data_9C7Y
# 
_entry.id   9C7Y 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   9C7Y         pdb_00009c7y 10.2210/pdb9c7y/pdb 
WWPDB D_1000284831 ?            ?                   
EMDB  EMD-45296    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-08 
# 
_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             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9C7Y 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Structure Of Respiratory Syncytial Virus Polymerase in complex with JNJ-2729' 
_pdbx_database_related.db_id          EMD-45296 
_pdbx_database_related.content_type   'associated EM volume' 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 xyu6@its.jnj.com     Yu  Xiaodi   ?       'principal investigator/group leader' 0000-0001-7520-0646 
4 tjoncker@its.jnj.com Tim Jonckers 'H. M.' 'principal investigator/group leader' 0000-0003-3974-822X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yin, Y.'      1 0000-0001-9310-1094 
'Tran, M.T.'   2 0009-0009-8047-9333 
'Yu, X.'       3 0000-0001-7520-0646 
'Jonckers, T.' 4 0000-0003-3974-822X 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Med.Chem.Lett.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1948-5875 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                1549 
_citation.page_last                 1558 
_citation.title                     
'Structure-Activity Relationship of Oxacyclo- and Triazolo-Containing Respiratory Syncytial Virus Polymerase Inhibitors.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsmedchemlett.4c00272 
_citation.pdbx_database_id_PubMed   39291020 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Tran, M.T.'       1  0009-0009-8047-9333 
primary 'Grosse, S.'       2  ?                   
primary 'Carbajo, R.J.'    3  ?                   
primary 'Jacoby, E.'       4  ?                   
primary 'Yin, Y.'          5  ?                   
primary 'Yu, X.'           6  ?                   
primary 'Martinez, C.'     7  ?                   
primary 'Stoops, B.'       8  ?                   
primary 'Cooymans, L.'     9  ?                   
primary 'Hu, L.'           10 ?                   
primary 'Lutter, F.H.'     11 ?                   
primary 'Pieters, S.'      12 ?                   
primary 'Tan, E.'          13 ?                   
primary 'Alcazar, J.'      14 ?                   
primary 'Roymans, D.'      15 ?                   
primary 'van Vlijmen, H.'  16 0000-0002-1915-3141 
primary 'Rigaux, P.'       17 ?                   
primary 'Sharma, S.'       18 ?                   
primary 'Jonckers, T.H.M.' 19 0000-0003-3974-822X 
# 
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' 254482.750 1 2.7.7.48,2.1.1.56,2.7.7.-,2.7.7.88 ? ? ? 
2 polymer     man Phosphoprotein 29062.895  4 ?                                  ? ? ? 
3 non-polymer syn 
;(2S)-1,1,1-trifluoro-2-[5-fluoro-6-(4-fluorophenyl)-4-(2-hydroxypropan-2-yl)pyridin-2-yl]-3-[(4M)-4-(8-methoxyquinolin-6-yl)-1H-1,2,3-triazol-1-yl]propan-2-ol
;
585.525    1 ?                                  ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Protein L,Large structural protein,Replicase,Transcriptase' 
2 'Protein P'                                                  
# 
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 
;MGSWSHPQFEKGSGSGSSWSHPQFEKGSGSLVPRGSMDPIINGNSANVYLTDSYLKGVISFSECNALGSYIFNGPYLKND
YTNLISRQNPLIEHMNLKKLNITQSLISKYHKGEIKLEEPTYFQSLLMTYKSMTSSEQIATTNLLKKIIRRAIEISDVKV
YAILNKLGLKEKDKIKSNNGQDEDNSVITTIIKDDILSAVKDNQSHLKADKNHSTKQKDTIKTTLLKKLMCSMQHPPSWL
IHWFNLYTKLNNILTQYRSNEVKNHGFTLIDNQTLSGFQFILNQYGCIVYHKELKRITVTTYNQFLTWKDISLSRLNVCL
ITWISNCLNTLNKSLGLRCGFNNVILTQLFLYGDCILKLFHNEGFYIIKEVEGFIMSLILNITEEDQFRKRFYNSMLNNI
TDAANKAQKNLLSRVCHTLLDKTVSDNIINGRWIILLSKFLKLIKLAGDNNLNNLSELYFLFRIFGHPMVDERQAMDAVK
INCNETKFYLLSSLSMLRGAFIYRIIKGFVNNYNRWPTLRNAIVLPLRWLTYYKLNTYPSLLELTERDLIVLSGLRFYRE
FRLPKKVDLEMIINDKAISPPKNLIWTSFPRNYMPSHIQNYIEHEKLKFSESDKSRRVLEYYLRDNKFNECDLYNCVVNQ
SYLNNPNHVVSLTGKERELSVGRMFAMQPGMFRQVQILAEKMIAENILQFFPESLTRYGDLELQKILELKAGISNKSNRY
NDNYNNYISKCSIITDLSKFNQAFRYETSCICSDVLDELHGVQSLFSWLHLTIPHVTIICTYRHAPPYIGDHIVDLNNVD
EQSGLYRYHMGGIEGWCQKLWTIEAISLLDLISLKGKFSITALINGDNQSIDISKPIRLMEGQTHAQADYLLALNSLKLL
YKEYAGIGHKLKGTETYISRDMQFMSKTIQHNGVYYPASIKKVLRVGPWINTILDDFKVSLESIGSLTQELEYRGESLLC
SLIFRNVWLYNQIALQLKNHALCNNKLYLDILKVLKHLKTFFNLDNIDTALTLYMNLPMLFGGGDPNLLYRSFYRRTPDF
LTEAIVHSVFILSYYTNHDLKDKLQDLSDDRLNKFLTCIITFDKNPNAEFVTLMRDPQALGSERQAKITSEINRLAVTEV
LSTAPNKIFSKSAQHYTTTEIDLNDIMQNIEPTYPHGLRVVYESLPFYKAEKIVNLISGTKSITNILEKTSAIDLTDIDR
ATEMMRKNITLLIRILPLDCNRDKREILSMENLSITELSKYVRERSWSLSNIVGVTSPSIMYTMDIKYTTSTISSGIIIE
KYNVNSLTRGERGPTKPWVGSSTQEKKTMPVYNRQVLTKKQRDQIDLLAKLDWVYASIDNKDEFMEELSIGTLGLTYEKA
KKLFPQYLSVNYLHRLTVSSRPCEFPASIPAYRTTNYHFDTSPINRILTEKYGDEDIDIVFQNCISFGLSLMSVVEQFTN
VCPNRIILIPKLNEIHLMKPPIFTGDVDIHKLKQVIQKQHMFLPDKISLTQYVELFLSNKTLKSGSHVNSNLILAHKISD
YFHNTYILSTNLAGHWILIIQLMKDSKGIFEKDWGEGYITDHMFINLKVFFNAYKTYLLCFHKGYGKAKLECDMNTSDLL
CVLELIDSSYWKSMSKVFLEQKVIKYILSQDASLHRVKGCHSFKLWFLKRLNVAEFTVCPWVVNIDYHPTHMKAILTYID
LVRMGLINIDRIHIKNKHKFNDEFYTSNLFYINYNFSDNTHLLTKHIRIANSELENNYNKLYHPTPETLENILANPIKSN
DKKTLNDYCIGKNVDSIMLPLLSNKKLIKSSAMIRTNYSKQDLYNLFPMVVIDRIIDHSGNTAKSNQLYTTTSHQISLVH
NSTSLYCMLPWHHINRFNFVFSSTGCKISIEYILKDLKIKDPNCIAFIGEGAGNLLLRTVVELHPDIRYIYRSLKDCNDH
SLPIEFLRLYNGHINIDYGENLTIPATDATNNIHWSYLHIKFAEPISLFVCDAELSVTVNWSKIIIEWSKHVRKCKYCSS
VNKCMLIVKYHAQDDIDFKLDNITILKTYVCLGSKLKGSEVYLVLTIGPANIFPVFNVVQNAKLILSRTKNFIMPKKADK
ESIDANIKSLIPFLCYPITKKGINTALSKLKSVVSGDILSYSIAGRNEVFSNKLINHKHMNILKWFNHVLNFRSTELNYN
HLYMVESTYPYLSELLNSLTTNELKKLIKITGSLLYNFHNE
;
;MGSWSHPQFEKGSGSGSSWSHPQFEKGSGSLVPRGSMDPIINGNSANVYLTDSYLKGVISFSECNALGSYIFNGPYLKND
YTNLISRQNPLIEHMNLKKLNITQSLISKYHKGEIKLEEPTYFQSLLMTYKSMTSSEQIATTNLLKKIIRRAIEISDVKV
YAILNKLGLKEKDKIKSNNGQDEDNSVITTIIKDDILSAVKDNQSHLKADKNHSTKQKDTIKTTLLKKLMCSMQHPPSWL
IHWFNLYTKLNNILTQYRSNEVKNHGFTLIDNQTLSGFQFILNQYGCIVYHKELKRITVTTYNQFLTWKDISLSRLNVCL
ITWISNCLNTLNKSLGLRCGFNNVILTQLFLYGDCILKLFHNEGFYIIKEVEGFIMSLILNITEEDQFRKRFYNSMLNNI
TDAANKAQKNLLSRVCHTLLDKTVSDNIINGRWIILLSKFLKLIKLAGDNNLNNLSELYFLFRIFGHPMVDERQAMDAVK
INCNETKFYLLSSLSMLRGAFIYRIIKGFVNNYNRWPTLRNAIVLPLRWLTYYKLNTYPSLLELTERDLIVLSGLRFYRE
FRLPKKVDLEMIINDKAISPPKNLIWTSFPRNYMPSHIQNYIEHEKLKFSESDKSRRVLEYYLRDNKFNECDLYNCVVNQ
SYLNNPNHVVSLTGKERELSVGRMFAMQPGMFRQVQILAEKMIAENILQFFPESLTRYGDLELQKILELKAGISNKSNRY
NDNYNNYISKCSIITDLSKFNQAFRYETSCICSDVLDELHGVQSLFSWLHLTIPHVTIICTYRHAPPYIGDHIVDLNNVD
EQSGLYRYHMGGIEGWCQKLWTIEAISLLDLISLKGKFSITALINGDNQSIDISKPIRLMEGQTHAQADYLLALNSLKLL
YKEYAGIGHKLKGTETYISRDMQFMSKTIQHNGVYYPASIKKVLRVGPWINTILDDFKVSLESIGSLTQELEYRGESLLC
SLIFRNVWLYNQIALQLKNHALCNNKLYLDILKVLKHLKTFFNLDNIDTALTLYMNLPMLFGGGDPNLLYRSFYRRTPDF
LTEAIVHSVFILSYYTNHDLKDKLQDLSDDRLNKFLTCIITFDKNPNAEFVTLMRDPQALGSERQAKITSEINRLAVTEV
LSTAPNKIFSKSAQHYTTTEIDLNDIMQNIEPTYPHGLRVVYESLPFYKAEKIVNLISGTKSITNILEKTSAIDLTDIDR
ATEMMRKNITLLIRILPLDCNRDKREILSMENLSITELSKYVRERSWSLSNIVGVTSPSIMYTMDIKYTTSTISSGIIIE
KYNVNSLTRGERGPTKPWVGSSTQEKKTMPVYNRQVLTKKQRDQIDLLAKLDWVYASIDNKDEFMEELSIGTLGLTYEKA
KKLFPQYLSVNYLHRLTVSSRPCEFPASIPAYRTTNYHFDTSPINRILTEKYGDEDIDIVFQNCISFGLSLMSVVEQFTN
VCPNRIILIPKLNEIHLMKPPIFTGDVDIHKLKQVIQKQHMFLPDKISLTQYVELFLSNKTLKSGSHVNSNLILAHKISD
YFHNTYILSTNLAGHWILIIQLMKDSKGIFEKDWGEGYITDHMFINLKVFFNAYKTYLLCFHKGYGKAKLECDMNTSDLL
CVLELIDSSYWKSMSKVFLEQKVIKYILSQDASLHRVKGCHSFKLWFLKRLNVAEFTVCPWVVNIDYHPTHMKAILTYID
LVRMGLINIDRIHIKNKHKFNDEFYTSNLFYINYNFSDNTHLLTKHIRIANSELENNYNKLYHPTPETLENILANPIKSN
DKKTLNDYCIGKNVDSIMLPLLSNKKLIKSSAMIRTNYSKQDLYNLFPMVVIDRIIDHSGNTAKSNQLYTTTSHQISLVH
NSTSLYCMLPWHHINRFNFVFSSTGCKISIEYILKDLKIKDPNCIAFIGEGAGNLLLRTVVELHPDIRYIYRSLKDCNDH
SLPIEFLRLYNGHINIDYGENLTIPATDATNNIHWSYLHIKFAEPISLFVCDAELSVTVNWSKIIIEWSKHVRKCKYCSS
VNKCMLIVKYHAQDDIDFKLDNITILKTYVCLGSKLKGSEVYLVLTIGPANIFPVFNVVQNAKLILSRTKNFIMPKKADK
ESIDANIKSLIPFLCYPITKKGINTALSKLKSVVSGDILSYSIAGRNEVFSNKLINHKHMNILKWFNHVLNFRSTELNYN
HLYMVESTYPYLSELLNSLTTNELKKLIKITGSLLYNFHNE
;
A       ? 
2 'polypeptide(L)' no no 
;MEKFAPEFHGEDANNRATKFLESIKGKFTSPKDPKKKDSIISVNSIDIEVTKESPITSNSTIINPTNETDDTAGNKPNYQ
RKPLVSFKEDPTPSDNPFSKLYKETIETFDNNEEESSYSYEEINDQTNDNITARLDRIDEKLSEILGMLHTLVVASAGPT
SARDGIRDAMIGLREEMIEKIRTEALMTNDRLEAMARLRNEESEKMAKDTSDEVSLNPTSEKLNNLLEGNDSDNDLSLED
FKGENKYFQGHHHHHH
;
;MEKFAPEFHGEDANNRATKFLESIKGKFTSPKDPKKKDSIISVNSIDIEVTKESPITSNSTIINPTNETDDTAGNKPNYQ
RKPLVSFKEDPTPSDNPFSKLYKETIETFDNNEEESSYSYEEINDQTNDNITARLDRIDEKLSEILGMLHTLVVASAGPT
SARDGIRDAMIGLREEMIEKIRTEALMTNDRLEAMARLRNEESEKMAKDTSDEVSLNPTSEKLNNLLEGNDSDNDLSLED
FKGENKYFQGHHHHHH
;
B,C,D,E ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        
;(2S)-1,1,1-trifluoro-2-[5-fluoro-6-(4-fluorophenyl)-4-(2-hydroxypropan-2-yl)pyridin-2-yl]-3-[(4M)-4-(8-methoxyquinolin-6-yl)-1H-1,2,3-triazol-1-yl]propan-2-ol
;
_pdbx_entity_nonpoly.comp_id     A1AWZ 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    GLY n 
1 3    SER n 
1 4    TRP n 
1 5    SER n 
1 6    HIS n 
1 7    PRO n 
1 8    GLN n 
1 9    PHE n 
1 10   GLU n 
1 11   LYS n 
1 12   GLY n 
1 13   SER n 
1 14   GLY n 
1 15   SER n 
1 16   GLY n 
1 17   SER n 
1 18   SER n 
1 19   TRP n 
1 20   SER n 
1 21   HIS n 
1 22   PRO n 
1 23   GLN n 
1 24   PHE n 
1 25   GLU n 
1 26   LYS n 
1 27   GLY n 
1 28   SER n 
1 29   GLY n 
1 30   SER n 
1 31   LEU n 
1 32   VAL n 
1 33   PRO n 
1 34   ARG n 
1 35   GLY n 
1 36   SER n 
1 37   MET n 
1 38   ASP n 
1 39   PRO n 
1 40   ILE n 
1 41   ILE n 
1 42   ASN n 
1 43   GLY n 
1 44   ASN n 
1 45   SER n 
1 46   ALA n 
1 47   ASN n 
1 48   VAL n 
1 49   TYR n 
1 50   LEU n 
1 51   THR n 
1 52   ASP n 
1 53   SER n 
1 54   TYR n 
1 55   LEU n 
1 56   LYS n 
1 57   GLY n 
1 58   VAL n 
1 59   ILE n 
1 60   SER n 
1 61   PHE n 
1 62   SER n 
1 63   GLU n 
1 64   CYS n 
1 65   ASN n 
1 66   ALA n 
1 67   LEU n 
1 68   GLY n 
1 69   SER n 
1 70   TYR n 
1 71   ILE n 
1 72   PHE n 
1 73   ASN n 
1 74   GLY n 
1 75   PRO n 
1 76   TYR n 
1 77   LEU n 
1 78   LYS n 
1 79   ASN n 
1 80   ASP n 
1 81   TYR n 
1 82   THR n 
1 83   ASN n 
1 84   LEU n 
1 85   ILE n 
1 86   SER n 
1 87   ARG n 
1 88   GLN n 
1 89   ASN n 
1 90   PRO n 
1 91   LEU n 
1 92   ILE n 
1 93   GLU n 
1 94   HIS n 
1 95   MET n 
1 96   ASN n 
1 97   LEU n 
1 98   LYS n 
1 99   LYS n 
1 100  LEU n 
1 101  ASN n 
1 102  ILE n 
1 103  THR n 
1 104  GLN n 
1 105  SER n 
1 106  LEU n 
1 107  ILE n 
1 108  SER n 
1 109  LYS n 
1 110  TYR n 
1 111  HIS n 
1 112  LYS n 
1 113  GLY n 
1 114  GLU n 
1 115  ILE n 
1 116  LYS n 
1 117  LEU n 
1 118  GLU n 
1 119  GLU n 
1 120  PRO n 
1 121  THR n 
1 122  TYR n 
1 123  PHE n 
1 124  GLN n 
1 125  SER n 
1 126  LEU n 
1 127  LEU n 
1 128  MET n 
1 129  THR n 
1 130  TYR n 
1 131  LYS n 
1 132  SER n 
1 133  MET n 
1 134  THR n 
1 135  SER n 
1 136  SER n 
1 137  GLU n 
1 138  GLN n 
1 139  ILE n 
1 140  ALA n 
1 141  THR n 
1 142  THR n 
1 143  ASN n 
1 144  LEU n 
1 145  LEU n 
1 146  LYS n 
1 147  LYS n 
1 148  ILE n 
1 149  ILE n 
1 150  ARG n 
1 151  ARG n 
1 152  ALA n 
1 153  ILE n 
1 154  GLU n 
1 155  ILE n 
1 156  SER n 
1 157  ASP n 
1 158  VAL n 
1 159  LYS n 
1 160  VAL n 
1 161  TYR n 
1 162  ALA n 
1 163  ILE n 
1 164  LEU n 
1 165  ASN n 
1 166  LYS n 
1 167  LEU n 
1 168  GLY n 
1 169  LEU n 
1 170  LYS n 
1 171  GLU n 
1 172  LYS n 
1 173  ASP n 
1 174  LYS n 
1 175  ILE n 
1 176  LYS n 
1 177  SER n 
1 178  ASN n 
1 179  ASN n 
1 180  GLY n 
1 181  GLN n 
1 182  ASP n 
1 183  GLU n 
1 184  ASP n 
1 185  ASN n 
1 186  SER n 
1 187  VAL n 
1 188  ILE n 
1 189  THR n 
1 190  THR n 
1 191  ILE n 
1 192  ILE n 
1 193  LYS n 
1 194  ASP n 
1 195  ASP n 
1 196  ILE n 
1 197  LEU n 
1 198  SER n 
1 199  ALA n 
1 200  VAL n 
1 201  LYS n 
1 202  ASP n 
1 203  ASN n 
1 204  GLN n 
1 205  SER n 
1 206  HIS n 
1 207  LEU n 
1 208  LYS n 
1 209  ALA n 
1 210  ASP n 
1 211  LYS n 
1 212  ASN n 
1 213  HIS n 
1 214  SER n 
1 215  THR n 
1 216  LYS n 
1 217  GLN n 
1 218  LYS n 
1 219  ASP n 
1 220  THR n 
1 221  ILE n 
1 222  LYS n 
1 223  THR n 
1 224  THR n 
1 225  LEU n 
1 226  LEU n 
1 227  LYS n 
1 228  LYS n 
1 229  LEU n 
1 230  MET n 
1 231  CYS n 
1 232  SER n 
1 233  MET n 
1 234  GLN n 
1 235  HIS n 
1 236  PRO n 
1 237  PRO n 
1 238  SER n 
1 239  TRP n 
1 240  LEU n 
1 241  ILE n 
1 242  HIS n 
1 243  TRP n 
1 244  PHE n 
1 245  ASN n 
1 246  LEU n 
1 247  TYR n 
1 248  THR n 
1 249  LYS n 
1 250  LEU n 
1 251  ASN n 
1 252  ASN n 
1 253  ILE n 
1 254  LEU n 
1 255  THR n 
1 256  GLN n 
1 257  TYR n 
1 258  ARG n 
1 259  SER n 
1 260  ASN n 
1 261  GLU n 
1 262  VAL n 
1 263  LYS n 
1 264  ASN n 
1 265  HIS n 
1 266  GLY n 
1 267  PHE n 
1 268  THR n 
1 269  LEU n 
1 270  ILE n 
1 271  ASP n 
1 272  ASN n 
1 273  GLN n 
1 274  THR n 
1 275  LEU n 
1 276  SER n 
1 277  GLY n 
1 278  PHE n 
1 279  GLN n 
1 280  PHE n 
1 281  ILE n 
1 282  LEU n 
1 283  ASN n 
1 284  GLN n 
1 285  TYR n 
1 286  GLY n 
1 287  CYS n 
1 288  ILE n 
1 289  VAL n 
1 290  TYR n 
1 291  HIS n 
1 292  LYS n 
1 293  GLU n 
1 294  LEU n 
1 295  LYS n 
1 296  ARG n 
1 297  ILE n 
1 298  THR n 
1 299  VAL n 
1 300  THR n 
1 301  THR n 
1 302  TYR n 
1 303  ASN n 
1 304  GLN n 
1 305  PHE n 
1 306  LEU n 
1 307  THR n 
1 308  TRP n 
1 309  LYS n 
1 310  ASP n 
1 311  ILE n 
1 312  SER n 
1 313  LEU n 
1 314  SER n 
1 315  ARG n 
1 316  LEU n 
1 317  ASN n 
1 318  VAL n 
1 319  CYS n 
1 320  LEU n 
1 321  ILE n 
1 322  THR n 
1 323  TRP n 
1 324  ILE n 
1 325  SER n 
1 326  ASN n 
1 327  CYS n 
1 328  LEU n 
1 329  ASN n 
1 330  THR n 
1 331  LEU n 
1 332  ASN n 
1 333  LYS n 
1 334  SER n 
1 335  LEU n 
1 336  GLY n 
1 337  LEU n 
1 338  ARG n 
1 339  CYS n 
1 340  GLY n 
1 341  PHE n 
1 342  ASN n 
1 343  ASN n 
1 344  VAL n 
1 345  ILE n 
1 346  LEU n 
1 347  THR n 
1 348  GLN n 
1 349  LEU n 
1 350  PHE n 
1 351  LEU n 
1 352  TYR n 
1 353  GLY n 
1 354  ASP n 
1 355  CYS n 
1 356  ILE n 
1 357  LEU n 
1 358  LYS n 
1 359  LEU n 
1 360  PHE n 
1 361  HIS n 
1 362  ASN n 
1 363  GLU n 
1 364  GLY n 
1 365  PHE n 
1 366  TYR n 
1 367  ILE n 
1 368  ILE n 
1 369  LYS n 
1 370  GLU n 
1 371  VAL n 
1 372  GLU n 
1 373  GLY n 
1 374  PHE n 
1 375  ILE n 
1 376  MET n 
1 377  SER n 
1 378  LEU n 
1 379  ILE n 
1 380  LEU n 
1 381  ASN n 
1 382  ILE n 
1 383  THR n 
1 384  GLU n 
1 385  GLU n 
1 386  ASP n 
1 387  GLN n 
1 388  PHE n 
1 389  ARG n 
1 390  LYS n 
1 391  ARG n 
1 392  PHE n 
1 393  TYR n 
1 394  ASN n 
1 395  SER n 
1 396  MET n 
1 397  LEU n 
1 398  ASN n 
1 399  ASN n 
1 400  ILE n 
1 401  THR n 
1 402  ASP n 
1 403  ALA n 
1 404  ALA n 
1 405  ASN n 
1 406  LYS n 
1 407  ALA n 
1 408  GLN n 
1 409  LYS n 
1 410  ASN n 
1 411  LEU n 
1 412  LEU n 
1 413  SER n 
1 414  ARG n 
1 415  VAL n 
1 416  CYS n 
1 417  HIS n 
1 418  THR n 
1 419  LEU n 
1 420  LEU n 
1 421  ASP n 
1 422  LYS n 
1 423  THR n 
1 424  VAL n 
1 425  SER n 
1 426  ASP n 
1 427  ASN n 
1 428  ILE n 
1 429  ILE n 
1 430  ASN n 
1 431  GLY n 
1 432  ARG n 
1 433  TRP n 
1 434  ILE n 
1 435  ILE n 
1 436  LEU n 
1 437  LEU n 
1 438  SER n 
1 439  LYS n 
1 440  PHE n 
1 441  LEU n 
1 442  LYS n 
1 443  LEU n 
1 444  ILE n 
1 445  LYS n 
1 446  LEU n 
1 447  ALA n 
1 448  GLY n 
1 449  ASP n 
1 450  ASN n 
1 451  ASN n 
1 452  LEU n 
1 453  ASN n 
1 454  ASN n 
1 455  LEU n 
1 456  SER n 
1 457  GLU n 
1 458  LEU n 
1 459  TYR n 
1 460  PHE n 
1 461  LEU n 
1 462  PHE n 
1 463  ARG n 
1 464  ILE n 
1 465  PHE n 
1 466  GLY n 
1 467  HIS n 
1 468  PRO n 
1 469  MET n 
1 470  VAL n 
1 471  ASP n 
1 472  GLU n 
1 473  ARG n 
1 474  GLN n 
1 475  ALA n 
1 476  MET n 
1 477  ASP n 
1 478  ALA n 
1 479  VAL n 
1 480  LYS n 
1 481  ILE n 
1 482  ASN n 
1 483  CYS n 
1 484  ASN n 
1 485  GLU n 
1 486  THR n 
1 487  LYS n 
1 488  PHE n 
1 489  TYR n 
1 490  LEU n 
1 491  LEU n 
1 492  SER n 
1 493  SER n 
1 494  LEU n 
1 495  SER n 
1 496  MET n 
1 497  LEU n 
1 498  ARG n 
1 499  GLY n 
1 500  ALA n 
1 501  PHE n 
1 502  ILE n 
1 503  TYR n 
1 504  ARG n 
1 505  ILE n 
1 506  ILE n 
1 507  LYS n 
1 508  GLY n 
1 509  PHE n 
1 510  VAL n 
1 511  ASN n 
1 512  ASN n 
1 513  TYR n 
1 514  ASN n 
1 515  ARG n 
1 516  TRP n 
1 517  PRO n 
1 518  THR n 
1 519  LEU n 
1 520  ARG n 
1 521  ASN n 
1 522  ALA n 
1 523  ILE n 
1 524  VAL n 
1 525  LEU n 
1 526  PRO n 
1 527  LEU n 
1 528  ARG n 
1 529  TRP n 
1 530  LEU n 
1 531  THR n 
1 532  TYR n 
1 533  TYR n 
1 534  LYS n 
1 535  LEU n 
1 536  ASN n 
1 537  THR n 
1 538  TYR n 
1 539  PRO n 
1 540  SER n 
1 541  LEU n 
1 542  LEU n 
1 543  GLU n 
1 544  LEU n 
1 545  THR n 
1 546  GLU n 
1 547  ARG n 
1 548  ASP n 
1 549  LEU n 
1 550  ILE n 
1 551  VAL n 
1 552  LEU n 
1 553  SER n 
1 554  GLY n 
1 555  LEU n 
1 556  ARG n 
1 557  PHE n 
1 558  TYR n 
1 559  ARG n 
1 560  GLU n 
1 561  PHE n 
1 562  ARG n 
1 563  LEU n 
1 564  PRO n 
1 565  LYS n 
1 566  LYS n 
1 567  VAL n 
1 568  ASP n 
1 569  LEU n 
1 570  GLU n 
1 571  MET n 
1 572  ILE n 
1 573  ILE n 
1 574  ASN n 
1 575  ASP n 
1 576  LYS n 
1 577  ALA n 
1 578  ILE n 
1 579  SER n 
1 580  PRO n 
1 581  PRO n 
1 582  LYS n 
1 583  ASN n 
1 584  LEU n 
1 585  ILE n 
1 586  TRP n 
1 587  THR n 
1 588  SER n 
1 589  PHE n 
1 590  PRO n 
1 591  ARG n 
1 592  ASN n 
1 593  TYR n 
1 594  MET n 
1 595  PRO n 
1 596  SER n 
1 597  HIS n 
1 598  ILE n 
1 599  GLN n 
1 600  ASN n 
1 601  TYR n 
1 602  ILE n 
1 603  GLU n 
1 604  HIS n 
1 605  GLU n 
1 606  LYS n 
1 607  LEU n 
1 608  LYS n 
1 609  PHE n 
1 610  SER n 
1 611  GLU n 
1 612  SER n 
1 613  ASP n 
1 614  LYS n 
1 615  SER n 
1 616  ARG n 
1 617  ARG n 
1 618  VAL n 
1 619  LEU n 
1 620  GLU n 
1 621  TYR n 
1 622  TYR n 
1 623  LEU n 
1 624  ARG n 
1 625  ASP n 
1 626  ASN n 
1 627  LYS n 
1 628  PHE n 
1 629  ASN n 
1 630  GLU n 
1 631  CYS n 
1 632  ASP n 
1 633  LEU n 
1 634  TYR n 
1 635  ASN n 
1 636  CYS n 
1 637  VAL n 
1 638  VAL n 
1 639  ASN n 
1 640  GLN n 
1 641  SER n 
1 642  TYR n 
1 643  LEU n 
1 644  ASN n 
1 645  ASN n 
1 646  PRO n 
1 647  ASN n 
1 648  HIS n 
1 649  VAL n 
1 650  VAL n 
1 651  SER n 
1 652  LEU n 
1 653  THR n 
1 654  GLY n 
1 655  LYS n 
1 656  GLU n 
1 657  ARG n 
1 658  GLU n 
1 659  LEU n 
1 660  SER n 
1 661  VAL n 
1 662  GLY n 
1 663  ARG n 
1 664  MET n 
1 665  PHE n 
1 666  ALA n 
1 667  MET n 
1 668  GLN n 
1 669  PRO n 
1 670  GLY n 
1 671  MET n 
1 672  PHE n 
1 673  ARG n 
1 674  GLN n 
1 675  VAL n 
1 676  GLN n 
1 677  ILE n 
1 678  LEU n 
1 679  ALA n 
1 680  GLU n 
1 681  LYS n 
1 682  MET n 
1 683  ILE n 
1 684  ALA n 
1 685  GLU n 
1 686  ASN n 
1 687  ILE n 
1 688  LEU n 
1 689  GLN n 
1 690  PHE n 
1 691  PHE n 
1 692  PRO n 
1 693  GLU n 
1 694  SER n 
1 695  LEU n 
1 696  THR n 
1 697  ARG n 
1 698  TYR n 
1 699  GLY n 
1 700  ASP n 
1 701  LEU n 
1 702  GLU n 
1 703  LEU n 
1 704  GLN n 
1 705  LYS n 
1 706  ILE n 
1 707  LEU n 
1 708  GLU n 
1 709  LEU n 
1 710  LYS n 
1 711  ALA n 
1 712  GLY n 
1 713  ILE n 
1 714  SER n 
1 715  ASN n 
1 716  LYS n 
1 717  SER n 
1 718  ASN n 
1 719  ARG n 
1 720  TYR n 
1 721  ASN n 
1 722  ASP n 
1 723  ASN n 
1 724  TYR n 
1 725  ASN n 
1 726  ASN n 
1 727  TYR n 
1 728  ILE n 
1 729  SER n 
1 730  LYS n 
1 731  CYS n 
1 732  SER n 
1 733  ILE n 
1 734  ILE n 
1 735  THR n 
1 736  ASP n 
1 737  LEU n 
1 738  SER n 
1 739  LYS n 
1 740  PHE n 
1 741  ASN n 
1 742  GLN n 
1 743  ALA n 
1 744  PHE n 
1 745  ARG n 
1 746  TYR n 
1 747  GLU n 
1 748  THR n 
1 749  SER n 
1 750  CYS n 
1 751  ILE n 
1 752  CYS n 
1 753  SER n 
1 754  ASP n 
1 755  VAL n 
1 756  LEU n 
1 757  ASP n 
1 758  GLU n 
1 759  LEU n 
1 760  HIS n 
1 761  GLY n 
1 762  VAL n 
1 763  GLN n 
1 764  SER n 
1 765  LEU n 
1 766  PHE n 
1 767  SER n 
1 768  TRP n 
1 769  LEU n 
1 770  HIS n 
1 771  LEU n 
1 772  THR n 
1 773  ILE n 
1 774  PRO n 
1 775  HIS n 
1 776  VAL n 
1 777  THR n 
1 778  ILE n 
1 779  ILE n 
1 780  CYS n 
1 781  THR n 
1 782  TYR n 
1 783  ARG n 
1 784  HIS n 
1 785  ALA n 
1 786  PRO n 
1 787  PRO n 
1 788  TYR n 
1 789  ILE n 
1 790  GLY n 
1 791  ASP n 
1 792  HIS n 
1 793  ILE n 
1 794  VAL n 
1 795  ASP n 
1 796  LEU n 
1 797  ASN n 
1 798  ASN n 
1 799  VAL n 
1 800  ASP n 
1 801  GLU n 
1 802  GLN n 
1 803  SER n 
1 804  GLY n 
1 805  LEU n 
1 806  TYR n 
1 807  ARG n 
1 808  TYR n 
1 809  HIS n 
1 810  MET n 
1 811  GLY n 
1 812  GLY n 
1 813  ILE n 
1 814  GLU n 
1 815  GLY n 
1 816  TRP n 
1 817  CYS n 
1 818  GLN n 
1 819  LYS n 
1 820  LEU n 
1 821  TRP n 
1 822  THR n 
1 823  ILE n 
1 824  GLU n 
1 825  ALA n 
1 826  ILE n 
1 827  SER n 
1 828  LEU n 
1 829  LEU n 
1 830  ASP n 
1 831  LEU n 
1 832  ILE n 
1 833  SER n 
1 834  LEU n 
1 835  LYS n 
1 836  GLY n 
1 837  LYS n 
1 838  PHE n 
1 839  SER n 
1 840  ILE n 
1 841  THR n 
1 842  ALA n 
1 843  LEU n 
1 844  ILE n 
1 845  ASN n 
1 846  GLY n 
1 847  ASP n 
1 848  ASN n 
1 849  GLN n 
1 850  SER n 
1 851  ILE n 
1 852  ASP n 
1 853  ILE n 
1 854  SER n 
1 855  LYS n 
1 856  PRO n 
1 857  ILE n 
1 858  ARG n 
1 859  LEU n 
1 860  MET n 
1 861  GLU n 
1 862  GLY n 
1 863  GLN n 
1 864  THR n 
1 865  HIS n 
1 866  ALA n 
1 867  GLN n 
1 868  ALA n 
1 869  ASP n 
1 870  TYR n 
1 871  LEU n 
1 872  LEU n 
1 873  ALA n 
1 874  LEU n 
1 875  ASN n 
1 876  SER n 
1 877  LEU n 
1 878  LYS n 
1 879  LEU n 
1 880  LEU n 
1 881  TYR n 
1 882  LYS n 
1 883  GLU n 
1 884  TYR n 
1 885  ALA n 
1 886  GLY n 
1 887  ILE n 
1 888  GLY n 
1 889  HIS n 
1 890  LYS n 
1 891  LEU n 
1 892  LYS n 
1 893  GLY n 
1 894  THR n 
1 895  GLU n 
1 896  THR n 
1 897  TYR n 
1 898  ILE n 
1 899  SER n 
1 900  ARG n 
1 901  ASP n 
1 902  MET n 
1 903  GLN n 
1 904  PHE n 
1 905  MET n 
1 906  SER n 
1 907  LYS n 
1 908  THR n 
1 909  ILE n 
1 910  GLN n 
1 911  HIS n 
1 912  ASN n 
1 913  GLY n 
1 914  VAL n 
1 915  TYR n 
1 916  TYR n 
1 917  PRO n 
1 918  ALA n 
1 919  SER n 
1 920  ILE n 
1 921  LYS n 
1 922  LYS n 
1 923  VAL n 
1 924  LEU n 
1 925  ARG n 
1 926  VAL n 
1 927  GLY n 
1 928  PRO n 
1 929  TRP n 
1 930  ILE n 
1 931  ASN n 
1 932  THR n 
1 933  ILE n 
1 934  LEU n 
1 935  ASP n 
1 936  ASP n 
1 937  PHE n 
1 938  LYS n 
1 939  VAL n 
1 940  SER n 
1 941  LEU n 
1 942  GLU n 
1 943  SER n 
1 944  ILE n 
1 945  GLY n 
1 946  SER n 
1 947  LEU n 
1 948  THR n 
1 949  GLN n 
1 950  GLU n 
1 951  LEU n 
1 952  GLU n 
1 953  TYR n 
1 954  ARG n 
1 955  GLY n 
1 956  GLU n 
1 957  SER n 
1 958  LEU n 
1 959  LEU n 
1 960  CYS n 
1 961  SER n 
1 962  LEU n 
1 963  ILE n 
1 964  PHE n 
1 965  ARG n 
1 966  ASN n 
1 967  VAL n 
1 968  TRP n 
1 969  LEU n 
1 970  TYR n 
1 971  ASN n 
1 972  GLN n 
1 973  ILE n 
1 974  ALA n 
1 975  LEU n 
1 976  GLN n 
1 977  LEU n 
1 978  LYS n 
1 979  ASN n 
1 980  HIS n 
1 981  ALA n 
1 982  LEU n 
1 983  CYS n 
1 984  ASN n 
1 985  ASN n 
1 986  LYS n 
1 987  LEU n 
1 988  TYR n 
1 989  LEU n 
1 990  ASP n 
1 991  ILE n 
1 992  LEU n 
1 993  LYS n 
1 994  VAL n 
1 995  LEU n 
1 996  LYS n 
1 997  HIS n 
1 998  LEU n 
1 999  LYS n 
1 1000 THR n 
1 1001 PHE n 
1 1002 PHE n 
1 1003 ASN n 
1 1004 LEU n 
1 1005 ASP n 
1 1006 ASN n 
1 1007 ILE n 
1 1008 ASP n 
1 1009 THR n 
1 1010 ALA n 
1 1011 LEU n 
1 1012 THR n 
1 1013 LEU n 
1 1014 TYR n 
1 1015 MET n 
1 1016 ASN n 
1 1017 LEU n 
1 1018 PRO n 
1 1019 MET n 
1 1020 LEU n 
1 1021 PHE n 
1 1022 GLY n 
1 1023 GLY n 
1 1024 GLY n 
1 1025 ASP n 
1 1026 PRO n 
1 1027 ASN n 
1 1028 LEU n 
1 1029 LEU n 
1 1030 TYR n 
1 1031 ARG n 
1 1032 SER n 
1 1033 PHE n 
1 1034 TYR n 
1 1035 ARG n 
1 1036 ARG n 
1 1037 THR n 
1 1038 PRO n 
1 1039 ASP n 
1 1040 PHE n 
1 1041 LEU n 
1 1042 THR n 
1 1043 GLU n 
1 1044 ALA n 
1 1045 ILE n 
1 1046 VAL n 
1 1047 HIS n 
1 1048 SER n 
1 1049 VAL n 
1 1050 PHE n 
1 1051 ILE n 
1 1052 LEU n 
1 1053 SER n 
1 1054 TYR n 
1 1055 TYR n 
1 1056 THR n 
1 1057 ASN n 
1 1058 HIS n 
1 1059 ASP n 
1 1060 LEU n 
1 1061 LYS n 
1 1062 ASP n 
1 1063 LYS n 
1 1064 LEU n 
1 1065 GLN n 
1 1066 ASP n 
1 1067 LEU n 
1 1068 SER n 
1 1069 ASP n 
1 1070 ASP n 
1 1071 ARG n 
1 1072 LEU n 
1 1073 ASN n 
1 1074 LYS n 
1 1075 PHE n 
1 1076 LEU n 
1 1077 THR n 
1 1078 CYS n 
1 1079 ILE n 
1 1080 ILE n 
1 1081 THR n 
1 1082 PHE n 
1 1083 ASP n 
1 1084 LYS n 
1 1085 ASN n 
1 1086 PRO n 
1 1087 ASN n 
1 1088 ALA n 
1 1089 GLU n 
1 1090 PHE n 
1 1091 VAL n 
1 1092 THR n 
1 1093 LEU n 
1 1094 MET n 
1 1095 ARG n 
1 1096 ASP n 
1 1097 PRO n 
1 1098 GLN n 
1 1099 ALA n 
1 1100 LEU n 
1 1101 GLY n 
1 1102 SER n 
1 1103 GLU n 
1 1104 ARG n 
1 1105 GLN n 
1 1106 ALA n 
1 1107 LYS n 
1 1108 ILE n 
1 1109 THR n 
1 1110 SER n 
1 1111 GLU n 
1 1112 ILE n 
1 1113 ASN n 
1 1114 ARG n 
1 1115 LEU n 
1 1116 ALA n 
1 1117 VAL n 
1 1118 THR n 
1 1119 GLU n 
1 1120 VAL n 
1 1121 LEU n 
1 1122 SER n 
1 1123 THR n 
1 1124 ALA n 
1 1125 PRO n 
1 1126 ASN n 
1 1127 LYS n 
1 1128 ILE n 
1 1129 PHE n 
1 1130 SER n 
1 1131 LYS n 
1 1132 SER n 
1 1133 ALA n 
1 1134 GLN n 
1 1135 HIS n 
1 1136 TYR n 
1 1137 THR n 
1 1138 THR n 
1 1139 THR n 
1 1140 GLU n 
1 1141 ILE n 
1 1142 ASP n 
1 1143 LEU n 
1 1144 ASN n 
1 1145 ASP n 
1 1146 ILE n 
1 1147 MET n 
1 1148 GLN n 
1 1149 ASN n 
1 1150 ILE n 
1 1151 GLU n 
1 1152 PRO n 
1 1153 THR n 
1 1154 TYR n 
1 1155 PRO n 
1 1156 HIS n 
1 1157 GLY n 
1 1158 LEU n 
1 1159 ARG n 
1 1160 VAL n 
1 1161 VAL n 
1 1162 TYR n 
1 1163 GLU n 
1 1164 SER n 
1 1165 LEU n 
1 1166 PRO n 
1 1167 PHE n 
1 1168 TYR n 
1 1169 LYS n 
1 1170 ALA n 
1 1171 GLU n 
1 1172 LYS n 
1 1173 ILE n 
1 1174 VAL n 
1 1175 ASN n 
1 1176 LEU n 
1 1177 ILE n 
1 1178 SER n 
1 1179 GLY n 
1 1180 THR n 
1 1181 LYS n 
1 1182 SER n 
1 1183 ILE n 
1 1184 THR n 
1 1185 ASN n 
1 1186 ILE n 
1 1187 LEU n 
1 1188 GLU n 
1 1189 LYS n 
1 1190 THR n 
1 1191 SER n 
1 1192 ALA n 
1 1193 ILE n 
1 1194 ASP n 
1 1195 LEU n 
1 1196 THR n 
1 1197 ASP n 
1 1198 ILE n 
1 1199 ASP n 
1 1200 ARG n 
1 1201 ALA n 
1 1202 THR n 
1 1203 GLU n 
1 1204 MET n 
1 1205 MET n 
1 1206 ARG n 
1 1207 LYS n 
1 1208 ASN n 
1 1209 ILE n 
1 1210 THR n 
1 1211 LEU n 
1 1212 LEU n 
1 1213 ILE n 
1 1214 ARG n 
1 1215 ILE n 
1 1216 LEU n 
1 1217 PRO n 
1 1218 LEU n 
1 1219 ASP n 
1 1220 CYS n 
1 1221 ASN n 
1 1222 ARG n 
1 1223 ASP n 
1 1224 LYS n 
1 1225 ARG n 
1 1226 GLU n 
1 1227 ILE n 
1 1228 LEU n 
1 1229 SER n 
1 1230 MET n 
1 1231 GLU n 
1 1232 ASN n 
1 1233 LEU n 
1 1234 SER n 
1 1235 ILE n 
1 1236 THR n 
1 1237 GLU n 
1 1238 LEU n 
1 1239 SER n 
1 1240 LYS n 
1 1241 TYR n 
1 1242 VAL n 
1 1243 ARG n 
1 1244 GLU n 
1 1245 ARG n 
1 1246 SER n 
1 1247 TRP n 
1 1248 SER n 
1 1249 LEU n 
1 1250 SER n 
1 1251 ASN n 
1 1252 ILE n 
1 1253 VAL n 
1 1254 GLY n 
1 1255 VAL n 
1 1256 THR n 
1 1257 SER n 
1 1258 PRO n 
1 1259 SER n 
1 1260 ILE n 
1 1261 MET n 
1 1262 TYR n 
1 1263 THR n 
1 1264 MET n 
1 1265 ASP n 
1 1266 ILE n 
1 1267 LYS n 
1 1268 TYR n 
1 1269 THR n 
1 1270 THR n 
1 1271 SER n 
1 1272 THR n 
1 1273 ILE n 
1 1274 SER n 
1 1275 SER n 
1 1276 GLY n 
1 1277 ILE n 
1 1278 ILE n 
1 1279 ILE n 
1 1280 GLU n 
1 1281 LYS n 
1 1282 TYR n 
1 1283 ASN n 
1 1284 VAL n 
1 1285 ASN n 
1 1286 SER n 
1 1287 LEU n 
1 1288 THR n 
1 1289 ARG n 
1 1290 GLY n 
1 1291 GLU n 
1 1292 ARG n 
1 1293 GLY n 
1 1294 PRO n 
1 1295 THR n 
1 1296 LYS n 
1 1297 PRO n 
1 1298 TRP n 
1 1299 VAL n 
1 1300 GLY n 
1 1301 SER n 
1 1302 SER n 
1 1303 THR n 
1 1304 GLN n 
1 1305 GLU n 
1 1306 LYS n 
1 1307 LYS n 
1 1308 THR n 
1 1309 MET n 
1 1310 PRO n 
1 1311 VAL n 
1 1312 TYR n 
1 1313 ASN n 
1 1314 ARG n 
1 1315 GLN n 
1 1316 VAL n 
1 1317 LEU n 
1 1318 THR n 
1 1319 LYS n 
1 1320 LYS n 
1 1321 GLN n 
1 1322 ARG n 
1 1323 ASP n 
1 1324 GLN n 
1 1325 ILE n 
1 1326 ASP n 
1 1327 LEU n 
1 1328 LEU n 
1 1329 ALA n 
1 1330 LYS n 
1 1331 LEU n 
1 1332 ASP n 
1 1333 TRP n 
1 1334 VAL n 
1 1335 TYR n 
1 1336 ALA n 
1 1337 SER n 
1 1338 ILE n 
1 1339 ASP n 
1 1340 ASN n 
1 1341 LYS n 
1 1342 ASP n 
1 1343 GLU n 
1 1344 PHE n 
1 1345 MET n 
1 1346 GLU n 
1 1347 GLU n 
1 1348 LEU n 
1 1349 SER n 
1 1350 ILE n 
1 1351 GLY n 
1 1352 THR n 
1 1353 LEU n 
1 1354 GLY n 
1 1355 LEU n 
1 1356 THR n 
1 1357 TYR n 
1 1358 GLU n 
1 1359 LYS n 
1 1360 ALA n 
1 1361 LYS n 
1 1362 LYS n 
1 1363 LEU n 
1 1364 PHE n 
1 1365 PRO n 
1 1366 GLN n 
1 1367 TYR n 
1 1368 LEU n 
1 1369 SER n 
1 1370 VAL n 
1 1371 ASN n 
1 1372 TYR n 
1 1373 LEU n 
1 1374 HIS n 
1 1375 ARG n 
1 1376 LEU n 
1 1377 THR n 
1 1378 VAL n 
1 1379 SER n 
1 1380 SER n 
1 1381 ARG n 
1 1382 PRO n 
1 1383 CYS n 
1 1384 GLU n 
1 1385 PHE n 
1 1386 PRO n 
1 1387 ALA n 
1 1388 SER n 
1 1389 ILE n 
1 1390 PRO n 
1 1391 ALA n 
1 1392 TYR n 
1 1393 ARG n 
1 1394 THR n 
1 1395 THR n 
1 1396 ASN n 
1 1397 TYR n 
1 1398 HIS n 
1 1399 PHE n 
1 1400 ASP n 
1 1401 THR n 
1 1402 SER n 
1 1403 PRO n 
1 1404 ILE n 
1 1405 ASN n 
1 1406 ARG n 
1 1407 ILE n 
1 1408 LEU n 
1 1409 THR n 
1 1410 GLU n 
1 1411 LYS n 
1 1412 TYR n 
1 1413 GLY n 
1 1414 ASP n 
1 1415 GLU n 
1 1416 ASP n 
1 1417 ILE n 
1 1418 ASP n 
1 1419 ILE n 
1 1420 VAL n 
1 1421 PHE n 
1 1422 GLN n 
1 1423 ASN n 
1 1424 CYS n 
1 1425 ILE n 
1 1426 SER n 
1 1427 PHE n 
1 1428 GLY n 
1 1429 LEU n 
1 1430 SER n 
1 1431 LEU n 
1 1432 MET n 
1 1433 SER n 
1 1434 VAL n 
1 1435 VAL n 
1 1436 GLU n 
1 1437 GLN n 
1 1438 PHE n 
1 1439 THR n 
1 1440 ASN n 
1 1441 VAL n 
1 1442 CYS n 
1 1443 PRO n 
1 1444 ASN n 
1 1445 ARG n 
1 1446 ILE n 
1 1447 ILE n 
1 1448 LEU n 
1 1449 ILE n 
1 1450 PRO n 
1 1451 LYS n 
1 1452 LEU n 
1 1453 ASN n 
1 1454 GLU n 
1 1455 ILE n 
1 1456 HIS n 
1 1457 LEU n 
1 1458 MET n 
1 1459 LYS n 
1 1460 PRO n 
1 1461 PRO n 
1 1462 ILE n 
1 1463 PHE n 
1 1464 THR n 
1 1465 GLY n 
1 1466 ASP n 
1 1467 VAL n 
1 1468 ASP n 
1 1469 ILE n 
1 1470 HIS n 
1 1471 LYS n 
1 1472 LEU n 
1 1473 LYS n 
1 1474 GLN n 
1 1475 VAL n 
1 1476 ILE n 
1 1477 GLN n 
1 1478 LYS n 
1 1479 GLN n 
1 1480 HIS n 
1 1481 MET n 
1 1482 PHE n 
1 1483 LEU n 
1 1484 PRO n 
1 1485 ASP n 
1 1486 LYS n 
1 1487 ILE n 
1 1488 SER n 
1 1489 LEU n 
1 1490 THR n 
1 1491 GLN n 
1 1492 TYR n 
1 1493 VAL n 
1 1494 GLU n 
1 1495 LEU n 
1 1496 PHE n 
1 1497 LEU n 
1 1498 SER n 
1 1499 ASN n 
1 1500 LYS n 
1 1501 THR n 
1 1502 LEU n 
1 1503 LYS n 
1 1504 SER n 
1 1505 GLY n 
1 1506 SER n 
1 1507 HIS n 
1 1508 VAL n 
1 1509 ASN n 
1 1510 SER n 
1 1511 ASN n 
1 1512 LEU n 
1 1513 ILE n 
1 1514 LEU n 
1 1515 ALA n 
1 1516 HIS n 
1 1517 LYS n 
1 1518 ILE n 
1 1519 SER n 
1 1520 ASP n 
1 1521 TYR n 
1 1522 PHE n 
1 1523 HIS n 
1 1524 ASN n 
1 1525 THR n 
1 1526 TYR n 
1 1527 ILE n 
1 1528 LEU n 
1 1529 SER n 
1 1530 THR n 
1 1531 ASN n 
1 1532 LEU n 
1 1533 ALA n 
1 1534 GLY n 
1 1535 HIS n 
1 1536 TRP n 
1 1537 ILE n 
1 1538 LEU n 
1 1539 ILE n 
1 1540 ILE n 
1 1541 GLN n 
1 1542 LEU n 
1 1543 MET n 
1 1544 LYS n 
1 1545 ASP n 
1 1546 SER n 
1 1547 LYS n 
1 1548 GLY n 
1 1549 ILE n 
1 1550 PHE n 
1 1551 GLU n 
1 1552 LYS n 
1 1553 ASP n 
1 1554 TRP n 
1 1555 GLY n 
1 1556 GLU n 
1 1557 GLY n 
1 1558 TYR n 
1 1559 ILE n 
1 1560 THR n 
1 1561 ASP n 
1 1562 HIS n 
1 1563 MET n 
1 1564 PHE n 
1 1565 ILE n 
1 1566 ASN n 
1 1567 LEU n 
1 1568 LYS n 
1 1569 VAL n 
1 1570 PHE n 
1 1571 PHE n 
1 1572 ASN n 
1 1573 ALA n 
1 1574 TYR n 
1 1575 LYS n 
1 1576 THR n 
1 1577 TYR n 
1 1578 LEU n 
1 1579 LEU n 
1 1580 CYS n 
1 1581 PHE n 
1 1582 HIS n 
1 1583 LYS n 
1 1584 GLY n 
1 1585 TYR n 
1 1586 GLY n 
1 1587 LYS n 
1 1588 ALA n 
1 1589 LYS n 
1 1590 LEU n 
1 1591 GLU n 
1 1592 CYS n 
1 1593 ASP n 
1 1594 MET n 
1 1595 ASN n 
1 1596 THR n 
1 1597 SER n 
1 1598 ASP n 
1 1599 LEU n 
1 1600 LEU n 
1 1601 CYS n 
1 1602 VAL n 
1 1603 LEU n 
1 1604 GLU n 
1 1605 LEU n 
1 1606 ILE n 
1 1607 ASP n 
1 1608 SER n 
1 1609 SER n 
1 1610 TYR n 
1 1611 TRP n 
1 1612 LYS n 
1 1613 SER n 
1 1614 MET n 
1 1615 SER n 
1 1616 LYS n 
1 1617 VAL n 
1 1618 PHE n 
1 1619 LEU n 
1 1620 GLU n 
1 1621 GLN n 
1 1622 LYS n 
1 1623 VAL n 
1 1624 ILE n 
1 1625 LYS n 
1 1626 TYR n 
1 1627 ILE n 
1 1628 LEU n 
1 1629 SER n 
1 1630 GLN n 
1 1631 ASP n 
1 1632 ALA n 
1 1633 SER n 
1 1634 LEU n 
1 1635 HIS n 
1 1636 ARG n 
1 1637 VAL n 
1 1638 LYS n 
1 1639 GLY n 
1 1640 CYS n 
1 1641 HIS n 
1 1642 SER n 
1 1643 PHE n 
1 1644 LYS n 
1 1645 LEU n 
1 1646 TRP n 
1 1647 PHE n 
1 1648 LEU n 
1 1649 LYS n 
1 1650 ARG n 
1 1651 LEU n 
1 1652 ASN n 
1 1653 VAL n 
1 1654 ALA n 
1 1655 GLU n 
1 1656 PHE n 
1 1657 THR n 
1 1658 VAL n 
1 1659 CYS n 
1 1660 PRO n 
1 1661 TRP n 
1 1662 VAL n 
1 1663 VAL n 
1 1664 ASN n 
1 1665 ILE n 
1 1666 ASP n 
1 1667 TYR n 
1 1668 HIS n 
1 1669 PRO n 
1 1670 THR n 
1 1671 HIS n 
1 1672 MET n 
1 1673 LYS n 
1 1674 ALA n 
1 1675 ILE n 
1 1676 LEU n 
1 1677 THR n 
1 1678 TYR n 
1 1679 ILE n 
1 1680 ASP n 
1 1681 LEU n 
1 1682 VAL n 
1 1683 ARG n 
1 1684 MET n 
1 1685 GLY n 
1 1686 LEU n 
1 1687 ILE n 
1 1688 ASN n 
1 1689 ILE n 
1 1690 ASP n 
1 1691 ARG n 
1 1692 ILE n 
1 1693 HIS n 
1 1694 ILE n 
1 1695 LYS n 
1 1696 ASN n 
1 1697 LYS n 
1 1698 HIS n 
1 1699 LYS n 
1 1700 PHE n 
1 1701 ASN n 
1 1702 ASP n 
1 1703 GLU n 
1 1704 PHE n 
1 1705 TYR n 
1 1706 THR n 
1 1707 SER n 
1 1708 ASN n 
1 1709 LEU n 
1 1710 PHE n 
1 1711 TYR n 
1 1712 ILE n 
1 1713 ASN n 
1 1714 TYR n 
1 1715 ASN n 
1 1716 PHE n 
1 1717 SER n 
1 1718 ASP n 
1 1719 ASN n 
1 1720 THR n 
1 1721 HIS n 
1 1722 LEU n 
1 1723 LEU n 
1 1724 THR n 
1 1725 LYS n 
1 1726 HIS n 
1 1727 ILE n 
1 1728 ARG n 
1 1729 ILE n 
1 1730 ALA n 
1 1731 ASN n 
1 1732 SER n 
1 1733 GLU n 
1 1734 LEU n 
1 1735 GLU n 
1 1736 ASN n 
1 1737 ASN n 
1 1738 TYR n 
1 1739 ASN n 
1 1740 LYS n 
1 1741 LEU n 
1 1742 TYR n 
1 1743 HIS n 
1 1744 PRO n 
1 1745 THR n 
1 1746 PRO n 
1 1747 GLU n 
1 1748 THR n 
1 1749 LEU n 
1 1750 GLU n 
1 1751 ASN n 
1 1752 ILE n 
1 1753 LEU n 
1 1754 ALA n 
1 1755 ASN n 
1 1756 PRO n 
1 1757 ILE n 
1 1758 LYS n 
1 1759 SER n 
1 1760 ASN n 
1 1761 ASP n 
1 1762 LYS n 
1 1763 LYS n 
1 1764 THR n 
1 1765 LEU n 
1 1766 ASN n 
1 1767 ASP n 
1 1768 TYR n 
1 1769 CYS n 
1 1770 ILE n 
1 1771 GLY n 
1 1772 LYS n 
1 1773 ASN n 
1 1774 VAL n 
1 1775 ASP n 
1 1776 SER n 
1 1777 ILE n 
1 1778 MET n 
1 1779 LEU n 
1 1780 PRO n 
1 1781 LEU n 
1 1782 LEU n 
1 1783 SER n 
1 1784 ASN n 
1 1785 LYS n 
1 1786 LYS n 
1 1787 LEU n 
1 1788 ILE n 
1 1789 LYS n 
1 1790 SER n 
1 1791 SER n 
1 1792 ALA n 
1 1793 MET n 
1 1794 ILE n 
1 1795 ARG n 
1 1796 THR n 
1 1797 ASN n 
1 1798 TYR n 
1 1799 SER n 
1 1800 LYS n 
1 1801 GLN n 
1 1802 ASP n 
1 1803 LEU n 
1 1804 TYR n 
1 1805 ASN n 
1 1806 LEU n 
1 1807 PHE n 
1 1808 PRO n 
1 1809 MET n 
1 1810 VAL n 
1 1811 VAL n 
1 1812 ILE n 
1 1813 ASP n 
1 1814 ARG n 
1 1815 ILE n 
1 1816 ILE n 
1 1817 ASP n 
1 1818 HIS n 
1 1819 SER n 
1 1820 GLY n 
1 1821 ASN n 
1 1822 THR n 
1 1823 ALA n 
1 1824 LYS n 
1 1825 SER n 
1 1826 ASN n 
1 1827 GLN n 
1 1828 LEU n 
1 1829 TYR n 
1 1830 THR n 
1 1831 THR n 
1 1832 THR n 
1 1833 SER n 
1 1834 HIS n 
1 1835 GLN n 
1 1836 ILE n 
1 1837 SER n 
1 1838 LEU n 
1 1839 VAL n 
1 1840 HIS n 
1 1841 ASN n 
1 1842 SER n 
1 1843 THR n 
1 1844 SER n 
1 1845 LEU n 
1 1846 TYR n 
1 1847 CYS n 
1 1848 MET n 
1 1849 LEU n 
1 1850 PRO n 
1 1851 TRP n 
1 1852 HIS n 
1 1853 HIS n 
1 1854 ILE n 
1 1855 ASN n 
1 1856 ARG n 
1 1857 PHE n 
1 1858 ASN n 
1 1859 PHE n 
1 1860 VAL n 
1 1861 PHE n 
1 1862 SER n 
1 1863 SER n 
1 1864 THR n 
1 1865 GLY n 
1 1866 CYS n 
1 1867 LYS n 
1 1868 ILE n 
1 1869 SER n 
1 1870 ILE n 
1 1871 GLU n 
1 1872 TYR n 
1 1873 ILE n 
1 1874 LEU n 
1 1875 LYS n 
1 1876 ASP n 
1 1877 LEU n 
1 1878 LYS n 
1 1879 ILE n 
1 1880 LYS n 
1 1881 ASP n 
1 1882 PRO n 
1 1883 ASN n 
1 1884 CYS n 
1 1885 ILE n 
1 1886 ALA n 
1 1887 PHE n 
1 1888 ILE n 
1 1889 GLY n 
1 1890 GLU n 
1 1891 GLY n 
1 1892 ALA n 
1 1893 GLY n 
1 1894 ASN n 
1 1895 LEU n 
1 1896 LEU n 
1 1897 LEU n 
1 1898 ARG n 
1 1899 THR n 
1 1900 VAL n 
1 1901 VAL n 
1 1902 GLU n 
1 1903 LEU n 
1 1904 HIS n 
1 1905 PRO n 
1 1906 ASP n 
1 1907 ILE n 
1 1908 ARG n 
1 1909 TYR n 
1 1910 ILE n 
1 1911 TYR n 
1 1912 ARG n 
1 1913 SER n 
1 1914 LEU n 
1 1915 LYS n 
1 1916 ASP n 
1 1917 CYS n 
1 1918 ASN n 
1 1919 ASP n 
1 1920 HIS n 
1 1921 SER n 
1 1922 LEU n 
1 1923 PRO n 
1 1924 ILE n 
1 1925 GLU n 
1 1926 PHE n 
1 1927 LEU n 
1 1928 ARG n 
1 1929 LEU n 
1 1930 TYR n 
1 1931 ASN n 
1 1932 GLY n 
1 1933 HIS n 
1 1934 ILE n 
1 1935 ASN n 
1 1936 ILE n 
1 1937 ASP n 
1 1938 TYR n 
1 1939 GLY n 
1 1940 GLU n 
1 1941 ASN n 
1 1942 LEU n 
1 1943 THR n 
1 1944 ILE n 
1 1945 PRO n 
1 1946 ALA n 
1 1947 THR n 
1 1948 ASP n 
1 1949 ALA n 
1 1950 THR n 
1 1951 ASN n 
1 1952 ASN n 
1 1953 ILE n 
1 1954 HIS n 
1 1955 TRP n 
1 1956 SER n 
1 1957 TYR n 
1 1958 LEU n 
1 1959 HIS n 
1 1960 ILE n 
1 1961 LYS n 
1 1962 PHE n 
1 1963 ALA n 
1 1964 GLU n 
1 1965 PRO n 
1 1966 ILE n 
1 1967 SER n 
1 1968 LEU n 
1 1969 PHE n 
1 1970 VAL n 
1 1971 CYS n 
1 1972 ASP n 
1 1973 ALA n 
1 1974 GLU n 
1 1975 LEU n 
1 1976 SER n 
1 1977 VAL n 
1 1978 THR n 
1 1979 VAL n 
1 1980 ASN n 
1 1981 TRP n 
1 1982 SER n 
1 1983 LYS n 
1 1984 ILE n 
1 1985 ILE n 
1 1986 ILE n 
1 1987 GLU n 
1 1988 TRP n 
1 1989 SER n 
1 1990 LYS n 
1 1991 HIS n 
1 1992 VAL n 
1 1993 ARG n 
1 1994 LYS n 
1 1995 CYS n 
1 1996 LYS n 
1 1997 TYR n 
1 1998 CYS n 
1 1999 SER n 
1 2000 SER n 
1 2001 VAL n 
1 2002 ASN n 
1 2003 LYS n 
1 2004 CYS n 
1 2005 MET n 
1 2006 LEU n 
1 2007 ILE n 
1 2008 VAL n 
1 2009 LYS n 
1 2010 TYR n 
1 2011 HIS n 
1 2012 ALA n 
1 2013 GLN n 
1 2014 ASP n 
1 2015 ASP n 
1 2016 ILE n 
1 2017 ASP n 
1 2018 PHE n 
1 2019 LYS n 
1 2020 LEU n 
1 2021 ASP n 
1 2022 ASN n 
1 2023 ILE n 
1 2024 THR n 
1 2025 ILE n 
1 2026 LEU n 
1 2027 LYS n 
1 2028 THR n 
1 2029 TYR n 
1 2030 VAL n 
1 2031 CYS n 
1 2032 LEU n 
1 2033 GLY n 
1 2034 SER n 
1 2035 LYS n 
1 2036 LEU n 
1 2037 LYS n 
1 2038 GLY n 
1 2039 SER n 
1 2040 GLU n 
1 2041 VAL n 
1 2042 TYR n 
1 2043 LEU n 
1 2044 VAL n 
1 2045 LEU n 
1 2046 THR n 
1 2047 ILE n 
1 2048 GLY n 
1 2049 PRO n 
1 2050 ALA n 
1 2051 ASN n 
1 2052 ILE n 
1 2053 PHE n 
1 2054 PRO n 
1 2055 VAL n 
1 2056 PHE n 
1 2057 ASN n 
1 2058 VAL n 
1 2059 VAL n 
1 2060 GLN n 
1 2061 ASN n 
1 2062 ALA n 
1 2063 LYS n 
1 2064 LEU n 
1 2065 ILE n 
1 2066 LEU n 
1 2067 SER n 
1 2068 ARG n 
1 2069 THR n 
1 2070 LYS n 
1 2071 ASN n 
1 2072 PHE n 
1 2073 ILE n 
1 2074 MET n 
1 2075 PRO n 
1 2076 LYS n 
1 2077 LYS n 
1 2078 ALA n 
1 2079 ASP n 
1 2080 LYS n 
1 2081 GLU n 
1 2082 SER n 
1 2083 ILE n 
1 2084 ASP n 
1 2085 ALA n 
1 2086 ASN n 
1 2087 ILE n 
1 2088 LYS n 
1 2089 SER n 
1 2090 LEU n 
1 2091 ILE n 
1 2092 PRO n 
1 2093 PHE n 
1 2094 LEU n 
1 2095 CYS n 
1 2096 TYR n 
1 2097 PRO n 
1 2098 ILE n 
1 2099 THR n 
1 2100 LYS n 
1 2101 LYS n 
1 2102 GLY n 
1 2103 ILE n 
1 2104 ASN n 
1 2105 THR n 
1 2106 ALA n 
1 2107 LEU n 
1 2108 SER n 
1 2109 LYS n 
1 2110 LEU n 
1 2111 LYS n 
1 2112 SER n 
1 2113 VAL n 
1 2114 VAL n 
1 2115 SER n 
1 2116 GLY n 
1 2117 ASP n 
1 2118 ILE n 
1 2119 LEU n 
1 2120 SER n 
1 2121 TYR n 
1 2122 SER n 
1 2123 ILE n 
1 2124 ALA n 
1 2125 GLY n 
1 2126 ARG n 
1 2127 ASN n 
1 2128 GLU n 
1 2129 VAL n 
1 2130 PHE n 
1 2131 SER n 
1 2132 ASN n 
1 2133 LYS n 
1 2134 LEU n 
1 2135 ILE n 
1 2136 ASN n 
1 2137 HIS n 
1 2138 LYS n 
1 2139 HIS n 
1 2140 MET n 
1 2141 ASN n 
1 2142 ILE n 
1 2143 LEU n 
1 2144 LYS n 
1 2145 TRP n 
1 2146 PHE n 
1 2147 ASN n 
1 2148 HIS n 
1 2149 VAL n 
1 2150 LEU n 
1 2151 ASN n 
1 2152 PHE n 
1 2153 ARG n 
1 2154 SER n 
1 2155 THR n 
1 2156 GLU n 
1 2157 LEU n 
1 2158 ASN n 
1 2159 TYR n 
1 2160 ASN n 
1 2161 HIS n 
1 2162 LEU n 
1 2163 TYR n 
1 2164 MET n 
1 2165 VAL n 
1 2166 GLU n 
1 2167 SER n 
1 2168 THR n 
1 2169 TYR n 
1 2170 PRO n 
1 2171 TYR n 
1 2172 LEU n 
1 2173 SER n 
1 2174 GLU n 
1 2175 LEU n 
1 2176 LEU n 
1 2177 ASN n 
1 2178 SER n 
1 2179 LEU n 
1 2180 THR n 
1 2181 THR n 
1 2182 ASN n 
1 2183 GLU n 
1 2184 LEU n 
1 2185 LYS n 
1 2186 LYS n 
1 2187 LEU n 
1 2188 ILE n 
1 2189 LYS n 
1 2190 ILE n 
1 2191 THR n 
1 2192 GLY n 
1 2193 SER n 
1 2194 LEU n 
1 2195 LEU n 
1 2196 TYR n 
1 2197 ASN n 
1 2198 PHE n 
1 2199 HIS n 
1 2200 ASN n 
1 2201 GLU n 
2 1    MET n 
2 2    GLU n 
2 3    LYS n 
2 4    PHE n 
2 5    ALA n 
2 6    PRO n 
2 7    GLU n 
2 8    PHE n 
2 9    HIS n 
2 10   GLY n 
2 11   GLU n 
2 12   ASP n 
2 13   ALA n 
2 14   ASN n 
2 15   ASN n 
2 16   ARG n 
2 17   ALA n 
2 18   THR n 
2 19   LYS n 
2 20   PHE n 
2 21   LEU n 
2 22   GLU n 
2 23   SER n 
2 24   ILE n 
2 25   LYS n 
2 26   GLY n 
2 27   LYS n 
2 28   PHE n 
2 29   THR n 
2 30   SER n 
2 31   PRO n 
2 32   LYS n 
2 33   ASP n 
2 34   PRO n 
2 35   LYS n 
2 36   LYS n 
2 37   LYS n 
2 38   ASP n 
2 39   SER n 
2 40   ILE n 
2 41   ILE n 
2 42   SER n 
2 43   VAL n 
2 44   ASN n 
2 45   SER n 
2 46   ILE n 
2 47   ASP n 
2 48   ILE n 
2 49   GLU n 
2 50   VAL n 
2 51   THR n 
2 52   LYS n 
2 53   GLU n 
2 54   SER n 
2 55   PRO n 
2 56   ILE n 
2 57   THR n 
2 58   SER n 
2 59   ASN n 
2 60   SER n 
2 61   THR n 
2 62   ILE n 
2 63   ILE n 
2 64   ASN n 
2 65   PRO n 
2 66   THR n 
2 67   ASN n 
2 68   GLU n 
2 69   THR n 
2 70   ASP n 
2 71   ASP n 
2 72   THR n 
2 73   ALA n 
2 74   GLY n 
2 75   ASN n 
2 76   LYS n 
2 77   PRO n 
2 78   ASN n 
2 79   TYR n 
2 80   GLN n 
2 81   ARG n 
2 82   LYS n 
2 83   PRO n 
2 84   LEU n 
2 85   VAL n 
2 86   SER n 
2 87   PHE n 
2 88   LYS n 
2 89   GLU n 
2 90   ASP n 
2 91   PRO n 
2 92   THR n 
2 93   PRO n 
2 94   SER n 
2 95   ASP n 
2 96   ASN n 
2 97   PRO n 
2 98   PHE n 
2 99   SER n 
2 100  LYS n 
2 101  LEU n 
2 102  TYR n 
2 103  LYS n 
2 104  GLU n 
2 105  THR n 
2 106  ILE n 
2 107  GLU n 
2 108  THR n 
2 109  PHE n 
2 110  ASP n 
2 111  ASN n 
2 112  ASN n 
2 113  GLU n 
2 114  GLU n 
2 115  GLU n 
2 116  SER n 
2 117  SER n 
2 118  TYR n 
2 119  SER n 
2 120  TYR n 
2 121  GLU n 
2 122  GLU n 
2 123  ILE n 
2 124  ASN n 
2 125  ASP n 
2 126  GLN n 
2 127  THR n 
2 128  ASN n 
2 129  ASP n 
2 130  ASN n 
2 131  ILE n 
2 132  THR n 
2 133  ALA n 
2 134  ARG n 
2 135  LEU n 
2 136  ASP n 
2 137  ARG n 
2 138  ILE n 
2 139  ASP n 
2 140  GLU n 
2 141  LYS n 
2 142  LEU n 
2 143  SER n 
2 144  GLU n 
2 145  ILE n 
2 146  LEU n 
2 147  GLY n 
2 148  MET n 
2 149  LEU n 
2 150  HIS n 
2 151  THR n 
2 152  LEU n 
2 153  VAL n 
2 154  VAL n 
2 155  ALA n 
2 156  SER n 
2 157  ALA n 
2 158  GLY n 
2 159  PRO n 
2 160  THR n 
2 161  SER n 
2 162  ALA n 
2 163  ARG n 
2 164  ASP n 
2 165  GLY n 
2 166  ILE n 
2 167  ARG n 
2 168  ASP n 
2 169  ALA n 
2 170  MET n 
2 171  ILE n 
2 172  GLY n 
2 173  LEU n 
2 174  ARG n 
2 175  GLU n 
2 176  GLU n 
2 177  MET n 
2 178  ILE n 
2 179  GLU n 
2 180  LYS n 
2 181  ILE n 
2 182  ARG n 
2 183  THR n 
2 184  GLU n 
2 185  ALA n 
2 186  LEU n 
2 187  MET n 
2 188  THR n 
2 189  ASN n 
2 190  ASP n 
2 191  ARG n 
2 192  LEU n 
2 193  GLU n 
2 194  ALA n 
2 195  MET n 
2 196  ALA n 
2 197  ARG n 
2 198  LEU n 
2 199  ARG n 
2 200  ASN n 
2 201  GLU n 
2 202  GLU n 
2 203  SER n 
2 204  GLU n 
2 205  LYS n 
2 206  MET n 
2 207  ALA n 
2 208  LYS n 
2 209  ASP n 
2 210  THR n 
2 211  SER n 
2 212  ASP n 
2 213  GLU n 
2 214  VAL n 
2 215  SER n 
2 216  LEU n 
2 217  ASN n 
2 218  PRO n 
2 219  THR n 
2 220  SER n 
2 221  GLU n 
2 222  LYS n 
2 223  LEU n 
2 224  ASN n 
2 225  ASN n 
2 226  LEU n 
2 227  LEU n 
2 228  GLU n 
2 229  GLY n 
2 230  ASN n 
2 231  ASP n 
2 232  SER n 
2 233  ASP n 
2 234  ASN n 
2 235  ASP n 
2 236  LEU n 
2 237  SER n 
2 238  LEU n 
2 239  GLU n 
2 240  ASP n 
2 241  PHE n 
2 242  LYS n 
2 243  GLY n 
2 244  GLU n 
2 245  ASN n 
2 246  LYS n 
2 247  TYR n 
2 248  PHE n 
2 249  GLN n 
2 250  GLY n 
2 251  HIS n 
2 252  HIS n 
2 253  HIS n 
2 254  HIS n 
2 255  HIS n 
2 256  HIS 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 2201 ? ? ? ? ? ? ? ? ? 'Human respiratory syncytial virus A2' 11259 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 256  ? ? ? ? ? ? ? ? ? 'Human respiratory syncytial virus A2' 11259 ? ? ? ? ? ? ? ? 
'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 
A1AWZ non-polymer         . 
;(2S)-1,1,1-trifluoro-2-[5-fluoro-6-(4-fluorophenyl)-4-(2-hydroxypropan-2-yl)pyridin-2-yl]-3-[(4M)-4-(8-methoxyquinolin-6-yl)-1H-1,2,3-triazol-1-yl]propan-2-ol
;
JNJ-2729 'C29 H24 F5 N5 O3' 585.525 
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 
# 
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    -35  ?    ?   ?   A . n 
A 1 2    GLY 2    -34  ?    ?   ?   A . n 
A 1 3    SER 3    -33  ?    ?   ?   A . n 
A 1 4    TRP 4    -32  ?    ?   ?   A . n 
A 1 5    SER 5    -31  ?    ?   ?   A . n 
A 1 6    HIS 6    -30  ?    ?   ?   A . n 
A 1 7    PRO 7    -29  ?    ?   ?   A . n 
A 1 8    GLN 8    -28  ?    ?   ?   A . n 
A 1 9    PHE 9    -27  ?    ?   ?   A . n 
A 1 10   GLU 10   -26  ?    ?   ?   A . n 
A 1 11   LYS 11   -25  ?    ?   ?   A . n 
A 1 12   GLY 12   -24  ?    ?   ?   A . n 
A 1 13   SER 13   -23  ?    ?   ?   A . n 
A 1 14   GLY 14   -22  ?    ?   ?   A . n 
A 1 15   SER 15   -21  ?    ?   ?   A . n 
A 1 16   GLY 16   -20  ?    ?   ?   A . n 
A 1 17   SER 17   -19  ?    ?   ?   A . n 
A 1 18   SER 18   -18  ?    ?   ?   A . n 
A 1 19   TRP 19   -17  ?    ?   ?   A . n 
A 1 20   SER 20   -16  ?    ?   ?   A . n 
A 1 21   HIS 21   -15  ?    ?   ?   A . n 
A 1 22   PRO 22   -14  ?    ?   ?   A . n 
A 1 23   GLN 23   -13  ?    ?   ?   A . n 
A 1 24   PHE 24   -12  ?    ?   ?   A . n 
A 1 25   GLU 25   -11  ?    ?   ?   A . n 
A 1 26   LYS 26   -10  ?    ?   ?   A . n 
A 1 27   GLY 27   -9   ?    ?   ?   A . n 
A 1 28   SER 28   -8   ?    ?   ?   A . n 
A 1 29   GLY 29   -7   ?    ?   ?   A . n 
A 1 30   SER 30   -6   ?    ?   ?   A . n 
A 1 31   LEU 31   -5   ?    ?   ?   A . n 
A 1 32   VAL 32   -4   ?    ?   ?   A . n 
A 1 33   PRO 33   -3   ?    ?   ?   A . n 
A 1 34   ARG 34   -2   ?    ?   ?   A . n 
A 1 35   GLY 35   -1   ?    ?   ?   A . n 
A 1 36   SER 36   0    ?    ?   ?   A . n 
A 1 37   MET 37   1    ?    ?   ?   A . n 
A 1 38   ASP 38   2    ?    ?   ?   A . n 
A 1 39   PRO 39   3    ?    ?   ?   A . n 
A 1 40   ILE 40   4    ?    ?   ?   A . n 
A 1 41   ILE 41   5    ?    ?   ?   A . n 
A 1 42   ASN 42   6    ?    ?   ?   A . n 
A 1 43   GLY 43   7    ?    ?   ?   A . n 
A 1 44   ASN 44   8    ?    ?   ?   A . n 
A 1 45   SER 45   9    ?    ?   ?   A . n 
A 1 46   ALA 46   10   ?    ?   ?   A . n 
A 1 47   ASN 47   11   11   ASN ASN A . n 
A 1 48   VAL 48   12   12   VAL VAL A . n 
A 1 49   TYR 49   13   13   TYR TYR A . n 
A 1 50   LEU 50   14   14   LEU LEU A . n 
A 1 51   THR 51   15   15   THR THR A . n 
A 1 52   ASP 52   16   16   ASP ASP A . n 
A 1 53   SER 53   17   17   SER SER A . n 
A 1 54   TYR 54   18   18   TYR TYR A . n 
A 1 55   LEU 55   19   19   LEU LEU A . n 
A 1 56   LYS 56   20   20   LYS LYS A . n 
A 1 57   GLY 57   21   21   GLY GLY A . n 
A 1 58   VAL 58   22   22   VAL VAL A . n 
A 1 59   ILE 59   23   23   ILE ILE A . n 
A 1 60   SER 60   24   24   SER SER A . n 
A 1 61   PHE 61   25   25   PHE PHE A . n 
A 1 62   SER 62   26   26   SER SER A . n 
A 1 63   GLU 63   27   27   GLU GLU A . n 
A 1 64   CYS 64   28   28   CYS CYS A . n 
A 1 65   ASN 65   29   29   ASN ASN A . n 
A 1 66   ALA 66   30   30   ALA ALA A . n 
A 1 67   LEU 67   31   31   LEU LEU A . n 
A 1 68   GLY 68   32   32   GLY GLY A . n 
A 1 69   SER 69   33   33   SER SER A . n 
A 1 70   TYR 70   34   34   TYR TYR A . n 
A 1 71   ILE 71   35   35   ILE ILE A . n 
A 1 72   PHE 72   36   36   PHE PHE A . n 
A 1 73   ASN 73   37   37   ASN ASN A . n 
A 1 74   GLY 74   38   38   GLY GLY A . n 
A 1 75   PRO 75   39   39   PRO PRO A . n 
A 1 76   TYR 76   40   40   TYR TYR A . n 
A 1 77   LEU 77   41   41   LEU LEU A . n 
A 1 78   LYS 78   42   42   LYS LYS A . n 
A 1 79   ASN 79   43   43   ASN ASN A . n 
A 1 80   ASP 80   44   44   ASP ASP A . n 
A 1 81   TYR 81   45   45   TYR TYR A . n 
A 1 82   THR 82   46   46   THR THR A . n 
A 1 83   ASN 83   47   47   ASN ASN A . n 
A 1 84   LEU 84   48   48   LEU LEU A . n 
A 1 85   ILE 85   49   49   ILE ILE A . n 
A 1 86   SER 86   50   50   SER SER A . n 
A 1 87   ARG 87   51   51   ARG ARG A . n 
A 1 88   GLN 88   52   52   GLN GLN A . n 
A 1 89   ASN 89   53   53   ASN ASN A . n 
A 1 90   PRO 90   54   54   PRO PRO A . n 
A 1 91   LEU 91   55   55   LEU LEU A . n 
A 1 92   ILE 92   56   56   ILE ILE A . n 
A 1 93   GLU 93   57   57   GLU GLU A . n 
A 1 94   HIS 94   58   58   HIS HIS A . n 
A 1 95   MET 95   59   59   MET MET A . n 
A 1 96   ASN 96   60   60   ASN ASN A . n 
A 1 97   LEU 97   61   61   LEU LEU A . n 
A 1 98   LYS 98   62   62   LYS LYS A . n 
A 1 99   LYS 99   63   63   LYS LYS A . n 
A 1 100  LEU 100  64   64   LEU LEU A . n 
A 1 101  ASN 101  65   65   ASN ASN A . n 
A 1 102  ILE 102  66   66   ILE ILE A . n 
A 1 103  THR 103  67   67   THR THR A . n 
A 1 104  GLN 104  68   68   GLN GLN A . n 
A 1 105  SER 105  69   69   SER SER A . n 
A 1 106  LEU 106  70   70   LEU LEU A . n 
A 1 107  ILE 107  71   71   ILE ILE A . n 
A 1 108  SER 108  72   72   SER SER A . n 
A 1 109  LYS 109  73   73   LYS LYS A . n 
A 1 110  TYR 110  74   74   TYR TYR A . n 
A 1 111  HIS 111  75   75   HIS HIS A . n 
A 1 112  LYS 112  76   76   LYS LYS A . n 
A 1 113  GLY 113  77   77   GLY GLY A . n 
A 1 114  GLU 114  78   78   GLU GLU A . n 
A 1 115  ILE 115  79   79   ILE ILE A . n 
A 1 116  LYS 116  80   80   LYS LYS A . n 
A 1 117  LEU 117  81   81   LEU LEU A . n 
A 1 118  GLU 118  82   82   GLU GLU A . n 
A 1 119  GLU 119  83   83   GLU GLU A . n 
A 1 120  PRO 120  84   84   PRO PRO A . n 
A 1 121  THR 121  85   85   THR THR A . n 
A 1 122  TYR 122  86   86   TYR TYR A . n 
A 1 123  PHE 123  87   87   PHE PHE A . n 
A 1 124  GLN 124  88   88   GLN GLN A . n 
A 1 125  SER 125  89   89   SER SER A . n 
A 1 126  LEU 126  90   90   LEU LEU A . n 
A 1 127  LEU 127  91   91   LEU LEU A . n 
A 1 128  MET 128  92   92   MET MET A . n 
A 1 129  THR 129  93   93   THR THR A . n 
A 1 130  TYR 130  94   94   TYR TYR A . n 
A 1 131  LYS 131  95   95   LYS LYS A . n 
A 1 132  SER 132  96   96   SER SER A . n 
A 1 133  MET 133  97   97   MET MET A . n 
A 1 134  THR 134  98   98   THR THR A . n 
A 1 135  SER 135  99   99   SER SER A . n 
A 1 136  SER 136  100  100  SER SER A . n 
A 1 137  GLU 137  101  101  GLU GLU A . n 
A 1 138  GLN 138  102  102  GLN GLN A . n 
A 1 139  ILE 139  103  103  ILE ILE A . n 
A 1 140  ALA 140  104  104  ALA ALA A . n 
A 1 141  THR 141  105  105  THR THR A . n 
A 1 142  THR 142  106  106  THR THR A . n 
A 1 143  ASN 143  107  107  ASN ASN A . n 
A 1 144  LEU 144  108  108  LEU LEU A . n 
A 1 145  LEU 145  109  109  LEU LEU A . n 
A 1 146  LYS 146  110  110  LYS LYS A . n 
A 1 147  LYS 147  111  111  LYS LYS A . n 
A 1 148  ILE 148  112  112  ILE ILE A . n 
A 1 149  ILE 149  113  113  ILE ILE A . n 
A 1 150  ARG 150  114  114  ARG ARG A . n 
A 1 151  ARG 151  115  115  ARG ARG A . n 
A 1 152  ALA 152  116  116  ALA ALA A . n 
A 1 153  ILE 153  117  117  ILE ILE A . n 
A 1 154  GLU 154  118  118  GLU GLU A . n 
A 1 155  ILE 155  119  119  ILE ILE A . n 
A 1 156  SER 156  120  120  SER SER A . n 
A 1 157  ASP 157  121  121  ASP ASP A . n 
A 1 158  VAL 158  122  122  VAL VAL A . n 
A 1 159  LYS 159  123  123  LYS LYS A . n 
A 1 160  VAL 160  124  124  VAL VAL A . n 
A 1 161  TYR 161  125  125  TYR TYR A . n 
A 1 162  ALA 162  126  126  ALA ALA A . n 
A 1 163  ILE 163  127  127  ILE ILE A . n 
A 1 164  LEU 164  128  128  LEU LEU A . n 
A 1 165  ASN 165  129  129  ASN ASN A . n 
A 1 166  LYS 166  130  130  LYS LYS A . n 
A 1 167  LEU 167  131  131  LEU LEU A . n 
A 1 168  GLY 168  132  132  GLY GLY A . n 
A 1 169  LEU 169  133  133  LEU LEU A . n 
A 1 170  LYS 170  134  134  LYS LYS A . n 
A 1 171  GLU 171  135  ?    ?   ?   A . n 
A 1 172  LYS 172  136  ?    ?   ?   A . n 
A 1 173  ASP 173  137  ?    ?   ?   A . n 
A 1 174  LYS 174  138  ?    ?   ?   A . n 
A 1 175  ILE 175  139  ?    ?   ?   A . n 
A 1 176  LYS 176  140  ?    ?   ?   A . n 
A 1 177  SER 177  141  ?    ?   ?   A . n 
A 1 178  ASN 178  142  ?    ?   ?   A . n 
A 1 179  ASN 179  143  ?    ?   ?   A . n 
A 1 180  GLY 180  144  ?    ?   ?   A . n 
A 1 181  GLN 181  145  ?    ?   ?   A . n 
A 1 182  ASP 182  146  ?    ?   ?   A . n 
A 1 183  GLU 183  147  ?    ?   ?   A . n 
A 1 184  ASP 184  148  ?    ?   ?   A . n 
A 1 185  ASN 185  149  ?    ?   ?   A . n 
A 1 186  SER 186  150  ?    ?   ?   A . n 
A 1 187  VAL 187  151  ?    ?   ?   A . n 
A 1 188  ILE 188  152  ?    ?   ?   A . n 
A 1 189  THR 189  153  ?    ?   ?   A . n 
A 1 190  THR 190  154  ?    ?   ?   A . n 
A 1 191  ILE 191  155  ?    ?   ?   A . n 
A 1 192  ILE 192  156  ?    ?   ?   A . n 
A 1 193  LYS 193  157  ?    ?   ?   A . n 
A 1 194  ASP 194  158  ?    ?   ?   A . n 
A 1 195  ASP 195  159  ?    ?   ?   A . n 
A 1 196  ILE 196  160  ?    ?   ?   A . n 
A 1 197  LEU 197  161  ?    ?   ?   A . n 
A 1 198  SER 198  162  ?    ?   ?   A . n 
A 1 199  ALA 199  163  ?    ?   ?   A . n 
A 1 200  VAL 200  164  ?    ?   ?   A . n 
A 1 201  LYS 201  165  ?    ?   ?   A . n 
A 1 202  ASP 202  166  ?    ?   ?   A . n 
A 1 203  ASN 203  167  ?    ?   ?   A . n 
A 1 204  GLN 204  168  ?    ?   ?   A . n 
A 1 205  SER 205  169  ?    ?   ?   A . n 
A 1 206  HIS 206  170  ?    ?   ?   A . n 
A 1 207  LEU 207  171  ?    ?   ?   A . n 
A 1 208  LYS 208  172  ?    ?   ?   A . n 
A 1 209  ALA 209  173  ?    ?   ?   A . n 
A 1 210  ASP 210  174  ?    ?   ?   A . n 
A 1 211  LYS 211  175  ?    ?   ?   A . n 
A 1 212  ASN 212  176  ?    ?   ?   A . n 
A 1 213  HIS 213  177  ?    ?   ?   A . n 
A 1 214  SER 214  178  ?    ?   ?   A . n 
A 1 215  THR 215  179  ?    ?   ?   A . n 
A 1 216  LYS 216  180  ?    ?   ?   A . n 
A 1 217  GLN 217  181  ?    ?   ?   A . n 
A 1 218  LYS 218  182  ?    ?   ?   A . n 
A 1 219  ASP 219  183  183  ASP ASP A . n 
A 1 220  THR 220  184  184  THR THR A . n 
A 1 221  ILE 221  185  185  ILE ILE A . n 
A 1 222  LYS 222  186  186  LYS LYS A . n 
A 1 223  THR 223  187  187  THR THR A . n 
A 1 224  THR 224  188  188  THR THR A . n 
A 1 225  LEU 225  189  189  LEU LEU A . n 
A 1 226  LEU 226  190  190  LEU LEU A . n 
A 1 227  LYS 227  191  191  LYS LYS A . n 
A 1 228  LYS 228  192  192  LYS LYS A . n 
A 1 229  LEU 229  193  193  LEU LEU A . n 
A 1 230  MET 230  194  194  MET MET A . n 
A 1 231  CYS 231  195  195  CYS CYS A . n 
A 1 232  SER 232  196  196  SER SER A . n 
A 1 233  MET 233  197  197  MET MET A . n 
A 1 234  GLN 234  198  198  GLN GLN A . n 
A 1 235  HIS 235  199  199  HIS HIS A . n 
A 1 236  PRO 236  200  200  PRO PRO A . n 
A 1 237  PRO 237  201  201  PRO PRO A . n 
A 1 238  SER 238  202  202  SER SER A . n 
A 1 239  TRP 239  203  203  TRP TRP A . n 
A 1 240  LEU 240  204  204  LEU LEU A . n 
A 1 241  ILE 241  205  205  ILE ILE A . n 
A 1 242  HIS 242  206  206  HIS HIS A . n 
A 1 243  TRP 243  207  207  TRP TRP A . n 
A 1 244  PHE 244  208  208  PHE PHE A . n 
A 1 245  ASN 245  209  209  ASN ASN A . n 
A 1 246  LEU 246  210  210  LEU LEU A . n 
A 1 247  TYR 247  211  211  TYR TYR A . n 
A 1 248  THR 248  212  212  THR THR A . n 
A 1 249  LYS 249  213  213  LYS LYS A . n 
A 1 250  LEU 250  214  214  LEU LEU A . n 
A 1 251  ASN 251  215  215  ASN ASN A . n 
A 1 252  ASN 252  216  216  ASN ASN A . n 
A 1 253  ILE 253  217  217  ILE ILE A . n 
A 1 254  LEU 254  218  218  LEU LEU A . n 
A 1 255  THR 255  219  219  THR THR A . n 
A 1 256  GLN 256  220  220  GLN GLN A . n 
A 1 257  TYR 257  221  221  TYR TYR A . n 
A 1 258  ARG 258  222  222  ARG ARG A . n 
A 1 259  SER 259  223  223  SER SER A . n 
A 1 260  ASN 260  224  224  ASN ASN A . n 
A 1 261  GLU 261  225  225  GLU GLU A . n 
A 1 262  VAL 262  226  226  VAL VAL A . n 
A 1 263  LYS 263  227  227  LYS LYS A . n 
A 1 264  ASN 264  228  228  ASN ASN A . n 
A 1 265  HIS 265  229  229  HIS HIS A . n 
A 1 266  GLY 266  230  230  GLY GLY A . n 
A 1 267  PHE 267  231  231  PHE PHE A . n 
A 1 268  THR 268  232  232  THR THR A . n 
A 1 269  LEU 269  233  233  LEU LEU A . n 
A 1 270  ILE 270  234  234  ILE ILE A . n 
A 1 271  ASP 271  235  235  ASP ASP A . n 
A 1 272  ASN 272  236  236  ASN ASN A . n 
A 1 273  GLN 273  237  237  GLN GLN A . n 
A 1 274  THR 274  238  238  THR THR A . n 
A 1 275  LEU 275  239  239  LEU LEU A . n 
A 1 276  SER 276  240  240  SER SER A . n 
A 1 277  GLY 277  241  241  GLY GLY A . n 
A 1 278  PHE 278  242  242  PHE PHE A . n 
A 1 279  GLN 279  243  243  GLN GLN A . n 
A 1 280  PHE 280  244  244  PHE PHE A . n 
A 1 281  ILE 281  245  245  ILE ILE A . n 
A 1 282  LEU 282  246  246  LEU LEU A . n 
A 1 283  ASN 283  247  247  ASN ASN A . n 
A 1 284  GLN 284  248  248  GLN GLN A . n 
A 1 285  TYR 285  249  249  TYR TYR A . n 
A 1 286  GLY 286  250  250  GLY GLY A . n 
A 1 287  CYS 287  251  251  CYS CYS A . n 
A 1 288  ILE 288  252  252  ILE ILE A . n 
A 1 289  VAL 289  253  253  VAL VAL A . n 
A 1 290  TYR 290  254  254  TYR TYR A . n 
A 1 291  HIS 291  255  255  HIS HIS A . n 
A 1 292  LYS 292  256  256  LYS LYS A . n 
A 1 293  GLU 293  257  257  GLU GLU A . n 
A 1 294  LEU 294  258  258  LEU LEU A . n 
A 1 295  LYS 295  259  259  LYS LYS A . n 
A 1 296  ARG 296  260  260  ARG ARG A . n 
A 1 297  ILE 297  261  261  ILE ILE A . n 
A 1 298  THR 298  262  262  THR THR A . n 
A 1 299  VAL 299  263  263  VAL VAL A . n 
A 1 300  THR 300  264  264  THR THR A . n 
A 1 301  THR 301  265  265  THR THR A . n 
A 1 302  TYR 302  266  266  TYR TYR A . n 
A 1 303  ASN 303  267  267  ASN ASN A . n 
A 1 304  GLN 304  268  268  GLN GLN A . n 
A 1 305  PHE 305  269  269  PHE PHE A . n 
A 1 306  LEU 306  270  270  LEU LEU A . n 
A 1 307  THR 307  271  271  THR THR A . n 
A 1 308  TRP 308  272  272  TRP TRP A . n 
A 1 309  LYS 309  273  273  LYS LYS A . n 
A 1 310  ASP 310  274  274  ASP ASP A . n 
A 1 311  ILE 311  275  275  ILE ILE A . n 
A 1 312  SER 312  276  276  SER SER A . n 
A 1 313  LEU 313  277  277  LEU LEU A . n 
A 1 314  SER 314  278  278  SER SER A . n 
A 1 315  ARG 315  279  279  ARG ARG A . n 
A 1 316  LEU 316  280  280  LEU LEU A . n 
A 1 317  ASN 317  281  281  ASN ASN A . n 
A 1 318  VAL 318  282  282  VAL VAL A . n 
A 1 319  CYS 319  283  283  CYS CYS A . n 
A 1 320  LEU 320  284  284  LEU LEU A . n 
A 1 321  ILE 321  285  285  ILE ILE A . n 
A 1 322  THR 322  286  286  THR THR A . n 
A 1 323  TRP 323  287  287  TRP TRP A . n 
A 1 324  ILE 324  288  288  ILE ILE A . n 
A 1 325  SER 325  289  289  SER SER A . n 
A 1 326  ASN 326  290  290  ASN ASN A . n 
A 1 327  CYS 327  291  291  CYS CYS A . n 
A 1 328  LEU 328  292  292  LEU LEU A . n 
A 1 329  ASN 329  293  293  ASN ASN A . n 
A 1 330  THR 330  294  294  THR THR A . n 
A 1 331  LEU 331  295  295  LEU LEU A . n 
A 1 332  ASN 332  296  296  ASN ASN A . n 
A 1 333  LYS 333  297  297  LYS LYS A . n 
A 1 334  SER 334  298  298  SER SER A . n 
A 1 335  LEU 335  299  299  LEU LEU A . n 
A 1 336  GLY 336  300  300  GLY GLY A . n 
A 1 337  LEU 337  301  301  LEU LEU A . n 
A 1 338  ARG 338  302  302  ARG ARG A . n 
A 1 339  CYS 339  303  303  CYS CYS A . n 
A 1 340  GLY 340  304  304  GLY GLY A . n 
A 1 341  PHE 341  305  305  PHE PHE A . n 
A 1 342  ASN 342  306  306  ASN ASN A . n 
A 1 343  ASN 343  307  307  ASN ASN A . n 
A 1 344  VAL 344  308  308  VAL VAL A . n 
A 1 345  ILE 345  309  309  ILE ILE A . n 
A 1 346  LEU 346  310  310  LEU LEU A . n 
A 1 347  THR 347  311  311  THR THR A . n 
A 1 348  GLN 348  312  312  GLN GLN A . n 
A 1 349  LEU 349  313  313  LEU LEU A . n 
A 1 350  PHE 350  314  314  PHE PHE A . n 
A 1 351  LEU 351  315  315  LEU LEU A . n 
A 1 352  TYR 352  316  316  TYR TYR A . n 
A 1 353  GLY 353  317  317  GLY GLY A . n 
A 1 354  ASP 354  318  318  ASP ASP A . n 
A 1 355  CYS 355  319  319  CYS CYS A . n 
A 1 356  ILE 356  320  320  ILE ILE A . n 
A 1 357  LEU 357  321  321  LEU LEU A . n 
A 1 358  LYS 358  322  322  LYS LYS A . n 
A 1 359  LEU 359  323  323  LEU LEU A . n 
A 1 360  PHE 360  324  324  PHE PHE A . n 
A 1 361  HIS 361  325  325  HIS HIS A . n 
A 1 362  ASN 362  326  326  ASN ASN A . n 
A 1 363  GLU 363  327  327  GLU GLU A . n 
A 1 364  GLY 364  328  328  GLY GLY A . n 
A 1 365  PHE 365  329  329  PHE PHE A . n 
A 1 366  TYR 366  330  330  TYR TYR A . n 
A 1 367  ILE 367  331  331  ILE ILE A . n 
A 1 368  ILE 368  332  332  ILE ILE A . n 
A 1 369  LYS 369  333  333  LYS LYS A . n 
A 1 370  GLU 370  334  334  GLU GLU A . n 
A 1 371  VAL 371  335  335  VAL VAL A . n 
A 1 372  GLU 372  336  336  GLU GLU A . n 
A 1 373  GLY 373  337  337  GLY GLY A . n 
A 1 374  PHE 374  338  338  PHE PHE A . n 
A 1 375  ILE 375  339  339  ILE ILE A . n 
A 1 376  MET 376  340  340  MET MET A . n 
A 1 377  SER 377  341  341  SER SER A . n 
A 1 378  LEU 378  342  342  LEU LEU A . n 
A 1 379  ILE 379  343  343  ILE ILE A . n 
A 1 380  LEU 380  344  344  LEU LEU A . n 
A 1 381  ASN 381  345  345  ASN ASN A . n 
A 1 382  ILE 382  346  346  ILE ILE A . n 
A 1 383  THR 383  347  347  THR THR A . n 
A 1 384  GLU 384  348  348  GLU GLU A . n 
A 1 385  GLU 385  349  349  GLU GLU A . n 
A 1 386  ASP 386  350  350  ASP ASP A . n 
A 1 387  GLN 387  351  351  GLN GLN A . n 
A 1 388  PHE 388  352  352  PHE PHE A . n 
A 1 389  ARG 389  353  353  ARG ARG A . n 
A 1 390  LYS 390  354  354  LYS LYS A . n 
A 1 391  ARG 391  355  355  ARG ARG A . n 
A 1 392  PHE 392  356  356  PHE PHE A . n 
A 1 393  TYR 393  357  357  TYR TYR A . n 
A 1 394  ASN 394  358  358  ASN ASN A . n 
A 1 395  SER 395  359  359  SER SER A . n 
A 1 396  MET 396  360  360  MET MET A . n 
A 1 397  LEU 397  361  361  LEU LEU A . n 
A 1 398  ASN 398  362  362  ASN ASN A . n 
A 1 399  ASN 399  363  363  ASN ASN A . n 
A 1 400  ILE 400  364  364  ILE ILE A . n 
A 1 401  THR 401  365  365  THR THR A . n 
A 1 402  ASP 402  366  366  ASP ASP A . n 
A 1 403  ALA 403  367  367  ALA ALA A . n 
A 1 404  ALA 404  368  368  ALA ALA A . n 
A 1 405  ASN 405  369  369  ASN ASN A . n 
A 1 406  LYS 406  370  370  LYS LYS A . n 
A 1 407  ALA 407  371  371  ALA ALA A . n 
A 1 408  GLN 408  372  372  GLN GLN A . n 
A 1 409  LYS 409  373  373  LYS LYS A . n 
A 1 410  ASN 410  374  374  ASN ASN A . n 
A 1 411  LEU 411  375  375  LEU LEU A . n 
A 1 412  LEU 412  376  376  LEU LEU A . n 
A 1 413  SER 413  377  377  SER SER A . n 
A 1 414  ARG 414  378  378  ARG ARG A . n 
A 1 415  VAL 415  379  379  VAL VAL A . n 
A 1 416  CYS 416  380  380  CYS CYS A . n 
A 1 417  HIS 417  381  381  HIS HIS A . n 
A 1 418  THR 418  382  382  THR THR A . n 
A 1 419  LEU 419  383  383  LEU LEU A . n 
A 1 420  LEU 420  384  384  LEU LEU A . n 
A 1 421  ASP 421  385  385  ASP ASP A . n 
A 1 422  LYS 422  386  386  LYS LYS A . n 
A 1 423  THR 423  387  387  THR THR A . n 
A 1 424  VAL 424  388  388  VAL VAL A . n 
A 1 425  SER 425  389  389  SER SER A . n 
A 1 426  ASP 426  390  390  ASP ASP A . n 
A 1 427  ASN 427  391  391  ASN ASN A . n 
A 1 428  ILE 428  392  392  ILE ILE A . n 
A 1 429  ILE 429  393  393  ILE ILE A . n 
A 1 430  ASN 430  394  394  ASN ASN A . n 
A 1 431  GLY 431  395  395  GLY GLY A . n 
A 1 432  ARG 432  396  396  ARG ARG A . n 
A 1 433  TRP 433  397  397  TRP TRP A . n 
A 1 434  ILE 434  398  398  ILE ILE A . n 
A 1 435  ILE 435  399  399  ILE ILE A . n 
A 1 436  LEU 436  400  400  LEU LEU A . n 
A 1 437  LEU 437  401  401  LEU LEU A . n 
A 1 438  SER 438  402  402  SER SER A . n 
A 1 439  LYS 439  403  403  LYS LYS A . n 
A 1 440  PHE 440  404  404  PHE PHE A . n 
A 1 441  LEU 441  405  405  LEU LEU A . n 
A 1 442  LYS 442  406  406  LYS LYS A . n 
A 1 443  LEU 443  407  407  LEU LEU A . n 
A 1 444  ILE 444  408  408  ILE ILE A . n 
A 1 445  LYS 445  409  409  LYS LYS A . n 
A 1 446  LEU 446  410  410  LEU LEU A . n 
A 1 447  ALA 447  411  411  ALA ALA A . n 
A 1 448  GLY 448  412  412  GLY GLY A . n 
A 1 449  ASP 449  413  413  ASP ASP A . n 
A 1 450  ASN 450  414  414  ASN ASN A . n 
A 1 451  ASN 451  415  415  ASN ASN A . n 
A 1 452  LEU 452  416  416  LEU LEU A . n 
A 1 453  ASN 453  417  417  ASN ASN A . n 
A 1 454  ASN 454  418  418  ASN ASN A . n 
A 1 455  LEU 455  419  419  LEU LEU A . n 
A 1 456  SER 456  420  420  SER SER A . n 
A 1 457  GLU 457  421  421  GLU GLU A . n 
A 1 458  LEU 458  422  422  LEU LEU A . n 
A 1 459  TYR 459  423  423  TYR TYR A . n 
A 1 460  PHE 460  424  424  PHE PHE A . n 
A 1 461  LEU 461  425  425  LEU LEU A . n 
A 1 462  PHE 462  426  426  PHE PHE A . n 
A 1 463  ARG 463  427  427  ARG ARG A . n 
A 1 464  ILE 464  428  428  ILE ILE A . n 
A 1 465  PHE 465  429  429  PHE PHE A . n 
A 1 466  GLY 466  430  430  GLY GLY A . n 
A 1 467  HIS 467  431  431  HIS HIS A . n 
A 1 468  PRO 468  432  432  PRO PRO A . n 
A 1 469  MET 469  433  433  MET MET A . n 
A 1 470  VAL 470  434  434  VAL VAL A . n 
A 1 471  ASP 471  435  435  ASP ASP A . n 
A 1 472  GLU 472  436  436  GLU GLU A . n 
A 1 473  ARG 473  437  437  ARG ARG A . n 
A 1 474  GLN 474  438  438  GLN GLN A . n 
A 1 475  ALA 475  439  439  ALA ALA A . n 
A 1 476  MET 476  440  440  MET MET A . n 
A 1 477  ASP 477  441  441  ASP ASP A . n 
A 1 478  ALA 478  442  442  ALA ALA A . n 
A 1 479  VAL 479  443  443  VAL VAL A . n 
A 1 480  LYS 480  444  444  LYS LYS A . n 
A 1 481  ILE 481  445  445  ILE ILE A . n 
A 1 482  ASN 482  446  446  ASN ASN A . n 
A 1 483  CYS 483  447  447  CYS CYS A . n 
A 1 484  ASN 484  448  448  ASN ASN A . n 
A 1 485  GLU 485  449  449  GLU GLU A . n 
A 1 486  THR 486  450  450  THR THR A . n 
A 1 487  LYS 487  451  451  LYS LYS A . n 
A 1 488  PHE 488  452  452  PHE PHE A . n 
A 1 489  TYR 489  453  453  TYR TYR A . n 
A 1 490  LEU 490  454  454  LEU LEU A . n 
A 1 491  LEU 491  455  455  LEU LEU A . n 
A 1 492  SER 492  456  456  SER SER A . n 
A 1 493  SER 493  457  457  SER SER A . n 
A 1 494  LEU 494  458  458  LEU LEU A . n 
A 1 495  SER 495  459  459  SER SER A . n 
A 1 496  MET 496  460  460  MET MET A . n 
A 1 497  LEU 497  461  461  LEU LEU A . n 
A 1 498  ARG 498  462  462  ARG ARG A . n 
A 1 499  GLY 499  463  463  GLY GLY A . n 
A 1 500  ALA 500  464  464  ALA ALA A . n 
A 1 501  PHE 501  465  465  PHE PHE A . n 
A 1 502  ILE 502  466  466  ILE ILE A . n 
A 1 503  TYR 503  467  467  TYR TYR A . n 
A 1 504  ARG 504  468  468  ARG ARG A . n 
A 1 505  ILE 505  469  469  ILE ILE A . n 
A 1 506  ILE 506  470  470  ILE ILE A . n 
A 1 507  LYS 507  471  471  LYS LYS A . n 
A 1 508  GLY 508  472  472  GLY GLY A . n 
A 1 509  PHE 509  473  473  PHE PHE A . n 
A 1 510  VAL 510  474  474  VAL VAL A . n 
A 1 511  ASN 511  475  475  ASN ASN A . n 
A 1 512  ASN 512  476  476  ASN ASN A . n 
A 1 513  TYR 513  477  477  TYR TYR A . n 
A 1 514  ASN 514  478  478  ASN ASN A . n 
A 1 515  ARG 515  479  479  ARG ARG A . n 
A 1 516  TRP 516  480  480  TRP TRP A . n 
A 1 517  PRO 517  481  481  PRO PRO A . n 
A 1 518  THR 518  482  482  THR THR A . n 
A 1 519  LEU 519  483  483  LEU LEU A . n 
A 1 520  ARG 520  484  484  ARG ARG A . n 
A 1 521  ASN 521  485  485  ASN ASN A . n 
A 1 522  ALA 522  486  486  ALA ALA A . n 
A 1 523  ILE 523  487  487  ILE ILE A . n 
A 1 524  VAL 524  488  488  VAL VAL A . n 
A 1 525  LEU 525  489  489  LEU LEU A . n 
A 1 526  PRO 526  490  490  PRO PRO A . n 
A 1 527  LEU 527  491  491  LEU LEU A . n 
A 1 528  ARG 528  492  492  ARG ARG A . n 
A 1 529  TRP 529  493  493  TRP TRP A . n 
A 1 530  LEU 530  494  494  LEU LEU A . n 
A 1 531  THR 531  495  495  THR THR A . n 
A 1 532  TYR 532  496  496  TYR TYR A . n 
A 1 533  TYR 533  497  497  TYR TYR A . n 
A 1 534  LYS 534  498  498  LYS LYS A . n 
A 1 535  LEU 535  499  499  LEU LEU A . n 
A 1 536  ASN 536  500  500  ASN ASN A . n 
A 1 537  THR 537  501  501  THR THR A . n 
A 1 538  TYR 538  502  502  TYR TYR A . n 
A 1 539  PRO 539  503  503  PRO PRO A . n 
A 1 540  SER 540  504  504  SER SER A . n 
A 1 541  LEU 541  505  505  LEU LEU A . n 
A 1 542  LEU 542  506  506  LEU LEU A . n 
A 1 543  GLU 543  507  507  GLU GLU A . n 
A 1 544  LEU 544  508  508  LEU LEU A . n 
A 1 545  THR 545  509  509  THR THR A . n 
A 1 546  GLU 546  510  510  GLU GLU A . n 
A 1 547  ARG 547  511  511  ARG ARG A . n 
A 1 548  ASP 548  512  512  ASP ASP A . n 
A 1 549  LEU 549  513  513  LEU LEU A . n 
A 1 550  ILE 550  514  514  ILE ILE A . n 
A 1 551  VAL 551  515  515  VAL VAL A . n 
A 1 552  LEU 552  516  516  LEU LEU A . n 
A 1 553  SER 553  517  517  SER SER A . n 
A 1 554  GLY 554  518  518  GLY GLY A . n 
A 1 555  LEU 555  519  519  LEU LEU A . n 
A 1 556  ARG 556  520  520  ARG ARG A . n 
A 1 557  PHE 557  521  521  PHE PHE A . n 
A 1 558  TYR 558  522  522  TYR TYR A . n 
A 1 559  ARG 559  523  523  ARG ARG A . n 
A 1 560  GLU 560  524  524  GLU GLU A . n 
A 1 561  PHE 561  525  525  PHE PHE A . n 
A 1 562  ARG 562  526  526  ARG ARG A . n 
A 1 563  LEU 563  527  527  LEU LEU A . n 
A 1 564  PRO 564  528  528  PRO PRO A . n 
A 1 565  LYS 565  529  529  LYS LYS A . n 
A 1 566  LYS 566  530  530  LYS LYS A . n 
A 1 567  VAL 567  531  531  VAL VAL A . n 
A 1 568  ASP 568  532  532  ASP ASP A . n 
A 1 569  LEU 569  533  533  LEU LEU A . n 
A 1 570  GLU 570  534  534  GLU GLU A . n 
A 1 571  MET 571  535  535  MET MET A . n 
A 1 572  ILE 572  536  536  ILE ILE A . n 
A 1 573  ILE 573  537  537  ILE ILE A . n 
A 1 574  ASN 574  538  538  ASN ASN A . n 
A 1 575  ASP 575  539  539  ASP ASP A . n 
A 1 576  LYS 576  540  540  LYS LYS A . n 
A 1 577  ALA 577  541  541  ALA ALA A . n 
A 1 578  ILE 578  542  542  ILE ILE A . n 
A 1 579  SER 579  543  543  SER SER A . n 
A 1 580  PRO 580  544  544  PRO PRO A . n 
A 1 581  PRO 581  545  545  PRO PRO A . n 
A 1 582  LYS 582  546  546  LYS LYS A . n 
A 1 583  ASN 583  547  547  ASN ASN A . n 
A 1 584  LEU 584  548  548  LEU LEU A . n 
A 1 585  ILE 585  549  549  ILE ILE A . n 
A 1 586  TRP 586  550  550  TRP TRP A . n 
A 1 587  THR 587  551  551  THR THR A . n 
A 1 588  SER 588  552  552  SER SER A . n 
A 1 589  PHE 589  553  553  PHE PHE A . n 
A 1 590  PRO 590  554  554  PRO PRO A . n 
A 1 591  ARG 591  555  555  ARG ARG A . n 
A 1 592  ASN 592  556  556  ASN ASN A . n 
A 1 593  TYR 593  557  557  TYR TYR A . n 
A 1 594  MET 594  558  558  MET MET A . n 
A 1 595  PRO 595  559  559  PRO PRO A . n 
A 1 596  SER 596  560  560  SER SER A . n 
A 1 597  HIS 597  561  561  HIS HIS A . n 
A 1 598  ILE 598  562  562  ILE ILE A . n 
A 1 599  GLN 599  563  563  GLN GLN A . n 
A 1 600  ASN 600  564  564  ASN ASN A . n 
A 1 601  TYR 601  565  565  TYR TYR A . n 
A 1 602  ILE 602  566  566  ILE ILE A . n 
A 1 603  GLU 603  567  567  GLU GLU A . n 
A 1 604  HIS 604  568  568  HIS HIS A . n 
A 1 605  GLU 605  569  569  GLU GLU A . n 
A 1 606  LYS 606  570  570  LYS LYS A . n 
A 1 607  LEU 607  571  571  LEU LEU A . n 
A 1 608  LYS 608  572  572  LYS LYS A . n 
A 1 609  PHE 609  573  573  PHE PHE A . n 
A 1 610  SER 610  574  574  SER SER A . n 
A 1 611  GLU 611  575  575  GLU GLU A . n 
A 1 612  SER 612  576  576  SER SER A . n 
A 1 613  ASP 613  577  577  ASP ASP A . n 
A 1 614  LYS 614  578  578  LYS LYS A . n 
A 1 615  SER 615  579  579  SER SER A . n 
A 1 616  ARG 616  580  580  ARG ARG A . n 
A 1 617  ARG 617  581  581  ARG ARG A . n 
A 1 618  VAL 618  582  582  VAL VAL A . n 
A 1 619  LEU 619  583  583  LEU LEU A . n 
A 1 620  GLU 620  584  584  GLU GLU A . n 
A 1 621  TYR 621  585  585  TYR TYR A . n 
A 1 622  TYR 622  586  586  TYR TYR A . n 
A 1 623  LEU 623  587  587  LEU LEU A . n 
A 1 624  ARG 624  588  588  ARG ARG A . n 
A 1 625  ASP 625  589  589  ASP ASP A . n 
A 1 626  ASN 626  590  590  ASN ASN A . n 
A 1 627  LYS 627  591  591  LYS LYS A . n 
A 1 628  PHE 628  592  592  PHE PHE A . n 
A 1 629  ASN 629  593  593  ASN ASN A . n 
A 1 630  GLU 630  594  594  GLU GLU A . n 
A 1 631  CYS 631  595  595  CYS CYS A . n 
A 1 632  ASP 632  596  596  ASP ASP A . n 
A 1 633  LEU 633  597  597  LEU LEU A . n 
A 1 634  TYR 634  598  598  TYR TYR A . n 
A 1 635  ASN 635  599  599  ASN ASN A . n 
A 1 636  CYS 636  600  600  CYS CYS A . n 
A 1 637  VAL 637  601  601  VAL VAL A . n 
A 1 638  VAL 638  602  602  VAL VAL A . n 
A 1 639  ASN 639  603  603  ASN ASN A . n 
A 1 640  GLN 640  604  604  GLN GLN A . n 
A 1 641  SER 641  605  605  SER SER A . n 
A 1 642  TYR 642  606  606  TYR TYR A . n 
A 1 643  LEU 643  607  607  LEU LEU A . n 
A 1 644  ASN 644  608  608  ASN ASN A . n 
A 1 645  ASN 645  609  609  ASN ASN A . n 
A 1 646  PRO 646  610  610  PRO PRO A . n 
A 1 647  ASN 647  611  611  ASN ASN A . n 
A 1 648  HIS 648  612  612  HIS HIS A . n 
A 1 649  VAL 649  613  613  VAL VAL A . n 
A 1 650  VAL 650  614  614  VAL VAL A . n 
A 1 651  SER 651  615  615  SER SER A . n 
A 1 652  LEU 652  616  616  LEU LEU A . n 
A 1 653  THR 653  617  617  THR THR A . n 
A 1 654  GLY 654  618  618  GLY GLY A . n 
A 1 655  LYS 655  619  ?    ?   ?   A . n 
A 1 656  GLU 656  620  ?    ?   ?   A . n 
A 1 657  ARG 657  621  ?    ?   ?   A . n 
A 1 658  GLU 658  622  ?    ?   ?   A . n 
A 1 659  LEU 659  623  ?    ?   ?   A . n 
A 1 660  SER 660  624  ?    ?   ?   A . n 
A 1 661  VAL 661  625  ?    ?   ?   A . n 
A 1 662  GLY 662  626  ?    ?   ?   A . n 
A 1 663  ARG 663  627  ?    ?   ?   A . n 
A 1 664  MET 664  628  628  MET MET A . n 
A 1 665  PHE 665  629  629  PHE PHE A . n 
A 1 666  ALA 666  630  630  ALA ALA A . n 
A 1 667  MET 667  631  631  MET MET A . n 
A 1 668  GLN 668  632  632  GLN GLN A . n 
A 1 669  PRO 669  633  633  PRO PRO A . n 
A 1 670  GLY 670  634  634  GLY GLY A . n 
A 1 671  MET 671  635  635  MET MET A . n 
A 1 672  PHE 672  636  636  PHE PHE A . n 
A 1 673  ARG 673  637  637  ARG ARG A . n 
A 1 674  GLN 674  638  638  GLN GLN A . n 
A 1 675  VAL 675  639  639  VAL VAL A . n 
A 1 676  GLN 676  640  640  GLN GLN A . n 
A 1 677  ILE 677  641  641  ILE ILE A . n 
A 1 678  LEU 678  642  642  LEU LEU A . n 
A 1 679  ALA 679  643  643  ALA ALA A . n 
A 1 680  GLU 680  644  644  GLU GLU A . n 
A 1 681  LYS 681  645  645  LYS LYS A . n 
A 1 682  MET 682  646  646  MET MET A . n 
A 1 683  ILE 683  647  647  ILE ILE A . n 
A 1 684  ALA 684  648  648  ALA ALA A . n 
A 1 685  GLU 685  649  649  GLU GLU A . n 
A 1 686  ASN 686  650  650  ASN ASN A . n 
A 1 687  ILE 687  651  651  ILE ILE A . n 
A 1 688  LEU 688  652  652  LEU LEU A . n 
A 1 689  GLN 689  653  653  GLN GLN A . n 
A 1 690  PHE 690  654  654  PHE PHE A . n 
A 1 691  PHE 691  655  655  PHE PHE A . n 
A 1 692  PRO 692  656  656  PRO PRO A . n 
A 1 693  GLU 693  657  657  GLU GLU A . n 
A 1 694  SER 694  658  658  SER SER A . n 
A 1 695  LEU 695  659  659  LEU LEU A . n 
A 1 696  THR 696  660  ?    ?   ?   A . n 
A 1 697  ARG 697  661  ?    ?   ?   A . n 
A 1 698  TYR 698  662  ?    ?   ?   A . n 
A 1 699  GLY 699  663  ?    ?   ?   A . n 
A 1 700  ASP 700  664  ?    ?   ?   A . n 
A 1 701  LEU 701  665  ?    ?   ?   A . n 
A 1 702  GLU 702  666  ?    ?   ?   A . n 
A 1 703  LEU 703  667  ?    ?   ?   A . n 
A 1 704  GLN 704  668  ?    ?   ?   A . n 
A 1 705  LYS 705  669  ?    ?   ?   A . n 
A 1 706  ILE 706  670  ?    ?   ?   A . n 
A 1 707  LEU 707  671  ?    ?   ?   A . n 
A 1 708  GLU 708  672  ?    ?   ?   A . n 
A 1 709  LEU 709  673  ?    ?   ?   A . n 
A 1 710  LYS 710  674  ?    ?   ?   A . n 
A 1 711  ALA 711  675  ?    ?   ?   A . n 
A 1 712  GLY 712  676  ?    ?   ?   A . n 
A 1 713  ILE 713  677  ?    ?   ?   A . n 
A 1 714  SER 714  678  ?    ?   ?   A . n 
A 1 715  ASN 715  679  ?    ?   ?   A . n 
A 1 716  LYS 716  680  ?    ?   ?   A . n 
A 1 717  SER 717  681  ?    ?   ?   A . n 
A 1 718  ASN 718  682  ?    ?   ?   A . n 
A 1 719  ARG 719  683  ?    ?   ?   A . n 
A 1 720  TYR 720  684  ?    ?   ?   A . n 
A 1 721  ASN 721  685  ?    ?   ?   A . n 
A 1 722  ASP 722  686  ?    ?   ?   A . n 
A 1 723  ASN 723  687  ?    ?   ?   A . n 
A 1 724  TYR 724  688  ?    ?   ?   A . n 
A 1 725  ASN 725  689  689  ASN ASN A . n 
A 1 726  ASN 726  690  690  ASN ASN A . n 
A 1 727  TYR 727  691  691  TYR TYR A . n 
A 1 728  ILE 728  692  692  ILE ILE A . n 
A 1 729  SER 729  693  693  SER SER A . n 
A 1 730  LYS 730  694  694  LYS LYS A . n 
A 1 731  CYS 731  695  695  CYS CYS A . n 
A 1 732  SER 732  696  696  SER SER A . n 
A 1 733  ILE 733  697  697  ILE ILE A . n 
A 1 734  ILE 734  698  698  ILE ILE A . n 
A 1 735  THR 735  699  699  THR THR A . n 
A 1 736  ASP 736  700  700  ASP ASP A . n 
A 1 737  LEU 737  701  701  LEU LEU A . n 
A 1 738  SER 738  702  702  SER SER A . n 
A 1 739  LYS 739  703  703  LYS LYS A . n 
A 1 740  PHE 740  704  704  PHE PHE A . n 
A 1 741  ASN 741  705  705  ASN ASN A . n 
A 1 742  GLN 742  706  706  GLN GLN A . n 
A 1 743  ALA 743  707  707  ALA ALA A . n 
A 1 744  PHE 744  708  708  PHE PHE A . n 
A 1 745  ARG 745  709  709  ARG ARG A . n 
A 1 746  TYR 746  710  710  TYR TYR A . n 
A 1 747  GLU 747  711  711  GLU GLU A . n 
A 1 748  THR 748  712  712  THR THR A . n 
A 1 749  SER 749  713  713  SER SER A . n 
A 1 750  CYS 750  714  714  CYS CYS A . n 
A 1 751  ILE 751  715  715  ILE ILE A . n 
A 1 752  CYS 752  716  716  CYS CYS A . n 
A 1 753  SER 753  717  717  SER SER A . n 
A 1 754  ASP 754  718  718  ASP ASP A . n 
A 1 755  VAL 755  719  719  VAL VAL A . n 
A 1 756  LEU 756  720  720  LEU LEU A . n 
A 1 757  ASP 757  721  721  ASP ASP A . n 
A 1 758  GLU 758  722  722  GLU GLU A . n 
A 1 759  LEU 759  723  723  LEU LEU A . n 
A 1 760  HIS 760  724  724  HIS HIS A . n 
A 1 761  GLY 761  725  725  GLY GLY A . n 
A 1 762  VAL 762  726  726  VAL VAL A . n 
A 1 763  GLN 763  727  727  GLN GLN A . n 
A 1 764  SER 764  728  728  SER SER A . n 
A 1 765  LEU 765  729  729  LEU LEU A . n 
A 1 766  PHE 766  730  730  PHE PHE A . n 
A 1 767  SER 767  731  731  SER SER A . n 
A 1 768  TRP 768  732  732  TRP TRP A . n 
A 1 769  LEU 769  733  733  LEU LEU A . n 
A 1 770  HIS 770  734  734  HIS HIS A . n 
A 1 771  LEU 771  735  735  LEU LEU A . n 
A 1 772  THR 772  736  736  THR THR A . n 
A 1 773  ILE 773  737  737  ILE ILE A . n 
A 1 774  PRO 774  738  738  PRO PRO A . n 
A 1 775  HIS 775  739  739  HIS HIS A . n 
A 1 776  VAL 776  740  740  VAL VAL A . n 
A 1 777  THR 777  741  741  THR THR A . n 
A 1 778  ILE 778  742  742  ILE ILE A . n 
A 1 779  ILE 779  743  743  ILE ILE A . n 
A 1 780  CYS 780  744  744  CYS CYS A . n 
A 1 781  THR 781  745  745  THR THR A . n 
A 1 782  TYR 782  746  746  TYR TYR A . n 
A 1 783  ARG 783  747  747  ARG ARG A . n 
A 1 784  HIS 784  748  748  HIS HIS A . n 
A 1 785  ALA 785  749  749  ALA ALA A . n 
A 1 786  PRO 786  750  750  PRO PRO A . n 
A 1 787  PRO 787  751  751  PRO PRO A . n 
A 1 788  TYR 788  752  752  TYR TYR A . n 
A 1 789  ILE 789  753  753  ILE ILE A . n 
A 1 790  GLY 790  754  754  GLY GLY A . n 
A 1 791  ASP 791  755  755  ASP ASP A . n 
A 1 792  HIS 792  756  756  HIS HIS A . n 
A 1 793  ILE 793  757  757  ILE ILE A . n 
A 1 794  VAL 794  758  758  VAL VAL A . n 
A 1 795  ASP 795  759  759  ASP ASP A . n 
A 1 796  LEU 796  760  760  LEU LEU A . n 
A 1 797  ASN 797  761  761  ASN ASN A . n 
A 1 798  ASN 798  762  762  ASN ASN A . n 
A 1 799  VAL 799  763  763  VAL VAL A . n 
A 1 800  ASP 800  764  764  ASP ASP A . n 
A 1 801  GLU 801  765  765  GLU GLU A . n 
A 1 802  GLN 802  766  766  GLN GLN A . n 
A 1 803  SER 803  767  767  SER SER A . n 
A 1 804  GLY 804  768  768  GLY GLY A . n 
A 1 805  LEU 805  769  769  LEU LEU A . n 
A 1 806  TYR 806  770  770  TYR TYR A . n 
A 1 807  ARG 807  771  771  ARG ARG A . n 
A 1 808  TYR 808  772  772  TYR TYR A . n 
A 1 809  HIS 809  773  773  HIS HIS A . n 
A 1 810  MET 810  774  774  MET MET A . n 
A 1 811  GLY 811  775  775  GLY GLY A . n 
A 1 812  GLY 812  776  776  GLY GLY A . n 
A 1 813  ILE 813  777  777  ILE ILE A . n 
A 1 814  GLU 814  778  778  GLU GLU A . n 
A 1 815  GLY 815  779  779  GLY GLY A . n 
A 1 816  TRP 816  780  780  TRP TRP A . n 
A 1 817  CYS 817  781  781  CYS CYS A . n 
A 1 818  GLN 818  782  782  GLN GLN A . n 
A 1 819  LYS 819  783  783  LYS LYS A . n 
A 1 820  LEU 820  784  784  LEU LEU A . n 
A 1 821  TRP 821  785  785  TRP TRP A . n 
A 1 822  THR 822  786  786  THR THR A . n 
A 1 823  ILE 823  787  787  ILE ILE A . n 
A 1 824  GLU 824  788  788  GLU GLU A . n 
A 1 825  ALA 825  789  789  ALA ALA A . n 
A 1 826  ILE 826  790  790  ILE ILE A . n 
A 1 827  SER 827  791  791  SER SER A . n 
A 1 828  LEU 828  792  792  LEU LEU A . n 
A 1 829  LEU 829  793  793  LEU LEU A . n 
A 1 830  ASP 830  794  794  ASP ASP A . n 
A 1 831  LEU 831  795  795  LEU LEU A . n 
A 1 832  ILE 832  796  796  ILE ILE A . n 
A 1 833  SER 833  797  797  SER SER A . n 
A 1 834  LEU 834  798  798  LEU LEU A . n 
A 1 835  LYS 835  799  799  LYS LYS A . n 
A 1 836  GLY 836  800  800  GLY GLY A . n 
A 1 837  LYS 837  801  801  LYS LYS A . n 
A 1 838  PHE 838  802  802  PHE PHE A . n 
A 1 839  SER 839  803  803  SER SER A . n 
A 1 840  ILE 840  804  804  ILE ILE A . n 
A 1 841  THR 841  805  805  THR THR A . n 
A 1 842  ALA 842  806  806  ALA ALA A . n 
A 1 843  LEU 843  807  807  LEU LEU A . n 
A 1 844  ILE 844  808  808  ILE ILE A . n 
A 1 845  ASN 845  809  809  ASN ASN A . n 
A 1 846  GLY 846  810  810  GLY GLY A . n 
A 1 847  ASP 847  811  811  ASP ASP A . n 
A 1 848  ASN 848  812  812  ASN ASN A . n 
A 1 849  GLN 849  813  813  GLN GLN A . n 
A 1 850  SER 850  814  814  SER SER A . n 
A 1 851  ILE 851  815  815  ILE ILE A . n 
A 1 852  ASP 852  816  816  ASP ASP A . n 
A 1 853  ILE 853  817  817  ILE ILE A . n 
A 1 854  SER 854  818  818  SER SER A . n 
A 1 855  LYS 855  819  819  LYS LYS A . n 
A 1 856  PRO 856  820  820  PRO PRO A . n 
A 1 857  ILE 857  821  821  ILE ILE A . n 
A 1 858  ARG 858  822  822  ARG ARG A . n 
A 1 859  LEU 859  823  823  LEU LEU A . n 
A 1 860  MET 860  824  824  MET MET A . n 
A 1 861  GLU 861  825  825  GLU GLU A . n 
A 1 862  GLY 862  826  826  GLY GLY A . n 
A 1 863  GLN 863  827  827  GLN GLN A . n 
A 1 864  THR 864  828  828  THR THR A . n 
A 1 865  HIS 865  829  829  HIS HIS A . n 
A 1 866  ALA 866  830  830  ALA ALA A . n 
A 1 867  GLN 867  831  831  GLN GLN A . n 
A 1 868  ALA 868  832  832  ALA ALA A . n 
A 1 869  ASP 869  833  833  ASP ASP A . n 
A 1 870  TYR 870  834  834  TYR TYR A . n 
A 1 871  LEU 871  835  835  LEU LEU A . n 
A 1 872  LEU 872  836  836  LEU LEU A . n 
A 1 873  ALA 873  837  837  ALA ALA A . n 
A 1 874  LEU 874  838  838  LEU LEU A . n 
A 1 875  ASN 875  839  839  ASN ASN A . n 
A 1 876  SER 876  840  840  SER SER A . n 
A 1 877  LEU 877  841  841  LEU LEU A . n 
A 1 878  LYS 878  842  842  LYS LYS A . n 
A 1 879  LEU 879  843  843  LEU LEU A . n 
A 1 880  LEU 880  844  844  LEU LEU A . n 
A 1 881  TYR 881  845  845  TYR TYR A . n 
A 1 882  LYS 882  846  846  LYS LYS A . n 
A 1 883  GLU 883  847  847  GLU GLU A . n 
A 1 884  TYR 884  848  848  TYR TYR A . n 
A 1 885  ALA 885  849  849  ALA ALA A . n 
A 1 886  GLY 886  850  850  GLY GLY A . n 
A 1 887  ILE 887  851  851  ILE ILE A . n 
A 1 888  GLY 888  852  852  GLY GLY A . n 
A 1 889  HIS 889  853  853  HIS HIS A . n 
A 1 890  LYS 890  854  854  LYS LYS A . n 
A 1 891  LEU 891  855  855  LEU LEU A . n 
A 1 892  LYS 892  856  856  LYS LYS A . n 
A 1 893  GLY 893  857  857  GLY GLY A . n 
A 1 894  THR 894  858  858  THR THR A . n 
A 1 895  GLU 895  859  859  GLU GLU A . n 
A 1 896  THR 896  860  860  THR THR A . n 
A 1 897  TYR 897  861  861  TYR TYR A . n 
A 1 898  ILE 898  862  862  ILE ILE A . n 
A 1 899  SER 899  863  863  SER SER A . n 
A 1 900  ARG 900  864  864  ARG ARG A . n 
A 1 901  ASP 901  865  865  ASP ASP A . n 
A 1 902  MET 902  866  866  MET MET A . n 
A 1 903  GLN 903  867  867  GLN GLN A . n 
A 1 904  PHE 904  868  868  PHE PHE A . n 
A 1 905  MET 905  869  869  MET MET A . n 
A 1 906  SER 906  870  870  SER SER A . n 
A 1 907  LYS 907  871  871  LYS LYS A . n 
A 1 908  THR 908  872  872  THR THR A . n 
A 1 909  ILE 909  873  873  ILE ILE A . n 
A 1 910  GLN 910  874  874  GLN GLN A . n 
A 1 911  HIS 911  875  875  HIS HIS A . n 
A 1 912  ASN 912  876  876  ASN ASN A . n 
A 1 913  GLY 913  877  877  GLY GLY A . n 
A 1 914  VAL 914  878  878  VAL VAL A . n 
A 1 915  TYR 915  879  879  TYR TYR A . n 
A 1 916  TYR 916  880  880  TYR TYR A . n 
A 1 917  PRO 917  881  881  PRO PRO A . n 
A 1 918  ALA 918  882  882  ALA ALA A . n 
A 1 919  SER 919  883  883  SER SER A . n 
A 1 920  ILE 920  884  884  ILE ILE A . n 
A 1 921  LYS 921  885  885  LYS LYS A . n 
A 1 922  LYS 922  886  886  LYS LYS A . n 
A 1 923  VAL 923  887  887  VAL VAL A . n 
A 1 924  LEU 924  888  888  LEU LEU A . n 
A 1 925  ARG 925  889  889  ARG ARG A . n 
A 1 926  VAL 926  890  890  VAL VAL A . n 
A 1 927  GLY 927  891  891  GLY GLY A . n 
A 1 928  PRO 928  892  892  PRO PRO A . n 
A 1 929  TRP 929  893  893  TRP TRP A . n 
A 1 930  ILE 930  894  894  ILE ILE A . n 
A 1 931  ASN 931  895  895  ASN ASN A . n 
A 1 932  THR 932  896  896  THR THR A . n 
A 1 933  ILE 933  897  897  ILE ILE A . n 
A 1 934  LEU 934  898  898  LEU LEU A . n 
A 1 935  ASP 935  899  899  ASP ASP A . n 
A 1 936  ASP 936  900  900  ASP ASP A . n 
A 1 937  PHE 937  901  901  PHE PHE A . n 
A 1 938  LYS 938  902  902  LYS LYS A . n 
A 1 939  VAL 939  903  903  VAL VAL A . n 
A 1 940  SER 940  904  904  SER SER A . n 
A 1 941  LEU 941  905  905  LEU LEU A . n 
A 1 942  GLU 942  906  906  GLU GLU A . n 
A 1 943  SER 943  907  907  SER SER A . n 
A 1 944  ILE 944  908  908  ILE ILE A . n 
A 1 945  GLY 945  909  909  GLY GLY A . n 
A 1 946  SER 946  910  910  SER SER A . n 
A 1 947  LEU 947  911  911  LEU LEU A . n 
A 1 948  THR 948  912  912  THR THR A . n 
A 1 949  GLN 949  913  913  GLN GLN A . n 
A 1 950  GLU 950  914  914  GLU GLU A . n 
A 1 951  LEU 951  915  915  LEU LEU A . n 
A 1 952  GLU 952  916  916  GLU GLU A . n 
A 1 953  TYR 953  917  917  TYR TYR A . n 
A 1 954  ARG 954  918  918  ARG ARG A . n 
A 1 955  GLY 955  919  919  GLY GLY A . n 
A 1 956  GLU 956  920  920  GLU GLU A . n 
A 1 957  SER 957  921  921  SER SER A . n 
A 1 958  LEU 958  922  922  LEU LEU A . n 
A 1 959  LEU 959  923  923  LEU LEU A . n 
A 1 960  CYS 960  924  924  CYS CYS A . n 
A 1 961  SER 961  925  925  SER SER A . n 
A 1 962  LEU 962  926  926  LEU LEU A . n 
A 1 963  ILE 963  927  927  ILE ILE A . n 
A 1 964  PHE 964  928  928  PHE PHE A . n 
A 1 965  ARG 965  929  929  ARG ARG A . n 
A 1 966  ASN 966  930  930  ASN ASN A . n 
A 1 967  VAL 967  931  931  VAL VAL A . n 
A 1 968  TRP 968  932  932  TRP TRP A . n 
A 1 969  LEU 969  933  933  LEU LEU A . n 
A 1 970  TYR 970  934  934  TYR TYR A . n 
A 1 971  ASN 971  935  935  ASN ASN A . n 
A 1 972  GLN 972  936  936  GLN GLN A . n 
A 1 973  ILE 973  937  937  ILE ILE A . n 
A 1 974  ALA 974  938  938  ALA ALA A . n 
A 1 975  LEU 975  939  939  LEU LEU A . n 
A 1 976  GLN 976  940  940  GLN GLN A . n 
A 1 977  LEU 977  941  941  LEU LEU A . n 
A 1 978  LYS 978  942  942  LYS LYS A . n 
A 1 979  ASN 979  943  943  ASN ASN A . n 
A 1 980  HIS 980  944  944  HIS HIS A . n 
A 1 981  ALA 981  945  945  ALA ALA A . n 
A 1 982  LEU 982  946  946  LEU LEU A . n 
A 1 983  CYS 983  947  947  CYS CYS A . n 
A 1 984  ASN 984  948  948  ASN ASN A . n 
A 1 985  ASN 985  949  949  ASN ASN A . n 
A 1 986  LYS 986  950  950  LYS LYS A . n 
A 1 987  LEU 987  951  951  LEU LEU A . n 
A 1 988  TYR 988  952  952  TYR TYR A . n 
A 1 989  LEU 989  953  953  LEU LEU A . n 
A 1 990  ASP 990  954  954  ASP ASP A . n 
A 1 991  ILE 991  955  955  ILE ILE A . n 
A 1 992  LEU 992  956  956  LEU LEU A . n 
A 1 993  LYS 993  957  957  LYS LYS A . n 
A 1 994  VAL 994  958  958  VAL VAL A . n 
A 1 995  LEU 995  959  959  LEU LEU A . n 
A 1 996  LYS 996  960  960  LYS LYS A . n 
A 1 997  HIS 997  961  961  HIS HIS A . n 
A 1 998  LEU 998  962  962  LEU LEU A . n 
A 1 999  LYS 999  963  963  LYS LYS A . n 
A 1 1000 THR 1000 964  964  THR THR A . n 
A 1 1001 PHE 1001 965  965  PHE PHE A . n 
A 1 1002 PHE 1002 966  966  PHE PHE A . n 
A 1 1003 ASN 1003 967  967  ASN ASN A . n 
A 1 1004 LEU 1004 968  968  LEU LEU A . n 
A 1 1005 ASP 1005 969  969  ASP ASP A . n 
A 1 1006 ASN 1006 970  970  ASN ASN A . n 
A 1 1007 ILE 1007 971  971  ILE ILE A . n 
A 1 1008 ASP 1008 972  972  ASP ASP A . n 
A 1 1009 THR 1009 973  973  THR THR A . n 
A 1 1010 ALA 1010 974  974  ALA ALA A . n 
A 1 1011 LEU 1011 975  975  LEU LEU A . n 
A 1 1012 THR 1012 976  976  THR THR A . n 
A 1 1013 LEU 1013 977  977  LEU LEU A . n 
A 1 1014 TYR 1014 978  978  TYR TYR A . n 
A 1 1015 MET 1015 979  979  MET MET A . n 
A 1 1016 ASN 1016 980  980  ASN ASN A . n 
A 1 1017 LEU 1017 981  981  LEU LEU A . n 
A 1 1018 PRO 1018 982  982  PRO PRO A . n 
A 1 1019 MET 1019 983  983  MET MET A . n 
A 1 1020 LEU 1020 984  984  LEU LEU A . n 
A 1 1021 PHE 1021 985  985  PHE PHE A . n 
A 1 1022 GLY 1022 986  986  GLY GLY A . n 
A 1 1023 GLY 1023 987  987  GLY GLY A . n 
A 1 1024 GLY 1024 988  988  GLY GLY A . n 
A 1 1025 ASP 1025 989  989  ASP ASP A . n 
A 1 1026 PRO 1026 990  990  PRO PRO A . n 
A 1 1027 ASN 1027 991  991  ASN ASN A . n 
A 1 1028 LEU 1028 992  992  LEU LEU A . n 
A 1 1029 LEU 1029 993  993  LEU LEU A . n 
A 1 1030 TYR 1030 994  994  TYR TYR A . n 
A 1 1031 ARG 1031 995  995  ARG ARG A . n 
A 1 1032 SER 1032 996  996  SER SER A . n 
A 1 1033 PHE 1033 997  997  PHE PHE A . n 
A 1 1034 TYR 1034 998  998  TYR TYR A . n 
A 1 1035 ARG 1035 999  999  ARG ARG A . n 
A 1 1036 ARG 1036 1000 1000 ARG ARG A . n 
A 1 1037 THR 1037 1001 1001 THR THR A . n 
A 1 1038 PRO 1038 1002 1002 PRO PRO A . n 
A 1 1039 ASP 1039 1003 1003 ASP ASP A . n 
A 1 1040 PHE 1040 1004 1004 PHE PHE A . n 
A 1 1041 LEU 1041 1005 1005 LEU LEU A . n 
A 1 1042 THR 1042 1006 1006 THR THR A . n 
A 1 1043 GLU 1043 1007 1007 GLU GLU A . n 
A 1 1044 ALA 1044 1008 1008 ALA ALA A . n 
A 1 1045 ILE 1045 1009 1009 ILE ILE A . n 
A 1 1046 VAL 1046 1010 1010 VAL VAL A . n 
A 1 1047 HIS 1047 1011 1011 HIS HIS A . n 
A 1 1048 SER 1048 1012 1012 SER SER A . n 
A 1 1049 VAL 1049 1013 1013 VAL VAL A . n 
A 1 1050 PHE 1050 1014 1014 PHE PHE A . n 
A 1 1051 ILE 1051 1015 1015 ILE ILE A . n 
A 1 1052 LEU 1052 1016 1016 LEU LEU A . n 
A 1 1053 SER 1053 1017 1017 SER SER A . n 
A 1 1054 TYR 1054 1018 1018 TYR TYR A . n 
A 1 1055 TYR 1055 1019 1019 TYR TYR A . n 
A 1 1056 THR 1056 1020 1020 THR THR A . n 
A 1 1057 ASN 1057 1021 1021 ASN ASN A . n 
A 1 1058 HIS 1058 1022 1022 HIS HIS A . n 
A 1 1059 ASP 1059 1023 1023 ASP ASP A . n 
A 1 1060 LEU 1060 1024 1024 LEU LEU A . n 
A 1 1061 LYS 1061 1025 1025 LYS LYS A . n 
A 1 1062 ASP 1062 1026 1026 ASP ASP A . n 
A 1 1063 LYS 1063 1027 1027 LYS LYS A . n 
A 1 1064 LEU 1064 1028 1028 LEU LEU A . n 
A 1 1065 GLN 1065 1029 1029 GLN GLN A . n 
A 1 1066 ASP 1066 1030 1030 ASP ASP A . n 
A 1 1067 LEU 1067 1031 1031 LEU LEU A . n 
A 1 1068 SER 1068 1032 1032 SER SER A . n 
A 1 1069 ASP 1069 1033 1033 ASP ASP A . n 
A 1 1070 ASP 1070 1034 1034 ASP ASP A . n 
A 1 1071 ARG 1071 1035 1035 ARG ARG A . n 
A 1 1072 LEU 1072 1036 1036 LEU LEU A . n 
A 1 1073 ASN 1073 1037 1037 ASN ASN A . n 
A 1 1074 LYS 1074 1038 1038 LYS LYS A . n 
A 1 1075 PHE 1075 1039 1039 PHE PHE A . n 
A 1 1076 LEU 1076 1040 1040 LEU LEU A . n 
A 1 1077 THR 1077 1041 1041 THR THR A . n 
A 1 1078 CYS 1078 1042 1042 CYS CYS A . n 
A 1 1079 ILE 1079 1043 1043 ILE ILE A . n 
A 1 1080 ILE 1080 1044 1044 ILE ILE A . n 
A 1 1081 THR 1081 1045 1045 THR THR A . n 
A 1 1082 PHE 1082 1046 1046 PHE PHE A . n 
A 1 1083 ASP 1083 1047 1047 ASP ASP A . n 
A 1 1084 LYS 1084 1048 1048 LYS LYS A . n 
A 1 1085 ASN 1085 1049 1049 ASN ASN A . n 
A 1 1086 PRO 1086 1050 1050 PRO PRO A . n 
A 1 1087 ASN 1087 1051 1051 ASN ASN A . n 
A 1 1088 ALA 1088 1052 1052 ALA ALA A . n 
A 1 1089 GLU 1089 1053 1053 GLU GLU A . n 
A 1 1090 PHE 1090 1054 1054 PHE PHE A . n 
A 1 1091 VAL 1091 1055 1055 VAL VAL A . n 
A 1 1092 THR 1092 1056 1056 THR THR A . n 
A 1 1093 LEU 1093 1057 1057 LEU LEU A . n 
A 1 1094 MET 1094 1058 1058 MET MET A . n 
A 1 1095 ARG 1095 1059 1059 ARG ARG A . n 
A 1 1096 ASP 1096 1060 1060 ASP ASP A . n 
A 1 1097 PRO 1097 1061 1061 PRO PRO A . n 
A 1 1098 GLN 1098 1062 1062 GLN GLN A . n 
A 1 1099 ALA 1099 1063 1063 ALA ALA A . n 
A 1 1100 LEU 1100 1064 1064 LEU LEU A . n 
A 1 1101 GLY 1101 1065 1065 GLY GLY A . n 
A 1 1102 SER 1102 1066 1066 SER SER A . n 
A 1 1103 GLU 1103 1067 1067 GLU GLU A . n 
A 1 1104 ARG 1104 1068 1068 ARG ARG A . n 
A 1 1105 GLN 1105 1069 1069 GLN GLN A . n 
A 1 1106 ALA 1106 1070 1070 ALA ALA A . n 
A 1 1107 LYS 1107 1071 1071 LYS LYS A . n 
A 1 1108 ILE 1108 1072 1072 ILE ILE A . n 
A 1 1109 THR 1109 1073 1073 THR THR A . n 
A 1 1110 SER 1110 1074 1074 SER SER A . n 
A 1 1111 GLU 1111 1075 1075 GLU GLU A . n 
A 1 1112 ILE 1112 1076 1076 ILE ILE A . n 
A 1 1113 ASN 1113 1077 1077 ASN ASN A . n 
A 1 1114 ARG 1114 1078 1078 ARG ARG A . n 
A 1 1115 LEU 1115 1079 1079 LEU LEU A . n 
A 1 1116 ALA 1116 1080 1080 ALA ALA A . n 
A 1 1117 VAL 1117 1081 1081 VAL VAL A . n 
A 1 1118 THR 1118 1082 1082 THR THR A . n 
A 1 1119 GLU 1119 1083 1083 GLU GLU A . n 
A 1 1120 VAL 1120 1084 1084 VAL VAL A . n 
A 1 1121 LEU 1121 1085 1085 LEU LEU A . n 
A 1 1122 SER 1122 1086 1086 SER SER A . n 
A 1 1123 THR 1123 1087 1087 THR THR A . n 
A 1 1124 ALA 1124 1088 1088 ALA ALA A . n 
A 1 1125 PRO 1125 1089 1089 PRO PRO A . n 
A 1 1126 ASN 1126 1090 1090 ASN ASN A . n 
A 1 1127 LYS 1127 1091 1091 LYS LYS A . n 
A 1 1128 ILE 1128 1092 1092 ILE ILE A . n 
A 1 1129 PHE 1129 1093 1093 PHE PHE A . n 
A 1 1130 SER 1130 1094 1094 SER SER A . n 
A 1 1131 LYS 1131 1095 1095 LYS LYS A . n 
A 1 1132 SER 1132 1096 1096 SER SER A . n 
A 1 1133 ALA 1133 1097 1097 ALA ALA A . n 
A 1 1134 GLN 1134 1098 1098 GLN GLN A . n 
A 1 1135 HIS 1135 1099 1099 HIS HIS A . n 
A 1 1136 TYR 1136 1100 1100 TYR TYR A . n 
A 1 1137 THR 1137 1101 1101 THR THR A . n 
A 1 1138 THR 1138 1102 1102 THR THR A . n 
A 1 1139 THR 1139 1103 1103 THR THR A . n 
A 1 1140 GLU 1140 1104 1104 GLU GLU A . n 
A 1 1141 ILE 1141 1105 1105 ILE ILE A . n 
A 1 1142 ASP 1142 1106 1106 ASP ASP A . n 
A 1 1143 LEU 1143 1107 1107 LEU LEU A . n 
A 1 1144 ASN 1144 1108 1108 ASN ASN A . n 
A 1 1145 ASP 1145 1109 1109 ASP ASP A . n 
A 1 1146 ILE 1146 1110 1110 ILE ILE A . n 
A 1 1147 MET 1147 1111 1111 MET MET A . n 
A 1 1148 GLN 1148 1112 1112 GLN GLN A . n 
A 1 1149 ASN 1149 1113 1113 ASN ASN A . n 
A 1 1150 ILE 1150 1114 1114 ILE ILE A . n 
A 1 1151 GLU 1151 1115 1115 GLU GLU A . n 
A 1 1152 PRO 1152 1116 1116 PRO PRO A . n 
A 1 1153 THR 1153 1117 1117 THR THR A . n 
A 1 1154 TYR 1154 1118 1118 TYR TYR A . n 
A 1 1155 PRO 1155 1119 1119 PRO PRO A . n 
A 1 1156 HIS 1156 1120 1120 HIS HIS A . n 
A 1 1157 GLY 1157 1121 1121 GLY GLY A . n 
A 1 1158 LEU 1158 1122 1122 LEU LEU A . n 
A 1 1159 ARG 1159 1123 1123 ARG ARG A . n 
A 1 1160 VAL 1160 1124 1124 VAL VAL A . n 
A 1 1161 VAL 1161 1125 1125 VAL VAL A . n 
A 1 1162 TYR 1162 1126 1126 TYR TYR A . n 
A 1 1163 GLU 1163 1127 1127 GLU GLU A . n 
A 1 1164 SER 1164 1128 1128 SER SER A . n 
A 1 1165 LEU 1165 1129 1129 LEU LEU A . n 
A 1 1166 PRO 1166 1130 1130 PRO PRO A . n 
A 1 1167 PHE 1167 1131 1131 PHE PHE A . n 
A 1 1168 TYR 1168 1132 1132 TYR TYR A . n 
A 1 1169 LYS 1169 1133 1133 LYS LYS A . n 
A 1 1170 ALA 1170 1134 1134 ALA ALA A . n 
A 1 1171 GLU 1171 1135 1135 GLU GLU A . n 
A 1 1172 LYS 1172 1136 1136 LYS LYS A . n 
A 1 1173 ILE 1173 1137 1137 ILE ILE A . n 
A 1 1174 VAL 1174 1138 1138 VAL VAL A . n 
A 1 1175 ASN 1175 1139 1139 ASN ASN A . n 
A 1 1176 LEU 1176 1140 1140 LEU LEU A . n 
A 1 1177 ILE 1177 1141 1141 ILE ILE A . n 
A 1 1178 SER 1178 1142 1142 SER SER A . n 
A 1 1179 GLY 1179 1143 1143 GLY GLY A . n 
A 1 1180 THR 1180 1144 1144 THR THR A . n 
A 1 1181 LYS 1181 1145 1145 LYS LYS A . n 
A 1 1182 SER 1182 1146 1146 SER SER A . n 
A 1 1183 ILE 1183 1147 1147 ILE ILE A . n 
A 1 1184 THR 1184 1148 1148 THR THR A . n 
A 1 1185 ASN 1185 1149 1149 ASN ASN A . n 
A 1 1186 ILE 1186 1150 1150 ILE ILE A . n 
A 1 1187 LEU 1187 1151 1151 LEU LEU A . n 
A 1 1188 GLU 1188 1152 1152 GLU GLU A . n 
A 1 1189 LYS 1189 1153 1153 LYS LYS A . n 
A 1 1190 THR 1190 1154 1154 THR THR A . n 
A 1 1191 SER 1191 1155 1155 SER SER A . n 
