407 C  C   . ILE A 1 1335 ? 131.187 129.440 79.439  1.00 182.02 ? 1335 ILE A C   1 
ATOM   10408 O  O   . ILE A 1 1335 ? 130.001 129.785 79.480  1.00 178.05 ? 1335 ILE A O   1 
ATOM   10409 C  CB  . ILE A 1 1335 ? 132.163 130.909 81.212  1.00 189.51 ? 1335 ILE A CB  1 
ATOM   10410 C  CG1 . ILE A 1 1335 ? 130.925 131.319 82.013  1.00 180.39 ? 1335 ILE A CG1 1 
ATOM   10411 C  CG2 . ILE A 1 1335 ? 132.398 131.868 80.049  1.00 187.56 ? 1335 ILE A CG2 1 
ATOM   10412 C  CD1 . ILE A 1 1335 ? 130.993 132.724 82.568  1.00 175.95 ? 1335 ILE A CD1 1 
ATOM   10413 N  N   . ASP A 1 1336 ? 131.771 129.027 78.321  1.00 174.56 ? 1336 ASP A N   1 
ATOM   10414 C  CA  . ASP A 1 1336 ? 131.149 129.091 77.009  1.00 164.87 ? 1336 ASP A CA  1 
ATOM   10415 C  C   . ASP A 1 1336 ? 131.128 127.707 76.361  1.00 165.64 ? 1336 ASP A C   1 
ATOM   10416 O  O   . ASP A 1 1336 ? 131.321 127.555 75.152  1.00 168.09 ? 1336 ASP A O   1 
ATOM   10417 C  CB  . ASP A 1 1336 ? 131.869 130.129 76.146  1.00 173.65 ? 1336 ASP A CB  1 
ATOM   10418 C  CG  . ASP A 1 1336 ? 131.139 130.439 74.857  1.00 177.87 ? 1336 ASP A CG  1 
ATOM   10419 O  OD1 . ASP A 1 1336 ? 130.093 129.820 74.603  1.00 172.58 ? 1336 ASP A OD1 1 
ATOM   10420 O  OD2 . ASP A 1 1336 ? 131.595 131.330 74.110  1.00 175.89 ? 1336 ASP A OD2 1 
ATOM   10421 N  N   . SER A 1 1337 ? 130.923 126.667 77.169  1.00 158.90 ? 1337 SER A N   1 
ATOM   10422 C  CA  . SER A 1 1337 ? 130.870 125.302 76.665  1.00 154.87 ? 1337 SER A CA  1 
ATOM   10423 C  C   . SER A 1 1337 ? 129.661 124.578 77.251  1.00 145.50 ? 1337 SER A C   1 
ATOM   10424 O  O   . SER A 1 1337 ? 128.919 125.118 78.079  1.00 145.68 ? 1337 SER A O   1 
ATOM   10425 C  CB  . SER A 1 1337 ? 132.167 124.546 76.981  1.00 151.14 ? 1337 SER A CB  1 
ATOM   10426 O  OG  . SER A 1 1337 ? 133.246 125.045 76.208  1.00 162.26 ? 1337 SER A OG  1 
ATOM   10427 N  N   . ASN A 1 1338 ? 129.475 123.333 76.808  1.00 139.29 ? 1338 ASN A N   1 
ATOM   10428 C  CA  . ASN A 1 1338 ? 128.392 122.476 77.278  1.00 131.54 ? 1338 ASN A CA  1 
ATOM   10429 C  C   . ASN A 1 1338 ? 128.693 121.784 78.599  1.00 137.18 ? 1338 ASN A C   1 
ATOM   10430 O  O   . ASN A 1 1338 ? 127.758 121.356 79.283  1.00 135.25 ? 1338 ASN A O   1 
ATOM   10431 C  CB  . ASN A 1 1338 ? 128.091 121.404 76.228  1.00 123.45 ? 1338 ASN A CB  1 
ATOM   10432 C  CG  . ASN A 1 1338 ? 127.286 121.935 75.064  1.00 120.40 ? 1338 ASN A CG  1 
ATOM   10433 O  OD1 . ASN A 1 1338 ? 127.631 121.709 73.904  1.00 119.47 ? 1338 ASN A OD1 1 
ATOM   10434 N  ND2 . ASN A 1 1338 ? 126.208 122.645 75.365  1.00 128.99 ? 1338 ASN A ND2 1 
ATOM   10435 N  N   . ILE A 1 1339 ? 129.967 121.658 78.964  1.00 132.83 ? 1339 ILE A N   1 
ATOM   10436 C  CA  . ILE A 1 1339 ? 130.351 120.779 80.060  1.00 124.69 ? 1339 ILE A CA  1 
ATOM   10437 C  C   . ILE A 1 1339 ? 129.857 121.349 81.382  1.00 136.31 ? 1339 ILE A C   1 
ATOM   10438 O  O   . ILE A 1 1339 ? 130.017 122.542 81.666  1.00 143.19 ? 1339 ILE A O   1 
ATOM   10439 C  CB  . ILE A 1 1339 ? 131.873 120.588 80.076  1.00 133.88 ? 1339 ILE A CB  1 
ATOM   10440 C  CG1 . ILE A 1 1339 ? 132.366 120.230 78.673  1.00 125.55 ? 1339 ILE A CG1 1 
ATOM   10441 C  CG2 . ILE A 1 1339 ? 132.259 119.493 81.056  1.00 130.70 ? 1339 ILE A CG2 1 
ATOM   10442 C  CD1 . ILE A 1 1339 ? 133.850 120.427 78.478  1.00 120.87 ? 1339 ILE A CD1 1 
ATOM   10443 N  N   . ILE A 1 1340 ? 129.249 120.493 82.197  1.00 123.21 ? 1340 ILE A N   1 
ATOM   10444 C  CA  . ILE A 1 1340 ? 128.890 120.823 83.569  1.00 124.84 ? 1340 ILE A CA  1 
ATOM   10445 C  C   . ILE A 1 1340 ? 129.838 120.033 84.458  1.00 117.59 ? 1340 ILE A C   1 
ATOM   10446 O  O   . ILE A 1 1340 ? 129.802 118.797 84.472  1.00 114.92 ? 1340 ILE A O   1 
ATOM   10447 C  CB  . ILE A 1 1340 ? 127.431 120.488 83.889  1.00 129.09 ? 1340 ILE A CB  1 
ATOM   10448 C  CG1 . ILE A 1 1340 ? 126.485 121.340 83.046  1.00 133.76 ? 1340 ILE A CG1 1 
ATOM   10449 C  CG2 . ILE A 1 1340 ? 127.163 120.807 85.349  1.00 126.17 ? 1340 ILE A CG2 1 
ATOM   10450 C  CD1 . ILE A 1 1340 ? 125.167 120.643 82.738  1.00 129.00 ? 1340 ILE A CD1 1 
ATOM   10451 N  N   . PHE A 1 1341 ? 130.690 120.735 85.197  1.00 118.40 ? 1341 PHE A N   1 
ATOM   10452 C  CA  . PHE A 1 1341 ? 131.775 120.080 85.914  1.00 108.64 ? 1341 PHE A CA  1 
ATOM   10453 C  C   . PHE A 1 1341 ? 131.358 119.517 87.265  1.00 109.28 ? 1341 PHE A C   1 
ATOM   10454 O  O   . PHE A 1 1341 ? 132.171 118.848 87.911  1.00 105.41 ? 1341 PHE A O   1 
ATOM   10455 C  CB  . PHE A 1 1341 ? 132.928 121.065 86.087  1.00 118.88 ? 1341 PHE A CB  1 
ATOM   10456 C  CG  . PHE A 1 1341 ? 133.297 121.760 84.816  1.00 134.94 ? 1341 PHE A CG  1 
ATOM   10457 C  CD1 . PHE A 1 1341 ? 132.796 123.019 84.534  1.00 148.92 ? 1341 PHE A CD1 1 
ATOM   10458 C  CD2 . PHE A 1 1341 ? 134.091 121.131 83.873  1.00 136.37 ? 1341 PHE A CD2 1 
ATOM   10459 C  CE1 . PHE A 1 1341 ? 133.114 123.656 83.353  1.00 153.53 ? 1341 PHE A CE1 1 
ATOM   10460 C  CE2 . PHE A 1 1341 ? 134.411 121.763 82.688  1.00 142.61 ? 1341 PHE A CE2 1 
ATOM   10461 C  CZ  . PHE A 1 1341 ? 133.921 123.028 82.428  1.00 151.23 ? 1341 PHE A CZ  1 
ATOM   10462 N  N   . GLN A 1 1342 ? 130.125 119.757 87.706  1.00 108.24 ? 1342 GLN A N   1 
ATOM   10463 C  CA  . GLN A 1 1342 ? 129.665 119.111 88.926  1.00 95.62  ? 1342 GLN A CA  1 
ATOM   10464 C  C   . GLN A 1 1342 ? 129.184 117.687 88.676  1.00 85.66  ? 1342 GLN A C   1 
ATOM   10465 O  O   . GLN A 1 1342 ? 129.208 116.867 89.600  1.00 93.60  ? 1342 GLN A O   1 
ATOM   10466 C  CB  . GLN A 1 1342 ? 128.552 119.949 89.565  1.00 125.39 ? 1342 GLN A CB  1 
ATOM   10467 C  CG  . GLN A 1 1342 ? 128.053 119.438 90.904  1.00 129.13 ? 1342 GLN A CG  1 
ATOM   10468 C  CD  . GLN A 1 1342 ? 127.006 120.347 91.515  1.00 134.22 ? 1342 GLN A CD  1 
ATOM   10469 O  OE1 . GLN A 1 1342 ? 126.926 121.531 91.190  1.00 128.96 ? 1342 GLN A OE1 1 
ATOM   10470 N  NE2 . GLN A 1 1342 ? 126.202 119.796 92.413  1.00 130.12 ? 1342 GLN A NE2 1 
ATOM   10471 N  N   . ASN A 1 1343 ? 128.769 117.367 87.447  1.00 91.13  ? 1343 ASN A N   1 
ATOM   10472 C  CA  . ASN A 1 1343 ? 128.248 116.038 87.144  1.00 79.22  ? 1343 ASN A CA  1 
ATOM   10473 C  C   . ASN A 1 1343 ? 129.329 115.056 86.716  1.00 76.87  ? 1343 ASN A C   1 
ATOM   10474 O  O   . ASN A 1 1343 ? 129.122 113.839 86.825  1.00 78.39  ? 1343 ASN A O   1 
ATOM   10475 C  CB  . ASN A 1 1343 ? 127.190 116.094 86.038  1.00 71.00  ? 1343 ASN A CB  1 
ATOM   10476 C  CG  . ASN A 1 1343 ? 126.309 117.314 86.128  1.00 94.73  ? 1343 ASN A CG  1 
ATOM   10477 O  OD1 . ASN A 1 1343 ? 125.849 117.687 87.205  1.00 109.17 ? 1343 ASN A OD1 1 
ATOM   10478 N  ND2 . ASN A 1 1343 ? 126.021 117.913 84.980  1.00 91.84  ? 1343 ASN A ND2 1 
ATOM   10479 N  N   . THR A 1 1344 ? 130.475 115.550 86.243  1.00 70.63  ? 1344 THR A N   1 
ATOM   10480 C  CA  . THR A 1 1344 ? 131.577 114.657 85.908  1.00 67.42  ? 1344 THR A CA  1 
ATOM   10481 C  C   . THR A 1 1344 ? 132.147 113.990 87.151  1.00 79.50  ? 1344 THR A C   1 
ATOM   10482 O  O   . THR A 1 1344 ? 132.616 112.848 87.081  1.00 79.28  ? 1344 THR A O   1 
ATOM   10483 C  CB  . THR A 1 1344 ? 132.673 115.427 85.169  1.00 67.57  ? 1344 THR A CB  1 
ATOM   10484 O  OG1 . THR A 1 1344 ? 133.068 116.561 85.948  1.00 88.97  ? 1344 THR A OG1 1 
ATOM   10485 C  CG2 . THR A 1 1344 ? 132.162 115.910 83.819  1.00 69.76  ? 1344 THR A CG2 1 
ATOM   10486 N  N   . ILE A 1 1345 ? 132.082 114.665 88.300  1.00 74.64  ? 1345 ILE A N   1 
ATOM   10487 C  CA  . ILE A 1 1345 ? 132.526 114.047 89.543  1.00 66.93  ? 1345 ILE A CA  1 
ATOM   10488 C  C   . ILE A 1 1345 ? 131.608 112.887 89.909  1.00 68.52  ? 1345 ILE A C   1 
ATOM   10489 O  O   . ILE A 1 1345 ? 132.070 111.806 90.305  1.00 72.20  ? 1345 ILE A O   1 
ATOM   10490 C  CB  . ILE A 1 1345 ? 132.587 115.101 90.662  1.00 66.20  ? 1345 ILE A CB  1 
ATOM   10491 C  CG1 . ILE A 1 1345 ? 133.574 116.209 90.286  1.00 71.91  ? 1345 ILE A CG1 1 
ATOM   10492 C  CG2 . ILE A 1 1345 ? 132.984 114.456 91.983  1.00 67.44  ? 1345 ILE A CG2 1 
ATOM   10493 C  CD1 . ILE A 1 1345 ? 133.557 117.392 91.229  1.00 100.48 ? 1345 ILE A CD1 1 
ATOM   10494 N  N   . ASN A 1 1346 ? 130.292 113.095 89.792  1.00 62.00  ? 1346 ASN A N   1 
ATOM   10495 C  CA  . ASN A 1 1346 ? 129.352 112.012 90.050  1.00 52.22  ? 1346 ASN A CA  1 
ATOM   10496 C  C   . ASN A 1 1346 ? 129.579 110.860 89.084  1.00 61.96  ? 1346 ASN A C   1 
ATOM   10497 O  O   . ASN A 1 1346 ? 129.534 109.691 89.483  1.00 75.36  ? 1346 ASN A O   1 
ATOM   10498 C  CB  . ASN A 1 1346 ? 127.910 112.515 89.951  1.00 60.08  ? 1346 ASN A CB  1 
ATOM   10499 C  CG  . ASN A 1 1346 ? 127.674 113.782 90.750  1.00 77.93  ? 1346 ASN A CG  1 
ATOM   10500 O  OD1 . ASN A 1 1346 ? 128.489 114.159 91.591  1.00 73.47  ? 1346 ASN A OD1 1 
ATOM   10501 N  ND2 . ASN A 1 1346 ? 126.548 114.441 90.498  1.00 87.98  ? 1346 ASN A ND2 1 
ATOM   10502 N  N   . LEU A 1 1347 ? 129.843 111.167 87.810  1.00 56.49  ? 1347 LEU A N   1 
ATOM   10503 C  CA  . LEU A 1 1347 ? 130.109 110.098 86.853  1.00 62.27  ? 1347 LEU A CA  1 
ATOM   10504 C  C   . LEU A 1 1347 ? 131.370 109.318 87.208  1.00 77.05  ? 1347 LEU A C   1 
ATOM   10505 O  O   . LEU A 1 1347 ? 131.383 108.086 87.125  1.00 72.94  ? 1347 LEU A O   1 
ATOM   10506 C  CB  . LEU A 1 1347 ? 130.218 110.664 85.438  1.00 67.47  ? 1347 LEU A CB  1 
ATOM   10507 C  CG  . LEU A 1 1347 ? 130.373 109.549 84.402  1.00 59.88  ? 1347 LEU A CG  1 
ATOM   10508 C  CD1 . LEU A 1 1347 ? 129.165 108.627 84.446  1.00 66.38  ? 1347 LEU A CD1 1 
ATOM   10509 C  CD2 . LEU A 1 1347 ? 130.583 110.111 83.004  1.00 58.69  ? 1347 LEU A CD2 1 
ATOM   10510 N  N   . GLY A 1 1348 ? 132.434 110.009 87.621  1.00 68.68  ? 1348 GLY A N   1 
ATOM   10511 C  CA  . GLY A 1 1348 ? 133.654 109.305 87.992  1.00 53.32  ? 1348 GLY A CA  1 
ATOM   10512 C  C   . GLY A 1 1348 ? 133.478 108.409 89.204  1.00 60.89  ? 1348 GLY A C   1 
ATOM   10513 O  O   . GLY A 1 1348 ? 133.893 107.242 89.201  1.00 71.74  ? 1348 GLY A O   1 
ATOM   10514 N  N   . VAL A 1 1349 ? 132.822 108.932 90.247  1.00 66.27  ? 1349 VAL A N   1 
ATOM   10515 C  CA  . VAL A 1 1349 ? 132.573 108.124 91.439  1.00 58.29  ? 1349 VAL A CA  1 
ATOM   10516 C  C   . VAL A 1 1349 ? 131.691 106.931 91.095  1.00 57.55  ? 1349 VAL A C   1 
ATOM   10517 O  O   . VAL A 1 1349 ? 131.940 105.804 91.544  1.00 61.01  ? 1349 VAL A O   1 
ATOM   10518 C  CB  . VAL A 1 1349 ? 131.952 108.984 92.558  1.00 51.80  ? 1349 VAL A CB  1 
ATOM   10519 C  CG1 . VAL A 1 1349 ? 131.499 108.105 93.718  1.00 58.63  ? 1349 VAL A CG1 1 
ATOM   10520 C  CG2 . VAL A 1 1349 ? 132.948 110.029 93.042  1.00 58.56  ? 1349 VAL A CG2 1 
ATOM   10521 N  N   . ALA A 1 1350 ? 130.663 107.155 90.276  1.00 59.95  ? 1350 ALA A N   1 
ATOM   10522 C  CA  . ALA A 1 1350 ? 129.742 106.082 89.937  1.00 56.01  ? 1350 ALA A CA  1 
ATOM   10523 C  C   . ALA A 1 1350 ? 130.425 105.011 89.096  1.00 67.76  ? 1350 ALA A C   1 
ATOM   10524 O  O   . ALA A 1 1350 ? 130.154 103.820 89.270  1.00 72.60  ? 1350 ALA A O   1 
ATOM   10525 C  CB  . ALA A 1 1350 ? 128.523 106.651 89.215  1.00 61.13  ? 1350 ALA A CB  1 
ATOM   10526 N  N   . VAL A 1 1351 ? 131.316 105.410 88.182  1.00 61.36  ? 1351 VAL A N   1 
ATOM   10527 C  CA  . VAL A 1 1351 ? 132.049 104.424 87.393  1.00 60.37  ? 1351 VAL A CA  1 
ATOM   10528 C  C   . VAL A 1 1351 ? 132.943 103.580 88.291  1.00 69.31  ? 1351 VAL A C   1 
ATOM   10529 O  O   . VAL A 1 1351 ? 132.957 102.344 88.198  1.00 70.96  ? 1351 VAL A O   1 
ATOM   10530 C  CB  . VAL A 1 1351 ? 132.872 105.118 86.291  1.00 55.14  ? 1351 VAL A CB  1 
ATOM   10531 C  CG1 . VAL A 1 1351 ? 133.884 104.149 85.692  1.00 62.89  ? 1351 VAL A CG1 1 
ATOM   10532 C  CG2 . VAL A 1 1351 ? 131.963 105.668 85.204  1.00 71.63  ? 1351 VAL A CG2 1 
ATOM   10533 N  N   . LEU A 1 1352 ? 133.673 104.231 89.205  1.00 69.45  ? 1352 LEU A N   1 
ATOM   10534 C  CA  . LEU A 1 1352 ? 134.537 103.465 90.100  1.00 61.81  ? 1352 LEU A CA  1 
ATOM   10535 C  C   . LEU A 1 1352 ? 133.733 102.501 90.962  1.00 59.56  ? 1352 LEU A C   1 
ATOM   10536 O  O   . LEU A 1 1352 ? 134.146 101.356 91.179  1.00 62.99  ? 1352 LEU A O   1 
ATOM   10537 C  CB  . LEU A 1 1352 ? 135.361 104.402 90.981  1.00 72.90  ? 1352 LEU A CB  1 
ATOM   10538 C  CG  . LEU A 1 1352 ? 136.360 103.664 91.876  1.00 64.50  ? 1352 LEU A CG  1 
ATOM   10539 C  CD1 . LEU A 1 1352 ? 137.565 103.200 91.074  1.00 62.88  ? 1352 LEU A CD1 1 
ATOM   10540 C  CD2 . LEU A 1 1352 ? 136.784 104.547 93.038  1.00 68.70  ? 1352 LEU A CD2 1 
ATOM   10541 N  N   . ASP A 1 1353 ? 132.567 102.937 91.438  1.00 66.69  ? 1353 ASP A N   1 
ATOM   10542 C  CA  . ASP A 1 1353 ? 131.750 102.080 92.291  1.00 51.10  ? 1353 ASP A CA  1 
ATOM   10543 C  C   . ASP A 1 1353 ? 131.154 100.910 91.514  1.00 56.14  ? 1353 ASP A C   1 
ATOM   10544 O  O   . ASP A 1 1353 ? 131.225 99.759  91.957  1.00 76.40  ? 1353 ASP A O   1 
ATOM   10545 C  CB  . ASP A 1 1353 ? 130.643 102.910 92.946  1.00 65.12  ? 1353 ASP A CB  1 
ATOM   10546 C  CG  . ASP A 1 1353 ? 129.912 102.153 94.042  1.00 99.06  ? 1353 ASP A CG  1 
ATOM   10547 O  OD1 . ASP A 1 1353 ? 129.857 102.662 95.181  1.00 102.03 ? 1353 ASP A OD1 1 
ATOM   10548 O  OD2 . ASP A 1 1353 ? 129.381 101.056 93.773  1.00 100.12 ? 1353 ASP A OD2 1 
ATOM   10549 N  N   . ILE A 1 1354 ? 130.563 101.186 90.349  1.00 63.18  ? 1354 ILE A N   1 
ATOM   10550 C  CA  . ILE A 1 1354 ? 129.849 100.152 89.607  1.00 63.24  ? 1354 ILE A CA  1 
ATOM   10551 C  C   . ILE A 1 1354 ? 130.807 99.124  89.010  1.00 74.85  ? 1354 ILE A C   1 
ATOM   10552 O  O   . ILE A 1 1354 ? 130.505 97.924  88.985  1.00 74.82  ? 1354 ILE A O   1 
ATOM   10553 C  CB  . ILE A 1 1354 ? 128.964 100.804 88.528  1.00 50.80  ? 1354 ILE A CB  1 
ATOM   10554 C  CG1 . ILE A 1 1354 ? 127.844 101.612 89.185  1.00 56.84  ? 1354 ILE A CG1 1 
ATOM   10555 C  CG2 . ILE A 1 1354 ? 128.337 99.743  87.636  1.00 56.12  ? 1354 ILE A CG2 1 
ATOM   10556 C  CD1 . ILE A 1 1354 ? 126.929 102.307 88.203  1.00 65.78  ? 1354 ILE A CD1 1 
ATOM   10557 N  N   . ALA A 1 1355 ? 131.977 99.561  88.531  1.00 63.83  ? 1355 ALA A N   1 
ATOM   10558 C  CA  . ALA A 1 1355 ? 132.902 98.615  87.910  1.00 46.34  ? 1355 ALA A CA  1 
ATOM   10559 C  C   . ALA A 1 1355 ? 133.384 97.550  88.894  1.00 58.31  ? 1355 ALA A C   1 
ATOM   10560 O  O   . ALA A 1 1355 ? 133.449 96.363  88.550  1.00 61.52  ? 1355 ALA A O   1 
ATOM   10561 C  CB  . ALA A 1 1355 ? 134.091 99.363  87.306  1.00 62.99  ? 1355 ALA A CB  1 
ATOM   10562 N  N   . LEU A 1 1356 ? 133.699 97.948  90.128  1.00 66.91  ? 1356 LEU A N   1 
ATOM   10563 C  CA  . LEU A 1 1356 ? 134.264 97.063  91.143  1.00 54.43  ? 1356 LEU A CA  1 
ATOM   10564 C  C   . LEU A 1 1356 ? 133.233 96.586  92.161  1.00 61.77  ? 1356 LEU A C   1 
ATOM   10565 O  O   . LEU A 1 1356 ? 133.579 96.350  93.323  1.00 74.54  ? 1356 LEU A O   1 
ATOM   10566 C  CB  . LEU A 1 1356 ? 135.421 97.754  91.863  1.00 55.04  ? 1356 LEU A CB  1 
ATOM   10567 C  CG  . LEU A 1 1356 ? 136.577 98.264  91.009  1.00 58.62  ? 1356 LEU A CG  1 
ATOM   10568 C  CD1 . LEU A 1 1356 ? 137.645 98.857  91.911  1.00 64.74  ? 1356 LEU A CD1 1 
ATOM   10569 C  CD2 . LEU A 1 1356 ? 137.145 97.139  90.155  1.00 68.58  ? 1356 LEU A CD2 1 
ATOM   10570 N  N   . SER A 1 1357 ? 131.976 96.415  91.751  1.00 66.68  ? 1357 SER A N   1 
ATOM   10571 C  CA  . SER A 1 1357 ? 130.949 96.023  92.711  1.00 62.19  ? 1357 SER A CA  1 
ATOM   10572 C  C   . SER A 1 1357 ? 131.052 94.556  93.117  1.00 71.19  ? 1357 SER A C   1 
ATOM   10573 O  O   . SER A 1 1357 ? 130.644 94.202  94.229  1.00 80.37  ? 1357 SER A O   1 
ATOM   10574 C  CB  . SER A 1 1357 ? 129.561 96.314  92.136  1.00 57.82  ? 1357 SER A CB  1 
ATOM   10575 O  OG  . SER A 1 1357 ? 129.402 95.719  90.860  1.00 67.99  ? 1357 SER A OG  1 
ATOM   10576 N  N   . LEU A 1 1358 ? 131.596 93.692  92.258  1.00 72.87  ? 1358 LEU A N   1 
ATOM   10577 C  CA  . LEU A 1 1358 ? 131.733 92.281  92.600  1.00 70.31  ? 1358 LEU A CA  1 
ATOM   10578 C  C   . LEU A 1 1358 ? 133.164 91.767  92.625  1.00 72.74  ? 1358 LEU A C   1 
ATOM   10579 O  O   . LEU A 1 1358 ? 133.372 90.594  92.962  1.00 77.74  ? 1358 LEU A O   1 
ATOM   10580 C  CB  . LEU A 1 1358 ? 130.911 91.411  91.642  1.00 71.08  ? 1358 LEU A CB  1 
ATOM   10581 C  CG  . LEU A 1 1358 ? 129.443 91.796  91.496  1.00 72.31  ? 1358 LEU A CG  1 
ATOM   10582 C  CD1 . LEU A 1 1358 ? 128.848 91.126  90.269  1.00 80.57  ? 1358 LEU A CD1 1 
ATOM   10583 C  CD2 . LEU A 1 1358 ? 128.676 91.423  92.758  1.00 69.15  ? 1358 LEU A CD2 1 
ATOM   10584 N  N   . ALA A 1 1359 ? 134.155 92.586  92.291  1.00 62.93  ? 1359 ALA A N   1 
ATOM   10585 C  CA  . ALA A 1 1359 ? 135.523 92.095  92.299  1.00 64.50  ? 1359 ALA A CA  1 
ATOM   10586 C  C   . ALA A 1 1359 ? 135.979 91.824  93.729  1.00 75.60  ? 1359 ALA A C   1 
ATOM   10587 O  O   . ALA A 1 1359 ? 135.556 92.485  94.680  1.00 74.36  ? 1359 ALA A O   1 
ATOM   10588 C  CB  . ALA A 1 1359 ? 136.460 93.098  91.626  1.00 69.14  ? 1359 ALA A CB  1 
ATOM   10589 N  N   . LYS A 1 1360 ? 136.856 90.834  93.869  1.00 77.59  ? 1360 LYS A N   1 
ATOM   10590 C  CA  . LYS A 1 1360 ? 137.441 90.474  95.155  1.00 77.25  ? 1360 LYS A CA  1 
ATOM   10591 C  C   . LYS A 1 1360 ? 138.765 91.212  95.305  1.00 85.56  ? 1360 LYS A C   1 
ATOM   10592 O  O   . LYS A 1 1360 ? 139.729 90.933  94.585  1.00 86.47  ? 1360 LYS A O   1 
ATOM   10593 C  CB  . LYS A 1 1360 ? 137.621 88.964  95.272  1.00 82.60  ? 1360 LYS A CB  1 
ATOM   10594 C  CG  . LYS A 1 1360 ? 136.316 88.191  95.177  1.00 96.34  ? 1360 LYS A CG  1 
ATOM   10595 C  CD  . LYS A 1 1360 ? 136.521 86.822  94.559  1.00 122.77 ? 1360 LYS A CD  1 
ATOM   10596 C  CE  . LYS A 1 1360 ? 135.305 85.940  94.776  1.00 121.88 ? 1360 LYS A CE  1 
ATOM   10597 N  NZ  . LYS A 1 1360 ? 134.040 86.673  94.494  1.00 91.77  ? 1360 LYS A NZ  1 
ATOM   10598 N  N   . LEU A 1 1361 ? 138.805 92.154  96.237  1.00 73.31  ? 1361 LEU A N   1 
ATOM   10599 C  CA  . LEU A 1 1361 ? 139.938 93.042  96.421  1.00 70.89  ? 1361 LEU A CA  1 
ATOM   10600 C  C   . LEU A 1 1361 ? 140.947 92.460  97.403  1.00 75.28  ? 1361 LEU A C   1 
ATOM   10601 O  O   . LEU A 1 1361 ? 140.703 91.462  98.084  1.00 80.36  ? 1361 LEU A O   1 
ATOM   10602 C  CB  . LEU A 1 1361 ? 139.464 94.404  96.927  1.00 76.37  ? 1361 LEU A CB  1 
ATOM   10603 C  CG  . LEU A 1 1361 ? 138.780 95.349  95.946  1.00 69.81  ? 1361 LEU A CG  1 
ATOM   10604 C  CD1 . LEU A 1 1361 ? 138.644 96.724  96.577  1.00 72.85  ? 1361 LEU A CD1 1 
ATOM   10605 C  CD2 . LEU A 1 1361 ? 139.585 95.425  94.659  1.00 79.12  ? 1361 LEU A CD2 1 
ATOM   10606 N  N   . SER A 1 1362 ? 142.107 93.104  97.453  1.00 78.77  ? 1362 SER A N   1 
ATOM   10607 C  CA  . SER A 1 1362 ? 143.188 92.728  98.347  1.00 76.33  ? 1362 SER A CA  1 
ATOM   10608 C  C   . SER A 1 1362 ? 143.899 94.006  98.770  1.00 87.95  ? 1362 SER A C   1 
ATOM   10609 O  O   . SER A 1 1362 ? 143.426 95.116  98.510  1.00 94.87  ? 1362 SER A O   1 
ATOM   10610 C  CB  . SER A 1 1362 ? 144.138 91.733  97.670  1.00 86.23  ? 1362 SER A CB  1 
ATOM   10611 O  OG  . SER A 1 1362 ? 145.377 91.666  98.355  1.00 92.23  ? 1362 SER A OG  1 
ATOM   10612 N  N   . SER A 1 1363 ? 145.042 93.850  99.428  1.00 92.55  ? 1363 SER A N   1 
ATOM   10613 C  CA  . SER A 1 1363 ? 145.826 94.993  99.870  1.00 98.51  ? 1363 SER A CA  1 
ATOM   10614 C  C   . SER A 1 1363 ? 146.766 95.522  98.793  1.00 104.90 ? 1363 SER A C   1 
ATOM   10615 O  O   . SER A 1 1363 ? 147.306 96.621  98.953  1.00 95.75  ? 1363 SER A O   1 
ATOM   10616 C  CB  . SER A 1 1363 ? 146.632 94.622  101.120 1.00 102.25 ? 1363 SER A CB  1 
ATOM   10617 O  OG  . SER A 1 1363 ? 145.780 94.327  102.213 1.00 100.25 ? 1363 SER A OG  1 
ATOM   10618 N  N   . ALA A 1 1364 ? 146.959 94.780  97.702  1.00 106.36 ? 1364 ALA A N   1 
ATOM   10619 C  CA  . ALA A 1 1364 ? 147.886 95.161  96.644  1.00 105.70 ? 1364 ALA A CA  1 
ATOM   10620 C  C   . ALA A 1 1364 ? 147.207 95.633  95.364  1.00 104.87 ? 1364 ALA A C   1 
ATOM   10621 O  O   . ALA A 1 1364 ? 147.905 95.910  94.382  1.00 111.65 ? 1364 ALA A O   1 
ATOM   10622 C  CB  . ALA A 1 1364 ? 148.822 93.989  96.324  1.00 110.59 ? 1364 ALA A CB  1 
ATOM   10623 N  N   . SER A 1 1365 ? 145.882 95.736  95.339  1.00 96.61  ? 1365 SER A N   1 
ATOM   10624 C  CA  . SER A 1 1365 ? 145.164 96.090  94.121  1.00 97.49  ? 1365 SER A CA  1 
ATOM   10625 C  C   . SER A 1 1365 ? 144.998 97.600  94.014  1.00 96.41  ? 1365 SER A C   1 
ATOM   10626 O  O   . SER A 1 1365 ? 144.715 98.280  95.004  1.00 94.76  ? 1365 SER A O   1 
ATOM   10627 C  CB  . SER A 1 1365 ? 143.792 95.412  94.084  1.00 77.88  ? 1365 SER A CB  1 
ATOM   10628 O  OG  . SER A 1 1365 ? 143.041 95.718  95.247  1.00 78.43  ? 1365 SER A OG  1 
ATOM   10629 N  N   . ASN A 1 1366 ? 145.174 98.121  92.799  1.00 83.39  ? 1366 ASN A N   1 
ATOM   10630 C  CA  . ASN A 1 1366 ? 144.960 99.533  92.521  1.00 78.42  ? 1366 ASN A CA  1 
ATOM   10631 C  C   . ASN A 1 1366 ? 144.356 99.697  91.133  1.00 84.69  ? 1366 ASN A C   1 
ATOM   10632 O  O   . ASN A 1 1366 ? 144.519 98.845  90.257  1.00 90.13  ? 1366 ASN A O   1 
ATOM   10633 C  CB  . ASN A 1 1366 ? 146.272 100.318 92.624  1.00 92.15  ? 1366 ASN A CB  1 
ATOM   10634 C  CG  . ASN A 1 1366 ? 147.352 99.763  91.711  1.00 110.95 ? 1366 ASN A CG  1 
ATOM   10635 O  OD1 . ASN A 1 1366 ? 147.242 98.641  91.214  1.00 100.41 ? 1366 ASN A OD1 1 
ATOM   10636 N  ND2 . ASN A 1 1366 ? 148.399 100.546 91.485  1.00 117.39 ? 1366 ASN A ND2 1 
ATOM   10637 N  N   . VAL A 1 1367 ? 143.673 100.825 90.937  1.00 80.19  ? 1367 VAL A N   1 
ATOM   10638 C  CA  . VAL A 1 1367 ? 142.898 101.095 89.727  1.00 78.93  ? 1367 VAL A CA  1 
ATOM   10639 C  C   . VAL A 1 1367 ? 143.004 102.579 89.398  1.00 84.00  ? 1367 VAL A C   1 
ATOM   10640 O  O   . VAL A 1 1367 ? 142.789 103.425 90.271  1.00 87.05  ? 1367 VAL A O   1 
ATOM   10641 C  CB  . VAL A 1 1367 ? 141.422 100.682 89.888  1.00 70.41  ? 1367 VAL A CB  1 
ATOM   10642 C  CG1 . VAL A 1 1367 ? 140.558 101.349 88.828  1.00 74.49  ? 1367 VAL A CG1 1 
ATOM   10643 C  CG2 . VAL A 1 1367 ? 141.277 99.173  89.826  1.00 71.18  ? 1367 VAL A CG2 1 
ATOM   10644 N  N   . THR A 1 1368 ? 143.340 102.899 88.147  1.00 77.14  ? 1368 THR A N   1 
ATOM   10645 C  CA  . THR A 1 1368 ? 143.264 104.273 87.666  1.00 75.24  ? 1368 THR A CA  1 
ATOM   10646 C  C   . THR A 1 1368 ? 142.833 104.306 86.204  1.00 81.85  ? 1368 THR A C   1 
ATOM   10647 O  O   . THR A 1 1368 ? 143.296 103.501 85.390  1.00 95.42  ? 1368 THR A O   1 
ATOM   10648 C  CB  . THR A 1 1368 ? 144.601 105.015 87.849  1.00 87.65  ? 1368 THR A CB  1 
ATOM   10649 O  OG1 . THR A 1 1368 ? 144.450 106.378 87.434  1.00 91.42  ? 1368 THR A OG1 1 
ATOM   10650 C  CG2 . THR A 1 1368 ? 145.711 104.368 87.048  1.00 91.75  ? 1368 THR A CG2 1 
ATOM   10651 N  N   . PHE A 1 1369 ? 141.914 105.221 85.883  1.00 71.68  ? 1369 PHE A N   1 
ATOM   10652 C  CA  . PHE A 1 1369 ? 141.404 105.375 84.526  1.00 77.35  ? 1369 PHE A CA  1 
ATOM   10653 C  C   . PHE A 1 1369 ? 141.152 106.858 84.266  1.00 77.11  ? 1369 PHE A C   1 
ATOM   10654 O  O   . PHE A 1 1369 ? 141.356 107.706 85.142  1.00 81.83  ? 1369 PHE A O   1 
ATOM   10655 C  CB  . PHE A 1 1369 ? 140.135 104.542 84.304  1.00 82.73  ? 1369 PHE A CB  1 
ATOM   10656 C  CG  . PHE A 1 1369 ? 138.978 104.953 85.165  1.00 75.33  ? 1369 PHE A CG  1 
ATOM   10657 C  CD1 . PHE A 1 1369 ? 138.839 104.458 86.450  1.00 83.54  ? 1369 PHE A CD1 1 
ATOM   10658 C  CD2 . PHE A 1 1369 ? 138.019 105.828 84.682  1.00 73.51  ? 1369 PHE A CD2 1 
ATOM   10659 C  CE1 . PHE A 1 1369 ? 137.769 104.840 87.243  1.00 80.33  ? 1369 PHE A CE1 1 
ATOM   10660 C  CE2 . PHE A 1 1369 ? 136.949 106.211 85.469  1.00 75.63  ? 1369 PHE A CE2 1 
ATOM   10661 C  CZ  . PHE A 1 1369 ? 136.824 105.716 86.751  1.00 60.38  ? 1369 PHE A CZ  1 
ATOM   10662 N  N   . ARG A 1 1370 ? 140.688 107.170 83.054  1.00 64.45  ? 1370 ARG A N   1 
ATOM   10663 C  CA  . ARG A 1 1370 ? 140.369 108.538 82.667  1.00 60.35  ? 1370 ARG A CA  1 
ATOM   10664 C  C   . ARG A 1 1370 ? 139.164 108.592 81.735  1.00 74.70  ? 1370 ARG A C   1 
ATOM   10665 O  O   . ARG A 1 1370 ? 138.964 107.708 80.898  1.00 87.82  ? 1370 ARG A O   1 
ATOM   10666 C  CB  . ARG A 1 1370 ? 141.572 109.226 82.013  1.00 79.73  ? 1370 ARG A CB  1 
ATOM   10667 C  CG  . ARG A 1 1370 ? 142.315 108.373 81.009  1.00 85.82  ? 1370 ARG A CG  1 
ATOM   10668 C  CD  . ARG A 1 1370 ? 143.476 109.148 80.410  1.00 107.25 ? 1370 ARG A CD  1 
ATOM   10669 N  NE  . ARG A 1 1370 ? 144.535 109.427 81.375  1.00 104.65 ? 1370 ARG A NE  1 
ATOM   10670 C  CZ  . ARG A 1 1370 ? 145.813 109.578 81.047  1.00 104.80 ? 1370 ARG A CZ  1 
ATOM   10671 N  NH1 . ARG A 1 1370 ? 146.186 109.469 79.779  1.00 95.16  ? 1370 ARG A NH1 1 
ATOM   10672 N  NH2 . ARG A 1 1370 ? 146.719 109.837 81.980  1.00 105.12 ? 1370 ARG A NH2 1 
ATOM   10673 N  N   . LEU A 1 1371 ? 138.375 109.654 81.898  1.00 78.37  ? 1371 LEU A N   1 
ATOM   10674 C  CA  . LEU A 1 1371 ? 137.228 109.976 81.048  1.00 88.83  ? 1371 LEU A CA  1 
ATOM   10675 C  C   . LEU A 1 1371 ? 137.637 110.916 79.918  1.00 97.47  ? 1371 LEU A C   1 
ATOM   10676 O  O   . LEU A 1 1371 ? 138.082 112.040 80.174  1.00 95.13  ? 1371 LEU A O   1 
ATOM   10677 C  CB  . LEU A 1 1371 ? 136.113 110.621 81.872  1.00 78.32  ? 1371 LEU A CB  1 
ATOM   10678 C  CG  . LEU A 1 1371 ? 135.577 109.889 83.097  1.00 79.44  ? 1371 LEU A CG  1 
ATOM   10679 C  CD1 . LEU A 1 1371 ? 134.921 110.884 84.034  1.00 68.97  ? 1371 LEU A CD1 1 
ATOM   10680 C  CD2 . LEU A 1 1371 ? 134.583 108.821 82.665  1.00 61.46  ? 1371 LEU A CD2 1 
ATOM   10681 N  N   . MET A 1 1372 ? 137.479 110.461 78.675  1.00 84.85  ? 1372 MET A N   1 
ATOM   10682 C  CA  . MET A 1 1372 ? 137.947 111.204 77.508  1.00 79.49  ? 1372 MET A CA  1 
ATOM   10683 C  C   . MET A 1 1372 ? 136.800 112.001 76.899  1.00 92.66  ? 1372 MET A C   1 
ATOM   10684 O  O   . MET A 1 1372 ? 135.676 111.510 76.788  1.00 99.18  ? 1372 MET A O   1 
ATOM   10685 C  CB  . MET A 1 1372 ? 138.453 110.244 76.424  1.00 95.99  ? 1372 MET A CB  1 
ATOM   10686 C  CG  . MET A 1 1372 ? 139.693 109.392 76.664  1.00 102.31 ? 1372 MET A CG  1 
ATOM   10687 S  SD  . MET A 1 1372 ? 141.245 110.273 76.475  1.00 139.40 ? 1372 MET A SD  1 
ATOM   10688 C  CE  . MET A 1 1372 ? 141.405 110.971 78.086  1.00 93.93  ? 1372 MET A CE  1 
ATOM   10689 N  N   . LEU A 1 1373 ? 137.092 113.236 76.521  1.00 83.84  ? 1373 LEU A N   1 
ATOM   10690 C  CA  . LEU A 1 1373 ? 136.082 114.084 75.925  1.00 78.25  ? 1373 LEU A CA  1 
ATOM   10691 C  C   . LEU A 1 1373 ? 135.937 113.795 74.431  1.00 83.61  ? 1373 LEU A C   1 
ATOM   10692 O  O   . LEU A 1 1373 ? 136.929 113.610 73.718  1.00 90.87  ? 1373 LEU A O   1 
ATOM   10693 C  CB  . LEU A 1 1373 ? 136.406 115.549 76.188  1.00 74.10  ? 1373 LEU A CB  1 
ATOM   10694 C  CG  . LEU A 1 1373 ? 135.284 116.528 75.911  1.00 81.40  ? 1373 LEU A CG  1 
ATOM   10695 C  CD1 . LEU A 1 1373 ? 134.024 116.068 76.629  1.00 92.44  ? 1373 LEU A CD1 1 
ATOM   10696 C  CD2 . LEU A 1 1373 ? 135.703 117.809 76.524  1.00 82.66  ? 1373 LEU A CD2 1 
ATOM   10697 N  N   . ASN A 1 1374 ? 134.692 113.765 73.936  1.00 89.15  ? 1374 ASN A N   1 
ATOM   10698 C  CA  . ASN A 1 1374 ? 134.414 113.574 72.524  1.00 98.42  ? 1374 ASN A CA  1 
ATOM   10699 C  C   . ASN A 1 1374 ? 133.975 114.866 71.845  1.00 103.08 ? 1374 ASN A C   1 
ATOM   10700 O  O   . ASN A 1 1374 ? 133.398 115.761 72.475  1.00 105.71 ? 1374 ASN A O   1 
ATOM   10701 C  CB  . ASN A 1 1374 ? 133.341 112.520 72.260  1.00 103.61 ? 1374 ASN A CB  1 
ATOM   10702 C  CG  . ASN A 1 1374 ? 133.882 111.113 72.314  1.00 114.42 ? 1374 ASN A CG  1 
ATOM   10703 O  OD1 . ASN A 1 1374 ? 135.093 110.897 72.334  1.00 114.69 ? 1374 ASN A OD1 1 
ATOM   10704 N  ND2 . ASN A 1 1374 ? 132.975 110.142 72.228  1.00 114.39 ? 1374 ASN A ND2 1 
ATOM   10705 N  N   . LYS A 1 1375 ? 134.258 114.943 70.548  1.00 110.87 ? 1375 LYS A N   1 
ATOM   10706 C  CA  . LYS A 1 1375 ? 134.043 116.152 69.767  1.00 111.66 ? 1375 LYS A CA  1 
ATOM   10707 C  C   . LYS A 1 1375 ? 132.639 116.270 69.186  1.00 122.83 ? 1375 LYS A C   1 
ATOM   10708 O  O   . LYS A 1 1375 ? 132.217 117.387 68.875  1.00 127.14 ? 1375 LYS A O   1 
ATOM   10709 C  CB  . LYS A 1 1375 ? 135.060 116.221 68.623  1.00 117.93 ? 1375 LYS A CB  1 
ATOM   10710 C  CG  . LYS A 1 1375 ? 136.520 116.263 69.057  1.00 128.89 ? 1375 LYS A CG  1 
ATOM   10711 C  CD  . LYS A 1 1375 ? 136.879 117.600 69.697  1.00 129.14 ? 1375 LYS A CD  1 
ATOM   10712 C  CE  . LYS A 1 1375 ? 136.750 117.582 71.215  1.00 129.48 ? 1375 LYS A CE  1 
ATOM   10713 N  NZ  . LYS A 1 1375 ? 137.203 118.858 71.827  1.00 132.15 ? 1375 LYS A NZ  1 
ATOM   10714 N  N   . CYS A 1 1376 ? 131.911 115.162 69.029  1.00 117.08 ? 1376 CYS A N   1 
ATOM   10715 C  CA  . CYS A 1 1376 ? 130.630 115.236 68.327  1.00 106.14 ? 1376 CYS A CA  1 
ATOM   10716 C  C   . CYS A 1 1376 ? 129.626 116.098 69.084  1.00 110.47 ? 1376 CYS A C   1 
ATOM   10717 O  O   . CYS A 1 1376 ? 128.926 116.921 68.485  1.00 114.02 ? 1376 CYS A O   1 
ATOM   10718 C  CB  . CYS A 1 1376 ? 130.061 113.834 68.103  1.00 94.87  ? 1376 CYS A CB  1 
ATOM   10719 S  SG  . CYS A 1 1376 ? 129.334 113.069 69.574  1.00 126.27 ? 1376 CYS A SG  1 
ATOM   10720 N  N   . CYS A 1 1377 ? 129.548 115.928 70.404  1.00 101.76 ? 1377 CYS A N   1 
ATOM   10721 C  CA  . CYS A 1 1377 ? 128.510 116.573 71.199  1.00 91.46  ? 1377 CYS A CA  1 
ATOM   10722 C  C   . CYS A 1 1377 ? 128.874 117.970 71.686  1.00 92.63  ? 1377 CYS A C   1 
ATOM   10723 O  O   . CYS A 1 1377 ? 127.967 118.754 71.989  1.00 103.83 ? 1377 CYS A O   1 
ATOM   10724 C  CB  . CYS A 1 1377 ? 128.148 115.694 72.400  1.00 78.42  ? 1377 CYS A CB  1 
ATOM   10725 S  SG  . CYS A 1 1377 ? 127.048 114.316 71.987  1.00 86.82  ? 1377 CYS A SG  1 
ATOM   10726 N  N   . THR A 1 1378 ? 130.159 118.309 71.772  1.00 97.45  ? 1378 THR A N   1 
ATOM   10727 C  CA  . THR A 1 1378 ? 130.540 119.604 72.324  1.00 105.50 ? 1378 THR A CA  1 
ATOM   10728 C  C   . THR A 1 1378 ? 130.223 120.732 71.350  1.00 109.96 ? 1378 THR A C   1 
ATOM   10729 O  O   . THR A 1 1378 ? 130.583 120.671 70.169  1.00 100.46 ? 1378 THR A O   1 
ATOM   10730 C  CB  . THR A 1 1378 ? 132.029 119.619 72.670  1.00 103.76 ? 1378 THR A CB  1 
ATOM   10731 O  OG1 . THR A 1 1378 ? 132.387 118.388 73.311  1.00 100.61 ? 1378 THR A OG1 1 
ATOM   10732 C  CG2 . THR A 1 1378 ? 132.347 120.780 73.603  1.00 87.66  ? 1378 THR A CG2 1 
ATOM   10733 N  N   . ARG A 1 1379 ? 129.546 121.766 71.852  1.00 120.54 ? 1379 ARG A N   1 
ATOM   10734 C  CA  . ARG A 1 1379 ? 129.209 122.946 71.070  1.00 125.53 ? 1379 ARG A CA  1 
ATOM   10735 C  C   . ARG A 1 1379 ? 129.668 124.192 71.815  1.00 124.54 ? 1379 ARG A C   1 
ATOM   10736 O  O   . ARG A 1 1379 ? 129.823 124.187 73.040  1.00 122.13 ? 1379 ARG A O   1 
ATOM   10737 C  CB  . ARG A 1 1379 ? 127.704 123.009 70.787  1.00 110.65 ? 1379 ARG A CB  1 
ATOM   10738 C  CG  . ARG A 1 1379 ? 127.200 121.746 70.128  1.00 97.95  ? 1379 ARG A CG  1 
ATOM   10739 C  CD  . ARG A 1 1379 ? 127.808 121.585 68.748  1.00 116.85 ? 1379 ARG A CD  1 
ATOM   10740 N  NE  . ARG A 1 1379 ? 127.711 120.207 68.280  1.00 110.11 ? 1379 ARG A NE  1 
ATOM   10741 C  CZ  . ARG A 1 1379 ? 126.641 119.689 67.688  1.00 112.68 ? 1379 ARG A CZ  1 
ATOM   10742 N  NH1 . ARG A 1 1379 ? 125.563 120.432 67.492  1.00 119.18 ? 1379 ARG A NH1 1 
ATOM   10743 N  NH2 . ARG A 1 1379 ? 126.651 118.421 67.300  1.00 106.63 ? 1379 ARG A NH2 1 
ATOM   10744 N  N   . HIS A 1 1380 ? 129.889 125.269 71.062  1.00 140.89 ? 1380 HIS A N   1 
ATOM   10745 C  CA  . HIS A 1 1380 ? 130.302 126.555 71.617  1.00 151.61 ? 1380 HIS A CA  1 
ATOM   10746 C  C   . HIS A 1 1380 ? 129.106 127.503 71.547  1.00 149.84 ? 1380 HIS A C   1 
ATOM   10747 O  O   . HIS A 1 1380 ? 128.772 127.999 70.465  1.00 148.48 ? 1380 HIS A O   1 
ATOM   10748 C  CB  . HIS A 1 1380 ? 131.499 127.104 70.845  1.00 167.52 ? 1380 HIS A CB  1 
ATOM   10749 C  CG  . HIS A 1 1380 ? 132.151 128.282 71.494  1.00 171.70 ? 1380 HIS A CG  1 
ATOM   10750 N  ND1 . HIS A 1 1380 ? 132.929 128.160 72.625  1.00 170.11 ? 1380 HIS A ND1 1 
ATOM   10751 C  CD2 . HIS A 1 1380 ? 132.133 129.601 71.188  1.00 177.16 ? 1380 HIS A CD2 1 
ATOM   10752 C  CE1 . HIS A 1 1380 ? 133.381 129.350 72.975  1.00 174.56 ? 1380 HIS A CE1 1 
ATOM   10753 N  NE2 . HIS A 1 1380 ? 132.905 130.243 72.126  1.00 181.11 ? 1380 HIS A NE2 1 
ATOM   10754 N  N   . VAL A 1 1381 ? 128.465 127.764 72.683  1.00 157.86 ? 1381 VAL A N   1 
ATOM   10755 C  CA  . VAL A 1 1381 ? 127.177 128.452 72.713  1.00 169.46 ? 1381 VAL A CA  1 
ATOM   10756 C  C   . VAL A 1 1381 ? 127.412 129.942 72.976  1.00 171.30 ? 1381 VAL A C   1 
ATOM   10757 O  O   . VAL A 1 1381 ? 127.690 130.325 74.124  1.00 168.78 ? 1381 VAL A O   1 
ATOM   10758 C  CB  . VAL A 1 1381 ? 126.224 127.819 73.739  1.00 168.39 ? 1381 VAL A CB  1 
ATOM   10759 C  CG1 . VAL A 1 1381 ? 125.913 126.395 73.327  1.00 145.10 ? 1381 VAL A CG1 1 
ATOM   10760 C  CG2 . VAL A 1 1381 ? 126.849 127.763 75.134  1.00 159.22 ? 1381 VAL A CG2 1 
ATOM   10761 N  N   . PRO A 1 1382 ? 127.254 130.811 71.978  1.00 168.26 ? 1382 PRO A N   1 
ATOM   10762 C  CA  . PRO A 1 1382 ? 127.567 132.233 72.171  1.00 163.47 ? 1382 PRO A CA  1 
ATOM   10763 C  C   . PRO A 1 1382 ? 126.606 132.902 73.143  1.00 161.41 ? 1382 PRO A C   1 
ATOM   10764 O  O   . PRO A 1 1382 ? 125.439 132.522 73.264  1.00 166.33 ? 1382 PRO A O   1 
ATOM   10765 C  CB  . PRO A 1 1382 ? 127.437 132.826 70.760  1.00 161.31 ? 1382 PRO A CB  1 
ATOM   10766 C  CG  . PRO A 1 1382 ? 127.311 131.646 69.828  1.00 161.91 ? 1382 PRO A CG  1 
ATOM   10767 C  CD  . PRO A 1 1382 ? 126.718 130.543 70.635  1.00 160.00 ? 1382 PRO A CD  1 
ATOM   10768 N  N   . SER A 1 1383 ? 127.117 133.911 73.847  1.00 159.66 ? 1383 SER A N   1 
ATOM   10769 C  CA  . SER A 1 1383 ? 126.296 134.668 74.786  1.00 171.56 ? 1383 SER A CA  1 
ATOM   10770 C  C   . SER A 1 1383 ? 125.224 135.452 74.036  1.00 171.69 ? 1383 SER A C   1 
ATOM   10771 O  O   . SER A 1 1383 ? 125.523 136.169 73.076  1.00 164.33 ? 1383 SER A O   1 
ATOM   10772 C  CB  . SER A 1 1383 ? 127.179 135.612 75.600  1.00 170.08 ? 1383 SER A CB  1 
ATOM   10773 O  OG  . SER A 1 1383 ? 126.415 136.415 76.477  1.00 158.59 ? 1383 SER A OG  1 
ATOM   10774 N  N   . GLU A 1 1384 ? 123.970 135.317 74.477  1.00 162.88 ? 1384 GLU A N   1 
ATOM   10775 C  CA  . GLU A 1 1384 ? 122.840 135.883 73.752  1.00 156.83 ? 1384 GLU A CA  1 
ATOM   10776 C  C   . GLU A 1 1384 ? 121.749 136.384 74.692  1.00 149.23 ? 1384 GLU A C   1 
ATOM   10777 O  O   . GLU A 1 1384 ? 121.456 135.754 75.711  1.00 153.24 ? 1384 GLU A O   1 
ATOM   10778 C  CB  . GLU A 1 1384 ? 122.259 134.848 72.787  1.00 147.90 ? 1384 GLU A CB  1 
ATOM   10779 C  CG  . GLU A 1 1384 ? 121.343 135.427 71.740  1.00 142.36 ? 1384 GLU A CG  1 
ATOM   10780 C  CD  . GLU A 1 1384 ? 120.994 134.412 70.683  1.00 151.76 ? 1384 GLU A CD  1 
ATOM   10781 O  OE1 . GLU A 1 1384 ? 120.460 134.806 69.624  1.00 152.51 ? 1384 GLU A OE1 1 
ATOM   10782 O  OE2 . GLU A 1 1384 ? 121.260 133.212 70.906  1.00 146.40 ? 1384 GLU A OE2 1 
ATOM   10783 N  N   . TYR A 1 1385 ? 121.156 137.524 74.336  1.00 140.13 ? 1385 TYR A N   1 
ATOM   10784 C  CA  . TYR A 1 1385 ? 120.102 138.189 75.093  1.00 131.00 ? 1385 TYR A CA  1 
ATOM   10785 C  C   . TYR A 1 1385 ? 118.729 137.998 74.452  1.00 114.31 ? 1385 TYR A C   1 
ATOM   10786 O  O   . TYR A 1 1385 ? 118.607 137.795 73.242  1.00 120.86 ? 1385 TYR A O   1 
ATOM   10787 C  CB  . TYR A 1 1385 ? 120.407 139.679 75.245  1.00 141.64 ? 1385 TYR A CB  1 
ATOM   10788 C  CG  . TYR A 1 1385 ? 121.427 139.974 76.317  1.00 145.68 ? 1385 TYR A CG  1 
ATOM   10789 C  CD1 . TYR A 1 1385 ? 121.450 139.242 77.494  1.00 144.72 ? 1385 TYR A CD1 1 
ATOM   10790 C  CD2 . TYR A 1 1385 ? 122.388 140.955 76.141  1.00 156.90 ? 1385 TYR A CD2 1 
ATOM   10791 C  CE1 . TYR A 1 1385 ? 122.374 139.509 78.485  1.00 150.49 ? 1385 TYR A CE1 1 
ATOM   10792 C  CE2 . TYR A 1 1385 ? 123.326 141.223 77.124  1.00 165.18 ? 1385 TYR A CE2 1 
ATOM   10793 C  CZ  . TYR A 1 1385 ? 123.315 140.494 78.292  1.00 155.44 ? 1385 TYR A CZ  1 
ATOM   10794 O  OH  . TYR A 1 1385 ? 124.246 140.754 79.271  1.00 141.53 ? 1385 TYR A OH  1 
ATOM   10795 N  N   . LEU A 1 1386 ? 117.692 138.068 75.289  1.00 103.19 ? 1386 LEU A N   1 
ATOM   10796 C  CA  . LEU A 1 1386 ? 116.298 138.005 74.857  1.00 96.89  ? 1386 LEU A CA  1 
ATOM   10797 C  C   . LEU A 1 1386 ? 115.713 139.406 74.707  1.00 104.88 ? 1386 LEU A C   1 
ATOM   10798 O  O   . LEU A 1 1386 ? 115.853 140.242 75.607  1.00 107.83 ? 1386 LEU A O   1 
ATOM   10799 C  CB  . LEU A 1 1386 ? 115.454 137.208 75.851  1.00 93.84  ? 1386 LEU A CB  1 
ATOM   10800 C  CG  . LEU A 1 1386 ? 115.918 135.800 76.217  1.00 101.96 ? 1386 LEU A CG  1 
ATOM   10801 C  CD1 . LEU A 1 1386 ? 114.825 135.072 76.989  1.00 97.62  ? 1386 LEU A CD1 1 
ATOM   10802 C  CD2 . LEU A 1 1386 ? 116.333 135.018 74.991  1.00 110.75 ? 1386 LEU A CD2 1 
ATOM   10803 N  N   . TYR A 1 1387 ? 115.058 139.655 73.574  1.00 99.94  ? 1387 TYR A N   1 
ATOM   10804 C  CA  . TYR A 1 1387 ? 114.510 140.966 73.235  1.00 102.49 ? 1387 TYR A CA  1 
ATOM   10805 C  C   . TYR A 1 1387 ? 112.982 140.918 73.235  1.00 103.55 ? 1387 TYR A C   1 
ATOM   10806 O  O   . TYR A 1 1387 ? 112.374 140.368 72.311  1.00 107.67 ? 1387 TYR A O   1 
ATOM   10807 C  CB  . TYR A 1 1387 ? 115.049 141.415 71.878  1.00 119.94 ? 1387 TYR A CB  1 
ATOM   10808 C  CG  . TYR A 1 1387 ? 114.335 142.605 71.286  1.00 121.83 ? 1387 TYR A CG  1 
ATOM   10809 C  CD1 . TYR A 1 1387 ? 114.407 143.853 71.887  1.00 123.51 ? 1387 TYR A CD1 1 
ATOM   10810 C  CD2 . TYR A 1 1387 ? 113.591 142.479 70.122  1.00 124.52 ? 1387 TYR A CD2 1 
ATOM   10811 C  CE1 . TYR A 1 1387 ? 113.754 144.943 71.345  1.00 130.55 ? 1387 TYR A CE1 1 
ATOM   10812 C  CE2 . TYR A 1 1387 ? 112.934 143.562 69.572  1.00 129.37 ? 1387 TYR A CE2 1 
ATOM   10813 C  CZ  . TYR A 1 1387 ? 113.020 144.792 70.188  1.00 135.04 ? 1387 TYR A CZ  1 
ATOM   10814 O  OH  . TYR A 1 1387 ? 112.366 145.875 69.643  1.00 135.34 ? 1387 TYR A OH  1 
ATOM   10815 N  N   . PHE A 1 1388 ? 112.366 141.496 74.269  1.00 108.67 ? 1388 PHE A N   1 
ATOM   10816 C  CA  . PHE A 1 1388 ? 110.916 141.676 74.330  1.00 105.39 ? 1388 PHE A CA  1 
ATOM   10817 C  C   . PHE A 1 1388 ? 110.536 142.999 73.673  1.00 118.78 ? 1388 PHE A C   1 
ATOM   10818 O  O   . PHE A 1 1388 ? 111.002 144.061 74.099  1.00 130.63 ? 1388 PHE A O   1 
ATOM   10819 C  CB  . PHE A 1 1388 ? 110.413 141.659 75.774  1.00 105.45 ? 1388 PHE A CB  1 
ATOM   10820 C  CG  . PHE A 1 1388 ? 110.384 140.296 76.393  1.00 99.37  ? 1388 PHE A CG  1 
ATOM   10821 C  CD1 . PHE A 1 1388 ? 111.318 139.940 77.351  1.00 93.95  ? 1388 PHE A CD1 1 
ATOM   10822 C  CD2 . PHE A 1 1388 ? 109.431 139.365 76.016  1.00 96.86  ? 1388 PHE A CD2 1 
ATOM   10823 C  CE1 . PHE A 1 1388 ? 111.299 138.687 77.927  1.00 76.94  ? 1388 PHE A CE1 1 
ATOM   10824 C  CE2 . PHE A 1 1388 ? 109.409 138.106 76.587  1.00 95.29  ? 1388 PHE A CE2 1 
ATOM   10825 C  CZ  . PHE A 1 1388 ? 110.345 137.768 77.545  1.00 85.49  ? 1388 PHE A CZ  1 
ATOM   10826 N  N   . ASP A 1 1389 ? 109.688 142.942 72.647  1.00 120.48 ? 1389 ASP A N   1 
ATOM   10827 C  CA  . ASP A 1 1389 ? 109.323 144.138 71.899  1.00 128.56 ? 1389 ASP A CA  1 
ATOM   10828 C  C   . ASP A 1 1389 ? 108.019 144.769 72.380  1.00 136.29 ? 1389 ASP A C   1 
ATOM   10829 O  O   . ASP A 1 1389 ? 107.551 145.732 71.763  1.00 135.43 ? 1389 ASP A O   1 
ATOM   10830 C  CB  . ASP A 1 1389 ? 109.205 143.822 70.408  1.00 132.57 ? 1389 ASP A CB  1 
ATOM   10831 C  CG  . ASP A 1 1389 ? 107.914 143.102 70.068  1.00 144.86 ? 1389 ASP A CG  1 
ATOM   10832 O  OD1 . ASP A 1 1389 ? 107.636 142.050 70.678  1.00 142.15 ? 1389 ASP A OD1 1 
ATOM   10833 O  OD2 . ASP A 1 1389 ? 107.168 143.605 69.201  1.00 137.66 ? 1389 ASP A OD2 1 
ATOM   10834 N  N   . LYS A 1 1390 ? 107.428 144.269 73.469  1.00 139.14 ? 1390 LYS A N   1 
ATOM   10835 C  CA  . LYS A 1 1390 ? 106.123 144.769 73.891  1.00 138.58 ? 1390 LYS A CA  1 
ATOM   10836 C  C   . LYS A 1 1390 ? 105.858 144.378 75.342  1.00 137.38 ? 1390 LYS A C   1 
ATOM   10837 O  O   . LYS A 1 1390 ? 105.940 143.193 75.687  1.00 135.19 ? 1390 LYS A O   1 
ATOM   10838 C  CB  . LYS A 1 1390 ? 105.029 144.207 72.979  1.00 137.85 ? 1390 LYS A CB  1 
ATOM   10839 C  CG  . LYS A 1 1390 ? 103.624 144.701 73.268  1.00 143.57 ? 1390 LYS A CG  1 
ATOM   10840 C  CD  . LYS A 1 1390 ? 103.521 146.198 73.046  1.00 145.73 ? 1390 LYS A CD  1 
ATOM   10841 C  CE  . LYS A 1 1390 ? 103.727 146.539 71.580  1.00 138.94 ? 1390 LYS A CE  1 
ATOM   10842 N  NZ  . LYS A 1 1390 ? 102.606 146.033 70.744  1.00 135.56 ? 1390 LYS A NZ  1 
ATOM   10843 N  N   . PRO A 1 1391 ? 105.530 145.329 76.215  1.00 130.73 ? 1391 PRO A N   1 
ATOM   10844 C  CA  . PRO A 1 1391 ? 105.197 144.973 77.600  1.00 127.78 ? 1391 PRO A CA  1 
ATOM   10845 C  C   . PRO A 1 1391 ? 103.825 144.328 77.747  1.00 129.49 ? 1391 PRO A C   1 
ATOM   10846 O  O   . PRO A 1 1391 ? 102.946 144.433 76.888  1.00 125.82 ? 1391 PRO A O   1 
ATOM   10847 C  CB  . PRO A 1 1391 ? 105.258 146.312 78.347  1.00 124.05 ? 1391 PRO A CB  1 
ATOM   10848 C  CG  . PRO A 1 1391 ? 105.313 147.383 77.301  1.00 132.97 ? 1391 PRO A CG  1 
ATOM   10849 C  CD  . PRO A 1 1391 ? 105.336 146.762 75.941  1.00 125.47 ? 1391 PRO A CD  1 
ATOM   10850 N  N   . LEU A 1 1392 ? 103.673 143.637 78.875  1.00 129.01 ? 1392 LEU A N   1 
ATOM   10851 C  CA  . LEU A 1 1392 ? 102.454 142.905 79.201  1.00 127.01 ? 1392 LEU A CA  1 
ATOM   10852 C  C   . LEU A 1 1392 ? 101.282 143.866 79.368  1.00 129.09 ? 1392 LEU A C   1 
ATOM   10853 O  O   . LEU A 1 1392 ? 101.367 144.840 80.122  1.00 134.31 ? 1392 LEU A O   1 
ATOM   10854 C  CB  . LEU A 1 1392 ? 102.657 142.087 80.474  1.00 116.50 ? 1392 LEU A CB  1 
ATOM   10855 C  CG  . LEU A 1 1392 ? 101.427 141.361 81.016  1.00 111.81 ? 1392 LEU A CG  1 
ATOM   10856 C  CD1 . LEU A 1 1392 ? 100.772 140.516 79.929  1.00 126.40 ? 1392 LEU A CD1 1 
ATOM   10857 C  CD2 . LEU A 1 1392 ? 101.810 140.504 82.211  1.00 99.62  ? 1392 LEU A CD2 1 
ATOM   10858 N  N   . ASP A 1 1393 ? 100.184 143.600 78.665  1.00 127.47 ? 1393 ASP A N   1 
ATOM   10859 C  CA  . ASP A 1 1393 ? 98.996  144.447 78.747  1.00 144.68 ? 1393 ASP A CA  1 
ATOM   10860 C  C   . ASP A 1 1393 ? 97.824  143.694 79.379  1.00 146.94 ? 1393 ASP A C   1 
ATOM   10861 O  O   . ASP A 1 1393 ? 96.858  143.325 78.713  1.00 142.18 ? 1393 ASP A O   1 
ATOM   10862 C  CB  . ASP A 1 1393 ? 98.655  144.985 77.335  1.00 153.56 ? 1393 ASP A CB  1 
ATOM   10863 C  CG  . ASP A 1 1393 ? 98.350  143.876 76.334  1.00 161.21 ? 1393 ASP A CG  1 
ATOM   10864 O  OD1 . ASP A 1 1393 ? 98.451  142.682 76.691  1.00 147.71 ? 1393 ASP A OD1 1 
ATOM   10865 O  OD2 . ASP A 1 1393 ? 97.998  144.204 75.182  1.00 168.46 ? 1393 ASP A OD2 1 
ATOM   10866 N  N   . VAL A 1 1394 ? 97.873  143.569 80.706  1.00 134.48 ? 1394 VAL A N   1 
ATOM   10867 C  CA  . VAL A 1 1394 ? 96.815  142.946 81.503  1.00 121.53 ? 1394 VAL A CA  1 
ATOM   10868 C  C   . VAL A 1 1394 ? 96.943  143.496 82.918  1.00 123.26 ? 1394 VAL A C   1 
ATOM   10869 O  O   . VAL A 1 1394 ? 98.050  143.654 83.439  1.00 120.13 ? 1394 VAL A O   1 
ATOM   10870 C  CB  . VAL A 1 1394 ? 96.901  141.396 81.495  1.00 114.13 ? 1394 VAL A CB  1 
ATOM   10871 C  CG1 . VAL A 1 1394 ? 96.071  140.809 82.627  1.00 111.66 ? 1394 VAL A CG1 1 
ATOM   10872 C  CG2 . VAL A 1 1394 ? 96.415  140.800 80.180  1.00 114.12 ? 1394 VAL A CG2 1 
ATOM   10873 N  N   . ASP A 1 1395 ? 95.801  143.813 83.527  1.00 127.75 ? 1395 ASP A N   1 
ATOM   10874 C  CA  . ASP A 1 1395 ? 95.744  144.312 84.901  1.00 126.12 ? 1395 ASP A CA  1 
ATOM   10875 C  C   . ASP A 1 1395 ? 95.866  143.142 85.875  1.00 131.19 ? 1395 ASP A C   1 
ATOM   10876 O  O   . ASP A 1 1395 ? 94.878  142.472 86.183  1.00 126.33 ? 1395 ASP A O   1 
ATOM   10877 C  CB  . ASP A 1 1395 ? 94.457  145.100 85.120  1.00 122.85 ? 1395 ASP A CB  1 
ATOM   10878 C  CG  . ASP A 1 1395 ? 94.387  145.734 86.491  1.00 120.39 ? 1395 ASP A CG  1 
ATOM   10879 O  OD1 . ASP A 1 1395 ? 95.333  146.462 86.857  1.00 117.07 ? 1395 ASP A OD1 1 
ATOM   10880 O  OD2 . ASP A 1 1395 ? 93.383  145.514 87.199  1.00 120.99 ? 1395 ASP A OD2 1 
ATOM   10881 N  N   . LEU A 1 1396 ? 97.080  142.892 86.370  1.00 128.38 ? 1396 LEU A N   1 
ATOM   10882 C  CA  . LEU A 1 1396 ? 97.333  141.881 87.395  1.00 118.19 ? 1396 LEU A CA  1 
ATOM   10883 C  C   . LEU A 1 1396 ? 97.179  142.395 88.823  1.00 107.59 ? 1396 LEU A C   1 
ATOM   10884 O  O   . LEU A 1 1396 ? 97.475  141.651 89.764  1.00 107.23 ? 1396 LEU A O   1 
ATOM   10885 C  CB  . LEU A 1 1396 ? 98.721  141.250 87.235  1.00 103.34 ? 1396 LEU A CB  1 
ATOM   10886 C  CG  . LEU A 1 1396 ? 98.981  140.270 86.084  1.00 109.47 ? 1396 LEU A CG  1 
ATOM   10887 C  CD1 . LEU A 1 1396 ? 98.891  140.912 84.714  1.00 133.41 ? 1396 LEU A CD1 1 
ATOM   10888 C  CD2 . LEU A 1 1396 ? 100.318 139.567 86.274  1.00 113.46 ? 1396 LEU A CD2 1 
ATOM   10889 N  N   . ASN A 1 1397 ? 96.740  143.637 89.018  1.00 111.22 ? 1397 ASN A N   1 
ATOM   10890 C  CA  . ASN A 1 1397 ? 96.599  144.190 90.363  1.00 112.37 ? 1397 ASN A CA  1 
ATOM   10891 C  C   . ASN A 1 1397 ? 95.149  144.001 90.798  1.00 114.80 ? 1397 ASN A C   1 
ATOM   10892 O  O   . ASN A 1 1397 ? 94.311  144.899 90.702  1.00 116.74 ? 1397 ASN A O   1 
ATOM   10893 C  CB  . ASN A 1 1397 ? 97.011  145.660 90.397  1.00 115.70 ? 1397 ASN A CB  1 
ATOM   10894 C  CG  . ASN A 1 1397 ? 97.192  146.185 91.810  1.00 121.05 ? 1397 ASN A CG  1 
ATOM   10895 O  OD1 . ASN A 1 1397 ? 96.672  145.613 92.768  1.00 120.92 ? 1397 ASN A OD1 1 
ATOM   10896 N  ND2 . ASN A 1 1397 ? 97.922  147.286 91.946  1.00 128.94 ? 1397 ASN A ND2 1 
ATOM   10897 N  N   . LYS A 1 1398 ? 94.856  142.787 91.283  1.00 106.00 ? 1398 LYS A N   1 
ATOM   10898 C  CA  . LYS A 1 1398 ? 93.510  142.460 91.733  1.00 95.61  ? 1398 LYS A CA  1 
ATOM   10899 C  C   . LYS A 1 1398 ? 93.468  141.660 93.034  1.00 86.57  ? 1398 LYS A C   1 
ATOM   10900 O  O   . LYS A 1 1398 ? 92.384  141.224 93.429  1.00 85.12  ? 1398 LYS A O   1 
ATOM   10901 C  CB  . LYS A 1 1398 ? 92.788  141.672 90.632  1.00 90.60  ? 1398 LYS A CB  1 
ATOM   10902 C  CG  . LYS A 1 1398 ? 92.402  142.508 89.434  1.00 109.72 ? 1398 LYS A CG  1 
ATOM   10903 C  CD  . LYS A 1 1398 ? 91.636  141.715 88.404  1.00 123.08 ? 1398 LYS A CD  1 
ATOM   10904 C  CE  . LYS A 1 1398 ? 91.198  142.629 87.281  1.00 131.90 ? 1398 LYS A CE  1 
ATOM   10905 N  NZ  . LYS A 1 1398 ? 90.256  143.665 87.790  1.00 131.12 ? 1398 LYS A NZ  1 
ATOM   10906 N  N   . TYR A 1 1399 ? 94.598  141.450 93.715  1.00 88.06  ? 1399 TYR A N   1 
ATOM   10907 C  CA  . TYR A 1 1399 ? 94.721  140.516 94.836  1.00 88.00  ? 1399 TYR A CA  1 
ATOM   10908 C  C   . TYR A 1 1399 ? 95.197  141.237 96.083  1.00 99.49  ? 1399 TYR A C   1 
ATOM   10909 O  O   . TYR A 1 1399 ? 95.820  140.654 96.969  1.00 103.19 ? 1399 TYR A O   1 
ATOM   10910 C  CB  . TYR A 1 1399 ? 95.673  139.378 94.506  1.00 85.53  ? 1399 TYR A CB  1 
ATOM   10911 C  CG  . TYR A 1 1399 ? 95.432  138.734 93.183  1.00 87.22  ? 1399 TYR A CG  1 
ATOM   10912 C  CD1 . TYR A 1 1399 ? 94.509  137.719 93.068  1.00 95.34  ? 1399 TYR A CD1 1 
ATOM   10913 C  CD2 . TYR A 1 1399 ? 96.145  139.111 92.050  1.00 89.40  ? 1399 TYR A CD2 1 
ATOM   10914 C  CE1 . TYR A 1 1399 ? 94.272  137.084 91.866  1.00 89.85  ? 1399 TYR A CE1 1 
ATOM   10915 C  CE2 . TYR A 1 1399 ? 95.918  138.483 90.839  1.00 86.81  ? 1399 TYR A CE2 1 
ATOM   10916 C  CZ  . TYR A 1 1399 ? 94.980  137.470 90.753  1.00 88.49  ? 1399 TYR A CZ  1 
ATOM   10917 O  OH  . TYR A 1 1399 ? 94.754  136.849 89.545  1.00 86.94  ? 1399 TYR A OH  1 
ATOM   10918 N  N   . MET A 1 1400 ? 94.878  142.505 96.145  1.00 102.58 ? 1400 MET A N   1 
ATOM   10919 C  CA  . MET A 1 1400 ? 95.226  143.361 97.252  1.00 104.42 ? 1400 MET A CA  1 
ATOM   10920 C  C   . MET A 1 1400 ? 94.541  142.952 98.526  1.00 106.05 ? 1400 MET A C   1 
ATOM   10921 O  O   . MET A 1 1400 ? 94.952  143.384 99.608  1.00 106.02 ? 1400 MET A O   1 
ATOM   10922 C  CB  . MET A 1 1400 ? 94.706  144.725 96.895  1.00 116.17 ? 1400 MET A CB  1 
ATOM   10923 C  CG  . MET A 1 1400 ? 95.386  145.379 95.738  1.00 122.41 ? 1400 MET A CG  1 
ATOM   10924 S  SD  . MET A 1 1400 ? 94.386  146.858 95.594  1.00 159.14 ? 1400 MET A SD  1 
ATOM   10925 C  CE  . MET A 1 1400 ? 92.834  146.062 95.049  1.00 114.37 ? 1400 MET A CE  1 
ATOM   10926 N  N   . ASP A 1 1401 ? 93.545  142.112 98.416  1.00 108.44 ? 1401 ASP A N   1 
ATOM   10927 C  CA  . ASP A 1 1401 ? 92.796  141.595 99.541  1.00 103.62 ? 1401 ASP A CA  1 
ATOM   10928 C  C   . ASP A 1 1401 ? 93.301  140.287 100.111 1.00 102.83 ? 1401 ASP A C   1 
ATOM   10929 O  O   . ASP A 1 1401 ? 93.207  140.062 101.327 1.00 108.45 ? 1401 ASP A O   1 
ATOM   10930 C  CB  . ASP A 1 1401 ? 91.414  141.355 98.971  1.00 117.88 ? 1401 ASP A CB  1 
ATOM   10931 C  CG  . ASP A 1 1401 ? 90.723  142.633 98.557  1.00 138.77 ? 1401 ASP A CG  1 
ATOM   10932 O  OD1 . ASP A 1 1401 ? 90.968  143.730 99.114  1.00 134.41 ? 1401 ASP A OD1 1 
ATOM   10933 O  OD2 . ASP A 1 1401 ? 89.846  142.484 97.683  1.00 149.01 ? 1401 ASP A OD2 1 
ATOM   10934 N  N   . ASN A 1 1402 ? 93.867  139.454 99.246  1.00 98.27  ? 1402 ASN A N   1 
ATOM   10935 C  CA  . ASN A 1 1402 ? 94.436  138.174 99.636  1.00 94.32  ? 1402 ASN A CA  1 
ATOM   10936 C  C   . ASN A 1 1402 ? 95.747  138.353 100.376 1.00 104.87 ? 1402 ASN A C   1 
ATOM   10937 O  O   . ASN A 1 1402 ? 96.711  138.895 99.826  1.00 110.61 ? 1402 ASN A O   1 
ATOM   10938 C  CB  . ASN A 1 1402 ? 94.644  137.286 98.409  1.00 91.20  ? 1402 ASN A CB  1 
ATOM   10939 C  CG  . ASN A 1 1402 ? 93.372  136.578 97.955  1.00 87.67  ? 1402 ASN A CG  1 
ATOM   10940 O  OD1 . ASN A 1 1402 ? 92.843  136.869 96.885  1.00 91.65  ? 1402 ASN A OD1 1 
ATOM   10941 N  ND2 . ASN A 1 1402 ? 92.878  135.653 98.769  1.00 100.27 ? 1402 ASN A ND2 1 
ATOM   10942 N  N   . GLU A 1 1403 ? 95.797  137.869 101.614 1.00 103.92 ? 1403 GLU A N   1 
ATOM   10943 C  CA  . GLU A 1 1403 ? 97.084  137.727 102.275 1.00 111.20 ? 1403 GLU A CA  1 
ATOM   10944 C  C   . GLU A 1 1403 ? 97.791  136.446 101.860 1.00 106.68 ? 1403 GLU A C   1 
ATOM   10945 O  O   . GLU A 1 1403 ? 98.974  136.283 102.172 1.00 105.15 ? 1403 GLU A O   1 
ATOM   10946 C  CB  . GLU A 1 1403 ? 96.917  137.757 103.796 1.00 114.99 ? 1403 GLU A CB  1 
ATOM   10947 C  CG  . GLU A 1 1403 ? 96.040  136.654 104.360 1.00 129.61 ? 1403 GLU A CG  1 
ATOM   10948 C  CD  . GLU A 1 1403 ? 94.744  137.180 104.937 1.00 139.58 ? 1403 GLU A CD  1 
ATOM   10949 O  OE1 . GLU A 1 1403 ? 94.081  137.996 104.265 1.00 127.53 ? 1403 GLU A OE1 1 
ATOM   10950 O  OE2 . GLU A 1 1403 ? 94.396  136.787 106.070 1.00 125.15 ? 1403 GLU A OE2 1 
ATOM   10951 N  N   . LEU A 1 1404 ? 97.091  135.538 101.173 1.00 103.91 ? 1404 LEU A N   1 
ATOM   10952 C  CA  . LEU A 1 1404 ? 97.753  134.361 100.625 1.00 105.98 ? 1404 LEU A CA  1 
ATOM   10953 C  C   . LEU A 1 1404 ? 98.659  134.735 99.461  1.00 111.88 ? 1404 LEU A C   1 
ATOM   10954 O  O   . LEU A 1 1404 ? 99.687  134.085 99.241  1.00 113.10 ? 1404 LEU A O   1 
ATOM   10955 C  CB  . LEU A 1 1404 ? 96.708  133.327 100.190 1.00 106.27 ? 1404 LEU A CB  1 
ATOM   10956 C  CG  . LEU A 1 1404 ? 97.143  131.902 99.821  1.00 133.41 ? 1404 LEU A CG  1 
ATOM   10957 C  CD1 . LEU A 1 1404 ? 95.974  130.949 99.992  1.00 128.43 ? 1404 LEU A CD1 1 
ATOM   10958 C  CD2 . LEU A 1 1404 ? 97.670  131.804 98.391  1.00 129.71 ? 1404 LEU A CD2 1 
ATOM   10959 N  N   . VAL A 1 1405 ? 98.310  135.787 98.725  1.00 109.75 ? 1405 VAL A N   1 
ATOM   10960 C  CA  . VAL A 1 1405 ? 99.018  136.177 97.517  1.00 98.38  ? 1405 VAL A CA  1 
ATOM   10961 C  C   . VAL A 1 1405 ? 99.798  137.470 97.715  1.00 100.32 ? 1405 VAL A C   1 
ATOM   10962 O  O   . VAL A 1 1405 ? 100.908 137.615 97.198  1.00 109.74 ? 1405 VAL A O   1 
ATOM   10963 C  CB  . VAL A 1 1405 ? 98.039  136.301 96.328  1.00 101.89 ? 1405 VAL A CB  1 
ATOM   10964 C  CG1 . VAL A 1 1405 ? 98.799  136.466 95.018  1.00 86.32  ? 1405 VAL A CG1 1 
ATOM   10965 C  CG2 . VAL A 1 1405 ? 97.120  135.089 96.267  1.00 107.66 ? 1405 VAL A CG2 1 
ATOM   10966 N  N   . TYR A 1 1406 ? 99.241  138.412 98.468  1.00 96.22  ? 1406 TYR A N   1 
ATOM   10967 C  CA  . TYR A 1 1406 ? 99.750  139.771 98.536  1.00 90.82  ? 1406 TYR A CA  1 
ATOM   10968 C  C   . TYR A 1 1406 ? 100.333 140.085 99.907  1.00 106.25 ? 1406 TYR A C   1 
ATOM   10969 O  O   . TYR A 1 1406 ? 99.864  139.592 100.936 1.00 113.17 ? 1406 TYR A O   1 
ATOM   10970 C  CB  . TYR A 1 1406 ? 98.642  140.777 98.218  1.00 99.53  ? 1406 TYR A CB  1 
ATOM   10971 C  CG  . TYR A 1 1406 ? 99.142  142.142 97.820  1.00 109.03 ? 1406 TYR A CG  1 
ATOM   10972 C  CD1 . TYR A 1 1406 ? 99.759  142.353 96.597  1.00 114.64 ? 1406 TYR A CD1 1 
ATOM   10973 C  CD2 . TYR A 1 1406 ? 98.993  143.224 98.676  1.00 106.68 ? 1406 TYR A CD2 1 
ATOM   10974 C  CE1 . TYR A 1 1406 ? 100.220 143.608 96.239  1.00 114.07 ? 1406 TYR A CE1 1 
ATOM   10975 C  CE2 . TYR A 1 1406 ? 99.447  144.478 98.328  1.00 113.63 ? 1406 TYR A CE2 1 
ATOM   10976 C  CZ  . TYR A 1 1406 ? 100.060 144.666 97.109  1.00 115.69 ? 1406 TYR A CZ  1 
ATOM   10977 O  OH  . TYR A 1 1406 ? 100.512 145.918 96.762  1.00 117.54 ? 1406 TYR A OH  1 
ATOM   10978 N  N   . ASP A 1 1407 ? 101.369 140.917 99.896  1.00 106.36 ? 1407 ASP A N   1 
ATOM   10979 C  CA  . ASP A 1 1407 ? 101.997 141.441 101.101 1.00 115.49 ? 1407 ASP A CA  1 
ATOM   10980 C  C   . ASP A 1 1407 ? 101.748 142.944 101.129 1.00 121.56 ? 1407 ASP A C   1 
ATOM   10981 O  O   . ASP A 1 1407 ? 102.365 143.693 100.364 1.00 125.02 ? 1407 ASP A O   1 
ATOM   10982 C  CB  . ASP A 1 1407 ? 103.491 141.125 101.133 1.00 130.88 ? 1407 ASP A CB  1 
ATOM   10983 C  CG  . ASP A 1 1407 ? 104.066 141.172 102.534 1.00 134.33 ? 1407 ASP A CG  1 
ATOM   10984 O  OD1 . ASP A 1 1407 ? 103.442 141.802 103.413 1.00 137.19 ? 1407 ASP A OD1 1 
ATOM   10985 O  OD2 . ASP A 1 1407 ? 105.143 140.581 102.756 1.00 129.35 ? 1407 ASP A OD2 1 
ATOM   10986 N  N   . ASN A 1 1408 ? 100.850 143.385 102.012 1.00 115.85 ? 1408 ASN A N   1 
ATOM   10987 C  CA  . ASN A 1 1408 ? 100.438 144.785 101.994 1.00 106.61 ? 1408 ASN A CA  1 
ATOM   10988 C  C   . ASN A 1 1408 ? 101.542 145.668 102.557 1.00 119.53 ? 1408 ASN A C   1 
ATOM   10989 O  O   . ASN A 1 1408 ? 101.777 146.775 102.059 1.00 126.21 ? 1408 ASN A O   1 
ATOM   10990 C  CB  . ASN A 1 1408 ? 99.140  144.972 102.780 1.00 111.95 ? 1408 ASN A CB  1 
ATOM   10991 C  CG  . ASN A 1 1408 ? 98.532  146.354 102.590 1.00 130.71 ? 1408 ASN A CG  1 
ATOM   10992 O  OD1 . ASN A 1 1408 ? 99.085  147.200 101.885 1.00 116.51 ? 1408 ASN A OD1 1 
ATOM   10993 N  ND2 . ASN A 1 1408 ? 97.391  146.590 103.227 1.00 137.80 ? 1408 ASN A ND2 1 
ATOM   10994 N  N   . ASP A 1 1409 ? 102.244 145.187 103.581 1.00 126.04 ? 1409 ASP A N   1 
ATOM   10995 C  CA  . ASP A 1 1409 ? 103.394 145.883 104.154 1.00 134.98 ? 1409 ASP A CA  1 
ATOM   10996 C  C   . ASP A 1 1409 ? 104.545 144.890 104.071 1.00 141.76 ? 1409 ASP A C   1 
ATOM   10997 O  O   . ASP A 1 1409 ? 104.782 144.104 105.004 1.00 149.40 ? 1409 ASP A O   1 
ATOM   10998 C  CB  . ASP A 1 1409 ? 103.133 146.347 105.585 1.00 146.37 ? 1409 ASP A CB  1 
ATOM   10999 C  CG  . ASP A 1 1409 ? 104.393 146.833 106.280 1.00 157.23 ? 1409 ASP A CG  1 
ATOM   11000 O  OD1 . ASP A 1 1409 ? 105.347 147.237 105.581 1.00 151.70 ? 1409 ASP A OD1 1 
ATOM   11001 O  OD2 . ASP A 1 1409 ? 104.424 146.825 107.527 1.00 156.89 ? 1409 ASP A OD2 1 
ATOM   11002 N  N   . PRO A 1 1410 ? 105.275 144.885 102.955 1.00 136.87 ? 1410 PRO A N   1 
ATOM   11003 C  CA  . PRO A 1 1410 ? 106.286 143.841 102.714 1.00 137.10 ? 1410 PRO A CA  1 
ATOM   11004 C  C   . PRO A 1 1410 ? 107.429 143.841 103.711 1.00 143.82 ? 1410 PRO A C   1 
ATOM   11005 O  O   . PRO A 1 1410 ? 107.978 142.773 104.006 1.00 136.13 ? 1410 PRO A O   1 
ATOM   11006 C  CB  . PRO A 1 1410 ? 106.769 144.147 101.292 1.00 140.24 ? 1410 PRO A CB  1 
ATOM   11007 C  CG  . PRO A 1 1410 ? 106.491 145.588 101.108 1.00 146.65 ? 1410 PRO A CG  1 
ATOM   11008 C  CD  . PRO A 1 1410 ? 105.248 145.891 101.881 1.00 138.95 ? 1410 PRO A CD  1 
ATOM   11009 N  N   . LEU A 1 1411 ? 107.810 145.003 104.240 1.00 152.32 ? 1411 LEU A N   1 
ATOM   11010 C  CA  . LEU A 1 1411 ? 108.968 145.128 105.125 1.00 160.03 ? 1411 LEU A CA  1 
ATOM   11011 C  C   . LEU A 1 1411 ? 108.525 145.816 106.417 1.00 162.92 ? 1411 LEU A C   1 
ATOM   11012 O  O   . LEU A 1 1411 ? 108.564 147.040 106.570 1.00 162.54 ? 1411 LEU A O   1 
ATOM   11013 C  CB  . LEU A 1 1411 ? 110.124 145.864 104.418 1.00 162.02 ? 1411 LEU A CB  1 
ATOM   11014 C  CG  . LEU A 1 1411 ? 110.120 147.367 104.105 1.00 161.20 ? 1411 LEU A CG  1 
ATOM   11015 C  CD1 . LEU A 1 1411 ? 111.502 147.827 103.663 1.00 151.23 ? 1411 LEU A CD1 1 
ATOM   11016 C  CD2 . LEU A 1 1411 ? 109.068 147.731 103.069 1.00 154.64 ? 1411 LEU A CD2 1 
ATOM   11017 N  N   . CYS A 1 1412 ? 108.072 144.986 107.357 1.00 172.25 ? 1412 CYS A N   1 
ATOM   11018 C  CA  . CYS A 1 1412 ? 107.747 145.405 108.711 1.00 182.39 ? 1412 CYS A CA  1 
ATOM   11019 C  C   . CYS A 1 1412 ? 108.744 144.897 109.738 1.00 190.32 ? 1412 CYS A C   1 
ATOM   11020 O  O   . CYS A 1 1412 ? 108.872 145.505 110.804 1.00 182.34 ? 1412 CYS A O   1 
ATOM   11021 C  CB  . CYS A 1 1412 ? 106.343 144.919 109.100 1.00 180.35 ? 1412 CYS A CB  1 
ATOM   11022 S  SG  . CYS A 1 1412 ? 106.191 143.121 109.212 1.00 191.51 ? 1412 CYS A SG  1 
ATOM   11023 N  N   . SER A 1 1413 ? 109.446 143.805 109.444 1.00 190.18 ? 1413 SER A N   1 
ATOM   11024 C  CA  . SER A 1 1413 ? 110.501 143.328 110.320 1.00 185.41 ? 1413 SER A CA  1 
ATOM   11025 C  C   . SER A 1 1413 ? 111.728 144.227 110.175 1.00 180.95 ? 1413 SER A C   1 
ATOM   11026 O  O   . SER A 1 1413 ? 111.712 145.240 109.470 1.00 178.49 ? 1413 SER A O   1 
ATOM   11027 C  CB  . SER A 1 1413 ? 110.831 141.873 109.999 1.00 168.45 ? 1413 SER A CB  1 
ATOM   11028 O  OG  . SER A 1 1413 ? 109.680 141.061 110.138 1.00 153.04 ? 1413 SER A OG  1 
ATOM   11029 N  N   . GLY A 1 1414 ? 112.810 143.856 110.854 1.00 172.40 ? 1414 GLY A N   1 
ATOM   11030 C  CA  . GLY A 1 1414 ? 114.000 144.687 110.816 1.00 175.31 ? 1414 GLY A CA  1 
ATOM   11031 C  C   . GLY A 1 1414 ? 114.595 144.747 109.421 1.00 178.87 ? 1414 GLY A C   1 
ATOM   11032 O  O   . GLY A 1 1414 ? 114.593 143.763 108.677 1.00 172.69 ? 1414 GLY A O   1 
ATOM   11033 N  N   . ILE A 1 1415 ? 115.110 145.926 109.067 1.00 184.29 ? 1415 ILE A N   1 
ATOM   11034 C  CA  . ILE A 1 1415 ? 115.760 146.099 107.771 1.00 182.58 ? 1415 ILE A CA  1 
ATOM   11035 C  C   . ILE A 1 1415 ? 117.067 145.316 107.718 1.00 185.72 ? 1415 ILE A C   1 
ATOM   11036 O  O   . ILE A 1 1415 ? 117.434 144.771 106.670 1.00 180.36 ? 1415 ILE A O   1 
ATOM   11037 C  CB  . ILE A 1 1415 ? 115.969 147.596 107.476 1.00 175.30 ? 1415 ILE A CB  1 
ATOM   11038 C  CG1 . ILE A 1 1415 ? 116.850 148.244 108.545 1.00 174.78 ? 1415 ILE A CG1 1 
ATOM   11039 C  CG2 . ILE A 1 1415 ? 114.629 148.311 107.398 1.00 159.19 ? 1415 ILE A CG2 1 
ATOM   11040 C  CD1 . ILE A 1 1415 ? 117.413 149.588 108.139 1.00 155.21 ? 1415 ILE A CD1 1 
ATOM   11041 N  N   . LYS A 1 1416 ? 117.773 145.235 108.845 1.00 185.62 ? 1416 LYS A N   1 
ATOM   11042 C  CA  . LYS A 1 1416 ? 119.055 144.538 108.952 1.00 180.42 ? 1416 LYS A CA  1 
ATOM   11043 C  C   . LYS A 1 1416 ? 120.022 144.873 107.815 1.00 173.91 ? 1416 LYS A C   1 
ATOM   11044 O  O   . LYS A 1 1416 ? 120.061 146.004 107.331 1.00 162.05 ? 1416 LYS A O   1 
ATOM   11045 C  CB  . LYS A 1 1416 ? 118.817 143.029 109.006 1.00 169.29 ? 1416 LYS A CB  1 
ATOM   11046 C  CG  . LYS A 1 1416 ? 120.061 142.198 109.253 1.00 153.85 ? 1416 LYS A CG  1 
ATOM   11047 C  CD  . LYS A 1 1416 ? 119.724 140.719 109.190 1.00 167.65 ? 1416 LYS A CD  1 
ATOM   11048 C  CE  . LYS A 1 1416 ? 120.941 139.850 109.433 1.00 168.70 ? 1416 LYS A CE  1 
ATOM   11049 N  NZ  . LYS A 1 1416 ? 120.575 138.407 109.407 1.00 160.36 ? 1416 LYS A NZ  1 
ATOM   11050 N  N   . MET B 2 455  ? 131.322 148.073 155.147 1.00 202.94 ? 113  MET B N   1 
ATOM   11051 C  CA  . MET B 2 455  ? 130.697 146.756 155.118 1.00 210.71 ? 113  MET B CA  1 
ATOM   11052 C  C   . MET B 2 455  ? 130.254 146.411 153.702 1.00 205.92 ? 113  MET B C   1 
ATOM   11053 O  O   . MET B 2 455  ? 129.215 145.781 153.502 1.00 195.56 ? 113  MET B O   1 
ATOM   11054 C  CB  . MET B 2 455  ? 129.501 146.711 156.070 1.00 210.87 ? 113  MET B CB  1 
ATOM   11055 C  CG  . MET B 2 455  ? 129.867 146.829 157.540 1.00 208.84 ? 113  MET B CG  1 
ATOM   11056 S  SD  . MET B 2 455  ? 128.433 146.658 158.620 1.00 215.11 ? 113  MET B SD  1 
ATOM   11057 C  CE  . MET B 2 455  ? 127.621 148.232 158.353 1.00 191.93 ? 113  MET B CE  1 
ATOM   11058 N  N   . GLY B 2 456  ? 131.056 146.833 152.721 1.00 203.79 ? 114  GLY B N   1 
ATOM   11059 C  CA  . GLY B 2 456  ? 130.684 146.630 151.330 1.00 201.95 ? 114  GLY B CA  1 
ATOM   11060 C  C   . GLY B 2 456  ? 130.559 145.167 150.945 1.00 202.74 ? 114  GLY B C   1 
ATOM   11061 O  O   . GLY B 2 456  ? 129.607 144.774 150.268 1.00 195.93 ? 114  GLY B O   1 
ATOM   11062 N  N   . ARG B 2 457  ? 131.521 144.342 151.366 1.00 203.26 ? 115  ARG B N   1 
ATOM   11063 C  CA  . ARG B 2 457  ? 131.504 142.931 150.991 1.00 207.60 ? 115  ARG B CA  1 
ATOM   11064 C  C   . ARG B 2 457  ? 130.349 142.193 151.657 1.00 202.49 ? 115  ARG B C   1 
ATOM   11065 O  O   . ARG B 2 457  ? 129.606 141.447 150.998 1.00 191.27 ? 115  ARG B O   1 
ATOM   11066 C  CB  . ARG B 2 457  ? 132.838 142.283 151.364 1.00 200.75 ? 115  ARG B CB  1 
ATOM   11067 C  CG  . ARG B 2 457  ? 134.031 142.874 150.639 1.00 193.34 ? 115  ARG B CG  1 
ATOM   11068 C  CD  . ARG B 2 457  ? 133.789 142.906 149.142 1.00 194.66 ? 115  ARG B CD  1 
ATOM   11069 N  NE  . ARG B 2 457  ? 135.017 142.683 148.387 1.00 191.50 ? 115  ARG B NE  1 
ATOM   11070 C  CZ  . ARG B 2 457  ? 135.738 143.653 147.835 1.00 187.44 ? 115  ARG B CZ  1 
ATOM   11071 N  NH1 . ARG B 2 457  ? 136.843 143.361 147.165 1.00 182.38 ? 115  ARG B NH1 1 
ATOM   11072 N  NH2 . ARG B 2 457  ? 135.349 144.916 147.948 1.00 188.83 ? 115  ARG B NH2 1 
ATOM   11073 N  N   . THR B 2 458  ? 130.174 142.404 152.965 1.00 201.46 ? 116  THR B N   1 
ATOM   11074 C  CA  . THR B 2 458  ? 129.110 141.753 153.717 1.00 201.00 ? 116  THR B CA  1 
ATOM   11075 C  C   . THR B 2 458  ? 127.726 142.230 153.307 1.00 201.96 ? 116  THR B C   1 
ATOM   11076 O  O   . THR B 2 458  ? 126.734 141.604 153.694 1.00 191.19 ? 116  THR B O   1 
ATOM   11077 C  CB  . THR B 2 458  ? 129.308 141.988 155.217 1.00 191.42 ? 116  THR B CB  1 
ATOM   11078 O  OG1 . THR B 2 458  ? 129.301 143.395 155.488 1.00 193.36 ? 116  THR B OG1 1 
ATOM   11079 C  CG2 . THR B 2 458  ? 130.635 141.401 155.677 1.00 174.12 ? 116  THR B CG2 1 
ATOM   11080 N  N   . LEU B 2 459  ? 127.635 143.310 152.534 1.00 197.83 ? 117  LEU B N   1 
ATOM   11081 C  CA  . LEU B 2 459  ? 126.369 143.788 151.998 1.00 190.42 ? 117  LEU B CA  1 
ATOM   11082 C  C   . LEU B 2 459  ? 126.125 143.313 150.573 1.00 178.33 ? 117  LEU B C   1 
ATOM   11083 O  O   . LEU B 2 459  ? 125.004 142.918 150.237 1.00 168.91 ? 117  LEU B O   1 
ATOM   11084 C  CB  . LEU B 2 459  ? 126.327 145.319 152.038 1.00 189.87 ? 117  LEU B CB  1 
ATOM   11085 C  CG  . LEU B 2 459  ? 125.000 145.982 151.675 1.00 184.74 ? 117  LEU B CG  1 
ATOM   11086 C  CD1 . LEU B 2 459  ? 123.928 145.613 152.691 1.00 176.12 ? 117  LEU B CD1 1 
ATOM   11087 C  CD2 . LEU B 2 459  ? 125.162 147.492 151.578 1.00 169.26 ? 117  LEU B CD2 1 
ATOM   11088 N  N   . GLU B 2 460  ? 127.164 143.323 149.734 1.00 179.16 ? 118  GLU B N   1 
ATOM   11089 C  CA  . GLU B 2 460  ? 127.017 142.860 148.359 1.00 174.70 ? 118  GLU B CA  1 
ATOM   11090 C  C   . GLU B 2 460  ? 126.742 141.361 148.296 1.00 172.08 ? 118  GLU B C   1 
ATOM   11091 O  O   . GLU B 2 460  ? 125.951 140.904 147.458 1.00 171.24 ? 118  GLU B O   1 
ATOM   11092 C  CB  . GLU B 2 460  ? 128.272 143.214 147.564 1.00 177.38 ? 118  GLU B CB  1 
ATOM   11093 C  CG  . GLU B 2 460  ? 128.129 143.069 146.066 1.00 179.77 ? 118  GLU B CG  1 
ATOM   11094 C  CD  . GLU B 2 460  ? 129.217 143.806 145.317 1.00 187.24 ? 118  GLU B CD  1 
ATOM   11095 O  OE1 . GLU B 2 460  ? 130.243 144.146 145.944 1.00 189.98 ? 118  GLU B OE1 1 
ATOM   11096 O  OE2 . GLU B 2 460  ? 129.047 144.050 144.104 1.00 180.44 ? 118  GLU B OE2 1 
ATOM   11097 N  N   . ALA B 2 461  ? 127.397 140.575 149.160 1.00 175.43 ? 119  ALA B N   1 
ATOM   11098 C  CA  . ALA B 2 461  ? 127.120 139.140 149.183 1.00 175.68 ? 119  ALA B CA  1 
ATOM   11099 C  C   . ALA B 2 461  ? 125.655 138.870 149.516 1.00 167.42 ? 119  ALA B C   1 
ATOM   11100 O  O   . ALA B 2 461  ? 124.983 138.061 148.848 1.00 161.61 ? 119  ALA B O   1 
ATOM   11101 C  CB  . ALA B 2 461  ? 128.043 138.449 150.187 1.00 174.59 ? 119  ALA B CB  1 
ATOM   11102 N  N   . ILE B 2 462  ? 125.137 139.585 150.518 1.00 165.72 ? 120  ILE B N   1 
ATOM   11103 C  CA  . ILE B 2 462  ? 123.741 139.445 150.912 1.00 167.36 ? 120  ILE B CA  1 
ATOM   11104 C  C   . ILE B 2 462  ? 122.820 139.882 149.782 1.00 165.14 ? 120  ILE B C   1 
ATOM   11105 O  O   . ILE B 2 462  ? 121.791 139.249 149.524 1.00 151.84 ? 120  ILE B O   1 
ATOM   11106 C  CB  . ILE B 2 462  ? 123.485 140.242 152.209 1.00 171.68 ? 120  ILE B CB  1 
ATOM   11107 C  CG1 . ILE B 2 462  ? 124.004 139.460 153.419 1.00 172.18 ? 120  ILE B CG1 1 
ATOM   11108 C  CG2 . ILE B 2 462  ? 122.009 140.580 152.371 1.00 170.09 ? 120  ILE B CG2 1 
ATOM   11109 C  CD1 . ILE B 2 462  ? 123.981 140.235 154.716 1.00 179.31 ? 120  ILE B CD1 1 
ATOM   11110 N  N   . SER B 2 463  ? 123.185 140.955 149.072 1.00 168.72 ? 121  SER B N   1 
ATOM   11111 C  CA  . SER B 2 463  ? 122.368 141.418 147.952 1.00 161.69 ? 121  SER B CA  1 
ATOM   11112 C  C   . SER B 2 463  ? 122.251 140.365 146.850 1.00 144.10 ? 121  SER B C   1 
ATOM   11113 O  O   . SER B 2 463  ? 121.137 140.028 146.412 1.00 139.04 ? 121  SER B O   1 
ATOM   11114 C  CB  . SER B 2 463  ? 122.944 142.713 147.379 1.00 158.92 ? 121  SER B CB  1 
ATOM   11115 O  OG  . SER B 2 463  ? 124.020 142.436 146.499 1.00 161.68 ? 121  SER B OG  1 
ATOM   11116 N  N   . LYS B 2 464  ? 123.383 139.789 146.422 1.00 139.85 ? 122  LYS B N   1 
ATOM   11117 C  CA  . LYS B 2 464  ? 123.333 138.801 145.340 1.00 129.25 ? 122  LYS B CA  1 
ATOM   11118 C  C   . LYS B 2 464  ? 122.536 137.571 145.733 1.00 132.83 ? 122  LYS B C   1 
ATOM   11119 O  O   . LYS B 2 464  ? 121.692 137.081 144.961 1.00 135.80 ? 122  LYS B O   1 
ATOM   11120 C  CB  . LYS B 2 464  ? 124.745 138.382 144.931 1.00 132.85 ? 122  LYS B CB  1 
ATOM   11121 C  CG  . LYS B 2 464  ? 125.589 139.461 144.311 1.00 140.28 ? 122  LYS B CG  1 
ATOM   11122 C  CD  . LYS B 2 464  ? 126.807 138.823 143.678 1.00 136.37 ? 122  LYS B CD  1 
ATOM   11123 C  CE  . LYS B 2 464  ? 127.842 139.859 143.322 1.00 154.15 ? 122  LYS B CE  1 
ATOM   11124 N  NZ  . LYS B 2 464  ? 127.233 140.880 142.421 1.00 132.77 ? 122  LYS B NZ  1 
ATOM   11125 N  N   . GLY B 2 465  ? 122.797 137.053 146.935 1.00 133.55 ? 123  GLY B N   1 
ATOM   11126 C  CA  . GLY B 2 465  ? 122.067 135.887 147.404 1.00 140.33 ? 123  GLY B CA  1 
ATOM   11127 C  C   . GLY B 2 465  ? 120.581 136.137 147.567 1.00 140.92 ? 123  GLY B C   1 
ATOM   11128 O  O   . GLY B 2 465  ? 119.760 135.257 147.298 1.00 129.88 ? 123  GLY B O   1 
ATOM   11129 N  N   . MET B 2 466  ? 120.212 137.331 148.042 1.00 140.80 ? 124  MET B N   1 
ATOM   11130 C  CA  . MET B 2 466  ? 118.790 137.643 148.191 1.00 128.36 ? 124  MET B CA  1 
ATOM   11131 C  C   . MET B 2 466  ? 118.131 137.641 146.829 1.00 111.59 ? 124  MET B C   1 
ATOM   11132 O  O   . MET B 2 466  ? 117.012 137.146 146.674 1.00 99.44  ? 124  MET B O   1 
ATOM   11133 C  CB  . MET B 2 466  ? 118.605 139.008 148.862 1.00 127.32 ? 124  MET B CB  1 
ATOM   11134 C  CG  . MET B 2 466  ? 118.576 139.018 150.379 1.00 127.17 ? 124  MET B CG  1 
ATOM   11135 S  SD  . MET B 2 466  ? 117.472 137.740 151.037 1.00 152.88 ? 124  MET B SD  1 
ATOM   11136 C  CE  . MET B 2 466  ? 115.994 138.699 151.361 1.00 158.14 ? 124  MET B CE  1 
ATOM   11137 N  N   . SER B 2 467  ? 118.819 138.188 145.821 1.00 115.33 ? 125  SER B N   1 
ATOM   11138 C  CA  . SER B 2 467  ? 118.267 138.147 144.470 1.00 94.70  ? 125  SER B CA  1 
ATOM   11139 C  C   . SER B 2 467  ? 118.073 136.697 144.015 1.00 94.44  ? 125  SER B C   1 
ATOM   11140 O  O   . SER B 2 467  ? 117.024 136.338 143.455 1.00 101.33 ? 125  SER B O   1 
ATOM   11141 C  CB  . SER B 2 467  ? 119.188 138.902 143.511 1.00 97.12  ? 125  SER B CB  1 
ATOM   11142 O  OG  . SER B 2 467  ? 119.527 140.175 144.036 1.00 120.76 ? 125  SER B OG  1 
ATOM   11143 N  N   . GLU B 2 468  ? 119.075 135.847 144.265 1.00 96.04  ? 126  GLU B N   1 
ATOM   11144 C  CA  . GLU B 2 468  ? 118.988 134.445 143.852 1.00 88.28  ? 126  GLU B CA  1 
ATOM   11145 C  C   . GLU B 2 468  ? 117.844 133.715 144.557 1.00 99.31  ? 126  GLU B C   1 
ATOM   11146 O  O   . GLU B 2 468  ? 117.066 132.983 143.922 1.00 101.78 ? 126  GLU B O   1 
ATOM   11147 C  CB  . GLU B 2 468  ? 120.327 133.762 144.144 1.00 100.75 ? 126  GLU B CB  1 
ATOM   11148 C  CG  . GLU B 2 468  ? 120.440 132.319 143.690 1.00 110.22 ? 126  GLU B CG  1 
ATOM   11149 C  CD  . GLU B 2 468  ? 121.754 131.692 144.119 1.00 118.53 ? 126  GLU B CD  1 
ATOM   11150 O  OE1 . GLU B 2 468  ? 122.015 130.530 143.743 1.00 113.79 ? 126  GLU B OE1 1 
ATOM   11151 O  OE2 . GLU B 2 468  ? 122.525 132.364 144.835 1.00 113.56 ? 126  GLU B OE2 1 
ATOM   11152 N  N   . MET B 2 469  ? 117.724 133.908 145.874 1.00 104.06 ? 127  MET B N   1 
ATOM   11153 C  CA  . MET B 2 469  ? 116.662 133.270 146.646 1.00 97.97  ? 127  MET B CA  1 
ATOM   11154 C  C   . MET B 2 469  ? 115.298 133.726 146.153 1.00 94.65  ? 127  MET B C   1 
ATOM   11155 O  O   . MET B 2 469  ? 114.366 132.917 146.016 1.00 91.95  ? 127  MET B O   1 
ATOM   11156 C  CB  . MET B 2 469  ? 116.857 133.579 148.136 1.00 116.07 ? 127  MET B CB  1 
ATOM   11157 C  CG  . MET B 2 469  ? 115.985 132.792 149.110 1.00 126.96 ? 127  MET B CG  1 
ATOM   11158 S  SD  . MET B 2 469  ? 114.295 133.410 149.252 1.00 150.62 ? 127  MET B SD  1 
ATOM   11159 C  CE  . MET B 2 469  ? 114.580 135.179 149.313 1.00 130.94 ? 127  MET B CE  1 
ATOM   11160 N  N   . LEU B 2 470  ? 115.175 135.026 145.868 1.00 105.82 ? 128  LEU B N   1 
ATOM   11161 C  CA  . LEU B 2 470  ? 113.940 135.581 145.333 1.00 100.72 ? 128  LEU B CA  1 
ATOM   11162 C  C   . LEU B 2 470  ? 113.557 134.911 144.022 1.00 84.63  ? 128  LEU B C   1 
ATOM   11163 O  O   . LEU B 2 470  ? 112.406 134.500 143.837 1.00 87.59  ? 128  LEU B O   1 
ATOM   11164 C  CB  . LEU B 2 470  ? 114.097 137.088 145.143 1.00 96.85  ? 128  LEU B CB  1 
ATOM   11165 C  CG  . LEU B 2 470  ? 112.809 137.876 144.938 1.00 101.28 ? 128  LEU B CG  1 
ATOM   11166 C  CD1 . LEU B 2 470  ? 112.116 138.057 146.271 1.00 118.43 ? 128  LEU B CD1 1 
ATOM   11167 C  CD2 . LEU B 2 470  ? 113.118 139.219 144.302 1.00 107.53 ? 128  LEU B CD2 1 
ATOM   11168 N  N   . ALA B 2 471  ? 114.513 134.793 143.097 1.00 90.20  ? 129  ALA B N   1 
ATOM   11169 C  CA  . ALA B 2 471  ? 114.209 134.185 141.805 1.00 71.80  ? 129  ALA B CA  1 
ATOM   11170 C  C   . ALA B 2 471  ? 113.722 132.751 141.984 1.00 68.08  ? 129  ALA B C   1 
ATOM   11171 O  O   . ALA B 2 471  ? 112.691 132.352 141.420 1.00 86.74  ? 129  ALA B O   1 
ATOM   11172 C  CB  . ALA B 2 471  ? 115.438 134.232 140.897 1.00 79.38  ? 129  ALA B CB  1 
ATOM   11173 N  N   . LYS B 2 472  ? 114.438 131.969 142.797 1.00 72.78  ? 130  LYS B N   1 
ATOM   11174 C  CA  . LYS B 2 472  ? 114.091 130.556 142.924 1.00 73.90  ? 130  LYS B CA  1 
ATOM   11175 C  C   . LYS B 2 472  ? 112.714 130.377 143.556 1.00 79.29  ? 130  LYS B C   1 
ATOM   11176 O  O   . LYS B 2 472  ? 111.889 129.591 143.063 1.00 83.81  ? 130  LYS B O   1 
ATOM   11177 C  CB  . LYS B 2 472  ? 115.161 129.823 143.731 1.00 92.16  ? 130  LYS B CB  1 
ATOM   11178 C  CG  . LYS B 2 472  ? 116.469 129.666 142.978 1.00 94.91  ? 130  LYS B CG  1 
ATOM   11179 C  CD  . LYS B 2 472  ? 117.573 129.119 143.857 1.00 80.89  ? 130  LYS B CD  1 
ATOM   11180 C  CE  . LYS B 2 472  ? 118.766 128.710 143.012 1.00 80.59  ? 130  LYS B CE  1 
ATOM   11181 N  NZ  . LYS B 2 472  ? 119.893 128.207 143.840 1.00 95.04  ? 130  LYS B NZ  1 
ATOM   11182 N  N   . TYR B 2 473  ? 112.422 131.126 144.622 1.00 82.22  ? 131  TYR B N   1 
ATOM   11183 C  CA  . TYR B 2 473  ? 111.134 130.930 145.279 1.00 78.77  ? 131  TYR B CA  1 
ATOM   11184 C  C   . TYR B 2 473  ? 109.976 131.534 144.495 1.00 87.39  ? 131  TYR B C   1 
ATOM   11185 O  O   . TYR B 2 473  ? 108.852 131.025 144.580 1.00 90.45  ? 131  TYR B O   1 
ATOM   11186 C  CB  . TYR B 2 473  ? 111.173 131.478 146.702 1.00 85.43  ? 131  TYR B CB  1 
ATOM   11187 C  CG  . TYR B 2 473  ? 111.746 130.451 147.638 1.00 102.00 ? 131  TYR B CG  1 
ATOM   11188 C  CD1 . TYR B 2 473  ? 110.964 129.411 148.116 1.00 106.50 ? 131  TYR B CD1 1 
ATOM   11189 C  CD2 . TYR B 2 473  ? 113.077 130.500 148.015 1.00 106.02 ? 131  TYR B CD2 1 
ATOM   11190 C  CE1 . TYR B 2 473  ? 111.491 128.454 148.959 1.00 93.29  ? 131  TYR B CE1 1 
ATOM   11191 C  CE2 . TYR B 2 473  ? 113.612 129.554 148.861 1.00 118.16 ? 131  TYR B CE2 1 
ATOM   11192 C  CZ  . TYR B 2 473  ? 112.816 128.532 149.331 1.00 108.95 ? 131  TYR B CZ  1 
ATOM   11193 O  OH  . TYR B 2 473  ? 113.350 127.585 150.172 1.00 113.19 ? 131  TYR B OH  1 
ATOM   11194 N  N   . ASP B 2 474  ? 110.218 132.593 143.718 1.00 88.68  ? 132  ASP B N   1 
ATOM   11195 C  CA  . ASP B 2 474  ? 109.180 133.084 142.819 1.00 72.69  ? 132  ASP B CA  1 
ATOM   11196 C  C   . ASP B 2 474  ? 108.820 132.033 141.779 1.00 72.66  ? 132  ASP B C   1 
ATOM   11197 O  O   . ASP B 2 474  ? 107.635 131.788 141.507 1.00 82.78  ? 132  ASP B O   1 
ATOM   11198 C  CB  . ASP B 2 474  ? 109.646 134.371 142.142 1.00 84.20  ? 132  ASP B CB  1 
ATOM   11199 C  CG  . ASP B 2 474  ? 108.573 134.991 141.276 1.00 101.39 ? 132  ASP B CG  1 
ATOM   11200 O  OD1 . ASP B 2 474  ? 108.772 135.069 140.046 1.00 100.40 ? 132  ASP B OD1 1 
ATOM   11201 O  OD2 . ASP B 2 474  ? 107.528 135.396 141.825 1.00 111.66 ? 132  ASP B OD2 1 
ATOM   11202 N  N   . HIS B 2 475  ? 109.836 131.389 141.191 1.00 78.27  ? 133  HIS B N   1 
ATOM   11203 C  CA  . HIS B 2 475  ? 109.551 130.300 140.264 1.00 58.26  ? 133  HIS B CA  1 
ATOM   11204 C  C   . HIS B 2 475  ? 108.737 129.210 140.951 1.00 67.53  ? 133  HIS B C   1 
ATOM   11205 O  O   . HIS B 2 475  ? 107.746 128.712 140.394 1.00 93.05  ? 133  HIS B O   1 
ATOM   11206 C  CB  . HIS B 2 475  ? 110.844 129.723 139.691 1.00 76.12  ? 133  HIS B CB  1 
ATOM   11207 C  CG  . HIS B 2 475  ? 110.623 128.588 138.738 1.00 76.18  ? 133  HIS B CG  1 
ATOM   11208 N  ND1 . HIS B 2 475  ? 110.460 127.285 139.156 1.00 79.20  ? 133  HIS B ND1 1 