A 1 1192 ALA 1192 1156 1156 ALA ALA A . n 
A 1 1193 ILE 1193 1157 1157 ILE ILE A . n 
A 1 1194 ASP 1194 1158 1158 ASP ASP A . n 
A 1 1195 LEU 1195 1159 1159 LEU LEU A . n 
A 1 1196 THR 1196 1160 1160 THR THR A . n 
A 1 1197 ASP 1197 1161 1161 ASP ASP A . n 
A 1 1198 ILE 1198 1162 1162 ILE ILE A . n 
A 1 1199 ASP 1199 1163 1163 ASP ASP A . n 
A 1 1200 ARG 1200 1164 1164 ARG ARG A . n 
A 1 1201 ALA 1201 1165 1165 ALA ALA A . n 
A 1 1202 THR 1202 1166 1166 THR THR A . n 
A 1 1203 GLU 1203 1167 1167 GLU GLU A . n 
A 1 1204 MET 1204 1168 1168 MET MET A . n 
A 1 1205 MET 1205 1169 1169 MET MET A . n 
A 1 1206 ARG 1206 1170 1170 ARG ARG A . n 
A 1 1207 LYS 1207 1171 1171 LYS LYS A . n 
A 1 1208 ASN 1208 1172 1172 ASN ASN A . n 
A 1 1209 ILE 1209 1173 1173 ILE ILE A . n 
A 1 1210 THR 1210 1174 1174 THR THR A . n 
A 1 1211 LEU 1211 1175 1175 LEU LEU A . n 
A 1 1212 LEU 1212 1176 1176 LEU LEU A . n 
A 1 1213 ILE 1213 1177 1177 ILE ILE A . n 
A 1 1214 ARG 1214 1178 1178 ARG ARG A . n 
A 1 1215 ILE 1215 1179 1179 ILE ILE A . n 
A 1 1216 LEU 1216 1180 1180 LEU LEU A . n 
A 1 1217 PRO 1217 1181 1181 PRO PRO A . n 
A 1 1218 LEU 1218 1182 1182 LEU LEU A . n 
A 1 1219 ASP 1219 1183 1183 ASP ASP A . n 
A 1 1220 CYS 1220 1184 1184 CYS ALA A . n 
A 1 1221 ASN 1221 1185 ?    ?   ?   A . n 
A 1 1222 ARG 1222 1186 ?    ?   ?   A . n 
A 1 1223 ASP 1223 1187 ?    ?   ?   A . n 
A 1 1224 LYS 1224 1188 ?    ?   ?   A . n 
A 1 1225 ARG 1225 1189 ?    ?   ?   A . n 
A 1 1226 GLU 1226 1190 1190 GLU ALA A . n 
A 1 1227 ILE 1227 1191 1191 ILE ILE A . n 
A 1 1228 LEU 1228 1192 1192 LEU LEU A . n 
A 1 1229 SER 1229 1193 1193 SER SER A . n 
A 1 1230 MET 1230 1194 1194 MET MET A . n 
A 1 1231 GLU 1231 1195 1195 GLU GLU A . n 
A 1 1232 ASN 1232 1196 1196 ASN ASN A . n 
A 1 1233 LEU 1233 1197 1197 LEU LEU A . n 
A 1 1234 SER 1234 1198 1198 SER SER A . n 
A 1 1235 ILE 1235 1199 1199 ILE ILE A . n 
A 1 1236 THR 1236 1200 1200 THR THR A . n 
A 1 1237 GLU 1237 1201 1201 GLU GLU A . n 
A 1 1238 LEU 1238 1202 1202 LEU LEU A . n 
A 1 1239 SER 1239 1203 1203 SER SER A . n 
A 1 1240 LYS 1240 1204 1204 LYS LYS A . n 
A 1 1241 TYR 1241 1205 1205 TYR TYR A . n 
A 1 1242 VAL 1242 1206 1206 VAL VAL A . n 
A 1 1243 ARG 1243 1207 1207 ARG ARG A . n 
A 1 1244 GLU 1244 1208 1208 GLU GLU A . n 
A 1 1245 ARG 1245 1209 1209 ARG ARG A . n 
A 1 1246 SER 1246 1210 1210 SER SER A . n 
A 1 1247 TRP 1247 1211 1211 TRP TRP A . n 
A 1 1248 SER 1248 1212 1212 SER SER A . n 
A 1 1249 LEU 1249 1213 1213 LEU LEU A . n 
A 1 1250 SER 1250 1214 1214 SER SER A . n 
A 1 1251 ASN 1251 1215 1215 ASN ASN A . n 
A 1 1252 ILE 1252 1216 1216 ILE ILE A . n 
A 1 1253 VAL 1253 1217 1217 VAL VAL A . n 
A 1 1254 GLY 1254 1218 1218 GLY GLY A . n 
A 1 1255 VAL 1255 1219 1219 VAL VAL A . n 
A 1 1256 THR 1256 1220 1220 THR THR A . n 
A 1 1257 SER 1257 1221 1221 SER SER A . n 
A 1 1258 PRO 1258 1222 1222 PRO PRO A . n 
A 1 1259 SER 1259 1223 1223 SER SER A . n 
A 1 1260 ILE 1260 1224 1224 ILE ILE A . n 
A 1 1261 MET 1261 1225 1225 MET MET A . n 
A 1 1262 TYR 1262 1226 1226 TYR TYR A . n 
A 1 1263 THR 1263 1227 1227 THR THR A . n 
A 1 1264 MET 1264 1228 1228 MET MET A . n 
A 1 1265 ASP 1265 1229 1229 ASP ASP A . n 
A 1 1266 ILE 1266 1230 1230 ILE ILE A . n 
A 1 1267 LYS 1267 1231 1231 LYS LYS A . n 
A 1 1268 TYR 1268 1232 1232 TYR TYR A . n 
A 1 1269 THR 1269 1233 1233 THR THR A . n 
A 1 1270 THR 1270 1234 1234 THR THR A . n 
A 1 1271 SER 1271 1235 1235 SER SER A . n 
A 1 1272 THR 1272 1236 1236 THR THR A . n 
A 1 1273 ILE 1273 1237 1237 ILE ILE A . n 
A 1 1274 SER 1274 1238 1238 SER SER A . n 
A 1 1275 SER 1275 1239 1239 SER SER A . n 
A 1 1276 GLY 1276 1240 1240 GLY GLY A . n 
A 1 1277 ILE 1277 1241 1241 ILE ILE A . n 
A 1 1278 ILE 1278 1242 1242 ILE ILE A . n 
A 1 1279 ILE 1279 1243 1243 ILE ILE A . n 
A 1 1280 GLU 1280 1244 1244 GLU GLU A . n 
A 1 1281 LYS 1281 1245 1245 LYS LYS A . n 
A 1 1282 TYR 1282 1246 1246 TYR TYR A . n 
A 1 1283 ASN 1283 1247 1247 ASN ASN A . n 
A 1 1284 VAL 1284 1248 1248 VAL VAL A . n 
A 1 1285 ASN 1285 1249 1249 ASN ASN A . n 
A 1 1286 SER 1286 1250 1250 SER SER A . n 
A 1 1287 LEU 1287 1251 1251 LEU LEU A . n 
A 1 1288 THR 1288 1252 1252 THR THR A . n 
A 1 1289 ARG 1289 1253 1253 ARG ARG A . n 
A 1 1290 GLY 1290 1254 1254 GLY GLY A . n 
A 1 1291 GLU 1291 1255 1255 GLU GLU A . n 
A 1 1292 ARG 1292 1256 1256 ARG ARG A . n 
A 1 1293 GLY 1293 1257 1257 GLY GLY A . n 
A 1 1294 PRO 1294 1258 1258 PRO PRO A . n 
A 1 1295 THR 1295 1259 1259 THR THR A . n 
A 1 1296 LYS 1296 1260 1260 LYS LYS A . n 
A 1 1297 PRO 1297 1261 1261 PRO PRO A . n 
A 1 1298 TRP 1298 1262 1262 TRP TRP A . n 
A 1 1299 VAL 1299 1263 1263 VAL VAL A . n 
A 1 1300 GLY 1300 1264 1264 GLY GLY A . n 
A 1 1301 SER 1301 1265 1265 SER SER A . n 
A 1 1302 SER 1302 1266 1266 SER SER A . n 
A 1 1303 THR 1303 1267 1267 THR THR A . n 
A 1 1304 GLN 1304 1268 1268 GLN GLN A . n 
A 1 1305 GLU 1305 1269 1269 GLU GLU A . n 
A 1 1306 LYS 1306 1270 1270 LYS LYS A . n 
A 1 1307 LYS 1307 1271 1271 LYS LYS A . n 
A 1 1308 THR 1308 1272 1272 THR THR A . n 
A 1 1309 MET 1309 1273 1273 MET MET A . n 
A 1 1310 PRO 1310 1274 1274 PRO PRO A . n 
A 1 1311 VAL 1311 1275 1275 VAL VAL A . n 
A 1 1312 TYR 1312 1276 1276 TYR TYR A . n 
A 1 1313 ASN 1313 1277 1277 ASN ASN A . n 
A 1 1314 ARG 1314 1278 1278 ARG ARG A . n 
A 1 1315 GLN 1315 1279 1279 GLN GLN A . n 
A 1 1316 VAL 1316 1280 1280 VAL VAL A . n 
A 1 1317 LEU 1317 1281 1281 LEU LEU A . n 
A 1 1318 THR 1318 1282 1282 THR THR A . n 
A 1 1319 LYS 1319 1283 1283 LYS LYS A . n 
A 1 1320 LYS 1320 1284 1284 LYS LYS A . n 
A 1 1321 GLN 1321 1285 1285 GLN GLN A . n 
A 1 1322 ARG 1322 1286 1286 ARG ARG A . n 
A 1 1323 ASP 1323 1287 1287 ASP ASP A . n 
A 1 1324 GLN 1324 1288 1288 GLN GLN A . n 
A 1 1325 ILE 1325 1289 1289 ILE ILE A . n 
A 1 1326 ASP 1326 1290 1290 ASP ASP A . n 
A 1 1327 LEU 1327 1291 1291 LEU LEU A . n 
A 1 1328 LEU 1328 1292 1292 LEU LEU A . n 
A 1 1329 ALA 1329 1293 1293 ALA ALA A . n 
A 1 1330 LYS 1330 1294 1294 LYS LYS A . n 
A 1 1331 LEU 1331 1295 1295 LEU LEU A . n 
A 1 1332 ASP 1332 1296 1296 ASP ASP A . n 
A 1 1333 TRP 1333 1297 1297 TRP TRP A . n 
A 1 1334 VAL 1334 1298 1298 VAL VAL A . n 
A 1 1335 TYR 1335 1299 1299 TYR TYR A . n 
A 1 1336 ALA 1336 1300 1300 ALA ALA A . n 
A 1 1337 SER 1337 1301 1301 SER SER A . n 
A 1 1338 ILE 1338 1302 1302 ILE ILE A . n 
A 1 1339 ASP 1339 1303 1303 ASP ASP A . n 
A 1 1340 ASN 1340 1304 1304 ASN ASN A . n 
A 1 1341 LYS 1341 1305 1305 LYS LYS A . n 
A 1 1342 ASP 1342 1306 1306 ASP ASP A . n 
A 1 1343 GLU 1343 1307 1307 GLU GLU A . n 
A 1 1344 PHE 1344 1308 1308 PHE PHE A . n 
A 1 1345 MET 1345 1309 1309 MET MET A . n 
A 1 1346 GLU 1346 1310 1310 GLU GLU A . n 
A 1 1347 GLU 1347 1311 1311 GLU GLU A . n 
A 1 1348 LEU 1348 1312 1312 LEU LEU A . n 
A 1 1349 SER 1349 1313 1313 SER SER A . n 
A 1 1350 ILE 1350 1314 1314 ILE ILE A . n 
A 1 1351 GLY 1351 1315 1315 GLY GLY A . n 
A 1 1352 THR 1352 1316 1316 THR THR A . n 
A 1 1353 LEU 1353 1317 1317 LEU LEU A . n 
A 1 1354 GLY 1354 1318 1318 GLY GLY A . n 
A 1 1355 LEU 1355 1319 1319 LEU LEU A . n 
A 1 1356 THR 1356 1320 1320 THR THR A . n 
A 1 1357 TYR 1357 1321 1321 TYR TYR A . n 
A 1 1358 GLU 1358 1322 1322 GLU GLU A . n 
A 1 1359 LYS 1359 1323 1323 LYS LYS A . n 
A 1 1360 ALA 1360 1324 1324 ALA ALA A . n 
A 1 1361 LYS 1361 1325 1325 LYS LYS A . n 
A 1 1362 LYS 1362 1326 1326 LYS LYS A . n 
A 1 1363 LEU 1363 1327 1327 LEU LEU A . n 
A 1 1364 PHE 1364 1328 1328 PHE PHE A . n 
A 1 1365 PRO 1365 1329 1329 PRO PRO A . n 
A 1 1366 GLN 1366 1330 1330 GLN GLN A . n 
A 1 1367 TYR 1367 1331 1331 TYR TYR A . n 
A 1 1368 LEU 1368 1332 1332 LEU LEU A . n 
A 1 1369 SER 1369 1333 1333 SER SER A . n 
A 1 1370 VAL 1370 1334 1334 VAL VAL A . n 
A 1 1371 ASN 1371 1335 1335 ASN ASN A . n 
A 1 1372 TYR 1372 1336 1336 TYR TYR A . n 
A 1 1373 LEU 1373 1337 1337 LEU LEU A . n 
A 1 1374 HIS 1374 1338 1338 HIS HIS A . n 
A 1 1375 ARG 1375 1339 1339 ARG ARG A . n 
A 1 1376 LEU 1376 1340 1340 LEU LEU A . n 
A 1 1377 THR 1377 1341 1341 THR THR A . n 
A 1 1378 VAL 1378 1342 1342 VAL VAL A . n 
A 1 1379 SER 1379 1343 1343 SER SER A . n 
A 1 1380 SER 1380 1344 1344 SER SER A . n 
A 1 1381 ARG 1381 1345 1345 ARG ARG A . n 
A 1 1382 PRO 1382 1346 1346 PRO PRO A . n 
A 1 1383 CYS 1383 1347 1347 CYS CYS A . n 
A 1 1384 GLU 1384 1348 1348 GLU GLU A . n 
A 1 1385 PHE 1385 1349 1349 PHE PHE A . n 
A 1 1386 PRO 1386 1350 1350 PRO PRO A . n 
A 1 1387 ALA 1387 1351 1351 ALA ALA A . n 
A 1 1388 SER 1388 1352 1352 SER SER A . n 
A 1 1389 ILE 1389 1353 1353 ILE ILE A . n 
A 1 1390 PRO 1390 1354 1354 PRO PRO A . n 
A 1 1391 ALA 1391 1355 1355 ALA ALA A . n 
A 1 1392 TYR 1392 1356 1356 TYR TYR A . n 
A 1 1393 ARG 1393 1357 1357 ARG ARG A . n 
A 1 1394 THR 1394 1358 1358 THR THR A . n 
A 1 1395 THR 1395 1359 1359 THR THR A . n 
A 1 1396 ASN 1396 1360 1360 ASN ASN A . n 
A 1 1397 TYR 1397 1361 1361 TYR TYR A . n 
A 1 1398 HIS 1398 1362 1362 HIS HIS A . n 
A 1 1399 PHE 1399 1363 1363 PHE PHE A . n 
A 1 1400 ASP 1400 1364 1364 ASP ASP A . n 
A 1 1401 THR 1401 1365 1365 THR THR A . n 
A 1 1402 SER 1402 1366 1366 SER SER A . n 
A 1 1403 PRO 1403 1367 1367 PRO PRO A . n 
A 1 1404 ILE 1404 1368 1368 ILE ILE A . n 
A 1 1405 ASN 1405 1369 1369 ASN ASN A . n 
A 1 1406 ARG 1406 1370 1370 ARG ARG A . n 
A 1 1407 ILE 1407 1371 1371 ILE ILE A . n 
A 1 1408 LEU 1408 1372 1372 LEU LEU A . n 
A 1 1409 THR 1409 1373 1373 THR THR A . n 
A 1 1410 GLU 1410 1374 1374 GLU GLU A . n 
A 1 1411 LYS 1411 1375 1375 LYS LYS A . n 
A 1 1412 TYR 1412 1376 1376 TYR TYR A . n 
A 1 1413 GLY 1413 1377 1377 GLY GLY A . n 
A 1 1414 ASP 1414 1378 1378 ASP ASP A . n 
A 1 1415 GLU 1415 1379 1379 GLU GLU A . n 
A 1 1416 ASP 1416 1380 1380 ASP ASP A . n 
A 1 1417 ILE 1417 1381 1381 ILE ILE A . n 
A 1 1418 ASP 1418 1382 1382 ASP ASP A . n 
A 1 1419 ILE 1419 1383 1383 ILE ILE A . n 
A 1 1420 VAL 1420 1384 1384 VAL VAL A . n 
A 1 1421 PHE 1421 1385 1385 PHE PHE A . n 
A 1 1422 GLN 1422 1386 1386 GLN GLN A . n 
A 1 1423 ASN 1423 1387 1387 ASN ASN A . n 
A 1 1424 CYS 1424 1388 1388 CYS CYS A . n 
A 1 1425 ILE 1425 1389 1389 ILE ILE A . n 
A 1 1426 SER 1426 1390 1390 SER SER A . n 
A 1 1427 PHE 1427 1391 1391 PHE PHE A . n 
A 1 1428 GLY 1428 1392 1392 GLY GLY A . n 
A 1 1429 LEU 1429 1393 1393 LEU LEU A . n 
A 1 1430 SER 1430 1394 1394 SER SER A . n 
A 1 1431 LEU 1431 1395 1395 LEU LEU A . n 
A 1 1432 MET 1432 1396 1396 MET MET A . n 
A 1 1433 SER 1433 1397 1397 SER SER A . n 
A 1 1434 VAL 1434 1398 1398 VAL VAL A . n 
A 1 1435 VAL 1435 1399 1399 VAL VAL A . n 
A 1 1436 GLU 1436 1400 1400 GLU GLU A . n 
A 1 1437 GLN 1437 1401 1401 GLN GLN A . n 
A 1 1438 PHE 1438 1402 1402 PHE PHE A . n 
A 1 1439 THR 1439 1403 1403 THR THR A . n 
A 1 1440 ASN 1440 1404 1404 ASN ASN A . n 
A 1 1441 VAL 1441 1405 1405 VAL VAL A . n 
A 1 1442 CYS 1442 1406 1406 CYS CYS A . n 
A 1 1443 PRO 1443 1407 1407 PRO PRO A . n 
A 1 1444 ASN 1444 1408 1408 ASN ASN A . n 
A 1 1445 ARG 1445 1409 1409 ARG ARG A . n 
A 1 1446 ILE 1446 1410 1410 ILE ILE A . n 
A 1 1447 ILE 1447 1411 1411 ILE ILE A . n 
A 1 1448 LEU 1448 1412 1412 LEU LEU A . n 
A 1 1449 ILE 1449 1413 1413 ILE ILE A . n 
A 1 1450 PRO 1450 1414 1414 PRO PRO A . n 
A 1 1451 LYS 1451 1415 1415 LYS LYS A . n 
A 1 1452 LEU 1452 1416 1416 LEU LEU A . n 
A 1 1453 ASN 1453 1417 1417 ASN ASN A . n 
A 1 1454 GLU 1454 1418 1418 GLU GLU A . n 
A 1 1455 ILE 1455 1419 1419 ILE ILE A . n 
A 1 1456 HIS 1456 1420 1420 HIS HIS A . n 
A 1 1457 LEU 1457 1421 1421 LEU LEU A . n 
A 1 1458 MET 1458 1422 1422 MET MET A . n 
A 1 1459 LYS 1459 1423 1423 LYS LYS A . n 
A 1 1460 PRO 1460 1424 1424 PRO PRO A . n 
A 1 1461 PRO 1461 1425 1425 PRO PRO A . n 
A 1 1462 ILE 1462 1426 1426 ILE ILE A . n 
A 1 1463 PHE 1463 1427 1427 PHE PHE A . n 
A 1 1464 THR 1464 1428 1428 THR THR A . n 
A 1 1465 GLY 1465 1429 1429 GLY GLY A . n 
A 1 1466 ASP 1466 1430 1430 ASP ASP A . n 
A 1 1467 VAL 1467 1431 1431 VAL VAL A . n 
A 1 1468 ASP 1468 1432 1432 ASP ASP A . n 
A 1 1469 ILE 1469 1433 1433 ILE ILE A . n 
A 1 1470 HIS 1470 1434 1434 HIS HIS A . n 
A 1 1471 LYS 1471 1435 1435 LYS LYS A . n 
A 1 1472 LEU 1472 1436 1436 LEU LEU A . n 
A 1 1473 LYS 1473 1437 1437 LYS LYS A . n 
A 1 1474 GLN 1474 1438 1438 GLN GLN A . n 
A 1 1475 VAL 1475 1439 1439 VAL VAL A . n 
A 1 1476 ILE 1476 1440 1440 ILE ILE A . n 
A 1 1477 GLN 1477 1441 1441 GLN GLN A . n 
A 1 1478 LYS 1478 1442 1442 LYS LYS A . n 
A 1 1479 GLN 1479 1443 1443 GLN GLN A . n 
A 1 1480 HIS 1480 1444 1444 HIS HIS A . n 
A 1 1481 MET 1481 1445 1445 MET MET A . n 
A 1 1482 PHE 1482 1446 1446 PHE PHE A . n 
A 1 1483 LEU 1483 1447 1447 LEU LEU A . n 
A 1 1484 PRO 1484 1448 1448 PRO PRO A . n 
A 1 1485 ASP 1485 1449 1449 ASP ASP A . n 
A 1 1486 LYS 1486 1450 1450 LYS LYS A . n 
A 1 1487 ILE 1487 1451 1451 ILE ILE A . n 
A 1 1488 SER 1488 1452 1452 SER SER A . n 
A 1 1489 LEU 1489 1453 1453 LEU LEU A . n 
A 1 1490 THR 1490 1454 1454 THR THR A . n 
A 1 1491 GLN 1491 1455 1455 GLN GLN A . n 
A 1 1492 TYR 1492 1456 1456 TYR TYR A . n 
A 1 1493 VAL 1493 1457 1457 VAL VAL A . n 
A 1 1494 GLU 1494 1458 1458 GLU GLU A . n 
A 1 1495 LEU 1495 1459 1459 LEU LEU A . n 
A 1 1496 PHE 1496 1460 1460 PHE PHE A . n 
A 1 1497 LEU 1497 1461 ?    ?   ?   A . n 
A 1 1498 SER 1498 1462 ?    ?   ?   A . n 
A 1 1499 ASN 1499 1463 ?    ?   ?   A . n 
A 1 1500 LYS 1500 1464 ?    ?   ?   A . n 
A 1 1501 THR 1501 1465 ?    ?   ?   A . n 
A 1 1502 LEU 1502 1466 ?    ?   ?   A . n 
A 1 1503 LYS 1503 1467 ?    ?   ?   A . n 
A 1 1504 SER 1504 1468 ?    ?   ?   A . n 
A 1 1505 GLY 1505 1469 ?    ?   ?   A . n 
A 1 1506 SER 1506 1470 ?    ?   ?   A . n 
A 1 1507 HIS 1507 1471 ?    ?   ?   A . n 
A 1 1508 VAL 1508 1472 ?    ?   ?   A . n 
A 1 1509 ASN 1509 1473 ?    ?   ?   A . n 
A 1 1510 SER 1510 1474 ?    ?   ?   A . n 
A 1 1511 ASN 1511 1475 ?    ?   ?   A . n 
A 1 1512 LEU 1512 1476 ?    ?   ?   A . n 
A 1 1513 ILE 1513 1477 ?    ?   ?   A . n 
A 1 1514 LEU 1514 1478 ?    ?   ?   A . n 
A 1 1515 ALA 1515 1479 ?    ?   ?   A . n 
A 1 1516 HIS 1516 1480 ?    ?   ?   A . n 
A 1 1517 LYS 1517 1481 ?    ?   ?   A . n 
A 1 1518 ILE 1518 1482 ?    ?   ?   A . n 
A 1 1519 SER 1519 1483 ?    ?   ?   A . n 
A 1 1520 ASP 1520 1484 ?    ?   ?   A . n 
A 1 1521 TYR 1521 1485 ?    ?   ?   A . n 
A 1 1522 PHE 1522 1486 ?    ?   ?   A . n 
A 1 1523 HIS 1523 1487 ?    ?   ?   A . n 
A 1 1524 ASN 1524 1488 ?    ?   ?   A . n 
A 1 1525 THR 1525 1489 ?    ?   ?   A . n 
A 1 1526 TYR 1526 1490 ?    ?   ?   A . n 
A 1 1527 ILE 1527 1491 ?    ?   ?   A . n 
A 1 1528 LEU 1528 1492 ?    ?   ?   A . n 
A 1 1529 SER 1529 1493 ?    ?   ?   A . n 
A 1 1530 THR 1530 1494 ?    ?   ?   A . n 
A 1 1531 ASN 1531 1495 ?    ?   ?   A . n 
A 1 1532 LEU 1532 1496 ?    ?   ?   A . n 
A 1 1533 ALA 1533 1497 ?    ?   ?   A . n 
A 1 1534 GLY 1534 1498 ?    ?   ?   A . n 
A 1 1535 HIS 1535 1499 ?    ?   ?   A . n 
A 1 1536 TRP 1536 1500 ?    ?   ?   A . n 
A 1 1537 ILE 1537 1501 ?    ?   ?   A . n 
A 1 1538 LEU 1538 1502 ?    ?   ?   A . n 
A 1 1539 ILE 1539 1503 ?    ?   ?   A . n 
A 1 1540 ILE 1540 1504 ?    ?   ?   A . n 
A 1 1541 GLN 1541 1505 ?    ?   ?   A . n 
A 1 1542 LEU 1542 1506 ?    ?   ?   A . n 
A 1 1543 MET 1543 1507 ?    ?   ?   A . n 
A 1 1544 LYS 1544 1508 ?    ?   ?   A . n 
A 1 1545 ASP 1545 1509 ?    ?   ?   A . n 
A 1 1546 SER 1546 1510 ?    ?   ?   A . n 
A 1 1547 LYS 1547 1511 ?    ?   ?   A . n 
A 1 1548 GLY 1548 1512 ?    ?   ?   A . n 
A 1 1549 ILE 1549 1513 ?    ?   ?   A . n 
A 1 1550 PHE 1550 1514 ?    ?   ?   A . n 
A 1 1551 GLU 1551 1515 ?    ?   ?   A . n 
A 1 1552 LYS 1552 1516 ?    ?   ?   A . n 
A 1 1553 ASP 1553 1517 ?    ?   ?   A . n 
A 1 1554 TRP 1554 1518 ?    ?   ?   A . n 
A 1 1555 GLY 1555 1519 ?    ?   ?   A . n 
A 1 1556 GLU 1556 1520 ?    ?   ?   A . n 
A 1 1557 GLY 1557 1521 ?    ?   ?   A . n 
A 1 1558 TYR 1558 1522 ?    ?   ?   A . n 
A 1 1559 ILE 1559 1523 ?    ?   ?   A . n 
A 1 1560 THR 1560 1524 ?    ?   ?   A . n 
A 1 1561 ASP 1561 1525 ?    ?   ?   A . n 
A 1 1562 HIS 1562 1526 ?    ?   ?   A . n 
A 1 1563 MET 1563 1527 ?    ?   ?   A . n 
A 1 1564 PHE 1564 1528 ?    ?   ?   A . n 
A 1 1565 ILE 1565 1529 ?    ?   ?   A . n 
A 1 1566 ASN 1566 1530 ?    ?   ?   A . n 
A 1 1567 LEU 1567 1531 ?    ?   ?   A . n 
A 1 1568 LYS 1568 1532 ?    ?   ?   A . n 
A 1 1569 VAL 1569 1533 ?    ?   ?   A . n 
A 1 1570 PHE 1570 1534 ?    ?   ?   A . n 
A 1 1571 PHE 1571 1535 ?    ?   ?   A . n 
A 1 1572 ASN 1572 1536 ?    ?   ?   A . n 
A 1 1573 ALA 1573 1537 ?    ?   ?   A . n 
A 1 1574 TYR 1574 1538 ?    ?   ?   A . n 
A 1 1575 LYS 1575 1539 ?    ?   ?   A . n 
A 1 1576 THR 1576 1540 ?    ?   ?   A . n 
A 1 1577 TYR 1577 1541 ?    ?   ?   A . n 
A 1 1578 LEU 1578 1542 ?    ?   ?   A . n 
A 1 1579 LEU 1579 1543 ?    ?   ?   A . n 
A 1 1580 CYS 1580 1544 ?    ?   ?   A . n 
A 1 1581 PHE 1581 1545 ?    ?   ?   A . n 
A 1 1582 HIS 1582 1546 ?    ?   ?   A . n 
A 1 1583 LYS 1583 1547 ?    ?   ?   A . n 
A 1 1584 GLY 1584 1548 ?    ?   ?   A . n 
A 1 1585 TYR 1585 1549 ?    ?   ?   A . n 
A 1 1586 GLY 1586 1550 ?    ?   ?   A . n 
A 1 1587 LYS 1587 1551 ?    ?   ?   A . n 
A 1 1588 ALA 1588 1552 ?    ?   ?   A . n 
A 1 1589 LYS 1589 1553 ?    ?   ?   A . n 
A 1 1590 LEU 1590 1554 ?    ?   ?   A . n 
A 1 1591 GLU 1591 1555 ?    ?   ?   A . n 
A 1 1592 CYS 1592 1556 ?    ?   ?   A . n 
A 1 1593 ASP 1593 1557 ?    ?   ?   A . n 
A 1 1594 MET 1594 1558 ?    ?   ?   A . n 
A 1 1595 ASN 1595 1559 ?    ?   ?   A . n 
A 1 1596 THR 1596 1560 ?    ?   ?   A . n 
A 1 1597 SER 1597 1561 ?    ?   ?   A . n 
A 1 1598 ASP 1598 1562 ?    ?   ?   A . n 
A 1 1599 LEU 1599 1563 ?    ?   ?   A . n 
A 1 1600 LEU 1600 1564 ?    ?   ?   A . n 
A 1 1601 CYS 1601 1565 ?    ?   ?   A . n 
A 1 1602 VAL 1602 1566 ?    ?   ?   A . n 
A 1 1603 LEU 1603 1567 ?    ?   ?   A . n 
A 1 1604 GLU 1604 1568 ?    ?   ?   A . n 
A 1 1605 LEU 1605 1569 ?    ?   ?   A . n 
A 1 1606 ILE 1606 1570 ?    ?   ?   A . n 
A 1 1607 ASP 1607 1571 ?    ?   ?   A . n 
A 1 1608 SER 1608 1572 ?    ?   ?   A . n 
A 1 1609 SER 1609 1573 ?    ?   ?   A . n 
A 1 1610 TYR 1610 1574 ?    ?   ?   A . n 
A 1 1611 TRP 1611 1575 ?    ?   ?   A . n 
A 1 1612 LYS 1612 1576 ?    ?   ?   A . n 
A 1 1613 SER 1613 1577 ?    ?   ?   A . n 
A 1 1614 MET 1614 1578 ?    ?   ?   A . n 
A 1 1615 SER 1615 1579 ?    ?   ?   A . n 
A 1 1616 LYS 1616 1580 ?    ?   ?   A . n 
A 1 1617 VAL 1617 1581 ?    ?   ?   A . n 
A 1 1618 PHE 1618 1582 ?    ?   ?   A . n 
A 1 1619 LEU 1619 1583 ?    ?   ?   A . n 
A 1 1620 GLU 1620 1584 ?    ?   ?   A . n 
A 1 1621 GLN 1621 1585 ?    ?   ?   A . n 
A 1 1622 LYS 1622 1586 ?    ?   ?   A . n 
A 1 1623 VAL 1623 1587 ?    ?   ?   A . n 
A 1 1624 ILE 1624 1588 ?    ?   ?   A . n 
A 1 1625 LYS 1625 1589 ?    ?   ?   A . n 
A 1 1626 TYR 1626 1590 ?    ?   ?   A . n 
A 1 1627 ILE 1627 1591 ?    ?   ?   A . n 
A 1 1628 LEU 1628 1592 ?    ?   ?   A . n 
A 1 1629 SER 1629 1593 ?    ?   ?   A . n 
A 1 1630 GLN 1630 1594 ?    ?   ?   A . n 
A 1 1631 ASP 1631 1595 ?    ?   ?   A . n 
A 1 1632 ALA 1632 1596 ?    ?   ?   A . n 
A 1 1633 SER 1633 1597 ?    ?   ?   A . n 
A 1 1634 LEU 1634 1598 ?    ?   ?   A . n 
A 1 1635 HIS 1635 1599 ?    ?   ?   A . n 
A 1 1636 ARG 1636 1600 ?    ?   ?   A . n 
A 1 1637 VAL 1637 1601 ?    ?   ?   A . n 
A 1 1638 LYS 1638 1602 ?    ?   ?   A . n 
A 1 1639 GLY 1639 1603 ?    ?   ?   A . n 
A 1 1640 CYS 1640 1604 ?    ?   ?   A . n 
A 1 1641 HIS 1641 1605 ?    ?   ?   A . n 
A 1 1642 SER 1642 1606 ?    ?   ?   A . n 
A 1 1643 PHE 1643 1607 ?    ?   ?   A . n 
A 1 1644 LYS 1644 1608 ?    ?   ?   A . n 
A 1 1645 LEU 1645 1609 ?    ?   ?   A . n 
A 1 1646 TRP 1646 1610 ?    ?   ?   A . n 
A 1 1647 PHE 1647 1611 ?    ?   ?   A . n 
A 1 1648 LEU 1648 1612 ?    ?   ?   A . n 
A 1 1649 LYS 1649 1613 ?    ?   ?   A . n 
A 1 1650 ARG 1650 1614 ?    ?   ?   A . n 
A 1 1651 LEU 1651 1615 ?    ?   ?   A . n 
A 1 1652 ASN 1652 1616 ?    ?   ?   A . n 
A 1 1653 VAL 1653 1617 ?    ?   ?   A . n 
A 1 1654 ALA 1654 1618 ?    ?   ?   A . n 
A 1 1655 GLU 1655 1619 ?    ?   ?   A . n 
A 1 1656 PHE 1656 1620 ?    ?   ?   A . n 
A 1 1657 THR 1657 1621 ?    ?   ?   A . n 
A 1 1658 VAL 1658 1622 ?    ?   ?   A . n 
A 1 1659 CYS 1659 1623 ?    ?   ?   A . n 
A 1 1660 PRO 1660 1624 ?    ?   ?   A . n 
A 1 1661 TRP 1661 1625 ?    ?   ?   A . n 
A 1 1662 VAL 1662 1626 ?    ?   ?   A . n 
A 1 1663 VAL 1663 1627 ?    ?   ?   A . n 
A 1 1664 ASN 1664 1628 ?    ?   ?   A . n 
A 1 1665 ILE 1665 1629 ?    ?   ?   A . n 
A 1 1666 ASP 1666 1630 ?    ?   ?   A . n 
A 1 1667 TYR 1667 1631 ?    ?   ?   A . n 
A 1 1668 HIS 1668 1632 ?    ?   ?   A . n 
A 1 1669 PRO 1669 1633 ?    ?   ?   A . n 
A 1 1670 THR 1670 1634 ?    ?   ?   A . n 
A 1 1671 HIS 1671 1635 ?    ?   ?   A . n 
A 1 1672 MET 1672 1636 ?    ?   ?   A . n 
A 1 1673 LYS 1673 1637 ?    ?   ?   A . n 
A 1 1674 ALA 1674 1638 ?    ?   ?   A . n 
A 1 1675 ILE 1675 1639 ?    ?   ?   A . n 
A 1 1676 LEU 1676 1640 ?    ?   ?   A . n 
A 1 1677 THR 1677 1641 ?    ?   ?   A . n 
A 1 1678 TYR 1678 1642 ?    ?   ?   A . n 
A 1 1679 ILE 1679 1643 ?    ?   ?   A . n 
A 1 1680 ASP 1680 1644 ?    ?   ?   A . n 
A 1 1681 LEU 1681 1645 ?    ?   ?   A . n 
A 1 1682 VAL 1682 1646 ?    ?   ?   A . n 
A 1 1683 ARG 1683 1647 ?    ?   ?   A . n 
A 1 1684 MET 1684 1648 ?    ?   ?   A . n 
A 1 1685 GLY 1685 1649 ?    ?   ?   A . n 
A 1 1686 LEU 1686 1650 ?    ?   ?   A . n 
A 1 1687 ILE 1687 1651 ?    ?   ?   A . n 
A 1 1688 ASN 1688 1652 ?    ?   ?   A . n 
A 1 1689 ILE 1689 1653 ?    ?   ?   A . n 
A 1 1690 ASP 1690 1654 ?    ?   ?   A . n 
A 1 1691 ARG 1691 1655 ?    ?   ?   A . n 
A 1 1692 ILE 1692 1656 ?    ?   ?   A . n 
A 1 1693 HIS 1693 1657 ?    ?   ?   A . n 
A 1 1694 ILE 1694 1658 ?    ?   ?   A . n 
A 1 1695 LYS 1695 1659 ?    ?   ?   A . n 
A 1 1696 ASN 1696 1660 ?    ?   ?   A . n 
A 1 1697 LYS 1697 1661 ?    ?   ?   A . n 
A 1 1698 HIS 1698 1662 ?    ?   ?   A . n 
A 1 1699 LYS 1699 1663 ?    ?   ?   A . n 
A 1 1700 PHE 1700 1664 ?    ?   ?   A . n 
A 1 1701 ASN 1701 1665 ?    ?   ?   A . n 
A 1 1702 ASP 1702 1666 ?    ?   ?   A . n 
A 1 1703 GLU 1703 1667 ?    ?   ?   A . n 
A 1 1704 PHE 1704 1668 ?    ?   ?   A . n 
A 1 1705 TYR 1705 1669 ?    ?   ?   A . n 
A 1 1706 THR 1706 1670 ?    ?   ?   A . n 
A 1 1707 SER 1707 1671 ?    ?   ?   A . n 
A 1 1708 ASN 1708 1672 ?    ?   ?   A . n 
A 1 1709 LEU 1709 1673 ?    ?   ?   A . n 
A 1 1710 PHE 1710 1674 ?    ?   ?   A . n 
A 1 1711 TYR 1711 1675 ?    ?   ?   A . n 
A 1 1712 ILE 1712 1676 ?    ?   ?   A . n 
A 1 1713 ASN 1713 1677 ?    ?   ?   A . n 
A 1 1714 TYR 1714 1678 ?    ?   ?   A . n 
A 1 1715 ASN 1715 1679 ?    ?   ?   A . n 
A 1 1716 PHE 1716 1680 ?    ?   ?   A . n 
A 1 1717 SER 1717 1681 ?    ?   ?   A . n 
A 1 1718 ASP 1718 1682 ?    ?   ?   A . n 
A 1 1719 ASN 1719 1683 ?    ?   ?   A . n 
A 1 1720 THR 1720 1684 ?    ?   ?   A . n 
A 1 1721 HIS 1721 1685 ?    ?   ?   A . n 
A 1 1722 LEU 1722 1686 ?    ?   ?   A . n 
A 1 1723 LEU 1723 1687 ?    ?   ?   A . n 
A 1 1724 THR 1724 1688 ?    ?   ?   A . n 
A 1 1725 LYS 1725 1689 ?    ?   ?   A . n 
A 1 1726 HIS 1726 1690 ?    ?   ?   A . n 
A 1 1727 ILE 1727 1691 ?    ?   ?   A . n 
A 1 1728 ARG 1728 1692 ?    ?   ?   A . n 
A 1 1729 ILE 1729 1693 ?    ?   ?   A . n 
A 1 1730 ALA 1730 1694 ?    ?   ?   A . n 
A 1 1731 ASN 1731 1695 ?    ?   ?   A . n 
A 1 1732 SER 1732 1696 ?    ?   ?   A . n 
A 1 1733 GLU 1733 1697 ?    ?   ?   A . n 
A 1 1734 LEU 1734 1698 ?    ?   ?   A . n 
A 1 1735 GLU 1735 1699 ?    ?   ?   A . n 
A 1 1736 ASN 1736 1700 ?    ?   ?   A . n 
A 1 1737 ASN 1737 1701 ?    ?   ?   A . n 
A 1 1738 TYR 1738 1702 ?    ?   ?   A . n 
A 1 1739 ASN 1739 1703 ?    ?   ?   A . n 
A 1 1740 LYS 1740 1704 ?    ?   ?   A . n 
A 1 1741 LEU 1741 1705 ?    ?   ?   A . n 
A 1 1742 TYR 1742 1706 ?    ?   ?   A . n 
A 1 1743 HIS 1743 1707 ?    ?   ?   A . n 
A 1 1744 PRO 1744 1708 ?    ?   ?   A . n 
A 1 1745 THR 1745 1709 ?    ?   ?   A . n 
A 1 1746 PRO 1746 1710 ?    ?   ?   A . n 
A 1 1747 GLU 1747 1711 ?    ?   ?   A . n 
A 1 1748 THR 1748 1712 ?    ?   ?   A . n 
A 1 1749 LEU 1749 1713 ?    ?   ?   A . n 
A 1 1750 GLU 1750 1714 ?    ?   ?   A . n 
A 1 1751 ASN 1751 1715 ?    ?   ?   A . n 
A 1 1752 ILE 1752 1716 ?    ?   ?   A . n 
A 1 1753 LEU 1753 1717 ?    ?   ?   A . n 
A 1 1754 ALA 1754 1718 ?    ?   ?   A . n 
A 1 1755 ASN 1755 1719 ?    ?   ?   A . n 
A 1 1756 PRO 1756 1720 ?    ?   ?   A . n 
A 1 1757 ILE 1757 1721 ?    ?   ?   A . n 
A 1 1758 LYS 1758 1722 ?    ?   ?   A . n 
A 1 1759 SER 1759 1723 ?    ?   ?   A . n 
A 1 1760 ASN 1760 1724 ?    ?   ?   A . n 
A 1 1761 ASP 1761 1725 ?    ?   ?   A . n 
A 1 1762 LYS 1762 1726 ?    ?   ?   A . n 
A 1 1763 LYS 1763 1727 ?    ?   ?   A . n 
A 1 1764 THR 1764 1728 ?    ?   ?   A . n 
A 1 1765 LEU 1765 1729 ?    ?   ?   A . n 
A 1 1766 ASN 1766 1730 ?    ?   ?   A . n 
A 1 1767 ASP 1767 1731 ?    ?   ?   A . n 
A 1 1768 TYR 1768 1732 ?    ?   ?   A . n 
A 1 1769 CYS 1769 1733 ?    ?   ?   A . n 
A 1 1770 ILE 1770 1734 ?    ?   ?   A . n 
A 1 1771 GLY 1771 1735 ?    ?   ?   A . n 
A 1 1772 LYS 1772 1736 ?    ?   ?   A . n 
A 1 1773 ASN 1773 1737 ?    ?   ?   A . n 
A 1 1774 VAL 1774 1738 ?    ?   ?   A . n 
A 1 1775 ASP 1775 1739 ?    ?   ?   A . n 
A 1 1776 SER 1776 1740 ?    ?   ?   A . n 
A 1 1777 ILE 1777 1741 ?    ?   ?   A . n 
A 1 1778 MET 1778 1742 ?    ?   ?   A . n 
A 1 1779 LEU 1779 1743 ?    ?   ?   A . n 
A 1 1780 PRO 1780 1744 ?    ?   ?   A . n 
A 1 1781 LEU 1781 1745 ?    ?   ?   A . n 
A 1 1782 LEU 1782 1746 ?    ?   ?   A . n 
A 1 1783 SER 1783 1747 ?    ?   ?   A . n 
A 1 1784 ASN 1784 1748 ?    ?   ?   A . n 
A 1 1785 LYS 1785 1749 ?    ?   ?   A . n 
A 1 1786 LYS 1786 1750 ?    ?   ?   A . n 
A 1 1787 LEU 1787 1751 ?    ?   ?   A . n 
A 1 1788 ILE 1788 1752 ?    ?   ?   A . n 
A 1 1789 LYS 1789 1753 ?    ?   ?   A . n 
A 1 1790 SER 1790 1754 ?    ?   ?   A . n 
A 1 1791 SER 1791 1755 ?    ?   ?   A . n 
A 1 1792 ALA 1792 1756 ?    ?   ?   A . n 
A 1 1793 MET 1793 1757 ?    ?   ?   A . n 
A 1 1794 ILE 1794 1758 ?    ?   ?   A . n 
A 1 1795 ARG 1795 1759 ?    ?   ?   A . n 
A 1 1796 THR 1796 1760 ?    ?   ?   A . n 
A 1 1797 ASN 1797 1761 ?    ?   ?   A . n 
A 1 1798 TYR 1798 1762 ?    ?   ?   A . n 
A 1 1799 SER 1799 1763 ?    ?   ?   A . n 
A 1 1800 LYS 1800 1764 ?    ?   ?   A . n 
A 1 1801 GLN 1801 1765 ?    ?   ?   A . n 
A 1 1802 ASP 1802 1766 ?    ?   ?   A . n 
A 1 1803 LEU 1803 1767 ?    ?   ?   A . n 
A 1 1804 TYR 1804 1768 ?    ?   ?   A . n 
A 1 1805 ASN 1805 1769 ?    ?   ?   A . n 
A 1 1806 LEU 1806 1770 ?    ?   ?   A . n 
A 1 1807 PHE 1807 1771 ?    ?   ?   A . n 
A 1 1808 PRO 1808 1772 ?    ?   ?   A . n 
A 1 1809 MET 1809 1773 ?    ?   ?   A . n 
A 1 1810 VAL 1810 1774 ?    ?   ?   A . n 
A 1 1811 VAL 1811 1775 ?    ?   ?   A . n 
A 1 1812 ILE 1812 1776 ?    ?   ?   A . n 
A 1 1813 ASP 1813 1777 ?    ?   ?   A . n 
A 1 1814 ARG 1814 1778 ?    ?   ?   A . n 
A 1 1815 ILE 1815 1779 ?    ?   ?   A . n 
A 1 1816 ILE 1816 1780 ?    ?   ?   A . n 
A 1 1817 ASP 1817 1781 ?    ?   ?   A . n 
A 1 1818 HIS 1818 1782 ?    ?   ?   A . n 
A 1 1819 SER 1819 1783 ?    ?   ?   A . n 
A 1 1820 GLY 1820 1784 ?    ?   ?   A . n 
A 1 1821 ASN 1821 1785 ?    ?   ?   A . n 
A 1 1822 THR 1822 1786 ?    ?   ?   A . n 
A 1 1823 ALA 1823 1787 ?    ?   ?   A . n 
A 1 1824 LYS 1824 1788 ?    ?   ?   A . n 
A 1 1825 SER 1825 1789 ?    ?   ?   A . n 
A 1 1826 ASN 1826 1790 ?    ?   ?   A . n 
A 1 1827 GLN 1827 1791 ?    ?   ?   A . n 
A 1 1828 LEU 1828 1792 ?    ?   ?   A . n 
A 1 1829 TYR 1829 1793 ?    ?   ?   A . n 
A 1 1830 THR 1830 1794 ?    ?   ?   A . n 
A 1 1831 THR 1831 1795 ?    ?   ?   A . n 
A 1 1832 THR 1832 1796 ?    ?   ?   A . n 
A 1 1833 SER 1833 1797 ?    ?   ?   A . n 
A 1 1834 HIS 1834 1798 ?    ?   ?   A . n 
A 1 1835 GLN 1835 1799 ?    ?   ?   A . n 
A 1 1836 ILE 1836 1800 ?    ?   ?   A . n 
A 1 1837 SER 1837 1801 ?    ?   ?   A . n 
A 1 1838 LEU 1838 1802 ?    ?   ?   A . n 
A 1 1839 VAL 1839 1803 ?    ?   ?   A . n 
A 1 1840 HIS 1840 1804 ?    ?   ?   A . n 
A 1 1841 ASN 1841 1805 ?    ?   ?   A . n 
A 1 1842 SER 1842 1806 ?    ?   ?   A . n 
A 1 1843 THR 1843 1807 ?    ?   ?   A . n 
A 1 1844 SER 1844 1808 ?    ?   ?   A . n 
A 1 1845 LEU 1845 1809 ?    ?   ?   A . n 
A 1 1846 TYR 1846 1810 ?    ?   ?   A . n 
A 1 1847 CYS 1847 1811 ?    ?   ?   A . n 
A 1 1848 MET 1848 1812 ?    ?   ?   A . n 
A 1 1849 LEU 1849 1813 ?    ?   ?   A . n 
A 1 1850 PRO 1850 1814 ?    ?   ?   A . n 
A 1 1851 TRP 1851 1815 ?    ?   ?   A . n 
A 1 1852 HIS 1852 1816 ?    ?   ?   A . n 
A 1 1853 HIS 1853 1817 ?    ?   ?   A . n 
A 1 1854 ILE 1854 1818 ?    ?   ?   A . n 
A 1 1855 ASN 1855 1819 ?    ?   ?   A . n 
A 1 1856 ARG 1856 1820 ?    ?   ?   A . n 
A 1 1857 PHE 1857 1821 ?    ?   ?   A . n 
A 1 1858 ASN 1858 1822 ?    ?   ?   A . n 
A 1 1859 PHE 1859 1823 ?    ?   ?   A . n 
A 1 1860 VAL 1860 1824 ?    ?   ?   A . n 
A 1 1861 PHE 1861 1825 ?    ?   ?   A . n 
A 1 1862 SER 1862 1826 ?    ?   ?   A . n 
A 1 1863 SER 1863 1827 ?    ?   ?   A . n 
A 1 1864 THR 1864 1828 ?    ?   ?   A . n 
A 1 1865 GLY 1865 1829 ?    ?   ?   A . n 
A 1 1866 CYS 1866 1830 ?    ?   ?   A . n 
A 1 1867 LYS 1867 1831 ?    ?   ?   A . n 
A 1 1868 ILE 1868 1832 ?    ?   ?   A . n 
A 1 1869 SER 1869 1833 ?    ?   ?   A . n 
A 1 1870 ILE 1870 1834 ?    ?   ?   A . n 
A 1 1871 GLU 1871 1835 ?    ?   ?   A . n 
A 1 1872 TYR 1872 1836 ?    ?   ?   A . n 
A 1 1873 ILE 1873 1837 ?    ?   ?   A . n 
A 1 1874 LEU 1874 1838 ?    ?   ?   A . n 
A 1 1875 LYS 1875 1839 ?    ?   ?   A . n 
A 1 1876 ASP 1876 1840 ?    ?   ?   A . n 
A 1 1877 LEU 1877 1841 ?    ?   ?   A . n 
A 1 1878 LYS 1878 1842 ?    ?   ?   A . n 
A 1 1879 ILE 1879 1843 ?    ?   ?   A . n 
A 1 1880 LYS 1880 1844 ?    ?   ?   A . n 
A 1 1881 ASP 1881 1845 ?    ?   ?   A . n 
A 1 1882 PRO 1882 1846 ?    ?   ?   A . n 
A 1 1883 ASN 1883 1847 ?    ?   ?   A . n 
A 1 1884 CYS 1884 1848 ?    ?   ?   A . n 
A 1 1885 ILE 1885 1849 ?    ?   ?   A . n 
A 1 1886 ALA 1886 1850 ?    ?   ?   A . n 
A 1 1887 PHE 1887 1851 ?    ?   ?   A . n 
A 1 1888 ILE 1888 1852 ?    ?   ?   A . n 
A 1 1889 GLY 1889 1853 ?    ?   ?   A . n 
A 1 1890 GLU 1890 1854 ?    ?   ?   A . n 
A 1 1891 GLY 1891 1855 ?    ?   ?   A . n 
A 1 1892 ALA 1892 1856 ?    ?   ?   A . n 
A 1 1893 GLY 1893 1857 ?    ?   ?   A . n 
A 1 1894 ASN 1894 1858 ?    ?   ?   A . n 
A 1 1895 LEU 1895 1859 ?    ?   ?   A . n 
A 1 1896 LEU 1896 1860 ?    ?   ?   A . n 
A 1 1897 LEU 1897 1861 ?    ?   ?   A . n 
A 1 1898 ARG 1898 1862 ?    ?   ?   A . n 
A 1 1899 THR 1899 1863 ?    ?   ?   A . n 
A 1 1900 VAL 1900 1864 ?    ?   ?   A . n 
A 1 1901 VAL 1901 1865 ?    ?   ?   A . n 
A 1 1902 GLU 1902 1866 ?    ?   ?   A . n 
A 1 1903 LEU 1903 1867 ?    ?   ?   A . n 
A 1 1904 HIS 1904 1868 ?    ?   ?   A . n 
A 1 1905 PRO 1905 1869 ?    ?   ?   A . n 
A 1 1906 ASP 1906 1870 ?    ?   ?   A . n 
A 1 1907 ILE 1907 1871 ?    ?   ?   A . n 
A 1 1908 ARG 1908 1872 ?    ?   ?   A . n 
A 1 1909 TYR 1909 1873 ?    ?   ?   A . n 
A 1 1910 ILE 1910 1874 ?    ?   ?   A . n 
A 1 1911 TYR 1911 1875 ?    ?   ?   A . n 
A 1 1912 ARG 1912 1876 ?    ?   ?   A . n 
A 1 1913 SER 1913 1877 ?    ?   ?   A . n 
A 1 1914 LEU 1914 1878 ?    ?   ?   A . n 
A 1 1915 LYS 1915 1879 ?    ?   ?   A . n 
A 1 1916 ASP 1916 1880 ?    ?   ?   A . n 
A 1 1917 CYS 1917 1881 ?    ?   ?   A . n 
A 1 1918 ASN 1918 1882 ?    ?   ?   A . n 
A 1 1919 ASP 1919 1883 ?    ?   ?   A . n 
A 1 1920 HIS 1920 1884 ?    ?   ?   A . n 
A 1 1921 SER 1921 1885 ?    ?   ?   A . n 
A 1 1922 LEU 1922 1886 ?    ?   ?   A . n 
A 1 1923 PRO 1923 1887 ?    ?   ?   A . n 
A 1 1924 ILE 1924 1888 ?    ?   ?   A . n 
A 1 1925 GLU 1925 1889 ?    ?   ?   A . n 
A 1 1926 PHE 1926 1890 ?    ?   ?   A . n 
A 1 1927 LEU 1927 1891 ?    ?   ?   A . n 
A 1 1928 ARG 1928 1892 ?    ?   ?   A . n 
A 1 1929 LEU 1929 1893 ?    ?   ?   A . n 
A 1 1930 TYR 1930 1894 ?    ?   ?   A . n 
A 1 1931 ASN 1931 1895 ?    ?   ?   A . n 
A 1 1932 GLY 1932 1896 ?    ?   ?   A . n 
A 1 1933 HIS 1933 1897 ?    ?   ?   A . n 
A 1 1934 ILE 1934 1898 ?    ?   ?   A . n 
A 1 1935 ASN 1935 1899 ?    ?   ?   A . n 
A 1 1936 ILE 1936 1900 ?    ?   ?   A . n 
A 1 1937 ASP 1937 1901 ?    ?   ?   A . n 
A 1 1938 TYR 1938 1902 ?    ?   ?   A . n 
A 1 1939 GLY 1939 1903 ?    ?   ?   A . n 
A 1 1940 GLU 1940 1904 ?    ?   ?   A . n 
A 1 1941 ASN 1941 1905 ?    ?   ?   A . n 
A 1 1942 LEU 1942 1906 ?    ?   ?   A . n 
A 1 1943 THR 1943 1907 ?    ?   ?   A . n 
A 1 1944 ILE 1944 1908 ?    ?   ?   A . n 
A 1 1945 PRO 1945 1909 ?    ?   ?   A . n 
A 1 1946 ALA 1946 1910 ?    ?   ?   A . n 
A 1 1947 THR 1947 1911 ?    ?   ?   A . n 
A 1 1948 ASP 1948 1912 ?    ?   ?   A . n 
A 1 1949 ALA 1949 1913 ?    ?   ?   A . n 
A 1 1950 THR 1950 1914 ?    ?   ?   A . n 
A 1 1951 ASN 1951 1915 ?    ?   ?   A . n 
A 1 1952 ASN 1952 1916 ?    ?   ?   A . n 
A 1 1953 ILE 1953 1917 ?    ?   ?   A . n 
A 1 1954 HIS 1954 1918 ?    ?   ?   A . n 
A 1 1955 TRP 1955 1919 ?    ?   ?   A . n 
A 1 1956 SER 1956 1920 ?    ?   ?   A . n 
A 1 1957 TYR 1957 1921 ?    ?   ?   A . n 
A 1 1958 LEU 1958 1922 ?    ?   ?   A . n 
A 1 1959 HIS 1959 1923 ?    ?   ?   A . n 
A 1 1960 ILE 1960 1924 ?    ?   ?   A . n 
A 1 1961 LYS 1961 1925 ?    ?   ?   A . n 
A 1 1962 PHE 1962 1926 ?    ?   ?   A . n 
A 1 1963 ALA 1963 1927 ?    ?   ?   A . n 
A 1 1964 GLU 1964 1928 ?    ?   ?   A . n 
A 1 1965 PRO 1965 1929 ?    ?   ?   A . n 
A 1 1966 ILE 1966 1930 ?    ?   ?   A . n 
A 1 1967 SER 1967 1931 ?    ?   ?   A . n 
A 1 1968 LEU 1968 1932 ?    ?   ?   A . n 
A 1 1969 PHE 1969 1933 ?    ?   ?   A . n 
A 1 1970 VAL 1970 1934 ?    ?   ?   A . n 
A 1 1971 CYS 1971 1935 ?    ?   ?   A . n 
A 1 1972 ASP 1972 1936 ?    ?   ?   A . n 
A 1 1973 ALA 1973 1937 ?    ?   ?   A . n 
A 1 1974 GLU 1974 1938 ?    ?   ?   A . n 
A 1 1975 LEU 1975 1939 ?    ?   ?   A . n 
A 1 1976 SER 1976 1940 ?    ?   ?   A . n 
A 1 1977 VAL 1977 1941 ?    ?   ?   A . n 
A 1 1978 THR 1978 1942 ?    ?   ?   A . n 
A 1 1979 VAL 1979 1943 ?    ?   ?   A . n 
A 1 1980 ASN 1980 1944 ?    ?   ?   A . n 
A 1 1981 TRP 1981 1945 ?    ?   ?   A . n 
A 1 1982 SER 1982 1946 ?    ?   ?   A . n 
A 1 1983 LYS 1983 1947 ?    ?   ?   A . n 
A 1 1984 ILE 1984 1948 ?    ?   ?   A . n 
A 1 1985 ILE 1985 1949 ?    ?   ?   A . n 
A 1 1986 ILE 1986 1950 ?    ?   ?   A . n 
A 1 1987 GLU 1987 1951 ?    ?   ?   A . n 
A 1 1988 TRP 1988 1952 ?    ?   ?   A . n 
A 1 1989 SER 1989 1953 ?    ?   ?   A . n 
A 1 1990 LYS 1990 1954 ?    ?   ?   A . n 
A 1 1991 HIS 1991 1955 ?    ?   ?   A . n 
A 1 1992 VAL 1992 1956 ?    ?   ?   A . n 
A 1 1993 ARG 1993 1957 ?    ?   ?   A . n 
A 1 1994 LYS 1994 1958 ?    ?   ?   A . n 
A 1 1995 CYS 1995 1959 ?    ?   ?   A . n 
A 1 1996 LYS 1996 1960 ?    ?   ?   A . n 
A 1 1997 TYR 1997 1961 ?    ?   ?   A . n 
A 1 1998 CYS 1998 1962 ?    ?   ?   A . n 
A 1 1999 SER 1999 1963 ?    ?   ?   A . n 
A 1 2000 SER 2000 1964 ?    ?   ?   A . n 
A 1 2001 VAL 2001 1965 ?    ?   ?   A . n 
A 1 2002 ASN 2002 1966 ?    ?   ?   A . n 
A 1 2003 LYS 2003 1967 ?    ?   ?   A . n 
A 1 2004 CYS 2004 1968 ?    ?   ?   A . n 
A 1 2005 MET 2005 1969 ?    ?   ?   A . n 
A 1 2006 LEU 2006 1970 ?    ?   ?   A . n 
A 1 2007 ILE 2007 1971 ?    ?   ?   A . n 
A 1 2008 VAL 2008 1972 ?    ?   ?   A . n 
A 1 2009 LYS 2009 1973 ?    ?   ?   A . n 
A 1 2010 TYR 2010 1974 ?    ?   ?   A . n 
A 1 2011 HIS 2011 1975 ?    ?   ?   A . n 
A 1 2012 ALA 2012 1976 ?    ?   ?   A . n 
A 1 2013 GLN 2013 1977 ?    ?   ?   A . n 
A 1 2014 ASP 2014 1978 ?    ?   ?   A . n 
A 1 2015 ASP 2015 1979 ?    ?   ?   A . n 
A 1 2016 ILE 2016 1980 ?    ?   ?   A . n 
A 1 2017 ASP 2017 1981 ?    ?   ?   A . n 
A 1 2018 PHE 2018 1982 ?    ?   ?   A . n 
A 1 2019 LYS 2019 1983 ?    ?   ?   A . n 
A 1 2020 LEU 2020 1984 ?    ?   ?   A . n 
A 1 2021 ASP 2021 1985 ?    ?   ?   A . n 
A 1 2022 ASN 2022 1986 ?    ?   ?   A . n 
A 1 2023 ILE 2023 1987 ?    ?   ?   A . n 
A 1 2024 THR 2024 1988 ?    ?   ?   A . n 
A 1 2025 ILE 2025 1989 ?    ?   ?   A . n 
A 1 2026 LEU 2026 1990 ?    ?   ?   A . n 
A 1 2027 LYS 2027 1991 ?    ?   ?   A . n 
A 1 2028 THR 2028 1992 ?    ?   ?   A . n 
A 1 2029 TYR 2029 1993 ?    ?   ?   A . n 
A 1 2030 VAL 2030 1994 ?    ?   ?   A . n 
A 1 2031 CYS 2031 1995 ?    ?   ?   A . n 
A 1 2032 LEU 2032 1996 ?    ?   ?   A . n 
A 1 2033 GLY 2033 1997 ?    ?   ?   A . n 
A 1 2034 SER 2034 1998 ?    ?   ?   A . n 
A 1 2035 LYS 2035 1999 ?    ?   ?   A . n 
A 1 2036 LEU 2036 2000 ?    ?   ?   A . n 
A 1 2037 LYS 2037 2001 ?    ?   ?   A . n 
A 1 2038 GLY 2038 2002 ?    ?   ?   A . n 
A 1 2039 SER 2039 2003 ?    ?   ?   A . n 
A 1 2040 GLU 2040 2004 ?    ?   ?   A . n 
A 1 2041 VAL 2041 2005 ?    ?   ?   A . n 
A 1 2042 TYR 2042 2006 ?    ?   ?   A . n 
A 1 2043 LEU 2043 2007 ?    ?   ?   A . n 
A 1 2044 VAL 2044 2008 ?    ?   ?   A . n 
A 1 2045 LEU 2045 2009 ?    ?   ?   A . n 
A 1 2046 THR 2046 2010 ?    ?   ?   A . n 
A 1 2047 ILE 2047 2011 ?    ?   ?   A . n 
A 1 2048 GLY 2048 2012 ?    ?   ?   A . n 
A 1 2049 PRO 2049 2013 ?    ?   ?   A . n 
A 1 2050 ALA 2050 2014 ?    ?   ?   A . n 
A 1 2051 ASN 2051 2015 ?    ?   ?   A . n 
A 1 2052 ILE 2052 2016 ?    ?   ?   A . n 
A 1 2053 PHE 2053 2017 ?    ?   ?   A . n 
A 1 2054 PRO 2054 2018 ?    ?   ?   A . n 
A 1 2055 VAL 2055 2019 ?    ?   ?   A . n 
A 1 2056 PHE 2056 2020 ?    ?   ?   A . n 
A 1 2057 ASN 2057 2021 ?    ?   ?   A . n 
A 1 2058 VAL 2058 2022 ?    ?   ?   A . n 
A 1 2059 VAL 2059 2023 ?    ?   ?   A . n 
A 1 2060 GLN 2060 2024 ?    ?   ?   A . n 
A 1 2061 ASN 2061 2025 ?    ?   ?   A . n 
A 1 2062 ALA 2062 2026 ?    ?   ?   A . n 
A 1 2063 LYS 2063 2027 ?    ?   ?   A . n 
A 1 2064 LEU 2064 2028 ?    ?   ?   A . n 
A 1 2065 ILE 2065 2029 ?    ?   ?   A . n 
A 1 2066 LEU 2066 2030 ?    ?   ?   A . n 
A 1 2067 SER 2067 2031 ?    ?   ?   A . n 
A 1 2068 ARG 2068 2032 ?    ?   ?   A . n 
A 1 2069 THR 2069 2033 ?    ?   ?   A . n 
A 1 2070 LYS 2070 2034 ?    ?   ?   A . n 
A 1 2071 ASN 2071 2035 ?    ?   ?   A . n 
A 1 2072 PHE 2072 2036 ?    ?   ?   A . n 
A 1 2073 ILE 2073 2037 ?    ?   ?   A . n 
A 1 2074 MET 2074 2038 ?    ?   ?   A . n 
A 1 2075 PRO 2075 2039 ?    ?   ?   A . n 
A 1 2076 LYS 2076 2040 ?    ?   ?   A . n 
A 1 2077 LYS 2077 2041 ?    ?   ?   A . n 
A 1 2078 ALA 2078 2042 ?    ?   ?   A . n 
A 1 2079 ASP 2079 2043 ?    ?   ?   A . n 
A 1 2080 LYS 2080 2044 ?    ?   ?   A . n 
A 1 2081 GLU 2081 2045 ?    ?   ?   A . n 
A 1 2082 SER 2082 2046 ?    ?   ?   A . n 
A 1 2083 ILE 2083 2047 ?    ?   ?   A . n 
A 1 2084 ASP 2084 2048 ?    ?   ?   A . n 
A 1 2085 ALA 2085 2049 ?    ?   ?   A . n 
A 1 2086 ASN 2086 2050 ?    ?   ?   A . n 
A 1 2087 ILE 2087 2051 ?    ?   ?   A . n 
A 1 2088 LYS 2088 2052 ?    ?   ?   A . n 
A 1 2089 SER 2089 2053 ?    ?   ?   A . n 
A 1 2090 LEU 2090 2054 ?    ?   ?   A . n 
A 1 2091 ILE 2091 2055 ?    ?   ?   A . n 
A 1 2092 PRO 2092 2056 ?    ?   ?   A . n 
A 1 2093 PHE 2093 2057 ?    ?   ?   A . n 
A 1 2094 LEU 2094 2058 ?    ?   ?   A . n 
A 1 2095 CYS 2095 2059 ?    ?   ?   A . n 
A 1 2096 TYR 2096 2060 ?    ?   ?   A . n 
A 1 2097 PRO 2097 2061 ?    ?   ?   A . n 
A 1 2098 ILE 2098 2062 ?    ?   ?   A . n 
A 1 2099 THR 2099 2063 ?    ?   ?   A . n 
A 1 2100 LYS 2100 2064 ?    ?   ?   A . n 
A 1 2101 LYS 2101 2065 ?    ?   ?   A . n 
A 1 2102 GLY 2102 2066 ?    ?   ?   A . n 
A 1 2103 ILE 2103 2067 ?    ?   ?   A . n 
A 1 2104 ASN 2104 2068 ?    ?   ?   A . n 
A 1 2105 THR 2105 2069 ?    ?   ?   A . n 
A 1 2106 ALA 2106 2070 ?    ?   ?   A . n 
A 1 2107 LEU 2107 2071 ?    ?   ?   A . n 
A 1 2108 SER 2108 2072 ?    ?   ?   A . n 
A 1 2109 LYS 2109 2073 ?    ?   ?   A . n 
A 1 2110 LEU 2110 2074 ?    ?   ?   A . n 
A 1 2111 LYS 2111 2075 ?    ?   ?   A . n 
A 1 2112 SER 2112 2076 ?    ?   ?   A . n 
A 1 2113 VAL 2113 2077 ?    ?   ?   A . n 
A 1 2114 VAL 2114 2078 ?    ?   ?   A . n 
A 1 2115 SER 2115 2079 ?    ?   ?   A . n 
A 1 2116 GLY 2116 2080 ?    ?   ?   A . n 
A 1 2117 ASP 2117 2081 ?    ?   ?   A . n 
A 1 2118 ILE 2118 2082 ?    ?   ?   A . n 
A 1 2119 LEU 2119 2083 ?    ?   ?   A . n 
A 1 2120 SER 2120 2084 ?    ?   ?   A . n 
A 1 2121 TYR 2121 2085 ?    ?   ?   A . n 
A 1 2122 SER 2122 2086 ?    ?   ?   A . n 
A 1 2123 ILE 2123 2087 ?    ?   ?   A . n 
A 1 2124 ALA 2124 2088 ?    ?   ?   A . n 
A 1 2125 GLY 2125 2089 ?    ?   ?   A . n 
A 1 2126 ARG 2126 2090 ?    ?   ?   A . n 
A 1 2127 ASN 2127 2091 ?    ?   ?   A . n 
A 1 2128 GLU 2128 2092 ?    ?   ?   A . n 
A 1 2129 VAL 2129 2093 ?    ?   ?   A . n 
A 1 2130 PHE 2130 2094 ?    ?   ?   A . n 
A 1 2131 SER 2131 2095 ?    ?   ?   A . n 
A 1 2132 ASN 2132 2096 ?    ?   ?   A . n 
A 1 2133 LYS 2133 2097 ?    ?   ?   A . n 
A 1 2134 LEU 2134 2098 ?    ?   ?   A . n 
A 1 2135 ILE 2135 2099 ?    ?   ?   A . n 
A 1 2136 ASN 2136 2100 ?    ?   ?   A . n 
A 1 2137 HIS 2137 2101 ?    ?   ?   A . n 
A 1 2138 LYS 2138 2102 ?    ?   ?   A . n 
A 1 2139 HIS 2139 2103 ?    ?   ?   A . n 
A 1 2140 MET 2140 2104 ?    ?   ?   A . n 
A 1 2141 ASN 2141 2105 ?    ?   ?   A . n 
A 1 2142 ILE 2142 2106 ?    ?   ?   A . n 
A 1 2143 LEU 2143 2107 ?    ?   ?   A . n 
A 1 2144 LYS 2144 2108 ?    ?   ?   A . n 
A 1 2145 TRP 2145 2109 ?    ?   ?   A . n 
A 1 2146 PHE 2146 2110 ?    ?   ?   A . n 
A 1 2147 ASN 2147 2111 ?    ?   ?   A . n 
A 1 2148 HIS 2148 2112 ?    ?   ?   A . n 
A 1 2149 VAL 2149 2113 ?    ?   ?   A . n 
A 1 2150 LEU 2150 2114 ?    ?   ?   A . n 
A 1 2151 ASN 2151 2115 ?    ?   ?   A . n 
A 1 2152 PHE 2152 2116 ?    ?   ?   A . n 
A 1 2153 ARG 2153 2117 ?    ?   ?   A . n 
A 1 2154 SER 2154 2118 ?    ?   ?   A . n 
A 1 2155 THR 2155 2119 ?    ?   ?   A . n 
A 1 2156 GLU 2156 2120 ?    ?   ?   A . n 
A 1 2157 LEU 2157 2121 ?    ?   ?   A . n 
A 1 2158 ASN 2158 2122 ?    ?   ?   A . n 
A 1 2159 TYR 2159 2123 ?    ?   ?   A . n 
A 1 2160 ASN 2160 2124 ?    ?   ?   A . n 
A 1 2161 HIS 2161 2125 ?    ?   ?   A . n 
A 1 2162 LEU 2162 2126 ?    ?   ?   A . n 
A 1 2163 TYR 2163 2127 ?    ?   ?   A . n 
A 1 2164 MET 2164 2128 ?    ?   ?   A . n 
A 1 2165 VAL 2165 2129 ?    ?   ?   A . n 
A 1 2166 GLU 2166 2130 ?    ?   ?   A . n 
A 1 2167 SER 2167 2131 ?    ?   ?   A . n 
A 1 2168 THR 2168 2132 ?    ?   ?   A . n 
A 1 2169 TYR 2169 2133 ?    ?   ?   A . n 
A 1 2170 PRO 2170 2134 ?    ?   ?   A . n 
A 1 2171 TYR 2171 2135 ?    ?   ?   A . n 
A 1 2172 LEU 2172 2136 ?    ?   ?   A . n 
A 1 2173 SER 2173 2137 ?    ?   ?   A . n 
A 1 2174 GLU 2174 2138 ?    ?   ?   A . n 
A 1 2175 LEU 2175 2139 ?    ?   ?   A . n 
A 1 2176 LEU 2176 2140 ?    ?   ?   A . n 
A 1 2177 ASN 2177 2141 ?    ?   ?   A . n 
A 1 2178 SER 2178 2142 ?    ?   ?   A . n 
A 1 2179 LEU 2179 2143 ?    ?   ?   A . n 
A 1 2180 THR 2180 2144 ?    ?   ?   A . n 
A 1 2181 THR 2181 2145 ?    ?   ?   A . n 
A 1 2182 ASN 2182 2146 ?    ?   ?   A . n 
A 1 2183 GLU 2183 2147 ?    ?   ?   A . n 
A 1 2184 LEU 2184 2148 ?    ?   ?   A . n 
A 1 2185 LYS 2185 2149 ?    ?   ?   A . n 
A 1 2186 LYS 2186 2150 ?    ?   ?   A . n 
A 1 2187 LEU 2187 2151 ?    ?   ?   A . n 
A 1 2188 ILE 2188 2152 ?    ?   ?   A . n 
A 1 2189 LYS 2189 2153 ?    ?   ?   A . n 
A 1 2190 ILE 2190 2154 ?    ?   ?   A . n 
A 1 2191 THR 2191 2155 ?    ?   ?   A . n 
A 1 2192 GLY 2192 2156 ?    ?   ?   A . n 
A 1 2193 SER 2193 2157 ?    ?   ?   A . n 
A 1 2194 LEU 2194 2158 ?    ?   ?   A . n 
A 1 2195 LEU 2195 2159 ?    ?   ?   A . n 
A 1 2196 TYR 2196 2160 ?    ?   ?   A . n 
A 1 2197 ASN 2197 2161 ?    ?   ?   A . n 
A 1 2198 PHE 2198 2162 ?    ?   ?   A . n 
A 1 2199 HIS 2199 2163 ?    ?   ?   A . n 
A 1 2200 ASN 2200 2164 ?    ?   ?   A . n 
A 1 2201 GLU 2201 2165 ?    ?   ?   A . n 
B 2 1    MET 1    1    ?    ?   ?   B . n 
B 2 2    GLU 2    2    ?    ?   ?   B . n 
B 2 3    LYS 3    3    ?    ?   ?   B . n 
B 2 4    PHE 4    4    ?    ?   ?   B . n 
B 2 5    ALA 5    5    ?    ?   ?   B . n 
B 2 6    PRO 6    6    ?    ?   ?   B . n 
B 2 7    GLU 7    7    ?    ?   ?   B . n 
B 2 8    PHE 8    8    ?    ?   ?   B . n 
B 2 9    HIS 9    9    ?    ?   ?   B . n 
B 2 10   GLY 10   10   ?    ?   ?   B . n 
B 2 11   GLU 11   11   ?    ?   ?   B . n 
B 2 12   ASP 12   12   ?    ?   ?   B . n 
B 2 13   ALA 13   13   ?    ?   ?   B . n 
B 2 14   ASN 14   14   ?    ?   ?   B . n 
B 2 15   ASN 15   15   ?    ?   ?   B . n 
B 2 16   ARG 16   16   ?    ?   ?   B . n 
B 2 17   ALA 17   17   ?    ?   ?   B . n 
B 2 18   THR 18   18   ?    ?   ?   B . n 
B 2 19   LYS 19   19   ?    ?   ?   B . n 
B 2 20   PHE 20   20   ?    ?   ?   B . n 
B 2 21   LEU 21   21   ?    ?   ?   B . n 
B 2 22   GLU 22   22   ?    ?   ?   B . n 
B 2 23   SER 23   23   ?    ?   ?   B . n 
B 2 24   ILE 24   24   ?    ?   ?   B . n 
B 2 25   LYS 25   25   ?    ?   ?   B . n 
B 2 26   GLY 26   26   ?    ?   ?   B . n 
B 2 27   LYS 27   27   ?    ?   ?   B . n 
B 2 28   PHE 28   28   ?    ?   ?   B . n 
B 2 29   THR 29   29   ?    ?   ?   B . n 
B 2 30   SER 30   30   ?    ?   ?   B . n 
B 2 31   PRO 31   31   ?    ?   ?   B . n 
B 2 32   LYS 32   32   ?    ?   ?   B . n 
B 2 33   ASP 33   33   ?    ?   ?   B . n 
B 2 34   PRO 34   34   ?    ?   ?   B . n 
B 2 35   LYS 35   35   ?    ?   ?   B . n 
B 2 36   LYS 36   36   ?    ?   ?   B . n 
B 2 37   LYS 37   37   ?    ?   ?   B . n 
B 2 38   ASP 38   38   ?    ?   ?   B . n 
B 2 39   SER 39   39   ?    ?   ?   B . n 
B 2 40   ILE 40   40   ?    ?   ?   B . n 
B 2 41   ILE 41   41   ?    ?   ?   B . n 
B 2 42   SER 42   42   ?    ?   ?   B . n 
B 2 43   VAL 43   43   ?    ?   ?   B . n 
B 2 44   ASN 44   44   ?    ?   ?   B . n 
B 2 45   SER 45   45   ?    ?   ?   B . n 
B 2 46   ILE 46   46   ?    ?   ?   B . n 
B 2 47   ASP 47   47   ?    ?   ?   B . n 
B 2 48   ILE 48   48   ?    ?   ?   B . n 
B 2 49   GLU 49   49   ?    ?   ?   B . n 
B 2 50   VAL 50   50   ?    ?   ?   B . n 
B 2 51   THR 51   51   ?    ?   ?   B . n 
B 2 52   LYS 52   52   ?    ?   ?   B . n 
B 2 53   GLU 53   53   ?    ?   ?   B . n 
B 2 54   SER 54   54   ?    ?   ?   B . n 
B 2 55   PRO 55   55   ?    ?   ?   B . n 
B 2 56   ILE 56   56   ?    ?   ?   B . n 
B 2 57   THR 57   57   ?    ?   ?   B . n 
B 2 58   SER 58   58   ?    ?   ?   B . n 
B 2 59   ASN 59   59   ?    ?   ?   B . n 
B 2 60   SER 60   60   ?    ?   ?   B . n 
B 2 61   THR 61   61   ?    ?   ?   B . n 
B 2 62   ILE 62   62   ?    ?   ?   B . n 
B 2 63   ILE 63   63   ?    ?   ?   B . n 
B 2 64   ASN 64   64   ?    ?   ?   B . n 
B 2 65   PRO 65   65   ?    ?   ?   B . n 
B 2 66   THR 66   66   ?    ?   ?   B . n 
B 2 67   ASN 67   67   ?    ?   ?   B . n 
B 2 68   GLU 68   68   ?    ?   ?   B . n 
B 2 69   THR 69   69   ?    ?   ?   B . n 
B 2 70   ASP 70   70   ?    ?   ?   B . n 
B 2 71   ASP 71   71   ?    ?   ?   B . n 
B 2 72   THR 72   72   ?    ?   ?   B . n 
B 2 73   ALA 73   73   ?    ?   ?   B . n 
B 2 74   GLY 74   74   ?    ?   ?   B . n 
B 2 75   ASN 75   75   ?    ?   ?   B . n 
B 2 76   LYS 76   76   ?    ?   ?   B . n 
B 2 77   PRO 77   77   ?    ?   ?   B . n 
B 2 78   ASN 78   78   ?    ?   ?   B . n 
B 2 79   TYR 79   79   ?    ?   ?   B . n 
B 2 80   GLN 80   80   ?    ?   ?   B . n 
B 2 81   ARG 81   81   ?    ?   ?   B . n 
B 2 82   LYS 82   82   ?    ?   ?   B . n 
B 2 83   PRO 83   83   ?    ?   ?   B . n 
B 2 84   LEU 84   84   ?    ?   ?   B . n 
B 2 85   VAL 85   85   ?    ?   ?   B . n 
B 2 86   SER 86   86   ?    ?   ?   B . n 
B 2 87   PHE 87   87   ?    ?   ?   B . n 
B 2 88   LYS 88   88   ?    ?   ?   B . n 
B 2 89   GLU 89   89   ?    ?   ?   B . n 
B 2 90   ASP 90   90   ?    ?   ?   B . n 
B 2 91   PRO 91   91   ?    ?   ?   B . n 
B 2 92   THR 92   92   ?    ?   ?   B . n 
B 2 93   PRO 93   93   ?    ?   ?   B . n 
B 2 94   SER 94   94   ?    ?   ?   B . n 
B 2 95   ASP 95   95   ?    ?   ?   B . n 
B 2 96   ASN 96   96   ?    ?   ?   B . n 
B 2 97   PRO 97   97   ?    ?   ?   B . n 
B 2 98   PHE 98   98   ?    ?   ?   B . n 
B 2 99   SER 99   99   ?    ?   ?   B . n 
B 2 100  LYS 100  100  ?    ?   ?   B . n 
B 2 101  LEU 101  101  ?    ?   ?   B . n 
B 2 102  TYR 102  102  ?    ?   ?   B . n 
B 2 103  LYS 103  103  ?    ?   ?   B . n 
B 2 104  GLU 104  104  ?    ?   ?   B . n 
B 2 105  THR 105  105  ?    ?   ?   B . n 
B 2 106  ILE 106  106  ?    ?   ?   B . n 
B 2 107  GLU 107  107  ?    ?   ?   B . n 
B 2 108  THR 108  108  ?    ?   ?   B . n 
B 2 109  PHE 109  109  ?    ?   ?   B . n 
B 2 110  ASP 110  110  ?    ?   ?   B . n 
B 2 111  ASN 111  111  ?    ?   ?   B . n 
B 2 112  ASN 112  112  ?    ?   ?   B . n 
B 2 113  GLU 113  113  ?    ?   ?   B . n 
B 2 114  GLU 114  114  ?    ?   ?   B . n 
B 2 115  GLU 115  115  ?    ?   ?   B . n 
B 2 116  SER 116  116  ?    ?   ?   B . n 
B 2 117  SER 117  117  ?    ?   ?   B . n 
B 2 118  TYR 118  118  ?    ?   ?   B . n 
B 2 119  SER 119  119  ?    ?   ?   B . n 
B 2 120  TYR 120  120  ?    ?   ?   B . n 
B 2 121  GLU 121  121  ?    ?   ?   B . n 
B 2 122  GLU 122  122  ?    ?   ?   B . n 
B 2 123  ILE 123  123  ?    ?   ?   B . n 
B 2 124  ASN 124  124  ?    ?   ?   B . n 
B 2 125  ASP 125  125  ?    ?   ?   B . n 
B 2 126  GLN 126  126  ?    ?   ?   B . n 
B 2 127  THR 127  127  ?    ?   ?   B . n 
B 2 128  ASN 128  128  128  ASN ASN B . n 
B 2 129  ASP 129  129  129  ASP ASP B . n 
B 2 130  ASN 130  130  130  ASN ASN B . n 
B 2 131  ILE 131  131  131  ILE ILE B . n 
B 2 132  THR 132  132  132  THR THR B . n 
B 2 133  ALA 133  133  133  ALA ALA B . n 
B 2 134  ARG 134  134  134  ARG ARG B . n 
B 2 135  LEU 135  135  135  LEU LEU B . n 
B 2 136  ASP 136  136  136  ASP ASP B . n 
B 2 137  ARG 137  137  137  ARG ARG B . n 
B 2 138  ILE 138  138  138  ILE ILE B . n 
B 2 139  ASP 139  139  139  ASP ASP B . n 
B 2 140  GLU 140  140  140  GLU GLU B . n 
B 2 141  LYS 141  141  141  LYS LYS B . n 
B 2 142  LEU 142  142  142  LEU LEU B . n 
B 2 143  SER 143  143  143  SER SER B . n 
B 2 144  GLU 144  144  144  GLU GLU B . n 
B 2 145  ILE 145  145  145  ILE ILE B . n 
B 2 146  LEU 146  146  146  LEU LEU B . n 
B 2 147  GLY 147  147  147  GLY GLY B . n 
B 2 148  MET 148  148  148  MET MET B . n 
B 2 149  LEU 149  149  149  LEU LEU B . n 
B 2 150  HIS 150  150  150  HIS HIS B . n 
B 2 151  THR 151  151  151  THR THR B . n 
B 2 152  LEU 152  152  152  LEU LEU B . n 
B 2 153  VAL 153  153  153  VAL VAL B . n 
B 2 154  VAL 154  154  154  VAL VAL B . n 
B 2 155  ALA 155  155  155  ALA ALA B . n 
B 2 156  SER 156  156  156  SER SER B . n 
B 2 157  ALA 157  157  157  ALA ALA B . n 
B 2 158  GLY 158  158  158  GLY GLY B . n 
B 2 159  PRO 159  159  159  PRO PRO B . n 
B 2 160  THR 160  160  160  THR THR B . n 
B 2 161  SER 161  161  161  SER SER B . n 
B 2 162  ALA 162  162  162  ALA ALA B . n 
B 2 163  ARG 163  163  163  ARG ARG B . n 
B 2 164  ASP 164  164  164  ASP ASP B . n 
B 2 165  GLY 165  165  165  GLY GLY B . n 
B 2 166  ILE 166  166  166  ILE ILE B . n 
B 2 167  ARG 167  167  167  ARG ARG B . n 
B 2 168  ASP 168  168  168  ASP ASP B . n 
B 2 169  ALA 169  169  169  ALA ALA B . n 
B 2 170  MET 170  170  170  MET MET B . n 
B 2 171  ILE 171  171  171  ILE ILE B . n 
B 2 172  GLY 172  172  172  GLY GLY B . n 
B 2 173  LEU 173  173  173  LEU LEU B . n 
B 2 174  ARG 174  174  174  ARG ARG B . n 
B 2 175  GLU 175  175  175  GLU GLU B . n 
B 2 176  GLU 176  176  176  GLU GLU B . n 
B 2 177  MET 177  177  177  MET MET B . n 
B 2 178  ILE 178  178  178  ILE ILE B . n 
B 2 179  GLU 179  179  179  GLU GLU B . n 
B 2 180  LYS 180  180  180  LYS LYS B . n 
B 2 181  ILE 181  181  181  ILE ILE B . n 
B 2 182  ARG 182  182  182  ARG ARG B . n 
B 2 183  THR 183  183  183  THR THR B . n 
B 2 184  GLU 184  184  184  GLU GLU B . n 
B 2 185  ALA 185  185  185  ALA ALA B . n 
B 2 186  LEU 186  186  186  LEU LEU B . n 
B 2 187  MET 187  187  187  MET MET B . n 
B 2 188  THR 188  188  188  THR THR B . n 
B 2 189  ASN 189  189  189  ASN ASN B . n 
B 2 190  ASP 190  190  190  ASP ASP B . n 
B 2 191  ARG 191  191  191  ARG ARG B . n 
B 2 192  LEU 192  192  192  LEU LEU B . n 
B 2 193  GLU 193  193  193  GLU GLU B . n 
B 2 194  ALA 194  194  194  ALA ALA B . n 
B 2 195  MET 195  195  195  MET MET B . n 
B 2 196  ALA 196  196  196  ALA ALA B . n 
B 2 197  ARG 197  197  197  ARG ARG B . n 
B 2 198  LEU 198  198  198  LEU LEU B . n 
B 2 199  ARG 199  199  199  ARG ARG B . n 
B 2 200  ASN 200  200  200  ASN ASN B . n 
B 2 201  GLU 201  201  201  GLU GLU B . n 
B 2 202  GLU 202  202  202  GLU GLU B . n 
B 2 203  SER 203  203  203  SER SER B . n 
B 2 204  GLU 204  204  204  GLU GLU B . n 
B 2 205  LYS 205  205  205  LYS LYS B . n 
B 2 206  MET 206  206  206  MET MET B . n 
B 2 207  ALA 207  207  207  ALA ALA B . n 
B 2 208  LYS 208  208  208  LYS LYS B . n 
B 2 209  ASP 209  209  209  ASP ASP B . n 
B 2 210  THR 210  210  210  THR THR B . n 
B 2 211  SER 211  211  211  SER SER B . n 
B 2 212  ASP 212  212  212  ASP ASP B . n 
B 2 213  GLU 213  213  213  GLU GLU B . n 
B 2 214  VAL 214  214  214  VAL VAL B . n 
B 2 215  SER 215  215  215  SER SER B . n 
B 2 216  LEU 216  216  216  LEU LEU B . n 
B 2 217  ASN 217  217  217  ASN ASN B . n 
B 2 218  PRO 218  218  218  PRO PRO B . n 
B 2 219  THR 219  219  219  THR THR B . n 
B 2 220  SER 220  220  220  SER SER B . n 
B 2 221  GLU 221  221  221  GLU GLU B . n 
B 2 222  LYS 222  222  222  LYS LYS B . n 
B 2 223  LEU 223  223  223  LEU LEU B . n 
B 2 224  ASN 224  224  224  ASN ASN B . n 
B 2 225  ASN 225  225  225  ASN ASN B . n 
B 2 226  LEU 226  226  226  LEU LEU B . n 
B 2 227  LEU 227  227  227  LEU LEU B . n 
B 2 228  GLU 228  228  228  GLU GLU B . n 
B 2 229  GLY 229  229  229  GLY GLY B . n 
B 2 230  ASN 230  230  230  ASN ASN B . n 
B 2 231  ASP 231  231  231  ASP ASP B . n 
B 2 232  SER 232  232  232  SER SER B . n 
B 2 233  ASP 233  233  233  ASP ASP B . n 
B 2 234  ASN 234  234  234  ASN ASN B . n 
B 2 235  ASP 235  235  235  ASP ASP B . n 
B 2 236  LEU 236  236  236  LEU LEU B . n 
B 2 237  SER 237  237  237  SER SER B . n 
B 2 238  LEU 238  238  238  LEU LEU B . n 
B 2 239  GLU 239  239  239  GLU GLU B . n 
B 2 240  ASP 240  240  240  ASP ASP B . n 
B 2 241  PHE 241  241  241  PHE PHE B . n 
B 2 242  LYS 242  242  ?    ?   ?   B . n 
B 2 243  GLY 243  243  ?    ?   ?   B . n 
B 2 244  GLU 244  244  ?    ?   ?   B . n 
B 2 245  ASN 245  245  ?    ?   ?   B . n 
B 2 246  LYS 246  246  ?    ?   ?   B . n 
B 2 247  TYR 247  247  ?    ?   ?   B . n 
B 2 248  PHE 248  248  ?    ?   ?   B . n 
B 2 249  GLN 249  249  ?    ?   ?   B . n 
B 2 250  GLY 250  250  ?    ?   ?   B . n 
B 2 251  HIS 251  251  ?    ?   ?   B . n 
B 2 252  HIS 252  252  ?    ?   ?   B . n 
B 2 253  HIS 253  253  ?    ?   ?   B . n 
B 2 254  HIS 254  254  ?    ?   ?   B . n 
B 2 255  HIS 255  255  ?    ?   ?   B . n 
B 2 256  HIS 256  256  ?    ?   ?   B . n 
C 2 1    MET 1    1    ?    ?   ?   C . n 
C 2 2    GLU 2    2    ?    ?   ?   C . n 
C 2 3    LYS 3    3    ?    ?   ?   C . n 
C 2 4    PHE 4    4    ?    ?   ?   C . n 
C 2 5    ALA 5    5    ?    ?   ?   C . n 
C 2 6    PRO 6    6    ?    ?   ?   C . n 
C 2 7    GLU 7    7    ?    ?   ?   C . n 
C 2 8    PHE 8    8    ?    ?   ?   C . n 
C 2 9    HIS 9    9    ?    ?   ?   C . n 
C 2 10   GLY 10   10   ?    ?   ?   C . n 
C 2 11   GLU 11   11   ?    ?   ?   C . n 
C 2 12   ASP 12   12   ?    ?   ?   C . n 
C 2 13   ALA 13   13   ?    ?   ?   C . n 
C 2 14   ASN 14   14   ?    ?   ?   C . n 
C 2 15   ASN 15   15   ?    ?   ?   C . n 
C 2 16   ARG 16   16   ?    ?   ?   C . n 
C 2 17   ALA 17   17   ?    ?   ?   C . n 
C 2 18   THR 18   18   ?    ?   ?   C . n 
C 2 19   LYS 19   19   ?    ?   ?   C . n 
C 2 20   PHE 20   20   ?    ?   ?   C . n 
C 2 21   LEU 21   21   ?    ?   ?   C . n 
C 2 22   GLU 22   22   ?    ?   ?   C . n 
C 2 23   SER 23   23   ?    ?   ?   C . n 
C 2 24   ILE 24   24   ?    ?   ?   C . n 
C 2 25   LYS 25   25   ?    ?   ?   C . n 
C 2 26   GLY 26   26   ?    ?   ?   C . n 
C 2 27   LYS 27   27   ?    ?   ?   C . n 
C 2 28   PHE 28   28   ?    ?   ?   C . n 
C 2 29   THR 29   29   ?    ?   ?   C . n 
C 2 30   SER 30   30   ?    ?   ?   C . n 
C 2 31   PRO 31   31   ?    ?   ?   C . n 
C 2 32   LYS 32   32   ?    ?   ?   C . n 
C 2 33   ASP 33   33   ?    ?   ?   C . n 
C 2 34   PRO 34   34   ?    ?   ?   C . n 
C 2 35   LYS 35   35   ?    ?   ?   C . n 
C 2 36   LYS 36   36   ?    ?   ?   C . n 
C 2 37   LYS 37   37   ?    ?   ?   C . n 
C 2 38   ASP 38   38   ?    ?   ?   C . n 
C 2 39   SER 39   39   ?    ?   ?   C . n 
C 2 40   ILE 40   40   ?    ?   ?   C . n 
C 2 41   ILE 41   41   ?    ?   ?   C . n 
C 2 42   SER 42   42   ?    ?   ?   C . n 
C 2 43   VAL 43   43   ?    ?   ?   C . n 
C 2 44   ASN 44   44   ?    ?   ?   C . n 
C 2 45   SER 45   45   ?    ?   ?   C . n 
C 2 46   ILE 46   46   ?    ?   ?   C . n 
C 2 47   ASP 47   47   ?    ?   ?   C . n 
C 2 48   ILE 48   48   ?    ?   ?   C . n 
C 2 49   GLU 49   49   ?    ?   ?   C . n 
C 2 50   VAL 50   50   ?    ?   ?   C . n 
C 2 51   THR 51   51   ?    ?   ?   C . n 
C 2 52   LYS 52   52   ?    ?   ?   C . n 
C 2 53   GLU 53   53   ?    ?   ?   C . n 
C 2 54   SER 54   54   ?    ?   ?   C . n 
C 2 55   PRO 55   55   ?    ?   ?   C . n 
C 2 56   ILE 56   56   ?    ?   ?   C . n 
C 2 57   THR 57   57   ?    ?   ?   C . n 
C 2 58   SER 58   58   ?    ?   ?   C . n 
C 2 59   ASN 59   59   ?    ?   ?   C . n 
C 2 60   SER 60   60   ?    ?   ?   C . n 
C 2 61   THR 61   61   ?    ?   ?   C . n 
C 2 62   ILE 62   62   ?    ?   ?   C . n 
C 2 63   ILE 63   63   ?    ?   ?   C . n 
C 2 64   ASN 64   64   ?    ?   ?   C . n 
C 2 65   PRO 65   65   ?    ?   ?   C . n 
C 2 66   THR 66   66   ?    ?   ?   C . n 
C 2 67   ASN 67   67   ?    ?   ?   C . n 
C 2 68   GLU 68   68   ?    ?   ?   C . n 
C 2 69   THR 69   69   ?    ?   ?   C . n 
C 2 70   ASP 70   70   ?    ?   ?   C . n 
C 2 71   ASP 71   71   ?    ?   ?   C . n 
C 2 72   THR 72   72   ?    ?   ?   C . n 
C 2 73   ALA 73   73   ?    ?   ?   C . n 
C 2 74   GLY 74   74   ?    ?   ?   C . n 
C 2 75   ASN 75   75   ?    ?   ?   C . n 
C 2 76   LYS 76   76   ?    ?   ?   C . n 
C 2 77   PRO 77   77   ?    ?   ?   C . n 
C 2 78   ASN 78   78   ?    ?   ?   C . n 
C 2 79   TYR 79   79   ?    ?   ?   C . n 
C 2 80   GLN 80   80   ?    ?   ?   C . n 
C 2 81   ARG 81   81   ?    ?   ?   C . n 
C 2 82   LYS 82   82   ?    ?   ?   C . n 
C 2 83   PRO 83   83   ?    ?   ?   C . n 
C 2 84   LEU 84   84   ?    ?   ?   C . n 
C 2 85   VAL 85   85   ?    ?   ?   C . n 
C 2 86   SER 86   86   ?    ?   ?   C . n 
C 2 87   PHE 87   87   ?    ?   ?   C . n 
C 2 88   LYS 88   88   ?    ?   ?   C . n 
C 2 89   GLU 89   89   ?    ?   ?   C . n 
C 2 90   ASP 90   90   ?    ?   ?   C . n 
C 2 91   PRO 91   91   ?    ?   ?   C . n 
C 2 92   THR 92   92   ?    ?   ?   C . n 
C 2 93   PRO 93   93   ?    ?   ?   C . n 
C 2 94   SER 94   94   ?    ?   ?   C . n 
C 2 95   ASP 95   95   ?    ?   ?   C . n 
C 2 96   ASN 96   96   ?    ?   ?   C . n 
C 2 97   PRO 97   97   ?    ?   ?   C . n 
C 2 98   PHE 98   98   ?    ?   ?   C . n 
C 2 99   SER 99   99   ?    ?   ?   C . n 
C 2 100  LYS 100  100  ?    ?   ?   C . n 
C 2 101  LEU 101  101  ?    ?   ?   C . n 
C 2 102  TYR 102  102  ?    ?   ?   C . n 
C 2 103  LYS 103  103  ?    ?   ?   C . n 
C 2 104  GLU 104  104  ?    ?   ?   C . n 
C 2 105  THR 105  105  ?    ?   ?   C . n 
C 2 106  ILE 106  106  ?    ?   ?   C . n 
C 2 107  GLU 107  107  ?    ?   ?   C . n 
C 2 108  THR 108  108  ?    ?   ?   C . n 
C 2 109  PHE 109  109  ?    ?   ?   C . n 
C 2 110  ASP 110  110  ?    ?   ?   C . n 
C 2 111  ASN 111  111  ?    ?   ?   C . n 
C 2 112  ASN 112  112  ?    ?   ?   C . n 
C 2 113  GLU 113  113  ?    ?   ?   C . n 
C 2 114  GLU 114  114  ?    ?   ?   C . n 
C 2 115  GLU 115  115  ?    ?   ?   C . n 
C 2 116  SER 116  116  ?    ?   ?   C . n 
C 2 117  SER 117  117  ?    ?   ?   C . n 
C 2 118  TYR 118  118  ?    ?   ?   C . n 
C 2 119  SER 119  119  ?    ?   ?   C . n 
C 2 120  TYR 120  120  ?    ?   ?   C . n 
C 2 121  GLU 121  121  ?    ?   ?   C . n 
C 2 122  GLU 122  122  ?    ?   ?   C . n 
C 2 123  ILE 123  123  ?    ?   ?   C . n 
C 2 124  ASN 124  124  ?    ?   ?   C . n 
C 2 125  ASP 125  125  ?    ?   ?   C . n 
C 2 126  GLN 126  126  ?    ?   ?   C . n 
C 2 127  THR 127  127  ?    ?   ?   C . n 
C 2 128  ASN 128  128  ?    ?   ?   C . n 
C 2 129  ASP 129  129  ?    ?   ?   C . n 
C 2 130  ASN 130  130  130  ASN ASN C . n 
C 2 131  ILE 131  131  131  ILE ILE C . n 
C 2 132  THR 132  132  132  THR THR C . n 
C 2 133  ALA 133  133  133  ALA ALA C . n 
C 2 134  ARG 134  134  134  ARG ARG C . n 
C 2 135  LEU 135  135  135  LEU LEU C . n 
C 2 136  ASP 136  136  136  ASP ASP C . n 
C 2 137  ARG 137  137  137  ARG ARG C . n 
C 2 138  ILE 138  138  138  ILE ILE C . n 
C 2 139  ASP 139  139  139  ASP ASP C . n 
C 2 140  GLU 140  140  140  GLU GLU C . n 
C 2 141  LYS 141  141  141  LYS LYS C . n 
C 2 142  LEU 142  142  142  LEU LEU C . n 
C 2 143  SER 143  143  143  SER SER C . n 
C 2 144  GLU 144  144  144  GLU GLU C . n 
C 2 145  ILE 145  145  145  ILE ILE C . n 
C 2 146  LEU 146  146  146  LEU LEU C . n 
C 2 147  GLY 147  147  147  GLY GLY C . n 
C 2 148  MET 148  148  148  MET MET C . n 
C 2 149  LEU 149  149  149  LEU LEU C . n 
C 2 150  HIS 150  150  150  HIS HIS C . n 
C 2 151  THR 151  151  151  THR THR C . n 
C 2 152  LEU 152  152  152  LEU LEU C . n 
C 2 153  VAL 153  153  153  VAL VAL C . n 
C 2 154  VAL 154  154  154  VAL VAL C . n 
C 2 155  ALA 155  155  155  ALA ALA C . n 
C 2 156  SER 156  156  156  SER SER C . n 
C 2 157  ALA 157  157  157  ALA ALA C . n 
C 2 158  GLY 158  158  158  GLY GLY C . n 
C 2 159  PRO 159  159  159  PRO PRO C . n 
C 2 160  THR 160  160  160  THR THR C . n 
C 2 161  SER 161  161  161  SER SER C . n 
C 2 162  ALA 162  162  162  ALA ALA C . n 
C 2 163  ARG 163  163  163  ARG ARG C . n 
C 2 164  ASP 164  164  164  ASP ASP C . n 
C 2 165  GLY 165  165  165  GLY GLY C . n 
C 2 166  ILE 166  166  166  ILE ILE C . n 
C 2 167  ARG 167  167  167  ARG ARG C . n 
C 2 168  ASP 168  168  168  ASP ASP C . n 
C 2 169  ALA 169  169  169  ALA ALA C . n 
C 2 170  MET 170  170  170  MET MET C . n 
C 2 171  ILE 171  171  171  ILE ILE C . n 
C 2 172  GLY 172  172  172  GLY GLY C . n 
C 2 173  LEU 173  173  173  LEU LEU C . n 
C 2 174  ARG 174  174  174  ARG ARG C . n 
C 2 175  GLU 175  175  175  GLU GLU C . n 
C 2 176  GLU 176  176  176  GLU GLU C . n 
C 2 177  MET 177  177  177  MET MET C . n 
C 2 178  ILE 178  178  178  ILE ILE C . n 
C 2 179  GLU 179  179  179  GLU GLU C . n 
C 2 180  LYS 180  180  180  LYS LYS C . n 
C 2 181  ILE 181  181  181  ILE ILE C . n 
C 2 182  ARG 182  182  182  ARG ARG C . n 
C 2 183  THR 183  183  183  THR THR C . n 
C 2 184  GLU 184  184  184  GLU GLU C . n 
C 2 185  ALA 185  185  185  ALA ALA C . n 
C 2 186  LEU 186  186  186  LEU LEU C . n 
C 2 187  MET 187  187  ?    ?   ?   C . n 
C 2 188  THR 188  188  ?    ?   ?   C . n 
C 2 189  ASN 189  189  ?    ?   ?   C . n 
C 2 190  ASP 190  190  ?    ?   ?   C . n 
C 2 191  ARG 191  191  ?    ?   ?   C . n 
C 2 192  LEU 192  192  ?    ?   ?   C . n 
C 2 193  GLU 193  193  ?    ?   ?   C . n 
C 2 194  ALA 194  194  ?    ?   ?   C . n 
C 2 195  MET 195  195  ?    ?   ?   C . n 
C 2 196  ALA 196  196  ?    ?   ?   C . n 
C 2 197  ARG 197  197  ?    ?   ?   C . n 
C 2 198  LEU 198  198  ?    ?   ?   C . n 
C 2 199  ARG 199  199  ?    ?   ?   C . n 
C 2 200  ASN 200  200  ?    ?   ?   C . n 
C 2 201  GLU 201  201  ?    ?   ?   C . n 
C 2 202  GLU 202  202  ?    ?   ?   C . n 
C 2 203  SER 203  203  ?    ?   ?   C . n 
C 2 204  GLU 204  204  ?    ?   ?   C . n 
C 2 205  LYS 205  205  ?    ?   ?   C . n 
C 2 206  MET 206  206  ?    ?   ?   C . n 
C 2 207  ALA 207  207  ?    ?   ?   C . n 
C 2 208  LYS 208  208  ?    ?   ?   C . n 
C 2 209  ASP 209  209  ?    ?   ?   C . n 
C 2 210  THR 210  210  ?    ?   ?   C . n 
C 2 211  SER 211  211  ?    ?   ?   C . n 
C 2 212  ASP 212  212  ?    ?   ?   C . n 
C 2 213  GLU 213  213  ?    ?   ?   C . n 
C 2 214  VAL 214  214  ?    ?   ?   C . n 
C 2 215  SER 215  215  ?    ?   ?   C . n 
C 2 216  LEU 216  216  ?    ?   ?   C . n 
C 2 217  ASN 217  217  ?    ?   ?   C . n 
C 2 218  PRO 218  218  ?    ?   ?   C . n 
C 2 219  THR 219  219  ?    ?   ?   C . n 
C 2 220  SER 220  220  ?    ?   ?   C . n 
C 2 221  GLU 221  221  ?    ?   ?   C . n 
C 2 222  LYS 222  222  ?    ?   ?   C . n 
C 2 223  LEU 223  223  ?    ?   ?   C . n 
C 2 224  ASN 224  224  ?    ?   ?   C . n 
C 2 225  ASN 225  225  ?    ?   ?   C . n 
C 2 226  LEU 226  226  ?    ?   ?   C . n 
C 2 227  LEU 227  227  ?    ?   ?   C . n 
C 2 228  GLU 228  228  ?    ?   ?   C . n 
C 2 229  GLY 229  229  ?    ?   ?   C . n 
C 2 230  ASN 230  230  ?    ?   ?   C . n 
C 2 231  ASP 231  231  ?    ?   ?   C . n 
C 2 232  SER 232  232  ?    ?   ?   C . n 
C 2 233  ASP 233  233  ?    ?   ?   C . n 
C 2 234  ASN 234  234  ?    ?   ?   C . n 
C 2 235  ASP 235  235  ?    ?   ?   C . n 
C 2 236  LEU 236  236  ?    ?   ?   C . n 
C 2 237  SER 237  237  ?    ?   ?   C . n 
C 2 238  LEU 238  238  ?    ?   ?   C . n 
C 2 239  GLU 239  239  ?    ?   ?   C . n 
C 2 240  ASP 240  240  ?    ?   ?   C . n 
C 2 241  PHE 241  241  ?    ?   ?   C . n 
C 2 242  LYS 242  242  ?    ?   ?   C . n 
C 2 243  GLY 243  243  ?    ?   ?   C . n 
C 2 244  GLU 244  244  ?    ?   ?   C . n 
C 2 245  ASN 245  245  ?    ?   ?   C . n 
C 2 246  LYS 246  246  ?    ?   ?   C . n 
C 2 247  TYR 247  247  ?    ?   ?   C . n 
C 2 248  PHE 248  248  ?    ?   ?   C . n 
C 2 249  GLN 249  249  ?    ?   ?   C . n 
C 2 250  GLY 250  250  ?    ?   ?   C . n 
C 2 251  HIS 251  251  ?    ?   ?   C . n 
C 2 252  HIS 252  252  ?    ?   ?   C . n 
C 2 253  HIS 253  253  ?    ?   ?   C . n 
C 2 254  HIS 254  254  ?    ?   ?   C . n 
C 2 255  HIS 255  255  ?    ?   ?   C . n 
C 2 256  HIS 256  256  ?    ?   ?   C . n 
D 2 1    MET 1    1    ?    ?   ?   D . n 
D 2 2    GLU 2    2    ?    ?   ?   D . n 
D 2 3    LYS 3    3    ?    ?   ?   D . n 
D 2 4    PHE 4    4    ?    ?   ?   D . n 
D 2 5    ALA 5    5    ?    ?   ?   D . n 
D 2 6    PRO 6    6    ?    ?   ?   D . n 
D 2 7    GLU 7    7    ?    ?   ?   D . n 
D 2 8    PHE 8    8    ?    ?   ?   D . n 
D 2 9    HIS 9    9    ?    ?   ?   D . n 
D 2 10   GLY 10   10   ?    ?   ?   D . n 
D 2 11   GLU 11   11   ?    ?   ?   D . n 
D 2 12   ASP 12   12   ?    ?   ?   D . n 
D 2 13   ALA 13   13   ?    ?   ?   D . n 
D 2 14   ASN 14   14   ?    ?   ?   D . n 
D 2 15   ASN 15   15   ?    ?   ?   D . n 
D 2 16   ARG 16   16   ?    ?   ?   D . n 
D 2 17   ALA 17   17   ?    ?   ?   D . n 
D 2 18   THR 18   18   ?    ?   ?   D . n 
D 2 19   LYS 19   19   ?    ?   ?   D . n 
D 2 20   PHE 20   20   ?    ?   ?   D . n 
D 2 21   LEU 21   21   ?    ?   ?   D . n 
D 2 22   GLU 22   22   ?    ?   ?   D . n 
D 2 23   SER 23   23   ?    ?   ?   D . n 
D 2 24   ILE 24   24   ?    ?   ?   D . n 
D 2 25   LYS 25   25   ?    ?   ?   D . n 
D 2 26   GLY 26   26   ?    ?   ?   D . n 
D 2 27   LYS 27   27   ?    ?   ?   D . n 
D 2 28   PHE 28   28   ?    ?   ?   D . n 
D 2 29   THR 29   29   ?    ?   ?   D . n 
D 2 30   SER 30   30   ?    ?   ?   D . n 
D 2 31   PRO 31   31   ?    ?   ?   D . n 
D 2 32   LYS 32   32   ?    ?   ?   D . n 
D 2 33   ASP 33   33   ?    ?   ?   D . n 
D 2 34   PRO 34   34   ?    ?   ?   D . n 
D 2 35   LYS 35   35   ?    ?   ?   D . n 
D 2 36   LYS 36   36   ?    ?   ?   D . n 
D 2 37   LYS 37   37   ?    ?   ?   D . n 
D 2 38   ASP 38   38   ?    ?   ?   D . n 
D 2 39   SER 39   39   ?    ?   ?   D . n 
D 2 40   ILE 40   40   ?    ?   ?   D . n 
D 2 41   ILE 41   41   ?    ?   ?   D . n 
D 2 42   SER 42   42   ?    ?   ?   D . n 
D 2 43   VAL 43   43   ?    ?   ?   D . n 
D 2 44   ASN 44   44   ?    ?   ?   D . n 
D 2 45   SER 45   45   ?    ?   ?   D . n 
D 2 46   ILE 46   46   ?    ?   ?   D . n 
D 2 47   ASP 47   47   ?    ?   ?   D . n 
D 2 48   ILE 48   48   ?    ?   ?   D . n 
D 2 49   GLU 49   49   ?    ?   ?   D . n 
D 2 50   VAL 50   50   ?    ?   ?   D . n 
D 2 51   THR 51   51   ?    ?   ?   D . n 
D 2 52   LYS 52   52   ?    ?   ?   D . n 
D 2 53   GLU 53   53   ?    ?   ?   D . n 
D 2 54   SER 54   54   ?    ?   ?   D . n 
D 2 55   PRO 55   55   ?    ?   ?   D . n 
D 2 56   ILE 56   56   ?    ?   ?   D . n 
D 2 57   THR 57   57   ?    ?   ?   D . n 
D 2 58   SER 58   58   ?    ?   ?   D . n 
D 2 59   ASN 59   59   ?    ?   ?   D . n 
D 2 60   SER 60   60   ?    ?   ?   D . n 
D 2 61   THR 61   61   ?    ?   ?   D . n 
D 2 62   ILE 62   62   ?    ?   ?   D . n 
D 2 63   ILE 63   63   ?    ?   ?   D . n 
D 2 64   ASN 64   64   ?    ?   ?   D . n 
D 2 65   PRO 65   65   ?    ?   ?   D . n 
D 2 66   THR 66   66   ?    ?   ?   D . n 
D 2 67   ASN 67   67   ?    ?   ?   D . n 
D 2 68   GLU 68   68   ?    ?   ?   D . n 
D 2 69   THR 69   69   ?    ?   ?   D . n 
D 2 70   ASP 70   70   ?    ?   ?   D . n 
D 2 71   ASP 71   71   ?    ?   ?   D . n 
D 2 72   THR 72   72   ?    ?   ?   D . n 
D 2 73   ALA 73   73   ?    ?   ?   D . n 
D 2 74   GLY 74   74   ?    ?   ?   D . n 
D 2 75   ASN 75   75   ?    ?   ?   D . n 
D 2 76   LYS 76   76   ?    ?   ?   D . n 
D 2 77   PRO 77   77   ?    ?   ?   D . n 
D 2 78   ASN 78   78   ?    ?   ?   D . n 
D 2 79   TYR 79   79   ?    ?   ?   D . n 
D 2 80   GLN 80   80   ?    ?   ?   D . n 
D 2 81   ARG 81   81   ?    ?   ?   D . n 
D 2 82   LYS 82   82   ?    ?   ?   D . n 
D 2 83   PRO 83   83   ?    ?   ?   D . n 
D 2 84   LEU 84   84   ?    ?   ?   D . n 
D 2 85   VAL 85   85   ?    ?   ?   D . n 
D 2 86   SER 86   86   ?    ?   ?   D . n 
D 2 87   PHE 87   87   ?    ?   ?   D . n 
D 2 88   LYS 88   88   ?    ?   ?   D . n 
D 2 89   GLU 89   89   ?    ?   ?   D . n 
D 2 90   ASP 90   90   ?    ?   ?   D . n 
D 2 91   PRO 91   91   ?    ?   ?   D . n 
D 2 92   THR 92   92   ?    ?   ?   D . n 
D 2 93   PRO 93   93   ?    ?   ?   D . n 
D 2 94   SER 94   94   ?    ?   ?   D . n 
D 2 95   ASP 95   95   ?    ?   ?   D . n 
D 2 96   ASN 96   96   ?    ?   ?   D . n 
D 2 97   PRO 97   97   ?    ?   ?   D . n 
D 2 98   PHE 98   98   ?    ?   ?   D . n 
D 2 99   SER 99   99   ?    ?   ?   D . n 
D 2 100  LYS 100  100  ?    ?   ?   D . n 
D 2 101  LEU 101  101  ?    ?   ?   D . n 
D 2 102  TYR 102  102  ?    ?   ?   D . n 
D 2 103  LYS 103  103  ?    ?   ?   D . n 
D 2 104  GLU 104  104  ?    ?   ?   D . n 
D 2 105  THR 105  105  ?    ?   ?   D . n 
D 2 106  ILE 106  106  ?    ?   ?   D . n 
D 2 107  GLU 107  107  ?    ?   ?   D . n 
D 2 108  THR 108  108  ?    ?   ?   D . n 
D 2 109  PHE 109  109  ?    ?   ?   D . n 
D 2 110  ASP 110  110  ?    ?   ?   D . n 
D 2 111  ASN 111  111  ?    ?   ?   D . n 
D 2 112  ASN 112  112  ?    ?   ?   D . n 
D 2 113  GLU 113  113  ?    ?   ?   D . n 
D 2 114  GLU 114  114  ?    ?   ?   D . n 
D 2 115  GLU 115  115  ?    ?   ?   D . n 
D 2 116  SER 116  116  ?    ?   ?   D . n 
D 2 117  SER 117  117  ?    ?   ?   D . n 
D 2 118  TYR 118  118  ?    ?   ?   D . n 
D 2 119  SER 119  119  ?    ?   ?   D . n 
D 2 120  TYR 120  120  ?    ?   ?   D . n 
D 2 121  GLU 121  121  ?    ?   ?   D . n 
D 2 122  GLU 122  122  ?    ?   ?   D . n 
D 2 123  ILE 123  123  ?    ?   ?   D . n 
D 2 124  ASN 124  124  ?    ?   ?   D . n 
D 2 125  ASP 125  125  ?    ?   ?   D . n 
D 2 126  GLN 126  126  ?    ?   ?   D . n 
D 2 127  THR 127  127  ?    ?   ?   D . n 
D 2 128  ASN 128  128  ?    ?   ?   D . n 
D 2 129  ASP 129  129  ?    ?   ?   D . n 
D 2 130  ASN 130  130  130  ASN ASN D . n 
D 2 131  ILE 131  131  131  ILE ILE D . n 
D 2 132  THR 132  132  132  THR THR D . n 
D 2 133  ALA 133  133  133  ALA ALA D . n 
D 2 134  ARG 134  134  134  ARG ARG D . n 
D 2 135  LEU 135  135  135  LEU LEU D . n 
D 2 136  ASP 136  136  136  ASP ASP D . n 
D 2 137  ARG 137  137  137  ARG ARG D . n 
D 2 138  ILE 138  138  138  ILE ILE D . n 
D 2 139  ASP 139  139  139  ASP ASP D . n 
D 2 140  GLU 140  140  140  GLU GLU D . n 
D 2 141  LYS 141  141  141  LYS LYS D . n 
D 2 142  LEU 142  142  142  LEU LEU D . n 
D 2 143  SER 143  143  143  SER SER D . n 
D 2 144  GLU 144  144  144  GLU GLU D . n 
D 2 145  ILE 145  145  145  ILE ILE D . n 
D 2 146  LEU 146  146  146  LEU LEU D . n 
D 2 147  GLY 147  147  147  GLY GLY D . n 
D 2 148  MET 148  148  148  MET MET D . n 
D 2 149  LEU 149  149  149  LEU LEU D . n 
D 2 150  HIS 150  150  150  HIS HIS D . n 
D 2 151  THR 151  151  151  THR THR D . n 
D 2 152  LEU 152  152  152  LEU LEU D . n 
D 2 153  VAL 153  153  153  VAL VAL D . n 
D 2 154  VAL 154  154  154  VAL VAL D . n 
D 2 155  ALA 155  155  155  ALA ALA D . n 
D 2 156  SER 156  156  156  SER SER D . n 
D 2 157  ALA 157  157  157  ALA ALA D . n 
D 2 158  GLY 158  158  158  GLY GLY D . n 
D 2 159  PRO 159  159  159  PRO PRO D . n 
D 2 160  THR 160  160  160  THR THR D . n 
D 2 161  SER 161  161  161  SER SER D . n 
D 2 162  ALA 162  162  162  ALA ALA D . n 
D 2 163  ARG 163  163  163  ARG ARG D . n 
D 2 164  ASP 164  164  164  ASP ASP D . n 
D 2 165  GLY 165  165  165  GLY GLY D . n 
D 2 166  ILE 166  166  166  ILE ILE D . n 
D 2 167  ARG 167  167  167  ARG ARG D . n 
D 2 168  ASP 168  168  168  ASP ASP D . n 
D 2 169  ALA 169  169  169  ALA ALA D . n 
D 2 170  MET 170  170  170  MET MET D . n 
D 2 171  ILE 171  171  171  ILE ILE D . n 
D 2 172  GLY 172  172  172  GLY GLY D . n 
D 2 173  LEU 173  173  173  LEU LEU D . n 
D 2 174  ARG 174  174  174  ARG ARG D . n 
D 2 175  GLU 175  175  175  GLU GLU D . n 
D 2 176  GLU 176  176  176  GLU GLU D . n 
D 2 177  MET 177  177  177  MET MET D . n 
D 2 178  ILE 178  178  178  ILE ILE D . n 
D 2 179  GLU 179  179  179  GLU GLU D . n 
D 2 180  LYS 180  180  180  LYS LYS D . n 
D 2 181  ILE 181  181  181  ILE ILE D . n 
D 2 182  ARG 182  182  182  ARG ARG D . n 
D 2 183  THR 183  183  183  THR THR D . n 
D 2 184  GLU 184  184  184  GLU GLU D . n 
D 2 185  ALA 185  185  ?    ?   ?   D . n 
D 2 186  LEU 186  186  ?    ?   ?   D . n 
D 2 187  MET 187  187  ?    ?   ?   D . n 
D 2 188  THR 188  188  ?    ?   ?   D . n 
D 2 189  ASN 189  189  ?    ?   ?   D . n 
D 2 190  ASP 190  190  ?    ?   ?   D . n 
D 2 191  ARG 191  191  ?    ?   ?   D . n 
D 2 192  LEU 192  192  ?    ?   ?   D . n 
D 2 193  GLU 193  193  ?    ?   ?   D . n 
D 2 194  ALA 194  194  ?    ?   ?   D . n 
D 2 195  MET 195  195  ?    ?   ?   D . n 
D 2 196  ALA 196  196  ?    ?   ?   D . n 
D 2 197  ARG 197  197  ?    ?   ?   D . n 
D 2 198  LEU 198  198  ?    ?   ?   D . n 
D 2 199  ARG 199  199  ?    ?   ?   D . n 
D 2 200  ASN 200  200  ?    ?   ?   D . n 
D 2 201  GLU 201  201  ?    ?   ?   D . n 
D 2 202  GLU 202  202  ?    ?   ?   D . n 
D 2 203  SER 203  203  ?    ?   ?   D . n 
D 2 204  GLU 204  204  ?    ?   ?   D . n 
D 2 205  LYS 205  205  ?    ?   ?   D . n 
D 2 206  MET 206  206  ?    ?   ?   D . n 
D 2 207  ALA 207  207  ?    ?   ?   D . n 
D 2 208  LYS 208  208  ?    ?   ?   D . n 
D 2 209  ASP 209  209  ?    ?   ?   D . n 
D 2 210  THR 210  210  ?    ?   ?   D . n 
D 2 211  SER 211  211  ?    ?   ?   D . n 
D 2 212  ASP 212  212  ?    ?   ?   D . n 
D 2 213  GLU 213  213  ?    ?   ?   D . n 
D 2 214  VAL 214  214  ?    ?   ?   D . n 
D 2 215  SER 215  215  ?    ?   ?   D . n 
D 2 216  LEU 216  216  ?    ?   ?   D . n 
D 2 217  ASN 217  217  ?    ?   ?   D . n 
D 2 218  PRO 218  218  ?    ?   ?   D . n 
D 2 219  THR 219  219  ?    ?   ?   D . n 
D 2 220  SER 220  220  ?    ?   ?   D . n 
D 2 221  GLU 221  221  ?    ?   ?   D . n 
D 2 222  LYS 222  222  ?    ?   ?   D . n 
D 2 223  LEU 223  223  ?    ?   ?   D . n 
D 2 224  ASN 224  224  ?    ?   ?   D . n 
D 2 225  ASN 225  225  ?    ?   ?   D . n 
D 2 226  LEU 226  226  ?    ?   ?   D . n 
D 2 227  LEU 227  227  ?    ?   ?   D . n 
D 2 228  GLU 228  228  ?    ?   ?   D . n 
D 2 229  GLY 229  229  ?    ?   ?   D . n 
D 2 230  ASN 230  230  ?    ?   ?   D . n 
D 2 231  ASP 231  231  ?    ?   ?   D . n 
D 2 232  SER 232  232  ?    ?   ?   D . n 
D 2 233  ASP 233  233  ?    ?   ?   D . n 
D 2 234  ASN 234  234  ?    ?   ?   D . n 
D 2 235  ASP 235  235  ?    ?   ?   D . n 
D 2 236  LEU 236  236  ?    ?   ?   D . n 
D 2 237  SER 237  237  ?    ?   ?   D . n 
D 2 238  LEU 238  238  ?    ?   ?   D . n 
D 2 239  GLU 239  239  ?    ?   ?   D . n 
D 2 240  ASP 240  240  ?    ?   ?   D . n 
D 2 241  PHE 241  241  ?    ?   ?   D . n 
D 2 242  LYS 242  242  ?    ?   ?   D . n 
D 2 243  GLY 243  243  ?    ?   ?   D . n 
D 2 244  GLU 244  244  ?    ?   ?   D . n 
D 2 245  ASN 245  245  ?    ?   ?   D . n 
D 2 246  LYS 246  246  ?    ?   ?   D . n 
D 2 247  TYR 247  247  ?    ?   ?   D . n 
D 2 248  PHE 248  248  ?    ?   ?   D . n 
D 2 249  GLN 249  249  ?    ?   ?   D . n 
D 2 250  GLY 250  250  ?    ?   ?   D . n 
D 2 251  HIS 251  251  ?    ?   ?   D . n 
D 2 252  HIS 252  252  ?    ?   ?   D . n 
D 2 253  HIS 253  253  ?    ?   ?   D . n 
D 2 254  HIS 254  254  ?    ?   ?   D . n 
D 2 255  HIS 255  255  ?    ?   ?   D . n 
D 2 256  HIS 256  256  ?    ?   ?   D . n 
E 2 1    MET 1    1    ?    ?   ?   E . n 
E 2 2    GLU 2    2    ?    ?   ?   E . n 
E 2 3    LYS 3    3    ?    ?   ?   E . n 
E 2 4    PHE 4    4    ?    ?   ?   E . n 
E 2 5    ALA 5    5    ?    ?   ?   E . n 
E 2 6    PRO 6    6    ?    ?   ?   E . n 
E 2 7    GLU 7    7    ?    ?   ?   E . n 
E 2 8    PHE 8    8    ?    ?   ?   E . n 
E 2 9    HIS 9    9    ?    ?   ?   E . n 
E 2 10   GLY 10   10   ?    ?   ?   E . n 
E 2 11   GLU 11   11   ?    ?   ?   E . n 
E 2 12   ASP 12   12   ?    ?   ?   E . n 
E 2 13   ALA 13   13   ?    ?   ?   E . n 
E 2 14   ASN 14   14   ?    ?   ?   E . n 
E 2 15   ASN 15   15   ?    ?   ?   E . n 
E 2 16   ARG 16   16   ?    ?   ?   E . n 
E 2 17   ALA 17   17   ?    ?   ?   E . n 
E 2 18   THR 18   18   ?    ?   ?   E . n 
E 2 19   LYS 19   19   ?    ?   ?   E . n 
E 2 20   PHE 20   20   ?    ?   ?   E . n 
E 2 21   LEU 21   21   ?    ?   ?   E . n 
E 2 22   GLU 22   22   ?    ?   ?   E . n 
E 2 23   SER 23   23   ?    ?   ?   E . n 
E 2 24   ILE 24   24   ?    ?   ?   E . n 
E 2 25   LYS 25   25   ?    ?   ?   E . n 
E 2 26   GLY 26   26   ?    ?   ?   E . n 
E 2 27   LYS 27   27   ?    ?   ?   E . n 
E 2 28   PHE 28   28   ?    ?   ?   E . n 
E 2 29   THR 29   29   ?    ?   ?   E . n 
E 2 30   SER 30   30   ?    ?   ?   E . n 
E 2 31   PRO 31   31   ?    ?   ?   E . n 
E 2 32   LYS 32   32   ?    ?   ?   E . n 
E 2 33   ASP 33   33   ?    ?   ?   E . n 
E 2 34   PRO 34   34   ?    ?   ?   E . n 
E 2 35   LYS 35   35   ?    ?   ?   E . n 
E 2 36   LYS 36   36   ?    ?   ?   E . n 
E 2 37   LYS 37   37   ?    ?   ?   E . n 
E 2 38   ASP 38   38   ?    ?   ?   E . n 
E 2 39   SER 39   39   ?    ?   ?   E . n 
E 2 40   ILE 40   40   ?    ?   ?   E . n 
E 2 41   ILE 41   41   ?    ?   ?   E . n 
E 2 42   SER 42   42   ?    ?   ?   E . n 
E 2 43   VAL 43   43   ?    ?   ?   E . n 
E 2 44   ASN 44   44   ?    ?   ?   E . n 
E 2 45   SER 45   45   ?    ?   ?   E . n 
E 2 46   ILE 46   46   ?    ?   ?   E . n 
E 2 47   ASP 47   47   ?    ?   ?   E . n 
E 2 48   ILE 48   48   ?    ?   ?   E . n 
E 2 49   GLU 49   49   ?    ?   ?   E . n 
E 2 50   VAL 50   50   ?    ?   ?   E . n 
E 2 51   THR 51   51   ?    ?   ?   E . n 
E 2 52   LYS 52   52   ?    ?   ?   E . n 
E 2 53   GLU 53   53   ?    ?   ?   E . n 
E 2 54   SER 54   54   ?    ?   ?   E . n 
E 2 55   PRO 55   55   ?    ?   ?   E . n 
E 2 56   ILE 56   56   ?    ?   ?   E . n 
E 2 57   THR 57   57   ?    ?   ?   E . n 
E 2 58   SER 58   58   ?    ?   ?   E . n 
E 2 59   ASN 59   59   ?    ?   ?   E . n 
E 2 60   SER 60   60   ?    ?   ?   E . n 
E 2 61   THR 61   61   ?    ?   ?   E . n 
E 2 62   ILE 62   62   ?    ?   ?   E . n 
E 2 63   ILE 63   63   ?    ?   ?   E . n 
E 2 64   ASN 64   64   ?    ?   ?   E . n 
E 2 65   PRO 65   65   ?    ?   ?   E . n 
E 2 66   THR 66   66   ?    ?   ?   E . n 
E 2 67   ASN 67   67   ?    ?   ?   E . n 
E 2 68   GLU 68   68   ?    ?   ?   E . n 
E 2 69   THR 69   69   ?    ?   ?   E . n 
E 2 70   ASP 70   70   ?    ?   ?   E . n 
E 2 71   ASP 71   71   ?    ?   ?   E . n 
E 2 72   THR 72   72   ?    ?   ?   E . n 
E 2 73   ALA 73   73   ?    ?   ?   E . n 
E 2 74   GLY 74   74   ?    ?   ?   E . n 
E 2 75   ASN 75   75   ?    ?   ?   E . n 
E 2 76   LYS 76   76   ?    ?   ?   E . n 
E 2 77   PRO 77   77   ?    ?   ?   E . n 
E 2 78   ASN 78   78   ?    ?   ?   E . n 
E 2 79   TYR 79   79   ?    ?   ?   E . n 
E 2 80   GLN 80   80   ?    ?   ?   E . n 
E 2 81   ARG 81   81   ?    ?   ?   E . n 
E 2 82   LYS 82   82   ?    ?   ?   E . n 
E 2 83   PRO 83   83   ?    ?   ?   E . n 
E 2 84   LEU 84   84   ?    ?   ?   E . n 
E 2 85   VAL 85   85   ?    ?   ?   E . n 
E 2 86   SER 86   86   ?    ?   ?   E . n 
E 2 87   PHE 87   87   ?    ?   ?   E . n 
E 2 88   LYS 88   88   ?    ?   ?   E . n 
E 2 89   GLU 89   89   ?    ?   ?   E . n 
E 2 90   ASP 90   90   ?    ?   ?   E . n 
E 2 91   PRO 91   91   ?    ?   ?   E . n 
E 2 92   THR 92   92   ?    ?   ?   E . n 
E 2 93   PRO 93   93   ?    ?   ?   E . n 
E 2 94   SER 94   94   ?    ?   ?   E . n 
E 2 95   ASP 95   95   ?    ?   ?   E . n 
E 2 96   ASN 96   96   ?    ?   ?   E . n 
E 2 97   PRO 97   97   ?    ?   ?   E . n 
E 2 98   PHE 98   98   ?    ?   ?   E . n 
E 2 99   SER 99   99   ?    ?   ?   E . n 
E 2 100  LYS 100  100  ?    ?   ?   E . n 
E 2 101  LEU 101  101  ?    ?   ?   E . n 
E 2 102  TYR 102  102  ?    ?   ?   E . n 
E 2 103  LYS 103  103  ?    ?   ?   E . n 
E 2 104  GLU 104  104  ?    ?   ?   E . n 
E 2 105  THR 105  105  ?    ?   ?   E . n 
E 2 106  ILE 106  106  ?    ?   ?   E . n 
E 2 107  GLU 107  107  ?    ?   ?   E . n 
E 2 108  THR 108  108  ?    ?   ?   E . n 
E 2 109  PHE 109  109  ?    ?   ?   E . n 
E 2 110  ASP 110  110  ?    ?   ?   E . n 
E 2 111  ASN 111  111  ?    ?   ?   E . n 
E 2 112  ASN 112  112  ?    ?   ?   E . n 
E 2 113  GLU 113  113  ?    ?   ?   E . n 
E 2 114  GLU 114  114  ?    ?   ?   E . n 
E 2 115  GLU 115  115  ?    ?   ?   E . n 
E 2 116  SER 116  116  ?    ?   ?   E . n 
E 2 117  SER 117  117  ?    ?   ?   E . n 
E 2 118  TYR 118  118  ?    ?   ?   E . n 
E 2 119  SER 119  119  ?    ?   ?   E . n 
E 2 120  TYR 120  120  ?    ?   ?   E . n 
E 2 121  GLU 121  121  ?    ?   ?   E . n 
E 2 122  GLU 122  122  ?    ?   ?   E . n 
E 2 123  ILE 123  123  ?    ?   ?   E . n 
E 2 124  ASN 124  124  ?    ?   ?   E . n 
E 2 125  ASP 125  125  ?    ?   ?   E . n 
E 2 126  GLN 126  126  ?    ?   ?   E . n 
E 2 127  THR 127  127  ?    ?   ?   E . n 
E 2 128  ASN 128  128  ?    ?   ?   E . n 
E 2 129  ASP 129  129  ?    ?   ?   E . n 
E 2 130  ASN 130  130  ?    ?   ?   E . n 
E 2 131  ILE 131  131  131  ILE ILE E . n 
E 2 132  THR 132  132  132  THR THR E . n 
E 2 133  ALA 133  133  133  ALA ALA E . n 
E 2 134  ARG 134  134  134  ARG ARG E . n 
E 2 135  LEU 135  135  135  LEU LEU E . n 
E 2 136  ASP 136  136  136  ASP ASP E . n 
E 2 137  ARG 137  137  137  ARG ARG E . n 
E 2 138  ILE 138  138  138  ILE ILE E . n 
E 2 139  ASP 139  139  139  ASP ASP E . n 
E 2 140  GLU 140  140  140  GLU GLU E . n 
E 2 141  LYS 141  141  141  LYS LYS E . n 
E 2 142  LEU 142  142  142  LEU LEU E . n 
E 2 143  SER 143  143  143  SER SER E . n 
E 2 144  GLU 144  144  144  GLU GLU E . n 
E 2 145  ILE 145  145  145  ILE ILE E . n 
E 2 146  LEU 146  146  146  LEU LEU E . n 
E 2 147  GLY 147  147  147  GLY GLY E . n 
E 2 148  MET 148  148  148  MET MET E . n 
E 2 149  LEU 149  149  149  LEU LEU E . n 
E 2 150  HIS 150  150  150  HIS HIS E . n 
E 2 151  THR 151  151  151  THR THR E . n 
E 2 152  LEU 152  152  152  LEU LEU E . n 
E 2 153  VAL 153  153  153  VAL VAL E . n 
E 2 154  VAL 154  154  154  VAL VAL E . n 
E 2 155  ALA 155  155  155  ALA ALA E . n 
E 2 156  SER 156  156  156  SER SER E . n 
E 2 157  ALA 157  157  157  ALA ALA E . n 
E 2 158  GLY 158  158  158  GLY GLY E . n 
E 2 159  PRO 159  159  159  PRO PRO E . n 
E 2 160  THR 160  160  160  THR THR E . n 
E 2 161  SER 161  161  161  SER SER E . n 
E 2 162  ALA 162  162  162  ALA ALA E . n 
E 2 163  ARG 163  163  163  ARG ARG E . n 
E 2 164  ASP 164  164  164  ASP ASP E . n 
E 2 165  GLY 165  165  165  GLY GLY E . n 
E 2 166  ILE 166  166  166  ILE ILE E . n 
E 2 167  ARG 167  167  167  ARG ARG E . n 
E 2 168  ASP 168  168  168  ASP ASP E . n 
E 2 169  ALA 169  169  169  ALA ALA E . n 
E 2 170  MET 170  170  170  MET MET E . n 
E 2 171  ILE 171  171  171  ILE ILE E . n 
E 2 172  GLY 172  172  172  GLY GLY E . n 
E 2 173  LEU 173  173  173  LEU LEU E . n 
E 2 174  ARG 174  174  174  ARG ARG E . n 
E 2 175  GLU 175  175  175  GLU GLU E . n 
E 2 176  GLU 176  176  176  GLU GLU E . n 
E 2 177  MET 177  177  177  MET MET E . n 
E 2 178  ILE 178  178  178  ILE ILE E . n 
E 2 179  GLU 179  179  179  GLU GLU E . n 
E 2 180  LYS 180  180  180  LYS LYS E . n 
E 2 181  ILE 181  181  181  ILE ILE E . n 
E 2 182  ARG 182  182  182  ARG ARG E . n 
E 2 183  THR 183  183  183  THR THR E . n 
E 2 184  GLU 184  184  184  GLU GLU E . n 
E 2 185  ALA 185  185  185  ALA ALA E . n 
E 2 186  LEU 186  186  186  LEU LEU E . n 
E 2 187  MET 187  187  187  MET MET E . n 
E 2 188  THR 188  188  188  THR THR E . n 
E 2 189  ASN 189  189  189  ASN ASN E . n 
E 2 190  ASP 190  190  190  ASP ASP E . n 
E 2 191  ARG 191  191  191  ARG ARG E . n 
E 2 192  LEU 192  192  192  LEU LEU E . n 
E 2 193  GLU 193  193  193  GLU GLU E . n 
E 2 194  ALA 194  194  194  ALA ALA E . n 
E 2 195  MET 195  195  195  MET MET E . n 
E 2 196  ALA 196  196  196  ALA ALA E . n 
E 2 197  ARG 197  197  197  ARG ARG E . n 
E 2 198  LEU 198  198  198  LEU LEU E . n 
E 2 199  ARG 199  199  199  ARG ARG E . n 
E 2 200  ASN 200  200  ?    ?   ?   E . n 
E 2 201  GLU 201  201  ?    ?   ?   E . n 
E 2 202  GLU 202  202  ?    ?   ?   E . n 
E 2 203  SER 203  203  ?    ?   ?   E . n 
E 2 204  GLU 204  204  ?    ?   ?   E . n 
E 2 205  LYS 205  205  ?    ?   ?   E . n 
E 2 206  MET 206  206  ?    ?   ?   E . n 
E 2 207  ALA 207  207  ?    ?   ?   E . n 
E 2 208  LYS 208  208  ?    ?   ?   E . n 
E 2 209  ASP 209  209  ?    ?   ?   E . n 
E 2 210  THR 210  210  ?    ?   ?   E . n 
E 2 211  SER 211  211  ?    ?   ?   E . n 
E 2 212  ASP 212  212  ?    ?   ?   E . n 
E 2 213  GLU 213  213  ?    ?   ?   E . n 
E 2 214  VAL 214  214  ?    ?   ?   E . n 
E 2 215  SER 215  215  ?    ?   ?   E . n 
E 2 216  LEU 216  216  ?    ?   ?   E . n 
E 2 217  ASN 217  217  ?    ?   ?   E . n 
E 2 218  PRO 218  218  ?    ?   ?   E . n 
E 2 219  THR 219  219  ?    ?   ?   E . n 
E 2 220  SER 220  220  ?    ?   ?   E . n 
E 2 221  GLU 221  221  ?    ?   ?   E . n 
E 2 222  LYS 222  222  ?    ?   ?   E . n 
E 2 223  LEU 223  223  ?    ?   ?   E . n 
E 2 224  ASN 224  224  ?    ?   ?   E . n 
E 2 225  ASN 225  225  ?    ?   ?   E . n 
E 2 226  LEU 226  226  ?    ?   ?   E . n 
E 2 227  LEU 227  227  ?    ?   ?   E . n 
E 2 228  GLU 228  228  ?    ?   ?   E . n 
E 2 229  GLY 229  229  ?    ?   ?   E . n 
E 2 230  ASN 230  230  ?    ?   ?   E . n 
E 2 231  ASP 231  231  ?    ?   ?   E . n 
E 2 232  SER 232  232  ?    ?   ?   E . n 
E 2 233  ASP 233  233  ?    ?   ?   E . n 
E 2 234  ASN 234  234  ?    ?   ?   E . n 
E 2 235  ASP 235  235  ?    ?   ?   E . n 
E 2 236  LEU 236  236  ?    ?   ?   E . n 
E 2 237  SER 237  237  ?    ?   ?   E . n 
E 2 238  LEU 238  238  ?    ?   ?   E . n 
E 2 239  GLU 239  239  ?    ?   ?   E . n 
E 2 240  ASP 240  240  ?    ?   ?   E . n 
E 2 241  PHE 241  241  ?    ?   ?   E . n 
E 2 242  LYS 242  242  ?    ?   ?   E . n 
E 2 243  GLY 243  243  ?    ?   ?   E . n 
E 2 244  GLU 244  244  ?    ?   ?   E . n 
E 2 245  ASN 245  245  ?    ?   ?   E . n 
E 2 246  LYS 246  246  ?    ?   ?   E . n 
E 2 247  TYR 247  247  ?    ?   ?   E . n 
E 2 248  PHE 248  248  ?    ?   ?   E . n 
E 2 249  GLN 249  249  ?    ?   ?   E . n 
E 2 250  GLY 250  250  ?    ?   ?   E . n 
E 2 251  HIS 251  251  ?    ?   ?   E . n 
E 2 252  HIS 252  252  ?    ?   ?   E . n 
E 2 253  HIS 253  253  ?    ?   ?   E . n 
E 2 254  HIS 254  254  ?    ?   ?   E . n 
E 2 255  HIS 255  255  ?    ?   ?   E . n 
E 2 256  HIS 256  256  ?    ?   ?   E . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AWZ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AWZ 
_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          A1AWZ 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     2201 
_pdbx_nonpoly_scheme.auth_seq_num    1501 
_pdbx_nonpoly_scheme.pdb_mon_id      A1AWZ 
_pdbx_nonpoly_scheme.auth_mon_id     LIG 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A CYS 1184 ? SG  ? A CYS 1220 SG  
2 1 Y 1 A GLU 1190 ? CG  ? A GLU 1226 CG  
3 1 Y 1 A GLU 1190 ? CD  ? A GLU 1226 CD  
4 1 Y 1 A GLU 1190 ? OE1 ? A GLU 1226 OE1 
5 1 Y 1 A GLU 1190 ? OE2 ? A GLU 1226 OE2 
# 
_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                     9C7Y 
_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                         9C7Y 
_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                   9C7Y 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9C7Y 
_struct.title                        'Structure Of Respiratory Syncytial Virus Polymerase in complex with JNJ-2729' 
_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        9C7Y 
_struct_keywords.text            'Non-Nucleoside Inhibitor, complex, Polymerase, RSV, VIRAL PROTEIN, TRANSFERASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN,TRANSFERASE/INHIBITOR' 
# 
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_HRSVA     P28887 ? 1 
;MDPIINGNSANVYLTDSYLKGVISFSECNALGSYIFNGPYLKNDYTNLISRQNPLIEHMNLKKLNITQSLISKYHKGEIK
LEEPTYFQSLLMTYKSMTSSEQIATTNLLKKIIRRAIEISDVKVYAILNKLGLKEKDKIKSNNGQDEDNSVITTIIKDDI
LSAVKDNQSHLKADKNHSTKQKDTIKTTLLKKLMCSMQHPPSWLIHWFNLYTKLNNILTQYRSNEVKNHGFTLIDNQTLS
GFQFILNQYGCIVYHKELKRITVTTYNQFLTWKDISLSRLNVCLITWISNCLNTLNKSLGLRCGFNNVILTQLFLYGDCI
LKLFHNEGFYIIKEVEGFIMSLILNITEEDQFRKRFYNSMLNNITDAANKAQKNLLSRVCHTLLDKTVSDNIINGRWIIL
LSKFLKLIKLAGDNNLNNLSELYFLFRIFGHPMVDERQAMDAVKINCNETKFYLLSSLSMLRGAFIYRIIKGFVNNYNRW
PTLRNAIVLPLRWLTYYKLNTYPSLLELTERDLIVLSGLRFYREFRLPKKVDLEMIINDKAISPPKNLIWTSFPRNYMPS
HIQNYIEHEKLKFSESDKSRRVLEYYLRDNKFNECDLYNCVVNQSYLNNPNHVVSLTGKERELSVGRMFAMQPGMFRQVQ
ILAEKMIAENILQFFPESLTRYGDLELQKILELKAGISNKSNRYNDNYNNYISKCSIITDLSKFNQAFRYETSCICSDVL
DELHGVQSLFSWLHLTIPHVTIICTYRHAPPYIGDHIVDLNNVDEQSGLYRYHMGGIEGWCQKLWTIEAISLLDLISLKG
KFSITALINGDNQSIDISKPIRLMEGQTHAQADYLLALNSLKLLYKEYAGIGHKLKGTETYISRDMQFMSKTIQHNGVYY
PASIKKVLRVGPWINTILDDFKVSLESIGSLTQELEYRGESLLCSLIFRNVWLYNQIALQLKNHALCNNKLYLDILKVLK
HLKTFFNLDNIDTALTLYMNLPMLFGGGDPNLLYRSFYRRTPDFLTEAIVHSVFILSYYTNHDLKDKLQDLSDDRLNKFL
TCIITFDKNPNAEFVTLMRDPQALGSERQAKITSEINRLAVTEVLSTAPNKIFSKSAQHYTTTEIDLNDIMQNIEPTYPH
GLRVVYESLPFYKAEKIVNLISGTKSITNILEKTSAIDLTDIDRATEMMRKNITLLIRILPLDCNRDKREILSMENLSIT
ELSKYVRERSWSLSNIVGVTSPSIMYTMDIKYTTSTISSGIIIEKYNVNSLTRGERGPTKPWVGSSTQEKKTMPVYNRQV
LTKKQRDQIDLLAKLDWVYASIDNKDEFMEELSIGTLGLTYEKAKKLFPQYLSVNYLHRLTVSSRPCEFPASIPAYRTTN
YHFDTSPINRILTEKYGDEDIDIVFQNCISFGLSLMSVVEQFTNVCPNRIILIPKLNEIHLMKPPIFTGDVDIHKLKQVI
QKQHMFLPDKISLTQYVELFLSNKTLKSGSHVNSNLILAHKISDYFHNTYILSTNLAGHWILIIQLMKDSKGIFEKDWGE
GYITDHMFINLKVFFNAYKTYLLCFHKGYGKAKLECDMNTSDLLCVLELIDSSYWKSMSKVFLEQKVIKYILSQDASLHR
VKGCHSFKLWFLKRLNVAEFTVCPWVVNIDYHPTHMKAILTYIDLVRMGLINIDRIHIKNKHKFNDEFYTSNLFYINYNF
SDNTHLLTKHIRIANSELENNYNKLYHPTPETLENILANPIKSNDKKTLNDYCIGKNVDSIMLPLLSNKKLIKSSAMIRT
NYSKQDLYNLFPMVVIDRIIDHSGNTAKSNQLYTTTSHQISLVHNSTSLYCMLPWHHINRFNFVFSSTGCKISIEYILKD
LKIKDPNCIAFIGEGAGNLLLRTVVELHPDIRYIYRSLKDCNDHSLPIEFLRLYNGHINIDYGENLTIPATDATNNIHWS
YLHIKFAEPISLFVCDAELSVTVNWSKIIIEWSKHVRKCKYCSSVNKCMLIVKYHAQDDIDFKLDNITILKTYVCLGSKL
KGSEVYLVLTIGPANIFPVFNVVQNAKLILSRTKNFIMPKKADKESIDANIKSLIPFLCYPITKKGINTALSKLKSVVSG
DILSYSIAGRNEVFSNKLINHKHMNILKWFNHVLNFRSTELNYNHLYMVESTYPYLSELLNSLTTNELKKLIKITGSLLY
NFHNE
;
1 
2 UNP PHOSP_HRSVA P03421 ? 2 
;MEKFAPEFHGEDANNRATKFLESIKGKFTSPKDPKKKDSIISVNSIDIEVTKESPITSNSTIINPTNETDDTAGNKPNYQ
RKPLVSFKEDPTPSDNPFSKLYKETIETFDNNEEESSYSYEEINDQTNDNITARLDRIDEKLSEILGMLHTLVVASAGPT
SARDGIRDAMIGLREEMIEKIRTEALMTNDRLEAMARLRNEESEKMAKDTSDEVSLNPTSEKLNNLLEGNDSDNDLSLED
F
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9C7Y A 37 ? 2201 ? P28887 1 ? 2165 ? 1 2165 
2 2 9C7Y B 1  ? 241  ? P03421 1 ? 241  ? 1 241  
3 2 9C7Y C 1  ? 241  ? P03421 1 ? 241  ? 1 241  
4 2 9C7Y D 1  ? 241  ? P03421 1 ? 241  ? 1 241  
5 2 9C7Y E 1  ? 241  ? P03421 1 ? 241  ? 1 241  
# 
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 9C7Y MET A 1   ? UNP P28887 ? ? 'initiating methionine' -35 1  
1 9C7Y GLY A 2   ? UNP P28887 ? ? 'expression tag'        -34 2  
1 9C7Y SER A 3   ? UNP P28887 ? ? 'expression tag'        -33 3  
1 9C7Y TRP A 4   ? UNP P28887 ? ? 'expression tag'        -32 4  
1 9C7Y SER A 5   ? UNP P28887 ? ? 'expression tag'        -31 5  
1 9C7Y HIS A 6   ? UNP P28887 ? ? 'expression tag'        -30 6  
1 9C7Y PRO A 7   ? UNP P28887 ? ? 'expression tag'        -29 7  
1 9C7Y GLN A 8   ? UNP P28887 ? ? 'expression tag'        -28 8  
1 9C7Y PHE A 9   ? UNP P28887 ? ? 'expression tag'        -27 9  
1 9C7Y GLU A 10  ? UNP P28887 ? ? 'expression tag'        -26 10 
1 9C7Y LYS A 11  ? UNP P28887 ? ? 'expression tag'        -25 11 
1 9C7Y GLY A 12  ? UNP P28887 ? ? 'expression tag'        -24 12 
1 9C7Y SER A 13  ? UNP P28887 ? ? 'expression tag'        -23 13 
1 9C7Y GLY A 14  ? UNP P28887 ? ? 'expression tag'        -22 14 
1 9C7Y SER A 15  ? UNP P28887 ? ? 'expression tag'        -21 15 
1 9C7Y GLY A 16  ? UNP P28887 ? ? 'expression tag'        -20 16 
1 9C7Y SER A 17  ? UNP P28887 ? ? 'expression tag'        -19 17 
1 9C7Y SER A 18  ? UNP P28887 ? ? 'expression tag'        -18 18 
1 9C7Y TRP A 19  ? UNP P28887 ? ? 'expression tag'        -17 19 
1 9C7Y SER A 20  ? UNP P28887 ? ? 'expression tag'        -16 20 
1 9C7Y HIS A 21  ? UNP P28887 ? ? 'expression tag'        -15 21 
1 9C7Y PRO A 22  ? UNP P28887 ? ? 'expression tag'        -14 22 
1 9C7Y GLN A 23  ? UNP P28887 ? ? 'expression tag'        -13 23 
1 9C7Y PHE A 24  ? UNP P28887 ? ? 'expression tag'        -12 24 
1 9C7Y GLU A 25  ? UNP P28887 ? ? 'expression tag'        -11 25 
1 9C7Y LYS A 26  ? UNP P28887 ? ? 'expression tag'        -10 26 
1 9C7Y GLY A 27  ? UNP P28887 ? ? 'expression tag'        -9  27 
1 9C7Y SER A 28  ? UNP P28887 ? ? 'expression tag'        -8  28 
1 9C7Y GLY A 29  ? UNP P28887 ? ? 'expression tag'        -7  29 
1 9C7Y SER A 30  ? UNP P28887 ? ? 'expression tag'        -6  30 
1 9C7Y LEU A 31  ? UNP P28887 ? ? 'expression tag'        -5  31 
1 9C7Y VAL A 32  ? UNP P28887 ? ? 'expression tag'        -4  32 
1 9C7Y PRO A 33  ? UNP P28887 ? ? 'expression tag'        -3  33 
1 9C7Y ARG A 34  ? UNP P28887 ? ? 'expression tag'        -2  34 
1 9C7Y GLY A 35  ? UNP P28887 ? ? 'expression tag'        -1  35 
1 9C7Y SER A 36  ? UNP P28887 ? ? 'expression tag'        0   36 
2 9C7Y LYS B 242 ? UNP P03421 ? ? 'expression tag'        242 37 
2 9C7Y GLY B 243 ? UNP P03421 ? ? 'expression tag'        243 38 
2 9C7Y GLU B 244 ? UNP P03421 ? ? 'expression tag'        244 39 
2 9C7Y ASN B 245 ? UNP P03421 ? ? 'expression tag'        245 40 
2 9C7Y LYS B 246 ? UNP P03421 ? ? 'expression tag'        246 41 
2 9C7Y TYR B 247 ? UNP P03421 ? ? 'expression tag'        247 42 
2 9C7Y PHE B 248 ? UNP P03421 ? ? 'expression tag'        248 43 
2 9C7Y GLN B 249 ? UNP P03421 ? ? 'expression tag'        249 44 
2 9C7Y GLY B 250 ? UNP P03421 ? ? 'expression tag'        250 45 
2 9C7Y HIS B 251 ? UNP P03421 ? ? 'expression tag'        251 46 
2 9C7Y HIS B 252 ? UNP P03421 ? ? 'expression tag'        252 47 
2 9C7Y HIS B 253 ? UNP P03421 ? ? 'expression tag'        253 48 