ATOM   11209 C  CD2 . HIS B 2 475  ? 110.522 128.565 137.386 1.00 78.21  ? 133  HIS B CD2 1 
ATOM   11210 C  CE1 . HIS B 2 475  ? 110.275 126.507 138.105 1.00 62.49  ? 133  HIS B CE1 1 
ATOM   11211 N  NE2 . HIS B 2 475  ? 110.308 127.259 137.020 1.00 66.05  ? 133  HIS B NE2 1 
ATOM   11212 N  N   . LEU B 2 476  ? 109.127 128.851 142.179 1.00 69.93  ? 134  LEU B N   1 
ATOM   11213 C  CA  . LEU B 2 476  ? 108.419 127.794 142.896 1.00 83.54  ? 134  LEU B CA  1 
ATOM   11214 C  C   . LEU B 2 476  ? 106.948 128.144 143.096 1.00 79.53  ? 134  LEU B C   1 
ATOM   11215 O  O   . LEU B 2 476  ? 106.063 127.329 142.808 1.00 79.15  ? 134  LEU B O   1 
ATOM   11216 C  CB  . LEU B 2 476  ? 109.088 127.540 144.246 1.00 83.63  ? 134  LEU B CB  1 
ATOM   11217 C  CG  . LEU B 2 476  ? 108.284 126.591 145.135 1.00 71.79  ? 134  LEU B CG  1 
ATOM   11218 C  CD1 . LEU B 2 476  ? 108.170 125.225 144.474 1.00 74.69  ? 134  LEU B CD1 1 
ATOM   11219 C  CD2 . LEU B 2 476  ? 108.886 126.484 146.528 1.00 64.14  ? 134  LEU B CD2 1 
ATOM   11220 N  N   . VAL B 2 477  ? 106.666 129.352 143.590 1.00 88.13  ? 135  VAL B N   1 
ATOM   11221 C  CA  . VAL B 2 477  ? 105.281 129.713 143.890 1.00 74.95  ? 135  VAL B CA  1 
ATOM   11222 C  C   . VAL B 2 477  ? 104.447 129.834 142.619 1.00 73.35  ? 135  VAL B C   1 
ATOM   11223 O  O   . VAL B 2 477  ? 103.261 129.482 142.618 1.00 80.12  ? 135  VAL B O   1 
ATOM   11224 C  CB  . VAL B 2 477  ? 105.201 131.000 144.734 1.00 86.68  ? 135  VAL B CB  1 
ATOM   11225 C  CG1 . VAL B 2 477  ? 105.614 132.223 143.930 1.00 105.74 ? 135  VAL B CG1 1 
ATOM   11226 C  CG2 . VAL B 2 477  ? 103.788 131.176 145.290 1.00 100.29 ? 135  VAL B CG2 1 
ATOM   11227 N  N   . ILE B 2 478  ? 105.037 130.308 141.518 1.00 86.86  ? 136  ILE B N   1 
ATOM   11228 C  CA  . ILE B 2 478  ? 104.286 130.372 140.266 1.00 76.17  ? 136  ILE B CA  1 
ATOM   11229 C  C   . ILE B 2 478  ? 103.967 128.977 139.747 1.00 69.40  ? 136  ILE B C   1 
ATOM   11230 O  O   . ILE B 2 478  ? 102.888 128.742 139.191 1.00 69.50  ? 136  ILE B O   1 
ATOM   11231 C  CB  . ILE B 2 478  ? 105.051 131.193 139.211 1.00 67.88  ? 136  ILE B CB  1 
ATOM   11232 C  CG1 . ILE B 2 478  ? 105.126 132.665 139.611 1.00 84.93  ? 136  ILE B CG1 1 
ATOM   11233 C  CG2 . ILE B 2 478  ? 104.389 131.064 137.840 1.00 66.40  ? 136  ILE B CG2 1 
ATOM   11234 C  CD1 . ILE B 2 478  ? 105.874 133.519 138.609 1.00 97.63  ? 136  ILE B CD1 1 
ATOM   11235 N  N   . SER B 2 479  ? 104.874 128.018 139.948 1.00 74.74  ? 137  SER B N   1 
ATOM   11236 C  CA  . SER B 2 479  ? 104.650 126.699 139.363 1.00 71.47  ? 137  SER B CA  1 
ATOM   11237 C  C   . SER B 2 479  ? 103.451 125.981 139.981 1.00 83.09  ? 137  SER B C   1 
ATOM   11238 O  O   . SER B 2 479  ? 102.672 125.346 139.258 1.00 94.07  ? 137  SER B O   1 
ATOM   11239 C  CB  . SER B 2 479  ? 105.911 125.845 139.505 1.00 69.83  ? 137  SER B CB  1 
ATOM   11240 O  OG  . SER B 2 479  ? 105.734 124.571 138.907 1.00 81.13  ? 137  SER B OG  1 
ATOM   11241 N  N   . THR B 2 480  ? 103.270 126.064 141.301 1.00 86.80  ? 138  THR B N   1 
ATOM   11242 C  CA  . THR B 2 480  ? 102.201 125.325 141.969 1.00 81.10  ? 138  THR B CA  1 
ATOM   11243 C  C   . THR B 2 480  ? 101.086 126.207 142.528 1.00 81.73  ? 138  THR B C   1 
ATOM   11244 O  O   . THR B 2 480  ? 100.370 125.774 143.436 1.00 96.75  ? 138  THR B O   1 
ATOM   11245 C  CB  . THR B 2 480  ? 102.777 124.467 143.094 1.00 79.81  ? 138  THR B CB  1 
ATOM   11246 O  OG1 . THR B 2 480  ? 103.403 125.311 144.069 1.00 75.98  ? 138  THR B OG1 1 
ATOM   11247 C  CG2 . THR B 2 480  ? 103.804 123.500 142.544 1.00 103.32 ? 138  THR B CG2 1 
ATOM   11248 N  N   . GLY B 2 481  ? 100.905 127.419 142.015 1.00 78.22  ? 139  GLY B N   1 
ATOM   11249 C  CA  . GLY B 2 481  ? 100.226 128.431 142.799 1.00 74.83  ? 139  GLY B CA  1 
ATOM   11250 C  C   . GLY B 2 481  ? 98.728  128.204 142.884 1.00 81.55  ? 139  GLY B C   1 
ATOM   11251 O  O   . GLY B 2 481  ? 98.123  127.499 142.075 1.00 89.28  ? 139  GLY B O   1 
ATOM   11252 N  N   . ARG B 2 482  ? 98.126  128.807 143.910 1.00 86.89  ? 140  ARG B N   1 
ATOM   11253 C  CA  . ARG B 2 482  ? 96.711  129.141 144.017 1.00 79.94  ? 140  ARG B CA  1 
ATOM   11254 C  C   . ARG B 2 482  ? 95.846  127.913 144.340 1.00 73.68  ? 140  ARG B C   1 
ATOM   11255 O  O   . ARG B 2 482  ? 94.687  128.081 144.724 1.00 85.64  ? 140  ARG B O   1 
ATOM   11256 C  CB  . ARG B 2 482  ? 96.187  129.849 142.747 1.00 100.29 ? 140  ARG B CB  1 
ATOM   11257 C  CG  . ARG B 2 482  ? 94.768  130.402 142.753 1.00 96.01  ? 140  ARG B CG  1 
ATOM   11258 C  CD  . ARG B 2 482  ? 93.776  129.437 142.126 1.00 87.61  ? 140  ARG B CD  1 
ATOM   11259 N  NE  . ARG B 2 482  ? 92.478  130.070 141.920 1.00 93.32  ? 140  ARG B NE  1 
ATOM   11260 C  CZ  . ARG B 2 482  ? 91.378  129.424 141.550 1.00 100.72 ? 140  ARG B CZ  1 
ATOM   11261 N  NH1 . ARG B 2 482  ? 90.243  130.090 141.385 1.00 117.03 ? 140  ARG B NH1 1 
ATOM   11262 N  NH2 . ARG B 2 482  ? 91.408  128.116 141.340 1.00 97.46  ? 140  ARG B NH2 1 
ATOM   11263 N  N   . THR B 2 483  ? 96.388  126.694 144.282 1.00 75.32  ? 141  THR B N   1 
ATOM   11264 C  CA  . THR B 2 483  ? 95.639  125.499 144.651 1.00 70.74  ? 141  THR B CA  1 
ATOM   11265 C  C   . THR B 2 483  ? 96.439  124.521 145.501 1.00 79.57  ? 141  THR B C   1 
ATOM   11266 O  O   . THR B 2 483  ? 95.921  123.447 145.824 1.00 82.23  ? 141  THR B O   1 
ATOM   11267 C  CB  . THR B 2 483  ? 95.134  124.762 143.399 1.00 63.66  ? 141  THR B CB  1 
ATOM   11268 O  OG1 . THR B 2 483  ? 96.207  124.616 142.462 1.00 69.61  ? 141  THR B OG1 1 
ATOM   11269 C  CG2 . THR B 2 483  ? 93.989  125.525 142.742 1.00 81.07  ? 141  THR B CG2 1 
ATOM   11270 N  N   . THR B 2 484  ? 97.676  124.848 145.867 1.00 76.71  ? 142  THR B N   1 
ATOM   11271 C  CA  . THR B 2 484  ? 98.508  123.928 146.627 1.00 70.07  ? 142  THR B CA  1 
ATOM   11272 C  C   . THR B 2 484  ? 97.932  123.697 148.020 1.00 82.40  ? 142  THR B C   1 
ATOM   11273 O  O   . THR B 2 484  ? 97.344  124.594 148.630 1.00 91.83  ? 142  THR B O   1 
ATOM   11274 C  CB  . THR B 2 484  ? 99.938  124.465 146.726 1.00 73.13  ? 142  THR B CB  1 
ATOM   11275 O  OG1 . THR B 2 484  ? 100.781 123.483 147.340 1.00 93.14  ? 142  THR B OG1 1 
ATOM   11276 C  CG2 . THR B 2 484  ? 99.980  125.741 147.547 1.00 79.15  ? 142  THR B CG2 1 
ATOM   11277 N  N   . ALA B 2 485  ? 98.070  122.464 148.499 1.00 78.02  ? 143  ALA B N   1 
ATOM   11278 C  CA  . ALA B 2 485  ? 97.485  122.054 149.768 1.00 76.48  ? 143  ALA B CA  1 
ATOM   11279 C  C   . ALA B 2 485  ? 98.442  122.367 150.910 1.00 85.08  ? 143  ALA B C   1 
ATOM   11280 O  O   . ALA B 2 485  ? 99.588  121.899 150.884 1.00 91.20  ? 143  ALA B O   1 
ATOM   11281 C  CB  . ALA B 2 485  ? 97.166  120.570 149.754 1.00 79.41  ? 143  ALA B CB  1 
ATOM   11282 N  N   . PRO B 2 486  ? 98.035  123.149 151.907 1.00 91.14  ? 144  PRO B N   1 
ATOM   11283 C  CA  . PRO B 2 486  ? 98.918  123.400 153.052 1.00 97.38  ? 144  PRO B CA  1 
ATOM   11284 C  C   . PRO B 2 486  ? 99.069  122.145 153.901 1.00 114.94 ? 144  PRO B C   1 
ATOM   11285 O  O   . PRO B 2 486  ? 98.404  121.127 153.690 1.00 118.43 ? 144  PRO B O   1 
ATOM   11286 C  CB  . PRO B 2 486  ? 98.203  124.517 153.823 1.00 100.77 ? 144  PRO B CB  1 
ATOM   11287 C  CG  . PRO B 2 486  ? 97.179  125.071 152.857 1.00 106.54 ? 144  PRO B CG  1 
ATOM   11288 C  CD  . PRO B 2 486  ? 96.781  123.910 152.006 1.00 93.84  ? 144  PRO B CD  1 
ATOM   11289 N  N   . ALA B 2 487  ? 99.976  122.227 154.877 1.00 107.50 ? 145  ALA B N   1 
ATOM   11290 C  CA  . ALA B 2 487  ? 100.348 121.044 155.648 1.00 104.03 ? 145  ALA B CA  1 
ATOM   11291 C  C   . ALA B 2 487  ? 99.166  120.495 156.442 1.00 113.03 ? 145  ALA B C   1 
ATOM   11292 O  O   . ALA B 2 487  ? 98.915  119.282 156.450 1.00 110.31 ? 145  ALA B O   1 
ATOM   11293 C  CB  . ALA B 2 487  ? 101.516 121.375 156.578 1.00 103.16 ? 145  ALA B CB  1 
ATOM   11294 N  N   . ALA B 2 488  ? 98.417  121.380 157.104 1.00 113.66 ? 146  ALA B N   1 
ATOM   11295 C  CA  . ALA B 2 488  ? 97.317  120.940 157.958 1.00 111.62 ? 146  ALA B CA  1 
ATOM   11296 C  C   . ALA B 2 488  ? 96.216  120.260 157.153 1.00 112.55 ? 146  ALA B C   1 
ATOM   11297 O  O   . ALA B 2 488  ? 95.743  119.178 157.522 1.00 113.76 ? 146  ALA B O   1 
ATOM   11298 C  CB  . ALA B 2 488  ? 96.757  122.129 158.739 1.00 113.13 ? 146  ALA B CB  1 
ATOM   11299 N  N   . ALA B 2 489  ? 95.785  120.887 156.055 1.00 109.52 ? 147  ALA B N   1 
ATOM   11300 C  CA  . ALA B 2 489  ? 94.739  120.292 155.229 1.00 115.01 ? 147  ALA B CA  1 
ATOM   11301 C  C   . ALA B 2 489  ? 95.198  118.982 154.602 1.00 113.47 ? 147  ALA B C   1 
ATOM   11302 O  O   . ALA B 2 489  ? 94.424  118.020 154.522 1.00 111.65 ? 147  ALA B O   1 
ATOM   11303 C  CB  . ALA B 2 489  ? 94.298  121.278 154.148 1.00 116.81 ? 147  ALA B CB  1 
ATOM   11304 N  N   . PHE B 2 490  ? 96.456  118.923 154.159 1.00 108.32 ? 148  PHE B N   1 
ATOM   11305 C  CA  . PHE B 2 490  ? 96.981  117.682 153.600 1.00 100.07 ? 148  PHE B CA  1 
ATOM   11306 C  C   . PHE B 2 490  ? 96.923  116.560 154.626 1.00 111.47 ? 148  PHE B C   1 
ATOM   11307 O  O   . PHE B 2 490  ? 96.435  115.459 154.338 1.00 113.21 ? 148  PHE B O   1 
ATOM   11308 C  CB  . PHE B 2 490  ? 98.419  117.890 153.114 1.00 96.62  ? 148  PHE B CB  1 
ATOM   11309 C  CG  . PHE B 2 490  ? 99.038  116.661 152.499 1.00 115.84 ? 148  PHE B CG  1 
ATOM   11310 C  CD1 . PHE B 2 490  ? 99.683  115.718 153.288 1.00 110.26 ? 148  PHE B CD1 1 
ATOM   11311 C  CD2 . PHE B 2 490  ? 98.975  116.450 151.133 1.00 122.78 ? 148  PHE B CD2 1 
ATOM   11312 C  CE1 . PHE B 2 490  ? 100.248 114.589 152.723 1.00 101.79 ? 148  PHE B CE1 1 
ATOM   11313 C  CE2 . PHE B 2 490  ? 99.540  115.323 150.562 1.00 92.20  ? 148  PHE B CE2 1 
ATOM   11314 C  CZ  . PHE B 2 490  ? 100.176 114.393 151.359 1.00 99.02  ? 148  PHE B CZ  1 
ATOM   11315 N  N   . ASP B 2 491  ? 97.401  116.833 155.843 1.00 112.21 ? 149  ASP B N   1 
ATOM   11316 C  CA  . ASP B 2 491  ? 97.414  115.800 156.871 1.00 110.86 ? 149  ASP B CA  1 
ATOM   11317 C  C   . ASP B 2 491  ? 96.000  115.381 157.254 1.00 117.47 ? 149  ASP B C   1 
ATOM   11318 O  O   . ASP B 2 491  ? 95.726  114.186 157.415 1.00 122.76 ? 149  ASP B O   1 
ATOM   11319 C  CB  . ASP B 2 491  ? 98.183  116.294 158.097 1.00 121.36 ? 149  ASP B CB  1 
ATOM   11320 C  CG  . ASP B 2 491  ? 98.521  115.176 159.065 1.00 134.18 ? 149  ASP B CG  1 
ATOM   11321 O  OD1 . ASP B 2 491  ? 97.591  114.608 159.675 1.00 144.14 ? 149  ASP B OD1 1 
ATOM   11322 O  OD2 . ASP B 2 491  ? 99.720  114.863 159.216 1.00 128.96 ? 149  ASP B OD2 1 
ATOM   11323 N  N   . ALA B 2 492  ? 95.088  116.347 157.401 1.00 114.81 ? 150  ALA B N   1 
ATOM   11324 C  CA  . ALA B 2 492  ? 93.708  116.029 157.757 1.00 122.69 ? 150  ALA B CA  1 
ATOM   11325 C  C   . ALA B 2 492  ? 93.044  115.159 156.696 1.00 125.74 ? 150  ALA B C   1 
ATOM   11326 O  O   . ALA B 2 492  ? 92.424  114.135 157.014 1.00 127.52 ? 150  ALA B O   1 
ATOM   11327 C  CB  . ALA B 2 492  ? 92.914  117.316 157.975 1.00 116.35 ? 150  ALA B CB  1 
ATOM   11328 N  N   . TYR B 2 493  ? 93.159  115.556 155.423 1.00 115.30 ? 151  TYR B N   1 
ATOM   11329 C  CA  . TYR B 2 493  ? 92.565  114.772 154.346 1.00 105.94 ? 151  TYR B CA  1 
ATOM   11330 C  C   . TYR B 2 493  ? 93.152  113.373 154.293 1.00 111.05 ? 151  TYR B C   1 
ATOM   11331 O  O   . TYR B 2 493  ? 92.417  112.387 154.154 1.00 117.96 ? 151  TYR B O   1 
ATOM   11332 C  CB  . TYR B 2 493  ? 92.771  115.482 153.004 1.00 103.94 ? 151  TYR B CB  1 
ATOM   11333 C  CG  . TYR B 2 493  ? 91.963  114.902 151.860 1.00 102.76 ? 151  TYR B CG  1 
ATOM   11334 C  CD1 . TYR B 2 493  ? 90.820  115.533 151.393 1.00 106.17 ? 151  TYR B CD1 1 
ATOM   11335 C  CD2 . TYR B 2 493  ? 92.364  113.729 151.232 1.00 101.25 ? 151  TYR B CD2 1 
ATOM   11336 C  CE1 . TYR B 2 493  ? 90.091  115.002 150.340 1.00 106.38 ? 151  TYR B CE1 1 
ATOM   11337 C  CE2 . TYR B 2 493  ? 91.642  113.190 150.186 1.00 95.57  ? 151  TYR B CE2 1 
ATOM   11338 C  CZ  . TYR B 2 493  ? 90.508  113.830 149.741 1.00 97.78  ? 151  TYR B CZ  1 
ATOM   11339 O  OH  . TYR B 2 493  ? 89.787  113.290 148.700 1.00 92.65  ? 151  TYR B OH  1 
ATOM   11340 N  N   . LEU B 2 494  ? 94.477  113.263 154.411 1.00 111.99 ? 152  LEU B N   1 
ATOM   11341 C  CA  . LEU B 2 494  ? 95.109  111.955 154.333 1.00 112.67 ? 152  LEU B CA  1 
ATOM   11342 C  C   . LEU B 2 494  ? 94.670  111.063 155.488 1.00 120.03 ? 152  LEU B C   1 
ATOM   11343 O  O   . LEU B 2 494  ? 94.392  109.874 155.292 1.00 124.65 ? 152  LEU B O   1 
ATOM   11344 C  CB  . LEU B 2 494  ? 96.627  112.106 154.299 1.00 103.61 ? 152  LEU B CB  1 
ATOM   11345 C  CG  . LEU B 2 494  ? 97.382  110.783 154.228 1.00 112.28 ? 152  LEU B CG  1 
ATOM   11346 C  CD1 . LEU B 2 494  ? 96.895  109.981 153.034 1.00 110.03 ? 152  LEU B CD1 1 
ATOM   11347 C  CD2 . LEU B 2 494  ? 98.870  111.043 154.117 1.00 116.11 ? 152  LEU B CD2 1 
ATOM   11348 N  N   . ASN B 2 495  ? 94.595  111.621 156.698 1.00 122.89 ? 153  ASN B N   1 
ATOM   11349 C  CA  . ASN B 2 495  ? 94.193  110.823 157.850 1.00 127.57 ? 153  ASN B CA  1 
ATOM   11350 C  C   . ASN B 2 495  ? 92.738  110.389 157.747 1.00 129.01 ? 153  ASN B C   1 
ATOM   11351 O  O   . ASN B 2 495  ? 92.395  109.261 158.123 1.00 121.90 ? 153  ASN B O   1 
ATOM   11352 C  CB  . ASN B 2 495  ? 94.414  111.622 159.133 1.00 120.31 ? 153  ASN B CB  1 
ATOM   11353 C  CG  . ASN B 2 495  ? 95.876  111.742 159.501 1.00 128.03 ? 153  ASN B CG  1 
ATOM   11354 O  OD1 . ASN B 2 495  ? 96.685  110.876 159.171 1.00 132.22 ? 153  ASN B OD1 1 
ATOM   11355 N  ND2 . ASN B 2 495  ? 96.225  112.824 160.186 1.00 131.52 ? 153  ASN B ND2 1 
ATOM   11356 N  N   . GLU B 2 496  ? 91.862  111.262 157.243 1.00 128.69 ? 154  GLU B N   1 
ATOM   11357 C  CA  . GLU B 2 496  ? 90.442  110.938 157.296 1.00 125.88 ? 154  GLU B CA  1 
ATOM   11358 C  C   . GLU B 2 496  ? 90.005  110.069 156.122 1.00 126.89 ? 154  GLU B C   1 
ATOM   11359 O  O   . GLU B 2 496  ? 89.091  109.250 156.272 1.00 128.48 ? 154  GLU B O   1 
ATOM   11360 C  CB  . GLU B 2 496  ? 89.613  112.225 157.340 1.00 129.89 ? 154  GLU B CB  1 
ATOM   11361 C  CG  . GLU B 2 496  ? 88.133  112.015 157.647 1.00 152.07 ? 154  GLU B CG  1 
ATOM   11362 C  CD  . GLU B 2 496  ? 87.325  111.662 156.417 1.00 155.65 ? 154  GLU B CD  1 
ATOM   11363 O  OE1 . GLU B 2 496  ? 87.718  112.089 155.314 1.00 139.99 ? 154  GLU B OE1 1 
ATOM   11364 O  OE2 . GLU B 2 496  ? 86.307  110.951 156.550 1.00 146.75 ? 154  GLU B OE2 1 
ATOM   11365 N  N   . HIS B 2 497  ? 90.655  110.206 154.964 1.00 123.06 ? 155  HIS B N   1 
ATOM   11366 C  CA  . HIS B 2 497  ? 90.290  109.433 153.783 1.00 115.33 ? 155  HIS B CA  1 
ATOM   11367 C  C   . HIS B 2 497  ? 91.210  108.249 153.514 1.00 115.95 ? 155  HIS B C   1 
ATOM   11368 O  O   . HIS B 2 497  ? 90.756  107.245 152.953 1.00 115.02 ? 155  HIS B O   1 
ATOM   11369 C  CB  . HIS B 2 497  ? 90.242  110.348 152.553 1.00 123.77 ? 155  HIS B CB  1 
ATOM   11370 C  CG  . HIS B 2 497  ? 88.956  111.108 152.423 1.00 127.15 ? 155  HIS B CG  1 
ATOM   11371 N  ND1 . HIS B 2 497  ? 88.846  112.447 152.734 1.00 119.58 ? 155  HIS B ND1 1 
ATOM   11372 C  CD2 . HIS B 2 497  ? 87.720  110.710 152.035 1.00 128.35 ? 155  HIS B CD2 1 
ATOM   11373 C  CE1 . HIS B 2 497  ? 87.603  112.844 152.529 1.00 115.36 ? 155  HIS B CE1 1 
ATOM   11374 N  NE2 . HIS B 2 497  ? 86.898  111.809 152.109 1.00 129.49 ? 155  HIS B NE2 1 
ATOM   11375 N  N   . GLY B 2 498  ? 92.486  108.332 153.894 1.00 117.94 ? 156  GLY B N   1 
ATOM   11376 C  CA  . GLY B 2 498  ? 93.462  107.315 153.563 1.00 120.29 ? 156  GLY B CA  1 
ATOM   11377 C  C   . GLY B 2 498  ? 94.248  107.529 152.283 1.00 125.98 ? 156  GLY B C   1 
ATOM   11378 O  O   . GLY B 2 498  ? 95.194  106.773 152.027 1.00 126.32 ? 156  GLY B O   1 
ATOM   11379 N  N   . VAL B 2 499  ? 93.900  108.528 151.476 1.00 123.85 ? 157  VAL B N   1 
ATOM   11380 C  CA  . VAL B 2 499  ? 94.679  108.847 150.275 1.00 111.24 ? 157  VAL B CA  1 
ATOM   11381 C  C   . VAL B 2 499  ? 94.856  110.350 150.186 1.00 101.22 ? 157  VAL B C   1 
ATOM   11382 O  O   . VAL B 2 499  ? 94.005  111.126 150.641 1.00 108.21 ? 157  VAL B O   1 
ATOM   11383 C  CB  . VAL B 2 499  ? 93.999  108.322 148.988 1.00 121.35 ? 157  VAL B CB  1 
ATOM   11384 C  CG1 . VAL B 2 499  ? 94.139  106.807 148.891 1.00 110.41 ? 157  VAL B CG1 1 
ATOM   11385 C  CG2 . VAL B 2 499  ? 92.535  108.735 148.942 1.00 129.75 ? 157  VAL B CG2 1 
ATOM   11386 N  N   . PRO B 2 500  ? 95.963  110.797 149.594 1.00 96.78  ? 158  PRO B N   1 
ATOM   11387 C  CA  . PRO B 2 500  ? 96.253  112.234 149.583 1.00 91.78  ? 158  PRO B CA  1 
ATOM   11388 C  C   . PRO B 2 500  ? 95.327  112.976 148.639 1.00 92.37  ? 158  PRO B C   1 
ATOM   11389 O  O   . PRO B 2 500  ? 94.767  112.383 147.703 1.00 98.66  ? 158  PRO B O   1 
ATOM   11390 C  CB  . PRO B 2 500  ? 97.713  112.294 149.109 1.00 77.86  ? 158  PRO B CB  1 
ATOM   11391 C  CG  . PRO B 2 500  ? 97.885  111.081 148.280 1.00 91.46  ? 158  PRO B CG  1 
ATOM   11392 C  CD  . PRO B 2 500  ? 96.996  110.022 148.882 1.00 90.13  ? 158  PRO B CD  1 
ATOM   11393 N  N   . PRO B 2 501  ? 95.142  114.276 148.852 1.00 89.90  ? 159  PRO B N   1 
ATOM   11394 C  CA  . PRO B 2 501  ? 94.225  115.056 148.013 1.00 81.20  ? 159  PRO B CA  1 
ATOM   11395 C  C   . PRO B 2 501  ? 94.703  115.113 146.573 1.00 91.38  ? 159  PRO B C   1 
ATOM   11396 O  O   . PRO B 2 501  ? 95.877  114.840 146.282 1.00 103.53 ? 159  PRO B O   1 
ATOM   11397 C  CB  . PRO B 2 501  ? 94.244  116.450 148.664 1.00 80.29  ? 159  PRO B CB  1 
ATOM   11398 C  CG  . PRO B 2 501  ? 95.462  116.466 149.538 1.00 85.08  ? 159  PRO B CG  1 
ATOM   11399 C  CD  . PRO B 2 501  ? 95.666  115.059 149.983 1.00 91.41  ? 159  PRO B CD  1 
ATOM   11400 N  N   . PRO B 2 502  ? 93.812  115.463 145.638 1.00 93.10  ? 160  PRO B N   1 
ATOM   11401 C  CA  . PRO B 2 502  ? 94.199  115.530 144.221 1.00 84.08  ? 160  PRO B CA  1 
ATOM   11402 C  C   . PRO B 2 502  ? 94.931  116.819 143.870 1.00 73.25  ? 160  PRO B C   1 
ATOM   11403 O  O   . PRO B 2 502  ? 95.036  117.176 142.692 1.00 73.64  ? 160  PRO B O   1 
ATOM   11404 C  CB  . PRO B 2 502  ? 92.855  115.437 143.482 1.00 85.38  ? 160  PRO B CB  1 
ATOM   11405 C  CG  . PRO B 2 502  ? 91.834  115.040 144.533 1.00 91.35  ? 160  PRO B CG  1 
ATOM   11406 C  CD  . PRO B 2 502  ? 92.358  115.591 145.813 1.00 98.04  ? 160  PRO B CD  1 
ATOM   11407 N  N   . GLN B 2 503  ? 95.431  117.527 144.873 1.00 78.06  ? 161  GLN B N   1 
ATOM   11408 C  CA  . GLN B 2 503  ? 96.117  118.793 144.674 1.00 80.16  ? 161  GLN B CA  1 
ATOM   11409 C  C   . GLN B 2 503  ? 97.625  118.645 144.821 1.00 79.73  ? 161  GLN B C   1 
ATOM   11410 O  O   . GLN B 2 503  ? 98.114  117.711 145.463 1.00 78.02  ? 161  GLN B O   1 
ATOM   11411 C  CB  . GLN B 2 503  ? 95.595  119.823 145.680 1.00 79.43  ? 161  GLN B CB  1 
ATOM   11412 C  CG  . GLN B 2 503  ? 94.085  119.813 145.803 1.00 80.09  ? 161  GLN B CG  1 
ATOM   11413 C  CD  . GLN B 2 503  ? 93.599  120.518 147.046 1.00 77.11  ? 161  GLN B CD  1 
ATOM   11414 O  OE1 . GLN B 2 503  ? 92.846  119.953 147.839 1.00 79.65  ? 161  GLN B OE1 1 
ATOM   11415 N  NE2 . GLN B 2 503  ? 94.030  121.759 147.228 1.00 78.59  ? 161  GLN B NE2 1 
ATOM   11416 N  N   . PRO B 2 504  ? 98.394  119.558 144.228 1.00 67.23  ? 162  PRO B N   1 
ATOM   11417 C  CA  . PRO B 2 504  ? 99.850  119.526 144.408 1.00 62.35  ? 162  PRO B CA  1 
ATOM   11418 C  C   . PRO B 2 504  ? 100.243 119.800 145.851 1.00 74.67  ? 162  PRO B C   1 
ATOM   11419 O  O   . PRO B 2 504  ? 99.518  120.449 146.609 1.00 92.70  ? 162  PRO B O   1 
ATOM   11420 C  CB  . PRO B 2 504  ? 100.353 120.639 143.478 1.00 60.36  ? 162  PRO B CB  1 
ATOM   11421 C  CG  . PRO B 2 504  ? 99.150  121.487 143.183 1.00 69.51  ? 162  PRO B CG  1 
ATOM   11422 C  CD  . PRO B 2 504  ? 97.980  120.563 143.234 1.00 72.63  ? 162  PRO B CD  1 
ATOM   11423 N  N   . ALA B 2 505  ? 101.414 119.290 146.226 1.00 60.01  ? 163  ALA B N   1 
ATOM   11424 C  CA  . ALA B 2 505  ? 101.940 119.447 147.574 1.00 56.90  ? 163  ALA B CA  1 
ATOM   11425 C  C   . ALA B 2 505  ? 103.448 119.640 147.506 1.00 65.33  ? 163  ALA B C   1 
ATOM   11426 O  O   . ALA B 2 505  ? 104.095 119.295 146.515 1.00 72.97  ? 163  ALA B O   1 
ATOM   11427 C  CB  . ALA B 2 505  ? 101.597 118.243 148.460 1.00 86.13  ? 163  ALA B CB  1 
ATOM   11428 N  N   . ILE B 2 506  ? 104.004 120.207 148.576 1.00 72.30  ? 164  ILE B N   1 
ATOM   11429 C  CA  . ILE B 2 506  ? 105.435 120.469 148.680 1.00 78.78  ? 164  ILE B CA  1 
ATOM   11430 C  C   . ILE B 2 506  ? 105.981 119.662 149.848 1.00 86.59  ? 164  ILE B C   1 
ATOM   11431 O  O   . ILE B 2 506  ? 105.453 119.739 150.964 1.00 94.72  ? 164  ILE B O   1 
ATOM   11432 C  CB  . ILE B 2 506  ? 105.730 121.968 148.872 1.00 72.95  ? 164  ILE B CB  1 
ATOM   11433 C  CG1 . ILE B 2 506  ? 104.983 122.802 147.830 1.00 75.41  ? 164  ILE B CG1 1 
ATOM   11434 C  CG2 . ILE B 2 506  ? 107.225 122.229 148.773 1.00 78.94  ? 164  ILE B CG2 1 
ATOM   11435 C  CD1 . ILE B 2 506  ? 105.215 124.294 147.965 1.00 71.69  ? 164  ILE B CD1 1 
ATOM   11436 N  N   . PHE B 2 507  ? 107.038 118.897 149.591 1.00 70.71  ? 165  PHE B N   1 
ATOM   11437 C  CA  . PHE B 2 507  ? 107.681 118.061 150.592 1.00 62.49  ? 165  PHE B CA  1 
ATOM   11438 C  C   . PHE B 2 507  ? 109.088 118.560 150.886 1.00 69.43  ? 165  PHE B C   1 
ATOM   11439 O  O   . PHE B 2 507  ? 109.727 119.215 150.058 1.00 82.49  ? 165  PHE B O   1 
ATOM   11440 C  CB  . PHE B 2 507  ? 107.753 116.609 150.112 1.00 63.55  ? 165  PHE B CB  1 
ATOM   11441 C  CG  . PHE B 2 507  ? 106.417 116.007 149.814 1.00 61.29  ? 165  PHE B CG  1 
ATOM   11442 C  CD1 . PHE B 2 507  ? 105.694 115.361 150.800 1.00 79.35  ? 165  PHE B CD1 1 
ATOM   11443 C  CD2 . PHE B 2 507  ? 105.876 116.100 148.543 1.00 60.80  ? 165  PHE B CD2 1 
ATOM   11444 C  CE1 . PHE B 2 507  ? 104.456 114.811 150.522 1.00 68.61  ? 165  PHE B CE1 1 
ATOM   11445 C  CE2 . PHE B 2 507  ? 104.641 115.555 148.259 1.00 74.41  ? 165  PHE B CE2 1 
ATOM   11446 C  CZ  . PHE B 2 507  ? 103.930 114.909 149.250 1.00 62.98  ? 165  PHE B CZ  1 
ATOM   11447 N  N   . LYS B 2 508  ? 109.567 118.245 152.090 1.00 65.54  ? 166  LYS B N   1 
ATOM   11448 C  CA  . LYS B 2 508  ? 110.902 118.681 152.482 1.00 62.78  ? 166  LYS B CA  1 
ATOM   11449 C  C   . LYS B 2 508  ? 111.975 117.902 151.732 1.00 77.26  ? 166  LYS B C   1 
ATOM   11450 O  O   . LYS B 2 508  ? 112.910 118.488 151.177 1.00 85.74  ? 166  LYS B O   1 
ATOM   11451 C  CB  . LYS B 2 508  ? 111.091 118.510 153.987 1.00 77.93  ? 166  LYS B CB  1 
ATOM   11452 C  CG  . LYS B 2 508  ? 112.452 118.966 154.467 1.00 87.57  ? 166  LYS B CG  1 
ATOM   11453 C  CD  . LYS B 2 508  ? 112.526 118.985 155.976 1.00 110.08 ? 166  LYS B CD  1 
ATOM   11454 C  CE  . LYS B 2 508  ? 112.473 117.568 156.517 1.00 114.35 ? 166  LYS B CE  1 
ATOM   11455 N  NZ  . LYS B 2 508  ? 113.778 116.866 156.357 1.00 114.10 ? 166  LYS B NZ  1 
ATOM   11456 N  N   . ASP B 2 509  ? 111.840 116.576 151.693 1.00 78.12  ? 167  ASP B N   1 
ATOM   11457 C  CA  . ASP B 2 509  ? 112.811 115.677 151.086 1.00 66.05  ? 167  ASP B CA  1 
ATOM   11458 C  C   . ASP B 2 509  ? 112.072 114.636 150.258 1.00 60.46  ? 167  ASP B C   1 
ATOM   11459 O  O   . ASP B 2 509  ? 110.847 114.506 150.331 1.00 74.93  ? 167  ASP B O   1 
ATOM   11460 C  CB  . ASP B 2 509  ? 113.682 114.969 152.135 1.00 100.95 ? 167  ASP B CB  1 
ATOM   11461 C  CG  . ASP B 2 509  ? 114.771 115.861 152.703 1.00 119.89 ? 167  ASP B CG  1 
ATOM   11462 O  OD1 . ASP B 2 509  ? 114.886 117.027 152.277 1.00 115.31 ? 167  ASP B OD1 1 
ATOM   11463 O  OD2 . ASP B 2 509  ? 115.522 115.385 153.580 1.00 105.65 ? 167  ASP B OD2 1 
ATOM   11464 N  N   . LEU B 2 510  ? 112.831 113.894 149.451 1.00 64.54  ? 168  LEU B N   1 
ATOM   11465 C  CA  . LEU B 2 510  ? 112.253 112.740 148.773 1.00 70.11  ? 168  LEU B CA  1 
ATOM   11466 C  C   . LEU B 2 510  ? 111.851 111.656 149.769 1.00 92.11  ? 168  LEU B C   1 
ATOM   11467 O  O   . LEU B 2 510  ? 110.823 110.991 149.592 1.00 90.61  ? 168  LEU B O   1 
ATOM   11468 C  CB  . LEU B 2 510  ? 113.233 112.191 147.738 1.00 62.64  ? 168  LEU B CB  1 
ATOM   11469 C  CG  . LEU B 2 510  ? 112.654 111.050 146.906 1.00 54.50  ? 168  LEU B CG  1 
ATOM   11470 C  CD1 . LEU B 2 510  ? 111.507 111.572 146.058 1.00 62.16  ? 168  LEU B CD1 1 
ATOM   11471 C  CD2 . LEU B 2 510  ? 113.727 110.415 146.038 1.00 65.77  ? 168  LEU B CD2 1 
ATOM   11472 N  N   . GLY B 2 511  ? 112.644 111.471 150.828 1.00 88.07  ? 169  GLY B N   1 
ATOM   11473 C  CA  . GLY B 2 511  ? 112.303 110.484 151.840 1.00 87.13  ? 169  GLY B CA  1 
ATOM   11474 C  C   . GLY B 2 511  ? 111.003 110.777 152.565 1.00 83.68  ? 169  GLY B C   1 
ATOM   11475 O  O   . GLY B 2 511  ? 110.251 109.852 152.900 1.00 95.44  ? 169  GLY B O   1 
ATOM   11476 N  N   . VAL B 2 512  ? 110.698 112.059 152.787 1.00 81.75  ? 170  VAL B N   1 
ATOM   11477 C  CA  . VAL B 2 512  ? 109.418 112.408 153.396 1.00 78.80  ? 170  VAL B CA  1 
ATOM   11478 C  C   . VAL B 2 512  ? 108.275 111.972 152.493 1.00 77.40  ? 170  VAL B C   1 
ATOM   11479 O  O   . VAL B 2 512  ? 107.262 111.438 152.961 1.00 88.87  ? 170  VAL B O   1 
ATOM   11480 C  CB  . VAL B 2 512  ? 109.353 113.916 153.700 1.00 72.79  ? 170  VAL B CB  1 
ATOM   11481 C  CG1 . VAL B 2 512  ? 107.985 114.290 154.262 1.00 67.57  ? 170  VAL B CG1 1 
ATOM   11482 C  CG2 . VAL B 2 512  ? 110.458 114.316 154.670 1.00 83.20  ? 170  VAL B CG2 1 
ATOM   11483 N  N   . ALA B 2 513  ? 108.422 112.175 151.181 1.00 67.73  ? 171  ALA B N   1 
ATOM   11484 C  CA  . ALA B 2 513  ? 107.389 111.701 150.271 1.00 64.90  ? 171  ALA B CA  1 
ATOM   11485 C  C   . ALA B 2 513  ? 107.317 110.181 150.281 1.00 79.07  ? 171  ALA B C   1 
ATOM   11486 O  O   . ALA B 2 513  ? 106.229 109.613 150.132 1.00 92.18  ? 171  ALA B O   1 
ATOM   11487 C  CB  . ALA B 2 513  ? 107.651 112.217 148.856 1.00 78.87  ? 171  ALA B CB  1 
ATOM   11488 N  N   . GLN B 2 514  ? 108.458 109.509 150.464 1.00 84.68  ? 172  GLN B N   1 
ATOM   11489 C  CA  . GLN B 2 514  ? 108.431 108.052 150.513 1.00 88.03  ? 172  GLN B CA  1 
ATOM   11490 C  C   . GLN B 2 514  ? 107.717 107.547 151.758 1.00 94.93  ? 172  GLN B C   1 
ATOM   11491 O  O   . GLN B 2 514  ? 107.192 106.428 151.757 1.00 91.26  ? 172  GLN B O   1 
ATOM   11492 C  CB  . GLN B 2 514  ? 109.854 107.495 150.474 1.00 81.50  ? 172  GLN B CB  1 
ATOM   11493 C  CG  . GLN B 2 514  ? 110.572 107.694 149.159 1.00 84.73  ? 172  GLN B CG  1 
ATOM   11494 C  CD  . GLN B 2 514  ? 111.838 106.869 149.066 1.00 94.47  ? 172  GLN B CD  1 
ATOM   11495 O  OE1 . GLN B 2 514  ? 112.946 107.392 149.190 1.00 88.41  ? 172  GLN B OE1 1 
ATOM   11496 N  NE2 . GLN B 2 514  ? 111.679 105.570 148.850 1.00 102.69 ? 172  GLN B NE2 1 
ATOM   11497 N  N   . GLN B 2 515  ? 107.678 108.352 152.820 1.00 97.84  ? 173  GLN B N   1 
ATOM   11498 C  CA  . GLN B 2 515  ? 107.058 107.940 154.074 1.00 89.74  ? 173  GLN B CA  1 
ATOM   11499 C  C   . GLN B 2 515  ? 105.665 108.520 154.291 1.00 100.75 ? 173  GLN B C   1 
ATOM   11500 O  O   . GLN B 2 515  ? 105.155 108.456 155.413 1.00 113.61 ? 173  GLN B O   1 
ATOM   11501 C  CB  . GLN B 2 515  ? 107.949 108.299 155.262 1.00 98.91  ? 173  GLN B CB  1 
ATOM   11502 C  CG  . GLN B 2 515  ? 109.352 107.740 155.185 1.00 113.34 ? 173  GLN B CG  1 
ATOM   11503 C  CD  . GLN B 2 515  ? 110.250 108.318 156.255 1.00 129.20 ? 173  GLN B CD  1 
ATOM   11504 O  OE1 . GLN B 2 515  ? 109.777 108.965 157.190 1.00 128.77 ? 173  GLN B OE1 1 
ATOM   11505 N  NE2 . GLN B 2 515  ? 111.550 108.088 156.129 1.00 132.46 ? 173  GLN B NE2 1 
ATOM   11506 N  N   . ALA B 2 516  ? 105.035 109.082 153.262 1.00 109.29 ? 174  ALA B N   1 
ATOM   11507 C  CA  . ALA B 2 516  ? 103.708 109.664 153.441 1.00 112.24 ? 174  ALA B CA  1 
ATOM   11508 C  C   . ALA B 2 516  ? 102.656 108.571 153.303 1.00 113.80 ? 174  ALA B C   1 
ATOM   11509 O  O   . ALA B 2 516  ? 102.361 108.113 152.195 1.00 121.47 ? 174  ALA B O   1 
ATOM   11510 C  CB  . ALA B 2 516  ? 103.476 110.786 152.434 1.00 86.13  ? 174  ALA B CB  1 
ATOM   11511 N  N   . CYS B 2 517  ? 102.077 108.169 154.433 1.00 113.77 ? 175  CYS B N   1 
ATOM   11512 C  CA  . CYS B 2 517  ? 101.069 107.122 154.480 1.00 123.86 ? 175  CYS B CA  1 
ATOM   11513 C  C   . CYS B 2 517  ? 100.098 107.456 155.601 1.00 140.78 ? 175  CYS B C   1 
ATOM   11514 O  O   . CYS B 2 517  ? 100.386 108.290 156.464 1.00 137.85 ? 175  CYS B O   1 
ATOM   11515 C  CB  . CYS B 2 517  ? 101.684 105.734 154.696 1.00 135.91 ? 175  CYS B CB  1 
ATOM   11516 S  SG  . CYS B 2 517  ? 102.625 105.089 153.293 1.00 155.89 ? 175  CYS B SG  1 
ATOM   11517 N  N   . SER B 2 518  ? 98.939  106.801 155.581 1.00 146.91 ? 176  SER B N   1 
ATOM   11518 C  CA  . SER B 2 518  ? 97.962  107.043 156.631 1.00 142.06 ? 176  SER B CA  1 
ATOM   11519 C  C   . SER B 2 518  ? 98.537  106.605 157.972 1.00 159.17 ? 176  SER B C   1 
ATOM   11520 O  O   . SER B 2 518  ? 99.247  105.601 158.065 1.00 165.80 ? 176  SER B O   1 
ATOM   11521 C  CB  . SER B 2 518  ? 96.667  106.287 156.338 1.00 138.75 ? 176  SER B CB  1 
ATOM   11522 O  OG  . SER B 2 518  ? 96.901  104.892 156.258 1.00 155.62 ? 176  SER B OG  1 
ATOM   11523 N  N   . LYS B 2 519  ? 98.233  107.379 159.013 1.00 155.64 ? 177  LYS B N   1 
ATOM   11524 C  CA  . LYS B 2 519  ? 98.753  107.071 160.340 1.00 160.35 ? 177  LYS B CA  1 
ATOM   11525 C  C   . LYS B 2 519  ? 98.240  105.732 160.860 1.00 167.39 ? 177  LYS B C   1 
ATOM   11526 O  O   . LYS B 2 519  ? 99.000  104.954 161.448 1.00 163.06 ? 177  LYS B O   1 
ATOM   11527 C  CB  . LYS B 2 519  ? 98.404  108.200 161.311 1.00 171.78 ? 177  LYS B CB  1 
ATOM   11528 C  CG  . LYS B 2 519  ? 98.714  107.892 162.769 1.00 183.25 ? 177  LYS B CG  1 
ATOM   11529 C  CD  . LYS B 2 519  ? 98.370  109.063 163.680 1.00 187.62 ? 177  LYS B CD  1 
ATOM   11530 C  CE  . LYS B 2 519  ? 96.983  109.622 163.391 1.00 176.92 ? 177  LYS B CE  1 
ATOM   11531 N  NZ  . LYS B 2 519  ? 95.923  108.576 163.427 1.00 176.90 ? 177  LYS B NZ  1 
ATOM   11532 N  N   . GLY B 2 520  ? 96.953  105.440 160.647 1.00 164.86 ? 178  GLY B N   1 
ATOM   11533 C  CA  . GLY B 2 520  ? 96.392  104.199 161.163 1.00 167.98 ? 178  GLY B CA  1 
ATOM   11534 C  C   . GLY B 2 520  ? 96.996  102.939 160.570 1.00 174.39 ? 178  GLY B C   1 
ATOM   11535 O  O   . GLY B 2 520  ? 97.319  101.998 161.300 1.00 172.87 ? 178  GLY B O   1 
ATOM   11536 N  N   . THR B 2 521  ? 97.177  102.902 159.251 1.00 171.24 ? 179  THR B N   1 
ATOM   11537 C  CA  . THR B 2 521  ? 97.753  101.729 158.607 1.00 176.34 ? 179  THR B CA  1 
ATOM   11538 C  C   . THR B 2 521  ? 98.662  102.151 157.466 1.00 173.68 ? 179  THR B C   1 
ATOM   11539 O  O   . THR B 2 521  ? 98.417  103.157 156.796 1.00 169.39 ? 179  THR B O   1 
ATOM   11540 C  CB  . THR B 2 521  ? 96.675  100.778 158.054 1.00 168.84 ? 179  THR B CB  1 
ATOM   11541 O  OG1 . THR B 2 521  ? 95.694  101.529 157.328 1.00 161.83 ? 179  THR B OG1 1 
ATOM   11542 C  CG2 . THR B 2 521  ? 95.999  100.000 159.176 1.00 168.57 ? 179  THR B CG2 1 
ATOM   11543 N  N   . MET B 2 522  ? 99.717  101.369 157.248 1.00 173.26 ? 180  MET B N   1 
ATOM   11544 C  CA  . MET B 2 522  ? 100.671 101.661 156.183 1.00 173.46 ? 180  MET B CA  1 
ATOM   11545 C  C   . MET B 2 522  ? 100.221 100.922 154.930 1.00 162.52 ? 180  MET B C   1 
ATOM   11546 O  O   . MET B 2 522  ? 100.380 99.703  154.824 1.00 154.36 ? 180  MET B O   1 
ATOM   11547 C  CB  . MET B 2 522  ? 102.080 101.250 156.593 1.00 181.46 ? 180  MET B CB  1 
ATOM   11548 C  CG  . MET B 2 522  ? 102.539 101.826 157.922 1.00 186.89 ? 180  MET B CG  1 
ATOM   11549 S  SD  . MET B 2 522  ? 102.247 103.596 158.081 1.00 191.66 ? 180  MET B SD  1 
ATOM   11550 C  CE  . MET B 2 522  ? 102.975 103.907 159.687 1.00 145.71 ? 180  MET B CE  1 
ATOM   11551 N  N   . VAL B 2 523  ? 99.658  101.654 153.973 1.00 149.99 ? 181  VAL B N   1 
ATOM   11552 C  CA  . VAL B 2 523  ? 99.212  101.092 152.705 1.00 146.12 ? 181  VAL B CA  1 
ATOM   11553 C  C   . VAL B 2 523  ? 99.796  101.973 151.612 1.00 142.10 ? 181  VAL B C   1 
ATOM   11554 O  O   . VAL B 2 523  ? 99.725  103.203 151.704 1.00 129.00 ? 181  VAL B O   1 
ATOM   11555 C  CB  . VAL B 2 523  ? 97.677  101.010 152.595 1.00 140.23 ? 181  VAL B CB  1 
ATOM   11556 C  CG1 . VAL B 2 523  ? 97.275  100.418 151.251 1.00 129.54 ? 181  VAL B CG1 1 
ATOM   11557 C  CG2 . VAL B 2 523  ? 97.108  100.167 153.730 1.00 140.58 ? 181  VAL B CG2 1 
ATOM   11558 N  N   . LYS B 2 524  ? 100.374 101.354 150.589 1.00 133.39 ? 182  LYS B N   1 
ATOM   11559 C  CA  . LYS B 2 524  ? 100.956 102.136 149.511 1.00 118.05 ? 182  LYS B CA  1 
ATOM   11560 C  C   . LYS B 2 524  ? 99.892  102.900 148.730 1.00 122.67 ? 182  LYS B C   1 
ATOM   11561 O  O   . LYS B 2 524  ? 98.800  102.393 148.461 1.00 128.77 ? 182  LYS B O   1 
ATOM   11562 C  CB  . LYS B 2 524  ? 101.760 101.228 148.583 1.00 114.17 ? 182  LYS B CB  1 
ATOM   11563 C  CG  . LYS B 2 524  ? 102.914 100.550 149.301 1.00 128.14 ? 182  LYS B CG  1 
ATOM   11564 C  CD  . LYS B 2 524  ? 103.746 101.570 150.069 1.00 124.83 ? 182  LYS B CD  1 
ATOM   11565 C  CE  . LYS B 2 524  ? 104.871 100.907 150.844 1.00 143.07 ? 182  LYS B CE  1 
ATOM   11566 N  NZ  . LYS B 2 524  ? 105.841 100.224 149.950 1.00 130.75 ? 182  LYS B NZ  1 
ATOM   11567 N  N   . ASN B 2 525  ? 100.236 104.134 148.372 1.00 100.45 ? 183  ASN B N   1 
ATOM   11568 C  CA  . ASN B 2 525  ? 99.401  105.046 147.608 1.00 74.46  ? 183  ASN B CA  1 
ATOM   11569 C  C   . ASN B 2 525  ? 100.252 105.614 146.479 1.00 86.80  ? 183  ASN B C   1 
ATOM   11570 O  O   . ASN B 2 525  ? 101.483 105.611 146.553 1.00 101.35 ? 183  ASN B O   1 
ATOM   11571 C  CB  . ASN B 2 525  ? 98.786  106.154 148.483 1.00 69.01  ? 183  ASN B CB  1 
ATOM   11572 C  CG  . ASN B 2 525  ? 99.821  106.930 149.266 1.00 79.78  ? 183  ASN B CG  1 
ATOM   11573 O  OD1 . ASN B 2 525  ? 101.023 106.742 149.093 1.00 91.88  ? 183  ASN B OD1 1 
ATOM   11574 N  ND2 . ASN B 2 525  ? 99.356  107.812 150.144 1.00 82.26  ? 183  ASN B ND2 1 
ATOM   11575 N  N   . ALA B 2 526  ? 99.589  106.078 145.421 1.00 79.13  ? 184  ALA B N   1 
ATOM   11576 C  CA  . ALA B 2 526  ? 100.257 106.599 144.229 1.00 80.98  ? 184  ALA B CA  1 
ATOM   11577 C  C   . ALA B 2 526  ? 101.453 107.516 144.499 1.00 89.21  ? 184  ALA B C   1 
ATOM   11578 O  O   . ALA B 2 526  ? 102.477 107.413 143.809 1.00 98.22  ? 184  ALA B O   1 
ATOM   11579 C  CB  . ALA B 2 526  ? 99.239  107.345 143.362 1.00 72.41  ? 184  ALA B CB  1 
ATOM   11580 N  N   . THR B 2 527  ? 101.359 108.389 145.509 1.00 78.08  ? 185  THR B N   1 
ATOM   11581 C  CA  . THR B 2 527  ? 102.485 109.272 145.813 1.00 68.41  ? 185  THR B CA  1 
ATOM   11582 C  C   . THR B 2 527  ? 103.712 108.478 146.245 1.00 88.03  ? 185  THR B C   1 
ATOM   11583 O  O   . THR B 2 527  ? 104.839 108.760 145.802 1.00 102.51 ? 185  THR B O   1 
ATOM   11584 C  CB  . THR B 2 527  ? 102.089 110.269 146.909 1.00 63.64  ? 185  THR B CB  1 
ATOM   11585 O  OG1 . THR B 2 527  ? 101.162 111.227 146.383 1.00 75.63  ? 185  THR B OG1 1 
ATOM   11586 C  CG2 . THR B 2 527  ? 103.315 111.004 147.446 1.00 59.15  ? 185  THR B CG2 1 
ATOM   11587 N  N   . THR B 2 528  ? 103.508 107.441 147.062 1.00 83.99  ? 186  THR B N   1 
ATOM   11588 C  CA  . THR B 2 528  ? 104.639 106.637 147.504 1.00 78.81  ? 186  THR B CA  1 
ATOM   11589 C  C   . THR B 2 528  ? 105.263 105.885 146.337 1.00 89.33  ? 186  THR B C   1 
ATOM   11590 O  O   . THR B 2 528  ? 106.489 105.750 146.269 1.00 95.71  ? 186  THR B O   1 
ATOM   11591 C  CB  . THR B 2 528  ? 104.209 105.673 148.611 1.00 79.76  ? 186  THR B CB  1 
ATOM   11592 O  OG1 . THR B 2 528  ? 102.975 105.037 148.251 1.00 101.61 ? 186  THR B OG1 1 
ATOM   11593 C  CG2 . THR B 2 528  ? 104.033 106.416 149.933 1.00 71.52  ? 186  THR B CG2 1 
ATOM   11594 N  N   . ASP B 2 529  ? 104.438 105.360 145.425 1.00 76.02  ? 187  ASP B N   1 
ATOM   11595 C  CA  . ASP B 2 529  ? 104.995 104.651 144.279 1.00 87.95  ? 187  ASP B CA  1 
ATOM   11596 C  C   . ASP B 2 529  ? 105.821 105.589 143.407 1.00 91.80  ? 187  ASP B C   1 
ATOM   11597 O  O   . ASP B 2 529  ? 106.893 105.209 142.914 1.00 99.48  ? 187  ASP B O   1 
ATOM   11598 C  CB  . ASP B 2 529  ? 103.878 103.998 143.466 1.00 104.13 ? 187  ASP B CB  1 
ATOM   11599 C  CG  . ASP B 2 529  ? 103.090 102.985 144.272 1.00 116.60 ? 187  ASP B CG  1 
ATOM   11600 O  OD1 . ASP B 2 529  ? 103.432 102.772 145.455 1.00 110.10 ? 187  ASP B OD1 1 
ATOM   11601 O  OD2 . ASP B 2 529  ? 102.137 102.392 143.722 1.00 120.84 ? 187  ASP B OD2 1 
ATOM   11602 N  N   . ALA B 2 530  ? 105.340 106.822 143.205 1.00 80.83  ? 188  ALA B N   1 
ATOM   11603 C  CA  . ALA B 2 530  ? 106.096 107.775 142.394 1.00 72.87  ? 188  ALA B CA  1 
ATOM   11604 C  C   . ALA B 2 530  ? 107.443 108.086 143.038 1.00 74.45  ? 188  ALA B C   1 
ATOM   11605 O  O   . ALA B 2 530  ? 108.490 108.101 142.364 1.00 84.74  ? 188  ALA B O   1 
ATOM   11606 C  CB  . ALA B 2 530  ? 105.281 109.051 142.186 1.00 73.01  ? 188  ALA B CB  1 
ATOM   11607 N  N   . ALA B 2 531  ? 107.449 108.224 144.366 1.00 67.70  ? 189  ALA B N   1 
ATOM   11608 C  CA  . ALA B 2 531  ? 108.696 108.521 145.062 1.00 56.30  ? 189  ALA B CA  1 
ATOM   11609 C  C   . ALA B 2 531  ? 109.654 107.334 145.021 1.00 80.15  ? 189  ALA B C   1 
ATOM   11610 O  O   . ALA B 2 531  ? 110.867 107.515 144.861 1.00 90.58  ? 189  ALA B O   1 
ATOM   11611 C  CB  . ALA B 2 531  ? 108.403 108.933 146.505 1.00 68.16  ? 189  ALA B CB  1 
ATOM   11612 N  N   . ASP B 2 532  ? 109.133 106.114 145.164 1.00 76.40  ? 190  ASP B N   1 
ATOM   11613 C  CA  . ASP B 2 532  ? 109.977 104.921 145.112 1.00 79.00  ? 190  ASP B CA  1 
ATOM   11614 C  C   . ASP B 2 532  ? 110.600 104.735 143.727 1.00 80.37  ? 190  ASP B C   1 
ATOM   11615 O  O   . ASP B 2 532  ? 111.776 104.352 143.604 1.00 92.50  ? 190  ASP B O   1 
ATOM   11616 C  CB  . ASP B 2 532  ? 109.153 103.698 145.509 1.00 95.58  ? 190  ASP B CB  1 
ATOM   11617 C  CG  . ASP B 2 532  ? 108.990 103.573 147.012 1.00 102.97 ? 190  ASP B CG  1 
ATOM   11618 O  OD1 . ASP B 2 532  ? 108.026 102.915 147.459 1.00 96.51  ? 190  ASP B OD1 1 
ATOM   11619 O  OD2 . ASP B 2 532  ? 109.814 104.156 147.747 1.00 102.67 ? 190  ASP B OD2 1 
ATOM   11620 N  N   . LYS B 2 533  ? 109.814 104.982 142.676 1.00 79.22  ? 191  LYS B N   1 
ATOM   11621 C  CA  . LYS B 2 533  ? 110.329 104.958 141.309 1.00 78.70  ? 191  LYS B CA  1 
ATOM   11622 C  C   . LYS B 2 533  ? 111.506 105.921 141.170 1.00 76.97  ? 191  LYS B C   1 
ATOM   11623 O  O   . LYS B 2 533  ? 112.586 105.563 140.657 1.00 83.61  ? 191  LYS B O   1 
ATOM   11624 C  CB  . LYS B 2 533  ? 109.195 105.319 140.353 1.00 73.96  ? 191  LYS B CB  1 
ATOM   11625 C  CG  . LYS B 2 533  ? 109.205 104.609 139.019 1.00 82.92  ? 191  LYS B CG  1 
ATOM   11626 C  CD  . LYS B 2 533  ? 107.984 105.026 138.214 1.00 77.28  ? 191  LYS B CD  1 
ATOM   11627 C  CE  . LYS B 2 533  ? 107.829 104.188 136.961 1.00 84.13  ? 191  LYS B CE  1 
ATOM   11628 N  NZ  . LYS B 2 533  ? 109.069 104.182 136.145 1.00 110.03 ? 191  LYS B NZ  1 
ATOM   11629 N  N   . MET B 2 534  ? 111.334 107.135 141.690 1.00 79.09  ? 192  MET B N   1 
ATOM   11630 C  CA  . MET B 2 534  ? 112.400 108.120 141.577 1.00 67.26  ? 192  MET B CA  1 
ATOM   11631 C  C   . MET B 2 534  ? 113.625 107.675 142.381 1.00 66.87  ? 192  MET B C   1 
ATOM   11632 O  O   . MET B 2 534  ? 114.766 107.905 141.957 1.00 80.54  ? 192  MET B O   1 
ATOM   11633 C  CB  . MET B 2 534  ? 111.902 109.501 142.024 1.00 68.42  ? 192  MET B CB  1 
ATOM   11634 C  CG  . MET B 2 534  ? 112.782 110.651 141.558 1.00 67.42  ? 192  MET B CG  1 
ATOM   11635 S  SD  . MET B 2 534  ? 113.007 110.650 139.767 1.00 91.51  ? 192  MET B SD  1 
ATOM   11636 C  CE  . MET B 2 534  ? 114.792 110.686 139.652 1.00 70.24  ? 192  MET B CE  1 
ATOM   11637 N  N   . SER B 2 535  ? 113.413 107.022 143.534 1.00 73.88  ? 193  SER B N   1 
ATOM   11638 C  CA  . SER B 2 535  ? 114.553 106.554 144.319 1.00 80.58  ? 193  SER B CA  1 
ATOM   11639 C  C   . SER B 2 535  ? 115.376 105.502 143.571 1.00 81.62  ? 193  SER B C   1 
ATOM   11640 O  O   . SER B 2 535  ? 116.610 105.521 143.655 1.00 92.01  ? 193  SER B O   1 
ATOM   11641 C  CB  . SER B 2 535  ? 114.041 106.036 145.682 1.00 87.70  ? 193  SER B CB  1 
ATOM   11642 O  OG  . SER B 2 535  ? 113.549 104.726 145.574 1.00 94.79  ? 193  SER B OG  1 
ATOM   11643 N  N   . LYS B 2 536  ? 114.730 104.553 142.886 1.00 77.70  ? 194  LYS B N   1 
ATOM   11644 C  CA  . LYS B 2 536  ? 115.518 103.618 142.082 1.00 74.47  ? 194  LYS B CA  1 
ATOM   11645 C  C   . LYS B 2 536  ? 116.293 104.338 141.003 1.00 77.28  ? 194  LYS B C   1 
ATOM   11646 O  O   . LYS B 2 536  ? 117.403 103.913 140.653 1.00 83.73  ? 194  LYS B O   1 
ATOM   11647 C  CB  . LYS B 2 536  ? 114.701 102.572 141.368 1.00 77.51  ? 194  LYS B CB  1 
ATOM   11648 C  CG  . LYS B 2 536  ? 114.277 101.417 142.102 1.00 91.89  ? 194  LYS B CG  1 
ATOM   11649 C  CD  . LYS B 2 536  ? 113.202 101.810 143.089 1.00 111.35 ? 194  LYS B CD  1 
ATOM   11650 C  CE  . LYS B 2 536  ? 112.777 100.379 143.681 1.00 110.62 ? 194  LYS B CE  1 
ATOM   11651 N  NZ  . LYS B 2 536  ? 111.939 100.813 144.798 1.00 98.81  ? 194  LYS B NZ  1 
ATOM   11652 N  N   . VAL B 2 537  ? 115.720 105.383 140.426 1.00 79.60  ? 195  VAL B N   1 
ATOM   11653 C  CA  . VAL B 2 537  ? 116.510 106.146 139.466 1.00 77.00  ? 195  VAL B CA  1 
ATOM   11654 C  C   . VAL B 2 537  ? 117.745 106.759 140.135 1.00 65.36  ? 195  VAL B C   1 
ATOM   11655 O  O   . VAL B 2 537  ? 118.846 106.700 139.582 1.00 68.76  ? 195  VAL B O   1 
ATOM   11656 C  CB  . VAL B 2 537  ? 115.652 107.221 138.778 1.00 83.14  ? 195  VAL B CB  1 
ATOM   11657 C  CG1 . VAL B 2 537  ? 116.547 108.086 137.903 1.00 57.16  ? 195  VAL B CG1 1 
ATOM   11658 C  CG2 . VAL B 2 537  ? 114.572 106.560 137.942 1.00 93.23  ? 195  VAL B CG2 1 
ATOM   11659 N  N   . LEU B 2 538  ? 117.609 107.310 141.354 1.00 77.14  ? 196  LEU B N   1 
ATOM   11660 C  CA  . LEU B 2 538  ? 118.794 107.906 142.000 1.00 63.45  ? 196  LEU B CA  1 
ATOM   11661 C  C   . LEU B 2 538  ? 119.899 106.906 142.330 1.00 74.49  ? 196  LEU B C   1 
ATOM   11662 O  O   . LEU B 2 538  ? 121.052 107.311 142.489 1.00 76.99  ? 196  LEU B O   1 
ATOM   11663 C  CB  . LEU B 2 538  ? 118.412 108.671 143.269 1.00 74.19  ? 196  LEU B CB  1 
ATOM   11664 C  CG  . LEU B 2 538  ? 117.826 110.052 143.027 1.00 72.99  ? 196  LEU B CG  1 
ATOM   11665 C  CD1 . LEU B 2 538  ? 117.481 110.703 144.344 1.00 86.52  ? 196  LEU B CD1 1 
ATOM   11666 C  CD2 . LEU B 2 538  ? 118.910 110.837 142.336 1.00 71.66  ? 196  LEU B CD2 1 
ATOM   11667 N  N   . GLU B 2 539  ? 119.582 105.615 142.446 1.00 88.92  ? 197  GLU B N   1 
ATOM   11668 C  CA  . GLU B 2 539  ? 120.615 104.644 142.769 1.00 94.33  ? 197  GLU B CA  1 
ATOM   11669 C  C   . GLU B 2 539  ? 121.582 104.402 141.619 1.00 86.92  ? 197  GLU B C   1 
ATOM   11670 O  O   . GLU B 2 539  ? 122.596 103.711 141.829 1.00 90.21  ? 197  GLU B O   1 
ATOM   11671 C  CB  . GLU B 2 539  ? 120.002 103.308 143.168 1.00 97.07  ? 197  GLU B CB  1 
ATOM   11672 C  CG  . GLU B 2 539  ? 119.685 103.182 144.637 1.00 111.79 ? 197  GLU B CG  1 
ATOM   11673 C  CD  . GLU B 2 539  ? 118.620 102.143 144.891 1.00 118.52 ? 197  GLU B CD  1 
ATOM   11674 O  OE1 . GLU B 2 539  ? 118.561 101.159 144.126 1.00 120.07 ? 197  GLU B OE1 1 
ATOM   11675 O  OE2 . GLU B 2 539  ? 117.843 102.310 145.854 1.00 120.61 ? 197  GLU B OE2 1 
ATOM   11676 N  N   . LEU B 2 540  ? 121.315 104.949 140.439 1.00 88.94  ? 198  LEU B N   1 
ATOM   11677 C  CA  . LEU B 2 540  ? 122.155 104.622 139.306 1.00 92.18  ? 198  LEU B CA  1 
ATOM   11678 C  C   . LEU B 2 540  ? 123.575 105.122 139.503 1.00 86.76  ? 198  LEU B C   1 
ATOM   11679 O  O   . LEU B 2 540  ? 123.814 106.176 140.106 1.00 86.74  ? 198  LEU B O   1 
ATOM   11680 C  CB  . LEU B 2 540  ? 121.585 105.214 138.013 1.00 83.81  ? 198  LEU B CB  1 
ATOM   11681 C  CG  . LEU B 2 540  ? 120.374 104.467 137.479 1.00 86.36  ? 198  LEU B CG  1 
ATOM   11682 C  CD1 . LEU B 2 540  ? 119.807 105.182 136.272 1.00 68.94  ? 198  LEU B CD1 1 
ATOM   11683 C  CD2 . LEU B 2 540  ? 120.767 103.034 137.130 1.00 75.13  ? 198  LEU B CD2 1 
ATOM   11684 N  N   . SER B 2 541  ? 124.512 104.347 138.986 1.00 88.06  ? 199  SER B N   1 
ATOM   11685 C  CA  . SER B 2 541  ? 125.901 104.730 138.931 1.00 89.67  ? 199  SER B CA  1 
ATOM   11686 C  C   . SER B 2 541  ? 126.399 104.472 137.521 1.00 83.71  ? 199  SER B C   1 
ATOM   11687 O  O   . SER B 2 541  ? 125.833 103.652 136.779 1.00 88.91  ? 199  SER B O   1 
ATOM   11688 C  CB  . SER B 2 541  ? 126.725 103.954 139.963 1.00 102.53 ? 199  SER B CB  1 
ATOM   11689 O  OG  . SER B 2 541  ? 126.483 102.565 139.874 1.00 101.86 ? 199  SER B OG  1 
ATOM   11690 N  N   . GLU B 2 542  ? 127.472 105.148 137.151 1.00 81.18  ? 200  GLU B N   1 
ATOM   11691 C  CA  . GLU B 2 542  ? 127.927 105.131 135.775 1.00 76.87  ? 200  GLU B CA  1 
ATOM   11692 C  C   . GLU B 2 542  ? 128.821 103.960 135.418 1.00 82.16  ? 200  GLU B C   1 
ATOM   11693 O  O   . GLU B 2 542  ? 129.119 103.763 134.236 1.00 71.30  ? 200  GLU B O   1 
ATOM   11694 C  CB  . GLU B 2 542  ? 128.614 106.462 135.445 1.00 82.12  ? 200  GLU B CB  1 
ATOM   11695 C  CG  . GLU B 2 542  ? 129.816 106.794 136.302 1.00 103.06 ? 200  GLU B CG  1 
ATOM   11696 C  CD  . GLU B 2 542  ? 131.160 106.239 135.866 1.00 107.48 ? 200  GLU B CD  1 
ATOM   11697 O  OE1 . GLU B 2 542  ? 131.333 105.839 134.671 1.00 101.34 ? 200  GLU B OE1 1 
ATOM   11698 O  OE2 . GLU B 2 542  ? 132.059 106.291 136.748 1.00 112.50 ? 200  GLU B OE2 1 
ATOM   11699 N  N   . GLU B 2 543  ? 129.270 103.163 136.390 1.00 106.73 ? 201  GLU B N   1 
ATOM   11700 C  CA  . GLU B 2 543  ? 129.969 101.939 136.042 1.00 90.75  ? 201  GLU B CA  1 
ATOM   11701 C  C   . GLU B 2 543  ? 128.997 100.808 135.742 1.00 81.94  ? 201  GLU B C   1 
ATOM   11702 O  O   . GLU B 2 543  ? 129.358 99.860  135.030 1.00 90.41  ? 201  GLU B O   1 
ATOM   11703 C  CB  . GLU B 2 543  ? 130.915 101.520 137.169 1.00 101.34 ? 201  GLU B CB  1 
ATOM   11704 C  CG  . GLU B 2 543  ? 131.994 102.541 137.470 1.00 116.99 ? 201  GLU B CG  1 
ATOM   11705 C  CD  . GLU B 2 543  ? 131.562 103.511 138.555 1.00 133.90 ? 201  GLU B CD  1 
ATOM   11706 O  OE1 . GLU B 2 543  ? 132.295 104.491 138.800 1.00 127.50 ? 201  GLU B OE1 1 
ATOM   11707 O  OE2 . GLU B 2 543  ? 130.478 103.309 139.142 1.00 116.86 ? 201  GLU B OE2 1 
ATOM   11708 N  N   . THR B 2 544  ? 127.772 100.897 136.261 1.00 84.39  ? 202  THR B N   1 
ATOM   11709 C  CA  . THR B 2 544  ? 126.767 99.850  136.144 1.00 80.14  ? 202  THR B CA  1 
ATOM   11710 C  C   . THR B 2 544  ? 125.493 100.341 135.460 1.00 79.35  ? 202  THR B C   1 
ATOM   11711 O  O   . THR B 2 544  ? 124.398 99.862  135.761 1.00 86.91  ? 202  THR B O   1 
ATOM   11712 C  CB  . THR B 2 544  ? 126.428 99.282  137.521 1.00 94.51  ? 202  THR B CB  1 
ATOM   11713 O  OG1 . THR B 2 544  ? 125.612 100.220 138.234 1.00 88.99  ? 202  THR B OG1 1 
ATOM   11714 C  CG2 . THR B 2 544  ? 127.698 99.032  138.321 1.00 94.51  ? 202  THR B CG2 1 
ATOM   11715 N  N   . PHE B 2 545  ? 125.611 101.292 134.537 1.00 78.53  ? 203  PHE B N   1 
ATOM   11716 C  CA  . PHE B 2 545  ? 124.447 101.780 133.808 1.00 79.19  ? 203  PHE B CA  1 
ATOM   11717 C  C   . PHE B 2 545  ? 124.074 100.751 132.750 1.00 79.37  ? 203  PHE B C   1 
ATOM   11718 O  O   . PHE B 2 545  ? 124.891 100.432 131.879 1.00 84.52  ? 203  PHE B O   1 
ATOM   11719 C  CB  . PHE B 2 545  ? 124.716 103.135 133.162 1.00 79.94  ? 203  PHE B CB  1 
ATOM   11720 C  CG  . PHE B 2 545  ? 123.523 103.697 132.442 1.00 87.67  ? 203  PHE B CG  1 
ATOM   11721 C  CD1 . PHE B 2 545  ? 123.479 103.714 131.058 1.00 90.91  ? 203  PHE B CD1 1 
ATOM   11722 C  CD2 . PHE B 2 545  ? 122.438 104.187 133.148 1.00 94.20  ? 203  PHE B CD2 1 
ATOM   11723 C  CE1 . PHE B 2 545  ? 122.375 104.217 130.391 1.00 87.82  ? 203  PHE B CE1 1 
ATOM   11724 C  CE2 . PHE B 2 545  ? 121.332 104.694 132.487 1.00 101.00 ? 203  PHE B CE2 1 
ATOM   11725 C  CZ  . PHE B 2 545  ? 121.301 104.708 131.108 1.00 87.54  ? 203  PHE B CZ  1 
ATOM   11726 N  N   . SER B 2 546  ? 122.857 100.211 132.840 1.00 77.63  ? 204  SER B N   1 
ATOM   11727 C  CA  . SER B 2 546  ? 122.361 99.197  131.916 1.00 79.15  ? 204  SER B CA  1 
ATOM   11728 C  C   . SER B 2 546  ? 123.144 97.898  132.021 1.00 81.62  ? 204  SER B C   1 
ATOM   11729 O  O   . SER B 2 546  ? 123.166 97.105  131.076 1.00 79.01  ? 204  SER B O   1 
ATOM   11730 C  CB  . SER B 2 546  ? 122.353 99.691  130.463 1.00 78.35  ? 204  SER B CB  1 
ATOM   11731 O  OG  . SER B 2 546  ? 122.062 98.625  129.573 1.00 78.82  ? 204  SER B OG  1 
ATOM   11732 N  N   . LYS B 2 547  ? 123.787 97.663  133.157 1.00 91.76  ? 205  LYS B N   1 
ATOM   11733 C  CA  . LYS B 2 547  ? 124.462 96.395  133.369 1.00 83.70  ? 205  LYS B CA  1 
ATOM   11734 C  C   . LYS B 2 547  ? 123.424 95.301  133.563 1.00 78.30  ? 205  LYS B C   1 
ATOM   11735 O  O   . LYS B 2 547  ? 122.469 95.486  134.327 1.00 95.77  ? 205  LYS B O   1 
ATOM   11736 C  CB  . LYS B 2 547  ? 125.357 96.478  134.600 1.00 82.11  ? 205  LYS B CB  1 
ATOM   11737 C  CG  . LYS B 2 547  ? 126.222 95.259  134.818 1.00 76.16  ? 205  LYS B CG  1 
ATOM   11738 C  CD  . LYS B 2 547  ? 127.349 95.555  135.779 1.00 87.47  ? 205  LYS B CD  1 
ATOM   11739 C  CE  . LYS B 2 547  ? 127.896 94.270  136.367 1.00 90.27  ? 205  LYS B CE  1 
ATOM   11740 N  NZ  . LYS B 2 547  ? 129.137 93.837  135.673 1.00 91.58  ? 205  LYS B NZ  1 
ATOM   11741 N  N   . PRO B 2 548  ? 123.562 94.158  132.894 1.00 70.91  ? 206  PRO B N   1 
ATOM   11742 C  CA  . PRO B 2 548  ? 122.551 93.108  133.041 1.00 91.05  ? 206  PRO B CA  1 
ATOM   11743 C  C   . PRO B 2 548  ? 122.643 92.459  134.412 1.00 99.94  ? 206  PRO B C   1 
ATOM   11744 O  O   . PRO B 2 548  ? 123.731 92.121  134.883 1.00 94.86  ? 206  PRO B O   1 
ATOM   11745 C  CB  . PRO B 2 548  ? 122.903 92.112  131.926 1.00 83.93  ? 206  PRO B CB  1 
ATOM   11746 C  CG  . PRO B 2 548  ? 123.882 92.827  131.032 1.00 86.44  ? 206  PRO B CG  1 
ATOM   11747 C  CD  . PRO B 2 548  ? 124.596 93.799  131.911 1.00 80.99  ? 206  PRO B CD  1 
ATOM   11748 N  N   . ASN B 2 549  ? 121.494 92.294  135.051 1.00 101.48 ? 207  ASN B N   1 
ATOM   11749 C  CA  . ASN B 2 549  ? 121.408 91.622  136.337 1.00 100.47 ? 207  ASN B CA  1 
ATOM   11750 C  C   . ASN B 2 549  ? 120.682 90.323  136.021 1.00 96.91  ? 207  ASN B C   1 
ATOM   11751 O  O   . ASN B 2 549  ? 119.518 90.350  135.607 1.00 89.21  ? 207  ASN B O   1 
ATOM   11752 C  CB  . ASN B 2 549  ? 120.669 92.480  137.364 1.00 90.71  ? 207  ASN B CB  1 
ATOM   11753 C  CG  . ASN B 2 549  ? 120.788 91.942  138.771 1.00 112.05 ? 207  ASN B CG  1 
ATOM   11754 O  OD1 . ASN B 2 549  ? 121.397 90.898  139.001 1.00 111.34 ? 207  ASN B OD1 1 
ATOM   11755 N  ND2 . ASN B 2 549  ? 120.230 92.671  139.730 1.00 121.57 ? 207  ASN B ND2 1 
ATOM   11756 N  N   . LEU B 2 550  ? 121.354 89.194  136.222 1.00 89.71  ? 208  LEU B N   1 
ATOM   11757 C  CA  . LEU B 2 550  ? 120.779 87.904  135.864 1.00 88.99  ? 208  LEU B CA  1 
ATOM   11758 C  C   . LEU B 2 550  ? 120.770 86.901  137.000 1.00 88.25  ? 208  LEU B C   1 
ATOM   11759 O  O   . LEU B 2 550  ? 121.773 86.727  137.700 1.00 94.03  ? 208  LEU B O   1 
ATOM   11760 C  CB  . LEU B 2 550  ? 121.532 87.285  134.681 1.00 83.75  ? 208  LEU B CB  1 
ATOM   11761 C  CG  . LEU B 2 550  ? 121.654 88.073  133.381 1.00 85.54  ? 208  LEU B CG  1 
ATOM   11762 C  CD1 . LEU B 2 550  ? 122.489 87.284  132.388 1.00 75.81  ? 208  LEU B CD1 1 
ATOM   11763 C  CD2 . LEU B 2 550  ? 120.272 88.366  132.813 1.00 105.69 ? 208  LEU B CD2 1 
ATOM   11764 N  N   . SER B 2 551  ? 119.631 86.239  137.167 1.00 84.01  ? 209  SER B N   1 
ATOM   11765 C  CA  . SER B 2 551  ? 119.491 85.180  138.145 1.00 79.53  ? 209  SER B CA  1 
ATOM   11766 C  C   . SER B 2 551  ? 120.076 83.908  137.534 1.00 90.85  ? 209  SER B C   1 
ATOM   11767 O  O   . SER B 2 551  ? 120.370 83.851  136.338 1.00 95.26  ? 209  SER B O   1 
ATOM   11768 C  CB  . SER B 2 551  ? 118.026 84.997  138.545 1.00 78.82  ? 209  SER B CB  1 
ATOM   11769 O  OG  . SER B 2 551  ? 117.224 84.657  137.428 1.00 93.74  ? 209  SER B OG  1 
ATOM   11770 N  N   . ALA B 2 552  ? 120.249 82.876  138.360 1.00 83.40  ? 210  ALA B N   1 
ATOM   11771 C  CA  . ALA B 2 552  ? 120.841 81.634  137.866 1.00 69.38  ? 210  ALA B CA  1 
ATOM   11772 C  C   . ALA B 2 552  ? 120.017 81.023  136.734 1.00 85.75  ? 210  ALA B C   1 
ATOM   11773 O  O   . ALA B 2 552  ? 120.571 80.594  135.710 1.00 93.68  ? 210  ALA B O   1 
ATOM   11774 C  CB  . ALA B 2 552  ? 120.999 80.639  139.014 1.00 71.48  ? 210  ALA B CB  1 
ATOM   11775 N  N   . LYS B 2 553  ? 118.691 81.023  136.875 1.00 87.18  ? 211  LYS B N   1 
ATOM   11776 C  CA  . LYS B 2 553  ? 117.828 80.489  135.826 1.00 83.49  ? 211  LYS B CA  1 
ATOM   11777 C  C   . LYS B 2 553  ? 117.943 81.306  134.543 1.00 86.80  ? 211  LYS B C   1 
ATOM   11778 O  O   . LYS B 2 553  ? 118.029 80.746  133.439 1.00 88.67  ? 211  LYS B O   1 
ATOM   11779 C  CB  . LYS B 2 553  ? 116.385 80.472  136.330 1.00 84.37  ? 211  LYS B CB  1 
ATOM   11780 C  CG  . LYS B 2 553  ? 115.331 80.186  135.283 1.00 105.82 ? 211  LYS B CG  1 
ATOM   11781 C  CD  . LYS B 2 553  ? 113.947 80.361  135.884 1.00 124.88 ? 211  LYS B CD  1 
ATOM   11782 C  CE  . LYS B 2 553  ? 112.856 80.167  134.850 1.00 134.37 ? 211  LYS B CE  1 
ATOM   11783 N  NZ  . LYS B 2 553  ? 111.510 80.376  135.448 1.00 123.33 ? 211  LYS B NZ  1 
ATOM   11784 N  N   . ASP B 2 554  ? 117.981 82.634  134.671 1.00 84.30  ? 212  ASP B N   1 
ATOM   11785 C  CA  . ASP B 2 554  ? 118.084 83.488  133.494 1.00 85.86  ? 212  ASP B CA  1 
ATOM   11786 C  C   . ASP B 2 554  ? 119.414 83.272  132.781 1.00 83.86  ? 212  ASP B C   1 
ATOM   11787 O  O   . ASP B 2 554  ? 119.474 83.219  131.540 1.00 94.23  ? 212  ASP B O   1 
ATOM   11788 C  CB  . ASP B 2 554  ? 117.921 84.946  133.918 1.00 108.40 ? 212  ASP B CB  1 
ATOM   11789 C  CG  . ASP B 2 554  ? 117.235 85.783  132.870 1.00 137.69 ? 212  ASP B CG  1 
ATOM   11790 O  OD1 . ASP B 2 554  ? 117.326 85.430  131.676 1.00 130.29 ? 212  ASP B OD1 1 
ATOM   11791 O  OD2 . ASP B 2 554  ? 116.590 86.784  133.244 1.00 130.60 ? 212  ASP B OD2 1 
ATOM   11792 N  N   . LEU B 2 555  ? 120.496 83.134  133.553 1.00 79.74  ? 213  LEU B N   1 
ATOM   11793 C  CA  . LEU B 2 555  ? 121.802 82.909  132.949 1.00 72.73  ? 213  LEU B CA  1 
ATOM   11794 C  C   . LEU B 2 555  ? 121.816 81.583  132.202 1.00 79.78  ? 213  LEU B C   1 
ATOM   11795 O  O   . LEU B 2 555  ? 122.392 81.477  131.104 1.00 78.60  ? 213  LEU B O   1 
ATOM   11796 C  CB  . LEU B 2 555  ? 122.886 82.948  134.025 1.00 70.42  ? 213  LEU B CB  1 
ATOM   11797 C  CG  . LEU B 2 555  ? 124.315 82.807  133.513 1.00 73.74  ? 213  LEU B CG  1 
ATOM   11798 C  CD1 . LEU B 2 555  ? 124.577 83.839  132.431 1.00 81.82  ? 213  LEU B CD1 1 
ATOM   11799 C  CD2 . LEU B 2 555  ? 125.296 82.967  134.659 1.00 64.69  ? 213  LEU B CD2 1 
ATOM   11800 N  N   . ALA B 2 556  ? 121.183 80.557  132.782 1.00 79.20  ? 214  ALA B N   1 
ATOM   11801 C  CA  . ALA B 2 556  ? 121.144 79.270  132.102 1.00 57.60  ? 214  ALA B CA  1 
ATOM   11802 C  C   . ALA B 2 556  ? 120.393 79.397  130.784 1.00 67.59  ? 214  ALA B C   1 
ATOM   11803 O  O   . ALA B 2 556  ? 120.792 78.808  129.772 1.00 77.12  ? 214  ALA B O   1 
ATOM   11804 C  CB  . ALA B 2 556  ? 120.498 78.217  133.001 1.00 63.18  ? 214  ALA B CB  1 
ATOM   11805 N  N   . LEU B 2 557  ? 119.299 80.169  130.779 1.00 67.23  ? 215  LEU B N   1 
ATOM   11806 C  CA  . LEU B 2 557  ? 118.535 80.344  129.545 1.00 60.49  ? 215  LEU B CA  1 
ATOM   11807 C  C   . LEU B 2 557  ? 119.376 81.018  128.463 1.00 65.69  ? 215  LEU B C   1 
ATOM   11808 O  O   . LEU B 2 557  ? 119.318 80.638  127.286 1.00 76.07  ? 215  LEU B O   1 
ATOM   11809 C  CB  . LEU B 2 557  ? 117.253 81.132  129.806 1.00 66.40  ? 215  LEU B CB  1 
ATOM   11810 C  CG  . LEU B 2 557  ? 116.105 80.259  130.318 1.00 85.00  ? 215  LEU B CG  1 
ATOM   11811 C  CD1 . LEU B 2 557  ? 114.868 81.095  130.611 1.00 78.56  ? 215  LEU B CD1 1 
ATOM   11812 C  CD2 . LEU B 2 557  ? 115.803 79.148  129.315 1.00 68.61  ? 215  LEU B CD2 1 
ATOM   11813 N  N   . LEU B 2 558  ? 120.178 82.016  128.850 1.00 68.20  ? 216  LEU B N   1 
ATOM   11814 C  CA  . LEU B 2 558  ? 121.039 82.684  127.871 1.00 62.20  ? 216  LEU B CA  1 
ATOM   11815 C  C   . LEU B 2 558  ? 122.063 81.714  127.280 1.00 60.11  ? 216  LEU B C   1 
ATOM   11816 O  O   . LEU B 2 558  ? 122.234 81.625  126.046 1.00 66.24  ? 216  LEU B O   1 
ATOM   11817 C  CB  . LEU B 2 558  ? 121.733 83.876  128.535 1.00 56.88  ? 216  LEU B CB  1 
ATOM   11818 C  CG  . LEU B 2 558  ? 122.530 84.864  127.682 1.00 53.27  ? 216  LEU B CG  1 
ATOM   11819 C  CD1 . LEU B 2 558  ? 122.475 86.239  128.323 1.00 61.05  ? 216  LEU B CD1 1 
ATOM   11820 C  CD2 . LEU B 2 558  ? 123.979 84.412  127.526 1.00 65.16  ? 216  LEU B CD2 1 
ATOM   11821 N  N   . LEU B 2 559  ? 122.728 80.944  128.145 1.00 70.07  ? 217  LEU B N   1 
ATOM   11822 C  CA  . LEU B 2 559  ? 123.705 79.985  127.638 1.00 55.73  ? 217  LEU B CA  1 
ATOM   11823 C  C   . LEU B 2 559  ? 123.037 78.975  126.718 1.00 54.57  ? 217  LEU B C   1 
ATOM   11824 O  O   . LEU B 2 559  ? 123.623 78.553  125.715 1.00 63.97  ? 217  LEU B O   1 
ATOM   11825 C  CB  . LEU B 2 559  ? 124.431 79.294  128.789 1.00 61.22  ? 217  LEU B CB  1 
ATOM   11826 C  CG  . LEU B 2 559  ? 125.242 80.270  129.635 1.00 57.83  ? 217  LEU B CG  1 
ATOM   11827 C  CD1 . LEU B 2 559  ? 126.033 79.523  130.691 1.00 61.23  ? 217  LEU B CD1 1 
ATOM   11828 C  CD2 . LEU B 2 559  ? 126.170 81.069  128.722 1.00 80.81  ? 217  LEU B CD2 1 
ATOM   11829 N  N   . PHE B 2 560  ? 121.804 78.580  127.043 1.00 64.29  ? 218  PHE B N   1 
ATOM   11830 C  CA  . PHE B 2 560  ? 121.072 77.670  126.171 1.00 61.80  ? 218  PHE B CA  1 
ATOM   11831 C  C   . PHE B 2 560  ? 120.844 78.307  124.810 1.00 56.35  ? 218  PHE B C   1 
ATOM   11832 O  O   . PHE B 2 560  ? 120.950 77.640  123.774 1.00 68.74  ? 218  PHE B O   1 
ATOM   11833 C  CB  . PHE B 2 560  ? 119.730 77.306  126.801 1.00 69.94  ? 218  PHE B CB  1 
ATOM   11834 C  CG  . PHE B 2 560  ? 119.830 76.289  127.889 1.00 72.67  ? 218  PHE B CG  1 
ATOM   11835 C  CD1 . PHE B 2 560  ? 118.691 75.705  128.407 1.00 79.00  ? 218  PHE B CD1 1 
ATOM   11836 C  CD2 . PHE B 2 560  ? 121.063 75.919  128.397 1.00 73.92  ? 218  PHE B CD2 1 
ATOM   11837 C  CE1 . PHE B 2 560  ? 118.780 74.766  129.412 1.00 94.06  ? 218  PHE B CE1 1 
ATOM   11838 C  CE2 . PHE B 2 560  ? 121.159 74.984  129.401 1.00 82.37  ? 218  PHE B CE2 1 
ATOM   11839 C  CZ  . PHE B 2 560  ? 120.016 74.405  129.909 1.00 92.61  ? 218  PHE B CZ  1 
ATOM   11840 N  N   . THR B 2 561  ? 120.525 79.604  124.802 1.00 71.39  ? 219  THR B N   1 
ATOM   11841 C  CA  . THR B 2 561  ? 120.341 80.316  123.543 1.00 69.66  ? 219  THR B CA  1 
ATOM   11842 C  C   . THR B 2 561  ? 121.595 80.264  122.680 1.00 63.68  ? 219  THR B C   1 
ATOM   11843 O  O   . THR B 2 561  ? 121.494 80.238  121.449 1.00 66.50  ? 219  THR B O   1 
ATOM   11844 C  CB  . THR B 2 561  ? 119.949 81.775  123.806 1.00 59.72  ? 219  THR B CB  1 
ATOM   11845 O  OG1 . THR B 2 561  ? 118.792 81.818  124.649 1.00 76.59  ? 219  THR B OG1 1 
ATOM   11846 C  CG2 . THR B 2 561  ? 119.635 82.496  122.497 1.00 51.99  ? 219  THR B CG2 1 
ATOM   11847 N  N   . HIS B 2 562  ? 122.779 80.208  123.290 1.00 72.50  ? 220  HIS B N   1 
ATOM   11848 C  CA  . HIS B 2 562  ? 123.986 80.148  122.461 1.00 59.57  ? 220  HIS B CA  1 
ATOM   11849 C  C   . HIS B 2 562  ? 124.405 78.744  122.009 1.00 66.03  ? 220  HIS B C   1 
ATOM   11850 O  O   . HIS B 2 562  ? 125.385 78.626  121.267 1.00 66.14  ? 220  HIS B O   1 
ATOM   11851 C  CB  . HIS B 2 562  ? 125.162 80.826  123.168 1.00 66.54  ? 220  HIS B CB  1 
ATOM   11852 C  CG  . HIS B 2 562  ? 125.121 82.320  123.079 1.00 58.58  ? 220  HIS B CG  1 
ATOM   11853 N  ND1 . HIS B 2 562  ? 125.751 83.022  122.073 1.00 62.59  ? 220  HIS B ND1 1 
ATOM   11854 C  CD2 . HIS B 2 562  ? 124.523 83.243  123.867 1.00 58.00  ? 220  HIS B CD2 1 
ATOM   11855 C  CE1 . HIS B 2 562  ? 125.539 84.314  122.244 1.00 64.46  ? 220  HIS B CE1 1 
ATOM   11856 N  NE2 . HIS B 2 562  ? 124.798 84.475  123.327 1.00 60.68  ? 220  HIS B NE2 1 
ATOM   11857 N  N   . LEU B 2 563  ? 123.690 77.670  122.411 1.00 74.10  ? 221  LEU B N   1 
ATOM   11858 C  CA  . LEU B 2 563  ? 124.211 76.340  122.093 1.00 63.53  ? 221  LEU B CA  1 
ATOM   11859 C  C   . LEU B 2 563  ? 123.433 75.676  120.962 1.00 77.68  ? 221  LEU B C   1 
ATOM   11860 O  O   . LEU B 2 563  ? 122.226 75.890  120.816 1.00 86.76  ? 221  LEU B O   1 
ATOM   11861 C  CB  . LEU B 2 563  ? 124.167 75.416  123.313 1.00 60.17  ? 221  LEU B CB  1 
ATOM   11862 C  CG  . LEU B 2 563  ? 125.183 75.586  124.433 1.00 55.86  ? 221  LEU B CG  1 
ATOM   11863 C  CD1 . LEU B 2 563  ? 124.652 74.930  125.689 1.00 86.07  ? 221  LEU B CD1 1 
ATOM   11864 C  CD2 . LEU B 2 563  ? 126.492 74.933  124.007 1.00 71.67  ? 221  LEU B CD2 1 
ATOM   11865 N  N   . PRO B 2 564  ? 124.101 74.852  120.155 1.00 77.07  ? 222  PRO B N   1 
ATOM   11866 C  CA  . PRO B 2 564  ? 123.409 74.142  119.080 1.00 76.37  ? 222  PRO B CA  1 
ATOM   11867 C  C   . PRO B 2 564  ? 122.911 72.787  119.554 1.00 75.44  ? 222  PRO B C   1 
ATOM   11868 O  O   . PRO B 2 564  ? 123.457 72.170  120.470 1.00 89.81  ? 222  PRO B O   1 
ATOM   11869 C  CB  . PRO B 2 564  ? 124.502 73.973  118.015 1.00 77.46  ? 222  PRO B CB  1 
ATOM   11870 C  CG  . PRO B 2 564  ? 125.799 73.977  118.786 1.00 83.26  ? 222  PRO B CG  1 
ATOM   11871 C  CD  . PRO B 2 564  ? 125.552 74.588  120.148 1.00 80.48  ? 222  PRO B CD  1 
ATOM   11872 N  N   . GLY B 2 565  ? 121.851 72.328  118.909 1.00 79.75  ? 223  GLY B N   1 
ATOM   11873 C  CA  . GLY B 2 565  ? 121.264 71.054  119.257 1.00 85.92  ? 223  GLY B CA  1 
ATOM   11874 C  C   . GLY B 2 565  ? 120.264 71.189  120.390 1.00 85.24  ? 223  GLY B C   1 
ATOM   11875 O  O   . GLY B 2 565  ? 119.724 72.262  120.672 1.00 82.86  ? 223  GLY B O   1 
ATOM   11876 N  N   . ASN B 2 566  ? 120.031 70.065  121.063 1.00 91.58  ? 224  ASN B N   1 
ATOM   11877 C  CA  . ASN B 2 566  ? 119.102 70.036  122.181 1.00 98.15  ? 224  ASN B CA  1 
ATOM   11878 C  C   . ASN B 2 566  ? 119.431 68.849  123.073 1.00 109.12 ? 224  ASN B C   1 
ATOM   11879 O  O   . ASN B 2 566  ? 119.712 67.755  122.576 1.00 114.27 ? 224  ASN B O   1 
ATOM   11880 C  CB  . ASN B 2 566  ? 117.653 69.947  121.690 1.00 94.96  ? 224  ASN B CB  1 
ATOM   11881 C  CG  . ASN B 2 566  ? 116.702 70.777  122.526 1.00 100.11 ? 224  ASN B CG  1 
ATOM   11882 O  OD1 . ASN B 2 566  ? 117.047 71.230  123.616 1.00 102.34 ? 224  ASN B OD1 1 
ATOM   11883 N  ND2 . ASN B 2 566  ? 115.494 70.981  122.015 1.00 111.21 ? 224  ASN B ND2 1 
ATOM   11884 N  N   . ASN B 2 567  ? 119.405 69.079  124.389 1.00 104.67 ? 225  ASN B N   1 
ATOM   11885 C  CA  . ASN B 2 567  ? 119.640 68.031  125.383 1.00 110.18 ? 225  ASN B CA  1 
ATOM   11886 C  C   . ASN B 2 567  ? 121.009 67.378  125.218 1.00 111.61 ? 225  ASN B C   1 
ATOM   11887 O  O   . ASN B 2 567  ? 121.183 66.194  125.512 1.00 111.80 ? 225  ASN B O   1 
ATOM   11888 C  CB  . ASN B 2 567  ? 118.538 66.968  125.342 1.00 113.12 ? 225  ASN B CB  1 
ATOM   11889 C  CG  . ASN B 2 567  ? 117.297 67.385  126.101 1.00 111.39 ? 225  ASN B CG  1 
ATOM   11890 O  OD1 . ASN B 2 567  ? 117.382 67.931  127.200 1.00 112.47 ? 225  ASN B OD1 1 
ATOM   11891 N  ND2 . ASN B 2 567  ? 116.133 67.130  125.514 1.00 109.18 ? 225  ASN B ND2 1 
ATOM   11892 N  N   . THR B 2 568  ? 121.989 68.136  124.743 1.00 105.25 ? 226  THR B N   1 
ATOM   11893 C  CA  . THR B 2 568  ? 123.354 67.646  124.668 1.00 102.52 ? 226  THR B CA  1 
ATOM   11894 C  C   . THR B 2 568  ? 123.992 67.725  126.052 1.00 100.13 ? 226  THR B C   1 
ATOM   11895 O  O   . THR B 2 568  ? 123.436 68.330  126.971 1.00 105.57 ? 226  THR B O   1 
ATOM   11896 C  CB  . THR B 2 568  ? 124.131 68.458  123.631 1.00 101.26 ? 226  THR B CB  1 
ATOM   11897 O  OG1 . THR B 2 568  ? 124.066 69.851  123.958 1.00 97.23  ? 226  THR B OG1 1 
ATOM   11898 C  CG2 . THR B 2 568  ? 123.545 68.244  122.238 1.00 103.73 ? 226  THR B CG2 1 
ATOM   11899 N  N   . PRO B 2 569  ? 125.165 67.109  126.242 1.00 93.99  ? 227  PRO B N   1 
ATOM   11900 C  CA  . PRO B 2 569  ? 125.857 67.248  127.537 1.00 94.05  ? 227  PRO B CA  1 
ATOM   11901 C  C   . PRO B 2 569  ? 126.161 68.689  127.916 1.00 90.84  ? 227  PRO B C   1 
ATOM   11902 O  O   . PRO B 2 569  ? 126.202 69.025  129.111 1.00 91.63  ? 227  PRO B O   1 
ATOM   11903 C  CB  . PRO B 2 569  ? 127.142 66.433  127.335 1.00 87.30  ? 227  PRO B CB  1 
ATOM   11904 C  CG  . PRO B 2 569  ? 126.788 65.427  126.293 1.00 92.58  ? 227  PRO B CG  1 
ATOM   11905 C  CD  . PRO B 2 569  ? 125.814 66.104  125.376 1.00 97.77  ? 227  PRO B CD  1 
ATOM   11906 N  N   . PHE B 2 570  ? 126.354 69.560  126.925 1.00 84.65  ? 228  PHE B N   1 
ATOM   11907 C  CA  . PHE B 2 570  ? 126.710 70.944  127.212 1.00 77.57  ? 228  PHE B CA  1 
ATOM   11908 C  C   . PHE B 2 570  ? 125.560 71.709  127.849 1.00 88.14  ? 228  PHE B C   1 
ATOM   11909 O  O   . PHE B 2 570  ? 125.799 72.663  128.591 1.00 95.58  ? 228  PHE B O   1 
ATOM   11910 C  CB  . PHE B 2 570  ? 127.160 71.646  125.931 1.00 84.91  ? 228  PHE B CB  1 
ATOM   11911 C  CG  . PHE B 2 570  ? 128.462 71.138  125.394 1.00 100.86 ? 228  PHE B CG  1 
ATOM   11912 C  CD1 . PHE B 2 570  ? 129.663 71.647  125.857 1.00 99.13  ? 228  PHE B CD1 1 
ATOM   11913 C  CD2 . PHE B 2 570  ? 128.485 70.150  124.425 1.00 104.88 ? 228  PHE B CD2 1 
ATOM   11914 C  CE1 . PHE B 2 570  ? 130.865 71.176  125.366 1.00 99.98  ? 228  PHE B CE1 1 
ATOM   11915 C  CE2 . PHE B 2 570  ? 129.683 69.676  123.929 1.00 104.22 ? 228  PHE B CE2 1 
ATOM   11916 C  CZ  . PHE B 2 570  ? 130.875 70.189  124.401 1.00 105.81 ? 228  PHE B CZ  1 
ATOM   11917 N  N   . HIS B 2 571  ? 124.316 71.297  127.607 1.00 87.21  ? 229  HIS B N   1 
ATOM   11918 C  CA  . HIS B 2 571  ? 123.192 71.936  128.285 1.00 87.42  ? 229  HIS B CA  1 
ATOM   11919 C  C   . HIS B 2 571  ? 123.212 71.655  129.788 1.00 91.59  ? 229  HIS B C   1 
ATOM   11920 O  O   . HIS B 2 571  ? 123.014 72.570  130.607 1.00 100.48 ? 229  HIS B O   1 
ATOM   11921 C  CB  . HIS B 2 571  ? 121.883 71.451  127.657 1.00 98.02  ? 229  HIS B CB  1 
ATOM   11922 C  CG  . HIS B 2 571  ? 121.674 71.937  126.254 1.00 98.82  ? 229  HIS B CG  1 
ATOM   11923 N  ND1 . HIS B 2 571  ? 122.325 71.384  125.172 1.00 91.19  ? 229  HIS B ND1 1 
ATOM   11924 C  CD2 . HIS B 2 571  ? 120.901 72.932  125.760 1.00 91.97  ? 229  HIS B CD2 1 
ATOM   11925 C  CE1 . HIS B 2 571  ? 121.954 72.011  124.071 1.00 97.56  ? 229  HIS B CE1 1 
ATOM   11926 N  NE2 . HIS B 2 571  ? 121.093 72.956  124.400 1.00 93.48  ? 229  HIS B NE2 1 
ATOM   11927 N  N   . ILE B 2 572  ? 123.490 70.407  130.170 1.00 85.66  ? 230  ILE B N   1 
ATOM   11928 C  CA  . ILE B 2 572  ? 123.622 70.069  131.585 1.00 94.40  ? 230  ILE B CA  1 
ATOM   11929 C  C   . ILE B 2 572  ? 124.811 70.804  132.193 1.00 92.21  ? 230  ILE B C   1 
ATOM   11930 O  O   . ILE B 2 572  ? 124.738 71.319  133.323 1.00 93.72  ? 230  ILE B O   1 
ATOM   11931 C  CB  . ILE B 2 572  ? 123.749 68.544  131.753 1.00 87.64  ? 230  ILE B CB  1 
ATOM   11932 C  CG1 . ILE B 2 572  ? 122.774 67.829  130.815 1.00 95.37  ? 230  ILE B CG1 1 
ATOM   11933 C  CG2 . ILE B 2 572  ? 123.469 68.146  133.194 1.00 104.69 ? 230  ILE B CG2 1 
ATOM   11934 C  CD1 . ILE B 2 572  ? 122.770 66.322  130.956 1.00 119.58 ? 230  ILE B CD1 1 
ATOM   11935 N  N   . LEU B 2 573  ? 125.925 70.859  131.457 1.00 78.97  ? 231  LEU B N   1 
ATOM   11936 C  CA  . LEU B 2 573  ? 127.080 71.610  131.939 1.00 71.88  ? 231  LEU B CA  1 
ATOM   11937 C  C   . LEU B 2 573  ? 126.727 73.076  132.162 1.00 76.89  ? 231  LEU B C   1 
ATOM   11938 O  O   . LEU B 2 573  ? 127.168 73.687  133.144 1.00 90.37  ? 231  LEU B O   1 
ATOM   11939 C  CB  . LEU B 2 573  ? 128.250 71.472  130.966 1.00 85.72  ? 231  LEU B CB  1 
ATOM   11940 C  CG  . LEU B 2 573  ? 129.494 72.272  131.355 1.00 76.98  ? 231  LEU B CG  1 
ATOM   11941 C  CD1 . LEU B 2 573  ? 129.948 71.887  132.754 1.00 75.77  ? 231  LEU B CD1 1 
ATOM   11942 C  CD2 . LEU B 2 573  ? 130.609 72.043  130.350 1.00 77.01  ? 231  LEU B CD2 1 
ATOM   11943 N  N   . ALA B 2 574  ? 125.936 73.659  131.257 1.00 69.99  ? 232  ALA B N   1 
ATOM   11944 C  CA  . ALA B 2 574  ? 125.546 75.056  131.401 1.00 69.14  ? 232  ALA B CA  1 
ATOM   11945 C  C   . ALA B 2 574  ? 124.710 75.269  132.657 1.00 77.75  ? 232  ALA B C   1 
ATOM   11946 O  O   . ALA B 2 574  ? 124.933 76.237  133.396 1.00 87.35  ? 232  ALA B O   1 
ATOM   11947 C  CB  . ALA B 2 574  ? 124.779 75.514  130.160 1.00 63.12  ? 232  ALA B CB  1 
ATOM   11948 N  N   . GLN B 2 575  ? 123.757 74.370  132.927 1.00 78.16  ? 233  GLN B N   1 
ATOM   11949 C  CA  . GLN B 2 575  ? 122.973 74.506  134.157 1.00 80.89  ? 233  GLN B CA  1 
ATOM   11950 C  C   . GLN B 2 575  ? 123.867 74.452  135.393 1.00 87.50  ? 233  GLN B C   1 
ATOM   11951 O  O   . GLN B 2 575  ? 123.755 75.298  136.297 1.00 92.44  ? 233  GLN B O   1 
ATOM   11952 C  CB  . GLN B 2 575  ? 121.886 73.435  134.254 1.00 84.50  ? 233  GLN B CB  1 
ATOM   11953 C  CG  . GLN B 2 575  ? 120.695 73.643  133.346 1.00 94.13  ? 233  GLN B CG  1 
ATOM   11954 C  CD  . GLN B 2 575  ? 119.843 72.399  133.231 1.00 109.81 ? 233  GLN B CD  1 
ATOM   11955 O  OE1 . GLN B 2 575  ? 120.114 71.387  133.876 1.00 112.87 ? 233  GLN B OE1 1 
ATOM   11956 N  NE2 . GLN B 2 575  ? 118.796 72.471  132.419 1.00 107.57 ? 233  GLN B NE2 1 
ATOM   11957 N  N   . VAL B 2 576  ? 124.773 73.469  135.441 1.00 82.97  ? 234  VAL B N   1 
ATOM   11958 C  CA  . VAL B 2 576  ? 125.631 73.306  136.616 1.00 84.14  ? 234  VAL B CA  1 
ATOM   11959 C  C   . VAL B 2 576  ? 126.498 74.545  136.822 1.00 84.70  ? 234  VAL B C   1 
ATOM   11960 O  O   . VAL B 2 576  ? 126.589 75.090  137.934 1.00 89.42  ? 234  VAL B O   1 
ATOM   11961 C  CB  . VAL B 2 576  ? 126.489 72.035  136.484 1.00 87.48  ? 234  VAL B CB  1 
ATOM   11962 C  CG1 . VAL B 2 576  ? 127.653 72.071  137.466 1.00 89.27  ? 234  VAL B CG1 1 
ATOM   11963 C  CG2 . VAL B 2 576  ? 125.641 70.792  136.714 1.00 93.73  ? 234  VAL B CG2 1 
ATOM   11964 N  N   . LEU B 2 577  ? 127.145 75.009  135.749 1.00 78.83  ? 235  LEU B N   1 
ATOM   11965 C  CA  . LEU B 2 577  ? 128.029 76.162  135.864 1.00 77.62  ? 235  LEU B CA  1 
ATOM   11966 C  C   . LEU B 2 577  ? 127.266 77.408  136.283 1.00 90.82  ? 235  LEU B C   1 
ATOM   11967 O  O   . LEU B 2 577  ? 127.751 78.185  137.113 1.00 94.55  ? 235  LEU B O   1 
ATOM   11968 C  CB  . LEU B 2 577  ? 128.769 76.395  134.548 1.00 79.99  ? 235  LEU B CB  1 
ATOM   11969 C  CG  . LEU B 2 577  ? 129.826 75.336  134.249 1.00 92.05  ? 235  LEU B CG  1 
ATOM   11970 C  CD1 . LEU B 2 577  ? 130.709 75.779  133.098 1.00 103.37 ? 235  LEU B CD1 1 
ATOM   11971 C  CD2 . LEU B 2 577  ? 130.658 75.085  135.501 1.00 103.87 ? 235  LEU B CD2 1 
ATOM   11972 N  N   . SER B 2 578  ? 126.074 77.627  135.716 1.00 86.23  ? 236  SER B N   1 
ATOM   11973 C  CA  . SER B 2 578  ? 125.318 78.820  136.076 1.00 81.44  ? 236  SER B CA  1 
ATOM   11974 C  C   . SER B 2 578  ? 124.931 78.801  137.549 1.00 98.65  ? 236  SER B C   1 
ATOM   11975 O  O   . SER B 2 578  ? 125.068 79.818  138.246 1.00 106.49 ? 236  SER B O   1 
ATOM   11976 C  CB  . SER B 2 578  ? 124.073 78.931  135.195 1.00 82.25  ? 236  SER B CB  1 
ATOM   11977 O  OG  . SER B 2 578  ? 123.131 77.920  135.515 1.00 93.67  ? 236  SER B OG  1 
ATOM   11978 N  N   . LYS B 2 579  ? 124.484 77.646  138.057 1.00 95.54  ? 237  LYS B N   1 
ATOM   11979 C  CA  . LYS B 2 579  ? 124.122 77.575  139.471 1.00 99.14  ? 237  LYS B CA  1 
ATOM   11980 C  C   . LYS B 2 579  ? 125.325 77.846  140.369 1.00 96.66  ? 237  LYS B C   1 
ATOM   11981 O  O   . LYS B 2 579  ? 125.248 78.646  141.315 1.00 99.01  ? 237  LYS B O   1 
ATOM   11982 C  CB  . LYS B 2 579  ? 123.505 76.217  139.801 1.00 101.00 ? 237  LYS B CB  1 
ATOM   11983 C  CG  . LYS B 2 579  ? 122.749 76.219  141.123 1.00 107.49 ? 237  LYS B CG  1 
ATOM   11984 C  CD  . LYS B 2 579  ? 121.742 75.093  141.198 1.00 112.23 ? 237  LYS B CD  1 
ATOM   11985 C  CE  . LYS B 2 579  ? 120.779 75.176  140.032 1.00 111.13 ? 237  LYS B CE  1 
ATOM   11986 N  NZ  . LYS B 2 579  ? 119.976 76.428  140.087 1.00 108.94 ? 237  LYS B NZ  1 
ATOM   11987 N  N   . ILE B 2 580  ? 126.460 77.208  140.065 1.00 87.08  ? 238  ILE B N   1 
ATOM   11988 C  CA  . ILE B 2 580  ? 127.644 77.375  140.906 1.00 83.81  ? 238  ILE B CA  1 
ATOM   11989 C  C   . ILE B 2 580  ? 128.127 78.818  140.877 1.00 89.05  ? 238  ILE B C   1 
ATOM   11990 O  O   . ILE B 2 580  ? 128.464 79.395  141.919 1.00 93.02  ? 238  ILE B O   1 
ATOM   11991 C  CB  . ILE B 2 580  ? 128.752 76.393  140.486 1.00 84.80  ? 238  ILE B CB  1 
ATOM   11992 C  CG1 . ILE B 2 580  ? 128.356 74.965  140.862 1.00 97.75  ? 238  ILE B CG1 1 
ATOM   11993 C  CG2 . ILE B 2 580  ? 130.075 76.766  141.144 1.00 81.12  ? 238  ILE B CG2 1 
ATOM   11994 C  CD1 . ILE B 2 580  ? 129.263 73.913  140.281 1.00 113.24 ? 238  ILE B CD1 1 
ATOM   11995 N  N   . ALA B 2 581  ? 128.154 79.431  139.692 1.00 89.04  ? 239  ALA B N   1 
ATOM   11996 C  CA  . ALA B 2 581  ? 128.618 80.810  139.594 1.00 85.34  ? 239  ALA B CA  1 
ATOM   11997 C  C   . ALA B 2 581  ? 127.699 81.753  140.358 1.00 96.81  ? 239  ALA B C   1 
ATOM   11998 O  O   . ALA B 2 581  ? 128.172 82.675  141.033 1.00 103.67 ? 239  ALA B O   1 
ATOM   11999 C  CB  . ALA B 2 581  ? 128.722 81.229  138.129 1.00 105.02 ? 239  ALA B CB  1 
ATOM   12000 N  N   . TYR B 2 582  ? 126.381 81.542  140.273 1.00 97.78  ? 240  TYR B N   1 
ATOM   12001 C  CA  . TYR B 2 582  ? 125.474 82.437  140.984 1.00 90.95  ? 240  TYR B CA  1 
ATOM   12002 C  C   . TYR B 2 582  ? 125.598 82.288  142.497 1.00 95.22  ? 240  TYR B C   1 
ATOM   12003 O  O   . TYR B 2 582  ? 125.473 83.281  143.222 1.00 94.32  ? 240  TYR B O   1 
ATOM   12004 C  CB  . TYR B 2 582  ? 124.025 82.221  140.553 1.00 92.13  ? 240  TYR B CB  1 
ATOM   12005 C  CG  . TYR B 2 582  ? 123.091 83.231  141.187 1.00 98.38  ? 240  TYR B CG  1 
ATOM   12006 C  CD1 . TYR B 2 582  ? 122.991 84.522  140.682 1.00 98.98  ? 240  TYR B CD1 1 
ATOM   12007 C  CD2 . TYR B 2 582  ? 122.332 82.909  142.305 1.00 105.66 ? 240  TYR B CD2 1 
ATOM   12008 C  CE1 . TYR B 2 582  ? 122.150 85.457  141.261 1.00 99.40  ? 240  TYR B CE1 1 
ATOM   12009 C  CE2 . TYR B 2 582  ? 121.489 83.838  142.892 1.00 105.21 ? 240  TYR B CE2 1 
ATOM   12010 C  CZ  . TYR B 2 582  ? 121.402 85.111  142.365 1.00 106.91 ? 240  TYR B CZ  1 
ATOM   12011 O  OH  . TYR B 2 582  ? 120.566 86.039  142.945 1.00 102.76 ? 240  TYR B OH  1 