2 9C7Y HIS B 254 ? UNP P03421 ? ? 'expression tag'        254 49 
2 9C7Y HIS B 255 ? UNP P03421 ? ? 'expression tag'        255 50 
2 9C7Y HIS B 256 ? UNP P03421 ? ? 'expression tag'        256 51 
3 9C7Y LYS C 242 ? UNP P03421 ? ? 'expression tag'        242 52 
3 9C7Y GLY C 243 ? UNP P03421 ? ? 'expression tag'        243 53 
3 9C7Y GLU C 244 ? UNP P03421 ? ? 'expression tag'        244 54 
3 9C7Y ASN C 245 ? UNP P03421 ? ? 'expression tag'        245 55 
3 9C7Y LYS C 246 ? UNP P03421 ? ? 'expression tag'        246 56 
3 9C7Y TYR C 247 ? UNP P03421 ? ? 'expression tag'        247 57 
3 9C7Y PHE C 248 ? UNP P03421 ? ? 'expression tag'        248 58 
3 9C7Y GLN C 249 ? UNP P03421 ? ? 'expression tag'        249 59 
3 9C7Y GLY C 250 ? UNP P03421 ? ? 'expression tag'        250 60 
3 9C7Y HIS C 251 ? UNP P03421 ? ? 'expression tag'        251 61 
3 9C7Y HIS C 252 ? UNP P03421 ? ? 'expression tag'        252 62 
3 9C7Y HIS C 253 ? UNP P03421 ? ? 'expression tag'        253 63 
3 9C7Y HIS C 254 ? UNP P03421 ? ? 'expression tag'        254 64 
3 9C7Y HIS C 255 ? UNP P03421 ? ? 'expression tag'        255 65 
3 9C7Y HIS C 256 ? UNP P03421 ? ? 'expression tag'        256 66 
4 9C7Y LYS D 242 ? UNP P03421 ? ? 'expression tag'        242 67 
4 9C7Y GLY D 243 ? UNP P03421 ? ? 'expression tag'        243 68 
4 9C7Y GLU D 244 ? UNP P03421 ? ? 'expression tag'        244 69 
4 9C7Y ASN D 245 ? UNP P03421 ? ? 'expression tag'        245 70 
4 9C7Y LYS D 246 ? UNP P03421 ? ? 'expression tag'        246 71 
4 9C7Y TYR D 247 ? UNP P03421 ? ? 'expression tag'        247 72 
4 9C7Y PHE D 248 ? UNP P03421 ? ? 'expression tag'        248 73 
4 9C7Y GLN D 249 ? UNP P03421 ? ? 'expression tag'        249 74 
4 9C7Y GLY D 250 ? UNP P03421 ? ? 'expression tag'        250 75 
4 9C7Y HIS D 251 ? UNP P03421 ? ? 'expression tag'        251 76 
4 9C7Y HIS D 252 ? UNP P03421 ? ? 'expression tag'        252 77 
4 9C7Y HIS D 253 ? UNP P03421 ? ? 'expression tag'        253 78 
4 9C7Y HIS D 254 ? UNP P03421 ? ? 'expression tag'        254 79 
4 9C7Y HIS D 255 ? UNP P03421 ? ? 'expression tag'        255 80 
4 9C7Y HIS D 256 ? UNP P03421 ? ? 'expression tag'        256 81 
5 9C7Y LYS E 242 ? UNP P03421 ? ? 'expression tag'        242 82 
5 9C7Y GLY E 243 ? UNP P03421 ? ? 'expression tag'        243 83 
5 9C7Y GLU E 244 ? UNP P03421 ? ? 'expression tag'        244 84 
5 9C7Y ASN E 245 ? UNP P03421 ? ? 'expression tag'        245 85 
5 9C7Y LYS E 246 ? UNP P03421 ? ? 'expression tag'        246 86 
5 9C7Y TYR E 247 ? UNP P03421 ? ? 'expression tag'        247 87 
5 9C7Y PHE E 248 ? UNP P03421 ? ? 'expression tag'        248 88 
5 9C7Y GLN E 249 ? UNP P03421 ? ? 'expression tag'        249 89 
5 9C7Y GLY E 250 ? UNP P03421 ? ? 'expression tag'        250 90 
5 9C7Y HIS E 251 ? UNP P03421 ? ? 'expression tag'        251 91 
5 9C7Y HIS E 252 ? UNP P03421 ? ? 'expression tag'        252 92 
5 9C7Y HIS E 253 ? UNP P03421 ? ? 'expression tag'        253 93 
5 9C7Y HIS E 254 ? UNP P03421 ? ? 'expression tag'        254 94 
5 9C7Y HIS E 255 ? UNP P03421 ? ? 'expression tag'        255 95 
5 9C7Y HIS E 256 ? UNP P03421 ? ? 'expression tag'        256 96 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_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   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 60   ? ASN A 73   ? SER A 24   ASN A 37   1 ? 14 
HELX_P HELX_P2  AA2 ASP A 80   ? ASN A 89   ? ASP A 44   ASN A 53   1 ? 10 
HELX_P HELX_P3  AA3 LEU A 91   ? LYS A 99   ? LEU A 55   LYS A 63   1 ? 9  
HELX_P HELX_P4  AA4 LEU A 100  ? HIS A 111  ? LEU A 64   HIS A 75   1 ? 12 
HELX_P HELX_P5  AA5 GLU A 119  ? MET A 128  ? GLU A 83   MET A 92   1 ? 10 
HELX_P HELX_P6  AA6 THR A 134  ? GLY A 168  ? THR A 98   GLY A 132  1 ? 35 
HELX_P HELX_P7  AA7 THR A 223  ? GLN A 234  ? THR A 187  GLN A 198  1 ? 12 
HELX_P HELX_P8  AA8 PRO A 237  ? ASN A 264  ? PRO A 201  ASN A 228  1 ? 28 
HELX_P HELX_P9  AA9 THR A 301  ? ASN A 332  ? THR A 265  ASN A 296  1 ? 32 
HELX_P HELX_P10 AB1 ASN A 342  ? PHE A 360  ? ASN A 306  PHE A 324  1 ? 19 
HELX_P HELX_P11 AB2 GLU A 363  ? GLU A 370  ? GLU A 327  GLU A 334  1 ? 8  
HELX_P HELX_P12 AB3 GLU A 370  ? GLU A 384  ? GLU A 334  GLU A 348  1 ? 15 
HELX_P HELX_P13 AB4 GLU A 385  ? VAL A 415  ? GLU A 349  VAL A 379  1 ? 31 
HELX_P HELX_P14 AB5 LEU A 420  ? VAL A 424  ? LEU A 384  VAL A 388  5 ? 5  
HELX_P HELX_P15 AB6 SER A 425  ? ASN A 430  ? SER A 389  ASN A 394  1 ? 6  
HELX_P HELX_P16 AB7 ARG A 432  ? ASP A 449  ? ARG A 396  ASP A 413  1 ? 18 
HELX_P HELX_P17 AB8 ASN A 451  ? LEU A 458  ? ASN A 415  LEU A 422  1 ? 8  
HELX_P HELX_P18 AB9 PHE A 460  ? PHE A 465  ? PHE A 424  PHE A 429  1 ? 6  
HELX_P HELX_P19 AC1 ASP A 471  ? ASN A 484  ? ASP A 435  ASN A 448  1 ? 14 
HELX_P HELX_P20 AC2 LEU A 491  ? ASN A 514  ? LEU A 455  ASN A 478  1 ? 24 
HELX_P HELX_P21 AC3 ASN A 521  ? LEU A 525  ? ASN A 485  LEU A 489  5 ? 5  
HELX_P HELX_P22 AC4 LEU A 527  ? ASN A 536  ? LEU A 491  ASN A 500  1 ? 10 
HELX_P HELX_P23 AC5 SER A 540  ? LEU A 544  ? SER A 504  LEU A 508  5 ? 5  
HELX_P HELX_P24 AC6 THR A 545  ? SER A 553  ? THR A 509  SER A 517  1 ? 9  
HELX_P HELX_P25 AC7 LEU A 584  ? PHE A 589  ? LEU A 548  PHE A 553  5 ? 6  
HELX_P HELX_P26 AC8 PRO A 595  ? LYS A 606  ? PRO A 559  LYS A 570  1 ? 12 
HELX_P HELX_P27 AC9 SER A 612  ? ARG A 616  ? SER A 576  ARG A 580  5 ? 5  
HELX_P HELX_P28 AD1 ARG A 617  ? ARG A 624  ? ARG A 581  ARG A 588  1 ? 8  
HELX_P HELX_P29 AD2 CYS A 631  ? GLN A 640  ? CYS A 595  GLN A 604  1 ? 10 
HELX_P HELX_P30 AD3 GLY A 670  ? ILE A 687  ? GLY A 634  ILE A 651  1 ? 18 
HELX_P HELX_P31 AD4 LEU A 688  ? PHE A 691  ? LEU A 652  PHE A 655  5 ? 4  
HELX_P HELX_P32 AD5 LYS A 739  ? PHE A 744  ? LYS A 703  PHE A 708  1 ? 6  
HELX_P HELX_P33 AD6 ARG A 745  ? GLY A 761  ? ARG A 709  GLY A 725  1 ? 17 
HELX_P HELX_P34 AD7 SER A 767  ? ILE A 773  ? SER A 731  ILE A 737  1 ? 7  
HELX_P HELX_P35 AD8 ASP A 795  ? VAL A 799  ? ASP A 759  VAL A 763  5 ? 5  
HELX_P HELX_P36 AD9 CYS A 817  ? LYS A 837  ? CYS A 781  LYS A 801  1 ? 21 
HELX_P HELX_P37 AE1 THR A 864  ? ILE A 887  ? THR A 828  ILE A 851  1 ? 24 
HELX_P HELX_P38 AE2 PHE A 904  ? THR A 908  ? PHE A 868  THR A 872  5 ? 5  
HELX_P HELX_P39 AE3 ASP A 936  ? GLN A 949  ? ASP A 900  GLN A 913  1 ? 14 
HELX_P HELX_P40 AE4 GLN A 949  ? ARG A 954  ? GLN A 913  ARG A 918  1 ? 6  
HELX_P HELX_P41 AE5 SER A 957  ? ALA A 974  ? SER A 921  ALA A 938  1 ? 18 
HELX_P HELX_P42 AE6 GLN A 976  ? HIS A 980  ? GLN A 940  HIS A 944  5 ? 5  
HELX_P HELX_P43 AE7 ASN A 985  ? ASN A 1003 ? ASN A 949  ASN A 967  1 ? 19 
HELX_P HELX_P44 AE8 ASN A 1006 ? MET A 1015 ? ASN A 970  MET A 979  1 ? 10 
HELX_P HELX_P45 AE9 LEU A 1028 ? PHE A 1033 ? LEU A 992  PHE A 997  5 ? 6  
HELX_P HELX_P46 AF1 ASP A 1039 ? ASN A 1057 ? ASP A 1003 ASN A 1021 1 ? 19 
HELX_P HELX_P47 AF2 ASP A 1070 ? THR A 1081 ? ASP A 1034 THR A 1045 1 ? 12 
HELX_P HELX_P48 AF3 ALA A 1088 ? ASP A 1096 ? ALA A 1052 ASP A 1060 1 ? 9  
HELX_P HELX_P49 AF4 ILE A 1108 ? SER A 1122 ? ILE A 1072 SER A 1086 1 ? 15 
HELX_P HELX_P50 AF5 ASN A 1126 ? HIS A 1135 ? ASN A 1090 HIS A 1099 1 ? 10 
HELX_P HELX_P51 AF6 HIS A 1135 ? MET A 1147 ? HIS A 1099 MET A 1111 1 ? 13 
HELX_P HELX_P52 AF7 TYR A 1154 ? SER A 1164 ? TYR A 1118 SER A 1128 1 ? 11 
HELX_P HELX_P53 AF8 PRO A 1166 ? GLY A 1179 ? PRO A 1130 GLY A 1143 1 ? 14 
HELX_P HELX_P54 AF9 ILE A 1183 ? GLU A 1188 ? ILE A 1147 GLU A 1152 5 ? 6  
HELX_P HELX_P55 AG1 ASP A 1194 ? LEU A 1216 ? ASP A 1158 LEU A 1180 1 ? 23 
HELX_P HELX_P56 AG2 SER A 1234 ? SER A 1248 ? SER A 1198 SER A 1212 1 ? 15 
HELX_P HELX_P57 AG3 SER A 1259 ? THR A 1263 ? SER A 1223 THR A 1227 1 ? 5  
HELX_P HELX_P58 AG4 ASN A 1313 ? LEU A 1317 ? ASN A 1277 LEU A 1281 5 ? 5  
HELX_P HELX_P59 AG5 THR A 1318 ? TYR A 1335 ? THR A 1282 TYR A 1299 1 ? 18 
HELX_P HELX_P60 AG6 ASN A 1340 ? THR A 1352 ? ASN A 1304 THR A 1316 1 ? 13 
HELX_P HELX_P61 AG7 THR A 1356 ? LYS A 1362 ? THR A 1320 LYS A 1326 1 ? 7  
HELX_P HELX_P62 AG8 PRO A 1390 ? THR A 1395 ? PRO A 1354 THR A 1359 1 ? 6  
HELX_P HELX_P63 AG9 THR A 1401 ? GLY A 1413 ? THR A 1365 GLY A 1377 1 ? 13 
HELX_P HELX_P64 AH1 VAL A 1420 ? ASN A 1440 ? VAL A 1384 ASN A 1404 1 ? 21 
HELX_P HELX_P65 AH2 LEU A 1452 ? ILE A 1455 ? LEU A 1416 ILE A 1419 5 ? 4  
HELX_P HELX_P66 AH3 ASP A 1468 ? GLN A 1479 ? ASP A 1432 GLN A 1443 1 ? 12 
HELX_P HELX_P67 AH4 HIS A 1480 ? LEU A 1483 ? HIS A 1444 LEU A 1447 5 ? 4  
HELX_P HELX_P68 AH5 SER A 1488 ? PHE A 1496 ? SER A 1452 PHE A 1460 1 ? 9  
HELX_P HELX_P69 AH6 ASP B 129  ? THR B 151  ? ASP B 129  THR B 151  1 ? 23 
HELX_P HELX_P70 AH7 THR B 160  ? ASP B 164  ? THR B 160  ASP B 164  5 ? 5  
HELX_P HELX_P71 AH8 ARG B 174  ? THR B 183  ? ARG B 174  THR B 183  1 ? 10 
HELX_P HELX_P72 AH9 ARG B 191  ? ARG B 199  ? ARG B 191  ARG B 199  1 ? 9  
HELX_P HELX_P73 AI1 SER B 203  ? THR B 210  ? SER B 203  THR B 210  1 ? 8  
HELX_P HELX_P74 AI2 ASN B 217  ? GLU B 228  ? ASN B 217  GLU B 228  1 ? 12 
HELX_P HELX_P75 AI3 SER B 237  ? PHE B 241  ? SER B 237  PHE B 241  5 ? 5  
HELX_P HELX_P76 AI4 ILE C 131  ? SER C 156  ? ILE C 131  SER C 156  1 ? 26 
HELX_P HELX_P77 AI5 GLY C 158  ? GLY C 165  ? GLY C 158  GLY C 165  1 ? 8  
HELX_P HELX_P78 AI6 ILE C 166  ? GLY C 172  ? ILE C 166  GLY C 172  1 ? 7  
HELX_P HELX_P79 AI7 ARG C 174  ? ALA C 185  ? ARG C 174  ALA C 185  1 ? 12 
HELX_P HELX_P80 AI8 ILE D 131  ? SER D 156  ? ILE D 131  SER D 156  1 ? 26 
HELX_P HELX_P81 AI9 PRO D 159  ? THR D 183  ? PRO D 159  THR D 183  1 ? 25 
HELX_P HELX_P82 AJ1 THR E 132  ? GLY E 158  ? THR E 132  GLY E 158  1 ? 27 
HELX_P HELX_P83 AJ2 ARG E 174  ? ARG E 197  ? ARG E 174  ARG E 197  1 ? 24 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          LYS 
_struct_mon_prot_cis.label_seq_id           112 
_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           LYS 
_struct_mon_prot_cis.auth_seq_id            76 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   GLY 
_struct_mon_prot_cis.pdbx_label_seq_id_2    113 
_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    GLY 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     77 
_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       1.84 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 2 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? 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 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 116  ? LEU A 117  ? LYS A 80   LEU A 81   
AA1 2 ARG A 296  ? THR A 300  ? ARG A 260  THR A 264  
AA1 3 GLY A 286  ? HIS A 291  ? GLY A 250  HIS A 255  
AA1 4 PHE A 278  ? ASN A 283  ? PHE A 242  ASN A 247  
AA1 5 LEU A 269  ? ASP A 271  ? LEU A 233  ASP A 235  
AA2 1 PHE A 488  ? LEU A 490  ? PHE A 452  LEU A 454  
AA2 2 LEU B 152  ? ALA B 155  ? LEU B 152  ALA B 155  
AA2 3 ILE B 171  ? LEU B 173  ? ILE B 171  LEU B 173  
AA3 1 PHE A 665  ? MET A 667  ? PHE A 629  MET A 631  
AA3 2 VAL A 650  ? THR A 653  ? VAL A 614  THR A 617  
AA3 3 THR A 777  ? CYS A 780  ? THR A 741  CYS A 744  
AA3 4 LEU A 805  ? ARG A 807  ? LEU A 769  ARG A 771  
AA4 1 SER A 839  ? ILE A 844  ? SER A 803  ILE A 808  
AA4 2 ASN A 848  ? ILE A 857  ? ASN A 812  ILE A 821  
AA4 3 TYR A 727  ? ASP A 736  ? TYR A 691  ASP A 700  
AA4 4 TYR A 897  ? SER A 899  ? TYR A 861  SER A 863  
AA5 1 ILE A 909  ? HIS A 911  ? ILE A 873  HIS A 875  
AA5 2 VAL A 914  ? TYR A 916  ? VAL A 878  TYR A 880  
AA6 1 MET A 1264 ? LYS A 1267 ? MET A 1228 LYS A 1231 
AA6 2 ARG A 1445 ? PRO A 1450 ? ARG A 1409 PRO A 1414 
AA6 3 ILE A 1277 ? LYS A 1281 ? ILE A 1241 LYS A 1245 
AA6 4 TYR A 1397 ? ASP A 1400 ? TYR A 1361 ASP A 1364 
AA7 1 LYS A 1307 ? THR A 1308 ? LYS A 1271 THR A 1272 
AA7 2 GLN A 1366 ? TYR A 1367 ? GLN A 1330 TYR A 1331 
# 
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 LYS A 116  ? N LYS A 80   O ILE A 297  ? O ILE A 261  
AA1 2 3 O THR A 300  ? O THR A 264  N CYS A 287  ? N CYS A 251  
AA1 3 4 O GLY A 286  ? O GLY A 250  N ASN A 283  ? N ASN A 247  
AA1 4 5 O PHE A 280  ? O PHE A 244  N ASP A 271  ? N ASP A 235  
AA2 1 2 N TYR A 489  ? N TYR A 453  O VAL B 154  ? O VAL B 154  
AA2 2 3 N VAL B 153  ? N VAL B 153  O GLY B 172  ? O GLY B 172  
AA3 1 2 O PHE A 665  ? O PHE A 629  N THR A 653  ? N THR A 617  
AA3 2 3 N VAL A 650  ? N VAL A 614  O ILE A 779  ? O ILE A 743  
AA3 3 4 N ILE A 778  ? N ILE A 742  O TYR A 806  ? O TYR A 770  
AA4 1 2 N THR A 841  ? N THR A 805  O ASP A 852  ? O ASP A 816  
AA4 2 3 O ILE A 857  ? O ILE A 821  N TYR A 727  ? N TYR A 691  
AA4 3 4 N SER A 732  ? N SER A 696  O SER A 899  ? O SER A 863  
AA5 1 2 N ILE A 909  ? N ILE A 873  O TYR A 916  ? O TYR A 880  
AA6 1 2 N ASP A 1265 ? N ASP A 1229 O ILE A 1449 ? O ILE A 1413 
AA6 2 3 O ILE A 1446 ? O ILE A 1410 N ILE A 1279 ? N ILE A 1243 
AA6 3 4 N GLU A 1280 ? N GLU A 1244 O HIS A 1398 ? O HIS A 1362 
AA7 1 2 N THR A 1308 ? N THR A 1272 O GLN A 1366 ? O GLN A 1330 
# 
_pdbx_entry_details.entry_id                   9C7Y 
_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 O   A THR 912  ? ? OG  A SER 925  ? ? 2.15 
2 1 OD2 A ASP 1003 ? ? OG1 A THR 1006 ? ? 2.16 
# 
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 ASN A 43   ? ? -93.41  58.54   
2  1 LEU A 133  ? ? -95.83  30.75   
3  1 THR A 264  ? ? -125.70 -168.96 
4  1 LEU A 422  ? ? -67.66  7.54    
5  1 MET A 433  ? ? -69.27  97.85   
6  1 LEU A 491  ? ? -137.04 -40.15  
7  1 SER A 517  ? ? -59.05  -7.99   
8  1 PRO A 545  ? ? -57.77  172.51  
9  1 ARG A 580  ? ? 73.00   -7.50   
10 1 ARG A 889  ? ? -91.60  30.20   
11 1 TRP A 893  ? ? -102.29 64.42   
12 1 LEU A 1064 ? ? -92.99  -62.13  
13 1 SER A 1352 ? ? -93.71  49.10   
14 1 ASN A 1404 ? ? 73.41   -0.13   
15 1 GLU B 184  ? ? 39.15   36.52   
16 1 ALA C 185  ? ? -91.36  52.44   
17 1 THR E 160  ? ? 65.58   -1.21   
18 1 ILE E 171  ? ? -120.36 -57.02  
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9C7Y 
_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                    9C7Y 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.24 
_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               267890 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.5 
# 
_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                 'Respiratory syncytial virus polymerase in complex with non-nucleoside inhibitor' 
_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                        9C7Y 
_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                            DIFFRACTION 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1400 
_em_imaging.nominal_defocus_max             2300 
_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_vitrification.entry_id              9C7Y 
_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                9C7Y 
_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 -35  ? A MET 1    
2    1 Y 1 A GLY -34  ? A GLY 2    
3    1 Y 1 A SER -33  ? A SER 3    
4    1 Y 1 A TRP -32  ? A TRP 4    
5    1 Y 1 A SER -31  ? A SER 5    
6    1 Y 1 A HIS -30  ? A HIS 6    
7    1 Y 1 A PRO -29  ? A PRO 7    
8    1 Y 1 A GLN -28  ? A GLN 8    
9    1 Y 1 A PHE -27  ? A PHE 9    
10   1 Y 1 A GLU -26  ? A GLU 10   
11   1 Y 1 A LYS -25  ? A LYS 11   
12   1 Y 1 A GLY -24  ? A GLY 12   
13   1 Y 1 A SER -23  ? A SER 13   
14   1 Y 1 A GLY -22  ? A GLY 14   
15   1 Y 1 A SER -21  ? A SER 15   
16   1 Y 1 A GLY -20  ? A GLY 16   
17   1 Y 1 A SER -19  ? A SER 17   
18   1 Y 1 A SER -18  ? A SER 18   
19   1 Y 1 A TRP -17  ? A TRP 19   
20   1 Y 1 A SER -16  ? A SER 20   
21   1 Y 1 A HIS -15  ? A HIS 21   
22   1 Y 1 A PRO -14  ? A PRO 22   
23   1 Y 1 A GLN -13  ? A GLN 23   
24   1 Y 1 A PHE -12  ? A PHE 24   
25   1 Y 1 A GLU -11  ? A GLU 25   
26   1 Y 1 A LYS -10  ? A LYS 26   
27   1 Y 1 A GLY -9   ? A GLY 27   
28   1 Y 1 A SER -8   ? A SER 28   
29   1 Y 1 A GLY -7   ? A GLY 29   
30   1 Y 1 A SER -6   ? A SER 30   
31   1 Y 1 A LEU -5   ? A LEU 31   
32   1 Y 1 A VAL -4   ? A VAL 32   
33   1 Y 1 A PRO -3   ? A PRO 33   
34   1 Y 1 A ARG -2   ? A ARG 34   
35   1 Y 1 A GLY -1   ? A GLY 35   
36   1 Y 1 A SER 0    ? A SER 36   
37   1 Y 1 A MET 1    ? A MET 37   
38   1 Y 1 A ASP 2    ? A ASP 38   
39   1 Y 1 A PRO 3    ? A PRO 39   
40   1 Y 1 A ILE 4    ? A ILE 40   
41   1 Y 1 A ILE 5    ? A ILE 41   
42   1 Y 1 A ASN 6    ? A ASN 42   
43   1 Y 1 A GLY 7    ? A GLY 43   
44   1 Y 1 A ASN 8    ? A ASN 44   
45   1 Y 1 A SER 9    ? A SER 45   
46   1 Y 1 A ALA 10   ? A ALA 46   
47   1 Y 1 A GLU 135  ? A GLU 171  
48   1 Y 1 A LYS 136  ? A LYS 172  
49   1 Y 1 A ASP 137  ? A ASP 173  
50   1 Y 1 A LYS 138  ? A LYS 174  
51   1 Y 1 A ILE 139  ? A ILE 175  
52   1 Y 1 A LYS 140  ? A LYS 176  
53   1 Y 1 A SER 141  ? A SER 177  
54   1 Y 1 A ASN 142  ? A ASN 178  
55   1 Y 1 A ASN 143  ? A ASN 179  
56   1 Y 1 A GLY 144  ? A GLY 180  
57   1 Y 1 A GLN 145  ? A GLN 181  
58   1 Y 1 A ASP 146  ? A ASP 182  
59   1 Y 1 A GLU 147  ? A GLU 183  
60   1 Y 1 A ASP 148  ? A ASP 184  
61   1 Y 1 A ASN 149  ? A ASN 185  
62   1 Y 1 A SER 150  ? A SER 186  
63   1 Y 1 A VAL 151  ? A VAL 187  
64   1 Y 1 A ILE 152  ? A ILE 188  
65   1 Y 1 A THR 153  ? A THR 189  
66   1 Y 1 A THR 154  ? A THR 190  
67   1 Y 1 A ILE 155  ? A ILE 191  
68   1 Y 1 A ILE 156  ? A ILE 192  
69   1 Y 1 A LYS 157  ? A LYS 193  
70   1 Y 1 A ASP 158  ? A ASP 194  
71   1 Y 1 A ASP 159  ? A ASP 195  
72   1 Y 1 A ILE 160  ? A ILE 196  
73   1 Y 1 A LEU 161  ? A LEU 197  
74   1 Y 1 A SER 162  ? A SER 198  
75   1 Y 1 A ALA 163  ? A ALA 199  
76   1 Y 1 A VAL 164  ? A VAL 200  
77   1 Y 1 A LYS 165  ? A LYS 201  
78   1 Y 1 A ASP 166  ? A ASP 202  
79   1 Y 1 A ASN 167  ? A ASN 203  
80   1 Y 1 A GLN 168  ? A GLN 204  
81   1 Y 1 A SER 169  ? A SER 205  
82   1 Y 1 A HIS 170  ? A HIS 206  
83   1 Y 1 A LEU 171  ? A LEU 207  
84   1 Y 1 A LYS 172  ? A LYS 208  
85   1 Y 1 A ALA 173  ? A ALA 209  
86   1 Y 1 A ASP 174  ? A ASP 210  
87   1 Y 1 A LYS 175  ? A LYS 211  
88   1 Y 1 A ASN 176  ? A ASN 212  
89   1 Y 1 A HIS 177  ? A HIS 213  
90   1 Y 1 A SER 178  ? A SER 214  
91   1 Y 1 A THR 179  ? A THR 215  
92   1 Y 1 A LYS 180  ? A LYS 216  
93   1 Y 1 A GLN 181  ? A GLN 217  
94   1 Y 1 A LYS 182  ? A LYS 218  
95   1 Y 1 A LYS 619  ? A LYS 655  
96   1 Y 1 A GLU 620  ? A GLU 656  
97   1 Y 1 A ARG 621  ? A ARG 657  
98   1 Y 1 A GLU 622  ? A GLU 658  
99   1 Y 1 A LEU 623  ? A LEU 659  
100  1 Y 1 A SER 624  ? A SER 660  
101  1 Y 1 A VAL 625  ? A VAL 661  
102  1 Y 1 A GLY 626  ? A GLY 662  
103  1 Y 1 A ARG 627  ? A ARG 663  
104  1 Y 1 A THR 660  ? A THR 696  
105  1 Y 1 A ARG 661  ? A ARG 697  
106  1 Y 1 A TYR 662  ? A TYR 698  
107  1 Y 1 A GLY 663  ? A GLY 699  
108  1 Y 1 A ASP 664  ? A ASP 700  
109  1 Y 1 A LEU 665  ? A LEU 701  
110  1 Y 1 A GLU 666  ? A GLU 702  
111  1 Y 1 A LEU 667  ? A LEU 703  
112  1 Y 1 A GLN 668  ? A GLN 704  
113  1 Y 1 A LYS 669  ? A LYS 705  
114  1 Y 1 A ILE 670  ? A ILE 706  
115  1 Y 1 A LEU 671  ? A LEU 707  
116  1 Y 1 A GLU 672  ? A GLU 708  
117  1 Y 1 A LEU 673  ? A LEU 709  
118  1 Y 1 A LYS 674  ? A LYS 710  
119  1 Y 1 A ALA 675  ? A ALA 711  
120  1 Y 1 A GLY 676  ? A GLY 712  
121  1 Y 1 A ILE 677  ? A ILE 713  
122  1 Y 1 A SER 678  ? A SER 714  
123  1 Y 1 A ASN 679  ? A ASN 715  
124  1 Y 1 A LYS 680  ? A LYS 716  
125  1 Y 1 A SER 681  ? A SER 717  
126  1 Y 1 A ASN 682  ? A ASN 718  
127  1 Y 1 A ARG 683  ? A ARG 719  
128  1 Y 1 A TYR 684  ? A TYR 720  
129  1 Y 1 A ASN 685  ? A ASN 721  
130  1 Y 1 A ASP 686  ? A ASP 722  
131  1 Y 1 A ASN 687  ? A ASN 723  
132  1 Y 1 A TYR 688  ? A TYR 724  
133  1 Y 1 A ASN 1185 ? A ASN 1221 
134  1 Y 1 A ARG 1186 ? A ARG 1222 
135  1 Y 1 A ASP 1187 ? A ASP 1223 
136  1 Y 1 A LYS 1188 ? A LYS 1224 
137  1 Y 1 A ARG 1189 ? A ARG 1225 
138  1 Y 1 A LEU 1461 ? A LEU 1497 
139  1 Y 1 A SER 1462 ? A SER 1498 
140  1 Y 1 A ASN 1463 ? A ASN 1499 
141  1 Y 1 A LYS 1464 ? A LYS 1500 
142  1 Y 1 A THR 1465 ? A THR 1501 
143  1 Y 1 A LEU 1466 ? A LEU 1502 
144  1 Y 1 A LYS 1467 ? A LYS 1503 
145  1 Y 1 A SER 1468 ? A SER 1504 
146  1 Y 1 A GLY 1469 ? A GLY 1505 
147  1 Y 1 A SER 1470 ? A SER 1506 
148  1 Y 1 A HIS 1471 ? A HIS 1507 
149  1 Y 1 A VAL 1472 ? A VAL 1508 
150  1 Y 1 A ASN 1473 ? A ASN 1509 
151  1 Y 1 A SER 1474 ? A SER 1510 
152  1 Y 1 A ASN 1475 ? A ASN 1511 
153  1 Y 1 A LEU 1476 ? A LEU 1512 
154  1 Y 1 A ILE 1477 ? A ILE 1513 
155  1 Y 1 A LEU 1478 ? A LEU 1514 
156  1 Y 1 A ALA 1479 ? A ALA 1515 
157  1 Y 1 A HIS 1480 ? A HIS 1516 
158  1 Y 1 A LYS 1481 ? A LYS 1517 
159  1 Y 1 A ILE 1482 ? A ILE 1518 
160  1 Y 1 A SER 1483 ? A SER 1519 
161  1 Y 1 A ASP 1484 ? A ASP 1520 
162  1 Y 1 A TYR 1485 ? A TYR 1521 
163  1 Y 1 A PHE 1486 ? A PHE 1522 
164  1 Y 1 A HIS 1487 ? A HIS 1523 
165  1 Y 1 A ASN 1488 ? A ASN 1524 
166  1 Y 1 A THR 1489 ? A THR 1525 
167  1 Y 1 A TYR 1490 ? A TYR 1526 
168  1 Y 1 A ILE 1491 ? A ILE 1527 
169  1 Y 1 A LEU 1492 ? A LEU 1528 
170  1 Y 1 A SER 1493 ? A SER 1529 
171  1 Y 1 A THR 1494 ? A THR 1530 
172  1 Y 1 A ASN 1495 ? A ASN 1531 
173  1 Y 1 A LEU 1496 ? A LEU 1532 
174  1 Y 1 A ALA 1497 ? A ALA 1533 
175  1 Y 1 A GLY 1498 ? A GLY 1534 
176  1 Y 1 A HIS 1499 ? A HIS 1535 
177  1 Y 1 A TRP 1500 ? A TRP 1536 
178  1 Y 1 A ILE 1501 ? A ILE 1537 
179  1 Y 1 A LEU 1502 ? A LEU 1538 
180  1 Y 1 A ILE 1503 ? A ILE 1539 
181  1 Y 1 A ILE 1504 ? A ILE 1540 
182  1 Y 1 A GLN 1505 ? A GLN 1541 
183  1 Y 1 A LEU 1506 ? A LEU 1542 
184  1 Y 1 A MET 1507 ? A MET 1543 
185  1 Y 1 A LYS 1508 ? A LYS 1544 
186  1 Y 1 A ASP 1509 ? A ASP 1545 
187  1 Y 1 A SER 1510 ? A SER 1546 
188  1 Y 1 A LYS 1511 ? A LYS 1547 
189  1 Y 1 A GLY 1512 ? A GLY 1548 
190  1 Y 1 A ILE 1513 ? A ILE 1549 
191  1 Y 1 A PHE 1514 ? A PHE 1550 
192  1 Y 1 A GLU 1515 ? A GLU 1551 
193  1 Y 1 A LYS 1516 ? A LYS 1552 
194  1 Y 1 A ASP 1517 ? A ASP 1553 
195  1 Y 1 A TRP 1518 ? A TRP 1554 
196  1 Y 1 A GLY 1519 ? A GLY 1555 
197  1 Y 1 A GLU 1520 ? A GLU 1556 
198  1 Y 1 A GLY 1521 ? A GLY 1557 
199  1 Y 1 A TYR 1522 ? A TYR 1558 
200  1 Y 1 A ILE 1523 ? A ILE 1559 
201  1 Y 1 A THR 1524 ? A THR 1560 
202  1 Y 1 A ASP 1525 ? A ASP 1561 
203  1 Y 1 A HIS 1526 ? A HIS 1562 
204  1 Y 1 A MET 1527 ? A MET 1563 
205  1 Y 1 A PHE 1528 ? A PHE 1564 
206  1 Y 1 A ILE 1529 ? A ILE 1565 
207  1 Y 1 A ASN 1530 ? A ASN 1566 
208  1 Y 1 A LEU 1531 ? A LEU 1567 
209  1 Y 1 A LYS 1532 ? A LYS 1568 
210  1 Y 1 A VAL 1533 ? A VAL 1569 
211  1 Y 1 A PHE 1534 ? A PHE 1570 
212  1 Y 1 A PHE 1535 ? A PHE 1571 
213  1 Y 1 A ASN 1536 ? A ASN 1572 
214  1 Y 1 A ALA 1537 ? A ALA 1573 
215  1 Y 1 A TYR 1538 ? A TYR 1574 
216  1 Y 1 A LYS 1539 ? A LYS 1575 
217  1 Y 1 A THR 1540 ? A THR 1576 
218  1 Y 1 A TYR 1541 ? A TYR 1577 
219  1 Y 1 A LEU 1542 ? A LEU 1578 
220  1 Y 1 A LEU 1543 ? A LEU 1579 
221  1 Y 1 A CYS 1544 ? A CYS 1580 
222  1 Y 1 A PHE 1545 ? A PHE 1581 
223  1 Y 1 A HIS 1546 ? A HIS 1582 
224  1 Y 1 A LYS 1547 ? A LYS 1583 
225  1 Y 1 A GLY 1548 ? A GLY 1584 
226  1 Y 1 A TYR 1549 ? A TYR 1585 
227  1 Y 1 A GLY 1550 ? A GLY 1586 
228  1 Y 1 A LYS 1551 ? A LYS 1587 
229  1 Y 1 A ALA 1552 ? A ALA 1588 
230  1 Y 1 A LYS 1553 ? A LYS 1589 
231  1 Y 1 A LEU 1554 ? A LEU 1590 
232  1 Y 1 A GLU 1555 ? A GLU 1591 
233  1 Y 1 A CYS 1556 ? A CYS 1592 
234  1 Y 1 A ASP 1557 ? A ASP 1593 
235  1 Y 1 A MET 1558 ? A MET 1594 
236  1 Y 1 A ASN 1559 ? A ASN 1595 
237  1 Y 1 A THR 1560 ? A THR 1596 
238  1 Y 1 A SER 1561 ? A SER 1597 
239  1 Y 1 A ASP 1562 ? A ASP 1598 
240  1 Y 1 A LEU 1563 ? A LEU 1599 
241  1 Y 1 A LEU 1564 ? A LEU 1600 
242  1 Y 1 A CYS 1565 ? A CYS 1601 
243  1 Y 1 A VAL 1566 ? A VAL 1602 
244  1 Y 1 A LEU 1567 ? A LEU 1603 
245  1 Y 1 A GLU 1568 ? A GLU 1604 
246  1 Y 1 A LEU 1569 ? A LEU 1605 
247  1 Y 1 A ILE 1570 ? A ILE 1606 
248  1 Y 1 A ASP 1571 ? A ASP 1607 
249  1 Y 1 A SER 1572 ? A SER 1608 
250  1 Y 1 A SER 1573 ? A SER 1609 
251  1 Y 1 A TYR 1574 ? A TYR 1610 
252  1 Y 1 A TRP 1575 ? A TRP 1611 
253  1 Y 1 A LYS 1576 ? A LYS 1612 
254  1 Y 1 A SER 1577 ? A SER 1613 
255  1 Y 1 A MET 1578 ? A MET 1614 
256  1 Y 1 A SER 1579 ? A SER 1615 
257  1 Y 1 A LYS 1580 ? A LYS 1616 
258  1 Y 1 A VAL 1581 ? A VAL 1617 
259  1 Y 1 A PHE 1582 ? A PHE 1618 
260  1 Y 1 A LEU 1583 ? A LEU 1619 
261  1 Y 1 A GLU 1584 ? A GLU 1620 
262  1 Y 1 A GLN 1585 ? A GLN 1621 
263  1 Y 1 A LYS 1586 ? A LYS 1622 
264  1 Y 1 A VAL 1587 ? A VAL 1623 
265  1 Y 1 A ILE 1588 ? A ILE 1624 
266  1 Y 1 A LYS 1589 ? A LYS 1625 
267  1 Y 1 A TYR 1590 ? A TYR 1626 
268  1 Y 1 A ILE 1591 ? A ILE 1627 
269  1 Y 1 A LEU 1592 ? A LEU 1628 
270  1 Y 1 A SER 1593 ? A SER 1629 
271  1 Y 1 A GLN 1594 ? A GLN 1630 
272  1 Y 1 A ASP 1595 ? A ASP 1631 
273  1 Y 1 A ALA 1596 ? A ALA 1632 
274  1 Y 1 A SER 1597 ? A SER 1633 
275  1 Y 1 A LEU 1598 ? A LEU 1634 
276  1 Y 1 A HIS 1599 ? A HIS 1635 
277  1 Y 1 A ARG 1600 ? A ARG 1636 
278  1 Y 1 A VAL 1601 ? A VAL 1637 
279  1 Y 1 A LYS 1602 ? A LYS 1638 
280  1 Y 1 A GLY 1603 ? A GLY 1639 
281  1 Y 1 A CYS 1604 ? A CYS 1640 
282  1 Y 1 A HIS 1605 ? A HIS 1641 
283  1 Y 1 A SER 1606 ? A SER 1642 
284  1 Y 1 A PHE 1607 ? A PHE 1643 
285  1 Y 1 A LYS 1608 ? A LYS 1644 
286  1 Y 1 A LEU 1609 ? A LEU 1645 
287  1 Y 1 A TRP 1610 ? A TRP 1646 
288  1 Y 1 A PHE 1611 ? A PHE 1647 
289  1 Y 1 A LEU 1612 ? A LEU 1648 
290  1 Y 1 A LYS 1613 ? A LYS 1649 
291  1 Y 1 A ARG 1614 ? A ARG 1650 
292  1 Y 1 A LEU 1615 ? A LEU 1651 
293  1 Y 1 A ASN 1616 ? A ASN 1652 
294  1 Y 1 A VAL 1617 ? A VAL 1653 
295  1 Y 1 A ALA 1618 ? A ALA 1654 
296  1 Y 1 A GLU 1619 ? A GLU 1655 
297  1 Y 1 A PHE 1620 ? A PHE 1656 
298  1 Y 1 A THR 1621 ? A THR 1657 
299  1 Y 1 A VAL 1622 ? A VAL 1658 
300  1 Y 1 A CYS 1623 ? A CYS 1659 
301  1 Y 1 A PRO 1624 ? A PRO 1660 
302  1 Y 1 A TRP 1625 ? A TRP 1661 
303  1 Y 1 A VAL 1626 ? A VAL 1662 
304  1 Y 1 A VAL 1627 ? A VAL 1663 
305  1 Y 1 A ASN 1628 ? A ASN 1664 
306  1 Y 1 A ILE 1629 ? A ILE 1665 
307  1 Y 1 A ASP 1630 ? A ASP 1666 
308  1 Y 1 A TYR 1631 ? A TYR 1667 
309  1 Y 1 A HIS 1632 ? A HIS 1668 
310  1 Y 1 A PRO 1633 ? A PRO 1669 
311  1 Y 1 A THR 1634 ? A THR 1670 
312  1 Y 1 A HIS 1635 ? A HIS 1671 
313  1 Y 1 A MET 1636 ? A MET 1672 
314  1 Y 1 A LYS 1637 ? A LYS 1673 
315  1 Y 1 A ALA 1638 ? A ALA 1674 
316  1 Y 1 A ILE 1639 ? A ILE 1675 
317  1 Y 1 A LEU 1640 ? A LEU 1676 
318  1 Y 1 A THR 1641 ? A THR 1677 
319  1 Y 1 A TYR 1642 ? A TYR 1678 
320  1 Y 1 A ILE 1643 ? A ILE 1679 
321  1 Y 1 A ASP 1644 ? A ASP 1680 
322  1 Y 1 A LEU 1645 ? A LEU 1681 
323  1 Y 1 A VAL 1646 ? A VAL 1682 
324  1 Y 1 A ARG 1647 ? A ARG 1683 
325  1 Y 1 A MET 1648 ? A MET 1684 
326  1 Y 1 A GLY 1649 ? A GLY 1685 
327  1 Y 1 A LEU 1650 ? A LEU 1686 
328  1 Y 1 A ILE 1651 ? A ILE 1687 
329  1 Y 1 A ASN 1652 ? A ASN 1688 
330  1 Y 1 A ILE 1653 ? A ILE 1689 
331  1 Y 1 A ASP 1654 ? A ASP 1690 
332  1 Y 1 A ARG 1655 ? A ARG 1691 
333  1 Y 1 A ILE 1656 ? A ILE 1692 
334  1 Y 1 A HIS 1657 ? A HIS 1693 
335  1 Y 1 A ILE 1658 ? A ILE 1694 
336  1 Y 1 A LYS 1659 ? A LYS 1695 
337  1 Y 1 A ASN 1660 ? A ASN 1696 
338  1 Y 1 A LYS 1661 ? A LYS 1697 
339  1 Y 1 A HIS 1662 ? A HIS 1698 
340  1 Y 1 A LYS 1663 ? A LYS 1699 
341  1 Y 1 A PHE 1664 ? A PHE 1700 
342  1 Y 1 A ASN 1665 ? A ASN 1701 
343  1 Y 1 A ASP 1666 ? A ASP 1702 
344  1 Y 1 A GLU 1667 ? A GLU 1703 
345  1 Y 1 A PHE 1668 ? A PHE 1704 
346  1 Y 1 A TYR 1669 ? A TYR 1705 
347  1 Y 1 A THR 1670 ? A THR 1706 
348  1 Y 1 A SER 1671 ? A SER 1707 
349  1 Y 1 A ASN 1672 ? A ASN 1708 
350  1 Y 1 A LEU 1673 ? A LEU 1709 
351  1 Y 1 A PHE 1674 ? A PHE 1710 
352  1 Y 1 A TYR 1675 ? A TYR 1711 
353  1 Y 1 A ILE 1676 ? A ILE 1712 
354  1 Y 1 A ASN 1677 ? A ASN 1713 
355  1 Y 1 A TYR 1678 ? A TYR 1714 
356  1 Y 1 A ASN 1679 ? A ASN 1715 
357  1 Y 1 A PHE 1680 ? A PHE 1716 
358  1 Y 1 A SER 1681 ? A SER 1717 
359  1 Y 1 A ASP 1682 ? A ASP 1718 
360  1 Y 1 A ASN 1683 ? A ASN 1719 
361  1 Y 1 A THR 1684 ? A THR 1720 
362  1 Y 1 A HIS 1685 ? A HIS 1721 
363  1 Y 1 A LEU 1686 ? A LEU 1722 
364  1 Y 1 A LEU 1687 ? A LEU 1723 
365  1 Y 1 A THR 1688 ? A THR 1724 
366  1 Y 1 A LYS 1689 ? A LYS 1725 
367  1 Y 1 A HIS 1690 ? A HIS 1726 
368  1 Y 1 A ILE 1691 ? A ILE 1727 
369  1 Y 1 A ARG 1692 ? A ARG 1728 
370  1 Y 1 A ILE 1693 ? A ILE 1729 
371  1 Y 1 A ALA 1694 ? A ALA 1730 
372  1 Y 1 A ASN 1695 ? A ASN 1731 
373  1 Y 1 A SER 1696 ? A SER 1732 
374  1 Y 1 A GLU 1697 ? A GLU 1733 
375  1 Y 1 A LEU 1698 ? A LEU 1734 
376  1 Y 1 A GLU 1699 ? A GLU 1735 
377  1 Y 1 A ASN 1700 ? A ASN 1736 
378  1 Y 1 A ASN 1701 ? A ASN 1737 
379  1 Y 1 A TYR 1702 ? A TYR 1738 
380  1 Y 1 A ASN 1703 ? A ASN 1739 
381  1 Y 1 A LYS 1704 ? A LYS 1740 
382  1 Y 1 A LEU 1705 ? A LEU 1741 
383  1 Y 1 A TYR 1706 ? A TYR 1742 
384  1 Y 1 A HIS 1707 ? A HIS 1743 
385  1 Y 1 A PRO 1708 ? A PRO 1744 
386  1 Y 1 A THR 1709 ? A THR 1745 
387  1 Y 1 A PRO 1710 ? A PRO 1746 
388  1 Y 1 A GLU 1711 ? A GLU 1747 
389  1 Y 1 A THR 1712 ? A THR 1748 
390  1 Y 1 A LEU 1713 ? A LEU 1749 
391  1 Y 1 A GLU 1714 ? A GLU 1750 
392  1 Y 1 A ASN 1715 ? A ASN 1751 
393  1 Y 1 A ILE 1716 ? A ILE 1752 
394  1 Y 1 A LEU 1717 ? A LEU 1753 
395  1 Y 1 A ALA 1718 ? A ALA 1754 
396  1 Y 1 A ASN 1719 ? A ASN 1755 
397  1 Y 1 A PRO 1720 ? A PRO 1756 
398  1 Y 1 A ILE 1721 ? A ILE 1757 
399  1 Y 1 A LYS 1722 ? A LYS 1758 
400  1 Y 1 A SER 1723 ? A SER 1759 
401  1 Y 1 A ASN 1724 ? A ASN 1760 
402  1 Y 1 A ASP 1725 ? A ASP 1761 
403  1 Y 1 A LYS 1726 ? A LYS 1762 
404  1 Y 1 A LYS 1727 ? A LYS 1763 
405  1 Y 1 A THR 1728 ? A THR 1764 
406  1 Y 1 A LEU 1729 ? A LEU 1765 
407  1 Y 1 A ASN 1730 ? A ASN 1766 
408  1 Y 1 A ASP 1731 ? A ASP 1767 
409  1 Y 1 A TYR 1732 ? A TYR 1768 
410  1 Y 1 A CYS 1733 ? A CYS 1769 
411  1 Y 1 A ILE 1734 ? A ILE 1770 
412  1 Y 1 A GLY 1735 ? A GLY 1771 
413  1 Y 1 A LYS 1736 ? A LYS 1772 
414  1 Y 1 A ASN 1737 ? A ASN 1773 
415  1 Y 1 A VAL 1738 ? A VAL 1774 
416  1 Y 1 A ASP 1739 ? A ASP 1775 
417  1 Y 1 A SER 1740 ? A SER 1776 
418  1 Y 1 A ILE 1741 ? A ILE 1777 
419  1 Y 1 A MET 1742 ? A MET 1778 
420  1 Y 1 A LEU 1743 ? A LEU 1779 
421  1 Y 1 A PRO 1744 ? A PRO 1780 
422  1 Y 1 A LEU 1745 ? A LEU 1781 
423  1 Y 1 A LEU 1746 ? A LEU 1782 
424  1 Y 1 A SER 1747 ? A SER 1783 
425  1 Y 1 A ASN 1748 ? A ASN 1784 
426  1 Y 1 A LYS 1749 ? A LYS 1785 
427  1 Y 1 A LYS 1750 ? A LYS 1786 
428  1 Y 1 A LEU 1751 ? A LEU 1787 
429  1 Y 1 A ILE 1752 ? A ILE 1788 
430  1 Y 1 A LYS 1753 ? A LYS 1789 
431  1 Y 1 A SER 1754 ? A SER 1790 
432  1 Y 1 A SER 1755 ? A SER 1791 
433  1 Y 1 A ALA 1756 ? A ALA 1792 
434  1 Y 1 A MET 1757 ? A MET 1793 
435  1 Y 1 A ILE 1758 ? A ILE 1794 
436  1 Y 1 A ARG 1759 ? A ARG 1795 
437  1 Y 1 A THR 1760 ? A THR 1796 
438  1 Y 1 A ASN 1761 ? A ASN 1797 
439  1 Y 1 A TYR 1762 ? A TYR 1798 
440  1 Y 1 A SER 1763 ? A SER 1799 
441  1 Y 1 A LYS 1764 ? A LYS 1800 
442  1 Y 1 A GLN 1765 ? A GLN 1801 
443  1 Y 1 A ASP 1766 ? A ASP 1802 
444  1 Y 1 A LEU 1767 ? A LEU 1803 
445  1 Y 1 A TYR 1768 ? A TYR 1804 
446  1 Y 1 A ASN 1769 ? A ASN 1805 
447  1 Y 1 A LEU 1770 ? A LEU 1806 
448  1 Y 1 A PHE 1771 ? A PHE 1807 
449  1 Y 1 A PRO 1772 ? A PRO 1808 
450  1 Y 1 A MET 1773 ? A MET 1809 
451  1 Y 1 A VAL 1774 ? A VAL 1810 
452  1 Y 1 A VAL 1775 ? A VAL 1811 
453  1 Y 1 A ILE 1776 ? A ILE 1812 
454  1 Y 1 A ASP 1777 ? A ASP 1813 
455  1 Y 1 A ARG 1778 ? A ARG 1814 
456  1 Y 1 A ILE 1779 ? A ILE 1815 
457  1 Y 1 A ILE 1780 ? A ILE 1816 
458  1 Y 1 A ASP 1781 ? A ASP 1817 
459  1 Y 1 A HIS 1782 ? A HIS 1818 
460  1 Y 1 A SER 1783 ? A SER 1819 
461  1 Y 1 A GLY 1784 ? A GLY 1820 
462  1 Y 1 A ASN 1785 ? A ASN 1821 
463  1 Y 1 A THR 1786 ? A THR 1822 
464  1 Y 1 A ALA 1787 ? A ALA 1823 
465  1 Y 1 A LYS 1788 ? A LYS 1824 
466  1 Y 1 A SER 1789 ? A SER 1825 
467  1 Y 1 A ASN 1790 ? A ASN 1826 
468  1 Y 1 A GLN 1791 ? A GLN 1827 
469  1 Y 1 A LEU 1792 ? A LEU 1828 
470  1 Y 1 A TYR 1793 ? A TYR 1829 
471  1 Y 1 A THR 1794 ? A THR 1830 
472  1 Y 1 A THR 1795 ? A THR 1831 
473  1 Y 1 A THR 1796 ? A THR 1832 
474  1 Y 1 A SER 1797 ? A SER 1833 
475  1 Y 1 A HIS 1798 ? A HIS 1834 
476  1 Y 1 A GLN 1799 ? A GLN 1835 
477  1 Y 1 A ILE 1800 ? A ILE 1836 
478  1 Y 1 A SER 1801 ? A SER 1837 
479  1 Y 1 A LEU 1802 ? A LEU 1838 
480  1 Y 1 A VAL 1803 ? A VAL 1839 
481  1 Y 1 A HIS 1804 ? A HIS 1840 
482  1 Y 1 A ASN 1805 ? A ASN 1841 
483  1 Y 1 A SER 1806 ? A SER 1842 
484  1 Y 1 A THR 1807 ? A THR 1843 
485  1 Y 1 A SER 1808 ? A SER 1844 
486  1 Y 1 A LEU 1809 ? A LEU 1845 
487  1 Y 1 A TYR 1810 ? A TYR 1846 
488  1 Y 1 A CYS 1811 ? A CYS 1847 
489  1 Y 1 A MET 1812 ? A MET 1848 
490  1 Y 1 A LEU 1813 ? A LEU 1849 
491  1 Y 1 A PRO 1814 ? A PRO 1850 
492  1 Y 1 A TRP 1815 ? A TRP 1851 
493  1 Y 1 A HIS 1816 ? A HIS 1852 
494  1 Y 1 A HIS 1817 ? A HIS 1853 
495  1 Y 1 A ILE 1818 ? A ILE 1854 
496  1 Y 1 A ASN 1819 ? A ASN 1855 
497  1 Y 1 A ARG 1820 ? A ARG 1856 
498  1 Y 1 A PHE 1821 ? A PHE 1857 
499  1 Y 1 A ASN 1822 ? A ASN 1858 
500  1 Y 1 A PHE 1823 ? A PHE 1859 
501  1 Y 1 A VAL 1824 ? A VAL 1860 
502  1 Y 1 A PHE 1825 ? A PHE 1861 
503  1 Y 1 A SER 1826 ? A SER 1862 
504  1 Y 1 A SER 1827 ? A SER 1863 
505  1 Y 1 A THR 1828 ? A THR 1864 
506  1 Y 1 A GLY 1829 ? A GLY 1865 
507  1 Y 1 A CYS 1830 ? A CYS 1866 
508  1 Y 1 A LYS 1831 ? A LYS 1867 
509  1 Y 1 A ILE 1832 ? A ILE 1868 
510  1 Y 1 A SER 1833 ? A SER 1869 
511  1 Y 1 A ILE 1834 ? A ILE 1870 
512  1 Y 1 A GLU 1835 ? A GLU 1871 
513  1 Y 1 A TYR 1836 ? A TYR 1872 
514  1 Y 1 A ILE 1837 ? A ILE 1873 
515  1 Y 1 A LEU 1838 ? A LEU 1874 
516  1 Y 1 A LYS 1839 ? A LYS 1875 
517  1 Y 1 A ASP 1840 ? A ASP 1876 
518  1 Y 1 A LEU 1841 ? A LEU 1877 
519  1 Y 1 A LYS 1842 ? A LYS 1878 
520  1 Y 1 A ILE 1843 ? A ILE 1879 
521  1 Y 1 A LYS 1844 ? A LYS 1880 
522  1 Y 1 A ASP 1845 ? A ASP 1881 
523  1 Y 1 A PRO 1846 ? A PRO 1882 
524  1 Y 1 A ASN 1847 ? A ASN 1883 
525  1 Y 1 A CYS 1848 ? A CYS 1884 
526  1 Y 1 A ILE 1849 ? A ILE 1885 
527  1 Y 1 A ALA 1850 ? A ALA 1886 
528  1 Y 1 A PHE 1851 ? A PHE 1887 
529  1 Y 1 A ILE 1852 ? A ILE 1888 
530  1 Y 1 A GLY 1853 ? A GLY 1889 
531  1 Y 1 A GLU 1854 ? A GLU 1890 
532  1 Y 1 A GLY 1855 ? A GLY 1891 
533  1 Y 1 A ALA 1856 ? A ALA 1892 
534  1 Y 1 A GLY 1857 ? A GLY 1893 
535  1 Y 1 A ASN 1858 ? A ASN 1894 
536  1 Y 1 A LEU 1859 ? A LEU 1895 
537  1 Y 1 A LEU 1860 ? A LEU 1896 
538  1 Y 1 A LEU 1861 ? A LEU 1897 
539  1 Y 1 A ARG 1862 ? A ARG 1898 
540  1 Y 1 A THR 1863 ? A THR 1899 
541  1 Y 1 A VAL 1864 ? A VAL 1900 
542  1 Y 1 A VAL 1865 ? A VAL 1901 
543  1 Y 1 A GLU 1866 ? A GLU 1902 
544  1 Y 1 A LEU 1867 ? A LEU 1903 
545  1 Y 1 A HIS 1868 ? A HIS 1904 
546  1 Y 1 A PRO 1869 ? A PRO 1905 
547  1 Y 1 A ASP 1870 ? A ASP 1906 
548  1 Y 1 A ILE 1871 ? A ILE 1907 
549  1 Y 1 A ARG 1872 ? A ARG 1908 
550  1 Y 1 A TYR 1873 ? A TYR 1909 
551  1 Y 1 A ILE 1874 ? A ILE 1910 
552  1 Y 1 A TYR 1875 ? A TYR 1911 
553  1 Y 1 A ARG 1876 ? A ARG 1912 
554  1 Y 1 A SER 1877 ? A SER 1913 
555  1 Y 1 A LEU 1878 ? A LEU 1914 
556  1 Y 1 A LYS 1879 ? A LYS 1915 
557  1 Y 1 A ASP 1880 ? A ASP 1916 
558  1 Y 1 A CYS 1881 ? A CYS 1917 
559  1 Y 1 A ASN 1882 ? A ASN 1918 
560  1 Y 1 A ASP 1883 ? A ASP 1919 
561  1 Y 1 A HIS 1884 ? A HIS 1920 
562  1 Y 1 A SER 1885 ? A SER 1921 
563  1 Y 1 A LEU 1886 ? A LEU 1922 
564  1 Y 1 A PRO 1887 ? A PRO 1923 
565  1 Y 1 A ILE 1888 ? A ILE 1924 
566  1 Y 1 A GLU 1889 ? A GLU 1925 
567  1 Y 1 A PHE 1890 ? A PHE 1926 
568  1 Y 1 A LEU 1891 ? A LEU 1927 
569  1 Y 1 A ARG 1892 ? A ARG 1928 
570  1 Y 1 A LEU 1893 ? A LEU 1929 
571  1 Y 1 A TYR 1894 ? A TYR 1930 
572  1 Y 1 A ASN 1895 ? A ASN 1931 
573  1 Y 1 A GLY 1896 ? A GLY 1932 
574  1 Y 1 A HIS 1897 ? A HIS 1933 
575  1 Y 1 A ILE 1898 ? A ILE 1934 
576  1 Y 1 A ASN 1899 ? A ASN 1935 
577  1 Y 1 A ILE 1900 ? A ILE 1936 
578  1 Y 1 A ASP 1901 ? A ASP 1937 
579  1 Y 1 A TYR 1902 ? A TYR 1938 
580  1 Y 1 A GLY 1903 ? A GLY 1939 
581  1 Y 1 A GLU 1904 ? A GLU 1940 
582  1 Y 1 A ASN 1905 ? A ASN 1941 
583  1 Y 1 A LEU 1906 ? A LEU 1942 
584  1 Y 1 A THR 1907 ? A THR 1943 
585  1 Y 1 A ILE 1908 ? A ILE 1944 
586  1 Y 1 A PRO 1909 ? A PRO 1945 
587  1 Y 1 A ALA 1910 ? A ALA 1946 
588  1 Y 1 A THR 1911 ? A THR 1947 
589  1 Y 1 A ASP 1912 ? A ASP 1948 
590  1 Y 1 A ALA 1913 ? A ALA 1949 
591  1 Y 1 A THR 1914 ? A THR 1950 
592  1 Y 1 A ASN 1915 ? A ASN 1951 
593  1 Y 1 A ASN 1916 ? A ASN 1952 
594  1 Y 1 A ILE 1917 ? A ILE 1953 
595  1 Y 1 A HIS 1918 ? A HIS 1954 
596  1 Y 1 A TRP 1919 ? A TRP 1955 
597  1 Y 1 A SER 1920 ? A SER 1956 
598  1 Y 1 A TYR 1921 ? A TYR 1957 
599  1 Y 1 A LEU 1922 ? A LEU 1958 
600  1 Y 1 A HIS 1923 ? A HIS 1959 
601  1 Y 1 A ILE 1924 ? A ILE 1960 
602  1 Y 1 A LYS 1925 ? A LYS 1961 
603  1 Y 1 A PHE 1926 ? A PHE 1962 
604  1 Y 1 A ALA 1927 ? A ALA 1963 
605  1 Y 1 A GLU 1928 ? A GLU 1964 
606  1 Y 1 A PRO 1929 ? A PRO 1965 
607  1 Y 1 A ILE 1930 ? A ILE 1966 
608  1 Y 1 A SER 1931 ? A SER 1967 
609  1 Y 1 A LEU 1932 ? A LEU 1968 
610  1 Y 1 A PHE 1933 ? A PHE 1969 
611  1 Y 1 A VAL 1934 ? A VAL 1970 
612  1 Y 1 A CYS 1935 ? A CYS 1971 
613  1 Y 1 A ASP 1936 ? A ASP 1972 
614  1 Y 1 A ALA 1937 ? A ALA 1973 
615  1 Y 1 A GLU 1938 ? A GLU 1974 
616  1 Y 1 A LEU 1939 ? A LEU 1975 
617  1 Y 1 A SER 1940 ? A SER 1976 
618  1 Y 1 A VAL 1941 ? A VAL 1977 
619  1 Y 1 A THR 1942 ? A THR 1978 
620  1 Y 1 A VAL 1943 ? A VAL 1979 
621  1 Y 1 A ASN 1944 ? A ASN 1980 
622  1 Y 1 A TRP 1945 ? A TRP 1981 
623  1 Y 1 A SER 1946 ? A SER 1982 
624  1 Y 1 A LYS 1947 ? A LYS 1983 
625  1 Y 1 A ILE 1948 ? A ILE 1984 
626  1 Y 1 A ILE 1949 ? A ILE 1985 
627  1 Y 1 A ILE 1950 ? A ILE 1986 
628  1 Y 1 A GLU 1951 ? A GLU 1987 
629  1 Y 1 A TRP 1952 ? A TRP 1988 
630  1 Y 1 A SER 1953 ? A SER 1989 
631  1 Y 1 A LYS 1954 ? A LYS 1990 
632  1 Y 1 A HIS 1955 ? A HIS 1991 
633  1 Y 1 A VAL 1956 ? A VAL 1992 
634  1 Y 1 A ARG 1957 ? A ARG 1993 
635  1 Y 1 A LYS 1958 ? A LYS 1994 
636  1 Y 1 A CYS 1959 ? A CYS 1995 
637  1 Y 1 A LYS 1960 ? A LYS 1996 
638  1 Y 1 A TYR 1961 ? A TYR 1997 
639  1 Y 1 A CYS 1962 ? A CYS 1998 
640  1 Y 1 A SER 1963 ? A SER 1999 
641  1 Y 1 A SER 1964 ? A SER 2000 
642  1 Y 1 A VAL 1965 ? A VAL 2001 
643  1 Y 1 A ASN 1966 ? A ASN 2002 
644  1 Y 1 A LYS 1967 ? A LYS 2003 
645  1 Y 1 A CYS 1968 ? A CYS 2004 
646  1 Y 1 A MET 1969 ? A MET 2005 
647  1 Y 1 A LEU 1970 ? A LEU 2006 
648  1 Y 1 A ILE 1971 ? A ILE 2007 
649  1 Y 1 A VAL 1972 ? A VAL 2008 
650  1 Y 1 A LYS 1973 ? A LYS 2009 
651  1 Y 1 A TYR 1974 ? A TYR 2010 
652  1 Y 1 A HIS 1975 ? A HIS 2011 
653  1 Y 1 A ALA 1976 ? A ALA 2012 
654  1 Y 1 A GLN 1977 ? A GLN 2013 
655  1 Y 1 A ASP 1978 ? A ASP 2014 
656  1 Y 1 A ASP 1979 ? A ASP 2015 
657  1 Y 1 A ILE 1980 ? A ILE 2016 
658  1 Y 1 A ASP 1981 ? A ASP 2017 
659  1 Y 1 A PHE 1982 ? A PHE 2018 
660  1 Y 1 A LYS 1983 ? A LYS 2019 
661  1 Y 1 A LEU 1984 ? A LEU 2020 
662  1 Y 1 A ASP 1985 ? A ASP 2021 
663  1 Y 1 A ASN 1986 ? A ASN 2022 
664  1 Y 1 A ILE 1987 ? A ILE 2023 
665  1 Y 1 A THR 1988 ? A THR 2024 
666  1 Y 1 A ILE 1989 ? A ILE 2025 
667  1 Y 1 A LEU 1990 ? A LEU 2026 
668  1 Y 1 A LYS 1991 ? A LYS 2027 
669  1 Y 1 A THR 1992 ? A THR 2028 
670  1 Y 1 A TYR 1993 ? A TYR 2029 
671  1 Y 1 A VAL 1994 ? A VAL 2030 
672  1 Y 1 A CYS 1995 ? A CYS 2031 
673  1 Y 1 A LEU 1996 ? A LEU 2032 
674  1 Y 1 A GLY 1997 ? A GLY 2033 
675  1 Y 1 A SER 1998 ? A SER 2034 
676  1 Y 1 A LYS 1999 ? A LYS 2035 
677  1 Y 1 A LEU 2000 ? A LEU 2036 
678  1 Y 1 A LYS 2001 ? A LYS 2037 
679  1 Y 1 A GLY 2002 ? A GLY 2038 
680  1 Y 1 A SER 2003 ? A SER 2039 
681  1 Y 1 A GLU 2004 ? A GLU 2040 
682  1 Y 1 A VAL 2005 ? A VAL 2041 
683  1 Y 1 A TYR 2006 ? A TYR 2042 
684  1 Y 1 A LEU 2007 ? A LEU 2043 
685  1 Y 1 A VAL 2008 ? A VAL 2044 
686  1 Y 1 A LEU 2009 ? A LEU 2045 
687  1 Y 1 A THR 2010 ? A THR 2046 
688  1 Y 1 A ILE 2011 ? A ILE 2047 
689  1 Y 1 A GLY 2012 ? A GLY 2048 
690  1 Y 1 A PRO 2013 ? A PRO 2049 
691  1 Y 1 A ALA 2014 ? A ALA 2050 
692  1 Y 1 A ASN 2015 ? A ASN 2051 
693  1 Y 1 A ILE 2016 ? A ILE 2052 
694  1 Y 1 A PHE 2017 ? A PHE 2053 
695  1 Y 1 A PRO 2018 ? A PRO 2054 
696  1 Y 1 A VAL 2019 ? A VAL 2055 
697  1 Y 1 A PHE 2020 ? A PHE 2056 
698  1 Y 1 A ASN 2021 ? A ASN 2057 
699  1 Y 1 A VAL 2022 ? A VAL 2058 
700  1 Y 1 A VAL 2023 ? A VAL 2059 
701  1 Y 1 A GLN 2024 ? A GLN 2060 
702  1 Y 1 A ASN 2025 ? A ASN 2061 
703  1 Y 1 A ALA 2026 ? A ALA 2062 
704  1 Y 1 A LYS 2027 ? A LYS 2063 
705  1 Y 1 A LEU 2028 ? A LEU 2064 
706  1 Y 1 A ILE 2029 ? A ILE 2065 
707  1 Y 1 A LEU 2030 ? A LEU 2066 
708  1 Y 1 A SER 2031 ? A SER 2067 
709  1 Y 1 A ARG 2032 ? A ARG 2068 
710  1 Y 1 A THR 2033 ? A THR 2069 
711  1 Y 1 A LYS 2034 ? A LYS 2070 
712  1 Y 1 A ASN 2035 ? A ASN 2071 
713  1 Y 1 A PHE 2036 ? A PHE 2072 
714  1 Y 1 A ILE 2037 ? A ILE 2073 
715  1 Y 1 A MET 2038 ? A MET 2074 
716  1 Y 1 A PRO 2039 ? A PRO 2075 
717  1 Y 1 A LYS 2040 ? A LYS 2076 
718  1 Y 1 A LYS 2041 ? A LYS 2077 
719  1 Y 1 A ALA 2042 ? A ALA 2078 
720  1 Y 1 A ASP 2043 ? A ASP 2079 
721  1 Y 1 A LYS 2044 ? A LYS 2080 
722  1 Y 1 A GLU 2045 ? A GLU 2081 
723  1 Y 1 A SER 2046 ? A SER 2082 
724  1 Y 1 A ILE 2047 ? A ILE 2083 
725  1 Y 1 A ASP 2048 ? A ASP 2084 
726  1 Y 1 A ALA 2049 ? A ALA 2085 
727  1 Y 1 A ASN 2050 ? A ASN 2086 
728  1 Y 1 A ILE 2051 ? A ILE 2087 
729  1 Y 1 A LYS 2052 ? A LYS 2088 
730  1 Y 1 A SER 2053 ? A SER 2089 
731  1 Y 1 A LEU 2054 ? A LEU 2090 
732  1 Y 1 A ILE 2055 ? A ILE 2091 
733  1 Y 1 A PRO 2056 ? A PRO 2092 
734  1 Y 1 A PHE 2057 ? A PHE 2093 
735  1 Y 1 A LEU 2058 ? A LEU 2094 
736  1 Y 1 A CYS 2059 ? A CYS 2095 
737  1 Y 1 A TYR 2060 ? A TYR 2096 
738  1 Y 1 A PRO 2061 ? A PRO 2097 
739  1 Y 1 A ILE 2062 ? A ILE 2098 
740  1 Y 1 A THR 2063 ? A THR 2099 
741  1 Y 1 A LYS 2064 ? A LYS 2100 
742  1 Y 1 A LYS 2065 ? A LYS 2101 
743  1 Y 1 A GLY 2066 ? A GLY 2102 
744  1 Y 1 A ILE 2067 ? A ILE 2103 
745  1 Y 1 A ASN 2068 ? A ASN 2104 
746  1 Y 1 A THR 2069 ? A THR 2105 
747  1 Y 1 A ALA 2070 ? A ALA 2106 
748  1 Y 1 A LEU 2071 ? A LEU 2107 
749  1 Y 1 A SER 2072 ? A SER 2108 
750  1 Y 1 A LYS 2073 ? A LYS 2109 
751  1 Y 1 A LEU 2074 ? A LEU 2110 
752  1 Y 1 A LYS 2075 ? A LYS 2111 
753  1 Y 1 A SER 2076 ? A SER 2112 
754  1 Y 1 A VAL 2077 ? A VAL 2113 
755  1 Y 1 A VAL 2078 ? A VAL 2114 
756  1 Y 1 A SER 2079 ? A SER 2115 
757  1 Y 1 A GLY 2080 ? A GLY 2116 
758  1 Y 1 A ASP 2081 ? A ASP 2117 
759  1 Y 1 A ILE 2082 ? A ILE 2118 
760  1 Y 1 A LEU 2083 ? A LEU 2119 
761  1 Y 1 A SER 2084 ? A SER 2120 
762  1 Y 1 A TYR 2085 ? A TYR 2121 
763  1 Y 1 A SER 2086 ? A SER 2122 
764  1 Y 1 A ILE 2087 ? A ILE 2123 
765  1 Y 1 A ALA 2088 ? A ALA 2124 
766  1 Y 1 A GLY 2089 ? A GLY 2125 
767  1 Y 1 A ARG 2090 ? A ARG 2126 
768  1 Y 1 A ASN 2091 ? A ASN 2127 
769  1 Y 1 A GLU 2092 ? A GLU 2128 
770  1 Y 1 A VAL 2093 ? A VAL 2129 
771  1 Y 1 A PHE 2094 ? A PHE 2130 
772  1 Y 1 A SER 2095 ? A SER 2131 
773  1 Y 1 A ASN 2096 ? A ASN 2132 
774  1 Y 1 A LYS 2097 ? A LYS 2133 
775  1 Y 1 A LEU 2098 ? A LEU 2134 
776  1 Y 1 A ILE 2099 ? A ILE 2135 
777  1 Y 1 A ASN 2100 ? A ASN 2136 
778  1 Y 1 A HIS 2101 ? A HIS 2137 
779  1 Y 1 A LYS 2102 ? A LYS 2138 
780  1 Y 1 A HIS 2103 ? A HIS 2139 
781  1 Y 1 A MET 2104 ? A MET 2140 
782  1 Y 1 A ASN 2105 ? A ASN 2141 
783  1 Y 1 A ILE 2106 ? A ILE 2142 
784  1 Y 1 A LEU 2107 ? A LEU 2143 
785  1 Y 1 A LYS 2108 ? A LYS 2144 
786  1 Y 1 A TRP 2109 ? A TRP 2145 
787  1 Y 1 A PHE 2110 ? A PHE 2146 
788  1 Y 1 A ASN 2111 ? A ASN 2147 
789  1 Y 1 A HIS 2112 ? A HIS 2148 
790  1 Y 1 A VAL 2113 ? A VAL 2149 
791  1 Y 1 A LEU 2114 ? A LEU 2150 
792  1 Y 1 A ASN 2115 ? A ASN 2151 
793  1 Y 1 A PHE 2116 ? A PHE 2152 
794  1 Y 1 A ARG 2117 ? A ARG 2153 
795  1 Y 1 A SER 2118 ? A SER 2154 
796  1 Y 1 A THR 2119 ? A THR 2155 
797  1 Y 1 A GLU 2120 ? A GLU 2156 
798  1 Y 1 A LEU 2121 ? A LEU 2157 
799  1 Y 1 A ASN 2122 ? A ASN 2158 
800  1 Y 1 A TYR 2123 ? A TYR 2159 
801  1 Y 1 A ASN 2124 ? A ASN 2160 
802  1 Y 1 A HIS 2125 ? A HIS 2161 
803  1 Y 1 A LEU 2126 ? A LEU 2162 
804  1 Y 1 A TYR 2127 ? A TYR 2163 
805  1 Y 1 A MET 2128 ? A MET 2164 
806  1 Y 1 A VAL 2129 ? A VAL 2165 
807  1 Y 1 A GLU 2130 ? A GLU 2166 
808  1 Y 1 A SER 2131 ? A SER 2167 
809  1 Y 1 A THR 2132 ? A THR 2168 
810  1 Y 1 A TYR 2133 ? A TYR 2169 
811  1 Y 1 A PRO 2134 ? A PRO 2170 
812  1 Y 1 A TYR 2135 ? A TYR 2171 
813  1 Y 1 A LEU 2136 ? A LEU 2172 
814  1 Y 1 A SER 2137 ? A SER 2173 
815  1 Y 1 A GLU 2138 ? A GLU 2174 
816  1 Y 1 A LEU 2139 ? A LEU 2175 
817  1 Y 1 A LEU 2140 ? A LEU 2176 
818  1 Y 1 A ASN 2141 ? A ASN 2177 
819  1 Y 1 A SER 2142 ? A SER 2178 
820  1 Y 1 A LEU 2143 ? A LEU 2179 
821  1 Y 1 A THR 2144 ? A THR 2180 
822  1 Y 1 A THR 2145 ? A THR 2181 
823  1 Y 1 A ASN 2146 ? A ASN 2182 
824  1 Y 1 A GLU 2147 ? A GLU 2183 
825  1 Y 1 A LEU 2148 ? A LEU 2184 
826  1 Y 1 A LYS 2149 ? A LYS 2185 
827  1 Y 1 A LYS 2150 ? A LYS 2186 
828  1 Y 1 A LEU 2151 ? A LEU 2187 
829  1 Y 1 A ILE 2152 ? A ILE 2188 
830  1 Y 1 A LYS 2153 ? A LYS 2189 
831  1 Y 1 A ILE 2154 ? A ILE 2190 
832  1 Y 1 A THR 2155 ? A THR 2191 
833  1 Y 1 A GLY 2156 ? A GLY 2192 
834  1 Y 1 A SER 2157 ? A SER 2193 
835  1 Y 1 A LEU 2158 ? A LEU 2194 
836  1 Y 1 A LEU 2159 ? A LEU 2195 
837  1 Y 1 A TYR 2160 ? A TYR 2196 
838  1 Y 1 A ASN 2161 ? A ASN 2197 
839  1 Y 1 A PHE 2162 ? A PHE 2198 
840  1 Y 1 A HIS 2163 ? A HIS 2199 
841  1 Y 1 A ASN 2164 ? A ASN 2200 
842  1 Y 1 A GLU 2165 ? A GLU 2201 
843  1 Y 1 B MET 1    ? B MET 1    
844  1 Y 1 B GLU 2    ? B GLU 2    
845  1 Y 1 B LYS 3    ? B LYS 3    
846  1 Y 1 B PHE 4    ? B PHE 4    
847  1 Y 1 B ALA 5    ? B ALA 5    
848  1 Y 1 B PRO 6    ? B PRO 6    
849  1 Y 1 B GLU 7    ? B GLU 7    
850  1 Y 1 B PHE 8    ? B PHE 8    
851  1 Y 1 B HIS 9    ? B HIS 9    
852  1 Y 1 B GLY 10   ? B GLY 10   
853  1 Y 1 B GLU 11   ? B GLU 11   
854  1 Y 1 B ASP 12   ? B ASP 12   
855  1 Y 1 B ALA 13   ? B ALA 13   
856  1 Y 1 B ASN 14   ? B ASN 14   
857  1 Y 1 B ASN 15   ? B ASN 15   
858  1 Y 1 B ARG 16   ? B ARG 16   
859  1 Y 1 B ALA 17   ? B ALA 17   
860  1 Y 1 B THR 18   ? B THR 18   
861  1 Y 1 B LYS 19   ? B LYS 19   
862  1 Y 1 B PHE 20   ? B PHE 20   
863  1 Y 1 B LEU 21   ? B LEU 21   
864  1 Y 1 B GLU 22   ? B GLU 22   
865  1 Y 1 B SER 23   ? B SER 23   
866  1 Y 1 B ILE 24   ? B ILE 24   
867  1 Y 1 B LYS 25   ? B LYS 25   
868  1 Y 1 B GLY 26   ? B GLY 26   
869  1 Y 1 B LYS 27   ? B LYS 27   
870  1 Y 1 B PHE 28   ? B PHE 28   
871  1 Y 1 B THR 29   ? B THR 29   
872  1 Y 1 B SER 30   ? B SER 30   
873  1 Y 1 B PRO 31   ? B PRO 31   
874  1 Y 1 B LYS 32   ? B LYS 32   
875  1 Y 1 B ASP 33   ? B ASP 33   
876  1 Y 1 B PRO 34   ? B PRO 34   
877  1 Y 1 B LYS 35   ? B LYS 35   
878  1 Y 1 B LYS 36   ? B LYS 36   
879  1 Y 1 B LYS 37   ? B LYS 37   
880  1 Y 1 B ASP 38   ? B ASP 38   
881  1 Y 1 B SER 39   ? B SER 39   
882  1 Y 1 B ILE 40   ? B ILE 40   
883  1 Y 1 B ILE 41   ? B ILE 41   
884  1 Y 1 B SER 42   ? B SER 42   
885  1 Y 1 B VAL 43   ? B VAL 43   
886  1 Y 1 B ASN 44   ? B ASN 44   
887  1 Y 1 B SER 45   ? B SER 45   
888  1 Y 1 B ILE 46   ? B ILE 46   
889  1 Y 1 B ASP 47   ? B ASP 47   
890  1 Y 1 B ILE 48   ? B ILE 48   
891  1 Y 1 B GLU 49   ? B GLU 49   
892  1 Y 1 B VAL 50   ? B VAL 50   
893  1 Y 1 B THR 51   ? B THR 51   
894  1 Y 1 B LYS 52   ? B LYS 52   
895  1 Y 1 B GLU 53   ? B GLU 53   
896  1 Y 1 B SER 54   ? B SER 54   
897  1 Y 1 B PRO 55   ? B PRO 55   
898  1 Y 1 B ILE 56   ? B ILE 56   
899  1 Y 1 B THR 57   ? B THR 57   
900  1 Y 1 B SER 58   ? B SER 58   
901  1 Y 1 B ASN 59   ? B ASN 59   
902  1 Y 1 B SER 60   ? B SER 60   
903  1 Y 1 B THR 61   ? B THR 61   
904  1 Y 1 B ILE 62   ? B ILE 62   
905  1 Y 1 B ILE 63   ? B ILE 63   
906  1 Y 1 B ASN 64   ? B ASN 64   
907  1 Y 1 B PRO 65   ? B PRO 65   
908  1 Y 1 B THR 66   ? B THR 66   
909  1 Y 1 B ASN 67   ? B ASN 67   
910  1 Y 1 B GLU 68   ? B GLU 68   
911  1 Y 1 B THR 69   ? B THR 69   
912  1 Y 1 B ASP 70   ? B ASP 70   
913  1 Y 1 B ASP 71   ? B ASP 71   
914  1 Y 1 B THR 72   ? B THR 72   
915  1 Y 1 B ALA 73   ? B ALA 73   
916  1 Y 1 B GLY 74   ? B GLY 74   
917  1 Y 1 B ASN 75   ? B ASN 75   
918  1 Y 1 B LYS 76   ? B LYS 76   
919  1 Y 1 B PRO 77   ? B PRO 77   
920  1 Y 1 B ASN 78   ? B ASN 78   
921  1 Y 1 B TYR 79   ? B TYR 79   
922  1 Y 1 B GLN 80   ? B GLN 80   
923  1 Y 1 B ARG 81   ? B ARG 81   
924  1 Y 1 B LYS 82   ? B LYS 82   
925  1 Y 1 B PRO 83   ? B PRO 83   
926  1 Y 1 B LEU 84   ? B LEU 84   
927  1 Y 1 B VAL 85   ? B VAL 85   
928  1 Y 1 B SER 86   ? B SER 86   
929  1 Y 1 B PHE 87   ? B PHE 87   
930  1 Y 1 B LYS 88   ? B LYS 88   
931  1 Y 1 B GLU 89   ? B GLU 89   
932  1 Y 1 B ASP 90   ? B ASP 90   
933  1 Y 1 B PRO 91   ? B PRO 91   
934  1 Y 1 B THR 92   ? B THR 92   
935  1 Y 1 B PRO 93   ? B PRO 93   
936  1 Y 1 B SER 94   ? B SER 94   
937  1 Y 1 B ASP 95   ? B ASP 95   
938  1 Y 1 B ASN 96   ? B ASN 96   
939  1 Y 1 B PRO 97   ? B PRO 97   
940  1 Y 1 B PHE 98   ? B PHE 98   
941  1 Y 1 B SER 99   ? B SER 99   
942  1 Y 1 B LYS 100  ? B LYS 100  
943  1 Y 1 B LEU 101  ? B LEU 101  
944  1 Y 1 B TYR 102  ? B TYR 102  
945  1 Y 1 B LYS 103  ? B LYS 103  
946  1 Y 1 B GLU 104  ? B GLU 104  
947  1 Y 1 B THR 105  ? B THR 105  
948  1 Y 1 B ILE 106  ? B ILE 106  
949  1 Y 1 B GLU 107  ? B GLU 107  
950  1 Y 1 B THR 108  ? B THR 108  
951  1 Y 1 B PHE 109  ? B PHE 109  
952  1 Y 1 B ASP 110  ? B ASP 110  
953  1 Y 1 B ASN 111  ? B ASN 111  
954  1 Y 1 B ASN 112  ? B ASN 112  
955  1 Y 1 B GLU 113  ? B GLU 113  
956  1 Y 1 B GLU 114  ? B GLU 114  
957  1 Y 1 B GLU 115  ? B GLU 115  
958  1 Y 1 B SER 116  ? B SER 116  
959  1 Y 1 B SER 117  ? B SER 117  
960  1 Y 1 B TYR 118  ? B TYR 118  
961  1 Y 1 B SER 119  ? B SER 119  
962  1 Y 1 B TYR 120  ? B TYR 120  
963  1 Y 1 B GLU 121  ? B GLU 121  
964  1 Y 1 B GLU 122  ? B GLU 122  
965  1 Y 1 B ILE 123  ? B ILE 123  
966  1 Y 1 B ASN 124  ? B ASN 124  
967  1 Y 1 B ASP 125  ? B ASP 125  
968  1 Y 1 B GLN 126  ? B GLN 126  
969  1 Y 1 B THR 127  ? B THR 127  
970  1 Y 1 B LYS 242  ? B LYS 242  
971  1 Y 1 B GLY 243  ? B GLY 243  
972  1 Y 1 B GLU 244  ? B GLU 244  
973  1 Y 1 B ASN 245  ? B ASN 245  
974  1 Y 1 B LYS 246  ? B LYS 246  
975  1 Y 1 B TYR 247  ? B TYR 247  
976  1 Y 1 B PHE 248  ? B PHE 248  
977  1 Y 1 B GLN 249  ? B GLN 249  
978  1 Y 1 B GLY 250  ? B GLY 250  
979  1 Y 1 B HIS 251  ? B HIS 251  
980  1 Y 1 B HIS 252  ? B HIS 252  
981  1 Y 1 B HIS 253  ? B HIS 253  
982  1 Y 1 B HIS 254  ? B HIS 254  
983  1 Y 1 B HIS 255  ? B HIS 255  
984  1 Y 1 B HIS 256  ? B HIS 256  
985  1 Y 1 C MET 1    ? C MET 1    
986  1 Y 1 C GLU 2    ? C GLU 2    
987  1 Y 1 C LYS 3    ? C LYS 3    
988  1 Y 1 C PHE 4    ? C PHE 4    
989  1 Y 1 C ALA 5    ? C ALA 5    
990  1 Y 1 C PRO 6    ? C PRO 6    
991  1 Y 1 C GLU 7    ? C GLU 7    
992  1 Y 1 C PHE 8    ? C PHE 8    
993  1 Y 1 C HIS 9    ? C HIS 9    
994  1 Y 1 C GLY 10   ? C GLY 10   
995  1 Y 1 C GLU 11   ? C GLU 11   
996  1 Y 1 C ASP 12   ? C ASP 12   
997  1 Y 1 C ALA 13   ? C ALA 13   
998  1 Y 1 C ASN 14   ? C ASN 14   
999  1 Y 1 C ASN 15   ? C ASN 15   
1000 1 Y 1 C ARG 16   ? C ARG 16   
1001 1 Y 1 C ALA 17   ? C ALA 17   
1002 1 Y 1 C THR 18   ? C THR 18   
1003 1 Y 1 C LYS 19   ? C LYS 19   
1004 1 Y 1 C PHE 20   ? C PHE 20   
1005 1 Y 1 C LEU 21   ? C LEU 21   
1006 1 Y 1 C GLU 22   ? C GLU 22   
1007 1 Y 1 C SER 23   ? C SER 23   
1008 1 Y 1 C ILE 24   ? C ILE 24   
1009 1 Y 1 C LYS 25   ? C LYS 25   
1010 1 Y 1 C GLY 26   ? C GLY 26   
1011 1 Y 1 C LYS 27   ? C LYS 27   
1012 1 Y 1 C PHE 28   ? C PHE 28   
1013 1 Y 1 C THR 29   ? C THR 29   
1014 1 Y 1 C SER 30   ? C SER 30   
1015 1 Y 1 C PRO 31   ? C PRO 31   
1016 1 Y 1 C LYS 32   ? C LYS 32   
1017 1 Y 1 C ASP 33   ? C ASP 33   
1018 1 Y 1 C PRO 34   ? C PRO 34   
1019 1 Y 1 C LYS 35   ? C LYS 35   
1020 1 Y 1 C LYS 36   ? C LYS 36   
1021 1 Y 1 C LYS 37   ? C LYS 37   
1022 1 Y 1 C ASP 38   ? C ASP 38   
1023 1 Y 1 C SER 39   ? C SER 39   
1024 1 Y 1 C ILE 40   ? C ILE 40   
1025 1 Y 1 C ILE 41   ? C ILE 41   
1026 1 Y 1 C SER 42   ? C SER 42   
1027 1 Y 1 C VAL 43   ? C VAL 43   
1028 1 Y 1 C ASN 44   ? C ASN 44   
1029 1 Y 1 C SER 45   ? C SER 45   
1030 1 Y 1 C ILE 46   ? C ILE 46   
1031 1 Y 1 C ASP 47   ? C ASP 47   
1032 1 Y 1 C ILE 48   ? C ILE 48   
1033 1 Y 1 C GLU 49   ? C GLU 49   
1034 1 Y 1 C VAL 50   ? C VAL 50   
1035 1 Y 1 C THR 51   ? C THR 51   
1036 1 Y 1 C LYS 52   ? C LYS 52   
1037 1 Y 1 C GLU 53   ? C GLU 53   
1038 1 Y 1 C SER 54   ? C SER 54   
1039 1 Y 1 C PRO 55   ? C PRO 55   
1040 1 Y 1 C ILE 56   ? C ILE 56   
1041 1 Y 1 C THR 57   ? C THR 57   
1042 1 Y 1 C SER 58   ? C SER 58   
1043 1 Y 1 C ASN 59   ? C ASN 59   
1044 1 Y 1 C SER 60   ? C SER 60   
1045 1 Y 1 C THR 61   ? C THR 61   
1046 1 Y 1 C ILE 62   ? C ILE 62   
1047 1 Y 1 C ILE 63   ? C ILE 63   
1048 1 Y 1 C ASN 64   ? C ASN 64   
1049 1 Y 1 C PRO 65   ? C PRO 65   
1050 1 Y 1 C THR 66   ? C THR 66   
1051 1 Y 1 C ASN 67   ? C ASN 67   
1052 1 Y 1 C GLU 68   ? C GLU 68   
1053 1 Y 1 C THR 69   ? C THR 69   
1054 1 Y 1 C ASP 70   ? C ASP 70   
1055 1 Y 1 C ASP 71   ? C ASP 71   
1056 1 Y 1 C THR 72   ? C THR 72   
1057 1 Y 1 C ALA 73   ? C ALA 73   
1058 1 Y 1 C GLY 74   ? C GLY 74   
1059 1 Y 1 C ASN 75   ? C ASN 75   
1060 1 Y 1 C LYS 76   ? C LYS 76   
1061 1 Y 1 C PRO 77   ? C PRO 77   
1062 1 Y 1 C ASN 78   ? C ASN 78   
1063 1 Y 1 C TYR 79   ? C TYR 79   
1064 1 Y 1 C GLN 80   ? C GLN 80   
1065 1 Y 1 C ARG 81   ? C ARG 81   
1066 1 Y 1 C LYS 82   ? C LYS 82   
1067 1 Y 1 C PRO 83   ? C PRO 83   
1068 1 Y 1 C LEU 84   ? C LEU 84   
1069 1 Y 1 C VAL 85   ? C VAL 85   
1070 1 Y 1 C SER 86   ? C SER 86   
1071 1 Y 1 C PHE 87   ? C PHE 87   
1072 1 Y 1 C LYS 88   ? C LYS 88   
1073 1 Y 1 C GLU 89   ? C GLU 89   
1074 1 Y 1 C ASP 90   ? C ASP 90   
1075 1 Y 1 C PRO 91   ? C PRO 91   
1076 1 Y 1 C THR 92   ? C THR 92   
1077 1 Y 1 C PRO 93   ? C PRO 93   
1078 1 Y 1 C SER 94   ? C SER 94   
1079 1 Y 1 C ASP 95   ? C ASP 95   
1080 1 Y 1 C ASN 96   ? C ASN 96   
1081 1 Y 1 C PRO 97   ? C PRO 97   
1082 1 Y 1 C PHE 98   ? C PHE 98   
1083 1 Y 1 C SER 99   ? C SER 99   
1084 1 Y 1 C LYS 100  ? C LYS 100  
1085 1 Y 1 C LEU 101  ? C LEU 101  
1086 1 Y 1 C TYR 102  ? C TYR 102  
1087 1 Y 1 C LYS 103  ? C LYS 103  
1088 1 Y 1 C GLU 104  ? C GLU 104  
1089 1 Y 1 C THR 105  ? C THR 105  
1090 1 Y 1 C ILE 106  ? C ILE 106  
1091 1 Y 1 C GLU 107  ? C GLU 107  
1092 1 Y 1 C THR 108  ? C THR 108  
1093 1 Y 1 C PHE 109  ? C PHE 109  
1094 1 Y 1 C ASP 110  ? C ASP 110  
1095 1 Y 1 C ASN 111  ? C ASN 111  
1096 1 Y 1 C ASN 112  ? C ASN 112  
1097 1 Y 1 C GLU 113  ? C GLU 113  
1098 1 Y 1 C GLU 114  ? C GLU 114  
1099 1 Y 1 C GLU 115  ? C GLU 115  
1100 1 Y 1 C SER 116  ? C SER 116  
1101 1 Y 1 C SER 117  ? C SER 117  
1102 1 Y 1 C TYR 118  ? C TYR 118  
1103 1 Y 1 C SER 119  ? C SER 119  
1104 1 Y 1 C TYR 120  ? C TYR 120  
1105 1 Y 1 C GLU 121  ? C GLU 121  
1106 1 Y 1 C GLU 122  ? C GLU 122  
1107 1 Y 1 C ILE 123  ? C ILE 123  
1108 1 Y 1 C ASN 124  ? C ASN 124  
1109 1 Y 1 C ASP 125  ? C ASP 125  
1110 1 Y 1 C GLN 126  ? C GLN 126  
1111 1 Y 1 C THR 127  ? C THR 127  
1112 1 Y 1 C ASN 128  ? C ASN 128  
1113 1 Y 1 C ASP 129  ? C ASP 129  
1114 1 Y 1 C MET 187  ? C MET 187  
1115 1 Y 1 C THR 188  ? C THR 188  
1116 1 Y 1 C ASN 189  ? C ASN 189  
1117 1 Y 1 C ASP 190  ? C ASP 190  
1118 1 Y 1 C ARG 191  ? C ARG 191  
1119 1 Y 1 C LEU 192  ? C LEU 192  
1120 1 Y 1 C GLU 193  ? C GLU 193  
1121 1 Y 1 C ALA 194  ? C ALA 194  
1122 1 Y 1 C MET 195  ? C MET 195  
1123 1 Y 1 C ALA 196  ? C ALA 196  
1124 1 Y 1 C ARG 197  ? C ARG 197  
1125 1 Y 1 C LEU 198  ? C LEU 198  
1126 1 Y 1 C ARG 199  ? C ARG 199  
1127 1 Y 1 C ASN 200  ? C ASN 200  
1128 1 Y 1 C GLU 201  ? C GLU 201  
1129 1 Y 1 C GLU 202  ? C GLU 202  
1130 1 Y 1 C SER 203  ? C SER 203  
1131 1 Y 1 C GLU 204  ? C GLU 204  
1132 1 Y 1 C LYS 205  ? C LYS 205  
1133 1 Y 1 C MET 206  ? C MET 206  
1134 1 Y 1 C ALA 207  ? C ALA 207  
1135 1 Y 1 C LYS 208  ? C LYS 208  
1136 1 Y 1 C ASP 209  ? C ASP 209  
1137 1 Y 1 C THR 210  ? C THR 210  
1138 1 Y 1 C SER 211  ? C SER 211  
1139 1 Y 1 C ASP 212  ? C ASP 212  
1140 1 Y 1 C GLU 213  ? C GLU 213  
1141 1 Y 1 C VAL 214  ? C VAL 214  
1142 1 Y 1 C SER 215  ? C SER 215  
1143 1 Y 1 C LEU 216  ? C LEU 216  
1144 1 Y 1 C ASN 217  ? C ASN 217  
1145 1 Y 1 C PRO 218  ? C PRO 218  
1146 1 Y 1 C THR 219  ? C THR 219  
1147 1 Y 1 C SER 220  ? C SER 220  
1148 1 Y 1 C GLU 221  ? C GLU 221  
1149 1 Y 1 C LYS 222  ? C LYS 222  
1150 1 Y 1 C LEU 223  ? C LEU 223  
1151 1 Y 1 C ASN 224  ? C ASN 224  
1152 1 Y 1 C ASN 225  ? C ASN 225  
1153 1 Y 1 C LEU 226  ? C LEU 226  
1154 1 Y 1 C LEU 227  ? C LEU 227  
1155 1 Y 1 C GLU 228  ? C GLU 228  
1156 1 Y 1 C GLY 229  ? C GLY 229  
1157 1 Y 1 C ASN 230  ? C ASN 230  
1158 1 Y 1 C ASP 231  ? C ASP 231  
1159 1 Y 1 C SER 232  ? C SER 232  
1160 1 Y 1 C ASP 233  ? C ASP 233  
1161 1 Y 1 C ASN 234  ? C ASN 234  
1162 1 Y 1 C ASP 235  ? C ASP 235  
1163 1 Y 1 C LEU 236  ? C LEU 236  
1164 1 Y 1 C SER 237  ? C SER 237  
1165 1 Y 1 C LEU 238  ? C LEU 238  
1166 1 Y 1 C GLU 239  ? C GLU 239  
1167 1 Y 1 C ASP 240  ? C ASP 240  
1168 1 Y 1 C PHE 241  ? C PHE 241  
1169 1 Y 1 C LYS 242  ? C LYS 242  
1170 1 Y 1 C GLY 243  ? C GLY 243  
1171 1 Y 1 C GLU 244  ? C GLU 244  
1172 1 Y 1 C ASN 245  ? C ASN 245  
1173 1 Y 1 C LYS 246  ? C LYS 246  
1174 1 Y 1 C TYR 247  ? C TYR 247  
1175 1 Y 1 C PHE 248  ? C PHE 248  
1176 1 Y 1 C GLN 249  ? C GLN 249  
1177 1 Y 1 C GLY 250  ? C GLY 250  
1178 1 Y 1 C HIS 251  ? C HIS 251  
1179 1 Y 1 C HIS 252  ? C HIS 252  
1180 1 Y 1 C HIS 253  ? C HIS 253  
1181 1 Y 1 C HIS 254  ? C HIS 254  
1182 1 Y 1 C HIS 255  ? C HIS 255  
1183 1 Y 1 C HIS 256  ? C HIS 256  
1184 1 Y 1 D MET 1    ? D MET 1    
1185 1 Y 1 D GLU 2    ? D GLU 2    
1186 1 Y 1 D LYS 3    ? D LYS 3    
1187 1 Y 1 D PHE 4    ? D PHE 4    
1188 1 Y 1 D ALA 5    ? D ALA 5    
1189 1 Y 1 D PRO 6    ? D PRO 6    
1190 1 Y 1 D GLU 7    ? D GLU 7    
1191 1 Y 1 D PHE 8    ? D PHE 8    
1192 1 Y 1 D HIS 9    ? D HIS 9    
1193 1 Y 1 D GLY 10   ? D GLY 10   
1194 1 Y 1 D GLU 11   ? D GLU 11   
1195 1 Y 1 D ASP 12   ? D ASP 12   
1196 1 Y 1 D ALA 13   ? D ALA 13   
1197 1 Y 1 D ASN 14   ? D ASN 14   
1198 1 Y 1 D ASN 15   ? D ASN 15   
1199 1 Y 1 D ARG 16   ? D ARG 16   
1200 1 Y 1 D ALA 17   ? D ALA 17   
1201 1 Y 1 D THR 18   ? D THR 18   
1202 1 Y 1 D LYS 19   ? D LYS 19   
1203 1 Y 1 D PHE 20   ? D PHE 20   
1204 1 Y 1 D LEU 21   ? D LEU 21   
1205 1 Y 1 D GLU 22   ? D GLU 22   
1206 1 Y 1 D SER 23   ? D SER 23   
1207 1 Y 1 D ILE 24   ? D ILE 24   
1208 1 Y 1 D LYS 25   ? D LYS 25   
1209 1 Y 1 D GLY 26   ? D GLY 26   
1210 1 Y 1 D LYS 27   ? D LYS 27   
1211 1 Y 1 D PHE 28   ? D PHE 28   
1212 1 Y 1 D THR 29   ? D THR 29   
1213 1 Y 1 D SER 30   ? D SER 30   
1214 1 Y 1 D PRO 31   ? D PRO 31   
1215 1 Y 1 D LYS 32   ? D LYS 32   
1216 1 Y 1 D ASP 33   ? D ASP 33   
1217 1 Y 1 D PRO 34   ? D PRO 34   
1218 1 Y 1 D LYS 35   ? D LYS 35   
1219 1 Y 1 D LYS 36   ? D LYS 36   
1220 1 Y 1 D LYS 37   ? D LYS 37   
1221 1 Y 1 D ASP 38   ? D ASP 38   
1222 1 Y 1 D SER 39   ? D SER 39   
1223 1 Y 1 D ILE 40   ? D ILE 40   
1224 1 Y 1 D ILE 41   ? D ILE 41   
1225 1 Y 1 D SER 42   ? D SER 42   
1226 1 Y 1 D VAL 43   ? D VAL 43   
1227 1 Y 1 D ASN 44   ? D ASN 44   
1228 1 Y 1 D SER 45   ? D SER 45   
1229 1 Y 1 D ILE 46   ? D ILE 46   
1230 1 Y 1 D ASP 47   ? D ASP 47   
1231 1 Y 1 D ILE 48   ? D ILE 48   
1232 1 Y 1 D GLU 49   ? D GLU 49   
1233 1 Y 1 D VAL 50   ? D VAL 50   
1234 1 Y 1 D THR 51   ? D THR 51   
1235 1 Y 1 D LYS 52   ? D LYS 52   
1236 1 Y 1 D GLU 53   ? D GLU 53   
1237 1 Y 1 D SER 54   ? D SER 54   
1238 1 Y 1 D PRO 55   ? D PRO 55   
1239 1 Y 1 D ILE 56   ? D ILE 56   
1240 1 Y 1 D THR 57   ? D THR 57   
1241 1 Y 1 D SER 58   ? D SER 58   
1242 1 Y 1 D ASN 59   ? D ASN 59   
1243 1 Y 1 D SER 60   ? D SER 60   
1244 1 Y 1 D THR 61   ? D THR 61   
1245 1 Y 1 D ILE 62   ? D ILE 62   
1246 1 Y 1 D ILE 63   ? D ILE 63   
1247 1 Y 1 D ASN 64   ? D ASN 64   
1248 1 Y 1 D PRO 65   ? D PRO 65   
1249 1 Y 1 D THR 66   ? D THR 66   
1250 1 Y 1 D ASN 67   ? D ASN 67   
1251 1 Y 1 D GLU 68   ? D GLU 68   
1252 1 Y 1 D THR 69   ? D THR 69   
1253 1 Y 1 D ASP 70   ? D ASP 70   
1254 1 Y 1 D ASP 71   ? D ASP 71   
1255 1 Y 1 D THR 72   ? D THR 72   
1256 1 Y 1 D ALA 73   ? D ALA 73   
1257 1 Y 1 D GLY 74   ? D GLY 74   
1258 1 Y 1 D ASN 75   ? D ASN 75   
1259 1 Y 1 D LYS 76   ? D LYS 76   
1260 1 Y 1 D PRO 77   ? D PRO 77   
1261 1 Y 1 D ASN 78   ? D ASN 78   
1262 1 Y 1 D TYR 79   ? D TYR 79   
1263 1 Y 1 D GLN 80   ? D GLN 80   
1264 1 Y 1 D ARG 81   ? D ARG 81   
1265 1 Y 1 D LYS 82   ? D LYS 82   
1266 1 Y 1 D PRO 83   ? D PRO 83   
1267 1 Y 1 D LEU 84   ? D LEU 84   
1268 1 Y 1 D VAL 85   ? D VAL 85   
1269 1 Y 1 D SER 86   ? D SER 86   
1270 1 Y 1 D PHE 87   ? D PHE 87   
1271 1 Y 1 D LYS 88   ? D LYS 88   
1272 1 Y 1 D GLU 89   ? D GLU 89   
1273 1 Y 1 D ASP 90   ? D ASP 90   
1274 1 Y 1 D PRO 91   ? D PRO 91   
1275 1 Y 1 D THR 92   ? D THR 92   
1276 1 Y 1 D PRO 93   ? D PRO 93   
1277 1 Y 1 D SER 94   ? D SER 94   
1278 1 Y 1 D ASP 95   ? D ASP 95   
1279 1 Y 1 D ASN 96   ? D ASN 96   
1280 1 Y 1 D PRO 97   ? D PRO 97   
1281 1 Y 1 D PHE 98   ? D PHE 98   
1282 1 Y 1 D SER 99   ? D SER 99   
1283 1 Y 1 D LYS 100  ? D LYS 100  
1284 1 Y 1 D LEU 101  ? D LEU 101  
1285 1 Y 1 D TYR 102  ? D TYR 102  
1286 1 Y 1 D LYS 103  ? D LYS 103  
1287 1 Y 1 D GLU 104  ? D GLU 104  
1288 1 Y 1 D THR 105  ? D THR 105  
1289 1 Y 1 D ILE 106  ? D ILE 106  
1290 1 Y 1 D GLU 107  ? D GLU 107  
1291 1 Y 1 D THR 108  ? D THR 108  
1292 1 Y 1 D PHE 109  ? D PHE 109  
1293 1 Y 1 D ASP 110  ? D ASP 110  
1294 1 Y 1 D ASN 111  ? D ASN 111  
1295 1 Y 1 D ASN 112  ? D ASN 112  
1296 1 Y 1 D GLU 113  ? D GLU 113  
1297 1 Y 1 D GLU 114  ? D GLU 114  
1298 1 Y 1 D GLU 115  ? D GLU 115  
1299 1 Y 1 D SER 116  ? D SER 116  
1300 1 Y 1 D SER 117  ? D SER 117  
1301 1 Y 1 D TYR 118  ? D TYR 118  
1302 1 Y 1 D SER 119  ? D SER 119  
1303 1 Y 1 D TYR 120  ? D TYR 120  
1304 1 Y 1 D GLU 121  ? D GLU 121  
1305 1 Y 1 D GLU 122  ? D GLU 122  
1306 1 Y 1 D ILE 123  ? D ILE 123  
1307 1 Y 1 D ASN 124  ? D ASN 124  
1308 1 Y 1 D ASP 125  ? D ASP 125  
1309 1 Y 1 D GLN 126  ? D GLN 126  
1310 1 Y 1 D THR 127  ? D THR 127  
1311 1 Y 1 D ASN 128  ? D ASN 128  
1312 1 Y 1 D ASP 129  ? D ASP 129  
1313 1 Y 1 D ALA 185  ? D ALA 185  
1314 1 Y 1 D LEU 186  ? D LEU 186  
1315 1 Y 1 D MET 187  ? D MET 187  
1316 1 Y 1 D THR 188  ? D THR 188  
1317 1 Y 1 D ASN 189  ? D ASN 189  
1318 1 Y 1 D ASP 190  ? D ASP 190  
1319 1 Y 1 D ARG 191  ? D ARG 191  
1320 1 Y 1 D LEU 192  ? D LEU 192  
1321 1 Y 1 D GLU 193  ? D GLU 193  
1322 1 Y 1 D ALA 194  ? D ALA 194  
1323 1 Y 1 D MET 195  ? D MET 195  
1324 1 Y 1 D ALA 196  ? D ALA 196  
1325 1 Y 1 D ARG 197  ? D ARG 197  
1326 1 Y 1 D LEU 198  ? D LEU 198  
1327 1 Y 1 D ARG 199  ? D ARG 199  
1328 1 Y 1 D ASN 200  ? D ASN 200  
1329 1 Y 1 D GLU 201  ? D GLU 201  
1330 1 Y 1 D GLU 202  ? D GLU 202  
1331 1 Y 1 D SER 203  ? D SER 203  
1332 1 Y 1 D GLU 204  ? D GLU 204  
1333 1 Y 1 D LYS 205  ? D LYS 205  
1334 1 Y 1 D MET 206  ? D MET 206  
1335 1 Y 1 D ALA 207  ? D ALA 207  
1336 1 Y 1 D LYS 208  ? D LYS 208  
1337 1 Y 1 D ASP 209  ? D ASP 209  
1338 1 Y 1 D THR 210  ? D THR 210  
1339 1 Y 1 D SER 211  ? D SER 211  
1340 1 Y 1 D ASP 212  ? D ASP 212  
1341 1 Y 1 D GLU 213  ? D GLU 213  
1342 1 Y 1 D VAL 214  ? D VAL 214  
1343 1 Y 1 D SER 215  ? D SER 215  
1344 1 Y 1 D LEU 216  ? D LEU 216  
1345 1 Y 1 D ASN 217  ? D ASN 217  
1346 1 Y 1 D PRO 218  ? D PRO 218  
1347 1 Y 1 D THR 219  ? D THR 219  
1348 1 Y 1 D SER 220  ? D SER 220  
1349 1 Y 1 D GLU 221  ? D GLU 221  
1350 1 Y 1 D LYS 222  ? D LYS 222  
1351 1 Y 1 D LEU 223  ? D LEU 223  
1352 1 Y 1 D ASN 224  ? D ASN 224  
1353 1 Y 1 D ASN 225  ? D ASN 225  
1354 1 Y 1 D LEU 226  ? D LEU 226  
1355 1 Y 1 D LEU 227  ? D LEU 227  
1356 1 Y 1 D GLU 228  ? D GLU 228  
1357 1 Y 1 D GLY 229  ? D GLY 229  
1358 1 Y 1 D ASN 230  ? D ASN 230  
1359 1 Y 1 D ASP 231  ? D ASP 231  
1360 1 Y 1 D SER 232  ? D SER 232  
1361 1 Y 1 D ASP 233  ? D ASP 233  
1362 1 Y 1 D ASN 234  ? D ASN 234  
1363 1 Y 1 D ASP 235  ? D ASP 235  
1364 1 Y 1 D LEU 236  ? D LEU 236  
1365 1 Y 1 D SER 237  ? D SER 237  
1366 1 Y 1 D LEU 238  ? D LEU 238  
1367 1 Y 1 D GLU 239  ? D GLU 239  
1368 1 Y 1 D ASP 240  ? D ASP 240  
1369 1 Y 1 D PHE 241  ? D PHE 241  
1370 1 Y 1 D LYS 242  ? D LYS 242  
1371 1 Y 1 D GLY 243  ? D GLY 243  
1372 1 Y 1 D GLU 244  ? D GLU 244  
1373 1 Y 1 D ASN 245  ? D ASN 245  
1374 1 Y 1 D LYS 246  ? D LYS 246  
1375 1 Y 1 D TYR 247  ? D TYR 247  
1376 1 Y 1 D PHE 248  ? D PHE 248  
1377 1 Y 1 D GLN 249  ? D GLN 249  
1378 1 Y 1 D GLY 250  ? D GLY 250  
1379 1 Y 1 D HIS 251  ? D HIS 251  
1380 1 Y 1 D HIS 252  ? D HIS 252  
1381 1 Y 1 D HIS 253  ? D HIS 253  
1382 1 Y 1 D HIS 254  ? D HIS 254  
1383 1 Y 1 D HIS 255  ? D HIS 255  
1384 1 Y 1 D HIS 256  ? D HIS 256  
1385 1 Y 1 E MET 1    ? E MET 1    
1386 1 Y 1 E GLU 2    ? E GLU 2    
1387 1 Y 1 E LYS 3    ? E LYS 3    
1388 1 Y 1 E PHE 4    ? E PHE 4    
1389 1 Y 1 E ALA 5    ? E ALA 5    
1390 1 Y 1 E PRO 6    ? E PRO 6    
1391 1 Y 1 E GLU 7    ? E GLU 7    
1392 1 Y 1 E PHE 8    ? E PHE 8    
1393 1 Y 1 E HIS 9    ? E HIS 9    
1394 1 Y 1 E GLY 10   ? E GLY 10   
1395 1 Y 1 E GLU 11   ? E GLU 11   
1396 1 Y 1 E ASP 12   ? E ASP 12   
1397 1 Y 1 E ALA 13   ? E ALA 13   
1398 1 Y 1 E ASN 14   ? E ASN 14   
1399 1 Y 1 E ASN 15   ? E ASN 15   
1400 1 Y 1 E ARG 16   ? E ARG 16   
1401 1 Y 1 E ALA 17   ? E ALA 17   
1402 1 Y 1 E THR 18   ? E THR 18   
1403 1 Y 1 E LYS 19   ? E LYS 19   
1404 1 Y 1 E PHE 20   ? E PHE 20   
1405 1 Y 1 E LEU 21   ? E LEU 21   
1406 1 Y 1 E GLU 22   ? E GLU 22   
1407 1 Y 1 E SER 23   ? E SER 23   
1408 1 Y 1 E ILE 24   ? E ILE 24   
1409 1 Y 1 E LYS 25   ? E LYS 25   
1410 1 Y 1 E GLY 26   ? E GLY 26   
1411 1 Y 1 E LYS 27   ? E LYS 27   
1412 1 Y 1 E PHE 28   ? E PHE 28   
1413 1 Y 1 E THR 29   ? E THR 29   
1414 1 Y 1 E SER 30   ? E SER 30   
1415 1 Y 1 E PRO 31   ? E PRO 31   
1416 1 Y 1 E LYS 32   ? E LYS 32   
1417 1 Y 1 E ASP 33   ? E ASP 33   
1418 1 Y 1 E PRO 34   ? E PRO 34   
1419 1 Y 1 E LYS 35   ? E LYS 35   
1420 1 Y 1 E LYS 36   ? E LYS 36   
1421 1 Y 1 E LYS 37   ? E LYS 37   
1422 1 Y 1 E ASP 38   ? E ASP 38   
1423 1 Y 1 E SER 39   ? E SER 39   
1424 1 Y 1 E ILE 40   ? E ILE 40   
1425 1 Y 1 E ILE 41   ? E ILE 41   
1426 1 Y 1 E SER 42   ? E SER 42   
1427 1 Y 1 E VAL 43   ? E VAL 43   
1428 1 Y 1 E ASN 44   ? E ASN 44   
1429 1 Y 1 E SER 45   ? E SER 45   
1430 1 Y 1 E ILE 46   ? E ILE 46   
1431 1 Y 1 E ASP 47   ? E ASP 47   
1432 1 Y 1 E ILE 48   ? E ILE 48   
1433 1 Y 1 E GLU 49   ? E GLU 49   
1434 1 Y 1 E VAL 50   ? E VAL 50   
1435 1 Y 1 E THR 51   ? E THR 51   
1436 1 Y 1 E LYS 52   ? E LYS 52   
1437 1 Y 1 E GLU 53   ? E GLU 53   
1438 1 Y 1 E SER 54   ? E SER 54   
1439 1 Y 1 E PRO 55   ? E PRO 55   
1440 1 Y 1 E ILE 56   ? E ILE 56   
1441 1 Y 1 E THR 57   ? E THR 57   
1442 1 Y 1 E SER 58   ? E SER 58   
1443 1 Y 1 E ASN 59   ? E ASN 59   
1444 1 Y 1 E SER 60   ? E SER 60   
1445 1 Y 1 E THR 61   ? E THR 61   
1446 1 Y 1 E ILE 62   ? E ILE 62   
1447 1 Y 1 E ILE 63   ? E ILE 63   
1448 1 Y 1 E ASN 64   ? E ASN 64   
1449 1 Y 1 E PRO 65   ? E PRO 65   
1450 1 Y 1 E THR 66   ? E THR 66   
1451 1 Y 1 E ASN 67   ? E ASN 67   
1452 1 Y 1 E GLU 68   ? E GLU 68   
1453 1 Y 1 E THR 69   ? E THR 69   
1454 1 Y 1 E ASP 70   ? E ASP 70   
1455 1 Y 1 E ASP 71   ? E ASP 71   
1456 1 Y 1 E THR 72   ? E THR 72   
1457 1 Y 1 E ALA 73   ? E ALA 73   
1458 1 Y 1 E GLY 74   ? E GLY 74   
1459 1 Y 1 E ASN 75   ? E ASN 75   
1460 1 Y 1 E LYS 76   ? E LYS 76   
1461 1 Y 1 E PRO 77   ? E PRO 77   
1462 1 Y 1 E ASN 78   ? E ASN 78   
1463 1 Y 1 E TYR 79   ? E TYR 79   
1464 1 Y 1 E GLN 80   ? E GLN 80   
1465 1 Y 1 E ARG 81   ? E ARG 81   
1466 1 Y 1 E LYS 82   ? E LYS 82   
1467 1 Y 1 E PRO 83   ? E PRO 83   
1468 1 Y 1 E LEU 84   ? E LEU 84   
1469 1 Y 1 E VAL 85   ? E VAL 85   
1470 1 Y 1 E SER 86   ? E SER 86   
1471 1 Y 1 E PHE 87   ? E PHE 87   
1472 1 Y 1 E LYS 88   ? E LYS 88   
1473 1 Y 1 E GLU 89   ? E GLU 89   
1474 1 Y 1 E ASP 90   ? E ASP 90   
1475 1 Y 1 E PRO 91   ? E PRO 91   
1476 1 Y 1 E THR 92   ? E THR 92   
1477 1 Y 1 E PRO 93   ? E PRO 93   
1478 1 Y 1 E SER 94   ? E SER 94   
1479 1 Y 1 E ASP 95   ? E ASP 95   
1480 1 Y 1 E ASN 96   ? E ASN 96   
1481 1 Y 1 E PRO 97   ? E PRO 97   
1482 1 Y 1 E PHE 98   ? E PHE 98   
1483 1 Y 1 E SER 99   ? E SER 99   
1484 1 Y 1 E LYS 100  ? E LYS 100  
1485 1 Y 1 E LEU 101  ? E LEU 101  
1486 1 Y 1 E TYR 102  ? E TYR 102  
1487 1 Y 1 E LYS 103  ? E LYS 103  
1488 1 Y 1 E GLU 104  ? E GLU 104  
1489 1 Y 1 E THR 105  ? E THR 105  
1490 1 Y 1 E ILE 106  ? E ILE 106  
1491 1 Y 1 E GLU 107  ? E GLU 107  
1492 1 Y 1 E THR 108  ? E THR 108  
1493 1 Y 1 E PHE 109  ? E PHE 109  
1494 1 Y 1 E ASP 110  ? E ASP 110  
1495 1 Y 1 E ASN 111  ? E ASN 111  
1496 1 Y 1 E ASN 112  ? E ASN 112  
1497 1 Y 1 E GLU 113  ? E GLU 113  
1498 1 Y 1 E GLU 114  ? E GLU 114  
1499 1 Y 1 E GLU 115  ? E GLU 115  
1500 1 Y 1 E SER 116  ? E SER 116  
1501 1 Y 1 E SER 117  ? E SER 117  
1502 1 Y 1 E TYR 118  ? E TYR 118  
1503 1 Y 1 E SER 119  ? E SER 119  
1504 1 Y 1 E TYR 120  ? E TYR 120  
1505 1 Y 1 E GLU 121  ? E GLU 121  
1506 1 Y 1 E GLU 122  ? E GLU 122  
1507 1 Y 1 E ILE 123  ? E ILE 123  
1508 1 Y 1 E ASN 124  ? E ASN 124  
1509 1 Y 1 E ASP 125  ? E ASP 125  
1510 1 Y 1 E GLN 126  ? E GLN 126  
1511 1 Y 1 E THR 127  ? E THR 127  
1512 1 Y 1 E ASN 128  ? E ASN 128  
1513 1 Y 1 E ASP 129  ? E ASP 129  
1514 1 Y 1 E ASN 130  ? E ASN 130  
1515 1 Y 1 E ASN 200  ? E ASN 200  
1516 1 Y 1 E GLU 201  ? E GLU 201  
1517 1 Y 1 E GLU 202  ? E GLU 202  
1518 1 Y 1 E SER 203  ? E SER 203  
1519 1 Y 1 E GLU 204  ? E GLU 204  
1520 1 Y 1 E LYS 205  ? E LYS 205  
1521 1 Y 1 E MET 206  ? E MET 206  
1522 1 Y 1 E ALA 207  ? E ALA 207  
1523 1 Y 1 E LYS 208  ? E LYS 208  
1524 1 Y 1 E ASP 209  ? E ASP 209  
1525 1 Y 1 E THR 210  ? E THR 210  
1526 1 Y 1 E SER 211  ? E SER 211  
1527 1 Y 1 E ASP 212  ? E ASP 212  
1528 1 Y 1 E GLU 213  ? E GLU 213  
1529 1 Y 1 E VAL 214  ? E VAL 214  
1530 1 Y 1 E SER 215  ? E SER 215  
1531 1 Y 1 E LEU 216  ? E LEU 216  
1532 1 Y 1 E ASN 217  ? E ASN 217  
1533 1 Y 1 E PRO 218  ? E PRO 218  
1534 1 Y 1 E THR 219  ? E THR 219  
1535 1 Y 1 E SER 220  ? E SER 220  
1536 1 Y 1 E GLU 221  ? E GLU 221  
1537 1 Y 1 E LYS 222  ? E LYS 222  
1538 1 Y 1 E LEU 223  ? E LEU 223  
1539 1 Y 1 E ASN 224  ? E ASN 224  
1540 1 Y 1 E ASN 225  ? E ASN 225  
1541 1 Y 1 E LEU 226  ? E LEU 226  
1542 1 Y 1 E LEU 227  ? E LEU 227  
1543 1 Y 1 E GLU 228  ? E GLU 228  
1544 1 Y 1 E GLY 229  ? E GLY 229  
1545 1 Y 1 E ASN 230  ? E ASN 230  
1546 1 Y 1 E ASP 231  ? E ASP 231  
1547 1 Y 1 E SER 232  ? E SER 232  
1548 1 Y 1 E ASP 233  ? E ASP 233  
1549 1 Y 1 E ASN 234  ? E ASN 234  
1550 1 Y 1 E ASP 235  ? E ASP 235  
1551 1 Y 1 E LEU 236  ? E LEU 236  
1552 1 Y 1 E SER 237  ? E SER 237  
1553 1 Y 1 E LEU 238  ? E LEU 238  
1554 1 Y 1 E GLU 239  ? E GLU 239  
1555 1 Y 1 E ASP 240  ? E ASP 240  
1556 1 Y 1 E PHE 241  ? E PHE 241  
1557 1 Y 1 E LYS 242  ? E LYS 242  
1558 1 Y 1 E GLY 243  ? E GLY 243  
1559 1 Y 1 E GLU 244  ? E GLU 244  
1560 1 Y 1 E ASN 245  ? E ASN 245  
1561 1 Y 1 E LYS 246  ? E LYS 246  
1562 1 Y 1 E TYR 247  ? E TYR 247  
1563 1 Y 1 E PHE 248  ? E PHE 248  
1564 1 Y 1 E GLN 249  ? E GLN 249  
1565 1 Y 1 E GLY 250  ? E GLY 250  
1566 1 Y 1 E HIS 251  ? E HIS 251  
1567 1 Y 1 E HIS 252  ? E HIS 252  
1568 1 Y 1 E HIS 253  ? E HIS 253  
1569 1 Y 1 E HIS 254  ? E HIS 254  
1570 1 Y 1 E HIS 255  ? E HIS 255  
1571 1 Y 1 E HIS 256  ? E HIS 256  
# 
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 
A1AWZ N1   N Y N 1   
A1AWZ N3   N Y N 2   
A1AWZ C4   C Y N 3   
A1AWZ C5   C Y N 4   
A1AWZ C6   C Y N 5   
A1AWZ C7   C Y N 6   
A1AWZ C8   C Y N 7   
A1AWZ C10  C Y N 8   
A1AWZ C13  C N N 9   
A1AWZ C15  C Y N 10  
A1AWZ C17  C Y N 11  
A1AWZ C20  C Y N 12  
A1AWZ C21  C Y N 13  
A1AWZ C22  C Y N 14  
A1AWZ C24  C Y N 15  
A1AWZ C26  C N N 16  
A1AWZ C28  C N N 17  
A1AWZ C1   C N N 18  
A1AWZ O1   O N N 19  
A1AWZ C2   C Y N 20  
A1AWZ N2   N Y N 21  
A1AWZ O2   O N N 22  
A1AWZ C3   C Y N 23  
A1AWZ O3   O N N 24  
A1AWZ N4   N Y N 25  
A1AWZ N5   N Y N 26  
A1AWZ C9   C Y N 27  
A1AWZ C11  C Y N 28  
A1AWZ C12  C Y N 29  
A1AWZ C14  C N S 30  
A1AWZ C16  C Y N 31  
A1AWZ C18  C Y N 32  
A1AWZ C19  C Y N 33  
A1AWZ C23  C Y N 34  
A1AWZ C25  C Y N 35  
A1AWZ C27  C N N 36  
A1AWZ C29  C N N 37  
A1AWZ F1   F N N 38  
A1AWZ F2   F N N 39  
A1AWZ F3   F N N 40  
A1AWZ F4   F N N 41  
A1AWZ F5   F N N 42  
A1AWZ H1   H N N 43  
A1AWZ H2   H N N 44  
A1AWZ H3   H N N 45  
A1AWZ H4   H N N 46  
A1AWZ H5   H N N 47  
A1AWZ H6   H N N 48  
A1AWZ H7   H N N 49  
A1AWZ H8   H N N 50  
A1AWZ H9   H N N 51  
A1AWZ H10  H N N 52  
A1AWZ H11  H N N 53  
A1AWZ H12  H N N 54  
A1AWZ H13  H N N 55  
A1AWZ H14  H N N 56  
A1AWZ H15  H N N 57  
A1AWZ H16  H N N 58  
A1AWZ H17  H N N 59  
A1AWZ H18  H N N 60  
A1AWZ H19  H N N 61  
A1AWZ H20  H N N 62  
A1AWZ H21  H N N 63  
A1AWZ H22  H N N 64  
A1AWZ H23  H N N 65  
A1AWZ H24  H N N 66  
ALA   N    N N N 67  
ALA   CA   C N S 68  
ALA   C    C N N 69  
ALA   O    O N N 70  
ALA   CB   C N N 71  
ALA   OXT  O N N 72  
ALA   H    H N N 73  
ALA   H2   H N N 74  
ALA   HA   H N N 75  
ALA   HB1  H N N 76  
ALA   HB2  H N N 77  
ALA   HB3  H N N 78  
ALA   HXT  H N N 79  
ARG   N    N N N 80  
ARG   CA   C N S 81  
ARG   C    C N N 82  
ARG   O    O N N 83  
ARG   CB   C N N 84  
ARG   CG   C N N 85  
ARG   CD   C N N 86  
ARG   NE   N N N 87  
ARG   CZ   C N N 88  
ARG   NH1  N N N 89  
ARG   NH2  N N N 90  
ARG   OXT  O N N 91  
ARG   H    H N N 92  
ARG   H2   H N N 93  
ARG   HA   H N N 94  
ARG   HB2  H N N 95  
ARG   HB3  H N N 96  
ARG   HG2  H N N 97  
ARG   HG3  H N N 98  
ARG   HD2  H N N 99  
ARG   HD3  H N N 100 
ARG   HE   H N N 101 
ARG   HH11 H N N 102 
ARG   HH12 H N N 103 
ARG   HH21 H N N 104 
ARG   HH22 H N N 105 
ARG   HXT  H N N 106 
ASN   N    N N N 107 
ASN   CA   C N S 108 
ASN   C    C N N 109 
ASN   O    O N N 110 
ASN   CB   C N N 111 
ASN   CG   C N N 112 
ASN   OD1  O N N 113 
ASN   ND2  N N N 114 
ASN   OXT  O N N 115 
ASN   H    H N N 116 
ASN   H2   H N N 117 
ASN   HA   H N N 118 
ASN   HB2  H N N 119 
ASN   HB3  H N N 120 
ASN   HD21 H N N 121 
ASN   HD22 H N N 122 
ASN   HXT  H N N 123 
ASP   N    N N N 124 
ASP   CA   C N S 125 
ASP   C    C N N 126 
ASP   O    O N N 127 
ASP   CB   C N N 128 
ASP   CG   C N N 129 
ASP   OD1  O N N 130 
ASP   OD2  O N N 131 
ASP   OXT  O N N 132 
ASP   H    H N N 133 
ASP   H2   H N N 134 
ASP   HA   H N N 135 
ASP   HB2  H N N 136 
ASP   HB3  H N N 137 
ASP   HD2  H N N 138 
ASP   HXT  H N N 139 
CYS   N    N N N 140 
CYS   CA   C N R 141 
CYS   C    C N N 142 
CYS   O    O N N 143 
CYS   CB   C N N 144 
CYS   SG   S N N 145 
CYS   OXT  O N N 146 
CYS   H    H N N 147 
CYS   H2   H N N 148 
CYS   HA   H N N 149 
CYS   HB2  H N N 150 
CYS   HB3  H N N 151 
CYS   HG   H N N 152 
CYS   HXT  H N N 153 
GLN   N    N N N 154 
GLN   CA   C N S 155 
GLN   C    C N N 156 
GLN   O    O N N 157 
GLN   CB   C N N 158 
GLN   CG   C N N 159 
GLN   CD   C N N 160 
GLN   OE1  O N N 161 
GLN   NE2  N N N 162 
GLN   OXT  O N N 163 
GLN   H    H N N 164 
GLN   H2   H N N 165 
GLN   HA   H N N 166 
GLN   HB2  H N N 167 
GLN   HB3  H N N 168 
GLN   HG2  H N N 169 
GLN   HG3  H N N 170 
GLN   HE21 H N N 171 
GLN   HE22 H N N 172 
GLN   HXT  H N N 173 
GLU   N    N N N 174 
GLU   CA   C N S 175 
GLU   C    C N N 176 
GLU   O    O N N 177 
GLU   CB   C N N 178 
GLU   CG   C N N 179 
GLU   CD   C N N 180 
GLU   OE1  O N N 181 
GLU   OE2  O N N 182 
GLU   OXT  O N N 183 
GLU   H    H N N 184 
GLU   H2   H N N 185 
GLU   HA   H N N 186 
GLU   HB2  H N N 187 
GLU   HB3  H N N 188 
GLU   HG2  H N N 189 
GLU   HG3  H N N 190 
GLU   HE2  H N N 191 
GLU   HXT  H N N 192 
GLY   N    N N N 193 
GLY   CA   C N N 194 
GLY   C    C N N 195 
GLY   O    O N N 196 
GLY   OXT  O N N 197 
GLY   H    H N N 198 
GLY   H2   H N N 199 
GLY   HA2  H N N 200 
GLY   HA3  H N N 201 
GLY   HXT  H N N 202 
HIS   N    N N N 203 
HIS   CA   C N S 204 
HIS   C    C N N 205 
HIS   O    O N N 206 
HIS   CB   C N N 207 
HIS   CG   C Y N 208 
HIS   ND1  N Y N 209 
HIS   CD2  C Y N 210 
HIS   CE1  C Y N 211 
HIS   NE2  N Y N 212 
HIS   OXT  O N N 213 
HIS   H    H N N 214 
HIS   H2   H N N 215 
HIS   HA   H N N 216 
HIS   HB2  H N N 217 
HIS   HB3  H N N 218 
HIS   HD1  H N N 219 
HIS   HD2  H N N 220 
HIS   HE1  H N N 221 
HIS   HE2  H N N 222 
HIS   HXT  H N N 223 
ILE   N    N N N 224 
ILE   CA   C N S 225 
ILE   C    C N N 226 
ILE   O    O N N 227 
ILE   CB   C N S 228 
ILE   CG1  C N N 229 
ILE   CG2  C N N 230 
ILE   CD1  C N N 231 
ILE   OXT  O N N 232 
ILE   H    H N N 233 
ILE   H2   H N N 234 
ILE   HA   H N N 235 
ILE   HB   H N N 236 
ILE   HG12 H N N 237 
ILE   HG13 H N N 238 
ILE   HG21 H N N 239 
ILE   HG22 H N N 240 
ILE   HG23 H N N 241 
ILE   HD11 H N N 242 
ILE   HD12 H N N 243 
ILE   HD13 H N N 244 
ILE   HXT  H N N 245 
LEU   N    N N N 246 
LEU   CA   C N S 247 
LEU   C    C N N 248 
LEU   O    O N N 249 
LEU   CB   C N N 250 
LEU   CG   C N N 251 
LEU   CD1  C N N 252 
LEU   CD2  C N N 253 
LEU   OXT  O N N 254 
LEU   H    H N N 255 
LEU   H2   H N N 256 
LEU   HA   H N N 257 
LEU   HB2  H N N 258 
LEU   HB3  H N N 259 
LEU   HG   H N N 260 
LEU   HD11 H N N 261 
LEU   HD12 H N N 262 
LEU   HD13 H N N 263 
LEU   HD21 H N N 264 
LEU   HD22 H N N 265 
LEU   HD23 H N N 266 
LEU   HXT  H N N 267 
LYS   N    N N N 268 
LYS   CA   C N S 269 
LYS   C    C N N 270 
LYS   O    O N N 271 
LYS   CB   C N N 272 
LYS   CG   C N N 273 
LYS   CD   C N N 274 
LYS   CE   C N N 275 
LYS   NZ   N N N 276 
LYS   OXT  O N N 277 
LYS   H    H N N 278 
LYS   H2   H N N 279 
LYS   HA   H N N 280 
LYS   HB2  H N N 281 
LYS   HB3  H N N 282 
LYS   HG2  H N N 283 
LYS   HG3  H N N 284 
LYS   HD2  H N N 285 
LYS   HD3  H N N 286 
LYS   HE2  H N N 287 
LYS   HE3  H N N 288 
LYS   HZ1  H N N 289 
LYS   HZ2  H N N 290 
LYS   HZ3  H N N 291 
LYS   HXT  H N N 292 
MET   N    N N N 293 
MET   CA   C N S 294 
MET   C    C N N 295 
MET   O    O N N 296 
MET   CB   C N N 297 
MET   CG   C N N 298 
MET   SD   S N N 299 
MET   CE   C N N 300 
MET   OXT  O N N 301 
MET   H    H N N 302 
MET   H2   H N N 303 
MET   HA   H N N 304 
MET   HB2  H N N 305 
MET   HB3  H N N 306 
MET   HG2  H N N 307 
MET   HG3  H N N 308 
MET   HE1  H N N 309 
MET   HE2  H N N 310 
MET   HE3  H N N 311 
MET   HXT  H N N 312 
PHE   N    N N N 313 
PHE   CA   C N S 314 
PHE   C    C N N 315 
PHE   O    O N N 316 
PHE   CB   C N N 317 
PHE   CG   C Y N 318 
PHE   CD1  C Y N 319 
PHE   CD2  C Y N 320 
PHE   CE1  C Y N 321 
PHE   CE2  C Y N 322 
PHE   CZ   C Y N 323 
PHE   OXT  O N N 324 
PHE   H    H N N 325 
PHE   H2   H N N 326 
PHE   HA   H N N 327 
PHE   HB2  H N N 328 
PHE   HB3  H N N 329 
PHE   HD1  H N N 330 
PHE   HD2  H N N 331 
PHE   HE1  H N N 332 
PHE   HE2  H N N 333 
PHE   HZ   H N N 334 
PHE   HXT  H N N 335 
PRO   N    N N N 336 
PRO   CA   C N S 337 
PRO   C    C N N 338 
PRO   O    O N N 339 
PRO   CB   C N N 340 
PRO   CG   C N N 341 
PRO   CD   C N N 342 
PRO   OXT  O N N 343 
PRO   H    H N N 344 
PRO   HA   H N N 345 
PRO   HB2  H N N 346 
PRO   HB3  H N N 347 
PRO   HG2  H N N 348 
PRO   HG3  H N N 349 
PRO   HD2  H N N 350 
PRO   HD3  H N N 351 
PRO   HXT  H N N 352 
SER   N    N N N 353 
SER   CA   C N S 354 
SER   C    C N N 355 
SER   O    O N N 356 
SER   CB   C N N 357 
SER   OG   O N N 358 
SER   OXT  O N N 359 
SER   H    H N N 360 
SER   H2   H N N 361 
SER   HA   H N N 362 
SER   HB2  H N N 363 
SER   HB3  H N N 364 
SER   HG   H N N 365 
SER   HXT  H N N 366 
THR   N    N N N 367 
THR   CA   C N S 368 
THR   C    C N N 369 
THR   O    O N N 370 
THR   CB   C N R 371 
THR   OG1  O N N 372 
THR   CG2  C N N 373 
THR   OXT  O N N 374 
THR   H    H N N 375 
THR   H2   H N N 376 
THR   HA   H N N 377 
THR   HB   H N N 378 
THR   HG1  H N N 379 
THR   HG21 H N N 380 
THR   HG22 H N N 381 
THR   HG23 H N N 382 
THR   HXT  H N N 383 
TRP   N    N N N 384 
TRP   CA   C N S 385 
TRP   C    C N N 386 
TRP   O    O N N 387 
TRP   CB   C N N 388 
TRP   CG   C Y N 389 
TRP   CD1  C Y N 390 
TRP   CD2  C Y N 391 
TRP   NE1  N Y N 392 
TRP   CE2  C Y N 393 
TRP   CE3  C Y N 394 
TRP   CZ2  C Y N 395 
TRP   CZ3  C Y N 396 
TRP   CH2  C Y N 397 
TRP   OXT  O N N 398 
TRP   H    H N N 399 
TRP   H2   H N N 400 
TRP   HA   H N N 401 
TRP   HB2  H N N 402 
TRP   HB3  H N N 403 
TRP   HD1  H N N 404 
TRP   HE1  H N N 405 
TRP   HE3  H N N 406 
TRP   HZ2  H N N 407 
TRP   HZ3  H N N 408 
TRP   HH2  H N N 409 
TRP   HXT  H N N 410 
TYR   N    N N N 411 
TYR   CA   C N S 412 
TYR   C    C N N 413 
TYR   O    O N N 414 
TYR   CB   C N N 415 
TYR   CG   C Y N 416 
TYR   CD1  C Y N 417 
TYR   CD2  C Y N 418 
TYR   CE1  C Y N 419 
TYR   CE2  C Y N 420 
TYR   CZ   C Y N 421 
TYR   OH   O N N 422 
TYR   OXT  O N N 423 
TYR   H    H N N 424 
TYR   H2   H N N 425 
TYR   HA   H N N 426 
TYR   HB2  H N N 427 
TYR   HB3  H N N 428 
TYR   HD1  H N N 429 
TYR   HD2  H N N 430 
TYR   HE1  H N N 431 
TYR   HE2  H N N 432 
TYR   HH   H N N 433 
TYR   HXT  H N N 434 
VAL   N    N N N 435 
VAL   CA   C N S 436 
VAL   C    C N N 437 
VAL   O    O N N 438 
VAL   CB   C N N 439 
VAL   CG1  C N N 440 
VAL   CG2  C N N 441 
VAL   OXT  O N N 442 
VAL   H    H N N 443 
VAL   H2   H N N 444 
VAL   HA   H N N 445 
VAL   HB   H N N 446 
VAL   HG11 H N N 447 
VAL   HG12 H N N 448 
VAL   HG13 H N N 449 
VAL   HG21 H N N 450 
VAL   HG22 H N N 451 
VAL   HG23 H N N 452 
VAL   HXT  H N N 453 
# 
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 
A1AWZ C22 C21  doub Y N 1   
A1AWZ C22 C23  sing Y N 2   
A1AWZ F2  C23  sing N N 3   
A1AWZ O3  C26  sing N N 4   
A1AWZ C21 C20  sing Y N 5   
A1AWZ F1  C18  sing N N 6   
A1AWZ C23 C24  doub Y N 7   
A1AWZ C26 C27  sing N N 8   
A1AWZ C26 C28  sing N N 9   
A1AWZ C26 C17  sing N N 10  
A1AWZ C20 C19  sing N N 11  
A1AWZ C20 C25  doub Y N 12  
A1AWZ C18 C19  doub Y N 13  
A1AWZ C18 C17  sing Y N 14  
A1AWZ C24 C25  sing Y N 15  
A1AWZ C19 N3   sing Y N 16  
A1AWZ C17 C16  doub Y N 17  
A1AWZ N3  C15  doub Y N 18  
A1AWZ C16 C15  sing Y N 19  
A1AWZ C15 C14  sing N N 20  
A1AWZ F3  C29  sing N N 21  
A1AWZ F5  C29  sing N N 22  
A1AWZ C14 C29  sing N N 23  
A1AWZ C14 C13  sing N N 24  
A1AWZ C14 O2   sing N N 25  
A1AWZ C29 F4   sing N N 26  
A1AWZ C13 N2   sing N N 27  
A1AWZ N2  N4   sing Y N 28  
A1AWZ N2  C12  sing Y N 29  
A1AWZ N4  N5   doub Y N 30  
A1AWZ C12 C11  doub Y N 31  
A1AWZ N5  C11  sing Y N 32  
A1AWZ C11 C4   sing N N 33  
A1AWZ C4  C5   doub Y N 34  
A1AWZ C4  C3   sing Y N 35  
A1AWZ C5  C6   sing Y N 36  
A1AWZ C3  C2   doub Y N 37  
A1AWZ C6  C7   sing Y N 38  
A1AWZ C6  C10  doub Y N 39  
A1AWZ C7  C8   doub Y N 40  
A1AWZ C2  C10  sing Y N 41  
A1AWZ C2  O1   sing N N 42  
A1AWZ C10 N1   sing Y N 43  
A1AWZ C1  O1   sing N N 44  
A1AWZ C8  C9   sing Y N 45  
A1AWZ N1  C9   doub Y N 46  
A1AWZ C5  H1   sing N N 47  
A1AWZ C7  H2   sing N N 48  
A1AWZ C8  H3   sing N N 49  
A1AWZ C13 H4   sing N N 50  
A1AWZ C13 H5   sing N N 51  
A1AWZ C21 H6   sing N N 52  
A1AWZ C22 H7   sing N N 53  
A1AWZ C24 H8   sing N N 54  
A1AWZ C28 H9   sing N N 55  
A1AWZ C28 H10  sing N N 56  
A1AWZ C28 H11  sing N N 57  
A1AWZ C1  H12  sing N N 58  
A1AWZ C1  H13  sing N N 59  
A1AWZ C1  H14  sing N N 60  
A1AWZ O2  H15  sing N N 61  
A1AWZ C3  H16  sing N N 62  
A1AWZ O3  H17  sing N N 63  
A1AWZ C9  H18  sing N N 64  
A1AWZ C12 H19  sing N N 65  
A1AWZ C16 H20  sing N N 66  
A1AWZ C25 H21  sing N N 67  
A1AWZ C27 H22  sing N N 68  
A1AWZ C27 H23  sing N N 69  
A1AWZ C27 H24  sing N N 70  
ALA   N   CA   sing N N 71  
ALA   N   H    sing N N 72  
ALA   N   H2   sing N N 73  
ALA   CA  C    sing N N 74  
ALA   CA  CB   sing N N 75  
ALA   CA  HA   sing N N 76  
ALA   C   O    doub N N 77  
ALA   C   OXT  sing N N 78  
ALA   CB  HB1  sing N N 79  
ALA   CB  HB2  sing N N 80  
ALA   CB  HB3  sing N N 81  
ALA   OXT HXT  sing N N 82  
ARG   N   CA   sing N N 83  
ARG   N   H    sing N N 84  
ARG   N   H2   sing N N 85  
ARG   CA  C    sing N N 86  
ARG   CA  CB   sing N N 87  
ARG   CA  HA   sing N N 88  
ARG   C   O    doub N N 89  
ARG   C   OXT  sing N N 90  
ARG   CB  CG   sing N N 91  
ARG   CB  HB2  sing N N 92  
ARG   CB  HB3  sing N N 93  
ARG   CG  CD   sing N N 94  
ARG   CG  HG2  sing N N 95  
ARG   CG  HG3  sing N N 96  
ARG   CD  NE   sing N N 97  
ARG   CD  HD2  sing N N 98  
ARG   CD  HD3  sing N N 99  
ARG   NE  CZ   sing N N 100 
ARG   NE  HE   sing N N 101 
ARG   CZ  NH1  sing N N 102 
ARG   CZ  NH2  doub N N 103 
ARG   NH1 HH11 sing N N 104 
ARG   NH1 HH12 sing N N 105 
ARG   NH2 HH21 sing N N 106 
ARG   NH2 HH22 sing N N 107 
ARG   OXT HXT  sing N N 108 
ASN   N   CA   sing N N 109 
ASN   N   H    sing N N 110 
ASN   N   H2   sing N N 111 
ASN   CA  C    sing N N 112 
ASN   CA  CB   sing N N 113 
ASN   CA  HA   sing N N 114 
ASN   C   O    doub N N 115 
ASN   C   OXT  sing N N 116 
ASN   CB  CG   sing N N 117 
ASN   CB  HB2  sing N N 118 
ASN   CB  HB3  sing N N 119 
ASN   CG  OD1  doub N N 120 
ASN   CG  ND2  sing N N 121 
ASN   ND2 HD21 sing N N 122 
ASN   ND2 HD22 sing N N 123 
ASN   OXT HXT  sing N N 124 
ASP   N   CA   sing N N 125 
ASP   N   H    sing N N 126 
ASP   N   H2   sing N N 127 
ASP   CA  C    sing N N 128 
ASP   CA  CB   sing N N 129 
ASP   CA  HA   sing N N 130 
ASP   C   O    doub N N 131 
ASP   C   OXT  sing N N 132 
ASP   CB  CG   sing N N 133 
ASP   CB  HB2  sing N N 134 
ASP   CB  HB3  sing N N 135 
ASP   CG  OD1  doub N N 136 
ASP   CG  OD2  sing N N 137 
ASP   OD2 HD2  sing N N 138 
ASP   OXT HXT  sing N N 139 
CYS   N   CA   sing N N 140 
CYS   N   H    sing N N 141 
CYS   N   H2   sing N N 142 
CYS   CA  C    sing N N 143 
CYS   CA  CB   sing N N 144 
CYS   CA  HA   sing N N 145 
CYS   C   O    doub N N 146 
CYS   C   OXT  sing N N 147 
CYS   CB  SG   sing N N 148 
CYS   CB  HB2  sing N N 149 
CYS   CB  HB3  sing N N 150 
CYS   SG  HG   sing N N 151 
CYS   OXT HXT  sing N N 152 
GLN   N   CA   sing N N 153 
GLN   N   H    sing N N 154 
GLN   N   H2   sing N N 155 
GLN   CA  C    sing N N 156 
GLN   CA  CB   sing N N 157 
GLN   CA  HA   sing N N 158 
GLN   C   O    doub N N 159 
GLN   C   OXT  sing N N 160 
GLN   CB  CG   sing N N 161 
GLN   CB  HB2  sing N N 162 
GLN   CB  HB3  sing N N 163 
GLN   CG  CD   sing N N 164 
GLN   CG  HG2  sing N N 165 
GLN   CG  HG3  sing N N 166 
GLN   CD  OE1  doub N N 167 
GLN   CD  NE2  sing N N 168 
GLN   NE2 HE21 sing N N 169 
GLN   NE2 HE22 sing N N 170 
GLN   OXT HXT  sing N N 171 
GLU   N   CA   sing N N 172 
GLU   N   H    sing N N 173 
GLU   N   H2   sing N N 174 
GLU   CA  C    sing N N 175 
GLU   CA  CB   sing N N 176 
GLU   CA  HA   sing N N 177 
GLU   C   O    doub N N 178 
GLU   C   OXT  sing N N 179 
GLU   CB  CG   sing N N 180 
GLU   CB  HB2  sing N N 181 
GLU   CB  HB3  sing N N 182 
GLU   CG  CD   sing N N 183 
GLU   CG  HG2  sing N N 184 
GLU   CG  HG3  sing N N 185 
GLU   CD  OE1  doub N N 186 
GLU   CD  OE2  sing N N 187 
GLU   OE2 HE2  sing N N 188 
GLU   OXT HXT  sing N N 189 
GLY   N   CA   sing N N 190 
GLY   N   H    sing N N 191 
GLY   N   H2   sing N N 192 
GLY   CA  C    sing N N 193 
GLY   CA  HA2  sing N N 194 
GLY   CA  HA3  sing N N 195 
GLY   C   O    doub N N 196 
GLY   C   OXT  sing N N 197 
GLY   OXT HXT  sing N N 198 
HIS   N   CA   sing N N 199 
HIS   N   H    sing N N 200 
HIS   N   H2   sing N N 201 
HIS   CA  C    sing N N 202 
HIS   CA  CB   sing N N 203 
HIS   CA  HA   sing N N 204 
HIS   C   O    doub N N 205 
HIS   C   OXT  sing N N 206 
HIS   CB  CG   sing N N 207 
HIS   CB  HB2  sing N N 208 
HIS   CB  HB3  sing N N 209 
HIS   CG  ND1  sing Y N 210 
HIS   CG  CD2  doub Y N 211 
HIS   ND1 CE1  doub Y N 212 
HIS   ND1 HD1  sing N N 213 
HIS   CD2 NE2  sing Y N 214 
HIS   CD2 HD2  sing N N 215 
HIS   CE1 NE2  sing Y N 216 
HIS   CE1 HE1  sing N N 217 
HIS   NE2 HE2  sing N N 218 
HIS   OXT HXT  sing N N 219 
ILE   N   CA   sing N N 220 
ILE   N   H    sing N N 221 
ILE   N   H2   sing N N 222 
ILE   CA  C    sing N N 223 
ILE   CA  CB   sing N N 224 
ILE   CA  HA   sing N N 225 
ILE   C   O    doub N N 226 
ILE   C   OXT  sing N N 227 
ILE   CB  CG1  sing N N 228 
ILE   CB  CG2  sing N N 229 
ILE   CB  HB   sing N N 230 
ILE   CG1 CD1  sing N N 231 
ILE   CG1 HG12 sing N N 232 
ILE   CG1 HG13 sing N N 233 
ILE   CG2 HG21 sing N N 234 
ILE   CG2 HG22 sing N N 235 
ILE   CG2 HG23 sing N N 236 
ILE   CD1 HD11 sing N N 237 
ILE   CD1 HD12 sing N N 238 
ILE   CD1 HD13 sing N N 239 
ILE   OXT HXT  sing N N 240 
LEU   N   CA   sing N N 241 
LEU   N   H    sing N N 242 
LEU   N   H2   sing N N 243 
LEU   CA  C    sing N N 244 
LEU   CA  CB   sing N N 245 
LEU   CA  HA   sing N N 246 
LEU   C   O    doub N N 247 
LEU   C   OXT  sing N N 248 
LEU   CB  CG   sing N N 249 
LEU   CB  HB2  sing N N 250 
LEU   CB  HB3  sing N N 251 
LEU   CG  CD1  sing N N 252 
LEU   CG  CD2  sing N N 253 
LEU   CG  HG   sing N N 254 
LEU   CD1 HD11 sing N N 255 
LEU   CD1 HD12 sing N N 256 
LEU   CD1 HD13 sing N N 257 
LEU   CD2 HD21 sing N N 258 
LEU   CD2 HD22 sing N N 259 
LEU   CD2 HD23 sing N N 260 
LEU   OXT HXT  sing N N 261 
LYS   N   CA   sing N N 262 
LYS   N   H    sing N N 263 
LYS   N   H2   sing N N 264 
LYS   CA  C    sing N N 265 
LYS   CA  CB   sing N N 266 
LYS   CA  HA   sing N N 267 
LYS   C   O    doub N N 268 
LYS   C   OXT  sing N N 269 
LYS   CB  CG   sing N N 270 
LYS   CB  HB2  sing N N 271 
LYS   CB  HB3  sing N N 272 
LYS   CG  CD   sing N N 273 
LYS   CG  HG2  sing N N 274 
LYS   CG  HG3  sing N N 275 
LYS   CD  CE   sing N N 276 
LYS   CD  HD2  sing N N 277 
LYS   CD  HD3  sing N N 278 
LYS   CE  NZ   sing N N 279 
LYS   CE  HE2  sing N N 280 
LYS   CE  HE3  sing N N 281 
LYS   NZ  HZ1  sing N N 282 
LYS   NZ  HZ2  sing N N 283 
LYS   NZ  HZ3  sing N N 284 
LYS   OXT HXT  sing N N 285 
MET   N   CA   sing N N 286 
MET   N   H    sing N N 287 
MET   N   H2   sing N N 288 
MET   CA  C    sing N N 289 
MET   CA  CB   sing N N 290 
MET   CA  HA   sing N N 291 
MET   C   O    doub N N 292 
MET   C   OXT  sing N N 293 
MET   CB  CG   sing N N 294 
MET   CB  HB2  sing N N 295 
MET   CB  HB3  sing N N 296 
MET   CG  SD   sing N N 297 
MET   CG  HG2  sing N N 298 
MET   CG  HG3  sing N N 299 
MET   SD  CE   sing N N 300 
MET   CE  HE1  sing N N 301 
MET   CE  HE2  sing N N 302 
MET   CE  HE3  sing N N 303 
MET   OXT HXT  sing N N 304 
PHE   N   CA   sing N N 305 
PHE   N   H    sing N N 306 
PHE   N   H2   sing N N 307 
PHE   CA  C    sing N N 308 
PHE   CA  CB   sing N N 309 
PHE   CA  HA   sing N N 310 
PHE   C   O    doub N N 311 
PHE   C   OXT  sing N N 312 
PHE   CB  CG   sing N N 313 
PHE   CB  HB2  sing N N 314 
PHE   CB  HB3  sing N N 315 
PHE   CG  CD1  doub Y N 316 
PHE   CG  CD2  sing Y N 317 
PHE   CD1 CE1  sing Y N 318 
PHE   CD1 HD1  sing N N 319 
PHE   CD2 CE2  doub Y N 320 
PHE   CD2 HD2  sing N N 321 
PHE   CE1 CZ   doub Y N 322 
PHE   CE1 HE1  sing N N 323 
PHE   CE2 CZ   sing Y N 324 
PHE   CE2 HE2  sing N N 325 
PHE   CZ  HZ   sing N N 326 
PHE   OXT HXT  sing N N 327 
PRO   N   CA   sing N N 328 
PRO   N   CD   sing N N 329 
PRO   N   H    sing N N 330 
PRO   CA  C    sing N N 331 
PRO   CA  CB   sing N N 332 
PRO   CA  HA   sing N N 333 
PRO   C   O    doub N N 334 
PRO   C   OXT  sing N N 335 
PRO   CB  CG   sing N N 336 
PRO   CB  HB2  sing N N 337 
PRO   CB  HB3  sing N N 338 
PRO   CG  CD   sing N N 339 
PRO   CG  HG2  sing N N 340 
PRO   CG  HG3  sing N N 341 
PRO   CD  HD2  sing N N 342 
PRO   CD  HD3  sing N N 343 
PRO   OXT HXT  sing N N 344 
SER   N   CA   sing N N 345 
SER   N   H    sing N N 346 
SER   N   H2   sing N N 347 
SER   CA  C    sing N N 348 
SER   CA  CB   sing N N 349 
SER   CA  HA   sing N N 350 
SER   C   O    doub N N 351 
SER   C   OXT  sing N N 352 
SER   CB  OG   sing N N 353 
SER   CB  HB2  sing N N 354 
SER   CB  HB3  sing N N 355 
SER   OG  HG   sing N N 356 
SER   OXT HXT  sing N N 357 
THR   N   CA   sing N N 358 
THR   N   H    sing N N 359 
THR   N   H2   sing N N 360 
THR   CA  C    sing N N 361 
THR   CA  CB   sing N N 362 
THR   CA  HA   sing N N 363 
THR   C   O    doub N N 364 
THR   C   OXT  sing N N 365 
THR   CB  OG1  sing N N 366 
THR   CB  CG2  sing N N 367 
THR   CB  HB   sing N N 368 
THR   OG1 HG1  sing N N 369 
THR   CG2 HG21 sing N N 370 
THR   CG2 HG22 sing N N 371 
THR   CG2 HG23 sing N N 372 
THR   OXT HXT  sing N N 373 
TRP   N   CA   sing N N 374 
TRP   N   H    sing N N 375 
TRP   N   H2   sing N N 376 
TRP   CA  C    sing N N 377 
TRP   CA  CB   sing N N 378 
TRP   CA  HA   sing N N 379 
TRP   C   O    doub N N 380 
TRP   C   OXT  sing N N 381 
TRP   CB  CG   sing N N 382 
TRP   CB  HB2  sing N N 383 
TRP   CB  HB3  sing N N 384 
TRP   CG  CD1  doub Y N 385 
TRP   CG  CD2  sing Y N 386 
TRP   CD1 NE1  sing Y N 387 
TRP   CD1 HD1  sing N N 388 
TRP   CD2 CE2  doub Y N 389 
TRP   CD2 CE3  sing Y N 390 
TRP   NE1 CE2  sing Y N 391 
TRP   NE1 HE1  sing N N 392 
TRP   CE2 CZ2  sing Y N 393 
TRP   CE3 CZ3  doub Y N 394 
TRP   CE3 HE3  sing N N 395 
TRP   CZ2 CH2  doub Y N 396 
TRP   CZ2 HZ2  sing N N 397 
TRP   CZ3 CH2  sing Y N 398 
TRP   CZ3 HZ3  sing N N 399 
TRP   CH2 HH2  sing N N 400 
TRP   OXT HXT  sing N N 401 
TYR   N   CA   sing N N 402 
TYR   N   H    sing N N 403 
TYR   N   H2   sing N N 404 
TYR   CA  C    sing N N 405 
TYR   CA  CB   sing N N 406 
TYR   CA  HA   sing N N 407 
TYR   C   O    doub N N 408 
TYR   C   OXT  sing N N 409 
TYR   CB  CG   sing N N 410 
TYR   CB  HB2  sing N N 411 
TYR   CB  HB3  sing N N 412 
TYR   CG  CD1  doub Y N 413 
TYR   CG  CD2  sing Y N 414 
TYR   CD1 CE1  sing Y N 415 
TYR   CD1 HD1  sing N N 416 
TYR   CD2 CE2  doub Y N 417 
TYR   CD2 HD2  sing N N 418 
TYR   CE1 CZ   doub Y N 419 
TYR   CE1 HE1  sing N N 420 
TYR   CE2 CZ   sing Y N 421 
TYR   CE2 HE2  sing N N 422 
TYR   CZ  OH   sing N N 423 
TYR   OH  HH   sing N N 424 
TYR   OXT HXT  sing N N 425 
VAL   N   CA   sing N N 426 
VAL   N   H    sing N N 427 
VAL   N   H2   sing N N 428 
VAL   CA  C    sing N N 429 
VAL   CA  CB   sing N N 430 
VAL   CA  HA   sing N N 431 
VAL   C   O    doub N N 432 
VAL   C   OXT  sing N N 433 
VAL   CB  CG1  sing N N 434 
VAL   CB  CG2  sing N N 435 
VAL   CB  HB   sing N N 436 
VAL   CG1 HG11 sing N N 437 
VAL   CG1 HG12 sing N N 438 
VAL   CG1 HG13 sing N N 439 
VAL   CG2 HG21 sing N N 440 
VAL   CG2 HG22 sing N N 441 
VAL   CG2 HG23 sing N N 442 
VAL   OXT HXT  sing N N 443 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-06-11 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9C7Y 
_em_admin.last_update        2025-01-08 
_em_admin.map_release_date   2025-01-08 
_em_admin.title              'EM map Of Respiratory Syncytial Virus Polymerase in complex with JNJ-2729' 
# 
_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_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          11259 
_em_entity_assembly_naturalsource.organism             'Human respiratory syncytial virus A2' 
_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         1.368 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? ? ? 