ATOM   12012 N  N   . LYS B 2 583  ? 125.851 81.072  142.998 1.00 107.34 ? 241  LYS B N   1 
ATOM   12013 C  CA  . LYS B 2 583  ? 125.966 80.903  144.446 1.00 110.15 ? 241  LYS B CA  1 
ATOM   12014 C  C   . LYS B 2 583  ? 127.141 81.695  145.010 1.00 102.67 ? 241  LYS B C   1 
ATOM   12015 O  O   . LYS B 2 583  ? 127.048 82.249  146.113 1.00 109.86 ? 241  LYS B O   1 
ATOM   12016 C  CB  . LYS B 2 583  ? 126.102 79.424  144.806 1.00 121.20 ? 241  LYS B CB  1 
ATOM   12017 C  CG  . LYS B 2 583  ? 124.781 78.700  144.985 1.00 136.11 ? 241  LYS B CG  1 
ATOM   12018 C  CD  . LYS B 2 583  ? 125.001 77.202  145.058 1.00 140.47 ? 241  LYS B CD  1 
ATOM   12019 C  CE  . LYS B 2 583  ? 123.728 76.440  144.739 1.00 139.93 ? 241  LYS B CE  1 
ATOM   12020 N  NZ  . LYS B 2 583  ? 122.645 76.761  145.706 1.00 139.26 ? 241  LYS B NZ  1 
ATOM   12021 N  N   . SER B 2 584  ? 128.250 81.775  144.266 1.00 97.43  ? 242  SER B N   1 
ATOM   12022 C  CA  . SER B 2 584  ? 129.445 82.460  144.745 1.00 99.94  ? 242  SER B CA  1 
ATOM   12023 C  C   . SER B 2 584  ? 129.496 83.938  144.405 1.00 99.96  ? 242  SER B C   1 
ATOM   12024 O  O   . SER B 2 584  ? 130.481 84.598  144.748 1.00 102.04 ? 242  SER B O   1 
ATOM   12025 C  CB  . SER B 2 584  ? 130.694 81.826  144.127 1.00 98.75  ? 242  SER B CB  1 
ATOM   12026 O  OG  . SER B 2 584  ? 131.860 82.536  144.517 1.00 102.72 ? 242  SER B OG  1 
ATOM   12027 N  N   . GLY B 2 585  ? 128.463 84.485  143.773 1.00 103.17 ? 243  GLY B N   1 
ATOM   12028 C  CA  . GLY B 2 585  ? 128.434 85.906  143.515 1.00 109.63 ? 243  GLY B CA  1 
ATOM   12029 C  C   . GLY B 2 585  ? 129.377 86.374  142.428 1.00 106.72 ? 243  GLY B C   1 
ATOM   12030 O  O   . GLY B 2 585  ? 129.757 87.546  142.422 1.00 104.05 ? 243  GLY B O   1 
ATOM   12031 N  N   . LYS B 2 586  ? 129.769 85.497  141.502 1.00 103.89 ? 244  LYS B N   1 
ATOM   12032 C  CA  . LYS B 2 586  ? 130.706 85.827  140.428 1.00 98.36  ? 244  LYS B CA  1 
ATOM   12033 C  C   . LYS B 2 586  ? 130.089 85.611  139.052 1.00 104.53 ? 244  LYS B C   1 
ATOM   12034 O  O   . LYS B 2 586  ? 130.749 85.144  138.120 1.00 107.12 ? 244  LYS B O   1 
ATOM   12035 C  CB  . LYS B 2 586  ? 132.010 85.046  140.566 1.00 103.15 ? 244  LYS B CB  1 
ATOM   12036 C  CG  . LYS B 2 586  ? 132.844 85.469  141.759 1.00 109.39 ? 244  LYS B CG  1 
ATOM   12037 C  CD  . LYS B 2 586  ? 134.227 84.848  141.716 1.00 111.15 ? 244  LYS B CD  1 
ATOM   12038 C  CE  . LYS B 2 586  ? 134.993 85.155  142.987 1.00 129.18 ? 244  LYS B CE  1 
ATOM   12039 N  NZ  . LYS B 2 586  ? 134.328 84.540  144.168 1.00 131.08 ? 244  LYS B NZ  1 
ATOM   12040 N  N   . SER B 2 587  ? 128.811 85.959  138.905 1.00 98.17  ? 245  SER B N   1 
ATOM   12041 C  CA  . SER B 2 587  ? 128.118 85.731  137.641 1.00 92.94  ? 245  SER B CA  1 
ATOM   12042 C  C   . SER B 2 587  ? 128.553 86.717  136.562 1.00 103.11 ? 245  SER B C   1 
ATOM   12043 O  O   . SER B 2 587  ? 128.692 86.340  135.390 1.00 102.94 ? 245  SER B O   1 
ATOM   12044 C  CB  . SER B 2 587  ? 126.608 85.808  137.863 1.00 91.39  ? 245  SER B CB  1 
ATOM   12045 O  OG  . SER B 2 587  ? 126.265 86.933  138.655 1.00 95.73  ? 245  SER B OG  1 
ATOM   12046 N  N   . GLY B 2 588  ? 128.793 87.977  136.930 1.00 98.50  ? 246  GLY B N   1 
ATOM   12047 C  CA  . GLY B 2 588  ? 129.201 88.960  135.937 1.00 80.88  ? 246  GLY B CA  1 
ATOM   12048 C  C   . GLY B 2 588  ? 130.555 88.673  135.313 1.00 87.52  ? 246  GLY B C   1 
ATOM   12049 O  O   . GLY B 2 588  ? 130.720 88.772  134.092 1.00 100.17 ? 246  GLY B O   1 
ATOM   12050 N  N   . ALA B 2 589  ? 131.537 88.293  136.136 1.00 76.61  ? 247  ALA B N   1 
ATOM   12051 C  CA  . ALA B 2 589  ? 132.847 87.936  135.599 1.00 85.82  ? 247  ALA B CA  1 
ATOM   12052 C  C   . ALA B 2 589  ? 132.760 86.700  134.712 1.00 90.57  ? 247  ALA B C   1 
ATOM   12053 O  O   . ALA B 2 589  ? 133.421 86.623  133.667 1.00 89.92  ? 247  ALA B O   1 
ATOM   12054 C  CB  . ALA B 2 589  ? 133.836 87.710  136.743 1.00 87.74  ? 247  ALA B CB  1 
ATOM   12055 N  N   . PHE B 2 590  ? 131.925 85.734  135.101 1.00 82.91  ? 248  PHE B N   1 
ATOM   12056 C  CA  . PHE B 2 590  ? 131.732 84.536  134.292 1.00 78.82  ? 248  PHE B CA  1 
ATOM   12057 C  C   . PHE B 2 590  ? 131.154 84.879  132.925 1.00 81.14  ? 248  PHE B C   1 
ATOM   12058 O  O   . PHE B 2 590  ? 131.641 84.402  131.887 1.00 90.98  ? 248  PHE B O   1 
ATOM   12059 C  CB  . PHE B 2 590  ? 130.802 83.575  135.034 1.00 87.48  ? 248  PHE B CB  1 
ATOM   12060 C  CG  . PHE B 2 590  ? 130.396 82.380  134.226 1.00 88.46  ? 248  PHE B CG  1 
ATOM   12061 C  CD1 . PHE B 2 590  ? 131.334 81.456  133.805 1.00 98.61  ? 248  PHE B CD1 1 
ATOM   12062 C  CD2 . PHE B 2 590  ? 129.070 82.194  133.869 1.00 81.18  ? 248  PHE B CD2 1 
ATOM   12063 C  CE1 . PHE B 2 590  ? 130.956 80.361  133.052 1.00 87.57  ? 248  PHE B CE1 1 
ATOM   12064 C  CE2 . PHE B 2 590  ? 128.686 81.102  133.115 1.00 68.41  ? 248  PHE B CE2 1 
ATOM   12065 C  CZ  . PHE B 2 590  ? 129.631 80.185  132.706 1.00 76.93  ? 248  PHE B CZ  1 
ATOM   12066 N  N   . LEU B 2 591  ? 130.131 85.735  132.905 1.00 75.80  ? 249  LEU B N   1 
ATOM   12067 C  CA  . LEU B 2 591  ? 129.526 86.135  131.640 1.00 69.50  ? 249  LEU B CA  1 
ATOM   12068 C  C   . LEU B 2 591  ? 130.514 86.887  130.756 1.00 78.99  ? 249  LEU B C   1 
ATOM   12069 O  O   . LEU B 2 591  ? 130.568 86.660  129.539 1.00 89.53  ? 249  LEU B O   1 
ATOM   12070 C  CB  . LEU B 2 591  ? 128.284 86.981  131.913 1.00 65.97  ? 249  LEU B CB  1 
ATOM   12071 C  CG  . LEU B 2 591  ? 127.355 87.192  130.723 1.00 79.57  ? 249  LEU B CG  1 
ATOM   12072 C  CD1 . LEU B 2 591  ? 126.811 85.854  130.259 1.00 72.15  ? 249  LEU B CD1 1 
ATOM   12073 C  CD2 . LEU B 2 591  ? 126.224 88.126  131.112 1.00 78.51  ? 249  LEU B CD2 1 
ATOM   12074 N  N   . ASP B 2 592  ? 131.301 87.790  131.347 1.00 77.60  ? 250  ASP B N   1 
ATOM   12075 C  CA  . ASP B 2 592  ? 132.277 88.536  130.556 1.00 63.14  ? 250  ASP B CA  1 
ATOM   12076 C  C   . ASP B 2 592  ? 133.349 87.623  129.963 1.00 68.96  ? 250  ASP B C   1 
ATOM   12077 O  O   . ASP B 2 592  ? 133.738 87.791  128.799 1.00 78.03  ? 250  ASP B O   1 
ATOM   12078 C  CB  . ASP B 2 592  ? 132.901 89.641  131.406 1.00 87.94  ? 250  ASP B CB  1 
ATOM   12079 C  CG  . ASP B 2 592  ? 131.886 90.687  131.830 1.00 90.88  ? 250  ASP B CG  1 
ATOM   12080 O  OD1 . ASP B 2 592  ? 132.185 91.481  132.746 1.00 88.76  ? 250  ASP B OD1 1 
ATOM   12081 O  OD2 . ASP B 2 592  ? 130.780 90.706  131.249 1.00 84.31  ? 250  ASP B OD2 1 
ATOM   12082 N  N   . ALA B 2 593  ? 133.823 86.638  130.734 1.00 70.65  ? 251  ALA B N   1 
ATOM   12083 C  CA  . ALA B 2 593  ? 134.812 85.706  130.191 1.00 77.03  ? 251  ALA B CA  1 
ATOM   12084 C  C   . ALA B 2 593  ? 134.227 84.891  129.043 1.00 79.91  ? 251  ALA B C   1 
ATOM   12085 O  O   . ALA B 2 593  ? 134.888 84.676  128.012 1.00 87.07  ? 251  ALA B O   1 
ATOM   12086 C  CB  . ALA B 2 593  ? 135.325 84.785  131.298 1.00 80.05  ? 251  ALA B CB  1 
ATOM   12087 N  N   . PHE B 2 594  ? 132.975 84.451  129.197 1.00 71.10  ? 252  PHE B N   1 
ATOM   12088 C  CA  . PHE B 2 594  ? 132.309 83.710  128.130 1.00 62.62  ? 252  PHE B CA  1 
ATOM   12089 C  C   . PHE B 2 594  ? 132.220 84.545  126.855 1.00 68.64  ? 252  PHE B C   1 
ATOM   12090 O  O   . PHE B 2 594  ? 132.553 84.073  125.757 1.00 78.52  ? 252  PHE B O   1 
ATOM   12091 C  CB  . PHE B 2 594  ? 130.923 83.286  128.620 1.00 63.22  ? 252  PHE B CB  1 
ATOM   12092 C  CG  . PHE B 2 594  ? 130.071 82.635  127.573 1.00 58.88  ? 252  PHE B CG  1 
ATOM   12093 C  CD1 . PHE B 2 594  ? 130.308 81.332  127.174 1.00 63.82  ? 252  PHE B CD1 1 
ATOM   12094 C  CD2 . PHE B 2 594  ? 129.004 83.320  127.014 1.00 64.03  ? 252  PHE B CD2 1 
ATOM   12095 C  CE1 . PHE B 2 594  ? 129.511 80.733  126.214 1.00 65.91  ? 252  PHE B CE1 1 
ATOM   12096 C  CE2 . PHE B 2 594  ? 128.204 82.726  126.056 1.00 56.86  ? 252  PHE B CE2 1 
ATOM   12097 C  CZ  . PHE B 2 594  ? 128.457 81.432  125.656 1.00 48.00  ? 252  PHE B CZ  1 
ATOM   12098 N  N   . HIS B 2 595  ? 131.779 85.799  126.988 1.00 72.99  ? 253  HIS B N   1 
ATOM   12099 C  CA  . HIS B 2 595  ? 131.667 86.676  125.824 1.00 58.92  ? 253  HIS B CA  1 
ATOM   12100 C  C   . HIS B 2 595  ? 133.022 86.910  125.166 1.00 66.74  ? 253  HIS B C   1 
ATOM   12101 O  O   . HIS B 2 595  ? 133.117 86.984  123.935 1.00 80.29  ? 253  HIS B O   1 
ATOM   12102 C  CB  . HIS B 2 595  ? 131.015 87.996  126.224 1.00 67.04  ? 253  HIS B CB  1 
ATOM   12103 C  CG  . HIS B 2 595  ? 129.535 87.888  126.420 1.00 70.51  ? 253  HIS B CG  1 
ATOM   12104 N  ND1 . HIS B 2 595  ? 128.730 87.144  125.585 1.00 72.75  ? 253  HIS B ND1 1 
ATOM   12105 C  CD2 . HIS B 2 595  ? 128.717 88.421  127.357 1.00 67.91  ? 253  HIS B CD2 1 
ATOM   12106 C  CE1 . HIS B 2 595  ? 127.479 87.224  125.998 1.00 68.59  ? 253  HIS B CE1 1 
ATOM   12107 N  NE2 . HIS B 2 595  ? 127.443 87.993  127.071 1.00 68.54  ? 253  HIS B NE2 1 
ATOM   12108 N  N   . GLN B 2 596  ? 134.078 87.059  125.970 1.00 75.50  ? 254  GLN B N   1 
ATOM   12109 C  CA  . GLN B 2 596  ? 135.408 87.265  125.400 1.00 69.17  ? 254  GLN B CA  1 
ATOM   12110 C  C   . GLN B 2 596  ? 135.844 86.075  124.559 1.00 63.76  ? 254  GLN B C   1 
ATOM   12111 O  O   . GLN B 2 596  ? 136.352 86.243  123.437 1.00 75.53  ? 254  GLN B O   1 
ATOM   12112 C  CB  . GLN B 2 596  ? 136.435 87.497  126.501 1.00 69.67  ? 254  GLN B CB  1 
ATOM   12113 C  CG  . GLN B 2 596  ? 137.811 87.789  125.937 1.00 80.77  ? 254  GLN B CG  1 
ATOM   12114 C  CD  . GLN B 2 596  ? 138.830 88.086  127.006 1.00 98.74  ? 254  GLN B CD  1 
ATOM   12115 O  OE1 . GLN B 2 596  ? 139.519 89.102  126.960 1.00 111.95 ? 254  GLN B OE1 1 
ATOM   12116 N  NE2 . GLN B 2 596  ? 138.945 87.185  127.975 1.00 90.88  ? 254  GLN B NE2 1 
ATOM   12117 N  N   . ILE B 2 597  ? 135.633 84.862  125.075 1.00 76.49  ? 255  ILE B N   1 
ATOM   12118 C  CA  . ILE B 2 597  ? 136.013 83.682  124.303 1.00 76.88  ? 255  ILE B CA  1 
ATOM   12119 C  C   . ILE B 2 597  ? 135.196 83.612  123.020 1.00 76.94  ? 255  ILE B C   1 
ATOM   12120 O  O   . ILE B 2 597  ? 135.705 83.213  121.965 1.00 81.35  ? 255  ILE B O   1 
ATOM   12121 C  CB  . ILE B 2 597  ? 135.858 82.406  125.147 1.00 83.82  ? 255  ILE B CB  1 
ATOM   12122 C  CG1 . ILE B 2 597  ? 136.755 82.480  126.380 1.00 87.85  ? 255  ILE B CG1 1 
ATOM   12123 C  CG2 . ILE B 2 597  ? 136.258 81.190  124.326 1.00 91.06  ? 255  ILE B CG2 1 
ATOM   12124 C  CD1 . ILE B 2 597  ? 136.655 81.271  127.278 1.00 102.13 ? 255  ILE B CD1 1 
ATOM   12125 N  N   . LEU B 2 598  ? 133.923 84.013  123.082 1.00 78.92  ? 256  LEU B N   1 
ATOM   12126 C  CA  . LEU B 2 598  ? 133.128 84.077  121.856 1.00 68.12  ? 256  LEU B CA  1 
ATOM   12127 C  C   . LEU B 2 598  ? 133.724 85.058  120.853 1.00 73.95  ? 256  LEU B C   1 
ATOM   12128 O  O   . LEU B 2 598  ? 133.809 84.760  119.656 1.00 81.12  ? 256  LEU B O   1 
ATOM   12129 C  CB  . LEU B 2 598  ? 131.690 84.482  122.165 1.00 60.08  ? 256  LEU B CB  1 
ATOM   12130 C  CG  . LEU B 2 598  ? 130.700 83.404  122.576 1.00 66.38  ? 256  LEU B CG  1 
ATOM   12131 C  CD1 . LEU B 2 598  ? 129.300 83.974  122.453 1.00 70.31  ? 256  LEU B CD1 1 
ATOM   12132 C  CD2 . LEU B 2 598  ? 130.870 82.186  121.683 1.00 68.88  ? 256  LEU B CD2 1 
ATOM   12133 N  N   . SER B 2 599  ? 134.154 86.228  121.329 1.00 81.61  ? 257  SER B N   1 
ATOM   12134 C  CA  . SER B 2 599  ? 134.687 87.242  120.425 1.00 79.77  ? 257  SER B CA  1 
ATOM   12135 C  C   . SER B 2 599  ? 135.992 86.802  119.782 1.00 82.92  ? 257  SER B C   1 
ATOM   12136 O  O   . SER B 2 599  ? 136.288 87.214  118.653 1.00 82.60  ? 257  SER B O   1 
ATOM   12137 C  CB  . SER B 2 599  ? 134.897 88.562  121.165 1.00 73.20  ? 257  SER B CB  1 
ATOM   12138 O  OG  . SER B 2 599  ? 135.929 88.438  122.126 1.00 92.02  ? 257  SER B OG  1 
ATOM   12139 N  N   . GLU B 2 600  ? 136.785 85.973  120.465 1.00 86.61  ? 258  GLU B N   1 
ATOM   12140 C  CA  . GLU B 2 600  ? 138.023 85.531  119.829 1.00 83.51  ? 258  GLU B CA  1 
ATOM   12141 C  C   . GLU B 2 600  ? 137.778 84.707  118.561 1.00 88.23  ? 258  GLU B C   1 
ATOM   12142 O  O   . GLU B 2 600  ? 138.711 84.521  117.776 1.00 98.20  ? 258  GLU B O   1 
ATOM   12143 C  CB  . GLU B 2 600  ? 138.906 84.782  120.830 1.00 89.97  ? 258  GLU B CB  1 
ATOM   12144 C  CG  . GLU B 2 600  ? 139.443 85.703  121.919 1.00 96.66  ? 258  GLU B CG  1 
ATOM   12145 C  CD  . GLU B 2 600  ? 140.289 84.983  122.938 1.00 119.40 ? 258  GLU B CD  1 
ATOM   12146 O  OE1 . GLU B 2 600  ? 140.385 83.740  122.859 1.00 121.34 ? 258  GLU B OE1 1 
ATOM   12147 O  OE2 . GLU B 2 600  ? 140.858 85.660  123.819 1.00 111.93 ? 258  GLU B OE2 1 
ATOM   12148 N  N   . GLY B 2 601  ? 136.566 84.203  118.339 1.00 86.42  ? 259  GLY B N   1 
ATOM   12149 C  CA  . GLY B 2 601  ? 136.247 83.504  117.102 1.00 77.21  ? 259  GLY B CA  1 
ATOM   12150 C  C   . GLY B 2 601  ? 135.854 82.037  117.176 1.00 89.29  ? 259  GLY B C   1 
ATOM   12151 O  O   . GLY B 2 601  ? 135.770 81.362  116.152 1.00 100.01 ? 259  GLY B O   1 
ATOM   12152 N  N   . GLU B 2 602  ? 135.581 81.548  118.374 1.00 87.23  ? 260  GLU B N   1 
ATOM   12153 C  CA  . GLU B 2 602  ? 135.210 80.170  118.672 1.00 89.11  ? 260  GLU B CA  1 
ATOM   12154 C  C   . GLU B 2 602  ? 133.719 80.009  118.923 1.00 84.99  ? 260  GLU B C   1 
ATOM   12155 O  O   . GLU B 2 602  ? 132.966 80.980  119.048 1.00 87.62  ? 260  GLU B O   1 
ATOM   12156 C  CB  . GLU B 2 602  ? 136.100 79.691  119.817 1.00 85.99  ? 260  GLU B CB  1 
ATOM   12157 C  CG  . GLU B 2 602  ? 137.341 78.868  119.437 1.00 121.33 ? 260  GLU B CG  1 
ATOM   12158 C  CD  . GLU B 2 602  ? 138.482 79.005  120.432 1.00 141.53 ? 260  GLU B CD  1 
ATOM   12159 O  OE1 . GLU B 2 602  ? 138.937 80.163  120.569 1.00 137.15 ? 260  GLU B OE1 1 
ATOM   12160 O  OE2 . GLU B 2 602  ? 138.612 78.080  121.321 1.00 126.35 ? 260  GLU B OE2 1 
ATOM   12161 N  N   . ASN B 2 603  ? 133.298 78.750  119.036 1.00 78.97  ? 261  ASN B N   1 
ATOM   12162 C  CA  . ASN B 2 603  ? 131.902 78.466  119.302 1.00 83.02  ? 261  ASN B CA  1 
ATOM   12163 C  C   . ASN B 2 603  ? 131.680 78.290  120.798 1.00 92.38  ? 261  ASN B C   1 
ATOM   12164 O  O   . ASN B 2 603  ? 132.618 78.232  121.597 1.00 100.22 ? 261  ASN B O   1 
ATOM   12165 C  CB  . ASN B 2 603  ? 131.418 77.235  118.528 1.00 91.65  ? 261  ASN B CB  1 
ATOM   12166 C  CG  . ASN B 2 603  ? 132.382 76.072  118.599 1.00 101.54 ? 261  ASN B CG  1 
ATOM   12167 O  OD1 . ASN B 2 603  ? 133.490 76.203  119.104 1.00 101.32 ? 261  ASN B OD1 1 
ATOM   12168 N  ND2 . ASN B 2 603  ? 131.954 74.913  118.093 1.00 98.88  ? 261  ASN B ND2 1 
ATOM   12169 N  N   . ALA B 2 604  ? 130.407 78.168  121.173 1.00 84.76  ? 262  ALA B N   1 
ATOM   12170 C  CA  . ALA B 2 604  ? 130.069 78.137  122.590 1.00 67.32  ? 262  ALA B CA  1 
ATOM   12171 C  C   . ALA B 2 604  ? 130.584 76.882  123.285 1.00 82.26  ? 262  ALA B C   1 
ATOM   12172 O  O   . ALA B 2 604  ? 130.872 76.922  124.486 1.00 95.97  ? 262  ALA B O   1 
ATOM   12173 C  CB  . ALA B 2 604  ? 128.555 78.258  122.768 1.00 60.61  ? 262  ALA B CB  1 
ATOM   12174 N  N   . GLN B 2 605  ? 130.726 75.772  122.561 1.00 86.02  ? 263  GLN B N   1 
ATOM   12175 C  CA  . GLN B 2 605  ? 131.129 74.524  123.203 1.00 84.14  ? 263  GLN B CA  1 
ATOM   12176 C  C   . GLN B 2 605  ? 132.586 74.576  123.662 1.00 90.33  ? 263  GLN B C   1 
ATOM   12177 O  O   . GLN B 2 605  ? 132.907 74.235  124.812 1.00 92.89  ? 263  GLN B O   1 
ATOM   12178 C  CB  . GLN B 2 605  ? 130.899 73.376  122.222 1.00 89.41  ? 263  GLN B CB  1 
ATOM   12179 C  CG  . GLN B 2 605  ? 129.425 73.173  121.910 1.00 93.49  ? 263  GLN B CG  1 
ATOM   12180 C  CD  . GLN B 2 605  ? 129.179 72.058  120.923 1.00 119.11 ? 263  GLN B CD  1 
ATOM   12181 O  OE1 . GLN B 2 605  ? 130.117 71.453  120.403 1.00 126.17 ? 263  GLN B OE1 1 
ATOM   12182 N  NE2 . GLN B 2 605  ? 127.910 71.791  120.638 1.00 121.85 ? 263  GLN B NE2 1 
ATOM   12183 N  N   . ALA B 2 606  ? 133.479 75.035  122.780 1.00 84.03  ? 264  ALA B N   1 
ATOM   12184 C  CA  . ALA B 2 606  ? 134.879 75.209  123.153 1.00 84.04  ? 264  ALA B CA  1 
ATOM   12185 C  C   . ALA B 2 606  ? 135.021 76.251  124.254 1.00 86.37  ? 264  ALA B C   1 
ATOM   12186 O  O   . ALA B 2 606  ? 135.853 76.107  125.160 1.00 91.91  ? 264  ALA B O   1 
ATOM   12187 C  CB  . ALA B 2 606  ? 135.705 75.593  121.926 1.00 96.73  ? 264  ALA B CB  1 
ATOM   12188 N  N   . ALA B 2 607  ? 134.207 77.309  124.190 1.00 82.11  ? 265  ALA B N   1 
ATOM   12189 C  CA  . ALA B 2 607  ? 134.213 78.333  125.227 1.00 82.91  ? 265  ALA B CA  1 
ATOM   12190 C  C   . ALA B 2 607  ? 133.862 77.740  126.584 1.00 91.01  ? 265  ALA B C   1 
ATOM   12191 O  O   . ALA B 2 607  ? 134.524 78.026  127.590 1.00 100.51 ? 265  ALA B O   1 
ATOM   12192 C  CB  . ALA B 2 607  ? 133.235 79.451  124.860 1.00 71.20  ? 265  ALA B CB  1 
ATOM   12193 N  N   . LEU B 2 608  ? 132.826 76.900  126.629 1.00 83.11  ? 266  LEU B N   1 
ATOM   12194 C  CA  . LEU B 2 608  ? 132.429 76.293  127.894 1.00 82.79  ? 266  LEU B CA  1 
ATOM   12195 C  C   . LEU B 2 608  ? 133.514 75.368  128.426 1.00 87.71  ? 266  LEU B C   1 
ATOM   12196 O  O   . LEU B 2 608  ? 133.789 75.356  129.632 1.00 87.90  ? 266  LEU B O   1 
ATOM   12197 C  CB  . LEU B 2 608  ? 131.112 75.536  127.732 1.00 81.07  ? 266  LEU B CB  1 
ATOM   12198 C  CG  . LEU B 2 608  ? 129.856 76.393  127.865 1.00 73.20  ? 266  LEU B CG  1 
ATOM   12199 C  CD1 . LEU B 2 608  ? 128.612 75.523  127.791 1.00 76.04  ? 266  LEU B CD1 1 
ATOM   12200 C  CD2 . LEU B 2 608  ? 129.897 77.182  129.168 1.00 65.64  ? 266  LEU B CD2 1 
ATOM   12201 N  N   . THR B 2 609  ? 134.144 74.587  127.544 1.00 87.24  ? 267  THR B N   1 
ATOM   12202 C  CA  . THR B 2 609  ? 135.210 73.700  128.008 1.00 83.98  ? 267  THR B CA  1 
ATOM   12203 C  C   . THR B 2 609  ? 136.382 74.493  128.586 1.00 87.54  ? 267  THR B C   1 
ATOM   12204 O  O   . THR B 2 609  ? 136.905 74.162  129.664 1.00 96.26  ? 267  THR B O   1 
ATOM   12205 C  CB  . THR B 2 609  ? 135.685 72.802  126.866 1.00 87.65  ? 267  THR B CB  1 
ATOM   12206 O  OG1 . THR B 2 609  ? 136.085 73.611  125.753 1.00 97.62  ? 267  THR B OG1 1 
ATOM   12207 C  CG2 . THR B 2 609  ? 134.569 71.866  126.425 1.00 79.47  ? 267  THR B CG2 1 
ATOM   12208 N  N   . ARG B 2 610  ? 136.804 75.554  127.892 1.00 86.25  ? 268  ARG B N   1 
ATOM   12209 C  CA  . ARG B 2 610  ? 137.922 76.353  128.389 1.00 86.20  ? 268  ARG B CA  1 
ATOM   12210 C  C   . ARG B 2 610  ? 137.576 77.050  129.702 1.00 82.61  ? 268  ARG B C   1 
ATOM   12211 O  O   . ARG B 2 610  ? 138.421 77.148  130.602 1.00 94.42  ? 268  ARG B O   1 
ATOM   12212 C  CB  . ARG B 2 610  ? 138.363 77.358  127.327 1.00 85.46  ? 268  ARG B CB  1 
ATOM   12213 C  CG  . ARG B 2 610  ? 139.603 78.145  127.715 1.00 95.75  ? 268  ARG B CG  1 
ATOM   12214 C  CD  . ARG B 2 610  ? 140.076 79.007  126.566 1.00 101.17 ? 268  ARG B CD  1 
ATOM   12215 N  NE  . ARG B 2 610  ? 139.999 78.272  125.307 1.00 109.20 ? 268  ARG B NE  1 
ATOM   12216 C  CZ  . ARG B 2 610  ? 140.068 78.830  124.105 1.00 119.72 ? 268  ARG B CZ  1 
ATOM   12217 N  NH1 . ARG B 2 610  ? 139.993 78.072  123.020 1.00 113.43 ? 268  ARG B NH1 1 
ATOM   12218 N  NH2 . ARG B 2 610  ? 140.217 80.141  123.986 1.00 116.18 ? 268  ARG B NH2 1 
ATOM   12219 N  N   . LEU B 2 611  ? 136.334 77.524  129.840 1.00 85.24  ? 269  LEU B N   1 
ATOM   12220 C  CA  . LEU B 2 611  ? 135.923 78.133  131.102 1.00 89.08  ? 269  LEU B CA  1 
ATOM   12221 C  C   . LEU B 2 611  ? 135.904 77.109  132.227 1.00 88.09  ? 269  LEU B C   1 
ATOM   12222 O  O   . LEU B 2 611  ? 136.273 77.422  133.365 1.00 95.12  ? 269  LEU B O   1 
ATOM   12223 C  CB  . LEU B 2 611  ? 134.562 78.807  130.954 1.00 84.33  ? 269  LEU B CB  1 
ATOM   12224 C  CG  . LEU B 2 611  ? 134.653 80.123  130.188 1.00 86.49  ? 269  LEU B CG  1 
ATOM   12225 C  CD1 . LEU B 2 611  ? 133.275 80.718  129.977 1.00 90.87  ? 269  LEU B CD1 1 
ATOM   12226 C  CD2 . LEU B 2 611  ? 135.561 81.085  130.943 1.00 88.58  ? 269  LEU B CD2 1 
ATOM   12227 N  N   . SER B 2 612  ? 135.479 75.879  131.929 1.00 92.58  ? 270  SER B N   1 
ATOM   12228 C  CA  . SER B 2 612  ? 135.508 74.827  132.937 1.00 90.39  ? 270  SER B CA  1 
ATOM   12229 C  C   . SER B 2 612  ? 136.933 74.568  133.406 1.00 98.00  ? 270  SER B C   1 
ATOM   12230 O  O   . SER B 2 612  ? 137.171 74.356  134.601 1.00 100.72 ? 270  SER B O   1 
ATOM   12231 C  CB  . SER B 2 612  ? 134.877 73.547  132.386 1.00 80.19  ? 270  SER B CB  1 
ATOM   12232 O  OG  . SER B 2 612  ? 135.564 73.090  131.235 1.00 98.81  ? 270  SER B OG  1 
ATOM   12233 N  N   . ARG B 2 613  ? 137.898 74.578  132.481 1.00 102.60 ? 271  ARG B N   1 
ATOM   12234 C  CA  . ARG B 2 613  ? 139.284 74.365  132.896 1.00 92.96  ? 271  ARG B CA  1 
ATOM   12235 C  C   . ARG B 2 613  ? 139.828 75.526  133.724 1.00 92.81  ? 271  ARG B C   1 
ATOM   12236 O  O   . ARG B 2 613  ? 140.397 75.314  134.802 1.00 95.97  ? 271  ARG B O   1 
ATOM   12237 C  CB  . ARG B 2 613  ? 140.205 74.147  131.694 1.00 97.49  ? 271  ARG B CB  1 
ATOM   12238 C  CG  . ARG B 2 613  ? 140.267 72.750  131.127 1.00 111.43 ? 271  ARG B CG  1 
ATOM   12239 C  CD  . ARG B 2 613  ? 140.425 72.789  129.614 1.00 118.62 ? 271  ARG B CD  1 
ATOM   12240 N  NE  . ARG B 2 613  ? 140.392 71.472  128.975 1.00 122.88 ? 271  ARG B NE  1 
ATOM   12241 C  CZ  . ARG B 2 613  ? 139.448 70.547  129.136 1.00 127.03 ? 271  ARG B CZ  1 
ATOM   12242 N  NH1 . ARG B 2 613  ? 138.387 70.765  129.902 1.00 117.25 ? 271  ARG B NH1 1 
ATOM   12243 N  NH2 . ARG B 2 613  ? 139.558 69.393  128.495 1.00 125.54 ? 271  ARG B NH2 1 
ATOM   12244 N  N   . THR B 2 614  ? 139.655 76.760  133.252 1.00 96.74  ? 272  THR B N   1 
ATOM   12245 C  CA  . THR B 2 614  ? 140.475 77.860  133.757 1.00 101.36 ? 272  THR B CA  1 
ATOM   12246 C  C   . THR B 2 614  ? 139.792 78.797  134.745 1.00 99.15  ? 272  THR B C   1 
ATOM   12247 O  O   . THR B 2 614  ? 140.483 79.370  135.594 1.00 106.54 ? 272  THR B O   1 
ATOM   12248 C  CB  . THR B 2 614  ? 141.011 78.700  132.592 1.00 110.07 ? 272  THR B CB  1 
ATOM   12249 O  OG1 . THR B 2 614  ? 139.992 79.601  132.138 1.00 110.30 ? 272  THR B OG1 1 
ATOM   12250 C  CG2 . THR B 2 614  ? 141.448 77.803  131.444 1.00 105.83 ? 272  THR B CG2 1 
ATOM   12251 N  N   . PHE B 2 615  ? 138.477 78.984  134.671 1.00 100.41 ? 273  PHE B N   1 
ATOM   12252 C  CA  . PHE B 2 615  ? 137.836 79.976  135.529 1.00 100.92 ? 273  PHE B CA  1 
ATOM   12253 C  C   . PHE B 2 615  ? 138.012 79.639  137.008 1.00 108.28 ? 273  PHE B C   1 
ATOM   12254 O  O   . PHE B 2 615  ? 137.855 78.490  137.428 1.00 115.75 ? 273  PHE B O   1 
ATOM   12255 C  CB  . PHE B 2 615  ? 136.350 80.088  135.190 1.00 100.71 ? 273  PHE B CB  1 
ATOM   12256 C  CG  . PHE B 2 615  ? 135.702 81.330  135.729 1.00 101.14 ? 273  PHE B CG  1 
ATOM   12257 C  CD1 . PHE B 2 615  ? 136.039 82.572  135.215 1.00 97.09  ? 273  PHE B CD1 1 
ATOM   12258 C  CD2 . PHE B 2 615  ? 134.778 81.265  136.757 1.00 110.30 ? 273  PHE B CD2 1 
ATOM   12259 C  CE1 . PHE B 2 615  ? 135.455 83.724  135.704 1.00 94.66  ? 273  PHE B CE1 1 
ATOM   12260 C  CE2 . PHE B 2 615  ? 134.191 82.417  137.253 1.00 101.19 ? 273  PHE B CE2 1 
ATOM   12261 C  CZ  . PHE B 2 615  ? 134.531 83.647  136.725 1.00 91.42  ? 273  PHE B CZ  1 
ATOM   12262 N  N   . ASP B 2 616  ? 138.332 80.673  137.796 1.00 105.83 ? 274  ASP B N   1 
ATOM   12263 C  CA  . ASP B 2 616  ? 138.797 80.486  139.169 1.00 113.71 ? 274  ASP B CA  1 
ATOM   12264 C  C   . ASP B 2 616  ? 137.739 79.872  140.075 1.00 109.30 ? 274  ASP B C   1 
ATOM   12265 O  O   . ASP B 2 616  ? 138.072 79.098  140.980 1.00 112.36 ? 274  ASP B O   1 
ATOM   12266 C  CB  . ASP B 2 616  ? 139.260 81.818  139.760 1.00 126.28 ? 274  ASP B CB  1 
ATOM   12267 C  CG  . ASP B 2 616  ? 139.932 81.651  141.109 1.00 135.49 ? 274  ASP B CG  1 
ATOM   12268 O  OD1 . ASP B 2 616  ? 140.893 80.858  141.204 1.00 134.48 ? 274  ASP B OD1 1 
ATOM   12269 O  OD2 . ASP B 2 616  ? 139.484 82.295  142.081 1.00 128.49 ? 274  ASP B OD2 1 
ATOM   12270 N  N   . ALA B 2 617  ? 136.466 80.199  139.857 1.00 109.96 ? 275  ALA B N   1 
ATOM   12271 C  CA  . ALA B 2 617  ? 135.404 79.765  140.755 1.00 104.09 ? 275  ALA B CA  1 
ATOM   12272 C  C   . ALA B 2 617  ? 135.164 78.260  140.730 1.00 99.28  ? 275  ALA B C   1 
ATOM   12273 O  O   . ALA B 2 617  ? 134.437 77.758  141.594 1.00 107.64 ? 275  ALA B O   1 
ATOM   12274 C  CB  . ALA B 2 617  ? 134.103 80.500  140.421 1.00 107.95 ? 275  ALA B CB  1 
ATOM   12275 N  N   . PHE B 2 618  ? 135.752 77.529  139.782 1.00 101.36 ? 276  PHE B N   1 
ATOM   12276 C  CA  . PHE B 2 618  ? 135.494 76.102  139.633 1.00 103.43 ? 276  PHE B CA  1 
ATOM   12277 C  C   . PHE B 2 618  ? 136.671 75.225  140.045 1.00 119.61 ? 276  PHE B C   1 
ATOM   12278 O  O   . PHE B 2 618  ? 136.604 74.004  139.870 1.00 127.22 ? 276  PHE B O   1 
ATOM   12279 C  CB  . PHE B 2 618  ? 135.116 75.784  138.185 1.00 104.90 ? 276  PHE B CB  1 
ATOM   12280 C  CG  . PHE B 2 618  ? 134.103 76.723  137.606 1.00 107.04 ? 276  PHE B CG  1 
ATOM   12281 C  CD1 . PHE B 2 618  ? 132.944 77.024  138.296 1.00 107.42 ? 276  PHE B CD1 1 
ATOM   12282 C  CD2 . PHE B 2 618  ? 134.314 77.312  136.370 1.00 104.81 ? 276  PHE B CD2 1 
ATOM   12283 C  CE1 . PHE B 2 618  ? 132.011 77.892  137.767 1.00 107.31 ? 276  PHE B CE1 1 
ATOM   12284 C  CE2 . PHE B 2 618  ? 133.385 78.180  135.834 1.00 98.40  ? 276  PHE B CE2 1 
ATOM   12285 C  CZ  . PHE B 2 618  ? 132.231 78.470  136.533 1.00 97.17  ? 276  PHE B CZ  1 
ATOM   12286 N  N   . LEU B 2 619  ? 137.741 75.800  140.586 1.00 124.81 ? 277  LEU B N   1 
ATOM   12287 C  CA  . LEU B 2 619  ? 138.867 74.981  141.014 1.00 128.94 ? 277  LEU B CA  1 
ATOM   12288 C  C   . LEU B 2 619  ? 138.524 74.217  142.286 1.00 128.41 ? 277  LEU B C   1 
ATOM   12289 O  O   . LEU B 2 619  ? 138.121 74.808  143.292 1.00 125.68 ? 277  LEU B O   1 
ATOM   12290 C  CB  . LEU B 2 619  ? 140.111 75.841  141.230 1.00 128.06 ? 277  LEU B CB  1 
ATOM   12291 C  CG  . LEU B 2 619  ? 140.956 76.165  139.993 1.00 134.84 ? 277  LEU B CG  1 
ATOM   12292 C  CD1 . LEU B 2 619  ? 141.532 74.879  139.413 1.00 135.13 ? 277  LEU B CD1 1 
ATOM   12293 C  CD2 . LEU B 2 619  ? 140.180 76.936  138.934 1.00 122.51 ? 277  LEU B CD2 1 
ATOM   12294 N  N   . GLY B 2 620  ? 138.686 72.896  142.236 1.00 124.84 ? 278  GLY B N   1 
ATOM   12295 C  CA  . GLY B 2 620  ? 138.458 72.051  143.390 1.00 124.37 ? 278  GLY B CA  1 
ATOM   12296 C  C   . GLY B 2 620  ? 137.031 72.045  143.899 1.00 123.69 ? 278  GLY B C   1 
ATOM   12297 O  O   . GLY B 2 620  ? 136.809 72.147  145.109 1.00 122.88 ? 278  GLY B O   1 
ATOM   12298 N  N   . VAL B 2 621  ? 136.053 71.928  143.003 1.00 124.88 ? 279  VAL B N   1 
ATOM   12299 C  CA  . VAL B 2 621  ? 134.644 71.891  143.377 1.00 132.72 ? 279  VAL B CA  1 
ATOM   12300 C  C   . VAL B 2 621  ? 134.074 70.532  142.998 1.00 125.94 ? 279  VAL B C   1 
ATOM   12301 O  O   . VAL B 2 621  ? 134.197 70.100  141.846 1.00 122.15 ? 279  VAL B O   1 
ATOM   12302 C  CB  . VAL B 2 621  ? 133.847 73.026  142.706 1.00 127.27 ? 279  VAL B CB  1 
ATOM   12303 C  CG1 . VAL B 2 621  ? 132.374 72.931  143.075 1.00 118.44 ? 279  VAL B CG1 1 
ATOM   12304 C  CG2 . VAL B 2 621  ? 134.415 74.380  143.107 1.00 118.55 ? 279  VAL B CG2 1 
ATOM   12305 N  N   . VAL B 2 622  ? 133.456 69.865  143.966 1.00 125.06 ? 280  VAL B N   1 
ATOM   12306 C  CA  . VAL B 2 622  ? 132.874 68.540  143.714 1.00 125.18 ? 280  VAL B CA  1 
ATOM   12307 C  C   . VAL B 2 622  ? 131.596 68.690  142.897 1.00 124.02 ? 280  VAL B C   1 
ATOM   12308 O  O   . VAL B 2 622  ? 130.806 69.618  143.149 1.00 124.64 ? 280  VAL B O   1 
ATOM   12309 C  CB  . VAL B 2 622  ? 132.610 67.816  145.037 1.00 132.77 ? 280  VAL B CB  1 
ATOM   12310 C  CG1 . VAL B 2 622  ? 133.924 67.354  145.652 1.00 133.58 ? 280  VAL B CG1 1 
ATOM   12311 C  CG2 . VAL B 2 622  ? 131.873 68.729  146.007 1.00 134.49 ? 280  VAL B CG2 1 
ATOM   12312 N  N   . PRO B 2 623  ? 131.362 67.831  141.909 1.00 121.24 ? 281  PRO B N   1 
ATOM   12313 C  CA  . PRO B 2 623  ? 130.137 67.919  141.126 1.00 113.29 ? 281  PRO B CA  1 
ATOM   12314 C  C   . PRO B 2 623  ? 128.896 67.629  142.003 1.00 114.44 ? 281  PRO B C   1 
ATOM   12315 O  O   . PRO B 2 623  ? 128.981 66.844  142.949 1.00 121.37 ? 281  PRO B O   1 
ATOM   12316 C  CB  . PRO B 2 623  ? 130.313 66.845  140.050 1.00 117.16 ? 281  PRO B CB  1 
ATOM   12317 C  CG  . PRO B 2 623  ? 131.358 65.921  140.593 1.00 129.79 ? 281  PRO B CG  1 
ATOM   12318 C  CD  . PRO B 2 623  ? 132.267 66.783  141.404 1.00 125.40 ? 281  PRO B CD  1 
ATOM   12319 N  N   . PRO B 2 624  ? 127.779 68.266  141.683 1.00 110.52 ? 282  PRO B N   1 
ATOM   12320 C  CA  . PRO B 2 624  ? 126.545 68.004  142.448 1.00 123.12 ? 282  PRO B CA  1 
ATOM   12321 C  C   . PRO B 2 624  ? 125.970 66.633  142.109 1.00 126.11 ? 282  PRO B C   1 
ATOM   12322 O  O   . PRO B 2 624  ? 126.409 65.955  141.181 1.00 125.99 ? 282  PRO B O   1 
ATOM   12323 C  CB  . PRO B 2 624  ? 125.612 69.138  142.008 1.00 114.03 ? 282  PRO B CB  1 
ATOM   12324 C  CG  . PRO B 2 624  ? 126.080 69.485  140.633 1.00 103.64 ? 282  PRO B CG  1 
ATOM   12325 C  CD  . PRO B 2 624  ? 127.575 69.278  140.636 1.00 100.11 ? 282  PRO B CD  1 
ATOM   12326 N  N   . VAL B 2 625  ? 124.962 66.226  142.883 1.00 124.68 ? 283  VAL B N   1 
ATOM   12327 C  CA  . VAL B 2 625  ? 124.326 64.915  142.741 1.00 137.49 ? 283  VAL B CA  1 
ATOM   12328 C  C   . VAL B 2 625  ? 122.881 65.096  142.289 1.00 136.82 ? 283  VAL B C   1 
ATOM   12329 O  O   . VAL B 2 625  ? 122.134 65.889  142.875 1.00 137.12 ? 283  VAL B O   1 
ATOM   12330 C  CB  . VAL B 2 625  ? 124.392 64.123  144.058 1.00 146.32 ? 283  VAL B CB  1 
ATOM   12331 C  CG1 . VAL B 2 625  ? 123.584 62.838  143.953 1.00 151.78 ? 283  VAL B CG1 1 
ATOM   12332 C  CG2 . VAL B 2 625  ? 125.839 63.828  144.429 1.00 137.43 ? 283  VAL B CG2 1 
ATOM   12333 N  N   . ILE B 2 626  ? 122.491 64.359  141.247 1.00 138.83 ? 284  ILE B N   1 
ATOM   12334 C  CA  . ILE B 2 626  ? 121.151 64.421  140.664 1.00 143.55 ? 284  ILE B CA  1 
ATOM   12335 C  C   . ILE B 2 626  ? 120.435 63.088  140.874 1.00 163.16 ? 284  ILE B C   1 
ATOM   12336 O  O   . ILE B 2 626  ? 120.980 62.025  140.548 1.00 160.02 ? 284  ILE B O   1 
ATOM   12337 C  CB  . ILE B 2 626  ? 121.214 64.776  139.168 1.00 137.58 ? 284  ILE B CB  1 
ATOM   12338 C  CG1 . ILE B 2 626  ? 121.375 66.286  138.989 1.00 127.33 ? 284  ILE B CG1 1 
ATOM   12339 C  CG2 . ILE B 2 626  ? 119.957 64.307  138.451 1.00 159.02 ? 284  ILE B CG2 1 
ATOM   12340 C  CD1 . ILE B 2 626  ? 121.472 66.722  137.544 1.00 125.16 ? 284  ILE B CD1 1 
ATOM   12341 N  N   . ARG B 2 627  ? 119.222 63.145  141.426 1.00 162.70 ? 285  ARG B N   1 
ATOM   12342 C  CA  . ARG B 2 627  ? 118.400 61.965  141.702 1.00 164.16 ? 285  ARG B CA  1 
ATOM   12343 C  C   . ARG B 2 627  ? 117.538 61.607  140.488 1.00 155.37 ? 285  ARG B C   1 
ATOM   12344 O  O   . ARG B 2 627  ? 116.796 62.458  139.986 1.00 153.02 ? 285  ARG B O   1 
ATOM   12345 C  CB  . ARG B 2 627  ? 117.511 62.193  142.924 1.00 168.44 ? 285  ARG B CB  1 
ATOM   12346 C  CG  . ARG B 2 627  ? 118.253 62.386  144.230 1.00 169.98 ? 285  ARG B CG  1 
ATOM   12347 C  CD  . ARG B 2 627  ? 118.879 61.075  144.668 1.00 172.92 ? 285  ARG B CD  1 
ATOM   12348 N  NE  . ARG B 2 627  ? 117.887 60.088  145.085 1.00 178.65 ? 285  ARG B NE  1 
ATOM   12349 C  CZ  . ARG B 2 627  ? 117.520 59.050  144.339 1.00 175.24 ? 285  ARG B CZ  1 
ATOM   12350 N  NH1 . ARG B 2 627  ? 118.068 58.863  143.145 1.00 168.74 ? 285  ARG B NH1 1 
ATOM   12351 N  NH2 . ARG B 2 627  ? 116.609 58.195  144.784 1.00 172.84 ? 285  ARG B NH2 1 
ATOM   12352 N  N   . VAL B 2 628  ? 117.632 60.352  140.015 1.00 160.34 ? 286  VAL B N   1 
ATOM   12353 C  CA  . VAL B 2 628  ? 116.853 59.848  138.880 1.00 165.32 ? 286  VAL B CA  1 
ATOM   12354 C  C   . VAL B 2 628  ? 116.230 58.488  139.215 1.00 175.26 ? 286  VAL B C   1 
ATOM   12355 O  O   . VAL B 2 628  ? 116.670 57.790  140.131 1.00 177.79 ? 286  VAL B O   1 
ATOM   12356 C  CB  . VAL B 2 628  ? 117.707 59.751  137.595 1.00 165.73 ? 286  VAL B CB  1 
ATOM   12357 C  CG1 . VAL B 2 628  ? 118.148 61.138  137.150 1.00 163.81 ? 286  VAL B CG1 1 
ATOM   12358 C  CG2 . VAL B 2 628  ? 118.908 58.846  137.822 1.00 165.20 ? 286  VAL B CG2 1 
ATOM   12359 N  N   . LYS B 2 629  ? 115.189 58.104  138.449 1.00 165.22 ? 287  LYS B N   1 
ATOM   12360 C  CA  . LYS B 2 629  ? 114.539 56.815  138.700 1.00 168.47 ? 287  LYS B CA  1 
ATOM   12361 C  C   . LYS B 2 629  ? 115.438 55.665  138.252 1.00 166.31 ? 287  LYS B C   1 
ATOM   12362 O  O   . LYS B 2 629  ? 115.630 54.680  138.979 1.00 164.67 ? 287  LYS B O   1 
ATOM   12363 C  CB  . LYS B 2 629  ? 113.188 56.724  137.963 1.00 165.09 ? 287  LYS B CB  1 
ATOM   12364 C  CG  . LYS B 2 629  ? 112.470 55.437  138.354 1.00 158.83 ? 287  LYS B CG  1 
ATOM   12365 C  CD  . LYS B 2 629  ? 111.954 55.526  139.871 1.00 161.02 ? 287  LYS B CD  1 
ATOM   12366 C  CE  . LYS B 2 629  ? 110.555 56.178  140.175 1.00 145.62 ? 287  LYS B CE  1 
ATOM   12367 N  NZ  . LYS B 2 629  ? 109.519 55.091  139.846 1.00 142.36 ? 287  LYS B NZ  1 
ATOM   12368 N  N   . ASN B 2 630  ? 116.019 55.790  137.063 1.00 163.70 ? 288  ASN B N   1 
ATOM   12369 C  CA  . ASN B 2 630  ? 116.955 54.819  136.515 1.00 163.02 ? 288  ASN B CA  1 
ATOM   12370 C  C   . ASN B 2 630  ? 117.814 55.517  135.462 1.00 168.10 ? 288  ASN B C   1 
ATOM   12371 O  O   . ASN B 2 630  ? 117.814 56.749  135.349 1.00 161.59 ? 288  ASN B O   1 
ATOM   12372 C  CB  . ASN B 2 630  ? 116.199 53.621  135.940 1.00 154.57 ? 288  ASN B CB  1 
ATOM   12373 C  CG  . ASN B 2 630  ? 115.066 54.037  135.018 1.00 161.14 ? 288  ASN B CG  1 
ATOM   12374 O  OD1 . ASN B 2 630  ? 114.755 55.223  134.887 1.00 165.18 ? 288  ASN B OD1 1 
ATOM   12375 N  ND2 . ASN B 2 630  ? 114.436 53.058  134.381 1.00 156.04 ? 288  ASN B ND2 1 
ATOM   12376 N  N   . PHE B 2 631  ? 118.549 54.725  134.684 1.00 166.84 ? 289  PHE B N   1 
ATOM   12377 C  CA  . PHE B 2 631  ? 119.415 55.274  133.649 1.00 162.53 ? 289  PHE B CA  1 
ATOM   12378 C  C   . PHE B 2 631  ? 118.703 55.419  132.310 1.00 166.70 ? 289  PHE B C   1 
ATOM   12379 O  O   . PHE B 2 631  ? 119.319 55.880  131.345 1.00 161.48 ? 289  PHE B O   1 
ATOM   12380 C  CB  . PHE B 2 631  ? 120.665 54.405  133.473 1.00 151.44 ? 289  PHE B CB  1 
ATOM   12381 C  CG  . PHE B 2 631  ? 121.486 54.271  134.720 1.00 164.32 ? 289  PHE B CG  1 
ATOM   12382 C  CD1 . PHE B 2 631  ? 121.501 55.284  135.662 1.00 166.52 ? 289  PHE B CD1 1 
ATOM   12383 C  CD2 . PHE B 2 631  ? 122.255 53.142  134.943 1.00 169.34 ? 289  PHE B CD2 1 
ATOM   12384 C  CE1 . PHE B 2 631  ? 122.253 55.171  136.813 1.00 160.90 ? 289  PHE B CE1 1 
ATOM   12385 C  CE2 . PHE B 2 631  ? 123.015 53.023  136.092 1.00 163.73 ? 289  PHE B CE2 1 
ATOM   12386 C  CZ  . PHE B 2 631  ? 123.011 54.038  137.029 1.00 160.21 ? 289  PHE B CZ  1 
ATOM   12387 N  N   . GLN B 2 632  ? 117.429 55.033  132.229 1.00 170.78 ? 290  GLN B N   1 
ATOM   12388 C  CA  . GLN B 2 632  ? 116.607 55.350  131.070 1.00 165.16 ? 290  GLN B CA  1 
ATOM   12389 C  C   . GLN B 2 632  ? 115.982 56.733  131.167 1.00 159.85 ? 290  GLN B C   1 
ATOM   12390 O  O   . GLN B 2 632  ? 115.458 57.235  130.167 1.00 160.47 ? 290  GLN B O   1 
ATOM   12391 C  CB  . GLN B 2 632  ? 115.522 54.288  130.883 1.00 160.46 ? 290  GLN B CB  1 
ATOM   12392 C  CG  . GLN B 2 632  ? 116.091 52.887  130.792 1.00 165.24 ? 290  GLN B CG  1 
ATOM   12393 C  CD  . GLN B 2 632  ? 117.163 52.777  129.723 1.00 162.25 ? 290  GLN B CD  1 
ATOM   12394 O  OE1 . GLN B 2 632  ? 118.229 52.208  129.954 1.00 152.24 ? 290  GLN B OE1 1 
ATOM   12395 N  NE2 . GLN B 2 632  ? 116.883 53.321  128.543 1.00 161.58 ? 290  GLN B NE2 1 
ATOM   12396 N  N   . THR B 2 633  ? 116.029 57.354  132.347 1.00 159.80 ? 291  THR B N   1 
ATOM   12397 C  CA  . THR B 2 633  ? 115.473 58.684  132.539 1.00 157.45 ? 291  THR B CA  1 
ATOM   12398 C  C   . THR B 2 633  ? 116.388 59.774  131.996 1.00 158.94 ? 291  THR B C   1 
ATOM   12399 O  O   . THR B 2 633  ? 115.902 60.852  131.637 1.00 151.64 ? 291  THR B O   1 
ATOM   12400 C  CB  . THR B 2 633  ? 115.206 58.925  134.030 1.00 159.85 ? 291  THR B CB  1 
ATOM   12401 O  OG1 . THR B 2 633  ? 114.539 57.785  134.586 1.00 165.02 ? 291  THR B OG1 1 
ATOM   12402 C  CG2 . THR B 2 633  ? 114.325 60.150  134.230 1.00 165.19 ? 291  THR B CG2 1 
ATOM   12403 N  N   . VAL B 2 634  ? 117.688 59.509  131.908 1.00 159.55 ? 292  VAL B N   1 
ATOM   12404 C  CA  . VAL B 2 634  ? 118.654 60.485  131.408 1.00 154.32 ? 292  VAL B CA  1 
ATOM   12405 C  C   . VAL B 2 634  ? 118.370 60.751  129.933 1.00 157.92 ? 292  VAL B C   1 
ATOM   12406 O  O   . VAL B 2 634  ? 117.883 59.857  129.223 1.00 155.04 ? 292  VAL B O   1 
ATOM   12407 C  CB  . VAL B 2 634  ? 120.099 60.010  131.631 1.00 150.64 ? 292  VAL B CB  1 
ATOM   12408 C  CG1 . VAL B 2 634  ? 120.306 59.602  133.082 1.00 156.02 ? 292  VAL B CG1 1 
ATOM   12409 C  CG2 . VAL B 2 634  ? 120.443 58.856  130.705 1.00 149.26 ? 292  VAL B CG2 1 
ATOM   12410 N  N   . PRO B 2 635  ? 118.622 61.966  129.442 1.00 154.51 ? 293  PRO B N   1 
ATOM   12411 C  CA  . PRO B 2 635  ? 118.278 62.283  128.052 1.00 145.03 ? 293  PRO B CA  1 
ATOM   12412 C  C   . PRO B 2 635  ? 119.047 61.408  127.074 1.00 135.40 ? 293  PRO B C   1 
ATOM   12413 O  O   . PRO B 2 635  ? 120.165 60.965  127.343 1.00 138.64 ? 293  PRO B O   1 
ATOM   12414 C  CB  . PRO B 2 635  ? 118.679 63.756  127.918 1.00 145.12 ? 293  PRO B CB  1 
ATOM   12415 C  CG  . PRO B 2 635  ? 118.599 64.287  129.313 1.00 142.06 ? 293  PRO B CG  1 
ATOM   12416 C  CD  . PRO B 2 635  ? 119.071 63.156  130.182 1.00 139.68 ? 293  PRO B CD  1 
ATOM   12417 N  N   . ARG B 2 636  ? 118.415 61.154  125.930 1.00 131.85 ? 294  ARG B N   1 
ATOM   12418 C  CA  . ARG B 2 636  ? 118.993 60.257  124.931 1.00 145.53 ? 294  ARG B CA  1 
ATOM   12419 C  C   . ARG B 2 636  ? 120.355 60.700  124.407 1.00 149.34 ? 294  ARG B C   1 
ATOM   12420 O  O   . ARG B 2 636  ? 121.263 59.854  124.334 1.00 150.67 ? 294  ARG B O   1 
ATOM   12421 C  CB  . ARG B 2 636  ? 117.994 60.064  123.786 1.00 147.50 ? 294  ARG B CB  1 
ATOM   12422 C  CG  . ARG B 2 636  ? 118.504 59.170  122.675 1.00 154.04 ? 294  ARG B CG  1 
ATOM   12423 C  CD  . ARG B 2 636  ? 117.376 58.329  122.098 1.00 170.43 ? 294  ARG B CD  1 
ATOM   12424 N  NE  . ARG B 2 636  ? 116.784 57.440  123.099 1.00 176.52 ? 294  ARG B NE  1 
ATOM   12425 C  CZ  . ARG B 2 636  ? 117.435 56.488  123.765 1.00 176.78 ? 294  ARG B CZ  1 
ATOM   12426 N  NH1 . ARG B 2 636  ? 118.723 56.253  123.540 1.00 162.28 ? 294  ARG B NH1 1 
ATOM   12427 N  NH2 . ARG B 2 636  ? 116.786 55.749  124.654 1.00 168.15 ? 294  ARG B NH2 1 
ATOM   12428 N  N   . PRO B 2 637  ? 120.580 61.964  124.024 1.00 138.99 ? 295  PRO B N   1 
ATOM   12429 C  CA  . PRO B 2 637  ? 121.919 62.334  123.526 1.00 127.68 ? 295  PRO B CA  1 
ATOM   12430 C  C   . PRO B 2 637  ? 123.037 62.216  124.550 1.00 134.36 ? 295  PRO B C   1 
ATOM   12431 O  O   . PRO B 2 637  ? 124.203 62.123  124.150 1.00 136.11 ? 295  PRO B O   1 
ATOM   12432 C  CB  . PRO B 2 637  ? 121.736 63.794  123.082 1.00 117.51 ? 295  PRO B CB  1 
ATOM   12433 C  CG  . PRO B 2 637  ? 120.267 63.963  122.890 1.00 127.49 ? 295  PRO B CG  1 
ATOM   12434 C  CD  . PRO B 2 637  ? 119.643 63.098  123.934 1.00 135.21 ? 295  PRO B CD  1 
ATOM   12435 N  N   . CYS B 2 638  ? 122.733 62.206  125.846 1.00 139.61 ? 296  CYS B N   1 
ATOM   12436 C  CA  . CYS B 2 638  ? 123.767 62.122  126.870 1.00 136.46 ? 296  CYS B CA  1 
ATOM   12437 C  C   . CYS B 2 638  ? 124.056 60.699  127.333 1.00 144.55 ? 296  CYS B C   1 
ATOM   12438 O  O   . CYS B 2 638  ? 124.955 60.506  128.158 1.00 144.26 ? 296  CYS B O   1 
ATOM   12439 C  CB  . CYS B 2 638  ? 123.379 62.984  128.076 1.00 130.77 ? 296  CYS B CB  1 
ATOM   12440 S  SG  . CYS B 2 638  ? 123.179 64.738  127.691 1.00 130.45 ? 296  CYS B SG  1 
ATOM   12441 N  N   . GLN B 2 639  ? 123.330 59.703  126.820 1.00 151.38 ? 297  GLN B N   1 
ATOM   12442 C  CA  . GLN B 2 639  ? 123.521 58.331  127.284 1.00 149.00 ? 297  GLN B CA  1 
ATOM   12443 C  C   . GLN B 2 639  ? 124.920 57.816  126.970 1.00 149.29 ? 297  GLN B C   1 
ATOM   12444 O  O   . GLN B 2 639  ? 125.546 57.149  127.803 1.00 146.29 ? 297  GLN B O   1 
ATOM   12445 C  CB  . GLN B 2 639  ? 122.464 57.421  126.661 1.00 145.04 ? 297  GLN B CB  1 
ATOM   12446 C  CG  . GLN B 2 639  ? 121.042 57.857  126.953 1.00 150.24 ? 297  GLN B CG  1 
ATOM   12447 C  CD  . GLN B 2 639  ? 120.345 56.941  127.934 1.00 153.38 ? 297  GLN B CD  1 
ATOM   12448 O  OE1 . GLN B 2 639  ? 120.991 56.177  128.652 1.00 153.82 ? 297  GLN B OE1 1 
ATOM   12449 N  NE2 . GLN B 2 639  ? 119.021 57.024  127.984 1.00 151.86 ? 297  GLN B NE2 1 
ATOM   12450 N  N   . LYS B 2 640  ? 125.429 58.117  125.775 1.00 147.85 ? 298  LYS B N   1 
ATOM   12451 C  CA  . LYS B 2 640  ? 126.680 57.528  125.312 1.00 156.03 ? 298  LYS B CA  1 
ATOM   12452 C  C   . LYS B 2 640  ? 127.900 58.020  126.087 1.00 151.60 ? 298  LYS B C   1 
ATOM   12453 O  O   . LYS B 2 640  ? 128.964 57.400  125.995 1.00 146.87 ? 298  LYS B O   1 
ATOM   12454 C  CB  . LYS B 2 640  ? 126.850 57.794  123.815 1.00 155.56 ? 298  LYS B CB  1 
ATOM   12455 C  CG  . LYS B 2 640  ? 127.684 56.747  123.098 1.00 157.37 ? 298  LYS B CG  1 
ATOM   12456 C  CD  . LYS B 2 640  ? 127.713 56.994  121.601 1.00 157.54 ? 298  LYS B CD  1 
ATOM   12457 C  CE  . LYS B 2 640  ? 126.324 56.833  121.002 1.00 149.50 ? 298  LYS B CE  1 
ATOM   12458 N  NZ  . LYS B 2 640  ? 126.317 57.058  119.530 1.00 146.20 ? 298  LYS B NZ  1 
ATOM   12459 N  N   . SER B 2 641  ? 127.773 59.107  126.845 1.00 151.89 ? 299  SER B N   1 
ATOM   12460 C  CA  . SER B 2 641  ? 128.898 59.715  127.547 1.00 147.37 ? 299  SER B CA  1 
ATOM   12461 C  C   . SER B 2 641  ? 129.011 59.287  129.007 1.00 152.22 ? 299  SER B C   1 
ATOM   12462 O  O   . SER B 2 641  ? 129.934 59.731  129.697 1.00 146.83 ? 299  SER B O   1 
ATOM   12463 C  CB  . SER B 2 641  ? 128.803 61.243  127.466 1.00 136.50 ? 299  SER B CB  1 
ATOM   12464 O  OG  . SER B 2 641  ? 128.861 61.687  126.121 1.00 136.41 ? 299  SER B OG  1 
ATOM   12465 N  N   . LEU B 2 642  ? 128.106 58.441  129.494 1.00 151.84 ? 300  LEU B N   1 
ATOM   12466 C  CA  . LEU B 2 642  ? 128.151 57.997  130.882 1.00 146.71 ? 300  LEU B CA  1 
ATOM   12467 C  C   . LEU B 2 642  ? 129.348 57.087  131.137 1.00 154.06 ? 300  LEU B C   1 
ATOM   12468 O  O   . LEU B 2 642  ? 129.744 56.298  130.274 1.00 158.89 ? 300  LEU B O   1 
ATOM   12469 C  CB  . LEU B 2 642  ? 126.861 57.261  131.238 1.00 142.60 ? 300  LEU B CB  1 
ATOM   12470 C  CG  . LEU B 2 642  ? 125.588 58.100  131.329 1.00 143.67 ? 300  LEU B CG  1 
ATOM   12471 C  CD1 . LEU B 2 642  ? 124.410 57.231  131.740 1.00 144.36 ? 300  LEU B CD1 1 
ATOM   12472 C  CD2 . LEU B 2 642  ? 125.779 59.253  132.304 1.00 148.47 ? 300  LEU B CD2 1 
ATOM   12473 N  N   . ARG B 2 643  ? 129.925 57.201  132.336 1.00 151.08 ? 301  ARG B N   1 
ATOM   12474 C  CA  . ARG B 2 643  ? 131.110 56.439  132.710 1.00 149.19 ? 301  ARG B CA  1 
ATOM   12475 C  C   . ARG B 2 643  ? 130.957 55.952  134.148 1.00 156.81 ? 301  ARG B C   1 
ATOM   12476 O  O   . ARG B 2 643  ? 129.919 56.152  134.786 1.00 155.31 ? 301  ARG B O   1 
ATOM   12477 C  CB  . ARG B 2 643  ? 132.383 57.282  132.561 1.00 150.19 ? 301  ARG B CB  1 
ATOM   12478 C  CG  . ARG B 2 643  ? 132.638 57.785  131.154 1.00 156.37 ? 301  ARG B CG  1 
ATOM   12479 C  CD  . ARG B 2 643  ? 132.992 56.653  130.209 1.00 156.45 ? 301  ARG B CD  1 
ATOM   12480 N  NE  . ARG B 2 643  ? 133.205 57.146  128.854 1.00 160.48 ? 301  ARG B NE  1 
ATOM   12481 C  CZ  . ARG B 2 643  ? 134.378 57.561  128.389 1.00 156.55 ? 301  ARG B CZ  1 
ATOM   12482 N  NH1 . ARG B 2 643  ? 135.446 57.550  129.175 1.00 157.45 ? 301  ARG B NH1 1 
ATOM   12483 N  NH2 . ARG B 2 643  ? 134.481 57.998  127.141 1.00 148.41 ? 301  ARG B NH2 1 
ATOM   12484 N  N   . ALA B 2 644  ? 132.009 55.320  134.663 1.00 159.45 ? 302  ALA B N   1 
ATOM   12485 C  CA  . ALA B 2 644  ? 132.062 54.890  136.052 1.00 153.07 ? 302  ALA B CA  1 
ATOM   12486 C  C   . ALA B 2 644  ? 132.708 55.952  136.935 1.00 154.58 ? 302  ALA B C   1 
ATOM   12487 O  O   . ALA B 2 644  ? 133.622 56.668  136.514 1.00 157.51 ? 302  ALA B O   1 
ATOM   12488 C  CB  . ALA B 2 644  ? 132.829 53.572  136.180 1.00 148.65 ? 302  ALA B CB  1 
ATOM   12489 N  N   . VAL B 2 645  ? 132.223 56.044  138.170 1.00 155.72 ? 303  VAL B N   1 
ATOM   12490 C  CA  . VAL B 2 645  ? 132.628 57.092  139.107 1.00 160.94 ? 303  VAL B CA  1 
ATOM   12491 C  C   . VAL B 2 645  ? 134.112 56.964  139.437 1.00 168.50 ? 303  VAL B C   1 
ATOM   12492 O  O   . VAL B 2 645  ? 134.555 55.904  139.907 1.00 165.82 ? 303  VAL B O   1 
ATOM   12493 C  CB  . VAL B 2 645  ? 131.783 57.051  140.390 1.00 159.88 ? 303  VAL B CB  1 
ATOM   12494 C  CG1 . VAL B 2 645  ? 132.248 58.125  141.364 1.00 148.01 ? 303  VAL B CG1 1 
ATOM   12495 C  CG2 . VAL B 2 645  ? 130.309 57.234  140.060 1.00 157.65 ? 303  VAL B CG2 1 
ATOM   12496 N  N   . PRO B 2 646  ? 134.908 58.004  139.214 1.00 177.55 ? 304  PRO B N   1 
ATOM   12497 C  CA  . PRO B 2 646  ? 136.326 57.954  139.579 1.00 176.87 ? 304  PRO B CA  1 
ATOM   12498 C  C   . PRO B 2 646  ? 136.502 58.116  141.079 1.00 177.46 ? 304  PRO B C   1 
ATOM   12499 O  O   . PRO B 2 646  ? 135.535 58.434  141.789 1.00 167.80 ? 304  PRO B O   1 
ATOM   12500 C  CB  . PRO B 2 646  ? 136.925 59.141  138.809 1.00 167.17 ? 304  PRO B CB  1 
ATOM   12501 C  CG  . PRO B 2 646  ? 135.798 60.097  138.672 1.00 172.60 ? 304  PRO B CG  1 
ATOM   12502 C  CD  . PRO B 2 646  ? 134.548 59.267  138.548 1.00 180.14 ? 304  PRO B CD  1 
ATOM   12503 N  N   . PRO B 2 647  ? 137.719 57.886  141.606 1.00 174.59 ? 305  PRO B N   1 
ATOM   12504 C  CA  . PRO B 2 647  ? 137.939 58.009  143.056 1.00 173.53 ? 305  PRO B CA  1 
ATOM   12505 C  C   . PRO B 2 647  ? 137.535 59.361  143.624 1.00 167.88 ? 305  PRO B C   1 
ATOM   12506 O  O   . PRO B 2 647  ? 136.707 59.431  144.539 1.00 161.89 ? 305  PRO B O   1 
ATOM   12507 C  CB  . PRO B 2 647  ? 139.447 57.774  143.201 1.00 171.92 ? 305  PRO B CB  1 
ATOM   12508 C  CG  . PRO B 2 647  ? 139.796 56.907  142.047 1.00 164.38 ? 305  PRO B CG  1 
ATOM   12509 C  CD  . PRO B 2 647  ? 138.902 57.335  140.918 1.00 163.49 ? 305  PRO B CD  1 
ATOM   12510 N  N   . ASN B 2 648  ? 138.103 60.441  143.091 1.00 169.02 ? 306  ASN B N   1 
ATOM   12511 C  CA  . ASN B 2 648  ? 137.842 61.798  143.571 1.00 165.06 ? 306  ASN B CA  1 
ATOM   12512 C  C   . ASN B 2 648  ? 137.461 62.678  142.388 1.00 163.43 ? 306  ASN B C   1 
ATOM   12513 O  O   . ASN B 2 648  ? 138.292 63.431  141.861 1.00 155.87 ? 306  ASN B O   1 
ATOM   12514 C  CB  . ASN B 2 648  ? 139.058 62.361  144.310 1.00 168.08 ? 306  ASN B CB  1 
ATOM   12515 C  CG  . ASN B 2 648  ? 139.289 61.686  145.649 1.00 173.35 ? 306  ASN B CG  1 
ATOM   12516 O  OD1 . ASN B 2 648  ? 138.389 61.051  146.199 1.00 173.20 ? 306  ASN B OD1 1 
ATOM   12517 N  ND2 . ASN B 2 648  ? 140.500 61.816  146.177 1.00 170.51 ? 306  ASN B ND2 1 
ATOM   12518 N  N   . PRO B 2 649  ? 136.208 62.606  141.944 1.00 161.89 ? 307  PRO B N   1 
ATOM   12519 C  CA  . PRO B 2 649  ? 135.780 63.420  140.803 1.00 155.89 ? 307  PRO B CA  1 
ATOM   12520 C  C   . PRO B 2 649  ? 135.777 64.904  141.135 1.00 151.14 ? 307  PRO B C   1 
ATOM   12521 O  O   . PRO B 2 649  ? 135.517 65.314  142.270 1.00 142.42 ? 307  PRO B O   1 
ATOM   12522 C  CB  . PRO B 2 649  ? 134.362 62.911  140.518 1.00 147.82 ? 307  PRO B CB  1 
ATOM   12523 C  CG  . PRO B 2 649  ? 133.877 62.410  141.836 1.00 142.42 ? 307  PRO B CG  1 
ATOM   12524 C  CD  . PRO B 2 649  ? 135.086 61.875  142.562 1.00 154.92 ? 307  PRO B CD  1 
ATOM   12525 N  N   . THR B 2 650  ? 136.069 65.712  140.119 1.00 146.23 ? 308  THR B N   1 
ATOM   12526 C  CA  . THR B 2 650  ? 136.099 67.159  140.263 1.00 140.57 ? 308  THR B CA  1 
ATOM   12527 C  C   . THR B 2 650  ? 135.807 67.794  138.910 1.00 136.36 ? 308  THR B C   1 
ATOM   12528 O  O   . THR B 2 650  ? 136.068 67.201  137.860 1.00 130.26 ? 308  THR B O   1 
ATOM   12529 C  CB  . THR B 2 650  ? 137.443 67.650  140.815 1.00 135.05 ? 308  THR B CB  1 
ATOM   12530 O  OG1 . THR B 2 650  ? 137.421 69.078  140.939 1.00 124.11 ? 308  THR B OG1 1 
ATOM   12531 C  CG2 . THR B 2 650  ? 138.582 67.230  139.904 1.00 130.66 ? 308  THR B CG2 1 
ATOM   12532 N  N   . ILE B 2 651  ? 135.257 69.009  138.952 1.00 135.08 ? 309  ILE B N   1 
ATOM   12533 C  CA  . ILE B 2 651  ? 134.741 69.643  137.740 1.00 126.48 ? 309  ILE B CA  1 
ATOM   12534 C  C   . ILE B 2 651  ? 135.872 70.054  136.804 1.00 126.23 ? 309  ILE B C   1 
ATOM   12535 O  O   . ILE B 2 651  ? 135.785 69.852  135.586 1.00 124.96 ? 309  ILE B O   1 
ATOM   12536 C  CB  . ILE B 2 651  ? 133.855 70.844  138.112 1.00 112.99 ? 309  ILE B CB  1 
ATOM   12537 C  CG1 . ILE B 2 651  ? 132.548 70.364  138.745 1.00 118.19 ? 309  ILE B CG1 1 
ATOM   12538 C  CG2 . ILE B 2 651  ? 133.583 71.715  136.890 1.00 106.93 ? 309  ILE B CG2 1 
ATOM   12539 C  CD1 . ILE B 2 651  ? 131.697 71.479  139.290 1.00 117.38 ? 309  ILE B CD1 1 
ATOM   12540 N  N   . ASP B 2 652  ? 136.954 70.616  137.346 1.00 128.66 ? 310  ASP B N   1 
ATOM   12541 C  CA  . ASP B 2 652  ? 138.029 71.087  136.476 1.00 122.76 ? 310  ASP B CA  1 
ATOM   12542 C  C   . ASP B 2 652  ? 138.764 69.960  135.759 1.00 128.23 ? 310  ASP B C   1 
ATOM   12543 O  O   . ASP B 2 652  ? 139.688 70.246  134.991 1.00 122.36 ? 310  ASP B O   1 
ATOM   12544 C  CB  . ASP B 2 652  ? 139.024 71.942  137.269 1.00 123.01 ? 310  ASP B CB  1 
ATOM   12545 C  CG  . ASP B 2 652  ? 139.719 71.171  138.375 1.00 133.11 ? 310  ASP B CG  1 
ATOM   12546 O  OD1 . ASP B 2 652  ? 139.410 69.980  138.571 1.00 137.39 ? 310  ASP B OD1 1 
ATOM   12547 O  OD2 . ASP B 2 652  ? 140.590 71.761  139.049 1.00 131.04 ? 310  ASP B OD2 1 
ATOM   12548 N  N   . LYS B 2 653  ? 138.381 68.702  135.978 1.00 129.80 ? 311  LYS B N   1 
ATOM   12549 C  CA  . LYS B 2 653  ? 138.963 67.582  135.254 1.00 130.52 ? 311  LYS B CA  1 
ATOM   12550 C  C   . LYS B 2 653  ? 138.001 66.976  134.242 1.00 130.39 ? 311  LYS B C   1 
ATOM   12551 O  O   . LYS B 2 653  ? 138.350 65.987  133.591 1.00 131.12 ? 311  LYS B O   1 
ATOM   12552 C  CB  . LYS B 2 653  ? 139.419 66.494  136.235 1.00 124.91 ? 311  LYS B CB  1 
ATOM   12553 C  CG  . LYS B 2 653  ? 140.663 66.839  137.039 1.00 127.27 ? 311  LYS B CG  1 
ATOM   12554 C  CD  . LYS B 2 653  ? 141.863 67.115  136.155 1.00 134.75 ? 311  LYS B CD  1 
ATOM   12555 C  CE  . LYS B 2 653  ? 143.020 67.670  136.976 1.00 128.49 ? 311  LYS B CE  1 
ATOM   12556 N  NZ  . LYS B 2 653  ? 143.295 69.102  136.671 1.00 125.04 ? 311  LYS B NZ  1 
ATOM   12557 N  N   . GLY B 2 654  ? 136.807 67.542  134.086 1.00 122.12 ? 312  GLY B N   1 
ATOM   12558 C  CA  . GLY B 2 654  ? 135.875 67.120  133.061 1.00 111.86 ? 312  GLY B CA  1 
ATOM   12559 C  C   . GLY B 2 654  ? 134.675 66.313  133.518 1.00 128.34 ? 312  GLY B C   1 
ATOM   12560 O  O   . GLY B 2 654  ? 133.957 65.780  132.665 1.00 136.66 ? 312  GLY B O   1 
ATOM   12561 N  N   . TRP B 2 655  ? 134.428 66.202  134.823 1.00 141.29 ? 313  TRP B N   1 
ATOM   12562 C  CA  . TRP B 2 655  ? 133.289 65.451  135.341 1.00 141.08 ? 313  TRP B CA  1 
ATOM   12563 C  C   . TRP B 2 655  ? 132.179 66.434  135.696 1.00 130.54 ? 313  TRP B C   1 
ATOM   12564 O  O   . TRP B 2 655  ? 132.359 67.279  136.580 1.00 130.06 ? 313  TRP B O   1 
ATOM   12565 C  CB  . TRP B 2 655  ? 133.697 64.634  136.567 1.00 138.03 ? 313  TRP B CB  1 
ATOM   12566 C  CG  . TRP B 2 655  ? 134.851 63.715  136.309 1.00 142.93 ? 313  TRP B CG  1 
ATOM   12567 C  CD1 . TRP B 2 655  ? 136.155 63.931  136.645 1.00 143.47 ? 313  TRP B CD1 1 
ATOM   12568 C  CD2 . TRP B 2 655  ? 134.813 62.441  135.652 1.00 142.97 ? 313  TRP B CD2 1 
ATOM   12569 N  NE1 . TRP B 2 655  ? 136.930 62.872  136.243 1.00 147.44 ? 313  TRP B NE1 1 
ATOM   12570 C  CE2 . TRP B 2 655  ? 136.132 61.943  135.631 1.00 150.44 ? 313  TRP B CE2 1 
ATOM   12571 C  CE3 . TRP B 2 655  ? 133.794 61.671  135.083 1.00 145.67 ? 313  TRP B CE3 1 
ATOM   12572 C  CZ2 . TRP B 2 655  ? 136.457 60.712  135.064 1.00 153.33 ? 313  TRP B CZ2 1 
ATOM   12573 C  CZ3 . TRP B 2 655  ? 134.120 60.448  134.521 1.00 153.74 ? 313  TRP B CZ3 1 
ATOM   12574 C  CH2 . TRP B 2 655  ? 135.439 59.982  134.514 1.00 154.88 ? 313  TRP B CH2 1 
ATOM   12575 N  N   . VAL B 2 656  ? 131.035 66.320  135.021 1.00 126.58 ? 314  VAL B N   1 
ATOM   12576 C  CA  . VAL B 2 656  ? 129.979 67.318  135.186 1.00 122.57 ? 314  VAL B CA  1 
ATOM   12577 C  C   . VAL B 2 656  ? 129.146 67.050  136.436 1.00 125.74 ? 314  VAL B C   1 
ATOM   12578 O  O   . VAL B 2 656  ? 129.115 67.866  137.363 1.00 133.39 ? 314  VAL B O   1 
ATOM   12579 C  CB  . VAL B 2 656  ? 129.094 67.384  133.928 1.00 125.03 ? 314  VAL B CB  1 
ATOM   12580 C  CG1 . VAL B 2 656  ? 127.975 68.393  134.133 1.00 111.56 ? 314  VAL B CG1 1 
ATOM   12581 C  CG2 . VAL B 2 656  ? 129.930 67.769  132.719 1.00 121.00 ? 314  VAL B CG2 1 
ATOM   12582 N  N   . CYS B 2 657  ? 128.454 65.912  136.483 1.00 117.66 ? 315  CYS B N   1 
ATOM   12583 C  CA  . CYS B 2 657  ? 127.578 65.614  137.608 1.00 112.17 ? 315  CYS B CA  1 
ATOM   12584 C  C   . CYS B 2 657  ? 127.507 64.109  137.834 1.00 128.16 ? 315  CYS B C   1 
ATOM   12585 O  O   . CYS B 2 657  ? 128.040 63.314  137.057 1.00 137.51 ? 315  CYS B O   1 
ATOM   12586 C  CB  . CYS B 2 657  ? 126.176 66.192  137.389 1.00 113.31 ? 315  CYS B CB  1 
ATOM   12587 S  SG  . CYS B 2 657  ? 125.172 65.283  136.194 1.00 144.85 ? 315  CYS B SG  1 
ATOM   12588 N  N   . VAL B 2 658  ? 126.827 63.730  138.916 1.00 127.71 ? 316  VAL B N   1 
ATOM   12589 C  CA  . VAL B 2 658  ? 126.654 62.335  139.308 1.00 129.67 ? 316  VAL B CA  1 
ATOM   12590 C  C   . VAL B 2 658  ? 125.166 62.007  139.355 1.00 139.03 ? 316  VAL B C   1 
ATOM   12591 O  O   . VAL B 2 658  ? 124.402 62.650  140.088 1.00 138.40 ? 316  VAL B O   1 
ATOM   12592 C  CB  . VAL B 2 658  ? 127.324 62.037  140.659 1.00 129.27 ? 316  VAL B CB  1 
ATOM   12593 C  CG1 . VAL B 2 658  ? 126.738 60.776  141.281 1.00 144.75 ? 316  VAL B CG1 1 
ATOM   12594 C  CG2 . VAL B 2 658  ? 128.829 61.898  140.478 1.00 127.58 ? 316  VAL B CG2 1 
ATOM   12595 N  N   . TYR B 2 659  ? 124.758 61.013  138.568 1.00 149.71 ? 317  TYR B N   1 
ATOM   12596 C  CA  . TYR B 2 659  ? 123.389 60.510  138.555 1.00 156.62 ? 317  TYR B CA  1 
ATOM   12597 C  C   . TYR B 2 659  ? 123.277 59.326  139.505 1.00 170.09 ? 317  TYR B C   1 
ATOM   12598 O  O   . TYR B 2 659  ? 123.962 58.315  139.321 1.00 170.21 ? 317  TYR B O   1 
ATOM   12599 C  CB  . TYR B 2 659  ? 122.965 60.068  137.156 1.00 152.66 ? 317  TYR B CB  1 
ATOM   12600 C  CG  . TYR B 2 659  ? 122.629 61.176  136.195 1.00 152.30 ? 317  TYR B CG  1 
ATOM   12601 C  CD1 . TYR B 2 659  ? 121.431 61.866  136.305 1.00 156.38 ? 317  TYR B CD1 1 
ATOM   12602 C  CD2 . TYR B 2 659  ? 123.485 61.512  135.159 1.00 150.51 ? 317  TYR B CD2 1 
ATOM   12603 C  CE1 . TYR B 2 659  ? 121.104 62.874  135.424 1.00 154.85 ? 317  TYR B CE1 1 
ATOM   12604 C  CE2 . TYR B 2 659  ? 123.166 62.520  134.270 1.00 149.18 ? 317  TYR B CE2 1 
ATOM   12605 C  CZ  . TYR B 2 659  ? 121.973 63.198  134.408 1.00 154.15 ? 317  TYR B CZ  1 
ATOM   12606 O  OH  . TYR B 2 659  ? 121.648 64.203  133.527 1.00 151.94 ? 317  TYR B OH  1 
ATOM   12607 N  N   . SER B 2 660  ? 122.409 59.437  140.506 1.00 169.98 ? 318  SER B N   1 
ATOM   12608 C  CA  . SER B 2 660  ? 122.183 58.352  141.451 1.00 172.18 ? 318  SER B CA  1 
ATOM   12609 C  C   . SER B 2 660  ? 120.773 57.824  141.233 1.00 174.28 ? 318  SER B C   1 
ATOM   12610 O  O   . SER B 2 660  ? 119.794 58.559  141.399 1.00 171.29 ? 318  SER B O   1 
ATOM   12611 C  CB  . SER B 2 660  ? 122.367 58.821  142.892 1.00 165.73 ? 318  SER B CB  1 
ATOM   12612 O  OG  . SER B 2 660  ? 121.208 59.486  143.358 1.00 161.93 ? 318  SER B OG  1 
ATOM   12613 N  N   . SER B 2 661  ? 120.679 56.548  140.869 1.00 176.26 ? 319  SER B N   1 
ATOM   12614 C  CA  . SER B 2 661  ? 119.413 55.891  140.597 1.00 180.62 ? 319  SER B CA  1 
ATOM   12615 C  C   . SER B 2 661  ? 118.680 55.577  141.898 1.00 184.67 ? 319  SER B C   1 
ATOM   12616 O  O   . SER B 2 661  ? 119.182 55.802  143.003 1.00 181.30 ? 319  SER B O   1 
ATOM   12617 C  CB  . SER B 2 661  ? 119.641 54.618  139.787 1.00 177.16 ? 319  SER B CB  1 
ATOM   12618 O  OG  . SER B 2 661  ? 120.479 53.717  140.489 1.00 180.15 ? 319  SER B OG  1 
ATOM   12619 N  N   . GLU B 2 662  ? 117.463 55.050  141.757 1.00 181.74 ? 320  GLU B N   1 
ATOM   12620 C  CA  . GLU B 2 662  ? 116.652 54.708  142.916 1.00 181.83 ? 320  GLU B CA  1 
ATOM   12621 C  C   . GLU B 2 662  ? 117.252 53.553  143.704 1.00 176.86 ? 320  GLU B C   1 
ATOM   12622 O  O   . GLU B 2 662  ? 116.897 53.363  144.873 1.00 170.40 ? 320  GLU B O   1 
ATOM   12623 C  CB  . GLU B 2 662  ? 115.232 54.347  142.477 1.00 172.92 ? 320  GLU B CB  1 
ATOM   12624 C  CG  . GLU B 2 662  ? 114.187 54.473  143.572 1.00 173.57 ? 320  GLU B CG  1 
ATOM   12625 C  CD  . GLU B 2 662  ? 113.567 55.852  143.628 1.00 169.23 ? 320  GLU B CD  1 
ATOM   12626 O  OE1 . GLU B 2 662  ? 113.616 56.568  142.606 1.00 169.28 ? 320  GLU B OE1 1 
ATOM   12627 O  OE2 . GLU B 2 662  ? 113.033 56.219  144.694 1.00 164.99 ? 320  GLU B OE2 1 
ATOM   12628 N  N   . GLN B 2 663  ? 118.156 52.785  143.096 1.00 179.44 ? 321  GLN B N   1 
ATOM   12629 C  CA  . GLN B 2 663  ? 118.706 51.586  143.712 1.00 180.42 ? 321  GLN B CA  1 
ATOM   12630 C  C   . GLN B 2 663  ? 120.181 51.736  144.075 1.00 176.30 ? 321  GLN B C   1 
ATOM   12631 O  O   . GLN B 2 663  ? 120.890 50.732  144.193 1.00 171.89 ? 321  GLN B O   1 
ATOM   12632 C  CB  . GLN B 2 663  ? 118.509 50.398  142.773 1.00 175.59 ? 321  GLN B CB  1 
ATOM   12633 C  CG  . GLN B 2 663  ? 117.053 50.145  142.420 1.00 170.10 ? 321  GLN B CG  1 
ATOM   12634 C  CD  . GLN B 2 663  ? 116.838 48.806  141.753 1.00 175.89 ? 321  GLN B CD  1 
ATOM   12635 O  OE1 . GLN B 2 663  ? 117.788 48.066  141.498 1.00 173.20 ? 321  GLN B OE1 1 
ATOM   12636 N  NE2 . GLN B 2 663  ? 115.583 48.485  141.461 1.00 172.28 ? 321  GLN B NE2 1 
ATOM   12637 N  N   . GLY B 2 664  ? 120.660 52.967  144.248 1.00 176.46 ? 322  GLY B N   1 
ATOM   12638 C  CA  . GLY B 2 664  ? 122.014 53.191  144.707 1.00 175.63 ? 322  GLY B CA  1 
ATOM   12639 C  C   . GLY B 2 664  ? 123.089 53.141  143.644 1.00 177.60 ? 322  GLY B C   1 
ATOM   12640 O  O   . GLY B 2 664  ? 124.273 53.273  143.983 1.00 175.05 ? 322  GLY B O   1 
ATOM   12641 N  N   . GLU B 2 665  ? 122.729 52.961  142.377 1.00 181.00 ? 323  GLU B N   1 
ATOM   12642 C  CA  . GLU B 2 665  ? 123.713 52.963  141.302 1.00 185.90 ? 323  GLU B CA  1 
ATOM   12643 C  C   . GLU B 2 665  ? 124.023 54.383  140.850 1.00 182.75 ? 323  GLU B C   1 
ATOM   12644 O  O   . GLU B 2 665  ? 123.116 55.159  140.532 1.00 176.62 ? 323  GLU B O   1 
ATOM   12645 C  CB  . GLU B 2 665  ? 123.221 52.124  140.123 1.00 189.90 ? 323  GLU B CB  1 
ATOM   12646 C  CG  . GLU B 2 665  ? 123.128 50.646  140.443 1.00 185.64 ? 323  GLU B CG  1 
ATOM   12647 C  CD  . GLU B 2 665  ? 124.480 50.048  140.780 1.00 189.88 ? 323  GLU B CD  1 
ATOM   12648 O  OE1 . GLU B 2 665  ? 125.495 50.511  140.216 1.00 179.44 ? 323  GLU B OE1 1 
ATOM   12649 O  OE2 . GLU B 2 665  ? 124.531 49.124  141.618 1.00 190.04 ? 323  GLU B OE2 1 
ATOM   12650 N  N   . THR B 2 666  ? 125.311 54.721  140.829 1.00 178.00 ? 324  THR B N   1 
ATOM   12651 C  CA  . THR B 2 666  ? 125.767 56.071  140.533 1.00 171.94 ? 324  THR B CA  1 
ATOM   12652 C  C   . THR B 2 666  ? 126.599 56.069  139.258 1.00 166.49 ? 324  THR B C   1 
ATOM   12653 O  O   . THR B 2 666  ? 127.536 55.274  139.123 1.00 157.92 ? 324  THR B O   1 
ATOM   12654 C  CB  . THR B 2 666  ? 126.587 56.632  141.699 1.00 167.98 ? 324  THR B CB  1 
ATOM   12655 O  OG1 . THR B 2 666  ? 127.563 55.665  142.106 1.00 164.98 ? 324  THR B OG1 1 
ATOM   12656 C  CG2 . THR B 2 666  ? 125.681 56.945  142.882 1.00 166.75 ? 324  THR B CG2 1 
ATOM   12657 N  N   . ARG B 2 667  ? 126.254 56.962  138.332 1.00 165.07 ? 325  ARG B N   1 
ATOM   12658 C  CA  . ARG B 2 667  ? 127.004 57.191  137.103 1.00 158.08 ? 325  ARG B CA  1 
ATOM   12659 C  C   . ARG B 2 667  ? 127.483 58.635  137.041 1.00 149.49 ? 325  ARG B C   1 
ATOM   12660 O  O   . ARG B 2 667  ? 126.740 59.562  137.379 1.00 146.04 ? 325  ARG B O   1 
ATOM   12661 C  CB  . ARG B 2 667  ? 126.169 56.861  135.860 1.00 157.09 ? 325  ARG B CB  1 
ATOM   12662 C  CG  . ARG B 2 667  ? 125.882 55.382  135.682 1.00 156.92 ? 325  ARG B CG  1 
ATOM   12663 C  CD  . ARG B 2 667  ? 127.097 54.677  135.094 1.00 153.25 ? 325  ARG B CD  1 
ATOM   12664 N  NE  . ARG B 2 667  ? 126.866 53.254  134.869 1.00 163.12 ? 325  ARG B NE  1 
ATOM   12665 C  CZ  . ARG B 2 667  ? 127.272 52.292  135.690 1.00 172.81 ? 325  ARG B CZ  1 
ATOM   12666 N  NH1 . ARG B 2 667  ? 127.930 52.598  136.799 1.00 175.47 ? 325  ARG B NH1 1 
ATOM   12667 N  NH2 . ARG B 2 667  ? 127.018 51.023  135.403 1.00 166.91 ? 325  ARG B NH2 1 
ATOM   12668 N  N   . ALA B 2 668  ? 128.726 58.818  136.604 1.00 147.90 ? 326  ALA B N   1 
ATOM   12669 C  CA  . ALA B 2 668  ? 129.354 60.129  136.506 1.00 139.31 ? 326  ALA B CA  1 
ATOM   12670 C  C   . ALA B 2 668  ? 129.380 60.579  135.050 1.00 137.71 ? 326  ALA B C   1 
ATOM   12671 O  O   . ALA B 2 668  ? 129.792 59.817  134.169 1.00 144.42 ? 326  ALA B O   1 
ATOM   12672 C  CB  . ALA B 2 668  ? 130.772 60.098  137.076 1.00 140.18 ? 326  ALA B CB  1 
ATOM   12673 N  N   . LEU B 2 669  ? 128.938 61.811  134.800 1.00 129.11 ? 327  LEU B N   1 
ATOM   12674 C  CA  . LEU B 2 669  ? 128.924 62.362  133.451 1.00 120.66 ? 327  LEU B CA  1 
ATOM   12675 C  C   . LEU B 2 669  ? 130.260 63.027  133.133 1.00 127.89 ? 327  LEU B C   1 
ATOM   12676 O  O   . LEU B 2 669  ? 130.692 63.943  133.843 1.00 135.21 ? 327  LEU B O   1 
ATOM   12677 C  CB  . LEU B 2 669  ? 127.786 63.369  133.296 1.00 117.36 ? 327  LEU B CB  1 
ATOM   12678 C  CG  . LEU B 2 669  ? 127.716 64.048  131.927 1.00 114.45 ? 327  LEU B CG  1 
ATOM   12679 C  CD1 . LEU B 2 669  ? 127.657 63.013  130.814 1.00 133.89 ? 327  LEU B CD1 1 
ATOM   12680 C  CD2 . LEU B 2 669  ? 126.528 64.995  131.855 1.00 109.48 ? 327  LEU B CD2 1 
ATOM   12681 N  N   . LYS B 2 670  ? 130.900 62.565  132.063 1.00 137.20 ? 328  LYS B N   1 
ATOM   12682 C  CA  . LYS B 2 670  ? 132.202 63.044  131.625 1.00 133.05 ? 328  LYS B CA  1 
ATOM   12683 C  C   . LYS B 2 670  ? 132.073 63.742  130.277 1.00 133.04 ? 328  LYS B C   1 
ATOM   12684 O  O   . LYS B 2 670  ? 131.400 63.237  129.372 1.00 142.48 ? 328  LYS B O   1 
ATOM   12685 C  CB  . LYS B 2 670  ? 133.209 61.895  131.523 1.00 138.04 ? 328  LYS B CB  1 
ATOM   12686 C  CG  . LYS B 2 670  ? 134.505 62.279  130.833 1.00 140.77 ? 328  LYS B CG  1 
ATOM   12687 C  CD  . LYS B 2 670  ? 135.452 62.969  131.804 1.00 144.35 ? 328  LYS B CD  1 
ATOM   12688 C  CE  . LYS B 2 670  ? 136.755 63.355  131.129 1.00 131.82 ? 328  LYS B CE  1 
ATOM   12689 N  NZ  . LYS B 2 670  ? 137.523 62.159  130.692 1.00 137.06 ? 328  LYS B NZ  1 
ATOM   12690 N  N   . ILE B 2 671  ? 132.712 64.900  130.141 1.00 138.16 ? 329  ILE B N   1 
ATOM   12691 C  CA  . ILE B 2 671  ? 132.644 65.635  128.884 1.00 145.44 ? 329  ILE B CA  1 
ATOM   12692 C  C   . ILE B 2 671  ? 134.058 65.833  128.347 1.00 152.03 ? 329  ILE B C   1 
ATOM   12693 O  O   . ILE B 2 671  ? 135.039 65.702  129.079 1.00 152.80 ? 329  ILE B O   1 
ATOM   12694 C  CB  . ILE B 2 671  ? 131.927 66.985  129.047 1.00 142.68 ? 329  ILE B CB  1 
ATOM   12695 C  CG1 . ILE B 2 671  ? 131.452 67.496  127.686 1.00 132.43 ? 329  ILE B CG1 1 
ATOM   12696 C  CG2 . ILE B 2 671  ? 132.860 68.009  129.676 1.00 147.93 ? 329  ILE B CG2 1 
ATOM   12697 C  CD1 . ILE B 2 671  ? 130.440 68.614  127.770 1.00 124.82 ? 329  ILE B CD1 1 
ATOM   12698 O  OXT . ILE B 2 671  ? 134.258 66.119  127.166 1.00 148.34 ? 329  ILE B OXT 1 
ATOM   12699 N  N   . VAL C 2 452  ? 123.714 152.189 163.480 1.00 211.73 ? 110  VAL C N   1 
ATOM   12700 C  CA  . VAL C 2 452  ? 124.698 151.267 162.929 1.00 222.76 ? 110  VAL C CA  1 
ATOM   12701 C  C   . VAL C 2 452  ? 124.593 149.899 163.601 1.00 226.36 ? 110  VAL C C   1 
ATOM   12702 O  O   . VAL C 2 452  ? 124.615 148.870 162.923 1.00 221.70 ? 110  VAL C O   1 
ATOM   12703 C  CB  . VAL C 2 452  ? 126.126 151.836 163.059 1.00 214.73 ? 110  VAL C CB  1 
ATOM   12704 C  CG1 . VAL C 2 452  ? 127.162 150.753 162.789 1.00 199.26 ? 110  VAL C CG1 1 
ATOM   12705 C  CG2 . VAL C 2 452  ? 126.319 153.003 162.103 1.00 201.11 ? 110  VAL C CG2 1 
ATOM   12706 N  N   . LEU C 2 453  ? 124.484 149.887 164.934 1.00 226.15 ? 111  LEU C N   1 
ATOM   12707 C  CA  . LEU C 2 453  ? 124.364 148.617 165.645 1.00 228.85 ? 111  LEU C CA  1 
ATOM   12708 C  C   . LEU C 2 453  ? 123.089 147.892 165.251 1.00 225.79 ? 111  LEU C C   1 
ATOM   12709 O  O   . LEU C 2 453  ? 123.083 146.664 165.082 1.00 219.43 ? 111  LEU C O   1 
ATOM   12710 C  CB  . LEU C 2 453  ? 124.393 148.852 167.156 1.00 222.72 ? 111  LEU C CB  1 
ATOM   12711 C  CG  . LEU C 2 453  ? 125.754 148.967 167.850 1.00 215.90 ? 111  LEU C CG  1 
ATOM   12712 C  CD1 . LEU C 2 453  ? 126.542 147.674 167.692 1.00 206.32 ? 111  LEU C CD1 1 
ATOM   12713 C  CD2 . LEU C 2 453  ? 126.559 150.162 167.351 1.00 213.79 ? 111  LEU C CD2 1 
ATOM   12714 N  N   . LYS C 2 454  ? 121.994 148.635 165.111 1.00 222.47 ? 112  LYS C N   1 
ATOM   12715 C  CA  . LYS C 2 454  ? 120.773 148.031 164.600 1.00 219.00 ? 112  LYS C CA  1 
ATOM   12716 C  C   . LYS C 2 454  ? 120.967 147.466 163.188 1.00 216.17 ? 112  LYS C C   1 
ATOM   12717 O  O   . LYS C 2 454  ? 120.468 146.388 162.882 1.00 214.73 ? 112  LYS C O   1 
ATOM   12718 C  CB  . LYS C 2 454  ? 119.630 149.050 164.583 1.00 206.03 ? 112  LYS C CB  1 
ATOM   12719 C  CG  . LYS C 2 454  ? 119.434 149.857 165.854 1.00 198.57 ? 112  LYS C CG  1 
ATOM   12720 C  CD  . LYS C 2 454  ? 118.401 150.956 165.640 1.00 188.67 ? 112  LYS C CD  1 
ATOM   12721 C  CE  . LYS C 2 454  ? 118.343 151.912 166.819 1.00 179.02 ? 112  LYS C CE  1 
ATOM   12722 N  NZ  . LYS C 2 454  ? 117.377 153.020 166.570 1.00 163.96 ? 112  LYS C NZ  1 
ATOM   12723 N  N   . MET C 2 455  ? 121.693 148.168 162.322 1.00 216.25 ? 113  MET C N   1 
ATOM   12724 C  CA  . MET C 2 455  ? 122.042 147.636 161.018 1.00 217.97 ? 113  MET C CA  1 
ATOM   12725 C  C   . MET C 2 455  ? 122.879 146.348 161.163 1.00 218.08 ? 113  MET C C   1 
ATOM   12726 O  O   . MET C 2 455  ? 122.686 145.378 160.427 1.00 210.21 ? 113  MET C O   1 
ATOM   12727 C  CB  . MET C 2 455  ? 122.874 148.716 160.338 1.00 214.19 ? 113  MET C CB  1 
ATOM   12728 C  CG  . MET C 2 455  ? 121.999 149.942 159.988 1.00 211.66 ? 113  MET C CG  1 
ATOM   12729 S  SD  . MET C 2 455  ? 122.957 151.269 159.235 1.00 214.53 ? 113  MET C SD  1 
ATOM   12730 C  CE  . MET C 2 455  ? 121.670 152.480 159.065 1.00 186.89 ? 113  MET C CE  1 
ATOM   12731 N  N   . GLY C 2 456  ? 123.848 146.321 162.096 1.00 215.42 ? 114  GLY C N   1 
ATOM   12732 C  CA  . GLY C 2 456  ? 124.644 145.099 162.274 1.00 205.56 ? 114  GLY C CA  1 
ATOM   12733 C  C   . GLY C 2 456  ? 123.806 143.902 162.696 1.00 207.82 ? 114  GLY C C   1 
ATOM   12734 O  O   . GLY C 2 456  ? 123.936 142.804 162.140 1.00 199.97 ? 114  GLY C O   1 
ATOM   12735 N  N   . ARG C 2 457  ? 122.901 144.109 163.657 1.00 210.20 ? 115  ARG C N   1 
ATOM   12736 C  CA  . ARG C 2 457  ? 122.023 143.030 164.101 1.00 206.17 ? 115  ARG C CA  1 
ATOM   12737 C  C   . ARG C 2 457  ? 121.077 142.578 162.991 1.00 204.14 ? 115  ARG C C   1 
ATOM   12738 O  O   . ARG C 2 457  ? 120.877 141.370 162.788 1.00 198.62 ? 115  ARG C O   1 
ATOM   12739 C  CB  . ARG C 2 457  ? 121.241 143.483 165.334 1.00 199.62 ? 115  ARG C CB  1 
ATOM   12740 C  CG  . ARG C 2 457  ? 122.115 143.660 166.568 1.00 191.84 ? 115  ARG C CG  1 
ATOM   12741 C  CD  . ARG C 2 457  ? 121.306 144.028 167.800 1.00 193.31 ? 115  ARG C CD  1 
ATOM   12742 N  NE  . ARG C 2 457  ? 120.868 145.421 167.771 1.00 200.39 ? 115  ARG C NE  1 
ATOM   12743 C  CZ  . ARG C 2 457  ? 119.597 145.805 167.809 1.00 197.28 ? 115  ARG C CZ  1 
ATOM   12744 N  NH1 . ARG C 2 457  ? 118.631 144.901 167.879 1.00 192.15 ? 115  ARG C NH1 1 
ATOM   12745 N  NH2 . ARG C 2 457  ? 119.292 147.095 167.777 1.00 190.41 ? 115  ARG C NH2 1 
ATOM   12746 N  N   . THR C 2 458  ? 120.498 143.528 162.252 1.00 204.03 ? 116  THR C N   1 
ATOM   12747 C  CA  . THR C 2 458  ? 119.615 143.166 161.148 1.00 198.16 ? 116  THR C CA  1 
ATOM   12748 C  C   . THR C 2 458  ? 120.364 142.394 160.070 1.00 198.44 ? 116  THR C C   1 
ATOM   12749 O  O   . THR C 2 458  ? 119.832 141.432 159.508 1.00 188.28 ? 116  THR C O   1 
ATOM   12750 C  CB  . THR C 2 458  ? 118.955 144.412 160.560 1.00 190.15 ? 116  THR C CB  1 
ATOM   12751 O  OG1 . THR C 2 458  ? 119.935 145.442 160.394 1.00 199.73 ? 116  THR C OG1 1 
ATOM   12752 C  CG2 . THR C 2 458  ? 117.851 144.914 161.481 1.00 168.73 ? 116  THR C CG2 1 
ATOM   12753 N  N   . LEU C 2 459  ? 121.595 142.808 159.749 1.00 199.84 ? 117  LEU C N   1 
ATOM   12754 C  CA  . LEU C 2 459  ? 122.376 142.083 158.751 1.00 194.29 ? 117  LEU C CA  1 
ATOM   12755 C  C   . LEU C 2 459  ? 122.703 140.669 159.214 1.00 188.91 ? 117  LEU C C   1 
ATOM   12756 O  O   . LEU C 2 459  ? 122.643 139.717 158.422 1.00 181.76 ? 117  LEU C O   1 
ATOM   12757 C  CB  . LEU C 2 459  ? 123.670 142.842 158.454 1.00 185.65 ? 117  LEU C CB  1 
ATOM   12758 C  CG  . LEU C 2 459  ? 123.624 144.045 157.515 1.00 190.99 ? 117  LEU C CG  1 
ATOM   12759 C  CD1 . LEU C 2 459  ? 125.033 144.405 157.071 1.00 180.88 ? 117  LEU C CD1 1 
ATOM   12760 C  CD2 . LEU C 2 459  ? 122.743 143.743 156.318 1.00 189.65 ? 117  LEU C CD2 1 
ATOM   12761 N  N   . GLU C 2 460  ? 123.041 140.508 160.496 1.00 191.49 ? 118  GLU C N   1 
ATOM   12762 C  CA  . GLU C 2 460  ? 123.345 139.173 161.001 1.00 188.01 ? 118  GLU C CA  1 
ATOM   12763 C  C   . GLU C 2 460  ? 122.112 138.276 161.018 1.00 186.76 ? 118  GLU C C   1 
ATOM   12764 O  O   . GLU C 2 460  ? 122.235 137.056 160.867 1.00 178.52 ? 118  GLU C O   1 
ATOM   12765 C  CB  . GLU C 2 460  ? 123.975 139.264 162.390 1.00 185.39 ? 118  GLU C CB  1 
ATOM   12766 C  CG  . GLU C 2 460  ? 125.397 139.811 162.371 1.00 185.02 ? 118  GLU C CG  1 
ATOM   12767 C  CD  . GLU C 2 460  ? 126.346 138.965 161.536 1.00 182.01 ? 118  GLU C CD  1 
ATOM   12768 O  OE1 . GLU C 2 460  ? 126.127 137.740 161.428 1.00 179.50 ? 118  GLU C OE1 1 
ATOM   12769 O  OE2 . GLU C 2 460  ? 127.309 139.532 160.978 1.00 171.29 ? 118  GLU C OE2 1 
ATOM   12770 N  N   . ALA C 2 461  ? 120.921 138.857 161.191 1.00 189.10 ? 119  ALA C N   1 
ATOM   12771 C  CA  . ALA C 2 461  ? 119.697 138.064 161.068 1.00 181.79 ? 119  ALA C CA  1 
ATOM   12772 C  C   . ALA C 2 461  ? 119.394 137.718 159.610 1.00 184.62 ? 119  ALA C C   1 
ATOM   12773 O  O   . ALA C 2 461  ? 119.012 136.579 159.294 1.00 180.69 ? 119  ALA C O   1 
ATOM   12774 C  CB  . ALA C 2 461  ? 118.525 138.815 161.699 1.00 166.78 ? 119  ALA C CB  1 
ATOM   12775 N  N   . ILE C 2 462  ? 119.565 138.692 158.711 1.00 181.33 ? 120  ILE C N   1 
ATOM   12776 C  CA  . ILE C 2 462  ? 119.218 138.508 157.304 1.00 179.23 ? 120  ILE C CA  1 
ATOM   12777 C  C   . ILE C 2 462  ? 120.088 137.430 156.673 1.00 182.32 ? 120  ILE C C   1 
ATOM   12778 O  O   . ILE C 2 462  ? 119.595 136.577 155.920 1.00 175.12 ? 120  ILE C O   1 
ATOM   12779 C  CB  . ILE C 2 462  ? 119.335 139.847 156.549 1.00 173.32 ? 120  ILE C CB  1 
ATOM   12780 C  CG1 . ILE C 2 462  ? 118.152 140.758 156.888 1.00 169.37 ? 120  ILE C CG1 1 
ATOM   12781 C  CG2 . ILE C 2 462  ? 119.403 139.618 155.045 1.00 167.21 ? 120  ILE C CG2 1 
ATOM   12782 C  CD1 . ILE C 2 462  ? 118.228 142.124 156.240 1.00 166.91 ? 120  ILE C CD1 1 
ATOM   12783 N  N   . SER C 2 463  ? 121.397 137.459 156.948 1.00 176.61 ? 121  SER C N   1 
ATOM   12784 C  CA  . SER C 2 463  ? 122.293 136.472 156.349 1.00 161.46 ? 121  SER C CA  1 
ATOM   12785 C  C   . SER C 2 463  ? 121.940 135.061 156.804 1.00 162.69 ? 121  SER C C   1 
ATOM   12786 O  O   . SER C 2 463  ? 121.947 134.116 156.000 1.00 157.81 ? 121  SER C O   1 
ATOM   12787 C  CB  . SER C 2 463  ? 123.746 136.794 156.695 1.00 153.00 ? 121  SER C CB  1 
ATOM   12788 O  OG  . SER C 2 463  ? 123.932 136.858 158.096 1.00 169.92 ? 121  SER C OG  1 
ATOM   12789 N  N   . LYS C 2 464  ? 121.626 134.898 158.092 1.00 168.08 ? 122  LYS C N   1 
ATOM   12790 C  CA  . LYS C 2 464  ? 121.222 133.593 158.608 1.00 170.31 ? 122  LYS C CA  1 
ATOM   12791 C  C   . LYS C 2 464  ? 119.970 133.091 157.905 1.00 171.54 ? 122  LYS C C   1 
ATOM   12792 O  O   . LYS C 2 464  ? 119.909 131.936 157.461 1.00 168.34 ? 122  LYS C O   1 
ATOM   12793 C  CB  . LYS C 2 464  ? 121.001 133.674 160.118 1.00 160.72 ? 122  LYS C CB  1 
ATOM   12794 C  CG  . LYS C 2 464  ? 122.280 133.540 160.904 1.00 164.75 ? 122  LYS C CG  1 
ATOM   12795 C  CD  . LYS C 2 464  ? 122.032 133.491 162.393 1.00 166.96 ? 122  LYS C CD  1 
ATOM   12796 C  CE  . LYS C 2 464  ? 123.349 133.319 163.127 1.00 160.82 ? 122  LYS C CE  1 
ATOM   12797 N  NZ  . LYS C 2 464  ? 123.169 133.258 164.601 1.00 147.94 ? 122  LYS C NZ  1 
ATOM   12798 N  N   . GLY C 2 465  ? 118.957 133.955 157.790 1.00 166.32 ? 123  GLY C N   1 
ATOM   12799 C  CA  . GLY C 2 465  ? 117.726 133.553 157.124 1.00 156.18 ? 123  GLY C CA  1 
ATOM   12800 C  C   . GLY C 2 465  ? 117.957 133.153 155.682 1.00 157.39 ? 123  GLY C C   1 
ATOM   12801 O  O   . GLY C 2 465  ? 117.401 132.164 155.194 1.00 155.50 ? 123  GLY C O   1 
ATOM   12802 N  N   . MET C 2 466  ? 118.780 133.918 154.991 1.00 158.31 ? 124  MET C N   1 
ATOM   12803 C  CA  . MET C 2 466  ? 119.074 133.662 153.595 1.00 159.14 ? 124  MET C CA  1 
ATOM   12804 C  C   . MET C 2 466  ? 119.790 132.337 153.389 1.00 157.70 ? 124  MET C C   1 
ATOM   12805 O  O   . MET C 2 466  ? 119.440 131.561 152.483 1.00 145.20 ? 124  MET C O   1 
ATOM   12806 C  CB  . MET C 2 466  ? 119.954 134.795 153.151 1.00 163.02 ? 124  MET C CB  1 
ATOM   12807 C  CG  . MET C 2 466  ? 120.750 134.485 152.009 1.00 157.23 ? 124  MET C CG  1 
ATOM   12808 S  SD  . MET C 2 466  ? 121.780 135.911 152.137 1.00 179.25 ? 124  MET C SD  1 
ATOM   12809 C  CE  . MET C 2 466  ? 122.217 135.979 150.506 1.00 144.57 ? 124  MET C CE  1 
ATOM   12810 N  N   . SER C 2 467  ? 120.797 132.071 154.215 1.00 156.45 ? 125  SER C N   1 
ATOM   12811 C  CA  . SER C 2 467  ? 121.504 130.805 154.111 1.00 147.59 ? 125  SER C CA  1 
ATOM   12812 C  C   . SER C 2 467  ? 120.572 129.646 154.405 1.00 142.88 ? 125  SER C C   1 
ATOM   12813 O  O   . SER C 2 467  ? 120.631 128.606 153.734 1.00 142.38 ? 125  SER C O   1 