'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           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9C7Y 
_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 
F 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . ASN   A 1 47   ? 127.993 153.479 157.547 1.00 66.18  0  11   ASN   A N   1 
ATOM   2     C CA  . ASN   A 1 47   ? 127.561 152.089 157.616 1.00 67.51  0  11   ASN   A CA  1 
ATOM   3     C C   . ASN   A 1 47   ? 126.130 151.953 157.115 1.00 66.17  0  11   ASN   A C   1 
ATOM   4     O O   . ASN   A 1 47   ? 125.220 151.642 157.879 1.00 65.42  0  11   ASN   A O   1 
ATOM   5     C CB  . ASN   A 1 47   ? 127.687 151.563 159.046 1.00 67.04  0  11   ASN   A CB  1 
ATOM   6     C CG  . ASN   A 1 47   ? 127.674 150.052 159.114 1.00 67.60  0  11   ASN   A CG  1 
ATOM   7     O OD1 . ASN   A 1 47   ? 126.670 149.416 158.803 1.00 70.49  0  11   ASN   A OD1 1 
ATOM   8     N ND2 . ASN   A 1 47   ? 128.797 149.468 159.512 1.00 64.07  0  11   ASN   A ND2 1 
ATOM   9     N N   . VAL   A 1 48   ? 125.942 152.189 155.821 1.00 61.04  0  12   VAL   A N   1 
ATOM   10    C CA  . VAL   A 1 48   ? 124.628 152.175 155.207 1.00 57.83  0  12   VAL   A CA  1 
ATOM   11    C C   . VAL   A 1 48   ? 124.447 150.870 154.445 1.00 56.51  0  12   VAL   A C   1 
ATOM   12    O O   . VAL   A 1 48   ? 125.404 150.153 154.143 1.00 57.99  0  12   VAL   A O   1 
ATOM   13    C CB  . VAL   A 1 48   ? 124.423 153.388 154.275 1.00 56.60  0  12   VAL   A CB  1 
ATOM   14    C CG1 . VAL   A 1 48   ? 124.826 154.669 154.978 1.00 60.51  0  12   VAL   A CG1 1 
ATOM   15    C CG2 . VAL   A 1 48   ? 125.217 153.206 152.997 1.00 56.12  0  12   VAL   A CG2 1 
ATOM   16    N N   . TYR   A 1 49   ? 123.194 150.559 154.126 1.00 62.37  0  13   TYR   A N   1 
ATOM   17    C CA  . TYR   A 1 49   ? 122.840 149.385 153.341 1.00 63.43  0  13   TYR   A CA  1 
ATOM   18    C C   . TYR   A 1 49   ? 122.332 149.832 151.979 1.00 58.11  0  13   TYR   A C   1 
ATOM   19    O O   . TYR   A 1 49   ? 121.451 150.691 151.892 1.00 59.17  0  13   TYR   A O   1 
ATOM   20    C CB  . TYR   A 1 49   ? 121.775 148.546 154.047 1.00 61.86  0  13   TYR   A CB  1 
ATOM   21    C CG  . TYR   A 1 49   ? 122.298 147.724 155.198 1.00 61.08  0  13   TYR   A CG  1 
ATOM   22    C CD1 . TYR   A 1 49   ? 122.597 148.314 156.416 1.00 62.44  0  13   TYR   A CD1 1 
ATOM   23    C CD2 . TYR   A 1 49   ? 122.493 146.359 155.066 1.00 60.49  0  13   TYR   A CD2 1 
ATOM   24    C CE1 . TYR   A 1 49   ? 123.075 147.566 157.474 1.00 63.39  0  13   TYR   A CE1 1 
ATOM   25    C CE2 . TYR   A 1 49   ? 122.972 145.603 156.117 1.00 62.80  0  13   TYR   A CE2 1 
ATOM   26    C CZ  . TYR   A 1 49   ? 123.263 146.212 157.317 1.00 65.10  0  13   TYR   A CZ  1 
ATOM   27    O OH  . TYR   A 1 49   ? 123.741 145.464 158.366 1.00 68.75  0  13   TYR   A OH  1 
ATOM   28    N N   . LEU   A 1 50   ? 122.891 149.255 150.922 1.00 45.31  0  14   LEU   A N   1 
ATOM   29    C CA  . LEU   A 1 50   ? 122.472 149.543 149.559 1.00 48.09  0  14   LEU   A CA  1 
ATOM   30    C C   . LEU   A 1 50   ? 121.944 148.262 148.933 1.00 54.78  0  14   LEU   A C   1 
ATOM   31    O O   . LEU   A 1 50   ? 122.629 147.235 148.939 1.00 55.93  0  14   LEU   A O   1 
ATOM   32    C CB  . LEU   A 1 50   ? 123.626 150.112 148.735 1.00 48.23  0  14   LEU   A CB  1 
ATOM   33    C CG  . LEU   A 1 50   ? 123.350 150.489 147.282 1.00 46.78  0  14   LEU   A CG  1 
ATOM   34    C CD1 . LEU   A 1 50   ? 122.356 151.629 147.202 1.00 48.53  0  14   LEU   A CD1 1 
ATOM   35    C CD2 . LEU   A 1 50   ? 124.644 150.863 146.593 1.00 43.72  0  14   LEU   A CD2 1 
ATOM   36    N N   . THR   A 1 51   ? 120.730 148.327 148.402 1.00 49.22  0  15   THR   A N   1 
ATOM   37    C CA  . THR   A 1 51   ? 120.061 147.180 147.813 1.00 40.26  0  15   THR   A CA  1 
ATOM   38    C C   . THR   A 1 51   ? 120.282 147.156 146.306 1.00 36.68  0  15   THR   A C   1 
ATOM   39    O O   . THR   A 1 51   ? 120.699 148.141 145.694 1.00 39.35  0  15   THR   A O   1 
ATOM   40    C CB  . THR   A 1 51   ? 118.567 147.213 148.137 1.00 40.27  0  15   THR   A CB  1 
ATOM   41    O OG1 . THR   A 1 51   ? 118.024 148.480 147.749 1.00 38.42  0  15   THR   A OG1 1 
ATOM   42    C CG2 . THR   A 1 51   ? 118.342 147.011 149.626 1.00 37.97  0  15   THR   A CG2 1 
ATOM   43    N N   . ASP   A 1 52   ? 119.993 146.005 145.708 1.00 40.07  0  16   ASP   A N   1 
ATOM   44    C CA  . ASP   A 1 52   ? 120.198 145.831 144.281 1.00 39.90  0  16   ASP   A CA  1 
ATOM   45    C C   . ASP   A 1 52   ? 119.148 146.601 143.488 1.00 37.52  0  16   ASP   A C   1 
ATOM   46    O O   . ASP   A 1 52   ? 118.045 146.873 143.964 1.00 47.80  0  16   ASP   A O   1 
ATOM   47    C CB  . ASP   A 1 52   ? 120.139 144.351 143.909 1.00 39.62  0  16   ASP   A CB  1 
ATOM   48    C CG  . ASP   A 1 52   ? 120.885 143.473 144.891 1.00 48.19  0  16   ASP   A CG  1 
ATOM   49    O OD1 . ASP   A 1 52   ? 121.890 143.935 145.468 1.00 48.85  0  16   ASP   A OD1 1 
ATOM   50    O OD2 . ASP   A 1 52   ? 120.463 142.315 145.088 1.00 53.14  -1 16   ASP   A OD2 1 
ATOM   51    N N   . SER   A 1 53   ? 119.509 146.962 142.258 1.00 22.03  0  17   SER   A N   1 
ATOM   52    C CA  . SER   A 1 53   ? 118.557 147.544 141.325 1.00 23.36  0  17   SER   A CA  1 
ATOM   53    C C   . SER   A 1 53   ? 118.133 146.580 140.231 1.00 32.65  0  17   SER   A C   1 
ATOM   54    O O   . SER   A 1 53   ? 117.103 146.810 139.592 1.00 35.89  0  17   SER   A O   1 
ATOM   55    C CB  . SER   A 1 53   ? 119.135 148.812 140.681 1.00 28.78  0  17   SER   A CB  1 
ATOM   56    O OG  . SER   A 1 53   ? 120.451 148.598 140.210 1.00 36.27  0  17   SER   A OG  1 
ATOM   57    N N   . TYR   A 1 54   ? 118.898 145.517 140.006 1.00 41.27  0  18   TYR   A N   1 
ATOM   58    C CA  . TYR   A 1 54   ? 118.554 144.462 139.069 1.00 35.21  0  18   TYR   A CA  1 
ATOM   59    C C   . TYR   A 1 54   ? 118.681 143.127 139.779 1.00 33.81  0  18   TYR   A C   1 
ATOM   60    O O   . TYR   A 1 54   ? 119.369 143.013 140.796 1.00 44.67  0  18   TYR   A O   1 
ATOM   61    C CB  . TYR   A 1 54   ? 119.453 144.484 137.830 1.00 34.17  0  18   TYR   A CB  1 
ATOM   62    C CG  . TYR   A 1 54   ? 119.456 145.811 137.125 1.00 34.95  0  18   TYR   A CG  1 
ATOM   63    C CD1 . TYR   A 1 54   ? 120.326 146.817 137.506 1.00 32.41  0  18   TYR   A CD1 1 
ATOM   64    C CD2 . TYR   A 1 54   ? 118.569 146.069 136.093 1.00 40.64  0  18   TYR   A CD2 1 
ATOM   65    C CE1 . TYR   A 1 54   ? 120.321 148.036 136.873 1.00 39.94  0  18   TYR   A CE1 1 
ATOM   66    C CE2 . TYR   A 1 54   ? 118.558 147.286 135.453 1.00 47.27  0  18   TYR   A CE2 1 
ATOM   67    C CZ  . TYR   A 1 54   ? 119.436 148.266 135.849 1.00 45.67  0  18   TYR   A CZ  1 
ATOM   68    O OH  . TYR   A 1 54   ? 119.431 149.483 135.215 1.00 43.06  0  18   TYR   A OH  1 
ATOM   69    N N   . LEU   A 1 55   ? 118.008 142.115 139.242 1.00 19.50  0  19   LEU   A N   1 
ATOM   70    C CA  . LEU   A 1 55   ? 118.045 140.805 139.872 1.00 25.80  0  19   LEU   A CA  1 
ATOM   71    C C   . LEU   A 1 55   ? 119.445 140.215 139.784 1.00 30.01  0  19   LEU   A C   1 
ATOM   72    O O   . LEU   A 1 55   ? 119.865 139.752 138.720 1.00 39.54  0  19   LEU   A O   1 
ATOM   73    C CB  . LEU   A 1 55   ? 117.030 139.869 139.220 1.00 23.25  0  19   LEU   A CB  1 
ATOM   74    C CG  . LEU   A 1 55   ? 116.779 138.577 139.987 1.00 25.56  0  19   LEU   A CG  1 
ATOM   75    C CD1 . LEU   A 1 55   ? 115.897 138.845 141.185 1.00 27.15  0  19   LEU   A CD1 1 
ATOM   76    C CD2 . LEU   A 1 55   ? 116.156 137.547 139.078 1.00 32.74  0  19   LEU   A CD2 1 
ATOM   77    N N   . LYS   A 1 56   ? 120.179 140.235 140.893 1.00 26.05  0  20   LYS   A N   1 
ATOM   78    C CA  . LYS   A 1 56   ? 121.516 139.667 140.937 1.00 31.18  0  20   LYS   A CA  1 
ATOM   79    C C   . LYS   A 1 56   ? 121.545 138.291 141.578 1.00 33.81  0  20   LYS   A C   1 
ATOM   80    O O   . LYS   A 1 56   ? 122.631 137.746 141.799 1.00 39.10  0  20   LYS   A O   1 
ATOM   81    C CB  . LYS   A 1 56   ? 122.470 140.606 141.683 1.00 30.66  0  20   LYS   A CB  1 
ATOM   82    C CG  . LYS   A 1 56   ? 122.460 142.033 141.167 1.00 34.46  0  20   LYS   A CG  1 
ATOM   83    C CD  . LYS   A 1 56   ? 123.689 142.332 140.331 1.00 37.30  0  20   LYS   A CD  1 
ATOM   84    C CE  . LYS   A 1 56   ? 123.662 143.757 139.810 1.00 41.25  0  20   LYS   A CE  1 
ATOM   85    N NZ  . LYS   A 1 56   ? 123.605 144.744 140.921 1.00 39.70  1  20   LYS   A NZ  1 
ATOM   86    N N   . GLY   A 1 57   ? 120.387 137.718 141.886 1.00 33.00  0  21   GLY   A N   1 
ATOM   87    C CA  . GLY   A 1 57   ? 120.325 136.403 142.486 1.00 33.03  0  21   GLY   A CA  1 
ATOM   88    C C   . GLY   A 1 57   ? 119.178 135.587 141.935 1.00 37.73  0  21   GLY   A C   1 
ATOM   89    O O   . GLY   A 1 57   ? 118.934 135.584 140.726 1.00 41.77  0  21   GLY   A O   1 
ATOM   90    N N   . VAL   A 1 58   ? 118.462 134.891 142.810 1.00 34.49  0  22   VAL   A N   1 
ATOM   91    C CA  . VAL   A 1 58   ? 117.347 134.043 142.416 1.00 28.12  0  22   VAL   A CA  1 
ATOM   92    C C   . VAL   A 1 58   ? 116.120 134.436 143.225 1.00 34.76  0  22   VAL   A C   1 
ATOM   93    O O   . VAL   A 1 58   ? 116.225 134.786 144.406 1.00 34.70  0  22   VAL   A O   1 
ATOM   94    C CB  . VAL   A 1 58   ? 117.672 132.544 142.600 1.00 27.46  0  22   VAL   A CB  1 
ATOM   95    C CG1 . VAL   A 1 58   ? 118.913 132.171 141.816 1.00 29.32  0  22   VAL   A CG1 1 
ATOM   96    C CG2 . VAL   A 1 58   ? 117.860 132.204 144.067 1.00 28.47  0  22   VAL   A CG2 1 
ATOM   97    N N   . ILE   A 1 59   ? 114.959 134.405 142.574 1.00 33.50  0  23   ILE   A N   1 
ATOM   98    C CA  . ILE   A 1 59   ? 113.700 134.531 143.292 1.00 26.56  0  23   ILE   A CA  1 
ATOM   99    C C   . ILE   A 1 59   ? 113.503 133.283 144.136 1.00 30.56  0  23   ILE   A C   1 
ATOM   100   O O   . ILE   A 1 59   ? 113.662 132.157 143.651 1.00 35.47  0  23   ILE   A O   1 
ATOM   101   C CB  . ILE   A 1 59   ? 112.540 134.728 142.311 1.00 26.68  0  23   ILE   A CB  1 
ATOM   102   C CG1 . ILE   A 1 59   ? 112.926 135.743 141.240 1.00 22.19  0  23   ILE   A CG1 1 
ATOM   103   C CG2 . ILE   A 1 59   ? 111.303 135.182 143.051 1.00 31.57  0  23   ILE   A CG2 1 
ATOM   104   C CD1 . ILE   A 1 59   ? 112.005 135.737 140.061 1.00 23.67  0  23   ILE   A CD1 1 
ATOM   105   N N   . SER   A 1 60   ? 113.169 133.470 145.403 1.00 30.00  0  24   SER   A N   1 
ATOM   106   C CA  . SER   A 1 60   ? 113.159 132.370 146.353 1.00 30.21  0  24   SER   A CA  1 
ATOM   107   C C   . SER   A 1 60   ? 111.738 131.883 146.592 1.00 31.80  0  24   SER   A C   1 
ATOM   108   O O   . SER   A 1 60   ? 110.855 132.669 146.945 1.00 34.34  0  24   SER   A O   1 
ATOM   109   C CB  . SER   A 1 60   ? 113.798 132.787 147.673 1.00 34.94  0  24   SER   A CB  1 
ATOM   110   O OG  . SER   A 1 60   ? 113.886 131.677 148.539 1.00 34.39  0  24   SER   A OG  1 
ATOM   111   N N   . PHE   A 1 61   ? 111.525 130.583 146.389 1.00 32.25  0  25   PHE   A N   1 
ATOM   112   C CA  . PHE   A 1 61   ? 110.256 129.970 146.758 1.00 30.59  0  25   PHE   A CA  1 
ATOM   113   C C   . PHE   A 1 61   ? 110.097 129.916 148.269 1.00 30.23  0  25   PHE   A C   1 
ATOM   114   O O   . PHE   A 1 61   ? 109.023 130.218 148.798 1.00 32.41  0  25   PHE   A O   1 
ATOM   115   C CB  . PHE   A 1 61   ? 110.171 128.569 146.157 1.00 33.89  0  25   PHE   A CB  1 
ATOM   116   C CG  . PHE   A 1 61   ? 108.806 127.953 146.222 1.00 34.23  0  25   PHE   A CG  1 
ATOM   117   C CD1 . PHE   A 1 61   ? 108.446 127.151 147.288 1.00 33.83  0  25   PHE   A CD1 1 
ATOM   118   C CD2 . PHE   A 1 61   ? 107.895 128.154 145.204 1.00 33.61  0  25   PHE   A CD2 1 
ATOM   119   C CE1 . PHE   A 1 61   ? 107.201 126.578 147.344 1.00 36.01  0  25   PHE   A CE1 1 
ATOM   120   C CE2 . PHE   A 1 61   ? 106.650 127.582 145.255 1.00 32.52  0  25   PHE   A CE2 1 
ATOM   121   C CZ  . PHE   A 1 61   ? 106.302 126.792 146.326 1.00 37.13  0  25   PHE   A CZ  1 
ATOM   122   N N   . SER   A 1 62   ? 111.162 129.538 148.980 1.00 34.96  0  26   SER   A N   1 
ATOM   123   C CA  . SER   A 1 62   ? 111.075 129.393 150.428 1.00 40.28  0  26   SER   A CA  1 
ATOM   124   C C   . SER   A 1 62   ? 110.810 130.723 151.117 1.00 38.19  0  26   SER   A C   1 
ATOM   125   O O   . SER   A 1 62   ? 110.055 130.773 152.090 1.00 42.40  0  26   SER   A O   1 
ATOM   126   C CB  . SER   A 1 62   ? 112.353 128.759 150.972 1.00 34.31  0  26   SER   A CB  1 
ATOM   127   O OG  . SER   A 1 62   ? 112.477 127.418 150.537 1.00 35.90  0  26   SER   A OG  1 
ATOM   128   N N   . GLU   A 1 63   ? 111.424 131.806 150.641 1.00 36.90  0  27   GLU   A N   1 
ATOM   129   C CA  . GLU   A 1 63   ? 111.214 133.104 151.273 1.00 25.41  0  27   GLU   A CA  1 
ATOM   130   C C   . GLU   A 1 63   ? 109.776 133.576 151.099 1.00 30.19  0  27   GLU   A C   1 
ATOM   131   O O   . GLU   A 1 63   ? 109.144 134.031 152.060 1.00 39.57  0  27   GLU   A O   1 
ATOM   132   C CB  . GLU   A 1 63   ? 112.195 134.127 150.704 1.00 25.37  0  27   GLU   A CB  1 
ATOM   133   C CG  . GLU   A 1 63   ? 112.453 135.308 151.619 1.00 38.32  0  27   GLU   A CG  1 
ATOM   134   C CD  . GLU   A 1 63   ? 113.430 136.299 151.025 1.00 44.62  0  27   GLU   A CD  1 
ATOM   135   O OE1 . GLU   A 1 63   ? 113.692 136.219 149.807 1.00 35.01  0  27   GLU   A OE1 1 
ATOM   136   O OE2 . GLU   A 1 63   ? 113.936 137.158 151.776 1.00 47.92  -1 27   GLU   A OE2 1 
ATOM   137   N N   . CYS   A 1 64   ? 109.241 133.473 149.879 1.00 33.56  0  28   CYS   A N   1 
ATOM   138   C CA  . CYS   A 1 64   ? 107.843 133.831 149.658 1.00 30.36  0  28   CYS   A CA  1 
ATOM   139   C C   . CYS   A 1 64   ? 106.922 132.957 150.492 1.00 33.62  0  28   CYS   A C   1 
ATOM   140   O O   . CYS   A 1 64   ? 105.962 133.452 151.093 1.00 32.70  0  28   CYS   A O   1 
ATOM   141   C CB  . CYS   A 1 64   ? 107.481 133.705 148.180 1.00 25.73  0  28   CYS   A CB  1 
ATOM   142   S SG  . CYS   A 1 64   ? 108.265 134.899 147.093 1.00 58.20  0  28   CYS   A SG  1 
ATOM   143   N N   . ASN   A 1 65   ? 107.199 131.654 150.543 1.00 30.16  0  29   ASN   A N   1 
ATOM   144   C CA  . ASN   A 1 65   ? 106.372 130.752 151.334 1.00 30.66  0  29   ASN   A CA  1 
ATOM   145   C C   . ASN   A 1 65   ? 106.374 131.157 152.800 1.00 38.32  0  29   ASN   A C   1 
ATOM   146   O O   . ASN   A 1 65   ? 105.313 131.299 153.414 1.00 45.37  0  29   ASN   A O   1 
ATOM   147   C CB  . ASN   A 1 65   ? 106.862 129.315 151.170 1.00 21.46  0  29   ASN   A CB  1 
ATOM   148   C CG  . ASN   A 1 65   ? 105.911 128.307 151.769 1.00 28.94  0  29   ASN   A CG  1 
ATOM   149   O OD1 . ASN   A 1 65   ? 104.735 128.268 151.421 1.00 35.70  0  29   ASN   A OD1 1 
ATOM   150   N ND2 . ASN   A 1 65   ? 106.416 127.480 152.673 1.00 30.29  0  29   ASN   A ND2 1 
ATOM   151   N N   . ALA   A 1 66   ? 107.561 131.374 153.372 1.00 25.89  0  30   ALA   A N   1 
ATOM   152   C CA  . ALA   A 1 66   ? 107.657 131.711 154.788 1.00 24.78  0  30   ALA   A CA  1 
ATOM   153   C C   . ALA   A 1 66   ? 106.971 133.033 155.093 1.00 29.54  0  30   ALA   A C   1 
ATOM   154   O O   . ALA   A 1 66   ? 106.203 133.136 156.058 1.00 38.82  0  30   ALA   A O   1 
ATOM   155   C CB  . ALA   A 1 66   ? 109.121 131.763 155.215 1.00 27.05  0  30   ALA   A CB  1 
ATOM   156   N N   . LEU   A 1 67   ? 107.212 134.050 154.267 1.00 31.17  0  31   LEU   A N   1 
ATOM   157   C CA  . LEU   A 1 67   ? 106.637 135.362 154.534 1.00 29.12  0  31   LEU   A CA  1 
ATOM   158   C C   . LEU   A 1 67   ? 105.119 135.337 154.395 1.00 35.01  0  31   LEU   A C   1 
ATOM   159   O O   . LEU   A 1 67   ? 104.397 135.782 155.292 1.00 44.29  0  31   LEU   A O   1 
ATOM   160   C CB  . LEU   A 1 67   ? 107.257 136.400 153.603 1.00 26.30  0  31   LEU   A CB  1 
ATOM   161   C CG  . LEU   A 1 67   ? 106.820 137.837 153.857 1.00 28.44  0  31   LEU   A CG  1 
ATOM   162   C CD1 . LEU   A 1 67   ? 107.063 138.238 155.294 1.00 32.78  0  31   LEU   A CD1 1 
ATOM   163   C CD2 . LEU   A 1 67   ? 107.530 138.769 152.901 1.00 38.83  0  31   LEU   A CD2 1 
ATOM   164   N N   . GLY   A 1 68   ? 104.611 134.801 153.282 1.00 26.70  0  32   GLY   A N   1 
ATOM   165   C CA  . GLY   A 1 68   ? 103.175 134.746 153.088 1.00 29.01  0  32   GLY   A CA  1 
ATOM   166   C C   . GLY   A 1 68   ? 102.455 133.832 154.052 1.00 22.77  0  32   GLY   A C   1 
ATOM   167   O O   . GLY   A 1 68   ? 101.281 134.068 154.350 1.00 18.52  0  32   GLY   A O   1 
ATOM   168   N N   . SER   A 1 69   ? 103.122 132.790 154.543 1.00 21.65  0  33   SER   A N   1 
ATOM   169   C CA  . SER   A 1 69   ? 102.529 131.928 155.547 1.00 24.17  0  33   SER   A CA  1 
ATOM   170   C C   . SER   A 1 69   ? 102.538 132.549 156.932 1.00 36.48  0  33   SER   A C   1 
ATOM   171   O O   . SER   A 1 69   ? 101.659 132.234 157.739 1.00 41.88  0  33   SER   A O   1 
ATOM   172   C CB  . SER   A 1 69   ? 103.254 130.583 155.578 1.00 20.97  0  33   SER   A CB  1 
ATOM   173   O OG  . SER   A 1 69   ? 104.591 130.737 156.002 1.00 28.25  0  33   SER   A OG  1 
ATOM   174   N N   . TYR   A 1 70   ? 103.507 133.415 157.236 1.00 36.02  0  34   TYR   A N   1 
ATOM   175   C CA  . TYR   A 1 70   ? 103.443 134.147 158.496 1.00 29.40  0  34   TYR   A CA  1 
ATOM   176   C C   . TYR   A 1 70   ? 102.378 135.235 158.442 1.00 26.42  0  34   TYR   A C   1 
ATOM   177   O O   . TYR   A 1 70   ? 101.621 135.422 159.400 1.00 28.77  0  34   TYR   A O   1 
ATOM   178   C CB  . TYR   A 1 70   ? 104.802 134.753 158.834 1.00 28.73  0  34   TYR   A CB  1 
ATOM   179   C CG  . TYR   A 1 70   ? 104.739 135.700 160.008 1.00 37.29  0  34   TYR   A CG  1 
ATOM   180   C CD1 . TYR   A 1 70   ? 104.336 135.256 161.258 1.00 40.33  0  34   TYR   A CD1 1 
ATOM   181   C CD2 . TYR   A 1 70   ? 105.063 137.038 159.864 1.00 34.52  0  34   TYR   A CD2 1 
ATOM   182   C CE1 . TYR   A 1 70   ? 104.266 136.114 162.330 1.00 29.90  0  34   TYR   A CE1 1 
ATOM   183   C CE2 . TYR   A 1 70   ? 104.997 137.903 160.934 1.00 36.31  0  34   TYR   A CE2 1 
ATOM   184   C CZ  . TYR   A 1 70   ? 104.597 137.435 162.164 1.00 34.57  0  34   TYR   A CZ  1 
ATOM   185   O OH  . TYR   A 1 70   ? 104.528 138.292 163.235 1.00 43.35  0  34   TYR   A OH  1 
ATOM   186   N N   . ILE   A 1 71   ? 102.304 135.962 157.325 1.00 22.74  0  35   ILE   A N   1 
ATOM   187   C CA  . ILE   A 1 71   ? 101.368 137.079 157.224 1.00 27.78  0  35   ILE   A CA  1 
ATOM   188   C C   . ILE   A 1 71   ? 99.929  136.589 157.322 1.00 33.91  0  35   ILE   A C   1 
ATOM   189   O O   . ILE   A 1 71   ? 99.107  137.173 158.037 1.00 38.56  0  35   ILE   A O   1 
ATOM   190   C CB  . ILE   A 1 71   ? 101.602 137.863 155.919 1.00 29.73  0  35   ILE   A CB  1 
ATOM   191   C CG1 . ILE   A 1 71   ? 103.002 138.470 155.888 1.00 24.59  0  35   ILE   A CG1 1 
ATOM   192   C CG2 . ILE   A 1 71   ? 100.560 138.952 155.757 1.00 27.79  0  35   ILE   A CG2 1 
ATOM   193   C CD1 . ILE   A 1 71   ? 103.176 139.642 156.789 1.00 26.91  0  35   ILE   A CD1 1 
ATOM   194   N N   . PHE   A 1 72   ? 99.600  135.514 156.610 1.00 33.02  0  36   PHE   A N   1 
ATOM   195   C CA  . PHE   A 1 72   ? 98.229  135.036 156.513 1.00 33.65  0  36   PHE   A CA  1 
ATOM   196   C C   . PHE   A 1 72   ? 97.936  133.844 157.414 1.00 34.40  0  36   PHE   A C   1 
ATOM   197   O O   . PHE   A 1 72   ? 96.810  133.339 157.396 1.00 29.53  0  36   PHE   A O   1 
ATOM   198   C CB  . PHE   A 1 72   ? 97.906  134.680 155.063 1.00 31.07  0  36   PHE   A CB  1 
ATOM   199   C CG  . PHE   A 1 72   ? 98.009  135.842 154.126 1.00 26.95  0  36   PHE   A CG  1 
ATOM   200   C CD1 . PHE   A 1 72   ? 97.123  136.898 154.213 1.00 31.05  0  36   PHE   A CD1 1 
ATOM   201   C CD2 . PHE   A 1 72   ? 98.994  135.884 153.161 1.00 29.57  0  36   PHE   A CD2 1 
ATOM   202   C CE1 . PHE   A 1 72   ? 97.218  137.969 153.354 1.00 29.01  0  36   PHE   A CE1 1 
ATOM   203   C CE2 . PHE   A 1 72   ? 99.090  136.951 152.303 1.00 31.18  0  36   PHE   A CE2 1 
ATOM   204   C CZ  . PHE   A 1 72   ? 98.202  137.995 152.398 1.00 23.48  0  36   PHE   A CZ  1 
ATOM   205   N N   . ASN   A 1 73   ? 98.913  133.388 158.197 1.00 37.46  0  37   ASN   A N   1 
ATOM   206   C CA  . ASN   A 1 73   ? 98.730  132.326 159.186 1.00 33.08  0  37   ASN   A CA  1 
ATOM   207   C C   . ASN   A 1 73   ? 98.132  131.071 158.542 1.00 38.61  0  37   ASN   A C   1 
ATOM   208   O O   . ASN   A 1 73   ? 97.032  130.624 158.866 1.00 50.10  0  37   ASN   A O   1 
ATOM   209   C CB  . ASN   A 1 73   ? 97.864  132.813 160.351 1.00 36.18  0  37   ASN   A CB  1 
ATOM   210   C CG  . ASN   A 1 73   ? 97.978  131.924 161.569 1.00 41.35  0  37   ASN   A CG  1 
ATOM   211   O OD1 . ASN   A 1 73   ? 99.060  131.440 161.899 1.00 37.64  0  37   ASN   A OD1 1 
ATOM   212   N ND2 . ASN   A 1 73   ? 96.857  131.696 162.241 1.00 42.14  0  37   ASN   A ND2 1 
ATOM   213   N N   . GLY   A 1 74   ? 98.899  130.515 157.612 1.00 26.43  0  38   GLY   A N   1 
ATOM   214   C CA  . GLY   A 1 74   ? 98.513  129.307 156.925 1.00 27.69  0  38   GLY   A CA  1 
ATOM   215   C C   . GLY   A 1 74   ? 99.385  129.067 155.713 1.00 36.91  0  38   GLY   A C   1 
ATOM   216   O O   . GLY   A 1 74   ? 100.018 129.989 155.194 1.00 46.96  0  38   GLY   A O   1 
ATOM   217   N N   . PRO   A 1 75   ? 99.430  127.824 155.233 1.00 39.34  0  39   PRO   A N   1 
ATOM   218   C CA  . PRO   A 1 75   ? 100.316 127.493 154.111 1.00 34.61  0  39   PRO   A CA  1 
ATOM   219   C C   . PRO   A 1 75   ? 100.028 128.371 152.904 1.00 34.50  0  39   PRO   A C   1 
ATOM   220   O O   . PRO   A 1 75   ? 98.888  128.484 152.455 1.00 44.99  0  39   PRO   A O   1 
ATOM   221   C CB  . PRO   A 1 75   ? 99.989  126.025 153.828 1.00 37.26  0  39   PRO   A CB  1 
ATOM   222   C CG  . PRO   A 1 75   ? 99.412  125.513 155.100 1.00 39.77  0  39   PRO   A CG  1 
ATOM   223   C CD  . PRO   A 1 75   ? 98.662  126.658 155.693 1.00 38.53  0  39   PRO   A CD  1 
ATOM   224   N N   . TYR   A 1 76   ? 101.077 128.994 152.372 1.00 17.09  0  40   TYR   A N   1 
ATOM   225   C CA  . TYR   A 1 76   ? 100.916 129.985 151.315 1.00 23.22  0  40   TYR   A CA  1 
ATOM   226   C C   . TYR   A 1 76   ? 101.168 129.397 149.932 1.00 33.10  0  40   TYR   A C   1 
ATOM   227   O O   . TYR   A 1 76   ? 100.293 129.448 149.064 1.00 33.30  0  40   TYR   A O   1 
ATOM   228   C CB  . TYR   A 1 76   ? 101.846 131.174 151.572 1.00 30.41  0  40   TYR   A CB  1 
ATOM   229   C CG  . TYR   A 1 76   ? 101.782 132.229 150.500 1.00 29.39  0  40   TYR   A CG  1 
ATOM   230   C CD1 . TYR   A 1 76   ? 100.566 132.675 150.019 1.00 26.23  0  40   TYR   A CD1 1 
ATOM   231   C CD2 . TYR   A 1 76   ? 102.935 132.778 149.971 1.00 22.27  0  40   TYR   A CD2 1 
ATOM   232   C CE1 . TYR   A 1 76   ? 100.500 133.631 149.040 1.00 26.25  0  40   TYR   A CE1 1 
ATOM   233   C CE2 . TYR   A 1 76   ? 102.876 133.735 148.992 1.00 28.67  0  40   TYR   A CE2 1 
ATOM   234   C CZ  . TYR   A 1 76   ? 101.656 134.159 148.531 1.00 31.13  0  40   TYR   A CZ  1 
ATOM   235   O OH  . TYR   A 1 76   ? 101.589 135.116 147.552 1.00 40.32  0  40   TYR   A OH  1 
ATOM   236   N N   . LEU   A 1 77   ? 102.355 128.834 149.708 1.00 34.44  0  41   LEU   A N   1 
ATOM   237   C CA  . LEU   A 1 77   ? 102.691 128.237 148.425 1.00 27.88  0  41   LEU   A CA  1 
ATOM   238   C C   . LEU   A 1 77   ? 102.899 126.734 148.485 1.00 31.57  0  41   LEU   A C   1 
ATOM   239   O O   . LEU   A 1 77   ? 102.746 126.069 147.459 1.00 38.18  0  41   LEU   A O   1 
ATOM   240   C CB  . LEU   A 1 77   ? 103.958 128.883 147.846 1.00 26.64  0  41   LEU   A CB  1 
ATOM   241   C CG  . LEU   A 1 77   ? 103.872 130.337 147.389 1.00 25.01  0  41   LEU   A CG  1 
ATOM   242   C CD1 . LEU   A 1 77   ? 105.238 130.840 146.991 1.00 31.88  0  41   LEU   A CD1 1 
ATOM   243   C CD2 . LEU   A 1 77   ? 102.914 130.464 146.235 1.00 24.51  0  41   LEU   A CD2 1 
ATOM   244   N N   . LYS   A 1 78   ? 103.244 126.189 149.647 1.00 35.96  0  42   LYS   A N   1 
ATOM   245   C CA  . LYS   A 1 78   ? 103.480 124.762 149.786 1.00 37.02  0  42   LYS   A CA  1 
ATOM   246   C C   . LYS   A 1 78   ? 103.360 124.400 151.256 1.00 35.41  0  42   LYS   A C   1 
ATOM   247   O O   . LYS   A 1 78   ? 103.655 125.214 152.132 1.00 41.23  0  42   LYS   A O   1 
ATOM   248   C CB  . LYS   A 1 78   ? 104.857 124.365 149.242 1.00 38.63  0  42   LYS   A CB  1 
ATOM   249   C CG  . LYS   A 1 78   ? 105.160 122.878 149.309 1.00 37.71  0  42   LYS   A CG  1 
ATOM   250   C CD  . LYS   A 1 78   ? 106.609 122.591 148.973 1.00 43.13  0  42   LYS   A CD  1 
ATOM   251   C CE  . LYS   A 1 78   ? 106.966 121.141 149.261 1.00 45.86  0  42   LYS   A CE  1 
ATOM   252   N NZ  . LYS   A 1 78   ? 108.438 120.911 149.219 1.00 43.11  1  42   LYS   A NZ  1 
ATOM   253   N N   . ASN   A 1 79   ? 102.921 123.171 151.515 1.00 40.53  0  43   ASN   A N   1 
ATOM   254   C CA  . ASN   A 1 79   ? 102.752 122.682 152.881 1.00 43.34  0  43   ASN   A CA  1 
ATOM   255   C C   . ASN   A 1 79   ? 104.009 121.945 153.347 1.00 45.97  0  43   ASN   A C   1 
ATOM   256   O O   . ASN   A 1 79   ? 103.985 120.771 153.713 1.00 45.72  0  43   ASN   A O   1 
ATOM   257   C CB  . ASN   A 1 79   ? 101.519 121.792 152.968 1.00 42.24  0  43   ASN   A CB  1 
ATOM   258   C CG  . ASN   A 1 79   ? 100.690 122.066 154.202 1.00 47.57  0  43   ASN   A CG  1 
ATOM   259   O OD1 . ASN   A 1 79   ? 101.204 122.528 155.220 1.00 48.52  0  43   ASN   A OD1 1 
ATOM   260   N ND2 . ASN   A 1 79   ? 99.396  121.789 154.117 1.00 44.02  0  43   ASN   A ND2 1 
ATOM   261   N N   . ASP   A 1 80   ? 105.125 122.665 153.326 1.00 43.02  0  44   ASP   A N   1 
ATOM   262   C CA  . ASP   A 1 80   ? 106.410 122.137 153.752 1.00 42.05  0  44   ASP   A CA  1 
ATOM   263   C C   . ASP   A 1 80   ? 106.669 122.519 155.206 1.00 42.54  0  44   ASP   A C   1 
ATOM   264   O O   . ASP   A 1 80   ? 105.775 122.980 155.919 1.00 40.95  0  44   ASP   A O   1 
ATOM   265   C CB  . ASP   A 1 80   ? 107.517 122.636 152.824 1.00 38.29  0  44   ASP   A CB  1 
ATOM   266   C CG  . ASP   A 1 80   ? 107.419 124.116 152.547 1.00 39.09  0  44   ASP   A CG  1 
ATOM   267   O OD1 . ASP   A 1 80   ? 106.339 124.691 152.782 1.00 38.77  0  44   ASP   A OD1 1 
ATOM   268   O OD2 . ASP   A 1 80   ? 108.419 124.706 152.087 1.00 44.66  -1 44   ASP   A OD2 1 
ATOM   269   N N   . TYR   A 1 81   ? 107.900 122.301 155.667 1.00 35.00  0  45   TYR   A N   1 
ATOM   270   C CA  . TYR   A 1 81   ? 108.283 122.711 157.012 1.00 32.83  0  45   TYR   A CA  1 
ATOM   271   C C   . TYR   A 1 81   ? 108.576 124.201 157.100 1.00 38.02  0  45   TYR   A C   1 
ATOM   272   O O   . TYR   A 1 81   ? 108.595 124.756 158.207 1.00 43.85  0  45   TYR   A O   1 
ATOM   273   C CB  . TYR   A 1 81   ? 109.502 121.916 157.471 1.00 26.60  0  45   TYR   A CB  1 
ATOM   274   C CG  . TYR   A 1 81   ? 109.985 122.275 158.849 1.00 20.75  0  45   TYR   A CG  1 
ATOM   275   C CD1 . TYR   A 1 81   ? 109.173 122.099 159.953 1.00 33.92  0  45   TYR   A CD1 1 
ATOM   276   C CD2 . TYR   A 1 81   ? 111.253 122.786 159.046 1.00 28.22  0  45   TYR   A CD2 1 
ATOM   277   C CE1 . TYR   A 1 81   ? 109.610 122.426 161.217 1.00 42.65  0  45   TYR   A CE1 1 
ATOM   278   C CE2 . TYR   A 1 81   ? 111.700 123.114 160.307 1.00 36.12  0  45   TYR   A CE2 1 
ATOM   279   C CZ  . TYR   A 1 81   ? 110.875 122.932 161.389 1.00 40.93  0  45   TYR   A CZ  1 
ATOM   280   O OH  . TYR   A 1 81   ? 111.320 123.258 162.648 1.00 38.57  0  45   TYR   A OH  1 
ATOM   281   N N   . THR   A 1 82   ? 108.790 124.858 155.958 1.00 43.08  0  46   THR   A N   1 
ATOM   282   C CA  . THR   A 1 82   ? 109.077 126.287 155.948 1.00 37.67  0  46   THR   A CA  1 
ATOM   283   C C   . THR   A 1 82   ? 107.959 127.076 156.612 1.00 39.34  0  46   THR   A C   1 
ATOM   284   O O   . THR   A 1 82   ? 108.210 127.919 157.476 1.00 35.57  0  46   THR   A O   1 
ATOM   285   C CB  . THR   A 1 82   ? 109.281 126.768 154.511 1.00 34.39  0  46   THR   A CB  1 
ATOM   286   O OG1 . THR   A 1 82   ? 110.353 126.037 153.905 1.00 41.49  0  46   THR   A OG1 1 
ATOM   287   C CG2 . THR   A 1 82   ? 109.600 128.246 154.483 1.00 33.78  0  46   THR   A CG2 1 
ATOM   288   N N   . ASN   A 1 83   ? 106.711 126.803 156.227 1.00 40.13  0  47   ASN   A N   1 
ATOM   289   C CA  . ASN   A 1 83   ? 105.584 127.519 156.815 1.00 32.55  0  47   ASN   A CA  1 
ATOM   290   C C   . ASN   A 1 83   ? 105.410 127.173 158.287 1.00 33.78  0  47   ASN   A C   1 
ATOM   291   O O   . ASN   A 1 83   ? 105.086 128.045 159.102 1.00 50.14  0  47   ASN   A O   1 
ATOM   292   C CB  . ASN   A 1 83   ? 104.310 127.226 156.021 1.00 39.19  0  47   ASN   A CB  1 
ATOM   293   C CG  . ASN   A 1 83   ? 103.700 125.872 156.345 1.00 51.34  0  47   ASN   A CG  1 
ATOM   294   O OD1 . ASN   A 1 83   ? 104.333 125.009 156.949 1.00 51.01  0  47   ASN   A OD1 1 
ATOM   295   N ND2 . ASN   A 1 83   ? 102.455 125.685 155.941 1.00 45.10  0  47   ASN   A ND2 1 
ATOM   296   N N   . LEU   A 1 84   ? 105.622 125.906 158.647 1.00 28.26  0  48   LEU   A N   1 
ATOM   297   C CA  . LEU   A 1 84   ? 105.467 125.502 160.038 1.00 35.00  0  48   LEU   A CA  1 
ATOM   298   C C   . LEU   A 1 84   ? 106.433 126.261 160.934 1.00 42.18  0  48   LEU   A C   1 
ATOM   299   O O   . LEU   A 1 84   ? 106.048 126.757 161.999 1.00 43.91  0  48   LEU   A O   1 
ATOM   300   C CB  . LEU   A 1 84   ? 105.681 123.997 160.169 1.00 35.06  0  48   LEU   A CB  1 
ATOM   301   C CG  . LEU   A 1 84   ? 105.178 123.334 161.449 1.00 39.18  0  48   LEU   A CG  1 
ATOM   302   C CD1 . LEU   A 1 84   ? 103.662 123.320 161.477 1.00 37.70  0  48   LEU   A CD1 1 
ATOM   303   C CD2 . LEU   A 1 84   ? 105.737 121.925 161.574 1.00 36.22  0  48   LEU   A CD2 1 
ATOM   304   N N   . ILE   A 1 85   ? 107.687 126.396 160.502 1.00 30.74  0  49   ILE   A N   1 
ATOM   305   C CA  . ILE   A 1 85   ? 108.667 127.118 161.305 1.00 27.03  0  49   ILE   A CA  1 
ATOM   306   C C   . ILE   A 1 85   ? 108.572 128.633 161.148 1.00 29.38  0  49   ILE   A C   1 
ATOM   307   O O   . ILE   A 1 85   ? 109.027 129.365 162.037 1.00 34.51  0  49   ILE   A O   1 
ATOM   308   C CB  . ILE   A 1 85   ? 110.091 126.636 160.980 1.00 31.34  0  49   ILE   A CB  1 
ATOM   309   C CG1 . ILE   A 1 85   ? 111.032 126.960 162.136 1.00 33.02  0  49   ILE   A CG1 1 
ATOM   310   C CG2 . ILE   A 1 85   ? 110.587 127.245 159.680 1.00 35.56  0  49   ILE   A CG2 1 
ATOM   311   C CD1 . ILE   A 1 85   ? 110.631 126.313 163.434 1.00 34.70  0  49   ILE   A CD1 1 
ATOM   312   N N   . SER   A 1 86   ? 107.987 129.127 160.060 1.00 27.73  0  50   SER   A N   1 
ATOM   313   C CA  . SER   A 1 86   ? 107.795 130.556 159.867 1.00 26.38  0  50   SER   A CA  1 
ATOM   314   C C   . SER   A 1 86   ? 106.566 131.087 160.581 1.00 29.79  0  50   SER   A C   1 
ATOM   315   O O   . SER   A 1 86   ? 106.431 132.303 160.730 1.00 38.10  0  50   SER   A O   1 
ATOM   316   C CB  . SER   A 1 86   ? 107.688 130.879 158.377 1.00 34.41  0  50   SER   A CB  1 
ATOM   317   O OG  . SER   A 1 86   ? 107.180 132.185 158.182 1.00 37.46  0  50   SER   A OG  1 
ATOM   318   N N   . ARG   A 1 87   ? 105.656 130.211 160.991 1.00 34.41  0  51   ARG   A N   1 
ATOM   319   C CA  . ARG   A 1 87   ? 104.557 130.600 161.859 1.00 33.01  0  51   ARG   A CA  1 
ATOM   320   C C   . ARG   A 1 87   ? 104.786 130.230 163.313 1.00 38.18  0  51   ARG   A C   1 
ATOM   321   O O   . ARG   A 1 87   ? 104.274 130.916 164.197 1.00 37.47  0  51   ARG   A O   1 
ATOM   322   C CB  . ARG   A 1 87   ? 103.248 129.964 161.377 1.00 34.38  0  51   ARG   A CB  1 
ATOM   323   C CG  . ARG   A 1 87   ? 102.931 130.249 159.921 1.00 33.69  0  51   ARG   A CG  1 
ATOM   324   C CD  . ARG   A 1 87   ? 101.645 129.569 159.494 1.00 38.57  0  51   ARG   A CD  1 
ATOM   325   N NE  . ARG   A 1 87   ? 101.715 128.122 159.653 1.00 40.05  0  51   ARG   A NE  1 
ATOM   326   C CZ  . ARG   A 1 87   ? 100.673 127.348 159.916 1.00 43.58  0  51   ARG   A CZ  1 
ATOM   327   N NH1 . ARG   A 1 87   ? 99.458  127.850 160.054 1.00 39.53  1  51   ARG   A NH1 1 
ATOM   328   N NH2 . ARG   A 1 87   ? 100.854 126.038 160.044 1.00 40.08  0  51   ARG   A NH2 1 
ATOM   329   N N   . GLN   A 1 88   ? 105.551 129.169 163.578 1.00 34.91  0  52   GLN   A N   1 
ATOM   330   C CA  . GLN   A 1 88   ? 105.858 128.795 164.953 1.00 38.66  0  52   GLN   A CA  1 
ATOM   331   C C   . GLN   A 1 88   ? 106.900 129.719 165.572 1.00 39.76  0  52   GLN   A C   1 
ATOM   332   O O   . GLN   A 1 88   ? 106.814 130.037 166.763 1.00 39.32  0  52   GLN   A O   1 
ATOM   333   C CB  . GLN   A 1 88   ? 106.329 127.341 164.992 1.00 39.69  0  52   GLN   A CB  1 
ATOM   334   C CG  . GLN   A 1 88   ? 107.144 126.956 166.212 1.00 45.65  0  52   GLN   A CG  1 
ATOM   335   C CD  . GLN   A 1 88   ? 107.635 125.520 166.155 1.00 48.02  0  52   GLN   A CD  1 
ATOM   336   O OE1 . GLN   A 1 88   ? 107.360 124.795 165.200 1.00 43.82  0  52   GLN   A OE1 1 
ATOM   337   N NE2 . GLN   A 1 88   ? 108.369 125.105 167.180 1.00 43.18  0  52   GLN   A NE2 1 
ATOM   338   N N   . ASN   A 1 89   ? 107.877 130.168 164.787 1.00 36.59  0  53   ASN   A N   1 
ATOM   339   C CA  . ASN   A 1 89   ? 108.974 130.994 165.278 1.00 33.56  0  53   ASN   A CA  1 
ATOM   340   C C   . ASN   A 1 89   ? 109.365 132.013 164.216 1.00 30.46  0  53   ASN   A C   1 
ATOM   341   O O   . ASN   A 1 89   ? 110.339 131.801 163.486 1.00 39.42  0  53   ASN   A O   1 
ATOM   342   C CB  . ASN   A 1 89   ? 110.168 130.113 165.648 1.00 36.52  0  53   ASN   A CB  1 
ATOM   343   C CG  . ASN   A 1 89   ? 110.845 130.550 166.928 1.00 46.89  0  53   ASN   A CG  1 
ATOM   344   O OD1 . ASN   A 1 89   ? 110.353 131.424 167.639 1.00 48.94  0  53   ASN   A OD1 1 
ATOM   345   N ND2 . ASN   A 1 89   ? 111.978 129.931 167.234 1.00 47.95  0  53   ASN   A ND2 1 
ATOM   346   N N   . PRO   A 1 90   ? 108.647 133.129 164.103 1.00 26.59  0  54   PRO   A N   1 
ATOM   347   C CA  . PRO   A 1 90   ? 108.834 134.018 162.948 1.00 32.29  0  54   PRO   A CA  1 
ATOM   348   C C   . PRO   A 1 90   ? 110.147 134.782 162.969 1.00 36.52  0  54   PRO   A C   1 
ATOM   349   O O   . PRO   A 1 90   ? 110.938 134.653 163.908 1.00 42.29  0  54   PRO   A O   1 
ATOM   350   C CB  . PRO   A 1 90   ? 107.638 134.976 163.044 1.00 22.49  0  54   PRO   A CB  1 
ATOM   351   C CG  . PRO   A 1 90   ? 106.723 134.381 164.068 1.00 27.64  0  54   PRO   A CG  1 
ATOM   352   C CD  . PRO   A 1 90   ? 107.590 133.614 164.996 1.00 32.70  0  54   PRO   A CD  1 
ATOM   353   N N   . LEU   A 1 91   ? 110.388 135.577 161.930 1.00 39.64  0  55   LEU   A N   1 
ATOM   354   C CA  . LEU   A 1 91   ? 111.578 136.407 161.828 1.00 37.20  0  55   LEU   A CA  1 
ATOM   355   C C   . LEU   A 1 91   ? 111.250 137.852 162.169 1.00 38.44  0  55   LEU   A C   1 
ATOM   356   O O   . LEU   A 1 91   ? 110.119 138.308 161.997 1.00 38.90  0  55   LEU   A O   1 
ATOM   357   C CB  . LEU   A 1 91   ? 112.181 136.350 160.425 1.00 35.59  0  55   LEU   A CB  1 
ATOM   358   C CG  . LEU   A 1 91   ? 112.885 135.070 160.000 1.00 36.95  0  55   LEU   A CG  1 
ATOM   359   C CD1 . LEU   A 1 91   ? 113.314 135.187 158.552 1.00 33.49  0  55   LEU   A CD1 1 
ATOM   360   C CD2 . LEU   A 1 91   ? 114.074 134.813 160.901 1.00 38.53  0  55   LEU   A CD2 1 
ATOM   361   N N   . ILE   A 1 92   ? 112.270 138.576 162.632 1.00 36.35  0  56   ILE   A N   1 
ATOM   362   C CA  . ILE   A 1 92   ? 112.077 139.965 163.037 1.00 36.81  0  56   ILE   A CA  1 
ATOM   363   C C   . ILE   A 1 92   ? 111.642 140.816 161.852 1.00 41.72  0  56   ILE   A C   1 
ATOM   364   O O   . ILE   A 1 92   ? 110.753 141.665 161.975 1.00 45.15  0  56   ILE   A O   1 
ATOM   365   C CB  . ILE   A 1 92   ? 113.357 140.510 163.693 1.00 39.17  0  56   ILE   A CB  1 
ATOM   366   C CG1 . ILE   A 1 92   ? 113.692 139.698 164.945 1.00 39.19  0  56   ILE   A CG1 1 
ATOM   367   C CG2 . ILE   A 1 92   ? 113.189 141.975 164.041 1.00 39.96  0  56   ILE   A CG2 1 
ATOM   368   C CD1 . ILE   A 1 92   ? 115.170 139.466 165.150 1.00 40.17  0  56   ILE   A CD1 1 
ATOM   369   N N   . GLU   A 1 93   ? 112.261 140.608 160.689 1.00 38.89  0  57   GLU   A N   1 
ATOM   370   C CA  . GLU   A 1 93   ? 111.862 141.358 159.502 1.00 41.48  0  57   GLU   A CA  1 
ATOM   371   C C   . GLU   A 1 93   ? 110.429 141.033 159.096 1.00 46.11  0  57   GLU   A C   1 
ATOM   372   O O   . GLU   A 1 93   ? 109.672 141.926 158.691 1.00 50.90  0  57   GLU   A O   1 
ATOM   373   C CB  . GLU   A 1 93   ? 112.831 141.077 158.357 1.00 38.16  0  57   GLU   A CB  1 
ATOM   374   C CG  . GLU   A 1 93   ? 113.204 139.620 158.189 1.00 44.01  0  57   GLU   A CG  1 
ATOM   375   C CD  . GLU   A 1 93   ? 114.535 139.285 158.825 1.00 48.75  0  57   GLU   A CD  1 
ATOM   376   O OE1 . GLU   A 1 93   ? 115.043 140.110 159.612 1.00 44.85  0  57   GLU   A OE1 1 
ATOM   377   O OE2 . GLU   A 1 93   ? 115.076 138.198 158.536 1.00 49.82  -1 57   GLU   A OE2 1 
ATOM   378   N N   . HIS   A 1 94   ? 110.038 139.761 159.200 1.00 40.29  0  58   HIS   A N   1 
ATOM   379   C CA  . HIS   A 1 94   ? 108.660 139.384 158.904 1.00 33.74  0  58   HIS   A CA  1 
ATOM   380   C C   . HIS   A 1 94   ? 107.688 140.012 159.894 1.00 34.04  0  58   HIS   A C   1 
ATOM   381   O O   . HIS   A 1 94   ? 106.608 140.473 159.505 1.00 33.14  0  58   HIS   A O   1 
ATOM   382   C CB  . HIS   A 1 94   ? 108.523 137.863 158.905 1.00 35.86  0  58   HIS   A CB  1 
ATOM   383   C CG  . HIS   A 1 94   ? 109.356 137.182 157.865 1.00 36.76  0  58   HIS   A CG  1 
ATOM   384   N ND1 . HIS   A 1 94   ? 109.870 137.845 156.772 1.00 39.35  0  58   HIS   A ND1 1 
ATOM   385   C CD2 . HIS   A 1 94   ? 109.763 135.896 157.750 1.00 37.17  0  58   HIS   A CD2 1 
ATOM   386   C CE1 . HIS   A 1 94   ? 110.556 136.997 156.028 1.00 38.82  0  58   HIS   A CE1 1 
ATOM   387   N NE2 . HIS   A 1 94   ? 110.509 135.809 156.600 1.00 38.05  0  58   HIS   A NE2 1 
ATOM   388   N N   . MET   A 1 95   ? 108.049 140.038 161.179 1.00 36.17  0  59   MET   A N   1 
ATOM   389   C CA  . MET   A 1 95   ? 107.202 140.701 162.166 1.00 34.98  0  59   MET   A CA  1 
ATOM   390   C C   . MET   A 1 95   ? 107.052 142.181 161.852 1.00 40.55  0  59   MET   A C   1 
ATOM   391   O O   . MET   A 1 95   ? 105.951 142.732 161.946 1.00 53.39  0  59   MET   A O   1 
ATOM   392   C CB  . MET   A 1 95   ? 107.772 140.515 163.571 1.00 36.80  0  59   MET   A CB  1 
ATOM   393   C CG  . MET   A 1 95   ? 107.899 139.077 164.021 1.00 40.85  0  59   MET   A CG  1 
ATOM   394   S SD  . MET   A 1 95   ? 108.754 138.947 165.599 1.00 56.30  0  59   MET   A SD  1 
ATOM   395   C CE  . MET   A 1 95   ? 108.736 137.178 165.852 1.00 39.82  0  59   MET   A CE  1 
ATOM   396   N N   . ASN   A 1 96   ? 108.147 142.843 161.476 1.00 29.54  0  60   ASN   A N   1 
ATOM   397   C CA  . ASN   A 1 96   ? 108.069 144.259 161.135 1.00 32.38  0  60   ASN   A CA  1 
ATOM   398   C C   . ASN   A 1 96   ? 107.196 144.493 159.910 1.00 36.85  0  60   ASN   A C   1 
ATOM   399   O O   . ASN   A 1 96   ? 106.491 145.504 159.839 1.00 44.95  0  60   ASN   A O   1 
ATOM   400   C CB  . ASN   A 1 96   ? 109.467 144.827 160.905 1.00 34.48  0  60   ASN   A CB  1 
ATOM   401   C CG  . ASN   A 1 96   ? 110.379 144.624 162.095 1.00 44.85  0  60   ASN   A CG  1 
ATOM   402   O OD1 . ASN   A 1 96   ? 109.938 144.209 163.165 1.00 49.93  0  60   ASN   A OD1 1 
ATOM   403   N ND2 . ASN   A 1 96   ? 111.661 144.915 161.915 1.00 43.90  0  60   ASN   A ND2 1 
ATOM   404   N N   . LEU   A 1 97   ? 107.247 143.589 158.930 1.00 38.33  0  61   LEU   A N   1 
ATOM   405   C CA  . LEU   A 1 97   ? 106.350 143.703 157.783 1.00 35.45  0  61   LEU   A CA  1 
ATOM   406   C C   . LEU   A 1 97   ? 104.894 143.519 158.191 1.00 34.33  0  61   LEU   A C   1 
ATOM   407   O O   . LEU   A 1 97   ? 104.012 144.235 157.705 1.00 36.67  0  61   LEU   A O   1 
ATOM   408   C CB  . LEU   A 1 97   ? 106.729 142.684 156.713 1.00 37.53  0  61   LEU   A CB  1 
ATOM   409   C CG  . LEU   A 1 97   ? 107.498 143.208 155.505 1.00 37.30  0  61   LEU   A CG  1 
ATOM   410   C CD1 . LEU   A 1 97   ? 108.049 142.044 154.722 1.00 31.64  0  61   LEU   A CD1 1 
ATOM   411   C CD2 . LEU   A 1 97   ? 106.602 144.064 154.629 1.00 31.09  0  61   LEU   A CD2 1 
ATOM   412   N N   . LYS   A 1 98   ? 104.621 142.561 159.079 1.00 38.98  0  62   LYS   A N   1 
ATOM   413   C CA  . LYS   A 1 98   ? 103.238 142.253 159.429 1.00 35.86  0  62   LYS   A CA  1 
ATOM   414   C C   . LYS   A 1 98   ? 102.618 143.321 160.319 1.00 38.92  0  62   LYS   A C   1 
ATOM   415   O O   . LYS   A 1 98   ? 101.408 143.555 160.246 1.00 42.60  0  62   LYS   A O   1 
ATOM   416   C CB  . LYS   A 1 98   ? 103.156 140.895 160.123 1.00 32.79  0  62   LYS   A CB  1 
ATOM   417   C CG  . LYS   A 1 98   ? 101.740 140.377 160.283 1.00 34.87  0  62   LYS   A CG  1 
ATOM   418   C CD  . LYS   A 1 98   ? 101.718 139.017 160.948 1.00 36.02  0  62   LYS   A CD  1 
ATOM   419   C CE  . LYS   A 1 98   ? 100.308 138.469 161.041 1.00 35.31  0  62   LYS   A CE  1 
ATOM   420   N NZ  . LYS   A 1 98   ? 100.290 137.109 161.642 1.00 41.84  1  62   LYS   A NZ  1 
ATOM   421   N N   . LYS   A 1 99   ? 103.414 143.977 161.153 1.00 37.70  0  63   LYS   A N   1 
ATOM   422   C CA  . LYS   A 1 99   ? 102.887 144.829 162.207 1.00 34.38  0  63   LYS   A CA  1 
ATOM   423   C C   . LYS   A 1 99   ? 102.666 146.268 161.766 1.00 43.34  0  63   LYS   A C   1 
ATOM   424   O O   . LYS   A 1 99   ? 102.344 147.114 162.604 1.00 45.85  0  63   LYS   A O   1 
ATOM   425   C CB  . LYS   A 1 99   ? 103.814 144.782 163.421 1.00 38.22  0  63   LYS   A CB  1 
ATOM   426   C CG  . LYS   A 1 99   ? 103.778 143.441 164.134 1.00 42.00  0  63   LYS   A CG  1 
ATOM   427   C CD  . LYS   A 1 99   ? 104.834 143.342 165.213 1.00 48.95  0  63   LYS   A CD  1 
ATOM   428   C CE  . LYS   A 1 99   ? 104.777 141.991 165.901 1.00 47.88  0  63   LYS   A CE  1 
ATOM   429   N NZ  . LYS   A 1 99   ? 105.747 141.904 167.026 1.00 49.01  1  63   LYS   A NZ  1 
ATOM   430   N N   . LEU   A 1 100  ? 102.821 146.567 160.480 1.00 48.32  0  64   LEU   A N   1 
ATOM   431   C CA  . LEU   A 1 100  ? 102.481 147.892 159.992 1.00 48.47  0  64   LEU   A CA  1 
ATOM   432   C C   . LEU   A 1 100  ? 100.969 148.092 160.028 1.00 38.72  0  64   LEU   A C   1 
ATOM   433   O O   . LEU   A 1 100  ? 100.189 147.140 160.071 1.00 43.49  0  64   LEU   A O   1 
ATOM   434   C CB  . LEU   A 1 100  ? 103.000 148.096 158.570 1.00 46.75  0  64   LEU   A CB  1 
ATOM   435   C CG  . LEU   A 1 100  ? 104.476 147.819 158.302 1.00 44.29  0  64   LEU   A CG  1 
ATOM   436   C CD1 . LEU   A 1 100  ? 104.807 148.194 156.872 1.00 41.66  0  64   LEU   A CD1 1 
ATOM   437   C CD2 . LEU   A 1 100  ? 105.357 148.573 159.280 1.00 40.04  0  64   LEU   A CD2 1 
ATOM   438   N N   . ASN   A 1 101  ? 100.553 149.359 160.018 1.00 37.96  0  65   ASN   A N   1 
ATOM   439   C CA  . ASN   A 1 101  ? 99.127  149.663 160.048 1.00 46.93  0  65   ASN   A CA  1 
ATOM   440   C C   . ASN   A 1 101  ? 98.429  149.157 158.792 1.00 53.58  0  65   ASN   A C   1 
ATOM   441   O O   . ASN   A 1 101  ? 97.359  148.540 158.868 1.00 53.70  0  65   ASN   A O   1 
ATOM   442   C CB  . ASN   A 1 101  ? 98.917  151.168 160.211 1.00 46.14  0  65   ASN   A CB  1 
ATOM   443   C CG  . ASN   A 1 101  ? 99.279  151.660 161.596 1.00 52.43  0  65   ASN   A CG  1 
ATOM   444   O OD1 . ASN   A 1 101  ? 99.237  150.905 162.567 1.00 54.85  0  65   ASN   A OD1 1 
ATOM   445   N ND2 . ASN   A 1 101  ? 99.642  152.934 161.694 1.00 52.25  0  65   ASN   A ND2 1 
ATOM   446   N N   . ILE   A 1 102  ? 99.027  149.400 157.624 1.00 49.37  0  66   ILE   A N   1 
ATOM   447   C CA  . ILE   A 1 102  ? 98.396  149.000 156.372 1.00 44.37  0  66   ILE   A CA  1 
ATOM   448   C C   . ILE   A 1 102  ? 98.360  147.482 156.251 1.00 40.99  0  66   ILE   A C   1 
ATOM   449   O O   . ILE   A 1 102  ? 97.383  146.909 155.753 1.00 43.30  0  66   ILE   A O   1 
ATOM   450   C CB  . ILE   A 1 102  ? 99.114  149.657 155.179 1.00 38.72  0  66   ILE   A CB  1 
ATOM   451   C CG1 . ILE   A 1 102  ? 98.465  149.231 153.865 1.00 39.38  0  66   ILE   A CG1 1 
ATOM   452   C CG2 . ILE   A 1 102  ? 100.596 149.331 155.191 1.00 35.89  0  66   ILE   A CG2 1 
ATOM   453   C CD1 . ILE   A 1 102  ? 97.025  149.667 153.737 1.00 41.03  0  66   ILE   A CD1 1 
ATOM   454   N N   . THR   A 1 103  ? 99.413  146.804 156.711 1.00 38.05  0  67   THR   A N   1 
ATOM   455   C CA  . THR   A 1 103  ? 99.409  145.346 156.686 1.00 39.12  0  67   THR   A CA  1 
ATOM   456   C C   . THR   A 1 103  ? 98.330  144.784 157.600 1.00 44.91  0  67   THR   A C   1 
ATOM   457   O O   . THR   A 1 103  ? 97.655  143.810 157.248 1.00 52.73  0  67   THR   A O   1 
ATOM   458   C CB  . THR   A 1 103  ? 100.778 144.804 157.084 1.00 37.42  0  67   THR   A CB  1 
ATOM   459   O OG1 . THR   A 1 103  ? 101.757 145.255 156.143 1.00 52.37  0  67   THR   A OG1 1 
ATOM   460   C CG2 . THR   A 1 103  ? 100.759 143.293 157.087 1.00 35.05  0  67   THR   A CG2 1 
ATOM   461   N N   . GLN   A 1 104  ? 98.151  145.379 158.779 1.00 37.43  0  68   GLN   A N   1 
ATOM   462   C CA  . GLN   A 1 104  ? 97.091  144.919 159.668 1.00 34.32  0  68   GLN   A CA  1 
ATOM   463   C C   . GLN   A 1 104  ? 95.721  145.156 159.051 1.00 41.36  0  68   GLN   A C   1 
ATOM   464   O O   . GLN   A 1 104  ? 94.826  144.313 159.174 1.00 51.37  0  68   GLN   A O   1 
ATOM   465   C CB  . GLN   A 1 104  ? 97.200  145.606 161.025 1.00 36.61  0  68   GLN   A CB  1 
ATOM   466   C CG  . GLN   A 1 104  ? 98.421  145.192 161.827 1.00 45.85  0  68   GLN   A CG  1 
ATOM   467   C CD  . GLN   A 1 104  ? 98.358  143.760 162.309 1.00 44.57  0  68   GLN   A CD  1 
ATOM   468   O OE1 . GLN   A 1 104  ? 97.318  143.110 162.228 1.00 49.39  0  68   GLN   A OE1 1 
ATOM   469   N NE2 . GLN   A 1 104  ? 99.477  143.259 162.815 1.00 39.10  0  68   GLN   A NE2 1 
ATOM   470   N N   . SER   A 1 105  ? 95.540  146.292 158.374 1.00 36.69  0  69   SER   A N   1 
ATOM   471   C CA  . SER   A 1 105  ? 94.277  146.547 157.687 1.00 44.93  0  69   SER   A CA  1 
ATOM   472   C C   . SER   A 1 105  ? 94.014  145.499 156.612 1.00 42.94  0  69   SER   A C   1 
ATOM   473   O O   . SER   A 1 105  ? 92.899  144.976 156.496 1.00 37.87  0  69   SER   A O   1 
ATOM   474   C CB  . SER   A 1 105  ? 94.288  147.948 157.078 1.00 44.67  0  69   SER   A CB  1 
ATOM   475   O OG  . SER   A 1 105  ? 93.221  148.109 156.162 1.00 50.09  0  69   SER   A OG  1 
ATOM   476   N N   . LEU   A 1 106  ? 95.036  145.176 155.816 1.00 38.49  0  70   LEU   A N   1 
ATOM   477   C CA  . LEU   A 1 106  ? 94.862  144.189 154.754 1.00 35.88  0  70   LEU   A CA  1 
ATOM   478   C C   . LEU   A 1 106  ? 94.577  142.801 155.318 1.00 37.54  0  70   LEU   A C   1 
ATOM   479   O O   . LEU   A 1 106  ? 93.743  142.067 154.778 1.00 44.72  0  70   LEU   A O   1 
ATOM   480   C CB  . LEU   A 1 106  ? 96.095  144.161 153.856 1.00 34.98  0  70   LEU   A CB  1 
ATOM   481   C CG  . LEU   A 1 106  ? 96.354  145.429 153.047 1.00 33.31  0  70   LEU   A CG  1 
ATOM   482   C CD1 . LEU   A 1 106  ? 97.589  145.259 152.187 1.00 43.61  0  70   LEU   A CD1 1 
ATOM   483   C CD2 . LEU   A 1 106  ? 95.152  145.773 152.194 1.00 31.13  0  70   LEU   A CD2 1 
ATOM   484   N N   . ILE   A 1 107  ? 95.262  142.421 156.399 1.00 35.26  0  71   ILE   A N   1 
ATOM   485   C CA  . ILE   A 1 107  ? 95.005  141.125 157.022 1.00 40.64  0  71   ILE   A CA  1 
ATOM   486   C C   . ILE   A 1 107  ? 93.584  141.069 157.569 1.00 49.30  0  71   ILE   A C   1 
ATOM   487   O O   . ILE   A 1 107  ? 92.886  140.058 157.422 1.00 49.80  0  71   ILE   A O   1 
ATOM   488   C CB  . ILE   A 1 107  ? 96.043  140.841 158.120 1.00 43.24  0  71   ILE   A CB  1 
ATOM   489   C CG1 . ILE   A 1 107  ? 97.399  140.517 157.505 1.00 43.27  0  71   ILE   A CG1 1 
ATOM   490   C CG2 . ILE   A 1 107  ? 95.591  139.694 158.999 1.00 48.31  0  71   ILE   A CG2 1 
ATOM   491   C CD1 . ILE   A 1 107  ? 98.502  140.403 158.525 1.00 44.43  0  71   ILE   A CD1 1 
ATOM   492   N N   . SER   A 1 108  ? 93.133  142.150 158.212 1.00 41.76  0  72   SER   A N   1 
ATOM   493   C CA  . SER   A 1 108  ? 91.759  142.193 158.700 1.00 40.80  0  72   SER   A CA  1 
ATOM   494   C C   . SER   A 1 108  ? 90.767  142.081 157.551 1.00 46.62  0  72   SER   A C   1 
ATOM   495   O O   . SER   A 1 108  ? 89.718  141.442 157.688 1.00 52.18  0  72   SER   A O   1 
ATOM   496   C CB  . SER   A 1 108  ? 91.523  143.478 159.491 1.00 42.79  0  72   SER   A CB  1 
ATOM   497   O OG  . SER   A 1 108  ? 90.167  143.592 159.884 1.00 42.42  0  72   SER   A OG  1 
ATOM   498   N N   . LYS   A 1 109  ? 91.076  142.702 156.412 1.00 40.56  0  73   LYS   A N   1 
ATOM   499   C CA  . LYS   A 1 109  ? 90.220  142.546 155.241 1.00 35.11  0  73   LYS   A CA  1 
ATOM   500   C C   . LYS   A 1 109  ? 90.194  141.104 154.759 1.00 40.75  0  73   LYS   A C   1 
ATOM   501   O O   . LYS   A 1 109  ? 89.140  140.607 154.352 1.00 51.76  0  73   LYS   A O   1 
ATOM   502   C CB  . LYS   A 1 109  ? 90.685  143.462 154.113 1.00 40.85  0  73   LYS   A CB  1 
ATOM   503   C CG  . LYS   A 1 109  ? 90.216  144.895 154.226 1.00 45.75  0  73   LYS   A CG  1 
ATOM   504   C CD  . LYS   A 1 109  ? 90.754  145.720 153.075 1.00 45.67  0  73   LYS   A CD  1 
ATOM   505   C CE  . LYS   A 1 109  ? 90.456  147.192 153.260 1.00 43.80  0  73   LYS   A CE  1 
ATOM   506   N NZ  . LYS   A 1 109  ? 91.121  148.013 152.212 1.00 45.79  1  73   LYS   A NZ  1 
ATOM   507   N N   . TYR   A 1 110  ? 91.338  140.423 154.786 1.00 45.27  0  74   TYR   A N   1 
ATOM   508   C CA  . TYR   A 1 110  ? 91.430  139.056 154.286 1.00 46.96  0  74   TYR   A CA  1 
ATOM   509   C C   . TYR   A 1 110  ? 90.835  138.031 155.243 1.00 43.57  0  74   TYR   A C   1 
ATOM   510   O O   . TYR   A 1 110  ? 90.256  137.036 154.798 1.00 49.80  0  74   TYR   A O   1 
ATOM   511   C CB  . TYR   A 1 110  ? 92.889  138.697 153.993 1.00 46.27  0  74   TYR   A CB  1 
ATOM   512   C CG  . TYR   A 1 110  ? 93.098  137.237 153.675 1.00 44.48  0  74   TYR   A CG  1 
ATOM   513   C CD1 . TYR   A 1 110  ? 92.771  136.725 152.429 1.00 38.02  0  74   TYR   A CD1 1 
ATOM   514   C CD2 . TYR   A 1 110  ? 93.613  136.368 154.626 1.00 45.15  0  74   TYR   A CD2 1 
ATOM   515   C CE1 . TYR   A 1 110  ? 92.956  135.392 152.138 1.00 41.17  0  74   TYR   A CE1 1 
ATOM   516   C CE2 . TYR   A 1 110  ? 93.799  135.034 154.344 1.00 42.53  0  74   TYR   A CE2 1 
ATOM   517   C CZ  . TYR   A 1 110  ? 93.469  134.552 153.100 1.00 45.61  0  74   TYR   A CZ  1 
ATOM   518   O OH  . TYR   A 1 110  ? 93.655  133.221 152.816 1.00 53.38  0  74   TYR   A OH  1 
ATOM   519   N N   . HIS   A 1 111  ? 90.965  138.241 156.542 1.00 43.60  0  75   HIS   A N   1 
ATOM   520   C CA  . HIS   A 1 111  ? 90.455  137.255 157.490 1.00 48.49  0  75   HIS   A CA  1 
ATOM   521   C C   . HIS   A 1 111  ? 88.939  137.266 157.611 1.00 52.60  0  75   HIS   A C   1 
ATOM   522   O O   . HIS   A 1 111  ? 88.413  136.540 158.462 1.00 53.18  0  75   HIS   A O   1 
ATOM   523   C CB  . HIS   A 1 111  ? 91.083  137.481 158.864 1.00 54.00  0  75   HIS   A CB  1 
ATOM   524   C CG  . HIS   A 1 111  ? 92.339  136.701 159.092 1.00 56.29  0  75   HIS   A CG  1 
ATOM   525   N ND1 . HIS   A 1 111  ? 92.443  135.722 160.056 1.00 55.34  0  75   HIS   A ND1 1 
ATOM   526   C CD2 . HIS   A 1 111  ? 93.546  136.757 158.481 1.00 55.42  0  75   HIS   A CD2 1 
ATOM   527   C CE1 . HIS   A 1 111  ? 93.659  135.208 160.030 1.00 58.55  0  75   HIS   A CE1 1 
ATOM   528   N NE2 . HIS   A 1 111  ? 94.349  135.819 159.083 1.00 58.87  0  75   HIS   A NE2 1 
ATOM   529   N N   . LYS   A 1 112  ? 88.217  138.049 156.810 1.00 56.03  0  76   LYS   A N   1 
ATOM   530   C CA  . LYS   A 1 112  ? 86.761  138.119 156.887 1.00 55.15  0  76   LYS   A CA  1 
ATOM   531   C C   . LYS   A 1 112  ? 86.068  137.156 155.923 1.00 58.52  0  76   LYS   A C   1 
ATOM   532   O O   . LYS   A 1 112  ? 85.216  136.374 156.354 1.00 59.32  0  76   LYS   A O   1 
ATOM   533   C CB  . LYS   A 1 112  ? 86.287  139.562 156.653 1.00 47.66  0  76   LYS   A CB  1 
ATOM   534   C CG  . LYS   A 1 112  ? 86.595  140.503 157.801 1.00 50.60  0  76   LYS   A CG  1 
ATOM   535   C CD  . LYS   A 1 112  ? 86.058  141.895 157.529 1.00 55.59  0  76   LYS   A CD  1 
ATOM   536   C CE  . LYS   A 1 112  ? 86.412  142.849 158.654 1.00 55.27  0  76   LYS   A CE  1 
ATOM   537   N NZ  . LYS   A 1 112  ? 86.029  144.248 158.327 1.00 55.85  1  76   LYS   A NZ  1 
ATOM   538   N N   . GLY   A 1 113  ? 86.402  137.184 154.630 1.00 51.57  0  77   GLY   A N   1 
ATOM   539   C CA  . GLY   A 1 113  ? 87.380  137.974 153.903 1.00 49.11  0  77   GLY   A CA  1 
ATOM   540   C C   . GLY   A 1 113  ? 86.859  138.577 152.616 1.00 49.63  0  77   GLY   A C   1 
ATOM   541   O O   . GLY   A 1 113  ? 86.288  137.883 151.779 1.00 53.74  0  77   GLY   A O   1 
ATOM   542   N N   . GLU   A 1 114  ? 87.058  139.886 152.463 1.00 50.83  0  78   GLU   A N   1 
ATOM   543   C CA  . GLU   A 1 114  ? 86.646  140.572 151.248 1.00 51.37  0  78   GLU   A CA  1 
ATOM   544   C C   . GLU   A 1 114  ? 87.670  140.453 150.129 1.00 53.34  0  78   GLU   A C   1 
ATOM   545   O O   . GLU   A 1 114  ? 87.299  140.564 148.957 1.00 57.24  0  78   GLU   A O   1 
ATOM   546   C CB  . GLU   A 1 114  ? 86.380  142.051 151.539 1.00 52.18  0  78   GLU   A CB  1 
ATOM   547   C CG  . GLU   A 1 114  ? 85.157  142.309 152.399 1.00 52.68  0  78   GLU   A CG  1 
ATOM   548   C CD  . GLU   A 1 114  ? 85.477  142.333 153.879 1.00 57.91  0  78   GLU   A CD  1 
ATOM   549   O OE1 . GLU   A 1 114  ? 86.555  141.839 154.262 1.00 63.93  0  78   GLU   A OE1 1 
ATOM   550   O OE2 . GLU   A 1 114  ? 84.650  142.848 154.659 1.00 57.41  -1 78   GLU   A OE2 1 
ATOM   551   N N   . ILE   A 1 115  ? 88.939  140.231 150.458 1.00 48.22  0  79   ILE   A N   1 
ATOM   552   C CA  . ILE   A 1 115  ? 89.997  140.133 149.461 1.00 49.60  0  79   ILE   A CA  1 
ATOM   553   C C   . ILE   A 1 115  ? 90.457  138.686 149.368 1.00 50.90  0  79   ILE   A C   1 
ATOM   554   O O   . ILE   A 1 115  ? 90.318  137.903 150.314 1.00 47.68  0  79   ILE   A O   1 
ATOM   555   C CB  . ILE   A 1 115  ? 91.179  141.070 149.786 1.00 38.56  0  79   ILE   A CB  1 
ATOM   556   C CG1 . ILE   A 1 115  ? 91.911  140.601 151.041 1.00 35.58  0  79   ILE   A CG1 1 
ATOM   557   C CG2 . ILE   A 1 115  ? 90.691  142.490 149.970 1.00 40.67  0  79   ILE   A CG2 1 
ATOM   558   C CD1 . ILE   A 1 115  ? 93.094  141.456 151.404 1.00 31.73  0  79   ILE   A CD1 1 
ATOM   559   N N   . LYS   A 1 116  ? 91.003  138.330 148.209 1.00 45.20  0  80   LYS   A N   1 
ATOM   560   C CA  . LYS   A 1 116  ? 91.429  136.968 147.926 1.00 37.29  0  80   LYS   A CA  1 
ATOM   561   C C   . LYS   A 1 116  ? 92.938  136.907 147.744 1.00 34.78  0  80   LYS   A C   1 
ATOM   562   O O   . LYS   A 1 116  ? 93.541  137.800 147.141 1.00 30.95  0  80   LYS   A O   1 
ATOM   563   C CB  . LYS   A 1 116  ? 90.732  136.423 146.679 1.00 31.29  0  80   LYS   A CB  1 
ATOM   564   C CG  . LYS   A 1 116  ? 89.267  136.796 146.574 1.00 38.73  0  80   LYS   A CG  1 
ATOM   565   C CD  . LYS   A 1 116  ? 88.525  135.841 145.656 1.00 49.05  0  80   LYS   A CD  1 
ATOM   566   C CE  . LYS   A 1 116  ? 88.613  134.410 146.158 1.00 47.79  0  80   LYS   A CE  1 
ATOM   567   N NZ  . LYS   A 1 116  ? 87.968  134.251 147.490 1.00 46.21  1  80   LYS   A NZ  1 
ATOM   568   N N   . LEU   A 1 117  ? 93.538  135.842 148.265 1.00 31.81  0  81   LEU   A N   1 
ATOM   569   C CA  . LEU   A 1 117  ? 94.973  135.630 148.185 1.00 25.67  0  81   LEU   A CA  1 
ATOM   570   C C   . LEU   A 1 117  ? 95.333  134.971 146.860 1.00 34.37  0  81   LEU   A C   1 
ATOM   571   O O   . LEU   A 1 117  ? 94.639  134.063 146.399 1.00 47.26  0  81   LEU   A O   1 
ATOM   572   C CB  . LEU   A 1 117  ? 95.434  134.759 149.352 1.00 27.87  0  81   LEU   A CB  1 
ATOM   573   C CG  . LEU   A 1 117  ? 96.907  134.387 149.391 1.00 29.33  0  81   LEU   A CG  1 
ATOM   574   C CD1 . LEU   A 1 117  ? 97.727  135.651 149.383 1.00 31.15  0  81   LEU   A CD1 1 
ATOM   575   C CD2 . LEU   A 1 117  ? 97.202  133.559 150.622 1.00 31.12  0  81   LEU   A CD2 1 
ATOM   576   N N   . GLU   A 1 118  ? 96.415  135.441 146.241 1.00 26.29  0  82   GLU   A N   1 
ATOM   577   C CA  . GLU   A 1 118  ? 96.847  134.926 144.950 1.00 23.81  0  82   GLU   A CA  1 
ATOM   578   C C   . GLU   A 1 118  ? 98.361  134.774 144.931 1.00 30.02  0  82   GLU   A C   1 
ATOM   579   O O   . GLU   A 1 118  ? 99.078  135.338 145.759 1.00 37.85  0  82   GLU   A O   1 
ATOM   580   C CB  . GLU   A 1 118  ? 96.385  135.829 143.799 1.00 23.85  0  82   GLU   A CB  1 
ATOM   581   C CG  . GLU   A 1 118  ? 95.155  135.311 143.074 1.00 29.13  0  82   GLU   A CG  1 
ATOM   582   C CD  . GLU   A 1 118  ? 93.861  135.658 143.782 1.00 40.74  0  82   GLU   A CD  1 
ATOM   583   O OE1 . GLU   A 1 118  ? 93.905  136.441 144.751 1.00 43.24  0  82   GLU   A OE1 1 
ATOM   584   O OE2 . GLU   A 1 118  ? 92.799  135.139 143.377 1.00 38.22  -1 82   GLU   A OE2 1 
ATOM   585   N N   . GLU   A 1 119  ? 98.839  133.986 143.971 1.00 35.40  0  83   GLU   A N   1 
ATOM   586   C CA  . GLU   A 1 119  ? 100.260 133.747 143.755 1.00 36.20  0  83   GLU   A CA  1 
ATOM   587   C C   . GLU   A 1 119  ? 100.886 134.941 143.031 1.00 40.94  0  83   GLU   A C   1 
ATOM   588   O O   . GLU   A 1 119  ? 100.199 135.631 142.273 1.00 40.32  0  83   GLU   A O   1 
ATOM   589   C CB  . GLU   A 1 119  ? 100.461 132.466 142.939 1.00 33.70  0  83   GLU   A CB  1 
ATOM   590   C CG  . GLU   A 1 119  ? 101.814 131.798 143.127 1.00 41.24  0  83   GLU   A CG  1 
ATOM   591   C CD  . GLU   A 1 119  ? 101.833 130.343 142.713 1.00 44.42  0  83   GLU   A CD  1 
ATOM   592   O OE1 . GLU   A 1 119  ? 100.952 129.582 143.161 1.00 40.44  0  83   GLU   A OE1 1 
ATOM   593   O OE2 . GLU   A 1 119  ? 102.735 129.959 141.941 1.00 45.75  -1 83   GLU   A OE2 1 
ATOM   594   N N   . PRO   A 1 120  ? 102.186 135.214 143.257 1.00 36.13  0  84   PRO   A N   1 
ATOM   595   C CA  . PRO   A 1 120  ? 102.835 136.362 142.610 1.00 31.72  0  84   PRO   A CA  1 
ATOM   596   C C   . PRO   A 1 120  ? 102.598 136.488 141.114 1.00 28.09  0  84   PRO   A C   1 
ATOM   597   O O   . PRO   A 1 120  ? 102.510 137.605 140.593 1.00 33.32  0  84   PRO   A O   1 
ATOM   598   C CB  . PRO   A 1 120  ? 104.317 136.113 142.904 1.00 30.03  0  84   PRO   A CB  1 
ATOM   599   C CG  . PRO   A 1 120  ? 104.313 135.439 144.227 1.00 28.50  0  84   PRO   A CG  1 
ATOM   600   C CD  . PRO   A 1 120  ? 103.010 134.688 144.360 1.00 33.91  0  84   PRO   A CD  1 
ATOM   601   N N   . THR   A 1 121  ? 102.498 135.364 140.408 1.00 26.27  0  85   THR   A N   1 
ATOM   602   C CA  . THR   A 1 121  ? 102.364 135.426 138.958 1.00 30.55  0  85   THR   A CA  1 
ATOM   603   C C   . THR   A 1 121  ? 101.031 136.014 138.515 1.00 31.66  0  85   THR   A C   1 
ATOM   604   O O   . THR   A 1 121  ? 100.956 136.602 137.427 1.00 19.52  0  85   THR   A O   1 
ATOM   605   C CB  . THR   A 1 121  ? 102.547 134.041 138.350 1.00 20.01  0  85   THR   A CB  1 
ATOM   606   O OG1 . THR   A 1 121  ? 103.564 133.338 139.073 1.00 25.59  0  85   THR   A OG1 1 
ATOM   607   C CG2 . THR   A 1 121  ? 103.004 134.191 136.928 1.00 23.46  0  85   THR   A CG2 1 
ATOM   608   N N   . TYR   A 1 122  ? 99.989  135.895 139.341 1.00 38.80  0  86   TYR   A N   1 
ATOM   609   C CA  . TYR   A 1 122  ? 98.722  136.557 139.046 1.00 35.83  0  86   TYR   A CA  1 
ATOM   610   C C   . TYR   A 1 122  ? 98.921  138.063 138.916 1.00 35.14  0  86   TYR   A C   1 
ATOM   611   O O   . TYR   A 1 122  ? 98.478  138.684 137.945 1.00 43.72  0  86   TYR   A O   1 
ATOM   612   C CB  . TYR   A 1 122  ? 97.704  136.235 140.144 1.00 30.55  0  86   TYR   A CB  1 
ATOM   613   C CG  . TYR   A 1 122  ? 96.275  136.595 139.796 1.00 39.01  0  86   TYR   A CG  1 
ATOM   614   C CD1 . TYR   A 1 122  ? 95.827  137.907 139.865 1.00 40.36  0  86   TYR   A CD1 1 
ATOM   615   C CD2 . TYR   A 1 122  ? 95.369  135.617 139.418 1.00 37.76  0  86   TYR   A CD2 1 
ATOM   616   C CE1 . TYR   A 1 122  ? 94.526  138.235 139.546 1.00 36.72  0  86   TYR   A CE1 1 
ATOM   617   C CE2 . TYR   A 1 122  ? 94.066  135.937 139.103 1.00 38.67  0  86   TYR   A CE2 1 
ATOM   618   C CZ  . TYR   A 1 122  ? 93.650  137.243 139.168 1.00 37.28  0  86   TYR   A CZ  1 
ATOM   619   O OH  . TYR   A 1 122  ? 92.348  137.548 138.851 1.00 38.68  0  86   TYR   A OH  1 
ATOM   620   N N   . PHE   A 1 123  ? 99.620  138.663 139.880 1.00 33.70  0  87   PHE   A N   1 
ATOM   621   C CA  . PHE   A 1 123  ? 99.931  140.087 139.822 1.00 24.60  0  87   PHE   A CA  1 
ATOM   622   C C   . PHE   A 1 123  ? 100.995 140.426 138.793 1.00 22.24  0  87   PHE   A C   1 
ATOM   623   O O   . PHE   A 1 123  ? 101.013 141.554 138.302 1.00 26.85  0  87   PHE   A O   1 
ATOM   624   C CB  . PHE   A 1 123  ? 100.339 140.588 141.200 1.00 21.23  0  87   PHE   A CB  1 
ATOM   625   C CG  . PHE   A 1 123  ? 99.186  140.775 142.120 1.00 20.02  0  87   PHE   A CG  1 
ATOM   626   C CD1 . PHE   A 1 123  ? 98.180  141.657 141.807 1.00 32.60  0  87   PHE   A CD1 1 
ATOM   627   C CD2 . PHE   A 1 123  ? 99.058  140.007 143.245 1.00 18.05  0  87   PHE   A CD2 1 
ATOM   628   C CE1 . PHE   A 1 123  ? 97.104  141.816 142.644 1.00 38.08  0  87   PHE   A CE1 1 
ATOM   629   C CE2 . PHE   A 1 123  ? 97.993  140.161 144.087 1.00 25.42  0  87   PHE   A CE2 1 
ATOM   630   C CZ  . PHE   A 1 123  ? 97.017  141.063 143.786 1.00 37.41  0  87   PHE   A CZ  1 
ATOM   631   N N   . GLN   A 1 124  ? 101.886 139.498 138.447 1.00 24.46  0  88   GLN   A N   1 
ATOM   632   C CA  . GLN   A 1 124  ? 102.761 139.773 137.313 1.00 25.70  0  88   GLN   A CA  1 
ATOM   633   C C   . GLN   A 1 124  ? 101.935 139.964 136.049 1.00 29.26  0  88   GLN   A C   1 
ATOM   634   O O   . GLN   A 1 124  ? 102.133 140.931 135.302 1.00 35.51  0  88   GLN   A O   1 
ATOM   635   C CB  . GLN   A 1 124  ? 103.781 138.652 137.129 1.00 23.39  0  88   GLN   A CB  1 
ATOM   636   C CG  . GLN   A 1 124  ? 104.610 138.788 135.853 1.00 25.45  0  88   GLN   A CG  1 
ATOM   637   C CD  . GLN   A 1 124  ? 105.517 137.600 135.601 1.00 25.00  0  88   GLN   A CD  1 
ATOM   638   O OE1 . GLN   A 1 124  ? 106.220 137.142 136.499 1.00 18.80  0  88   GLN   A OE1 1 
ATOM   639   N NE2 . GLN   A 1 124  ? 105.503 137.095 134.374 1.00 20.94  0  88   GLN   A NE2 1 
ATOM   640   N N   . SER   A 1 125  ? 100.965 139.076 135.827 1.00 23.34  0  89   SER   A N   1 
ATOM   641   C CA  . SER   A 1 125  ? 100.062 139.219 134.690 1.00 25.04  0  89   SER   A CA  1 
ATOM   642   C C   . SER   A 1 125  ? 99.227  140.490 134.794 1.00 27.03  0  89   SER   A C   1 
ATOM   643   O O   . SER   A 1 125  ? 98.969  141.152 133.783 1.00 19.18  0  89   SER   A O   1 
ATOM   644   C CB  . SER   A 1 125  ? 99.162  137.991 134.589 1.00 31.17  0  89   SER   A CB  1 
ATOM   645   O OG  . SER   A 1 125  ? 98.547  137.714 135.833 1.00 31.11  0  89   SER   A OG  1 
ATOM   646   N N   . LEU   A 1 126  ? 98.778  140.833 136.005 1.00 33.45  0  90   LEU   A N   1 
ATOM   647   C CA  . LEU   A 1 126  ? 97.986  142.047 136.200 1.00 27.94  0  90   LEU   A CA  1 
ATOM   648   C C   . LEU   A 1 126  ? 98.795  143.303 135.899 1.00 32.68  0  90   LEU   A C   1 
ATOM   649   O O   . LEU   A 1 126  ? 98.298  144.230 135.250 1.00 35.96  0  90   LEU   A O   1 
ATOM   650   C CB  . LEU   A 1 126  ? 97.446  142.100 137.627 1.00 21.28  0  90   LEU   A CB  1 
ATOM   651   C CG  . LEU   A 1 126  ? 96.014  141.619 137.821 1.00 24.69  0  90   LEU   A CG  1 
ATOM   652   C CD1 . LEU   A 1 126  ? 95.669  141.589 139.292 1.00 33.78  0  90   LEU   A CD1 1 
ATOM   653   C CD2 . LEU   A 1 126  ? 95.073  142.534 137.070 1.00 29.56  0  90   LEU   A CD2 1 
ATOM   654   N N   . LEU   A 1 127  ? 100.035 143.361 136.382 1.00 29.90  0  91   LEU   A N   1 
ATOM   655   C CA  . LEU   A 1 127  ? 100.885 144.518 136.139 1.00 18.92  0  91   LEU   A CA  1 
ATOM   656   C C   . LEU   A 1 127  ? 101.184 144.670 134.660 1.00 26.59  0  91   LEU   A C   1 
ATOM   657   O O   . LEU   A 1 127  ? 100.950 145.730 134.075 1.00 37.50  0  91   LEU   A O   1 
ATOM   658   C CB  . LEU   A 1 127  ? 102.186 144.395 136.930 1.00 17.65  0  91   LEU   A CB  1 
ATOM   659   C CG  . LEU   A 1 127  ? 102.133 144.663 138.426 1.00 28.75  0  91   LEU   A CG  1 
ATOM   660   C CD1 . LEU   A 1 127  ? 103.201 143.870 139.125 1.00 14.66  0  91   LEU   A CD1 1 
ATOM   661   C CD2 . LEU   A 1 127  ? 102.327 146.140 138.680 1.00 38.55  0  91   LEU   A CD2 1 
ATOM   662   N N   . MET   A 1 128  ? 101.668 143.603 134.025 1.00 25.05  0  92   MET   A N   1 
ATOM   663   C CA  . MET   A 1 128  ? 102.169 143.750 132.664 1.00 25.69  0  92   MET   A CA  1 
ATOM   664   C C   . MET   A 1 128  ? 101.072 144.083 131.660 1.00 28.91  0  92   MET   A C   1 
ATOM   665   O O   . MET   A 1 128  ? 101.353 144.257 130.472 1.00 40.08  0  92   MET   A O   1 
ATOM   666   C CB  . MET   A 1 128  ? 102.923 142.495 132.236 1.00 27.44  0  92   MET   A CB  1 
ATOM   667   C CG  . MET   A 1 128  ? 103.983 142.063 133.227 1.00 27.24  0  92   MET   A CG  1 
ATOM   668   S SD  . MET   A 1 128  ? 105.421 143.142 133.211 1.00 35.90  0  92   MET   A SD  1 
ATOM   669   C CE  . MET   A 1 128  ? 105.915 143.049 134.927 1.00 34.19  0  92   MET   A CE  1 
ATOM   670   N N   . THR   A 1 129  ? 99.825  144.183 132.118 1.00 30.43  0  93   THR   A N   1 
ATOM   671   C CA  . THR   A 1 129  ? 98.730  144.649 131.277 1.00 34.51  0  93   THR   A CA  1 
ATOM   672   C C   . THR   A 1 129  ? 98.068  145.905 131.828 1.00 38.37  0  93   THR   A C   1 
ATOM   673   O O   . THR   A 1 129  ? 96.981  146.271 131.369 1.00 44.50  0  93   THR   A O   1 
ATOM   674   C CB  . THR   A 1 129  ? 97.680  143.552 131.098 1.00 39.75  0  93   THR   A CB  1 
ATOM   675   O OG1 . THR   A 1 129  ? 96.694  143.990 130.157 1.00 40.42  0  93   THR   A OG1 1 
ATOM   676   C CG2 . THR   A 1 129  ? 97.001  143.245 132.419 1.00 34.32  0  93   THR   A CG2 1 
ATOM   677   N N   . TYR   A 1 130  ? 98.699  146.581 132.788 1.00 45.09  0  94   TYR   A N   1 
ATOM   678   C CA  . TYR   A 1 130  ? 98.128  147.768 133.413 1.00 43.86  0  94   TYR   A CA  1 
ATOM   679   C C   . TYR   A 1 130  ? 97.989  148.891 132.395 1.00 50.66  0  94   TYR   A C   1 
ATOM   680   O O   . TYR   A 1 130  ? 98.984  149.485 131.972 1.00 47.82  0  94   TYR   A O   1 
ATOM   681   C CB  . TYR   A 1 130  ? 98.995  148.199 134.601 1.00 45.12  0  94   TYR   A CB  1 
ATOM   682   C CG  . TYR   A 1 130  ? 98.898  149.658 134.998 1.00 47.24  0  94   TYR   A CG  1 
ATOM   683   C CD1 . TYR   A 1 130  ? 97.867  150.110 135.806 1.00 48.52  0  94   TYR   A CD1 1 
ATOM   684   C CD2 . TYR   A 1 130  ? 99.859  150.575 134.594 1.00 48.77  0  94   TYR   A CD2 1 
ATOM   685   C CE1 . TYR   A 1 130  ? 97.782  151.437 136.179 1.00 48.91  0  94   TYR   A CE1 1 
ATOM   686   C CE2 . TYR   A 1 130  ? 99.780  151.901 134.959 1.00 47.77  0  94   TYR   A CE2 1 
ATOM   687   C CZ  . TYR   A 1 130  ? 98.742  152.327 135.753 1.00 47.67  0  94   TYR   A CZ  1 
ATOM   688   O OH  . TYR   A 1 130  ? 98.662  153.649 136.121 1.00 47.32  0  94   TYR   A OH  1 
ATOM   689   N N   . LYS   A 1 131  ? 96.757  149.170 131.980 1.00 61.81  0  95   LYS   A N   1 
ATOM   690   C CA  . LYS   A 1 131  ? 96.465  150.243 131.043 1.00 62.36  0  95   LYS   A CA  1 
ATOM   691   C C   . LYS   A 1 131  ? 95.730  151.404 131.693 1.00 60.51  0  95   LYS   A C   1 
ATOM   692   O O   . LYS   A 1 131  ? 95.340  152.343 130.993 1.00 62.16  0  95   LYS   A O   1 
ATOM   693   C CB  . LYS   A 1 131  ? 95.642  149.709 129.866 1.00 59.82  0  95   LYS   A CB  1 
ATOM   694   C CG  . LYS   A 1 131  ? 96.464  149.340 128.643 1.00 62.35  0  95   LYS   A CG  1 
ATOM   695   C CD  . LYS   A 1 131  ? 96.651  150.535 127.724 1.00 63.80  0  95   LYS   A CD  1 
ATOM   696   C CE  . LYS   A 1 131  ? 97.812  150.324 126.767 1.00 60.39  0  95   LYS   A CE  1 
ATOM   697   N NZ  . LYS   A 1 131  ? 98.363  151.613 126.262 1.00 59.11  1  95   LYS   A NZ  1 
ATOM   698   N N   . SER   A 1 132  ? 95.536  151.366 133.011 1.00 67.75  0  96   SER   A N   1 
ATOM   699   C CA  . SER   A 1 132  ? 94.791  152.400 133.727 1.00 68.71  0  96   SER   A CA  1 
ATOM   700   C C   . SER   A 1 132  ? 95.660  153.650 133.826 1.00 67.66  0  96   SER   A C   1 
ATOM   701   O O   . SER   A 1 132  ? 96.253  153.964 134.861 1.00 67.28  0  96   SER   A O   1 
ATOM   702   C CB  . SER   A 1 132  ? 94.369  151.900 135.103 1.00 63.76  0  96   SER   A CB  1 
ATOM   703   O OG  . SER   A 1 132  ? 93.577  150.731 134.997 1.00 63.02  0  96   SER   A OG  1 
ATOM   704   N N   . MET   A 1 133  ? 95.735  154.375 132.714 1.00 69.06  0  97   MET   A N   1 
ATOM   705   C CA  . MET   A 1 133  ? 96.492  155.616 132.622 1.00 65.76  0  97   MET   A CA  1 
ATOM   706   C C   . MET   A 1 133  ? 95.517  156.756 132.370 1.00 66.45  0  97   MET   A C   1 
ATOM   707   O O   . MET   A 1 133  ? 94.740  156.711 131.411 1.00 67.21  0  97   MET   A O   1 
ATOM   708   C CB  . MET   A 1 133  ? 97.531  155.539 131.503 1.00 65.73  0  97   MET   A CB  1 
ATOM   709   C CG  . MET   A 1 133  ? 98.114  154.150 131.293 1.00 65.96  0  97   MET   A CG  1 
ATOM   710   S SD  . MET   A 1 133  ? 99.556  154.151 130.208 1.00 82.44  0  97   MET   A SD  1 
ATOM   711   C CE  . MET   A 1 133  ? 100.329 152.603 130.666 1.00 65.60  0  97   MET   A CE  1 
ATOM   712   N N   . THR   A 1 134  ? 95.557  157.773 133.226 1.00 67.53  0  98   THR   A N   1 
ATOM   713   C CA  . THR   A 1 134  ? 94.718  158.941 133.025 1.00 66.80  0  98   THR   A CA  1 
ATOM   714   C C   . THR   A 1 134  ? 95.261  159.789 131.878 1.00 65.65  0  98   THR   A C   1 
ATOM   715   O O   . THR   A 1 134  ? 96.350  159.550 131.349 1.00 66.82  0  98   THR   A O   1 
ATOM   716   C CB  . THR   A 1 134  ? 94.628  159.771 134.307 1.00 67.89  0  98   THR   A CB  1 
ATOM   717   O OG1 . THR   A 1 134  ? 93.774  160.900 134.087 1.00 68.51  0  98   THR   A OG1 1 
ATOM   718   C CG2 . THR   A 1 134  ? 95.999  160.259 134.726 1.00 63.62  0  98   THR   A CG2 1 
ATOM   719   N N   . SER   A 1 135  ? 94.474  160.792 131.485 1.00 65.20  0  99   SER   A N   1 
ATOM   720   C CA  . SER   A 1 135  ? 94.884  161.668 130.392 1.00 66.96  0  99   SER   A CA  1 
ATOM   721   C C   . SER   A 1 135  ? 96.167  162.414 130.733 1.00 66.48  0  99   SER   A C   1 
ATOM   722   O O   . SER   A 1 135  ? 97.057  162.556 129.885 1.00 66.92  0  99   SER   A O   1 
ATOM   723   C CB  . SER   A 1 135  ? 93.763  162.652 130.062 1.00 67.39  0  99   SER   A CB  1 
ATOM   724   O OG  . SER   A 1 135  ? 93.438  163.444 131.190 1.00 69.09  0  99   SER   A OG  1 
ATOM   725   N N   . SER   A 1 136  ? 96.280  162.898 131.972 1.00 62.78  0  100  SER   A N   1 
ATOM   726   C CA  . SER   A 1 136  ? 97.499  163.585 132.383 1.00 61.98  0  100  SER   A CA  1 
ATOM   727   C C   . SER   A 1 136  ? 98.698  162.649 132.351 1.00 65.57  0  100  SER   A C   1 
ATOM   728   O O   . SER   A 1 136  ? 99.778  163.032 131.890 1.00 69.62  0  100  SER   A O   1 
ATOM   729   C CB  . SER   A 1 136  ? 97.326  164.184 133.777 1.00 63.58  0  100  SER   A CB  1 
ATOM   730   O OG  . SER   A 1 136  ? 98.531  164.784 134.222 1.00 66.47  0  100  SER   A OG  1 
ATOM   731   N N   . GLU   A 1 137  ? 98.533  161.416 132.837 1.00 57.37  0  101  GLU   A N   1 
ATOM   732   C CA  . GLU   A 1 137  ? 99.637  160.461 132.809 1.00 60.46  0  101  GLU   A CA  1 
ATOM   733   C C   . GLU   A 1 137  ? 99.997  160.070 131.381 1.00 60.26  0  101  GLU   A C   1 
ATOM   734   O O   . GLU   A 1 137  ? 101.182 159.935 131.049 1.00 57.56  0  101  GLU   A O   1 
ATOM   735   C CB  . GLU   A 1 137  ? 99.289  159.224 133.633 1.00 58.96  0  101  GLU   A CB  1 
ATOM   736   C CG  . GLU   A 1 137  ? 100.498 158.497 134.184 1.00 54.37  0  101  GLU   A CG  1 
ATOM   737   C CD  . GLU   A 1 137  ? 101.306 159.353 135.134 1.00 57.87  0  101  GLU   A CD  1 
ATOM   738   O OE1 . GLU   A 1 137  ? 100.706 160.193 135.837 1.00 59.09  0  101  GLU   A OE1 1 
ATOM   739   O OE2 . GLU   A 1 137  ? 102.543 159.190 135.178 1.00 55.88  -1 101  GLU   A OE2 1 
ATOM   740   N N   . GLN   A 1 138  ? 98.989  159.872 130.528 1.00 58.81  0  102  GLN   A N   1 
ATOM   741   C CA  . GLN   A 1 138  ? 99.249  159.597 129.119 1.00 55.89  0  102  GLN   A CA  1 
ATOM   742   C C   . GLN   A 1 138  ? 100.081 160.707 128.498 1.00 59.97  0  102  GLN   A C   1 
ATOM   743   O O   . GLN   A 1 138  ? 101.092 160.448 127.836 1.00 65.39  0  102  GLN   A O   1 
ATOM   744   C CB  . GLN   A 1 138  ? 97.932  159.442 128.358 1.00 56.21  0  102  GLN   A CB  1 
ATOM   745   C CG  . GLN   A 1 138  ? 97.260  158.090 128.495 1.00 65.07  0  102  GLN   A CG  1 
ATOM   746   C CD  . GLN   A 1 138  ? 95.914  158.046 127.793 1.00 68.26  0  102  GLN   A CD  1 
ATOM   747   O OE1 . GLN   A 1 138  ? 95.735  158.644 126.732 1.00 67.43  0  102  GLN   A OE1 1 
ATOM   748   N NE2 . GLN   A 1 138  ? 94.957  157.339 128.386 1.00 61.30  0  102  GLN   A NE2 1 
ATOM   749   N N   . ILE   A 1 139  ? 99.670  161.958 128.712 1.00 47.52  0  103  ILE   A N   1 
ATOM   750   C CA  . ILE   A 1 139  ? 100.393 163.084 128.136 1.00 44.89  0  103  ILE   A CA  1 
ATOM   751   C C   . ILE   A 1 139  ? 101.804 163.164 128.704 1.00 46.15  0  103  ILE   A C   1 
ATOM   752   O O   . ILE   A 1 139  ? 102.769 163.392 127.966 1.00 54.51  0  103  ILE   A O   1 
ATOM   753   C CB  . ILE   A 1 139  ? 99.608  164.389 128.354 1.00 51.06  0  103  ILE   A CB  1 
ATOM   754   C CG1 . ILE   A 1 139  ? 98.498  164.515 127.311 1.00 49.53  0  103  ILE   A CG1 1 
ATOM   755   C CG2 . ILE   A 1 139  ? 100.530 165.594 128.292 1.00 49.71  0  103  ILE   A CG2 1 
ATOM   756   C CD1 . ILE   A 1 139  ? 97.631  165.738 127.488 1.00 52.74  0  103  ILE   A CD1 1 
ATOM   757   N N   . ALA   A 1 140  ? 101.952 162.967 130.015 1.00 39.24  0  104  ALA   A N   1 
ATOM   758   C CA  . ALA   A 1 140  ? 103.267 163.077 130.637 1.00 46.04  0  104  ALA   A CA  1 
ATOM   759   C C   . ALA   A 1 140  ? 104.230 162.040 130.077 1.00 50.00  0  104  ALA   A C   1 
ATOM   760   O O   . ALA   A 1 140  ? 105.351 162.372 129.675 1.00 55.12  0  104  ALA   A O   1 
ATOM   761   C CB  . ALA   A 1 140  ? 103.142 162.932 132.153 1.00 46.79  0  104  ALA   A CB  1 
ATOM   762   N N   . THR   A 1 141  ? 103.808 160.776 130.035 1.00 40.88  0  105  THR   A N   1 
ATOM   763   C CA  . THR   A 1 141  ? 104.676 159.727 129.513 1.00 38.48  0  105  THR   A CA  1 
ATOM   764   C C   . THR   A 1 141  ? 104.944 159.886 128.020 1.00 34.31  0  105  THR   A C   1 
ATOM   765   O O   . THR   A 1 141  ? 106.079 159.674 127.577 1.00 36.00  0  105  THR   A O   1 
ATOM   766   C CB  . THR   A 1 141  ? 104.077 158.354 129.809 1.00 36.95  0  105  THR   A CB  1 
ATOM   767   O OG1 . THR   A 1 141  ? 104.219 158.070 131.205 1.00 37.11  0  105  THR   A OG1 1 
ATOM   768   C CG2 . THR   A 1 141  ? 104.788 157.281 129.019 1.00 39.73  0  105  THR   A CG2 1 
ATOM   769   N N   . THR   A 1 142  ? 103.935 160.268 127.231 1.00 30.42  0  106  THR   A N   1 
ATOM   770   C CA  . THR   A 1 142  ? 104.160 160.479 125.806 1.00 34.58  0  106  THR   A CA  1 
ATOM   771   C C   . THR   A 1 142  ? 105.169 161.593 125.569 1.00 38.39  0  106  THR   A C   1 
ATOM   772   O O   . THR   A 1 142  ? 106.070 161.457 124.734 1.00 46.90  0  106  THR   A O   1 
ATOM   773   C CB  . THR   A 1 142  ? 102.841 160.800 125.106 1.00 39.02  0  106  THR   A CB  1 
ATOM   774   O OG1 . THR   A 1 142  ? 101.920 159.720 125.294 1.00 40.13  0  106  THR   A OG1 1 
ATOM   775   C CG2 . THR   A 1 142  ? 103.063 161.011 123.621 1.00 37.28  0  106  THR   A CG2 1 
ATOM   776   N N   . ASN   A 1 143  ? 105.046 162.699 126.306 1.00 29.27  0  107  ASN   A N   1 
ATOM   777   C CA  . ASN   A 1 143  ? 105.985 163.800 126.141 1.00 32.38  0  107  ASN   A CA  1 
ATOM   778   C C   . ASN   A 1 143  ? 107.382 163.428 126.618 1.00 34.58  0  107  ASN   A C   1 
ATOM   779   O O   . ASN   A 1 143  ? 108.369 163.816 125.986 1.00 34.70  0  107  ASN   A O   1 
ATOM   780   C CB  . ASN   A 1 143  ? 105.473 165.034 126.875 1.00 34.66  0  107  ASN   A CB  1 
ATOM   781   C CG  . ASN   A 1 143  ? 104.217 165.599 126.247 1.00 39.46  0  107  ASN   A CG  1 
ATOM   782   O OD1 . ASN   A 1 143  ? 103.821 165.196 125.154 1.00 39.96  0  107  ASN   A OD1 1 
ATOM   783   N ND2 . ASN   A 1 143  ? 103.582 166.539 126.934 1.00 38.22  0  107  ASN   A ND2 1 
ATOM   784   N N   . LEU   A 1 144  ? 107.491 162.678 127.717 1.00 26.86  0  108  LEU   A N   1 
ATOM   785   C CA  . LEU   A 1 144  ? 108.807 162.252 128.181 1.00 22.53  0  108  LEU   A CA  1 
ATOM   786   C C   . LEU   A 1 144  ? 109.486 161.343 127.164 1.00 28.97  0  108  LEU   A C   1 
ATOM   787   O O   . LEU   A 1 144  ? 110.680 161.498 126.880 1.00 38.15  0  108  LEU   A O   1 
ATOM   788   C CB  . LEU   A 1 144  ? 108.684 161.548 129.529 1.00 20.74  0  108  LEU   A CB  1 
ATOM   789   C CG  . LEU   A 1 144  ? 109.991 161.038 130.131 1.00 26.75  0  108  LEU   A CG  1 
ATOM   790   C CD1 . LEU   A 1 144  ? 110.953 162.187 130.336 1.00 32.42  0  108  LEU   A CD1 1 
ATOM   791   C CD2 . LEU   A 1 144  ? 109.736 160.319 131.440 1.00 23.47  0  108  LEU   A CD2 1 
ATOM   792   N N   . LEU   A 1 145  ? 108.741 160.392 126.598 1.00 27.80  0  109  LEU   A N   1 
ATOM   793   C CA  . LEU   A 1 145  ? 109.323 159.504 125.597 1.00 25.57  0  109  LEU   A CA  1 
ATOM   794   C C   . LEU   A 1 145  ? 109.692 160.264 124.331 1.00 18.84  0  109  LEU   A C   1 
ATOM   795   O O   . LEU   A 1 145  ? 110.733 159.994 123.722 1.00 20.25  0  109  LEU   A O   1 
ATOM   796   C CB  . LEU   A 1 145  ? 108.361 158.365 125.277 1.00 23.25  0  109  LEU   A CB  1 
ATOM   797   C CG  . LEU   A 1 145  ? 108.952 157.217 124.462 1.00 27.48  0  109  LEU   A CG  1 
ATOM   798   C CD1 . LEU   A 1 145  ? 109.995 156.468 125.272 1.00 27.54  0  109  LEU   A CD1 1 
ATOM   799   C CD2 . LEU   A 1 145  ? 107.858 156.281 124.000 1.00 26.78  0  109  LEU   A CD2 1 
ATOM   800   N N   . LYS   A 1 146  ? 108.853 161.217 123.918 1.00 18.90  0  110  LYS   A N   1 
ATOM   801   C CA  . LYS   A 1 146  ? 109.190 162.036 122.760 1.00 23.01  0  110  LYS   A CA  1 
ATOM   802   C C   . LYS   A 1 146  ? 110.471 162.821 123.002 1.00 31.66  0  110  LYS   A C   1 
ATOM   803   O O   . LYS   A 1 146  ? 111.331 162.910 122.118 1.00 35.94  0  110  LYS   A O   1 
ATOM   804   C CB  . LYS   A 1 146  ? 108.040 162.985 122.435 1.00 20.92  0  110  LYS   A CB  1 
ATOM   805   C CG  . LYS   A 1 146  ? 106.870 162.341 121.723 1.00 27.57  0  110  LYS   A CG  1 
ATOM   806   C CD  . LYS   A 1 146  ? 105.841 163.387 121.328 1.00 36.41  0  110  LYS   A CD  1 
ATOM   807   C CE  . LYS   A 1 146  ? 104.672 162.765 120.590 1.00 39.54  0  110  LYS   A CE  1 
ATOM   808   N NZ  . LYS   A 1 146  ? 103.662 163.781 120.196 1.00 32.16  1  110  LYS   A NZ  1 
ATOM   809   N N   . LYS   A 1 147  ? 110.616 163.396 124.198 1.00 34.84  0  111  LYS   A N   1 
ATOM   810   C CA  . LYS   A 1 147  ? 111.827 164.144 124.513 1.00 26.23  0  111  LYS   A CA  1 
ATOM   811   C C   . LYS   A 1 147  ? 113.051 163.243 124.501 1.00 26.60  0  111  LYS   A C   1 
ATOM   812   O O   . LYS   A 1 147  ? 114.099 163.624 123.972 1.00 36.72  0  111  LYS   A O   1 
ATOM   813   C CB  . LYS   A 1 147  ? 111.693 164.828 125.870 1.00 28.57  0  111  LYS   A CB  1 
ATOM   814   C CG  . LYS   A 1 147  ? 112.975 165.483 126.342 1.00 31.78  0  111  LYS   A CG  1 
ATOM   815   C CD  . LYS   A 1 147  ? 112.864 165.962 127.775 1.00 36.03  0  111  LYS   A CD  1 
ATOM   816   C CE  . LYS   A 1 147  ? 114.148 166.636 128.221 1.00 34.48  0  111  LYS   A CE  1 
ATOM   817   N NZ  . LYS   A 1 147  ? 114.053 167.154 129.612 1.00 36.65  1  111  LYS   A NZ  1 
ATOM   818   N N   . ILE   A 1 148  ? 112.942 162.046 125.083 1.00 18.15  0  112  ILE   A N   1 
ATOM   819   C CA  . ILE   A 1 148  ? 114.089 161.141 125.114 1.00 19.79  0  112  ILE   A CA  1 
ATOM   820   C C   . ILE   A 1 148  ? 114.490 160.737 123.702 1.00 18.20  0  112  ILE   A C   1 
ATOM   821   O O   . ILE   A 1 148  ? 115.679 160.708 123.363 1.00 19.88  0  112  ILE   A O   1 
ATOM   822   C CB  . ILE   A 1 148  ? 113.786 159.911 125.984 1.00 18.24  0  112  ILE   A CB  1 
ATOM   823   C CG1 . ILE   A 1 148  ? 113.683 160.310 127.451 1.00 20.44  0  112  ILE   A CG1 1 
ATOM   824   C CG2 . ILE   A 1 148  ? 114.867 158.874 125.819 1.00 12.65  0  112  ILE   A CG2 1 
ATOM   825   C CD1 . ILE   A 1 148  ? 113.063 159.248 128.312 1.00 26.36  0  112  ILE   A CD1 1 
ATOM   826   N N   . ILE   A 1 149  ? 113.508 160.424 122.855 1.00 24.87  0  113  ILE   A N   1 
ATOM   827   C CA  . ILE   A 1 149  ? 113.809 160.034 121.479 1.00 22.09  0  113  ILE   A CA  1 
ATOM   828   C C   . ILE   A 1 149  ? 114.469 161.183 120.730 1.00 21.16  0  113  ILE   A C   1 
ATOM   829   O O   . ILE   A 1 149  ? 115.467 160.997 120.022 1.00 38.14  0  113  ILE   A O   1 
ATOM   830   C CB  . ILE   A 1 149  ? 112.533 159.557 120.766 1.00 20.67  0  113  ILE   A CB  1 
ATOM   831   C CG1 . ILE   A 1 149  ? 112.111 158.192 121.302 1.00 21.79  0  113  ILE   A CG1 1 
ATOM   832   C CG2 . ILE   A 1 149  ? 112.755 159.492 119.274 1.00 17.83  0  113  ILE   A CG2 1 
ATOM   833   C CD1 . ILE   A 1 149  ? 113.201 157.157 121.223 1.00 22.98  0  113  ILE   A CD1 1 
ATOM   834   N N   . ARG   A 1 150  ? 113.921 162.392 120.872 1.00 15.60  0  114  ARG   A N   1 
ATOM   835   C CA  . ARG   A 1 150  ? 114.493 163.538 120.177 1.00 20.71  0  114  ARG   A CA  1 
ATOM   836   C C   . ARG   A 1 150  ? 115.915 163.803 120.638 1.00 23.26  0  114  ARG   A C   1 
ATOM   837   O O   . ARG   A 1 150  ? 116.803 164.066 119.819 1.00 30.08  0  114  ARG   A O   1 
ATOM   838   C CB  . ARG   A 1 150  ? 113.622 164.772 120.396 1.00 30.00  0  114  ARG   A CB  1 
ATOM   839   C CG  . ARG   A 1 150  ? 113.834 165.862 119.368 1.00 25.43  0  114  ARG   A CG  1 
ATOM   840   C CD  . ARG   A 1 150  ? 112.892 167.024 119.603 1.00 29.66  0  114  ARG   A CD  1 
ATOM   841   N NE  . ARG   A 1 150  ? 113.540 168.109 120.328 1.00 38.13  0  114  ARG   A NE  1 
ATOM   842   C CZ  . ARG   A 1 150  ? 113.308 168.403 121.600 1.00 41.74  0  114  ARG   A CZ  1 
ATOM   843   N NH1 . ARG   A 1 150  ? 112.456 167.700 122.328 1.00 37.62  1  114  ARG   A NH1 1 
ATOM   844   N NH2 . ARG   A 1 150  ? 113.945 169.429 122.155 1.00 32.28  0  114  ARG   A NH2 1 
ATOM   845   N N   . ARG   A 1 151  ? 116.156 163.730 121.945 1.00 27.39  0  115  ARG   A N   1 
ATOM   846   C CA  . ARG   A 1 151  ? 117.495 163.979 122.459 1.00 31.31  0  115  ARG   A CA  1 
ATOM   847   C C   . ARG   A 1 151  ? 118.477 162.918 121.983 1.00 31.77  0  115  ARG   A C   1 
ATOM   848   O O   . ARG   A 1 151  ? 119.614 163.240 121.624 1.00 40.54  0  115  ARG   A O   1 
ATOM   849   C CB  . ARG   A 1 151  ? 117.465 164.045 123.983 1.00 26.45  0  115  ARG   A CB  1 
ATOM   850   C CG  . ARG   A 1 151  ? 116.741 165.262 124.516 1.00 25.66  0  115  ARG   A CG  1 
ATOM   851   C CD  . ARG   A 1 151  ? 117.362 166.545 124.006 1.00 32.45  0  115  ARG   A CD  1 
ATOM   852   N NE  . ARG   A 1 151  ? 116.684 167.717 124.545 1.00 45.22  0  115  ARG   A NE  1 
ATOM   853   C CZ  . ARG   A 1 151  ? 116.496 168.846 123.876 1.00 43.64  0  115  ARG   A CZ  1 
ATOM   854   N NH1 . ARG   A 1 151  ? 116.919 168.991 122.630 1.00 39.52  1  115  ARG   A NH1 1 
ATOM   855   N NH2 . ARG   A 1 151  ? 115.863 169.854 124.470 1.00 33.92  0  115  ARG   A NH2 1 
ATOM   856   N N   . ALA   A 1 152  ? 118.064 161.651 121.971 1.00 12.31  0  116  ALA   A N   1 
ATOM   857   C CA  . ALA   A 1 152  ? 118.961 160.596 121.516 1.00 4.64   0  116  ALA   A CA  1 
ATOM   858   C C   . ALA   A 1 152  ? 119.298 160.745 120.040 1.00 19.85  0  116  ALA   A C   1 
ATOM   859   O O   . ALA   A 1 152  ? 120.444 160.523 119.636 1.00 22.14  0  116  ALA   A O   1 
ATOM   860   C CB  . ALA   A 1 152  ? 118.343 159.234 121.781 1.00 8.34   0  116  ALA   A CB  1 
ATOM   861   N N   . ILE   A 1 153  ? 118.318 161.110 119.216 1.00 25.27  0  117  ILE   A N   1 
ATOM   862   C CA  . ILE   A 1 153  ? 118.600 161.305 117.798 1.00 24.08  0  117  ILE   A CA  1 
ATOM   863   C C   . ILE   A 1 153  ? 119.502 162.518 117.590 1.00 31.27  0  117  ILE   A C   1 
ATOM   864   O O   . ILE   A 1 153  ? 120.414 162.495 116.754 1.00 32.94  0  117  ILE   A O   1 
ATOM   865   C CB  . ILE   A 1 153  ? 117.286 161.415 117.007 1.00 16.86  0  117  ILE   A CB  1 
ATOM   866   C CG1 . ILE   A 1 153  ? 116.597 160.054 116.962 1.00 11.87  0  117  ILE   A CG1 1 
ATOM   867   C CG2 . ILE   A 1 153  ? 117.546 161.914 115.602 1.00 26.57  0  117  ILE   A CG2 1 
ATOM   868   C CD1 . ILE   A 1 153  ? 115.206 160.102 116.410 1.00 21.87  0  117  ILE   A CD1 1 
ATOM   869   N N   . GLU   A 1 154  ? 119.283 163.588 118.361 1.00 23.20  0  118  GLU   A N   1 
ATOM   870   C CA  . GLU   A 1 154  ? 120.156 164.754 118.269 1.00 15.96  0  118  GLU   A CA  1 
ATOM   871   C C   . GLU   A 1 154  ? 121.584 164.415 118.680 1.00 23.81  0  118  GLU   A C   1 
ATOM   872   O O   . GLU   A 1 154  ? 122.542 164.909 118.076 1.00 38.90  0  118  GLU   A O   1 
ATOM   873   C CB  . GLU   A 1 154  ? 119.609 165.889 119.130 1.00 23.26  0  118  GLU   A CB  1 
ATOM   874   C CG  . GLU   A 1 154  ? 118.391 166.570 118.546 1.00 34.60  0  118  GLU   A CG  1 
ATOM   875   C CD  . GLU   A 1 154  ? 117.747 167.541 119.513 1.00 42.04  0  118  GLU   A CD  1 
ATOM   876   O OE1 . GLU   A 1 154  ? 118.186 167.602 120.681 1.00 38.44  0  118  GLU   A OE1 1 
ATOM   877   O OE2 . GLU   A 1 154  ? 116.800 168.244 119.104 1.00 40.92  -1 118  GLU   A OE2 1 
ATOM   878   N N   . ILE   A 1 155  ? 121.747 163.593 119.716 1.00 6.90   0  119  ILE   A N   1 
ATOM   879   C CA  . ILE   A 1 155  ? 123.082 163.189 120.139 1.00 9.34   0  119  ILE   A CA  1 
ATOM   880   C C   . ILE   A 1 155  ? 123.744 162.323 119.078 1.00 22.70  0  119  ILE   A C   1 
ATOM   881   O O   . ILE   A 1 155  ? 124.919 162.515 118.745 1.00 25.57  0  119  ILE   A O   1 
ATOM   882   C CB  . ILE   A 1 155  ? 123.017 162.465 121.493 1.00 7.17   0  119  ILE   A CB  1 
ATOM   883   C CG1 . ILE   A 1 155  ? 122.628 163.435 122.602 1.00 15.91  0  119  ILE   A CG1 1 
ATOM   884   C CG2 . ILE   A 1 155  ? 124.345 161.834 121.811 1.00 16.52  0  119  ILE   A CG2 1 
ATOM   885   C CD1 . ILE   A 1 155  ? 122.304 162.753 123.900 1.00 17.51  0  119  ILE   A CD1 1 
ATOM   886   N N   . SER   A 1 156  ? 123.008 161.353 118.532 1.00 26.94  0  120  SER   A N   1 
ATOM   887   C CA  . SER   A 1 156  ? 123.549 160.462 117.513 1.00 21.85  0  120  SER   A CA  1 
ATOM   888   C C   . SER   A 1 156  ? 123.870 161.179 116.214 1.00 16.35  0  120  SER   A C   1 
ATOM   889   O O   . SER   A 1 156  ? 124.683 160.674 115.429 1.00 22.40  0  120  SER   A O   1 
ATOM   890   C CB  . SER   A 1 156  ? 122.559 159.336 117.231 1.00 21.70  0  120  SER   A CB  1 
ATOM   891   O OG  . SER   A 1 156  ? 122.063 158.792 118.439 1.00 32.78  0  120  SER   A OG  1 
ATOM   892   N N   . ASP   A 1 157  ? 123.230 162.322 115.961 1.00 19.19  0  121  ASP   A N   1 
ATOM   893   C CA  . ASP   A 1 157  ? 123.517 163.076 114.750 1.00 20.98  0  121  ASP   A CA  1 
ATOM   894   C C   . ASP   A 1 157  ? 124.979 163.480 114.668 1.00 24.08  0  121  ASP   A C   1 
ATOM   895   O O   . ASP   A 1 157  ? 125.529 163.574 113.570 1.00 32.12  0  121  ASP   A O   1 
ATOM   896   C CB  . ASP   A 1 157  ? 122.623 164.309 114.676 1.00 20.85  0  121  ASP   A CB  1 
ATOM   897   C CG  . ASP   A 1 157  ? 122.905 165.154 113.461 1.00 29.14  0  121  ASP   A CG  1 
ATOM   898   O OD1 . ASP   A 1 157  ? 122.832 164.620 112.340 1.00 37.36  0  121  ASP   A OD1 1 
ATOM   899   O OD2 . ASP   A 1 157  ? 123.205 166.353 113.624 1.00 31.74  -1 121  ASP   A OD2 1 
ATOM   900   N N   . VAL   A 1 158  ? 125.633 163.702 115.809 1.00 24.37  0  122  VAL   A N   1 
ATOM   901   C CA  . VAL   A 1 158  ? 127.038 164.106 115.794 1.00 28.94  0  122  VAL   A CA  1 
ATOM   902   C C   . VAL   A 1 158  ? 127.898 163.010 115.177 1.00 32.87  0  122  VAL   A C   1 
ATOM   903   O O   . VAL   A 1 158  ? 128.672 163.249 114.241 1.00 29.11  0  122  VAL   A O   1 
ATOM   904   C CB  . VAL   A 1 158  ? 127.512 164.451 117.215 1.00 24.61  0  122  VAL   A CB  1 
ATOM   905   C CG1 . VAL   A 1 158  ? 128.889 165.075 117.171 1.00 29.15  0  122  VAL   A CG1 1 
ATOM   906   C CG2 . VAL   A 1 158  ? 126.525 165.379 117.888 1.00 19.86  0  122  VAL   A CG2 1 
ATOM   907   N N   . LYS   A 1 159  ? 127.755 161.781 115.677 1.00 28.53  0  123  LYS   A N   1 
ATOM   908   C CA  . LYS   A 1 159  ? 128.561 160.684 115.161 1.00 18.25  0  123  LYS   A CA  1 
ATOM   909   C C   . LYS   A 1 159  ? 128.142 160.297 113.752 1.00 27.01  0  123  LYS   A C   1 
ATOM   910   O O   . LYS   A 1 159  ? 128.991 159.911 112.943 1.00 36.22  0  123  LYS   A O   1 
ATOM   911   C CB  . LYS   A 1 159  ? 128.480 159.481 116.095 1.00 10.85  0  123  LYS   A CB  1 
ATOM   912   C CG  . LYS   A 1 159  ? 129.271 159.661 117.370 1.00 14.08  0  123  LYS   A CG  1 
ATOM   913   C CD  . LYS   A 1 159  ? 129.220 158.426 118.237 1.00 17.22  0  123  LYS   A CD  1 
ATOM   914   C CE  . LYS   A 1 159  ? 130.305 157.442 117.853 1.00 28.25  0  123  LYS   A CE  1 
ATOM   915   N NZ  . LYS   A 1 159  ? 130.407 156.329 118.833 1.00 29.91  1  123  LYS   A NZ  1 
ATOM   916   N N   . VAL   A 1 160  ? 126.852 160.402 113.431 1.00 22.82  0  124  VAL   A N   1 
ATOM   917   C CA  . VAL   A 1 160  ? 126.423 160.120 112.066 1.00 10.70  0  124  VAL   A CA  1 
ATOM   918   C C   . VAL   A 1 160  ? 127.040 161.118 111.098 1.00 27.09  0  124  VAL   A C   1 
ATOM   919   O O   . VAL   A 1 160  ? 127.510 160.744 110.020 1.00 38.53  0  124  VAL   A O   1 
ATOM   920   C CB  . VAL   A 1 160  ? 124.890 160.111 111.975 1.00 9.84   0  124  VAL   A CB  1 
ATOM   921   C CG1 . VAL   A 1 160  ? 124.442 160.287 110.538 1.00 12.42  0  124  VAL   A CG1 1 
ATOM   922   C CG2 . VAL   A 1 160  ? 124.354 158.821 112.542 1.00 21.71  0  124  VAL   A CG2 1 
ATOM   923   N N   . TYR   A 1 161  ? 127.055 162.400 111.466 1.00 29.83  0  125  TYR   A N   1 
ATOM   924   C CA  . TYR   A 1 161  ? 127.685 163.414 110.629 1.00 27.62  0  125  TYR   A CA  1 
ATOM   925   C C   . TYR   A 1 161  ? 129.178 163.167 110.489 1.00 27.04  0  125  TYR   A C   1 
ATOM   926   O O   . TYR   A 1 161  ? 129.731 163.305 109.395 1.00 36.91  0  125  TYR   A O   1 
ATOM   927   C CB  . TYR   A 1 161  ? 127.422 164.799 111.211 1.00 32.08  0  125  TYR   A CB  1 
ATOM   928   C CG  . TYR   A 1 161  ? 127.858 165.943 110.330 1.00 31.73  0  125  TYR   A CG  1 
ATOM   929   C CD1 . TYR   A 1 161  ? 129.120 166.500 110.462 1.00 28.03  0  125  TYR   A CD1 1 
ATOM   930   C CD2 . TYR   A 1 161  ? 127.007 166.472 109.375 1.00 33.28  0  125  TYR   A CD2 1 
ATOM   931   C CE1 . TYR   A 1 161  ? 129.523 167.546 109.669 1.00 32.30  0  125  TYR   A CE1 1 
ATOM   932   C CE2 . TYR   A 1 161  ? 127.402 167.520 108.575 1.00 33.27  0  125  TYR   A CE2 1 
ATOM   933   C CZ  . TYR   A 1 161  ? 128.662 168.052 108.727 1.00 40.53  0  125  TYR   A CZ  1 
ATOM   934   O OH  . TYR   A 1 161  ? 129.066 169.098 107.933 1.00 49.13  0  125  TYR   A OH  1 
ATOM   935   N N   . ALA   A 1 162  ? 129.847 162.798 111.583 1.00 21.67  0  126  ALA   A N   1 
ATOM   936   C CA  . ALA   A 1 162  ? 131.274 162.501 111.505 1.00 29.72  0  126  ALA   A CA  1 
ATOM   937   C C   . ALA   A 1 162  ? 131.543 161.347 110.545 1.00 35.16  0  126  ALA   A C   1 
ATOM   938   O O   . ALA   A 1 162  ? 132.428 161.430 109.684 1.00 35.21  0  126  ALA   A O   1 
ATOM   939   C CB  . ALA   A 1 162  ? 131.816 162.181 112.896 1.00 23.21  0  126  ALA   A CB  1 
ATOM   940   N N   . ILE   A 1 163  ? 130.772 160.265 110.671 1.00 31.15  0  127  ILE   A N   1 
ATOM   941   C CA  . ILE   A 1 163  ? 130.978 159.093 109.825 1.00 25.85  0  127  ILE   A CA  1 
ATOM   942   C C   . ILE   A 1 163  ? 130.691 159.428 108.368 1.00 26.91  0  127  ILE   A C   1 
ATOM   943   O O   . ILE   A 1 163  ? 131.455 159.066 107.468 1.00 40.82  0  127  ILE   A O   1 
ATOM   944   C CB  . ILE   A 1 163  ? 130.107 157.923 110.314 1.00 28.50  0  127  ILE   A CB  1 
ATOM   945   C CG1 . ILE   A 1 163  ? 130.615 157.410 111.658 1.00 30.35  0  127  ILE   A CG1 1 
ATOM   946   C CG2 . ILE   A 1 163  ? 130.091 156.809 109.292 1.00 24.07  0  127  ILE   A CG2 1 
ATOM   947   C CD1 . ILE   A 1 163  ? 129.583 156.644 112.441 1.00 29.98  0  127  ILE   A CD1 1 
ATOM   948   N N   . LEU   A 1 164  ? 129.584 160.125 108.113 1.00 19.62  0  128  LEU   A N   1 
ATOM   949   C CA  . LEU   A 1 164  ? 129.211 160.454 106.745 1.00 24.54  0  128  LEU   A CA  1 
ATOM   950   C C   . LEU   A 1 164  ? 130.159 161.460 106.113 1.00 36.22  0  128  LEU   A C   1 
ATOM   951   O O   . LEU   A 1 164  ? 130.306 161.467 104.888 1.00 44.38  0  128  LEU   A O   1 
ATOM   952   C CB  . LEU   A 1 164  ? 127.782 160.990 106.705 1.00 29.85  0  128  LEU   A CB  1 
ATOM   953   C CG  . LEU   A 1 164  ? 126.688 159.974 106.380 1.00 35.96  0  128  LEU   A CG  1 
ATOM   954   C CD1 . LEU   A 1 164  ? 126.632 158.893 107.440 1.00 30.75  0  128  LEU   A CD1 1 
ATOM   955   C CD2 . LEU   A 1 164  ? 125.341 160.662 106.244 1.00 38.15  0  128  LEU   A CD2 1 
ATOM   956   N N   . ASN   A 1 165  ? 130.796 162.313 106.912 1.00 35.95  0  129  ASN   A N   1 
ATOM   957   C CA  . ASN   A 1 165  ? 131.796 163.233 106.392 1.00 34.97  0  129  ASN   A CA  1 
ATOM   958   C C   . ASN   A 1 165  ? 133.116 162.533 106.110 1.00 37.79  0  129  ASN   A C   1 
ATOM   959   O O   . ASN   A 1 165  ? 133.789 162.861 105.129 1.00 46.42  0  129  ASN   A O   1 
ATOM   960   C CB  . ASN   A 1 165  ? 132.009 164.384 107.377 1.00 43.22  0  129  ASN   A CB  1 
ATOM   961   C CG  . ASN   A 1 165  ? 132.644 165.592 106.729 1.00 46.04  0  129  ASN   A CG  1 
ATOM   962   O OD1 . ASN   A 1 165  ? 132.946 165.584 105.537 1.00 46.26  0  129  ASN   A OD1 1 
ATOM   963   N ND2 . ASN   A 1 165  ? 132.845 166.645 107.510 1.00 44.83  0  129  ASN   A ND2 1 
ATOM   964   N N   . LYS   A 1 166  ? 133.502 161.571 106.951 1.00 33.84  0  130  LYS   A N   1 
ATOM   965   C CA  . LYS   A 1 166  ? 134.710 160.802 106.675 1.00 36.93  0  130  LYS   A CA  1 
ATOM   966   C C   . LYS   A 1 166  ? 134.539 159.946 105.427 1.00 35.57  0  130  LYS   A C   1 
ATOM   967   O O   . LYS   A 1 166  ? 135.380 159.973 104.522 1.00 46.24  0  130  LYS   A O   1 
ATOM   968   C CB  . LYS   A 1 166  ? 135.074 159.934 107.880 1.00 40.14  0  130  LYS   A CB  1 
ATOM   969   C CG  . LYS   A 1 166  ? 136.336 159.105 107.687 1.00 38.19  0  130  LYS   A CG  1 
ATOM   970   C CD  . LYS   A 1 166  ? 137.441 159.924 107.037 1.00 44.83  0  130  LYS   A CD  1 
ATOM   971   C CE  . LYS   A 1 166  ? 138.708 159.120 106.849 1.00 42.07  0  130  LYS   A CE  1 
ATOM   972   N NZ  . LYS   A 1 166  ? 139.634 159.304 107.992 1.00 39.81  1  130  LYS   A NZ  1 
ATOM   973   N N   . LEU   A 1 167  ? 133.449 159.182 105.355 1.00 27.14  0  131  LEU   A N   1 
ATOM   974   C CA  . LEU   A 1 167  ? 133.210 158.332 104.196 1.00 27.46  0  131  LEU   A CA  1 
ATOM   975   C C   . LEU   A 1 167  ? 132.893 159.125 102.938 1.00 31.43  0  131  LEU   A C   1 
ATOM   976   O O   . LEU   A 1 167  ? 132.936 158.557 101.844 1.00 41.53  0  131  LEU   A O   1 
ATOM   977   C CB  . LEU   A 1 167  ? 132.069 157.357 104.480 1.00 26.18  0  131  LEU   A CB  1 
ATOM   978   C CG  . LEU   A 1 167  ? 132.304 156.321 105.575 1.00 31.08  0  131  LEU   A CG  1 
ATOM   979   C CD1 . LEU   A 1 167  ? 131.023 155.567 105.861 1.00 30.11  0  131  LEU   A CD1 1 
ATOM   980   C CD2 . LEU   A 1 167  ? 133.406 155.367 105.174 1.00 38.30  0  131  LEU   A CD2 1 
ATOM   981   N N   . GLY   A 1 168  ? 132.580 160.409 103.061 1.00 28.24  0  132  GLY   A N   1 
ATOM   982   C CA  . GLY   A 1 168  ? 132.244 161.208 101.899 1.00 32.33  0  132  GLY   A CA  1 
ATOM   983   C C   . GLY   A 1 168  ? 130.958 160.791 101.223 1.00 44.27  0  132  GLY   A C   1 
ATOM   984   O O   . GLY   A 1 168  ? 130.892 160.766 99.988  1.00 49.51  0  132  GLY   A O   1 
ATOM   985   N N   . LEU   A 1 169  ? 129.927 160.467 102.004 1.00 49.70  0  133  LEU   A N   1 
ATOM   986   C CA  . LEU   A 1 169  ? 128.648 160.010 101.474 1.00 48.54  0  133  LEU   A CA  1 
ATOM   987   C C   . LEU   A 1 169  ? 127.626 161.133 101.343 1.00 52.74  0  133  LEU   A C   1 
ATOM   988   O O   . LEU   A 1 169  ? 126.420 160.885 101.470 1.00 52.32  0  133  LEU   A O   1 
ATOM   989   C CB  . LEU   A 1 169  ? 128.091 158.888 102.349 1.00 45.91  0  133  LEU   A CB  1 
ATOM   990   C CG  . LEU   A 1 169  ? 128.909 157.600 102.398 1.00 44.25  0  133  LEU   A CG  1 
ATOM   991   C CD1 . LEU   A 1 169  ? 128.414 156.708 103.516 1.00 50.86  0  133  LEU   A CD1 1 
ATOM   992   C CD2 . LEU   A 1 169  ? 128.841 156.880 101.068 1.00 43.53  0  133  LEU   A CD2 1 
ATOM   993   N N   . LYS   A 1 170  ? 128.069 162.360 101.093 1.00 59.52  0  134  LYS   A N   1 
ATOM   994   C CA  . LYS   A 1 170  ? 127.143 163.474 100.936 1.00 59.08  0  134  LYS   A CA  1 
ATOM   995   C C   . LYS   A 1 170  ? 126.569 163.505 99.525  1.00 57.98  0  134  LYS   A C   1 
ATOM   996   O O   . LYS   A 1 170  ? 125.940 162.545 99.081  1.00 58.06  0  134  LYS   A O   1 
ATOM   997   C CB  . LYS   A 1 170  ? 127.830 164.802 101.254 1.00 58.35  0  134  LYS   A CB  1 
ATOM   998   C CG  . LYS   A 1 170  ? 126.918 166.013 101.120 1.00 59.96  0  134  LYS   A CG  1 
ATOM   999   C CD  . LYS   A 1 170  ? 127.588 167.274 101.643 1.00 59.11  0  134  LYS   A CD  1 
ATOM   1000  C CE  . LYS   A 1 170  ? 126.626 168.451 101.649 1.00 56.19  0  134  LYS   A CE  1 
ATOM   1001  N NZ  . LYS   A 1 170  ? 127.249 169.670 102.233 1.00 57.16  1  134  LYS   A NZ  1 
ATOM   1002  N N   . ASP   A 1 219  ? 118.504 174.015 112.754 1.00 62.39  0  183  ASP   A N   1 
ATOM   1003  C CA  . ASP   A 1 219  ? 117.933 173.018 113.651 1.00 66.30  0  183  ASP   A CA  1 
ATOM   1004  C C   . ASP   A 1 219  ? 119.024 172.211 114.343 1.00 66.20  0  183  ASP   A C   1 
ATOM   1005  O O   . ASP   A 1 219  ? 120.203 172.326 114.009 1.00 67.41  0  183  ASP   A O   1 
ATOM   1006  C CB  . ASP   A 1 219  ? 116.993 172.084 112.887 1.00 64.65  0  183  ASP   A CB  1 
ATOM   1007  C CG  . ASP   A 1 219  ? 115.781 172.804 112.334 1.00 67.71  0  183  ASP   A CG  1 
ATOM   1008  O OD1 . ASP   A 1 219  ? 115.410 173.856 112.896 1.00 66.52  0  183  ASP   A OD1 1 
ATOM   1009  O OD2 . ASP   A 1 219  ? 115.200 172.320 111.339 1.00 64.36  -1 183  ASP   A OD2 1 
ATOM   1010  N N   . THR   A 1 220  ? 118.621 171.389 115.309 1.00 49.43  0  184  THR   A N   1 
ATOM   1011  C CA  . THR   A 1 220  ? 119.557 170.581 116.076 1.00 44.97  0  184  THR   A CA  1 
ATOM   1012  C C   . THR   A 1 220  ? 119.995 169.322 115.342 1.00 45.65  0  184  THR   A C   1 
ATOM   1013  O O   . THR   A 1 220  ? 120.861 168.601 115.848 1.00 42.53  0  184  THR   A O   1 
ATOM   1014  C CB  . THR   A 1 220  ? 118.939 170.198 117.421 1.00 44.84  0  184  THR   A CB  1 
ATOM   1015  O OG1 . THR   A 1 220  ? 117.671 169.569 117.204 1.00 44.40  0  184  THR   A OG1 1 
ATOM   1016  C CG2 . THR   A 1 220  ? 118.741 171.433 118.282 1.00 43.91  0  184  THR   A CG2 1 
ATOM   1017  N N   . ILE   A 1 221  ? 119.421 169.040 114.175 1.00 41.25  0  185  ILE   A N   1 
ATOM   1018  C CA  . ILE   A 1 221  ? 119.766 167.871 113.376 1.00 38.68  0  185  ILE   A CA  1 
ATOM   1019  C C   . ILE   A 1 221  ? 120.202 168.381 112.010 1.00 33.81  0  185  ILE   A C   1 
ATOM   1020  O O   . ILE   A 1 221  ? 119.398 168.971 111.278 1.00 41.93  0  185  ILE   A O   1 
ATOM   1021  C CB  . ILE   A 1 221  ? 118.593 166.890 113.248 1.00 36.17  0  185  ILE   A CB  1 
ATOM   1022  C CG1 . ILE   A 1 221  ? 118.456 166.056 114.520 1.00 32.79  0  185  ILE   A CG1 1 
ATOM   1023  C CG2 . ILE   A 1 221  ? 118.793 165.972 112.065 1.00 39.29  0  185  ILE   A CG2 1 
ATOM   1024  C CD1 . ILE   A 1 221  ? 117.030 165.864 114.963 1.00 27.20  0  185  ILE   A CD1 1 
ATOM   1025  N N   . LYS   A 1 222  ? 121.472 168.169 111.670 1.00 27.72  0  186  LYS   A N   1 
ATOM   1026  C CA  . LYS   A 1 222  ? 122.022 168.639 110.407 1.00 33.77  0  186  LYS   A CA  1 
ATOM   1027  C C   . LYS   A 1 222  ? 122.010 167.579 109.315 1.00 37.73  0  186  LYS   A C   1 
ATOM   1028  O O   . LYS   A 1 222  ? 122.358 167.888 108.171 1.00 40.48  0  186  LYS   A O   1 
ATOM   1029  C CB  . LYS   A 1 222  ? 123.456 169.136 110.608 1.00 36.12  0  186  LYS   A CB  1 
ATOM   1030  C CG  . LYS   A 1 222  ? 123.597 170.272 111.606 1.00 37.58  0  186  LYS   A CG  1 
ATOM   1031  C CD  . LYS   A 1 222  ? 124.921 170.995 111.419 1.00 41.75  0  186  LYS   A CD  1 
ATOM   1032  C CE  . LYS   A 1 222  ? 125.229 171.911 112.592 1.00 38.03  0  186  LYS   A CE  1 
ATOM   1033  N NZ  . LYS   A 1 222  ? 126.556 172.572 112.447 1.00 33.93  1  186  LYS   A NZ  1 
ATOM   1034  N N   . THR   A 1 223  ? 121.628 166.347 109.635 1.00 31.86  0  187  THR   A N   1 
ATOM   1035  C CA  . THR   A 1 223  ? 121.629 165.258 108.672 1.00 25.97  0  187  THR   A CA  1 
ATOM   1036  C C   . THR   A 1 223  ? 120.230 165.062 108.106 1.00 34.41  0  187  THR   A C   1 
ATOM   1037  O O   . THR   A 1 223  ? 119.249 165.026 108.852 1.00 39.91  0  187  THR   A O   1 
ATOM   1038  C CB  . THR   A 1 223  ? 122.102 163.960 109.329 1.00 26.75  0  187  THR   A CB  1 
ATOM   1039  O OG1 . THR   A 1 223  ? 123.331 164.192 110.026 1.00 23.13  0  187  THR   A OG1 1 
ATOM   1040  C CG2 . THR   A 1 223  ? 122.329 162.892 108.286 1.00 34.57  0  187  THR   A CG2 1 
ATOM   1041  N N   . THR   A 1 224  ? 120.141 164.942 106.780 1.00 37.68  0  188  THR   A N   1 
ATOM   1042  C CA  . THR   A 1 224  ? 118.851 164.635 106.170 1.00 36.20  0  188  THR   A CA  1 
ATOM   1043  C C   . THR   A 1 224  ? 118.365 163.252 106.577 1.00 36.19  0  188  THR   A C   1 
ATOM   1044  O O   . THR   A 1 224  ? 117.157 163.043 106.743 1.00 34.43  0  188  THR   A O   1 
ATOM   1045  C CB  . THR   A 1 224  ? 118.941 164.733 104.650 1.00 32.79  0  188  THR   A CB  1 
ATOM   1046  O OG1 . THR   A 1 224  ? 119.778 163.683 104.154 1.00 33.18  0  188  THR   A OG1 1 
ATOM   1047  C CG2 . THR   A 1 224  ? 119.525 166.071 104.238 1.00 36.33  0  188  THR   A CG2 1 
ATOM   1048  N N   . LEU   A 1 225  ? 119.290 162.306 106.748 1.00 30.34  0  189  LEU   A N   1 
ATOM   1049  C CA  . LEU   A 1 225  ? 118.919 160.957 107.158 1.00 30.63  0  189  LEU   A CA  1 
ATOM   1050  C C   . LEU   A 1 225  ? 118.192 160.972 108.497 1.00 35.98  0  189  LEU   A C   1 
ATOM   1051  O O   . LEU   A 1 225  ? 117.085 160.435 108.628 1.00 39.18  0  189  LEU   A O   1 
ATOM   1052  C CB  . LEU   A 1 225  ? 120.173 160.087 107.230 1.00 24.42  0  189  LEU   A CB  1 
ATOM   1053  C CG  . LEU   A 1 225  ? 120.030 158.611 107.587 1.00 30.92  0  189  LEU   A CG  1 
ATOM   1054  C CD1 . LEU   A 1 225  ? 119.624 157.820 106.359 1.00 28.05  0  189  LEU   A CD1 1 
ATOM   1055  C CD2 . LEU   A 1 225  ? 121.328 158.080 108.163 1.00 31.57  0  189  LEU   A CD2 1 
ATOM   1056  N N   . LEU   A 1 226  ? 118.783 161.613 109.503 1.00 31.98  0  190  LEU   A N   1 
ATOM   1057  C CA  . LEU   A 1 226  ? 118.133 161.654 110.803 1.00 25.67  0  190  LEU   A CA  1 
ATOM   1058  C C   . LEU   A 1 226  ? 116.998 162.666 110.863 1.00 26.03  0  190  LEU   A C   1 
ATOM   1059  O O   . LEU   A 1 226  ? 116.120 162.527 111.716 1.00 37.59  0  190  LEU   A O   1 
ATOM   1060  C CB  . LEU   A 1 226  ? 119.155 161.926 111.904 1.00 26.97  0  190  LEU   A CB  1 
ATOM   1061  C CG  . LEU   A 1 226  ? 120.165 160.788 112.057 1.00 25.49  0  190  LEU   A CG  1 
ATOM   1062  C CD1 . LEU   A 1 226  ? 121.037 160.996 113.271 1.00 21.51  0  190  LEU   A CD1 1 
ATOM   1063  C CD2 . LEU   A 1 226  ? 119.472 159.450 112.120 1.00 19.06  0  190  LEU   A CD2 1 
ATOM   1064  N N   . LYS   A 1 227  ? 116.966 163.654 109.967 1.00 16.90  0  191  LYS   A N   1 
ATOM   1065  C CA  . LYS   A 1 227  ? 115.756 164.458 109.824 1.00 24.22  0  191  LYS   A CA  1 
ATOM   1066  C C   . LYS   A 1 227  ? 114.573 163.580 109.439 1.00 32.31  0  191  LYS   A C   1 
ATOM   1067  O O   . LYS   A 1 227  ? 113.500 163.649 110.055 1.00 35.37  0  191  LYS   A O   1 
ATOM   1068  C CB  . LYS   A 1 227  ? 115.961 165.550 108.775 1.00 24.79  0  191  LYS   A CB  1 
ATOM   1069  C CG  . LYS   A 1 227  ? 116.615 166.819 109.275 1.00 25.70  0  191  LYS   A CG  1 
ATOM   1070  C CD  . LYS   A 1 227  ? 116.850 167.768 108.114 1.00 28.69  0  191  LYS   A CD  1 
ATOM   1071  C CE  . LYS   A 1 227  ? 117.618 169.002 108.537 1.00 35.20  0  191  LYS   A CE  1 
ATOM   1072  N NZ  . LYS   A 1 227  ? 117.956 169.853 107.364 1.00 38.70  1  191  LYS   A NZ  1 
ATOM   1073  N N   . LYS   A 1 228  ? 114.760 162.733 108.425 1.00 35.41  0  192  LYS   A N   1 