ATOM   12814 C  CB  . SER C 2 467  ? 122.698 130.787 155.065 1.00 149.64 ? 125  SER C CB  1 
ATOM   12815 O  OG  . SER C 2 467  ? 122.296 130.982 156.407 1.00 154.84 ? 125  SER C OG  1 
ATOM   12816 N  N   . GLU C 2 468  ? 119.682 129.815 155.390 1.00 142.16 ? 126  GLU C N   1 
ATOM   12817 C  CA  . GLU C 2 468  ? 118.717 128.758 155.695 1.00 141.89 ? 126  GLU C CA  1 
ATOM   12818 C  C   . GLU C 2 468  ? 117.788 128.476 154.514 1.00 133.17 ? 126  GLU C C   1 
ATOM   12819 O  O   . GLU C 2 468  ? 117.558 127.313 154.162 1.00 127.44 ? 126  GLU C O   1 
ATOM   12820 C  CB  . GLU C 2 468  ? 117.908 129.127 156.932 1.00 143.71 ? 126  GLU C CB  1 
ATOM   12821 C  CG  . GLU C 2 468  ? 116.948 128.044 157.367 1.00 148.50 ? 126  GLU C CG  1 
ATOM   12822 C  CD  . GLU C 2 468  ? 116.182 128.405 158.617 1.00 161.23 ? 126  GLU C CD  1 
ATOM   12823 O  OE1 . GLU C 2 468  ? 116.386 129.522 159.134 1.00 168.18 ? 126  GLU C OE1 1 
ATOM   12824 O  OE2 . GLU C 2 468  ? 115.367 127.579 159.076 1.00 152.60 ? 126  GLU C OE2 1 
ATOM   12825 N  N   . MET C 2 469  ? 117.273 129.533 153.878 1.00 133.08 ? 127  MET C N   1 
ATOM   12826 C  CA  . MET C 2 469  ? 116.380 129.339 152.737 1.00 117.87 ? 127  MET C CA  1 
ATOM   12827 C  C   . MET C 2 469  ? 117.086 128.641 151.580 1.00 119.08 ? 127  MET C C   1 
ATOM   12828 O  O   . MET C 2 469  ? 116.524 127.732 150.960 1.00 116.53 ? 127  MET C O   1 
ATOM   12829 C  CB  . MET C 2 469  ? 115.766 130.655 152.260 1.00 121.30 ? 127  MET C CB  1 
ATOM   12830 C  CG  . MET C 2 469  ? 114.797 131.351 153.216 1.00 140.42 ? 127  MET C CG  1 
ATOM   12831 S  SD  . MET C 2 469  ? 113.086 130.745 153.054 1.00 128.77 ? 127  MET C SD  1 
ATOM   12832 C  CE  . MET C 2 469  ? 113.069 129.257 154.040 1.00 117.35 ? 127  MET C CE  1 
ATOM   12833 N  N   . LEU C 2 470  ? 118.322 129.044 151.260 1.00 128.37 ? 128  LEU C N   1 
ATOM   12834 C  CA  . LEU C 2 470  ? 119.003 128.383 150.145 1.00 126.65 ? 128  LEU C CA  1 
ATOM   12835 C  C   . LEU C 2 470  ? 119.311 126.917 150.449 1.00 117.43 ? 128  LEU C C   1 
ATOM   12836 O  O   . LEU C 2 470  ? 119.087 126.034 149.599 1.00 112.25 ? 128  LEU C O   1 
ATOM   12837 C  CB  . LEU C 2 470  ? 120.286 129.133 149.786 1.00 116.49 ? 128  LEU C CB  1 
ATOM   12838 C  CG  . LEU C 2 470  ? 120.064 130.497 149.140 1.00 105.14 ? 128  LEU C CG  1 
ATOM   12839 C  CD1 . LEU C 2 470  ? 121.373 131.256 149.013 1.00 113.79 ? 128  LEU C CD1 1 
ATOM   12840 C  CD2 . LEU C 2 470  ? 119.394 130.325 147.781 1.00 98.15  ? 128  LEU C CD2 1 
ATOM   12841 N  N   . ALA C 2 471  ? 119.789 126.629 151.667 1.00 115.57 ? 129  ALA C N   1 
ATOM   12842 C  CA  . ALA C 2 471  ? 120.069 125.243 152.022 1.00 103.90 ? 129  ALA C CA  1 
ATOM   12843 C  C   . ALA C 2 471  ? 118.809 124.388 151.967 1.00 109.98 ? 129  ALA C C   1 
ATOM   12844 O  O   . ALA C 2 471  ? 118.842 123.250 151.479 1.00 110.34 ? 129  ALA C O   1 
ATOM   12845 C  CB  . ALA C 2 471  ? 120.705 125.176 153.410 1.00 106.61 ? 129  ALA C CB  1 
ATOM   12846 N  N   . LYS C 2 472  ? 117.681 124.913 152.457 1.00 112.22 ? 130  LYS C N   1 
ATOM   12847 C  CA  . LYS C 2 472  ? 116.432 124.164 152.352 1.00 100.16 ? 130  LYS C CA  1 
ATOM   12848 C  C   . LYS C 2 472  ? 115.975 123.997 150.910 1.00 95.43  ? 130  LYS C C   1 
ATOM   12849 O  O   . LYS C 2 472  ? 115.483 122.926 150.537 1.00 90.98  ? 130  LYS C O   1 
ATOM   12850 C  CB  . LYS C 2 472  ? 115.341 124.832 153.182 1.00 109.11 ? 130  LYS C CB  1 
ATOM   12851 C  CG  . LYS C 2 472  ? 115.585 124.747 154.667 1.00 120.40 ? 130  LYS C CG  1 
ATOM   12852 C  CD  . LYS C 2 472  ? 114.450 125.374 155.435 1.00 122.96 ? 130  LYS C CD  1 
ATOM   12853 C  CE  . LYS C 2 472  ? 114.725 125.332 156.918 1.00 132.16 ? 130  LYS C CE  1 
ATOM   12854 N  NZ  . LYS C 2 472  ? 114.711 123.929 157.413 1.00 128.53 ? 130  LYS C NZ  1 
ATOM   12855 N  N   . TYR C 2 473  ? 116.126 125.037 150.082 1.00 99.96  ? 131  TYR C N   1 
ATOM   12856 C  CA  . TYR C 2 473  ? 115.661 124.929 148.705 1.00 91.34  ? 131  TYR C CA  1 
ATOM   12857 C  C   . TYR C 2 473  ? 116.406 123.845 147.946 1.00 92.36  ? 131  TYR C C   1 
ATOM   12858 O  O   . TYR C 2 473  ? 115.839 123.227 147.038 1.00 92.18  ? 131  TYR C O   1 
ATOM   12859 C  CB  . TYR C 2 473  ? 115.789 126.263 147.970 1.00 90.32  ? 131  TYR C CB  1 
ATOM   12860 C  CG  . TYR C 2 473  ? 115.345 126.146 146.528 1.00 93.44  ? 131  TYR C CG  1 
ATOM   12861 C  CD1 . TYR C 2 473  ? 114.000 126.203 146.196 1.00 93.53  ? 131  TYR C CD1 1 
ATOM   12862 C  CD2 . TYR C 2 473  ? 116.264 125.962 145.502 1.00 105.35 ? 131  TYR C CD2 1 
ATOM   12863 C  CE1 . TYR C 2 473  ? 113.579 126.085 144.885 1.00 90.97  ? 131  TYR C CE1 1 
ATOM   12864 C  CE2 . TYR C 2 473  ? 115.851 125.841 144.185 1.00 90.62  ? 131  TYR C CE2 1 
ATOM   12865 C  CZ  . TYR C 2 473  ? 114.508 125.905 143.884 1.00 79.31  ? 131  TYR C CZ  1 
ATOM   12866 O  OH  . TYR C 2 473  ? 114.086 125.786 142.578 1.00 70.25  ? 131  TYR C OH  1 
ATOM   12867 N  N   . ASP C 2 474  ? 117.672 123.604 148.293 1.00 101.58 ? 132  ASP C N   1 
ATOM   12868 C  CA  . ASP C 2 474  ? 118.402 122.557 147.577 1.00 91.40  ? 132  ASP C CA  1 
ATOM   12869 C  C   . ASP C 2 474  ? 117.734 121.184 147.675 1.00 88.51  ? 132  ASP C C   1 
ATOM   12870 O  O   . ASP C 2 474  ? 117.942 120.351 146.786 1.00 84.70  ? 132  ASP C O   1 
ATOM   12871 C  CB  . ASP C 2 474  ? 119.851 122.467 148.054 1.00 106.50 ? 132  ASP C CB  1 
ATOM   12872 C  CG  . ASP C 2 474  ? 120.717 123.566 147.474 1.00 115.97 ? 132  ASP C CG  1 
ATOM   12873 O  OD1 . ASP C 2 474  ? 120.313 124.160 146.453 1.00 94.58  ? 132  ASP C OD1 1 
ATOM   12874 O  OD2 . ASP C 2 474  ? 121.810 123.818 148.022 1.00 130.83 ? 132  ASP C OD2 1 
ATOM   12875 N  N   . HIS C 2 475  ? 116.926 120.929 148.706 1.00 92.10  ? 133  HIS C N   1 
ATOM   12876 C  CA  . HIS C 2 475  ? 116.399 119.590 148.944 1.00 80.68  ? 133  HIS C CA  1 
ATOM   12877 C  C   . HIS C 2 475  ? 114.903 119.461 148.681 1.00 85.94  ? 133  HIS C C   1 
ATOM   12878 O  O   . HIS C 2 475  ? 114.360 118.362 148.834 1.00 80.07  ? 133  HIS C O   1 
ATOM   12879 C  CB  . HIS C 2 475  ? 116.671 119.161 150.392 1.00 87.50  ? 133  HIS C CB  1 
ATOM   12880 C  CG  . HIS C 2 475  ? 118.121 119.152 150.764 1.00 91.62  ? 133  HIS C CG  1 
ATOM   12881 N  ND1 . HIS C 2 475  ? 119.007 118.209 150.289 1.00 96.12  ? 133  HIS C ND1 1 
ATOM   12882 C  CD2 . HIS C 2 475  ? 118.832 119.956 151.589 1.00 94.23  ? 133  HIS C CD2 1 
ATOM   12883 C  CE1 . HIS C 2 475  ? 120.206 118.443 150.792 1.00 104.33 ? 133  HIS C CE1 1 
ATOM   12884 N  NE2 . HIS C 2 475  ? 120.126 119.496 151.585 1.00 101.31 ? 133  HIS C NE2 1 
ATOM   12885 N  N   . LEU C 2 476  ? 114.227 120.538 148.288 1.00 100.24 ? 134  LEU C N   1 
ATOM   12886 C  CA  . LEU C 2 476  ? 112.779 120.498 148.150 1.00 77.73  ? 134  LEU C CA  1 
ATOM   12887 C  C   . LEU C 2 476  ? 112.354 119.552 147.029 1.00 62.11  ? 134  LEU C C   1 
ATOM   12888 O  O   . LEU C 2 476  ? 113.111 119.260 146.100 1.00 83.87  ? 134  LEU C O   1 
ATOM   12889 C  CB  . LEU C 2 476  ? 112.230 121.897 147.877 1.00 69.52  ? 134  LEU C CB  1 
ATOM   12890 C  CG  . LEU C 2 476  ? 112.096 122.810 149.093 1.00 68.15  ? 134  LEU C CG  1 
ATOM   12891 C  CD1 . LEU C 2 476  ? 111.555 124.165 148.672 1.00 74.09  ? 134  LEU C CD1 1 
ATOM   12892 C  CD2 . LEU C 2 476  ? 111.197 122.163 150.138 1.00 94.48  ? 134  LEU C CD2 1 
ATOM   12893 N  N   . VAL C 2 477  ? 111.118 119.064 147.132 1.00 55.36  ? 135  VAL C N   1 
ATOM   12894 C  CA  . VAL C 2 477  ? 110.531 118.234 146.089 1.00 52.59  ? 135  VAL C CA  1 
ATOM   12895 C  C   . VAL C 2 477  ? 109.018 118.398 146.144 1.00 68.39  ? 135  VAL C C   1 
ATOM   12896 O  O   . VAL C 2 477  ? 108.438 118.605 147.214 1.00 82.72  ? 135  VAL C O   1 
ATOM   12897 C  CB  . VAL C 2 477  ? 110.960 116.754 146.240 1.00 55.06  ? 135  VAL C CB  1 
ATOM   12898 C  CG1 . VAL C 2 477  ? 110.311 116.109 147.466 1.00 87.22  ? 135  VAL C CG1 1 
ATOM   12899 C  CG2 . VAL C 2 477  ? 110.667 115.982 144.975 1.00 72.57  ? 135  VAL C CG2 1 
ATOM   12900 N  N   . ILE C 2 478  ? 108.372 118.314 144.978 1.00 66.01  ? 136  ILE C N   1 
ATOM   12901 C  CA  . ILE C 2 478  ? 106.933 118.517 144.891 1.00 64.95  ? 136  ILE C CA  1 
ATOM   12902 C  C   . ILE C 2 478  ? 106.307 117.365 144.118 1.00 63.79  ? 136  ILE C C   1 
ATOM   12903 O  O   . ILE C 2 478  ? 106.977 116.629 143.391 1.00 61.78  ? 136  ILE C O   1 
ATOM   12904 C  CB  . ILE C 2 478  ? 106.550 119.859 144.226 1.00 59.51  ? 136  ILE C CB  1 
ATOM   12905 C  CG1 . ILE C 2 478  ? 106.723 119.773 142.710 1.00 69.63  ? 136  ILE C CG1 1 
ATOM   12906 C  CG2 . ILE C 2 478  ? 107.383 121.004 144.795 1.00 62.69  ? 136  ILE C CG2 1 
ATOM   12907 C  CD1 . ILE C 2 478  ? 106.282 121.014 141.977 1.00 56.04  ? 136  ILE C CD1 1 
ATOM   12908 N  N   . SER C 2 479  ? 104.993 117.235 144.276 1.00 55.70  ? 137  SER C N   1 
ATOM   12909 C  CA  . SER C 2 479  ? 104.190 116.277 143.537 1.00 53.30  ? 137  SER C CA  1 
ATOM   12910 C  C   . SER C 2 479  ? 103.082 117.019 142.806 1.00 58.79  ? 137  SER C C   1 
ATOM   12911 O  O   . SER C 2 479  ? 102.604 118.063 143.261 1.00 78.22  ? 137  SER C O   1 
ATOM   12912 C  CB  . SER C 2 479  ? 103.574 115.219 144.456 1.00 58.79  ? 137  SER C CB  1 
ATOM   12913 O  OG  . SER C 2 479  ? 102.347 115.674 144.998 1.00 59.73  ? 137  SER C OG  1 
ATOM   12914 N  N   . THR C 2 480  ? 102.668 116.461 141.678 1.00 55.01  ? 138  THR C N   1 
ATOM   12915 C  CA  . THR C 2 480  ? 101.676 117.085 140.819 1.00 57.20  ? 138  THR C CA  1 
ATOM   12916 C  C   . THR C 2 480  ? 100.268 116.681 141.232 1.00 77.15  ? 138  THR C C   1 
ATOM   12917 O  O   . THR C 2 480  ? 100.053 115.696 141.942 1.00 76.51  ? 138  THR C O   1 
ATOM   12918 C  CB  . THR C 2 480  ? 101.901 116.698 139.357 1.00 63.34  ? 138  THR C CB  1 
ATOM   12919 O  OG1 . THR C 2 480  ? 101.512 115.333 139.160 1.00 67.51  ? 138  THR C OG1 1 
ATOM   12920 C  CG2 . THR C 2 480  ? 103.360 116.845 138.991 1.00 81.77  ? 138  THR C CG2 1 
ATOM   12921 N  N   . GLY C 2 481  ? 99.299  117.471 140.773 1.00 74.55  ? 139  GLY C N   1 
ATOM   12922 C  CA  . GLY C 2 481  ? 97.902  117.194 141.014 1.00 71.92  ? 139  GLY C CA  1 
ATOM   12923 C  C   . GLY C 2 481  ? 97.128  117.456 139.739 1.00 82.09  ? 139  GLY C C   1 
ATOM   12924 O  O   . GLY C 2 481  ? 97.698  117.855 138.722 1.00 91.04  ? 139  GLY C O   1 
ATOM   12925 N  N   . ARG C 2 482  ? 95.821  117.234 139.808 1.00 73.24  ? 140  ARG C N   1 
ATOM   12926 C  CA  . ARG C 2 482  ? 94.963  117.378 138.640 1.00 66.47  ? 140  ARG C CA  1 
ATOM   12927 C  C   . ARG C 2 482  ? 94.159  118.673 138.627 1.00 71.71  ? 140  ARG C C   1 
ATOM   12928 O  O   . ARG C 2 482  ? 93.341  118.869 137.723 1.00 72.65  ? 140  ARG C O   1 
ATOM   12929 C  CB  . ARG C 2 482  ? 94.021  116.179 138.558 1.00 62.45  ? 140  ARG C CB  1 
ATOM   12930 C  CG  . ARG C 2 482  ? 92.788  116.365 139.402 1.00 70.19  ? 140  ARG C CG  1 
ATOM   12931 C  CD  . ARG C 2 482  ? 91.766  115.288 139.172 1.00 79.66  ? 140  ARG C CD  1 
ATOM   12932 N  NE  . ARG C 2 482  ? 90.608  115.523 140.022 1.00 81.69  ? 140  ARG C NE  1 
ATOM   12933 C  CZ  . ARG C 2 482  ? 89.889  114.564 140.589 1.00 92.60  ? 140  ARG C CZ  1 
ATOM   12934 N  NH1 . ARG C 2 482  ? 90.209  113.292 140.395 1.00 97.49  ? 140  ARG C NH1 1 
ATOM   12935 N  NH2 . ARG C 2 482  ? 88.849  114.878 141.349 1.00 97.35  ? 140  ARG C NH2 1 
ATOM   12936 N  N   . THR C 2 483  ? 94.390  119.575 139.579 1.00 81.65  ? 141  THR C N   1 
ATOM   12937 C  CA  . THR C 2 483  ? 93.643  120.823 139.654 1.00 70.51  ? 141  THR C CA  1 
ATOM   12938 C  C   . THR C 2 483  ? 94.413  122.029 139.129 1.00 75.58  ? 141  THR C C   1 
ATOM   12939 O  O   . THR C 2 483  ? 93.930  123.156 139.262 1.00 87.71  ? 141  THR C O   1 
ATOM   12940 C  CB  . THR C 2 483  ? 93.215  121.094 141.098 1.00 67.01  ? 141  THR C CB  1 
ATOM   12941 O  OG1 . THR C 2 483  ? 94.361  121.465 141.872 1.00 71.24  ? 141  THR C OG1 1 
ATOM   12942 C  CG2 . THR C 2 483  ? 92.585  119.850 141.711 1.00 73.30  ? 141  THR C CG2 1 
ATOM   12943 N  N   . THR C 2 484  ? 95.587  121.831 138.529 1.00 69.75  ? 142  THR C N   1 
ATOM   12944 C  CA  . THR C 2 484  ? 96.417  122.979 138.174 1.00 62.28  ? 142  THR C CA  1 
ATOM   12945 C  C   . THR C 2 484  ? 95.937  123.650 136.888 1.00 76.39  ? 142  THR C C   1 
ATOM   12946 O  O   . THR C 2 484  ? 95.591  124.839 136.883 1.00 91.33  ? 142  THR C O   1 
ATOM   12947 C  CB  . THR C 2 484  ? 97.880  122.550 138.045 1.00 72.44  ? 142  THR C CB  1 
ATOM   12948 O  OG1 . THR C 2 484  ? 98.237  121.718 139.157 1.00 78.71  ? 142  THR C OG1 1 
ATOM   12949 C  CG2 . THR C 2 484  ? 98.787  123.770 138.034 1.00 76.32  ? 142  THR C CG2 1 
ATOM   12950 N  N   . ALA C 2 485  ? 95.899  122.896 135.791 1.00 67.73  ? 143  ALA C N   1 
ATOM   12951 C  CA  . ALA C 2 485  ? 95.503  123.480 134.513 1.00 65.50  ? 143  ALA C CA  1 
ATOM   12952 C  C   . ALA C 2 485  ? 94.057  123.969 134.488 1.00 75.88  ? 143  ALA C C   1 
ATOM   12953 O  O   . ALA C 2 485  ? 93.821  125.065 133.947 1.00 76.98  ? 143  ALA C O   1 
ATOM   12954 C  CB  . ALA C 2 485  ? 95.773  122.475 133.383 1.00 56.82  ? 143  ALA C CB  1 
ATOM   12955 N  N   . PRO C 2 486  ? 93.060  123.234 135.004 1.00 68.96  ? 144  PRO C N   1 
ATOM   12956 C  CA  . PRO C 2 486  ? 91.710  123.820 135.082 1.00 63.56  ? 144  PRO C CA  1 
ATOM   12957 C  C   . PRO C 2 486  ? 91.638  125.100 135.902 1.00 74.37  ? 144  PRO C C   1 
ATOM   12958 O  O   . PRO C 2 486  ? 90.902  126.022 135.527 1.00 97.09  ? 144  PRO C O   1 
ATOM   12959 C  CB  . PRO C 2 486  ? 90.884  122.693 135.714 1.00 65.51  ? 144  PRO C CB  1 
ATOM   12960 C  CG  . PRO C 2 486  ? 91.569  121.453 135.270 1.00 72.59  ? 144  PRO C CG  1 
ATOM   12961 C  CD  . PRO C 2 486  ? 93.035  121.794 135.329 1.00 73.28  ? 144  PRO C CD  1 
ATOM   12962 N  N   . ALA C 2 487  ? 92.373  125.186 137.014 1.00 61.20  ? 145  ALA C N   1 
ATOM   12963 C  CA  . ALA C 2 487  ? 92.362  126.420 137.796 1.00 59.89  ? 145  ALA C CA  1 
ATOM   12964 C  C   . ALA C 2 487  ? 92.951  127.575 137.001 1.00 74.48  ? 145  ALA C C   1 
ATOM   12965 O  O   . ALA C 2 487  ? 92.418  128.696 137.021 1.00 89.14  ? 145  ALA C O   1 
ATOM   12966 C  CB  . ALA C 2 487  ? 93.122  126.220 139.108 1.00 77.54  ? 145  ALA C CB  1 
ATOM   12967 N  N   . ALA C 2 488  ? 94.042  127.314 136.274 1.00 74.48  ? 146  ALA C N   1 
ATOM   12968 C  CA  . ALA C 2 488  ? 94.618  128.352 135.426 1.00 67.28  ? 146  ALA C CA  1 
ATOM   12969 C  C   . ALA C 2 488  ? 93.624  128.803 134.360 1.00 86.54  ? 146  ALA C C   1 
ATOM   12970 O  O   . ALA C 2 488  ? 93.476  130.006 134.108 1.00 92.62  ? 146  ALA C O   1 
ATOM   12971 C  CB  . ALA C 2 488  ? 95.910  127.851 134.784 1.00 79.28  ? 146  ALA C CB  1 
ATOM   12972 N  N   . ALA C 2 489  ? 92.927  127.851 133.733 1.00 83.81  ? 147  ALA C N   1 
ATOM   12973 C  CA  . ALA C 2 489  ? 91.966  128.203 132.689 1.00 74.91  ? 147  ALA C CA  1 
ATOM   12974 C  C   . ALA C 2 489  ? 90.815  129.031 133.251 1.00 80.29  ? 147  ALA C C   1 
ATOM   12975 O  O   . ALA C 2 489  ? 90.386  130.017 132.635 1.00 96.45  ? 147  ALA C O   1 
ATOM   12976 C  CB  . ALA C 2 489  ? 91.436  126.937 132.015 1.00 51.40  ? 147  ALA C CB  1 
ATOM   12977 N  N   . PHE C 2 490  ? 90.308  128.644 134.424 1.00 89.64  ? 148  PHE C N   1 
ATOM   12978 C  CA  . PHE C 2 490  ? 89.236  129.393 135.069 1.00 78.82  ? 148  PHE C CA  1 
ATOM   12979 C  C   . PHE C 2 490  ? 89.653  130.830 135.361 1.00 79.19  ? 148  PHE C C   1 
ATOM   12980 O  O   . PHE C 2 490  ? 88.927  131.782 135.036 1.00 92.96  ? 148  PHE C O   1 
ATOM   12981 C  CB  . PHE C 2 490  ? 88.823  128.677 136.358 1.00 83.97  ? 148  PHE C CB  1 
ATOM   12982 C  CG  . PHE C 2 490  ? 87.511  129.139 136.921 1.00 90.58  ? 148  PHE C CG  1 
ATOM   12983 C  CD1 . PHE C 2 490  ? 87.472  130.152 137.866 1.00 97.91  ? 148  PHE C CD1 1 
ATOM   12984 C  CD2 . PHE C 2 490  ? 86.319  128.571 136.507 1.00 95.16  ? 148  PHE C CD2 1 
ATOM   12985 C  CE1 . PHE C 2 490  ? 86.270  130.582 138.395 1.00 99.78  ? 148  PHE C CE1 1 
ATOM   12986 C  CE2 . PHE C 2 490  ? 85.112  129.003 137.027 1.00 99.22  ? 148  PHE C CE2 1 
ATOM   12987 C  CZ  . PHE C 2 490  ? 85.088  130.011 137.971 1.00 104.00 ? 148  PHE C CZ  1 
ATOM   12988 N  N   . ASP C 2 491  ? 90.829  131.006 135.973 1.00 69.02  ? 149  ASP C N   1 
ATOM   12989 C  CA  . ASP C 2 491  ? 91.291  132.358 136.273 1.00 69.96  ? 149  ASP C CA  1 
ATOM   12990 C  C   . ASP C 2 491  ? 91.513  133.174 135.007 1.00 72.18  ? 149  ASP C C   1 
ATOM   12991 O  O   . ASP C 2 491  ? 91.192  134.366 134.971 1.00 84.81  ? 149  ASP C O   1 
ATOM   12992 C  CB  . ASP C 2 491  ? 92.563  132.313 137.119 1.00 96.12  ? 149  ASP C CB  1 
ATOM   12993 C  CG  . ASP C 2 491  ? 92.396  131.478 138.371 1.00 111.04 ? 149  ASP C CG  1 
ATOM   12994 O  OD1 . ASP C 2 491  ? 91.242  131.298 138.814 1.00 106.58 ? 149  ASP C OD1 1 
ATOM   12995 O  OD2 . ASP C 2 491  ? 93.418  131.017 138.922 1.00 103.73 ? 149  ASP C OD2 1 
ATOM   12996 N  N   . ALA C 2 492  ? 92.059  132.554 133.958 1.00 70.18  ? 150  ALA C N   1 
ATOM   12997 C  CA  . ALA C 2 492  ? 92.270  133.287 132.714 1.00 71.33  ? 150  ALA C CA  1 
ATOM   12998 C  C   . ALA C 2 492  ? 90.948  133.752 132.118 1.00 80.56  ? 150  ALA C C   1 
ATOM   12999 O  O   . ALA C 2 492  ? 90.837  134.887 131.634 1.00 86.90  ? 150  ALA C O   1 
ATOM   13000 C  CB  . ALA C 2 492  ? 93.037  132.419 131.717 1.00 69.23  ? 150  ALA C CB  1 
ATOM   13001 N  N   . TYR C 2 493  ? 89.923  132.895 132.164 1.00 87.04  ? 151  TYR C N   1 
ATOM   13002 C  CA  . TYR C 2 493  ? 88.626  133.281 131.613 1.00 74.03  ? 151  TYR C CA  1 
ATOM   13003 C  C   . TYR C 2 493  ? 87.982  134.414 132.413 1.00 76.94  ? 151  TYR C C   1 
ATOM   13004 O  O   . TYR C 2 493  ? 87.442  135.359 131.822 1.00 90.79  ? 151  TYR C O   1 
ATOM   13005 C  CB  . TYR C 2 493  ? 87.693  132.075 131.534 1.00 74.18  ? 151  TYR C CB  1 
ATOM   13006 C  CG  . TYR C 2 493  ? 86.586  132.284 130.526 1.00 84.37  ? 151  TYR C CG  1 
ATOM   13007 C  CD1 . TYR C 2 493  ? 85.395  132.899 130.881 1.00 101.59 ? 151  TYR C CD1 1 
ATOM   13008 C  CD2 . TYR C 2 493  ? 86.738  131.864 129.210 1.00 81.84  ? 151  TYR C CD2 1 
ATOM   13009 C  CE1 . TYR C 2 493  ? 84.387  133.096 129.951 1.00 96.18  ? 151  TYR C CE1 1 
ATOM   13010 C  CE2 . TYR C 2 493  ? 85.735  132.052 128.276 1.00 81.80  ? 151  TYR C CE2 1 
ATOM   13011 C  CZ  . TYR C 2 493  ? 84.563  132.668 128.652 1.00 85.46  ? 151  TYR C CZ  1 
ATOM   13012 O  OH  . TYR C 2 493  ? 83.563  132.858 127.725 1.00 95.45  ? 151  TYR C OH  1 
ATOM   13013 N  N   . LEU C 2 494  ? 88.024  134.347 133.754 1.00 82.19  ? 152  LEU C N   1 
ATOM   13014 C  CA  . LEU C 2 494  ? 87.504  135.469 134.547 1.00 87.70  ? 152  LEU C CA  1 
ATOM   13015 C  C   . LEU C 2 494  ? 88.297  136.742 134.282 1.00 92.72  ? 152  LEU C C   1 
ATOM   13016 O  O   . LEU C 2 494  ? 87.722  137.838 134.241 1.00 101.25 ? 152  LEU C O   1 
ATOM   13017 C  CB  . LEU C 2 494  ? 87.450  135.136 136.037 1.00 78.95  ? 152  LEU C CB  1 
ATOM   13018 C  CG  . LEU C 2 494  ? 86.205  134.341 136.446 1.00 99.61  ? 152  LEU C CG  1 
ATOM   13019 C  CD1 . LEU C 2 494  ? 86.223  132.908 135.961 1.00 108.35 ? 152  LEU C CD1 1 
ATOM   13020 C  CD2 . LEU C 2 494  ? 86.036  134.415 137.957 1.00 107.35 ? 152  LEU C CD2 1 
ATOM   13021 N  N   . ASN C 2 495  ? 89.618  136.624 134.101 1.00 89.14  ? 153  ASN C N   1 
ATOM   13022 C  CA  . ASN C 2 495  ? 90.416  137.804 133.785 1.00 89.23  ? 153  ASN C CA  1 
ATOM   13023 C  C   . ASN C 2 495  ? 89.997  138.420 132.476 1.00 93.68  ? 153  ASN C C   1 
ATOM   13024 O  O   . ASN C 2 495  ? 89.881  139.646 132.363 1.00 101.95 ? 153  ASN C O   1 
ATOM   13025 C  CB  . ASN C 2 495  ? 91.896  137.416 133.660 1.00 95.19  ? 153  ASN C CB  1 
ATOM   13026 C  CG  . ASN C 2 495  ? 92.826  138.626 133.458 1.00 110.50 ? 153  ASN C CG  1 
ATOM   13027 O  OD1 . ASN C 2 495  ? 92.584  139.456 132.575 1.00 116.91 ? 153  ASN C OD1 1 
ATOM   13028 N  ND2 . ASN C 2 495  ? 93.863  138.743 134.283 1.00 120.37 ? 153  ASN C ND2 1 
ATOM   13029 N  N   . GLU C 2 496  ? 89.690  137.588 131.500 1.00 94.32  ? 154  GLU C N   1 
ATOM   13030 C  CA  . GLU C 2 496  ? 89.361  138.158 130.211 1.00 100.64 ? 154  GLU C CA  1 
ATOM   13031 C  C   . GLU C 2 496  ? 87.949  138.727 130.162 1.00 95.17  ? 154  GLU C C   1 
ATOM   13032 O  O   . GLU C 2 496  ? 87.745  139.823 129.625 1.00 100.98 ? 154  GLU C O   1 
ATOM   13033 C  CB  . GLU C 2 496  ? 89.580  137.127 129.116 1.00 101.51 ? 154  GLU C CB  1 
ATOM   13034 C  CG  . GLU C 2 496  ? 89.423  137.751 127.768 1.00 118.70 ? 154  GLU C CG  1 
ATOM   13035 C  CD  . GLU C 2 496  ? 90.390  138.911 127.590 1.00 133.02 ? 154  GLU C CD  1 
ATOM   13036 O  OE1 . GLU C 2 496  ? 89.918  140.049 127.390 1.00 129.37 ? 154  GLU C OE1 1 
ATOM   13037 O  OE2 . GLU C 2 496  ? 91.617  138.690 127.673 1.00 129.88 ? 154  GLU C OE2 1 
ATOM   13038 N  N   . HIS C 2 497  ? 86.968  138.024 130.730 1.00 95.69  ? 155  HIS C N   1 
ATOM   13039 C  CA  . HIS C 2 497  ? 85.581  138.419 130.545 1.00 98.71  ? 155  HIS C CA  1 
ATOM   13040 C  C   . HIS C 2 497  ? 84.860  138.864 131.806 1.00 100.61 ? 155  HIS C C   1 
ATOM   13041 O  O   . HIS C 2 497  ? 83.854  139.574 131.692 1.00 99.10  ? 155  HIS C O   1 
ATOM   13042 C  CB  . HIS C 2 497  ? 84.778  137.257 129.935 1.00 96.88  ? 155  HIS C CB  1 
ATOM   13043 C  CG  . HIS C 2 497  ? 85.296  136.788 128.610 1.00 95.80  ? 155  HIS C CG  1 
ATOM   13044 N  ND1 . HIS C 2 497  ? 85.071  137.472 127.435 1.00 104.73 ? 155  HIS C ND1 1 
ATOM   13045 C  CD2 . HIS C 2 497  ? 86.011  135.687 128.273 1.00 91.26  ? 155  HIS C CD2 1 
ATOM   13046 C  CE1 . HIS C 2 497  ? 85.635  136.819 126.434 1.00 95.88  ? 155  HIS C CE1 1 
ATOM   13047 N  NE2 . HIS C 2 497  ? 86.210  135.733 126.915 1.00 84.78  ? 155  HIS C NE2 1 
ATOM   13048 N  N   . GLY C 2 498  ? 85.324  138.483 132.992 1.00 105.99 ? 156  GLY C N   1 
ATOM   13049 C  CA  . GLY C 2 498  ? 84.625  138.872 134.195 1.00 106.95 ? 156  GLY C CA  1 
ATOM   13050 C  C   . GLY C 2 498  ? 83.519  137.936 134.631 1.00 107.96 ? 156  GLY C C   1 
ATOM   13051 O  O   . GLY C 2 498  ? 82.891  138.191 135.667 1.00 115.23 ? 156  GLY C O   1 
ATOM   13052 N  N   . VAL C 2 499  ? 83.255  136.867 133.886 1.00 102.55 ? 157  VAL C N   1 
ATOM   13053 C  CA  . VAL C 2 499  ? 82.223  135.909 134.273 1.00 107.33 ? 157  VAL C CA  1 
ATOM   13054 C  C   . VAL C 2 499  ? 82.768  134.496 134.123 1.00 110.49 ? 157  VAL C C   1 
ATOM   13055 O  O   . VAL C 2 499  ? 83.708  134.250 133.347 1.00 111.38 ? 157  VAL C O   1 
ATOM   13056 C  CB  . VAL C 2 499  ? 80.933  136.097 133.434 1.00 110.81 ? 157  VAL C CB  1 
ATOM   13057 C  CG1 . VAL C 2 499  ? 80.266  137.428 133.764 1.00 110.71 ? 157  VAL C CG1 1 
ATOM   13058 C  CG2 . VAL C 2 499  ? 81.243  136.005 131.946 1.00 103.14 ? 157  VAL C CG2 1 
ATOM   13059 N  N   . PRO C 2 500  ? 82.197  133.536 134.850 1.00 104.51 ? 158  PRO C N   1 
ATOM   13060 C  CA  . PRO C 2 500  ? 82.656  132.163 134.765 1.00 96.27  ? 158  PRO C CA  1 
ATOM   13061 C  C   . PRO C 2 500  ? 82.323  131.548 133.323 1.00 103.60 ? 158  PRO C C   1 
ATOM   13062 O  O   . PRO C 2 500  ? 81.367  131.986 132.730 1.00 108.50 ? 158  PRO C O   1 
ATOM   13063 C  CB  . PRO C 2 500  ? 81.880  131.426 135.851 1.00 102.66 ? 158  PRO C CB  1 
ATOM   13064 C  CG  . PRO C 2 500  ? 80.680  132.271 136.093 1.00 112.40 ? 158  PRO C CG  1 
ATOM   13065 C  CD  . PRO C 2 500  ? 81.132  133.682 135.866 1.00 109.43 ? 158  PRO C CD  1 
ATOM   13066 N  N   . PRO C 2 501  ? 83.150  130.615 132.928 1.00 93.88  ? 159  PRO C N   1 
ATOM   13067 C  CA  . PRO C 2 501  ? 82.904  130.039 131.589 1.00 85.17  ? 159  PRO C CA  1 
ATOM   13068 C  C   . PRO C 2 501  ? 81.555  129.282 131.561 1.00 105.43 ? 159  PRO C C   1 
ATOM   13069 O  O   . PRO C 2 501  ? 81.080  128.831 132.603 1.00 116.33 ? 159  PRO C O   1 
ATOM   13070 C  CB  . PRO C 2 501  ? 84.083  129.070 131.409 1.00 77.57  ? 159  PRO C CB  1 
ATOM   13071 C  CG  . PRO C 2 501  ? 84.560  128.782 132.792 1.00 87.12  ? 159  PRO C CG  1 
ATOM   13072 C  CD  . PRO C 2 501  ? 84.326  130.043 133.561 1.00 100.97 ? 159  PRO C CD  1 
ATOM   13073 N  N   . PRO C 2 502  ? 80.958  129.191 130.379 1.00 101.30 ? 160  PRO C N   1 
ATOM   13074 C  CA  . PRO C 2 502  ? 79.652  128.509 130.287 1.00 107.35 ? 160  PRO C CA  1 
ATOM   13075 C  C   . PRO C 2 502  ? 79.778  127.047 130.690 1.00 113.24 ? 160  PRO C C   1 
ATOM   13076 O  O   . PRO C 2 502  ? 80.812  126.410 130.474 1.00 108.81 ? 160  PRO C O   1 
ATOM   13077 C  CB  . PRO C 2 502  ? 79.282  128.652 128.803 1.00 109.69 ? 160  PRO C CB  1 
ATOM   13078 C  CG  . PRO C 2 502  ? 80.169  129.745 128.275 1.00 108.31 ? 160  PRO C CG  1 
ATOM   13079 C  CD  . PRO C 2 502  ? 81.430  129.652 129.070 1.00 89.51  ? 160  PRO C CD  1 
ATOM   13080 N  N   . GLN C 2 503  ? 78.697  126.517 131.280 1.00 113.05 ? 161  GLN C N   1 
ATOM   13081 C  CA  . GLN C 2 503  ? 78.674  125.143 131.777 1.00 108.91 ? 161  GLN C CA  1 
ATOM   13082 C  C   . GLN C 2 503  ? 79.841  124.907 132.737 1.00 106.63 ? 161  GLN C C   1 
ATOM   13083 O  O   . GLN C 2 503  ? 80.663  124.004 132.532 1.00 112.36 ? 161  GLN C O   1 
ATOM   13084 C  CB  . GLN C 2 503  ? 78.682  124.151 130.615 1.00 108.22 ? 161  GLN C CB  1 
ATOM   13085 C  CG  . GLN C 2 503  ? 77.376  124.175 129.834 1.00 111.48 ? 161  GLN C CG  1 
ATOM   13086 C  CD  . GLN C 2 503  ? 77.111  122.892 129.083 1.00 119.57 ? 161  GLN C CD  1 
ATOM   13087 O  OE1 . GLN C 2 503  ? 77.921  121.967 129.110 1.00 113.36 ? 161  GLN C OE1 1 
ATOM   13088 N  NE2 . GLN C 2 503  ? 75.969  122.826 128.409 1.00 112.13 ? 161  GLN C NE2 1 
ATOM   13089 N  N   . PRO C 2 504  ? 79.924  125.707 133.807 1.00 104.44 ? 162  PRO C N   1 
ATOM   13090 C  CA  . PRO C 2 504  ? 81.035  125.629 134.764 1.00 107.16 ? 162  PRO C CA  1 
ATOM   13091 C  C   . PRO C 2 504  ? 80.924  124.494 135.770 1.00 112.62 ? 162  PRO C C   1 
ATOM   13092 O  O   . PRO C 2 504  ? 81.768  124.407 136.668 1.00 121.05 ? 162  PRO C O   1 
ATOM   13093 C  CB  . PRO C 2 504  ? 80.958  126.983 135.477 1.00 111.36 ? 162  PRO C CB  1 
ATOM   13094 C  CG  . PRO C 2 504  ? 79.502  127.289 135.492 1.00 114.36 ? 162  PRO C CG  1 
ATOM   13095 C  CD  . PRO C 2 504  ? 78.904  126.679 134.249 1.00 103.81 ? 162  PRO C CD  1 
ATOM   13096 N  N   . ALA C 2 505  ? 79.912  123.633 135.644 1.00 117.86 ? 163  ALA C N   1 
ATOM   13097 C  CA  . ALA C 2 505  ? 79.719  122.538 136.592 1.00 121.42 ? 163  ALA C CA  1 
ATOM   13098 C  C   . ALA C 2 505  ? 80.943  121.631 136.672 1.00 119.72 ? 163  ALA C C   1 
ATOM   13099 O  O   . ALA C 2 505  ? 81.258  121.114 137.750 1.00 127.65 ? 163  ALA C O   1 
ATOM   13100 C  CB  . ALA C 2 505  ? 78.479  121.730 136.209 1.00 125.13 ? 163  ALA C CB  1 
ATOM   13101 N  N   . ILE C 2 506  ? 81.631  121.393 135.552 1.00 109.82 ? 164  ILE C N   1 
ATOM   13102 C  CA  . ILE C 2 506  ? 82.822  120.543 135.602 1.00 110.13 ? 164  ILE C CA  1 
ATOM   13103 C  C   . ILE C 2 506  ? 83.865  121.155 136.538 1.00 114.22 ? 164  ILE C C   1 
ATOM   13104 O  O   . ILE C 2 506  ? 84.541  120.442 137.294 1.00 125.75 ? 164  ILE C O   1 
ATOM   13105 C  CB  . ILE C 2 506  ? 83.391  120.298 134.190 1.00 107.74 ? 164  ILE C CB  1 
ATOM   13106 C  CG1 . ILE C 2 506  ? 84.604  119.369 134.272 1.00 95.92  ? 164  ILE C CG1 1 
ATOM   13107 C  CG2 . ILE C 2 506  ? 83.767  121.608 133.503 1.00 109.95 ? 164  ILE C CG2 1 
ATOM   13108 C  CD1 . ILE C 2 506  ? 85.162  118.960 132.931 1.00 105.00 ? 164  ILE C CD1 1 
ATOM   13109 N  N   . PHE C 2 507  ? 84.010  122.484 136.508 1.00 111.16 ? 165  PHE C N   1 
ATOM   13110 C  CA  . PHE C 2 507  ? 84.956  123.142 137.403 1.00 107.38 ? 165  PHE C CA  1 
ATOM   13111 C  C   . PHE C 2 507  ? 84.548  122.954 138.858 1.00 112.97 ? 165  PHE C C   1 
ATOM   13112 O  O   . PHE C 2 507  ? 85.411  122.828 139.735 1.00 117.32 ? 165  PHE C O   1 
ATOM   13113 C  CB  . PHE C 2 507  ? 85.060  124.631 137.066 1.00 114.47 ? 165  PHE C CB  1 
ATOM   13114 C  CG  . PHE C 2 507  ? 85.628  124.907 135.701 1.00 111.49 ? 165  PHE C CG  1 
ATOM   13115 C  CD1 . PHE C 2 507  ? 86.993  124.845 135.480 1.00 97.12  ? 165  PHE C CD1 1 
ATOM   13116 C  CD2 . PHE C 2 507  ? 84.795  125.210 134.637 1.00 112.08 ? 165  PHE C CD2 1 
ATOM   13117 C  CE1 . PHE C 2 507  ? 87.520  125.094 134.225 1.00 86.62  ? 165  PHE C CE1 1 
ATOM   13118 C  CE2 . PHE C 2 507  ? 85.315  125.456 133.379 1.00 91.93  ? 165  PHE C CE2 1 
ATOM   13119 C  CZ  . PHE C 2 507  ? 86.679  125.399 133.174 1.00 81.21  ? 165  PHE C CZ  1 
ATOM   13120 N  N   . LYS C 2 508  ? 83.240  122.932 139.133 1.00 116.00 ? 166  LYS C N   1 
ATOM   13121 C  CA  . LYS C 2 508  ? 82.767  122.571 140.468 1.00 113.56 ? 166  LYS C CA  1 
ATOM   13122 C  C   . LYS C 2 508  ? 83.131  121.133 140.813 1.00 119.78 ? 166  LYS C C   1 
ATOM   13123 O  O   . LYS C 2 508  ? 83.482  120.836 141.961 1.00 124.64 ? 166  LYS C O   1 
ATOM   13124 C  CB  . LYS C 2 508  ? 81.256  122.775 140.590 1.00 124.23 ? 166  LYS C CB  1 
ATOM   13125 C  CG  . LYS C 2 508  ? 80.803  124.201 140.884 1.00 139.79 ? 166  LYS C CG  1 
ATOM   13126 C  CD  . LYS C 2 508  ? 80.937  125.133 139.700 1.00 147.94 ? 166  LYS C CD  1 
ATOM   13127 C  CE  . LYS C 2 508  ? 80.387  126.505 140.048 1.00 141.92 ? 166  LYS C CE  1 
ATOM   13128 N  NZ  . LYS C 2 508  ? 80.606  127.494 138.961 1.00 130.82 ? 166  LYS C NZ  1 
ATOM   13129 N  N   . ASP C 2 509  ? 83.046  120.222 139.838 1.00 125.26 ? 167  ASP C N   1 
ATOM   13130 C  CA  . ASP C 2 509  ? 83.427  118.839 140.107 1.00 122.77 ? 167  ASP C CA  1 
ATOM   13131 C  C   . ASP C 2 509  ? 84.893  118.746 140.499 1.00 123.55 ? 167  ASP C C   1 
ATOM   13132 O  O   . ASP C 2 509  ? 85.254  117.986 141.405 1.00 119.02 ? 167  ASP C O   1 
ATOM   13133 C  CB  . ASP C 2 509  ? 83.163  117.959 138.884 1.00 110.30 ? 167  ASP C CB  1 
ATOM   13134 C  CG  . ASP C 2 509  ? 81.690  117.773 138.603 1.00 135.72 ? 167  ASP C CG  1 
ATOM   13135 O  OD1 . ASP C 2 509  ? 80.892  117.815 139.560 1.00 146.11 ? 167  ASP C OD1 1 
ATOM   13136 O  OD2 . ASP C 2 509  ? 81.335  117.573 137.422 1.00 131.74 ? 167  ASP C OD2 1 
ATOM   13137 N  N   . LEU C 2 510  ? 85.755  119.513 139.836 1.00 121.87 ? 168  LEU C N   1 
ATOM   13138 C  CA  . LEU C 2 510  ? 87.157  119.477 140.226 1.00 106.50 ? 168  LEU C CA  1 
ATOM   13139 C  C   . LEU C 2 510  ? 87.437  120.268 141.496 1.00 111.56 ? 168  LEU C C   1 
ATOM   13140 O  O   . LEU C 2 510  ? 88.552  120.186 142.022 1.00 109.14 ? 168  LEU C O   1 
ATOM   13141 C  CB  . LEU C 2 510  ? 88.044  119.990 139.091 1.00 102.23 ? 168  LEU C CB  1 
ATOM   13142 C  CG  . LEU C 2 510  ? 88.191  118.986 137.950 1.00 100.10 ? 168  LEU C CG  1 
ATOM   13143 C  CD1 . LEU C 2 510  ? 88.706  119.660 136.692 1.00 102.69 ? 168  LEU C CD1 1 
ATOM   13144 C  CD2 . LEU C 2 510  ? 89.113  117.860 138.384 1.00 99.94  ? 168  LEU C CD2 1 
ATOM   13145 N  N   . GLY C 2 511  ? 86.463  121.017 142.008 1.00 118.88 ? 169  GLY C N   1 
ATOM   13146 C  CA  . GLY C 2 511  ? 86.697  121.797 143.205 1.00 119.13 ? 169  GLY C CA  1 
ATOM   13147 C  C   . GLY C 2 511  ? 87.497  123.050 142.949 1.00 114.70 ? 169  GLY C C   1 
ATOM   13148 O  O   . GLY C 2 511  ? 88.241  123.494 143.830 1.00 115.47 ? 169  GLY C O   1 
ATOM   13149 N  N   . VAL C 2 512  ? 87.370  123.635 141.759 1.00 115.42 ? 170  VAL C N   1 
ATOM   13150 C  CA  . VAL C 2 512  ? 88.193  124.759 141.339 1.00 108.01 ? 170  VAL C CA  1 
ATOM   13151 C  C   . VAL C 2 512  ? 87.402  126.061 141.285 1.00 110.42 ? 170  VAL C C   1 
ATOM   13152 O  O   . VAL C 2 512  ? 87.920  127.115 141.661 1.00 107.71 ? 170  VAL C O   1 
ATOM   13153 C  CB  . VAL C 2 512  ? 88.852  124.456 139.974 1.00 101.40 ? 170  VAL C CB  1 
ATOM   13154 C  CG1 . VAL C 2 512  ? 89.274  125.738 139.279 1.00 103.36 ? 170  VAL C CG1 1 
ATOM   13155 C  CG2 . VAL C 2 512  ? 90.044  123.523 140.152 1.00 107.56 ? 170  VAL C CG2 1 
ATOM   13156 N  N   . ALA C 2 513  ? 86.139  126.010 140.865 1.00 117.61 ? 171  ALA C N   1 
ATOM   13157 C  CA  . ALA C 2 513  ? 85.381  127.235 140.636 1.00 116.33 ? 171  ALA C CA  1 
ATOM   13158 C  C   . ALA C 2 513  ? 85.029  127.921 141.947 1.00 120.90 ? 171  ALA C C   1 
ATOM   13159 O  O   . ALA C 2 513  ? 83.970  127.669 142.531 1.00 122.81 ? 171  ALA C O   1 
ATOM   13160 C  CB  . ALA C 2 513  ? 84.112  126.936 139.837 1.00 123.25 ? 171  ALA C CB  1 
ATOM   13161 N  N   . GLN C 2 514  ? 85.919  128.794 142.409 1.00 132.34 ? 172  GLN C N   1 
ATOM   13162 C  CA  . GLN C 2 514  ? 85.734  129.515 143.660 1.00 144.20 ? 172  GLN C CA  1 
ATOM   13163 C  C   . GLN C 2 514  ? 86.684  130.707 143.745 1.00 132.17 ? 172  GLN C C   1 
ATOM   13164 O  O   . GLN C 2 514  ? 86.935  131.387 142.749 1.00 119.98 ? 172  GLN C O   1 
ATOM   13165 C  CB  . GLN C 2 514  ? 85.945  128.580 144.852 1.00 151.32 ? 172  GLN C CB  1 
ATOM   13166 C  CG  . GLN C 2 514  ? 87.396  128.203 145.092 1.00 144.87 ? 172  GLN C CG  1 
ATOM   13167 C  CD  . GLN C 2 514  ? 88.010  128.977 146.236 1.00 156.43 ? 172  GLN C CD  1 
ATOM   13168 O  OE1 . GLN C 2 514  ? 87.334  129.306 147.211 1.00 157.48 ? 172  GLN C OE1 1 
ATOM   13169 N  NE2 . GLN C 2 514  ? 89.298  129.280 146.123 1.00 156.97 ? 172  GLN C NE2 1 
ATOM   13170 N  N   . ILE D 2 449  ? 121.124 161.095 147.388 1.00 214.73 ? 107  ILE D N   1 
ATOM   13171 C  CA  . ILE D 2 449  ? 121.304 161.364 148.811 1.00 225.42 ? 107  ILE D CA  1 
ATOM   13172 C  C   . ILE D 2 449  ? 120.177 160.731 149.622 1.00 230.36 ? 107  ILE D C   1 
ATOM   13173 O  O   . ILE D 2 449  ? 120.377 160.309 150.765 1.00 221.98 ? 107  ILE D O   1 
ATOM   13174 C  CB  . ILE D 2 449  ? 121.390 162.873 149.072 1.00 226.16 ? 107  ILE D CB  1 
ATOM   13175 C  CG1 . ILE D 2 449  ? 120.090 163.563 148.646 1.00 219.02 ? 107  ILE D CG1 1 
ATOM   13176 C  CG2 . ILE D 2 449  ? 122.576 163.475 148.335 1.00 217.59 ? 107  ILE D CG2 1 
ATOM   13177 C  CD1 . ILE D 2 449  ? 120.047 165.043 148.945 1.00 196.12 ? 107  ILE D CD1 1 
ATOM   13178 N  N   . THR D 2 450  ? 118.997 160.653 149.000 1.00 232.02 ? 108  THR D N   1 
ATOM   13179 C  CA  . THR D 2 450  ? 117.843 159.962 149.558 1.00 228.11 ? 108  THR D CA  1 
ATOM   13180 C  C   . THR D 2 450  ? 118.083 158.458 149.683 1.00 230.42 ? 108  THR D C   1 
ATOM   13181 O  O   . THR D 2 450  ? 117.464 157.828 150.550 1.00 218.15 ? 108  THR D O   1 
ATOM   13182 C  CB  . THR D 2 450  ? 116.593 160.201 148.711 1.00 211.70 ? 108  THR D CB  1 
ATOM   13183 O  OG1 . THR D 2 450  ? 116.929 160.097 147.323 1.00 209.74 ? 108  THR D OG1 1 
ATOM   13184 C  CG2 . THR D 2 450  ? 116.021 161.571 148.997 1.00 198.98 ? 108  THR D CG2 1 
ATOM   13185 N  N   . PRO D 2 451  ? 118.933 157.822 148.858 1.00 233.01 ? 109  PRO D N   1 
ATOM   13186 C  CA  . PRO D 2 451  ? 119.150 156.378 149.066 1.00 230.12 ? 109  PRO D CA  1 
ATOM   13187 C  C   . PRO D 2 451  ? 119.641 156.041 150.475 1.00 225.37 ? 109  PRO D C   1 
ATOM   13188 O  O   . PRO D 2 451  ? 119.332 154.961 150.990 1.00 218.62 ? 109  PRO D O   1 
ATOM   13189 C  CB  . PRO D 2 451  ? 120.192 156.034 147.993 1.00 222.60 ? 109  PRO D CB  1 
ATOM   13190 C  CG  . PRO D 2 451  ? 119.858 156.959 146.869 1.00 218.20 ? 109  PRO D CG  1 
ATOM   13191 C  CD  . PRO D 2 451  ? 119.475 158.244 147.543 1.00 226.03 ? 109  PRO D CD  1 
ATOM   13192 N  N   . VAL D 2 452  ? 120.343 156.939 151.156 1.00 224.83 ? 110  VAL D N   1 
ATOM   13193 C  CA  . VAL D 2 452  ? 120.879 156.588 152.472 1.00 227.59 ? 110  VAL D CA  1 
ATOM   13194 C  C   . VAL D 2 452  ? 119.752 156.436 153.493 1.00 223.83 ? 110  VAL D C   1 
ATOM   13195 O  O   . VAL D 2 452  ? 119.652 155.430 154.229 1.00 213.46 ? 110  VAL D O   1 
ATOM   13196 C  CB  . VAL D 2 452  ? 121.913 157.635 152.913 1.00 218.82 ? 110  VAL D CB  1 
ATOM   13197 C  CG1 . VAL D 2 452  ? 122.306 157.415 154.368 1.00 210.08 ? 110  VAL D CG1 1 
ATOM   13198 C  CG2 . VAL D 2 452  ? 123.159 157.562 152.023 1.00 207.13 ? 110  VAL D CG2 1 
ATOM   13199 N  N   . LEU D 2 453  ? 118.855 157.417 153.537 1.00 221.80 ? 111  LEU D N   1 
ATOM   13200 C  CA  . LEU D 2 453  ? 117.730 157.265 154.441 1.00 222.21 ? 111  LEU D CA  1 
ATOM   13201 C  C   . LEU D 2 453  ? 116.865 156.092 154.031 1.00 214.85 ? 111  LEU D C   1 
ATOM   13202 O  O   . LEU D 2 453  ? 116.406 155.329 154.890 1.00 205.57 ? 111  LEU D O   1 
ATOM   13203 C  CB  . LEU D 2 453  ? 116.922 158.559 154.506 1.00 218.78 ? 111  LEU D CB  1 
ATOM   13204 C  CG  . LEU D 2 453  ? 117.640 159.607 155.349 1.00 209.67 ? 111  LEU D CG  1 
ATOM   13205 C  CD1 . LEU D 2 453  ? 116.930 160.916 155.217 1.00 199.93 ? 111  LEU D CD1 1 
ATOM   13206 C  CD2 . LEU D 2 453  ? 117.723 159.180 156.809 1.00 202.56 ? 111  LEU D CD2 1 
ATOM   13207 N  N   . LYS D 2 454  ? 116.663 155.914 152.730 1.00 214.18 ? 112  LYS D N   1 
ATOM   13208 C  CA  . LYS D 2 454  ? 115.858 154.794 152.273 1.00 210.30 ? 112  LYS D CA  1 
ATOM   13209 C  C   . LYS D 2 454  ? 116.447 153.396 152.494 1.00 210.69 ? 112  LYS D C   1 
ATOM   13210 O  O   . LYS D 2 454  ? 115.671 152.459 152.707 1.00 205.72 ? 112  LYS D O   1 
ATOM   13211 C  CB  . LYS D 2 454  ? 115.564 154.964 150.789 1.00 211.72 ? 112  LYS D CB  1 
ATOM   13212 C  CG  . LYS D 2 454  ? 114.677 156.153 150.465 1.00 206.82 ? 112  LYS D CG  1 
ATOM   13213 C  CD  . LYS D 2 454  ? 114.474 156.342 148.962 1.00 198.94 ? 112  LYS D CD  1 
ATOM   13214 C  CE  . LYS D 2 454  ? 113.329 157.314 148.675 1.00 190.03 ? 112  LYS D CE  1 
ATOM   13215 N  NZ  . LYS D 2 454  ? 113.731 158.740 148.881 1.00 188.67 ? 112  LYS D NZ  1 
ATOM   13216 N  N   . MET D 2 455  ? 117.772 153.179 152.508 1.00 211.93 ? 113  MET D N   1 
ATOM   13217 C  CA  . MET D 2 455  ? 118.178 151.833 152.946 1.00 208.43 ? 113  MET D CA  1 
ATOM   13218 C  C   . MET D 2 455  ? 117.902 151.670 154.418 1.00 205.42 ? 113  MET D C   1 
ATOM   13219 O  O   . MET D 2 455  ? 117.398 150.633 154.856 1.00 191.19 ? 113  MET D O   1 
ATOM   13220 C  CB  . MET D 2 455  ? 119.637 151.363 152.713 1.00 203.74 ? 113  MET D CB  1 
ATOM   13221 C  CG  . MET D 2 455  ? 120.733 151.879 153.595 1.00 199.59 ? 113  MET D CG  1 
ATOM   13222 S  SD  . MET D 2 455  ? 121.288 153.483 153.197 1.00 213.81 ? 113  MET D SD  1 
ATOM   13223 C  CE  . MET D 2 455  ? 122.188 153.296 151.680 1.00 201.47 ? 113  MET D CE  1 
ATOM   13224 N  N   . GLY D 2 456  ? 118.318 152.676 155.210 1.00 204.40 ? 114  GLY D N   1 
ATOM   13225 C  CA  . GLY D 2 456  ? 118.068 152.589 156.627 1.00 194.81 ? 114  GLY D CA  1 
ATOM   13226 C  C   . GLY D 2 456  ? 116.624 152.269 156.947 1.00 194.03 ? 114  GLY D C   1 
ATOM   13227 O  O   . GLY D 2 456  ? 116.342 151.573 157.928 1.00 181.04 ? 114  GLY D O   1 
ATOM   13228 N  N   . ARG D 2 457  ? 115.691 152.762 156.134 1.00 200.25 ? 115  ARG D N   1 
ATOM   13229 C  CA  . ARG D 2 457  ? 114.284 152.397 156.295 1.00 201.75 ? 115  ARG D CA  1 
ATOM   13230 C  C   . ARG D 2 457  ? 113.978 150.995 155.765 1.00 197.19 ? 115  ARG D C   1 
ATOM   13231 O  O   . ARG D 2 457  ? 113.271 150.222 156.421 1.00 183.29 ? 115  ARG D O   1 
ATOM   13232 C  CB  . ARG D 2 457  ? 113.376 153.430 155.630 1.00 192.32 ? 115  ARG D CB  1 
ATOM   13233 C  CG  . ARG D 2 457  ? 113.190 154.672 156.467 1.00 193.34 ? 115  ARG D CG  1 
ATOM   13234 C  CD  . ARG D 2 457  ? 112.655 154.251 157.832 1.00 191.24 ? 115  ARG D CD  1 
ATOM   13235 N  NE  . ARG D 2 457  ? 112.573 155.353 158.782 1.00 185.58 ? 115  ARG D NE  1 
ATOM   13236 C  CZ  . ARG D 2 457  ? 111.505 156.132 158.926 1.00 181.44 ? 115  ARG D CZ  1 
ATOM   13237 N  NH1 . ARG D 2 457  ? 110.432 155.932 158.175 1.00 179.64 ? 115  ARG D NH1 1 
ATOM   13238 N  NH2 . ARG D 2 457  ? 111.514 157.113 159.819 1.00 178.61 ? 115  ARG D NH2 1 
ATOM   13239 N  N   . THR D 2 458  ? 114.502 150.651 154.582 1.00 199.22 ? 116  THR D N   1 
ATOM   13240 C  CA  . THR D 2 458  ? 114.064 149.464 153.850 1.00 193.76 ? 116  THR D CA  1 
ATOM   13241 C  C   . THR D 2 458  ? 114.652 148.162 154.382 1.00 186.67 ? 116  THR D C   1 
ATOM   13242 O  O   . THR D 2 458  ? 114.061 147.102 154.160 1.00 174.98 ? 116  THR D O   1 
ATOM   13243 C  CB  . THR D 2 458  ? 114.404 149.598 152.365 1.00 189.55 ? 116  THR D CB  1 
ATOM   13244 O  OG1 . THR D 2 458  ? 115.730 150.116 152.217 1.00 187.39 ? 116  THR D OG1 1 
ATOM   13245 C  CG2 . THR D 2 458  ? 113.416 150.526 151.668 1.00 180.89 ? 116  THR D CG2 1 
ATOM   13246 N  N   . LEU D 2 459  ? 115.821 148.195 155.023 1.00 184.78 ? 117  LEU D N   1 
ATOM   13247 C  CA  . LEU D 2 459  ? 116.305 146.981 155.677 1.00 178.83 ? 117  LEU D CA  1 
ATOM   13248 C  C   . LEU D 2 459  ? 115.337 146.461 156.736 1.00 181.86 ? 117  LEU D C   1 
ATOM   13249 O  O   . LEU D 2 459  ? 115.207 145.243 156.900 1.00 178.69 ? 117  LEU D O   1 
ATOM   13250 C  CB  . LEU D 2 459  ? 117.696 147.196 156.279 1.00 172.57 ? 117  LEU D CB  1 
ATOM   13251 C  CG  . LEU D 2 459  ? 118.905 147.094 155.337 1.00 175.67 ? 117  LEU D CG  1 
ATOM   13252 C  CD1 . LEU D 2 459  ? 119.034 148.233 154.352 1.00 174.71 ? 117  LEU D CD1 1 
ATOM   13253 C  CD2 . LEU D 2 459  ? 120.181 146.960 156.156 1.00 175.63 ? 117  LEU D CD2 1 
ATOM   13254 N  N   . GLU D 2 460  ? 114.628 147.343 157.444 1.00 180.81 ? 118  GLU D N   1 
ATOM   13255 C  CA  . GLU D 2 460  ? 113.624 146.859 158.390 1.00 184.31 ? 118  GLU D CA  1 
ATOM   13256 C  C   . GLU D 2 460  ? 112.477 146.153 157.668 1.00 184.84 ? 118  GLU D C   1 
ATOM   13257 O  O   . GLU D 2 460  ? 112.003 145.100 158.116 1.00 174.63 ? 118  GLU D O   1 
ATOM   13258 C  CB  . GLU D 2 460  ? 113.095 148.013 159.239 1.00 184.66 ? 118  GLU D CB  1 
ATOM   13259 C  CG  . GLU D 2 460  ? 112.119 147.577 160.315 1.00 188.64 ? 118  GLU D CG  1 
ATOM   13260 C  CD  . GLU D 2 460  ? 111.560 148.745 161.098 1.00 189.97 ? 118  GLU D CD  1 
ATOM   13261 O  OE1 . GLU D 2 460  ? 111.942 149.895 160.799 1.00 187.31 ? 118  GLU D OE1 1 
ATOM   13262 O  OE2 . GLU D 2 460  ? 110.741 148.512 162.012 1.00 182.61 ? 118  GLU D OE2 1 
ATOM   13263 N  N   . ALA D 2 461  ? 112.025 146.713 156.544 1.00 179.83 ? 119  ALA D N   1 
ATOM   13264 C  CA  . ALA D 2 461  ? 110.965 146.080 155.764 1.00 171.61 ? 119  ALA D CA  1 
ATOM   13265 C  C   . ALA D 2 461  ? 111.422 144.733 155.214 1.00 172.19 ? 119  ALA D C   1 
ATOM   13266 O  O   . ALA D 2 461  ? 110.650 143.763 155.182 1.00 167.03 ? 119  ALA D O   1 
ATOM   13267 C  CB  . ALA D 2 461  ? 110.521 147.006 154.632 1.00 152.27 ? 119  ALA D CB  1 
ATOM   13268 N  N   . ILE D 2 462  ? 112.676 144.667 154.763 1.00 170.97 ? 120  ILE D N   1 
ATOM   13269 C  CA  . ILE D 2 462  ? 113.235 143.419 154.258 1.00 170.31 ? 120  ILE D CA  1 
ATOM   13270 C  C   . ILE D 2 462  ? 113.300 142.382 155.368 1.00 172.65 ? 120  ILE D C   1 
ATOM   13271 O  O   . ILE D 2 462  ? 112.996 141.202 155.156 1.00 166.21 ? 120  ILE D O   1 
ATOM   13272 C  CB  . ILE D 2 462  ? 114.628 143.681 153.651 1.00 168.84 ? 120  ILE D CB  1 
ATOM   13273 C  CG1 . ILE D 2 462  ? 114.510 144.499 152.364 1.00 160.22 ? 120  ILE D CG1 1 
ATOM   13274 C  CG2 . ILE D 2 462  ? 115.362 142.373 153.385 1.00 171.52 ? 120  ILE D CG2 1 
ATOM   13275 C  CD1 . ILE D 2 462  ? 115.809 144.626 151.595 1.00 146.06 ? 120  ILE D CD1 1 
ATOM   13276 N  N   . SER D 2 463  ? 113.688 142.805 156.573 1.00 174.78 ? 121  SER D N   1 
ATOM   13277 C  CA  . SER D 2 463  ? 113.698 141.885 157.702 1.00 175.67 ? 121  SER D CA  1 
ATOM   13278 C  C   . SER D 2 463  ? 112.295 141.377 158.016 1.00 173.95 ? 121  SER D C   1 
ATOM   13279 O  O   . SER D 2 463  ? 112.115 140.194 158.321 1.00 163.96 ? 121  SER D O   1 
ATOM   13280 C  CB  . SER D 2 463  ? 114.299 142.567 158.933 1.00 169.97 ? 121  SER D CB  1 
ATOM   13281 O  OG  . SER D 2 463  ? 115.700 142.726 158.802 1.00 167.32 ? 121  SER D OG  1 
ATOM   13282 N  N   . LYS D 2 464  ? 111.285 142.254 157.955 1.00 177.57 ? 122  LYS D N   1 
ATOM   13283 C  CA  . LYS D 2 464  ? 109.911 141.808 158.195 1.00 180.81 ? 122  LYS D CA  1 
ATOM   13284 C  C   . LYS D 2 464  ? 109.419 140.792 157.164 1.00 172.36 ? 122  LYS D C   1 
ATOM   13285 O  O   . LYS D 2 464  ? 108.828 139.768 157.529 1.00 171.20 ? 122  LYS D O   1 
ATOM   13286 C  CB  . LYS D 2 464  ? 108.984 143.015 158.200 1.00 176.02 ? 122  LYS D CB  1 
ATOM   13287 C  CG  . LYS D 2 464  ? 108.992 143.813 159.476 1.00 176.16 ? 122  LYS D CG  1 
ATOM   13288 C  CD  . LYS D 2 464  ? 108.254 145.132 159.301 1.00 175.11 ? 122  LYS D CD  1 
ATOM   13289 C  CE  . LYS D 2 464  ? 108.406 145.994 160.542 1.00 168.43 ? 122  LYS D CE  1 
ATOM   13290 N  NZ  . LYS D 2 464  ? 107.977 147.396 160.295 1.00 156.83 ? 122  LYS D NZ  1 
ATOM   13291 N  N   . GLY D 2 465  ? 109.684 141.050 155.876 1.00 164.53 ? 123  GLY D N   1 
ATOM   13292 C  CA  . GLY D 2 465  ? 109.311 140.111 154.822 1.00 156.79 ? 123  GLY D CA  1 
ATOM   13293 C  C   . GLY D 2 465  ? 110.035 138.782 154.966 1.00 166.50 ? 123  GLY D C   1 
ATOM   13294 O  O   . GLY D 2 465  ? 109.469 137.708 154.762 1.00 160.56 ? 123  GLY D O   1 
ATOM   13295 N  N   . MET D 2 466  ? 111.313 138.847 155.312 1.00 165.44 ? 124  MET D N   1 
ATOM   13296 C  CA  . MET D 2 466  ? 112.098 137.654 155.540 1.00 164.03 ? 124  MET D CA  1 
ATOM   13297 C  C   . MET D 2 466  ? 111.521 136.848 156.708 1.00 164.80 ? 124  MET D C   1 
ATOM   13298 O  O   . MET D 2 466  ? 111.494 135.597 156.677 1.00 155.96 ? 124  MET D O   1 
ATOM   13299 C  CB  . MET D 2 466  ? 113.530 138.110 155.787 1.00 161.89 ? 124  MET D CB  1 
ATOM   13300 C  CG  . MET D 2 466  ? 114.488 137.076 155.938 1.00 164.31 ? 124  MET D CG  1 
ATOM   13301 S  SD  . MET D 2 466  ? 114.411 136.018 154.546 1.00 142.19 ? 124  MET D SD  1 
ATOM   13302 C  CE  . MET D 2 466  ? 115.233 134.704 155.446 1.00 154.29 ? 124  MET D CE  1 
ATOM   13303 N  N   . SER D 2 467  ? 111.118 137.539 157.775 1.00 166.66 ? 125  SER D N   1 
ATOM   13304 C  CA  . SER D 2 467  ? 110.482 136.863 158.905 1.00 155.42 ? 125  SER D CA  1 
ATOM   13305 C  C   . SER D 2 467  ? 109.192 136.190 158.440 1.00 159.29 ? 125  SER D C   1 
ATOM   13306 O  O   . SER D 2 467  ? 108.865 135.070 158.861 1.00 157.50 ? 125  SER D O   1 
ATOM   13307 C  CB  . SER D 2 467  ? 110.177 137.829 160.050 1.00 162.48 ? 125  SER D CB  1 
ATOM   13308 O  OG  . SER D 2 467  ? 109.328 138.861 159.601 1.00 173.47 ? 125  SER D OG  1 
ATOM   13309 N  N   . GLU D 2 468  ? 108.433 136.885 157.586 1.00 162.85 ? 126  GLU D N   1 
ATOM   13310 C  CA  . GLU D 2 468  ? 107.195 136.346 157.030 1.00 155.25 ? 126  GLU D CA  1 
ATOM   13311 C  C   . GLU D 2 468  ? 107.472 135.094 156.212 1.00 157.71 ? 126  GLU D C   1 
ATOM   13312 O  O   . GLU D 2 468  ? 106.663 134.162 156.202 1.00 154.00 ? 126  GLU D O   1 
ATOM   13313 C  CB  . GLU D 2 468  ? 106.480 137.400 156.183 1.00 150.59 ? 126  GLU D CB  1 
ATOM   13314 C  CG  . GLU D 2 468  ? 105.935 138.563 156.987 1.00 164.63 ? 126  GLU D CG  1 
ATOM   13315 C  CD  . GLU D 2 468  ? 105.233 139.606 156.142 1.00 172.29 ? 126  GLU D CD  1 
ATOM   13316 O  OE1 . GLU D 2 468  ? 105.271 139.498 154.900 1.00 171.94 ? 126  GLU D OE1 1 
ATOM   13317 O  OE2 . GLU D 2 468  ? 104.639 140.535 156.729 1.00 171.36 ? 126  GLU D OE2 1 
ATOM   13318 N  N   . MET D 2 469  ? 108.588 135.071 155.486 1.00 160.77 ? 127  MET D N   1 
ATOM   13319 C  CA  . MET D 2 469  ? 108.902 133.889 154.692 1.00 157.83 ? 127  MET D CA  1 
ATOM   13320 C  C   . MET D 2 469  ? 109.267 132.707 155.582 1.00 152.24 ? 127  MET D C   1 
ATOM   13321 O  O   . MET D 2 469  ? 108.851 131.570 155.312 1.00 143.42 ? 127  MET D O   1 
ATOM   13322 C  CB  . MET D 2 469  ? 110.071 134.197 153.755 1.00 153.22 ? 127  MET D CB  1 
ATOM   13323 C  CG  . MET D 2 469  ? 109.692 134.701 152.387 1.00 161.97 ? 127  MET D CG  1 
ATOM   13324 S  SD  . MET D 2 469  ? 108.809 133.442 151.455 1.00 180.45 ? 127  MET D SD  1 
ATOM   13325 C  CE  . MET D 2 469  ? 107.295 134.309 151.083 1.00 173.84 ? 127  MET D CE  1 
ATOM   13326 N  N   . LEU D 2 470  ? 110.033 132.948 156.653 1.00 155.13 ? 128  LEU D N   1 
ATOM   13327 C  CA  . LEU D 2 470  ? 110.239 131.884 157.641 1.00 157.70 ? 128  LEU D CA  1 
ATOM   13328 C  C   . LEU D 2 470  ? 108.929 131.385 158.247 1.00 154.10 ? 128  LEU D C   1 
ATOM   13329 O  O   . LEU D 2 470  ? 108.783 130.189 158.528 1.00 149.24 ? 128  LEU D O   1 
ATOM   13330 C  CB  . LEU D 2 470  ? 111.173 132.348 158.761 1.00 150.96 ? 128  LEU D CB  1 
ATOM   13331 C  CG  . LEU D 2 470  ? 112.688 132.259 158.579 1.00 136.86 ? 128  LEU D CG  1 
ATOM   13332 C  CD1 . LEU D 2 470  ? 113.109 130.802 158.446 1.00 133.12 ? 128  LEU D CD1 1 
ATOM   13333 C  CD2 . LEU D 2 470  ? 113.140 133.036 157.385 1.00 132.39 ? 128  LEU D CD2 1 
ATOM   13334 N  N   . ALA D 2 471  ? 107.958 132.282 158.447 1.00 155.07 ? 129  ALA D N   1 
ATOM   13335 C  CA  . ALA D 2 471  ? 106.656 131.856 158.960 1.00 151.84 ? 129  ALA D CA  1 
ATOM   13336 C  C   . ALA D 2 471  ? 105.883 131.012 157.951 1.00 144.46 ? 129  ALA D C   1 
ATOM   13337 O  O   . ALA D 2 471  ? 105.296 129.984 158.310 1.00 136.74 ? 129  ALA D O   1 
ATOM   13338 C  CB  . ALA D 2 471  ? 105.836 133.078 159.371 1.00 151.99 ? 129  ALA D CB  1 
ATOM   13339 N  N   . LYS D 2 472  ? 105.879 131.426 156.684 1.00 142.60 ? 130  LYS D N   1 
ATOM   13340 C  CA  . LYS D 2 472  ? 105.070 130.750 155.675 1.00 135.44 ? 130  LYS D CA  1 
ATOM   13341 C  C   . LYS D 2 472  ? 105.647 129.387 155.322 1.00 130.65 ? 130  LYS D C   1 
ATOM   13342 O  O   . LYS D 2 472  ? 104.899 128.439 155.031 1.00 125.79 ? 130  LYS D O   1 
ATOM   13343 C  CB  . LYS D 2 472  ? 104.949 131.643 154.443 1.00 129.97 ? 130  LYS D CB  1 
ATOM   13344 C  CG  . LYS D 2 472  ? 104.165 132.906 154.746 1.00 122.85 ? 130  LYS D CG  1 
ATOM   13345 C  CD  . LYS D 2 472  ? 104.035 133.826 153.556 1.00 136.33 ? 130  LYS D CD  1 
ATOM   13346 C  CE  . LYS D 2 472  ? 103.390 135.132 153.985 1.00 146.69 ? 130  LYS D CE  1 
ATOM   13347 N  NZ  . LYS D 2 472  ? 101.973 134.936 154.393 1.00 148.82 ? 130  LYS D NZ  1 
ATOM   13348 N  N   . TYR D 2 473  ? 106.979 129.277 155.329 1.00 133.88 ? 131  TYR D N   1 
ATOM   13349 C  CA  . TYR D 2 473  ? 107.622 128.002 155.037 1.00 138.77 ? 131  TYR D CA  1 
ATOM   13350 C  C   . TYR D 2 473  ? 107.179 126.909 156.001 1.00 133.01 ? 131  TYR D C   1 
ATOM   13351 O  O   . TYR D 2 473  ? 107.071 125.743 155.605 1.00 125.96 ? 131  TYR D O   1 
ATOM   13352 C  CB  . TYR D 2 473  ? 109.142 128.184 155.084 1.00 143.96 ? 131  TYR D CB  1 
ATOM   13353 C  CG  . TYR D 2 473  ? 109.939 126.921 154.853 1.00 142.63 ? 131  TYR D CG  1 
ATOM   13354 C  CD1 . TYR D 2 473  ? 110.174 126.024 155.890 1.00 144.94 ? 131  TYR D CD1 1 
ATOM   13355 C  CD2 . TYR D 2 473  ? 110.459 126.623 153.602 1.00 128.79 ? 131  TYR D CD2 1 
ATOM   13356 C  CE1 . TYR D 2 473  ? 110.896 124.869 155.686 1.00 135.84 ? 131  TYR D CE1 1 
ATOM   13357 C  CE2 . TYR D 2 473  ? 111.186 125.468 153.390 1.00 127.89 ? 131  TYR D CE2 1 
ATOM   13358 C  CZ  . TYR D 2 473  ? 111.398 124.594 154.435 1.00 127.26 ? 131  TYR D CZ  1 
ATOM   13359 O  OH  . TYR D 2 473  ? 112.122 123.444 154.231 1.00 120.41 ? 131  TYR D OH  1 
ATOM   13360 N  N   . ASP D 2 474  ? 106.899 127.263 157.258 1.00 133.30 ? 132  ASP D N   1 
ATOM   13361 C  CA  . ASP D 2 474  ? 106.505 126.254 158.235 1.00 130.00 ? 132  ASP D CA  1 
ATOM   13362 C  C   . ASP D 2 474  ? 105.099 125.717 158.000 1.00 125.79 ? 132  ASP D C   1 
ATOM   13363 O  O   . ASP D 2 474  ? 104.800 124.600 158.435 1.00 127.51 ? 132  ASP D O   1 
ATOM   13364 C  CB  . ASP D 2 474  ? 106.641 126.818 159.649 1.00 147.83 ? 132  ASP D CB  1 
ATOM   13365 C  CG  . ASP D 2 474  ? 108.085 127.099 160.020 1.00 145.83 ? 132  ASP D CG  1 
ATOM   13366 O  OD1 . ASP D 2 474  ? 108.967 126.338 159.569 1.00 125.92 ? 132  ASP D OD1 1 
ATOM   13367 O  OD2 . ASP D 2 474  ? 108.340 128.073 160.757 1.00 152.63 ? 132  ASP D OD2 1 
ATOM   13368 N  N   . HIS D 2 475  ? 104.230 126.475 157.331 1.00 126.72 ? 133  HIS D N   1 
ATOM   13369 C  CA  . HIS D 2 475  ? 102.889 125.982 157.041 1.00 130.04 ? 133  HIS D CA  1 
ATOM   13370 C  C   . HIS D 2 475  ? 102.793 125.320 155.678 1.00 116.98 ? 133  HIS D C   1 
ATOM   13371 O  O   . HIS D 2 475  ? 102.003 124.383 155.511 1.00 106.95 ? 133  HIS D O   1 
ATOM   13372 C  CB  . HIS D 2 475  ? 101.845 127.101 157.132 1.00 134.40 ? 133  HIS D CB  1 
ATOM   13373 C  CG  . HIS D 2 475  ? 101.927 127.920 158.382 1.00 152.72 ? 133  HIS D CG  1 
ATOM   13374 N  ND1 . HIS D 2 475  ? 101.347 129.166 158.493 1.00 155.86 ? 133  HIS D ND1 1 
ATOM   13375 C  CD2 . HIS D 2 475  ? 102.488 127.658 159.587 1.00 156.00 ? 133  HIS D CD2 1 
ATOM   13376 C  CE1 . HIS D 2 475  ? 101.564 129.643 159.705 1.00 160.68 ? 133  HIS D CE1 1 
ATOM   13377 N  NE2 . HIS D 2 475  ? 102.254 128.748 160.388 1.00 161.68 ? 133  HIS D NE2 1 
ATOM   13378 N  N   . LEU D 2 476  ? 103.568 125.779 154.695 1.00 111.33 ? 134  LEU D N   1 
ATOM   13379 C  CA  . LEU D 2 476  ? 103.422 125.208 153.360 1.00 104.41 ? 134  LEU D CA  1 
ATOM   13380 C  C   . LEU D 2 476  ? 104.061 123.827 153.234 1.00 115.55 ? 134  LEU D C   1 
ATOM   13381 O  O   . LEU D 2 476  ? 103.458 122.918 152.651 1.00 112.32 ? 134  LEU D O   1 
ATOM   13382 C  CB  . LEU D 2 476  ? 103.999 126.160 152.315 1.00 113.35 ? 134  LEU D CB  1 
ATOM   13383 C  CG  . LEU D 2 476  ? 102.915 126.989 151.627 1.00 123.23 ? 134  LEU D CG  1 
ATOM   13384 C  CD1 . LEU D 2 476  ? 103.482 127.744 150.440 1.00 135.09 ? 134  LEU D CD1 1 
ATOM   13385 C  CD2 . LEU D 2 476  ? 101.762 126.087 151.197 1.00 109.74 ? 134  LEU D CD2 1 
ATOM   13386 N  N   . VAL D 2 477  ? 105.261 123.635 153.777 1.00 114.22 ? 135  VAL D N   1 
ATOM   13387 C  CA  . VAL D 2 477  ? 106.073 122.464 153.460 1.00 88.92  ? 135  VAL D CA  1 
ATOM   13388 C  C   . VAL D 2 477  ? 105.782 121.346 154.453 1.00 93.77  ? 135  VAL D C   1 
ATOM   13389 O  O   . VAL D 2 477  ? 105.800 121.559 155.671 1.00 101.33 ? 135  VAL D O   1 
ATOM   13390 C  CB  . VAL D 2 477  ? 107.570 122.819 153.457 1.00 86.66  ? 135  VAL D CB  1 
ATOM   13391 C  CG1 . VAL D 2 477  ? 108.405 121.598 153.093 1.00 90.53  ? 135  VAL D CG1 1 
ATOM   13392 C  CG2 . VAL D 2 477  ? 107.840 123.966 152.492 1.00 83.62  ? 135  VAL D CG2 1 
ATOM   13393 N  N   . ILE D 2 478  ? 105.514 120.150 153.929 1.00 89.72  ? 136  ILE D N   1 
ATOM   13394 C  CA  . ILE D 2 478  ? 105.275 118.975 154.761 1.00 91.61  ? 136  ILE D CA  1 
ATOM   13395 C  C   . ILE D 2 478  ? 106.621 118.426 155.216 1.00 100.45 ? 136  ILE D C   1 
ATOM   13396 O  O   . ILE D 2 478  ? 107.517 118.191 154.397 1.00 105.30 ? 136  ILE D O   1 
ATOM   13397 C  CB  . ILE D 2 478  ? 104.477 117.917 153.985 1.00 75.56  ? 136  ILE D CB  1 
ATOM   13398 C  CG1 . ILE D 2 478  ? 103.140 118.494 153.519 1.00 83.42  ? 136  ILE D CG1 1 
ATOM   13399 C  CG2 . ILE D 2 478  ? 104.242 116.685 154.850 1.00 87.47  ? 136  ILE D CG2 1 
ATOM   13400 C  CD1 . ILE D 2 478  ? 102.489 117.705 152.403 1.00 72.97  ? 136  ILE D CD1 1 
ATOM   13401 N  N   . SER D 2 479  ? 106.765 118.205 156.528 1.00 103.61 ? 137  SER D N   1 
ATOM   13402 C  CA  . SER D 2 479  ? 108.042 117.747 157.063 1.00 110.66 ? 137  SER D CA  1 
ATOM   13403 C  C   . SER D 2 479  ? 107.900 116.662 158.128 1.00 102.88 ? 137  SER D C   1 
ATOM   13404 O  O   . SER D 2 479  ? 108.831 116.465 158.919 1.00 100.27 ? 137  SER D O   1 
ATOM   13405 C  CB  . SER D 2 479  ? 108.831 118.921 157.651 1.00 102.34 ? 137  SER D CB  1 
ATOM   13406 O  OG  . SER D 2 479  ? 108.368 119.241 158.951 1.00 102.16 ? 137  SER D OG  1 
ATOM   13407 N  N   . THR D 2 480  ? 106.778 115.952 158.179 1.00 115.12 ? 138  THR D N   1 
ATOM   13408 C  CA  . THR D 2 480  ? 106.613 114.905 159.185 1.00 130.87 ? 138  THR D CA  1 
ATOM   13409 C  C   . THR D 2 480  ? 107.535 113.724 158.901 1.00 123.85 ? 138  THR D C   1 
ATOM   13410 O  O   . THR D 2 480  ? 108.618 113.620 159.479 1.00 109.65 ? 138  THR D O   1 
ATOM   13411 C  CB  . THR D 2 480  ? 105.165 114.392 159.249 1.00 136.14 ? 138  THR D CB  1 
ATOM   13412 O  OG1 . THR D 2 480  ? 105.064 113.378 160.258 1.00 133.10 ? 138  THR D OG1 1 
ATOM   13413 C  CG2 . THR D 2 480  ? 104.758 113.796 157.912 1.00 112.76 ? 138  THR D CG2 1 
ATOM   13414 N  N   . VAL E 2 452  ? 127.668 153.961 146.496 1.00 195.80 ? 110  VAL E N   1 
ATOM   13415 C  CA  . VAL E 2 452  ? 126.776 153.402 147.503 1.00 205.07 ? 110  VAL E CA  1 
ATOM   13416 C  C   . VAL E 2 452  ? 125.324 153.618 147.076 1.00 212.62 ? 110  VAL E C   1 
ATOM   13417 O  O   . VAL E 2 452  ? 124.410 152.966 147.587 1.00 204.88 ? 110  VAL E O   1 
ATOM   13418 C  CB  . VAL E 2 452  ? 127.054 154.017 148.889 1.00 201.70 ? 110  VAL E CB  1 
ATOM   13419 C  CG1 . VAL E 2 452  ? 126.355 153.223 149.984 1.00 189.40 ? 110  VAL E CG1 1 
ATOM   13420 C  CG2 . VAL E 2 452  ? 128.552 154.079 149.147 1.00 198.91 ? 110  VAL E CG2 1 
ATOM   13421 N  N   . LEU E 2 453  ? 125.120 154.525 146.116 1.00 212.63 ? 111  LEU E N   1 
ATOM   13422 C  CA  . LEU E 2 453  ? 123.780 154.758 145.581 1.00 217.05 ? 111  LEU E CA  1 
ATOM   13423 C  C   . LEU E 2 453  ? 123.270 153.523 144.850 1.00 208.97 ? 111  LEU E C   1 
ATOM   13424 O  O   . LEU E 2 453  ? 122.082 153.181 144.929 1.00 199.17 ? 111  LEU E O   1 
ATOM   13425 C  CB  . LEU E 2 453  ? 123.793 155.963 144.649 1.00 215.41 ? 111  LEU E CB  1 
ATOM   13426 C  CG  . LEU E 2 453  ? 122.454 156.413 144.064 1.00 206.31 ? 111  LEU E CG  1 
ATOM   13427 C  CD1 . LEU E 2 453  ? 122.308 157.917 144.167 1.00 194.99 ? 111  LEU E CD1 1 
ATOM   13428 C  CD2 . LEU E 2 453  ? 122.343 155.963 142.615 1.00 196.35 ? 111  LEU E CD2 1 
ATOM   13429 N  N   . LYS E 2 454  ? 124.167 152.839 144.143 1.00 203.62 ? 112  LYS E N   1 
ATOM   13430 C  CA  . LYS E 2 454  ? 123.807 151.641 143.412 1.00 201.10 ? 112  LYS E CA  1 
ATOM   13431 C  C   . LYS E 2 454  ? 123.297 150.579 144.375 1.00 197.29 ? 112  LYS E C   1 
ATOM   13432 O  O   . LYS E 2 454  ? 122.357 149.831 144.057 1.00 180.60 ? 112  LYS E O   1 
ATOM   13433 C  CB  . LYS E 2 454  ? 125.017 151.135 142.638 1.00 189.60 ? 112  LYS E CB  1 
ATOM   13434 C  CG  . LYS E 2 454  ? 125.425 152.003 141.460 1.00 184.93 ? 112  LYS E CG  1 
ATOM   13435 C  CD  . LYS E 2 454  ? 126.598 151.403 140.702 1.00 180.87 ? 112  LYS E CD  1 
ATOM   13436 C  CE  . LYS E 2 454  ? 127.044 152.325 139.580 1.00 178.83 ? 112  LYS E CE  1 
ATOM   13437 N  NZ  . LYS E 2 454  ? 128.171 151.766 138.787 1.00 171.56 ? 112  LYS E NZ  1 
ATOM   13438 N  N   . MET E 2 455  ? 123.869 150.531 145.586 1.00 200.76 ? 113  MET E N   1 
ATOM   13439 C  CA  . MET E 2 455  ? 123.432 149.573 146.585 1.00 197.82 ? 113  MET E CA  1 
ATOM   13440 C  C   . MET E 2 455  ? 122.001 149.862 147.003 1.00 186.86 ? 113  MET E C   1 
ATOM   13441 O  O   . MET E 2 455  ? 121.170 148.951 147.106 1.00 172.40 ? 113  MET E O   1 
ATOM   13442 C  CB  . MET E 2 455  ? 124.350 149.645 147.809 1.00 191.73 ? 113  MET E CB  1 
ATOM   13443 C  CG  . MET E 2 455  ? 125.872 149.507 147.565 1.00 192.02 ? 113  MET E CG  1 
ATOM   13444 S  SD  . MET E 2 455  ? 126.635 148.241 146.519 1.00 202.33 ? 113  MET E SD  1 
ATOM   13445 C  CE  . MET E 2 455  ? 126.420 148.916 144.877 1.00 182.97 ? 113  MET E CE  1 
ATOM   13446 N  N   . GLY E 2 456  ? 121.701 151.137 147.255 1.00 189.31 ? 114  GLY E N   1 
ATOM   13447 C  CA  . GLY E 2 456  ? 120.349 151.511 147.658 1.00 188.19 ? 114  GLY E CA  1 
ATOM   13448 C  C   . GLY E 2 456  ? 119.333 151.186 146.582 1.00 186.38 ? 114  GLY E C   1 
ATOM   13449 O  O   . GLY E 2 456  ? 118.238 150.692 146.876 1.00 175.54 ? 114  GLY E O   1 
ATOM   13450 N  N   . ARG E 2 457  ? 119.672 151.481 145.325 1.00 186.89 ? 115  ARG E N   1 
ATOM   13451 C  CA  . ARG E 2 457  ? 118.747 151.185 144.236 1.00 182.75 ? 115  ARG E CA  1 
ATOM   13452 C  C   . ARG E 2 457  ? 118.503 149.684 144.134 1.00 173.38 ? 115  ARG E C   1 
ATOM   13453 O  O   . ARG E 2 457  ? 117.359 149.238 143.953 1.00 160.90 ? 115  ARG E O   1 
ATOM   13454 C  CB  . ARG E 2 457  ? 119.288 151.737 142.918 1.00 174.28 ? 115  ARG E CB  1 
ATOM   13455 C  CG  . ARG E 2 457  ? 119.292 153.251 142.849 1.00 176.51 ? 115  ARG E CG  1 
ATOM   13456 C  CD  . ARG E 2 457  ? 119.543 153.744 141.438 1.00 173.07 ? 115  ARG E CD  1 
ATOM   13457 N  NE  . ARG E 2 457  ? 119.388 155.192 141.346 1.00 181.15 ? 115  ARG E NE  1 
ATOM   13458 C  CZ  . ARG E 2 457  ? 119.383 155.871 140.205 1.00 182.27 ? 115  ARG E CZ  1 
ATOM   13459 N  NH1 . ARG E 2 457  ? 119.523 155.233 139.051 1.00 179.31 ? 115  ARG E NH1 1 
ATOM   13460 N  NH2 . ARG E 2 457  ? 119.237 157.189 140.217 1.00 173.32 ? 115  ARG E NH2 1 
ATOM   13461 N  N   . THR E 2 458  ? 119.568 148.885 144.267 1.00 172.30 ? 116  THR E N   1 
ATOM   13462 C  CA  . THR E 2 458  ? 119.411 147.437 144.190 1.00 171.29 ? 116  THR E CA  1 
ATOM   13463 C  C   . THR E 2 458  ? 118.528 146.936 145.327 1.00 169.04 ? 116  THR E C   1 
ATOM   13464 O  O   . THR E 2 458  ? 117.658 146.079 145.123 1.00 162.61 ? 116  THR E O   1 
ATOM   13465 C  CB  . THR E 2 458  ? 120.783 146.760 144.229 1.00 164.09 ? 116  THR E CB  1 
ATOM   13466 O  OG1 . THR E 2 458  ? 121.531 147.125 143.061 1.00 145.79 ? 116  THR E OG1 1 
ATOM   13467 C  CG2 . THR E 2 458  ? 120.638 145.245 144.275 1.00 156.69 ? 116  THR E CG2 1 
ATOM   13468 N  N   . LEU E 2 459  ? 118.734 147.473 146.534 1.00 165.32 ? 117  LEU E N   1 
ATOM   13469 C  CA  . LEU E 2 459  ? 117.935 147.059 147.681 1.00 159.02 ? 117  LEU E CA  1 
ATOM   13470 C  C   . LEU E 2 459  ? 116.466 147.402 147.481 1.00 165.22 ? 117  LEU E C   1 
ATOM   13471 O  O   . LEU E 2 459  ? 115.584 146.600 147.814 1.00 158.33 ? 117  LEU E O   1 
ATOM   13472 C  CB  . LEU E 2 459  ? 118.472 147.702 148.959 1.00 159.76 ? 117  LEU E CB  1 
ATOM   13473 C  CG  . LEU E 2 459  ? 119.853 147.216 149.399 1.00 164.02 ? 117  LEU E CG  1 
ATOM   13474 C  CD1 . LEU E 2 459  ? 120.408 148.089 150.512 1.00 171.69 ? 117  LEU E CD1 1 
ATOM   13475 C  CD2 . LEU E 2 459  ? 119.777 145.760 149.835 1.00 149.54 ? 117  LEU E CD2 1 
ATOM   13476 N  N   . GLU E 2 460  ? 116.177 148.599 146.960 1.00 167.45 ? 118  GLU E N   1 
ATOM   13477 C  CA  . GLU E 2 460  ? 114.780 148.967 146.739 1.00 165.86 ? 118  GLU E CA  1 
ATOM   13478 C  C   . GLU E 2 460  ? 114.137 148.050 145.701 1.00 160.38 ? 118  GLU E C   1 
ATOM   13479 O  O   . GLU E 2 460  ? 112.974 147.649 145.852 1.00 152.77 ? 118  GLU E O   1 
ATOM   13480 C  CB  . GLU E 2 460  ? 114.666 150.445 146.345 1.00 167.76 ? 118  GLU E CB  1 
ATOM   13481 C  CG  . GLU E 2 460  ? 114.787 150.762 144.864 1.00 173.61 ? 118  GLU E CG  1 
ATOM   13482 C  CD  . GLU E 2 460  ? 114.564 152.231 144.572 1.00 185.33 ? 118  GLU E CD  1 
ATOM   13483 O  OE1 . GLU E 2 460  ? 114.283 152.989 145.523 1.00 183.14 ? 118  GLU E OE1 1 
ATOM   13484 O  OE2 . GLU E 2 460  ? 114.667 152.628 143.391 1.00 182.46 ? 118  GLU E OE2 1 
ATOM   13485 N  N   . ALA E 2 461  ? 114.880 147.698 144.645 1.00 161.85 ? 119  ALA E N   1 
ATOM   13486 C  CA  . ALA E 2 461  ? 114.331 146.793 143.637 1.00 157.44 ? 119  ALA E CA  1 
ATOM   13487 C  C   . ALA E 2 461  ? 114.029 145.429 144.248 1.00 152.35 ? 119  ALA E C   1 
ATOM   13488 O  O   . ALA E 2 461  ? 112.980 144.820 143.972 1.00 145.77 ? 119  ALA E O   1 
ATOM   13489 C  CB  . ALA E 2 461  ? 115.300 146.659 142.462 1.00 139.89 ? 119  ALA E CB  1 
ATOM   13490 N  N   . ILE E 2 462  ? 114.945 144.941 145.091 1.00 148.22 ? 120  ILE E N   1 
ATOM   13491 C  CA  . ILE E 2 462  ? 114.752 143.650 145.743 1.00 138.21 ? 120  ILE E CA  1 
ATOM   13492 C  C   . ILE E 2 462  ? 113.528 143.700 146.643 1.00 143.42 ? 120  ILE E C   1 
ATOM   13493 O  O   . ILE E 2 462  ? 112.739 142.748 146.696 1.00 138.80 ? 120  ILE E O   1 
ATOM   13494 C  CB  . ILE E 2 462  ? 116.012 143.255 146.534 1.00 129.93 ? 120  ILE E CB  1 
ATOM   13495 C  CG1 . ILE E 2 462  ? 117.179 142.966 145.590 1.00 141.22 ? 120  ILE E CG1 1 
ATOM   13496 C  CG2 . ILE E 2 462  ? 115.736 142.046 147.422 1.00 134.98 ? 120  ILE E CG2 1 
ATOM   13497 C  CD1 . ILE E 2 462  ? 118.452 142.579 146.309 1.00 144.36 ? 120  ILE E CD1 1 
ATOM   13498 N  N   . SER E 2 463  ? 113.345 144.811 147.361 1.00 151.27 ? 121  SER E N   1 
ATOM   13499 C  CA  . SER E 2 463  ? 112.179 144.927 148.230 1.00 148.08 ? 121  SER E CA  1 
ATOM   13500 C  C   . SER E 2 463  ? 110.897 144.911 147.411 1.00 150.30 ? 121  SER E C   1 
ATOM   13501 O  O   . SER E 2 463  ? 109.897 144.317 147.827 1.00 143.18 ? 121  SER E O   1 
ATOM   13502 C  CB  . SER E 2 463  ? 112.266 146.207 149.059 1.00 151.00 ? 121  SER E CB  1 
ATOM   13503 O  OG  . SER E 2 463  ? 112.127 147.355 148.238 1.00 145.75 ? 121  SER E OG  1 
ATOM   13504 N  N   . LYS E 2 464  ? 110.896 145.594 146.264 1.00 152.88 ? 122  LYS E N   1 
ATOM   13505 C  CA  . LYS E 2 464  ? 109.713 145.603 145.408 1.00 152.37 ? 122  LYS E CA  1 
ATOM   13506 C  C   . LYS E 2 464  ? 109.336 144.180 145.001 1.00 153.30 ? 122  LYS E C   1 
ATOM   13507 O  O   . LYS E 2 464  ? 108.186 143.740 145.179 1.00 146.21 ? 122  LYS E O   1 
ATOM   13508 C  CB  . LYS E 2 464  ? 109.963 146.482 144.182 1.00 139.81 ? 122  LYS E CB  1 
ATOM   13509 C  CG  . LYS E 2 464  ? 108.788 146.566 143.232 1.00 156.75 ? 122  LYS E CG  1 
ATOM   13510 C  CD  . LYS E 2 464  ? 109.104 147.456 142.046 1.00 161.13 ? 122  LYS E CD  1 
ATOM   13511 C  CE  . LYS E 2 464  ? 107.873 147.662 141.184 1.00 161.34 ? 122  LYS E CE  1 
ATOM   13512 N  NZ  . LYS E 2 464  ? 107.406 146.388 140.576 1.00 168.55 ? 122  LYS E NZ  1 
ATOM   13513 N  N   . GLY E 2 465  ? 110.306 143.449 144.437 1.00 146.61 ? 123  GLY E N   1 
ATOM   13514 C  CA  . GLY E 2 465  ? 110.035 142.079 144.018 1.00 139.68 ? 123  GLY E CA  1 
ATOM   13515 C  C   . GLY E 2 465  ? 109.588 141.199 145.169 1.00 138.23 ? 123  GLY E C   1 
ATOM   13516 O  O   . GLY E 2 465  ? 108.681 140.371 145.025 1.00 130.09 ? 123  GLY E O   1 
ATOM   13517 N  N   . MET E 2 466  ? 110.234 141.354 146.325 1.00 145.80 ? 124  MET E N   1 
ATOM   13518 C  CA  . MET E 2 466  ? 109.850 140.619 147.523 1.00 146.56 ? 124  MET E CA  1 
ATOM   13519 C  C   . MET E 2 466  ? 108.407 140.904 147.912 1.00 144.59 ? 124  MET E C   1 
ATOM   13520 O  O   . MET E 2 466  ? 107.675 139.998 148.318 1.00 140.88 ? 124  MET E O   1 
ATOM   13521 C  CB  . MET E 2 466  ? 110.829 140.941 148.636 1.00 138.98 ? 124  MET E CB  1 
ATOM   13522 C  CG  . MET E 2 466  ? 110.533 140.365 149.975 1.00 150.04 ? 124  MET E CG  1 
ATOM   13523 S  SD  . MET E 2 466  ? 112.060 140.746 150.847 1.00 196.10 ? 124  MET E SD  1 
ATOM   13524 C  CE  . MET E 2 466  ? 111.546 140.421 152.497 1.00 180.90 ? 124  MET E CE  1 
ATOM   13525 N  N   . SER E 2 467  ? 107.992 142.170 147.835 1.00 147.38 ? 125  SER E N   1 
ATOM   13526 C  CA  . SER E 2 467  ? 106.617 142.519 148.165 1.00 151.39 ? 125  SER E CA  1 
ATOM   13527 C  C   . SER E 2 467  ? 105.662 141.780 147.237 1.00 153.05 ? 125  SER E C   1 
ATOM   13528 O  O   . SER E 2 467  ? 104.660 141.200 147.683 1.00 146.25 ? 125  SER E O   1 
ATOM   13529 C  CB  . SER E 2 467  ? 106.422 144.031 148.070 1.00 149.73 ? 125  SER E CB  1 
ATOM   13530 O  OG  . SER E 2 467  ? 106.771 144.495 146.779 1.00 147.56 ? 125  SER E OG  1 
ATOM   13531 N  N   . GLU E 2 468  ? 105.967 141.785 145.934 1.00 148.00 ? 126  GLU E N   1 
ATOM   13532 C  CA  . GLU E 2 468  ? 105.083 141.129 144.970 1.00 139.97 ? 126  GLU E CA  1 
ATOM   13533 C  C   . GLU E 2 468  ? 104.972 139.636 145.271 1.00 139.90 ? 126  GLU E C   1 
ATOM   13534 O  O   . GLU E 2 468  ? 103.879 139.053 145.234 1.00 137.53 ? 126  GLU E O   1 
ATOM   13535 C  CB  . GLU E 2 468  ? 105.622 141.335 143.556 1.00 131.20 ? 126  GLU E CB  1 
ATOM   13536 C  CG  . GLU E 2 468  ? 105.914 142.774 143.198 1.00 144.59 ? 126  GLU E CG  1 
ATOM   13537 C  CD  . GLU E 2 468  ? 106.699 142.893 141.909 1.00 160.02 ? 126  GLU E CD  1 
ATOM   13538 O  OE1 . GLU E 2 468  ? 106.630 143.959 141.265 1.00 160.50 ? 126  GLU E OE1 1 
ATOM   13539 O  OE2 . GLU E 2 468  ? 107.388 141.917 141.541 1.00 154.37 ? 126  GLU E OE2 1 
ATOM   13540 N  N   . MET E 2 469  ? 106.102 138.997 145.571 1.00 143.62 ? 127  MET E N   1 
ATOM   13541 C  CA  . MET E 2 469  ? 106.107 137.549 145.743 1.00 141.62 ? 127  MET E CA  1 
ATOM   13542 C  C   . MET E 2 469  ? 105.467 137.160 147.074 1.00 138.31 ? 127  MET E C   1 
ATOM   13543 O  O   . MET E 2 469  ? 104.847 136.096 147.180 1.00 133.94 ? 127  MET E O   1 
ATOM   13544 C  CB  . MET E 2 469  ? 107.524 136.986 145.599 1.00 150.66 ? 127  MET E CB  1 
ATOM   13545 C  CG  . MET E 2 469  ? 108.527 137.430 146.638 1.00 162.12 ? 127  MET E CG  1 
ATOM   13546 S  SD  . MET E 2 469  ? 108.489 136.403 148.117 1.00 197.96 ? 127  MET E SD  1 
ATOM   13547 C  CE  . MET E 2 469  ? 109.167 134.878 147.470 1.00 163.36 ? 127  MET E CE  1 
ATOM   13548 N  N   . LEU E 2 470  ? 105.565 138.038 148.079 1.00 142.94 ? 128  LEU E N   1 
ATOM   13549 C  CA  . LEU E 2 470  ? 104.785 137.871 149.302 1.00 142.51 ? 128  LEU E CA  1 
ATOM   13550 C  C   . LEU E 2 470  ? 103.290 137.970 149.038 1.00 140.22 ? 128  LEU E C   1 
ATOM   13551 O  O   . LEU E 2 470  ? 102.504 137.233 149.639 1.00 141.98 ? 128  LEU E O   1 
ATOM   13552 C  CB  . LEU E 2 470  ? 105.188 138.938 150.321 1.00 152.85 ? 128  LEU E CB  1 
ATOM   13553 C  CG  . LEU E 2 470  ? 106.497 138.851 151.099 1.00 154.44 ? 128  LEU E CG  1 
ATOM   13554 C  CD1 . LEU E 2 470  ? 106.607 140.040 152.029 1.00 165.02 ? 128  LEU E CD1 1 
ATOM   13555 C  CD2 . LEU E 2 470  ? 106.511 137.579 151.905 1.00 147.33 ? 128  LEU E CD2 1 
ATOM   13556 N  N   . ALA E 2 471  ? 102.868 138.878 148.155 1.00 136.94 ? 129  ALA E N   1 
ATOM   13557 C  CA  . ALA E 2 471  ? 101.450 138.920 147.801 1.00 141.35 ? 129  ALA E CA  1 
ATOM   13558 C  C   . ALA E 2 471  ? 101.017 137.608 147.151 1.00 140.62 ? 129  ALA E C   1 
ATOM   13559 O  O   . ALA E 2 471  ? 99.962  137.039 147.484 1.00 141.34 ? 129  ALA E O   1 
ATOM   13560 C  CB  . ALA E 2 471  ? 101.173 140.101 146.871 1.00 133.88 ? 129  ALA E CB  1 
ATOM   13561 N  N   . LYS E 2 472  ? 101.828 137.123 146.208 1.00 139.84 ? 130  LYS E N   1 
ATOM   13562 C  CA  . LYS E 2 472  ? 101.540 135.849 145.559 1.00 128.61 ? 130  LYS E CA  1 
ATOM   13563 C  C   . LYS E 2 472  ? 101.421 134.715 146.572 1.00 129.93 ? 130  LYS E C   1 
ATOM   13564 O  O   . LYS E 2 472  ? 100.518 133.877 146.469 1.00 130.26 ? 130  LYS E O   1 
ATOM   13565 C  CB  . LYS E 2 472  ? 102.632 135.543 144.535 1.00 124.56 ? 130  LYS E CB  1 
ATOM   13566 C  CG  . LYS E 2 472  ? 102.620 136.495 143.357 1.00 139.61 ? 130  LYS E CG  1 
ATOM   13567 C  CD  . LYS E 2 472  ? 103.701 136.163 142.351 1.00 129.16 ? 130  LYS E CD  1 
ATOM   13568 C  CE  . LYS E 2 472  ? 103.682 137.162 141.207 1.00 130.56 ? 130  LYS E CE  1 
ATOM   13569 N  NZ  . LYS E 2 472  ? 104.745 136.884 140.207 1.00 120.00 ? 130  LYS E NZ  1 
ATOM   13570 N  N   . TYR E 2 473  ? 102.323 134.666 147.560 1.00 137.37 ? 131  TYR E N   1 
ATOM   13571 C  CA  . TYR E 2 473  ? 102.216 133.632 148.586 1.00 133.74 ? 131  TYR E CA  1 
ATOM   13572 C  C   . TYR E 2 473  ? 101.005 133.834 149.488 1.00 141.23 ? 131  TYR E C   1 
ATOM   13573 O  O   . TYR E 2 473  ? 100.427 132.856 149.976 1.00 141.28 ? 131  TYR E O   1 
ATOM   13574 C  CB  . TYR E 2 473  ? 103.479 133.597 149.440 1.00 138.64 ? 131  TYR E CB  1 
ATOM   13575 C  CG  . TYR E 2 473  ? 104.543 132.687 148.892 1.00 146.34 ? 131  TYR E CG  1 
ATOM   13576 C  CD1 . TYR E 2 473  ? 105.555 133.185 148.086 1.00 138.13 ? 131  TYR E CD1 1 
ATOM   13577 C  CD2 . TYR E 2 473  ? 104.516 131.324 149.148 1.00 132.43 ? 131  TYR E CD2 1 
ATOM   13578 C  CE1 . TYR E 2 473  ? 106.527 132.357 147.573 1.00 123.43 ? 131  TYR E CE1 1 
ATOM   13579 C  CE2 . TYR E 2 473  ? 105.481 130.485 148.636 1.00 120.84 ? 131  TYR E CE2 1 
ATOM   13580 C  CZ  . TYR E 2 473  ? 106.485 131.006 147.848 1.00 122.32 ? 131  TYR E CZ  1 
ATOM   13581 O  OH  . TYR E 2 473  ? 107.455 130.177 147.335 1.00 111.63 ? 131  TYR E OH  1 
ATOM   13582 N  N   . ASP E 2 474  ? 100.613 135.089 149.721 1.00 152.52 ? 132  ASP E N   1 
ATOM   13583 C  CA  . ASP E 2 474  ? 99.424  135.366 150.519 1.00 156.34 ? 132  ASP E CA  1 
ATOM   13584 C  C   . ASP E 2 474  ? 98.190  134.795 149.852 1.00 148.69 ? 132  ASP E C   1 
ATOM   13585 O  O   . ASP E 2 474  ? 97.245  134.371 150.529 1.00 141.58 ? 132  ASP E O   1 
ATOM   13586 C  CB  . ASP E 2 474  ? 99.272  136.870 150.739 1.00 160.39 ? 132  ASP E CB  1 
ATOM   13587 C  CG  . ASP E 2 474  ? 100.108 137.371 151.897 1.00 167.67 ? 132  ASP E CG  1 
ATOM   13588 O  OD1 . ASP E 2 474  ? 100.949 136.597 152.397 1.00 161.72 ? 132  ASP E OD1 1 
ATOM   13589 O  OD2 . ASP E 2 474  ? 99.921  138.535 152.309 1.00 170.11 ? 132  ASP E OD2 1 
ATOM   13590 N  N   . HIS E 2 475  ? 98.190  134.782 148.520 1.00 147.08 ? 133  HIS E N   1 
ATOM   13591 C  CA  . HIS E 2 475  ? 97.084  134.178 147.784 1.00 140.67 ? 133  HIS E CA  1 
ATOM   13592 C  C   . HIS E 2 475  ? 96.923  132.699 148.130 1.00 138.69 ? 133  HIS E C   1 
ATOM   13593 O  O   . HIS E 2 475  ? 95.796  132.209 148.274 1.00 130.20 ? 133  HIS E O   1 
ATOM   13594 C  CB  . HIS E 2 475  ? 97.292  134.366 146.283 1.00 146.51 ? 133  HIS E CB  1 
ATOM   13595 C  CG  . HIS E 2 475  ? 96.777  135.673 145.770 1.00 159.29 ? 133  HIS E CG  1 
ATOM   13596 N  ND1 . HIS E 2 475  ? 97.376  136.356 144.733 1.00 157.72 ? 133  HIS E ND1 1 
ATOM   13597 C  CD2 . HIS E 2 475  ? 95.729  136.433 146.166 1.00 160.20 ? 133  HIS E CD2 1 
ATOM   13598 C  CE1 . HIS E 2 475  ? 96.712  137.475 144.506 1.00 162.26 ? 133  HIS E CE1 1 
ATOM   13599 N  NE2 . HIS E 2 475  ? 95.709  137.546 145.362 1.00 166.26 ? 133  HIS E NE2 1 
ATOM   13600 N  N   . LEU E 2 476  ? 98.035  131.972 148.264 1.00 146.63 ? 134  LEU E N   1 
ATOM   13601 C  CA  . LEU E 2 476  ? 97.968  130.526 148.475 1.00 144.16 ? 134  LEU E CA  1 
ATOM   13602 C  C   . LEU E 2 476  ? 97.318  130.179 149.811 1.00 147.77 ? 134  LEU E C   1 
ATOM   13603 O  O   . LEU E 2 476  ? 96.358  129.402 149.861 1.00 139.30 ? 134  LEU E O   1 
ATOM   13604 C  CB  . LEU E 2 476  ? 99.375  129.933 148.414 1.00 126.87 ? 134  LEU E CB  1 
ATOM   13605 C  CG  . LEU E 2 476  ? 99.940  129.441 147.084 1.00 124.41 ? 134  LEU E CG  1 
ATOM   13606 C  CD1 . LEU E 2 476  ? 99.924  130.553 146.055 1.00 141.23 ? 134  LEU E CD1 1 
ATOM   13607 C  CD2 . LEU E 2 476  ? 101.362 128.950 147.301 1.00 117.90 ? 134  LEU E CD2 1 
ATOM   13608 N  N   . VAL E 2 477  ? 97.819  130.750 150.900 1.00 160.28 ? 135  VAL E N   1 
ATOM   13609 C  CA  . VAL E 2 477  ? 97.336  130.391 152.228 1.00 175.18 ? 135  VAL E CA  1 
ATOM   13610 C  C   . VAL E 2 477  ? 96.086  131.191 152.572 1.00 171.56 ? 135  VAL E C   1 
ATOM   13611 O  O   . VAL E 2 477  ? 94.983  130.851 152.143 1.00 154.78 ? 135  VAL E O   1 
ATOM   13612 C  CB  . VAL E 2 477  ? 98.429  130.594 153.293 1.00 170.80 ? 135  VAL E CB  1 
ATOM   13613 C  CG1 . VAL E 2 477  ? 98.706  132.077 153.498 1.00 160.35 ? 135  VAL E CG1 1 
ATOM   13614 C  CG2 . VAL E 2 477  ? 98.030  129.925 154.601 1.00 155.52 ? 135  VAL E CG2 1 
HETATM 13615 ZN ZN  . ZN  F 3 .    ? 127.066 113.319 69.911  1.00 109.52 ? 2001 ZN  A ZN  1 
# 