ATOM   1074  C CA  . LYS   A 1 228  ? 113.703 161.809 108.029 1.00 36.37  0  192  LYS   A CA  1 
ATOM   1075  C C   . LYS   A 1 228  ? 113.374 160.839 109.156 1.00 29.60  0  192  LYS   A C   1 
ATOM   1076  O O   . LYS   A 1 228  ? 112.203 160.520 109.396 1.00 26.29  0  192  LYS   A O   1 
ATOM   1077  C CB  . LYS   A 1 228  ? 114.117 161.040 106.776 1.00 30.84  0  192  LYS   A CB  1 
ATOM   1078  C CG  . LYS   A 1 228  ? 114.463 161.886 105.574 1.00 27.68  0  192  LYS   A CG  1 
ATOM   1079  C CD  . LYS   A 1 228  ? 115.145 161.031 104.518 1.00 31.49  0  192  LYS   A CD  1 
ATOM   1080  C CE  . LYS   A 1 228  ? 115.511 161.839 103.286 1.00 39.77  0  192  LYS   A CE  1 
ATOM   1081  N NZ  . LYS   A 1 228  ? 116.233 161.010 102.280 1.00 34.50  1  192  LYS   A NZ  1 
ATOM   1082  N N   . LEU   A 1 229  ? 114.400 160.345 109.850 1.00 26.02  0  193  LEU   A N   1 
ATOM   1083  C CA  . LEU   A 1 229  ? 114.147 159.407 110.938 1.00 27.57  0  193  LEU   A CA  1 
ATOM   1084  C C   . LEU   A 1 229  ? 113.318 160.050 112.041 1.00 31.96  0  193  LEU   A C   1 
ATOM   1085  O O   . LEU   A 1 229  ? 112.398 159.425 112.575 1.00 41.83  0  193  LEU   A O   1 
ATOM   1086  C CB  . LEU   A 1 229  ? 115.459 158.870 111.503 1.00 29.84  0  193  LEU   A CB  1 
ATOM   1087  C CG  . LEU   A 1 229  ? 115.273 157.982 112.734 1.00 21.51  0  193  LEU   A CG  1 
ATOM   1088  C CD1 . LEU   A 1 229  ? 114.523 156.730 112.368 1.00 31.81  0  193  LEU   A CD1 1 
ATOM   1089  C CD2 . LEU   A 1 229  ? 116.597 157.631 113.344 1.00 21.62  0  193  LEU   A CD2 1 
ATOM   1090  N N   . MET   A 1 230  ? 113.625 161.297 112.400 1.00 26.47  0  194  MET   A N   1 
ATOM   1091  C CA  . MET   A 1 230  ? 112.828 161.987 113.409 1.00 26.47  0  194  MET   A CA  1 
ATOM   1092  C C   . MET   A 1 230  ? 111.405 162.234 112.929 1.00 37.96  0  194  MET   A C   1 
ATOM   1093  O O   . MET   A 1 230  ? 110.453 162.099 113.707 1.00 36.33  0  194  MET   A O   1 
ATOM   1094  C CB  . MET   A 1 230  ? 113.497 163.298 113.810 1.00 23.82  0  194  MET   A CB  1 
ATOM   1095  C CG  . MET   A 1 230  ? 112.862 163.922 115.030 1.00 36.31  0  194  MET   A CG  1 
ATOM   1096  S SD  . MET   A 1 230  ? 113.504 163.291 116.585 1.00 48.69  0  194  MET   A SD  1 
ATOM   1097  C CE  . MET   A 1 230  ? 111.997 163.256 117.554 1.00 34.65  0  194  MET   A CE  1 
ATOM   1098  N N   . CYS   A 1 231  ? 111.235 162.599 111.655 1.00 42.40  0  195  CYS   A N   1 
ATOM   1099  C CA  . CYS   A 1 231  ? 109.885 162.752 111.123 1.00 35.07  0  195  CYS   A CA  1 
ATOM   1100  C C   . CYS   A 1 231  ? 109.098 161.454 111.256 1.00 39.85  0  195  CYS   A C   1 
ATOM   1101  O O   . CYS   A 1 231  ? 107.903 161.472 111.570 1.00 41.11  0  195  CYS   A O   1 
ATOM   1102  C CB  . CYS   A 1 231  ? 109.934 163.201 109.665 1.00 36.39  0  195  CYS   A CB  1 
ATOM   1103  S SG  . CYS   A 1 231  ? 110.416 164.922 109.433 1.00 62.22  0  195  CYS   A SG  1 
ATOM   1104  N N   . SER   A 1 232  ? 109.752 160.317 111.014 1.00 46.35  0  196  SER   A N   1 
ATOM   1105  C CA  . SER   A 1 232  ? 109.100 159.028 111.232 1.00 33.63  0  196  SER   A CA  1 
ATOM   1106  C C   . SER   A 1 232  ? 108.799 158.805 112.709 1.00 29.29  0  196  SER   A C   1 
ATOM   1107  O O   . SER   A 1 232  ? 107.730 158.301 113.069 1.00 39.66  0  196  SER   A O   1 
ATOM   1108  C CB  . SER   A 1 232  ? 109.978 157.898 110.691 1.00 32.35  0  196  SER   A CB  1 
ATOM   1109  O OG  . SER   A 1 232  ? 110.029 157.913 109.276 1.00 36.78  0  196  SER   A OG  1 
ATOM   1110  N N   . MET   A 1 233  ? 109.728 159.188 113.578 1.00 20.95  0  197  MET   A N   1 
ATOM   1111  C CA  . MET   A 1 233  ? 109.699 158.858 114.997 1.00 28.95  0  197  MET   A CA  1 
ATOM   1112  C C   . MET   A 1 233  ? 108.947 159.876 115.838 1.00 39.83  0  197  MET   A C   1 
ATOM   1113  O O   . MET   A 1 233  ? 109.003 159.794 117.069 1.00 41.53  0  197  MET   A O   1 
ATOM   1114  C CB  . MET   A 1 233  ? 111.128 158.737 115.525 1.00 30.61  0  197  MET   A CB  1 
ATOM   1115  C CG  . MET   A 1 233  ? 111.753 157.381 115.337 1.00 31.33  0  197  MET   A CG  1 
ATOM   1116  S SD  . MET   A 1 233  ? 112.786 156.925 116.732 1.00 35.98  0  197  MET   A SD  1 
ATOM   1117  C CE  . MET   A 1 233  ? 113.432 155.380 116.138 1.00 22.74  0  197  MET   A CE  1 
ATOM   1118  N N   . GLN   A 1 234  ? 108.275 160.840 115.206 1.00 45.35  0  198  GLN   A N   1 
ATOM   1119  C CA  . GLN   A 1 234  ? 107.617 161.905 115.957 1.00 43.79  0  198  GLN   A CA  1 
ATOM   1120  C C   . GLN   A 1 234  ? 106.617 161.354 116.968 1.00 43.84  0  198  GLN   A C   1 
ATOM   1121  O O   . GLN   A 1 234  ? 106.584 161.801 118.120 1.00 36.90  0  198  GLN   A O   1 
ATOM   1122  C CB  . GLN   A 1 234  ? 106.925 162.864 114.991 1.00 38.62  0  198  GLN   A CB  1 
ATOM   1123  C CG  . GLN   A 1 234  ? 106.847 164.289 115.487 1.00 42.36  0  198  GLN   A CG  1 
ATOM   1124  C CD  . GLN   A 1 234  ? 108.111 165.068 115.200 1.00 46.02  0  198  GLN   A CD  1 
ATOM   1125  O OE1 . GLN   A 1 234  ? 108.402 165.396 114.051 1.00 50.50  0  198  GLN   A OE1 1 
ATOM   1126  N NE2 . GLN   A 1 234  ? 108.871 165.370 116.245 1.00 42.36  0  198  GLN   A NE2 1 
ATOM   1127  N N   . HIS   A 1 235  ? 105.797 160.383 116.564 1.00 47.76  0  199  HIS   A N   1 
ATOM   1128  C CA  . HIS   A 1 235  ? 104.744 159.855 117.425 1.00 46.28  0  199  HIS   A CA  1 
ATOM   1129  C C   . HIS   A 1 235  ? 105.055 158.422 117.826 1.00 48.38  0  199  HIS   A C   1 
ATOM   1130  O O   . HIS   A 1 235  ? 105.084 157.540 116.956 1.00 55.02  0  199  HIS   A O   1 
ATOM   1131  C CB  . HIS   A 1 235  ? 103.394 159.923 116.718 1.00 44.01  0  199  HIS   A CB  1 
ATOM   1132  C CG  . HIS   A 1 235  ? 103.067 161.277 116.176 1.00 52.59  0  199  HIS   A CG  1 
ATOM   1133  N ND1 . HIS   A 1 235  ? 102.755 162.347 116.985 1.00 52.21  0  199  HIS   A ND1 1 
ATOM   1134  C CD2 . HIS   A 1 235  ? 103.004 161.736 114.904 1.00 51.32  0  199  HIS   A CD2 1 
ATOM   1135  C CE1 . HIS   A 1 235  ? 102.515 163.408 116.236 1.00 48.58  0  199  HIS   A CE1 1 
ATOM   1136  N NE2 . HIS   A 1 235  ? 102.659 163.064 114.969 1.00 50.10  0  199  HIS   A NE2 1 
ATOM   1137  N N   . PRO   A 1 236  ? 105.293 158.141 119.109 1.00 38.13  0  200  PRO   A N   1 
ATOM   1138  C CA  . PRO   A 1 236  ? 105.531 156.759 119.517 1.00 31.08  0  200  PRO   A CA  1 
ATOM   1139  C C   . PRO   A 1 236  ? 104.257 155.942 119.425 1.00 33.26  0  200  PRO   A C   1 
ATOM   1140  O O   . PRO   A 1 236  ? 103.144 156.486 119.527 1.00 35.06  0  200  PRO   A O   1 
ATOM   1141  C CB  . PRO   A 1 236  ? 106.001 156.897 120.977 1.00 28.43  0  200  PRO   A CB  1 
ATOM   1142  C CG  . PRO   A 1 236  ? 106.316 158.342 121.162 1.00 37.21  0  200  PRO   A CG  1 
ATOM   1143  C CD  . PRO   A 1 236  ? 105.416 159.075 120.235 1.00 35.37  0  200  PRO   A CD  1 
ATOM   1144  N N   . PRO   A 1 237  ? 104.365 154.633 119.228 1.00 27.42  0  201  PRO   A N   1 
ATOM   1145  C CA  . PRO   A 1 237  ? 103.178 153.776 119.235 1.00 30.71  0  201  PRO   A CA  1 
ATOM   1146  C C   . PRO   A 1 237  ? 102.641 153.587 120.648 1.00 31.63  0  201  PRO   A C   1 
ATOM   1147  O O   . PRO   A 1 237  ? 103.280 153.926 121.643 1.00 32.65  0  201  PRO   A O   1 
ATOM   1148  C CB  . PRO   A 1 237  ? 103.688 152.453 118.653 1.00 26.24  0  201  PRO   A CB  1 
ATOM   1149  C CG  . PRO   A 1 237  ? 104.970 152.792 117.984 1.00 27.02  0  201  PRO   A CG  1 
ATOM   1150  C CD  . PRO   A 1 237  ? 105.557 153.896 118.793 1.00 22.59  0  201  PRO   A CD  1 
ATOM   1151  N N   . SER   A 1 238  ? 101.433 153.028 120.717 1.00 25.70  0  202  SER   A N   1 
ATOM   1152  C CA  . SER   A 1 238  ? 100.744 152.908 121.996 1.00 24.86  0  202  SER   A CA  1 
ATOM   1153  C C   . SER   A 1 238  ? 101.391 151.859 122.893 1.00 29.33  0  202  SER   A C   1 
ATOM   1154  O O   . SER   A 1 238  ? 101.511 152.064 124.106 1.00 36.78  0  202  SER   A O   1 
ATOM   1155  C CB  . SER   A 1 238  ? 99.272  152.582 121.760 1.00 35.40  0  202  SER   A CB  1 
ATOM   1156  O OG  . SER   A 1 238  ? 99.133  151.476 120.888 1.00 33.09  0  202  SER   A OG  1 
ATOM   1157  N N   . TRP   A 1 239  ? 101.800 150.724 122.324 1.00 36.57  0  203  TRP   A N   1 
ATOM   1158  C CA  . TRP   A 1 239  ? 102.400 149.674 123.141 1.00 33.63  0  203  TRP   A CA  1 
ATOM   1159  C C   . TRP   A 1 239  ? 103.740 150.104 123.718 1.00 35.34  0  203  TRP   A C   1 
ATOM   1160  O O   . TRP   A 1 239  ? 104.060 149.764 124.865 1.00 35.71  0  203  TRP   A O   1 
ATOM   1161  C CB  . TRP   A 1 239  ? 102.555 148.394 122.322 1.00 30.16  0  203  TRP   A CB  1 
ATOM   1162  C CG  . TRP   A 1 239  ? 101.248 147.850 121.814 1.00 46.10  0  203  TRP   A CG  1 
ATOM   1163  C CD1 . TRP   A 1 239  ? 100.949 147.509 120.528 1.00 45.50  0  203  TRP   A CD1 1 
ATOM   1164  C CD2 . TRP   A 1 239  ? 100.061 147.594 122.582 1.00 49.60  0  203  TRP   A CD2 1 
ATOM   1165  N NE1 . TRP   A 1 239  ? 99.655  147.053 120.447 1.00 45.92  0  203  TRP   A NE1 1 
ATOM   1166  C CE2 . TRP   A 1 239  ? 99.089  147.097 121.694 1.00 44.57  0  203  TRP   A CE2 1 
ATOM   1167  C CE3 . TRP   A 1 239  ? 99.728  147.735 123.935 1.00 41.29  0  203  TRP   A CE3 1 
ATOM   1168  C CZ2 . TRP   A 1 239  ? 97.810  146.742 122.112 1.00 42.60  0  203  TRP   A CZ2 1 
ATOM   1169  C CZ3 . TRP   A 1 239  ? 98.460  147.385 124.347 1.00 38.79  0  203  TRP   A CZ3 1 
ATOM   1170  C CH2 . TRP   A 1 239  ? 97.516  146.892 123.440 1.00 44.70  0  203  TRP   A CH2 1 
ATOM   1171  N N   . LEU   A 1 240  ? 104.533 150.844 122.945 1.00 33.79  0  204  LEU   A N   1 
ATOM   1172  C CA  . LEU   A 1 240  ? 105.800 151.348 123.459 1.00 26.91  0  204  LEU   A CA  1 
ATOM   1173  C C   . LEU   A 1 240  ? 105.575 152.305 124.621 1.00 27.66  0  204  LEU   A C   1 
ATOM   1174  O O   . LEU   A 1 240  ? 106.290 152.252 125.626 1.00 37.28  0  204  LEU   A O   1 
ATOM   1175  C CB  . LEU   A 1 240  ? 106.587 152.031 122.344 1.00 18.46  0  204  LEU   A CB  1 
ATOM   1176  C CG  . LEU   A 1 240  ? 107.879 152.670 122.842 1.00 26.25  0  204  LEU   A CG  1 
ATOM   1177  C CD1 . LEU   A 1 240  ? 108.787 151.621 123.453 1.00 26.73  0  204  LEU   A CD1 1 
ATOM   1178  C CD2 . LEU   A 1 240  ? 108.569 153.386 121.720 1.00 32.67  0  204  LEU   A CD2 1 
ATOM   1179  N N   . ILE   A 1 241  ? 104.586 153.191 124.498 1.00 27.68  0  205  ILE   A N   1 
ATOM   1180  C CA  . ILE   A 1 241  ? 104.261 154.096 125.595 1.00 22.36  0  205  ILE   A CA  1 
ATOM   1181  C C   . ILE   A 1 241  ? 103.805 153.307 126.812 1.00 16.31  0  205  ILE   A C   1 
ATOM   1182  O O   . ILE   A 1 241  ? 104.148 153.641 127.948 1.00 21.29  0  205  ILE   A O   1 
ATOM   1183  C CB  . ILE   A 1 241  ? 103.197 155.116 125.153 1.00 22.57  0  205  ILE   A CB  1 
ATOM   1184  C CG1 . ILE   A 1 241  ? 103.783 156.088 124.133 1.00 31.01  0  205  ILE   A CG1 1 
ATOM   1185  C CG2 . ILE   A 1 241  ? 102.656 155.873 126.342 1.00 16.71  0  205  ILE   A CG2 1 
ATOM   1186  C CD1 . ILE   A 1 241  ? 102.739 156.905 123.413 1.00 29.31  0  205  ILE   A CD1 1 
ATOM   1187  N N   . HIS   A 1 242  ? 103.025 152.249 126.591 1.00 30.12  0  206  HIS   A N   1 
ATOM   1188  C CA  . HIS   A 1 242  ? 102.578 151.403 127.694 1.00 31.18  0  206  HIS   A CA  1 
ATOM   1189  C C   . HIS   A 1 242  ? 103.764 150.817 128.450 1.00 26.79  0  206  HIS   A C   1 
ATOM   1190  O O   . HIS   A 1 242  ? 103.842 150.906 129.683 1.00 39.79  0  206  HIS   A O   1 
ATOM   1191  C CB  . HIS   A 1 242  ? 101.675 150.297 127.146 1.00 32.41  0  206  HIS   A CB  1 
ATOM   1192  C CG  . HIS   A 1 242  ? 101.429 149.174 128.104 1.00 34.44  0  206  HIS   A CG  1 
ATOM   1193  N ND1 . HIS   A 1 242  ? 100.389 149.181 129.005 1.00 36.18  0  206  HIS   A ND1 1 
ATOM   1194  C CD2 . HIS   A 1 242  ? 102.073 147.998 128.282 1.00 31.35  0  206  HIS   A CD2 1 
ATOM   1195  C CE1 . HIS   A 1 242  ? 100.411 148.063 129.708 1.00 36.50  0  206  HIS   A CE1 1 
ATOM   1196  N NE2 . HIS   A 1 242  ? 101.424 147.328 129.290 1.00 32.30  0  206  HIS   A NE2 1 
ATOM   1197  N N   . TRP   A 1 243  ? 104.711 150.229 127.719 1.00 21.82  0  207  TRP   A N   1 
ATOM   1198  C CA  . TRP   A 1 243  ? 105.860 149.604 128.370 1.00 18.81  0  207  TRP   A CA  1 
ATOM   1199  C C   . TRP   A 1 243  ? 106.754 150.640 129.040 1.00 19.70  0  207  TRP   A C   1 
ATOM   1200  O O   . TRP   A 1 243  ? 107.252 150.410 130.149 1.00 25.76  0  207  TRP   A O   1 
ATOM   1201  C CB  . TRP   A 1 243  ? 106.648 148.771 127.362 1.00 29.66  0  207  TRP   A CB  1 
ATOM   1202  C CG  . TRP   A 1 243  ? 105.873 147.601 126.848 1.00 30.25  0  207  TRP   A CG  1 
ATOM   1203  C CD1 . TRP   A 1 243  ? 105.577 147.324 125.550 1.00 24.30  0  207  TRP   A CD1 1 
ATOM   1204  C CD2 . TRP   A 1 243  ? 105.280 146.557 127.627 1.00 29.84  0  207  TRP   A CD2 1 
ATOM   1205  N NE1 . TRP   A 1 243  ? 104.838 146.172 125.469 1.00 27.11  0  207  TRP   A NE1 1 
ATOM   1206  C CE2 . TRP   A 1 243  ? 104.643 145.681 126.732 1.00 20.30  0  207  TRP   A CE2 1 
ATOM   1207  C CE3 . TRP   A 1 243  ? 105.227 146.278 128.995 1.00 33.49  0  207  TRP   A CE3 1 
ATOM   1208  C CZ2 . TRP   A 1 243  ? 103.963 144.548 127.158 1.00 20.57  0  207  TRP   A CZ2 1 
ATOM   1209  C CZ3 . TRP   A 1 243  ? 104.551 145.156 129.415 1.00 32.41  0  207  TRP   A CZ3 1 
ATOM   1210  C CH2 . TRP   A 1 243  ? 103.928 144.303 128.501 1.00 25.80  0  207  TRP   A CH2 1 
ATOM   1211  N N   . PHE   A 1 244  ? 106.964 151.787 128.390 1.00 20.88  0  208  PHE   A N   1 
ATOM   1212  C CA  . PHE   A 1 244  ? 107.788 152.833 128.985 1.00 18.26  0  208  PHE   A CA  1 
ATOM   1213  C C   . PHE   A 1 244  ? 107.158 153.379 130.258 1.00 21.31  0  208  PHE   A C   1 
ATOM   1214  O O   . PHE   A 1 244  ? 107.855 153.600 131.251 1.00 26.72  0  208  PHE   A O   1 
ATOM   1215  C CB  . PHE   A 1 244  ? 108.021 153.961 127.983 1.00 20.76  0  208  PHE   A CB  1 
ATOM   1216  C CG  . PHE   A 1 244  ? 108.796 155.115 128.545 1.00 28.57  0  208  PHE   A CG  1 
ATOM   1217  C CD1 . PHE   A 1 244  ? 109.990 154.904 129.212 1.00 30.19  0  208  PHE   A CD1 1 
ATOM   1218  C CD2 . PHE   A 1 244  ? 108.333 156.410 128.409 1.00 29.49  0  208  PHE   A CD2 1 
ATOM   1219  C CE1 . PHE   A 1 244  ? 110.705 155.960 129.732 1.00 19.28  0  208  PHE   A CE1 1 
ATOM   1220  C CE2 . PHE   A 1 244  ? 109.046 157.471 128.927 1.00 32.84  0  208  PHE   A CE2 1 
ATOM   1221  C CZ  . PHE   A 1 244  ? 110.233 157.245 129.588 1.00 23.37  0  208  PHE   A CZ  1 
ATOM   1222  N N   . ASN   A 1 245  ? 105.844 153.601 130.249 1.00 29.27  0  209  ASN   A N   1 
ATOM   1223  C CA  . ASN   A 1 245  ? 105.154 154.079 131.440 1.00 20.04  0  209  ASN   A CA  1 
ATOM   1224  C C   . ASN   A 1 245  ? 105.258 153.071 132.574 1.00 17.42  0  209  ASN   A C   1 
ATOM   1225  O O   . ASN   A 1 245  ? 105.523 153.437 133.726 1.00 27.79  0  209  ASN   A O   1 
ATOM   1226  C CB  . ASN   A 1 245  ? 103.692 154.359 131.104 1.00 19.66  0  209  ASN   A CB  1 
ATOM   1227  C CG  . ASN   A 1 245  ? 102.970 155.081 132.208 1.00 29.26  0  209  ASN   A CG  1 
ATOM   1228  O OD1 . ASN   A 1 245  ? 103.549 155.387 133.247 1.00 42.26  0  209  ASN   A OD1 1 
ATOM   1229  N ND2 . ASN   A 1 245  ? 101.693 155.361 131.992 1.00 31.93  0  209  ASN   A ND2 1 
ATOM   1230  N N   . LEU   A 1 246  ? 105.042 151.792 132.268 1.00 17.37  0  210  LEU   A N   1 
ATOM   1231  C CA  . LEU   A 1 246  ? 105.117 150.781 133.314 1.00 13.99  0  210  LEU   A CA  1 
ATOM   1232  C C   . LEU   A 1 246  ? 106.517 150.698 133.903 1.00 16.80  0  210  LEU   A C   1 
ATOM   1233  O O   . LEU   A 1 246  ? 106.674 150.630 135.133 1.00 22.86  0  210  LEU   A O   1 
ATOM   1234  C CB  . LEU   A 1 246  ? 104.685 149.433 132.749 1.00 20.70  0  210  LEU   A CB  1 
ATOM   1235  C CG  . LEU   A 1 246  ? 104.070 148.410 133.694 1.00 11.45  0  210  LEU   A CG  1 
ATOM   1236  C CD1 . LEU   A 1 246  ? 103.124 147.562 132.892 1.00 22.79  0  210  LEU   A CD1 1 
ATOM   1237  C CD2 . LEU   A 1 246  ? 105.122 147.550 134.344 1.00 16.48  0  210  LEU   A CD2 1 
ATOM   1238  N N   . TYR   A 1 247  ? 107.544 150.719 133.048 1.00 18.96  0  211  TYR   A N   1 
ATOM   1239  C CA  . TYR   A 1 247  ? 108.913 150.693 133.546 1.00 13.13  0  211  TYR   A CA  1 
ATOM   1240  C C   . TYR   A 1 247  ? 109.216 151.931 134.374 1.00 23.78  0  211  TYR   A C   1 
ATOM   1241  O O   . TYR   A 1 247  ? 109.866 151.840 135.418 1.00 21.84  0  211  TYR   A O   1 
ATOM   1242  C CB  . TYR   A 1 247  ? 109.908 150.585 132.393 1.00 11.90  0  211  TYR   A CB  1 
ATOM   1243  C CG  . TYR   A 1 247  ? 111.318 150.923 132.819 1.00 24.96  0  211  TYR   A CG  1 
ATOM   1244  C CD1 . TYR   A 1 247  ? 111.998 150.117 133.719 1.00 25.22  0  211  TYR   A CD1 1 
ATOM   1245  C CD2 . TYR   A 1 247  ? 111.963 152.051 132.337 1.00 19.48  0  211  TYR   A CD2 1 
ATOM   1246  C CE1 . TYR   A 1 247  ? 113.277 150.418 134.120 1.00 19.66  0  211  TYR   A CE1 1 
ATOM   1247  C CE2 . TYR   A 1 247  ? 113.245 152.360 132.736 1.00 16.38  0  211  TYR   A CE2 1 
ATOM   1248  C CZ  . TYR   A 1 247  ? 113.895 151.540 133.628 1.00 13.49  0  211  TYR   A CZ  1 
ATOM   1249  O OH  . TYR   A 1 247  ? 115.173 151.840 134.029 1.00 19.29  0  211  TYR   A OH  1 
ATOM   1250  N N   . THR   A 1 248  ? 108.758 153.098 133.919 1.00 22.53  0  212  THR   A N   1 
ATOM   1251  C CA  . THR   A 1 248  ? 109.019 154.333 134.643 1.00 14.49  0  212  THR   A CA  1 
ATOM   1252  C C   . THR   A 1 248  ? 108.411 154.291 136.035 1.00 24.84  0  212  THR   A C   1 
ATOM   1253  O O   . THR   A 1 248  ? 109.055 154.681 137.010 1.00 32.13  0  212  THR   A O   1 
ATOM   1254  C CB  . THR   A 1 248  ? 108.473 155.520 133.854 1.00 23.54  0  212  THR   A CB  1 
ATOM   1255  O OG1 . THR   A 1 248  ? 109.193 155.646 132.624 1.00 30.76  0  212  THR   A OG1 1 
ATOM   1256  C CG2 . THR   A 1 248  ? 108.614 156.800 134.645 1.00 23.85  0  212  THR   A CG2 1 
ATOM   1257  N N   . LYS   A 1 249  ? 107.179 153.796 136.152 1.00 28.74  0  213  LYS   A N   1 
ATOM   1258  C CA  . LYS   A 1 249  ? 106.532 153.759 137.460 1.00 13.47  0  213  LYS   A CA  1 
ATOM   1259  C C   . LYS   A 1 249  ? 107.183 152.739 138.389 1.00 14.81  0  213  LYS   A C   1 
ATOM   1260  O O   . LYS   A 1 249  ? 107.433 153.037 139.566 1.00 24.28  0  213  LYS   A O   1 
ATOM   1261  C CB  . LYS   A 1 249  ? 105.046 153.473 137.288 1.00 18.26  0  213  LYS   A CB  1 
ATOM   1262  C CG  . LYS   A 1 249  ? 104.356 154.518 136.440 1.00 20.00  0  213  LYS   A CG  1 
ATOM   1263  C CD  . LYS   A 1 249  ? 102.869 154.549 136.682 1.00 35.45  0  213  LYS   A CD  1 
ATOM   1264  C CE  . LYS   A 1 249  ? 102.267 155.811 136.097 1.00 33.88  0  213  LYS   A CE  1 
ATOM   1265  N NZ  . LYS   A 1 249  ? 103.209 156.956 136.227 1.00 28.97  1  213  LYS   A NZ  1 
ATOM   1266  N N   . LEU   A 1 250  ? 107.484 151.541 137.883 1.00 13.60  0  214  LEU   A N   1 
ATOM   1267  C CA  . LEU   A 1 250  ? 108.158 150.557 138.725 1.00 14.42  0  214  LEU   A CA  1 
ATOM   1268  C C   . LEU   A 1 250  ? 109.541 151.045 139.142 1.00 22.23  0  214  LEU   A C   1 
ATOM   1269  O O   . LEU   A 1 250  ? 109.964 150.850 140.291 1.00 24.73  0  214  LEU   A O   1 
ATOM   1270  C CB  . LEU   A 1 250  ? 108.254 149.220 137.995 1.00 32.69  0  214  LEU   A CB  1 
ATOM   1271  C CG  . LEU   A 1 250  ? 106.971 148.395 137.889 1.00 36.00  0  214  LEU   A CG  1 
ATOM   1272  C CD1 . LEU   A 1 250  ? 107.233 147.125 137.117 1.00 25.86  0  214  LEU   A CD1 1 
ATOM   1273  C CD2 . LEU   A 1 250  ? 106.425 148.074 139.262 1.00 25.93  0  214  LEU   A CD2 1 
ATOM   1274  N N   . ASN   A 1 251  ? 110.257 151.698 138.225 1.00 32.17  0  215  ASN   A N   1 
ATOM   1275  C CA  . ASN   A 1 251  ? 111.581 152.215 138.537 1.00 30.16  0  215  ASN   A CA  1 
ATOM   1276  C C   . ASN   A 1 251  ? 111.507 153.363 139.534 1.00 26.24  0  215  ASN   A C   1 
ATOM   1277  O O   . ASN   A 1 251  ? 112.401 153.518 140.367 1.00 29.41  0  215  ASN   A O   1 
ATOM   1278  C CB  . ASN   A 1 251  ? 112.276 152.658 137.254 1.00 19.26  0  215  ASN   A CB  1 
ATOM   1279  C CG  . ASN   A 1 251  ? 113.628 153.270 137.512 1.00 25.05  0  215  ASN   A CG  1 
ATOM   1280  O OD1 . ASN   A 1 251  ? 114.450 152.704 138.229 1.00 20.54  0  215  ASN   A OD1 1 
ATOM   1281  N ND2 . ASN   A 1 251  ? 113.870 154.433 136.924 1.00 30.43  0  215  ASN   A ND2 1 
ATOM   1282  N N   . ASN   A 1 252  ? 110.461 154.188 139.457 1.00 27.94  0  216  ASN   A N   1 
ATOM   1283  C CA  . ASN   A 1 252  ? 110.279 155.233 140.456 1.00 27.58  0  216  ASN   A CA  1 
ATOM   1284  C C   . ASN   A 1 252  ? 110.052 154.632 141.832 1.00 26.22  0  216  ASN   A C   1 
ATOM   1285  O O   . ASN   A 1 252  ? 110.608 155.114 142.825 1.00 35.09  0  216  ASN   A O   1 
ATOM   1286  C CB  . ASN   A 1 252  ? 109.112 156.140 140.072 1.00 27.57  0  216  ASN   A CB  1 
ATOM   1287  C CG  . ASN   A 1 252  ? 109.430 157.024 138.891 1.00 30.74  0  216  ASN   A CG  1 
ATOM   1288  O OD1 . ASN   A 1 252  ? 110.578 157.117 138.462 1.00 36.15  0  216  ASN   A OD1 1 
ATOM   1289  N ND2 . ASN   A 1 252  ? 108.411 157.683 138.355 1.00 25.76  0  216  ASN   A ND2 1 
ATOM   1290  N N   . ILE   A 1 253  ? 109.238 153.577 141.913 1.00 19.36  0  217  ILE   A N   1 
ATOM   1291  C CA  . ILE   A 1 253  ? 109.049 152.901 143.195 1.00 21.42  0  217  ILE   A CA  1 
ATOM   1292  C C   . ILE   A 1 253  ? 110.381 152.395 143.728 1.00 20.42  0  217  ILE   A C   1 
ATOM   1293  O O   . ILE   A 1 253  ? 110.726 152.601 144.902 1.00 33.12  0  217  ILE   A O   1 
ATOM   1294  C CB  . ILE   A 1 253  ? 108.037 151.752 143.056 1.00 24.18  0  217  ILE   A CB  1 
ATOM   1295  C CG1 . ILE   A 1 253  ? 106.672 152.283 142.648 1.00 18.93  0  217  ILE   A CG1 1 
ATOM   1296  C CG2 . ILE   A 1 253  ? 107.928 150.980 144.353 1.00 18.41  0  217  ILE   A CG2 1 
ATOM   1297  C CD1 . ILE   A 1 253  ? 105.713 151.205 142.233 1.00 28.48  0  217  ILE   A CD1 1 
ATOM   1298  N N   . LEU   A 1 254  ? 111.156 151.734 142.868 1.00 22.84  0  218  LEU   A N   1 
ATOM   1299  C CA  . LEU   A 1 254  ? 112.427 151.173 143.310 1.00 23.94  0  218  LEU   A CA  1 
ATOM   1300  C C   . LEU   A 1 254  ? 113.401 152.261 143.742 1.00 32.90  0  218  LEU   A C   1 
ATOM   1301  O O   . LEU   A 1 254  ? 114.088 152.115 144.757 1.00 43.12  0  218  LEU   A O   1 
ATOM   1302  C CB  . LEU   A 1 254  ? 113.037 150.322 142.203 1.00 22.66  0  218  LEU   A CB  1 
ATOM   1303  C CG  . LEU   A 1 254  ? 114.152 149.422 142.716 1.00 30.34  0  218  LEU   A CG  1 
ATOM   1304  C CD1 . LEU   A 1 254  ? 113.629 148.594 143.865 1.00 29.57  0  218  LEU   A CD1 1 
ATOM   1305  C CD2 . LEU   A 1 254  ? 114.663 148.536 141.608 1.00 32.81  0  218  LEU   A CD2 1 
ATOM   1306  N N   . THR   A 1 255  ? 113.483 153.352 142.979 1.00 24.91  0  219  THR   A N   1 
ATOM   1307  C CA  . THR   A 1 255  ? 114.399 154.434 143.316 1.00 18.97  0  219  THR   A CA  1 
ATOM   1308  C C   . THR   A 1 255  ? 114.010 155.097 144.629 1.00 26.38  0  219  THR   A C   1 
ATOM   1309  O O   . THR   A 1 255  ? 114.876 155.394 145.460 1.00 35.19  0  219  THR   A O   1 
ATOM   1310  C CB  . THR   A 1 255  ? 114.433 155.462 142.188 1.00 30.66  0  219  THR   A CB  1 
ATOM   1311  O OG1 . THR   A 1 255  ? 115.031 154.878 141.026 1.00 42.50  0  219  THR   A OG1 1 
ATOM   1312  C CG2 . THR   A 1 255  ? 115.236 156.678 142.597 1.00 33.59  0  219  THR   A CG2 1 
ATOM   1313  N N   . GLN   A 1 256  ? 112.713 155.338 144.835 1.00 28.27  0  220  GLN   A N   1 
ATOM   1314  C CA  . GLN   A 1 256  ? 112.270 155.922 146.095 1.00 24.38  0  220  GLN   A CA  1 
ATOM   1315  C C   . GLN   A 1 256  ? 112.643 155.028 147.265 1.00 23.96  0  220  GLN   A C   1 
ATOM   1316  O O   . GLN   A 1 256  ? 113.196 155.498 148.269 1.00 36.73  0  220  GLN   A O   1 
ATOM   1317  C CB  . GLN   A 1 256  ? 110.762 156.163 146.065 1.00 23.95  0  220  GLN   A CB  1 
ATOM   1318  C CG  . GLN   A 1 256  ? 110.337 157.317 145.183 1.00 33.01  0  220  GLN   A CG  1 
ATOM   1319  C CD  . GLN   A 1 256  ? 108.835 157.503 145.160 1.00 37.93  0  220  GLN   A CD  1 
ATOM   1320  O OE1 . GLN   A 1 256  ? 108.078 156.536 145.236 1.00 35.44  0  220  GLN   A OE1 1 
ATOM   1321  N NE2 . GLN   A 1 256  ? 108.394 158.750 145.055 1.00 32.70  0  220  GLN   A NE2 1 
ATOM   1322  N N   . TYR   A 1 257  ? 112.370 153.725 147.149 1.00 20.43  0  221  TYR   A N   1 
ATOM   1323  C CA  . TYR   A 1 257  ? 112.713 152.831 148.248 1.00 23.35  0  221  TYR   A CA  1 
ATOM   1324  C C   . TYR   A 1 257  ? 114.214 152.794 148.489 1.00 22.93  0  221  TYR   A C   1 
ATOM   1325  O O   . TYR   A 1 257  ? 114.661 152.821 149.638 1.00 30.99  0  221  TYR   A O   1 
ATOM   1326  C CB  . TYR   A 1 257  ? 112.209 151.416 147.993 1.00 27.71  0  221  TYR   A CB  1 
ATOM   1327  C CG  . TYR   A 1 257  ? 112.828 150.445 148.963 1.00 17.47  0  221  TYR   A CG  1 
ATOM   1328  C CD1 . TYR   A 1 257  ? 112.465 150.450 150.296 1.00 19.30  0  221  TYR   A CD1 1 
ATOM   1329  C CD2 . TYR   A 1 257  ? 113.803 149.554 148.557 1.00 23.75  0  221  TYR   A CD2 1 
ATOM   1330  C CE1 . TYR   A 1 257  ? 113.035 149.582 151.191 1.00 20.57  0  221  TYR   A CE1 1 
ATOM   1331  C CE2 . TYR   A 1 257  ? 114.380 148.682 149.448 1.00 26.48  0  221  TYR   A CE2 1 
ATOM   1332  C CZ  . TYR   A 1 257  ? 113.991 148.701 150.762 1.00 22.34  0  221  TYR   A CZ  1 
ATOM   1333  O OH  . TYR   A 1 257  ? 114.562 147.832 151.655 1.00 30.63  0  221  TYR   A OH  1 
ATOM   1334  N N   . ARG   A 1 258  ? 115.009 152.720 147.422 1.00 21.04  0  222  ARG   A N   1 
ATOM   1335  C CA  . ARG   A 1 258  ? 116.453 152.604 147.586 1.00 21.69  0  222  ARG   A CA  1 
ATOM   1336  C C   . ARG   A 1 258  ? 117.039 153.854 148.227 1.00 30.38  0  222  ARG   A C   1 
ATOM   1337  O O   . ARG   A 1 258  ? 117.866 153.766 149.142 1.00 40.03  0  222  ARG   A O   1 
ATOM   1338  C CB  . ARG   A 1 258  ? 117.106 152.325 146.236 1.00 24.68  0  222  ARG   A CB  1 
ATOM   1339  C CG  . ARG   A 1 258  ? 116.946 150.891 145.777 1.00 30.16  0  222  ARG   A CG  1 
ATOM   1340  C CD  . ARG   A 1 258  ? 117.519 150.682 144.395 1.00 22.14  0  222  ARG   A CD  1 
ATOM   1341  N NE  . ARG   A 1 258  ? 118.971 150.591 144.419 1.00 22.75  0  222  ARG   A NE  1 
ATOM   1342  C CZ  . ARG   A 1 258  ? 119.778 151.394 143.743 1.00 29.39  0  222  ARG   A CZ  1 
ATOM   1343  N NH1 . ARG   A 1 258  ? 119.304 152.362 142.978 1.00 29.19  1  222  ARG   A NH1 1 
ATOM   1344  N NH2 . ARG   A 1 258  ? 121.092 151.218 143.833 1.00 31.40  0  222  ARG   A NH2 1 
ATOM   1345  N N   . SER   A 1 259  ? 116.609 155.031 147.768 1.00 30.85  0  223  SER   A N   1 
ATOM   1346  C CA  . SER   A 1 259  ? 117.098 156.275 148.349 1.00 26.95  0  223  SER   A CA  1 
ATOM   1347  C C   . SER   A 1 259  ? 116.714 156.382 149.817 1.00 33.85  0  223  SER   A C   1 
ATOM   1348  O O   . SER   A 1 259  ? 117.564 156.651 150.676 1.00 40.26  0  223  SER   A O   1 
ATOM   1349  C CB  . SER   A 1 259  ? 116.552 157.463 147.562 1.00 29.79  0  223  SER   A CB  1 
ATOM   1350  O OG  . SER   A 1 259  ? 116.834 157.327 146.182 1.00 36.19  0  223  SER   A OG  1 
ATOM   1351  N N   . ASN   A 1 260  ? 115.437 156.155 150.133 1.00 28.44  0  224  ASN   A N   1 
ATOM   1352  C CA  . ASN   A 1 260  ? 114.992 156.306 151.510 1.00 21.25  0  224  ASN   A CA  1 
ATOM   1353  C C   . ASN   A 1 260  ? 115.461 155.179 152.418 1.00 23.99  0  224  ASN   A C   1 
ATOM   1354  O O   . ASN   A 1 260  ? 115.371 155.319 153.641 1.00 42.23  0  224  ASN   A O   1 
ATOM   1355  C CB  . ASN   A 1 260  ? 113.472 156.418 151.555 1.00 28.75  0  224  ASN   A CB  1 
ATOM   1356  C CG  . ASN   A 1 260  ? 112.960 157.615 150.788 1.00 33.97  0  224  ASN   A CG  1 
ATOM   1357  O OD1 . ASN   A 1 260  ? 113.716 158.529 150.469 1.00 28.71  0  224  ASN   A OD1 1 
ATOM   1358  N ND2 . ASN   A 1 260  ? 111.669 157.618 150.484 1.00 38.05  0  224  ASN   A ND2 1 
ATOM   1359  N N   . GLU   A 1 261  ? 115.952 154.073 151.863 1.00 14.40  0  225  GLU   A N   1 
ATOM   1360  C CA  . GLU   A 1 261  ? 116.577 153.041 152.676 1.00 16.64  0  225  GLU   A CA  1 
ATOM   1361  C C   . GLU   A 1 261  ? 118.050 153.311 152.911 1.00 27.77  0  225  GLU   A C   1 
ATOM   1362  O O   . GLU   A 1 261  ? 118.576 152.951 153.970 1.00 32.00  0  225  GLU   A O   1 
ATOM   1363  C CB  . GLU   A 1 261  ? 116.420 151.672 152.016 1.00 33.71  0  225  GLU   A CB  1 
ATOM   1364  C CG  . GLU   A 1 261  ? 116.351 150.516 152.999 1.00 38.05  0  225  GLU   A CG  1 
ATOM   1365  C CD  . GLU   A 1 261  ? 117.715 150.049 153.452 1.00 40.30  0  225  GLU   A CD  1 
ATOM   1366  O OE1 . GLU   A 1 261  ? 118.702 150.332 152.746 1.00 46.98  0  225  GLU   A OE1 1 
ATOM   1367  O OE2 . GLU   A 1 261  ? 117.800 149.390 154.508 1.00 35.50  -1 225  GLU   A OE2 1 
ATOM   1368  N N   . VAL   A 1 262  ? 118.734 153.917 151.939 1.00 41.74  0  226  VAL   A N   1 
ATOM   1369  C CA  . VAL   A 1 262  ? 120.097 154.381 152.178 1.00 36.16  0  226  VAL   A CA  1 
ATOM   1370  C C   . VAL   A 1 262  ? 120.096 155.458 153.253 1.00 35.90  0  226  VAL   A C   1 
ATOM   1371  O O   . VAL   A 1 262  ? 120.914 155.440 154.179 1.00 40.45  0  226  VAL   A O   1 
ATOM   1372  C CB  . VAL   A 1 262  ? 120.730 154.886 150.869 1.00 31.60  0  226  VAL   A CB  1 
ATOM   1373  C CG1 . VAL   A 1 262  ? 121.974 155.698 151.156 1.00 35.79  0  226  VAL   A CG1 1 
ATOM   1374  C CG2 . VAL   A 1 262  ? 121.061 153.720 149.966 1.00 32.36  0  226  VAL   A CG2 1 
ATOM   1375  N N   . LYS   A 1 263  ? 119.161 156.405 153.155 1.00 34.93  0  227  LYS   A N   1 
ATOM   1376  C CA  . LYS   A 1 263  ? 119.086 157.469 154.151 1.00 34.26  0  227  LYS   A CA  1 
ATOM   1377  C C   . LYS   A 1 263  ? 118.691 156.921 155.517 1.00 36.21  0  227  LYS   A C   1 
ATOM   1378  O O   . LYS   A 1 263  ? 119.356 157.190 156.522 1.00 40.45  0  227  LYS   A O   1 
ATOM   1379  C CB  . LYS   A 1 263  ? 118.096 158.540 153.696 1.00 34.08  0  227  LYS   A CB  1 
ATOM   1380  C CG  . LYS   A 1 263  ? 118.554 159.321 152.487 1.00 28.27  0  227  LYS   A CG  1 
ATOM   1381  C CD  . LYS   A 1 263  ? 117.707 160.554 152.281 1.00 31.94  0  227  LYS   A CD  1 
ATOM   1382  C CE  . LYS   A 1 263  ? 116.349 160.194 151.718 1.00 37.54  0  227  LYS   A CE  1 
ATOM   1383  N NZ  . LYS   A 1 263  ? 115.624 161.391 151.216 1.00 43.06  1  227  LYS   A NZ  1 
ATOM   1384  N N   . ASN   A 1 264  ? 117.615 156.140 155.571 1.00 38.45  0  228  ASN   A N   1 
ATOM   1385  C CA  . ASN   A 1 264  ? 117.064 155.635 156.822 1.00 37.24  0  228  ASN   A CA  1 
ATOM   1386  C C   . ASN   A 1 264  ? 117.050 154.116 156.779 1.00 42.94  0  228  ASN   A C   1 
ATOM   1387  O O   . ASN   A 1 264  ? 116.431 153.525 155.890 1.00 50.37  0  228  ASN   A O   1 
ATOM   1388  C CB  . ASN   A 1 264  ? 115.653 156.179 157.053 1.00 38.03  0  228  ASN   A CB  1 
ATOM   1389  C CG  . ASN   A 1 264  ? 115.105 155.815 158.418 1.00 47.43  0  228  ASN   A CG  1 
ATOM   1390  O OD1 . ASN   A 1 264  ? 114.125 155.081 158.531 1.00 49.13  0  228  ASN   A OD1 1 
ATOM   1391  N ND2 . ASN   A 1 264  ? 115.737 156.332 159.466 1.00 45.17  0  228  ASN   A ND2 1 
ATOM   1392  N N   . HIS   A 1 265  ? 117.722 153.489 157.738 1.00 48.72  0  229  HIS   A N   1 
ATOM   1393  C CA  . HIS   A 1 265  ? 117.772 152.036 157.779 1.00 48.32  0  229  HIS   A CA  1 
ATOM   1394  C C   . HIS   A 1 265  ? 116.432 151.464 158.229 1.00 46.91  0  229  HIS   A C   1 
ATOM   1395  O O   . HIS   A 1 265  ? 115.728 152.046 159.057 1.00 49.91  0  229  HIS   A O   1 
ATOM   1396  C CB  . HIS   A 1 265  ? 118.886 151.566 158.710 1.00 46.76  0  229  HIS   A CB  1 
ATOM   1397  C CG  . HIS   A 1 265  ? 119.022 150.078 158.786 1.00 53.57  0  229  HIS   A CG  1 
ATOM   1398  N ND1 . HIS   A 1 265  ? 119.061 149.277 157.665 1.00 59.61  0  229  HIS   A ND1 1 
ATOM   1399  C CD2 . HIS   A 1 265  ? 119.144 149.246 159.847 1.00 54.32  0  229  HIS   A CD2 1 
ATOM   1400  C CE1 . HIS   A 1 265  ? 119.191 148.015 158.032 1.00 53.90  0  229  HIS   A CE1 1 
ATOM   1401  N NE2 . HIS   A 1 265  ? 119.245 147.969 159.351 1.00 56.16  0  229  HIS   A NE2 1 
ATOM   1402  N N   . GLY   A 1 266  ? 116.082 150.309 157.666 1.00 43.98  0  230  GLY   A N   1 
ATOM   1403  C CA  . GLY   A 1 266  ? 114.825 149.656 157.964 1.00 46.77  0  230  GLY   A CA  1 
ATOM   1404  C C   . GLY   A 1 266  ? 113.614 150.256 157.287 1.00 47.26  0  230  GLY   A C   1 
ATOM   1405  O O   . GLY   A 1 266  ? 112.486 149.891 157.640 1.00 37.59  0  230  GLY   A O   1 
ATOM   1406  N N   . PHE   A 1 267  ? 113.809 151.158 156.330 1.00 39.90  0  231  PHE   A N   1 
ATOM   1407  C CA  . PHE   A 1 267  ? 112.691 151.843 155.698 1.00 32.50  0  231  PHE   A CA  1 
ATOM   1408  C C   . PHE   A 1 267  ? 111.827 150.862 154.919 1.00 34.22  0  231  PHE   A C   1 
ATOM   1409  O O   . PHE   A 1 267  ? 112.334 149.961 154.248 1.00 40.36  0  231  PHE   A O   1 
ATOM   1410  C CB  . PHE   A 1 267  ? 113.215 152.935 154.770 1.00 29.53  0  231  PHE   A CB  1 
ATOM   1411  C CG  . PHE   A 1 267  ? 112.141 153.694 154.054 1.00 28.89  0  231  PHE   A CG  1 
ATOM   1412  C CD1 . PHE   A 1 267  ? 111.412 154.669 154.707 1.00 34.06  0  231  PHE   A CD1 1 
ATOM   1413  C CD2 . PHE   A 1 267  ? 111.876 153.449 152.721 1.00 24.74  0  231  PHE   A CD2 1 
ATOM   1414  C CE1 . PHE   A 1 267  ? 110.432 155.375 154.046 1.00 33.54  0  231  PHE   A CE1 1 
ATOM   1415  C CE2 . PHE   A 1 267  ? 110.898 154.152 152.057 1.00 29.88  0  231  PHE   A CE2 1 
ATOM   1416  C CZ  . PHE   A 1 267  ? 110.175 155.117 152.719 1.00 32.14  0  231  PHE   A CZ  1 
ATOM   1417  N N   . THR   A 1 268  ? 110.512 151.041 155.019 1.00 28.76  0  232  THR   A N   1 
ATOM   1418  C CA  . THR   A 1 268  ? 109.538 150.255 154.271 1.00 30.47  0  232  THR   A CA  1 
ATOM   1419  C C   . THR   A 1 268  ? 108.710 151.202 153.418 1.00 30.83  0  232  THR   A C   1 
ATOM   1420  O O   . THR   A 1 268  ? 108.046 152.097 153.950 1.00 34.58  0  232  THR   A O   1 
ATOM   1421  C CB  . THR   A 1 268  ? 108.632 149.460 155.210 1.00 35.10  0  232  THR   A CB  1 
ATOM   1422  O OG1 . THR   A 1 268  ? 109.390 148.426 155.849 1.00 39.58  0  232  THR   A OG1 1 
ATOM   1423  C CG2 . THR   A 1 268  ? 107.488 148.841 154.437 1.00 34.70  0  232  THR   A CG2 1 
ATOM   1424  N N   . LEU   A 1 269  ? 108.738 151.003 152.104 1.00 29.01  0  233  LEU   A N   1 
ATOM   1425  C CA  . LEU   A 1 269  ? 108.061 151.916 151.193 1.00 35.55  0  233  LEU   A CA  1 
ATOM   1426  C C   . LEU   A 1 269  ? 106.609 151.499 151.024 1.00 31.53  0  233  LEU   A C   1 
ATOM   1427  O O   . LEU   A 1 269  ? 106.325 150.437 150.466 1.00 38.59  0  233  LEU   A O   1 
ATOM   1428  C CB  . LEU   A 1 269  ? 108.758 151.948 149.837 1.00 33.46  0  233  LEU   A CB  1 
ATOM   1429  C CG  . LEU   A 1 269  ? 108.021 152.776 148.783 1.00 29.23  0  233  LEU   A CG  1 
ATOM   1430  C CD1 . LEU   A 1 269  ? 107.942 154.230 149.203 1.00 37.06  0  233  LEU   A CD1 1 
ATOM   1431  C CD2 . LEU   A 1 269  ? 108.701 152.661 147.445 1.00 37.65  0  233  LEU   A CD2 1 
ATOM   1432  N N   . ILE   A 1 270  ? 105.692 152.339 151.488 1.00 32.90  0  234  ILE   A N   1 
ATOM   1433  C CA  . ILE   A 1 270  ? 104.261 152.105 151.352 1.00 37.12  0  234  ILE   A CA  1 
ATOM   1434  C C   . ILE   A 1 270  ? 103.723 153.135 150.375 1.00 37.20  0  234  ILE   A C   1 
ATOM   1435  O O   . ILE   A 1 270  ? 103.806 154.342 150.633 1.00 41.59  0  234  ILE   A O   1 
ATOM   1436  C CB  . ILE   A 1 270  ? 103.545 152.204 152.705 1.00 31.11  0  234  ILE   A CB  1 
ATOM   1437  C CG1 . ILE   A 1 270  ? 104.077 151.143 153.664 1.00 33.76  0  234  ILE   A CG1 1 
ATOM   1438  C CG2 . ILE   A 1 270  ? 102.053 152.058 152.522 1.00 32.10  0  234  ILE   A CG2 1 
ATOM   1439  C CD1 . ILE   A 1 270  ? 103.722 151.399 155.100 1.00 37.61  0  234  ILE   A CD1 1 
ATOM   1440  N N   . ASP   A 1 271  ? 103.172 152.674 149.255 1.00 32.60  0  235  ASP   A N   1 
ATOM   1441  C CA  . ASP   A 1 271  ? 102.670 153.636 148.283 1.00 34.93  0  235  ASP   A CA  1 
ATOM   1442  C C   . ASP   A 1 271  ? 101.544 153.031 147.461 1.00 29.13  0  235  ASP   A C   1 
ATOM   1443  O O   . ASP   A 1 271  ? 101.592 151.855 147.099 1.00 30.13  0  235  ASP   A O   1 
ATOM   1444  C CB  . ASP   A 1 271  ? 103.788 154.133 147.361 1.00 41.03  0  235  ASP   A CB  1 
ATOM   1445  C CG  . ASP   A 1 271  ? 104.337 153.046 146.468 1.00 44.37  0  235  ASP   A CG  1 
ATOM   1446  O OD1 . ASP   A 1 271  ? 103.689 152.727 145.451 1.00 47.32  0  235  ASP   A OD1 1 
ATOM   1447  O OD2 . ASP   A 1 271  ? 105.421 152.513 146.781 1.00 42.18  -1 235  ASP   A OD2 1 
ATOM   1448  N N   . ASN   A 1 272  ? 100.548 153.859 147.149 1.00 42.98  0  236  ASN   A N   1 
ATOM   1449  C CA  . ASN   A 1 272  ? 99.418  153.449 146.329 1.00 45.86  0  236  ASN   A CA  1 
ATOM   1450  C C   . ASN   A 1 272  ? 99.049  154.497 145.289 1.00 47.09  0  236  ASN   A C   1 
ATOM   1451  O O   . ASN   A 1 272  ? 97.985  154.388 144.669 1.00 45.10  0  236  ASN   A O   1 
ATOM   1452  C CB  . ASN   A 1 272  ? 98.202  153.144 147.209 1.00 43.47  0  236  ASN   A CB  1 
ATOM   1453  C CG  . ASN   A 1 272  ? 97.843  154.296 148.121 1.00 48.12  0  236  ASN   A CG  1 
ATOM   1454  O OD1 . ASN   A 1 272  ? 98.529  155.317 148.146 1.00 47.24  0  236  ASN   A OD1 1 
ATOM   1455  N ND2 . ASN   A 1 272  ? 96.763  154.141 148.876 1.00 46.54  0  236  ASN   A ND2 1 
ATOM   1456  N N   . GLN   A 1 273  ? 99.897  155.501 145.078 1.00 51.09  0  237  GLN   A N   1 
ATOM   1457  C CA  . GLN   A 1 273  ? 99.598  156.612 144.183 1.00 53.13  0  237  GLN   A CA  1 
ATOM   1458  C C   . GLN   A 1 273  ? 100.304 156.513 142.840 1.00 53.15  0  237  GLN   A C   1 
ATOM   1459  O O   . GLN   A 1 273  ? 99.715  156.864 141.813 1.00 55.09  0  237  GLN   A O   1 
ATOM   1460  C CB  . GLN   A 1 273  ? 99.974  157.938 144.851 1.00 51.69  0  237  GLN   A CB  1 
ATOM   1461  C CG  . GLN   A 1 273  ? 98.977  158.418 145.890 1.00 54.28  0  237  GLN   A CG  1 
ATOM   1462  C CD  . GLN   A 1 273  ? 97.746  159.044 145.268 1.00 56.44  0  237  GLN   A CD  1 
ATOM   1463  O OE1 . GLN   A 1 273  ? 96.629  158.558 145.447 1.00 56.64  0  237  GLN   A OE1 1 
ATOM   1464  N NE2 . GLN   A 1 273  ? 97.944  160.128 144.529 1.00 55.56  0  237  GLN   A NE2 1 
ATOM   1465  N N   . THR   A 1 274  ? 101.556 156.054 142.821 1.00 40.25  0  238  THR   A N   1 
ATOM   1466  C CA  . THR   A 1 274  ? 102.320 156.032 141.577 1.00 37.94  0  238  THR   A CA  1 
ATOM   1467  C C   . THR   A 1 274  ? 101.720 155.063 140.562 1.00 40.61  0  238  THR   A C   1 
ATOM   1468  O O   . THR   A 1 274  ? 101.551 155.412 139.389 1.00 39.63  0  238  THR   A O   1 
ATOM   1469  C CB  . THR   A 1 274  ? 103.786 155.704 141.871 1.00 39.12  0  238  THR   A CB  1 
ATOM   1470  O OG1 . THR   A 1 274  ? 104.540 155.704 140.653 1.00 41.55  0  238  THR   A OG1 1 
ATOM   1471  C CG2 . THR   A 1 274  ? 103.928 154.381 142.596 1.00 39.53  0  238  THR   A CG2 1 
ATOM   1472  N N   . LEU   A 1 275  ? 101.381 153.849 140.989 1.00 42.29  0  239  LEU   A N   1 
ATOM   1473  C CA  . LEU   A 1 275  ? 100.714 152.870 140.133 1.00 39.59  0  239  LEU   A CA  1 
ATOM   1474  C C   . LEU   A 1 275  ? 99.245  152.855 140.534 1.00 46.02  0  239  LEU   A C   1 
ATOM   1475  O O   . LEU   A 1 275  ? 98.888  152.347 141.599 1.00 47.54  0  239  LEU   A O   1 
ATOM   1476  C CB  . LEU   A 1 275  ? 101.353 151.492 140.267 1.00 36.21  0  239  LEU   A CB  1 
ATOM   1477  C CG  . LEU   A 1 275  ? 102.367 151.102 139.187 1.00 40.46  0  239  LEU   A CG  1 
ATOM   1478  C CD1 . LEU   A 1 275  ? 103.085 149.822 139.565 1.00 39.35  0  239  LEU   A CD1 1 
ATOM   1479  C CD2 . LEU   A 1 275  ? 101.697 150.951 137.834 1.00 36.08  0  239  LEU   A CD2 1 
ATOM   1480  N N   . SER   A 1 276  ? 98.395  153.417 139.680 1.00 49.42  0  240  SER   A N   1 
ATOM   1481  C CA  . SER   A 1 276  ? 96.993  153.601 140.030 1.00 49.41  0  240  SER   A CA  1 
ATOM   1482  C C   . SER   A 1 276  ? 96.303  152.257 140.207 1.00 51.90  0  240  SER   A C   1 
ATOM   1483  O O   . SER   A 1 276  ? 96.264  151.439 139.283 1.00 52.14  0  240  SER   A O   1 
ATOM   1484  C CB  . SER   A 1 276  ? 96.294  154.427 138.955 1.00 52.83  0  240  SER   A CB  1 
ATOM   1485  O OG  . SER   A 1 276  ? 96.857  155.724 138.871 1.00 53.72  0  240  SER   A OG  1 
ATOM   1486  N N   . GLY   A 1 277  ? 95.757  152.034 141.399 1.00 45.10  0  241  GLY   A N   1 
ATOM   1487  C CA  . GLY   A 1 277  ? 95.061  150.801 141.701 1.00 48.01  0  241  GLY   A CA  1 
ATOM   1488  C C   . GLY   A 1 277  ? 95.842  149.889 142.622 1.00 41.86  0  241  GLY   A C   1 
ATOM   1489  O O   . GLY   A 1 277  ? 95.279  149.300 143.548 1.00 39.90  0  241  GLY   A O   1 
ATOM   1490  N N   . PHE   A 1 278  ? 97.144  149.776 142.385 1.00 20.43  0  242  PHE   A N   1 
ATOM   1491  C CA  . PHE   A 1 278  ? 97.978  148.879 143.167 1.00 21.66  0  242  PHE   A CA  1 
ATOM   1492  C C   . PHE   A 1 278  ? 98.437  149.548 144.454 1.00 28.47  0  242  PHE   A C   1 
ATOM   1493  O O   . PHE   A 1 278  ? 98.549  150.772 144.538 1.00 43.27  0  242  PHE   A O   1 
ATOM   1494  C CB  . PHE   A 1 278  ? 99.193  148.438 142.356 1.00 33.84  0  242  PHE   A CB  1 
ATOM   1495  C CG  . PHE   A 1 278  ? 98.865  147.499 141.235 1.00 40.36  0  242  PHE   A CG  1 
ATOM   1496  C CD1 . PHE   A 1 278  ? 98.444  147.984 140.013 1.00 34.14  0  242  PHE   A CD1 1 
ATOM   1497  C CD2 . PHE   A 1 278  ? 98.988  146.133 141.402 1.00 34.68  0  242  PHE   A CD2 1 
ATOM   1498  C CE1 . PHE   A 1 278  ? 98.146  147.129 138.985 1.00 29.59  0  242  PHE   A CE1 1 
ATOM   1499  C CE2 . PHE   A 1 278  ? 98.691  145.276 140.376 1.00 26.86  0  242  PHE   A CE2 1 
ATOM   1500  C CZ  . PHE   A 1 278  ? 98.269  145.774 139.167 1.00 30.47  0  242  PHE   A CZ  1 
ATOM   1501  N N   . GLN   A 1 279  ? 98.707  148.726 145.462 1.00 23.94  0  243  GLN   A N   1 
ATOM   1502  C CA  . GLN   A 1 279  ? 99.224  149.185 146.745 1.00 22.03  0  243  GLN   A CA  1 
ATOM   1503  C C   . GLN   A 1 279  ? 100.440 148.336 147.075 1.00 15.14  0  243  GLN   A C   1 
ATOM   1504  O O   . GLN   A 1 279  ? 100.315 147.123 147.276 1.00 32.42  0  243  GLN   A O   1 
ATOM   1505  C CB  . GLN   A 1 279  ? 98.165  149.071 147.840 1.00 30.09  0  243  GLN   A CB  1 
ATOM   1506  C CG  . GLN   A 1 279  ? 98.708  149.153 149.253 1.00 32.46  0  243  GLN   A CG  1 
ATOM   1507  C CD  . GLN   A 1 279  ? 98.555  150.530 149.853 1.00 37.78  0  243  GLN   A CD  1 
ATOM   1508  O OE1 . GLN   A 1 279  ? 97.472  151.110 149.829 1.00 34.15  0  243  GLN   A OE1 1 
ATOM   1509  N NE2 . GLN   A 1 279  ? 99.639  151.060 150.401 1.00 37.35  0  243  GLN   A NE2 1 
ATOM   1510  N N   . PHE   A 1 280  ? 101.607 148.971 147.125 1.00 17.53  0  244  PHE   A N   1 
ATOM   1511  C CA  . PHE   A 1 280  ? 102.873 148.294 147.348 1.00 26.98  0  244  PHE   A CA  1 
ATOM   1512  C C   . PHE   A 1 280  ? 103.356 148.563 148.762 1.00 26.46  0  244  PHE   A C   1 
ATOM   1513  O O   . PHE   A 1 280  ? 103.380 149.717 149.207 1.00 34.28  0  244  PHE   A O   1 
ATOM   1514  C CB  . PHE   A 1 280  ? 103.934 148.770 146.356 1.00 25.84  0  244  PHE   A CB  1 
ATOM   1515  C CG  . PHE   A 1 280  ? 103.729 148.278 144.961 1.00 22.32  0  244  PHE   A CG  1 
ATOM   1516  C CD1 . PHE   A 1 280  ? 102.961 148.998 144.070 1.00 26.37  0  244  PHE   A CD1 1 
ATOM   1517  C CD2 . PHE   A 1 280  ? 104.317 147.105 144.535 1.00 22.63  0  244  PHE   A CD2 1 
ATOM   1518  C CE1 . PHE   A 1 280  ? 102.775 148.554 142.784 1.00 27.90  0  244  PHE   A CE1 1 
ATOM   1519  C CE2 . PHE   A 1 280  ? 104.132 146.656 143.250 1.00 32.64  0  244  PHE   A CE2 1 
ATOM   1520  C CZ  . PHE   A 1 280  ? 103.361 147.382 142.372 1.00 32.96  0  244  PHE   A CZ  1 
ATOM   1521  N N   . ILE   A 1 281  ? 103.731 147.501 149.457 1.00 20.46  0  245  ILE   A N   1 
ATOM   1522  C CA  . ILE   A 1 281  ? 104.484 147.578 150.702 1.00 15.51  0  245  ILE   A CA  1 
ATOM   1523  C C   . ILE   A 1 281  ? 105.801 146.872 150.414 1.00 17.63  0  245  ILE   A C   1 
ATOM   1524  O O   . ILE   A 1 281  ? 105.904 145.649 150.526 1.00 26.48  0  245  ILE   A O   1 
ATOM   1525  C CB  . ILE   A 1 281  ? 103.744 146.937 151.875 1.00 20.84  0  245  ILE   A CB  1 
ATOM   1526  C CG1 . ILE   A 1 281  ? 102.380 147.598 152.065 1.00 25.92  0  245  ILE   A CG1 1 
ATOM   1527  C CG2 . ILE   A 1 281  ? 104.575 147.020 153.138 1.00 23.33  0  245  ILE   A CG2 1 
ATOM   1528  C CD1 . ILE   A 1 281  ? 101.366 146.700 152.715 1.00 28.57  0  245  ILE   A CD1 1 
ATOM   1529  N N   . LEU   A 1 282  ? 106.804 147.642 150.013 1.00 27.56  0  246  LEU   A N   1 
ATOM   1530  C CA  . LEU   A 1 282  ? 108.067 147.126 149.511 1.00 21.44  0  246  LEU   A CA  1 
ATOM   1531  C C   . LEU   A 1 282  ? 109.156 147.266 150.566 1.00 28.40  0  246  LEU   A C   1 
ATOM   1532  O O   . LEU   A 1 282  ? 109.206 148.247 151.309 1.00 34.32  0  246  LEU   A O   1 
ATOM   1533  C CB  . LEU   A 1 282  ? 108.465 147.865 148.233 1.00 19.97  0  246  LEU   A CB  1 
ATOM   1534  C CG  . LEU   A 1 282  ? 109.718 147.439 147.478 1.00 31.58  0  246  LEU   A CG  1 
ATOM   1535  C CD1 . LEU   A 1 282  ? 109.674 145.960 147.168 1.00 32.79  0  246  LEU   A CD1 1 
ATOM   1536  C CD2 . LEU   A 1 282  ? 109.835 148.246 146.199 1.00 32.81  0  246  LEU   A CD2 1 
ATOM   1537  N N   . ASN   A 1 283  ? 110.032 146.269 150.622 1.00 29.74  0  247  ASN   A N   1 
ATOM   1538  C CA  . ASN   A 1 283  ? 111.064 146.179 151.639 1.00 24.39  0  247  ASN   A CA  1 
ATOM   1539  C C   . ASN   A 1 283  ? 112.092 145.167 151.163 1.00 32.80  0  247  ASN   A C   1 
ATOM   1540  O O   . ASN   A 1 283  ? 111.759 144.242 150.418 1.00 28.91  0  247  ASN   A O   1 
ATOM   1541  C CB  . ASN   A 1 283  ? 110.471 145.751 152.983 1.00 17.31  0  247  ASN   A CB  1 
ATOM   1542  C CG  . ASN   A 1 283  ? 111.332 146.143 154.151 1.00 18.78  0  247  ASN   A CG  1 
ATOM   1543  O OD1 . ASN   A 1 283  ? 112.555 146.072 154.084 1.00 25.55  0  247  ASN   A OD1 1 
ATOM   1544  N ND2 . ASN   A 1 283  ? 110.697 146.548 155.240 1.00 22.97  0  247  ASN   A ND2 1 
ATOM   1545  N N   . GLN   A 1 284  ? 113.335 145.327 151.620 1.00 41.45  0  248  GLN   A N   1 
ATOM   1546  C CA  . GLN   A 1 284  ? 114.390 144.446 151.136 1.00 39.27  0  248  GLN   A CA  1 
ATOM   1547  C C   . GLN   A 1 284  ? 114.140 142.993 151.514 1.00 42.43  0  248  GLN   A C   1 
ATOM   1548  O O   . GLN   A 1 284  ? 114.764 142.099 150.935 1.00 45.48  0  248  GLN   A O   1 
ATOM   1549  C CB  . GLN   A 1 284  ? 115.755 144.885 151.663 1.00 38.83  0  248  GLN   A CB  1 
ATOM   1550  C CG  . GLN   A 1 284  ? 116.063 144.422 153.069 1.00 39.35  0  248  GLN   A CG  1 
ATOM   1551  C CD  . GLN   A 1 284  ? 117.550 144.404 153.355 1.00 46.52  0  248  GLN   A CD  1 
ATOM   1552  O OE1 . GLN   A 1 284  ? 118.364 144.691 152.478 1.00 45.56  0  248  GLN   A OE1 1 
ATOM   1553  N NE2 . GLN   A 1 284  ? 117.913 144.048 154.580 1.00 44.92  0  248  GLN   A NE2 1 
ATOM   1554  N N   . TYR   A 1 285  ? 113.241 142.734 152.463 1.00 36.26  0  249  TYR   A N   1 
ATOM   1555  C CA  . TYR   A 1 285  ? 112.856 141.371 152.808 1.00 36.14  0  249  TYR   A CA  1 
ATOM   1556  C C   . TYR   A 1 285  ? 111.360 141.125 152.643 1.00 30.20  0  249  TYR   A C   1 
ATOM   1557  O O   . TYR   A 1 285  ? 110.797 140.292 153.358 1.00 36.41  0  249  TYR   A O   1 
ATOM   1558  C CB  . TYR   A 1 285  ? 113.295 141.024 154.231 1.00 34.83  0  249  TYR   A CB  1 
ATOM   1559  C CG  . TYR   A 1 285  ? 113.426 142.207 155.155 1.00 39.13  0  249  TYR   A CG  1 
ATOM   1560  C CD1 . TYR   A 1 285  ? 112.310 142.936 155.548 1.00 45.18  0  249  TYR   A CD1 1 
ATOM   1561  C CD2 . TYR   A 1 285  ? 114.663 142.581 155.659 1.00 37.53  0  249  TYR   A CD2 1 
ATOM   1562  C CE1 . TYR   A 1 285  ? 112.427 144.018 156.408 1.00 44.27  0  249  TYR   A CE1 1 
ATOM   1563  C CE2 . TYR   A 1 285  ? 114.792 143.662 156.513 1.00 45.52  0  249  TYR   A CE2 1 
ATOM   1564  C CZ  . TYR   A 1 285  ? 113.671 144.376 156.885 1.00 48.17  0  249  TYR   A CZ  1 
ATOM   1565  O OH  . TYR   A 1 285  ? 113.794 145.449 157.738 1.00 38.77  0  249  TYR   A OH  1 
ATOM   1566  N N   . GLY   A 1 286  ? 110.699 141.817 151.722 1.00 19.86  0  250  GLY   A N   1 
ATOM   1567  C CA  . GLY   A 1 286  ? 109.309 141.492 151.452 1.00 11.41  0  250  GLY   A CA  1 
ATOM   1568  C C   . GLY   A 1 286  ? 108.682 142.460 150.477 1.00 16.94  0  250  GLY   A C   1 
ATOM   1569  O O   . GLY   A 1 286  ? 109.220 143.529 150.184 1.00 29.79  0  250  GLY   A O   1 
ATOM   1570  N N   . CYS   A 1 287  ? 107.517 142.064 149.975 1.00 16.69  0  251  CYS   A N   1 
ATOM   1571  C CA  . CYS   A 1 287  ? 106.753 142.920 149.073 1.00 22.96  0  251  CYS   A CA  1 
ATOM   1572  C C   . CYS   A 1 287  ? 105.306 142.456 149.127 1.00 24.38  0  251  CYS   A C   1 
ATOM   1573  O O   . CYS   A 1 287  ? 104.974 141.407 148.572 1.00 39.26  0  251  CYS   A O   1 
ATOM   1574  C CB  . CYS   A 1 287  ? 107.307 142.849 147.656 1.00 15.03  0  251  CYS   A CB  1 
ATOM   1575  S SG  . CYS   A 1 287  ? 106.322 143.703 146.409 1.00 26.34  0  251  CYS   A SG  1 
ATOM   1576  N N   . ILE   A 1 288  ? 104.456 143.224 149.790 1.00 11.58  0  252  ILE   A N   1 
ATOM   1577  C CA  . ILE   A 1 288  ? 103.037 142.915 149.873 1.00 8.84   0  252  ILE   A CA  1 
ATOM   1578  C C   . ILE   A 1 288  ? 102.321 143.760 148.836 1.00 11.49  0  252  ILE   A C   1 
ATOM   1579  O O   . ILE   A 1 288  ? 102.385 144.993 148.880 1.00 32.95  0  252  ILE   A O   1 
ATOM   1580  C CB  . ILE   A 1 288  ? 102.484 143.175 151.280 1.00 25.99  0  252  ILE   A CB  1 
ATOM   1581  C CG1 . ILE   A 1 288  ? 103.141 142.231 152.284 1.00 25.13  0  252  ILE   A CG1 1 
ATOM   1582  C CG2 . ILE   A 1 288  ? 100.980 143.009 151.294 1.00 27.62  0  252  ILE   A CG2 1 
ATOM   1583  C CD1 . ILE   A 1 288  ? 102.916 142.621 153.712 1.00 27.92  0  252  ILE   A CD1 1 
ATOM   1584  N N   . VAL   A 1 289  ? 101.653 143.113 147.890 1.00 7.01   0  253  VAL   A N   1 
ATOM   1585  C CA  . VAL   A 1 289  ? 100.938 143.823 146.839 1.00 16.02  0  253  VAL   A CA  1 
ATOM   1586  C C   . VAL   A 1 289  ? 99.452  143.597 147.044 1.00 24.42  0  253  VAL   A C   1 
ATOM   1587  O O   . VAL   A 1 289  ? 99.013  142.468 147.282 1.00 34.14  0  253  VAL   A O   1 
ATOM   1588  C CB  . VAL   A 1 289  ? 101.371 143.381 145.429 1.00 17.19  0  253  VAL   A CB  1 
ATOM   1589  C CG1 . VAL   A 1 289  ? 100.841 144.354 144.388 1.00 12.98  0  253  VAL   A CG1 1 
ATOM   1590  C CG2 . VAL   A 1 289  ? 102.874 143.279 145.348 1.00 11.82  0  253  VAL   A CG2 1 
ATOM   1591  N N   . TYR   A 1 290  ? 98.681  144.678 146.985 1.00 26.84  0  254  TYR   A N   1 
ATOM   1592  C CA  . TYR   A 1 290  ? 97.237  144.604 147.167 1.00 24.31  0  254  TYR   A CA  1 
ATOM   1593  C C   . TYR   A 1 290  ? 96.555  145.361 146.041 1.00 25.17  0  254  TYR   A C   1 
ATOM   1594  O O   . TYR   A 1 290  ? 96.878  146.523 145.785 1.00 35.59  0  254  TYR   A O   1 
ATOM   1595  C CB  . TYR   A 1 290  ? 96.826  145.171 148.529 1.00 29.43  0  254  TYR   A CB  1 
ATOM   1596  C CG  . TYR   A 1 290  ? 95.357  145.502 148.641 1.00 28.57  0  254  TYR   A CG  1 
ATOM   1597  C CD1 . TYR   A 1 290  ? 94.418  144.508 148.854 1.00 28.51  0  254  TYR   A CD1 1 
ATOM   1598  C CD2 . TYR   A 1 290  ? 94.911  146.811 148.543 1.00 33.63  0  254  TYR   A CD2 1 
ATOM   1599  C CE1 . TYR   A 1 290  ? 93.079  144.805 148.956 1.00 28.04  0  254  TYR   A CE1 1 
ATOM   1600  C CE2 . TYR   A 1 290  ? 93.573  147.115 148.645 1.00 30.38  0  254  TYR   A CE2 1 
ATOM   1601  C CZ  . TYR   A 1 290  ? 92.662  146.108 148.851 1.00 26.40  0  254  TYR   A CZ  1 
ATOM   1602  O OH  . TYR   A 1 290  ? 91.326  146.404 148.953 1.00 32.26  0  254  TYR   A OH  1 
ATOM   1603  N N   . HIS   A 1 291  ? 95.617  144.707 145.371 1.00 22.77  0  255  HIS   A N   1 
ATOM   1604  C CA  . HIS   A 1 291  ? 94.784  145.344 144.364 1.00 30.93  0  255  HIS   A CA  1 
ATOM   1605  C C   . HIS   A 1 291  ? 93.386  145.516 144.942 1.00 38.94  0  255  HIS   A C   1 
ATOM   1606  O O   . HIS   A 1 291  ? 92.741  144.531 145.321 1.00 43.44  0  255  HIS   A O   1 
ATOM   1607  C CB  . HIS   A 1 291  ? 94.741  144.517 143.083 1.00 34.05  0  255  HIS   A CB  1 
ATOM   1608  C CG  . HIS   A 1 291  ? 94.460  145.324 141.858 1.00 31.89  0  255  HIS   A CG  1 
ATOM   1609  N ND1 . HIS   A 1 291  ? 93.209  145.818 141.566 1.00 32.92  0  255  HIS   A ND1 1 
ATOM   1610  C CD2 . HIS   A 1 291  ? 95.266  145.717 140.846 1.00 35.87  0  255  HIS   A CD2 1 
ATOM   1611  C CE1 . HIS   A 1 291  ? 93.257  146.486 140.428 1.00 34.63  0  255  HIS   A CE1 1 
ATOM   1612  N NE2 . HIS   A 1 291  ? 94.493  146.439 139.970 1.00 44.85  0  255  HIS   A NE2 1 
ATOM   1613  N N   . LYS   A 1 292  ? 92.924  146.765 145.006 1.00 42.44  0  256  LYS   A N   1 
ATOM   1614  C CA  . LYS   A 1 292  ? 91.661  147.074 145.666 1.00 35.08  0  256  LYS   A CA  1 
ATOM   1615  C C   . LYS   A 1 292  ? 90.470  146.800 144.760 1.00 38.60  0  256  LYS   A C   1 
ATOM   1616  O O   . LYS   A 1 292  ? 89.482  146.197 145.190 1.00 47.51  0  256  LYS   A O   1 
ATOM   1617  C CB  . LYS   A 1 292  ? 91.657  148.533 146.120 1.00 41.30  0  256  LYS   A CB  1 
ATOM   1618  C CG  . LYS   A 1 292  ? 90.318  149.029 146.630 1.00 41.38  0  256  LYS   A CG  1 
ATOM   1619  C CD  . LYS   A 1 292  ? 90.449  150.416 147.231 1.00 42.05  0  256  LYS   A CD  1 
ATOM   1620  C CE  . LYS   A 1 292  ? 90.965  150.352 148.657 1.00 43.64  0  256  LYS   A CE  1 
ATOM   1621  N NZ  . LYS   A 1 292  ? 90.195  149.381 149.480 1.00 49.30  1  256  LYS   A NZ  1 
ATOM   1622  N N   . GLU   A 1 293  ? 90.545  147.239 143.502 1.00 40.43  0  257  GLU   A N   1 
ATOM   1623  C CA  . GLU   A 1 293  ? 89.409  147.083 142.602 1.00 40.58  0  257  GLU   A CA  1 
ATOM   1624  C C   . GLU   A 1 293  ? 89.076  145.618 142.366 1.00 49.14  0  257  GLU   A C   1 
ATOM   1625  O O   . GLU   A 1 293  ? 87.906  145.274 142.168 1.00 57.72  0  257  GLU   A O   1 
ATOM   1626  C CB  . GLU   A 1 293  ? 89.687  147.781 141.272 1.00 45.69  0  257  GLU   A CB  1 
ATOM   1627  C CG  . GLU   A 1 293  ? 89.631  149.298 141.338 1.00 52.16  0  257  GLU   A CG  1 
ATOM   1628  C CD  . GLU   A 1 293  ? 90.972  149.924 141.675 1.00 59.65  0  257  GLU   A CD  1 
ATOM   1629  O OE1 . GLU   A 1 293  ? 91.930  149.172 141.948 1.00 57.01  0  257  GLU   A OE1 1 
ATOM   1630  O OE2 . GLU   A 1 293  ? 91.070  151.169 141.660 1.00 55.64  -1 257  GLU   A OE2 1 
ATOM   1631  N N   . LEU   A 1 294  ? 90.079  144.745 142.379 1.00 39.54  0  258  LEU   A N   1 
ATOM   1632  C CA  . LEU   A 1 294  ? 89.865  143.320 142.185 1.00 35.13  0  258  LEU   A CA  1 
ATOM   1633  C C   . LEU   A 1 294  ? 89.896  142.529 143.482 1.00 35.70  0  258  LEU   A C   1 
ATOM   1634  O O   . LEU   A 1 294  ? 89.717  141.309 143.444 1.00 44.47  0  258  LEU   A O   1 
ATOM   1635  C CB  . LEU   A 1 294  ? 90.910  142.754 141.220 1.00 35.20  0  258  LEU   A CB  1 
ATOM   1636  C CG  . LEU   A 1 294  ? 90.878  143.306 139.797 1.00 36.75  0  258  LEU   A CG  1 
ATOM   1637  C CD1 . LEU   A 1 294  ? 91.861  142.559 138.923 1.00 37.12  0  258  LEU   A CD1 1 
ATOM   1638  C CD2 . LEU   A 1 294  ? 89.479  143.218 139.224 1.00 37.53  0  258  LEU   A CD2 1 
ATOM   1639  N N   . LYS   A 1 295  ? 90.119  143.184 144.621 1.00 35.28  0  259  LYS   A N   1 
ATOM   1640  C CA  . LYS   A 1 295  ? 90.124  142.519 145.924 1.00 37.80  0  259  LYS   A CA  1 
ATOM   1641  C C   . LYS   A 1 295  ? 91.122  141.363 145.958 1.00 34.99  0  259  LYS   A C   1 
ATOM   1642  O O   . LYS   A 1 295  ? 90.799  140.254 146.386 1.00 32.82  0  259  LYS   A O   1 
ATOM   1643  C CB  . LYS   A 1 295  ? 88.722  142.036 146.302 1.00 36.71  0  259  LYS   A CB  1 
ATOM   1644  C CG  . LYS   A 1 295  ? 87.845  143.099 146.946 1.00 39.56  0  259  LYS   A CG  1 
ATOM   1645  C CD  . LYS   A 1 295  ? 86.370  142.759 146.812 1.00 43.14  0  259  LYS   A CD  1 
ATOM   1646  C CE  . LYS   A 1 295  ? 85.909  142.855 145.368 1.00 44.42  0  259  LYS   A CE  1 
ATOM   1647  N NZ  . LYS   A 1 295  ? 86.115  144.219 144.809 1.00 45.58  1  259  LYS   A NZ  1 
ATOM   1648  N N   . ARG   A 1 296  ? 92.343  141.624 145.503 1.00 29.25  0  260  ARG   A N   1 
ATOM   1649  C CA  . ARG   A 1 296  ? 93.384  140.611 145.433 1.00 29.76  0  260  ARG   A CA  1 
ATOM   1650  C C   . ARG   A 1 296  ? 94.581  141.028 146.279 1.00 25.96  0  260  ARG   A C   1 
ATOM   1651  O O   . ARG   A 1 296  ? 94.807  142.214 146.516 1.00 29.55  0  260  ARG   A O   1 
ATOM   1652  C CB  . ARG   A 1 296  ? 93.820  140.380 143.984 1.00 29.17  0  260  ARG   A CB  1 
ATOM   1653  C CG  . ARG   A 1 296  ? 92.697  140.075 143.020 1.00 30.39  0  260  ARG   A CG  1 
ATOM   1654  C CD  . ARG   A 1 296  ? 92.257  138.628 143.126 1.00 38.25  0  260  ARG   A CD  1 
ATOM   1655  N NE  . ARG   A 1 296  ? 91.472  138.215 141.970 1.00 39.73  0  260  ARG   A NE  1 
ATOM   1656  C CZ  . ARG   A 1 296  ? 90.233  137.752 142.036 1.00 35.23  0  260  ARG   A CZ  1 
ATOM   1657  N NH1 . ARG   A 1 296  ? 89.601  137.637 143.191 1.00 30.97  1  260  ARG   A NH1 1 
ATOM   1658  N NH2 . ARG   A 1 296  ? 89.612  137.397 140.916 1.00 33.64  0  260  ARG   A NH2 1 
ATOM   1659  N N   . ILE   A 1 297  ? 95.342  140.047 146.751 1.00 17.24  0  261  ILE   A N   1 
ATOM   1660  C CA  . ILE   A 1 297  ? 96.513  140.335 147.573 1.00 23.46  0  261  ILE   A CA  1 
ATOM   1661  C C   . ILE   A 1 297  ? 97.529  139.216 147.403 1.00 28.49  0  261  ILE   A C   1 
ATOM   1662  O O   . ILE   A 1 297  ? 97.163  138.043 147.292 1.00 32.35  0  261  ILE   A O   1 
ATOM   1663  C CB  . ILE   A 1 297  ? 96.128  140.521 149.059 1.00 29.50  0  261  ILE   A CB  1 
ATOM   1664  C CG1 . ILE   A 1 297  ? 97.340  140.921 149.897 1.00 20.55  0  261  ILE   A CG1 1 
ATOM   1665  C CG2 . ILE   A 1 297  ? 95.513  139.268 149.625 1.00 35.55  0  261  ILE   A CG2 1 
ATOM   1666  C CD1 . ILE   A 1 297  ? 96.991  141.320 151.306 1.00 19.85  0  261  ILE   A CD1 1 
ATOM   1667  N N   . THR   A 1 298  ? 98.814  139.582 147.390 1.00 28.08  0  262  THR   A N   1 
ATOM   1668  C CA  . THR   A 1 298  ? 99.900  138.613 147.430 1.00 22.97  0  262  THR   A CA  1 
ATOM   1669  C C   . THR   A 1 298  ? 100.974 139.101 148.388 1.00 25.34  0  262  THR   A C   1 
ATOM   1670  O O   . THR   A 1 298  ? 101.086 140.296 148.684 1.00 33.47  0  262  THR   A O   1 
ATOM   1671  C CB  . THR   A 1 298  ? 100.600 138.407 146.093 1.00 20.28  0  262  THR   A CB  1 
ATOM   1672  O OG1 . THR   A 1 298  ? 101.815 137.694 146.329 1.00 29.84  0  262  THR   A OG1 1 
ATOM   1673  C CG2 . THR   A 1 298  ? 101.064 139.736 145.589 1.00 25.24  0  262  THR   A CG2 1 
ATOM   1674  N N   . VAL   A 1 299  ? 101.805 138.158 148.816 1.00 11.28  0  263  VAL   A N   1 
ATOM   1675  C CA  . VAL   A 1 299  ? 102.996 138.440 149.599 1.00 12.29  0  263  VAL   A CA  1 
ATOM   1676  C C   . VAL   A 1 299  ? 104.162 137.753 148.903 1.00 22.59  0  263  VAL   A C   1 
ATOM   1677  O O   . VAL   A 1 299  ? 104.248 136.520 148.899 1.00 40.28  0  263  VAL   A O   1 
ATOM   1678  C CB  . VAL   A 1 299  ? 102.862 137.959 151.046 1.00 19.03  0  263  VAL   A CB  1 
ATOM   1679  C CG1 . VAL   A 1 299  ? 104.192 138.006 151.721 1.00 23.08  0  263  VAL   A CG1 1 
ATOM   1680  C CG2 . VAL   A 1 299  ? 101.876 138.828 151.796 1.00 25.04  0  263  VAL   A CG2 1 
ATOM   1681  N N   . THR   A 1 300  ? 105.059 138.544 148.319 1.00 22.64  0  264  THR   A N   1 
ATOM   1682  C CA  . THR   A 1 300  ? 106.215 138.032 147.599 1.00 20.93  0  264  THR   A CA  1 
ATOM   1683  C C   . THR   A 1 300  ? 107.488 138.654 148.158 1.00 23.15  0  264  THR   A C   1 
ATOM   1684  O O   . THR   A 1 300  ? 107.450 139.295 149.210 1.00 36.44  0  264  THR   A O   1 
ATOM   1685  C CB  . THR   A 1 300  ? 106.072 138.319 146.107 1.00 25.59  0  264  THR   A CB  1 
ATOM   1686  O OG1 . THR   A 1 300  ? 107.208 137.800 145.412 1.00 39.90  0  264  THR   A OG1 1 
ATOM   1687  C CG2 . THR   A 1 300  ? 105.963 139.801 145.861 1.00 19.91  0  264  THR   A CG2 1 
ATOM   1688  N N   . THR   A 1 301  ? 108.617 138.478 147.483 1.00 24.09  0  265  THR   A N   1 
ATOM   1689  C CA  . THR   A 1 301  ? 109.895 138.970 147.976 1.00 21.55  0  265  THR   A CA  1 
ATOM   1690  C C   . THR   A 1 301  ? 110.364 140.177 147.168 1.00 26.39  0  265  THR   A C   1 
ATOM   1691  O O   . THR   A 1 301  ? 109.783 140.542 146.145 1.00 33.37  0  265  THR   A O   1 
ATOM   1692  C CB  . THR   A 1 301  ? 110.941 137.859 147.950 1.00 19.13  0  265  THR   A CB  1 
ATOM   1693  O OG1 . THR   A 1 301  ? 110.965 137.258 146.651 1.00 30.55  0  265  THR   A OG1 1 
ATOM   1694  C CG2 . THR   A 1 301  ? 110.600 136.816 148.974 1.00 22.12  0  265  THR   A CG2 1 
ATOM   1695  N N   . TYR   A 1 302  ? 111.432 140.806 147.663 1.00 25.61  0  266  TYR   A N   1 
ATOM   1696  C CA  . TYR   A 1 302  ? 112.022 141.947 146.972 1.00 25.43  0  266  TYR   A CA  1 
ATOM   1697  C C   . TYR   A 1 302  ? 112.587 141.534 145.622 1.00 22.05  0  266  TYR   A C   1 
ATOM   1698  O O   . TYR   A 1 302  ? 112.493 142.284 144.641 1.00 25.17  0  266  TYR   A O   1 
ATOM   1699  C CB  . TYR   A 1 302  ? 113.106 142.571 147.851 1.00 29.81  0  266  TYR   A CB  1 
ATOM   1700  C CG  . TYR   A 1 302  ? 113.791 143.785 147.262 1.00 32.85  0  266  TYR   A CG  1 
ATOM   1701  C CD1 . TYR   A 1 302  ? 113.068 144.914 146.909 1.00 22.48  0  266  TYR   A CD1 1 
ATOM   1702  C CD2 . TYR   A 1 302  ? 115.164 143.806 147.078 1.00 27.10  0  266  TYR   A CD2 1 
ATOM   1703  C CE1 . TYR   A 1 302  ? 113.691 146.020 146.378 1.00 24.63  0  266  TYR   A CE1 1 
ATOM   1704  C CE2 . TYR   A 1 302  ? 115.793 144.906 146.547 1.00 23.21  0  266  TYR   A CE2 1 
ATOM   1705  C CZ  . TYR   A 1 302  ? 115.053 146.009 146.199 1.00 21.85  0  266  TYR   A CZ  1 
ATOM   1706  O OH  . TYR   A 1 302  ? 115.687 147.107 145.673 1.00 17.40  0  266  TYR   A OH  1 
ATOM   1707  N N   . ASN   A 1 303  ? 113.181 140.340 145.557 1.00 25.60  0  267  ASN   A N   1 
ATOM   1708  C CA  . ASN   A 1 303  ? 113.721 139.834 144.301 1.00 20.68  0  267  ASN   A CA  1 
ATOM   1709  C C   . ASN   A 1 303  ? 112.646 139.727 143.234 1.00 27.33  0  267  ASN   A C   1 
ATOM   1710  O O   . ASN   A 1 303  ? 112.922 139.948 142.052 1.00 32.26  0  267  ASN   A O   1 
ATOM   1711  C CB  . ASN   A 1 303  ? 114.377 138.476 144.529 1.00 26.83  0  267  ASN   A CB  1 
ATOM   1712  C CG  . ASN   A 1 303  ? 115.779 138.594 145.074 1.00 29.16  0  267  ASN   A CG  1 
ATOM   1713  O OD1 . ASN   A 1 303  ? 116.514 139.516 144.732 1.00 28.08  0  267  ASN   A OD1 1 
ATOM   1714  N ND2 . ASN   A 1 303  ? 116.157 137.659 145.936 1.00 29.77  0  267  ASN   A ND2 1 
ATOM   1715  N N   . GLN   A 1 304  ? 111.412 139.409 143.626 1.00 23.99  0  268  GLN   A N   1 
ATOM   1716  C CA  . GLN   A 1 304  ? 110.325 139.372 142.655 1.00 25.96  0  268  GLN   A CA  1 
ATOM   1717  C C   . GLN   A 1 304  ? 109.975 140.762 142.141 1.00 28.77  0  268  GLN   A C   1 
ATOM   1718  O O   . GLN   A 1 304  ? 109.626 140.913 140.967 1.00 31.15  0  268  GLN   A O   1 
ATOM   1719  C CB  . GLN   A 1 304  ? 109.097 138.709 143.264 1.00 18.33  0  268  GLN   A CB  1 
ATOM   1720  C CG  . GLN   A 1 304  ? 107.936 138.552 142.304 1.00 18.47  0  268  GLN   A CG  1 
ATOM   1721  C CD  . GLN   A 1 304  ? 108.193 137.502 141.250 1.00 30.54  0  268  GLN   A CD  1 
ATOM   1722  O OE1 . GLN   A 1 304  ? 108.391 136.330 141.563 1.00 41.07  0  268  GLN   A OE1 1 
ATOM   1723  N NE2 . GLN   A 1 304  ? 108.187 137.914 139.992 1.00 30.71  0  268  GLN   A NE2 1 
ATOM   1724  N N   . PHE   A 1 305  ? 110.050 141.788 142.989 1.00 18.52  0  269  PHE   A N   1 
ATOM   1725  C CA  . PHE   A 1 305  ? 109.829 143.138 142.484 1.00 14.60  0  269  PHE   A CA  1 
ATOM   1726  C C   . PHE   A 1 305  ? 110.941 143.553 141.530 1.00 23.64  0  269  PHE   A C   1 
ATOM   1727  O O   . PHE   A 1 305  ? 110.680 144.181 140.495 1.00 35.81  0  269  PHE   A O   1 
ATOM   1728  C CB  . PHE   A 1 305  ? 109.714 144.141 143.627 1.00 20.19  0  269  PHE   A CB  1 
ATOM   1729  C CG  . PHE   A 1 305  ? 109.346 145.514 143.163 1.00 28.79  0  269  PHE   A CG  1 
ATOM   1730  C CD1 . PHE   A 1 305  ? 108.033 145.826 142.871 1.00 27.47  0  269  PHE   A CD1 1 
ATOM   1731  C CD2 . PHE   A 1 305  ? 110.315 146.478 142.968 1.00 29.44  0  269  PHE   A CD2 1 
ATOM   1732  C CE1 . PHE   A 1 305  ? 107.692 147.078 142.421 1.00 26.61  0  269  PHE   A CE1 1 
ATOM   1733  C CE2 . PHE   A 1 305  ? 109.977 147.731 142.515 1.00 26.20  0  269  PHE   A CE2 1 
ATOM   1734  C CZ  . PHE   A 1 305  ? 108.664 148.030 142.242 1.00 27.26  0  269  PHE   A CZ  1 
ATOM   1735  N N   . LEU   A 1 306  ? 112.188 143.218 141.867 1.00 25.09  0  270  LEU   A N   1 
ATOM   1736  C CA  . LEU   A 1 306  ? 113.284 143.465 140.937 1.00 24.04  0  270  LEU   A CA  1 
ATOM   1737  C C   . LEU   A 1 306  ? 113.042 142.744 139.620 1.00 28.86  0  270  LEU   A C   1 
ATOM   1738  O O   . LEU   A 1 306  ? 113.328 143.282 138.547 1.00 20.97  0  270  LEU   A O   1 
ATOM   1739  C CB  . LEU   A 1 306  ? 114.610 143.016 141.545 1.00 24.76  0  270  LEU   A CB  1 
ATOM   1740  C CG  . LEU   A 1 306  ? 115.053 143.658 142.853 1.00 17.50  0  270  LEU   A CG  1 
ATOM   1741  C CD1 . LEU   A 1 306  ? 116.256 142.926 143.411 1.00 15.23  0  270  LEU   A CD1 1 
ATOM   1742  C CD2 . LEU   A 1 306  ? 115.368 145.112 142.623 1.00 22.26  0  270  LEU   A CD2 1 
ATOM   1743  N N   . THR   A 1 307  ? 112.512 141.522 139.687 1.00 26.05  0  271  THR   A N   1 
ATOM   1744  C CA  . THR   A 1 307  ? 112.226 140.758 138.480 1.00 12.20  0  271  THR   A CA  1 
ATOM   1745  C C   . THR   A 1 307  ? 111.121 141.405 137.658 1.00 20.49  0  271  THR   A C   1 
ATOM   1746  O O   . THR   A 1 307  ? 111.186 141.408 136.428 1.00 31.75  0  271  THR   A O   1 
ATOM   1747  C CB  . THR   A 1 307  ? 111.851 139.328 138.848 1.00 9.65   0  271  THR   A CB  1 
ATOM   1748  O OG1 . THR   A 1 307  ? 112.900 138.753 139.632 1.00 9.60   0  271  THR   A OG1 1 
ATOM   1749  C CG2 . THR   A 1 307  ? 111.657 138.503 137.603 1.00 30.19  0  271  THR   A CG2 1 
ATOM   1750  N N   . TRP   A 1 308  ? 110.089 141.940 138.312 1.00 27.71  0  272  TRP   A N   1 
ATOM   1751  C CA  . TRP   A 1 308  ? 109.045 142.652 137.577 1.00 22.79  0  272  TRP   A CA  1 
ATOM   1752  C C   . TRP   A 1 308  ? 109.611 143.884 136.885 1.00 18.84  0  272  TRP   A C   1 
ATOM   1753  O O   . TRP   A 1 308  ? 109.268 144.176 135.732 1.00 22.72  0  272  TRP   A O   1 
ATOM   1754  C CB  . TRP   A 1 308  ? 107.911 143.059 138.513 1.00 22.64  0  272  TRP   A CB  1 
ATOM   1755  C CG  . TRP   A 1 308  ? 107.079 141.931 138.994 1.00 14.64  0  272  TRP   A CG  1 
ATOM   1756  C CD1 . TRP   A 1 308  ? 107.005 140.686 138.461 1.00 18.68  0  272  TRP   A CD1 1 
ATOM   1757  C CD2 . TRP   A 1 308  ? 106.186 141.947 140.110 1.00 19.88  0  272  TRP   A CD2 1 
ATOM   1758  N NE1 . TRP   A 1 308  ? 106.126 139.916 139.180 1.00 27.61  0  272  TRP   A NE1 1 
ATOM   1759  C CE2 . TRP   A 1 308  ? 105.609 140.670 140.199 1.00 22.52  0  272  TRP   A CE2 1 
ATOM   1760  C CE3 . TRP   A 1 308  ? 105.825 142.915 141.047 1.00 22.88  0  272  TRP   A CE3 1 
ATOM   1761  C CZ2 . TRP   A 1 308  ? 104.688 140.336 141.183 1.00 20.11  0  272  TRP   A CZ2 1 
ATOM   1762  C CZ3 . TRP   A 1 308  ? 104.910 142.584 142.020 1.00 23.46  0  272  TRP   A CZ3 1 
ATOM   1763  C CH2 . TRP   A 1 308  ? 104.353 141.306 142.084 1.00 26.54  0  272  TRP   A CH2 1 
ATOM   1764  N N   . LYS   A 1 309  ? 110.475 144.624 137.579 1.00 17.50  0  273  LYS   A N   1 
ATOM   1765  C CA  . LYS   A 1 309  ? 111.119 145.773 136.952 1.00 21.48  0  273  LYS   A CA  1 
ATOM   1766  C C   . LYS   A 1 309  ? 111.974 145.340 135.769 1.00 24.08  0  273  LYS   A C   1 
ATOM   1767  O O   . LYS   A 1 309  ? 111.982 145.999 134.724 1.00 28.23  0  273  LYS   A O   1 
ATOM   1768  C CB  . LYS   A 1 309  ? 111.965 146.528 137.974 1.00 31.57  0  273  LYS   A CB  1 
ATOM   1769  C CG  . LYS   A 1 309  ? 112.467 147.866 137.473 1.00 32.86  0  273  LYS   A CG  1 
ATOM   1770  C CD  . LYS   A 1 309  ? 113.749 148.270 138.170 1.00 27.97  0  273  LYS   A CD  1 
ATOM   1771  C CE  . LYS   A 1 309  ? 114.965 147.844 137.372 1.00 29.22  0  273  LYS   A CE  1 
ATOM   1772  N NZ  . LYS   A 1 309  ? 115.360 148.876 136.376 1.00 29.77  1  273  LYS   A NZ  1 
ATOM   1773  N N   . ASP   A 1 310  ? 112.698 144.229 135.917 1.00 24.28  0  274  ASP   A N   1 
ATOM   1774  C CA  . ASP   A 1 310  ? 113.521 143.719 134.827 1.00 28.03  0  274  ASP   A CA  1 
ATOM   1775  C C   . ASP   A 1 310  ? 112.665 143.292 133.645 1.00 23.23  0  274  ASP   A C   1 
ATOM   1776  O O   . ASP   A 1 310  ? 113.046 143.501 132.493 1.00 22.51  0  274  ASP   A O   1 
ATOM   1777  C CB  . ASP   A 1 310  ? 114.375 142.550 135.314 1.00 34.04  0  274  ASP   A CB  1 
ATOM   1778  C CG  . ASP   A 1 310  ? 115.350 142.952 136.401 1.00 38.52  0  274  ASP   A CG  1 
ATOM   1779  O OD1 . ASP   A 1 310  ? 115.468 144.164 136.673 1.00 33.07  0  274  ASP   A OD1 1 
ATOM   1780  O OD2 . ASP   A 1 310  ? 115.997 142.058 136.986 1.00 34.45  -1 274  ASP   A OD2 1 
ATOM   1781  N N   . ILE   A 1 311  ? 111.512 142.679 133.911 1.00 24.68  0  275  ILE   A N   1 
ATOM   1782  C CA  . ILE   A 1 311  ? 110.604 142.269 132.843 1.00 16.65  0  275  ILE   A CA  1 
ATOM   1783  C C   . ILE   A 1 311  ? 110.089 143.485 132.089 1.00 18.72  0  275  ILE   A C   1 
ATOM   1784  O O   . ILE   A 1 311  ? 110.052 143.506 130.853 1.00 31.90  0  275  ILE   A O   1 
ATOM   1785  C CB  . ILE   A 1 311  ? 109.439 141.446 133.418 1.00 16.20  0  275  ILE   A CB  1 
ATOM   1786  C CG1 . ILE   A 1 311  ? 109.917 140.096 133.929 1.00 18.21  0  275  ILE   A CG1 1 
ATOM   1787  C CG2 . ILE   A 1 311  ? 108.376 141.243 132.380 1.00 22.37  0  275  ILE   A CG2 1 
ATOM   1788  C CD1 . ILE   A 1 311  ? 108.888 139.411 134.783 1.00 23.14  0  275  ILE   A CD1 1 
ATOM   1789  N N   . SER   A 1 312  ? 109.662 144.513 132.827 1.00 20.40  0  276  SER   A N   1 
ATOM   1790  C CA  . SER   A 1 312  ? 109.173 145.726 132.182 1.00 10.78  0  276  SER   A CA  1 
ATOM   1791  C C   . SER   A 1 312  ? 110.269 146.383 131.363 1.00 22.14  0  276  SER   A C   1 
ATOM   1792  O O   . SER   A 1 312  ? 110.026 146.840 130.241 1.00 35.73  0  276  SER   A O   1 
ATOM   1793  C CB  . SER   A 1 312  ? 108.632 146.698 133.225 1.00 28.37  0  276  SER   A CB  1 
ATOM   1794  O OG  . SER   A 1 312  ? 109.558 146.874 134.281 1.00 30.22  0  276  SER   A OG  1 
ATOM   1795  N N   . LEU   A 1 313  ? 111.489 146.424 131.901 1.00 22.49  0  277  LEU   A N   1 
ATOM   1796  C CA  . LEU   A 1 313  ? 112.614 146.990 131.166 1.00 17.97  0  277  LEU   A CA  1 
ATOM   1797  C C   . LEU   A 1 313  ? 112.932 146.173 129.924 1.00 17.30  0  277  LEU   A C   1 
ATOM   1798  O O   . LEU   A 1 313  ? 113.235 146.737 128.871 1.00 13.80  0  277  LEU   A O   1 
ATOM   1799  C CB  . LEU   A 1 313  ? 113.838 147.077 132.076 1.00 19.76  0  277  LEU   A CB  1 
ATOM   1800  C CG  . LEU   A 1 313  ? 115.186 147.385 131.429 1.00 14.61  0  277  LEU   A CG  1 
ATOM   1801  C CD1 . LEU   A 1 313  ? 115.149 148.719 130.717 1.00 9.52   0  277  LEU   A CD1 1 
ATOM   1802  C CD2 . LEU   A 1 313  ? 116.282 147.361 132.476 1.00 20.50  0  277  LEU   A CD2 1 
ATOM   1803  N N   . SER   A 1 314  ? 112.878 144.844 130.030 1.00 13.02  0  278  SER   A N   1 
ATOM   1804  C CA  . SER   A 1 314  ? 113.184 143.985 128.894 1.00 5.19   0  278  SER   A CA  1 
ATOM   1805  C C   . SER   A 1 314  ? 112.169 144.177 127.781 1.00 10.76  0  278  SER   A C   1 
ATOM   1806  O O   . SER   A 1 314  ? 112.531 144.268 126.605 1.00 40.03  0  278  SER   A O   1 
ATOM   1807  C CB  . SER   A 1 314  ? 113.221 142.526 129.339 1.00 6.29   0  278  SER   A CB  1 
ATOM   1808  O OG  . SER   A 1 314  ? 114.266 142.302 130.265 1.00 8.77   0  278  SER   A OG  1 
ATOM   1809  N N   . ARG   A 1 315  ? 110.887 144.242 128.133 1.00 7.58   0  279  ARG   A N   1 
ATOM   1810  C CA  . ARG   A 1 315  ? 109.867 144.451 127.113 1.00 10.15  0  279  ARG   A CA  1 
ATOM   1811  C C   . ARG   A 1 315  ? 109.948 145.851 126.524 1.00 6.19   0  279  ARG   A C   1 
ATOM   1812  O O   . ARG   A 1 315  ? 109.740 146.028 125.319 1.00 25.24  0  279  ARG   A O   1 
ATOM   1813  C CB  . ARG   A 1 315  ? 108.488 144.174 127.698 1.00 15.35  0  279  ARG   A CB  1 
ATOM   1814  C CG  . ARG   A 1 315  ? 108.368 142.762 128.220 1.00 13.06  0  279  ARG   A CG  1 
ATOM   1815  C CD  . ARG   A 1 315  ? 107.016 142.472 128.811 1.00 7.33   0  279  ARG   A CD  1 
ATOM   1816  N NE  . ARG   A 1 315  ? 107.005 141.160 129.440 1.00 6.59   0  279  ARG   A NE  1 
ATOM   1817  C CZ  . ARG   A 1 315  ? 105.908 140.496 129.768 1.00 12.52  0  279  ARG   A CZ  1 
ATOM   1818  N NH1 . ARG   A 1 315  ? 104.706 140.988 129.525 1.00 17.20  1  279  ARG   A NH1 1 
ATOM   1819  N NH2 . ARG   A 1 315  ? 106.020 139.309 130.353 1.00 14.79  0  279  ARG   A NH2 1 
ATOM   1820  N N   . LEU   A 1 316  ? 110.277 146.850 127.346 1.00 3.99   0  280  LEU   A N   1 
ATOM   1821  C CA  . LEU   A 1 316  ? 110.501 148.191 126.825 1.00 9.50   0  280  LEU   A CA  1 
ATOM   1822  C C   . LEU   A 1 316  ? 111.671 148.212 125.856 1.00 23.41  0  280  LEU   A C   1 
ATOM   1823  O O   . LEU   A 1 316  ? 111.613 148.875 124.819 1.00 29.69  0  280  LEU   A O   1 
ATOM   1824  C CB  . LEU   A 1 316  ? 110.746 149.165 127.975 1.00 12.16  0  280  LEU   A CB  1 
ATOM   1825  C CG  . LEU   A 1 316  ? 111.525 150.437 127.643 1.00 8.58   0  280  LEU   A CG  1 
ATOM   1826  C CD1 . LEU   A 1 316  ? 110.708 151.376 126.772 1.00 8.59   0  280  LEU   A CD1 1 
ATOM   1827  C CD2 . LEU   A 1 316  ? 111.969 151.126 128.917 1.00 7.32   0  280  LEU   A CD2 1 
ATOM   1828  N N   . ASN   A 1 317  ? 112.747 147.496 126.181 1.00 25.51  0  281  ASN   A N   1 
ATOM   1829  C CA  . ASN   A 1 317  ? 113.909 147.446 125.302 1.00 10.82  0  281  ASN   A CA  1 
ATOM   1830  C C   . ASN   A 1 317  ? 113.585 146.733 124.001 1.00 13.62  0  281  ASN   A C   1 
ATOM   1831  O O   . ASN   A 1 317  ? 114.011 147.169 122.929 1.00 25.65  0  281  ASN   A O   1 
ATOM   1832  C CB  . ASN   A 1 317  ? 115.069 146.757 126.009 1.00 0.00   0  281  ASN   A CB  1 
ATOM   1833  C CG  . ASN   A 1 317  ? 115.876 147.705 126.847 1.00 12.38  0  281  ASN   A CG  1 
ATOM   1834  O OD1 . ASN   A 1 317  ? 115.959 148.894 126.549 1.00 17.25  0  281  ASN   A OD1 1 
ATOM   1835  N ND2 . ASN   A 1 317  ? 116.478 147.190 127.907 1.00 13.88  0  281  ASN   A ND2 1 
ATOM   1836  N N   . VAL   A 1 318  ? 112.843 145.628 124.076 1.00 12.50  0  282  VAL   A N   1 
ATOM   1837  C CA  . VAL   A 1 318  ? 112.453 144.917 122.865 1.00 5.30   0  282  VAL   A CA  1 
ATOM   1838  C C   . VAL   A 1 318  ? 111.616 145.819 121.975 1.00 14.64  0  282  VAL   A C   1 
ATOM   1839  O O   . VAL   A 1 318  ? 111.839 145.899 120.764 1.00 32.66  0  282  VAL   A O   1 
ATOM   1840  C CB  . VAL   A 1 318  ? 111.704 143.620 123.216 1.00 8.60   0  282  VAL   A CB  1 
ATOM   1841  C CG1 . VAL   A 1 318  ? 111.087 143.020 121.973 1.00 25.21  0  282  VAL   A CG1 1 
ATOM   1842  C CG2 . VAL   A 1 318  ? 112.637 142.637 123.862 1.00 0.00   0  282  VAL   A CG2 1 
ATOM   1843  N N   . CYS   A 1 319  ? 110.651 146.529 122.561 1.00 11.77  0  283  CYS   A N   1 
ATOM   1844  C CA  . CYS   A 1 319  ? 109.828 147.426 121.761 1.00 9.71   0  283  CYS   A CA  1 
ATOM   1845  C C   . CYS   A 1 319  ? 110.629 148.604 121.224 1.00 19.00  0  283  CYS   A C   1 
ATOM   1846  O O   . CYS   A 1 319  ? 110.399 149.033 120.091 1.00 35.98  0  283  CYS   A O   1 
ATOM   1847  C CB  . CYS   A 1 319  ? 108.634 147.908 122.576 1.00 30.01  0  283  CYS   A CB  1 
ATOM   1848  S SG  . CYS   A 1 319  ? 107.325 146.672 122.716 1.00 58.37  0  283  CYS   A SG  1 
ATOM   1849  N N   . LEU   A 1 320  ? 111.576 149.132 122.003 1.00 11.35  0  284  LEU   A N   1 
ATOM   1850  C CA  . LEU   A 1 320  ? 112.418 150.221 121.519 1.00 15.69  0  284  LEU   A CA  1 
ATOM   1851  C C   . LEU   A 1 320  ? 113.251 149.779 120.329 1.00 17.64  0  284  LEU   A C   1 
ATOM   1852  O O   . LEU   A 1 320  ? 113.297 150.461 119.301 1.00 26.44  0  284  LEU   A O   1 
ATOM   1853  C CB  . LEU   A 1 320  ? 113.330 150.725 122.637 1.00 15.71  0  284  LEU   A CB  1 
ATOM   1854  C CG  . LEU   A 1 320  ? 112.877 151.924 123.462 1.00 18.74  0  284  LEU   A CG  1 
ATOM   1855  C CD1 . LEU   A 1 320  ? 113.778 152.095 124.661 1.00 13.02  0  284  LEU   A CD1 1 
ATOM   1856  C CD2 . LEU   A 1 320  ? 112.881 153.176 122.611 1.00 13.00  0  284  LEU   A CD2 1 
ATOM   1857  N N   . ILE   A 1 321  ? 113.925 148.637 120.456 1.00 24.74  0  285  ILE   A N   1 
ATOM   1858  C CA  . ILE   A 1 321  ? 114.751 148.128 119.368 1.00 20.27  0  285  ILE   A CA  1 
ATOM   1859  C C   . ILE   A 1 321  ? 113.891 147.850 118.146 1.00 21.70  0  285  ILE   A C   1 
ATOM   1860  O O   . ILE   A 1 321  ? 114.262 148.181 117.017 1.00 29.14  0  285  ILE   A O   1 
ATOM   1861  C CB  . ILE   A 1 321  ? 115.511 146.868 119.814 1.00 2.40   0  285  ILE   A CB  1 
ATOM   1862  C CG1 . ILE   A 1 321  ? 116.421 147.180 120.991 1.00 4.43   0  285  ILE   A CG1 1 
ATOM   1863  C CG2 . ILE   A 1 321  ? 116.330 146.325 118.681 1.00 9.82   0  285  ILE   A CG2 1 
ATOM   1864  C CD1 . ILE   A 1 321  ? 116.765 145.973 121.796 1.00 0.00   0  285  ILE   A CD1 1 
ATOM   1865  N N   . THR   A 1 322  ? 112.724 147.240 118.358 1.00 8.01   0  286  THR   A N   1 
ATOM   1866  C CA  . THR   A 1 322  ? 111.843 146.912 117.248 1.00 0.00   0  286  THR   A CA  1 
ATOM   1867  C C   . THR   A 1 322  ? 111.369 148.168 116.532 1.00 11.40  0  286  THR   A C   1 
ATOM   1868  O O   . THR   A 1 322  ? 111.371 148.223 115.300 1.00 21.84  0  286  THR   A O   1 
ATOM   1869  C CB  . THR   A 1 322  ? 110.659 146.097 117.765 1.00 12.27  0  286  THR   A CB  1 
ATOM   1870  O OG1 . THR   A 1 322  ? 111.053 144.729 117.908 1.00 24.36  0  286  THR   A OG1 1 
ATOM   1871  C CG2 . THR   A 1 322  ? 109.484 146.180 116.811 1.00 30.20  0  286  THR   A CG2 1 
ATOM   1872  N N   . TRP   A 1 323  ? 110.981 149.196 117.287 1.00 15.25  0  287  TRP   A N   1 
ATOM   1873  C CA  . TRP   A 1 323  ? 110.492 150.428 116.680 1.00 11.38  0  287  TRP   A CA  1 
ATOM   1874  C C   . TRP   A 1 323  ? 111.605 151.170 115.952 1.00 26.50  0  287  TRP   A C   1 
ATOM   1875  O O   . TRP   A 1 323  ? 111.404 151.662 114.834 1.00 34.16  0  287  TRP   A O   1 
ATOM   1876  C CB  . TRP   A 1 323  ? 109.859 151.305 117.756 1.00 9.54   0  287  TRP   A CB  1 
ATOM   1877  C CG  . TRP   A 1 323  ? 109.318 152.591 117.260 1.00 22.31  0  287  TRP   A CG  1 
ATOM   1878  C CD1 . TRP   A 1 323  ? 108.521 152.783 116.173 1.00 23.91  0  287  TRP   A CD1 1 
ATOM   1879  C CD2 . TRP   A 1 323  ? 109.515 153.878 117.846 1.00 22.17  0  287  TRP   A CD2 1 
ATOM   1880  N NE1 . TRP   A 1 323  ? 108.216 154.115 116.039 1.00 17.25  0  287  TRP   A NE1 1 
ATOM   1881  C CE2 . TRP   A 1 323  ? 108.816 154.809 117.056 1.00 24.46  0  287  TRP   A CE2 1 
ATOM   1882  C CE3 . TRP   A 1 323  ? 110.223 154.336 118.958 1.00 15.21  0  287  TRP   A CE3 1 
ATOM   1883  C CZ2 . TRP   A 1 323  ? 108.803 156.166 117.344 1.00 27.59  0  287  TRP   A CZ2 1 
ATOM   1884  C CZ3 . TRP   A 1 323  ? 110.205 155.679 119.243 1.00 27.72  0  287  TRP   A CZ3 1 
ATOM   1885  C CH2 . TRP   A 1 323  ? 109.503 156.581 118.440 1.00 28.44  0  287  TRP   A CH2 1 
ATOM   1886  N N   . ILE   A 1 324  ? 112.790 151.250 116.562 1.00 33.34  0  288  ILE   A N   1 
ATOM   1887  C CA  . ILE   A 1 324  ? 113.926 151.896 115.911 1.00 24.86  0  288  ILE   A CA  1 
ATOM   1888  C C   . ILE   A 1 324  ? 114.270 151.171 114.619 1.00 33.60  0  288  ILE   A C   1 
ATOM   1889  O O   . ILE   A 1 324  ? 114.465 151.792 113.567 1.00 30.97  0  288  ILE   A O   1 
ATOM   1890  C CB  . ILE   A 1 324  ? 115.137 151.940 116.862 1.00 20.61  0  288  ILE   A CB  1 
ATOM   1891  C CG1 . ILE   A 1 324  ? 114.863 152.844 118.061 1.00 10.08  0  288  ILE   A CG1 1 
ATOM   1892  C CG2 . ILE   A 1 324  ? 116.372 152.415 116.129 1.00 25.55  0  288  ILE   A CG2 1 
ATOM   1893  C CD1 . ILE   A 1 324  ? 115.825 152.638 119.195 1.00 21.33  0  288  ILE   A CD1 1 
ATOM   1894  N N   . SER   A 1 325  ? 114.343 149.840 114.682 1.00 27.65  0  289  SER   A N   1 
ATOM   1895  C CA  . SER   A 1 325  ? 114.703 149.052 113.515 1.00 14.50  0  289  SER   A CA  1 
ATOM   1896  C C   . SER   A 1 325  ? 113.654 149.169 112.423 1.00 19.13  0  289  SER   A C   1 
ATOM   1897  O O   . SER   A 1 325  ? 113.995 149.245 111.241 1.00 41.95  0  289  SER   A O   1 
ATOM   1898  C CB  . SER   A 1 325  ? 114.900 147.595 113.921 1.00 22.40  0  289  SER   A CB  1 
ATOM   1899  O OG  . SER   A 1 325  ? 115.179 146.787 112.796 1.00 34.09  0  289  SER   A OG  1 
ATOM   1900  N N   . ASN   A 1 326  ? 112.373 149.178 112.791 1.00 13.73  0  290  ASN   A N   1 
ATOM   1901  C CA  . ASN   A 1 326  ? 111.327 149.302 111.783 1.00 28.35  0  290  ASN   A CA  1 
ATOM   1902  C C   . ASN   A 1 326  ? 111.365 150.670 111.118 1.00 27.19  0  290  ASN   A C   1 
ATOM   1903  O O   . ASN   A 1 326  ? 111.199 150.773 109.899 1.00 37.76  0  290  ASN   A O   1 
ATOM   1904  C CB  . ASN   A 1 326  ? 109.956 149.042 112.404 1.00 28.27  0  290  ASN   A CB  1 
ATOM   1905  C CG  . ASN   A 1 326  ? 109.796 147.611 112.882 1.00 31.96  0  290  ASN   A CG  1 
ATOM   1906  O OD1 . ASN   A 1 326  ? 110.602 146.741 112.560 1.00 32.63  0  290  ASN   A OD1 1 
ATOM   1907  N ND2 . ASN   A 1 326  ? 108.752 147.364 113.662 1.00 33.10  0  290  ASN   A ND2 1 
ATOM   1908  N N   . CYS   A 1 327  ? 111.593 151.731 111.897 1.00 17.97  0  291  CYS   A N   1 
ATOM   1909  C CA  . CYS   A 1 327  ? 111.719 153.058 111.303 1.00 11.75  0  291  CYS   A CA  1 
ATOM   1910  C C   . CYS   A 1 327  ? 112.921 153.131 110.371 1.00 28.80  0  291  CYS   A C   1 
ATOM   1911  O O   . CYS   A 1 327  ? 112.828 153.677 109.265 1.00 40.23  0  291  CYS   A O   1 
ATOM   1912  C CB  . CYS   A 1 327  ? 111.824 154.115 112.398 1.00 16.75  0  291  CYS   A CB  1 
ATOM   1913  S SG  . CYS   A 1 327  ? 110.339 154.301 113.399 1.00 37.41  0  291  CYS   A SG  1 
ATOM   1914  N N   . LEU   A 1 328  ? 114.058 152.573 110.794 1.00 33.29  0  292  LEU   A N   1 
ATOM   1915  C CA  . LEU   A 1 328  ? 115.252 152.585 109.955 1.00 27.75  0  292  LEU   A CA  1 
ATOM   1916  C C   . LEU   A 1 328  ? 115.030 151.797 108.670 1.00 27.20  0  292  LEU   A C   1 
ATOM   1917  O O   . LEU   A 1 328  ? 115.386 152.253 107.579 1.00 33.73  0  292  LEU   A O   1 
ATOM   1918  C CB  . LEU   A 1 328  ? 116.440 152.019 110.734 1.00 25.03  0  292  LEU   A CB  1 
ATOM   1919  C CG  . LEU   A 1 328  ? 117.010 152.865 111.875 1.00 25.57  0  292  LEU   A CG  1 
ATOM   1920  C CD1 . LEU   A 1 328  ? 117.956 152.048 112.730 1.00 15.16  0  292  LEU   A CD1 1 
ATOM   1921  C CD2 . LEU   A 1 328  ? 117.715 154.085 111.326 1.00 25.95  0  292  LEU   A CD2 1 
ATOM   1922  N N   . ASN   A 1 329  ? 114.433 150.608 108.781 1.00 17.27  0  293  ASN   A N   1 
ATOM   1923  C CA  . ASN   A 1 329  ? 114.199 149.770 107.612 1.00 9.09   0  293  ASN   A CA  1 
ATOM   1924  C C   . ASN   A 1 329  ? 113.217 150.422 106.651 1.00 20.89  0  293  ASN   A C   1 
ATOM   1925  O O   . ASN   A 1 329  ? 113.399 150.357 105.431 1.00 34.58  0  293  ASN   A O   1 
ATOM   1926  C CB  . ASN   A 1 329  ? 113.695 148.398 108.049 1.00 15.69  0  293  ASN   A CB  1 
ATOM   1927  C CG  . ASN   A 1 329  ? 114.774 147.569 108.698 1.00 20.86  0  293  ASN   A CG  1 
ATOM   1928  O OD1 . ASN   A 1 329  ? 115.945 147.925 108.658 1.00 16.11  0  293  ASN   A OD1 1 
ATOM   1929  N ND2 . ASN   A 1 329  ? 114.387 146.452 109.296 1.00 22.72  0  293  ASN   A ND2 1 
ATOM   1930  N N   . THR   A 1 330  ? 112.160 151.044 107.177 1.00 26.53  0  294  THR   A N   1 
ATOM   1931  C CA  . THR   A 1 330  ? 111.277 151.825 106.322 1.00 26.81  0  294  THR   A CA  1 
ATOM   1932  C C   . THR   A 1 330  ? 112.038 152.952 105.648 1.00 20.24  0  294  THR   A C   1 
ATOM   1933  O O   . THR   A 1 330  ? 111.744 153.308 104.502 1.00 34.60  0  294  THR   A O   1 
ATOM   1934  C CB  . THR   A 1 330  ? 110.113 152.383 107.140 1.00 29.09  0  294  THR   A CB  1 
ATOM   1935  O OG1 . THR   A 1 330  ? 109.414 151.306 107.772 1.00 38.85  0  294  THR   A OG1 1 
ATOM   1936  C CG2 . THR   A 1 330  ? 109.152 153.144 106.249 1.00 31.26  0  294  THR   A CG2 1 
ATOM   1937  N N   . LEU   A 1 331  ? 113.022 153.518 106.341 1.00 16.85  0  295  LEU   A N   1 
ATOM   1938  C CA  . LEU   A 1 331  ? 113.878 154.530 105.740 1.00 28.51  0  295  LEU   A CA  1 
ATOM   1939  C C   . LEU   A 1 331  ? 114.881 153.922 104.766 1.00 38.55  0  295  LEU   A C   1 
ATOM   1940  O O   . LEU   A 1 331  ? 115.116 154.473 103.685 1.00 37.17  0  295  LEU   A O   1 
ATOM   1941  C CB  . LEU   A 1 331  ? 114.587 155.304 106.844 1.00 28.33  0  295  LEU   A CB  1 
ATOM   1942  C CG  . LEU   A 1 331  ? 115.368 156.523 106.397 1.00 34.37  0  295  LEU   A CG  1 
ATOM   1943  C CD1 . LEU   A 1 331  ? 114.407 157.663 106.241 1.00 39.62  0  295  LEU   A CD1 1 
ATOM   1944  C CD2 . LEU   A 1 331  ? 116.394 156.843 107.458 1.00 37.76  0  295  LEU   A CD2 1 
ATOM   1945  N N   . ASN   A 1 332  ? 115.476 152.787 105.131 1.00 47.28  0  296  ASN   A N   1 
ATOM   1946  C CA  . ASN   A 1 332  ? 116.451 152.095 104.297 1.00 26.79  0  296  ASN   A CA  1 
ATOM   1947  C C   . ASN   A 1 332  ? 116.593 150.657 104.770 1.00 23.93  0  296  ASN   A C   1 
ATOM   1948  O O   . ASN   A 1 332  ? 116.882 150.415 105.944 1.00 32.45  0  296  ASN   A O   1 
ATOM   1949  C CB  . ASN   A 1 332  ? 117.800 152.806 104.343 1.00 22.12  0  296  ASN   A CB  1 
ATOM   1950  C CG  . ASN   A 1 332  ? 118.848 152.112 103.511 1.00 33.39  0  296  ASN   A CG  1 
ATOM   1951  O OD1 . ASN   A 1 332  ? 118.533 151.280 102.665 1.00 39.28  0  296  ASN   A OD1 1 
ATOM   1952  N ND2 . ASN   A 1 332  ? 120.107 152.446 103.752 1.00 40.08  0  296  ASN   A ND2 1 
ATOM   1953  N N   . LYS   A 1 333  ? 116.420 149.697 103.864 1.00 19.40  0  297  LYS   A N   1 
ATOM   1954  C CA  . LYS   A 1 333  ? 116.344 148.294 104.257 1.00 28.19  0  297  LYS   A CA  1 
ATOM   1955  C C   . LYS   A 1 333  ? 117.652 147.748 104.808 1.00 28.65  0  297  LYS   A C   1 
ATOM   1956  O O   . LYS   A 1 333  ? 117.652 146.645 105.363 1.00 17.34  0  297  LYS   A O   1 
ATOM   1957  C CB  . LYS   A 1 333  ? 115.890 147.448 103.069 1.00 29.09  0  297  LYS   A CB  1 
ATOM   1958  C CG  . LYS   A 1 333  ? 114.667 147.999 102.358 1.00 30.83  0  297  LYS   A CG  1 
ATOM   1959  C CD  . LYS   A 1 333  ? 113.395 147.626 103.097 1.00 33.13  0  297  LYS   A CD  1 
ATOM   1960  C CE  . LYS   A 1 333  ? 112.213 147.548 102.152 1.00 30.62  0  297  LYS   A CE  1 
ATOM   1961  N NZ  . LYS   A 1 333  ? 112.483 146.626 101.018 1.00 31.77  1  297  LYS   A NZ  1 
ATOM   1962  N N   . SER   A 1 334  ? 118.758 148.479 104.670 1.00 31.26  0  298  SER   A N   1 
ATOM   1963  C CA  . SER   A 1 334  ? 120.044 148.034 105.185 1.00 27.97  0  298  SER   A CA  1 
ATOM   1964  C C   . SER   A 1 334  ? 120.398 148.640 106.534 1.00 31.27  0  298  SER   A C   1 
ATOM   1965  O O   . SER   A 1 334  ? 121.233 148.072 107.244 1.00 32.31  0  298  SER   A O   1 
ATOM   1966  C CB  . SER   A 1 334  ? 121.157 148.370 104.185 1.00 28.18  0  298  SER   A CB  1 
ATOM   1967  O OG  . SER   A 1 334  ? 120.917 147.766 102.928 1.00 37.34  0  298  SER   A OG  1 
ATOM   1968  N N   . LEU   A 1 335  ? 119.786 149.769 106.903 1.00 25.97  0  299  LEU   A N   1 
ATOM   1969  C CA  . LEU   A 1 335  ? 120.183 150.473 108.119 1.00 23.17  0  299  LEU   A CA  1 
ATOM   1970  C C   . LEU   A 1 335  ? 119.863 149.665 109.367 1.00 24.35  0  299  LEU   A C   1 
ATOM   1971  O O   . LEU   A 1 335  ? 120.727 149.457 110.226 1.00 32.36  0  299  LEU   A O   1 
ATOM   1972  C CB  . LEU   A 1 335  ? 119.498 151.835 108.182 1.00 18.83  0  299  LEU   A CB  1 
ATOM   1973  C CG  . LEU   A 1 335  ? 120.232 152.998 107.528 1.00 27.58  0  299  LEU   A CG  1 
ATOM   1974  C CD1 . LEU   A 1 335  ? 119.316 154.188 107.383 1.00 27.58  0  299  LEU   A CD1 1 
ATOM   1975  C CD2 . LEU   A 1 335  ? 121.431 153.358 108.372 1.00 30.78  0  299  LEU   A CD2 1 
ATOM   1976  N N   . GLY   A 1 336  ? 118.630 149.196 109.485 1.00 19.32  0  300  GLY   A N   1 
ATOM   1977  C CA  . GLY   A 1 336  ? 118.199 148.535 110.693 1.00 20.80  0  300  GLY   A CA  1 
ATOM   1978  C C   . GLY   A 1 336  ? 118.739 147.127 110.791 1.00 21.61  0  300  GLY   A C   1 
ATOM   1979  O O   . GLY   A 1 336  ? 119.569 146.676 110.002 1.00 35.85  0  300  GLY   A O   1 
ATOM   1980  N N   . LEU   A 1 337  ? 118.257 146.417 111.803 1.00 21.78  0  301  LEU   A N   1 
ATOM   1981  C CA  . LEU   A 1 337  ? 118.662 145.039 111.987 1.00 26.19  0  301  LEU   A CA  1 
ATOM   1982  C C   . LEU   A 1 337  ? 118.095 144.172 110.866 1.00 26.84  0  301  LEU   A C   1 
ATOM   1983  O O   . LEU   A 1 337  ? 117.206 144.575 110.113 1.00 22.60  0  301  LEU   A O   1 
ATOM   1984  C CB  . LEU   A 1 337  ? 118.195 144.521 113.343 1.00 38.98  0  301  LEU   A CB  1 
ATOM   1985  C CG  . LEU   A 1 337  ? 118.528 145.377 114.558 1.00 32.05  0  301  LEU   A CG  1 
ATOM   1986  C CD1 . LEU   A 1 337  ? 117.737 144.889 115.742 1.00 24.20  0  301  LEU   A CD1 1 
ATOM   1987  C CD2 . LEU   A 1 337  ? 120.006 145.317 114.847 1.00 34.80  0  301  LEU   A CD2 1 
ATOM   1988  N N   . ARG   A 1 338  ? 118.637 142.960 110.759 1.00 27.06  0  302  ARG   A N   1 
ATOM   1989  C CA  . ARG   A 1 338  ? 118.183 142.044 109.720 1.00 31.36  0  302  ARG   A CA  1 
ATOM   1990  C C   . ARG   A 1 338  ? 116.766 141.558 109.991 1.00 30.34  0  302  ARG   A C   1 
ATOM   1991  O O   . ARG   A 1 338  ? 115.991 141.337 109.054 1.00 32.94  0  302  ARG   A O   1 
ATOM   1992  C CB  . ARG   A 1 338  ? 119.148 140.867 109.609 1.00 38.40  0  302  ARG   A CB  1 
ATOM   1993  C CG  . ARG   A 1 338  ? 120.387 141.166 108.784 1.00 34.48  0  302  ARG   A CG  1 
ATOM   1994  C CD  . ARG   A 1 338  ? 121.008 139.896 108.247 1.00 33.09  0  302  ARG   A CD  1 
ATOM   1995  N NE  . ARG   A 1 338  ? 121.817 139.222 109.252 1.00 32.29  0  302  ARG   A NE  1 
ATOM   1996  C CZ  . ARG   A 1 338  ? 122.165 137.945 109.194 1.00 33.06  0  302  ARG   A CZ  1 
ATOM   1997  N NH1 . ARG   A 1 338  ? 121.797 137.175 108.185 1.00 30.25  1  302  ARG   A NH1 1 
ATOM   1998  N NH2 . ARG   A 1 338  ? 122.904 137.429 110.170 1.00 38.03  0  302  ARG   A NH2 1 
ATOM   1999  N N   . CYS   A 1 339  ? 116.409 141.385 111.260 1.00 24.81  0  303  CYS   A N   1 
ATOM   2000  C CA  . CYS   A 1 339  ? 115.088 140.879 111.603 1.00 23.36  0  303  CYS   A CA  1 
ATOM   2001  C C   . CYS   A 1 339  ? 114.038 141.972 111.457 1.00 28.34  0  303  CYS   A C   1 
ATOM   2002  O O   . CYS   A 1 339  ? 114.237 143.105 111.905 1.00 38.93  0  303  CYS   A O   1 
ATOM   2003  C CB  . CYS   A 1 339  ? 115.088 140.327 113.026 1.00 21.40  0  303  CYS   A CB  1 
ATOM   2004  S SG  . CYS   A 1 339  ? 115.323 141.553 114.326 1.00 37.15  0  303  CYS   A SG  1 
ATOM   2005  N N   . GLY   A 1 340  ? 112.921 141.633 110.820 1.00 18.50  0  304  GLY   A N   1 
ATOM   2006  C CA  . GLY   A 1 340  ? 111.807 142.554 110.706 1.00 27.77  0  304  GLY   A CA  1 
ATOM   2007  C C   . GLY   A 1 340  ? 110.615 142.090 111.514 1.00 37.11  0  304  GLY   A C   1 
ATOM   2008  O O   . GLY   A 1 340  ? 109.940 141.129 111.135 1.00 31.96  0  304  GLY   A O   1 
ATOM   2009  N N   . PHE   A 1 341  ? 110.341 142.769 112.622 1.00 41.97  0  305  PHE   A N   1 
ATOM   2010  C CA  . PHE   A 1 341  ? 109.335 142.340 113.581 1.00 30.64  0  305  PHE   A CA  1 
ATOM   2011  C C   . PHE   A 1 341  ? 108.068 143.182 113.468 1.00 34.32  0  305  PHE   A C   1 
ATOM   2012  O O   . PHE   A 1 341  ? 108.008 144.179 112.746 1.00 30.62  0  305  PHE   A O   1 
ATOM   2013  C CB  . PHE   A 1 341  ? 109.889 142.416 115.004 1.00 15.17  0  305  PHE   A CB  1 
ATOM   2014  C CG  . PHE   A 1 341  ? 110.430 141.119 115.515 1.00 14.17  0  305  PHE   A CG  1 
ATOM   2015  C CD1 . PHE   A 1 341  ? 109.587 140.061 115.780 1.00 19.30  0  305  PHE   A CD1 1 
ATOM   2016  C CD2 . PHE   A 1 341  ? 111.780 140.964 115.751 1.00 28.41  0  305  PHE   A CD2 1 
ATOM   2017  C CE1 . PHE   A 1 341  ? 110.082 138.869 116.259 1.00 30.44  0  305  PHE   A CE1 1 
ATOM   2018  C CE2 . PHE   A 1 341  ? 112.280 139.774 116.232 1.00 32.87  0  305  PHE   A CE2 1 
ATOM   2019  C CZ  . PHE   A 1 341  ? 111.430 138.726 116.485 1.00 23.30  0  305  PHE   A CZ  1 
ATOM   2020  N N   . ASN   A 1 342  ? 107.042 142.755 114.201 1.00 48.43  0  306  ASN   A N   1 
ATOM   2021  C CA  . ASN   A 1 342  ? 105.767 143.457 114.273 1.00 46.36  0  306  ASN   A CA  1 
ATOM   2022  C C   . ASN   A 1 342  ? 105.456 143.724 115.736 1.00 45.90  0  306  ASN   A C   1 
ATOM   2023  O O   . ASN   A 1 342  ? 105.413 142.789 116.541 1.00 50.42  0  306  ASN   A O   1 
ATOM   2024  C CB  . ASN   A 1 342  ? 104.648 142.642 113.621 1.00 39.56  0  306  ASN   A CB  1 
ATOM   2025  C CG  . ASN   A 1 342  ? 103.440 143.484 113.277 1.00 47.24  0  306  ASN   A CG  1 
ATOM   2026  O OD1 . ASN   A 1 342  ? 103.430 144.693 113.497 1.00 52.45  0  306  ASN   A OD1 1 
ATOM   2027  N ND2 . ASN   A 1 342  ? 102.413 142.848 112.731 1.00 46.18  0  306  ASN   A ND2 1 
ATOM   2028  N N   . ASN   A 1 343  ? 105.240 144.996 116.077 1.00 43.23  0  307  ASN   A N   1 
ATOM   2029  C CA  . ASN   A 1 343  ? 105.061 145.370 117.477 1.00 46.84  0  307  ASN   A CA  1 
ATOM   2030  C C   . ASN   A 1 343  ? 103.780 144.785 118.058 1.00 50.58  0  307  ASN   A C   1 
ATOM   2031  O O   . ASN   A 1 343  ? 103.767 144.322 119.205 1.00 51.84  0  307  ASN   A O   1 
ATOM   2032  C CB  . ASN   A 1 343  ? 105.069 146.894 117.610 1.00 59.23  0  307  ASN   A CB  1 
ATOM   2033  C CG  . ASN   A 1 343  ? 104.172 147.578 116.588 1.00 62.43  0  307  ASN   A CG  1 
ATOM   2034  O OD1 . ASN   A 1 343  ? 104.180 147.232 115.406 1.00 58.46  0  307  ASN   A OD1 1 
ATOM   2035  N ND2 . ASN   A 1 343  ? 103.399 148.563 117.041 1.00 51.01  0  307  ASN   A ND2 1 
ATOM   2036  N N   . VAL   A 1 344  ? 102.692 144.804 117.286 1.00 44.25  0  308  VAL   A N   1 
ATOM   2037  C CA  . VAL   A 1 344  ? 101.408 144.317 117.786 1.00 41.71  0  308  VAL   A CA  1 
ATOM   2038  C C   . VAL   A 1 344  ? 101.494 142.832 118.111 1.00 41.83  0  308  VAL   A C   1 
ATOM   2039  O O   . VAL   A 1 344  ? 101.034 142.378 119.168 1.00 47.16  0  308  VAL   A O   1 
ATOM   2040  C CB  . VAL   A 1 344  ? 100.297 144.604 116.762 1.00 41.72  0  308  VAL   A CB  1 
ATOM   2041  C CG1 . VAL   A 1 344  ? 99.000  143.947 117.189 1.00 43.33  0  308  VAL   A CG1 1 
ATOM   2042  C CG2 . VAL   A 1 344  ? 100.115 146.100 116.587 1.00 43.01  0  308  VAL   A CG2 1 
ATOM   2043  N N   . ILE   A 1 345  ? 102.090 142.055 117.207 1.00 37.49  0  309  ILE   A N   1 
ATOM   2044  C CA  . ILE   A 1 345  ? 102.219 140.621 117.436 1.00 39.48  0  309  ILE   A CA  1 
ATOM   2045  C C   . ILE   A 1 345  ? 103.053 140.358 118.678 1.00 35.56  0  309  ILE   A C   1 
ATOM   2046  O O   . ILE   A 1 345  ? 102.699 139.515 119.506 1.00 40.57  0  309  ILE   A O   1 
ATOM   2047  C CB  . ILE   A 1 345  ? 102.813 139.926 116.198 1.00 41.48  0  309  ILE   A CB  1 
ATOM   2048  C CG1 . ILE   A 1 345  ? 102.036 140.319 114.946 1.00 45.53  0  309  ILE   A CG1 1 
ATOM   2049  C CG2 . ILE   A 1 345  ? 102.786 138.426 116.374 1.00 34.73  0  309  ILE   A CG2 1 
ATOM   2050  C CD1 . ILE   A 1 345  ? 100.605 139.846 114.950 1.00 43.84  0  309  ILE   A CD1 1 
ATOM   2051  N N   . LEU   A 1 346  ? 104.162 141.083 118.838 1.00 27.84  0  310  LEU   A N   1 
ATOM   2052  C CA  . LEU   A 1 346  ? 105.011 140.885 120.007 1.00 27.71  0  310  LEU   A CA  1 
ATOM   2053  C C   . LEU   A 1 346  ? 104.266 141.213 121.292 1.00 31.79  0  310  LEU   A C   1 
ATOM   2054  O O   . LEU   A 1 346  ? 104.400 140.501 122.296 1.00 40.27  0  310  LEU   A O   1 
ATOM   2055  C CB  . LEU   A 1 346  ? 106.275 141.732 119.893 1.00 32.18  0  310  LEU   A CB  1 
ATOM   2056  C CG  . LEU   A 1 346  ? 107.254 141.399 118.773 1.00 30.47  0  310  LEU   A CG  1 
ATOM   2057  C CD1 . LEU   A 1 346  ? 108.415 142.369 118.810 1.00 29.09  0  310  LEU   A CD1 1 
ATOM   2058  C CD2 . LEU   A 1 346  ? 107.744 139.974 118.897 1.00 31.16  0  310  LEU   A CD2 1 
ATOM   2059  N N   . THR   A 1 347  ? 103.481 142.293 121.284 1.00 28.38  0  311  THR   A N   1 
ATOM   2060  C CA  . THR   A 1 347  ? 102.663 142.614 122.449 1.00 34.13  0  311  THR   A CA  1 
ATOM   2061  C C   . THR   A 1 347  ? 101.708 141.474 122.766 1.00 37.82  0  311  THR   A C   1 
ATOM   2062  O O   . THR   A 1 347  ? 101.523 141.108 123.935 1.00 32.18  0  311  THR   A O   1 
ATOM   2063  C CB  . THR   A 1 347  ? 101.891 143.911 122.209 1.00 39.85  0  311  THR   A CB  1 
ATOM   2064  O OG1 . THR   A 1 347  ? 102.816 144.985 122.004 1.00 41.32  0  311  THR   A OG1 1 
ATOM   2065  C CG2 . THR   A 1 347  ? 101.011 144.234 123.400 1.00 35.70  0  311  THR   A CG2 1 
ATOM   2066  N N   . GLN   A 1 348  ? 101.106 140.887 121.730 1.00 42.51  0  312  GLN   A N   1 
ATOM   2067  C CA  . GLN   A 1 348  ? 100.234 139.739 121.943 1.00 32.10  0  312  GLN   A CA  1 
ATOM   2068  C C   . GLN   A 1 348  ? 101.002 138.560 122.527 1.00 31.76  0  312  GLN   A C   1 
ATOM   2069  O O   . GLN   A 1 348  ? 100.475 137.832 123.374 1.00 36.14  0  312  GLN   A O   1 
ATOM   2070  C CB  . GLN   A 1 348  ? 99.548  139.351 120.636 1.00 26.81  0  312  GLN   A CB  1 
ATOM   2071  C CG  . GLN   A 1 348  ? 98.471  140.328 120.207 1.00 29.87  0  312  GLN   A CG  1 
ATOM   2072  C CD  . GLN   A 1 348  ? 97.907  140.015 118.836 1.00 42.59  0  312  GLN   A CD  1 
ATOM   2073  O OE1 . GLN   A 1 348  ? 98.054  138.905 118.329 1.00 44.67  0  312  GLN   A OE1 1 
ATOM   2074  N NE2 . GLN   A 1 348  ? 97.252  140.998 118.230 1.00 43.68  0  312  GLN   A NE2 1 
ATOM   2075  N N   . LEU   A 1 349  ? 102.243 138.345 122.084 1.00 33.98  0  313  LEU   A N   1 
ATOM   2076  C CA  . LEU   A 1 349  ? 103.052 137.279 122.674 1.00 27.38  0  313  LEU   A CA  1 
ATOM   2077  C C   . LEU   A 1 349  ? 103.281 137.516 124.159 1.00 30.48  0  313  LEU   A C   1 
ATOM   2078  O O   . LEU   A 1 349  ? 103.168 136.585 124.964 1.00 39.22  0  313  LEU   A O   1 
ATOM   2079  C CB  . LEU   A 1 349  ? 104.401 137.111 121.965 1.00 29.00  0  313  LEU   A CB  1 
ATOM   2080  C CG  . LEU   A 1 349  ? 104.592 136.409 120.617 1.00 22.66  0  313  LEU   A CG  1 
ATOM   2081  C CD1 . LEU   A 1 349  ? 104.608 137.320 119.427 1.00 23.19  0  313  LEU   A CD1 1 
ATOM   2082  C CD2 . LEU   A 1 349  ? 105.879 135.614 120.669 1.00 33.78  0  313  LEU   A CD2 1 
ATOM   2083  N N   . PHE   A 1 350  ? 103.621 138.749 124.545 1.00 21.47  0  314  PHE   A N   1 
ATOM   2084  C CA  . PHE   A 1 350  ? 103.810 139.004 125.973 1.00 19.97  0  314  PHE   A CA  1 
ATOM   2085  C C   . PHE   A 1 350  ? 102.520 138.745 126.740 1.00 33.93  0  314  PHE   A C   1 
ATOM   2086  O O   . PHE   A 1 350  ? 102.535 138.118 127.808 1.00 30.75  0  314  PHE   A O   1 
ATOM   2087  C CB  . PHE   A 1 350  ? 104.284 140.433 126.263 1.00 31.25  0  314  PHE   A CB  1 
ATOM   2088  C CG  . PHE   A 1 350  ? 105.397 140.929 125.385 1.00 37.51  0  314  PHE   A CG  1 
ATOM   2089  C CD1 . PHE   A 1 350  ? 105.207 142.036 124.581 1.00 35.89  0  314  PHE   A CD1 1 
ATOM   2090  C CD2 . PHE   A 1 350  ? 106.629 140.307 125.365 1.00 29.02  0  314  PHE   A CD2 1 
ATOM   2091  C CE1 . PHE   A 1 350  ? 106.218 142.514 123.775 1.00 34.02  0  314  PHE   A CE1 1 
ATOM   2092  C CE2 . PHE   A 1 350  ? 107.640 140.785 124.556 1.00 22.91  0  314  PHE   A CE2 1 
ATOM   2093  C CZ  . PHE   A 1 350  ? 107.434 141.885 123.763 1.00 33.95  0  314  PHE   A CZ  1 
ATOM   2094  N N   . LEU   A 1 351  ? 101.391 139.216 126.203 1.00 45.67  0  315  LEU   A N   1 
ATOM   2095  C CA  . LEU   A 1 351  ? 100.117 139.049 126.896 1.00 38.33  0  315  LEU   A CA  1 
ATOM   2096  C C   . LEU   A 1 351  ? 99.762  137.577 127.057 1.00 33.41  0  315  LEU   A C   1 
ATOM   2097  O O   . LEU   A 1 351  ? 99.322  137.152 128.129 1.00 41.74  0  315  LEU   A O   1 
ATOM   2098  C CB  . LEU   A 1 351  ? 99.005  139.783 126.147 1.00 38.15  0  315  LEU   A CB  1 
ATOM   2099  C CG  . LEU   A 1 351  ? 99.102  141.307 126.052 1.00 46.02  0  315  LEU   A CG  1 
ATOM   2100  C CD1 . LEU   A 1 351  ? 97.844  141.880 125.415 1.00 40.49  0  315  LEU   A CD1 1 
ATOM   2101  C CD2 . LEU   A 1 351  ? 99.356  141.933 127.415 1.00 40.74  0  315  LEU   A CD2 1 
ATOM   2102  N N   . TYR   A 1 352  ? 99.959  136.779 126.008 1.00 32.38  0  316  TYR   A N   1 
ATOM   2103  C CA  . TYR   A 1 352  ? 99.594  135.369 126.078 1.00 30.70  0  316  TYR   A CA  1 
ATOM   2104  C C   . TYR   A 1 352  ? 100.553 134.576 126.954 1.00 26.79  0  316  TYR   A C   1 
ATOM   2105  O O   . TYR   A 1 352  ? 100.129 133.640 127.635 1.00 34.56  0  316  TYR   A O   1 
ATOM   2106  C CB  . TYR   A 1 352  ? 99.530  134.773 124.675 1.00 39.08  0  316  TYR   A CB  1 
ATOM   2107  C CG  . TYR   A 1 352  ? 98.208  135.008 123.990 1.00 38.32  0  316  TYR   A CG  1 
ATOM   2108  C CD1 . TYR   A 1 352  ? 97.182  134.089 124.095 1.00 41.12  0  316  TYR   A CD1 1 
ATOM   2109  C CD2 . TYR   A 1 352  ? 97.984  136.153 123.247 1.00 44.05  0  316  TYR   A CD2 1 
ATOM   2110  C CE1 . TYR   A 1 352  ? 95.973  134.301 123.475 1.00 46.72  0  316  TYR   A CE1 1 
ATOM   2111  C CE2 . TYR   A 1 352  ? 96.780  136.371 122.618 1.00 43.46  0  316  TYR   A CE2 1 
ATOM   2112  C CZ  . TYR   A 1 352  ? 95.777  135.442 122.736 1.00 44.16  0  316  TYR   A CZ  1 
ATOM   2113  O OH  . TYR   A 1 352  ? 94.572  135.658 122.112 1.00 47.97  0  316  TYR   A OH  1 
ATOM   2114  N N   . GLY   A 1 353  ? 101.839 134.923 126.954 1.00 24.96  0  317  GLY   A N   1 
ATOM   2115  C CA  . GLY   A 1 353  ? 102.754 134.284 127.882 1.00 20.74  0  317  GLY   A CA  1 
ATOM   2116  C C   . GLY   A 1 353  ? 102.409 134.588 129.324 1.00 27.86  0  317  GLY   A C   1 
ATOM   2117  O O   . GLY   A 1 353  ? 102.491 133.714 130.191 1.00 33.63  0  317  GLY   A O   1 
ATOM   2118  N N   . ASP   A 1 354  ? 102.014 135.833 129.604 1.00 33.37  0  318  ASP   A N   1 
ATOM   2119  C CA  . ASP   A 1 354  ? 101.566 136.176 130.949 1.00 19.79  0  318  ASP   A CA  1 
ATOM   2120  C C   . ASP   A 1 354  ? 100.273 135.450 131.304 1.00 28.25  0  318  ASP   A C   1 
ATOM   2121  O O   . ASP   A 1 354  ? 100.090 135.023 132.447 1.00 25.28  0  318  ASP   A O   1 
ATOM   2122  C CB  . ASP   A 1 354  ? 101.389 137.687 131.068 1.00 26.52  0  318  ASP   A CB  1 
ATOM   2123  C CG  . ASP   A 1 354  ? 102.701 138.410 131.283 1.00 31.59  0  318  ASP   A CG  1 
ATOM   2124  O OD1 . ASP   A 1 354  ? 103.520 137.934 132.096 1.00 30.47  0  318  ASP   A OD1 1 
ATOM   2125  O OD2 . ASP   A 1 354  ? 102.916 139.453 130.633 1.00 40.29  -1 318  ASP   A OD2 1 
ATOM   2126  N N   . CYS   A 1 355  ? 99.366  135.296 130.336 1.00 38.41  0  319  CYS   A N   1 
ATOM   2127  C CA  . CYS   A 1 355  ? 98.145  134.532 130.576 1.00 28.98  0  319  CYS   A CA  1 
ATOM   2128  C C   . CYS   A 1 355  ? 98.460  133.077 130.890 1.00 24.82  0  319  CYS   A C   1 
ATOM   2129  O O   . CYS   A 1 355  ? 97.814  132.466 131.746 1.00 40.94  0  319  CYS   A O   1 
ATOM   2130  C CB  . CYS   A 1 355  ? 97.217  134.623 129.366 1.00 31.69  0  319  CYS   A CB  1 
ATOM   2131  S SG  . CYS   A 1 355  ? 96.235  136.136 129.272 1.00 50.56  0  319  CYS   A SG  1 
ATOM   2132  N N   . ILE   A 1 356  ? 99.432  132.497 130.186 1.00 24.63  0  320  ILE   A N   1 
ATOM   2133  C CA  . ILE   A 1 356  ? 99.846  131.125 130.466 1.00 27.52  0  320  ILE   A CA  1 
ATOM   2134  C C   . ILE   A 1 356  ? 100.431 131.029 131.866 1.00 15.95  0  320  ILE   A C   1 
ATOM   2135  O O   . ILE   A 1 356  ? 100.115 130.114 132.632 1.00 26.63  0  320  ILE   A O   1 
ATOM   2136  C CB  . ILE   A 1 356  ? 100.850 130.643 129.404 1.00 33.32  0  320  ILE   A CB  1 
ATOM   2137  C CG1 . ILE   A 1 356  ? 100.124 130.255 128.121 1.00 32.41  0  320  ILE   A CG1 1 
ATOM   2138  C CG2 . ILE   A 1 356  ? 101.661 129.471 129.919 1.00 24.81  0  320  ILE   A CG2 1 
ATOM   2139  C CD1 . ILE   A 1 356  ? 101.036 129.707 127.075 1.00 32.03  0  320  ILE   A CD1 1 
ATOM   2140  N N   . LEU   A 1 357  ? 101.296 131.979 132.221 1.00 27.18  0  321  LEU   A N   1 
ATOM   2141  C CA  . LEU   A 1 357  ? 101.879 132.004 133.555 1.00 31.46  0  321  LEU   A CA  1 
ATOM   2142  C C   . LEU   A 1 357  ? 100.843 132.292 134.631 1.00 31.98  0  321  LEU   A C   1 
ATOM   2143  O O   . LEU   A 1 357  ? 101.108 132.053 135.812 1.00 28.44  0  321  LEU   A O   1 
ATOM   2144  C CB  . LEU   A 1 357  ? 102.989 133.050 133.616 1.00 25.98  0  321  LEU   A CB  1 
ATOM   2145  C CG  . LEU   A 1 357  ? 104.263 132.765 132.832 1.00 19.30  0  321  LEU   A CG  1 
ATOM   2146  C CD1 . LEU   A 1 357  ? 105.040 134.041 132.633 1.00 26.62  0  321  LEU   A CD1 1 
ATOM   2147  C CD2 . LEU   A 1 357  ? 105.094 131.754 133.577 1.00 31.57  0  321  LEU   A CD2 1 
ATOM   2148  N N   . LYS   A 1 358  ? 99.686  132.829 134.249 1.00 33.50  0  322  LYS   A N   1 
ATOM   2149  C CA  . LYS   A 1 358  ? 98.622  133.113 135.204 1.00 31.64  0  322  LYS   A CA  1 
ATOM   2150  C C   . LYS   A 1 358  ? 97.711  131.909 135.402 1.00 35.77  0  322  LYS   A C   1 
ATOM   2151  O O   . LYS   A 1 358  ? 97.358  131.581 136.539 1.00 38.06  0  322  LYS   A O   1 
ATOM   2152  C CB  . LYS   A 1 358  ? 97.820  134.321 134.722 1.00 34.62  0  322  LYS   A CB  1 
ATOM   2153  C CG  . LYS   A 1 358  ? 96.561  134.618 135.501 1.00 30.40  0  322  LYS   A CG  1 
ATOM   2154  C CD  . LYS   A 1 358  ? 95.907  135.874 134.956 1.00 31.89  0  322  LYS   A CD  1 
ATOM   2155  C CE  . LYS   A 1 358  ? 94.531  136.092 135.549 1.00 39.17  0  322  LYS   A CE  1 
ATOM   2156  N NZ  . LYS   A 1 358  ? 93.941  137.384 135.102 1.00 38.21  1  322  LYS   A NZ  1 
ATOM   2157  N N   . LEU   A 1 359  ? 97.319  131.249 134.310 1.00 38.91  0  323  LEU   A N   1 
ATOM   2158  C CA  . LEU   A 1 359  ? 96.482  130.057 134.375 1.00 32.02  0  323  LEU   A CA  1 
ATOM   2159  C C   . LEU   A 1 359  ? 97.205  128.964 135.142 1.00 31.92  0  323  LEU   A C   1 
ATOM   2160  O O   . LEU   A 1 359  ? 96.787  128.580 136.238 1.00 41.86  0  323  LEU   A O   1 
ATOM   2161  C CB  . LEU   A 1 359  ? 96.130  129.565 132.973 1.00 33.55  0  323  LEU   A CB  1 
ATOM   2162  C CG  . LEU   A 1 359  ? 94.750  129.940 132.443 1.00 41.61  0  323  LEU   A CG  1 
ATOM   2163  C CD1 . LEU   A 1 359  ? 94.689  131.427 132.142 1.00 35.41  0  323  LEU   A CD1 1 
ATOM   2164  C CD2 . LEU   A 1 359  ? 94.424  129.121 131.209 1.00 38.91  0  323  LEU   A CD2 1 
ATOM   2165  N N   . PHE   A 1 360  ? 98.295  128.465 134.574 1.00 27.49  0  324  PHE   A N   1 
ATOM   2166  C CA  . PHE   A 1 360  ? 99.238  127.698 135.366 1.00 29.08  0  324  PHE   A CA  1 
ATOM   2167  C C   . PHE   A 1 360  ? 99.853  128.619 136.405 1.00 38.03  0  324  PHE   A C   1 
ATOM   2168  O O   . PHE   A 1 360  ? 99.951  129.829 136.209 1.00 42.36  0  324  PHE   A O   1 
ATOM   2169  C CB  . PHE   A 1 360  ? 100.337 127.107 134.485 1.00 33.97  0  324  PHE   A CB  1 
ATOM   2170  C CG  . PHE   A 1 360  ? 99.862  126.042 133.541 1.00 36.38  0  324  PHE   A CG  1 
ATOM   2171  C CD1 . PHE   A 1 360  ? 99.919  124.708 133.897 1.00 34.25  0  324  PHE   A CD1 1 
ATOM   2172  C CD2 . PHE   A 1 360  ? 99.378  126.376 132.290 1.00 33.20  0  324  PHE   A CD2 1 
ATOM   2173  C CE1 . PHE   A 1 360  ? 99.492  123.733 133.030 1.00 29.05  0  324  PHE   A CE1 1 
ATOM   2174  C CE2 . PHE   A 1 360  ? 98.949  125.404 131.421 1.00 32.05  0  324  PHE   A CE2 1 
ATOM   2175  C CZ  . PHE   A 1 360  ? 99.004  124.081 131.792 1.00 32.51  0  324  PHE   A CZ  1 
ATOM   2176  N N   . HIS   A 1 361  ? 100.237 128.053 137.536 1.00 39.08  0  325  HIS   A N   1 
ATOM   2177  C CA  . HIS   A 1 361  ? 100.956 128.837 138.528 1.00 31.99  0  325  HIS   A CA  1 
ATOM   2178  C C   . HIS   A 1 361  ? 102.437 128.841 138.178 1.00 28.81  0  325  HIS   A C   1 
ATOM   2179  O O   . HIS   A 1 361  ? 102.791 128.645 137.012 1.00 39.66  0  325  HIS   A O   1 
ATOM   2180  C CB  . HIS   A 1 361  ? 100.679 128.310 139.932 1.00 35.40  0  325  HIS   A CB  1 
ATOM   2181  C CG  . HIS   A 1 361  ? 99.337  128.716 140.455 1.00 31.06  0  325  HIS   A CG  1 
ATOM   2182  N ND1 . HIS   A 1 361  ? 99.156  129.258 141.709 1.00 30.91  0  325  HIS   A ND1 1 
ATOM   2183  C CD2 . HIS   A 1 361  ? 98.114  128.688 139.878 1.00 30.86  0  325  HIS   A CD2 1 
ATOM   2184  C CE1 . HIS   A 1 361  ? 97.877  129.529 141.888 1.00 37.29  0  325  HIS   A CE1 1 
ATOM   2185  N NE2 . HIS   A 1 361  ? 97.223  129.195 140.791 1.00 41.92  0  325  HIS   A NE2 1 
ATOM   2186  N N   . ASN   A 1 362  ? 103.291 129.149 139.153 1.00 28.63  0  326  ASN   A N   1 
ATOM   2187  C CA  . ASN   A 1 362  ? 104.744 129.121 139.001 1.00 30.99  0  326  ASN   A CA  1 
ATOM   2188  C C   . ASN   A 1 362  ? 105.214 128.011 138.065 1.00 39.66  0  326  ASN   A C   1 
ATOM   2189  O O   . ASN   A 1 362  ? 106.020 128.254 137.158 1.00 39.20  0  326  ASN   A O   1 
ATOM   2190  C CB  . ASN   A 1 362  ? 105.382 128.967 140.384 1.00 32.00  0  326  ASN   A CB  1 
ATOM   2191  C CG  . ASN   A 1 362  ? 106.873 128.772 140.325 1.00 33.65  0  326  ASN   A CG  1 
ATOM   2192  O OD1 . ASN   A 1 362  ? 107.595 129.591 139.762 1.00 41.95  0  326  ASN   A OD1 1 
ATOM   2193  N ND2 . ASN   A 1 362  ? 107.350 127.693 140.932 1.00 29.39  0  326  ASN   A ND2 1 
ATOM   2194  N N   . GLU   A 1 363  ? 104.673 126.800 138.243 1.00 49.13  0  327  GLU   A N   1 
ATOM   2195  C CA  . GLU   A 1 363  ? 104.990 125.680 137.361 1.00 42.73  0  327  GLU   A CA  1 
ATOM   2196  C C   . GLU   A 1 363  ? 104.780 126.004 135.888 1.00 37.20  0  327  GLU   A C   1 
ATOM   2197  O O   . GLU   A 1 363  ? 105.332 125.309 135.029 1.00 35.15  0  327  GLU   A O   1 
ATOM   2198  C CB  . GLU   A 1 363  ? 104.148 124.461 137.737 1.00 37.17  0  327  GLU   A CB  1 
ATOM   2199  C CG  . GLU   A 1 363  ? 104.662 123.711 138.945 1.00 43.94  0  327  GLU   A CG  1 
ATOM   2200  C CD  . GLU   A 1 363  ? 104.219 124.337 140.246 1.00 48.49  0  327  GLU   A CD  1 
ATOM   2201  O OE1 . GLU   A 1 363  ? 103.365 125.247 140.206 1.00 46.04  0  327  GLU   A OE1 1 
ATOM   2202  O OE2 . GLU   A 1 363  ? 104.727 123.921 141.308 1.00 45.99  -1 327  GLU   A OE2 1 
ATOM   2203  N N   . GLY   A 1 364  ? 104.001 127.040 135.575 1.00 38.17  0  328  GLY   A N   1 
ATOM   2204  C CA  . GLY   A 1 364  ? 103.805 127.429 134.192 1.00 22.83  0  328  GLY   A CA  1 
ATOM   2205  C C   . GLY   A 1 364  ? 105.090 127.740 133.466 1.00 30.33  0  328  GLY   A C   1 
ATOM   2206  O O   . GLY   A 1 364  ? 105.150 127.593 132.239 1.00 45.18  0  328  GLY   A O   1 
ATOM   2207  N N   . PHE   A 1 365  ? 106.133 128.145 134.196 1.00 22.56  0  329  PHE   A N   1 
ATOM   2208  C CA  . PHE   A 1 365  ? 107.412 128.410 133.547 1.00 24.73  0  329  PHE   A CA  1 
ATOM   2209  C C   . PHE   A 1 365  ? 107.940 127.177 132.832 1.00 28.01  0  329  PHE   A C   1 
ATOM   2210  O O   . PHE   A 1 365  ? 108.627 127.304 131.811 1.00 26.94  0  329  PHE   A O   1 
ATOM   2211  C CB  . PHE   A 1 365  ? 108.423 128.921 134.567 1.00 23.20  0  329  PHE   A CB  1 
ATOM   2212  C CG  . PHE   A 1 365  ? 108.237 130.364 134.912 1.00 27.57  0  329  PHE   A CG  1 
ATOM   2213  C CD1 . PHE   A 1 365  ? 108.682 131.352 134.059 1.00 20.06  0  329  PHE   A CD1 1 
ATOM   2214  C CD2 . PHE   A 1 365  ? 107.597 130.732 136.078 1.00 27.53  0  329  PHE   A CD2 1 
ATOM   2215  C CE1 . PHE   A 1 365  ? 108.501 132.674 134.367 1.00 20.46  0  329  PHE   A CE1 1 
ATOM   2216  C CE2 . PHE   A 1 365  ? 107.415 132.054 136.392 1.00 18.33  0  329  PHE   A CE2 1 
ATOM   2217  C CZ  . PHE   A 1 365  ? 107.868 133.026 135.536 1.00 21.58  0  329  PHE   A CZ  1 
ATOM   2218  N N   . TYR   A 1 366  ? 107.598 125.984 133.329 1.00 39.17  0  330  TYR   A N   1 
ATOM   2219  C CA  . TYR   A 1 366  ? 107.949 124.752 132.632 1.00 34.19  0  330  TYR   A CA  1 
ATOM   2220  C C   . TYR   A 1 366  ? 107.531 124.813 131.172 1.00 27.37  0  330  TYR   A C   1 
ATOM   2221  O O   . TYR   A 1 366  ? 108.341 124.552 130.276 1.00 36.60  0  330  TYR   A O   1 
ATOM   2222  C CB  . TYR   A 1 366  ? 107.285 123.557 133.310 1.00 36.14  0  330  TYR   A CB  1 
ATOM   2223  C CG  . TYR   A 1 366  ? 107.875 123.178 134.644 1.00 40.93  0  330  TYR   A CG  1 
ATOM   2224  C CD1 . TYR   A 1 366  ? 109.107 123.670 135.047 1.00 35.72  0  330  TYR   A CD1 1 
ATOM   2225  C CD2 . TYR   A 1 366  ? 107.195 122.325 135.502 1.00 37.70  0  330  TYR   A CD2 1 
ATOM   2226  C CE1 . TYR   A 1 366  ? 109.646 123.320 136.268 1.00 40.70  0  330  TYR   A CE1 1 
ATOM   2227  C CE2 . TYR   A 1 366  ? 107.724 121.971 136.723 1.00 37.52  0  330  TYR   A CE2 1 
ATOM   2228  C CZ  . TYR   A 1 366  ? 108.949 122.470 137.102 1.00 47.34  0  330  TYR   A CZ  1 
ATOM   2229  O OH  . TYR   A 1 366  ? 109.478 122.116 138.321 1.00 49.90  0  330  TYR   A OH  1 
ATOM   2230  N N   . ILE   A 1 367  ? 106.279 125.194 130.911 1.00 21.76  0  331  ILE   A N   1 
ATOM   2231  C CA  . ILE   A 1 367  ? 105.827 125.298 129.529 1.00 20.79  0  331  ILE   A CA  1 
ATOM   2232  C C   . ILE   A 1 367  ? 106.656 126.332 128.785 1.00 33.25  0  331  ILE   A C   1 
ATOM   2233  O O   . ILE   A 1 367  ? 107.103 126.095 127.656 1.00 44.88  0  331  ILE   A O   1 
ATOM   2234  C CB  . ILE   A 1 367  ? 104.326 125.627 129.474 1.00 26.26  0  331  ILE   A CB  1 
ATOM   2235  C CG1 . ILE   A 1 367  ? 103.510 124.477 130.059 1.00 31.75  0  331  ILE   A CG1 1 
ATOM   2236  C CG2 . ILE   A 1 367  ? 103.899 125.897 128.047 1.00 25.08  0  331  ILE   A CG2 1 
ATOM   2237  C CD1 . ILE   A 1 367  ? 103.121 124.674 131.495 1.00 31.59  0  331  ILE   A CD1 1 
ATOM   2238  N N   . ILE   A 1 368  ? 106.907 127.480 129.420 1.00 26.75  0  332  ILE   A N   1 
ATOM   2239  C CA  . ILE   A 1 368  ? 107.745 128.496 128.796 1.00 25.49  0  332  ILE   A CA  1 
ATOM   2240  C C   . ILE   A 1 368  ? 109.136 127.941 128.542 1.00 34.26  0  332  ILE   A C   1 
ATOM   2241  O O   . ILE   A 1 368  ? 109.768 128.264 127.530 1.00 35.30  0  332  ILE   A O   1 
ATOM   2242  C CB  . ILE   A 1 368  ? 107.787 129.764 129.669 1.00 33.83  0  332  ILE   A CB  1 
ATOM   2243  C CG1 . ILE   A 1 368  ? 106.371 130.282 129.923 1.00 32.20  0  332  ILE   A CG1 1 
ATOM   2244  C CG2 . ILE   A 1 368  ? 108.633 130.836 129.013 1.00 35.53  0  332  ILE   A CG2 1 
ATOM   2245  C CD1 . ILE   A 1 368  ? 105.760 130.990 128.740 1.00 36.66  0  332  ILE   A CD1 1 
ATOM   2246  N N   . LYS   A 1 369  ? 109.616 127.061 129.424 1.00 34.62  0  333  LYS   A N   1 
ATOM   2247  C CA  . LYS   A 1 369  ? 110.935 126.471 129.247 1.00 27.44  0  333  LYS   A CA  1 
ATOM   2248  C C   . LYS   A 1 369  ? 111.047 125.714 127.932 1.00 35.06  0  333  LYS   A C   1 
ATOM   2249  O O   . LYS   A 1 369  ? 112.157 125.542 127.420 1.00 45.70  0  333  LYS   A O   1 
ATOM   2250  C CB  . LYS   A 1 369  ? 111.244 125.550 130.431 1.00 32.83  0  333  LYS   A CB  1 
ATOM   2251  C CG  . LYS   A 1 369  ? 112.495 124.700 130.290 1.00 33.48  0  333  LYS   A CG  1 
ATOM   2252  C CD  . LYS   A 1 369  ? 113.132 124.434 131.641 1.00 37.31  0  333  LYS   A CD  1 
ATOM   2253  C CE  . LYS   A 1 369  ? 114.543 124.995 131.707 1.00 40.66  0  333  LYS   A CE  1 
ATOM   2254  N NZ  . LYS   A 1 369  ? 115.005 125.185 133.111 1.00 41.56  1  333  LYS   A NZ  1 
ATOM   2255  N N   . GLU   A 1 370  ? 109.926 125.286 127.356 1.00 38.46  0  334  GLU   A N   1 
ATOM   2256  C CA  . GLU   A 1 370  ? 109.952 124.529 126.113 1.00 32.36  0  334  GLU   A CA  1 
ATOM   2257  C C   . GLU   A 1 370  ? 109.825 125.404 124.875 1.00 34.11  0  334  GLU   A C   1 
ATOM   2258  O O   . GLU   A 1 370  ? 109.829 124.868 123.762 1.00 45.79  0  334  GLU   A O   1 
ATOM   2259  C CB  . GLU   A 1 370  ? 108.839 123.482 126.114 1.00 28.28  0  334  GLU   A CB  1 
ATOM   2260  C CG  . GLU   A 1 370  ? 108.760 122.684 127.393 1.00 36.83  0  334  GLU   A CG  1 
ATOM   2261  C CD  . GLU   A 1 370  ? 109.929 121.744 127.563 1.00 42.80  0  334  GLU   A CD  1 
ATOM   2262  O OE1 . GLU   A 1 370  ? 110.618 121.463 126.562 1.00 45.37  0  334  GLU   A OE1 1 
ATOM   2263  O OE2 . GLU   A 1 370  ? 110.166 121.289 128.700 1.00 49.71  -1 334  GLU   A OE2 1 
ATOM   2264  N N   . VAL   A 1 371  ? 109.737 126.728 125.033 1.00 32.07  0  335  VAL   A N   1 
ATOM   2265  C CA  . VAL   A 1 371  ? 109.493 127.589 123.878 1.00 38.78  0  335  VAL   A CA  1 
ATOM   2266  C C   . VAL   A 1 371  ? 110.575 127.393 122.824 1.00 46.76  0  335  VAL   A C   1 
ATOM   2267  O O   . VAL   A 1 371  ? 110.277 127.290 121.626 1.00 48.54  0  335  VAL   A O   1 
ATOM   2268  C CB  . VAL   A 1 371  ? 109.369 129.066 124.308 1.00 48.22  0  335  VAL   A CB  1 
ATOM   2269  C CG1 . VAL   A 1 371  ? 110.663 129.593 124.921 1.00 43.44  0  335  VAL   A CG1 1 
ATOM   2270  C CG2 . VAL   A 1 371  ? 108.955 129.926 123.130 1.00 41.76  0  335  VAL   A CG2 1 
ATOM   2271  N N   . GLU   A 1 372  ? 111.840 127.290 123.250 1.00 42.65  0  336  GLU   A N   1 
ATOM   2272  C CA  . GLU   A 1 372  ? 112.930 127.134 122.292 1.00 40.42  0  336  GLU   A CA  1 
ATOM   2273  C C   . GLU   A 1 372  ? 112.690 125.920 121.414 1.00 41.67  0  336  GLU   A C   1 
ATOM   2274  O O   . GLU   A 1 372  ? 112.924 125.961 120.200 1.00 44.08  0  336  GLU   A O   1 
ATOM   2275  C CB  . GLU   A 1 372  ? 114.274 126.996 123.004 1.00 39.96  0  336  GLU   A CB  1 
ATOM   2276  C CG  . GLU   A 1 372  ? 114.255 126.083 124.206 1.00 40.06  0  336  GLU   A CG  1 
ATOM   2277  C CD  . GLU   A 1 372  ? 114.179 126.838 125.502 1.00 47.96  0  336  GLU   A CD  1 
ATOM   2278  O OE1 . GLU   A 1 372  ? 113.177 127.550 125.710 1.00 48.48  0  336  GLU   A OE1 1 
ATOM   2279  O OE2 . GLU   A 1 372  ? 115.126 126.719 126.305 1.00 43.43  -1 336  GLU   A OE2 1 
ATOM   2280  N N   . GLY   A 1 373  ? 112.209 124.833 122.019 1.00 31.70  0  337  GLY   A N   1 
ATOM   2281  C CA  . GLY   A 1 373  ? 111.853 123.646 121.277 1.00 34.27  0  337  GLY   A CA  1 
ATOM   2282  C C   . GLY   A 1 373  ? 111.043 124.031 120.065 1.00 36.31  0  337  GLY   A C   1 
ATOM   2283  O O   . GLY   A 1 373  ? 111.485 123.821 118.931 1.00 47.47  0  337  GLY   A O   1 
ATOM   2284  N N   . PHE   A 1 374  ? 109.895 124.673 120.294 1.00 29.25  0  338  PHE   A N   1 
ATOM   2285  C CA  . PHE   A 1 374  ? 109.071 125.113 119.177 1.00 28.12  0  338  PHE   A CA  1 
ATOM   2286  C C   . PHE   A 1 374  ? 109.894 125.945 118.209 1.00 35.43  0  338  PHE   A C   1 
ATOM   2287  O O   . PHE   A 1 374  ? 109.967 125.636 117.013 1.00 45.60  0  338  PHE   A O   1 
ATOM   2288  C CB  . PHE   A 1 374  ? 107.867 125.904 119.684 1.00 28.76  0  338  PHE   A CB  1 
ATOM   2289  C CG  . PHE   A 1 374  ? 106.926 126.338 118.597 1.00 35.27  0  338  PHE   A CG  1 
ATOM   2290  C CD1 . PHE   A 1 374  ? 105.992 125.462 118.080 1.00 33.02  0  338  PHE   A CD1 1 
ATOM   2291  C CD2 . PHE   A 1 374  ? 106.973 127.622 118.094 1.00 32.62  0  338  PHE   A CD2 1 
ATOM   2292  C CE1 . PHE   A 1 374  ? 105.128 125.853 117.083 1.00 28.59  0  338  PHE   A CE1 1 
ATOM   2293  C CE2 . PHE   A 1 374  ? 106.107 128.020 117.097 1.00 32.49  0  338  PHE   A CE2 1 
ATOM   2294  C CZ  . PHE   A 1 374  ? 105.183 127.132 116.593 1.00 30.51  0  338  PHE   A CZ  1 
ATOM   2295  N N   . ILE   A 1 375  ? 110.585 126.962 118.728 1.00 23.85  0  339  ILE   A N   1 
ATOM   2296  C CA  . ILE   A 1 375  ? 111.400 127.812 117.869 1.00 29.15  0  339  ILE   A CA  1 
ATOM   2297  C C   . ILE   A 1 375  ? 112.417 126.970 117.118 1.00 38.76  0  339  ILE   A C   1 
ATOM   2298  O O   . ILE   A 1 375  ? 112.555 127.085 115.893 1.00 42.19  0  339  ILE   A O   1 
ATOM   2299  C CB  . ILE   A 1 375  ? 112.075 128.922 118.691 1.00 32.05  0  339  ILE   A CB  1 
ATOM   2300  C CG1 . ILE   A 1 375  ? 111.023 129.788 119.379 1.00 34.58  0  339  ILE   A CG1 1 
ATOM   2301  C CG2 . ILE   A 1 375  ? 112.941 129.780 117.797 1.00 34.57  0  339  ILE   A CG2 1 
ATOM   2302  C CD1 . ILE   A 1 375  ? 111.589 130.725 120.408 1.00 32.31  0  339  ILE   A CD1 1 
ATOM   2303  N N   . MET   A 1 376  ? 113.101 126.065 117.827 1.00 37.76  0  340  MET   A N   1 
ATOM   2304  C CA  . MET   A 1 376  ? 114.065 125.201 117.160 1.00 27.45  0  340  MET   A CA  1 
ATOM   2305  C C   . MET   A 1 376  ? 113.397 124.442 116.028 1.00 31.88  0  340  MET   A C   1 
ATOM   2306  O O   . MET   A 1 376  ? 113.879 124.453 114.889 1.00 34.19  0  340  MET   A O   1 
ATOM   2307  C CB  . MET   A 1 376  ? 114.698 124.233 118.157 1.00 26.79  0  340  MET   A CB  1 
ATOM   2308  C CG  . MET   A 1 376  ? 115.808 124.834 118.989 1.00 32.52  0  340  MET   A CG  1 
ATOM   2309  S SD  . MET   A 1 376  ? 117.011 123.606 119.529 1.00 55.58  0  340  MET   A SD  1 
ATOM   2310  C CE  . MET   A 1 376  ? 116.200 122.936 120.976 1.00 37.30  0  340  MET   A CE  1 
ATOM   2311  N N   . SER   A 1 377  ? 112.238 123.841 116.310 1.00 29.36  0  341  SER   A N   1 
ATOM   2312  C CA  . SER   A 1 377  ? 111.517 123.111 115.277 1.00 23.57  0  341  SER   A CA  1 
ATOM   2313  C C   . SER   A 1 377  ? 111.243 124.017 114.093 1.00 30.10  0  341  SER   A C   1 
ATOM   2314  O O   . SER   A 1 377  ? 111.499 123.649 112.940 1.00 45.75  0  341  SER   A O   1 
ATOM   2315  C CB  . SER   A 1 377  ? 110.215 122.554 115.841 1.00 31.42  0  341  SER   A CB  1 
ATOM   2316  O OG  . SER   A 1 377  ? 110.473 121.675 116.917 1.00 40.30  0  341  SER   A OG  1 
ATOM   2317  N N   . LEU   A 1 378  ? 110.785 125.238 114.370 1.00 20.24  0  342  LEU   A N   1 
ATOM   2318  C CA  . LEU   A 1 378  ? 110.510 126.181 113.296 1.00 23.32  0  342  LEU   A CA  1 
ATOM   2319  C C   . LEU   A 1 378  ? 111.739 126.366 112.426 1.00 32.93  0  342  LEU   A C   1 
ATOM   2320  O O   . LEU   A 1 378  ? 111.662 126.270 111.196 1.00 35.85  0  342  LEU   A O   1 
ATOM   2321  C CB  . LEU   A 1 378  ? 110.046 127.514 113.876 1.00 26.39  0  342  LEU   A CB  1 
ATOM   2322  C CG  . LEU   A 1 378  ? 108.540 127.746 113.902 1.00 31.00  0  342  LEU   A CG  1 
ATOM   2323  C CD1 . LEU   A 1 378  ? 108.030 127.992 112.497 1.00 30.34  0  342  LEU   A CD1 1 
ATOM   2324  C CD2 . LEU   A 1 378  ? 107.858 126.543 114.504 1.00 35.53  0  342  LEU   A CD2 1 
ATOM   2325  N N   . ILE   A 1 379  ? 112.900 126.557 113.056 1.00 32.91  0  343  ILE   A N   1 
ATOM   2326  C CA  . ILE   A 1 379  ? 114.128 126.759 112.297 1.00 28.24  0  343  ILE   A CA  1 
ATOM   2327  C C   . ILE   A 1 379  ? 114.385 125.567 111.392 1.00 30.93  0  343  ILE   A C   1 
ATOM   2328  O O   . ILE   A 1 379  ? 114.692 125.725 110.203 1.00 36.44  0  343  ILE   A O   1 
ATOM   2329  C CB  . ILE   A 1 379  ? 115.308 127.017 113.251 1.00 28.95  0  343  ILE   A CB  1 
ATOM   2330  C CG1 . ILE   A 1 379  ? 115.092 128.320 114.021 1.00 32.74  0  343  ILE   A CG1 1 
ATOM   2331  C CG2 . ILE   A 1 379  ? 116.608 127.065 112.482 1.00 31.06  0  343  ILE   A CG2 1 
ATOM   2332  C CD1 . ILE   A 1 379  ? 115.992 128.473 115.218 1.00 36.58  0  343  ILE   A CD1 1 
ATOM   2333  N N   . LEU   A 1 380  ? 114.211 124.352 111.923 1.00 25.25  0  344  LEU   A N   1 
ATOM   2334  C CA  . LEU   A 1 380  ? 114.482 123.170 111.118 1.00 21.95  0  344  LEU   A CA  1 
ATOM   2335  C C   . LEU   A 1 380  ? 113.579 123.115 109.897 1.00 21.37  0  344  LEU   A C   1 
ATOM   2336  O O   . LEU   A 1 380  ? 113.999 122.638 108.838 1.00 33.45  0  344  LEU   A O   1 
ATOM   2337  C CB  . LEU   A 1 380  ? 114.328 121.905 111.957 1.00 22.86  0  344  LEU   A CB  1 
ATOM   2338  C CG  . LEU   A 1 380  ? 115.279 121.760 113.145 1.00 23.58  0  344  LEU   A CG  1 
ATOM   2339  C CD1 . LEU   A 1 380  ? 115.390 120.307 113.552 1.00 30.20  0  344  LEU   A CD1 1 
ATOM   2340  C CD2 . LEU   A 1 380  ? 116.643 122.322 112.828 1.00 25.85  0  344  LEU   A CD2 1 
ATOM   2341  N N   . ASN   A 1 381  ? 112.362 123.649 110.001 1.00 23.04  0  345  ASN   A N   1 
ATOM   2342  C CA  . ASN   A 1 381  ? 111.453 123.592 108.867 1.00 30.42  0  345  ASN   A CA  1 
ATOM   2343  C C   . ASN   A 1 381  ? 111.948 124.405 107.681 1.00 34.51  0  345  ASN   A C   1 
ATOM   2344  O O   . ASN   A 1 381  ? 111.415 124.242 106.579 1.00 42.97  0  345  ASN   A O   1 
ATOM   2345  C CB  . ASN   A 1 381  ? 110.060 124.059 109.285 1.00 33.37  0  345  ASN   A CB  1 
ATOM   2346  C CG  . ASN   A 1 381  ? 109.451 123.181 110.361 1.00 34.03  0  345  ASN   A CG  1 
ATOM   2347  O OD1 . ASN   A 1 381  ? 109.998 122.137 110.708 1.00 34.26  0  345  ASN   A OD1 1 
ATOM   2348  N ND2 . ASN   A 1 381  ? 108.309 123.598 110.891 1.00 33.37  0  345  ASN   A ND2 1 
ATOM   2349  N N   . ILE   A 1 382  ? 112.946 125.269 107.870 1.00 37.19  0  346  ILE   A N   1 
ATOM   2350  C CA  . ILE   A 1 382  ? 113.602 125.919 106.741 1.00 36.00  0  346  ILE   A CA  1 
ATOM   2351  C C   . ILE   A 1 382  ? 114.948 125.276 106.419 1.00 34.92  0  346  ILE   A C   1 
ATOM   2352  O O   . ILE   A 1 382  ? 115.385 125.328 105.259 1.00 35.14  0  346  ILE   A O   1 
ATOM   2353  C CB  . ILE   A 1 382  ? 113.783 127.440 106.966 1.00 36.58  0  346  ILE   A CB  1 
ATOM   2354  C CG1 . ILE   A 1 382  ? 112.473 128.136 107.353 1.00 37.66  0  346  ILE   A CG1 1 
ATOM   2355  C CG2 . ILE   A 1 382  ? 114.348 128.118 105.726 1.00 35.83  0  346  ILE   A CG2 1 
ATOM   2356  C CD1 . ILE   A 1 382  ? 112.126 128.098 108.813 1.00 33.66  0  346  ILE   A CD1 1 
ATOM   2357  N N   . THR   A 1 383  ? 115.598 124.637 107.391 1.00 35.33  0  347  THR   A N   1 
ATOM   2358  C CA  . THR   A 1 383  ? 116.968 124.185 107.214 1.00 38.12  0  347  THR   A CA  1 
ATOM   2359  C C   . THR   A 1 383  ? 117.122 122.676 107.098 1.00 41.44  0  347  THR   A C   1 
ATOM   2360  O O   . THR   A 1 383  ? 118.257 122.200 107.003 1.00 50.79  0  347  THR   A O   1 
ATOM   2361  C CB  . THR   A 1 383  ? 117.843 124.676 108.376 1.00 36.44  0  347  THR   A CB  1 
ATOM   2362  O OG1 . THR   A 1 383  ? 117.523 123.942 109.561 1.00 33.36  0  347  THR   A OG1 1 
ATOM   2363  C CG2 . THR   A 1 383  ? 117.603 126.148 108.631 1.00 32.25  0  347  THR   A CG2 1 
ATOM   2364  N N   . GLU   A 1 384  ? 116.037 121.910 107.101 1.00 37.22  0  348  GLU   A N   1 
ATOM   2365  C CA  . GLU   A 1 384  ? 116.143 120.463 107.191 1.00 39.04  0  348  GLU   A CA  1 
ATOM   2366  C C   . GLU   A 1 384  ? 115.284 119.774 106.142 1.00 47.50  0  348  GLU   A C   1 
ATOM   2367  O O   . GLU   A 1 384  ? 114.444 120.387 105.480 1.00 47.95  0  348  GLU   A O   1 
ATOM   2368  C CB  . GLU   A 1 384  ? 115.744 119.976 108.587 1.00 47.39  0  348  GLU   A CB  1 
ATOM   2369  C CG  . GLU   A 1 384  ? 116.818 120.151 109.633 1.00 45.09  0  348  GLU   A CG  1 
ATOM   2370  C CD  . GLU   A 1 384  ? 117.881 119.083 109.575 1.00 43.82  0  348  GLU   A CD  1 
ATOM   2371  O OE1 . GLU   A 1 384  ? 118.136 118.534 108.485 1.00 47.79  0  348  GLU   A OE1 1 
ATOM   2372  O OE2 . GLU   A 1 384  ? 118.463 118.788 110.633 1.00 45.91  -1 348  GLU   A OE2 1 
ATOM   2373  N N   . GLU   A 1 385  ? 115.516 118.468 106.008 1.00 57.04  0  349  GLU   A N   1 
ATOM   2374  C CA  . GLU   A 1 385  ? 114.749 117.606 105.128 1.00 54.51  0  349  GLU   A CA  1 
ATOM   2375  C C   . GLU   A 1 385  ? 113.539 117.049 105.874 1.00 57.29  0  349  GLU   A C   1 
ATOM   2376  O O   . GLU   A 1 385  ? 113.287 117.379 107.034 1.00 58.79  0  349  GLU   A O   1 
ATOM   2377  C CB  . GLU   A 1 385  ? 115.628 116.482 104.586 1.00 52.59  0  349  GLU   A CB  1 
ATOM   2378  C CG  . GLU   A 1 385  ? 116.994 116.945 104.118 1.00 58.90  0  349  GLU   A CG  1 
ATOM   2379  C CD  . GLU   A 1 385  ? 116.918 117.921 102.963 1.00 58.36  0  349  GLU   A CD  1 
ATOM   2380  O OE1 . GLU   A 1 385  ? 115.983 117.804 102.143 1.00 61.41  0  349  GLU   A OE1 1 
ATOM   2381  O OE2 . GLU   A 1 385  ? 117.793 118.807 102.875 1.00 56.88  -1 349  GLU   A OE2 1 
ATOM   2382  N N   . ASP   A 1 386  ? 112.788 116.175 105.204 1.00 60.59  0  350  ASP   A N   1 
ATOM   2383  C CA  . ASP   A 1 386  ? 111.501 115.740 105.738 1.00 56.55  0  350  ASP   A CA  1 
ATOM   2384  C C   . ASP   A 1 386  ? 111.667 114.920 107.011 1.00 55.52  0  350  ASP   A C   1 
ATOM   2385  O O   . ASP   A 1 386  ? 111.016 115.193 108.025 1.00 56.89  0  350  ASP   A O   1 
ATOM   2386  C CB  . ASP   A 1 386  ? 110.746 114.940 104.680 1.00 58.92  0  350  ASP   A CB  1 
ATOM   2387  C CG  . ASP   A 1 386  ? 110.913 115.514 103.292 1.00 63.70  0  350  ASP   A CG  1 
ATOM   2388  O OD1 . ASP   A 1 386  ? 111.069 116.748 103.174 1.00 68.28  0  350  ASP   A OD1 1 
ATOM   2389  O OD2 . ASP   A 1 386  ? 110.890 114.733 102.318 1.00 60.15  -1 350  ASP   A OD2 1 
ATOM   2390  N N   . GLN   A 1 387  ? 112.535 113.909 106.978 1.00 52.74  0  351  GLN   A N   1 
ATOM   2391  C CA  . GLN   A 1 387  ? 112.593 112.954 108.080 1.00 52.24  0  351  GLN   A CA  1 
ATOM   2392  C C   . GLN   A 1 387  ? 113.089 113.609 109.364 1.00 57.35  0  351  GLN   A C   1 
ATOM   2393  O O   . GLN   A 1 387  ? 112.462 113.475 110.423 1.00 62.66  0  351  GLN   A O   1 
ATOM   2394  C CB  . GLN   A 1 387  ? 113.481 111.771 107.698 1.00 54.58  0  351  GLN   A CB  1 
ATOM   2395  C CG  . GLN   A 1 387  ? 112.937 110.934 106.552 1.00 57.13  0  351  GLN   A CG  1 
ATOM   2396  C CD  . GLN   A 1 387  ? 113.602 111.253 105.230 1.00 60.90  0  351  GLN   A CD  1 
ATOM   2397  O OE1 . GLN   A 1 387  ? 114.472 112.119 105.153 1.00 62.79  0  351  GLN   A OE1 1 
ATOM   2398  N NE2 . GLN   A 1 387  ? 113.195 110.553 104.180 1.00 60.26  0  351  GLN   A NE2 1 
ATOM   2399  N N   . PHE   A 1 388  ? 114.213 114.326 109.288 1.00 54.90  0  352  PHE   A N   1 
ATOM   2400  C CA  . PHE   A 1 388  ? 114.785 114.947 110.479 1.00 53.86  0  352  PHE   A CA  1 
ATOM   2401  C C   . PHE   A 1 388  ? 113.826 115.961 111.088 1.00 54.40  0  352  PHE   A C   1 
ATOM   2402  O O   . PHE   A 1 388  ? 113.594 115.965 112.304 1.00 52.36  0  352  PHE   A O   1 
ATOM   2403  C CB  . PHE   A 1 388  ? 116.111 115.622 110.134 1.00 53.03  0  352  PHE   A CB  1 
ATOM   2404  C CG  . PHE   A 1 388  ? 117.223 114.667 109.813 1.00 52.36  0  352  PHE   A CG  1 
ATOM   2405  C CD1 . PHE   A 1 388  ? 117.798 113.894 110.807 1.00 52.64  0  352  PHE   A CD1 1 
ATOM   2406  C CD2 . PHE   A 1 388  ? 117.714 114.565 108.526 1.00 48.85  0  352  PHE   A CD2 1 
ATOM   2407  C CE1 . PHE   A 1 388  ? 118.827 113.025 110.518 1.00 49.06  0  352  PHE   A CE1 1 
ATOM   2408  C CE2 . PHE   A 1 388  ? 118.741 113.699 108.233 1.00 54.51  0  352  PHE   A CE2 1 
ATOM   2409  C CZ  . PHE   A 1 388  ? 119.299 112.928 109.231 1.00 52.41  0  352  PHE   A CZ  1 
ATOM   2410  N N   . ARG   A 1 389  ? 113.256 116.834 110.253 1.00 48.18  0  353  ARG   A N   1 
ATOM   2411  C CA  . ARG   A 1 389  ? 112.396 117.885 110.779 1.00 44.20  0  353  ARG   A CA  1 
ATOM   2412  C C   . ARG   A 1 389  ? 111.087 117.323 111.315 1.00 51.06  0  353  ARG   A C   1 
ATOM   2413  O O   . ARG   A 1 389  ? 110.579 117.817 112.325 1.00 54.27  0  353  ARG   A O   1 
ATOM   2414  C CB  . ARG   A 1 389  ? 112.144 118.951 109.713 1.00 40.39  0  353  ARG   A CB  1 
ATOM   2415  C CG  . ARG   A 1 389  ? 110.995 118.679 108.770 1.00 46.12  0  353  ARG   A CG  1 
ATOM   2416  C CD  . ARG   A 1 389  ? 110.994 119.671 107.629 1.00 48.58  0  353  ARG   A CD  1 
ATOM   2417  N NE  . ARG   A 1 389  ? 109.876 119.455 106.722 1.00 53.77  0  353  ARG   A NE  1 
ATOM   2418  C CZ  . ARG   A 1 389  ? 109.738 120.058 105.550 1.00 55.44  0  353  ARG   A CZ  1 
ATOM   2419  N NH1 . ARG   A 1 389  ? 110.630 120.933 105.114 1.00 51.30  1  353  ARG   A NH1 1 
ATOM   2420  N NH2 . ARG   A 1 389  ? 108.681 119.775 104.796 1.00 52.62  0  353  ARG   A NH2 1 
ATOM   2421  N N   . LYS   A 1 390  ? 110.538 116.284 110.680 1.00 45.15  0  354  LYS   A N   1 
ATOM   2422  C CA  . LYS   A 1 390  ? 109.325 115.667 111.203 1.00 40.91  0  354  LYS   A CA  1 
ATOM   2423  C C   . LYS   A 1 390  ? 109.588 114.991 112.540 1.00 38.88  0  354  LYS   A C   1 
ATOM   2424  O O   . LYS   A 1 390  ? 108.780 115.106 113.470 1.00 50.30  0  354  LYS   A O   1 
ATOM   2425  C CB  . LYS   A 1 390  ? 108.767 114.666 110.194 1.00 44.28  0  354  LYS   A CB  1 
ATOM   2426  C CG  . LYS   A 1 390  ? 107.632 115.213 109.349 1.00 47.34  0  354  LYS   A CG  1 
ATOM   2427  C CD  . LYS   A 1 390  ? 107.772 114.791 107.897 1.00 50.86  0  354  LYS   A CD  1 
ATOM   2428  C CE  . LYS   A 1 390  ? 107.750 113.279 107.757 1.00 49.91  0  354  LYS   A CE  1 
ATOM   2429  N NZ  . LYS   A 1 390  ? 107.986 112.850 106.351 1.00 47.20  1  354  LYS   A NZ  1 
ATOM   2430  N N   . ARG   A 1 391  ? 110.716 114.290 112.658 1.00 36.16  0  355  ARG   A N   1 
ATOM   2431  C CA  . ARG   A 1 391  ? 111.059 113.659 113.925 1.00 41.60  0  355  ARG   A CA  1 
ATOM   2432  C C   . ARG   A 1 391  ? 111.229 114.696 115.027 1.00 44.50  0  355  ARG   A C   1 
ATOM   2433  O O   . ARG   A 1 391  ? 110.731 114.517 116.148 1.00 48.27  0  355  ARG   A O   1 
ATOM   2434  C CB  . ARG   A 1 391  ? 112.332 112.835 113.759 1.00 39.57  0  355  ARG   A CB  1 
ATOM   2435  C CG  . ARG   A 1 391  ? 112.628 111.906 114.906 1.00 37.26  0  355  ARG   A CG  1 
ATOM   2436  C CD  . ARG   A 1 391  ? 113.839 111.061 114.602 1.00 40.94  0  355  ARG   A CD  1 
ATOM   2437  N NE  . ARG   A 1 391  ? 113.983 109.963 115.546 1.00 41.43  0  355  ARG   A NE  1 
ATOM   2438  C CZ  . ARG   A 1 391  ? 114.562 110.072 116.732 1.00 45.13  0  355  ARG   A CZ  1 
ATOM   2439  N NH1 . ARG   A 1 391  ? 115.056 111.222 117.157 1.00 41.30  1  355  ARG   A NH1 1 
ATOM   2440  N NH2 . ARG   A 1 391  ? 114.647 109.000 117.512 1.00 51.29  0  355  ARG   A NH2 1 
ATOM   2441  N N   . PHE   A 1 392  ? 111.924 115.795 114.723 1.00 43.39  0  356  PHE   A N   1 
ATOM   2442  C CA  . PHE   A 1 392  ? 112.121 116.830 115.731 1.00 41.96  0  356  PHE   A CA  1 
ATOM   2443  C C   . PHE   A 1 392  ? 110.809 117.505 116.103 1.00 45.30  0  356  PHE   A C   1 
ATOM   2444  O O   . PHE   A 1 392  ? 110.579 117.804 117.275 1.00 46.50  0  356  PHE   A O   1 
ATOM   2445  C CB  . PHE   A 1 392  ? 113.134 117.863 115.247 1.00 41.66  0  356  PHE   A CB  1 
ATOM   2446  C CG  . PHE   A 1 392  ? 113.579 118.808 116.321 1.00 40.40  0  356  PHE   A CG  1 
ATOM   2447  C CD1 . PHE   A 1 392  ? 114.419 118.381 117.329 1.00 41.77  0  356  PHE   A CD1 1 
ATOM   2448  C CD2 . PHE   A 1 392  ? 113.150 120.119 116.327 1.00 32.18  0  356  PHE   A CD2 1 
ATOM   2449  C CE1 . PHE   A 1 392  ? 114.824 119.244 118.317 1.00 43.24  0  356  PHE   A CE1 1 
ATOM   2450  C CE2 . PHE   A 1 392  ? 113.554 120.985 117.313 1.00 32.10  0  356  PHE   A CE2 1 
ATOM   2451  C CZ  . PHE   A 1 392  ? 114.392 120.547 118.308 1.00 39.67  0  356  PHE   A CZ  1 
ATOM   2452  N N   . TYR   A 1 393  ? 109.936 117.754 115.124 1.00 44.68  0  357  TYR   A N   1 
ATOM   2453  C CA  . TYR   A 1 393  ? 108.641 118.361 115.416 1.00 40.60  0  357  TYR   A CA  1 
ATOM   2454  C C   . TYR   A 1 393  ? 107.803 117.465 116.318 1.00 37.07  0  357  TYR   A C   1 
ATOM   2455  O O   . TYR   A 1 393  ? 107.168 117.944 117.266 1.00 44.42  0  357  TYR   A O   1 
ATOM   2456  C CB  . TYR   A 1 393  ? 107.905 118.648 114.109 1.00 43.02  0  357  TYR   A CB  1 
ATOM   2457  C CG  . TYR   A 1 393  ? 106.812 119.687 114.202 1.00 46.48  0  357  TYR   A CG  1 
ATOM   2458  C CD1 . TYR   A 1 393  ? 105.516 119.330 114.537 1.00 45.89  0  357  TYR   A CD1 1 
ATOM   2459  C CD2 . TYR   A 1 393  ? 107.073 121.021 113.929 1.00 43.20  0  357  TYR   A CD2 1 
ATOM   2460  C CE1 . TYR   A 1 393  ? 104.512 120.275 114.612 1.00 41.66  0  357  TYR   A CE1 1 
ATOM   2461  C CE2 . TYR   A 1 393  ? 106.078 121.972 114.001 1.00 42.62  0  357  TYR   A CE2 1 
ATOM   2462  C CZ  . TYR   A 1 393  ? 104.799 121.594 114.343 1.00 44.99  0  357  TYR   A CZ  1 
ATOM   2463  O OH  . TYR   A 1 393  ? 103.803 122.540 114.416 1.00 44.99  0  357  TYR   A OH  1 
ATOM   2464  N N   . ASN   A 1 394  ? 107.789 116.160 116.042 1.00 34.50  0  358  ASN   A N   1 
ATOM   2465  C CA  . ASN   A 1 394  ? 107.015 115.248 116.877 1.00 38.71  0  358  ASN   A CA  1 
ATOM   2466  C C   . ASN   A 1 394  ? 107.577 115.171 118.292 1.00 40.86  0  358  ASN   A C   1 
ATOM   2467  O O   . ASN   A 1 394  ? 106.817 115.204 119.269 1.00 50.44  0  358  ASN   A O   1 
ATOM   2468  C CB  . ASN   A 1 394  ? 106.967 113.865 116.236 1.00 41.70  0  358  ASN   A CB  1 
ATOM   2469  C CG  . ASN   A 1 394  ? 106.146 113.846 114.965 1.00 43.38  0  358  ASN   A CG  1 
ATOM   2470  O OD1 . ASN   A 1 394  ? 105.529 114.844 114.596 1.00 37.46  0  358  ASN   A OD1 1 
ATOM   2471  N ND2 . ASN   A 1 394  ? 106.128 112.704 114.291 1.00 46.38  0  358  ASN   A ND2 1 
ATOM   2472  N N   . SER   A 1 395  ? 108.902 115.073 118.429 1.00 32.69  0  359  SER   A N   1 
ATOM   2473  C CA  . SER   A 1 395  ? 109.476 115.043 119.771 1.00 39.39  0  359  SER   A CA  1 
ATOM   2474  C C   . SER   A 1 395  ? 109.258 116.362 120.500 1.00 44.23  0  359  SER   A C   1 
ATOM   2475  O O   . SER   A 1 395  ? 109.063 116.372 121.718 1.00 44.36  0  359  SER   A O   1 
ATOM   2476  C CB  . SER   A 1 395  ? 110.963 114.709 119.711 1.00 46.96  0  359  SER   A CB  1 
ATOM   2477  O OG  . SER   A 1 395  ? 111.488 114.547 121.017 1.00 47.20  0  359  SER   A OG  1 
ATOM   2478  N N   . MET   A 1 396  ? 109.278 117.475 119.769 1.00 45.15  0  360  MET   A N   1 
ATOM   2479  C CA  . MET   A 1 396  ? 108.977 118.780 120.345 1.00 39.16  0  360  MET   A CA  1 
ATOM   2480  C C   . MET   A 1 396  ? 107.564 118.829 120.903 1.00 40.49  0  360  MET   A C   1 
ATOM   2481  O O   . MET   A 1 396  ? 107.344 119.299 122.025 1.00 39.15  0  360  MET   A O   1 
ATOM   2482  C CB  . MET   A 1 396  ? 109.185 119.847 119.271 1.00 33.17  0  360  MET   A CB  1 
ATOM   2483  C CG  . MET   A 1 396  ? 108.720 121.244 119.601 1.00 39.64  0  360  MET   A CG  1 
ATOM   2484  S SD  . MET   A 1 396  ? 106.965 121.444 119.233 1.00 60.52  0  360  MET   A SD  1 
ATOM   2485  C CE  . MET   A 1 396  ? 107.046 122.330 117.687 1.00 43.23  0  360  MET   A CE  1 
ATOM   2486  N N   . LEU   A 1 397  ? 106.585 118.376 120.119 1.00 39.71  0  361  LEU   A N   1 
ATOM   2487  C CA  . LEU   A 1 397  ? 105.206 118.390 120.596 1.00 29.23  0  361  LEU   A CA  1 
ATOM   2488  C C   . LEU   A 1 397  ? 105.042 117.488 121.809 1.00 32.81  0  361  LEU   A C   1 
ATOM   2489  O O   . LEU   A 1 397  ? 104.365 117.854 122.781 1.00 46.09  0  361  LEU   A O   1 
ATOM   2490  C CB  . LEU   A 1 397  ? 104.258 117.969 119.480 1.00 31.01  0  361  LEU   A CB  1 
ATOM   2491  C CG  . LEU   A 1 397  ? 103.959 119.069 118.466 1.00 36.30  0  361  LEU   A CG  1 
ATOM   2492  C CD1 . LEU   A 1 397  ? 103.078 118.540 117.358 1.00 44.20  0  361  LEU   A CD1 1 
ATOM   2493  C CD2 . LEU   A 1 397  ? 103.309 120.252 119.151 1.00 38.80  0  361  LEU   A CD2 1 
ATOM   2494  N N   . ASN   A 1 398  ? 105.662 116.306 121.775 1.00 35.55  0  362  ASN   A N   1 
ATOM   2495  C CA  . ASN   A 1 398  ? 105.595 115.416 122.928 1.00 40.96  0  362  ASN   A CA  1 
ATOM   2496  C C   . ASN   A 1 398  ? 106.191 116.078 124.161 1.00 39.44  0  362  ASN   A C   1 
ATOM   2497  O O   . ASN   A 1 398  ? 105.623 115.993 125.255 1.00 44.26  0  362  ASN   A O   1 
ATOM   2498  C CB  . ASN   A 1 398  ? 106.316 114.103 122.629 1.00 44.85  0  362  ASN   A CB  1 
ATOM   2499  C CG  . ASN   A 1 398  ? 105.590 113.259 121.608 1.00 44.67  0  362  ASN   A CG  1 
ATOM   2500  O OD1 . ASN   A 1 398  ? 104.453 113.548 121.245 1.00 47.65  0  362  ASN   A OD1 1 
ATOM   2501  N ND2 . ASN   A 1 398  ? 106.241 112.202 121.146 1.00 39.40  0  362  ASN   A ND2 1 
ATOM   2502  N N   . ASN   A 1 399  ? 107.329 116.757 124.001 1.00 39.20  0  363  ASN   A N   1 
ATOM   2503  C CA  . ASN   A 1 399  ? 107.968 117.427 125.129 1.00 41.90  0  363  ASN   A CA  1 
ATOM   2504  C C   . ASN   A 1 399  ? 107.089 118.538 125.686 1.00 41.08  0  363  ASN   A C   1 
ATOM   2505  O O   . ASN   A 1 399  ? 106.924 118.660 126.904 1.00 42.12  0  363  ASN   A O   1 
ATOM   2506  C CB  . ASN   A 1 399  ? 109.324 117.982 124.700 1.00 46.42  0  363  ASN   A CB  1 
ATOM   2507  C CG  . ASN   A 1 399  ? 110.477 117.190 125.265 1.00 50.32  0  363  ASN   A CG  1 
ATOM   2508  O OD1 . ASN   A 1 399  ? 110.279 116.253 126.038 1.00 54.25  0  363  ASN   A OD1 1 
ATOM   2509  N ND2 . ASN   A 1 399  ? 111.693 117.560 124.885 1.00 47.36  0  363  ASN   A ND2 1 
ATOM   2510  N N   . ILE   A 1 400  ? 106.513 119.359 124.806 1.00 38.74  0  364  ILE   A N   1 
ATOM   2511  C CA  . ILE   A 1 400  ? 105.702 120.486 125.262 1.00 36.47  0  364  ILE   A CA  1 
ATOM   2512  C C   . ILE   A 1 400  ? 104.487 119.990 126.033 1.00 37.40  0  364  ILE   A C   1 
ATOM   2513  O O   . ILE   A 1 400  ? 104.172 120.485 127.123 1.00 35.89  0  364  ILE   A O   1 
ATOM   2514  C CB  . ILE   A 1 400  ? 105.286 121.370 124.073 1.00 31.96  0  364  ILE   A CB  1 
ATOM   2515  C CG1 . ILE   A 1 400  ? 106.497 122.085 123.488 1.00 35.64  0  364  ILE   A CG1 1 
ATOM   2516  C CG2 . ILE   A 1 400  ? 104.253 122.384 124.503 1.00 30.27  0  364  ILE   A CG2 1 
ATOM   2517  C CD1 . ILE   A 1 400  ? 106.153 122.991 122.340 1.00 36.77  0  364  ILE   A CD1 1 
ATOM   2518  N N   . THR   A 1 401  ? 103.792 118.993 125.487 1.00 36.94  0  365  THR   A N   1 
ATOM   2519  C CA  . THR   A 1 401  ? 102.581 118.534 126.153 1.00 29.55  0  365  THR   A CA  1 
ATOM   2520  C C   . THR   A 1 401  ? 102.879 117.728 127.411 1.00 30.50  0  365  THR   A C   1 
ATOM   2521  O O   . THR   A 1 401  ? 102.114 117.803 128.378 1.00 40.12  0  365  THR   A O   1 
ATOM   2522  C CB  . THR   A 1 401  ? 101.727 117.732 125.182 1.00 39.89  0  365  THR   A CB  1 
ATOM   2523  O OG1 . THR   A 1 401  ? 102.522 116.703 124.586 1.00 47.56  0  365  THR   A OG1 1 
ATOM   2524  C CG2 . THR   A 1 401  ? 101.206 118.654 124.101 1.00 31.82  0  365  THR   A CG2 1 
ATOM   2525  N N   . ASP   A 1 402  ? 103.977 116.969 127.438 1.00 28.77  0  366  ASP   A N   1 
ATOM   2526  C CA  . ASP   A 1 402  ? 104.366 116.312 128.678 1.00 30.16  0  366  ASP   A CA  1 
ATOM   2527  C C   . ASP   A 1 402  ? 104.747 117.325 129.746 1.00 37.06  0  366  ASP   A C   1 
ATOM   2528  O O   . ASP   A 1 402  ? 104.440 117.123 130.925 1.00 42.93  0  366  ASP   A O   1 
ATOM   2529  C CB  . ASP   A 1 402  ? 105.516 115.340 128.424 1.00 37.60  0  366  ASP   A CB  1 
ATOM   2530  C CG  . ASP   A 1 402  ? 105.050 113.897 128.340 1.00 48.90  0  366  ASP   A CG  1 
ATOM   2531  O OD1 . ASP   A 1 402  ? 103.888 113.624 128.707 1.00 49.17  0  366  ASP   A OD1 1 
ATOM   2532  O OD2 . ASP   A 1 402  ? 105.847 113.036 127.913 1.00 46.75  -1 366  ASP   A OD2 1 
ATOM   2533  N N   . ALA   A 1 403  ? 105.407 118.420 129.358 1.00 40.05  0  367  ALA   A N   1 
ATOM   2534  C CA  . ALA   A 1 403  ? 105.697 119.486 130.310 1.00 32.85  0  367  ALA   A CA  1 
ATOM   2535  C C   . ALA   A 1 403  ? 104.417 120.115 130.838 1.00 38.07  0  367  ALA   A C   1 
ATOM   2536  O O   . ALA   A 1 403  ? 104.305 120.396 132.036 1.00 38.89  0  367  ALA   A O   1 
ATOM   2537  C CB  . ALA   A 1 403  ? 106.583 120.544 129.657 1.00 30.32  0  367  ALA   A CB  1 
ATOM   2538  N N   . ALA   A 1 404  ? 103.439 120.345 129.959 1.00 39.56  0  368  ALA   A N   1 
ATOM   2539  C CA  . ALA   A 1 404  ? 102.168 120.913 130.402 1.00 31.56  0  368  ALA   A CA  1 
ATOM   2540  C C   . ALA   A 1 404  ? 101.455 119.987 131.380 1.00 27.42  0  368  ALA   A C   1 
ATOM   2541  O O   . ALA   A 1 404  ? 100.935 120.436 132.409 1.00 34.51  0  368  ALA   A O   1 
ATOM   2542  C CB  . ALA   A 1 404  ? 101.279 121.211 129.198 1.00 28.35  0  368  ALA   A CB  1 
ATOM   2543  N N   . ASN   A 1 405  ? 101.421 118.688 131.077 1.00 31.31  0  369  ASN   A N   1 
ATOM   2544  C CA  . ASN   A 1 405  ? 100.776 117.737 131.977 1.00 36.20  0  369  ASN   A CA  1 
ATOM   2545  C C   . ASN   A 1 405  ? 101.504 117.654 133.313 1.00 43.28  0  369  ASN   A C   1 
ATOM   2546  O O   . ASN   A 1 405  ? 100.864 117.586 134.371 1.00 56.44  0  369  ASN   A O   1 
ATOM   2547  C CB  . ASN   A 1 405  ? 100.699 116.361 131.322 1.00 36.87  0  369  ASN   A CB  1 
ATOM   2548  C CG  . ASN   A 1 405  ? 99.782  116.343 130.122 1.00 42.19  0  369  ASN   A CG  1 
ATOM   2549  O OD1 . ASN   A 1 405  ? 98.864  117.152 130.020 1.00 40.06  0  369  ASN   A OD1 1 
ATOM   2550  N ND2 . ASN   A 1 405  ? 100.028 115.419 129.203 1.00 38.56  0  369  ASN   A ND2 1 
ATOM   2551  N N   . LYS   A 1 406  ? 102.839 117.656 133.289 1.00 36.90  0  370  LYS   A N   1 
ATOM   2552  C CA  . LYS   A 1 406  ? 103.596 117.640 134.536 1.00 41.20  0  370  LYS   A CA  1 
ATOM   2553  C C   . LYS   A 1 406  ? 103.333 118.894 135.357 1.00 38.97  0  370  LYS   A C   1 
ATOM   2554  O O   . LYS   A 1 406  ? 103.189 118.823 136.581 1.00 35.14  0  370  LYS   A O   1 
ATOM   2555  C CB  . LYS   A 1 406  ? 105.088 117.493 134.243 1.00 40.49  0  370  LYS   A CB  1 
ATOM   2556  C CG  . LYS   A 1 406  ? 105.967 117.630 135.471 1.00 39.31  0  370  LYS   A CG  1 
ATOM   2557  C CD  . LYS   A 1 406  ? 107.143 116.673 135.434 1.00 47.36  0  370  LYS   A CD  1 
ATOM   2558  C CE  . LYS   A 1 406  ? 108.193 117.058 136.461 1.00 44.94  0  370  LYS   A CE  1 
ATOM   2559  N NZ  . LYS   A 1 406  ? 108.919 118.298 136.073 1.00 42.92  1  370  LYS   A NZ  1 
ATOM   2560  N N   . ALA   A 1 407  ? 103.263 120.053 134.700 1.00 34.30  0  371  ALA   A N   1 
ATOM   2561  C CA  . ALA   A 1 407  ? 102.976 121.296 135.408 1.00 39.95  0  371  ALA   A CA  1 
ATOM   2562  C C   . ALA   A 1 407  ? 101.599 121.254 136.052 1.00 38.43  0  371  ALA   A C   1 
ATOM   2563  O O   . ALA   A 1 407  ? 101.429 121.651 137.212 1.00 39.23  0  371  ALA   A O   1 
ATOM   2564  C CB  . ALA   A 1 407  ? 103.083 122.479 134.448 1.00 40.51  0  371  ALA   A CB  1 
ATOM   2565  N N   . GLN   A 1 408  ? 100.598 120.780 135.309 1.00 36.34  0  372  GLN   A N   1 
ATOM   2566  C CA  . GLN   A 1 408  ? 99.250  120.689 135.859 1.00 35.68  0  372  GLN   A CA  1 
ATOM   2567  C C   . GLN   A 1 408  ? 99.214  119.760 137.065 1.00 32.18  0  372  GLN   A C   1 
ATOM   2568  O O   . GLN   A 1 408  ? 98.654  120.104 138.114 1.00 43.42  0  372  GLN   A O   1 
ATOM   2569  C CB  . GLN   A 1 408  ? 98.278  120.212 134.784 1.00 38.49  0  372  GLN   A CB  1 
ATOM   2570  C CG  . GLN   A 1 408  ? 97.015  119.600 135.342 1.00 42.58  0  372  GLN   A CG  1 
ATOM   2571  C CD  . GLN   A 1 408  ? 96.119  119.040 134.263 1.00 48.65  0  372  GLN   A CD  1 
ATOM   2572  O OE1 . GLN   A 1 408  ? 96.370  119.227 133.074 1.00 48.04  0  372  GLN   A OE1 1 
ATOM   2573  N NE2 . GLN   A 1 408  ? 95.068  118.344 134.673 1.00 49.97  0  372  GLN   A NE2 1 
ATOM   2574  N N   . LYS   A 1 409  ? 99.823  118.581 136.937 1.00 25.99  0  373  LYS   A N   1 
ATOM   2575  C CA  . LYS   A 1 409  ? 99.840  117.636 138.047 1.00 33.82  0  373  LYS   A CA  1 
ATOM   2576  C C   . LYS   A 1 409  ? 100.543 118.229 139.261 1.00 41.12  0  373  LYS   A C   1 
ATOM   2577  O O   . LYS   A 1 409  ? 100.056 118.115 140.392 1.00 49.71  0  373  LYS   A O   1 
ATOM   2578  C CB  . LYS   A 1 409  ? 100.516 116.335 137.613 1.00 38.63  0  373  LYS   A CB  1 
ATOM   2579  C CG  . LYS   A 1 409  ? 100.940 115.446 138.768 1.00 37.33  0  373  LYS   A CG  1 
ATOM   2580  C CD  . LYS   A 1 409  ? 101.709 114.232 138.286 1.00 41.02  0  373  LYS   A CD  1 
ATOM   2581  C CE  . LYS   A 1 409  ? 102.183 113.386 139.457 1.00 42.02  0  373  LYS   A CE  1 
ATOM   2582  N NZ  . LYS   A 1 409  ? 102.862 112.135 139.018 1.00 45.23  1  373  LYS   A NZ  1 
ATOM   2583  N N   . ASN   A 1 410  ? 101.689 118.881 139.043 1.00 32.12  0  374  ASN   A N   1 
ATOM   2584  C CA  . ASN   A 1 410  ? 102.445 119.440 140.157 1.00 32.24  0  374  ASN   A CA  1 
ATOM   2585  C C   . ASN   A 1 410  ? 101.673 120.543 140.863 1.00 40.81  0  374  ASN   A C   1 
ATOM   2586  O O   . ASN   A 1 410  ? 101.633 120.578 142.096 1.00 40.96  0  374  ASN   A O   1 
ATOM   2587  C CB  . ASN   A 1 410  ? 103.793 119.969 139.674 1.00 38.96  0  374  ASN   A CB  1 
ATOM   2588  C CG  . ASN   A 1 410  ? 104.798 118.868 139.434 1.00 47.05  0  374  ASN   A CG  1 
ATOM   2589  O OD1 . ASN   A 1 410  ? 105.283 118.690 138.322 1.00 47.78  0  374  ASN   A OD1 1 
ATOM   2590  N ND2 . ASN   A 1 410  ? 105.118 118.121 140.484 1.00 45.79  0  374  ASN   A ND2 1 
ATOM   2591  N N   . LEU   A 1 411  ? 101.058 121.459 140.111 1.00 39.14  0  375  LEU   A N   1 
ATOM   2592  C CA  . LEU   A 1 411  ? 100.352 122.550 140.773 1.00 27.87  0  375  LEU   A CA  1 
ATOM   2593  C C   . LEU   A 1 411  ? 99.123  122.037 141.509 1.00 29.43  0  375  LEU   A C   1 
ATOM   2594  O O   . LEU   A 1 411  ? 98.826  122.495 142.620 1.00 41.44  0  375  LEU   A O   1 
ATOM   2595  C CB  . LEU   A 1 411  ? 99.978  123.647 139.775 1.00 32.96  0  375  LEU   A CB  1 
ATOM   2596  C CG  . LEU   A 1 411  ? 98.898  123.457 138.716 1.00 40.93  0  375  LEU   A CG  1 
ATOM   2597  C CD1 . LEU   A 1 411  ? 97.573  123.962 139.238 1.00 36.98  0  375  LEU   A CD1 1 
ATOM   2598  C CD2 . LEU   A 1 411  ? 99.276  124.201 137.456 1.00 50.53  0  375  LEU   A CD2 1 
ATOM   2599  N N   . LEU   A 1 412  ? 98.402  121.076 140.921 1.00 34.53  0  376  LEU   A N   1 
ATOM   2600  C CA  . LEU   A 1 412  ? 97.239  120.529 141.608 1.00 25.60  0  376  LEU   A CA  1 
ATOM   2601  C C   . LEU   A 1 412  ? 97.636  119.771 142.866 1.00 26.47  0  376  LEU   A C   1 
ATOM   2602  O O   . LEU   A 1 412  ? 96.907  119.806 143.862 1.00 26.85  0  376  LEU   A O   1 
ATOM   2603  C CB  . LEU   A 1 412  ? 96.446  119.627 140.665 1.00 29.01  0  376  LEU   A CB  1 
ATOM   2604  C CG  . LEU   A 1 412  ? 95.681  120.368 139.569 1.00 32.96  0  376  LEU   A CG  1 
ATOM   2605  C CD1 . LEU   A 1 412  ? 95.054  119.391 138.596 1.00 34.83  0  376  LEU   A CD1 1 
ATOM   2606  C CD2 . LEU   A 1 412  ? 94.628  121.271 140.177 1.00 31.69  0  376  LEU   A CD2 1 
ATOM   2607  N N   . SER   A 1 413  ? 98.778  119.084 142.849 1.00 29.36  0  377  SER   A N   1 
ATOM   2608  C CA  . SER   A 1 413  ? 99.238  118.391 144.045 1.00 32.02  0  377  SER   A CA  1 
ATOM   2609  C C   . SER   A 1 413  ? 99.890  119.322 145.056 1.00 35.11  0  377  SER   A C   1 
ATOM   2610  O O   . SER   A 1 413  ? 100.031 118.944 146.224 1.00 32.60  0  377  SER   A O   1 
ATOM   2611  C CB  . SER   A 1 413  ? 100.224 117.285 143.669 1.00 38.91  0  377  SER   A CB  1 
ATOM   2612  O OG  . SER   A 1 413  ? 100.867 116.770 144.821 1.00 40.47  0  377  SER   A OG  1 
ATOM   2613  N N   . ARG   A 1 414  ? 100.299 120.519 144.636 1.00 41.66  0  378  ARG   A N   1 
ATOM   2614  C CA  . ARG   A 1 414  ? 100.959 121.467 145.524 1.00 35.56  0  378  ARG   A CA  1 
ATOM   2615  C C   . ARG   A 1 414  ? 99.975  122.384 146.236 1.00 37.74  0  378  ARG   A C   1 
ATOM   2616  O O   . ARG   A 1 414  ? 100.164 122.692 147.416 1.00 36.15  0  378  ARG   A O   1 
ATOM   2617  C CB  . ARG   A 1 414  ? 101.969 122.303 144.733 1.00 27.31  0  378  ARG   A CB  1 
ATOM   2618  C CG  . ARG   A 1 414  ? 102.625 123.411 145.531 1.00 32.53  0  378  ARG   A CG  1 
ATOM   2619  C CD  . ARG   A 1 414  ? 103.686 124.132 144.717 1.00 35.36  0  378  ARG   A CD  1 
ATOM   2620  N NE  . ARG   A 1 414  ? 103.114 124.938 143.647 1.00 37.52  0  378  ARG   A NE  1 
ATOM   2621  C CZ  . ARG   A 1 414  ? 102.627 126.160 143.809 1.00 30.17  0  378  ARG   A CZ  1 
ATOM   2622  N NH1 . ARG   A 1 414  ? 102.618 126.748 144.993 1.00 32.04  1  378  ARG   A NH1 1 
ATOM   2623  N NH2 . ARG   A 1 414  ? 102.137 126.808 142.757 1.00 19.06  0  378  ARG   A NH2 1 
ATOM   2624  N N   . VAL   A 1 415  ? 98.916  122.812 145.551 1.00 40.51  0  379  VAL   A N   1 
ATOM   2625  C CA  . VAL   A 1 415  ? 97.964  123.752 146.134 1.00 33.57  0  379  VAL   A CA  1 
ATOM   2626  C C   . VAL   A 1 415  ? 96.846  122.995 146.839 1.00 38.70  0  379  VAL   A C   1 
ATOM   2627  O O   . VAL   A 1 415  ? 95.798  123.568 147.156 1.00 44.18  0  379  VAL   A O   1 
ATOM   2628  C CB  . VAL   A 1 415  ? 97.396  124.703 145.067 1.00 28.16  0  379  VAL   A CB  1 
ATOM   2629  C CG1 . VAL   A 1 415  ? 98.518  125.344 144.282 1.00 37.17  0  379  VAL   A CG1 1 
ATOM   2630  C CG2 . VAL   A 1 415  ? 96.460  123.962 144.142 1.00 32.66  0  379  VAL   A CG2 1 
ATOM   2631  N N   . CYS   A 1 416  ? 97.063  121.704 147.096 1.00 44.77  0  380  CYS   A N   1 
ATOM   2632  C CA  . CYS   A 1 416  ? 96.006  120.871 147.662 1.00 52.53  0  380  CYS   A CA  1 
ATOM   2633  C C   . CYS   A 1 416  ? 95.567  121.375 149.031 1.00 54.75  0  380  CYS   A C   1 
ATOM   2634  O O   . CYS   A 1 416  ? 94.368  121.455 149.320 1.00 53.61  0  380  CYS   A O   1 
ATOM   2635  C CB  . CYS   A 1 416  ? 96.479  119.421 147.758 1.00 54.39  0  380  CYS   A CB  1 
ATOM   2636  S SG  . CYS   A 1 416  ? 97.723  119.130 149.038 1.00 61.79  0  380  CYS   A SG  1 
ATOM   2637  N N   . HIS   A 1 417  ? 96.525  121.722 149.892 1.00 51.86  0  381  HIS   A N   1 
ATOM   2638  C CA  . HIS   A 1 417  ? 96.226  122.084 151.274 1.00 53.54  0  381  HIS   A CA  1 
ATOM   2639  C C   . HIS   A 1 417  ? 96.729  123.476 151.639 1.00 53.32  0  381  HIS   A C   1 
ATOM   2640  O O   . HIS   A 1 417  ? 96.794  123.814 152.824 1.00 53.46  0  381  HIS   A O   1 
ATOM   2641  C CB  . HIS   A 1 417  ? 96.812  121.049 152.234 1.00 52.57  0  381  HIS   A CB  1 
ATOM   2642  C CG  . HIS   A 1 417  ? 95.921  119.870 152.470 1.00 56.45  0  381  HIS   A CG  1 
ATOM   2643  N ND1 . HIS   A 1 417  ? 95.470  119.063 151.448 1.00 55.60  0  381  HIS   A ND1 1 
ATOM   2644  C CD2 . HIS   A 1 417  ? 95.394  119.364 153.609 1.00 55.30  0  381  HIS   A CD2 1 
ATOM   2645  C CE1 . HIS   A 1 417  ? 94.706  118.109 151.948 1.00 54.97  0  381  HIS   A CE1 1 
ATOM   2646  N NE2 . HIS   A 1 417  ? 94.644  118.269 153.257 1.00 56.53  0  381  HIS   A NE2 1 
ATOM   2647  N N   . THR   A 1 418  ? 97.082  124.291 150.655 1.00 46.39  0  382  THR   A N   1 
ATOM   2648  C CA  . THR   A 1 418  ? 97.599  125.624 150.920 1.00 34.86  0  382  THR   A CA  1 
ATOM   2649  C C   . THR   A 1 418  ? 96.430  126.605 151.001 1.00 27.46  0  382  THR   A C   1 
ATOM   2650  O O   . THR   A 1 418  ? 95.267  126.199 151.048 1.00 39.97  0  382  THR   A O   1 
ATOM   2651  C CB  . THR   A 1 418  ? 98.609  126.014 149.841 1.00 42.87  0  382  THR   A CB  1 
ATOM   2652  O OG1 . THR   A 1 418  ? 97.934  126.161 148.588 1.00 44.48  0  382  THR   A OG1 1 
ATOM   2653  C CG2 . THR   A 1 418  ? 99.671  124.941 149.708 1.00 42.01  0  382  THR   A CG2 1 
ATOM   2654  N N   . LEU   A 1 419  ? 96.723  127.902 151.029 1.00 31.47  0  383  LEU   A N   1 
ATOM   2655  C CA  . LEU   A 1 419  ? 95.705  128.940 150.984 1.00 36.25  0  383  LEU   A CA  1 
ATOM   2656  C C   . LEU   A 1 419  ? 95.334  129.331 149.564 1.00 32.95  0  383  LEU   A C   1 
ATOM   2657  O O   . LEU   A 1 419  ? 94.476  130.198 149.377 1.00 21.76  0  383  LEU   A O   1 
ATOM   2658  C CB  . LEU   A 1 419  ? 96.178  130.178 151.751 1.00 31.57  0  383  LEU   A CB  1 
ATOM   2659  C CG  . LEU   A 1 419  ? 96.232  130.053 153.272 1.00 30.65  0  383  LEU   A CG  1 
ATOM   2660  C CD1 . LEU   A 1 419  ? 97.189  131.071 153.847 1.00 31.91  0  383  LEU   A CD1 1 
ATOM   2661  C CD2 . LEU   A 1 419  ? 94.850  130.231 153.865 1.00 32.46  0  383  LEU   A CD2 1 
ATOM   2662  N N   . LEU   A 1 420  ? 95.964  128.719 148.563 1.00 35.42  0  384  LEU   A N   1 
ATOM   2663  C CA  . LEU   A 1 420  ? 95.688  129.004 147.163 1.00 37.57  0  384  LEU   A CA  1 
ATOM   2664  C C   . LEU   A 1 420  ? 94.876  127.903 146.494 1.00 41.96  0  384  LEU   A C   1 
ATOM   2665  O O   . LEU   A 1 420  ? 94.828  127.844 145.262 1.00 44.09  0  384  LEU   A O   1 
ATOM   2666  C CB  . LEU   A 1 420  ? 96.996  129.224 146.402 1.00 30.65  0  384  LEU   A CB  1 
ATOM   2667  C CG  . LEU   A 1 420  ? 97.938  130.296 146.946 1.00 27.64  0  384  LEU   A CG  1 
ATOM   2668  C CD1 . LEU   A 1 420  ? 99.225  130.310 146.160 1.00 31.14  0  384  LEU   A CD1 1 
ATOM   2669  C CD2 . LEU   A 1 420  ? 97.273  131.648 146.889 1.00 35.97  0  384  LEU   A CD2 1 
ATOM   2670  N N   . ASP   A 1 421  ? 94.239  127.028 147.278 1.00 40.39  0  385  ASP   A N   1 
ATOM   2671  C CA  . ASP   A 1 421  ? 93.483  125.925 146.697 1.00 39.60  0  385  ASP   A CA  1 
ATOM   2672  C C   . ASP   A 1 421  ? 92.300  126.418 145.875 1.00 42.96  0  385  ASP   A C   1 
ATOM   2673  O O   . ASP   A 1 421  ? 91.871  125.737 144.937 1.00 48.03  0  385  ASP   A O   1 
ATOM   2674  C CB  . ASP   A 1 421  ? 93.012  124.975 147.798 1.00 39.94  0  385  ASP   A CB  1 
ATOM   2675  C CG  . ASP   A 1 421  ? 92.176  125.670 148.846 1.00 46.75  0  385  ASP   A CG  1 
ATOM   2676  O OD1 . ASP   A 1 421  ? 92.504  126.819 149.203 1.00 41.04  0  385  ASP   A OD1 1 
ATOM   2677  O OD2 . ASP   A 1 421  ? 91.192  125.066 149.320 1.00 50.93  -1 385  ASP   A OD2 1 
ATOM   2678  N N   . LYS   A 1 422  ? 91.762  127.590 146.202 1.00 35.51  0  386  LYS   A N   1 
ATOM   2679  C CA  . LYS   A 1 422  ? 90.669  128.159 145.427 1.00 35.55  0  386  LYS   A CA  1 
ATOM   2680  C C   . LYS   A 1 422  ? 91.149  128.949 144.220 1.00 37.25  0  386  LYS   A C   1 
ATOM   2681  O O   . LYS   A 1 422  ? 90.316  129.409 143.433 1.00 44.43  0  386  LYS   A O   1 
ATOM   2682  C CB  . LYS   A 1 422  ? 89.810  129.063 146.313 1.00 39.92  0  386  LYS   A CB  1 
ATOM   2683  C CG  . LYS   A 1 422  ? 89.151  128.351 147.481 1.00 45.00  0  386  LYS   A CG  1 
ATOM   2684  C CD  . LYS   A 1 422  ? 88.159  127.306 146.999 1.00 45.36  0  386  LYS   A CD  1 
ATOM   2685  C CE  . LYS   A 1 422  ? 87.299  126.796 148.141 1.00 45.55  0  386  LYS   A CE  1 
ATOM   2686  N NZ  . LYS   A 1 422  ? 88.094  126.026 149.133 1.00 45.63  1  386  LYS   A NZ  1 
ATOM   2687  N N   . THR   A 1 423  ? 92.461  129.119 144.055 1.00 39.21  0  387  THR   A N   1 
ATOM   2688  C CA  . THR   A 1 423  ? 92.987  129.975 143.001 1.00 41.47  0  387  THR   A CA  1 
ATOM   2689  C C   . THR   A 1 423  ? 93.136  129.264 141.664 1.00 42.21  0  387  THR   A C   1 
ATOM   2690  O O   . THR   A 1 423  ? 93.363  129.932 140.650 1.00 41.76  0  387  THR   A O   1 
ATOM   2691  C CB  . THR   A 1 423  ? 94.344  130.545 143.416 1.00 39.36  0  387  THR   A CB  1 
ATOM   2692  O OG1 . THR   A 1 423  ? 95.264  129.471 143.639 1.00 41.03  0  387  THR   A OG1 1 
ATOM   2693  C CG2 . THR   A 1 423  ? 94.208  131.352 144.690 1.00 34.16  0  387  THR   A CG2 1 
ATOM   2694  N N   . VAL   A 1 424  ? 93.013  127.937 141.631 1.00 44.52  0  388  VAL   A N   1 
ATOM   2695  C CA  . VAL   A 1 424  ? 93.224  127.201 140.391 1.00 41.30  0  388  VAL   A CA  1 
ATOM   2696  C C   . VAL   A 1 424  ? 92.087  127.494 139.426 1.00 44.88  0  388  VAL   A C   1 
ATOM   2697  O O   . VAL   A 1 424  ? 90.906  127.388 139.780 1.00 48.87  0  388  VAL   A O   1 
ATOM   2698  C CB  . VAL   A 1 424  ? 93.341  125.697 140.668 1.00 33.78  0  388  VAL   A CB  1 
ATOM   2699  C CG1 . VAL   A 1 424  ? 93.481  124.938 139.365 1.00 31.12  0  388  VAL   A CG1 1 
ATOM   2700  C CG2 . VAL   A 1 424  ? 94.519  125.422 141.570 1.00 36.51  0  388  VAL   A CG2 1 
ATOM   2701  N N   . SER   A 1 425  ? 92.439  127.868 138.201 1.00 46.11  0  389  SER   A N   1 
ATOM   2702  C CA  . SER   A 1 425  ? 91.434  128.176 137.200 1.00 47.16  0  389  SER   A CA  1 
ATOM   2703  C C   . SER   A 1 425  ? 90.652  126.921 136.831 1.00 48.63  0  389  SER   A C   1 
ATOM   2704  O O   . SER   A 1 425  ? 91.140  125.795 136.944 1.00 47.79  0  389  SER   A O   1 
ATOM   2705  C CB  . SER   A 1 425  ? 92.088  128.771 135.955 1.00 47.56  0  389  SER   A CB  1 
ATOM   2706  O OG  . SER   A 1 425  ? 91.150  128.910 134.906 1.00 45.23  0  389  SER   A OG  1 
ATOM   2707  N N   . ASP   A 1 426  ? 89.407  127.126 136.403 1.00 53.72  0  390  ASP   A N   1 
ATOM   2708  C CA  . ASP   A 1 426  ? 88.603  126.018 135.908 1.00 54.03  0  390  ASP   A CA  1 
ATOM   2709  C C   . ASP   A 1 426  ? 89.088  125.505 134.561 1.00 51.72  0  390  ASP   A C   1 
ATOM   2710  O O   . ASP   A 1 426  ? 88.705  124.400 134.165 1.00 52.09  0  390  ASP   A O   1 
ATOM   2711  C CB  . ASP   A 1 426  ? 87.135  126.431 135.804 1.00 53.02  0  390  ASP   A CB  1 
ATOM   2712  C CG  . ASP   A 1 426  ? 86.941  127.693 134.989 1.00 57.01  0  390  ASP   A CG  1 
ATOM   2713  O OD1 . ASP   A 1 426  ? 87.607  128.705 135.290 1.00 58.35  0  390  ASP   A OD1 1 
ATOM   2714  O OD2 . ASP   A 1 426  ? 86.122  127.673 134.047 1.00 58.15  -1 390  ASP   A OD2 1 
ATOM   2715  N N   . ASN   A 1 427  ? 89.916  126.274 133.857 1.00 41.13  0  391  ASN   A N   1 
ATOM   2716  C CA  . ASN   A 1 427  ? 90.490  125.850 132.589 1.00 36.73  0  391  ASN   A CA  1 
ATOM   2717  C C   . ASN   A 1 427  ? 91.688  124.932 132.760 1.00 36.70  0  391  ASN   A C   1 
ATOM   2718  O O   . ASN   A 1 427  ? 92.180  124.389 131.767 1.00 39.51  0  391  ASN   A O   1 
ATOM   2719  C CB  . ASN   A 1 427  ? 90.891  127.072 131.764 1.00 44.80  0  391  ASN   A CB  1 
ATOM   2720  C CG  . ASN   A 1 427  ? 89.697  127.880 131.316 1.00 50.11  0  391  ASN   A CG  1 
ATOM   2721  O OD1 . ASN   A 1 427  ? 88.617  127.337 131.094 1.00 45.85  0  391  ASN   A OD1 1 
ATOM   2722  N ND2 . ASN   A 1 427  ? 89.880  129.186 131.188 1.00 49.67  0  391  ASN   A ND2 1 
ATOM   2723  N N   . ILE   A 1 428  ? 92.177  124.760 133.982 1.00 36.30  0  392  ILE   A N   1 
ATOM   2724  C CA  . ILE   A 1 428  ? 93.206  123.765 134.246 1.00 35.68  0  392  ILE   A CA  1 
ATOM   2725  C C   . ILE   A 1 428  ? 92.577  122.413 134.565 1.00 41.19  0  392  ILE   A C   1 
ATOM   2726  O O   . ILE   A 1 428  ? 93.099  121.373 134.151 1.00 40.34  0  392  ILE   A O   1 
ATOM   2727  C CB  . ILE   A 1 428  ? 94.117  124.243 135.391 1.00 40.49  0  392  ILE   A CB  1 
ATOM   2728  C CG1 . ILE   A 1 428  ? 95.211  125.160 134.854 1.00 39.69  0  392  ILE   A CG1 1 
ATOM   2729  C CG2 . ILE   A 1 428  ? 94.748  123.069 136.119 1.00 37.60  0  392  ILE   A CG2 1 
ATOM   2730  C CD1 . ILE   A 1 428  ? 96.303  124.434 134.142 1.00 40.24  0  392  ILE   A CD1 1 
ATOM   2731  N N   . ILE   A 1 429  ? 91.450  122.414 135.278 1.00 46.12  0  393  ILE   A N   1 
ATOM   2732  C CA  . ILE   A 1 429  ? 90.797  121.168 135.667 1.00 45.53  0  393  ILE   A CA  1 
ATOM   2733  C C   . ILE   A 1 429  ? 90.261  120.436 134.442 1.00 45.67  0  393  ILE   A C   1 
ATOM   2734  O O   . ILE   A 1 429  ? 90.455  119.225 134.290 1.00 47.34  0  393  ILE   A O   1 
ATOM   2735  C CB  . ILE   A 1 429  ? 89.679  121.454 136.684 1.00 46.13  0  393  ILE   A CB  1 
ATOM   2736  C CG1 . ILE   A 1 429  ? 90.225  122.253 137.868 1.00 41.70  0  393  ILE   A CG1 1 
ATOM   2737  C CG2 . ILE   A 1 429  ? 89.056  120.157 137.167 1.00 48.26  0  393  ILE   A CG2 1 
ATOM   2738  C CD1 . ILE   A 1 429  ? 91.276  121.519 138.657 1.00 44.18  0  393  ILE   A CD1 1 
ATOM   2739  N N   . ASN   A 1 430  ? 89.586  121.158 133.546 1.00 43.55  0  394  ASN   A N   1 
ATOM   2740  C CA  . ASN   A 1 430  ? 88.925  120.552 132.400 1.00 42.98  0  394  ASN   A CA  1 
ATOM   2741  C C   . ASN   A 1 430  ? 89.833  120.458 131.179 1.00 45.53  0  394  ASN   A C   1 
ATOM   2742  O O   . ASN   A 1 430  ? 89.384  120.026 130.113 1.00 47.13  0  394  ASN   A O   1 
ATOM   2743  C CB  . ASN   A 1 430  ? 87.643  121.315 132.056 1.00 42.51  0  394  ASN   A CB  1 
ATOM   2744  C CG  . ASN   A 1 430  ? 87.895  122.767 131.693 1.00 43.27  0  394  ASN   A CG  1 
ATOM   2745  O OD1 . ASN   A 1 430  ? 89.024  123.173 131.431 1.00 51.93  0  394  ASN   A OD1 1 
ATOM   2746  N ND2 . ASN   A 1 430  ? 86.831  123.560 131.673 1.00 42.81  0  394  ASN   A ND2 1 
ATOM   2747  N N   . GLY   A 1 431  ? 91.093  120.863 131.309 1.00 48.46  0  395  GLY   A N   1 
ATOM   2748  C CA  . GLY   A 1 431  ? 92.033  120.730 130.214 1.00 43.26  0  395  GLY   A CA  1 
ATOM   2749  C C   . GLY   A 1 431  ? 91.806  121.675 129.059 1.00 42.78  0  395  GLY   A C   1 
ATOM   2750  O O   . GLY   A 1 431  ? 92.243  121.389 127.944 1.00 45.42  0  395  GLY   A O   1 
ATOM   2751  N N   . ARG   A 1 432  ? 91.130  122.798 129.289 1.00 44.09  0  396  ARG   A N   1 
ATOM   2752  C CA  . ARG   A 1 432  ? 90.926  123.783 128.236 1.00 45.17  0  396  ARG   A CA  1 
ATOM   2753  C C   . ARG   A 1 432  ? 92.191  124.571 127.913 1.00 52.30  0  396  ARG   A C   1 
ATOM   2754  O O   . ARG   A 1 432  ? 92.236  125.243 126.876 1.00 58.66  0  396  ARG   A O   1 
ATOM   2755  C CB  . ARG   A 1 432  ? 89.793  124.735 128.633 1.00 49.92  0  396  ARG   A CB  1 
ATOM   2756  C CG  . ARG   A 1 432  ? 89.328  125.670 127.529 1.00 52.62  0  396  ARG   A CG  1 
ATOM   2757  C CD  . ARG   A 1 432  ? 88.105  126.464 127.948 1.00 57.28  0  396  ARG   A CD  1 
ATOM   2758  N NE  . ARG   A 1 432  ? 87.838  127.565 127.031 1.00 57.76  0  396  ARG   A NE  1 
ATOM   2759  C CZ  . ARG   A 1 432  ? 87.186  127.445 125.884 1.00 61.36  0  396  ARG   A CZ  1 
ATOM   2760  N NH1 . ARG   A 1 432  ? 86.719  126.277 125.473 1.00 56.92  1  396  ARG   A NH1 1 
ATOM   2761  N NH2 . ARG   A 1 432  ? 86.999  128.523 125.128 1.00 60.88  0  396  ARG   A NH2 1 
ATOM   2762  N N   . TRP   A 1 433  ? 93.226  124.480 128.754 1.00 42.92  0  397  TRP   A N   1 
ATOM   2763  C CA  . TRP   A 1 433  ? 94.474  125.188 128.484 1.00 37.13  0  397  TRP   A CA  1 
ATOM   2764  C C   . TRP   A 1 433  ? 95.044  124.832 127.121 1.00 36.96  0  397  TRP   A C   1 
ATOM   2765  O O   . TRP   A 1 433  ? 95.704  125.664 126.488 1.00 38.38  0  397  TRP   A O   1 
ATOM   2766  C CB  . TRP   A 1 433  ? 95.503  124.882 129.572 1.00 40.23  0  397  TRP   A CB  1 
ATOM   2767  C CG  . TRP   A 1 433  ? 95.700  123.420 129.848 1.00 37.61  0  397  TRP   A CG  1 
ATOM   2768  C CD1 . TRP   A 1 433  ? 95.103  122.688 130.829 1.00 42.99  0  397  TRP   A CD1 1 
ATOM   2769  C CD2 . TRP   A 1 433  ? 96.554  122.515 129.139 1.00 38.91  0  397  TRP   A CD2 1 
ATOM   2770  N NE1 . TRP   A 1 433  ? 95.529  121.386 130.777 1.00 37.83  0  397  TRP   A NE1 1 
ATOM   2771  C CE2 . TRP   A 1 433  ? 96.421  121.253 129.747 1.00 43.31  0  397  TRP   A CE2 1 
ATOM   2772  C CE3 . TRP   A 1 433  ? 97.420  122.650 128.051 1.00 39.96  0  397  TRP   A CE3 1 
ATOM   2773  C CZ2 . TRP   A 1 433  ? 97.117  120.135 129.303 1.00 46.60  0  397  TRP   A CZ2 1 
ATOM   2774  C CZ3 . TRP   A 1 433  ? 98.106  121.537 127.609 1.00 38.47  0  397  TRP   A CZ3 1 
ATOM   2775  C CH2 . TRP   A 1 433  ? 97.952  120.296 128.234 1.00 39.79  0  397  TRP   A CH2 1 
ATOM   2776  N N   . ILE   A 1 434  ? 94.781  123.613 126.643 1.00 40.11  0  398  ILE   A N   1 
ATOM   2777  C CA  . ILE   A 1 434  ? 95.302  123.158 125.362 1.00 36.63  0  398  ILE   A CA  1 
ATOM   2778  C C   . ILE   A 1 434  ? 94.883  124.094 124.241 1.00 38.91  0  398  ILE   A C   1 
ATOM   2779  O O   . ILE   A 1 434  ? 95.562  124.176 123.214 1.00 43.77  0  398  ILE   A O   1 
ATOM   2780  C CB  . ILE   A 1 434  ? 94.839  121.708 125.095 1.00 36.62  0  398  ILE   A CB  1 
ATOM   2781  C CG1 . ILE   A 1 434  ? 95.481  121.143 123.829 1.00 38.59  0  398  ILE   A CG1 1 
ATOM   2782  C CG2 . ILE   A 1 434  ? 93.331  121.636 124.983 1.00 40.64  0  398  ILE   A CG2 1 
ATOM   2783  C CD1 . ILE   A 1 434  ? 96.951  121.430 123.716 1.00 39.97  0  398  ILE   A CD1 1 
ATOM   2784  N N   . ILE   A 1 435  ? 93.785  124.825 124.417 1.00 38.78  0  399  ILE   A N   1 
ATOM   2785  C CA  . ILE   A 1 435  ? 93.426  125.858 123.453 1.00 39.49  0  399  ILE   A CA  1 
ATOM   2786  C C   . ILE   A 1 435  ? 94.406  127.019 123.535 1.00 43.94  0  399  ILE   A C   1 
ATOM   2787  O O   . ILE   A 1 435  ? 95.108  127.333 122.565 1.00 49.73  0  399  ILE   A O   1 
ATOM   2788  C CB  . ILE   A 1 435  ? 91.981  126.332 123.684 1.00 41.89  0  399  ILE   A CB  1 
ATOM   2789  C CG1 . ILE   A 1 435  ? 91.041  125.137 123.844 1.00 44.42  0  399  ILE   A CG1 1 
ATOM   2790  C CG2 . ILE   A 1 435  ? 91.533  127.227 122.543 1.00 44.41  0  399  ILE   A CG2 1 
ATOM   2791  C CD1 . ILE   A 1 435  ? 90.988  124.233 122.643 1.00 44.02  0  399  ILE   A CD1 1 
ATOM   2792  N N   . LEU   A 1 436  ? 94.495  127.640 124.715 1.00 42.52  0  400  LEU   A N   1 
ATOM   2793  C CA  . LEU   A 1 436  ? 95.308  128.840 124.892 1.00 46.51  0  400  LEU   A CA  1 
ATOM   2794  C C   . LEU   A 1 436  ? 96.744  128.608 124.452 1.00 46.22  0  400  LEU   A C   1 
ATOM   2795  O O   . LEU   A 1 436  ? 97.284  129.364 123.635 1.00 46.98  0  400  LEU   A O   1 
ATOM   2796  C CB  . LEU   A 1 436  ? 95.267  129.277 126.355 1.00 47.90  0  400  LEU   A CB  1 
ATOM   2797  C CG  . LEU   A 1 436  ? 96.413  130.161 126.840 1.00 45.80  0  400  LEU   A CG  1 
ATOM   2798  C CD1 . LEU   A 1 436  ? 96.284  131.556 126.270 1.00 46.25  0  400  LEU   A CD1 1 
ATOM   2799  C CD2 . LEU   A 1 436  ? 96.441  130.198 128.355 1.00 47.79  0  400  LEU   A CD2 1 
ATOM   2800  N N   . LEU   A 1 437  ? 97.365  127.546 124.968 1.00 38.93  0  401  LEU   A N   1 
ATOM   2801  C CA  . LEU   A 1 437  ? 98.734  127.218 124.587 1.00 34.09  0  401  LEU   A CA  1 
ATOM   2802  C C   . LEU   A 1 437  ? 98.880  127.181 123.075 1.00 28.02  0  401  LEU   A C   1 
ATOM   2803  O O   . LEU   A 1 437  ? 99.794  127.798 122.515 1.00 36.16  0  401  LEU   A O   1 
ATOM   2804  C CB  . LEU   A 1 437  ? 99.137  125.881 125.203 1.00 29.02  0  401  LEU   A CB  1 
ATOM   2805  C CG  . LEU   A 1 437  ? 100.457 125.284 124.730 1.00 29.62  0  401  LEU   A CG  1 
ATOM   2806  C CD1 . LEU   A 1 437  ? 101.605 126.193 125.103 1.00 34.67  0  401  LEU   A CD1 1 
ATOM   2807  C CD2 . LEU   A 1 437  ? 100.652 123.905 125.329 1.00 37.86  0  401  LEU   A CD2 1 
ATOM   2808  N N   . SER   A 1 438  ? 97.948  126.510 122.393 1.00 28.36  0  402  SER   A N   1 
ATOM   2809  C CA  . SER   A 1 438  ? 98.010  126.442 120.938 1.00 31.44  0  402  SER   A CA  1 
ATOM   2810  C C   . SER   A 1 438  ? 98.101  127.837 120.341 1.00 38.43  0  402  SER   A C   1 
ATOM   2811  O O   . SER   A 1 438  ? 99.010  128.129 119.552 1.00 46.65  0  402  SER   A O   1 
ATOM   2812  C CB  . SER   A 1 438  ? 96.791  125.704 120.391 1.00 37.90  0  402  SER   A CB  1 
ATOM   2813  O OG  . SER   A 1 438  ? 95.679  126.575 120.290 1.00 39.11  0  402  SER   A OG  1 
ATOM   2814  N N   . LYS   A 1 439  ? 97.205  128.733 120.763 1.00 39.54  0  403  LYS   A N   1 
ATOM   2815  C CA  . LYS   A 1 439  ? 97.228  130.093 120.241 1.00 41.59  0  403  LYS   A CA  1 
ATOM   2816  C C   . LYS   A 1 439  ? 98.586  130.734 120.468 1.00 40.67  0  403  LYS   A C   1 
ATOM   2817  O O   . LYS   A 1 439  ? 99.158  131.330 119.546 1.00 38.17  0  403  LYS   A O   1 
ATOM   2818  C CB  . LYS   A 1 439  ? 96.122  130.925 120.886 1.00 43.80  0  403  LYS   A CB  1 
ATOM   2819  C CG  . LYS   A 1 439  ? 96.149  132.388 120.492 1.00 47.69  0  403  LYS   A CG  1 
ATOM   2820  C CD  . LYS   A 1 439  ? 96.102  132.557 118.986 1.00 50.31  0  403  LYS   A CD  1 
ATOM   2821  C CE  . LYS   A 1 439  ? 95.968  134.020 118.599 1.00 47.97  0  403  LYS   A CE  1 
ATOM   2822  N NZ  . LYS   A 1 439  ? 96.086  134.213 117.129 1.00 48.93  1  403  LYS   A NZ  1 
ATOM   2823  N N   . PHE   A 1 440  ? 99.142  130.570 121.673 1.00 32.37  0  404  PHE   A N   1 
ATOM   2824  C CA  . PHE   A 1 440  ? 100.464 131.115 121.956 1.00 31.41  0  404  PHE   A CA  1 
ATOM   2825  C C   . PHE   A 1 440  ? 101.463 130.654 120.908 1.00 37.21  0  404  PHE   A C   1 
ATOM   2826  O O   . PHE   A 1 440  ? 102.145 131.472 120.278 1.00 33.22  0  404  PHE   A O   1 
ATOM   2827  C CB  . PHE   A 1 440  ? 100.921 130.696 123.353 1.00 25.36  0  404  PHE   A CB  1 
ATOM   2828  C CG  . PHE   A 1 440  ? 102.255 131.259 123.749 1.00 31.88  0  404  PHE   A CG  1 
ATOM   2829  C CD1 . PHE   A 1 440  ? 102.626 132.536 123.367 1.00 33.13  0  404  PHE   A CD1 1 
ATOM   2830  C CD2 . PHE   A 1 440  ? 103.134 130.517 124.517 1.00 28.82  0  404  PHE   A CD2 1 
ATOM   2831  C CE1 . PHE   A 1 440  ? 103.848 133.057 123.737 1.00 25.33  0  404  PHE   A CE1 1 
ATOM   2832  C CE2 . PHE   A 1 440  ? 104.355 131.036 124.892 1.00 32.98  0  404  PHE   A CE2 1 
ATOM   2833  C CZ  . PHE   A 1 440  ? 104.712 132.307 124.499 1.00 29.77  0  404  PHE   A CZ  1 
ATOM   2834  N N   . LEU   A 1 441  ? 101.506 129.344 120.657 1.00 33.68  0  405  LEU   A N   1 
ATOM   2835  C CA  . LEU   A 1 441  ? 102.458 128.827 119.687 1.00 15.76  0  405  LEU   A CA  1 
ATOM   2836  C C   . LEU   A 1 441  ? 102.195 129.418 118.312 1.00 26.86  0  405  LEU   A C   1 
ATOM   2837  O O   . LEU   A 1 441  ? 103.135 129.813 117.611 1.00 42.71  0  405  LEU   A O   1 
ATOM   2838  C CB  . LEU   A 1 441  ? 102.400 127.303 119.656 1.00 22.86  0  405  LEU   A CB  1 
ATOM   2839  C CG  . LEU   A 1 441  ? 102.763 126.637 120.984 1.00 27.21  0  405  LEU   A CG  1 
ATOM   2840  C CD1 . LEU   A 1 441  ? 102.934 125.143 120.815 1.00 30.72  0  405  LEU   A CD1 1 
ATOM   2841  C CD2 . LEU   A 1 441  ? 104.016 127.249 121.562 1.00 25.63  0  405  LEU   A CD2 1 
ATOM   2842  N N   . LYS   A 1 442  ? 100.920 129.546 117.934 1.00 36.08  0  406  LYS   A N   1 
ATOM   2843  C CA  . LYS   A 1 442  ? 100.604 130.172 116.657 1.00 40.88  0  406  LYS   A CA  1 
ATOM   2844  C C   . LYS   A 1 442  ? 101.246 131.546 116.564 1.00 43.12  0  406  LYS   A C   1 
ATOM   2845  O O   . LYS   A 1 442  ? 101.892 131.872 115.559 1.00 48.34  0  406  LYS   A O   1 
ATOM   2846  C CB  . LYS   A 1 442  ? 99.092  130.279 116.476 1.00 47.00  0  406  LYS   A CB  1 
ATOM   2847  C CG  . LYS   A 1 442  ? 98.421  128.998 116.020 1.00 49.12  0  406  LYS   A CG  1 
ATOM   2848  C CD  . LYS   A 1 442  ? 96.925  129.203 115.846 1.00 52.15  0  406  LYS   A CD  1 
ATOM   2849  C CE  . LYS   A 1 442  ? 96.243  127.938 115.361 1.00 50.20  0  406  LYS   A CE  1 
ATOM   2850  N NZ  . LYS   A 1 442  ? 94.767  128.100 115.294 1.00 54.06  1  406  LYS   A NZ  1 
ATOM   2851  N N   . LEU   A 1 443  ? 101.139 132.337 117.633 1.00 33.52  0  407  LEU   A N   1 
ATOM   2852  C CA  . LEU   A 1 443  ? 101.720 133.672 117.616 1.00 33.60  0  407  LEU   A CA  1 
ATOM   2853  C C   . LEU   A 1 443  ? 103.216 133.608 117.363 1.00 38.94  0  407  LEU   A C   1 
ATOM   2854  O O   . LEU   A 1 443  ? 103.749 134.385 116.561 1.00 44.17  0  407  LEU   A O   1 
ATOM   2855  C CB  . LEU   A 1 443  ? 101.428 134.387 118.931 1.00 37.95  0  407  LEU   A CB  1 
ATOM   2856  C CG  . LEU   A 1 443  ? 100.050 135.034 118.999 1.00 38.60  0  407  LEU   A CG  1 
ATOM   2857  C CD1 . LEU   A 1 443  ? 99.717  135.369 120.428 1.00 32.45  0  407  LEU   A CD1 1 
ATOM   2858  C CD2 . LEU   A 1 443  ? 100.002 136.269 118.125 1.00 38.50  0  407  LEU   A CD2 1 
ATOM   2859  N N   . ILE   A 1 444  ? 103.904 132.658 118.003 1.00 35.71  0  408  ILE   A N   1 
ATOM   2860  C CA  . ILE   A 1 444  ? 105.339 132.528 117.784 1.00 26.00  0  408  ILE   A CA  1 
ATOM   2861  C C   . ILE   A 1 444  ? 105.617 132.276 116.312 1.00 21.48  0  408  ILE   A C   1 
ATOM   2862  O O   . ILE   A 1 444  ? 106.506 132.897 115.719 1.00 31.38  0  408  ILE   A O   1 
ATOM   2863  C CB  . ILE   A 1 444  ? 105.928 131.421 118.672 1.00 23.43  0  408  ILE   A CB  1 
ATOM   2864  C CG1 . ILE   A 1 444  ? 105.882 131.837 120.137 1.00 17.47  0  408  ILE   A CG1 1 
ATOM   2865  C CG2 . ILE   A 1 444  ? 107.353 131.132 118.274 1.00 29.35  0  408  ILE   A CG2 1 
ATOM   2866  C CD1 . ILE   A 1 444  ? 106.143 130.704 121.083 1.00 25.01  0  408  ILE   A CD1 1 
ATOM   2867  N N   . LYS   A 1 445  ? 104.827 131.401 115.686 1.00 20.77  0  409  LYS   A N   1 
ATOM   2868  C CA  . LYS   A 1 445  ? 104.994 131.182 114.256 1.00 26.56  0  409  LYS   A CA  1 
ATOM   2869  C C   . LYS   A 1 445  ? 104.765 132.475 113.491 1.00 25.23  0  409  LYS   A C   1 
ATOM   2870  O O   . LYS   A 1 445  ? 105.549 132.824 112.600 1.00 38.15  0  409  LYS   A O   1 
ATOM   2871  C CB  . LYS   A 1 445  ? 104.044 130.088 113.774 1.00 34.35  0  409  LYS   A CB  1 
ATOM   2872  C CG  . LYS   A 1 445  ? 104.372 129.549 112.396 1.00 33.92  0  409  LYS   A CG  1 
ATOM   2873  C CD  . LYS   A 1 445  ? 103.485 128.373 112.046 1.00 32.47  0  409  LYS   A CD  1 
ATOM   2874  C CE  . LYS   A 1 445  ? 103.729 127.208 112.987 1.00 37.62  0  409  LYS   A CE  1 
ATOM   2875  N NZ  . LYS   A 1 445  ? 102.915 126.015 112.623 1.00 31.15  1  409  LYS   A NZ  1 
ATOM   2876  N N   . LEU   A 1 446  ? 103.726 133.225 113.860 1.00 12.91  0  410  LEU   A N   1 
ATOM   2877  C CA  . LEU   A 1 446  ? 103.500 134.520 113.232 1.00 26.57  0  410  LEU   A CA  1 
ATOM   2878  C C   . LEU   A 1 446  ? 104.656 135.468 113.514 1.00 37.92  0  410  LEU   A C   1 
ATOM   2879  O O   . LEU   A 1 446  ? 105.007 136.300 112.670 1.00 37.19  0  410  LEU   A O   1 
ATOM   2880  C CB  . LEU   A 1 446  ? 102.181 135.117 113.716 1.00 34.23  0  410  LEU   A CB  1 
ATOM   2881  C CG  . LEU   A 1 446  ? 100.947 134.768 112.888 1.00 30.74  0  410  LEU   A CG  1 
ATOM   2882  C CD1 . LEU   A 1 446  ? 99.685  135.148 113.636 1.00 34.90  0  410  LEU   A CD1 1 
ATOM   2883  C CD2 . LEU   A 1 446  ? 101.006 135.468 111.545 1.00 31.47  0  410  LEU   A CD2 1 
ATOM   2884  N N   . ALA   A 1 447  ? 105.262 135.356 114.698 1.00 38.46  0  411  ALA   A N   1 
ATOM   2885  C CA  . ALA   A 1 447  ? 106.452 136.146 114.983 1.00 20.65  0  411  ALA   A CA  1 
ATOM   2886  C C   . ALA   A 1 447  ? 107.635 135.679 114.151 1.00 23.02  0  411  ALA   A C   1 
ATOM   2887  O O   . ALA   A 1 447  ? 108.476 136.494 113.761 1.00 30.70  0  411  ALA   A O   1 
ATOM   2888  C CB  . ALA   A 1 447  ? 106.786 136.084 116.471 1.00 19.62  0  411  ALA   A CB  1 
ATOM   2889  N N   . GLY   A 1 448  ? 107.719 134.378 113.870 1.00 36.07  0  412  GLY   A N   1 
ATOM   2890  C CA  . GLY   A 1 448  ? 108.801 133.887 113.035 1.00 33.86  0  412  GLY   A CA  1 
ATOM   2891  C C   . GLY   A 1 448  ? 108.687 134.355 111.599 1.00 31.09  0  412  GLY   A C   1 
ATOM   2892  O O   . GLY   A 1 448  ? 109.687 134.719 110.976 1.00 32.67  0  412  GLY   A O   1 
ATOM   2893  N N   . ASP   A 1 449  ? 107.470 134.359 111.058 1.00 42.12  0  413  ASP   A N   1 
ATOM   2894  C CA  . ASP   A 1 449  ? 107.219 134.747 109.672 1.00 44.86  0  413  ASP   A CA  1 
ATOM   2895  C C   . ASP   A 1 449  ? 108.088 133.941 108.711 1.00 45.02  0  413  ASP   A C   1 
ATOM   2896  O O   . ASP   A 1 449  ? 108.637 134.475 107.745 1.00 47.19  0  413  ASP   A O   1 
ATOM   2897  C CB  . ASP   A 1 449  ? 107.429 136.248 109.474 1.00 48.96  0  413  ASP   A CB  1 
ATOM   2898  C CG  . ASP   A 1 449  ? 106.720 136.778 108.242 1.00 53.72  0  413  ASP   A CG  1 
ATOM   2899  O OD1 . ASP   A 1 449  ? 106.037 135.986 107.560 1.00 50.27  0  413  ASP   A OD1 1 
ATOM   2900  O OD2 . ASP   A 1 449  ? 106.847 137.986 107.953 1.00 53.16  -1 413  ASP   A OD2 1 
ATOM   2901  N N   . ASN   A 1 450  ? 108.209 132.638 108.991 1.00 45.82  0  414  ASN   A N   1 
ATOM   2902  C CA  . ASN   A 1 450  ? 109.009 131.683 108.223 1.00 48.32  0  414  ASN   A CA  1 
ATOM   2903  C C   . ASN   A 1 450  ? 110.343 132.276 107.786 1.00 50.16  0  414  ASN   A C   1 
ATOM   2904  O O   . ASN   A 1 450  ? 110.784 132.075 106.650 1.00 49.03  0  414  ASN   A O   1 
ATOM   2905  C CB  . ASN   A 1 450  ? 108.221 131.154 107.013 1.00 50.21  0  414  ASN   A CB  1 
ATOM   2906  C CG  . ASN   A 1 450  ? 107.717 132.255 106.094 1.00 55.46  0  414  ASN   A CG  1 
ATOM   2907  O OD1 . ASN   A 1 450  ? 108.499 132.958 105.453 1.00 57.33  0  414  ASN   A OD1 1 
ATOM   2908  N ND2 . ASN   A 1 450  ? 106.400 132.410 106.030 1.00 47.50  0  414  ASN   A ND2 1 
ATOM   2909  N N   . ASN   A 1 451  ? 110.994 132.999 108.693 1.00 41.97  0  415  ASN   A N   1 
ATOM   2910  C CA  . ASN   A 1 451  ? 112.250 133.679 108.422 1.00 42.39  0  415  ASN   A CA  1 
ATOM   2911  C C   . ASN   A 1 451  ? 113.284 133.233 109.440 1.00 43.71  0  415  ASN   A C   1 
ATOM   2912  O O   . ASN   A 1 451  ? 112.976 133.094 110.625 1.00 49.89  0  415  ASN   A O   1 
ATOM   2913  C CB  . ASN   A 1 451  ? 112.077 135.196 108.487 1.00 34.45  0  415  ASN   A CB  1 
ATOM   2914  C CG  . ASN   A 1 451  ? 113.137 135.933 107.715 1.00 34.82  0  415  ASN   A CG  1 
ATOM   2915  O OD1 . ASN   A 1 451  ? 114.193 135.383 107.414 1.00 37.77  0  415  ASN   A OD1 1 
ATOM   2916  N ND2 . ASN   A 1 451  ? 112.868 137.191 107.395 1.00 39.27  0  415  ASN   A ND2 1 
ATOM   2917  N N   . LEU   A 1 452  ? 114.510 133.002 108.977 1.00 29.42  0  416  LEU   A N   1 
ATOM   2918  C CA  . LEU   A 1 452  ? 115.568 132.598 109.893 1.00 21.82  0  416  LEU   A CA  1 
ATOM   2919  C C   . LEU   A 1 452  ? 116.012 133.738 110.798 1.00 28.21  0  416  LEU   A C   1 
ATOM   2920  O O   . LEU   A 1 452  ? 116.377 133.495 111.953 1.00 31.40  0  416  LEU   A O   1 
ATOM   2921  C CB  . LEU   A 1 452  ? 116.759 132.048 109.114 1.00 28.27  0  416  LEU   A CB  1 
ATOM   2922  C CG  . LEU   A 1 452  ? 116.739 130.543 108.872 1.00 29.12  0  416  LEU   A CG  1 
ATOM   2923  C CD1 . LEU   A 1 452  ? 117.731 130.162 107.798 1.00 29.77  0  416  LEU   A CD1 1 
ATOM   2924  C CD2 . LEU   A 1 452  ? 117.059 129.828 110.166 1.00 30.86  0  416  LEU   A CD2 1 
ATOM   2925  N N   . ASN   A 1 453  ? 115.994 134.976 110.301 1.00 28.12  0  417  ASN   A N   1 
ATOM   2926  C CA  . ASN   A 1 453  ? 116.403 136.110 111.123 1.00 34.86  0  417  ASN   A CA  1 
ATOM   2927  C C   . ASN   A 1 453  ? 115.471 136.291 112.314 1.00 39.72  0  417  ASN   A C   1 
ATOM   2928  O O   . ASN   A 1 453  ? 115.924 136.397 113.459 1.00 38.84  0  417  ASN   A O   1 
ATOM   2929  C CB  . ASN   A 1 453  ? 116.442 137.381 110.279 1.00 33.37  0  417  ASN   A CB  1 
ATOM   2930  C CG  . ASN   A 1 453  ? 117.030 137.150 108.910 1.00 37.75  0  417  ASN   A CG  1 
ATOM   2931  O OD1 . ASN   A 1 453  ? 118.033 136.460 108.762 1.00 35.98  0  417  ASN   A OD1 1 
ATOM   2932  N ND2 . ASN   A 1 453  ? 116.403 137.727 107.894 1.00 41.07  0  417  ASN   A ND2 1 
ATOM   2933  N N   . ASN   A 1 454  ? 114.161 136.339 112.060 1.00 30.19  0  418  ASN   A N   1 
ATOM   2934  C CA  . ASN   A 1 454  ? 113.203 136.502 113.147 1.00 18.30  0  418  ASN   A CA  1 
ATOM   2935  C C   . ASN   A 1 454  ? 113.230 135.307 114.085 1.00 20.48  0  418  ASN   A C   1 
ATOM   2936  O O   . ASN   A 1 454  ? 113.192 135.470 115.307 1.00 41.75  0  418  ASN   A O   1 
ATOM   2937  C CB  . ASN   A 1 454  ? 111.798 136.702 112.588 1.00 19.13  0  418  ASN   A CB  1 
ATOM   2938  C CG  . ASN   A 1 454  ? 111.666 137.976 111.801 1.00 24.77  0  418  ASN   A CG  1 
ATOM   2939  O OD1 . ASN   A 1 454  ? 112.659 138.597 111.440 1.00 34.54  0  418  ASN   A OD1 1 
ATOM   2940  N ND2 . ASN   A 1 454  ? 110.434 138.380 111.531 1.00 27.46  0  418  ASN   A ND2 1 
ATOM   2941  N N   . LEU   A 1 455  ? 113.291 134.098 113.534 1.00 15.18  0  419  LEU   A N   1 
ATOM   2942  C CA  . LEU   A 1 455  ? 113.297 132.903 114.364 1.00 19.66  0  419  LEU   A CA  1 
ATOM   2943  C C   . LEU   A 1 455  ? 114.580 132.750 115.163 1.00 17.61  0  419  LEU   A C   1 
ATOM   2944  O O   . LEU   A 1 455  ? 114.587 132.015 116.154 1.00 23.58  0  419  LEU   A O   1 
ATOM   2945  C CB  . LEU   A 1 455  ? 113.076 131.665 113.501 1.00 28.33  0  419  LEU   A CB  1 
ATOM   2946  C CG  . LEU   A 1 455  ? 111.649 131.453 113.005 1.00 25.26  0  419  LEU   A CG  1 
ATOM   2947  C CD1 . LEU   A 1 455  ? 111.636 130.395 111.924 1.00 26.78  0  419  LEU   A CD1 1 
ATOM   2948  C CD2 . LEU   A 1 455  ? 110.734 131.074 114.152 1.00 24.91  0  419  LEU   A CD2 1 
ATOM   2949  N N   . SER   A 1 456  ? 115.662 133.404 114.751 1.00 15.14  0  420  SER   A N   1 
ATOM   2950  C CA  . SER   A 1 456  ? 116.884 133.413 115.539 1.00 25.08  0  420  SER   A CA  1 
ATOM   2951  C C   . SER   A 1 456  ? 116.856 134.499 116.603 1.00 37.21  0  420  SER   A C   1 
ATOM   2952  O O   . SER   A 1 456  ? 117.295 134.269 117.735 1.00 32.39  0  420  SER   A O   1 
ATOM   2953  C CB  . SER   A 1 456  ? 118.094 133.608 114.628 1.00 17.78  0  420  SER   A CB  1 
ATOM   2954  O OG  . SER   A 1 456  ? 118.123 132.619 113.618 1.00 21.18  0  420  SER   A OG  1 
ATOM   2955  N N   . GLU   A 1 457  ? 116.336 135.679 116.258 1.00 38.34  0  421  GLU   A N   1 
ATOM   2956  C CA  . GLU   A 1 457  ? 116.236 136.751 117.238 1.00 25.33  0  421  GLU   A CA  1 
ATOM   2957  C C   . GLU   A 1 457  ? 115.216 136.428 118.316 1.00 23.74  0  421  GLU   A C   1 
ATOM   2958  O O   . GLU   A 1 457  ? 115.333 136.919 119.441 1.00 44.85  0  421  GLU   A O   1 
ATOM   2959  C CB  . GLU   A 1 457  ? 115.880 138.069 116.551 1.00 25.28  0  421  GLU   A CB  1 
ATOM   2960  C CG  . GLU   A 1 457  ? 116.919 138.555 115.556 1.00 30.17  0  421  GLU   A CG  1 
ATOM   2961  C CD  . GLU   A 1 457  ? 117.881 139.564 116.153 1.00 38.11  0  421  GLU   A CD  1 
ATOM   2962  O OE1 . GLU   A 1 457  ? 118.133 139.497 117.372 1.00 39.36  0  421  GLU   A OE1 1 
ATOM   2963  O OE2 . GLU   A 1 457  ? 118.391 140.422 115.402 1.00 37.08  -1 421  GLU   A OE2 1 
ATOM   2964  N N   . LEU   A 1 458  ? 114.232 135.586 118.007 1.00 18.01  0  422  LEU   A N   1 
ATOM   2965  C CA  . LEU   A 1 458  ? 113.139 135.266 118.924 1.00 18.63  0  422  LEU   A CA  1 
ATOM   2966  C C   . LEU   A 1 458  ? 113.573 134.495 120.119 1.00 16.57  0  422  LEU   A C   1 
ATOM   2967  O O   . LEU   A 1 458  ? 112.696 134.055 120.854 1.00 24.82  0  422  LEU   A O   1 
ATOM   2968  C CB  . LEU   A 1 458  ? 112.050 134.486 118.189 1.00 21.58  0  422  LEU   A CB  1 
ATOM   2969  C CG  . LEU   A 1 458  ? 110.892 135.295 117.611 1.00 15.22  0  422  LEU   A CG  1 
ATOM   2970  C CD1 . LEU   A 1 458  ? 110.067 134.436 116.682 1.00 20.84  0  422  LEU   A CD1 1 
ATOM   2971  C CD2 . LEU   A 1 458  ? 110.034 135.835 118.724 1.00 18.38  0  422  LEU   A CD2 1 
ATOM   2972  N N   . TYR   A 1 459  ? 114.860 134.284 120.363 1.00 17.28  0  423  TYR   A N   1 
ATOM   2973  C CA  . TYR   A 1 459  ? 115.294 133.566 121.551 1.00 22.87  0  423  TYR   A CA  1 
ATOM   2974  C C   . TYR   A 1 459  ? 115.246 134.415 122.813 1.00 31.47  0  423  TYR   A C   1 
ATOM   2975  O O   . TYR   A 1 459  ? 115.566 133.903 123.890 1.00 34.47  0  423  TYR   A O   1 
ATOM   2976  C CB  . TYR   A 1 459  ? 116.706 133.022 121.349 1.00 28.79  0  423  TYR   A CB  1 
ATOM   2977  C CG  . TYR   A 1 459  ? 116.734 131.656 120.713 1.00 36.49  0  423  TYR   A CG  1 
ATOM   2978  C CD1 . TYR   A 1 459  ? 116.363 131.479 119.389 1.00 42.34  0  423  TYR   A CD1 1 
ATOM   2979  C CD2 . TYR   A 1 459  ? 117.125 130.541 121.438 1.00 36.08  0  423  TYR   A CD2 1 
ATOM   2980  C CE1 . TYR   A 1 459  ? 116.383 130.234 118.803 1.00 37.78  0  423  TYR   A CE1 1 
ATOM   2981  C CE2 . TYR   A 1 459  ? 117.148 129.291 120.859 1.00 41.43  0  423  TYR   A CE2 1 
ATOM   2982  C CZ  . TYR   A 1 459  ? 116.777 129.146 119.542 1.00 38.48  0  423  TYR   A CZ  1 
ATOM   2983  O OH  . TYR   A 1 459  ? 116.801 127.903 118.965 1.00 36.87  0  423  TYR   A OH  1 
ATOM   2984  N N   . PHE   A 1 460  ? 114.872 135.692 122.717 1.00 28.84  0  424  PHE   A N   1 
ATOM   2985  C CA  . PHE   A 1 460  ? 114.708 136.487 123.926 1.00 27.69  0  424  PHE   A CA  1 
ATOM   2986  C C   . PHE   A 1 460  ? 113.449 136.115 124.694 1.00 33.10  0  424  PHE   A C   1 
ATOM   2987  O O   . PHE   A 1 460  ? 113.277 136.569 125.829 1.00 39.72  0  424  PHE   A O   1 
ATOM   2988  C CB  . PHE   A 1 460  ? 114.696 137.984 123.600 1.00 21.59  0  424  PHE   A CB  1 
ATOM   2989  C CG  . PHE   A 1 460  ? 113.657 138.398 122.591 1.00 13.21  0  424  PHE   A CG  1 
ATOM   2990  C CD1 . PHE   A 1 460  ? 112.314 138.414 122.912 1.00 20.12  0  424  PHE   A CD1 1 
ATOM   2991  C CD2 . PHE   A 1 460  ? 114.034 138.823 121.335 1.00 13.95  0  424  PHE   A CD2 1 
ATOM   2992  C CE1 . PHE   A 1 460  ? 111.372 138.806 121.989 1.00 19.86  0  424  PHE   A CE1 1 
ATOM   2993  C CE2 . PHE   A 1 460  ? 113.095 139.218 120.411 1.00 19.45  0  424  PHE   A CE2 1 
ATOM   2994  C CZ  . PHE   A 1 460  ? 111.764 139.212 120.740 1.00 19.64  0  424  PHE   A CZ  1 
ATOM   2995  N N   . LEU   A 1 461  ? 112.571 135.302 124.104 1.00 21.22  0  425  LEU   A N   1 
ATOM   2996  C CA  . LEU   A 1 461  ? 111.295 134.999 124.738 1.00 19.30  0  425  LEU   A CA  1 
ATOM   2997  C C   . LEU   A 1 461  ? 111.478 134.313 126.083 1.00 30.69  0  425  LEU   A C   1 
ATOM   2998  O O   . LEU   A 1 461  ? 110.632 134.461 126.969 1.00 36.72  0  425  LEU   A O   1 
ATOM   2999  C CB  . LEU   A 1 461  ? 110.444 134.136 123.810 1.00 26.44  0  425  LEU   A CB  1 
ATOM   3000  C CG  . LEU   A 1 461  ? 109.577 134.874 122.793 1.00 20.21  0  425  LEU   A CG  1 
ATOM   3001  C CD1 . LEU   A 1 461  ? 109.216 133.948 121.662 1.00 29.97  0  425  LEU   A CD1 1 
ATOM   3002  C CD2 . LEU   A 1 461  ? 108.322 135.390 123.449 1.00 24.15  0  425  LEU   A CD2 1 
ATOM   3003  N N   . PHE   A 1 462  ? 112.565 133.560 126.260 1.00 41.25  0  426  PHE   A N   1 
ATOM   3004  C CA  . PHE   A 1 462  ? 112.848 132.962 127.560 1.00 47.89  0  426  PHE   A CA  1 
ATOM   3005  C C   . PHE   A 1 462  ? 113.025 133.993 128.665 1.00 49.59  0  426  PHE   A C   1 
ATOM   3006  O O   . PHE   A 1 462  ? 112.731 133.688 129.826 1.00 51.16  0  426  PHE   A O   1 
ATOM   3007  C CB  . PHE   A 1 462  ? 114.106 132.096 127.488 1.00 45.24  0  426  PHE   A CB  1 
ATOM   3008  C CG  . PHE   A 1 462  ? 114.026 130.838 128.304 1.00 51.18  0  426  PHE   A CG  1 
ATOM   3009  C CD1 . PHE   A 1 462  ? 114.173 129.598 127.715 1.00 49.02  0  426  PHE   A CD1 1 
ATOM   3010  C CD2 . PHE   A 1 462  ? 113.814 130.900 129.671 1.00 51.12  0  426  PHE   A CD2 1 
ATOM   3011  C CE1 . PHE   A 1 462  ? 114.105 128.447 128.476 1.00 48.91  0  426  PHE   A CE1 1 
ATOM   3012  C CE2 . PHE   A 1 462  ? 113.743 129.752 130.433 1.00 50.24  0  426  PHE   A CE2 1 
ATOM   3013  C CZ  . PHE   A 1 462  ? 113.890 128.525 129.833 1.00 53.24  0  426  PHE   A CZ  1 
ATOM   3014  N N   . ARG   A 1 463  ? 113.488 135.197 128.342 1.00 42.85  0  427  ARG   A N   1 
ATOM   3015  C CA  . ARG   A 1 463  ? 113.889 136.159 129.357 1.00 39.90  0  427  ARG   A CA  1 
ATOM   3016  C C   . ARG   A 1 463  ? 112.852 137.234 129.638 1.00 35.44  0  427  ARG   A C   1 
ATOM   3017  O O   . ARG   A 1 463  ? 112.878 137.824 130.718 1.00 41.59  0  427  ARG   A O   1 
ATOM   3018  C CB  . ARG   A 1 463  ? 115.205 136.834 128.949 1.00 45.43  0  427  ARG   A CB  1 
ATOM   3019  C CG  . ARG   A 1 463  ? 116.398 135.889 128.841 1.00 42.45  0  427  ARG   A CG  1 
ATOM   3020  C CD  . ARG   A 1 463  ? 116.270 134.697 129.782 1.00 45.64  0  427  ARG   A CD  1 
ATOM   3021  N NE  . ARG   A 1 463  ? 117.565 134.186 130.212 1.00 51.75  0  427  ARG   A NE  1 
ATOM   3022  C CZ  . ARG   A 1 463  ? 117.728 133.257 131.143 1.00 52.32  0  427  ARG   A CZ  1 
ATOM   3023  N NH1 . ARG   A 1 463  ? 116.695 132.709 131.760 1.00 43.50  1  427  ARG   A NH1 1 
ATOM   3024  N NH2 . ARG   A 1 463  ? 118.959 132.869 131.465 1.00 47.08  0  427  ARG   A NH2 1 
ATOM   3025  N N   . ILE   A 1 464  ? 111.941 137.499 128.706 1.00 18.69  0  428  ILE   A N   1 
ATOM   3026  C CA  . ILE   A 1 464  ? 110.987 138.590 128.857 1.00 26.44  0  428  ILE   A CA  1 
ATOM   3027  C C   . ILE   A 1 464  ? 109.828 138.167 129.748 1.00 34.82  0  428  ILE   A C   1 
ATOM   3028  O O   . ILE   A 1 464  ? 108.996 138.995 130.133 1.00 25.98  0  428  ILE   A O   1 
ATOM   3029  C CB  . ILE   A 1 464  ? 110.467 139.058 127.491 1.00 22.20  0  428  ILE   A CB  1 
ATOM   3030  C CG1 . ILE   A 1 464  ? 109.819 137.884 126.771 1.00 23.91  0  428  ILE   A CG1 1 
ATOM   3031  C CG2 . ILE   A 1 464  ? 111.591 139.641 126.666 1.00 23.31  0  428  ILE   A CG2 1 
ATOM   3032  C CD1 . ILE   A 1 464  ? 109.447 138.177 125.365 1.00 26.31  0  428  ILE   A CD1 1 
ATOM   3033  N N   . PHE   A 1 465  ? 109.751 136.877 130.070 1.00 34.76  0  429  PHE   A N   1 
ATOM   3034  C CA  . PHE   A 1 465  ? 108.678 136.353 130.903 1.00 20.60  0  429  PHE   A CA  1 
ATOM   3035  C C   . PHE   A 1 465  ? 109.116 136.137 132.343 1.00 24.60  0  429  PHE   A C   1 
ATOM   3036  O O   . PHE   A 1 465  ? 108.379 135.527 133.122 1.00 32.33  0  429  PHE   A O   1 
ATOM   3037  C CB  . PHE   A 1 465  ? 108.133 135.053 130.314 1.00 18.96  0  429  PHE   A CB  1 
ATOM   3038  C CG  . PHE   A 1 465  ? 107.389 135.241 129.031 1.00 16.34  0  429  PHE   A CG  1 
ATOM   3039  C CD1 . PHE   A 1 465  ? 106.339 136.130 128.950 1.00 16.68  0  429  PHE   A CD1 1 
ATOM   3040  C CD2 . PHE   A 1 465  ? 107.743 134.531 127.904 1.00 14.58  0  429  PHE   A CD2 1 
ATOM   3041  C CE1 . PHE   A 1 465  ? 105.659 136.310 127.770 1.00 13.46  0  429  PHE   A CE1 1 
ATOM   3042  C CE2 . PHE   A 1 465  ? 107.065 134.707 126.723 1.00 18.75  0  429  PHE   A CE2 1 
ATOM   3043  C CZ  . PHE   A 1 465  ? 106.022 135.597 126.656 1.00 19.64  0  429  PHE   A CZ  1 
ATOM   3044  N N   . GLY   A 1 466  ? 110.295 136.618 132.710 1.00 29.29  0  430  GLY   A N   1 
ATOM   3045  C CA  . GLY   A 1 466  ? 110.745 136.534 134.081 1.00 20.69  0  430  GLY   A CA  1 
ATOM   3046  C C   . GLY   A 1 466  ? 111.286 135.169 134.433 1.00 25.49  0  430  GLY   A C   1 
ATOM   3047  O O   . GLY   A 1 466  ? 111.301 134.233 133.634 1.00 30.18  0  430  GLY   A O   1 
ATOM   3048  N N   . HIS   A 1 467  ? 111.734 135.059 135.672 1.00 13.59  0  431  HIS   A N   1 
ATOM   3049  C CA  . HIS   A 1 467  ? 112.360 133.846 136.148 1.00 19.43  0  431  HIS   A CA  1 
ATOM   3050  C C   . HIS   A 1 467  ? 111.434 133.101 137.099 1.00 29.35  0  431  HIS   A C   1 
ATOM   3051  O O   . HIS   A 1 467  ? 110.670 133.721 137.844 1.00 31.99  0  431  HIS   A O   1 
ATOM   3052  C CB  . HIS   A 1 467  ? 113.680 134.161 136.858 1.00 17.13  0  431  HIS   A CB  1 
ATOM   3053  C CG  . HIS   A 1 467  ? 114.594 135.026 136.054 1.00 23.59  0  431  HIS   A CG  1 
ATOM   3054  N ND1 . HIS   A 1 467  ? 115.425 134.523 135.078 1.00 29.11  0  431  HIS   A ND1 1 
ATOM   3055  C CD2 . HIS   A 1 467  ? 114.796 136.364 136.067 1.00 22.96  0  431  HIS   A CD2 1 
ATOM   3056  C CE1 . HIS   A 1 467  ? 116.104 135.513 134.528 1.00 30.99  0  431  HIS   A CE1 1 
ATOM   3057  N NE2 . HIS   A 1 467  ? 115.742 136.640 135.111 1.00 27.30  0  431  HIS   A NE2 1 
ATOM   3058  N N   . PRO   A 1 468  ? 111.468 131.771 137.088 1.00 28.34  0  432  PRO   A N   1 
ATOM   3059  C CA  . PRO   A 1 468  ? 110.572 131.006 137.957 1.00 23.06  0  432  PRO   A CA  1 
ATOM   3060  C C   . PRO   A 1 468  ? 110.978 131.104 139.416 1.00 25.37  0  432  PRO   A C   1 
ATOM   3061  O O   . PRO   A 1 468  ? 112.161 131.166 139.754 1.00 27.80  0  432  PRO   A O   1 
ATOM   3062  C CB  . PRO   A 1 468  ? 110.723 129.572 137.439 1.00 11.00  0  432  PRO   A CB  1 
ATOM   3063  C CG  . PRO   A 1 468  ? 112.087 129.535 136.875 1.00 22.71  0  432  PRO   A CG  1 
ATOM   3064  C CD  . PRO   A 1 468  ? 112.339 130.895 136.289 1.00 24.80  0  432  PRO   A CD  1 
ATOM   3065  N N   . MET   A 1 469  ? 109.975 131.099 140.282 1.00 22.94  0  433  MET   A N   1 
ATOM   3066  C CA  . MET   A 1 469  ? 110.206 131.021 141.719 1.00 21.39  0  433  MET   A CA  1 
ATOM   3067  C C   . MET   A 1 469  ? 110.735 129.628 142.020 1.00 32.57  0  433  MET   A C   1 
ATOM   3068  O O   . MET   A 1 469  ? 109.968 128.671 142.140 1.00 33.39  0  433  MET   A O   1 
ATOM   3069  C CB  . MET   A 1 469  ? 108.914 131.308 142.471 1.00 26.32  0  433  MET   A CB  1 
ATOM   3070  C CG  . MET   A 1 469  ? 109.095 131.800 143.886 1.00 28.28  0  433  MET   A CG  1 
ATOM   3071  S SD  . MET   A 1 469  ? 107.684 132.780 144.417 1.00 47.80  0  433  MET   A SD  1 
ATOM   3072  C CE  . MET   A 1 469  ? 106.342 131.904 143.624 1.00 30.51  0  433  MET   A CE  1 
ATOM   3073  N N   . VAL   A 1 470  ? 112.050 129.505 142.139 1.00 38.84  0  434  VAL   A N   1 
ATOM   3074  C CA  . VAL   A 1 470  ? 112.689 128.196 142.157 1.00 37.69  0  434  VAL   A CA  1 
ATOM   3075  C C   . VAL   A 1 470  ? 112.520 127.559 143.527 1.00 31.17  0  434  VAL   A C   1 
ATOM   3076  O O   . VAL   A 1 470  ? 112.869 128.151 144.553 1.00 30.10  0  434  VAL   A O   1 
ATOM   3077  C CB  . VAL   A 1 470  ? 114.173 128.306 141.771 1.00 42.95  0  434  VAL   A CB  1 
ATOM   3078  C CG1 . VAL   A 1 470  ? 114.874 129.372 142.597 1.00 37.76  0  434  VAL   A CG1 1 
ATOM   3079  C CG2 . VAL   A 1 470  ? 114.862 126.963 141.941 1.00 43.08  0  434  VAL   A CG2 1 
ATOM   3080  N N   . ASP   A 1 471  ? 111.972 126.349 143.545 1.00 40.60  0  435  ASP   A N   1 
ATOM   3081  C CA  . ASP   A 1 471  ? 111.957 125.544 144.753 1.00 43.02  0  435  ASP   A CA  1 
ATOM   3082  C C   . ASP   A 1 471  ? 113.265 124.778 144.862 1.00 41.00  0  435  ASP   A C   1 
ATOM   3083  O O   . ASP   A 1 471  ? 113.782 124.262 143.869 1.00 51.61  0  435  ASP   A O   1 
ATOM   3084  C CB  . ASP   A 1 471  ? 110.779 124.572 144.746 1.00 48.75  0  435  ASP   A CB  1 
ATOM   3085  C CG  . ASP   A 1 471  ? 110.429 124.076 146.133 1.00 52.82  0  435  ASP   A CG  1 
ATOM   3086  O OD1 . ASP   A 1 471  ? 111.205 124.342 147.072 1.00 51.68  0  435  ASP   A OD1 1 
ATOM   3087  O OD2 . ASP   A 1 471  ? 109.380 123.417 146.284 1.00 51.68  -1 435  ASP   A OD2 1 
ATOM   3088  N N   . GLU   A 1 472  ? 113.806 124.717 146.074 1.00 37.24  0  436  GLU   A N   1 
ATOM   3089  C CA  . GLU   A 1 472  ? 115.097 124.088 146.309 1.00 43.69  0  436  GLU   A CA  1 
ATOM   3090  C C   . GLU   A 1 472  ? 114.968 122.634 146.742 1.00 50.99  0  436  GLU   A C   1 
ATOM   3091  O O   . GLU   A 1 472  ? 115.650 121.753 146.198 1.00 49.73  0  436  GLU   A O   1 
ATOM   3092  C CB  . GLU   A 1 472  ? 115.871 124.887 147.363 1.00 44.40  0  436  GLU   A CB  1 
ATOM   3093  C CG  . GLU   A 1 472  ? 115.932 126.384 147.084 1.00 49.51  0  436  GLU   A CG  1 
ATOM   3094  C CD  . GLU   A 1 472  ? 114.788 127.149 147.719 1.00 51.65  0  436  GLU   A CD  1 
ATOM   3095  O OE1 . GLU   A 1 472  ? 113.994 126.529 148.456 1.00 53.30  0  436  GLU   A OE1 1 
ATOM   3096  O OE2 . GLU   A 1 472  ? 114.679 128.368 147.477 1.00 49.41  -1 436  GLU   A OE2 1 
ATOM   3097  N N   . ARG   A 1 473  ? 114.090 122.370 147.710 1.00 41.73  0  437  ARG   A N   1 
ATOM   3098  C CA  . ARG   A 1 473  ? 113.902 121.010 148.197 1.00 45.17  0  437  ARG   A CA  1 
ATOM   3099  C C   . ARG   A 1 473  ? 113.457 120.084 147.073 1.00 40.73  0  437  ARG   A C   1 
ATOM   3100  O O   . ARG   A 1 473  ? 113.985 118.976 146.918 1.00 42.19  0  437  ARG   A O   1 
ATOM   3101  C CB  . ARG   A 1 473  ? 112.879 121.008 149.329 1.00 41.86  0  437  ARG   A CB  1 
ATOM   3102  C CG  . ARG   A 1 473  ? 113.247 121.852 150.533 1.00 29.93  0  437  ARG   A CG  1 
ATOM   3103  C CD  . ARG   A 1 473  ? 112.269 121.564 151.654 1.00 38.45  0  437  ARG   A CD  1 
ATOM   3104  N NE  . ARG   A 1 473  ? 112.652 122.146 152.932 1.00 33.24  0  437  ARG   A NE  1 
ATOM   3105  C CZ  . ARG   A 1 473  ? 112.173 123.284 153.411 1.00 34.24  0  437  ARG   A CZ  1 
ATOM   3106  N NH1 . ARG   A 1 473  ? 111.323 124.021 152.719 1.00 38.49  1  437  ARG   A NH1 1 
ATOM   3107  N NH2 . ARG   A 1 473  ? 112.552 123.688 154.619 1.00 37.48  0  437  ARG   A NH2 1 
ATOM   3108  N N   . GLN   A 1 474  ? 112.489 120.528 146.270 1.00 35.67  0  438  GLN   A N   1 
ATOM   3109  C CA  . GLN   A 1 474  ? 111.984 119.693 145.187 1.00 39.43  0  438  GLN   A CA  1 
ATOM   3110  C C   . GLN   A 1 474  ? 113.055 119.436 144.135 1.00 51.33  0  438  GLN   A C   1 
ATOM   3111  O O   . GLN   A 1 474  ? 113.184 118.311 143.634 1.00 57.48  0  438  GLN   A O   1 
ATOM   3112  C CB  . GLN   A 1 474  ? 110.754 120.344 144.558 1.00 39.72  0  438  GLN   A CB  1 
ATOM   3113  C CG  . GLN   A 1 474  ? 109.820 119.363 143.876 1.00 49.93  0  438  GLN   A CG  1 
ATOM   3114  C CD  . GLN   A 1 474  ? 109.367 118.251 144.801 1.00 50.98  0  438  GLN   A CD  1 
ATOM   3115  O OE1 . GLN   A 1 474  ? 109.026 118.491 145.960 1.00 51.14  0  438  GLN   A OE1 1 
ATOM   3116  N NE2 . GLN   A 1 474  ? 109.360 117.025 144.292 1.00 46.59  0  438  GLN   A NE2 1 
ATOM   3117  N N   . ALA   A 1 475  ? 113.834 120.460 143.791 1.00 34.14  0  439  ALA   A N   1 
ATOM   3118  C CA  . ALA   A 1 475  ? 114.872 120.285 142.782 1.00 30.42  0  439  ALA   A CA  1 
ATOM   3119  C C   . ALA   A 1 475  ? 115.916 119.278 143.241 1.00 36.07  0  439  ALA   A C   1 
ATOM   3120  O O   . ALA   A 1 475  ? 116.304 118.373 142.487 1.00 43.41  0  439  ALA   A O   1 
ATOM   3121  C CB  . ALA   A 1 475  ? 115.522 121.630 142.462 1.00 37.82  0  439  ALA   A CB  1 
ATOM   3122  N N   . MET   A 1 476  ? 116.374 119.398 144.486 1.00 33.22  0  440  MET   A N   1 
ATOM   3123  C CA  . MET   A 1 476  ? 117.427 118.478 144.886 1.00 36.51  0  440  MET   A CA  1 
ATOM   3124  C C   . MET   A 1 476  ? 116.879 117.089 145.208 1.00 37.30  0  440  MET   A C   1 
ATOM   3125  O O   . MET   A 1 476  ? 117.620 116.108 145.101 1.00 38.08  0  440  MET   A O   1 
ATOM   3126  C CB  . MET   A 1 476  ? 118.237 119.066 146.045 1.00 38.60  0  440  MET   A CB  1 
ATOM   3127  C CG  . MET   A 1 476  ? 118.871 118.053 146.968 1.00 39.20  0  440  MET   A CG  1 
ATOM   3128  S SD  . MET   A 1 476  ? 119.427 118.774 148.508 1.00 44.64  0  440  MET   A SD  1 
ATOM   3129  C CE  . MET   A 1 476  ? 117.924 118.616 149.425 1.00 37.87  0  440  MET   A CE  1 
ATOM   3130  N N   . ASP   A 1 477  ? 115.586 116.963 145.523 1.00 39.13  0  441  ASP   A N   1 
ATOM   3131  C CA  . ASP   A 1 477  ? 114.984 115.632 145.592 1.00 36.71  0  441  ASP   A CA  1 
ATOM   3132  C C   . ASP   A 1 477  ? 114.909 114.982 144.214 1.00 39.88  0  441  ASP   A C   1 
ATOM   3133  O O   . ASP   A 1 477  ? 115.143 113.772 144.073 1.00 42.15  0  441  ASP   A O   1 
ATOM   3134  C CB  . ASP   A 1 477  ? 113.595 115.713 146.217 1.00 39.18  0  441  ASP   A CB  1 
ATOM   3135  C CG  . ASP   A 1 477  ? 113.646 115.802 147.721 1.00 44.08  0  441  ASP   A CG  1 
ATOM   3136  O OD1 . ASP   A 1 477  ? 114.649 116.324 148.248 1.00 45.60  0  441  ASP   A OD1 1 
ATOM   3137  O OD2 . ASP   A 1 477  ? 112.689 115.342 148.378 1.00 42.61  -1 441  ASP   A OD2 1 
ATOM   3138  N N   . ALA   A 1 478  ? 114.577 115.766 143.187 1.00 43.25  0  442  ALA   A N   1 
ATOM   3139  C CA  . ALA   A 1 478  ? 114.598 115.240 141.827 1.00 47.91  0  442  ALA   A CA  1 
ATOM   3140  C C   . ALA   A 1 478  ? 115.997 114.773 141.448 1.00 43.37  0  442  ALA   A C   1 
ATOM   3141  O O   . ALA   A 1 478  ? 116.158 113.750 140.773 1.00 42.09  0  442  ALA   A O   1 
ATOM   3142  C CB  . ALA   A 1 478  ? 114.097 116.297 140.845 1.00 45.72  0  442  ALA   A CB  1 
ATOM   3143  N N   . VAL   A 1 479  ? 117.021 115.517 141.867 1.00 40.01  0  443  VAL   A N   1 
ATOM   3144  C CA  . VAL   A 1 479  ? 118.396 115.068 141.645 1.00 40.38  0  443  VAL   A CA  1 
ATOM   3145  C C   . VAL   A 1 479  ? 118.674 113.773 142.408 1.00 43.89  0  443  VAL   A C   1 
ATOM   3146  O O   . VAL   A 1 479  ? 119.301 112.845 141.879 1.00 45.38  0  443  VAL   A O   1 
ATOM   3147  C CB  . VAL   A 1 479  ? 119.388 116.178 142.029 1.00 41.49  0  443  VAL   A CB  1 
ATOM   3148  C CG1 . VAL   A 1 479  ? 120.806 115.650 142.015 1.00 45.50  0  443  VAL   A CG1 1 
ATOM   3149  C CG2 . VAL   A 1 479  ? 119.250 117.358 141.085 1.00 43.41  0  443  VAL   A CG2 1 
ATOM   3150  N N   . LYS   A 1 480  ? 118.217 113.690 143.662 1.00 46.61  0  444  LYS   A N   1 
ATOM   3151  C CA  . LYS   A 1 480  ? 118.435 112.490 144.466 1.00 41.56  0  444  LYS   A CA  1 
ATOM   3152  C C   . LYS   A 1 480  ? 117.850 111.259 143.794 1.00 35.37  0  444  LYS   A C   1 
ATOM   3153  O O   . LYS   A 1 480  ? 118.426 110.167 143.872 1.00 29.75  0  444  LYS   A O   1 
ATOM   3154  C CB  . LYS   A 1 480  ? 117.821 112.663 145.855 1.00 40.89  0  444  LYS   A CB  1 
ATOM   3155  C CG  . LYS   A 1 480  ? 117.370 111.354 146.491 1.00 34.37  0  444  LYS   A CG  1 
ATOM   3156  C CD  . LYS   A 1 480  ? 117.023 111.518 147.955 1.00 39.38  0  444  LYS   A CD  1 
ATOM   3157  C CE  . LYS   A 1 480  ? 115.606 112.021 148.142 1.00 43.28  0  444  LYS   A CE  1 
ATOM   3158  N NZ  . LYS   A 1 480  ? 115.247 112.113 149.586 1.00 40.20  1  444  LYS   A NZ  1 
ATOM   3159  N N   . ILE   A 1 481  ? 116.704 111.417 143.132 1.00 46.32  0  445  ILE   A N   1 
ATOM   3160  C CA  . ILE   A 1 481  ? 116.062 110.275 142.482 1.00 50.76  0  445  ILE   A CA  1 
ATOM   3161  C C   . ILE   A 1 481  ? 117.016 109.616 141.492 1.00 46.93  0  445  ILE   A C   1 
ATOM   3162  O O   . ILE   A 1 481  ? 117.093 108.385 141.406 1.00 49.18  0  445  ILE   A O   1 
ATOM   3163  C CB  . ILE   A 1 481  ? 114.750 110.714 141.805 1.00 53.20  0  445  ILE   A CB  1 
ATOM   3164  C CG1 . ILE   A 1 481  ? 113.685 111.020 142.860 1.00 51.52  0  445  ILE   A CG1 1 
ATOM   3165  C CG2 . ILE   A 1 481  ? 114.258 109.648 140.838 1.00 44.82  0  445  ILE   A CG2 1 
ATOM   3166  C CD1 . ILE   A 1 481  ? 113.433 109.879 143.824 1.00 47.98  0  445  ILE   A CD1 1 
ATOM   3167  N N   . ASN   A 1 482  ? 117.771 110.422 140.746 1.00 52.09  0  446  ASN   A N   1 
ATOM   3168  C CA  . ASN   A 1 482  ? 118.727 109.921 139.768 1.00 46.40  0  446  ASN   A CA  1 
ATOM   3169  C C   . ASN   A 1 482  ? 120.124 109.709 140.337 1.00 45.80  0  446  ASN   A C   1 
ATOM   3170  O O   . ASN   A 1 482  ? 120.984 109.179 139.626 1.00 44.23  0  446  ASN   A O   1 
ATOM   3171  C CB  . ASN   A 1 482  ? 118.822 110.888 138.586 1.00 43.09  0  446  ASN   A CB  1 
ATOM   3172  C CG  . ASN   A 1 482  ? 117.518 111.017 137.835 1.00 54.93  0  446  ASN   A CG  1 
ATOM   3173  O OD1 . ASN   A 1 482  ? 116.828 110.029 137.592 1.00 57.66  0  446  ASN   A OD1 1 
ATOM   3174  N ND2 . ASN   A 1 482  ? 117.166 112.242 137.470 1.00 52.48  0  446  ASN   A ND2 1 
ATOM   3175  N N   . CYS   A 1 483  ? 120.383 110.116 141.581 1.00 48.63  0  447  CYS   A N   1 
ATOM   3176  C CA  . CYS   A 1 483  ? 121.723 110.027 142.148 1.00 42.81  0  447  CYS   A CA  1 
ATOM   3177  C C   . CYS   A 1 483  ? 121.890 108.973 143.235 1.00 40.50  0  447  CYS   A C   1 
ATOM   3178  O O   . CYS   A 1 483  ? 122.980 108.872 143.807 1.00 32.43  0  447  CYS   A O   1 
ATOM   3179  C CB  . CYS   A 1 483  ? 122.150 111.387 142.705 1.00 47.07  0  447  CYS   A CB  1 
ATOM   3180  S SG  . CYS   A 1 483  ? 122.699 112.542 141.442 1.00 59.96  0  447  CYS   A SG  1 
ATOM   3181  N N   . ASN   A 1 484  ? 120.858 108.197 143.548 1.00 52.71  0  448  ASN   A N   1 
ATOM   3182  C CA  . ASN   A 1 484  ? 121.004 107.050 144.433 1.00 51.30  0  448  ASN   A CA  1 
ATOM   3183  C C   . ASN   A 1 484  ? 120.908 105.725 143.694 1.00 56.98  0  448  ASN   A C   1 
ATOM   3184  O O   . ASN   A 1 484  ? 121.160 104.675 144.295 1.00 56.48  0  448  ASN   A O   1 
ATOM   3185  C CB  . ASN   A 1 484  ? 119.942 107.081 145.539 1.00 50.07  0  448  ASN   A CB  1 
ATOM   3186  C CG  . ASN   A 1 484  ? 120.342 107.949 146.706 1.00 50.44  0  448  ASN   A CG  1 
ATOM   3187  O OD1 . ASN   A 1 484  ? 119.524 108.678 147.262 1.00 55.57  0  448  ASN   A OD1 1 
ATOM   3188  N ND2 . ASN   A 1 484  ? 121.607 107.878 147.084 1.00 49.69  0  448  ASN   A ND2 1 
ATOM   3189  N N   . GLU   A 1 485  ? 120.562 105.756 142.411 1.00 62.46  0  449  GLU   A N   1 
ATOM   3190  C CA  . GLU   A 1 485  ? 120.319 104.541 141.652 1.00 56.28  0  449  GLU   A CA  1 
ATOM   3191  C C   . GLU   A 1 485  ? 121.597 103.725 141.511 1.00 56.39  0  449  GLU   A C   1 
ATOM   3192  O O   . GLU   A 1 485  ? 122.686 104.264 141.302 1.00 60.50  0  449  GLU   A O   1 
ATOM   3193  C CB  . GLU   A 1 485  ? 119.760 104.898 140.275 1.00 52.11  0  449  GLU   A CB  1 
ATOM   3194  C CG  . GLU   A 1 485  ? 119.686 103.742 139.305 1.00 64.20  0  449  GLU   A CG  1 
ATOM   3195  C CD  . GLU   A 1 485  ? 118.881 104.078 138.071 1.00 67.55  0  449  GLU   A CD  1 
ATOM   3196  O OE1 . GLU   A 1 485  ? 118.863 105.264 137.681 1.00 63.67  0  449  GLU   A OE1 1 
ATOM   3197  O OE2 . GLU   A 1 485  ? 118.273 103.156 137.488 1.00 68.82  -1 449  GLU   A OE2 1 
ATOM   3198  N N   . THR   A 1 486  ? 121.456 102.409 141.641 1.00 63.13  0  450  THR   A N   1 
ATOM   3199  C CA  . THR   A 1 486  ? 122.558 101.488 141.415 1.00 61.87  0  450  THR   A CA  1 
ATOM   3200  C C   . THR   A 1 486  ? 122.707 101.240 139.922 1.00 60.19  0  450  THR   A C   1 
ATOM   3201  O O   . THR   A 1 486  ? 121.719 101.021 139.216 1.00 61.35  0  450  THR   A O   1 
ATOM   3202  C CB  . THR   A 1 486  ? 122.325 100.165 142.147 1.00 58.47  0  450  THR   A CB  1 
ATOM   3203  O OG1 . THR   A 1 486  ? 122.306 100.395 143.560 1.00 66.56  0  450  THR   A OG1 1 
ATOM   3204  C CG2 . THR   A 1 486  ? 123.425 99.180  141.830 1.00 57.84  0  450  THR   A CG2 1 
ATOM   3205  N N   . LYS   A 1 487  ? 123.945 101.289 139.443 1.00 46.25  0  451  LYS   A N   1 
ATOM   3206  C CA  . LYS   A 1 487  ? 124.253 101.111 138.034 1.00 43.95  0  451  LYS   A CA  1 
ATOM   3207  C C   . LYS   A 1 487  ? 124.999 99.800  137.841 1.00 49.66  0  451  LYS   A C   1 
ATOM   3208  O O   . LYS   A 1 487  ? 125.878 99.454  138.636 1.00 48.52  0  451  LYS   A O   1 
ATOM   3209  C CB  . LYS   A 1 487  ? 125.088 102.273 137.505 1.00 44.67  0  451  LYS   A CB  1 
ATOM   3210  C CG  . LYS   A 1 487  ? 124.500 103.637 137.795 1.00 45.28  0  451  LYS   A CG  1 
ATOM   3211  C CD  . LYS   A 1 487  ? 123.419 103.993 136.800 1.00 45.04  0  451  LYS   A CD  1 
ATOM   3212  C CE  . LYS   A 1 487  ? 123.017 105.445 136.933 1.00 43.66  0  451  LYS   A CE  1 
ATOM   3213  N NZ  . LYS   A 1 487  ? 122.068 105.853 135.868 1.00 41.51  1  451  LYS   A NZ  1 
ATOM   3214  N N   . PHE   A 1 488  ? 124.645 99.074  136.786 1.00 59.19  0  452  PHE   A N   1 
ATOM   3215  C CA  . PHE   A 1 488  ? 125.245 97.784  136.481 1.00 55.23  0  452  PHE   A CA  1 
ATOM   3216  C C   . PHE   A 1 488  ? 126.107 97.907  135.235 1.00 57.95  0  452  PHE   A C   1 
ATOM   3217  O O   . PHE   A 1 488  ? 125.636 98.368  134.191 1.00 59.99  0  452  PHE   A O   1 
ATOM   3218  C CB  . PHE   A 1 488  ? 124.167 96.722  136.287 1.00 60.99  0  452  PHE   A CB  1 
ATOM   3219  C CG  . PHE   A 1 488  ? 123.208 96.638  137.428 1.00 61.77  0  452  PHE   A CG  1 
ATOM   3220  C CD1 . PHE   A 1 488  ? 123.569 96.011  138.604 1.00 60.88  0  452  PHE   A CD1 1 
ATOM   3221  C CD2 . PHE   A 1 488  ? 121.952 97.200  137.334 1.00 62.20  0  452  PHE   A CD2 1 
ATOM   3222  C CE1 . PHE   A 1 488  ? 122.692 95.941  139.659 1.00 61.77  0  452  PHE   A CE1 1 
ATOM   3223  C CE2 . PHE   A 1 488  ? 121.073 97.129  138.385 1.00 62.68  0  452  PHE   A CE2 1 
ATOM   3224  C CZ  . PHE   A 1 488  ? 121.443 96.500  139.551 1.00 63.33  0  452  PHE   A CZ  1 
ATOM   3225  N N   . TYR   A 1 489  ? 127.360 97.481  135.347 1.00 50.16  0  453  TYR   A N   1 
ATOM   3226  C CA  . TYR   A 1 489  ? 128.361 97.681  134.312 1.00 48.99  0  453  TYR   A CA  1 
ATOM   3227  C C   . TYR   A 1 489  ? 128.895 96.344  133.829 1.00 49.46  0  453  TYR   A C   1 
ATOM   3228  O O   . TYR   A 1 489  ? 129.091 95.419  134.622 1.00 52.01  0  453  TYR   A O   1 
ATOM   3229  C CB  . TYR   A 1 489  ? 129.523 98.529  134.828 1.00 46.89  0  453  TYR   A CB  1 
ATOM   3230  C CG  . TYR   A 1 489  ? 129.122 99.886  135.342 1.00 42.96  0  453  TYR   A CG  1 
ATOM   3231  C CD1 . TYR   A 1 489  ? 128.361 100.743 134.568 1.00 41.26  0  453  TYR   A CD1 1 
ATOM   3232  C CD2 . TYR   A 1 489  ? 129.498 100.306 136.609 1.00 46.33  0  453  TYR   A CD2 1 
ATOM   3233  C CE1 . TYR   A 1 489  ? 127.994 101.981 135.036 1.00 47.04  0  453  TYR   A CE1 1 
ATOM   3234  C CE2 . TYR   A 1 489  ? 129.134 101.543 137.085 1.00 49.89  0  453  TYR   A CE2 1 
ATOM   3235  C CZ  . TYR   A 1 489  ? 128.383 102.378 136.294 1.00 53.11  0  453  TYR   A CZ  1 
ATOM   3236  O OH  . TYR   A 1 489  ? 128.016 103.616 136.765 1.00 49.50  0  453  TYR   A OH  1 
ATOM   3237  N N   . LEU   A 1 490  ? 129.133 96.254  132.525 1.00 45.79  0  454  LEU   A N   1 
ATOM   3238  C CA  . LEU   A 1 490  ? 129.821 95.116  131.936 1.00 45.83  0  454  LEU   A CA  1 
ATOM   3239  C C   . LEU   A 1 490  ? 131.321 95.370  132.016 1.00 49.63  0  454  LEU   A C   1 
ATOM   3240  O O   . LEU   A 1 490  ? 131.802 96.399  131.529 1.00 53.27  0  454  LEU   A O   1 
ATOM   3241  C CB  . LEU   A 1 490  ? 129.381 94.910  130.489 1.00 44.67  0  454  LEU   A CB  1 
ATOM   3242  C CG  . LEU   A 1 490  ? 128.476 93.711  130.205 1.00 49.19  0  454  LEU   A CG  1 
ATOM   3243  C CD1 . LEU   A 1 490  ? 128.554 93.330  128.740 1.00 50.00  0  454  LEU   A CD1 1 
ATOM   3244  C CD2 . LEU   A 1 490  ? 128.847 92.533  131.082 1.00 49.81  0  454  LEU   A CD2 1 
ATOM   3245  N N   . LEU   A 1 491  ? 132.056 94.435  132.628 1.00 46.89  0  455  LEU   A N   1 
ATOM   3246  C CA  . LEU   A 1 491  ? 133.489 94.631  132.828 1.00 44.72  0  455  LEU   A CA  1 
ATOM   3247  C C   . LEU   A 1 491  ? 134.209 94.891  131.516 1.00 38.36  0  455  LEU   A C   1 
ATOM   3248  O O   . LEU   A 1 491  ? 135.185 95.650  131.481 1.00 42.44  0  455  LEU   A O   1 
ATOM   3249  C CB  . LEU   A 1 491  ? 134.096 93.415  133.525 1.00 51.52  0  455  LEU   A CB  1 
ATOM   3250  C CG  . LEU   A 1 491  ? 135.509 93.612  134.073 1.00 49.90  0  455  LEU   A CG  1 
ATOM   3251  C CD1 . LEU   A 1 491  ? 135.506 94.657  135.171 1.00 45.39  0  455  LEU   A CD1 1 
ATOM   3252  C CD2 . LEU   A 1 491  ? 136.084 92.300  134.580 1.00 42.89  0  455  LEU   A CD2 1 
ATOM   3253  N N   . SER   A 1 492  ? 133.739 94.282  130.428 1.00 40.81  0  456  SER   A N   1 
ATOM   3254  C CA  . SER   A 1 492  ? 134.298 94.577  129.116 1.00 41.41  0  456  SER   A CA  1 
ATOM   3255  C C   . SER   A 1 492  ? 134.067 96.029  128.723 1.00 47.88  0  456  SER   A C   1 
ATOM   3256  O O   . SER   A 1 492  ? 134.955 96.655  128.142 1.00 52.86  0  456  SER   A O   1 
ATOM   3257  C CB  . SER   A 1 492  ? 133.700 93.648  128.065 1.00 43.54  0  456  SER   A CB  1 
ATOM   3258  O OG  . SER   A 1 492  ? 132.387 94.051  127.722 1.00 45.42  0  456  SER   A OG  1 
ATOM   3259  N N   . SER   A 1 493  ? 132.888 96.579  129.020 1.00 44.99  0  457  SER   A N   1 
ATOM   3260  C CA  . SER   A 1 493  ? 132.616 97.974  128.684 1.00 37.77  0  457  SER   A CA  1 
ATOM   3261  C C   . SER   A 1 493  ? 133.509 98.926  129.473 1.00 36.12  0  457  SER   A C   1 
ATOM   3262  O O   . SER   A 1 493  ? 134.026 99.905  128.919 1.00 41.84  0  457  SER   A O   1 
ATOM   3263  C CB  . SER   A 1 493  ? 131.143 98.289  128.928 1.00 43.92  0  457  SER   A CB  1 
ATOM   3264  O OG  . SER   A 1 493  ? 130.760 97.921  130.241 1.00 48.42  0  457  SER   A OG  1 
ATOM   3265  N N   . LEU   A 1 494  ? 133.698 98.662  130.768 1.00 30.08  0  458  LEU   A N   1 
ATOM   3266  C CA  . LEU   A 1 494  ? 134.608 99.483  131.559 1.00 35.54  0  458  LEU   A CA  1 
ATOM   3267  C C   . LEU   A 1 494  ? 136.034 99.379  131.036 1.00 41.32  0  458  LEU   A C   1 
ATOM   3268  O O   . LEU   A 1 494  ? 136.746 100.388 130.945 1.00 44.16  0  458  LEU   A O   1 
ATOM   3269  C CB  . LEU   A 1 494  ? 134.553 99.071  133.029 1.00 32.47  0  458  LEU   A CB  1 
ATOM   3270  C CG  . LEU   A 1 494  ? 133.209 99.187  133.738 1.00 28.67  0  458  LEU   A CG  1 
ATOM   3271  C CD1 . LEU   A 1 494  ? 133.371 98.884  135.210 1.00 33.03  0  458  LEU   A CD1 1 
ATOM   3272  C CD2 . LEU   A 1 494  ? 132.629 100.568 133.534 1.00 34.24  0  458  LEU   A CD2 1 
ATOM   3273  N N   . SER   A 1 495  ? 136.471 98.164  130.694 1.00 40.74  0  459  SER   A N   1 
ATOM   3274  C CA  . SER   A 1 495  ? 137.808 97.995  130.139 1.00 30.24  0  459  SER   A CA  1 
ATOM   3275  C C   . SER   A 1 495  ? 137.957 98.751  128.830 1.00 27.34  0  459  SER   A C   1 
ATOM   3276  O O   . SER   A 1 495  ? 138.993 99.368  128.582 1.00 34.82  0  459  SER   A O   1 
ATOM   3277  C CB  . SER   A 1 495  ? 138.115 96.514  129.936 1.00 40.61  0  459  SER   A CB  1 
ATOM   3278  O OG  . SER   A 1 495  ? 138.362 95.870  131.171 1.00 45.10  0  459  SER   A OG  1 
ATOM   3279  N N   . MET   A 1 496  ? 136.933 98.716  127.981 1.00 32.14  0  460  MET   A N   1 
ATOM   3280  C CA  . MET   A 1 496  ? 137.002 99.434  126.714 1.00 40.65  0  460  MET   A CA  1 
ATOM   3281  C C   . MET   A 1 496  ? 137.080 100.937 126.933 1.00 39.24  0  460  MET   A C   1 
ATOM   3282  O O   . MET   A 1 496  ? 137.844 101.627 126.252 1.00 41.14  0  460  MET   A O   1 
ATOM   3283  C CB  . MET   A 1 496  ? 135.794 99.085  125.847 1.00 39.22  0  460  MET   A CB  1 
ATOM   3284  C CG  . MET   A 1 496  ? 135.774 97.655  125.355 1.00 38.01  0  460  MET   A CG  1 
ATOM   3285  S SD  . MET   A 1 496  ? 135.072 97.459  123.715 1.00 59.37  0  460  MET   A SD  1 
ATOM   3286  C CE  . MET   A 1 496  ? 134.983 95.674  123.629 1.00 49.09  0  460  MET   A CE  1 
ATOM   3287  N N   . LEU   A 1 497  ? 136.297 101.469 127.873 1.00 35.23  0  461  LEU   A N   1 
ATOM   3288  C CA  . LEU   A 1 497  ? 136.342 102.906 128.130 1.00 34.14  0  461  LEU   A CA  1 
ATOM   3289  C C   . LEU   A 1 497  ? 137.704 103.325 128.672 1.00 41.77  0  461  LEU   A C   1 
ATOM   3290  O O   . LEU   A 1 497  ? 138.292 104.317 128.218 1.00 42.31  0  461  LEU   A O   1 
ATOM   3291  C CB  . LEU   A 1 497  ? 135.235 103.307 129.103 1.00 36.37  0  461  LEU   A CB  1 
ATOM   3292  C CG  . LEU   A 1 497  ? 135.211 104.797 129.443 1.00 39.88  0  461  LEU   A CG  1 
ATOM   3293  C CD1 . LEU   A 1 497  ? 134.968 105.621 128.188 1.00 37.02  0  461  LEU   A CD1 1 
ATOM   3294  C CD2 . LEU   A 1 497  ? 134.166 105.100 130.499 1.00 36.22  0  461  LEU   A CD2 1 
ATOM   3295  N N   . ARG   A 1 498  ? 138.228 102.571 129.642 1.00 37.88  0  462  ARG   A N   1 
ATOM   3296  C CA  . ARG   A 1 498  ? 139.544 102.885 130.187 1.00 28.43  0  462  ARG   A CA  1 
ATOM   3297  C C   . ARG   A 1 498  ? 140.626 102.755 129.124 1.00 34.44  0  462  ARG   A C   1 
ATOM   3298  O O   . ARG   A 1 498  ? 141.565 103.556 129.083 1.00 40.46  0  462  ARG   A O   1 
ATOM   3299  C CB  . ARG   A 1 498  ? 139.847 101.977 131.373 1.00 23.03  0  462  ARG   A CB  1 
ATOM   3300  C CG  . ARG   A 1 498  ? 141.186 102.236 132.017 1.00 21.15  0  462  ARG   A CG  1 
ATOM   3301  C CD  . ARG   A 1 498  ? 141.318 101.454 133.302 1.00 31.00  0  462  ARG   A CD  1 
ATOM   3302  N NE  . ARG   A 1 498  ? 142.361 101.990 134.164 1.00 29.91  0  462  ARG   A NE  1 
ATOM   3303  C CZ  . ARG   A 1 498  ? 143.615 101.563 134.166 1.00 29.78  0  462  ARG   A CZ  1 
ATOM   3304  N NH1 . ARG   A 1 498  ? 144.017 100.605 133.352 1.00 33.63  1  462  ARG   A NH1 1 
ATOM   3305  N NH2 . ARG   A 1 498  ? 144.485 102.111 135.007 1.00 29.83  0  462  ARG   A NH2 1 
ATOM   3306  N N   . GLY   A 1 499  ? 140.514 101.750 128.256 1.00 30.65  0  463  GLY   A N   1 
ATOM   3307  C CA  . GLY   A 1 499  ? 141.486 101.591 127.193 1.00 24.57  0  463  GLY   A CA  1 
ATOM   3308  C C   . GLY   A 1 499  ? 141.435 102.717 126.183 1.00 30.89  0  463  GLY   A C   1 
ATOM   3309  O O   . GLY   A 1 499  ? 142.470 103.151 125.684 1.00 40.18  0  463  GLY   A O   1 
ATOM   3310  N N   . ALA   A 1 500  ? 140.235 103.199 125.859 1.00 31.85  0  464  ALA   A N   1 
ATOM   3311  C CA  . ALA   A 1 500  ? 140.126 104.348 124.966 1.00 27.77  0  464  ALA   A CA  1 
ATOM   3312  C C   . ALA   A 1 500  ? 140.735 105.588 125.601 1.00 26.12  0  464  ALA   A C   1 
ATOM   3313  O O   . ALA   A 1 500  ? 141.418 106.370 124.928 1.00 35.77  0  464  ALA   A O   1 
ATOM   3314  C CB  . ALA   A 1 500  ? 138.666 104.594 124.598 1.00 32.04  0  464  ALA   A CB  1 
ATOM   3315  N N   . PHE   A 1 501  ? 140.508 105.776 126.900 1.00 30.02  0  465  PHE   A N   1 
ATOM   3316  C CA  . PHE   A 1 501  ? 141.128 106.889 127.610 1.00 31.41  0  465  PHE   A CA  1 
ATOM   3317  C C   . PHE   A 1 501  ? 142.650 106.794 127.563 1.00 27.40  0  465  PHE   A C   1 
ATOM   3318  O O   . PHE   A 1 501  ? 143.339 107.774 127.252 1.00 26.20  0  465  PHE   A O   1 
ATOM   3319  C CB  . PHE   A 1 501  ? 140.627 106.909 129.053 1.00 29.10  0  465  PHE   A CB  1 
ATOM   3320  C CG  . PHE   A 1 501  ? 141.212 108.002 129.884 1.00 27.82  0  465  PHE   A CG  1 
ATOM   3321  C CD1 . PHE   A 1 501  ? 140.802 109.308 129.718 1.00 29.88  0  465  PHE   A CD1 1 
ATOM   3322  C CD2 . PHE   A 1 501  ? 142.165 107.722 130.841 1.00 28.68  0  465  PHE   A CD2 1 
ATOM   3323  C CE1 . PHE   A 1 501  ? 141.338 110.309 130.484 1.00 35.72  0  465  PHE   A CE1 1 
ATOM   3324  C CE2 . PHE   A 1 501  ? 142.700 108.726 131.608 1.00 28.32  0  465  PHE   A CE2 1 
ATOM   3325  C CZ  . PHE   A 1 501  ? 142.286 110.019 131.429 1.00 32.23  0  465  PHE   A CZ  1 
ATOM   3326  N N   . ILE   A 1 502  ? 143.193 105.609 127.849 1.00 26.64  0  466  ILE   A N   1 
ATOM   3327  C CA  . ILE   A 1 502  ? 144.642 105.433 127.860 1.00 24.13  0  466  ILE   A CA  1 
ATOM   3328  C C   . ILE   A 1 502  ? 145.210 105.594 126.458 1.00 24.82  0  466  ILE   A C   1 
ATOM   3329  O O   . ILE   A 1 502  ? 146.305 106.134 126.274 1.00 32.00  0  466  ILE   A O   1 
ATOM   3330  C CB  . ILE   A 1 502  ? 145.013 104.070 128.470 1.00 24.33  0  466  ILE   A CB  1 
ATOM   3331  C CG1 . ILE   A 1 502  ? 144.723 104.063 129.965 1.00 29.69  0  466  ILE   A CG1 1 
ATOM   3332  C CG2 . ILE   A 1 502  ? 146.471 103.758 128.245 1.00 25.12  0  466  ILE   A CG2 1 
ATOM   3333  C CD1 . ILE   A 1 502  ? 145.206 102.823 130.658 1.00 33.13  0  466  ILE   A CD1 1 
ATOM   3334  N N   . TYR   A 1 503  ? 144.480 105.127 125.447 1.00 32.54  0  467  TYR   A N   1 
ATOM   3335  C CA  . TYR   A 1 503  ? 144.936 105.291 124.075 1.00 33.12  0  467  TYR   A CA  1 
ATOM   3336  C C   . TYR   A 1 503  ? 144.991 106.759 123.695 1.00 32.13  0  467  TYR   A C   1 
ATOM   3337  O O   . TYR   A 1 503  ? 145.922 107.195 123.012 1.00 44.62  0  467  TYR   A O   1 
ATOM   3338  C CB  . TYR   A 1 503  ? 144.024 104.530 123.119 1.00 34.10  0  467  TYR   A CB  1 
ATOM   3339  C CG  . TYR   A 1 503  ? 144.232 104.898 121.675 1.00 33.05  0  467  TYR   A CG  1 
ATOM   3340  C CD1 . TYR   A 1 503  ? 145.323 104.418 120.970 1.00 39.07  0  467  TYR   A CD1 1 
ATOM   3341  C CD2 . TYR   A 1 503  ? 143.340 105.729 121.015 1.00 29.34  0  467  TYR   A CD2 1 
ATOM   3342  C CE1 . TYR   A 1 503  ? 145.520 104.750 119.649 1.00 39.18  0  467  TYR   A CE1 1 
ATOM   3343  C CE2 . TYR   A 1 503  ? 143.530 106.068 119.693 1.00 38.11  0  467  TYR   A CE2 1 
ATOM   3344  C CZ  . TYR   A 1 503  ? 144.621 105.575 119.016 1.00 39.23  0  467  TYR   A CZ  1 
ATOM   3345  O OH  . TYR   A 1 503  ? 144.814 105.910 117.699 1.00 42.80  0  467  TYR   A OH  1 
ATOM   3346  N N   . ARG   A 1 504  ? 143.997 107.540 124.119 1.00 25.13  0  468  ARG   A N   1 
ATOM   3347  C CA  . ARG   A 1 504  ? 144.041 108.968 123.835 1.00 26.35  0  468  ARG   A CA  1 
ATOM   3348  C C   . ARG   A 1 504  ? 145.186 109.647 124.579 1.00 29.87  0  468  ARG   A C   1 
ATOM   3349  O O   . ARG   A 1 504  ? 145.829 110.549 124.031 1.00 31.12  0  468  ARG   A O   1 
ATOM   3350  C CB  . ARG   A 1 504  ? 142.705 109.617 124.183 1.00 22.59  0  468  ARG   A CB  1 
ATOM   3351  C CG  . ARG   A 1 504  ? 142.633 111.066 123.781 1.00 28.16  0  468  ARG   A CG  1 
ATOM   3352  C CD  . ARG   A 1 504  ? 142.619 111.206 122.281 1.00 22.19  0  468  ARG   A CD  1 
ATOM   3353  N NE  . ARG   A 1 504  ? 141.269 111.166 121.737 1.00 19.83  0  468  ARG   A NE  1 
ATOM   3354  C CZ  . ARG   A 1 504  ? 140.543 112.241 121.467 1.00 27.22  0  468  ARG   A CZ  1 
ATOM   3355  N NH1 . ARG   A 1 504  ? 141.002 113.459 121.693 1.00 30.28  1  468  ARG   A NH1 1 
ATOM   3356  N NH2 . ARG   A 1 504  ? 139.331 112.092 120.944 1.00 32.24  0  468  ARG   A NH2 1 
ATOM   3357  N N   . ILE   A 1 505  ? 145.467 109.214 125.810 1.00 31.53  0  469  ILE   A N   1 
ATOM   3358  C CA  . ILE   A 1 505  ? 146.615 109.744 126.548 1.00 26.16  0  469  ILE   A CA  1 
ATOM   3359  C C   . ILE   A 1 505  ? 147.912 109.454 125.799 1.00 31.55  0  469  ILE   A C   1 
ATOM   3360  O O   . ILE   A 1 505  ? 148.772 110.329 125.637 1.00 37.08  0  469  ILE   A O   1 
ATOM   3361  C CB  . ILE   A 1 505  ? 146.652 109.159 127.971 1.00 24.37  0  469  ILE   A CB  1 
ATOM   3362  C CG1 . ILE   A 1 505  ? 145.490 109.694 128.805 1.00 25.63  0  469  ILE   A CG1 1 
ATOM   3363  C CG2 . ILE   A 1 505  ? 147.979 109.453 128.640 1.00 19.61  0  469  ILE   A CG2 1 
ATOM   3364  C CD1 . ILE   A 1 505  ? 145.555 111.167 129.067 1.00 28.58  0  469  ILE   A CD1 1 
ATOM   3365  N N   . ILE   A 1 506  ? 148.070 108.213 125.334 1.00 32.52  0  470  ILE   A N   1 
ATOM   3366  C CA  . ILE   A 1 506  ? 149.286 107.811 124.629 1.00 24.01  0  470  ILE   A CA  1 
ATOM   3367  C C   . ILE   A 1 506  ? 149.424 108.581 123.324 1.00 19.14  0  470  ILE   A C   1 
ATOM   3368  O O   . ILE   A 1 506  ? 150.514 109.037 122.962 1.00 29.96  0  470  ILE   A O   1 
ATOM   3369  C CB  . ILE   A 1 506  ? 149.280 106.291 124.386 1.00 33.58  0  470  ILE   A CB  1 
ATOM   3370  C CG1 . ILE   A 1 506  ? 149.573 105.541 125.681 1.00 35.15  0  470  ILE   A CG1 1 
ATOM   3371  C CG2 . ILE   A 1 506  ? 150.271 105.912 123.306 1.00 30.41  0  470  ILE   A CG2 1 
ATOM   3372  C CD1 . ILE   A 1 506  ? 149.035 104.139 125.693 1.00 29.78  0  470  ILE   A CD1 1 
ATOM   3373  N N   . LYS   A 1 507  ? 148.320 108.722 122.589 1.00 17.39  0  471  LYS   A N   1 
ATOM   3374  C CA  . LYS   A 1 507  ? 148.352 109.462 121.335 1.00 20.24  0  471  LYS   A CA  1 
ATOM   3375  C C   . LYS   A 1 507  ? 148.731 110.917 121.567 1.00 34.88  0  471  LYS   A C   1 
ATOM   3376  O O   . LYS   A 1 507  ? 149.524 111.487 120.810 1.00 47.38  0  471  LYS   A O   1 
ATOM   3377  C CB  . LYS   A 1 507  ? 146.997 109.358 120.639 1.00 22.47  0  471  LYS   A CB  1 
ATOM   3378  C CG  . LYS   A 1 507  ? 146.788 110.369 119.536 1.00 33.11  0  471  LYS   A CG  1 
ATOM   3379  C CD  . LYS   A 1 507  ? 145.346 110.386 119.071 1.00 36.23  0  471  LYS   A CD  1 
ATOM   3380  C CE  . LYS   A 1 507  ? 145.073 111.599 118.201 1.00 37.14  0  471  LYS   A CE  1 
ATOM   3381  N NZ  . LYS   A 1 507  ? 143.630 111.736 117.873 1.00 37.21  1  471  LYS   A NZ  1 
ATOM   3382  N N   . GLY   A 1 508  ? 148.186 111.533 122.617 1.00 31.54  0  472  GLY   A N   1 
ATOM   3383  C CA  . GLY   A 1 508  ? 148.555 112.905 122.927 1.00 26.24  0  472  GLY   A CA  1 
ATOM   3384  C C   . GLY   A 1 508  ? 150.018 113.045 123.305 1.00 22.80  0  472  GLY   A C   1 
ATOM   3385  O O   . GLY   A 1 508  ? 150.693 113.983 122.874 1.00 23.37  0  472  GLY   A O   1 
ATOM   3386  N N   . PHE   A 1 509  ? 150.526 112.118 124.119 1.00 24.66  0  473  PHE   A N   1 
ATOM   3387  C CA  . PHE   A 1 509  ? 151.941 112.121 124.476 1.00 23.23  0  473  PHE   A CA  1 
ATOM   3388  C C   . PHE   A 1 509  ? 152.819 112.030 123.237 1.00 36.21  0  473  PHE   A C   1 
ATOM   3389  O O   . PHE   A 1 509  ? 153.745 112.827 123.065 1.00 37.17  0  473  PHE   A O   1 
ATOM   3390  C CB  . PHE   A 1 509  ? 152.273 110.963 125.415 1.00 30.63  0  473  PHE   A CB  1 
ATOM   3391  C CG  . PHE   A 1 509  ? 152.544 111.380 126.827 1.00 34.29  0  473  PHE   A CG  1 
ATOM   3392  C CD1 . PHE   A 1 509  ? 151.515 111.741 127.671 1.00 32.31  0  473  PHE   A CD1 1 
ATOM   3393  C CD2 . PHE   A 1 509  ? 153.838 111.406 127.311 1.00 33.16  0  473  PHE   A CD2 1 
ATOM   3394  C CE1 . PHE   A 1 509  ? 151.771 112.119 128.971 1.00 30.03  0  473  PHE   A CE1 1 
ATOM   3395  C CE2 . PHE   A 1 509  ? 154.099 111.784 128.608 1.00 36.05  0  473  PHE   A CE2 1 
ATOM   3396  C CZ  . PHE   A 1 509  ? 153.065 112.142 129.439 1.00 29.48  0  473  PHE   A CZ  1 
ATOM   3397  N N   . VAL   A 1 510  ? 152.527 111.065 122.364 1.00 52.41  0  474  VAL   A N   1 
ATOM   3398  C CA  . VAL   A 1 510  ? 153.349 110.855 121.176 1.00 35.04  0  474  VAL   A CA  1 
ATOM   3399  C C   . VAL   A 1 510  ? 153.269 112.047 120.234 1.00 39.86  0  474  VAL   A C   1 
ATOM   3400  O O   . VAL   A 1 510  ? 154.276 112.444 119.637 1.00 45.49  0  474  VAL   A O   1 
ATOM   3401  C CB  . VAL   A 1 510  ? 152.938 109.545 120.475 1.00 29.13  0  474  VAL   A CB  1 
ATOM   3402  C CG1 . VAL   A 1 510  ? 153.628 109.421 119.137 1.00 43.34  0  474  VAL   A CG1 1 
ATOM   3403  C CG2 . VAL   A 1 510  ? 153.276 108.358 121.353 1.00 27.36  0  474  VAL   A CG2 1 
ATOM   3404  N N   . ASN   A 1 511  ? 152.086 112.641 120.082 1.00 35.79  0  475  ASN   A N   1 
ATOM   3405  C CA  . ASN   A 1 511  ? 151.957 113.793 119.198 1.00 39.16  0  475  ASN   A CA  1 
ATOM   3406  C C   . ASN   A 1 511  ? 152.646 115.026 119.771 1.00 43.16  0  475  ASN   A C   1 
ATOM   3407  O O   . ASN   A 1 511  ? 153.166 115.854 119.015 1.00 45.23  0  475  ASN   A O   1 
ATOM   3408  C CB  . ASN   A 1 511  ? 150.482 114.087 118.933 1.00 38.32  0  475  ASN   A CB  1 
ATOM   3409  C CG  . ASN   A 1 511  ? 149.930 113.286 117.779 1.00 44.78  0  475  ASN   A CG  1 
ATOM   3410  O OD1 . ASN   A 1 511  ? 150.531 112.304 117.350 1.00 42.95  0  475  ASN   A OD1 1 
ATOM   3411  N ND2 . ASN   A 1 511  ? 148.781 113.702 117.266 1.00 45.76  0  475  ASN   A ND2 1 
ATOM   3412  N N   . ASN   A 1 512  ? 152.660 115.169 121.097 1.00 41.61  0  476  ASN   A N   1 
ATOM   3413  C CA  . ASN   A 1 512  ? 153.200 116.358 121.746 1.00 39.38  0  476  ASN   A CA  1 
ATOM   3414  C C   . ASN   A 1 512  ? 154.636 116.156 122.217 1.00 42.55  0  476  ASN   A C   1 
ATOM   3415  O O   . ASN   A 1 512  ? 155.533 116.908 121.827 1.00 47.85  0  476  ASN   A O   1 
ATOM   3416  C CB  . ASN   A 1 512  ? 152.308 116.756 122.929 1.00 38.67  0  476  ASN   A CB  1 
ATOM   3417  C CG  . ASN   A 1 512  ? 150.921 117.176 122.496 1.00 46.46  0  476  ASN   A CG  1 
ATOM   3418  O OD1 . ASN   A 1 512  ? 150.750 117.846 121.479 1.00 49.26  0  476  ASN   A OD1 1 
ATOM   3419  N ND2 . ASN   A 1 512  ? 149.918 116.775 123.263 1.00 47.05  0  476  ASN   A ND2 1 
ATOM   3420  N N   . TYR   A 1 513  ? 154.870 115.150 123.054 1.00 45.03  0  477  TYR   A N   1 
ATOM   3421  C CA  . TYR   A 1 513  ? 156.179 114.908 123.642 1.00 38.00  0  477  TYR   A CA  1 
ATOM   3422  C C   . TYR   A 1 513  ? 157.020 113.936 122.828 1.00 38.36  0  477  TYR   A C   1 
ATOM   3423  O O   . TYR   A 1 513  ? 158.160 113.658 123.209 1.00 40.10  0  477  TYR   A O   1 
ATOM   3424  C CB  . TYR   A 1 513  ? 156.024 114.382 125.068 1.00 35.47  0  477  TYR   A CB  1 
ATOM   3425  C CG  . TYR   A 1 513  ? 155.363 115.358 126.010 1.00 33.30  0  477  TYR   A CG  1 
ATOM   3426  C CD1 . TYR   A 1 513  ? 155.248 116.698 125.683 1.00 36.16  0  477  TYR   A CD1 1 
ATOM   3427  C CD2 . TYR   A 1 513  ? 154.850 114.936 127.226 1.00 39.30  0  477  TYR   A CD2 1 
ATOM   3428  C CE1 . TYR   A 1 513  ? 154.643 117.591 126.539 1.00 47.79  0  477  TYR   A CE1 1 
ATOM   3429  C CE2 . TYR   A 1 513  ? 154.245 115.822 128.089 1.00 40.83  0  477  TYR   A CE2 1 
ATOM   3430  C CZ  . TYR   A 1 513  ? 154.144 117.148 127.741 1.00 47.71  0  477  TYR   A CZ  1 
ATOM   3431  O OH  . TYR   A 1 513  ? 153.542 118.040 128.597 1.00 48.45  0  477  TYR   A OH  1 
ATOM   3432  N N   . ASN   A 1 514  ? 156.480 113.415 121.725 1.00 43.39  0  478  ASN   A N   1 
ATOM   3433  C CA  . ASN   A 1 514  ? 157.196 112.488 120.849 1.00 47.61  0  478  ASN   A CA  1 
ATOM   3434  C C   . ASN   A 1 514  ? 157.751 111.304 121.633 1.00 48.25  0  478  ASN   A C   1 
ATOM   3435  O O   . ASN   A 1 514  ? 158.867 110.841 121.397 1.00 45.19  0  478  ASN   A O   1 
ATOM   3436  C CB  . ASN   A 1 514  ? 158.304 113.208 120.080 1.00 44.37  0  478  ASN   A CB  1 
ATOM   3437  C CG  . ASN   A 1 514  ? 157.787 114.400 119.300 1.00 48.80  0  478  ASN   A CG  1 
ATOM   3438  O OD1 . ASN   A 1 514  ? 156.808 114.296 118.563 1.00 45.44  0  478  ASN   A OD1 1 
ATOM   3439  N ND2 . ASN   A 1 514  ? 158.440 115.544 119.464 1.00 52.00  0  478  ASN   A ND2 1 
ATOM   3440  N N   . ARG   A 1 515  ? 156.954 110.804 122.573 1.00 47.72  0  479  ARG   A N   1 
ATOM   3441  C CA  . ARG   A 1 515  ? 157.416 109.753 123.465 1.00 47.32  0  479  ARG   A CA  1 
ATOM   3442  C C   . ARG   A 1 515  ? 156.220 109.094 124.135 1.00 52.89  0  479  ARG   A C   1 
ATOM   3443  O O   . ARG   A 1 515  ? 155.211 109.744 124.416 1.00 52.55  0  479  ARG   A O   1 
ATOM   3444  C CB  . ARG   A 1 515  ? 158.373 110.315 124.518 1.00 38.24  0  479  ARG   A CB  1 
ATOM   3445  C CG  . ARG   A 1 515  ? 159.295 109.296 125.139 1.00 40.16  0  479  ARG   A CG  1 
ATOM   3446  C CD  . ARG   A 1 515  ? 160.062 109.926 126.275 1.00 39.57  0  479  ARG   A CD  1 
ATOM   3447  N NE  . ARG   A 1 515  ? 159.195 110.778 127.078 1.00 46.71  0  479  ARG   A NE  1 
ATOM   3448  C CZ  . ARG   A 1 515  ? 158.918 110.565 128.355 1.00 50.54  0  479  ARG   A CZ  1 
ATOM   3449  N NH1 . ARG   A 1 515  ? 159.445 109.549 129.014 1.00 49.06  1  479  ARG   A NH1 1 
ATOM   3450  N NH2 . ARG   A 1 515  ? 158.093 111.394 128.987 1.00 48.09  0  479  ARG   A NH2 1 
ATOM   3451  N N   . TRP   A 1 516  ? 156.343 107.803 124.372 1.00 49.07  0  480  TRP   A N   1 
ATOM   3452  C CA  . TRP   A 1 516  ? 155.386 107.070 125.186 1.00 41.17  0  480  TRP   A CA  1 
ATOM   3453  C C   . TRP   A 1 516  ? 155.606 107.375 126.664 1.00 49.92  0  480  TRP   A C   1 
ATOM   3454  O O   . TRP   A 1 516  ? 156.750 107.483 127.109 1.00 58.58  0  480  TRP   A O   1 
ATOM   3455  C CB  . TRP   A 1 516  ? 155.525 105.573 124.947 1.00 41.76  0  480  TRP   A CB  1 
ATOM   3456  C CG  . TRP   A 1 516  ? 154.710 105.063 123.817 1.00 43.80  0  480  TRP   A CG  1 
ATOM   3457  C CD1 . TRP   A 1 516  ? 154.845 105.373 122.501 1.00 45.47  0  480  TRP   A CD1 1 
ATOM   3458  C CD2 . TRP   A 1 516  ? 153.664 104.093 123.898 1.00 45.48  0  480  TRP   A CD2 1 
ATOM   3459  N NE1 . TRP   A 1 516  ? 153.920 104.684 121.756 1.00 46.00  0  480  TRP   A NE1 1 
ATOM   3460  C CE2 . TRP   A 1 516  ? 153.185 103.887 122.592 1.00 45.81  0  480  TRP   A CE2 1 
ATOM   3461  C CE3 . TRP   A 1 516  ? 153.076 103.387 124.951 1.00 43.93  0  480  TRP   A CE3 1 
ATOM   3462  C CZ2 . TRP   A 1 516  ? 152.148 103.006 122.310 1.00 46.43  0  480  TRP   A CZ2 1 
ATOM   3463  C CZ3 . TRP   A 1 516  ? 152.049 102.513 124.670 1.00 44.72  0  480  TRP   A CZ3 1 
ATOM   3464  C CH2 . TRP   A 1 516  ? 151.594 102.330 123.360 1.00 46.09  0  480  TRP   A CH2 1 
ATOM   3465  N N   . PRO   A 1 517  ? 154.536 107.526 127.441 1.00 37.26  0  481  PRO   A N   1 
ATOM   3466  C CA  . PRO   A 1 517  ? 154.699 107.627 128.893 1.00 31.45  0  481  PRO   A CA  1 
ATOM   3467  C C   . PRO   A 1 517  ? 155.369 106.375 129.431 1.00 40.01  0  481  PRO   A C   1 
ATOM   3468  O O   . PRO   A 1 517  ? 155.069 105.259 129.005 1.00 50.97  0  481  PRO   A O   1 
ATOM   3469  C CB  . PRO   A 1 517  ? 153.264 107.764 129.408 1.00 32.99  0  481  PRO   A CB  1 
ATOM   3470  C CG  . PRO   A 1 517  ? 152.466 108.194 128.235 1.00 36.11  0  481  PRO   A CG  1 
ATOM   3471  C CD  . PRO   A 1 517  ? 153.130 107.636 127.026 1.00 32.05  0  481  PRO   A CD  1 
ATOM   3472  N N   . THR   A 1 518  ? 156.285 106.563 130.374 1.00 40.84  0  482  THR   A N   1 
ATOM   3473  C CA  . THR   A 1 518  ? 157.081 105.446 130.873 1.00 48.31  0  482  THR   A CA  1 
ATOM   3474  C C   . THR   A 1 518  ? 156.191 104.521 131.689 1.00 49.71  0  482  THR   A C   1 
ATOM   3475  O O   . THR   A 1 518  ? 155.857 104.810 132.840 1.00 54.07  0  482  THR   A O   1 
ATOM   3476  C CB  . THR   A 1 518  ? 158.257 105.948 131.700 1.00 49.86  0  482  THR   A CB  1 
ATOM   3477  O OG1 . THR   A 1 518  ? 157.814 106.253 133.026 1.00 45.32  0  482  THR   A OG1 1 
ATOM   3478  C CG2 . THR   A 1 518  ? 158.855 107.183 131.074 1.00 48.86  0  482  THR   A CG2 1 
ATOM   3479  N N   . LEU   A 1 519  ? 155.808 103.399 131.088 1.00 44.08  0  483  LEU   A N   1 
ATOM   3480  C CA  . LEU   A 1 519  ? 155.005 102.404 131.776 1.00 41.60  0  483  LEU   A CA  1 
ATOM   3481  C C   . LEU   A 1 519  ? 155.835 101.698 132.837 1.00 45.33  0  483  LEU   A C   1 
ATOM   3482  O O   . LEU   A 1 519  ? 157.049 101.531 132.699 1.00 49.96  0  483  LEU   A O   1 
ATOM   3483  C CB  . LEU   A 1 519  ? 154.462 101.385 130.779 1.00 42.59  0  483  LEU   A CB  1 
ATOM   3484  C CG  . LEU   A 1 519  ? 154.184 101.919 129.376 1.00 43.82  0  483  LEU   A CG  1 
ATOM   3485  C CD1 . LEU   A 1 519  ? 153.955 100.777 128.411 1.00 45.35  0  483  LEU   A CD1 1 
ATOM   3486  C CD2 . LEU   A 1 519  ? 152.988 102.844 129.388 1.00 46.95  0  483  LEU   A CD2 1 
ATOM   3487  N N   . ARG   A 1 520  ? 155.171 101.283 133.912 1.00 48.19  0  484  ARG   A N   1 
ATOM   3488  C CA  . ARG   A 1 520  ? 155.836 100.528 134.963 1.00 52.37  0  484  ARG   A CA  1 
ATOM   3489  C C   . ARG   A 1 520  ? 155.589 99.030  134.863 1.00 54.81  0  484  ARG   A C   1 
ATOM   3490  O O   . ARG   A 1 520  ? 156.246 98.263  135.573 1.00 57.03  0  484  ARG   A O   1 
ATOM   3491  C CB  . ARG   A 1 520  ? 155.396 101.032 136.343 1.00 46.05  0  484  ARG   A CB  1 
ATOM   3492  C CG  . ARG   A 1 520  ? 154.039 100.541 136.793 1.00 48.21  0  484  ARG   A CG  1 
ATOM   3493  C CD  . ARG   A 1 520  ? 153.728 101.013 138.202 1.00 48.93  0  484  ARG   A CD  1 
ATOM   3494  N NE  . ARG   A 1 520  ? 153.532 102.456 138.263 1.00 55.92  0  484  ARG   A NE  1 
ATOM   3495  C CZ  . ARG   A 1 520  ? 154.078 103.251 139.173 1.00 56.10  0  484  ARG   A CZ  1 
ATOM   3496  N NH1 . ARG   A 1 520  ? 154.866 102.777 140.123 1.00 56.69  1  484  ARG   A NH1 1 
ATOM   3497  N NH2 . ARG   A 1 520  ? 153.822 104.555 139.131 1.00 49.68  0  484  ARG   A NH2 1 
ATOM   3498  N N   . ASN   A 1 521  ? 154.660 98.598  134.012 1.00 46.10  0  485  ASN   A N   1 
ATOM   3499  C CA  . ASN   A 1 521  ? 154.388 97.185  133.790 1.00 42.73  0  485  ASN   A CA  1 
ATOM   3500  C C   . ASN   A 1 521  ? 154.245 96.930  132.288 1.00 44.06  0  485  ASN   A C   1 
ATOM   3501  O O   . ASN   A 1 521  ? 153.289 96.324  131.817 1.00 54.92  0  485  ASN   A O   1 
ATOM   3502  C CB  . ASN   A 1 521  ? 153.151 96.730  134.562 1.00 49.30  0  485  ASN   A CB  1 
ATOM   3503  C CG  . ASN   A 1 521  ? 151.914 97.519  134.204 1.00 52.15  0  485  ASN   A CG  1 
ATOM   3504  O OD1 . ASN   A 1 521  ? 151.961 98.438  133.388 1.00 53.96  0  485  ASN   A OD1 1 
ATOM   3505  N ND2 . ASN   A 1 521  ? 150.793 97.167  134.820 1.00 48.65  0  485  ASN   A ND2 1 
ATOM   3506  N N   . ALA   A 1 522  ? 155.214 97.419  131.511 1.00 46.41  0  486  ALA   A N   1 
ATOM   3507  C CA  . ALA   A 1 522  ? 155.150 97.322  130.055 1.00 48.24  0  486  ALA   A CA  1 
ATOM   3508  C C   . ALA   A 1 522  ? 155.155 95.889  129.543 1.00 50.68  0  486  ALA   A C   1 
ATOM   3509  O O   . ALA   A 1 522  ? 155.064 95.689  128.327 1.00 54.08  0  486  ALA   A O   1 
ATOM   3510  C CB  . ALA   A 1 522  ? 156.315 98.085  129.429 1.00 49.58  0  486  ALA   A CB  1 
ATOM   3511  N N   . ILE   A 1 523  ? 155.258 94.894  130.428 1.00 61.33  0  487  ILE   A N   1 
ATOM   3512  C CA  . ILE   A 1 523  ? 155.236 93.496  130.005 1.00 62.44  0  487  ILE   A CA  1 
ATOM   3513  C C   . ILE   A 1 523  ? 153.881 93.120  129.427 1.00 60.54  0  487  ILE   A C   1 
ATOM   3514  O O   . ILE   A 1 523  ? 153.763 92.133  128.692 1.00 65.93  0  487  ILE   A O   1 
ATOM   3515  C CB  . ILE   A 1 523  ? 155.604 92.586  131.190 1.00 60.97  0  487  ILE   A CB  1 
ATOM   3516  C CG1 . ILE   A 1 523  ? 154.647 92.838  132.355 1.00 57.04  0  487  ILE   A CG1 1 
ATOM   3517  C CG2 . ILE   A 1 523  ? 157.038 92.825  131.614 1.00 59.10  0  487  ILE   A CG2 1 
ATOM   3518  C CD1 . ILE   A 1 523  ? 154.948 92.026  133.586 1.00 58.32  0  487  ILE   A CD1 1 
ATOM   3519  N N   . VAL   A 1 524  ? 152.841 93.891  129.747 1.00 49.67  0  488  VAL   A N   1 
ATOM   3520  C CA  . VAL   A 1 524  ? 151.486 93.537  129.339 1.00 52.24  0  488  VAL   A CA  1 
ATOM   3521  C C   . VAL   A 1 524  ? 151.352 93.571  127.822 1.00 50.86  0  488  VAL   A C   1 
ATOM   3522  O O   . VAL   A 1 524  ? 150.697 92.709  127.224 1.00 55.99  0  488  VAL   A O   1 
ATOM   3523  C CB  . VAL   A 1 524  ? 150.472 94.467  130.032 1.00 54.59  0  488  VAL   A CB  1 
ATOM   3524  C CG1 . VAL   A 1 524  ? 149.167 94.531  129.256 1.00 54.26  0  488  VAL   A CG1 1 
ATOM   3525  C CG2 . VAL   A 1 524  ? 150.230 94.010  131.461 1.00 46.26  0  488  VAL   A CG2 1 
ATOM   3526  N N   . LEU   A 1 525  ? 151.971 94.553  127.178 1.00 53.18  0  489  LEU   A N   1 
ATOM   3527  C CA  . LEU   A 1 525  ? 151.902 94.689  125.728 1.00 63.13  0  489  LEU   A CA  1 
ATOM   3528  C C   . LEU   A 1 525  ? 152.430 93.424  125.057 1.00 61.85  0  489  LEU   A C   1 
ATOM   3529  O O   . LEU   A 1 525  ? 153.633 93.140  125.156 1.00 57.93  0  489  LEU   A O   1 
ATOM   3530  C CB  . LEU   A 1 525  ? 152.705 95.906  125.287 1.00 59.38  0  489  LEU   A CB  1 
ATOM   3531  C CG  . LEU   A 1 525  ? 152.333 97.206  126.000 1.00 54.80  0  489  LEU   A CG  1 
ATOM   3532  C CD1 . LEU   A 1 525  ? 153.161 98.364  125.479 1.00 56.67  0  489  LEU   A CD1 1 
ATOM   3533  C CD2 . LEU   A 1 525  ? 150.849 97.492  125.855 1.00 56.14  0  489  LEU   A CD2 1 
ATOM   3534  N N   . PRO   A 1 526  ? 151.580 92.630  124.394 1.00 61.96  0  490  PRO   A N   1 
ATOM   3535  C CA  . PRO   A 1 526  ? 151.979 91.257  124.053 1.00 61.05  0  490  PRO   A CA  1 
ATOM   3536  C C   . PRO   A 1 526  ? 153.157 91.137  123.099 1.00 66.08  0  490  PRO   A C   1 
ATOM   3537  O O   . PRO   A 1 526  ? 154.238 90.701  123.505 1.00 72.72  0  490  PRO   A O   1 
ATOM   3538  C CB  . PRO   A 1 526  ? 150.710 90.677  123.408 1.00 61.59  0  490  PRO   A CB  1 
ATOM   3539  C CG  . PRO   A 1 526  ? 149.624 91.691  123.639 1.00 64.17  0  490  PRO   A CG  1 
ATOM   3540  C CD  . PRO   A 1 526  ? 150.298 93.001  123.781 1.00 60.81  0  490  PRO   A CD  1 
ATOM   3541  N N   . LEU   A 1 527  ? 152.971 91.519  121.835 1.00 65.27  0  491  LEU   A N   1 
ATOM   3542  C CA  . LEU   A 1 527  ? 154.077 91.497  120.884 1.00 64.05  0  491  LEU   A CA  1 
ATOM   3543  C C   . LEU   A 1 527  ? 154.110 92.741  120.011 1.00 62.15  0  491  LEU   A C   1 
ATOM   3544  O O   . LEU   A 1 527  ? 155.182 93.281  119.721 1.00 62.28  0  491  LEU   A O   1 
ATOM   3545  C CB  . LEU   A 1 527  ? 154.001 90.252  120.001 1.00 66.68  0  491  LEU   A CB  1 
ATOM   3546  C CG  . LEU   A 1 527  ? 155.052 90.193  118.891 1.00 66.92  0  491  LEU   A CG  1 
ATOM   3547  C CD1 . LEU   A 1 527  ? 156.447 90.083  119.487 1.00 61.50  0  491  LEU   A CD1 1 
ATOM   3548  C CD2 . LEU   A 1 527  ? 154.774 89.044  117.937 1.00 64.81  0  491  LEU   A CD2 1 
ATOM   3549  N N   . ARG   A 1 528  ? 152.933 93.197  119.582 1.00 57.74  0  492  ARG   A N   1 
ATOM   3550  C CA  . ARG   A 1 528  ? 152.867 94.297  118.630 1.00 57.69  0  492  ARG   A CA  1 
ATOM   3551  C C   . ARG   A 1 528  ? 152.835 95.638  119.339 1.00 60.66  0  492  ARG   A C   1 
ATOM   3552  O O   . ARG   A 1 528  ? 153.463 96.600  118.884 1.00 59.27  0  492  ARG   A O   1 
ATOM   3553  C CB  . ARG   A 1 528  ? 151.645 94.147  117.728 1.00 59.40  0  492  ARG   A CB  1 
ATOM   3554  C CG  . ARG   A 1 528  ? 151.583 95.178  116.617 1.00 60.67  0  492  ARG   A CG  1 
ATOM   3555  C CD  . ARG   A 1 528  ? 150.368 94.973  115.731 1.00 60.45  0  492  ARG   A CD  1 
ATOM   3556  N NE  . ARG   A 1 528  ? 149.130 95.341  116.406 1.00 62.10  0  492  ARG   A NE  1 
ATOM   3557  C CZ  . ARG   A 1 528  ? 148.169 94.485  116.724 1.00 63.40  0  492  ARG   A CZ  1 
ATOM   3558  N NH1 . ARG   A 1 528  ? 148.268 93.198  116.438 1.00 59.59  1  492  ARG   A NH1 1 
ATOM   3559  N NH2 . ARG   A 1 528  ? 147.080 94.933  117.343 1.00 61.24  0  492  ARG   A NH2 1 
ATOM   3560  N N   . TRP   A 1 529  ? 152.107 95.722  120.452 1.00 63.28  0  493  TRP   A N   1 
ATOM   3561  C CA  . TRP   A 1 529  ? 152.136 96.944  121.240 1.00 62.34  0  493  TRP   A CA  1 
ATOM   3562  C C   . TRP   A 1 529  ? 153.517 97.184  121.834 1.00 65.14  0  493  TRP   A C   1 
ATOM   3563  O O   . TRP   A 1 529  ? 153.912 98.337  122.025 1.00 65.53  0  493  TRP   A O   1 
ATOM   3564  C CB  . TRP   A 1 529  ? 151.066 96.892  122.327 1.00 53.72  0  493  TRP   A CB  1 
ATOM   3565  C CG  . TRP   A 1 529  ? 149.694 97.109  121.787 1.00 56.08  0  493  TRP   A CG  1 
ATOM   3566  C CD1 . TRP   A 1 529  ? 148.738 96.164  121.578 1.00 57.31  0  493  TRP   A CD1 1 
ATOM   3567  C CD2 . TRP   A 1 529  ? 149.127 98.354  121.367 1.00 56.68  0  493  TRP   A CD2 1 
ATOM   3568  N NE1 . TRP   A 1 529  ? 147.607 96.742  121.059 1.00 59.67  0  493  TRP   A NE1 1 
ATOM   3569  C CE2 . TRP   A 1 529  ? 147.822 98.087  120.920 1.00 56.40  0  493  TRP   A CE2 1 
ATOM   3570  C CE3 . TRP   A 1 529  ? 149.596 99.669  121.330 1.00 55.05  0  493  TRP   A CE3 1 
ATOM   3571  C CZ2 . TRP   A 1 529  ? 146.980 99.085  120.441 1.00 53.93  0  493  TRP   A CZ2 1 
ATOM   3572  C CZ3 . TRP   A 1 529  ? 148.758 100.658 120.854 1.00 54.11  0  493  TRP   A CZ3 1 
ATOM   3573  C CH2 . TRP   A 1 529  ? 147.466 100.362 120.418 1.00 53.06  0  493  TRP   A CH2 1 
ATOM   3574  N N   . LEU   A 1 530  ? 154.276 96.120  122.106 1.00 56.58  0  494  LEU   A N   1 
ATOM   3575  C CA  . LEU   A 1 530  ? 155.669 96.308  122.494 1.00 50.85  0  494  LEU   A CA  1 
ATOM   3576  C C   . LEU   A 1 530  ? 156.476 96.943  121.371 1.00 48.02  0  494  LEU   A C   1 
ATOM   3577  O O   . LEU   A 1 530  ? 157.327 97.799  121.628 1.00 50.59  0  494  LEU   A O   1 
ATOM   3578  C CB  . LEU   A 1 530  ? 156.295 94.981  122.913 1.00 52.74  0  494  LEU   A CB  1 
ATOM   3579  C CG  . LEU   A 1 530  ? 156.516 94.804  124.416 1.00 53.36  0  494  LEU   A CG  1 
ATOM   3580  C CD1 . LEU   A 1 530  ? 156.780 93.348  124.755 1.00 55.29  0  494  LEU   A CD1 1 
ATOM   3581  C CD2 . LEU   A 1 530  ? 157.656 95.680  124.896 1.00 51.15  0  494  LEU   A CD2 1 
ATOM   3582  N N   . THR   A 1 531  ? 156.232 96.534  120.125 1.00 51.19  0  495  THR   A N   1 
ATOM   3583  C CA  . THR   A 1 531  ? 156.896 97.178  118.996 1.00 55.31  0  495  THR   A CA  1 
ATOM   3584  C C   . THR   A 1 531  ? 156.483 98.639  118.876 1.00 57.21  0  495  THR   A C   1 
ATOM   3585  O O   . THR   A 1 531  ? 157.321 99.509  118.611 1.00 56.30  0  495  THR   A O   1 
ATOM   3586  C CB  . THR   A 1 531  ? 156.586 96.421  117.706 1.00 53.53  0  495  THR   A CB  1 
ATOM   3587  O OG1 . THR   A 1 531  ? 157.311 95.185  117.691 1.00 55.96  0  495  THR   A OG1 1 
ATOM   3588  C CG2 . THR   A 1 531  ? 156.975 97.245  116.492 1.00 51.80  0  495  THR   A CG2 1 
ATOM   3589  N N   . TYR   A 1 532  ? 155.195 98.927  119.077 1.00 55.66  0  496  TYR   A N   1 
ATOM   3590  C CA  . TYR   A 1 532  ? 154.733 100.311 119.070 1.00 48.91  0  496  TYR   A CA  1 
ATOM   3591  C C   . TYR   A 1 532  ? 155.409 101.130 120.161 1.00 52.05  0  496  TYR   A C   1 
ATOM   3592  O O   . TYR   A 1 532  ? 155.744 102.299 119.944 1.00 54.92  0  496  TYR   A O   1 
ATOM   3593  C CB  . TYR   A 1 532  ? 153.218 100.357 119.248 1.00 48.89  0  496  TYR   A CB  1 
ATOM   3594  C CG  . TYR   A 1 532  ? 152.429 100.042 118.003 1.00 53.26  0  496  TYR   A CG  1 
ATOM   3595  C CD1 . TYR   A 1 532  ? 152.469 100.883 116.903 1.00 52.34  0  496  TYR   A CD1 1 
ATOM   3596  C CD2 . TYR   A 1 532  ? 151.632 98.912  117.932 1.00 52.49  0  496  TYR   A CD2 1 
ATOM   3597  C CE1 . TYR   A 1 532  ? 151.742 100.603 115.764 1.00 52.40  0  496  TYR   A CE1 1 
ATOM   3598  C CE2 . TYR   A 1 532  ? 150.904 98.622  116.800 1.00 52.18  0  496  TYR   A CE2 1 
ATOM   3599  C CZ  . TYR   A 1 532  ? 150.963 99.471  115.719 1.00 54.40  0  496  TYR   A CZ  1 
ATOM   3600  O OH  . TYR   A 1 532  ? 150.236 99.187  114.587 1.00 55.17  0  496  TYR   A OH  1 
ATOM   3601  N N   . TYR   A 1 533  ? 155.603 100.535 121.337 1.00 51.81  0  497  TYR   A N   1 
ATOM   3602  C CA  . TYR   A 1 533  ? 156.243 101.221 122.453 1.00 54.61  0  497  TYR   A CA  1 
ATOM   3603  C C   . TYR   A 1 533  ? 157.717 101.484 122.174 1.00 62.29  0  497  TYR   A C   1 
ATOM   3604  O O   . TYR   A 1 533  ? 158.206 102.598 122.384 1.00 63.73  0  497  TYR   A O   1 
ATOM   3605  C CB  . TYR   A 1 533  ? 156.072 100.392 123.726 1.00 49.79  0  497  TYR   A CB  1 
ATOM   3606  C CG  . TYR   A 1 533  ? 156.784 100.928 124.945 1.00 50.81  0  497  TYR   A CG  1 
ATOM   3607  C CD1 . TYR   A 1 533  ? 156.877 102.290 125.177 1.00 54.85  0  497  TYR   A CD1 1 
ATOM   3608  C CD2 . TYR   A 1 533  ? 157.335 100.068 125.880 1.00 53.67  0  497  TYR   A CD2 1 
ATOM   3609  C CE1 . TYR   A 1 533  ? 157.518 102.781 126.293 1.00 57.80  0  497  TYR   A CE1 1 
ATOM   3610  C CE2 . TYR   A 1 533  ? 157.974 100.549 127.002 1.00 57.26  0  497  TYR   A CE2 1 
ATOM   3611  C CZ  . TYR   A 1 533  ? 158.062 101.906 127.204 1.00 60.85  0  497  TYR   A CZ  1 
ATOM   3612  O OH  . TYR   A 1 533  ? 158.698 102.395 128.319 1.00 59.31  0  497  TYR   A OH  1 
ATOM   3613  N N   . LYS   A 1 534  ? 158.441 100.470 121.695 1.00 59.79  0  498  LYS   A N   1 
ATOM   3614  C CA  . LYS   A 1 534  ? 159.872 100.634 121.464 1.00 54.13  0  498  LYS   A CA  1 
ATOM   3615  C C   . LYS   A 1 534  ? 160.151 101.593 120.317 1.00 52.93  0  498  LYS   A C   1 
ATOM   3616  O O   . LYS   A 1 534  ? 161.160 102.306 120.339 1.00 57.81  0  498  LYS   A O   1 
ATOM   3617  C CB  . LYS   A 1 534  ? 160.522 99.277  121.198 1.00 54.54  0  498  LYS   A CB  1 
ATOM   3618  C CG  . LYS   A 1 534  ? 160.363 98.284  122.338 1.00 58.50  0  498  LYS   A CG  1 
ATOM   3619  C CD  . LYS   A 1 534  ? 161.037 98.782  123.605 1.00 61.86  0  498  LYS   A CD  1 
ATOM   3620  C CE  . LYS   A 1 534  ? 160.504 98.062  124.834 1.00 59.67  0  498  LYS   A CE  1 
ATOM   3621  N NZ  . LYS   A 1 534  ? 161.377 98.255  126.026 1.00 58.41  1  498  LYS   A NZ  1 
ATOM   3622  N N   . LEU   A 1 535  ? 159.282 101.629 119.312 1.00 48.17  0  499  LEU   A N   1 
ATOM   3623  C CA  . LEU   A 1 535  ? 159.447 102.538 118.187 1.00 53.95  0  499  LEU   A CA  1 
ATOM   3624  C C   . LEU   A 1 535  ? 158.770 103.883 118.407 1.00 51.57  0  499  LEU   A C   1 
ATOM   3625  O O   . LEU   A 1 535  ? 158.894 104.766 117.553 1.00 53.08  0  499  LEU   A O   1 
ATOM   3626  C CB  . LEU   A 1 535  ? 158.909 101.899 116.904 1.00 53.55  0  499  LEU   A CB  1 
ATOM   3627  C CG  . LEU   A 1 535  ? 159.522 100.572 116.453 1.00 53.72  0  499  LEU   A CG  1 
ATOM   3628  C CD1 . LEU   A 1 535  ? 159.313 100.381 114.962 1.00 52.30  0  499  LEU   A CD1 1 
ATOM   3629  C CD2 . LEU   A 1 535  ? 161.001 100.492 116.798 1.00 51.81  0  499  LEU   A CD2 1 
ATOM   3630  N N   . ASN   A 1 536  ? 158.063 104.053 119.523 1.00 47.93  0  500  ASN   A N   1 
ATOM   3631  C CA  . ASN   A 1 536  ? 157.372 105.296 119.865 1.00 51.58  0  500  ASN   A CA  1 
ATOM   3632  C C   . ASN   A 1 536  ? 156.422 105.726 118.747 1.00 52.13  0  500  ASN   A C   1 
ATOM   3633  O O   . ASN   A 1 536  ? 156.532 106.810 118.173 1.00 45.03  0  500  ASN   A O   1 
ATOM   3634  C CB  . ASN   A 1 536  ? 158.373 106.404 120.198 1.00 51.77  0  500  ASN   A CB  1 
ATOM   3635  C CG  . ASN   A 1 536  ? 158.923 106.287 121.604 1.00 51.26  0  500  ASN   A CG  1 
ATOM   3636  O OD1 . ASN   A 1 536  ? 158.511 105.422 122.372 1.00 54.48  0  500  ASN   A OD1 1 
ATOM   3637  N ND2 . ASN   A 1 536  ? 159.859 107.160 121.948 1.00 51.85  0  500  ASN   A ND2 1 
ATOM   3638  N N   . THR   A 1 537  ? 155.475 104.841 118.445 1.00 56.74  0  501  THR   A N   1 
ATOM   3639  C CA  . THR   A 1 537  ? 154.458 105.102 117.439 1.00 59.40  0  501  THR   A CA  1 
ATOM   3640  C C   . THR   A 1 537  ? 153.145 104.487 117.902 1.00 58.07  0  501  THR   A C   1 
ATOM   3641  O O   . THR   A 1 537  ? 153.126 103.539 118.690 1.00 59.42  0  501  THR   A O   1 
ATOM   3642  C CB  . THR   A 1 537  ? 154.857 104.539 116.067 1.00 61.88  0  501  THR   A CB  1 
ATOM   3643  O OG1 . THR   A 1 537  ? 156.256 104.755 115.849 1.00 61.25  0  501  THR   A OG1 1 
ATOM   3644  C CG2 . THR   A 1 537  ? 154.073 105.220 114.956 1.00 61.02  0  501  THR   A CG2 1 
ATOM   3645  N N   . TYR   A 1 538  ? 152.042 105.042 117.407 1.00 50.72  0  502  TYR   A N   1 
ATOM   3646  C CA  . TYR   A 1 538  ? 150.725 104.562 117.779 1.00 50.82  0  502  TYR   A CA  1 
ATOM   3647  C C   . TYR   A 1 538  ? 149.919 104.199 116.537 1.00 57.68  0  502  TYR   A C   1 
ATOM   3648  O O   . TYR   A 1 538  ? 150.047 104.851 115.496 1.00 58.00  0  502  TYR   A O   1 
ATOM   3649  C CB  . TYR   A 1 538  ? 149.960 105.614 118.595 1.00 50.87  0  502  TYR   A CB  1 
ATOM   3650  C CG  . TYR   A 1 538  ? 149.678 106.903 117.852 1.00 48.69  0  502  TYR   A CG  1 
ATOM   3651  C CD1 . TYR   A 1 538  ? 148.509 107.068 117.125 1.00 45.34  0  502  TYR   A CD1 1 
ATOM   3652  C CD2 . TYR   A 1 538  ? 150.574 107.957 117.891 1.00 50.30  0  502  TYR   A CD2 1 
ATOM   3653  C CE1 . TYR   A 1 538  ? 148.248 108.241 116.450 1.00 46.44  0  502  TYR   A CE1 1 
ATOM   3654  C CE2 . TYR   A 1 538  ? 150.321 109.132 117.221 1.00 52.40  0  502  TYR   A CE2 1 
ATOM   3655  C CZ  . TYR   A 1 538  ? 149.157 109.270 116.503 1.00 53.28  0  502  TYR   A CZ  1 
ATOM   3656  O OH  . TYR   A 1 538  ? 148.900 110.442 115.832 1.00 51.40  0  502  TYR   A OH  1 
ATOM   3657  N N   . PRO   A 1 539  ? 149.084 103.165 116.616 1.00 65.82  0  503  PRO   A N   1 
ATOM   3658  C CA  . PRO   A 1 539  ? 148.247 102.804 115.467 1.00 61.26  0  503  PRO   A CA  1 
ATOM   3659  C C   . PRO   A 1 539  ? 147.136 103.815 115.261 1.00 54.20  0  503  PRO   A C   1 
ATOM   3660  O O   . PRO   A 1 539  ? 146.624 104.409 116.212 1.00 56.22  0  503  PRO   A O   1 
ATOM   3661  C CB  . PRO   A 1 539  ? 147.677 101.431 115.852 1.00 60.98  0  503  PRO   A CB  1 
ATOM   3662  C CG  . PRO   A 1 539  ? 148.321 101.061 117.160 1.00 61.70  0  503  PRO   A CG  1 
ATOM   3663  C CD  . PRO   A 1 539  ? 148.808 102.316 117.783 1.00 57.76  0  503  PRO   A CD  1 
ATOM   3664  N N   . SER   A 1 540  ? 146.753 103.999 114.002 1.00 52.63  0  504  SER   A N   1 
ATOM   3665  C CA  . SER   A 1 540  ? 145.651 104.894 113.699 1.00 58.49  0  504  SER   A CA  1 
ATOM   3666  C C   . SER   A 1 540  ? 144.341 104.299 114.203 1.00 65.59  0  504  SER   A C   1 
ATOM   3667  O O   . SER   A 1 540  ? 144.256 103.120 114.553 1.00 68.61  0  504  SER   A O   1 
ATOM   3668  C CB  . SER   A 1 540  ? 145.573 105.163 112.198 1.00 63.10  0  504  SER   A CB  1 
ATOM   3669  O OG  . SER   A 1 540  ? 145.102 104.025 111.500 1.00 64.78  0  504  SER   A OG  1 
ATOM   3670  N N   . LEU   A 1 541  ? 143.309 105.143 114.251 1.00 67.06  0  505  LEU   A N   1 
ATOM   3671  C CA  . LEU   A 1 541  ? 142.018 104.698 114.767 1.00 66.36  0  505  LEU   A CA  1 
ATOM   3672  C C   . LEU   A 1 541  ? 141.422 103.599 113.896 1.00 68.29  0  505  LEU   A C   1 
ATOM   3673  O O   . LEU   A 1 541  ? 140.812 102.654 114.409 1.00 63.79  0  505  LEU   A O   1 
ATOM   3674  C CB  . LEU   A 1 541  ? 141.062 105.884 114.874 1.00 67.62  0  505  LEU   A CB  1 
ATOM   3675  C CG  . LEU   A 1 541  ? 139.815 105.686 115.737 1.00 72.31  0  505  LEU   A CG  1 
ATOM   3676  C CD1 . LEU   A 1 541  ? 140.195 105.431 117.184 1.00 69.16  0  505  LEU   A CD1 1 
ATOM   3677  C CD2 . LEU   A 1 541  ? 138.898 106.894 115.627 1.00 70.32  0  505  LEU   A CD2 1 
ATOM   3678  N N   . LEU   A 1 542  ? 141.582 103.706 112.575 1.00 69.09  0  506  LEU   A N   1 
ATOM   3679  C CA  . LEU   A 1 542  ? 141.045 102.699 111.668 1.00 64.92  0  506  LEU   A CA  1 
ATOM   3680  C C   . LEU   A 1 542  ? 141.785 101.371 111.751 1.00 64.25  0  506  LEU   A C   1 
ATOM   3681  O O   . LEU   A 1 542  ? 141.232 100.351 111.327 1.00 64.24  0  506  LEU   A O   1 
ATOM   3682  C CB  . LEU   A 1 542  ? 141.067 103.210 110.225 1.00 67.14  0  506  LEU   A CB  1 
ATOM   3683  C CG  . LEU   A 1 542  ? 140.299 104.495 109.895 1.00 66.31  0  506  LEU   A CG  1 
ATOM   3684  C CD1 . LEU   A 1 542  ? 141.107 105.749 110.213 1.00 64.88  0  506  LEU   A CD1 1 
ATOM   3685  C CD2 . LEU   A 1 542  ? 139.848 104.494 108.440 1.00 66.65  0  506  LEU   A CD2 1 
ATOM   3686  N N   . GLU   A 1 543  ? 143.006 101.354 112.279 1.00 61.21  0  507  GLU   A N   1 
ATOM   3687  C CA  . GLU   A 1 543  ? 143.747 100.123 112.510 1.00 60.67  0  507  GLU   A CA  1 
ATOM   3688  C C   . GLU   A 1 543  ? 143.501 99.555  113.900 1.00 60.97  0  507  GLU   A C   1 
ATOM   3689  O O   . GLU   A 1 543  ? 144.122 98.555  114.270 1.00 61.30  0  507  GLU   A O   1 
ATOM   3690  C CB  . GLU   A 1 543  ? 145.246 100.361 112.316 1.00 63.15  0  507  GLU   A CB  1 
ATOM   3691  C CG  . GLU   A 1 543  ? 145.648 100.769 110.911 1.00 64.19  0  507  GLU   A CG  1 
ATOM   3692  C CD  . GLU   A 1 543  ? 146.942 101.557 110.889 1.00 68.83  0  507  GLU   A CD  1 
ATOM   3693  O OE1 . GLU   A 1 543  ? 147.963 101.036 111.384 1.00 69.80  0  507  GLU   A OE1 1 
ATOM   3694  O OE2 . GLU   A 1 543  ? 146.936 102.702 110.388 1.00 68.99  -1 507  GLU   A OE2 1 
ATOM   3695  N N   . LEU   A 1 544  ? 142.616 100.177 114.671 1.00 62.63  0  508  LEU   A N   1 
ATOM   3696  C CA  . LEU   A 1 544  ? 142.360 99.821  116.057 1.00 61.14  0  508  LEU   A CA  1 
ATOM   3697  C C   . LEU   A 1 544  ? 141.222 98.813  116.150 1.00 63.80  0  508  LEU   A C   1 
ATOM   3698  O O   . LEU   A 1 544  ? 140.311 98.798  115.318 1.00 62.43  0  508  LEU   A O   1 
ATOM   3699  C CB  . LEU   A 1 544  ? 142.012 101.071 116.867 1.00 58.52  0  508  LEU   A CB  1 
ATOM   3700  C CG  . LEU   A 1 544  ? 142.994 101.563 117.926 1.00 58.67  0  508  LEU   A CG  1 
ATOM   3701  C CD1 . LEU   A 1 544  ? 142.275 102.460 118.908 1.00 59.98  0  508  LEU   A CD1 1 
ATOM   3702  C CD2 . LEU   A 1 544  ? 143.635 100.398 118.645 1.00 59.06  0  508  LEU   A CD2 1 
ATOM   3703  N N   . THR   A 1 545  ? 141.286 97.962  117.173 1.00 65.96  0  509  THR   A N   1 
ATOM   3704  C CA  . THR   A 1 545  ? 140.254 96.973  117.445 1.00 64.67  0  509  THR   A CA  1 
ATOM   3705  C C   . THR   A 1 545  ? 139.861 97.046  118.914 1.00 57.05  0  509  THR   A C   1 
ATOM   3706  O O   . THR   A 1 545  ? 140.554 97.646  119.739 1.00 57.87  0  509  THR   A O   1 
ATOM   3707  C CB  . THR   A 1 545  ? 140.714 95.547  117.107 1.00 59.90  0  509  THR   A CB  1 
ATOM   3708  O OG1 . THR   A 1 545  ? 141.500 95.029  118.186 1.00 63.18  0  509  THR   A OG1 1 
ATOM   3709  C CG2 . THR   A 1 545  ? 141.545 95.527  115.834 1.00 58.67  0  509  THR   A CG2 1 
ATOM   3710  N N   . GLU   A 1 546  ? 138.731 96.414  119.236 1.00 48.22  0  510  GLU   A N   1 
ATOM   3711  C CA  . GLU   A 1 546  ? 138.289 96.343  120.624 1.00 51.49  0  510  GLU   A CA  1 
ATOM   3712  C C   . GLU   A 1 546  ? 139.277 95.555  121.476 1.00 56.45  0  510  GLU   A C   1 
ATOM   3713  O O   . GLU   A 1 546  ? 139.511 95.891  122.647 1.00 65.11  0  510  GLU   A O   1 
ATOM   3714  C CB  . GLU   A 1 546  ? 136.900 95.715  120.695 1.00 58.23  0  510  GLU   A CB  1 
ATOM   3715  C CG  . GLU   A 1 546  ? 135.772 96.591  120.163 1.00 62.79  0  510  GLU   A CG  1 
ATOM   3716  C CD  . GLU   A 1 546  ? 135.544 96.425  118.673 1.00 65.98  0  510  GLU   A CD  1 
ATOM   3717  O OE1 . GLU   A 1 546  ? 136.286 95.646  118.039 1.00 66.42  0  510  GLU   A OE1 1 
ATOM   3718  O OE2 . GLU   A 1 546  ? 134.617 97.070  118.139 1.00 64.53  -1 510  GLU   A OE2 1 
ATOM   3719  N N   . ARG   A 1 547  ? 139.854 94.494  120.907 1.00 59.70  0  511  ARG   A N   1 
ATOM   3720  C CA  . ARG   A 1 547  ? 140.891 93.732  121.594 1.00 62.37  0  511  ARG   A CA  1 
ATOM   3721  C C   . ARG   A 1 547  ? 142.027 94.640  122.042 1.00 65.56  0  511  ARG   A C   1 
ATOM   3722  O O   . ARG   A 1 547  ? 142.539 94.518  123.161 1.00 67.03  0  511  ARG   A O   1 
ATOM   3723  C CB  . ARG   A 1 547  ? 141.425 92.642  120.663 1.00 64.51  0  511  ARG   A CB  1 
ATOM   3724  C CG  . ARG   A 1 547  ? 142.149 91.512  121.360 1.00 64.77  0  511  ARG   A CG  1 
ATOM   3725  C CD  . ARG   A 1 547  ? 141.176 90.483  121.878 1.00 66.52  0  511  ARG   A CD  1 
ATOM   3726  N NE  . ARG   A 1 547  ? 141.771 89.152  121.924 1.00 69.56  0  511  ARG   A NE  1 
ATOM   3727  C CZ  . ARG   A 1 547  ? 141.418 88.145  121.138 1.00 67.73  0  511  ARG   A CZ  1 
ATOM   3728  N NH1 . ARG   A 1 547  ? 140.470 88.280  120.226 1.00 68.15  1  511  ARG   A NH1 1 
ATOM   3729  N NH2 . ARG   A 1 547  ? 142.031 86.972  121.271 1.00 63.02  0  511  ARG   A NH2 1 
ATOM   3730  N N   . ASP   A 1 548  ? 142.431 95.561  121.168 1.00 55.43  0  512  ASP   A N   1 
ATOM   3731  C CA  . ASP   A 1 548  ? 143.538 96.454  121.482 1.00 47.27  0  512  ASP   A CA  1 
ATOM   3732  C C   . ASP   A 1 548  ? 143.206 97.340  122.673 1.00 46.47  0  512  ASP   A C   1 
ATOM   3733  O O   . ASP   A 1 548  ? 144.051 97.567  123.542 1.00 48.48  0  512  ASP   A O   1 
ATOM   3734  C CB  . ASP   A 1 548  ? 143.882 97.300  120.258 1.00 52.12  0  512  ASP   A CB  1 
ATOM   3735  C CG  . ASP   A 1 548  ? 144.210 96.460  119.040 1.00 60.78  0  512  ASP   A CG  1 
ATOM   3736  O OD1 . ASP   A 1 548  ? 144.776 95.358  119.207 1.00 59.05  0  512  ASP   A OD1 1 
ATOM   3737  O OD2 . ASP   A 1 548  ? 143.900 96.901  117.914 1.00 61.73  -1 512  ASP   A OD2 1 
ATOM   3738  N N   . LEU   A 1 549  ? 141.978 97.862  122.723 1.00 46.69  0  513  LEU   A N   1 
ATOM   3739  C CA  . LEU   A 1 549  ? 141.586 98.714  123.841 1.00 39.65  0  513  LEU   A CA  1 
ATOM   3740  C C   . LEU   A 1 549  ? 141.522 97.927  125.141 1.00 35.87  0  513  LEU   A C   1 
ATOM   3741  O O   . LEU   A 1 549  ? 141.948 98.420  126.192 1.00 48.10  0  513  LEU   A O   1 
ATOM   3742  C CB  . LEU   A 1 549  ? 140.246 99.385  123.555 1.00 33.06  0  513  LEU   A CB  1 
ATOM   3743  C CG  . LEU   A 1 549  ? 140.215 100.363 122.382 1.00 32.81  0  513  LEU   A CG  1 
ATOM   3744  C CD1 . LEU   A 1 549  ? 139.047 101.310 122.520 1.00 32.06  0  513  LEU   A CD1 1 
ATOM   3745  C CD2 . LEU   A 1 549  ? 141.518 101.132 122.271 1.00 33.72  0  513  LEU   A CD2 1 
ATOM   3746  N N   . ILE   A 1 550  ? 140.997 96.701  125.096 1.00 37.75  0  514  ILE   A N   1 
ATOM   3747  C CA  . ILE   A 1 550  ? 140.976 95.902  126.316 1.00 44.01  0  514  ILE   A CA  1 
ATOM   3748  C C   . ILE   A 1 550  ? 142.395 95.586  126.774 1.00 50.77  0  514  ILE   A C   1 
ATOM   3749  O O   . ILE   A 1 550  ? 142.661 95.495  127.980 1.00 50.90  0  514  ILE   A O   1 
ATOM   3750  C CB  . ILE   A 1 550  ? 140.141 94.626  126.118 1.00 45.19  0  514  ILE   A CB  1 
ATOM   3751  C CG1 . ILE   A 1 550  ? 138.736 94.984  125.643 1.00 48.56  0  514  ILE   A CG1 1 
ATOM   3752  C CG2 . ILE   A 1 550  ? 140.041 93.855  127.415 1.00 44.94  0  514  ILE   A CG2 1 
ATOM   3753  C CD1 . ILE   A 1 550  ? 137.898 93.788  125.275 1.00 53.14  0  514  ILE   A CD1 1 
ATOM   3754  N N   . VAL   A 1 551  ? 143.327 95.410  125.833 1.00 52.01  0  515  VAL   A N   1 
ATOM   3755  C CA  . VAL   A 1 551  ? 144.726 95.187  126.197 1.00 49.83  0  515  VAL   A CA  1 
ATOM   3756  C C   . VAL   A 1 551  ? 145.328 96.444  126.820 1.00 53.34  0  515  VAL   A C   1 
ATOM   3757  O O   . VAL   A 1 551  ? 146.019 96.379  127.844 1.00 55.79  0  515  VAL   A O   1 
ATOM   3758  C CB  . VAL   A 1 551  ? 145.527 94.723  124.968 1.00 43.93  0  515  VAL   A CB  1 
ATOM   3759  C CG1 . VAL   A 1 551  ? 147.003 95.007  125.158 1.00 44.51  0  515  VAL   A CG1 1 
ATOM   3760  C CG2 . VAL   A 1 551  ? 145.295 93.244  124.719 1.00 47.10  0  515  VAL   A CG2 1 
ATOM   3761  N N   . LEU   A 1 552  ? 145.074 97.606  126.210 1.00 47.58  0  516  LEU   A N   1 
ATOM   3762  C CA  . LEU   A 1 552  ? 145.591 98.868  126.734 1.00 40.33  0  516  LEU   A CA  1 
ATOM   3763  C C   . LEU   A 1 552  ? 145.043 99.171  128.120 1.00 41.11  0  516  LEU   A C   1 
ATOM   3764  O O   . LEU   A 1 552  ? 145.710 99.833  128.921 1.00 40.70  0  516  LEU   A O   1 
ATOM   3765  C CB  . LEU   A 1 552  ? 145.245 100.016 125.789 1.00 37.01  0  516  LEU   A CB  1 
ATOM   3766  C CG  . LEU   A 1 552  ? 146.134 100.279 124.580 1.00 33.91  0  516  LEU   A CG  1 
ATOM   3767  C CD1 . LEU   A 1 552  ? 145.458 101.259 123.650 1.00 35.14  0  516  LEU   A CD1 1 
ATOM   3768  C CD2 . LEU   A 1 552  ? 147.467 100.818 125.023 1.00 41.52  0  516  LEU   A CD2 1 
ATOM   3769  N N   . SER   A 1 553  ? 143.834 98.698  128.419 1.00 35.77  0  517  SER   A N   1 
ATOM   3770  C CA  . SER   A 1 553  ? 143.208 98.961  129.708 1.00 34.63  0  517  SER   A CA  1 
ATOM   3771  C C   . SER   A 1 553  ? 144.022 98.456  130.892 1.00 46.33  0  517  SER   A C   1 
ATOM   3772  O O   . SER   A 1 553  ? 143.651 98.742  132.035 1.00 48.33  0  517  SER   A O   1 
ATOM   3773  C CB  . SER   A 1 553  ? 141.825 98.321  129.748 1.00 42.13  0  517  SER   A CB  1 
ATOM   3774  O OG  . SER   A 1 553  ? 141.928 96.910  129.833 1.00 45.60  0  517  SER   A OG  1 
ATOM   3775  N N   . GLY   A 1 554  ? 145.096 97.708  130.661 1.00 45.37  0  518  GLY   A N   1 
ATOM   3776  C CA  . GLY   A 1 554  ? 145.905 97.164  131.728 1.00 43.05  0  518  GLY   A CA  1 
ATOM   3777  C C   . GLY   A 1 554  ? 147.197 97.889  132.017 1.00 44.60  0  518  GLY   A C   1 
ATOM   3778  O O   . GLY   A 1 554  ? 147.937 97.466  132.908 1.00 46.96  0  518  GLY   A O   1 
ATOM   3779  N N   . LEU   A 1 555  ? 147.493 98.967  131.298 1.00 42.41  0  519  LEU   A N   1 
ATOM   3780  C CA  . LEU   A 1 555  ? 148.762 99.664  131.455 1.00 37.96  0  519  LEU   A CA  1 
ATOM   3781  C C   . LEU   A 1 555  ? 148.750 100.581 132.670 1.00 46.62  0  519  LEU   A C   1 
ATOM   3782  O O   . LEU   A 1 555  ? 147.749 101.239 132.964 1.00 52.61  0  519  LEU   A O   1 
ATOM   3783  C CB  . LEU   A 1 555  ? 149.074 100.483 130.206 1.00 40.53  0  519  LEU   A CB  1 
ATOM   3784  C CG  . LEU   A 1 555  ? 149.526 99.703  128.978 1.00 44.69  0  519  LEU   A CG  1 
ATOM   3785  C CD1 . LEU   A 1 555  ? 149.762 100.650 127.819 1.00 43.54  0  519  LEU   A CD1 1 
ATOM   3786  C CD2 . LEU   A 1 555  ? 150.775 98.908  129.295 1.00 43.34  0  519  LEU   A CD2 1 
ATOM   3787  N N   . ARG   A 1 556  ? 149.880 100.628 133.369 1.00 53.96  0  520  ARG   A N   1 
ATOM   3788  C CA  . ARG   A 1 556  ? 150.112 101.576 134.448 1.00 52.56  0  520  ARG   A CA  1 
ATOM   3789  C C   . ARG   A 1 556  ? 151.330 102.422 134.110 1.00 56.03  0  520  ARG   A C   1 
ATOM   3790  O O   . ARG   A 1 556  ? 152.312 101.918 133.558 1.00 58.97  0  520  ARG   A O   1 
ATOM   3791  C CB  . ARG   A 1 556  ? 150.327 100.865 135.778 1.00 48.20  0  520  ARG   A CB  1 
ATOM   3792  C CG  . ARG   A 1 556  ? 149.058 100.421 136.456 1.00 50.08  0  520  ARG   A CG  1 
ATOM   3793  C CD  . ARG   A 1 556  ? 149.353 99.963  137.866 1.00 53.63  0  520  ARG   A CD  1 
ATOM   3794  N NE  . ARG   A 1 556  ? 150.185 98.766  137.870 1.00 61.36  0  520  ARG   A NE  1 
ATOM   3795  C CZ  . ARG   A 1 556  ? 151.053 98.461  138.824 1.00 62.54  0  520  ARG   A CZ  1 
ATOM   3796  N NH1 . ARG   A 1 556  ? 151.230 99.247  139.874 1.00 60.76  1  520  ARG   A NH1 1 
ATOM   3797  N NH2 . ARG   A 1 556  ? 151.761 97.340  138.723 1.00 59.07  0  520  ARG   A NH2 1 
ATOM   3798  N N   . PHE   A 1 557  ? 151.268 103.704 134.446 1.00 41.76  0  521  PHE   A N   1 
ATOM   3799  C CA  . PHE   A 1 557  ? 152.314 104.647 134.085 1.00 37.72  0  521  PHE   A CA  1 
ATOM   3800  C C   . PHE   A 1 557  ? 153.159 105.021 135.296 1.00 37.84  0  521  PHE   A C   1 
ATOM   3801  O O   . PHE   A 1 557  ? 152.914 104.594 136.425 1.00 35.18  0  521  PHE   A O   1 
ATOM   3802  C CB  . PHE   A 1 557  ? 151.711 105.907 133.463 1.00 39.44  0  521  PHE   A CB  1 
ATOM   3803  C CG  . PHE   A 1 557  ? 150.773 105.635 132.328 1.00 39.26  0  521  PHE   A CG  1 
ATOM   3804  C CD1 . PHE   A 1 557  ? 151.252 105.477 131.044 1.00 46.62  0  521  PHE   A CD1 1 
ATOM   3805  C CD2 . PHE   A 1 557  ? 149.415 105.543 132.544 1.00 42.45  0  521  PHE   A CD2 1 
ATOM   3806  C CE1 . PHE   A 1 557  ? 150.396 105.233 129.997 1.00 48.27  0  521  PHE   A CE1 1 
ATOM   3807  C CE2 . PHE   A 1 557  ? 148.555 105.297 131.502 1.00 44.99  0  521  PHE   A CE2 1 
ATOM   3808  C CZ  . PHE   A 1 557  ? 149.047 105.143 130.226 1.00 49.56  0  521  PHE   A CZ  1 
ATOM   3809  N N   . TYR   A 1 558  ? 154.184 105.823 135.032 1.00 53.73  0  522  TYR   A N   1 
ATOM   3810  C CA  . TYR   A 1 558  ? 154.979 106.471 136.061 1.00 54.03  0  522  TYR   A CA  1 
ATOM   3811  C C   . TYR   A 1 558  ? 154.612 107.946 136.120 1.00 52.82  0  522  TYR   A C   1 
ATOM   3812  O O   . TYR   A 1 558  ? 154.065 108.502 135.164 1.00 47.92  0  522  TYR   A O   1 
ATOM   3813  C CB  . TYR   A 1 558  ? 156.474 106.327 135.779 1.00 52.98  0  522  TYR   A CB  1 
ATOM   3814  C CG  . TYR   A 1 558  ? 157.098 105.054 136.290 1.00 55.52  0  522  TYR   A CG  1 
ATOM   3815  C CD1 . TYR   A 1 558  ? 157.048 104.725 137.635 1.00 56.36  0  522  TYR   A CD1 1 
ATOM   3816  C CD2 . TYR   A 1 558  ? 157.746 104.185 135.428 1.00 56.93  0  522  TYR   A CD2 1 
ATOM   3817  C CE1 . TYR   A 1 558  ? 157.623 103.563 138.106 1.00 58.47  0  522  TYR   A CE1 1 
ATOM   3818  C CE2 . TYR   A 1 558  ? 158.322 103.021 135.890 1.00 59.41  0  522  TYR   A CE2 1 
ATOM   3819  C CZ  . TYR   A 1 558  ? 158.258 102.715 137.229 1.00 61.07  0  522  TYR   A CZ  1 
ATOM   3820  O OH  . TYR   A 1 558  ? 158.832 101.555 137.692 1.00 60.63  0  522  TYR   A OH  1 
ATOM   3821  N N   . ARG   A 1 559  ? 154.921 108.576 137.252 1.00 49.94  0  523  ARG   A N   1 
ATOM   3822  C CA  . ARG   A 1 559  ? 154.656 109.998 137.422 1.00 47.72  0  523  ARG   A CA  1 
ATOM   3823  C C   . ARG   A 1 559  ? 155.285 110.794 136.289 1.00 51.42  0  523  ARG   A C   1 
ATOM   3824  O O   . ARG   A 1 559  ? 156.511 110.832 136.151 1.00 57.48  0  523  ARG   A O   1 
ATOM   3825  C CB  . ARG   A 1 559  ? 155.182 110.489 138.769 1.00 49.93  0  523  ARG   A CB  1 
ATOM   3826  C CG  . ARG   A 1 559  ? 155.242 111.998 138.886 1.00 50.86  0  523  ARG   A CG  1 
ATOM   3827  C CD  . ARG   A 1 559  ? 155.476 112.435 140.318 1.00 52.68  0  523  ARG   A CD  1 
ATOM   3828  N NE  . ARG   A 1 559  ? 156.894 112.445 140.652 1.00 50.47  0  523  ARG   A NE  1 
ATOM   3829  C CZ  . ARG   A 1 559  ? 157.749 113.372 140.246 1.00 51.06  0  523  ARG   A CZ  1 
ATOM   3830  N NH1 . ARG   A 1 559  ? 157.362 114.383 139.489 1.00 48.40  1  523  ARG   A NH1 1 
ATOM   3831  N NH2 . ARG   A 1 559  ? 159.026 113.279 140.604 1.00 54.39  0  523  ARG   A NH2 1 
ATOM   3832  N N   . GLU   A 1 560  ? 154.450 111.424 135.469 1.00 42.06  0  524  GLU   A N   1 
ATOM   3833  C CA  . GLU   A 1 560  ? 154.915 112.165 134.311 1.00 41.08  0  524  GLU   A CA  1 
ATOM   3834  C C   . GLU   A 1 560  ? 154.590 113.646 134.380 1.00 39.84  0  524  GLU   A C   1 
ATOM   3835  O O   . GLU   A 1 560  ? 154.912 114.376 133.438 1.00 48.88  0  524  GLU   A O   1 
ATOM   3836  C CB  . GLU   A 1 560  ? 154.319 111.575 133.027 1.00 35.30  0  524  GLU   A CB  1 
ATOM   3837  C CG  . GLU   A 1 560  ? 155.033 110.332 132.533 1.00 52.12  0  524  GLU   A CG  1 
ATOM   3838  C CD  . GLU   A 1 560  ? 156.221 110.654 131.649 1.00 52.41  0  524  GLU   A CD  1 
ATOM   3839  O OE1 . GLU   A 1 560  ? 156.188 111.694 130.962 1.00 50.63  0  524  GLU   A OE1 1 
ATOM   3840  O OE2 . GLU   A 1 560  ? 157.190 109.870 131.639 1.00 49.76  -1 524  GLU   A OE2 1 
ATOM   3841  N N   . PHE   A 1 561  ? 153.962 114.113 135.453 1.00 26.14  0  525  PHE   A N   1 
ATOM   3842  C CA  . PHE   A 1 561  ? 153.630 115.520 135.596 1.00 35.36  0  525  PHE   A CA  1 
ATOM   3843  C C   . PHE   A 1 561  ? 153.974 115.985 137.002 1.00 40.70  0  525  PHE   A C   1 
ATOM   3844  O O   . PHE   A 1 561  ? 154.269 115.186 137.894 1.00 38.66  0  525  PHE   A O   1 
ATOM   3845  C CB  . PHE   A 1 561  ? 152.156 115.785 135.284 1.00 33.03  0  525  PHE   A CB  1 
ATOM   3846  C CG  . PHE   A 1 561  ? 151.814 115.636 133.836 1.00 28.42  0  525  PHE   A CG  1 
ATOM   3847  C CD1 . PHE   A 1 561  ? 152.373 116.472 132.893 1.00 32.24  0  525  PHE   A CD1 1 
ATOM   3848  C CD2 . PHE   A 1 561  ? 150.926 114.667 133.418 1.00 34.41  0  525  PHE   A CD2 1 
ATOM   3849  C CE1 . PHE   A 1 561  ? 152.059 116.340 131.564 1.00 35.50  0  525  PHE   A CE1 1 
ATOM   3850  C CE2 . PHE   A 1 561  ? 150.608 114.533 132.091 1.00 34.75  0  525  PHE   A CE2 1 
ATOM   3851  C CZ  . PHE   A 1 561  ? 151.174 115.370 131.163 1.00 36.95  0  525  PHE   A CZ  1 
ATOM   3852  N N   . ARG   A 1 562  ? 153.935 117.299 137.189 1.00 46.77  0  526  ARG   A N   1 
ATOM   3853  C CA  . ARG   A 1 562  ? 154.428 117.943 138.395 1.00 45.16  0  526  ARG   A CA  1 
ATOM   3854  C C   . ARG   A 1 562  ? 153.270 118.543 139.176 1.00 51.91  0  526  ARG   A C   1 
ATOM   3855  O O   . ARG   A 1 562  ? 152.397 119.197 138.596 1.00 54.71  0  526  ARG   A O   1 
ATOM   3856  C CB  . ARG   A 1 562  ? 155.446 119.030 138.047 1.00 47.71  0  526  ARG   A CB  1 
ATOM   3857  C CG  . ARG   A 1 562  ? 156.809 118.497 137.659 1.00 50.00  0  526  ARG   A CG  1 
ATOM   3858  C CD  . ARG   A 1 562  ? 157.302 117.480 138.669 1.00 55.45  0  526  ARG   A CD  1 
ATOM   3859  N NE  . ARG   A 1 562  ? 158.703 117.129 138.467 1.00 58.08  0  526  ARG   A NE  1 
ATOM   3860  C CZ  . ARG   A 1 562  ? 159.574 116.934 139.447 1.00 55.02  0  526  ARG   A CZ  1 
ATOM   3861  N NH1 . ARG   A 1 562  ? 159.225 117.061 140.717 1.00 53.48  1  526  ARG   A NH1 1 
ATOM   3862  N NH2 . ARG   A 1 562  ? 160.826 116.602 139.147 1.00 53.67  0  526  ARG   A NH2 1 
ATOM   3863  N N   . LEU   A 1 563  ? 153.268 118.318 140.489 1.00 47.74  0  527  LEU   A N   1 
ATOM   3864  C CA  . LEU   A 1 563  ? 152.275 118.906 141.373 1.00 41.11  0  527  LEU   A CA  1 
ATOM   3865  C C   . LEU   A 1 563  ? 152.873 120.128 142.050 1.00 43.73  0  527  LEU   A C   1 
ATOM   3866  O O   . LEU   A 1 563  ? 153.892 119.994 142.746 1.00 47.80  0  527  LEU   A O   1 
ATOM   3867  C CB  . LEU   A 1 563  ? 151.821 117.893 142.415 1.00 38.59  0  527  LEU   A CB  1 
ATOM   3868  C CG  . LEU   A 1 563  ? 150.395 118.071 142.927 1.00 40.92  0  527  LEU   A CG  1 
ATOM   3869  C CD1 . LEU   A 1 563  ? 149.400 117.586 141.890 1.00 41.44  0  527  LEU   A CD1 1 
ATOM   3870  C CD2 . LEU   A 1 563  ? 150.210 117.341 144.241 1.00 45.65  0  527  LEU   A CD2 1 
ATOM   3871  N N   . PRO   A 1 564  ? 152.298 121.320 141.879 1.00 45.67  0  528  PRO   A N   1 
ATOM   3872  C CA  . PRO   A 1 564  ? 152.911 122.529 142.447 1.00 47.77  0  528  PRO   A CA  1 
ATOM   3873  C C   . PRO   A 1 564  ? 152.928 122.483 143.968 1.00 49.34  0  528  PRO   A C   1 
ATOM   3874  O O   . PRO   A 1 564  ? 151.907 122.226 144.609 1.00 47.32  0  528  PRO   A O   1 
ATOM   3875  C CB  . PRO   A 1 564  ? 152.015 123.659 141.928 1.00 45.71  0  528  PRO   A CB  1 
ATOM   3876  C CG  . PRO   A 1 564  ? 151.277 123.071 140.772 1.00 42.33  0  528  PRO   A CG  1 
ATOM   3877  C CD  . PRO   A 1 564  ? 151.085 121.632 141.112 1.00 42.38  0  528  PRO   A CD  1 
ATOM   3878  N N   . LYS   A 1 565  ? 154.105 122.739 144.541 1.00 45.62  0  529  LYS   A N   1 
ATOM   3879  C CA  . LYS   A 1 565  ? 154.260 122.678 145.989 1.00 45.94  0  529  LYS   A CA  1 
ATOM   3880  C C   . LYS   A 1 565  ? 153.644 123.888 146.678 1.00 46.78  0  529  LYS   A C   1 
ATOM   3881  O O   . LYS   A 1 565  ? 153.046 123.756 147.751 1.00 47.63  0  529  LYS   A O   1 
ATOM   3882  C CB  . LYS   A 1 565  ? 155.737 122.561 146.354 1.00 47.46  0  529  LYS   A CB  1 
ATOM   3883  C CG  . LYS   A 1 565  ? 156.316 121.177 146.162 1.00 46.04  0  529  LYS   A CG  1 
ATOM   3884  C CD  . LYS   A 1 565  ? 157.532 120.989 147.046 1.00 50.23  0  529  LYS   A CD  1 
ATOM   3885  C CE  . LYS   A 1 565  ? 157.183 121.238 148.506 1.00 48.62  0  529  LYS   A CE  1 
ATOM   3886  N NZ  . LYS   A 1 565  ? 158.348 121.020 149.403 1.00 50.26  1  529  LYS   A NZ  1 
ATOM   3887  N N   . LYS   A 1 566  ? 153.784 125.070 146.088 1.00 51.02  0  530  LYS   A N   1 
ATOM   3888  C CA  . LYS   A 1 566  ? 153.287 126.307 146.675 1.00 52.97  0  530  LYS   A CA  1 
ATOM   3889  C C   . LYS   A 1 566  ? 151.983 126.689 145.988 1.00 56.85  0  530  LYS   A C   1 
ATOM   3890  O O   . LYS   A 1 566  ? 151.946 126.852 144.764 1.00 58.55  0  530  LYS   A O   1 
ATOM   3891  C CB  . LYS   A 1 566  ? 154.325 127.421 146.553 1.00 52.70  0  530  LYS   A CB  1 
ATOM   3892  C CG  . LYS   A 1 566  ? 155.568 127.173 147.395 1.00 53.15  0  530  LYS   A CG  1 
ATOM   3893  C CD  . LYS   A 1 566  ? 156.387 128.436 147.592 1.00 57.26  0  530  LYS   A CD  1 
ATOM   3894  C CE  . LYS   A 1 566  ? 157.476 128.561 146.544 1.00 55.48  0  530  LYS   A CE  1 
ATOM   3895  N NZ  . LYS   A 1 566  ? 158.330 129.756 146.779 1.00 54.45  1  530  LYS   A NZ  1 
ATOM   3896  N N   . VAL   A 1 567  ? 150.923 126.841 146.782 1.00 54.41  0  531  VAL   A N   1 
ATOM   3897  C CA  . VAL   A 1 567  ? 149.585 127.022 146.234 1.00 52.17  0  531  VAL   A CA  1 
ATOM   3898  C C   . VAL   A 1 567  ? 149.468 128.394 145.586 1.00 55.71  0  531  VAL   A C   1 
ATOM   3899  O O   . VAL   A 1 567  ? 149.844 129.415 146.176 1.00 60.57  0  531  VAL   A O   1 
ATOM   3900  C CB  . VAL   A 1 567  ? 148.526 126.832 147.330 1.00 59.37  0  531  VAL   A CB  1 
ATOM   3901  C CG1 . VAL   A 1 567  ? 148.870 127.651 148.561 1.00 53.59  0  531  VAL   A CG1 1 
ATOM   3902  C CG2 . VAL   A 1 567  ? 147.154 127.213 146.808 1.00 60.84  0  531  VAL   A CG2 1 
ATOM   3903  N N   . ASP   A 1 568  ? 148.946 128.422 144.364 1.00 59.69  0  532  ASP   A N   1 
ATOM   3904  C CA  . ASP   A 1 568  ? 148.638 129.682 143.704 1.00 58.44  0  532  ASP   A CA  1 
ATOM   3905  C C   . ASP   A 1 568  ? 147.459 130.336 144.408 1.00 56.70  0  532  ASP   A C   1 
ATOM   3906  O O   . ASP   A 1 568  ? 146.393 129.728 144.542 1.00 57.85  0  532  ASP   A O   1 
ATOM   3907  C CB  . ASP   A 1 568  ? 148.319 129.441 142.231 1.00 63.08  0  532  ASP   A CB  1 
ATOM   3908  C CG  . ASP   A 1 568  ? 148.183 130.728 141.440 1.00 64.20  0  532  ASP   A CG  1 
ATOM   3909  O OD1 . ASP   A 1 568  ? 148.267 131.818 142.040 1.00 62.48  0  532  ASP   A OD1 1 
ATOM   3910  O OD2 . ASP   A 1 568  ? 147.983 130.650 140.210 1.00 63.87  -1 532  ASP   A OD2 1 
ATOM   3911  N N   . LEU   A 1 569  ? 147.647 131.573 144.859 1.00 51.71  0  533  LEU   A N   1 
ATOM   3912  C CA  . LEU   A 1 569  ? 146.594 132.286 145.566 1.00 51.35  0  533  LEU   A CA  1 
ATOM   3913  C C   . LEU   A 1 569  ? 145.615 132.979 144.632 1.00 52.01  0  533  LEU   A C   1 
ATOM   3914  O O   . LEU   A 1 569  ? 144.631 133.549 145.109 1.00 54.82  0  533  LEU   A O   1 
ATOM   3915  C CB  . LEU   A 1 569  ? 147.208 133.309 146.519 1.00 50.65  0  533  LEU   A CB  1 
ATOM   3916  C CG  . LEU   A 1 569  ? 147.804 132.721 147.795 1.00 49.18  0  533  LEU   A CG  1 
ATOM   3917  C CD1 . LEU   A 1 569  ? 148.849 133.653 148.367 1.00 49.68  0  533  LEU   A CD1 1 
ATOM   3918  C CD2 . LEU   A 1 569  ? 146.708 132.452 148.810 1.00 50.62  0  533  LEU   A CD2 1 
ATOM   3919  N N   . GLU   A 1 570  ? 145.859 132.956 143.325 1.00 49.12  0  534  GLU   A N   1 
ATOM   3920  C CA  . GLU   A 1 570  ? 144.923 133.545 142.380 1.00 48.28  0  534  GLU   A CA  1 
ATOM   3921  C C   . GLU   A 1 570  ? 143.803 132.591 141.989 1.00 54.68  0  534  GLU   A C   1 
ATOM   3922  O O   . GLU   A 1 570  ? 142.804 133.034 141.413 1.00 53.72  0  534  GLU   A O   1 
ATOM   3923  C CB  . GLU   A 1 570  ? 145.679 134.016 141.135 1.00 57.61  0  534  GLU   A CB  1 
ATOM   3924  C CG  . GLU   A 1 570  ? 144.869 134.882 140.195 1.00 59.94  0  534  GLU   A CG  1 
ATOM   3925  C CD  . GLU   A 1 570  ? 144.895 136.338 140.595 1.00 63.09  0  534  GLU   A CD  1 
ATOM   3926  O OE1 . GLU   A 1 570  ? 145.968 136.816 141.014 1.00 61.58  0  534  GLU   A OE1 1 
ATOM   3927  O OE2 . GLU   A 1 570  ? 143.841 137.003 140.490 1.00 61.13  -1 534  GLU   A OE2 1 
ATOM   3928  N N   . MET   A 1 571  ? 143.929 131.305 142.307 1.00 62.06  0  535  MET   A N   1 
ATOM   3929  C CA  . MET   A 1 571  ? 142.902 130.327 141.977 1.00 58.49  0  535  MET   A CA  1 
ATOM   3930  C C   . MET   A 1 571  ? 141.984 129.998 143.143 1.00 52.39  0  535  MET   A C   1 
ATOM   3931  O O   . MET   A 1 571  ? 140.847 129.573 142.916 1.00 53.62  0  535  MET   A O   1 
ATOM   3932  C CB  . MET   A 1 571  ? 143.542 129.030 141.471 1.00 56.73  0  535  MET   A CB  1 
ATOM   3933  C CG  . MET   A 1 571  ? 144.274 128.248 142.546 1.00 58.72  0  535  MET   A CG  1 
ATOM   3934  S SD  . MET   A 1 571  ? 144.434 126.498 142.162 1.00 73.60  0  535  MET   A SD  1 
ATOM   3935  C CE  . MET   A 1 571  ? 145.248 125.906 143.640 1.00 58.01  0  535  MET   A CE  1 
ATOM   3936  N N   . ILE   A 1 572  ? 142.440 130.183 144.381 1.00 41.19  0  536  ILE   A N   1 
ATOM   3937  C CA  . ILE   A 1 572  ? 141.658 129.815 145.552 1.00 43.91  0  536  ILE   A CA  1 
ATOM   3938  C C   . ILE   A 1 572  ? 141.029 131.027 146.229 1.00 51.08  0  536  ILE   A C   1 
ATOM   3939  O O   . ILE   A 1 572  ? 140.470 130.898 147.321 1.00 55.80  0  536  ILE   A O   1 
ATOM   3940  C CB  . ILE   A 1 572  ? 142.506 129.017 146.553 1.00 45.25  0  536  ILE   A CB  1 
ATOM   3941  C CG1 . ILE   A 1 572  ? 143.707 129.841 147.009 1.00 45.06  0  536  ILE   A CG1 1 
ATOM   3942  C CG2 . ILE   A 1 572  ? 142.964 127.712 145.938 1.00 46.82  0  536  ILE   A CG2 1 
ATOM   3943  C CD1 . ILE   A 1 572  ? 144.444 129.236 148.177 1.00 45.44  0  536  ILE   A CD1 1 
ATOM   3944  N N   . ILE   A 1 573  ? 141.100 132.202 145.608 1.00 51.65  0  537  ILE   A N   1 
ATOM   3945  C CA  . ILE   A 1 573  ? 140.578 133.432 146.191 1.00 50.93  0  537  ILE   A CA  1 
ATOM   3946  C C   . ILE   A 1 573  ? 139.536 134.014 145.248 1.00 48.78  0  537  ILE   A C   1 
ATOM   3947  O O   . ILE   A 1 573  ? 139.820 134.238 144.067 1.00 48.44  0  537  ILE   A O   1 
ATOM   3948  C CB  . ILE   A 1 573  ? 141.699 134.453 146.459 1.00 46.57  0  537  ILE   A CB  1 
ATOM   3949  C CG1 . ILE   A 1 573  ? 142.647 133.928 147.530 1.00 48.84  0  537  ILE   A CG1 1 
ATOM   3950  C CG2 . ILE   A 1 573  ? 141.117 135.774 146.907 1.00 43.68  0  537  ILE   A CG2 1 
ATOM   3951  C CD1 . ILE   A 1 573  ? 142.070 133.988 148.909 1.00 49.28  0  537  ILE   A CD1 1 
ATOM   3952  N N   . ASN   A 1 574  ? 138.335 134.259 145.768 1.00 59.17  0  538  ASN   A N   1 
ATOM   3953  C CA  . ASN   A 1 574  ? 137.270 134.859 144.975 1.00 63.58  0  538  ASN   A CA  1 
ATOM   3954  C C   . ASN   A 1 574  ? 136.221 135.445 145.910 1.00 62.56  0  538  ASN   A C   1 
ATOM   3955  O O   . ASN   A 1 574  ? 136.183 135.144 147.106 1.00 57.12  0  538  ASN   A O   1 
ATOM   3956  C CB  . ASN   A 1 574  ? 136.642 133.844 144.016 1.00 61.52  0  538  ASN   A CB  1 
ATOM   3957  C CG  . ASN   A 1 574  ? 136.122 134.490 142.749 1.00 60.00  0  538  ASN   A CG  1 
ATOM   3958  O OD1 . ASN   A 1 574  ? 135.881 135.697 142.708 1.00 58.15  0  538  ASN   A OD1 1 
ATOM   3959  N ND2 . ASN   A 1 574  ? 135.945 133.690 141.705 1.00 60.19  0  538  ASN   A ND2 1 
ATOM   3960  N N   . ASP   A 1 575  ? 135.364 136.290 145.342 1.00 58.20  0  539  ASP   A N   1 
ATOM   3961  C CA  . ASP   A 1 575  ? 134.280 136.938 146.081 1.00 56.31  0  539  ASP   A CA  1 
ATOM   3962  C C   . ASP   A 1 575  ? 133.017 136.082 146.083 1.00 62.86  0  539  ASP   A C   1 
ATOM   3963  O O   . ASP   A 1 575  ? 131.935 136.525 145.705 1.00 65.94  0  539  ASP   A O   1 
ATOM   3964  C CB  . ASP   A 1 575  ? 134.004 138.316 145.493 1.00 61.25  0  539  ASP   A CB  1 
ATOM   3965  C CG  . ASP   A 1 575  ? 133.267 139.229 146.458 1.00 68.00  0  539  ASP   A CG  1 
ATOM   3966  O OD1 . ASP   A 1 575  ? 133.356 139.001 147.683 1.00 66.67  0  539  ASP   A OD1 1 
ATOM   3967  O OD2 . ASP   A 1 575  ? 132.596 140.174 145.991 1.00 67.09  -1 539  ASP   A OD2 1 
ATOM   3968  N N   . LYS   A 1 576  ? 133.156 134.834 146.516 1.00 59.00  0  540  LYS   A N   1 
ATOM   3969  C CA  . LYS   A 1 576  ? 132.056 133.887 146.573 1.00 55.55  0  540  LYS   A CA  1 
ATOM   3970  C C   . LYS   A 1 576  ? 131.943 133.329 147.984 1.00 55.38  0  540  LYS   A C   1 
ATOM   3971  O O   . LYS   A 1 576  ? 132.923 133.269 148.730 1.00 51.96  0  540  LYS   A O   1 
ATOM   3972  C CB  . LYS   A 1 576  ? 132.252 132.741 145.573 1.00 54.11  0  540  LYS   A CB  1 
ATOM   3973  C CG  . LYS   A 1 576  ? 132.184 133.157 144.116 1.00 51.85  0  540  LYS   A CG  1 
ATOM   3974  C CD  . LYS   A 1 576  ? 130.813 133.691 143.757 1.00 51.29  0  540  LYS   A CD  1 
ATOM   3975  C CE  . LYS   A 1 576  ? 129.978 132.632 143.061 1.00 56.64  0  540  LYS   A CE  1 
ATOM   3976  N NZ  . LYS   A 1 576  ? 128.522 132.828 143.304 1.00 57.22  1  540  LYS   A NZ  1 
ATOM   3977  N N   . ALA   A 1 577  ? 130.730 132.924 148.346 1.00 47.87  0  541  ALA   A N   1 
ATOM   3978  C CA  . ALA   A 1 577  ? 130.507 132.354 149.662 1.00 41.61  0  541  ALA   A CA  1 
ATOM   3979  C C   . ALA   A 1 577  ? 131.135 130.967 149.751 1.00 42.99  0  541  ALA   A C   1 
ATOM   3980  O O   . ALA   A 1 577  ? 131.425 130.315 148.746 1.00 44.02  0  541  ALA   A O   1 
ATOM   3981  C CB  . ALA   A 1 577  ? 129.014 132.285 149.971 1.00 39.90  0  541  ALA   A CB  1 
ATOM   3982  N N   . ILE   A 1 578  ? 131.358 130.522 150.982 1.00 40.73  0  542  ILE   A N   1 
ATOM   3983  C CA  . ILE   A 1 578  ? 131.905 129.199 151.246 1.00 34.52  0  542  ILE   A CA  1 
ATOM   3984  C C   . ILE   A 1 578  ? 131.005 128.520 152.265 1.00 42.80  0  542  ILE   A C   1 
ATOM   3985  O O   . ILE   A 1 578  ? 130.440 129.177 153.146 1.00 54.63  0  542  ILE   A O   1 
ATOM   3986  C CB  . ILE   A 1 578  ? 133.369 129.271 151.732 1.00 35.66  0  542  ILE   A CB  1 
ATOM   3987  C CG1 . ILE   A 1 578  ? 134.117 127.993 151.370 1.00 34.46  0  542  ILE   A CG1 1 
ATOM   3988  C CG2 . ILE   A 1 578  ? 133.452 129.496 153.233 1.00 35.39  0  542  ILE   A CG2 1 
ATOM   3989  C CD1 . ILE   A 1 578  ? 135.613 128.157 151.405 1.00 38.28  0  542  ILE   A CD1 1 
ATOM   3990  N N   . SER   A 1 579  ? 130.824 127.216 152.114 1.00 25.57  0  543  SER   A N   1 
ATOM   3991  C CA  . SER   A 1 579  ? 130.003 126.488 153.062 1.00 28.53  0  543  SER   A CA  1 
ATOM   3992  C C   . SER   A 1 579  ? 130.712 126.411 154.410 1.00 31.26  0  543  SER   A C   1 
ATOM   3993  O O   . SER   A 1 579  ? 131.924 126.198 154.462 1.00 33.31  0  543  SER   A O   1 
ATOM   3994  C CB  . SER   A 1 579  ? 129.706 125.082 152.551 1.00 33.35  0  543  SER   A CB  1 
ATOM   3995  O OG  . SER   A 1 579  ? 129.104 124.291 153.561 1.00 39.38  0  543  SER   A OG  1 
ATOM   3996  N N   . PRO   A 1 580  ? 129.997 126.599 155.512 1.00 25.55  0  544  PRO   A N   1 
ATOM   3997  C CA  . PRO   A 1 580  ? 130.591 126.363 156.823 1.00 23.43  0  544  PRO   A CA  1 
ATOM   3998  C C   . PRO   A 1 580  ? 130.887 124.887 157.008 1.00 25.66  0  544  PRO   A C   1 
ATOM   3999  O O   . PRO   A 1 580  ? 130.361 124.048 156.263 1.00 34.89  0  544  PRO   A O   1 
ATOM   4000  C CB  . PRO   A 1 580  ? 129.506 126.846 157.798 1.00 26.38  0  544  PRO   A CB  1 
ATOM   4001  C CG  . PRO   A 1 580  ? 128.251 126.832 157.015 1.00 27.95  0  544  PRO   A CG  1 
ATOM   4002  C CD  . PRO   A 1 580  ? 128.635 127.148 155.610 1.00 26.04  0  544  PRO   A CD  1 
ATOM   4003  N N   . PRO   A 1 581  ? 131.737 124.528 157.968 1.00 10.41  0  545  PRO   A N   1 
ATOM   4004  C CA  . PRO   A 1 581  ? 131.983 123.107 158.238 1.00 12.88  0  545  PRO   A CA  1 
ATOM   4005  C C   . PRO   A 1 581  ? 130.706 122.362 158.586 1.00 30.94  0  545  PRO   A C   1 
ATOM   4006  O O   . PRO   A 1 581  ? 129.650 122.979 158.745 1.00 41.87  0  545  PRO   A O   1 
ATOM   4007  C CB  . PRO   A 1 581  ? 132.952 123.136 159.424 1.00 20.01  0  545  PRO   A CB  1 
ATOM   4008  C CG  . PRO   A 1 581  ? 133.588 124.464 159.361 1.00 25.20  0  545  PRO   A CG  1 
ATOM   4009  C CD  . PRO   A 1 581  ? 132.566 125.401 158.812 1.00 13.84  0  545  PRO   A CD  1 
ATOM   4010  N N   . LYS   A 1 582  ? 130.782 121.037 158.701 1.00 34.53  0  546  LYS   A N   1 
ATOM   4011  C CA  . LYS   A 1 582  ? 129.589 120.270 159.040 1.00 33.90  0  546  LYS   A CA  1 
ATOM   4012  C C   . LYS   A 1 582  ? 129.049 120.679 160.405 1.00 37.26  0  546  LYS   A C   1 
ATOM   4013  O O   . LYS   A 1 582  ? 127.871 121.029 160.538 1.00 35.12  0  546  LYS   A O   1 
ATOM   4014  C CB  . LYS   A 1 582  ? 129.900 118.773 158.995 1.00 24.24  0  546  LYS   A CB  1 
ATOM   4015  C CG  . LYS   A 1 582  ? 128.685 117.877 159.150 1.00 29.57  0  546  LYS   A CG  1 
ATOM   4016  C CD  . LYS   A 1 582  ? 128.623 117.240 160.519 1.00 35.04  0  546  LYS   A CD  1 
ATOM   4017  C CE  . LYS   A 1 582  ? 129.648 116.135 160.642 1.00 33.22  0  546  LYS   A CE  1 
ATOM   4018  N NZ  . LYS   A 1 582  ? 129.612 115.480 161.974 1.00 39.53  1  546  LYS   A NZ  1 
ATOM   4019  N N   . ASN   A 1 583  ? 129.912 120.694 161.422 1.00 29.19  0  547  ASN   A N   1 
ATOM   4020  C CA  . ASN   A 1 583  ? 129.467 121.009 162.773 1.00 22.26  0  547  ASN   A CA  1 
ATOM   4021  C C   . ASN   A 1 583  ? 128.880 122.407 162.885 1.00 22.62  0  547  ASN   A C   1 
ATOM   4022  O O   . ASN   A 1 583  ? 128.102 122.667 163.808 1.00 39.36  0  547  ASN   A O   1 
ATOM   4023  C CB  . ASN   A 1 583  ? 130.627 120.855 163.752 1.00 29.75  0  547  ASN   A CB  1 
ATOM   4024  C CG  . ASN   A 1 583  ? 131.107 119.430 163.861 1.00 31.51  0  547  ASN   A CG  1 
ATOM   4025  O OD1 . ASN   A 1 583  ? 130.391 118.496 163.510 1.00 38.83  0  547  ASN   A OD1 1 
ATOM   4026  N ND2 . ASN   A 1 583  ? 132.324 119.251 164.352 1.00 33.43  0  547  ASN   A ND2 1 
ATOM   4027  N N   . LEU   A 1 584  ? 129.231 123.313 161.978 1.00 16.73  0  548  LEU   A N   1 
ATOM   4028  C CA  . LEU   A 1 584  ? 128.714 124.673 161.998 1.00 28.04  0  548  LEU   A CA  1 
ATOM   4029  C C   . LEU   A 1 584  ? 127.688 124.924 160.904 1.00 30.99  0  548  LEU   A C   1 
ATOM   4030  O O   . LEU   A 1 584  ? 127.319 126.080 160.670 1.00 28.61  0  548  LEU   A O   1 
ATOM   4031  C CB  . LEU   A 1 584  ? 129.860 125.676 161.874 1.00 29.69  0  548  LEU   A CB  1 
ATOM   4032  C CG  . LEU   A 1 584  ? 130.864 125.694 163.021 1.00 29.38  0  548  LEU   A CG  1 
ATOM   4033  C CD1 . LEU   A 1 584  ? 132.036 126.583 162.671 1.00 28.08  0  548  LEU   A CD1 1 
ATOM   4034  C CD2 . LEU   A 1 584  ? 130.194 126.165 164.294 1.00 32.24  0  548  LEU   A CD2 1 
ATOM   4035  N N   . ILE   A 1 585  ? 127.213 123.873 160.231 1.00 31.45  0  549  ILE   A N   1 
ATOM   4036  C CA  . ILE   A 1 585  ? 126.294 124.077 159.115 1.00 30.62  0  549  ILE   A CA  1 
ATOM   4037  C C   . ILE   A 1 585  ? 125.016 124.761 159.578 1.00 37.14  0  549  ILE   A C   1 
ATOM   4038  O O   . ILE   A 1 585  ? 124.415 125.543 158.829 1.00 34.31  0  549  ILE   A O   1 
ATOM   4039  C CB  . ILE   A 1 585  ? 126.005 122.739 158.408 1.00 27.11  0  549  ILE   A CB  1 
ATOM   4040  C CG1 . ILE   A 1 585  ? 125.402 122.997 157.032 1.00 33.48  0  549  ILE   A CG1 1 
ATOM   4041  C CG2 . ILE   A 1 585  ? 125.091 121.868 159.241 1.00 30.32  0  549  ILE   A CG2 1 
ATOM   4042  C CD1 . ILE   A 1 585  ? 126.344 123.690 156.089 1.00 34.72  0  549  ILE   A CD1 1 
ATOM   4043  N N   . TRP   A 1 586  ? 124.603 124.519 160.827 1.00 35.15  0  550  TRP   A N   1 
ATOM   4044  C CA  . TRP   A 1 586  ? 123.390 125.136 161.348 1.00 27.50  0  550  TRP   A CA  1 
ATOM   4045  C C   . TRP   A 1 586  ? 123.480 126.653 161.369 1.00 33.99  0  550  TRP   A C   1 
ATOM   4046  O O   . TRP   A 1 586  ? 122.445 127.322 161.440 1.00 38.85  0  550  TRP   A O   1 
ATOM   4047  C CB  . TRP   A 1 586  ? 123.094 124.625 162.755 1.00 28.32  0  550  TRP   A CB  1 
ATOM   4048  C CG  . TRP   A 1 586  ? 123.175 123.144 162.907 1.00 33.11  0  550  TRP   A CG  1 
ATOM   4049  C CD1 . TRP   A 1 586  ? 123.949 122.457 163.791 1.00 38.83  0  550  TRP   A CD1 1 
ATOM   4050  C CD2 . TRP   A 1 586  ? 122.444 122.161 162.166 1.00 32.38  0  550  TRP   A CD2 1 
ATOM   4051  N NE1 . TRP   A 1 586  ? 123.751 121.107 163.646 1.00 36.46  0  550  TRP   A NE1 1 
ATOM   4052  C CE2 . TRP   A 1 586  ? 122.831 120.900 162.653 1.00 35.28  0  550  TRP   A CE2 1 
ATOM   4053  C CE3 . TRP   A 1 586  ? 121.504 122.225 161.136 1.00 31.62  0  550  TRP   A CE3 1 
ATOM   4054  C CZ2 . TRP   A 1 586  ? 122.312 119.715 162.146 1.00 33.63  0  550  TRP   A CZ2 1 
ATOM   4055  C CZ3 . TRP   A 1 586  ? 120.991 121.049 160.634 1.00 32.51  0  550  TRP   A CZ3 1 
ATOM   4056  C CH2 . TRP   A 1 586  ? 121.394 119.811 161.140 1.00 32.42  0  550  TRP   A CH2 1 
ATOM   4057  N N   . THR   A 1 587  ? 124.685 127.210 161.304 1.00 32.80  0  551  THR   A N   1 
ATOM   4058  C CA  . THR   A 1 587  ? 124.803 128.660 161.255 1.00 33.25  0  551  THR   A CA  1 
ATOM   4059  C C   . THR   A 1 587  ? 124.340 129.239 159.943 1.00 29.30  0  551  THR   A C   1 
ATOM   4060  O O   . THR   A 1 587  ? 124.350 130.466 159.815 1.00 31.84  0  551  THR   A O   1 
ATOM   4061  C CB  . THR   A 1 587  ? 126.246 129.083 161.524 1.00 39.63  0  551  THR   A CB  1 
ATOM   4062  O OG1 . THR   A 1 587  ? 127.073 128.680 160.428 1.00 42.71  0  551  THR   A OG1 1 
ATOM   4063  C CG2 . THR   A 1 587  ? 126.756 128.442 162.801 1.00 38.34  0  551  THR   A CG2 1 
ATOM   4064  N N   . SER   A 1 588  ? 123.940 128.443 158.954 1.00 27.48  0  552  SER   A N   1 
ATOM   4065  C CA  . SER   A 1 588  ? 123.434 129.002 157.709 1.00 33.00  0  552  SER   A CA  1 
ATOM   4066  C C   . SER   A 1 588  ? 121.965 129.392 157.782 1.00 34.45  0  552  SER   A C   1 
ATOM   4067  O O   . SER   A 1 588  ? 121.464 130.021 156.846 1.00 35.91  0  552  SER   A O   1 
ATOM   4068  C CB  . SER   A 1 588  ? 123.629 128.012 156.561 1.00 29.95  0  552  SER   A CB  1 
ATOM   4069  O OG  . SER   A 1 588  ? 123.048 128.514 155.372 1.00 27.10  0  552  SER   A OG  1 
ATOM   4070  N N   . PHE   A 1 589  ? 121.270 129.039 158.865 1.00 36.26  0  553  PHE   A N   1 
ATOM   4071  C CA  . PHE   A 1 589  ? 119.851 129.297 159.033 1.00 26.63  0  553  PHE   A CA  1 
ATOM   4072  C C   . PHE   A 1 589  ? 119.619 130.289 160.164 1.00 33.68  0  553  PHE   A C   1 
ATOM   4073  O O   . PHE   A 1 589  ? 120.396 130.321 161.123 1.00 40.34  0  553  PHE   A O   1 
ATOM   4074  C CB  . PHE   A 1 589  ? 119.091 128.001 159.339 1.00 24.88  0  553  PHE   A CB  1 
ATOM   4075  C CG  . PHE   A 1 589  ? 119.408 126.873 158.400 1.00 32.99  0  553  PHE   A CG  1 
ATOM   4076  C CD1 . PHE   A 1 589  ? 119.016 126.925 157.077 1.00 28.31  0  553  PHE   A CD1 1 
ATOM   4077  C CD2 . PHE   A 1 589  ? 120.100 125.760 158.843 1.00 34.44  0  553  PHE   A CD2 1 
ATOM   4078  C CE1 . PHE   A 1 589  ? 119.307 125.890 156.219 1.00 30.24  0  553  PHE   A CE1 1 
ATOM   4079  C CE2 . PHE   A 1 589  ? 120.390 124.726 157.990 1.00 30.97  0  553  PHE   A CE2 1 
ATOM   4080  C CZ  . PHE   A 1 589  ? 119.994 124.792 156.676 1.00 33.38  0  553  PHE   A CZ  1 
ATOM   4081  N N   . PRO   A 1 590  ? 118.562 131.099 160.088 1.00 37.68  0  554  PRO   A N   1 
ATOM   4082  C CA  . PRO   A 1 590  ? 118.327 132.104 161.127 1.00 36.56  0  554  PRO   A CA  1 
ATOM   4083  C C   . PRO   A 1 590  ? 118.178 131.468 162.500 1.00 36.62  0  554  PRO   A C   1 
ATOM   4084  O O   . PRO   A 1 590  ? 117.679 130.351 162.638 1.00 44.87  0  554  PRO   A O   1 
ATOM   4085  C CB  . PRO   A 1 590  ? 117.028 132.779 160.677 1.00 28.45  0  554  PRO   A CB  1 
ATOM   4086  C CG  . PRO   A 1 590  ? 116.989 132.572 159.215 1.00 25.20  0  554  PRO   A CG  1 
ATOM   4087  C CD  . PRO   A 1 590  ? 117.607 131.230 158.977 1.00 33.20  0  554  PRO   A CD  1 
ATOM   4088  N N   . ARG   A 1 591  ? 118.638 132.194 163.520 1.00 39.71  0  555  ARG   A N   1 
ATOM   4089  C CA  . ARG   A 1 591  ? 118.571 131.693 164.886 1.00 46.04  0  555  ARG   A CA  1 
ATOM   4090  C C   . ARG   A 1 591  ? 117.140 131.443 165.342 1.00 49.30  0  555  ARG   A C   1 
ATOM   4091  O O   . ARG   A 1 591  ? 116.918 130.591 166.209 1.00 45.47  0  555  ARG   A O   1 
ATOM   4092  C CB  . ARG   A 1 591  ? 119.256 132.677 165.832 1.00 44.40  0  555  ARG   A CB  1 
ATOM   4093  C CG  . ARG   A 1 591  ? 119.856 132.039 167.066 1.00 43.61  0  555  ARG   A CG  1 
ATOM   4094  C CD  . ARG   A 1 591  ? 120.048 133.072 168.159 1.00 44.26  0  555  ARG   A CD  1 
ATOM   4095  N NE  . ARG   A 1 591  ? 118.770 133.517 168.701 1.00 48.62  0  555  ARG   A NE  1 
ATOM   4096  C CZ  . ARG   A 1 591  ? 118.354 133.271 169.935 1.00 47.09  0  555  ARG   A CZ  1 
ATOM   4097  N NH1 . ARG   A 1 591  ? 119.102 132.599 170.795 1.00 47.64  1  555  ARG   A NH1 1 
ATOM   4098  N NH2 . ARG   A 1 591  ? 117.158 133.708 170.315 1.00 43.22  0  555  ARG   A NH2 1 
ATOM   4099  N N   . ASN   A 1 592  ? 116.169 132.168 164.787 1.00 42.27  0  556  ASN   A N   1 
ATOM   4100  C CA  . ASN   A 1 592  ? 114.773 131.917 165.127 1.00 37.58  0  556  ASN   A CA  1 
ATOM   4101  C C   . ASN   A 1 592  ? 114.317 130.550 164.632 1.00 38.38  0  556  ASN   A C   1 
ATOM   4102  O O   . ASN   A 1 592  ? 113.601 129.835 165.341 1.00 41.72  0  556  ASN   A O   1 
ATOM   4103  C CB  . ASN   A 1 592  ? 113.888 133.017 164.545 1.00 37.72  0  556  ASN   A CB  1 
ATOM   4104  C CG  . ASN   A 1 592  ? 113.679 134.164 165.508 1.00 47.19  0  556  ASN   A CG  1 
ATOM   4105  O OD1 . ASN   A 1 592  ? 114.042 134.080 166.680 1.00 47.17  0  556  ASN   A OD1 1 
ATOM   4106  N ND2 . ASN   A 1 592  ? 113.089 135.246 165.017 1.00 49.90  0  556  ASN   A ND2 1 
ATOM   4107  N N   . TYR   A 1 593  ? 114.724 130.169 163.421 1.00 35.61  0  557  TYR   A N   1 
ATOM   4108  C CA  . TYR   A 1 593  ? 114.268 128.921 162.822 1.00 35.42  0  557  TYR   A CA  1 
ATOM   4109  C C   . TYR   A 1 593  ? 114.894 127.691 163.458 1.00 36.29  0  557  TYR   A C   1 
ATOM   4110  O O   . TYR   A 1 593  ? 114.474 126.574 163.144 1.00 45.66  0  557  TYR   A O   1 
ATOM   4111  C CB  . TYR   A 1 593  ? 114.559 128.916 161.323 1.00 26.37  0  557  TYR   A CB  1 
ATOM   4112  C CG  . TYR   A 1 593  ? 113.664 129.821 160.513 1.00 26.75  0  557  TYR   A CG  1 
ATOM   4113  C CD1 . TYR   A 1 593  ? 112.643 130.540 161.110 1.00 25.12  0  557  TYR   A CD1 1 
ATOM   4114  C CD2 . TYR   A 1 593  ? 113.842 129.955 159.147 1.00 32.13  0  557  TYR   A CD2 1 
ATOM   4115  C CE1 . TYR   A 1 593  ? 111.829 131.365 160.372 1.00 26.27  0  557  TYR   A CE1 1 
ATOM   4116  C CE2 . TYR   A 1 593  ? 113.032 130.777 158.401 1.00 34.09  0  557  TYR   A CE2 1 
ATOM   4117  C CZ  . TYR   A 1 593  ? 112.028 131.479 159.017 1.00 32.94  0  557  TYR   A CZ  1 
ATOM   4118  O OH  . TYR   A 1 593  ? 111.220 132.300 158.271 1.00 34.91  0  557  TYR   A OH  1 
ATOM   4119  N N   . MET   A 1 594  ? 115.854 127.854 164.303 1.00 35.86  0  558  MET   A N   1 
ATOM   4120  C CA  . MET   A 1 594  ? 116.461 126.671 164.879 1.00 40.31  0  558  MET   A CA  1 
ATOM   4121  C C   . MET   A 1 594  ? 115.962 126.437 166.299 1.00 48.92  0  558  MET   A C   1 
ATOM   4122  O O   . MET   A 1 594  ? 115.668 127.388 167.027 1.00 50.86  0  558  MET   A O   1 
ATOM   4123  C CB  . MET   A 1 594  ? 117.985 126.804 164.886 1.00 44.67  0  558  MET   A CB  1 
ATOM   4124  C CG  . MET   A 1 594  ? 118.582 126.760 163.500 1.00 48.18  0  558  MET   A CG  1 
ATOM   4125  S SD  . MET   A 1 594  ? 118.564 125.080 162.861 1.00 56.12  0  558  MET   A SD  1 
ATOM   4126  C CE  . MET   A 1 594  ? 117.755 125.321 161.288 1.00 43.23  0  558  MET   A CE  1 
ATOM   4127  N N   . PRO   A 1 595  ? 115.857 125.179 166.714 1.00 47.97  0  559  PRO   A N   1 
ATOM   4128  C CA  . PRO   A 1 595  ? 115.394 124.882 168.073 1.00 47.23  0  559  PRO   A CA  1 
ATOM   4129  C C   . PRO   A 1 595  ? 116.417 125.312 169.114 1.00 51.20  0  559  PRO   A C   1 
ATOM   4130  O O   . PRO   A 1 595  ? 117.541 125.709 168.807 1.00 53.75  0  559  PRO   A O   1 
ATOM   4131  C CB  . PRO   A 1 595  ? 115.208 123.362 168.065 1.00 48.92  0  559  PRO   A CB  1 
ATOM   4132  C CG  . PRO   A 1 595  ? 115.206 122.967 166.622 1.00 43.50  0  559  PRO   A CG  1 
ATOM   4133  C CD  . PRO   A 1 595  ? 116.069 123.957 165.926 1.00 39.97  0  559  PRO   A CD  1 
ATOM   4134  N N   . SER   A 1 596  ? 115.999 125.227 170.379 1.00 55.29  0  560  SER   A N   1 
ATOM   4135  C CA  . SER   A 1 596  ? 116.853 125.677 171.474 1.00 57.24  0  560  SER   A CA  1 
ATOM   4136  C C   . SER   A 1 596  ? 118.130 124.851 171.555 1.00 51.62  0  560  SER   A C   1 
ATOM   4137  O O   . SER   A 1 596  ? 119.224 125.394 171.753 1.00 54.90  0  560  SER   A O   1 
ATOM   4138  C CB  . SER   A 1 596  ? 116.092 125.607 172.795 1.00 56.69  0  560  SER   A CB  1 
ATOM   4139  O OG  . SER   A 1 596  ? 116.086 124.284 173.299 1.00 55.83  0  560  SER   A OG  1 
ATOM   4140  N N   . HIS   A 1 597  ? 118.008 123.530 171.413 1.00 43.31  0  561  HIS   A N   1 
ATOM   4141  C CA  . HIS   A 1 597  ? 119.184 122.676 171.520 1.00 51.13  0  561  HIS   A CA  1 
ATOM   4142  C C   . HIS   A 1 597  ? 120.180 122.957 170.404 1.00 53.32  0  561  HIS   A C   1 
ATOM   4143  O O   . HIS   A 1 597  ? 121.393 122.943 170.640 1.00 53.73  0  561  HIS   A O   1 
ATOM   4144  C CB  . HIS   A 1 597  ? 118.767 121.202 171.540 1.00 55.30  0  561  HIS   A CB  1 
ATOM   4145  C CG  . HIS   A 1 597  ? 118.302 120.677 170.217 1.00 56.96  0  561  HIS   A CG  1 
ATOM   4146  N ND1 . HIS   A 1 597  ? 117.267 121.248 169.509 1.00 55.07  0  561  HIS   A ND1 1 
ATOM   4147  C CD2 . HIS   A 1 597  ? 118.715 119.614 169.487 1.00 55.10  0  561  HIS   A CD2 1 
ATOM   4148  C CE1 . HIS   A 1 597  ? 117.073 120.569 168.392 1.00 48.63  0  561  HIS   A CE1 1 
ATOM   4149  N NE2 . HIS   A 1 597  ? 117.938 119.573 168.355 1.00 50.61  0  561  HIS   A NE2 1 
ATOM   4150  N N   . ILE   A 1 598  ? 119.692 123.241 169.194 1.00 51.79  0  562  ILE   A N   1 
ATOM   4151  C CA  . ILE   A 1 598  ? 120.588 123.577 168.092 1.00 51.76  0  562  ILE   A CA  1 
ATOM   4152  C C   . ILE   A 1 598  ? 121.323 124.879 168.377 1.00 51.44  0  562  ILE   A C   1 
ATOM   4153  O O   . ILE   A 1 598  ? 122.524 124.997 168.114 1.00 52.19  0  562  ILE   A O   1 
ATOM   4154  C CB  . ILE   A 1 598  ? 119.811 123.640 166.766 1.00 45.10  0  562  ILE   A CB  1 
ATOM   4155  C CG1 . ILE   A 1 598  ? 119.504 122.230 166.276 1.00 48.43  0  562  ILE   A CG1 1 
ATOM   4156  C CG2 . ILE   A 1 598  ? 120.603 124.389 165.717 1.00 36.04  0  562  ILE   A CG2 1 
ATOM   4157  C CD1 . ILE   A 1 598  ? 120.729 121.377 166.100 1.00 45.15  0  562  ILE   A CD1 1 
ATOM   4158  N N   . GLN   A 1 599  ? 120.620 125.879 168.912 1.00 43.86  0  563  GLN   A N   1 
ATOM   4159  C CA  . GLN   A 1 599  ? 121.273 127.146 169.225 1.00 46.06  0  563  GLN   A CA  1 
ATOM   4160  C C   . GLN   A 1 599  ? 122.327 126.977 170.313 1.00 47.51  0  563  GLN   A C   1 
ATOM   4161  O O   . GLN   A 1 599  ? 123.428 127.531 170.209 1.00 48.10  0  563  GLN   A O   1 
ATOM   4162  C CB  . GLN   A 1 599  ? 120.228 128.180 169.634 1.00 48.83  0  563  GLN   A CB  1 
ATOM   4163  C CG  . GLN   A 1 599  ? 119.352 128.641 168.484 1.00 49.42  0  563  GLN   A CG  1 
ATOM   4164  C CD  . GLN   A 1 599  ? 117.982 129.092 168.938 1.00 53.52  0  563  GLN   A CD  1 
ATOM   4165  O OE1 . GLN   A 1 599  ? 117.752 129.319 170.125 1.00 57.33  0  563  GLN   A OE1 1 
ATOM   4166  N NE2 . GLN   A 1 599  ? 117.060 129.222 167.994 1.00 48.61  0  563  GLN   A NE2 1 
ATOM   4167  N N   . ASN   A 1 600  ? 122.014 126.213 171.361 1.00 49.73  0  564  ASN   A N   1 
ATOM   4168  C CA  . ASN   A 1 600  ? 123.000 125.974 172.411 1.00 47.97  0  564  ASN   A CA  1 
ATOM   4169  C C   . ASN   A 1 600  ? 124.209 125.223 171.871 1.00 47.90  0  564  ASN   A C   1 
ATOM   4170  O O   . ASN   A 1 600  ? 125.354 125.541 172.215 1.00 51.76  0  564  ASN   A O   1 
ATOM   4171  C CB  . ASN   A 1 600  ? 122.366 125.202 173.567 1.00 52.94  0  564  ASN   A CB  1 
ATOM   4172  C CG  . ASN   A 1 600  ? 121.288 125.995 174.272 1.00 56.25  0  564  ASN   A CG  1 
ATOM   4173  O OD1 . ASN   A 1 600  ? 121.226 127.218 174.155 1.00 52.32  0  564  ASN   A OD1 1 
ATOM   4174  N ND2 . ASN   A 1 600  ? 120.431 125.302 175.010 1.00 56.11  0  564  ASN   A ND2 1 
ATOM   4175  N N   . TYR   A 1 601  ? 123.976 124.224 171.017 1.00 48.58  0  565  TYR   A N   1 
ATOM   4176  C CA  . TYR   A 1 601  ? 125.081 123.484 170.417 1.00 51.38  0  565  TYR   A CA  1 
ATOM   4177  C C   . TYR   A 1 601  ? 125.938 124.384 169.534 1.00 55.11  0  565  TYR   A C   1 
ATOM   4178  O O   . TYR   A 1 601  ? 127.168 124.278 169.542 1.00 56.33  0  565  TYR   A O   1 
ATOM   4179  C CB  . TYR   A 1 601  ? 124.531 122.301 169.623 1.00 45.31  0  565  TYR   A CB  1 
ATOM   4180  C CG  . TYR   A 1 601  ? 125.449 121.765 168.552 1.00 43.69  0  565  TYR   A CG  1 
ATOM   4181  C CD1 . TYR   A 1 601  ? 126.421 120.825 168.853 1.00 43.61  0  565  TYR   A CD1 1 
ATOM   4182  C CD2 . TYR   A 1 601  ? 125.324 122.179 167.233 1.00 42.99  0  565  TYR   A CD2 1 
ATOM   4183  C CE1 . TYR   A 1 601  ? 127.250 120.324 167.874 1.00 46.09  0  565  TYR   A CE1 1 
ATOM   4184  C CE2 . TYR   A 1 601  ? 126.150 121.687 166.251 1.00 42.78  0  565  TYR   A CE2 1 
ATOM   4185  C CZ  . TYR   A 1 601  ? 127.111 120.760 166.576 1.00 48.21  0  565  TYR   A CZ  1 
ATOM   4186  O OH  . TYR   A 1 601  ? 127.936 120.265 165.595 1.00 53.73  0  565  TYR   A OH  1 
ATOM   4187  N N   . ILE   A 1 602  ? 125.309 125.273 168.763 1.00 50.49  0  566  ILE   A N   1 
ATOM   4188  C CA  . ILE   A 1 602  ? 126.065 126.184 167.906 1.00 45.05  0  566  ILE   A CA  1 
ATOM   4189  C C   . ILE   A 1 602  ? 126.919 127.120 168.750 1.00 47.41  0  566  ILE   A C   1 
ATOM   4190  O O   . ILE   A 1 602  ? 128.094 127.363 168.446 1.00 54.51  0  566  ILE   A O   1 
ATOM   4191  C CB  . ILE   A 1 602  ? 125.115 126.966 166.983 1.00 44.18  0  566  ILE   A CB  1 
ATOM   4192  C CG1 . ILE   A 1 602  ? 124.695 126.095 165.803 1.00 46.92  0  566  ILE   A CG1 1 
ATOM   4193  C CG2 . ILE   A 1 602  ? 125.769 128.239 166.491 1.00 41.96  0  566  ILE   A CG2 1 
ATOM   4194  C CD1 . ILE   A 1 602  ? 125.855 125.625 164.968 1.00 51.02  0  566  ILE   A CD1 1 
ATOM   4195  N N   . GLU   A 1 603  ? 126.340 127.667 169.820 1.00 48.91  0  567  GLU   A N   1 
ATOM   4196  C CA  . GLU   A 1 603  ? 127.106 128.556 170.683 1.00 50.73  0  567  GLU   A CA  1 
ATOM   4197  C C   . GLU   A 1 603  ? 128.236 127.829 171.398 1.00 47.44  0  567  GLU   A C   1 
ATOM   4198  O O   . GLU   A 1 603  ? 129.280 128.435 171.652 1.00 47.03  0  567  GLU   A O   1 
ATOM   4199  C CB  . GLU   A 1 603  ? 126.192 129.230 171.707 1.00 52.01  0  567  GLU   A CB  1 
ATOM   4200  C CG  . GLU   A 1 603  ? 125.120 130.126 171.102 1.00 52.43  0  567  GLU   A CG  1 
ATOM   4201  C CD  . GLU   A 1 603  ? 125.661 131.072 170.047 1.00 56.50  0  567  GLU   A CD  1 
ATOM   4202  O OE1 . GLU   A 1 603  ? 126.693 131.728 170.298 1.00 54.29  0  567  GLU   A OE1 1 
ATOM   4203  O OE2 . GLU   A 1 603  ? 125.049 131.161 168.962 1.00 59.54  -1 567  GLU   A OE2 1 
ATOM   4204  N N   . HIS   A 1 604  ? 128.055 126.554 171.731 1.00 46.66  0  568  HIS   A N   1 
ATOM   4205  C CA  . HIS   A 1 604  ? 129.110 125.791 172.381 1.00 46.72  0  568  HIS   A CA  1 
ATOM   4206  C C   . HIS   A 1 604  ? 130.131 125.223 171.406 1.00 54.22  0  568  HIS   A C   1 
ATOM   4207  O O   . HIS   A 1 604  ? 131.204 124.794 171.843 1.00 63.43  0  568  HIS   A O   1 
ATOM   4208  C CB  . HIS   A 1 604  ? 128.507 124.650 173.203 1.00 47.05  0  568  HIS   A CB  1 
ATOM   4209  C CG  . HIS   A 1 604  ? 127.749 125.111 174.407 1.00 58.41  0  568  HIS   A CG  1 
ATOM   4210  N ND1 . HIS   A 1 604  ? 127.662 126.439 174.767 1.00 61.19  0  568  HIS   A ND1 1 
ATOM   4211  C CD2 . HIS   A 1 604  ? 127.045 124.423 175.337 1.00 55.28  0  568  HIS   A CD2 1 
ATOM   4212  C CE1 . HIS   A 1 604  ? 126.936 126.549 175.864 1.00 53.50  0  568  HIS   A CE1 1 
ATOM   4213  N NE2 . HIS   A 1 604  ? 126.549 125.341 176.231 1.00 57.03  0  568  HIS   A NE2 1 
ATOM   4214  N N   . GLU   A 1 605  ? 129.827 125.200 170.109 1.00 50.74  0  569  GLU   A N   1 
ATOM   4215  C CA  . GLU   A 1 605  ? 130.766 124.702 169.112 1.00 46.87  0  569  GLU   A CA  1 
ATOM   4216  C C   . GLU   A 1 605  ? 131.530 125.804 168.398 1.00 45.19  0  569  GLU   A C   1 
ATOM   4217  O O   . GLU   A 1 605  ? 132.612 125.536 167.865 1.00 42.25  0  569  GLU   A O   1 
ATOM   4218  C CB  . GLU   A 1 605  ? 130.037 123.850 168.069 1.00 48.13  0  569  GLU   A CB  1 
ATOM   4219  C CG  . GLU   A 1 605  ? 129.901 122.393 168.459 1.00 50.45  0  569  GLU   A CG  1 
ATOM   4220  C CD  . GLU   A 1 605  ? 131.186 121.618 168.283 1.00 55.12  0  569  GLU   A CD  1 
ATOM   4221  O OE1 . GLU   A 1 605  ? 131.660 121.510 167.133 1.00 56.36  0  569  GLU   A OE1 1 
ATOM   4222  O OE2 . GLU   A 1 605  ? 131.723 121.117 169.292 1.00 55.00  -1 569  GLU   A OE2 1 
ATOM   4223  N N   . LYS   A 1 606  ? 131.002 127.027 168.367 1.00 43.31  0  570  LYS   A N   1 
ATOM   4224  C CA  . LYS   A 1 606  ? 131.762 128.129 167.793 1.00 41.49  0  570  LYS   A CA  1 
ATOM   4225  C C   . LYS   A 1 606  ? 133.028 128.420 168.587 1.00 47.25  0  570  LYS   A C   1 
ATOM   4226  O O   . LYS   A 1 606  ? 133.931 129.087 168.072 1.00 49.56  0  570  LYS   A O   1 
ATOM   4227  C CB  . LYS   A 1 606  ? 130.893 129.382 167.712 1.00 40.00  0  570  LYS   A CB  1 
ATOM   4228  C CG  . LYS   A 1 606  ? 130.083 129.488 166.437 1.00 39.82  0  570  LYS   A CG  1 
ATOM   4229  C CD  . LYS   A 1 606  ? 129.361 130.816 166.362 1.00 45.34  0  570  LYS   A CD  1 
ATOM   4230  C CE  . LYS   A 1 606  ? 128.645 130.980 165.037 1.00 47.29  0  570  LYS   A CE  1 
ATOM   4231  N NZ  . LYS   A 1 606  ? 127.866 132.246 164.985 1.00 42.07  1  570  LYS   A NZ  1 
ATOM   4232  N N   . LEU   A 1 607  ? 133.113 127.935 169.823 1.00 50.26  0  571  LEU   A N   1 
ATOM   4233  C CA  . LEU   A 1 607  ? 134.290 128.097 170.663 1.00 46.58  0  571  LEU   A CA  1 
ATOM   4234  C C   . LEU   A 1 607  ? 135.315 126.991 170.455 1.00 48.38  0  571  LEU   A C   1 
ATOM   4235  O O   . LEU   A 1 607  ? 136.381 127.026 171.076 1.00 53.98  0  571  LEU   A O   1 
ATOM   4236  C CB  . LEU   A 1 607  ? 133.882 128.149 172.135 1.00 46.79  0  571  LEU   A CB  1 
ATOM   4237  C CG  . LEU   A 1 607  ? 132.648 128.989 172.461 1.00 51.28  0  571  LEU   A CG  1 
ATOM   4238  C CD1 . LEU   A 1 607  ? 132.343 128.927 173.947 1.00 51.78  0  571  LEU   A CD1 1 
ATOM   4239  C CD2 . LEU   A 1 607  ? 132.835 130.426 172.007 1.00 48.53  0  571  LEU   A CD2 1 
ATOM   4240  N N   . LYS   A 1 608  ? 135.013 126.007 169.610 1.00 48.76  0  572  LYS   A N   1 
ATOM   4241  C CA  . LYS   A 1 608  ? 135.953 124.948 169.283 1.00 50.30  0  572  LYS   A CA  1 
ATOM   4242  C C   . LYS   A 1 608  ? 136.495 125.033 167.866 1.00 49.85  0  572  LYS   A C   1 
ATOM   4243  O O   . LYS   A 1 608  ? 137.389 124.255 167.518 1.00 45.82  0  572  LYS   A O   1 
ATOM   4244  C CB  . LYS   A 1 608  ? 135.303 123.570 169.482 1.00 49.19  0  572  LYS   A CB  1 
ATOM   4245  C CG  . LYS   A 1 608  ? 135.039 123.219 170.929 1.00 50.39  0  572  LYS   A CG  1 
ATOM   4246  C CD  . LYS   A 1 608  ? 134.453 121.830 171.048 1.00 49.13  0  572  LYS   A CD  1 
ATOM   4247  C CE  . LYS   A 1 608  ? 135.456 120.785 170.598 1.00 50.88  0  572  LYS   A CE  1 
ATOM   4248  N NZ  . LYS   A 1 608  ? 136.669 120.778 171.458 1.00 49.00  1  572  LYS   A NZ  1 
ATOM   4249  N N   . PHE   A 1 609  ? 135.987 125.945 167.044 1.00 46.58  0  573  PHE   A N   1 
ATOM   4250  C CA  . PHE   A 1 609  ? 136.428 126.103 165.668 1.00 43.37  0  573  PHE   A CA  1 
ATOM   4251  C C   . PHE   A 1 609  ? 137.214 127.396 165.523 1.00 47.08  0  573  PHE   A C   1 
ATOM   4252  O O   . PHE   A 1 609  ? 136.864 128.417 166.121 1.00 48.13  0  573  PHE   A O   1 
ATOM   4253  C CB  . PHE   A 1 609  ? 135.237 126.105 164.709 1.00 40.91  0  573  PHE   A CB  1 
ATOM   4254  C CG  . PHE   A 1 609  ? 134.777 124.734 164.320 1.00 44.75  0  573  PHE   A CG  1 
ATOM   4255  C CD1 . PHE   A 1 609  ? 134.021 123.971 165.188 1.00 39.01  0  573  PHE   A CD1 1 
ATOM   4256  C CD2 . PHE   A 1 609  ? 135.106 124.207 163.085 1.00 43.78  0  573  PHE   A CD2 1 
ATOM   4257  C CE1 . PHE   A 1 609  ? 133.604 122.711 164.835 1.00 37.33  0  573  PHE   A CE1 1 
ATOM   4258  C CE2 . PHE   A 1 609  ? 134.689 122.948 162.727 1.00 39.28  0  573  PHE   A CE2 1 
ATOM   4259  C CZ  . PHE   A 1 609  ? 133.939 122.199 163.603 1.00 41.30  0  573  PHE   A CZ  1 
ATOM   4260  N N   . SER   A 1 610  ? 138.280 127.344 164.730 1.00 49.50  0  574  SER   A N   1 
ATOM   4261  C CA  . SER   A 1 610  ? 139.071 128.536 164.474 1.00 45.96  0  574  SER   A CA  1 
ATOM   4262  C C   . SER   A 1 610  ? 138.241 129.556 163.709 1.00 51.46  0  574  SER   A C   1 
ATOM   4263  O O   . SER   A 1 610  ? 137.234 129.223 163.080 1.00 58.82  0  574  SER   A O   1 
ATOM   4264  C CB  . SER   A 1 610  ? 140.327 128.182 163.683 1.00 46.59  0  574  SER   A CB  1 
ATOM   4265  O OG  . SER   A 1 610  ? 139.989 127.748 162.379 1.00 48.96  0  574  SER   A OG  1 
ATOM   4266  N N   . GLU   A 1 611  ? 138.669 130.817 163.772 1.00 50.72  0  575  GLU   A N   1 
ATOM   4267  C CA  . GLU   A 1 611  ? 137.899 131.884 163.149 1.00 49.89  0  575  GLU   A CA  1 
ATOM   4268  C C   . GLU   A 1 611  ? 137.794 131.677 161.646 1.00 49.73  0  575  GLU   A C   1 
ATOM   4269  O O   . GLU   A 1 611  ? 136.748 131.967 161.062 1.00 53.84  0  575  GLU   A O   1 
ATOM   4270  C CB  . GLU   A 1 611  ? 138.544 133.236 163.474 1.00 55.05  0  575  GLU   A CB  1 
ATOM   4271  C CG  . GLU   A 1 611  ? 138.154 134.426 162.595 1.00 57.38  0  575  GLU   A CG  1 
ATOM   4272  C CD  . GLU   A 1 611  ? 136.656 134.539 162.358 1.00 58.67  0  575  GLU   A CD  1 
ATOM   4273  O OE1 . GLU   A 1 611  ? 135.913 134.672 163.352 1.00 57.08  0  575  GLU   A OE1 1 
ATOM   4274  O OE2 . GLU   A 1 611  ? 136.219 134.518 161.190 1.00 53.97  -1 575  GLU   A OE2 1 
ATOM   4275  N N   . SER   A 1 612  ? 138.836 131.129 161.018 1.00 49.55  0  576  SER   A N   1 
ATOM   4276  C CA  . SER   A 1 612  ? 138.792 130.897 159.578 1.00 51.93  0  576  SER   A CA  1 
ATOM   4277  C C   . SER   A 1 612  ? 137.636 129.981 159.201 1.00 53.37  0  576  SER   A C   1 
ATOM   4278  O O   . SER   A 1 612  ? 136.973 130.197 158.181 1.00 52.94  0  576  SER   A O   1 
ATOM   4279  C CB  . SER   A 1 612  ? 140.117 130.307 159.097 1.00 52.17  0  576  SER   A CB  1 
ATOM   4280  O OG  . SER   A 1 612  ? 140.373 129.057 159.713 1.00 54.66  0  576  SER   A OG  1 
ATOM   4281  N N   . ASP   A 1 613  ? 137.378 128.953 160.011 1.00 49.39  0  577  ASP   A N   1 
ATOM   4282  C CA  . ASP   A 1 613  ? 136.266 128.051 159.729 1.00 44.67  0  577  ASP   A CA  1 
ATOM   4283  C C   . ASP   A 1 613  ? 134.934 128.787 159.766 1.00 45.73  0  577  ASP   A C   1 
ATOM   4284  O O   . ASP   A 1 613  ? 134.092 128.614 158.877 1.00 53.05  0  577  ASP   A O   1 
ATOM   4285  C CB  . ASP   A 1 613  ? 136.268 126.892 160.724 1.00 48.18  0  577  ASP   A CB  1 
ATOM   4286  C CG  . ASP   A 1 613  ? 137.411 125.931 160.492 1.00 51.83  0  577  ASP   A CG  1 
ATOM   4287  O OD1 . ASP   A 1 613  ? 137.866 125.814 159.336 1.00 54.38  0  577  ASP   A OD1 1 
ATOM   4288  O OD2 . ASP   A 1 613  ? 137.858 125.291 161.465 1.00 53.45  -1 577  ASP   A OD2 1 
ATOM   4289  N N   . LYS   A 1 614  ? 134.730 129.627 160.777 1.00 46.20  0  578  LYS   A N   1 
ATOM   4290  C CA  . LYS   A 1 614  ? 133.480 130.362 160.915 1.00 48.33  0  578  LYS   A CA  1 
ATOM   4291  C C   . LYS   A 1 614  ? 133.522 131.653 160.112 1.00 47.69  0  578  LYS   A C   1 
ATOM   4292  O O   . LYS   A 1 614  ? 133.373 132.740 160.677 1.00 53.23  0  578  LYS   A O   1 
ATOM   4293  C CB  . LYS   A 1 614  ? 133.209 130.672 162.386 1.00 47.47  0  578  LYS   A CB  1 
ATOM   4294  C CG  . LYS   A 1 614  ? 133.885 129.715 163.348 1.00 47.02  0  578  LYS   A CG  1 
ATOM   4295  C CD  . LYS   A 1 614  ? 133.465 129.986 164.777 1.00 51.40  0  578  LYS   A CD  1 
ATOM   4296  C CE  . LYS   A 1 614  ? 133.739 131.422 165.170 1.00 50.44  0  578  LYS   A CE  1 
ATOM   4297  N NZ  . LYS   A 1 614  ? 135.193 131.718 165.175 1.00 49.95  1  578  LYS   A NZ  1 
ATOM   4298  N N   . SER   A 1 615  ? 133.715 131.552 158.799 1.00 40.80  0  579  SER   A N   1 
ATOM   4299  C CA  . SER   A 1 615  ? 133.925 132.724 157.958 1.00 46.47  0  579  SER   A CA  1 
ATOM   4300  C C   . SER   A 1 615  ? 132.807 132.982 156.964 1.00 48.25  0  579  SER   A C   1 
ATOM   4301  O O   . SER   A 1 615  ? 132.503 134.144 156.688 1.00 47.56  0  579  SER   A O   1 
ATOM   4302  C CB  . SER   A 1 615  ? 135.245 132.594 157.198 1.00 45.92  0  579  SER   A CB  1 
ATOM   4303  O OG  . SER   A 1 615  ? 136.339 132.546 158.094 1.00 48.68  0  579  SER   A OG  1 
ATOM   4304  N N   . ARG   A 1 616  ? 132.228 131.931 156.380 1.00 50.10  0  580  ARG   A N   1 
ATOM   4305  C CA  . ARG   A 1 616  ? 131.046 132.027 155.526 1.00 51.49  0  580  ARG   A CA  1 
ATOM   4306  C C   . ARG   A 1 616  ? 131.385 132.640 154.167 1.00 49.07  0  580  ARG   A C   1 
ATOM   4307  O O   . ARG   A 1 616  ? 130.562 132.620 153.246 1.00 52.11  0  580  ARG   A O   1 
ATOM   4308  C CB  . ARG   A 1 616  ? 129.943 132.812 156.258 1.00 53.14  0  580  ARG   A CB  1 
ATOM   4309  C CG  . ARG   A 1 616  ? 128.778 133.327 155.424 1.00 53.53  0  580  ARG   A CG  1 
ATOM   4310  C CD  . ARG   A 1 616  ? 127.477 133.443 156.224 1.00 56.46  0  580  ARG   A CD  1 
ATOM   4311  N NE  . ARG   A 1 616  ? 127.026 132.177 156.792 1.00 56.71  0  580  ARG   A NE  1 
ATOM   4312  C CZ  . ARG   A 1 616  ? 127.334 131.738 158.005 1.00 55.49  0  580  ARG   A CZ  1 
ATOM   4313  N NH1 . ARG   A 1 616  ? 128.074 132.456 158.834 1.00 53.05  1  580  ARG   A NH1 1 
ATOM   4314  N NH2 . ARG   A 1 616  ? 126.879 130.553 158.401 1.00 55.47  0  580  ARG   A NH2 1 
ATOM   4315  N N   . ARG   A 1 617  ? 132.612 133.130 154.000 1.00 44.43  0  581  ARG   A N   1 
ATOM   4316  C CA  . ARG   A 1 617  ? 133.056 133.662 152.720 1.00 46.16  0  581  ARG   A CA  1 
ATOM   4317  C C   . ARG   A 1 617  ? 134.489 133.226 152.463 1.00 44.94  0  581  ARG   A C   1 
ATOM   4318  O O   . ARG   A 1 617  ? 135.279 133.055 153.391 1.00 48.29  0  581  ARG   A O   1 
ATOM   4319  C CB  . ARG   A 1 617  ? 132.948 135.188 152.671 1.00 50.22  0  581  ARG   A CB  1 
ATOM   4320  C CG  . ARG   A 1 617  ? 131.533 135.701 152.485 1.00 49.04  0  581  ARG   A CG  1 
ATOM   4321  C CD  . ARG   A 1 617  ? 131.531 137.097 151.898 1.00 46.55  0  581  ARG   A CD  1 
ATOM   4322  N NE  . ARG   A 1 617  ? 131.616 137.074 150.444 1.00 49.96  0  581  ARG   A NE  1 
ATOM   4323  C CZ  . ARG   A 1 617  ? 130.566 137.007 149.637 1.00 55.18  0  581  ARG   A CZ  1 
ATOM   4324  N NH1 . ARG   A 1 617  ? 129.333 136.951 150.111 1.00 53.56  1  581  ARG   A NH1 1 
ATOM   4325  N NH2 . ARG   A 1 617  ? 130.759 136.993 148.321 1.00 55.87  0  581  ARG   A NH2 1 
ATOM   4326  N N   . VAL   A 1 618  ? 134.817 133.049 151.183 1.00 41.86  0  582  VAL   A N   1 
ATOM   4327  C CA  . VAL   A 1 618  ? 136.132 132.530 150.807 1.00 42.88  0  582  VAL   A CA  1 
ATOM   4328  C C   . VAL   A 1 618  ? 137.223 133.538 151.144 1.00 50.15  0  582  VAL   A C   1 
ATOM   4329  O O   . VAL   A 1 618  ? 138.238 133.203 151.769 1.00 53.76  0  582  VAL   A O   1 
ATOM   4330  C CB  . VAL   A 1 618  ? 136.159 132.167 149.313 1.00 44.32  0  582  VAL   A CB  1 
ATOM   4331  C CG1 . VAL   A 1 618  ? 137.575 131.851 148.874 1.00 47.68  0  582  VAL   A CG1 1 
ATOM   4332  C CG2 . VAL   A 1 618  ? 135.239 131.001 149.038 1.00 45.22  0  582  VAL   A CG2 1 
ATOM   4333  N N   . LEU   A 1 619  ? 137.028 134.791 150.730 1.00 46.96  0  583  LEU   A N   1 
ATOM   4334  C CA  . LEU   A 1 619  ? 138.027 135.817 150.994 1.00 42.45  0  583  LEU   A CA  1 
ATOM   4335  C C   . LEU   A 1 619  ? 138.209 136.022 152.488 1.00 42.61  0  583  LEU   A C   1 
ATOM   4336  O O   . LEU   A 1 619  ? 139.336 136.162 152.970 1.00 45.53  0  583  LEU   A O   1 
ATOM   4337  C CB  . LEU   A 1 619  ? 137.625 137.122 150.314 1.00 40.86  0  583  LEU   A CB  1 
ATOM   4338  C CG  . LEU   A 1 619  ? 138.640 138.257 150.386 1.00 40.20  0  583  LEU   A CG  1 
ATOM   4339  C CD1 . LEU   A 1 619  ? 139.958 137.815 149.787 1.00 40.62  0  583  LEU   A CD1 1 
ATOM   4340  C CD2 . LEU   A 1 619  ? 138.104 139.478 149.666 1.00 42.40  0  583  LEU   A CD2 1 
ATOM   4341  N N   . GLU   A 1 620  ? 137.108 136.029 153.238 1.00 42.18  0  584  GLU   A N   1 
ATOM   4342  C CA  . GLU   A 1 620  ? 137.202 136.082 154.691 1.00 44.43  0  584  GLU   A CA  1 
ATOM   4343  C C   . GLU   A 1 620  ? 137.768 134.788 155.263 1.00 50.24  0  584  GLU   A C   1 
ATOM   4344  O O   . GLU   A 1 620  ? 138.408 134.809 156.319 1.00 54.97  0  584  GLU   A O   1 
ATOM   4345  C CB  . GLU   A 1 620  ? 135.826 136.385 155.282 1.00 41.50  0  584  GLU   A CB  1 
ATOM   4346  C CG  . GLU   A 1 620  ? 135.765 136.364 156.796 1.00 48.17  0  584  GLU   A CG  1 
ATOM   4347  C CD  . GLU   A 1 620  ? 134.515 137.026 157.336 1.00 58.82  0  584  GLU   A CD  1 
ATOM   4348  O OE1 . GLU   A 1 620  ? 133.423 136.783 156.780 1.00 57.27  0  584  GLU   A OE1 1 
ATOM   4349  O OE2 . GLU   A 1 620  ? 134.625 137.790 158.317 1.00 58.78  -1 584  GLU   A OE2 1 
ATOM   4350  N N   . TYR   A 1 621  ? 137.547 133.657 154.586 1.00 43.41  0  585  TYR   A N   1 
ATOM   4351  C CA  . TYR   A 1 621  ? 138.115 132.394 155.050 1.00 39.02  0  585  TYR   A CA  1 
ATOM   4352  C C   . TYR   A 1 621  ? 139.633 132.435 155.019 1.00 41.05  0  585  TYR   A C   1 
ATOM   4353  O O   . TYR   A 1 621  ? 140.294 131.939 155.938 1.00 45.56  0  585  TYR   A O   1 
ATOM   4354  C CB  . TYR   A 1 621  ? 137.603 131.232 154.198 1.00 41.82  0  585  TYR   A CB  1 
ATOM   4355  C CG  . TYR   A 1 621  ? 138.317 129.918 154.432 1.00 38.97  0  585  TYR   A CG  1 
ATOM   4356  C CD1 . TYR   A 1 621  ? 138.019 129.131 155.532 1.00 43.19  0  585  TYR   A CD1 1 
ATOM   4357  C CD2 . TYR   A 1 621  ? 139.278 129.459 153.548 1.00 40.23  0  585  TYR   A CD2 1 
ATOM   4358  C CE1 . TYR   A 1 621  ? 138.661 127.933 155.752 1.00 39.75  0  585  TYR   A CE1 1 
ATOM   4359  C CE2 . TYR   A 1 621  ? 139.927 128.262 153.762 1.00 46.37  0  585  TYR   A CE2 1 
ATOM   4360  C CZ  . TYR   A 1 621  ? 139.614 127.504 154.865 1.00 43.59  0  585  TYR   A CZ  1 
ATOM   4361  O OH  . TYR   A 1 621  ? 140.259 126.310 155.080 1.00 43.84  0  585  TYR   A OH  1 
ATOM   4362  N N   . TYR   A 1 622  ? 140.203 133.017 153.967 1.00 44.24  0  586  TYR   A N   1 
ATOM   4363  C CA  . TYR   A 1 622  ? 141.653 133.021 153.816 1.00 43.94  0  586  TYR   A CA  1 
ATOM   4364  C C   . TYR   A 1 622  ? 142.310 134.209 154.512 1.00 46.60  0  586  TYR   A C   1 
ATOM   4365  O O   . TYR   A 1 622  ? 143.389 134.064 155.094 1.00 48.31  0  586  TYR   A O   1 
ATOM   4366  C CB  . TYR   A 1 622  ? 142.020 132.990 152.333 1.00 40.66  0  586  TYR   A CB  1 
ATOM   4367  C CG  . TYR   A 1 622  ? 141.978 131.594 151.768 1.00 47.20  0  586  TYR   A CG  1 
ATOM   4368  C CD1 . TYR   A 1 622  ? 142.794 130.598 152.280 1.00 48.47  0  586  TYR   A CD1 1 
ATOM   4369  C CD2 . TYR   A 1 622  ? 141.100 131.261 150.751 1.00 45.37  0  586  TYR   A CD2 1 
ATOM   4370  C CE1 . TYR   A 1 622  ? 142.752 129.318 151.781 1.00 48.13  0  586  TYR   A CE1 1 
ATOM   4371  C CE2 . TYR   A 1 622  ? 141.052 129.983 150.246 1.00 44.19  0  586  TYR   A CE2 1 
ATOM   4372  C CZ  . TYR   A 1 622  ? 141.879 129.016 150.764 1.00 45.46  0  586  TYR   A CZ  1 
ATOM   4373  O OH  . TYR   A 1 622  ? 141.832 127.738 150.262 1.00 44.54  0  586  TYR   A OH  1 
ATOM   4374  N N   . LEU   A 1 623  ? 141.674 135.382 154.476 1.00 46.42  0  587  LEU   A N   1 
ATOM   4375  C CA  . LEU   A 1 623  ? 142.237 136.547 155.148 1.00 40.59  0  587  LEU   A CA  1 
ATOM   4376  C C   . LEU   A 1 623  ? 142.357 136.328 156.645 1.00 37.24  0  587  LEU   A C   1 
ATOM   4377  O O   . LEU   A 1 623  ? 143.256 136.880 157.284 1.00 50.77  0  587  LEU   A O   1 
ATOM   4378  C CB  . LEU   A 1 623  ? 141.381 137.783 154.879 1.00 36.56  0  587  LEU   A CB  1 
ATOM   4379  C CG  . LEU   A 1 623  ? 141.546 138.445 153.516 1.00 40.48  0  587  LEU   A CG  1 
ATOM   4380  C CD1 . LEU   A 1 623  ? 140.690 139.691 153.425 1.00 41.38  0  587  LEU   A CD1 1 
ATOM   4381  C CD2 . LEU   A 1 623  ? 143.001 138.770 153.280 1.00 47.39  0  587  LEU   A CD2 1 
ATOM   4382  N N   . ARG   A 1 624  ? 141.465 135.531 157.222 1.00 37.78  0  588  ARG   A N   1 
ATOM   4383  C CA  . ARG   A 1 624  ? 141.445 135.291 158.655 1.00 46.54  0  588  ARG   A CA  1 
ATOM   4384  C C   . ARG   A 1 624  ? 142.178 134.019 159.048 1.00 49.41  0  588  ARG   A C   1 
ATOM   4385  O O   . ARG   A 1 624  ? 142.114 133.614 160.212 1.00 52.80  0  588  ARG   A O   1 
ATOM   4386  C CB  . ARG   A 1 624  ? 140.004 135.246 159.152 1.00 48.17  0  588  ARG   A CB  1 
ATOM   4387  C CG  . ARG   A 1 624  ? 139.352 136.611 159.214 1.00 48.80  0  588  ARG   A CG  1 
ATOM   4388  C CD  . ARG   A 1 624  ? 137.918 136.508 159.668 1.00 49.14  0  588  ARG   A CD  1 
ATOM   4389  N NE  . ARG   A 1 624  ? 137.315 137.810 159.911 1.00 49.72  0  588  ARG   A NE  1 
ATOM   4390  C CZ  . ARG   A 1 624  ? 137.448 138.489 161.041 1.00 53.01  0  588  ARG   A CZ  1 
ATOM   4391  N NH1 . ARG   A 1 624  ? 138.170 138.022 162.046 1.00 53.38  1  588  ARG   A NH1 1 
ATOM   4392  N NH2 . ARG   A 1 624  ? 136.841 139.666 161.166 1.00 54.76  0  588  ARG   A NH2 1 
ATOM   4393  N N   . ASP   A 1 625  ? 142.874 133.383 158.109 1.00 50.23  0  589  ASP   A N   1 
ATOM   4394  C CA  . ASP   A 1 625  ? 143.603 132.145 158.379 1.00 53.33  0  589  ASP   A CA  1 
ATOM   4395  C C   . ASP   A 1 625  ? 144.975 132.520 158.918 1.00 56.94  0  589  ASP   A C   1 
ATOM   4396  O O   . ASP   A 1 625  ? 145.894 132.848 158.167 1.00 60.26  0  589  ASP   A O   1 
ATOM   4397  C CB  . ASP   A 1 625  ? 143.702 131.293 157.121 1.00 55.07  0  589  ASP   A CB  1 
ATOM   4398  C CG  . ASP   A 1 625  ? 143.587 129.810 157.411 1.00 59.08  0  589  ASP   A CG  1 
ATOM   4399  O OD1 . ASP   A 1 625  ? 143.594 129.013 156.450 1.00 54.44  0  589  ASP   A OD1 1 
ATOM   4400  O OD2 . ASP   A 1 625  ? 143.493 129.442 158.600 1.00 65.59  -1 589  ASP   A OD2 1 
ATOM   4401  N N   . ASN   A 1 626  ? 145.117 132.469 160.241 1.00 60.75  0  590  ASN   A N   1 
ATOM   4402  C CA  . ASN   A 1 626  ? 146.352 132.852 160.908 1.00 61.07  0  590  ASN   A CA  1 
ATOM   4403  C C   . ASN   A 1 626  ? 147.354 131.707 160.990 1.00 59.63  0  590  ASN   A C   1 
ATOM   4404  O O   . ASN   A 1 626  ? 148.473 131.907 161.472 1.00 59.72  0  590  ASN   A O   1 
ATOM   4405  C CB  . ASN   A 1 626  ? 146.032 133.431 162.293 1.00 58.55  0  590  ASN   A CB  1 
ATOM   4406  C CG  . ASN   A 1 626  ? 146.036 132.391 163.401 1.00 60.55  0  590  ASN   A CG  1 
ATOM   4407  O OD1 . ASN   A 1 626  ? 147.075 131.847 163.772 1.00 61.87  0  590  ASN   A OD1 1 
ATOM   4408  N ND2 . ASN   A 1 626  ? 144.856 132.118 163.944 1.00 57.42  0  590  ASN   A ND2 1 
ATOM   4409  N N   . LYS   A 1 627  ? 146.990 130.525 160.495 1.00 56.63  0  591  LYS   A N   1 
ATOM   4410  C CA  . LYS   A 1 627  ? 147.897 129.387 160.430 1.00 59.01  0  591  LYS   A CA  1 
ATOM   4411  C C   . LYS   A 1 627  ? 148.132 128.978 158.981 1.00 63.66  0  591  LYS   A C   1 
ATOM   4412  O O   . LYS   A 1 627  ? 148.398 127.810 158.690 1.00 63.37  0  591  LYS   A O   1 
ATOM   4413  C CB  . LYS   A 1 627  ? 147.359 128.213 161.245 1.00 60.16  0  591  LYS   A CB  1 
ATOM   4414  C CG  . LYS   A 1 627  ? 147.933 128.123 162.648 1.00 59.65  0  591  LYS   A CG  1 
ATOM   4415  C CD  . LYS   A 1 627  ? 147.210 127.072 163.477 1.00 65.14  0  591  LYS   A CD  1 
ATOM   4416  C CE  . LYS   A 1 627  ? 145.771 127.482 163.757 1.00 66.62  0  591  LYS   A CE  1 
ATOM   4417  N NZ  . LYS   A 1 627  ? 145.675 128.669 164.653 1.00 65.26  1  591  LYS   A NZ  1 
ATOM   4418  N N   . PHE   A 1 628  ? 148.027 129.937 158.066 1.00 60.54  0  592  PHE   A N   1 
ATOM   4419  C CA  . PHE   A 1 628  ? 148.185 129.654 156.649 1.00 53.24  0  592  PHE   A CA  1 
ATOM   4420  C C   . PHE   A 1 628  ? 149.619 129.250 156.336 1.00 52.96  0  592  PHE   A C   1 
ATOM   4421  O O   . PHE   A 1 628  ? 150.574 129.786 156.904 1.00 52.53  0  592  PHE   A O   1 
ATOM   4422  C CB  . PHE   A 1 628  ? 147.795 130.881 155.826 1.00 50.97  0  592  PHE   A CB  1 
ATOM   4423  C CG  . PHE   A 1 628  ? 147.647 130.610 154.361 1.00 53.02  0  592  PHE   A CG  1 
ATOM   4424  C CD1 . PHE   A 1 628  ? 147.117 129.416 153.914 1.00 56.74  0  592  PHE   A CD1 1 
ATOM   4425  C CD2 . PHE   A 1 628  ? 148.026 131.557 153.428 1.00 49.56  0  592  PHE   A CD2 1 
ATOM   4426  C CE1 . PHE   A 1 628  ? 146.975 129.167 152.566 1.00 56.49  0  592  PHE   A CE1 1 
ATOM   4427  C CE2 . PHE   A 1 628  ? 147.886 131.315 152.078 1.00 52.62  0  592  PHE   A CE2 1 
ATOM   4428  C CZ  . PHE   A 1 628  ? 147.360 130.119 151.647 1.00 57.41  0  592  PHE   A CZ  1 
ATOM   4429  N N   . ASN   A 1 629  ? 149.761 128.289 155.431 1.00 52.97  0  593  ASN   A N   1 
ATOM   4430  C CA  . ASN   A 1 629  ? 151.054 127.857 154.927 1.00 56.94  0  593  ASN   A CA  1 
ATOM   4431  C C   . ASN   A 1 629  ? 151.008 127.861 153.408 1.00 57.31  0  593  ASN   A C   1 
ATOM   4432  O O   . ASN   A 1 629  ? 149.948 127.679 152.805 1.00 58.53  0  593  ASN   A O   1 
ATOM   4433  C CB  . ASN   A 1 629  ? 151.422 126.459 155.436 1.00 58.40  0  593  ASN   A CB  1 
ATOM   4434  C CG  . ASN   A 1 629  ? 152.917 126.236 155.505 1.00 62.82  0  593  ASN   A CG  1 
ATOM   4435  O OD1 . ASN   A 1 629  ? 153.630 126.411 154.518 1.00 60.79  0  593  ASN   A OD1 1 
ATOM   4436  N ND2 . ASN   A 1 629  ? 153.399 125.838 156.675 1.00 63.57  0  593  ASN   A ND2 1 
ATOM   4437  N N   . GLU   A 1 630  ? 152.165 128.084 152.789 1.00 57.32  0  594  GLU   A N   1 
ATOM   4438  C CA  . GLU   A 1 630  ? 152.212 128.100 151.334 1.00 58.98  0  594  GLU   A CA  1 
ATOM   4439  C C   . GLU   A 1 630  ? 152.088 126.706 150.741 1.00 56.69  0  594  GLU   A C   1 
ATOM   4440  O O   . GLU   A 1 630  ? 151.737 126.576 149.564 1.00 53.68  0  594  GLU   A O   1 
ATOM   4441  C CB  . GLU   A 1 630  ? 153.508 128.751 150.853 1.00 59.24  0  594  GLU   A CB  1 
ATOM   4442  C CG  . GLU   A 1 630  ? 153.404 129.426 149.495 1.00 61.76  0  594  GLU   A CG  1 
ATOM   4443  C CD  . GLU   A 1 630  ? 152.215 130.363 149.394 1.00 63.64  0  594  GLU   A CD  1 
ATOM   4444  O OE1 . GLU   A 1 630  ? 152.358 131.545 149.769 1.00 58.59  0  594  GLU   A OE1 1 
ATOM   4445  O OE2 . GLU   A 1 630  ? 151.141 129.925 148.932 1.00 60.40  -1 594  GLU   A OE2 1 
ATOM   4446  N N   . CYS   A 1 631  ? 152.357 125.666 151.523 1.00 55.26  0  595  CYS   A N   1 
ATOM   4447  C CA  . CYS   A 1 631  ? 152.364 124.292 151.042 1.00 50.71  0  595  CYS   A CA  1 
ATOM   4448  C C   . CYS   A 1 631  ? 151.428 123.423 151.866 1.00 52.06  0  595  CYS   A C   1 
ATOM   4449  O O   . CYS   A 1 631  ? 151.682 122.236 152.084 1.00 52.34  0  595  CYS   A O   1 
ATOM   4450  C CB  . CYS   A 1 631  ? 153.780 123.723 151.049 1.00 55.19  0  595  CYS   A CB  1 
ATOM   4451  S SG  . CYS   A 1 631  ? 154.547 123.653 152.681 1.00 62.97  0  595  CYS   A SG  1 
ATOM   4452  N N   . ASP   A 1 632  ? 150.328 124.004 152.349 1.00 55.56  0  596  ASP   A N   1 
ATOM   4453  C CA  . ASP   A 1 632  ? 149.301 123.202 153.004 1.00 51.76  0  596  ASP   A CA  1 
ATOM   4454  C C   . ASP   A 1 632  ? 148.482 122.402 152.005 1.00 52.48  0  596  ASP   A C   1 
ATOM   4455  O O   . ASP   A 1 632  ? 148.088 121.271 152.302 1.00 54.96  0  596  ASP   A O   1 
ATOM   4456  C CB  . ASP   A 1 632  ? 148.372 124.087 153.835 1.00 51.36  0  596  ASP   A CB  1 
ATOM   4457  C CG  . ASP   A 1 632  ? 148.836 124.236 155.266 1.00 58.59  0  596  ASP   A CG  1 
ATOM   4458  O OD1 . ASP   A 1 632  ? 149.528 123.323 155.762 1.00 61.29  0  596  ASP   A OD1 1 
ATOM   4459  O OD2 . ASP   A 1 632  ? 148.498 125.257 155.900 1.00 59.24  -1 596  ASP   A OD2 1 
ATOM   4460  N N   . LEU   A 1 633  ? 148.207 122.968 150.830 1.00 42.37  0  597  LEU   A N   1 
ATOM   4461  C CA  . LEU   A 1 633  ? 147.426 122.251 149.828 1.00 36.99  0  597  LEU   A CA  1 
ATOM   4462  C C   . LEU   A 1 633  ? 148.169 121.019 149.328 1.00 36.83  0  597  LEU   A C   1 
ATOM   4463  O O   . LEU   A 1 633  ? 147.588 119.935 149.203 1.00 43.50  0  597  LEU   A O   1 
ATOM   4464  C CB  . LEU   A 1 633  ? 147.083 123.191 148.676 1.00 28.30  0  597  LEU   A CB  1 
ATOM   4465  C CG  . LEU   A 1 633  ? 146.241 122.600 147.555 1.00 34.62  0  597  LEU   A CG  1 
ATOM   4466  C CD1 . LEU   A 1 633  ? 144.979 122.011 148.127 1.00 43.15  0  597  LEU   A CD1 1 
ATOM   4467  C CD2 . LEU   A 1 633  ? 145.909 123.679 146.553 1.00 32.74  0  597  LEU   A CD2 1 
ATOM   4468  N N   . TYR   A 1 634  ? 149.462 121.169 149.036 1.00 36.11  0  598  TYR   A N   1 
ATOM   4469  C CA  . TYR   A 1 634  ? 150.256 120.034 148.580 1.00 36.47  0  598  TYR   A CA  1 
ATOM   4470  C C   . TYR   A 1 634  ? 150.359 118.967 149.659 1.00 34.28  0  598  TYR   A C   1 
ATOM   4471  O O   . TYR   A 1 634  ? 150.250 117.771 149.371 1.00 43.80  0  598  TYR   A O   1 
ATOM   4472  C CB  . TYR   A 1 634  ? 151.643 120.513 148.151 1.00 47.17  0  598  TYR   A CB  1 
ATOM   4473  C CG  . TYR   A 1 634  ? 152.692 119.426 148.052 1.00 45.99  0  598  TYR   A CG  1 
ATOM   4474  C CD1 . TYR   A 1 634  ? 153.522 119.138 149.126 1.00 47.26  0  598  TYR   A CD1 1 
ATOM   4475  C CD2 . TYR   A 1 634  ? 152.865 118.705 146.881 1.00 35.72  0  598  TYR   A CD2 1 
ATOM   4476  C CE1 . TYR   A 1 634  ? 154.479 118.155 149.044 1.00 40.28  0  598  TYR   A CE1 1 
ATOM   4477  C CE2 . TYR   A 1 634  ? 153.825 117.720 146.790 1.00 40.04  0  598  TYR   A CE2 1 
ATOM   4478  C CZ  . TYR   A 1 634  ? 154.629 117.450 147.875 1.00 43.02  0  598  TYR   A CZ  1 
ATOM   4479  O OH  . TYR   A 1 634  ? 155.590 116.470 147.798 1.00 50.54  0  598  TYR   A OH  1 
ATOM   4480  N N   . ASN   A 1 635  ? 150.575 119.378 150.909 1.00 30.98  0  599  ASN   A N   1 
ATOM   4481  C CA  . ASN   A 1 635  ? 150.629 118.417 152.003 1.00 37.77  0  599  ASN   A CA  1 
ATOM   4482  C C   . ASN   A 1 635  ? 149.296 117.718 152.222 1.00 47.86  0  599  ASN   A C   1 
ATOM   4483  O O   . ASN   A 1 635  ? 149.281 116.548 152.615 1.00 48.61  0  599  ASN   A O   1 
ATOM   4484  C CB  . ASN   A 1 635  ? 151.072 119.109 153.290 1.00 40.85  0  599  ASN   A CB  1 
ATOM   4485  C CG  . ASN   A 1 635  ? 152.562 119.356 153.332 1.00 45.29  0  599  ASN   A CG  1 
ATOM   4486  O OD1 . ASN   A 1 635  ? 153.354 118.419 153.411 1.00 48.98  0  599  ASN   A OD1 1 
ATOM   4487  N ND2 . ASN   A 1 635  ? 152.955 120.620 153.273 1.00 47.13  0  599  ASN   A ND2 1 
ATOM   4488  N N   . CYS   A 1 636  ? 148.182 118.409 151.987 1.00 47.08  0  600  CYS   A N   1 
ATOM   4489  C CA  . CYS   A 1 636  ? 146.870 117.779 152.068 1.00 41.44  0  600  CYS   A CA  1 
ATOM   4490  C C   . CYS   A 1 636  ? 146.693 116.741 150.968 1.00 38.99  0  600  CYS   A C   1 
ATOM   4491  O O   . CYS   A 1 636  ? 146.246 115.619 151.221 1.00 43.51  0  600  CYS   A O   1 
ATOM   4492  C CB  . CYS   A 1 636  ? 145.776 118.845 151.982 1.00 42.79  0  600  CYS   A CB  1 
ATOM   4493  S SG  . CYS   A 1 636  ? 144.093 118.208 152.034 1.00 63.96  0  600  CYS   A SG  1 
ATOM   4494  N N   . VAL   A 1 637  ? 147.051 117.102 149.735 1.00 38.58  0  601  VAL   A N   1 
ATOM   4495  C CA  . VAL   A 1 637  ? 146.872 116.186 148.612 1.00 36.00  0  601  VAL   A CA  1 
ATOM   4496  C C   . VAL   A 1 637  ? 147.751 114.954 148.775 1.00 36.66  0  601  VAL   A C   1 
ATOM   4497  O O   . VAL   A 1 637  ? 147.308 113.823 148.544 1.00 42.96  0  601  VAL   A O   1 
ATOM   4498  C CB  . VAL   A 1 637  ? 147.152 116.910 147.285 1.00 30.59  0  601  VAL   A CB  1 
ATOM   4499  C CG1 . VAL   A 1 637  ? 147.438 115.910 146.192 1.00 25.60  0  601  VAL   A CG1 1 
ATOM   4500  C CG2 . VAL   A 1 637  ? 145.972 117.771 146.915 1.00 34.45  0  601  VAL   A CG2 1 
ATOM   4501  N N   . VAL   A 1 638  ? 149.008 115.150 149.173 1.00 39.73  0  602  VAL   A N   1 
ATOM   4502  C CA  . VAL   A 1 638  ? 149.928 114.026 149.301 1.00 42.91  0  602  VAL   A CA  1 
ATOM   4503  C C   . VAL   A 1 638  ? 149.475 113.076 150.402 1.00 47.41  0  602  VAL   A C   1 
ATOM   4504  O O   . VAL   A 1 638  ? 149.463 111.854 150.219 1.00 51.15  0  602  VAL   A O   1 
ATOM   4505  C CB  . VAL   A 1 638  ? 151.357 114.540 149.543 1.00 45.78  0  602  VAL   A CB  1 
ATOM   4506  C CG1 . VAL   A 1 638  ? 152.241 113.432 150.082 1.00 42.45  0  602  VAL   A CG1 1 
ATOM   4507  C CG2 . VAL   A 1 638  ? 151.926 115.099 148.258 1.00 47.77  0  602  VAL   A CG2 1 
ATOM   4508  N N   . ASN   A 1 639  ? 149.084 113.615 151.555 1.00 41.39  0  603  ASN   A N   1 
ATOM   4509  C CA  . ASN   A 1 639  ? 148.666 112.786 152.676 1.00 43.56  0  603  ASN   A CA  1 
ATOM   4510  C C   . ASN   A 1 639  ? 147.208 112.361 152.598 1.00 48.73  0  603  ASN   A C   1 
ATOM   4511  O O   . ASN   A 1 639  ? 146.774 111.554 153.426 1.00 47.56  0  603  ASN   A O   1 
ATOM   4512  C CB  . ASN   A 1 639  ? 148.902 113.520 153.996 1.00 41.28  0  603  ASN   A CB  1 
ATOM   4513  C CG  . ASN   A 1 639  ? 150.279 114.124 154.083 1.00 46.14  0  603  ASN   A CG  1 
ATOM   4514  O OD1 . ASN   A 1 639  ? 151.215 113.653 153.444 1.00 48.32  0  603  ASN   A OD1 1 
ATOM   4515  N ND2 . ASN   A 1 639  ? 150.412 115.177 154.877 1.00 50.23  0  603  ASN   A ND2 1 
ATOM   4516  N N   . GLN   A 1 640  ? 146.452 112.880 151.632 1.00 47.30  0  604  GLN   A N   1 
ATOM   4517  C CA  . GLN   A 1 640  ? 145.029 112.588 151.485 1.00 41.26  0  604  GLN   A CA  1 
ATOM   4518  C C   . GLN   A 1 640  ? 144.283 112.856 152.790 1.00 44.25  0  604  GLN   A C   1 
ATOM   4519  O O   . GLN   A 1 640  ? 143.664 111.973 153.383 1.00 44.72  0  604  GLN   A O   1 
ATOM   4520  C CB  . GLN   A 1 640  ? 144.807 111.151 151.017 1.00 37.04  0  604  GLN   A CB  1 
ATOM   4521  C CG  . GLN   A 1 640  ? 145.463 110.811 149.701 1.00 31.51  0  604  GLN   A CG  1 
ATOM   4522  C CD  . GLN   A 1 640  ? 145.221 109.376 149.305 1.00 45.39  0  604  GLN   A CD  1 
ATOM   4523  O OE1 . GLN   A 1 640  ? 144.207 109.054 148.691 1.00 48.49  0  604  GLN   A OE1 1 
ATOM   4524  N NE2 . GLN   A 1 640  ? 146.149 108.498 149.666 1.00 44.98  0  604  GLN   A NE2 1 
ATOM   4525  N N   . SER   A 1 641  ? 144.367 114.105 153.240 1.00 42.56  0  605  SER   A N   1 
ATOM   4526  C CA  . SER   A 1 641  ? 143.652 114.523 154.435 1.00 40.91  0  605  SER   A CA  1 
ATOM   4527  C C   . SER   A 1 641  ? 142.185 114.825 154.167 1.00 47.96  0  605  SER   A C   1 
ATOM   4528  O O   . SER   A 1 641  ? 141.428 115.024 155.122 1.00 48.33  0  605  SER   A O   1 
ATOM   4529  C CB  . SER   A 1 641  ? 144.326 115.749 155.049 1.00 40.93  0  605  SER   A CB  1 
ATOM   4530  O OG  . SER   A 1 641  ? 144.278 116.848 154.161 1.00 43.08  0  605  SER   A OG  1 
ATOM   4531  N N   . TYR   A 1 642  ? 141.768 114.863 152.903 1.00 42.05  0  606  TYR   A N   1 
ATOM   4532  C CA  . TYR   A 1 642  ? 140.371 115.086 152.558 1.00 37.20  0  606  TYR   A CA  1 
ATOM   4533  C C   . TYR   A 1 642  ? 139.538 113.811 152.570 1.00 36.13  0  606  TYR   A C   1 
ATOM   4534  O O   . TYR   A 1 642  ? 138.326 113.884 152.349 1.00 40.38  0  606  TYR   A O   1 
ATOM   4535  C CB  . TYR   A 1 642  ? 140.271 115.764 151.190 1.00 27.86  0  606  TYR   A CB  1 
ATOM   4536  C CG  . TYR   A 1 642  ? 141.107 115.133 150.097 1.00 37.86  0  606  TYR   A CG  1 
ATOM   4537  C CD1 . TYR   A 1 642  ? 142.000 115.895 149.361 1.00 42.00  0  606  TYR   A CD1 1 
ATOM   4538  C CD2 . TYR   A 1 642  ? 140.998 113.785 149.789 1.00 40.16  0  606  TYR   A CD2 1 
ATOM   4539  C CE1 . TYR   A 1 642  ? 142.761 115.335 148.359 1.00 33.63  0  606  TYR   A CE1 1 
ATOM   4540  C CE2 . TYR   A 1 642  ? 141.759 113.219 148.789 1.00 40.51  0  606  TYR   A CE2 1 
ATOM   4541  C CZ  . TYR   A 1 642  ? 142.637 113.999 148.079 1.00 29.98  0  606  TYR   A CZ  1 
ATOM   4542  O OH  . TYR   A 1 642  ? 143.397 113.441 147.082 1.00 34.45  0  606  TYR   A OH  1 
ATOM   4543  N N   . LEU   A 1 643  ? 140.149 112.658 152.815 1.00 38.37  0  607  LEU   A N   1 
ATOM   4544  C CA  . LEU   A 1 643  ? 139.442 111.388 152.862 1.00 37.44  0  607  LEU   A CA  1 
ATOM   4545  C C   . LEU   A 1 643  ? 138.998 111.094 154.287 1.00 40.72  0  607  LEU   A C   1 
ATOM   4546  O O   . LEU   A 1 643  ? 139.776 111.249 155.232 1.00 47.19  0  607  LEU   A O   1 
ATOM   4547  C CB  . LEU   A 1 643  ? 140.327 110.251 152.352 1.00 34.04  0  607  LEU   A CB  1 
ATOM   4548  C CG  . LEU   A 1 643  ? 140.730 110.283 150.879 1.00 37.36  0  607  LEU   A CG  1 
ATOM   4549  C CD1 . LEU   A 1 643  ? 141.435 108.994 150.509 1.00 37.75  0  607  LEU   A CD1 1 
ATOM   4550  C CD2 . LEU   A 1 643  ? 139.526 110.505 149.992 1.00 38.66  0  607  LEU   A CD2 1 
ATOM   4551  N N   . ASN   A 1 644  ? 137.743 110.665 154.432 1.00 38.68  0  608  ASN   A N   1 
ATOM   4552  C CA  . ASN   A 1 644  ? 137.173 110.315 155.733 1.00 40.84  0  608  ASN   A CA  1 
ATOM   4553  C C   . ASN   A 1 644  ? 137.256 111.488 156.705 1.00 45.95  0  608  ASN   A C   1 
ATOM   4554  O O   . ASN   A 1 644  ? 137.564 111.320 157.886 1.00 47.94  0  608  ASN   A O   1 
ATOM   4555  C CB  . ASN   A 1 644  ? 137.854 109.078 156.318 1.00 46.16  0  608  ASN   A CB  1 
ATOM   4556  C CG  . ASN   A 1 644  ? 137.913 107.934 155.335 1.00 53.31  0  608  ASN   A CG  1 
ATOM   4557  O OD1 . ASN   A 1 644  ? 137.261 107.965 154.293 1.00 57.66  0  608  ASN   A OD1 1 
ATOM   4558  N ND2 . ASN   A 1 644  ? 138.701 106.916 155.657 1.00 55.46  0  608  ASN   A ND2 1 
ATOM   4559  N N   . ASN   A 1 645  ? 136.988 112.687 156.198 1.00 45.62  0  609  ASN   A N   1 
ATOM   4560  C CA  . ASN   A 1 645  ? 137.116 113.898 156.994 1.00 41.57  0  609  ASN   A CA  1 
ATOM   4561  C C   . ASN   A 1 645  ? 135.782 114.232 157.644 1.00 41.63  0  609  ASN   A C   1 
ATOM   4562  O O   . ASN   A 1 645  ? 134.773 114.338 156.935 1.00 43.18  0  609  ASN   A O   1 
ATOM   4563  C CB  . ASN   A 1 645  ? 137.582 115.055 156.133 1.00 34.65  0  609  ASN   A CB  1 
ATOM   4564  C CG  . ASN   A 1 645  ? 138.675 115.853 156.794 1.00 43.14  0  609  ASN   A CG  1 
ATOM   4565  O OD1 . ASN   A 1 645  ? 139.277 115.406 157.766 1.00 47.59  0  609  ASN   A OD1 1 
ATOM   4566  N ND2 . ASN   A 1 645  ? 138.946 117.033 156.269 1.00 41.05  0  609  ASN   A ND2 1 
ATOM   4567  N N   . PRO   A 1 646  ? 135.724 114.402 158.967 1.00 41.03  0  610  PRO   A N   1 
ATOM   4568  C CA  . PRO   A 1 646  ? 134.431 114.633 159.624 1.00 40.34  0  610  PRO   A CA  1 
ATOM   4569  C C   . PRO   A 1 646  ? 133.776 115.949 159.257 1.00 46.09  0  610  PRO   A C   1 
ATOM   4570  O O   . PRO   A 1 646  ? 132.566 116.089 159.466 1.00 55.87  0  610  PRO   A O   1 
ATOM   4571  C CB  . PRO   A 1 646  ? 134.788 114.599 161.113 1.00 38.75  0  610  PRO   A CB  1 
ATOM   4572  C CG  . PRO   A 1 646  ? 136.203 115.044 161.153 1.00 43.82  0  610  PRO   A CG  1 
ATOM   4573  C CD  . PRO   A 1 646  ? 136.846 114.486 159.915 1.00 45.67  0  610  PRO   A CD  1 
ATOM   4574  N N   . ASN   A 1 647  ? 134.517 116.914 158.721 1.00 31.79  0  611  ASN   A N   1 
ATOM   4575  C CA  . ASN   A 1 647  ? 133.988 118.245 158.471 1.00 29.07  0  611  ASN   A CA  1 
ATOM   4576  C C   . ASN   A 1 647  ? 133.430 118.412 157.067 1.00 27.68  0  611  ASN   A C   1 
ATOM   4577  O O   . ASN   A 1 647  ? 132.975 119.504 156.722 1.00 35.51  0  611  ASN   A O   1 
ATOM   4578  C CB  . ASN   A 1 647  ? 135.068 119.295 158.726 1.00 32.23  0  611  ASN   A CB  1 
ATOM   4579  C CG  . ASN   A 1 647  ? 135.329 119.510 160.197 1.00 35.79  0  611  ASN   A CG  1 
ATOM   4580  O OD1 . ASN   A 1 647  ? 134.430 119.879 160.949 1.00 32.68  0  611  ASN   A OD1 1 
ATOM   4581  N ND2 . ASN   A 1 647  ? 136.564 119.272 160.620 1.00 38.68  0  611  ASN   A ND2 1 
ATOM   4582  N N   . HIS   A 1 648  ? 133.451 117.368 156.249 1.00 23.96  0  612  HIS   A N   1 
ATOM   4583  C CA  . HIS   A 1 648  ? 132.981 117.495 154.878 1.00 24.26  0  612  HIS   A CA  1 
ATOM   4584  C C   . HIS   A 1 648  ? 131.462 117.556 154.846 1.00 21.08  0  612  HIS   A C   1 
ATOM   4585  O O   . HIS   A 1 648  ? 130.784 116.771 155.514 1.00 35.62  0  612  HIS   A O   1 
ATOM   4586  C CB  . HIS   A 1 648  ? 133.481 116.336 154.021 1.00 34.72  0  612  HIS   A CB  1 
ATOM   4587  C CG  . HIS   A 1 648  ? 133.413 116.605 152.550 1.00 29.58  0  612  HIS   A CG  1 
ATOM   4588  N ND1 . HIS   A 1 648  ? 133.835 115.697 151.606 1.00 26.37  0  612  HIS   A ND1 1 
ATOM   4589  C CD2 . HIS   A 1 648  ? 132.969 117.683 151.863 1.00 23.65  0  612  HIS   A CD2 1 
ATOM   4590  C CE1 . HIS   A 1 648  ? 133.656 116.203 150.400 1.00 29.38  0  612  HIS   A CE1 1 
ATOM   4591  N NE2 . HIS   A 1 648  ? 133.131 117.408 150.528 1.00 28.64  0  612  HIS   A NE2 1 
ATOM   4592  N N   . VAL   A 1 649  ? 130.933 118.491 154.063 1.00 19.31  0  613  VAL   A N   1 
ATOM   4593  C CA  . VAL   A 1 649  ? 129.497 118.628 153.874 1.00 21.59  0  613  VAL   A CA  1 
ATOM   4594  C C   . VAL   A 1 649  ? 129.268 119.299 152.530 1.00 26.45  0  613  VAL   A C   1 
ATOM   4595  O O   . VAL   A 1 649  ? 130.143 119.992 152.009 1.00 46.14  0  613  VAL   A O   1 
ATOM   4596  C CB  . VAL   A 1 649  ? 128.841 119.427 155.022 1.00 29.03  0  613  VAL   A CB  1 
ATOM   4597  C CG1 . VAL   A 1 649  ? 128.907 120.919 154.749 1.00 25.33  0  613  VAL   A CG1 1 
ATOM   4598  C CG2 . VAL   A 1 649  ? 127.415 118.984 155.214 1.00 33.98  0  613  VAL   A CG2 1 
ATOM   4599  N N   . VAL   A 1 650  ? 128.097 119.067 151.952 1.00 12.14  0  614  VAL   A N   1 
ATOM   4600  C CA  . VAL   A 1 650  ? 127.718 119.692 150.695 1.00 13.90  0  614  VAL   A CA  1 
ATOM   4601  C C   . VAL   A 1 650  ? 126.462 120.512 150.930 1.00 9.74   0  614  VAL   A C   1 
ATOM   4602  O O   . VAL   A 1 650  ? 125.476 120.017 151.488 1.00 30.92  0  614  VAL   A O   1 
ATOM   4603  C CB  . VAL   A 1 650  ? 127.501 118.662 149.572 1.00 19.81  0  614  VAL   A CB  1 
ATOM   4604  C CG1 . VAL   A 1 650  ? 127.234 119.370 148.256 1.00 17.15  0  614  VAL   A CG1 1 
ATOM   4605  C CG2 . VAL   A 1 650  ? 128.710 117.766 149.449 1.00 17.45  0  614  VAL   A CG2 1 
ATOM   4606  N N   . SER   A 1 651  ? 126.511 121.770 150.510 1.00 16.94  0  615  SER   A N   1 
ATOM   4607  C CA  . SER   A 1 651  ? 125.456 122.742 150.744 1.00 17.36  0  615  SER   A CA  1 
ATOM   4608  C C   . SER   A 1 651  ? 124.919 123.200 149.400 1.00 18.37  0  615  SER   A C   1 
ATOM   4609  O O   . SER   A 1 651  ? 125.686 123.669 148.554 1.00 40.88  0  615  SER   A O   1 
ATOM   4610  C CB  . SER   A 1 651  ? 125.993 123.929 151.540 1.00 18.36  0  615  SER   A CB  1 
ATOM   4611  O OG  . SER   A 1 651  ? 126.582 123.501 152.753 1.00 27.02  0  615  SER   A OG  1 
ATOM   4612  N N   . LEU   A 1 652  ? 123.613 123.073 149.208 1.00 17.56  0  616  LEU   A N   1 
ATOM   4613  C CA  . LEU   A 1 652  ? 122.977 123.470 147.960 1.00 21.92  0  616  LEU   A CA  1 
ATOM   4614  C C   . LEU   A 1 652  ? 122.254 124.795 148.152 1.00 28.94  0  616  LEU   A C   1 
ATOM   4615  O O   . LEU   A 1 652  ? 121.413 124.924 149.045 1.00 39.89  0  616  LEU   A O   1 
ATOM   4616  C CB  . LEU   A 1 652  ? 121.993 122.399 147.487 1.00 26.96  0  616  LEU   A CB  1 
ATOM   4617  C CG  . LEU   A 1 652  ? 122.478 121.227 146.626 1.00 31.22  0  616  LEU   A CG  1 
ATOM   4618  C CD1 . LEU   A 1 652  ? 122.846 121.692 145.233 1.00 31.57  0  616  LEU   A CD1 1 
ATOM   4619  C CD2 . LEU   A 1 652  ? 123.642 120.498 147.273 1.00 30.17  0  616  LEU   A CD2 1 
ATOM   4620  N N   . THR   A 1 653  ? 122.585 125.778 147.319 1.00 29.01  0  617  THR   A N   1 
ATOM   4621  C CA  . THR   A 1 653  ? 121.942 127.083 147.333 1.00 31.38  0  617  THR   A CA  1 
ATOM   4622  C C   . THR   A 1 653  ? 121.629 127.463 145.891 1.00 40.39  0  617  THR   A C   1 
ATOM   4623  O O   . THR   A 1 653  ? 121.842 126.678 144.961 1.00 47.15  0  617  THR   A O   1 
ATOM   4624  C CB  . THR   A 1 653  ? 122.829 128.137 148.011 1.00 33.99  0  617  THR   A CB  1 
ATOM   4625  O OG1 . THR   A 1 653  ? 124.010 128.342 147.228 1.00 29.43  0  617  THR   A OG1 1 
ATOM   4626  C CG2 . THR   A 1 653  ? 123.224 127.702 149.415 1.00 33.36  0  617  THR   A CG2 1 
ATOM   4627  N N   . GLY   A 1 654  ? 121.136 128.682 145.701 1.00 39.73  0  618  GLY   A N   1 
ATOM   4628  C CA  . GLY   A 1 654  ? 120.791 129.167 144.377 1.00 43.09  0  618  GLY   A CA  1 
ATOM   4629  C C   . GLY   A 1 654  ? 121.989 129.436 143.486 1.00 43.15  0  618  GLY   A C   1 
ATOM   4630  O O   . GLY   A 1 654  ? 122.442 130.574 143.359 1.00 41.02  0  618  GLY   A O   1 
ATOM   4631  N N   . MET   A 1 664  ? 121.442 124.487 140.166 1.00 46.86  0  628  MET   A N   1 
ATOM   4632  C CA  . MET   A 1 664  ? 121.765 124.553 141.586 1.00 43.00  0  628  MET   A CA  1 
ATOM   4633  C C   . MET   A 1 664  ? 123.245 124.830 141.801 1.00 40.90  0  628  MET   A C   1 
ATOM   4634  O O   . MET   A 1 664  ? 124.088 124.369 141.035 1.00 46.37  0  628  MET   A O   1 
ATOM   4635  C CB  . MET   A 1 664  ? 121.369 123.254 142.286 1.00 44.93  0  628  MET   A CB  1 
ATOM   4636  C CG  . MET   A 1 664  ? 119.946 123.258 142.798 1.00 48.58  0  628  MET   A CG  1 
ATOM   4637  S SD  . MET   A 1 664  ? 119.821 124.026 144.421 1.00 60.18  0  628  MET   A SD  1 
ATOM   4638  C CE  . MET   A 1 664  ? 118.096 124.487 144.428 1.00 44.17  0  628  MET   A CE  1 
ATOM   4639  N N   . PHE   A 1 665  ? 123.557 125.586 142.848 1.00 33.75  0  629  PHE   A N   1 
ATOM   4640  C CA  . PHE   A 1 665  ? 124.930 125.961 143.170 1.00 34.46  0  629  PHE   A CA  1 
ATOM   4641  C C   . PHE   A 1 665  ? 125.320 125.244 144.454 1.00 37.63  0  629  PHE   A C   1 
ATOM   4642  O O   . PHE   A 1 665  ? 124.804 125.556 145.527 1.00 47.48  0  629  PHE   A O   1 
ATOM   4643  C CB  . PHE   A 1 665  ? 125.058 127.473 143.312 1.00 33.43  0  629  PHE   A CB  1 
ATOM   4644  C CG  . PHE   A 1 665  ? 126.412 127.928 143.766 1.00 38.94  0  629  PHE   A CG  1 
ATOM   4645  C CD1 . PHE   A 1 665  ? 127.454 128.048 142.864 1.00 37.73  0  629  PHE   A CD1 1 
ATOM   4646  C CD2 . PHE   A 1 665  ? 126.644 128.239 145.095 1.00 36.90  0  629  PHE   A CD2 1 
ATOM   4647  C CE1 . PHE   A 1 665  ? 128.702 128.467 143.279 1.00 38.74  0  629  PHE   A CE1 1 
ATOM   4648  C CE2 . PHE   A 1 665  ? 127.890 128.658 145.514 1.00 38.98  0  629  PHE   A CE2 1 
ATOM   4649  C CZ  . PHE   A 1 665  ? 128.919 128.772 144.605 1.00 40.83  0  629  PHE   A CZ  1 
ATOM   4650  N N   . ALA   A 1 666  ? 126.235 124.290 144.352 1.00 25.19  0  630  ALA   A N   1 
ATOM   4651  C CA  . ALA   A 1 666  ? 126.667 123.528 145.511 1.00 20.93  0  630  ALA   A CA  1 
ATOM   4652  C C   . ALA   A 1 666  ? 128.041 123.995 145.970 1.00 24.14  0  630  ALA   A C   1 
ATOM   4653  O O   . ALA   A 1 666  ? 128.851 124.473 145.174 1.00 34.16  0  630  ALA   A O   1 
ATOM   4654  C CB  . ALA   A 1 666  ? 126.700 122.033 145.202 1.00 18.91  0  630  ALA   A CB  1 
ATOM   4655  N N   . MET   A 1 667  ? 128.290 123.858 147.268 1.00 13.61  0  631  MET   A N   1 
ATOM   4656  C CA  . MET   A 1 667  ? 129.563 124.284 147.830 1.00 18.44  0  631  MET   A CA  1 
ATOM   4657  C C   . MET   A 1 667  ? 129.927 123.377 148.995 1.00 12.66  0  631  MET   A C   1 
ATOM   4658  O O   . MET   A 1 667  ? 129.087 122.648 149.522 1.00 30.33  0  631  MET   A O   1 
ATOM   4659  C CB  . MET   A 1 667  ? 129.520 125.750 148.265 1.00 24.23  0  631  MET   A CB  1 
ATOM   4660  C CG  . MET   A 1 667  ? 128.241 126.166 148.955 1.00 24.97  0  631  MET   A CG  1 
ATOM   4661  S SD  . MET   A 1 667  ? 128.075 127.956 149.038 1.00 41.54  0  631  MET   A SD  1 
ATOM   4662  C CE  . MET   A 1 667  ? 126.836 128.118 150.317 1.00 26.50  0  631  MET   A CE  1 
ATOM   4663  N N   . GLN   A 1 668  ? 131.196 123.417 149.374 1.00 10.22  0  632  GLN   A N   1 
ATOM   4664  C CA  . GLN   A 1 668  ? 131.748 122.555 150.405 1.00 9.80   0  632  GLN   A CA  1 
ATOM   4665  C C   . GLN   A 1 668  ? 132.737 123.352 151.239 1.00 21.81  0  632  GLN   A C   1 
ATOM   4666  O O   . GLN   A 1 668  ? 133.287 124.354 150.770 1.00 33.20  0  632  GLN   A O   1 
ATOM   4667  C CB  . GLN   A 1 668  ? 132.424 121.324 149.789 1.00 16.61  0  632  GLN   A CB  1 
ATOM   4668  C CG  . GLN   A 1 668  ? 133.262 121.626 148.582 1.00 28.12  0  632  GLN   A CG  1 
ATOM   4669  C CD  . GLN   A 1 668  ? 133.846 120.381 147.987 1.00 18.88  0  632  GLN   A CD  1 
ATOM   4670  O OE1 . GLN   A 1 668  ? 133.701 119.294 148.540 1.00 24.74  0  632  GLN   A OE1 1 
ATOM   4671  N NE2 . GLN   A 1 668  ? 134.514 120.524 146.854 1.00 19.07  0  632  GLN   A NE2 1 
ATOM   4672  N N   . PRO   A 1 669  ? 132.988 122.932 152.486 1.00 15.91  0  633  PRO   A N   1 
ATOM   4673  C CA  . PRO   A 1 669  ? 133.663 123.807 153.452 1.00 27.96  0  633  PRO   A CA  1 
ATOM   4674  C C   . PRO   A 1 669  ? 135.170 123.862 153.263 1.00 29.17  0  633  PRO   A C   1 
ATOM   4675  O O   . PRO   A 1 669  ? 135.886 122.903 153.564 1.00 30.62  0  633  PRO   A O   1 
ATOM   4676  C CB  . PRO   A 1 669  ? 133.286 123.178 154.799 1.00 27.56  0  633  PRO   A CB  1 
ATOM   4677  C CG  . PRO   A 1 669  ? 133.148 121.756 154.494 1.00 20.84  0  633  PRO   A CG  1 
ATOM   4678  C CD  . PRO   A 1 669  ? 132.561 121.674 153.117 1.00 22.85  0  633  PRO   A CD  1 
ATOM   4679  N N   . GLY   A 1 670  ? 135.659 125.004 152.795 1.00 30.15  0  634  GLY   A N   1 
ATOM   4680  C CA  . GLY   A 1 670  ? 137.074 125.300 152.894 1.00 25.05  0  634  GLY   A CA  1 
ATOM   4681  C C   . GLY   A 1 670  ? 137.998 124.460 152.043 1.00 22.72  0  634  GLY   A C   1 
ATOM   4682  O O   . GLY   A 1 670  ? 138.060 124.637 150.824 1.00 26.13  0  634  GLY   A O   1 
ATOM   4683  N N   . MET   A 1 671  ? 138.740 123.552 152.684 1.00 19.60  0  635  MET   A N   1 
ATOM   4684  C CA  . MET   A 1 671  ? 139.797 122.835 151.979 1.00 30.54  0  635  MET   A CA  1 
ATOM   4685  C C   . MET   A 1 671  ? 139.236 121.910 150.907 1.00 33.95  0  635  MET   A C   1 
ATOM   4686  O O   . MET   A 1 671  ? 139.817 121.784 149.824 1.00 40.62  0  635  MET   A O   1 
ATOM   4687  C CB  . MET   A 1 671  ? 140.676 122.074 152.971 1.00 34.63  0  635  MET   A CB  1 
ATOM   4688  C CG  . MET   A 1 671  ? 140.338 120.623 153.189 1.00 29.14  0  635  MET   A CG  1 
ATOM   4689  S SD  . MET   A 1 671  ? 141.509 119.906 154.348 1.00 49.68  0  635  MET   A SD  1 
ATOM   4690  C CE  . MET   A 1 671  ? 140.465 119.687 155.776 1.00 38.85  0  635  MET   A CE  1 
ATOM   4691  N N   . PHE   A 1 672  ? 138.094 121.275 151.166 1.00 30.03  0  636  PHE   A N   1 
ATOM   4692  C CA  . PHE   A 1 672  ? 137.489 120.459 150.124 1.00 22.87  0  636  PHE   A CA  1 
ATOM   4693  C C   . PHE   A 1 672  ? 137.168 121.281 148.889 1.00 21.93  0  636  PHE   A C   1 
ATOM   4694  O O   . PHE   A 1 672  ? 137.025 120.717 147.801 1.00 36.13  0  636  PHE   A O   1 
ATOM   4695  C CB  . PHE   A 1 672  ? 136.231 119.774 150.646 1.00 26.60  0  636  PHE   A CB  1 
ATOM   4696  C CG  . PHE   A 1 672  ? 136.385 119.205 152.018 1.00 29.15  0  636  PHE   A CG  1 
ATOM   4697  C CD1 . PHE   A 1 672  ? 136.954 117.966 152.204 1.00 29.32  0  636  PHE   A CD1 1 
ATOM   4698  C CD2 . PHE   A 1 672  ? 135.968 119.914 153.121 1.00 31.57  0  636  PHE   A CD2 1 
ATOM   4699  C CE1 . PHE   A 1 672  ? 137.097 117.445 153.466 1.00 28.49  0  636  PHE   A CE1 1 
ATOM   4700  C CE2 . PHE   A 1 672  ? 136.111 119.398 154.380 1.00 29.68  0  636  PHE   A CE2 1 
ATOM   4701  C CZ  . PHE   A 1 672  ? 136.675 118.162 154.552 1.00 24.89  0  636  PHE   A CZ  1 
ATOM   4702  N N   . ARG   A 1 673  ? 137.048 122.599 149.031 1.00 8.84   0  637  ARG   A N   1 
ATOM   4703  C CA  . ARG   A 1 673  ? 136.907 123.451 147.861 1.00 12.71  0  637  ARG   A CA  1 
ATOM   4704  C C   . ARG   A 1 673  ? 138.218 123.585 147.099 1.00 28.40  0  637  ARG   A C   1 
ATOM   4705  O O   . ARG   A 1 673  ? 138.239 123.422 145.874 1.00 36.42  0  637  ARG   A O   1 
ATOM   4706  C CB  . ARG   A 1 673  ? 136.394 124.827 148.269 1.00 23.87  0  637  ARG   A CB  1 
ATOM   4707  C CG  . ARG   A 1 673  ? 136.333 125.805 147.121 1.00 25.71  0  637  ARG   A CG  1 
ATOM   4708  C CD  . ARG   A 1 673  ? 135.876 127.168 147.579 1.00 27.92  0  637  ARG   A CD  1 
ATOM   4709  N NE  . ARG   A 1 673  ? 136.076 128.169 146.541 1.00 25.37  0  637  ARG   A NE  1 
ATOM   4710  C CZ  . ARG   A 1 673  ? 137.201 128.845 146.364 1.00 25.84  0  637  ARG   A CZ  1 
ATOM   4711  N NH1 . ARG   A 1 673  ? 138.248 128.662 147.151 1.00 20.86  1  637  ARG   A NH1 1 
ATOM   4712  N NH2 . ARG   A 1 673  ? 137.278 129.727 145.373 1.00 28.90  0  637  ARG   A NH2 1 
ATOM   4713  N N   . GLN   A 1 674  ? 139.324 123.865 147.798 1.00 33.65  0  638  GLN   A N   1 
ATOM   4714  C CA  . GLN   A 1 674  ? 140.573 124.133 147.087 1.00 27.38  0  638  GLN   A CA  1 
ATOM   4715  C C   . GLN   A 1 674  ? 141.057 122.893 146.349 1.00 32.61  0  638  GLN   A C   1 
ATOM   4716  O O   . GLN   A 1 674  ? 141.494 122.983 145.195 1.00 32.66  0  638  GLN   A O   1 
ATOM   4717  C CB  . GLN   A 1 674  ? 141.642 124.661 148.048 1.00 21.53  0  638  GLN   A CB  1 
ATOM   4718  C CG  . GLN   A 1 674  ? 141.892 123.803 149.265 1.00 19.10  0  638  GLN   A CG  1 
ATOM   4719  C CD  . GLN   A 1 674  ? 142.943 124.374 150.189 1.00 34.12  0  638  GLN   A CD  1 
ATOM   4720  O OE1 . GLN   A 1 674  ? 143.160 125.583 150.229 1.00 40.26  0  638  GLN   A OE1 1 
ATOM   4721  N NE2 . GLN   A 1 674  ? 143.591 123.505 150.954 1.00 29.61  0  638  GLN   A NE2 1 
ATOM   4722  N N   . VAL   A 1 675  ? 140.950 121.723 146.983 1.00 37.66  0  639  VAL   A N   1 
ATOM   4723  C CA  . VAL   A 1 675  ? 141.211 120.469 146.283 1.00 27.57  0  639  VAL   A CA  1 
ATOM   4724  C C   . VAL   A 1 675  ? 140.328 120.369 145.048 1.00 20.36  0  639  VAL   A C   1 
ATOM   4725  O O   . VAL   A 1 675  ? 140.801 120.054 143.950 1.00 31.74  0  639  VAL   A O   1 
ATOM   4726  C CB  . VAL   A 1 675  ? 140.996 119.273 147.224 1.00 21.35  0  639  VAL   A CB  1 
ATOM   4727  C CG1 . VAL   A 1 675  ? 141.192 117.975 146.472 1.00 19.92  0  639  VAL   A CG1 1 
ATOM   4728  C CG2 . VAL   A 1 675  ? 141.937 119.356 148.407 1.00 26.79  0  639  VAL   A CG2 1 
ATOM   4729  N N   . GLN   A 1 676  ? 139.039 120.686 145.202 1.00 13.32  0  640  GLN   A N   1 
ATOM   4730  C CA  . GLN   A 1 676  ? 138.128 120.671 144.064 1.00 14.00  0  640  GLN   A CA  1 
ATOM   4731  C C   . GLN   A 1 676  ? 138.653 121.523 142.923 1.00 22.55  0  640  GLN   A C   1 
ATOM   4732  O O   . GLN   A 1 676  ? 138.439 121.191 141.753 1.00 31.99  0  640  GLN   A O   1 
ATOM   4733  C CB  . GLN   A 1 676  ? 136.742 121.160 144.483 1.00 24.61  0  640  GLN   A CB  1 
ATOM   4734  C CG  . GLN   A 1 676  ? 135.694 121.066 143.383 1.00 28.41  0  640  GLN   A CG  1 
ATOM   4735  C CD  . GLN   A 1 676  ? 135.618 122.309 142.522 1.00 27.29  0  640  GLN   A CD  1 
ATOM   4736  O OE1 . GLN   A 1 676  ? 135.797 123.424 143.004 1.00 25.59  0  640  GLN   A OE1 1 
ATOM   4737  N NE2 . GLN   A 1 676  ? 135.371 122.120 141.234 1.00 23.73  0  640  GLN   A NE2 1 
ATOM   4738  N N   . ILE   A 1 677  ? 139.334 122.621 143.235 1.00 20.00  0  641  ILE   A N   1 
ATOM   4739  C CA  . ILE   A 1 677  ? 139.937 123.429 142.185 1.00 27.41  0  641  ILE   A CA  1 
ATOM   4740  C C   . ILE   A 1 677  ? 141.258 122.832 141.732 1.00 30.56  0  641  ILE   A C   1 
ATOM   4741  O O   . ILE   A 1 677  ? 141.511 122.724 140.528 1.00 29.68  0  641  ILE   A O   1 
ATOM   4742  C CB  . ILE   A 1 677  ? 140.111 124.883 142.658 1.00 27.69  0  641  ILE   A CB  1 
ATOM   4743  C CG1 . ILE   A 1 677  ? 138.856 125.360 143.384 1.00 24.18  0  641  ILE   A CG1 1 
ATOM   4744  C CG2 . ILE   A 1 677  ? 140.401 125.782 141.474 1.00 26.19  0  641  ILE   A CG2 1 
ATOM   4745  C CD1 . ILE   A 1 677  ? 139.001 126.714 144.012 1.00 24.93  0  641  ILE   A CD1 1 
ATOM   4746  N N   . LEU   A 1 678  ? 142.089 122.401 142.685 1.00 36.31  0  642  LEU   A N   1 
ATOM   4747  C CA  . LEU   A 1 678  ? 143.435 121.951 142.344 1.00 28.77  0  642  LEU   A CA  1 
ATOM   4748  C C   . LEU   A 1 678  ? 143.390 120.837 141.313 1.00 30.50  0  642  LEU   A C   1 
ATOM   4749  O O   . LEU   A 1 678  ? 144.007 120.942 140.247 1.00 36.07  0  642  LEU   A O   1 
ATOM   4750  C CB  . LEU   A 1 678  ? 144.173 121.488 143.597 1.00 16.84  0  642  LEU   A CB  1 
ATOM   4751  C CG  . LEU   A 1 678  ? 145.541 120.884 143.294 1.00 23.98  0  642  LEU   A CG  1 
ATOM   4752  C CD1 . LEU   A 1 678  ? 146.417 121.902 142.588 1.00 30.73  0  642  LEU   A CD1 1 
ATOM   4753  C CD2 . LEU   A 1 678  ? 146.201 120.397 144.559 1.00 23.93  0  642  LEU   A CD2 1 
ATOM   4754  N N   . ALA   A 1 679  ? 142.618 119.785 141.593 1.00 22.75  0  643  ALA   A N   1 
ATOM   4755  C CA  . ALA   A 1 679  ? 142.449 118.714 140.621 1.00 18.07  0  643  ALA   A CA  1 
ATOM   4756  C C   . ALA   A 1 679  ? 142.009 119.281 139.284 1.00 28.99  0  643  ALA   A C   1 
ATOM   4757  O O   . ALA   A 1 679  ? 142.665 119.061 138.258 1.00 46.00  0  643  ALA   A O   1 
ATOM   4758  C CB  . ALA   A 1 679  ? 141.437 117.693 141.135 1.00 13.46  0  643  ALA   A CB  1 
ATOM   4759  N N   . GLU   A 1 680  ? 140.945 120.087 139.293 1.00 20.74  0  644  GLU   A N   1 
ATOM   4760  C CA  . GLU   A 1 680  ? 140.486 120.709 138.059 1.00 25.34  0  644  GLU   A CA  1 
ATOM   4761  C C   . GLU   A 1 680  ? 141.625 121.454 137.389 1.00 32.28  0  644  GLU   A C   1 
ATOM   4762  O O   . GLU   A 1 680  ? 141.893 121.263 136.196 1.00 45.22  0  644  GLU   A O   1 
ATOM   4763  C CB  . GLU   A 1 680  ? 139.320 121.653 138.349 1.00 31.39  0  644  GLU   A CB  1 
ATOM   4764  C CG  . GLU   A 1 680  ? 137.968 120.971 138.406 1.00 48.17  0  644  GLU   A CG  1 
ATOM   4765  C CD  . GLU   A 1 680  ? 137.372 120.750 137.033 1.00 50.96  0  644  GLU   A CD  1 
ATOM   4766  O OE1 . GLU   A 1 680  ? 136.712 121.676 136.516 1.00 52.63  0  644  GLU   A OE1 1 
ATOM   4767  O OE2 . GLU   A 1 680  ? 137.564 119.653 136.470 1.00 42.71  -1 644  GLU   A OE2 1 
ATOM   4768  N N   . LYS   A 1 681  ? 142.359 122.251 138.172 1.00 30.06  0  645  LYS   A N   1 
ATOM   4769  C CA  . LYS   A 1 681  ? 143.459 123.030 137.617 1.00 34.29  0  645  LYS   A CA  1 
ATOM   4770  C C   . LYS   A 1 681  ? 144.419 122.136 136.850 1.00 31.90  0  645  LYS   A C   1 
ATOM   4771  O O   . LYS   A 1 681  ? 144.782 122.435 135.708 1.00 29.50  0  645  LYS   A O   1 
ATOM   4772  C CB  . LYS   A 1 681  ? 144.191 123.776 138.731 1.00 33.51  0  645  LYS   A CB  1 
ATOM   4773  C CG  . LYS   A 1 681  ? 145.403 124.563 138.260 1.00 27.06  0  645  LYS   A CG  1 
ATOM   4774  C CD  . LYS   A 1 681  ? 146.127 125.200 139.432 1.00 35.46  0  645  LYS   A CD  1 
ATOM   4775  C CE  . LYS   A 1 681  ? 147.450 125.821 139.020 1.00 38.79  0  645  LYS   A CE  1 
ATOM   4776  N NZ  . LYS   A 1 681  ? 147.273 126.938 138.052 1.00 37.21  1  645  LYS   A NZ  1 
ATOM   4777  N N   . MET   A 1 682  ? 144.794 121.000 137.442 1.00 30.36  0  646  MET   A N   1 
ATOM   4778  C CA  . MET   A 1 682  ? 145.757 120.128 136.784 1.00 28.16  0  646  MET   A CA  1 
ATOM   4779  C C   . MET   A 1 682  ? 145.208 119.608 135.464 1.00 29.26  0  646  MET   A C   1 
ATOM   4780  O O   . MET   A 1 682  ? 145.909 119.619 134.444 1.00 33.86  0  646  MET   A O   1 
ATOM   4781  C CB  . MET   A 1 682  ? 146.139 118.983 137.714 1.00 20.12  0  646  MET   A CB  1 
ATOM   4782  C CG  . MET   A 1 682  ? 146.663 119.448 139.058 1.00 18.60  0  646  MET   A CG  1 
ATOM   4783  S SD  . MET   A 1 682  ? 148.440 119.731 139.065 1.00 43.43  0  646  MET   A SD  1 
ATOM   4784  C CE  . MET   A 1 682  ? 148.525 121.461 138.612 1.00 34.94  0  646  MET   A CE  1 
ATOM   4785  N N   . ILE   A 1 683  ? 143.936 119.206 135.448 1.00 28.88  0  647  ILE   A N   1 
ATOM   4786  C CA  . ILE   A 1 683  ? 143.342 118.726 134.206 1.00 29.51  0  647  ILE   A CA  1 
ATOM   4787  C C   . ILE   A 1 683  ? 143.358 119.826 133.158 1.00 25.45  0  647  ILE   A C   1 
ATOM   4788  O O   . ILE   A 1 683  ? 143.468 119.554 131.957 1.00 30.96  0  647  ILE   A O   1 
ATOM   4789  C CB  . ILE   A 1 683  ? 141.919 118.196 134.469 1.00 27.94  0  647  ILE   A CB  1 
ATOM   4790  C CG1 . ILE   A 1 683  ? 141.976 116.939 135.325 1.00 20.91  0  647  ILE   A CG1 1 
ATOM   4791  C CG2 . ILE   A 1 683  ? 141.217 117.866 133.184 1.00 28.42  0  647  ILE   A CG2 1 
ATOM   4792  C CD1 . ILE   A 1 683  ? 140.633 116.486 135.821 1.00 32.74  0  647  ILE   A CD1 1 
ATOM   4793  N N   . ALA   A 1 684  ? 143.287 121.083 133.589 1.00 15.69  0  648  ALA   A N   1 
ATOM   4794  C CA  . ALA   A 1 684  ? 143.294 122.188 132.647 1.00 22.55  0  648  ALA   A CA  1 
ATOM   4795  C C   . ALA   A 1 684  ? 144.658 122.412 132.009 1.00 36.36  0  648  ALA   A C   1 
ATOM   4796  O O   . ALA   A 1 684  ? 144.725 122.980 130.914 1.00 41.70  0  648  ALA   A O   1 
ATOM   4797  C CB  . ALA   A 1 684  ? 142.829 123.468 133.340 1.00 30.95  0  648  ALA   A CB  1 
ATOM   4798  N N   . GLU   A 1 685  ? 145.742 121.982 132.653 1.00 35.35  0  649  GLU   A N   1 
ATOM   4799  C CA  . GLU   A 1 685  ? 147.076 122.196 132.102 1.00 26.50  0  649  GLU   A CA  1 
ATOM   4800  C C   . GLU   A 1 685  ? 147.642 120.958 131.428 1.00 36.09  0  649  GLU   A C   1 
ATOM   4801  O O   . GLU   A 1 685  ? 148.060 121.014 130.269 1.00 38.96  0  649  GLU   A O   1 
ATOM   4802  C CB  . GLU   A 1 685  ? 148.049 122.641 133.196 1.00 24.25  0  649  GLU   A CB  1 
ATOM   4803  C CG  . GLU   A 1 685  ? 147.410 123.266 134.395 1.00 29.83  0  649  GLU   A CG  1 
ATOM   4804  C CD  . GLU   A 1 685  ? 148.436 123.741 135.388 1.00 45.61  0  649  GLU   A CD  1 
ATOM   4805  O OE1 . GLU   A 1 685  ? 148.042 124.240 136.457 1.00 46.04  0  649  GLU   A OE1 1 
ATOM   4806  O OE2 . GLU   A 1 685  ? 149.642 123.600 135.104 1.00 49.19  -1 649  GLU   A OE2 1 
ATOM   4807  N N   . ASN   A 1 686  ? 147.659 119.836 132.141 1.00 38.18  0  650  ASN   A N   1 
ATOM   4808  C CA  . ASN   A 1 686  ? 148.438 118.680 131.740 1.00 30.79  0  650  ASN   A CA  1 
ATOM   4809  C C   . ASN   A 1 686  ? 147.666 117.665 130.911 1.00 36.43  0  650  ASN   A C   1 
ATOM   4810  O O   . ASN   A 1 686  ? 148.298 116.825 130.263 1.00 44.81  0  650  ASN   A O   1 
ATOM   4811  C CB  . ASN   A 1 686  ? 148.998 117.986 132.984 1.00 33.60  0  650  ASN   A CB  1 
ATOM   4812  C CG  . ASN   A 1 686  ? 149.793 118.925 133.861 1.00 35.46  0  650  ASN   A CG  1 
ATOM   4813  O OD1 . ASN   A 1 686  ? 150.450 119.838 133.371 1.00 42.83  0  650  ASN   A OD1 1 
ATOM   4814  N ND2 . ASN   A 1 686  ? 149.737 118.708 135.164 1.00 36.74  0  650  ASN   A ND2 1 
ATOM   4815  N N   . ILE   A 1 687  ? 146.336 117.704 130.910 1.00 26.81  0  651  ILE   A N   1 
ATOM   4816  C CA  . ILE   A 1 687  ? 145.555 116.651 130.274 1.00 20.78  0  651  ILE   A CA  1 
ATOM   4817  C C   . ILE   A 1 687  ? 144.658 117.150 129.148 1.00 19.18  0  651  ILE   A C   1 
ATOM   4818  O O   . ILE   A 1 687  ? 144.371 116.377 128.222 1.00 31.63  0  651  ILE   A O   1 
ATOM   4819  C CB  . ILE   A 1 687  ? 144.720 115.876 131.313 1.00 23.35  0  651  ILE   A CB  1 
ATOM   4820  C CG1 . ILE   A 1 687  ? 145.575 115.513 132.525 1.00 28.89  0  651  ILE   A CG1 1 
ATOM   4821  C CG2 . ILE   A 1 687  ? 144.173 114.605 130.713 1.00 28.27  0  651  ILE   A CG2 1 
ATOM   4822  C CD1 . ILE   A 1 687  ? 146.733 114.606 132.203 1.00 22.68  0  651  ILE   A CD1 1 
ATOM   4823  N N   . LEU   A 1 688  ? 144.204 118.403 129.157 1.00 17.55  0  652  LEU   A N   1 
ATOM   4824  C CA  . LEU   A 1 688  ? 143.407 118.868 128.028 1.00 26.65  0  652  LEU   A CA  1 
ATOM   4825  C C   . LEU   A 1 688  ? 144.211 119.016 126.746 1.00 39.27  0  652  LEU   A C   1 
ATOM   4826  O O   . LEU   A 1 688  ? 143.608 119.145 125.676 1.00 36.56  0  652  LEU   A O   1 
ATOM   4827  C CB  . LEU   A 1 688  ? 142.721 120.196 128.345 1.00 27.50  0  652  LEU   A CB  1 
ATOM   4828  C CG  . LEU   A 1 688  ? 141.239 120.128 128.715 1.00 30.39  0  652  LEU   A CG  1 
ATOM   4829  C CD1 . LEU   A 1 688  ? 141.006 119.340 129.981 1.00 28.38  0  652  LEU   A CD1 1 
ATOM   4830  C CD2 . LEU   A 1 688  ? 140.677 121.531 128.845 1.00 34.54  0  652  LEU   A CD2 1 
ATOM   4831  N N   . GLN   A 1 689  ? 145.543 119.011 126.817 1.00 47.26  0  653  GLN   A N   1 
ATOM   4832  C CA  . GLN   A 1 689  ? 146.330 119.038 125.590 1.00 36.87  0  653  GLN   A CA  1 
ATOM   4833  C C   . GLN   A 1 689  ? 146.139 117.761 124.785 1.00 27.75  0  653  GLN   A C   1 
ATOM   4834  O O   . GLN   A 1 689  ? 146.244 117.782 123.554 1.00 42.47  0  653  GLN   A O   1 
ATOM   4835  C CB  . GLN   A 1 689  ? 147.807 119.256 125.914 1.00 31.32  0  653  GLN   A CB  1 
ATOM   4836  C CG  . GLN   A 1 689  ? 148.443 118.128 126.704 1.00 32.10  0  653  GLN   A CG  1 
ATOM   4837  C CD  . GLN   A 1 689  ? 149.646 118.575 127.499 1.00 35.01  0  653  GLN   A CD  1 
ATOM   4838  O OE1 . GLN   A 1 689  ? 149.568 118.767 128.708 1.00 35.33  0  653  GLN   A OE1 1 
ATOM   4839  N NE2 . GLN   A 1 689  ? 150.771 118.744 126.822 1.00 36.91  0  653  GLN   A NE2 1 
ATOM   4840  N N   . PHE   A 1 690  ? 145.850 116.647 125.458 1.00 16.00  0  654  PHE   A N   1 
ATOM   4841  C CA  . PHE   A 1 690  ? 145.584 115.381 124.793 1.00 27.89  0  654  PHE   A CA  1 
ATOM   4842  C C   . PHE   A 1 690  ? 144.172 115.288 124.233 1.00 29.38  0  654  PHE   A C   1 
ATOM   4843  O O   . PHE   A 1 690  ? 143.890 114.364 123.464 1.00 22.93  0  654  PHE   A O   1 
ATOM   4844  C CB  . PHE   A 1 690  ? 145.821 114.223 125.762 1.00 24.72  0  654  PHE   A CB  1 
ATOM   4845  C CG  . PHE   A 1 690  ? 147.107 114.323 126.528 1.00 22.14  0  654  PHE   A CG  1 
ATOM   4846  C CD1 . PHE   A 1 690  ? 148.278 114.690 125.898 1.00 29.56  0  654  PHE   A CD1 1 
ATOM   4847  C CD2 . PHE   A 1 690  ? 147.146 114.036 127.877 1.00 25.86  0  654  PHE   A CD2 1 
ATOM   4848  C CE1 . PHE   A 1 690  ? 149.458 114.774 126.600 1.00 29.39  0  654  PHE   A CE1 1 
ATOM   4849  C CE2 . PHE   A 1 690  ? 148.323 114.120 128.582 1.00 28.98  0  654  PHE   A CE2 1 
ATOM   4850  C CZ  . PHE   A 1 690  ? 149.478 114.491 127.943 1.00 28.93  0  654  PHE   A CZ  1 
ATOM   4851  N N   . PHE   A 1 691  ? 143.288 116.217 124.593 1.00 31.69  0  655  PHE   A N   1 
ATOM   4852  C CA  . PHE   A 1 691  ? 141.890 116.214 124.161 1.00 32.99  0  655  PHE   A CA  1 
ATOM   4853  C C   . PHE   A 1 691  ? 141.576 117.574 123.555 1.00 31.53  0  655  PHE   A C   1 
ATOM   4854  O O   . PHE   A 1 691  ? 140.905 118.407 124.174 1.00 33.83  0  655  PHE   A O   1 
ATOM   4855  C CB  . PHE   A 1 691  ? 140.950 115.903 125.326 1.00 23.77  0  655  PHE   A CB  1 
ATOM   4856  C CG  . PHE   A 1 691  ? 141.200 114.570 125.972 1.00 21.87  0  655  PHE   A CG  1 
ATOM   4857  C CD1 . PHE   A 1 691  ? 142.251 114.394 126.850 1.00 17.66  0  655  PHE   A CD1 1 
ATOM   4858  C CD2 . PHE   A 1 691  ? 140.378 113.496 125.706 1.00 28.63  0  655  PHE   A CD2 1 
ATOM   4859  C CE1 . PHE   A 1 691  ? 142.480 113.175 127.441 1.00 18.47  0  655  PHE   A CE1 1 
ATOM   4860  C CE2 . PHE   A 1 691  ? 140.603 112.275 126.298 1.00 26.13  0  655  PHE   A CE2 1 
ATOM   4861  C CZ  . PHE   A 1 691  ? 141.658 112.115 127.164 1.00 23.64  0  655  PHE   A CZ  1 
ATOM   4862  N N   . PRO   A 1 692  ? 142.051 117.832 122.335 1.00 38.54  0  656  PRO   A N   1 
ATOM   4863  C CA  . PRO   A 1 692  ? 141.922 119.181 121.763 1.00 43.22  0  656  PRO   A CA  1 
ATOM   4864  C C   . PRO   A 1 692  ? 140.493 119.599 121.475 1.00 40.65  0  656  PRO   A C   1 
ATOM   4865  O O   . PRO   A 1 692  ? 140.246 120.792 121.264 1.00 36.88  0  656  PRO   A O   1 
ATOM   4866  C CB  . PRO   A 1 692  ? 142.742 119.090 120.470 1.00 43.95  0  656  PRO   A CB  1 
ATOM   4867  C CG  . PRO   A 1 692  ? 142.691 117.648 120.105 1.00 40.98  0  656  PRO   A CG  1 
ATOM   4868  C CD  . PRO   A 1 692  ? 142.694 116.893 121.402 1.00 37.70  0  656  PRO   A CD  1 
ATOM   4869  N N   . GLU   A 1 693  ? 139.552 118.664 121.453 1.00 42.43  0  657  GLU   A N   1 
ATOM   4870  C CA  . GLU   A 1 693  ? 138.170 118.934 121.090 1.00 45.19  0  657  GLU   A CA  1 
ATOM   4871  C C   . GLU   A 1 693  ? 137.284 119.211 122.298 1.00 46.77  0  657  GLU   A C   1 
ATOM   4872  O O   . GLU   A 1 693  ? 136.060 119.265 122.156 1.00 50.39  0  657  GLU   A O   1 
ATOM   4873  C CB  . GLU   A 1 693  ? 137.626 117.760 120.278 1.00 46.04  0  657  GLU   A CB  1 
ATOM   4874  C CG  . GLU   A 1 693  ? 138.043 116.413 120.842 1.00 45.06  0  657  GLU   A CG  1 
ATOM   4875  C CD  . GLU   A 1 693  ? 138.129 115.336 119.784 1.00 47.09  0  657  GLU   A CD  1 
ATOM   4876  O OE1 . GLU   A 1 693  ? 137.783 115.616 118.619 1.00 52.58  0  657  GLU   A OE1 1 
ATOM   4877  O OE2 . GLU   A 1 693  ? 138.563 114.214 120.116 1.00 46.99  -1 657  GLU   A OE2 1 
ATOM   4878  N N   . SER   A 1 694  ? 137.875 119.395 123.478 1.00 41.10  0  658  SER   A N   1 
ATOM   4879  C CA  . SER   A 1 694  ? 137.138 119.662 124.705 1.00 42.50  0  658  SER   A CA  1 
ATOM   4880  C C   . SER   A 1 694  ? 136.969 121.149 124.980 1.00 38.99  0  658  SER   A C   1 
ATOM   4881  O O   . SER   A 1 694  ? 136.581 121.524 126.092 1.00 44.05  0  658  SER   A O   1 
ATOM   4882  C CB  . SER   A 1 694  ? 137.832 118.996 125.893 1.00 44.82  0  658  SER   A CB  1 
ATOM   4883  O OG  . SER   A 1 694  ? 139.012 119.697 126.239 1.00 44.58  0  658  SER   A OG  1 
ATOM   4884  N N   . LEU   A 1 695  ? 137.263 122.001 124.005 1.00 46.48  0  659  LEU   A N   1 
ATOM   4885  C CA  . LEU   A 1 695  ? 137.144 123.442 124.190 1.00 53.68  0  659  LEU   A CA  1 
ATOM   4886  C C   . LEU   A 1 695  ? 136.105 124.031 123.245 1.00 51.73  0  659  LEU   A C   1 
ATOM   4887  O O   . LEU   A 1 695  ? 135.086 124.561 123.684 1.00 50.54  0  659  LEU   A O   1 
ATOM   4888  C CB  . LEU   A 1 695  ? 138.499 124.122 123.978 1.00 54.04  0  659  LEU   A CB  1 
ATOM   4889  C CG  . LEU   A 1 695  ? 139.591 123.810 125.006 1.00 55.93  0  659  LEU   A CG  1 
ATOM   4890  C CD1 . LEU   A 1 695  ? 140.943 124.298 124.519 1.00 52.67  0  659  LEU   A CD1 1 
ATOM   4891  C CD2 . LEU   A 1 695  ? 139.255 124.430 126.352 1.00 48.63  0  659  LEU   A CD2 1 
ATOM   4892  N N   . ASN   A 1 725  ? 126.797 105.209 94.688  1.00 89.89  0  689  ASN   A N   1 
ATOM   4893  C CA  . ASN   A 1 725  ? 127.829 104.256 95.077  1.00 92.98  0  689  ASN   A CA  1 
ATOM   4894  C C   . ASN   A 1 725  ? 129.037 104.980 95.662  1.00 90.65  0  689  ASN   A C   1 
ATOM   4895  O O   . ASN   A 1 725  ? 129.387 106.073 95.217  1.00 85.42  0  689  ASN   A O   1 
ATOM   4896  C CB  . ASN   A 1 725  ? 128.246 103.400 93.878  1.00 93.07  0  689  ASN   A CB  1 
ATOM   4897  C CG  . ASN   A 1 725  ? 129.247 102.321 94.248  1.00 91.42  0  689  ASN   A CG  1 
ATOM   4898  O OD1 . ASN   A 1 725  ? 129.341 101.913 95.406  1.00 91.26  0  689  ASN   A OD1 1 
ATOM   4899  N ND2 . ASN   A 1 725  ? 129.997 101.847 93.260  1.00 87.96  0  689  ASN   A ND2 1 
ATOM   4900  N N   . ASN   A 1 726  ? 129.664 104.357 96.661  1.00 87.05  0  690  ASN   A N   1 
ATOM   4901  C CA  . ASN   A 1 726  ? 130.820 104.926 97.352  1.00 86.66  0  690  ASN   A CA  1 
ATOM   4902  C C   . ASN   A 1 726  ? 130.512 106.332 97.863  1.00 87.42  0  690  ASN   A C   1 
ATOM   4903  O O   . ASN   A 1 726  ? 131.288 107.274 97.686  1.00 85.08  0  690  ASN   A O   1 
ATOM   4904  C CB  . ASN   A 1 726  ? 132.055 104.923 96.449  1.00 87.70  0  690  ASN   A CB  1 
ATOM   4905  C CG  . ASN   A 1 726  ? 132.370 103.545 95.894  1.00 90.38  0  690  ASN   A CG  1 
ATOM   4906  O OD1 . ASN   A 1 726  ? 132.031 102.527 96.498  1.00 90.48  0  690  ASN   A OD1 1 
ATOM   4907  N ND2 . ASN   A 1 726  ? 133.029 103.508 94.742  1.00 88.16  0  690  ASN   A ND2 1 
ATOM   4908  N N   . TYR   A 1 727  ? 129.355 106.465 98.506  1.00 78.54  0  691  TYR   A N   1 
ATOM   4909  C CA  . TYR   A 1 727  ? 128.849 107.757 98.946  1.00 73.64  0  691  TYR   A CA  1 
ATOM   4910  C C   . TYR   A 1 727  ? 129.165 107.988 100.417 1.00 71.04  0  691  TYR   A C   1 
ATOM   4911  O O   . TYR   A 1 727  ? 128.997 107.094 101.250 1.00 67.53  0  691  TYR   A O   1 
ATOM   4912  C CB  . TYR   A 1 727  ? 127.340 107.835 98.710  1.00 74.22  0  691  TYR   A CB  1 
ATOM   4913  C CG  . TYR   A 1 727  ? 126.637 108.996 99.378  1.00 73.14  0  691  TYR   A CG  1 
ATOM   4914  C CD1 . TYR   A 1 727  ? 126.737 110.283 98.867  1.00 71.37  0  691  TYR   A CD1 1 
ATOM   4915  C CD2 . TYR   A 1 727  ? 125.853 108.799 100.506 1.00 73.51  0  691  TYR   A CD2 1 
ATOM   4916  C CE1 . TYR   A 1 727  ? 126.087 111.342 99.471  1.00 70.69  0  691  TYR   A CE1 1 
ATOM   4917  C CE2 . TYR   A 1 727  ? 125.200 109.851 101.116 1.00 73.20  0  691  TYR   A CE2 1 
ATOM   4918  C CZ  . TYR   A 1 727  ? 125.319 111.119 100.595 1.00 71.78  0  691  TYR   A CZ  1 
ATOM   4919  O OH  . TYR   A 1 727  ? 124.671 112.167 101.204 1.00 70.48  0  691  TYR   A OH  1 
ATOM   4920  N N   . ILE   A 1 728  ? 129.636 109.190 100.729 1.00 70.59  0  692  ILE   A N   1 
ATOM   4921  C CA  . ILE   A 1 728  ? 129.897 109.600 102.103 1.00 69.74  0  692  ILE   A CA  1 
ATOM   4922  C C   . ILE   A 1 728  ? 128.582 110.125 102.674 1.00 70.54  0  692  ILE   A C   1 
ATOM   4923  O O   . ILE   A 1 728  ? 127.894 110.937 102.046 1.00 73.00  0  692  ILE   A O   1 
ATOM   4924  C CB  . ILE   A 1 728  ? 131.039 110.630 102.182 1.00 70.43  0  692  ILE   A CB  1 
ATOM   4925  C CG1 . ILE   A 1 728  ? 131.901 110.382 103.421 1.00 71.64  0  692  ILE   A CG1 1 
ATOM   4926  C CG2 . ILE   A 1 728  ? 130.544 112.072 102.158 1.00 64.62  0  692  ILE   A CG2 1 
ATOM   4927  C CD1 . ILE   A 1 728  ? 132.664 109.085 103.385 1.00 66.67  0  692  ILE   A CD1 1 
ATOM   4928  N N   . SER   A 1 729  ? 128.191 109.611 103.835 1.00 65.80  0  693  SER   A N   1 
ATOM   4929  C CA  . SER   A 1 729  ? 126.956 110.003 104.497 1.00 62.88  0  693  SER   A CA  1 
ATOM   4930  C C   . SER   A 1 729  ? 127.302 110.631 105.836 1.00 63.42  0  693  SER   A C   1 
ATOM   4931  O O   . SER   A 1 729  ? 128.076 110.061 106.609 1.00 67.52  0  693  SER   A O   1 
ATOM   4932  C CB  . SER   A 1 729  ? 126.033 108.800 104.694 1.00 65.21  0  693  SER   A CB  1 
ATOM   4933  O OG  . SER   A 1 729  ? 126.677 107.789 105.447 1.00 64.73  0  693  SER   A OG  1 
ATOM   4934  N N   . LYS   A 1 730  ? 126.734 111.801 106.104 1.00 57.49  0  694  LYS   A N   1 
ATOM   4935  C CA  . LYS   A 1 730  ? 127.087 112.575 107.282 1.00 57.91  0  694  LYS   A CA  1 
ATOM   4936  C C   . LYS   A 1 730  ? 125.833 112.971 108.042 1.00 60.83  0  694  LYS   A C   1 
ATOM   4937  O O   . LYS   A 1 730  ? 124.830 113.369 107.445 1.00 68.82  0  694  LYS   A O   1 
ATOM   4938  C CB  . LYS   A 1 730  ? 127.888 113.821 106.894 1.00 58.67  0  694  LYS   A CB  1 
ATOM   4939  C CG  . LYS   A 1 730  ? 129.227 113.495 106.257 1.00 61.36  0  694  LYS   A CG  1 
ATOM   4940  C CD  . LYS   A 1 730  ? 130.028 114.740 105.934 1.00 62.03  0  694  LYS   A CD  1 
ATOM   4941  C CE  . LYS   A 1 730  ? 131.366 114.370 105.314 1.00 63.08  0  694  LYS   A CE  1 
ATOM   4942  N NZ  . LYS   A 1 730  ? 132.146 115.567 104.900 1.00 65.30  1  694  LYS   A NZ  1 
ATOM   4943  N N   . CYS   A 1 731  ? 125.902 112.856 109.365 1.00 57.10  0  695  CYS   A N   1 
ATOM   4944  C CA  . CYS   A 1 731  ? 124.835 113.290 110.251 1.00 56.26  0  695  CYS   A CA  1 
ATOM   4945  C C   . CYS   A 1 731  ? 125.462 114.000 111.440 1.00 56.00  0  695  CYS   A C   1 
ATOM   4946  O O   . CYS   A 1 731  ? 126.685 114.024 111.601 1.00 61.05  0  695  CYS   A O   1 
ATOM   4947  C CB  . CYS   A 1 731  ? 123.971 112.111 110.707 1.00 59.50  0  695  CYS   A CB  1 
ATOM   4948  S SG  . CYS   A 1 731  ? 124.700 111.143 112.039 1.00 66.91  0  695  CYS   A SG  1 
ATOM   4949  N N   . SER   A 1 732  ? 124.618 114.577 112.289 1.00 50.93  0  696  SER   A N   1 
ATOM   4950  C CA  . SER   A 1 732  ? 125.066 115.245 113.498 1.00 54.58  0  696  SER   A CA  1 
ATOM   4951  C C   . SER   A 1 732  ? 124.082 114.935 114.609 1.00 52.66  0  696  SER   A C   1 
ATOM   4952  O O   . SER   A 1 732  ? 122.875 114.870 114.376 1.00 55.14  0  696  SER   A O   1 
ATOM   4953  C CB  . SER   A 1 732  ? 125.174 116.757 113.297 1.00 56.86  0  696  SER   A CB  1 
ATOM   4954  O OG  . SER   A 1 732  ? 125.362 117.419 114.533 1.00 56.22  0  696  SER   A OG  1 
ATOM   4955  N N   . ILE   A 1 733  ? 124.603 114.731 115.811 1.00 48.11  0  697  ILE   A N   1 
ATOM   4956  C CA  . ILE   A 1 733  ? 123.793 114.378 116.967 1.00 49.06  0  697  ILE   A CA  1 
ATOM   4957  C C   . ILE   A 1 733  ? 124.148 115.331 118.095 1.00 50.60  0  697  ILE   A C   1 
ATOM   4958  O O   . ILE   A 1 733  ? 125.311 115.402 118.508 1.00 55.79  0  697  ILE   A O   1 
ATOM   4959  C CB  . ILE   A 1 733  ? 124.012 112.918 117.392 1.00 54.36  0  697  ILE   A CB  1 
ATOM   4960  C CG1 . ILE   A 1 733  ? 123.717 111.987 116.217 1.00 53.83  0  697  ILE   A CG1 1 
ATOM   4961  C CG2 . ILE   A 1 733  ? 123.146 112.568 118.588 1.00 49.48  0  697  ILE   A CG2 1 
ATOM   4962  C CD1 . ILE   A 1 733  ? 123.920 110.538 116.519 1.00 51.52  0  697  ILE   A CD1 1 
ATOM   4963  N N   . ILE   A 1 734  ? 123.157 116.065 118.588 1.00 50.64  0  698  ILE   A N   1 
ATOM   4964  C CA  . ILE   A 1 734  ? 123.346 117.023 119.670 1.00 50.84  0  698  ILE   A CA  1 
ATOM   4965  C C   . ILE   A 1 734  ? 122.759 116.426 120.938 1.00 51.43  0  698  ILE   A C   1 
ATOM   4966  O O   . ILE   A 1 734  ? 121.590 116.015 120.958 1.00 50.83  0  698  ILE   A O   1 
ATOM   4967  C CB  . ILE   A 1 734  ? 122.708 118.383 119.346 1.00 51.02  0  698  ILE   A CB  1 
ATOM   4968  C CG1 . ILE   A 1 734  ? 123.399 119.022 118.142 1.00 52.90  0  698  ILE   A CG1 1 
ATOM   4969  C CG2 . ILE   A 1 734  ? 122.812 119.304 120.541 1.00 53.63  0  698  ILE   A CG2 1 
ATOM   4970  C CD1 . ILE   A 1 734  ? 122.685 118.797 116.827 1.00 54.38  0  698  ILE   A CD1 1 
ATOM   4971  N N   . THR   A 1 735  ? 123.573 116.375 121.990 1.00 54.51  0  699  THR   A N   1 
ATOM   4972  C CA  . THR   A 1 735  ? 123.214 115.732 123.245 1.00 56.17  0  699  THR   A CA  1 
ATOM   4973  C C   . THR   A 1 735  ? 123.352 116.726 124.388 1.00 57.99  0  699  THR   A C   1 
ATOM   4974  O O   . THR   A 1 735  ? 124.364 117.428 124.486 1.00 58.67  0  699  THR   A O   1 
ATOM   4975  C CB  . THR   A 1 735  ? 124.102 114.510 123.503 1.00 52.58  0  699  THR   A CB  1 
ATOM   4976  O OG1 . THR   A 1 735  ? 124.007 113.608 122.395 1.00 57.06  0  699  THR   A OG1 1 
ATOM   4977  C CG2 . THR   A 1 735  ? 123.676 113.791 124.770 1.00 54.18  0  699  THR   A CG2 1 
ATOM   4978  N N   . ASP   A 1 736  ? 122.339 116.783 125.248 1.00 57.59  0  700  ASP   A N   1 
ATOM   4979  C CA  . ASP   A 1 736  ? 122.368 117.631 126.437 1.00 53.42  0  700  ASP   A CA  1 
ATOM   4980  C C   . ASP   A 1 736  ? 123.120 116.841 127.501 1.00 58.75  0  700  ASP   A C   1 
ATOM   4981  O O   . ASP   A 1 736  ? 122.642 115.812 127.984 1.00 60.50  0  700  ASP   A O   1 
ATOM   4982  C CB  . ASP   A 1 736  ? 120.943 117.995 126.856 1.00 60.10  0  700  ASP   A CB  1 
ATOM   4983  C CG  . ASP   A 1 736  ? 120.810 118.417 128.327 1.00 63.08  0  700  ASP   A CG  1 
ATOM   4984  O OD1 . ASP   A 1 736  ? 121.806 118.506 129.074 1.00 63.56  0  700  ASP   A OD1 1 
ATOM   4985  O OD2 . ASP   A 1 736  ? 119.662 118.667 128.748 1.00 62.80  -1 700  ASP   A OD2 1 
ATOM   4986  N N   . LEU   A 1 737  ? 124.299 117.326 127.878 1.00 53.56  0  701  LEU   A N   1 
ATOM   4987  C CA  . LEU   A 1 737  ? 125.152 116.642 128.837 1.00 51.82  0  701  LEU   A CA  1 
ATOM   4988  C C   . LEU   A 1 737  ? 125.008 117.183 130.252 1.00 56.48  0  701  LEU   A C   1 
ATOM   4989  O O   . LEU   A 1 737  ? 125.820 116.841 131.117 1.00 56.76  0  701  LEU   A O   1 
ATOM   4990  C CB  . LEU   A 1 737  ? 126.617 116.732 128.408 1.00 48.84  0  701  LEU   A CB  1 
ATOM   4991  C CG  . LEU   A 1 737  ? 126.988 116.199 127.028 1.00 51.54  0  701  LEU   A CG  1 
ATOM   4992  C CD1 . LEU   A 1 737  ? 128.494 116.253 126.847 1.00 54.26  0  701  LEU   A CD1 1 
ATOM   4993  C CD2 . LEU   A 1 737  ? 126.463 114.791 126.852 1.00 53.25  0  701  LEU   A CD2 1 
ATOM   4994  N N   . SER   A 1 738  ? 123.997 118.009 130.513 1.00 55.61  0  702  SER   A N   1 
ATOM   4995  C CA  . SER   A 1 738  ? 123.838 118.617 131.829 1.00 50.52  0  702  SER   A CA  1 
ATOM   4996  C C   . SER   A 1 738  ? 123.422 117.589 132.873 1.00 47.76  0  702  SER   A C   1 
ATOM   4997  O O   . SER   A 1 738  ? 123.254 117.926 134.048 1.00 49.03  0  702  SER   A O   1 
ATOM   4998  C CB  . SER   A 1 738  ? 122.819 119.756 131.770 1.00 53.16  0  702  SER   A CB  1 
ATOM   4999  O OG  . SER   A 1 738  ? 121.606 119.326 131.178 1.00 48.84  0  702  SER   A OG  1 
ATOM   5000  N N   . LYS   A 1 739  ? 123.252 116.335 132.457 1.00 54.50  0  703  LYS   A N   1 
ATOM   5001  C CA  . LYS   A 1 739  ? 122.897 115.255 133.363 1.00 58.44  0  703  LYS   A CA  1 
ATOM   5002  C C   . LYS   A 1 739  ? 124.033 114.269 133.608 1.00 56.90  0  703  LYS   A C   1 
ATOM   5003  O O   . LYS   A 1 739  ? 123.796 113.214 134.207 1.00 51.39  0  703  LYS   A O   1 
ATOM   5004  C CB  . LYS   A 1 739  ? 121.668 114.507 132.830 1.00 59.76  0  703  LYS   A CB  1 
ATOM   5005  C CG  . LYS   A 1 739  ? 120.511 115.424 132.466 1.00 58.83  0  703  LYS   A CG  1 
ATOM   5006  C CD  . LYS   A 1 739  ? 120.142 116.331 133.628 1.00 58.52  0  703  LYS   A CD  1 
ATOM   5007  C CE  . LYS   A 1 739  ? 118.900 117.148 133.323 1.00 55.47  0  703  LYS   A CE  1 
ATOM   5008  N NZ  . LYS   A 1 739  ? 118.664 118.185 134.362 1.00 51.06  1  703  LYS   A NZ  1 
ATOM   5009  N N   . PHE   A 1 740  ? 125.255 114.579 133.166 1.00 53.39  0  704  PHE   A N   1 
ATOM   5010  C CA  . PHE   A 1 740  ? 126.397 113.716 133.455 1.00 52.22  0  704  PHE   A CA  1 
ATOM   5011  C C   . PHE   A 1 740  ? 126.651 113.567 134.946 1.00 49.05  0  704  PHE   A C   1 
ATOM   5012  O O   . PHE   A 1 740  ? 126.997 112.475 135.405 1.00 49.29  0  704  PHE   A O   1 
ATOM   5013  C CB  . PHE   A 1 740  ? 127.657 114.253 132.779 1.00 55.97  0  704  PHE   A CB  1 
ATOM   5014  C CG  . PHE   A 1 740  ? 127.891 113.715 131.401 1.00 54.56  0  704  PHE   A CG  1 
ATOM   5015  C CD1 . PHE   A 1 740  ? 126.930 112.961 130.756 1.00 51.90  0  704  PHE   A CD1 1 
ATOM   5016  C CD2 . PHE   A 1 740  ? 129.090 113.959 130.755 1.00 50.23  0  704  PHE   A CD2 1 
ATOM   5017  C CE1 . PHE   A 1 740  ? 127.164 112.464 129.494 1.00 51.45  0  704  PHE   A CE1 1 
ATOM   5018  C CE2 . PHE   A 1 740  ? 129.324 113.466 129.499 1.00 51.06  0  704  PHE   A CE2 1 
ATOM   5019  C CZ  . PHE   A 1 740  ? 128.362 112.716 128.866 1.00 55.32  0  704  PHE   A CZ  1 
ATOM   5020  N N   . ASN   A 1 741  ? 126.507 114.649 135.713 1.00 41.68  0  705  ASN   A N   1 
ATOM   5021  C CA  . ASN   A 1 741  ? 126.855 114.598 137.128 1.00 44.22  0  705  ASN   A CA  1 
ATOM   5022  C C   . ASN   A 1 741  ? 126.069 113.524 137.867 1.00 53.79  0  705  ASN   A C   1 
ATOM   5023  O O   . ASN   A 1 741  ? 126.603 112.877 138.773 1.00 53.75  0  705  ASN   A O   1 
ATOM   5024  C CB  . ASN   A 1 741  ? 126.631 115.965 137.772 1.00 47.50  0  705  ASN   A CB  1 
ATOM   5025  C CG  . ASN   A 1 741  ? 125.189 116.418 137.693 1.00 53.67  0  705  ASN   A CG  1 
ATOM   5026  O OD1 . ASN   A 1 741  ? 124.571 116.371 136.632 1.00 58.08  0  705  ASN   A OD1 1 
ATOM   5027  N ND2 . ASN   A 1 741  ? 124.646 116.862 138.820 1.00 48.03  0  705  ASN   A ND2 1 
ATOM   5028  N N   . GLN   A 1 742  ? 124.806 113.313 137.496 1.00 48.19  0  706  GLN   A N   1 
ATOM   5029  C CA  . GLN   A 1 742  ? 124.019 112.274 138.148 1.00 41.06  0  706  GLN   A CA  1 
ATOM   5030  C C   . GLN   A 1 742  ? 124.438 110.883 137.689 1.00 45.05  0  706  GLN   A C   1 
ATOM   5031  O O   . GLN   A 1 742  ? 124.502 109.952 138.498 1.00 45.45  0  706  GLN   A O   1 
ATOM   5032  C CB  . GLN   A 1 742  ? 122.527 112.487 137.881 1.00 52.87  0  706  GLN   A CB  1 
ATOM   5033  C CG  . GLN   A 1 742  ? 121.965 113.825 138.346 1.00 48.53  0  706  GLN   A CG  1 
ATOM   5034  C CD  . GLN   A 1 742  ? 121.633 114.749 137.197 1.00 50.27  0  706  GLN   A CD  1 
ATOM   5035  O OE1 . GLN   A 1 742  ? 121.428 114.304 136.070 1.00 52.23  0  706  GLN   A OE1 1 
ATOM   5036  N NE2 . GLN   A 1 742  ? 121.573 116.044 137.476 1.00 46.98  0  706  GLN   A NE2 1 
ATOM   5037  N N   . ALA   A 1 743  ? 124.732 110.730 136.398 1.00 42.49  0  707  ALA   A N   1 
ATOM   5038  C CA  . ALA   A 1 743  ? 124.937 109.403 135.828 1.00 40.98  0  707  ALA   A CA  1 
ATOM   5039  C C   . ALA   A 1 743  ? 126.249 108.784 136.294 1.00 43.65  0  707  ALA   A C   1 
ATOM   5040  O O   . ALA   A 1 743  ? 126.299 107.598 136.636 1.00 41.84  0  707  ALA   A O   1 
ATOM   5041  C CB  . ALA   A 1 743  ? 124.895 109.483 134.303 1.00 42.22  0  707  ALA   A CB  1 
ATOM   5042  N N   . PHE   A 1 744  ? 127.324 109.568 136.306 1.00 43.51  0  708  PHE   A N   1 
ATOM   5043  C CA  . PHE   A 1 744  ? 128.645 109.017 136.571 1.00 37.37  0  708  PHE   A CA  1 
ATOM   5044  C C   . PHE   A 1 744  ? 128.746 108.515 138.002 1.00 35.07  0  708  PHE   A C   1 
ATOM   5045  O O   . PHE   A 1 744  ? 128.416 109.231 138.948 1.00 44.32  0  708  PHE   A O   1 
ATOM   5046  C CB  . PHE   A 1 744  ? 129.715 110.075 136.312 1.00 32.61  0  708  PHE   A CB  1 
ATOM   5047  C CG  . PHE   A 1 744  ? 130.071 110.233 134.866 1.00 42.28  0  708  PHE   A CG  1 
ATOM   5048  C CD1 . PHE   A 1 744  ? 130.826 109.277 134.216 1.00 41.76  0  708  PHE   A CD1 1 
ATOM   5049  C CD2 . PHE   A 1 744  ? 129.646 111.336 134.153 1.00 42.86  0  708  PHE   A CD2 1 
ATOM   5050  C CE1 . PHE   A 1 744  ? 131.150 109.422 132.885 1.00 39.07  0  708  PHE   A CE1 1 
ATOM   5051  C CE2 . PHE   A 1 744  ? 129.970 111.483 132.823 1.00 39.40  0  708  PHE   A CE2 1 
ATOM   5052  C CZ  . PHE   A 1 744  ? 130.722 110.527 132.190 1.00 40.39  0  708  PHE   A CZ  1 
ATOM   5053  N N   . ARG   A 1 745  ? 129.209 107.283 138.158 1.00 29.92  0  709  ARG   A N   1 
ATOM   5054  C CA  . ARG   A 1 745  ? 129.524 106.719 139.459 1.00 32.85  0  709  ARG   A CA  1 
ATOM   5055  C C   . ARG   A 1 745  ? 131.033 106.569 139.571 1.00 31.37  0  709  ARG   A C   1 
ATOM   5056  O O   . ARG   A 1 745  ? 131.782 106.948 138.672 1.00 35.72  0  709  ARG   A O   1 
ATOM   5057  C CB  . ARG   A 1 745  ? 128.829 105.372 139.670 1.00 33.66  0  709  ARG   A CB  1 
ATOM   5058  C CG  . ARG   A 1 745  ? 127.323 105.436 139.577 1.00 39.68  0  709  ARG   A CG  1 
ATOM   5059  C CD  . ARG   A 1 745  ? 126.674 105.585 140.942 1.00 33.20  0  709  ARG   A CD  1 
ATOM   5060  N NE  . ARG   A 1 745  ? 125.221 105.625 140.841 1.00 32.46  0  709  ARG   A NE  1 
ATOM   5061  C CZ  . ARG   A 1 745  ? 124.531 106.603 140.270 1.00 33.38  0  709  ARG   A CZ  1 
ATOM   5062  N NH1 . ARG   A 1 745  ? 125.127 107.671 139.768 1.00 31.07  1  709  ARG   A NH1 1 
ATOM   5063  N NH2 . ARG   A 1 745  ? 123.208 106.508 140.203 1.00 39.97  0  709  ARG   A NH2 1 
ATOM   5064  N N   . TYR   A 1 746  ? 131.480 106.010 140.694 1.00 38.00  0  710  TYR   A N   1 
ATOM   5065  C CA  . TYR   A 1 746  ? 132.908 105.774 140.860 1.00 38.99  0  710  TYR   A CA  1 
ATOM   5066  C C   . TYR   A 1 746  ? 133.424 104.800 139.814 1.00 36.75  0  710  TYR   A C   1 
ATOM   5067  O O   . TYR   A 1 746  ? 134.497 105.007 139.242 1.00 40.76  0  710  TYR   A O   1 
ATOM   5068  C CB  . TYR   A 1 746  ? 133.206 105.245 142.261 1.00 39.73  0  710  TYR   A CB  1 
ATOM   5069  C CG  . TYR   A 1 746  ? 134.631 104.772 142.424 1.00 34.84  0  710  TYR   A CG  1 
ATOM   5070  C CD1 . TYR   A 1 746  ? 135.628 105.647 142.815 1.00 36.40  0  710  TYR   A CD1 1 
ATOM   5071  C CD2 . TYR   A 1 746  ? 134.980 103.454 142.176 1.00 31.82  0  710  TYR   A CD2 1 
ATOM   5072  C CE1 . TYR   A 1 746  ? 136.926 105.221 142.964 1.00 38.69  0  710  TYR   A CE1 1 
ATOM   5073  C CE2 . TYR   A 1 746  ? 136.274 103.024 142.313 1.00 35.04  0  710  TYR   A CE2 1 
ATOM   5074  C CZ  . TYR   A 1 746  ? 137.243 103.910 142.707 1.00 37.86  0  710  TYR   A CZ  1 
ATOM   5075  O OH  . TYR   A 1 746  ? 138.539 103.476 142.851 1.00 34.90  0  710  TYR   A OH  1 
ATOM   5076  N N   . GLU   A 1 747  ? 132.673 103.735 139.543 1.00 38.41  0  711  GLU   A N   1 
ATOM   5077  C CA  . GLU   A 1 747  ? 133.154 102.688 138.652 1.00 39.82  0  711  GLU   A CA  1 
ATOM   5078  C C   . GLU   A 1 747  ? 133.350 103.169 137.223 1.00 36.95  0  711  GLU   A C   1 
ATOM   5079  O O   . GLU   A 1 747  ? 134.010 102.475 136.445 1.00 46.26  0  711  GLU   A O   1 
ATOM   5080  C CB  . GLU   A 1 747  ? 132.190 101.503 138.677 1.00 43.05  0  711  GLU   A CB  1 
ATOM   5081  C CG  . GLU   A 1 747  ? 132.248 100.696 139.956 1.00 41.83  0  711  GLU   A CG  1 
ATOM   5082  C CD  . GLU   A 1 747  ? 131.493 101.356 141.085 1.00 43.91  0  711  GLU   A CD  1 
ATOM   5083  O OE1 . GLU   A 1 747  ? 130.698 102.273 140.808 1.00 44.61  0  711  GLU   A OE1 1 
ATOM   5084  O OE2 . GLU   A 1 747  ? 131.702 100.972 142.251 1.00 47.91  -1 711  GLU   A OE2 1 
ATOM   5085  N N   . THR   A 1 748  ? 132.802 104.322 136.854 1.00 24.65  0  712  THR   A N   1 
ATOM   5086  C CA  . THR   A 1 748  ? 133.026 104.891 135.532 1.00 28.83  0  712  THR   A CA  1 
ATOM   5087  C C   . THR   A 1 748  ? 134.051 106.013 135.521 1.00 37.28  0  712  THR   A C   1 
ATOM   5088  O O   . THR   A 1 748  ? 134.903 106.046 134.635 1.00 46.20  0  712  THR   A O   1 
ATOM   5089  C CB  . THR   A 1 748  ? 131.714 105.411 134.943 1.00 24.75  0  712  THR   A CB  1 
ATOM   5090  O OG1 . THR   A 1 748  ? 131.102 106.317 135.866 1.00 41.51  0  712  THR   A OG1 1 
ATOM   5091  C CG2 . THR   A 1 748  ? 130.772 104.266 134.676 1.00 30.57  0  712  THR   A CG2 1 
ATOM   5092  N N   . SER   A 1 749  ? 133.997 106.939 136.477 1.00 29.16  0  713  SER   A N   1 
ATOM   5093  C CA  . SER   A 1 749  ? 134.951 108.041 136.481 1.00 24.02  0  713  SER   A CA  1 
ATOM   5094  C C   . SER   A 1 749  ? 136.336 107.591 136.925 1.00 32.70  0  713  SER   A C   1 
ATOM   5095  O O   . SER   A 1 749  ? 137.345 108.085 136.408 1.00 44.07  0  713  SER   A O   1 
ATOM   5096  C CB  . SER   A 1 749  ? 134.448 109.167 137.381 1.00 33.29  0  713  SER   A CB  1 
ATOM   5097  O OG  . SER   A 1 749  ? 133.486 109.959 136.710 1.00 38.88  0  713  SER   A OG  1 
ATOM   5098  N N   . CYS   A 1 750  ? 136.403 106.656 137.875 1.00 42.97  0  714  CYS   A N   1 
ATOM   5099  C CA  . CYS   A 1 750  ? 137.678 106.236 138.437 1.00 44.21  0  714  CYS   A CA  1 
ATOM   5100  C C   . CYS   A 1 750  ? 138.578 105.570 137.413 1.00 44.67  0  714  CYS   A C   1 
ATOM   5101  O O   . CYS   A 1 750  ? 139.794 105.721 137.500 1.00 47.97  0  714  CYS   A O   1 
ATOM   5102  C CB  . CYS   A 1 750  ? 137.466 105.266 139.592 1.00 47.28  0  714  CYS   A CB  1 
ATOM   5103  S SG  . CYS   A 1 750  ? 137.221 103.559 139.049 1.00 72.05  0  714  CYS   A SG  1 
ATOM   5104  N N   . ILE   A 1 751  ? 138.017 104.847 136.445 1.00 34.18  0  715  ILE   A N   1 
ATOM   5105  C CA  . ILE   A 1 751  ? 138.851 104.121 135.499 1.00 33.75  0  715  ILE   A CA  1 
ATOM   5106  C C   . ILE   A 1 751  ? 139.709 105.058 134.658 1.00 40.29  0  715  ILE   A C   1 
ATOM   5107  O O   . ILE   A 1 751  ? 140.695 104.620 134.059 1.00 50.36  0  715  ILE   A O   1 
ATOM   5108  C CB  . ILE   A 1 751  ? 137.970 103.212 134.619 1.00 36.63  0  715  ILE   A CB  1 
ATOM   5109  C CG1 . ILE   A 1 751  ? 137.061 104.047 133.722 1.00 32.78  0  715  ILE   A CG1 1 
ATOM   5110  C CG2 . ILE   A 1 751  ? 137.144 102.283 135.489 1.00 31.34  0  715  ILE   A CG2 1 
ATOM   5111  C CD1 . ILE   A 1 751  ? 136.172 103.224 132.834 1.00 31.19  0  715  ILE   A CD1 1 
ATOM   5112  N N   . CYS   A 1 752  ? 139.373 106.345 134.607 1.00 33.07  0  716  CYS   A N   1 
ATOM   5113  C CA  . CYS   A 1 752  ? 140.192 107.345 133.932 1.00 35.35  0  716  CYS   A CA  1 
ATOM   5114  C C   . CYS   A 1 752  ? 140.875 108.303 134.902 1.00 36.92  0  716  CYS   A C   1 
ATOM   5115  O O   . CYS   A 1 752  ? 142.033 108.697 134.689 1.00 50.07  0  716  CYS   A O   1 
ATOM   5116  C CB  . CYS   A 1 752  ? 139.333 108.137 132.944 1.00 36.11  0  716  CYS   A CB  1 
ATOM   5117  S SG  . CYS   A 1 752  ? 138.270 107.103 131.915 1.00 38.88  0  716  CYS   A SG  1 
ATOM   5118  N N   . SER   A 1 753  ? 140.189 108.682 135.979 1.00 23.13  0  717  SER   A N   1 
ATOM   5119  C CA  . SER   A 1 753  ? 140.837 109.508 136.982 1.00 21.21  0  717  SER   A CA  1 
ATOM   5120  C C   . SER   A 1 753  ? 142.021 108.800 137.618 1.00 32.38  0  717  SER   A C   1 
ATOM   5121  O O   . SER   A 1 753  ? 142.962 109.467 138.045 1.00 47.17  0  717  SER   A O   1 
ATOM   5122  C CB  . SER   A 1 753  ? 139.836 109.918 138.052 1.00 32.20  0  717  SER   A CB  1 
ATOM   5123  O OG  . SER   A 1 753  ? 139.424 108.793 138.795 1.00 39.79  0  717  SER   A OG  1 
ATOM   5124  N N   . ASP   A 1 754  ? 142.013 107.469 137.680 1.00 30.65  0  718  ASP   A N   1 
ATOM   5125  C CA  . ASP   A 1 754  ? 143.160 106.746 138.209 1.00 27.20  0  718  ASP   A CA  1 
ATOM   5126  C C   . ASP   A 1 754  ? 144.360 106.859 137.285 1.00 36.20  0  718  ASP   A C   1 
ATOM   5127  O O   . ASP   A 1 754  ? 145.496 106.972 137.752 1.00 51.03  0  718  ASP   A O   1 
ATOM   5128  C CB  . ASP   A 1 754  ? 142.809 105.281 138.432 1.00 35.65  0  718  ASP   A CB  1 
ATOM   5129  C CG  . ASP   A 1 754  ? 144.016 104.453 138.782 1.00 39.99  0  718  ASP   A CG  1 
ATOM   5130  O OD1 . ASP   A 1 754  ? 144.575 104.661 139.878 1.00 45.89  0  718  ASP   A OD1 1 
ATOM   5131  O OD2 . ASP   A 1 754  ? 144.418 103.603 137.961 1.00 39.33  -1 718  ASP   A OD2 1 
ATOM   5132  N N   . VAL   A 1 755  ? 144.131 106.826 135.973 1.00 32.80  0  719  VAL   A N   1 
ATOM   5133  C CA  . VAL   A 1 755  ? 145.218 107.079 135.035 1.00 30.45  0  719  VAL   A CA  1 
ATOM   5134  C C   . VAL   A 1 755  ? 145.758 108.487 135.233 1.00 30.62  0  719  VAL   A C   1 
ATOM   5135  O O   . VAL   A 1 755  ? 146.971 108.717 135.169 1.00 26.69  0  719  VAL   A O   1 
ATOM   5136  C CB  . VAL   A 1 755  ? 144.741 106.851 133.590 1.00 28.85  0  719  VAL   A CB  1 
ATOM   5137  C CG1 . VAL   A 1 755  ? 145.796 107.298 132.604 1.00 32.16  0  719  VAL   A CG1 1 
ATOM   5138  C CG2 . VAL   A 1 755  ? 144.393 105.395 133.375 1.00 34.15  0  719  VAL   A CG2 1 
ATOM   5139  N N   . LEU   A 1 756  ? 144.868 109.450 135.483 1.00 37.63  0  720  LEU   A N   1 
ATOM   5140  C CA  . LEU   A 1 756  ? 145.326 110.819 135.731 1.00 29.37  0  720  LEU   A CA  1 
ATOM   5141  C C   . LEU   A 1 756  ? 146.168 110.913 137.004 1.00 30.58  0  720  LEU   A C   1 
ATOM   5142  O O   . LEU   A 1 756  ? 147.218 111.567 137.015 1.00 49.17  0  720  LEU   A O   1 
ATOM   5143  C CB  . LEU   A 1 756  ? 144.136 111.774 135.794 1.00 27.11  0  720  LEU   A CB  1 
ATOM   5144  C CG  . LEU   A 1 756  ? 143.430 111.967 134.454 1.00 31.63  0  720  LEU   A CG  1 
ATOM   5145  C CD1 . LEU   A 1 756  ? 142.574 113.216 134.458 1.00 34.42  0  720  LEU   A CD1 1 
ATOM   5146  C CD2 . LEU   A 1 756  ? 144.448 112.025 133.343 1.00 30.95  0  720  LEU   A CD2 1 
ATOM   5147  N N   . ASP   A 1 757  ? 145.727 110.266 138.087 1.00 30.44  0  721  ASP   A N   1 
ATOM   5148  C CA  . ASP   A 1 757  ? 146.526 110.237 139.312 1.00 27.94  0  721  ASP   A CA  1 
ATOM   5149  C C   . ASP   A 1 757  ? 147.873 109.572 139.077 1.00 37.32  0  721  ASP   A C   1 
ATOM   5150  O O   . ASP   A 1 757  ? 148.896 110.016 139.610 1.00 42.12  0  721  ASP   A O   1 
ATOM   5151  C CB  . ASP   A 1 757  ? 145.797 109.500 140.436 1.00 37.38  0  721  ASP   A CB  1 
ATOM   5152  C CG  . ASP   A 1 757  ? 144.346 109.870 140.542 1.00 48.01  0  721  ASP   A CG  1 
ATOM   5153  O OD1 . ASP   A 1 757  ? 143.968 110.932 140.020 1.00 53.99  0  721  ASP   A OD1 1 
ATOM   5154  O OD2 . ASP   A 1 757  ? 143.580 109.091 141.147 1.00 43.17  -1 721  ASP   A OD2 1 
ATOM   5155  N N   . GLU   A 1 758  ? 147.886 108.487 138.304 1.00 42.42  0  722  GLU   A N   1 
ATOM   5156  C CA  . GLU   A 1 758  ? 149.136 107.803 137.996 1.00 37.99  0  722  GLU   A CA  1 
ATOM   5157  C C   . GLU   A 1 758  ? 150.080 108.707 137.215 1.00 34.79  0  722  GLU   A C   1 
ATOM   5158  O O   . GLU   A 1 758  ? 151.286 108.730 137.481 1.00 41.40  0  722  GLU   A O   1 
ATOM   5159  C CB  . GLU   A 1 758  ? 148.842 106.522 137.217 1.00 34.34  0  722  GLU   A CB  1 
ATOM   5160  C CG  . GLU   A 1 758  ? 150.011 105.572 137.129 1.00 48.22  0  722  GLU   A CG  1 
ATOM   5161  C CD  . GLU   A 1 758  ? 150.197 104.758 138.389 1.00 48.78  0  722  GLU   A CD  1 
ATOM   5162  O OE1 . GLU   A 1 758  ? 149.182 104.387 139.011 1.00 46.31  0  722  GLU   A OE1 1 
ATOM   5163  O OE2 . GLU   A 1 758  ? 151.358 104.493 138.762 1.00 50.28  -1 722  GLU   A OE2 1 
ATOM   5164  N N   . LEU   A 1 759  ? 149.549 109.460 136.251 1.00 20.29  0  723  LEU   A N   1 
ATOM   5165  C CA  . LEU   A 1 759  ? 150.378 110.412 135.521 1.00 29.64  0  723  LEU   A CA  1 
ATOM   5166  C C   . LEU   A 1 759  ? 150.936 111.483 136.449 1.00 37.27  0  723  LEU   A C   1 
ATOM   5167  O O   . LEU   A 1 759  ? 152.113 111.847 136.348 1.00 47.77  0  723  LEU   A O   1 
ATOM   5168  C CB  . LEU   A 1 759  ? 149.581 111.053 134.387 1.00 29.78  0  723  LEU   A CB  1 
ATOM   5169  C CG  . LEU   A 1 759  ? 149.416 110.244 133.102 1.00 37.06  0  723  LEU   A CG  1 
ATOM   5170  C CD1 . LEU   A 1 759  ? 148.690 111.061 132.048 1.00 33.24  0  723  LEU   A CD1 1 
ATOM   5171  C CD2 . LEU   A 1 759  ? 150.764 109.782 132.586 1.00 37.40  0  723  LEU   A CD2 1 
ATOM   5172  N N   . HIS   A 1 760  ? 150.114 112.001 137.358 1.00 31.04  0  724  HIS   A N   1 
ATOM   5173  C CA  . HIS   A 1 760  ? 150.575 113.045 138.266 1.00 20.91  0  724  HIS   A CA  1 
ATOM   5174  C C   . HIS   A 1 760  ? 151.256 112.501 139.513 1.00 23.03  0  724  HIS   A C   1 
ATOM   5175  O O   . HIS   A 1 760  ? 151.789 113.290 140.298 1.00 29.52  0  724  HIS   A O   1 
ATOM   5176  C CB  . HIS   A 1 760  ? 149.409 113.943 138.673 1.00 18.64  0  724  HIS   A CB  1 
ATOM   5177  C CG  . HIS   A 1 760  ? 148.892 114.793 137.559 1.00 12.92  0  724  HIS   A CG  1 
ATOM   5178  N ND1 . HIS   A 1 760  ? 148.105 114.291 136.547 1.00 20.13  0  724  HIS   A ND1 1 
ATOM   5179  C CD2 . HIS   A 1 760  ? 149.052 116.108 137.293 1.00 18.32  0  724  HIS   A CD2 1 
ATOM   5180  C CE1 . HIS   A 1 760  ? 147.799 115.261 135.707 1.00 21.43  0  724  HIS   A CE1 1 
ATOM   5181  N NE2 . HIS   A 1 760  ? 148.362 116.374 136.137 1.00 23.50  0  724  HIS   A NE2 1 
ATOM   5182  N N   . GLY   A 1 761  ? 151.246 111.190 139.724 1.00 34.97  0  725  GLY   A N   1 
ATOM   5183  C CA  . GLY   A 1 761  ? 151.952 110.591 140.834 1.00 37.12  0  725  GLY   A CA  1 
ATOM   5184  C C   . GLY   A 1 761  ? 151.235 110.640 142.161 1.00 43.82  0  725  GLY   A C   1 
ATOM   5185  O O   . GLY   A 1 761  ? 151.746 110.085 143.140 1.00 47.71  0  725  GLY   A O   1 
ATOM   5186  N N   . VAL   A 1 762  ? 150.076 111.273 142.231 1.00 43.06  0  726  VAL   A N   1 
ATOM   5187  C CA  . VAL   A 1 762  ? 149.309 111.350 143.463 1.00 36.25  0  726  VAL   A CA  1 
ATOM   5188  C C   . VAL   A 1 762  ? 148.380 110.148 143.548 1.00 43.49  0  726  VAL   A C   1 
ATOM   5189  O O   . VAL   A 1 762  ? 148.143 109.443 142.567 1.00 53.45  0  726  VAL   A O   1 
ATOM   5190  C CB  . VAL   A 1 762  ? 148.516 112.666 143.549 1.00 37.64  0  726  VAL   A CB  1 
ATOM   5191  C CG1 . VAL   A 1 762  ? 149.449 113.821 143.804 1.00 43.02  0  726  VAL   A CG1 1 
ATOM   5192  C CG2 . VAL   A 1 762  ? 147.756 112.890 142.259 1.00 39.35  0  726  VAL   A CG2 1 
ATOM   5193  N N   . GLN   A 1 763  ? 147.857 109.904 144.742 1.00 41.99  0  727  GLN   A N   1 
ATOM   5194  C CA  . GLN   A 1 763  ? 146.890 108.839 144.972 1.00 42.52  0  727  GLN   A CA  1 
ATOM   5195  C C   . GLN   A 1 763  ? 145.539 109.475 145.270 1.00 50.94  0  727  GLN   A C   1 
ATOM   5196  O O   . GLN   A 1 763  ? 145.360 110.097 146.323 1.00 61.47  0  727  GLN   A O   1 
ATOM   5197  C CB  . GLN   A 1 763  ? 147.337 107.935 146.115 1.00 42.21  0  727  GLN   A CB  1 
ATOM   5198  C CG  . GLN   A 1 763  ? 148.610 107.185 145.821 1.00 53.12  0  727  GLN   A CG  1 
ATOM   5199  C CD  . GLN   A 1 763  ? 149.194 106.540 147.049 1.00 58.07  0  727  GLN   A CD  1 
ATOM   5200  O OE1 . GLN   A 1 763  ? 149.590 105.378 147.022 1.00 57.83  0  727  GLN   A OE1 1 
ATOM   5201  N NE2 . GLN   A 1 763  ? 149.251 107.290 148.140 1.00 56.82  0  727  GLN   A NE2 1 
ATOM   5202  N N   . SER   A 1 764  ? 144.598 109.322 144.341 1.00 39.83  0  728  SER   A N   1 
ATOM   5203  C CA  . SER   A 1 764  ? 143.220 109.784 144.506 1.00 38.90  0  728  SER   A CA  1 
ATOM   5204  C C   . SER   A 1 764  ? 143.158 111.296 144.730 1.00 34.32  0  728  SER   A C   1 
ATOM   5205  O O   . SER   A 1 764  ? 142.715 111.779 145.771 1.00 42.97  0  728  SER   A O   1 
ATOM   5206  C CB  . SER   A 1 764  ? 142.523 109.038 145.648 1.00 37.90  0  728  SER   A CB  1 
ATOM   5207  O OG  . SER   A 1 764  ? 142.993 109.480 146.906 1.00 30.93  0  728  SER   A OG  1 
ATOM   5208  N N   . LEU   A 1 765  ? 143.622 112.041 143.729 1.00 17.63  0  729  LEU   A N   1 
ATOM   5209  C CA  . LEU   A 1 765  ? 143.385 113.477 143.686 1.00 27.48  0  729  LEU   A CA  1 
ATOM   5210  C C   . LEU   A 1 765  ? 142.343 113.866 142.651 1.00 27.69  0  729  LEU   A C   1 
ATOM   5211  O O   . LEU   A 1 765  ? 141.583 114.812 142.880 1.00 33.76  0  729  LEU   A O   1 
ATOM   5212  C CB  . LEU   A 1 765  ? 144.688 114.233 143.398 1.00 32.29  0  729  LEU   A CB  1 
ATOM   5213  C CG  . LEU   A 1 765  ? 144.577 115.679 142.902 1.00 27.47  0  729  LEU   A CG  1 
ATOM   5214  C CD1 . LEU   A 1 765  ? 144.075 116.590 144.002 1.00 24.85  0  729  LEU   A CD1 1 
ATOM   5215  C CD2 . LEU   A 1 765  ? 145.900 116.181 142.356 1.00 26.65  0  729  LEU   A CD2 1 
ATOM   5216  N N   . PHE   A 1 766  ? 142.285 113.162 141.530 1.00 21.52  0  730  PHE   A N   1 
ATOM   5217  C CA  . PHE   A 1 766  ? 141.298 113.421 140.498 1.00 23.57  0  730  PHE   A CA  1 
ATOM   5218  C C   . PHE   A 1 766  ? 140.061 112.554 140.651 1.00 30.26  0  730  PHE   A C   1 
ATOM   5219  O O   . PHE   A 1 766  ? 139.128 112.677 139.854 1.00 38.32  0  730  PHE   A O   1 
ATOM   5220  C CB  . PHE   A 1 766  ? 141.921 113.218 139.113 1.00 23.24  0  730  PHE   A CB  1 
ATOM   5221  C CG  . PHE   A 1 766  ? 143.123 114.086 138.858 1.00 33.14  0  730  PHE   A CG  1 
ATOM   5222  C CD1 . PHE   A 1 766  ? 144.341 113.807 139.448 1.00 32.82  0  730  PHE   A CD1 1 
ATOM   5223  C CD2 . PHE   A 1 766  ? 143.030 115.187 138.035 1.00 31.57  0  730  PHE   A CD2 1 
ATOM   5224  C CE1 . PHE   A 1 766  ? 145.431 114.603 139.224 1.00 32.09  0  730  PHE   A CE1 1 
ATOM   5225  C CE2 . PHE   A 1 766  ? 144.122 115.986 137.807 1.00 31.93  0  730  PHE   A CE2 1 
ATOM   5226  C CZ  . PHE   A 1 766  ? 145.321 115.691 138.402 1.00 38.02  0  730  PHE   A CZ  1 
ATOM   5227  N N   . SER   A 1 767  ? 140.029 111.689 141.657 1.00 24.54  0  731  SER   A N   1 
ATOM   5228  C CA  . SER   A 1 767  ? 138.889 110.831 141.941 1.00 22.26  0  731  SER   A CA  1 
ATOM   5229  C C   . SER   A 1 767  ? 138.307 111.139 143.313 1.00 22.37  0  731  SER   A C   1 
ATOM   5230  O O   . SER   A 1 767  ? 137.461 110.405 143.821 1.00 29.84  0  731  SER   A O   1 
ATOM   5231  C CB  . SER   A 1 767  ? 139.280 109.360 141.848 1.00 35.78  0  731  SER   A CB  1 
ATOM   5232  O OG  . SER   A 1 767  ? 140.331 109.053 142.742 1.00 37.84  0  731  SER   A OG  1 
ATOM   5233  N N   . TRP   A 1 768  ? 138.749 112.248 143.914 1.00 24.44  0  732  TRP   A N   1 
ATOM   5234  C CA  . TRP   A 1 768  ? 138.352 112.588 145.279 1.00 25.73  0  732  TRP   A CA  1 
ATOM   5235  C C   . TRP   A 1 768  ? 136.838 112.553 145.443 1.00 29.38  0  732  TRP   A C   1 
ATOM   5236  O O   . TRP   A 1 768  ? 136.325 112.015 146.433 1.00 31.45  0  732  TRP   A O   1 
ATOM   5237  C CB  . TRP   A 1 768  ? 138.887 113.975 145.638 1.00 16.07  0  732  TRP   A CB  1 
ATOM   5238  C CG  . TRP   A 1 768  ? 138.285 115.054 144.789 1.00 20.02  0  732  TRP   A CG  1 
ATOM   5239  C CD1 . TRP   A 1 768  ? 138.645 115.398 143.522 1.00 22.47  0  732  TRP   A CD1 1 
ATOM   5240  C CD2 . TRP   A 1 768  ? 137.197 115.914 145.143 1.00 27.43  0  732  TRP   A CD2 1 
ATOM   5241  N NE1 . TRP   A 1 768  ? 137.852 116.418 143.064 1.00 17.48  0  732  TRP   A NE1 1 
ATOM   5242  C CE2 . TRP   A 1 768  ? 136.955 116.754 144.042 1.00 24.88  0  732  TRP   A CE2 1 
ATOM   5243  C CE3 . TRP   A 1 768  ? 136.404 116.056 146.286 1.00 23.68  0  732  TRP   A CE3 1 
ATOM   5244  C CZ2 . TRP   A 1 768  ? 135.958 117.719 144.050 1.00 26.32  0  732  TRP   A CZ2 1 
ATOM   5245  C CZ3 . TRP   A 1 768  ? 135.416 117.016 146.291 1.00 13.24  0  732  TRP   A CZ3 1 
ATOM   5246  C CH2 . TRP   A 1 768  ? 135.201 117.835 145.182 1.00 20.79  0  732  TRP   A CH2 1 
ATOM   5247  N N   . LEU   A 1 769  ? 136.110 113.081 144.456 1.00 34.08  0  733  LEU   A N   1 
ATOM   5248  C CA  . LEU   A 1 769  ? 134.667 113.266 144.521 1.00 22.65  0  733  LEU   A CA  1 
ATOM   5249  C C   . LEU   A 1 769  ? 133.970 111.986 144.944 1.00 23.27  0  733  LEU   A C   1 
ATOM   5250  O O   . LEU   A 1 769  ? 133.391 111.913 146.032 1.00 30.31  0  733  LEU   A O   1 
ATOM   5251  C CB  . LEU   A 1 769  ? 134.140 113.725 143.161 1.00 12.71  0  733  LEU   A CB  1 
ATOM   5252  C CG  . LEU   A 1 769  ? 132.727 114.288 143.083 1.00 10.10  0  733  LEU   A CG  1 
ATOM   5253  C CD1 . LEU   A 1 769  ? 132.678 115.590 143.820 1.00 33.32  0  733  LEU   A CD1 1 
ATOM   5254  C CD2 . LEU   A 1 769  ? 132.334 114.506 141.646 1.00 24.94  0  733  LEU   A CD2 1 
ATOM   5255  N N   . HIS   A 1 770  ? 134.077 110.952 144.115 1.00 16.24  0  734  HIS   A N   1 
ATOM   5256  C CA  . HIS   A 1 770  ? 133.367 109.715 144.384 1.00 15.82  0  734  HIS   A CA  1 
ATOM   5257  C C   . HIS   A 1 770  ? 133.917 108.963 145.583 1.00 20.75  0  734  HIS   A C   1 
ATOM   5258  O O   . HIS   A 1 770  ? 133.261 108.027 146.047 1.00 38.20  0  734  HIS   A O   1 
ATOM   5259  C CB  . HIS   A 1 770  ? 133.388 108.827 143.146 1.00 23.24  0  734  HIS   A CB  1 
ATOM   5260  C CG  . HIS   A 1 770  ? 132.938 109.524 141.901 1.00 26.65  0  734  HIS   A CG  1 
ATOM   5261  N ND1 . HIS   A 1 770  ? 131.611 109.760 141.619 1.00 18.66  0  734  HIS   A ND1 1 
ATOM   5262  C CD2 . HIS   A 1 770  ? 133.639 110.032 140.860 1.00 32.25  0  734  HIS   A CD2 1 
ATOM   5263  C CE1 . HIS   A 1 770  ? 131.514 110.387 140.461 1.00 20.89  0  734  HIS   A CE1 1 
ATOM   5264  N NE2 . HIS   A 1 770  ? 132.730 110.563 139.979 1.00 24.04  0  734  HIS   A NE2 1 
ATOM   5265  N N   . LEU   A 1 771  ? 135.086 109.334 146.103 1.00 14.49  0  735  LEU   A N   1 
ATOM   5266  C CA  . LEU   A 1 771  ? 135.542 108.708 147.335 1.00 20.49  0  735  LEU   A CA  1 
ATOM   5267  C C   . LEU   A 1 771  ? 135.223 109.535 148.571 1.00 32.00  0  735  LEU   A C   1 
ATOM   5268  O O   . LEU   A 1 771  ? 135.499 109.082 149.686 1.00 20.18  0  735  LEU   A O   1 
ATOM   5269  C CB  . LEU   A 1 771  ? 137.047 108.430 147.291 1.00 20.54  0  735  LEU   A CB  1 
ATOM   5270  C CG  . LEU   A 1 771  ? 137.602 107.611 146.128 1.00 24.70  0  735  LEU   A CG  1 
ATOM   5271  C CD1 . LEU   A 1 771  ? 138.786 108.310 145.507 1.00 19.94  0  735  LEU   A CD1 1 
ATOM   5272  C CD2 . LEU   A 1 771  ? 137.987 106.224 146.583 1.00 36.06  0  735  LEU   A CD2 1 
ATOM   5273  N N   . THR   A 1 772  ? 134.649 110.722 148.401 1.00 37.78  0  736  THR   A N   1 
ATOM   5274  C CA  . THR   A 1 772  ? 134.345 111.614 149.513 1.00 24.63  0  736  THR   A CA  1 
ATOM   5275  C C   . THR   A 1 772  ? 132.872 111.962 149.621 1.00 23.43  0  736  THR   A C   1 
ATOM   5276  O O   . THR   A 1 772  ? 132.328 111.970 150.725 1.00 33.86  0  736  THR   A O   1 
ATOM   5277  C CB  . THR   A 1 772  ? 135.154 112.908 149.383 1.00 25.44  0  736  THR   A CB  1 
ATOM   5278  O OG1 . THR   A 1 772  ? 135.080 113.382 148.033 1.00 24.82  0  736  THR   A OG1 1 
ATOM   5279  C CG2 . THR   A 1 772  ? 136.602 112.670 149.744 1.00 32.18  0  736  THR   A CG2 1 
ATOM   5280  N N   . ILE   A 1 773  ? 132.215 112.252 148.495 1.00 19.15  0  737  ILE   A N   1 
ATOM   5281  C CA  . ILE   A 1 773  ? 130.809 112.665 148.540 1.00 29.75  0  737  ILE   A CA  1 
ATOM   5282  C C   . ILE   A 1 773  ? 129.891 111.608 149.137 1.00 37.30  0  737  ILE   A C   1 
ATOM   5283  O O   . ILE   A 1 773  ? 128.978 111.975 149.890 1.00 38.47  0  737  ILE   A O   1 
ATOM   5284  C CB  . ILE   A 1 773  ? 130.355 113.137 147.153 1.00 24.26  0  737  ILE   A CB  1 
ATOM   5285  C CG1 . ILE   A 1 773  ? 131.175 114.348 146.722 1.00 23.56  0  737  ILE   A CG1 1 
ATOM   5286  C CG2 . ILE   A 1 773  ? 128.884 113.468 147.163 1.00 24.46  0  737  ILE   A CG2 1 
ATOM   5287  C CD1 . ILE   A 1 773  ? 131.093 115.515 147.662 1.00 22.40  0  737  ILE   A CD1 1 
ATOM   5288  N N   . PRO   A 1 774  ? 130.034 110.308 148.843 1.00 27.52  0  738  PRO   A N   1 
ATOM   5289  C CA  . PRO   A 1 774  ? 129.081 109.339 149.407 1.00 27.71  0  738  PRO   A CA  1 
ATOM   5290  C C   . PRO   A 1 774  ? 128.926 109.411 150.915 1.00 28.15  0  738  PRO   A C   1 
ATOM   5291  O O   . PRO   A 1 774  ? 127.823 109.189 151.425 1.00 35.57  0  738  PRO   A O   1 
ATOM   5292  C CB  . PRO   A 1 774  ? 129.672 107.997 148.970 1.00 29.14  0  738  PRO   A CB  1 
ATOM   5293  C CG  . PRO   A 1 774  ? 130.317 108.296 147.694 1.00 24.58  0  738  PRO   A CG  1 
ATOM   5294  C CD  . PRO   A 1 774  ? 130.879 109.677 147.813 1.00 23.06  0  738  PRO   A CD  1 
ATOM   5295  N N   . HIS   A 1 775  ? 129.987 109.730 151.643 1.00 29.17  0  739  HIS   A N   1 
ATOM   5296  C CA  . HIS   A 1 775  ? 129.950 109.710 153.098 1.00 34.58  0  739  HIS   A CA  1 
ATOM   5297  C C   . HIS   A 1 775  ? 129.463 111.016 153.711 1.00 34.73  0  739  HIS   A C   1 
ATOM   5298  O O   . HIS   A 1 775  ? 129.346 111.097 154.937 1.00 37.74  0  739  HIS   A O   1 
ATOM   5299  C CB  . HIS   A 1 775  ? 131.338 109.367 153.646 1.00 30.03  0  739  HIS   A CB  1 
ATOM   5300  C CG  . HIS   A 1 775  ? 131.943 108.148 153.026 1.00 38.28  0  739  HIS   A CG  1 
ATOM   5301  N ND1 . HIS   A 1 775  ? 132.921 108.212 152.058 1.00 39.94  0  739  HIS   A ND1 1 
ATOM   5302  C CD2 . HIS   A 1 775  ? 131.703 106.832 153.230 1.00 39.90  0  739  HIS   A CD2 1 
ATOM   5303  C CE1 . HIS   A 1 775  ? 133.260 106.989 151.695 1.00 39.86  0  739  HIS   A CE1 1 
ATOM   5304  N NE2 . HIS   A 1 775  ? 132.535 106.133 152.391 1.00 42.18  0  739  HIS   A NE2 1 
ATOM   5305  N N   . VAL   A 1 776  ? 129.165 112.030 152.904 1.00 31.21  0  740  VAL   A N   1 
ATOM   5306  C CA  . VAL   A 1 776  ? 128.758 113.324 153.440 1.00 36.22  0  740  VAL   A CA  1 
ATOM   5307  C C   . VAL   A 1 776  ? 127.243 113.445 153.391 1.00 37.32  0  740  VAL   A C   1 
ATOM   5308  O O   . VAL   A 1 776  ? 126.566 112.658 152.723 1.00 42.20  0  740  VAL   A O   1 
ATOM   5309  C CB  . VAL   A 1 776  ? 129.425 114.484 152.679 1.00 30.50  0  740  VAL   A CB  1 
ATOM   5310  C CG1 . VAL   A 1 776  ? 130.889 114.192 152.461 1.00 26.27  0  740  VAL   A CG1 1 
ATOM   5311  C CG2 . VAL   A 1 776  ? 128.721 114.739 151.364 1.00 28.11  0  740  VAL   A CG2 1 
ATOM   5312  N N   . THR   A 1 777  ? 126.707 114.431 154.100 1.00 26.59  0  741  THR   A N   1 
ATOM   5313  C CA  . THR   A 1 777  ? 125.270 114.662 154.197 1.00 16.87  0  741  THR   A CA  1 
ATOM   5314  C C   . THR   A 1 777  ? 124.920 115.878 153.351 1.00 19.18  0  741  THR   A C   1 
ATOM   5315  O O   . THR   A 1 777  ? 125.152 117.016 153.763 1.00 38.77  0  741  THR   A O   1 
ATOM   5316  C CB  . THR   A 1 777  ? 124.857 114.871 155.648 1.00 33.11  0  741  THR   A CB  1 
ATOM   5317  O OG1 . THR   A 1 777  ? 125.291 113.757 156.438 1.00 39.91  0  741  THR   A OG1 1 
ATOM   5318  C CG2 . THR   A 1 777  ? 123.354 115.011 155.750 1.00 40.42  0  741  THR   A CG2 1 
ATOM   5319  N N   . ILE   A 1 778  ? 124.355 115.638 152.169 1.00 10.46  0  742  ILE   A N   1 
ATOM   5320  C CA  . ILE   A 1 778  ? 123.967 116.740 151.299 1.00 17.54  0  742  ILE   A CA  1 
ATOM   5321  C C   . ILE   A 1 778  ? 122.768 117.447 151.905 1.00 16.89  0  742  ILE   A C   1 
ATOM   5322  O O   . ILE   A 1 778  ? 121.769 116.812 152.260 1.00 35.40  0  742  ILE   A O   1 
ATOM   5323  C CB  . ILE   A 1 778  ? 123.665 116.224 149.884 1.00 19.65  0  742  ILE   A CB  1 
ATOM   5324  C CG1 . ILE   A 1 778  ? 124.959 115.844 149.168 1.00 21.11  0  742  ILE   A CG1 1 
ATOM   5325  C CG2 . ILE   A 1 778  ? 122.922 117.274 149.080 1.00 17.14  0  742  ILE   A CG2 1 
ATOM   5326  C CD1 . ILE   A 1 778  ? 125.444 114.451 149.471 1.00 23.74  0  742  ILE   A CD1 1 
ATOM   5327  N N   . ILE   A 1 779  ? 122.860 118.766 152.037 1.00 9.91   0  743  ILE   A N   1 
ATOM   5328  C CA  . ILE   A 1 779  ? 121.808 119.547 152.674 1.00 11.43  0  743  ILE   A CA  1 
ATOM   5329  C C   . ILE   A 1 779  ? 121.561 120.804 151.855 1.00 17.60  0  743  ILE   A C   1 
ATOM   5330  O O   . ILE   A 1 779  ? 122.497 121.411 151.327 1.00 38.66  0  743  ILE   A O   1 
ATOM   5331  C CB  . ILE   A 1 779  ? 122.174 119.890 154.133 1.00 16.13  0  743  ILE   A CB  1 
ATOM   5332  C CG1 . ILE   A 1 779  ? 121.156 120.854 154.743 1.00 25.55  0  743  ILE   A CG1 1 
ATOM   5333  C CG2 . ILE   A 1 779  ? 123.568 120.472 154.210 1.00 17.95  0  743  ILE   A CG2 1 
ATOM   5334  C CD1 . ILE   A 1 779  ? 121.215 120.923 156.252 1.00 21.37  0  743  ILE   A CD1 1 
ATOM   5335  N N   . CYS   A 1 780  ? 120.293 121.176 151.716 1.00 9.22   0  744  CYS   A N   1 
ATOM   5336  C CA  . CYS   A 1 780  ? 119.925 122.461 151.137 1.00 15.83  0  744  CYS   A CA  1 
ATOM   5337  C C   . CYS   A 1 780  ? 119.998 123.501 152.245 1.00 25.08  0  744  CYS   A C   1 
ATOM   5338  O O   . CYS   A 1 780  ? 119.144 123.526 153.137 1.00 30.81  0  744  CYS   A O   1 
ATOM   5339  C CB  . CYS   A 1 780  ? 118.531 122.409 150.523 1.00 27.54  0  744  CYS   A CB  1 
ATOM   5340  S SG  . CYS   A 1 780  ? 117.869 124.024 150.086 1.00 29.90  0  744  CYS   A SG  1 
ATOM   5341  N N   . THR   A 1 781  ? 121.016 124.356 152.195 1.00 24.57  0  745  THR   A N   1 
ATOM   5342  C CA  . THR   A 1 781  ? 121.277 125.323 153.257 1.00 20.73  0  745  THR   A CA  1 
ATOM   5343  C C   . THR   A 1 781  ? 120.815 126.716 152.879 1.00 21.57  0  745  THR   A C   1 
ATOM   5344  O O   . THR   A 1 781  ? 121.478 127.702 153.205 1.00 35.46  0  745  THR   A O   1 
ATOM   5345  C CB  . THR   A 1 781  ? 122.757 125.349 153.607 1.00 29.76  0  745  THR   A CB  1 
ATOM   5346  O OG1 . THR   A 1 781  ? 123.519 125.406 152.401 1.00 37.67  0  745  THR   A OG1 1 
ATOM   5347  C CG2 . THR   A 1 781  ? 123.139 124.106 154.380 1.00 23.46  0  745  THR   A CG2 1 
ATOM   5348  N N   . TYR   A 1 782  ? 119.699 126.836 152.174 1.00 20.49  0  746  TYR   A N   1 
ATOM   5349  C CA  . TYR   A 1 782  ? 119.131 128.154 151.963 1.00 28.06  0  746  TYR   A CA  1 
ATOM   5350  C C   . TYR   A 1 782  ? 118.658 128.726 153.294 1.00 40.50  0  746  TYR   A C   1 
ATOM   5351  O O   . TYR   A 1 782  ? 118.343 127.992 154.232 1.00 43.13  0  746  TYR   A O   1 
ATOM   5352  C CB  . TYR   A 1 782  ? 117.976 128.103 150.970 1.00 25.77  0  746  TYR   A CB  1 
ATOM   5353  C CG  . TYR   A 1 782  ? 117.442 129.473 150.671 1.00 33.16  0  746  TYR   A CG  1 
ATOM   5354  C CD1 . TYR   A 1 782  ? 118.237 130.424 150.058 1.00 35.61  0  746  TYR   A CD1 1 
ATOM   5355  C CD2 . TYR   A 1 782  ? 116.165 129.837 151.054 1.00 40.92  0  746  TYR   A CD2 1 
ATOM   5356  C CE1 . TYR   A 1 782  ? 117.760 131.689 149.800 1.00 35.05  0  746  TYR   A CE1 1 
ATOM   5357  C CE2 . TYR   A 1 782  ? 115.682 131.098 150.806 1.00 36.22  0  746  TYR   A CE2 1 
ATOM   5358  C CZ  . TYR   A 1 782  ? 116.480 132.018 150.176 1.00 35.35  0  746  TYR   A CZ  1 
ATOM   5359  O OH  . TYR   A 1 782  ? 116.001 133.279 149.923 1.00 39.38  0  746  TYR   A OH  1 
ATOM   5360  N N   . ARG   A 1 783  ? 118.625 130.057 153.373 1.00 36.09  0  747  ARG   A N   1 
ATOM   5361  C CA  . ARG   A 1 783  ? 118.295 130.714 154.633 1.00 33.95  0  747  ARG   A CA  1 
ATOM   5362  C C   . ARG   A 1 783  ? 116.898 130.339 155.112 1.00 32.53  0  747  ARG   A C   1 
ATOM   5363  O O   . ARG   A 1 783  ? 116.696 130.059 156.297 1.00 35.25  0  747  ARG   A O   1 
ATOM   5364  C CB  . ARG   A 1 783  ? 118.421 132.227 154.474 1.00 38.87  0  747  ARG   A CB  1 
ATOM   5365  C CG  . ARG   A 1 783  ? 118.629 132.978 155.771 1.00 37.83  0  747  ARG   A CG  1 
ATOM   5366  C CD  . ARG   A 1 783  ? 118.695 134.475 155.529 1.00 36.67  0  747  ARG   A CD  1 
ATOM   5367  N NE  . ARG   A 1 783  ? 118.053 135.232 156.597 1.00 41.94  0  747  ARG   A NE  1 
ATOM   5368  C CZ  . ARG   A 1 783  ? 118.562 135.404 157.809 1.00 47.18  0  747  ARG   A CZ  1 
ATOM   5369  N NH1 . ARG   A 1 783  ? 119.731 134.885 158.149 1.00 46.03  1  747  ARG   A NH1 1 
ATOM   5370  N NH2 . ARG   A 1 783  ? 117.883 136.116 158.703 1.00 41.74  0  747  ARG   A NH2 1 
ATOM   5371  N N   . HIS   A 1 784  ? 115.923 130.309 154.205 1.00 31.11  0  748  HIS   A N   1 
ATOM   5372  C CA  . HIS   A 1 784  ? 114.526 130.107 154.567 1.00 34.00  0  748  HIS   A CA  1 
ATOM   5373  C C   . HIS   A 1 784  ? 114.047 128.684 154.305 1.00 31.52  0  748  HIS   A C   1 
ATOM   5374  O O   . HIS   A 1 784  ? 112.841 128.455 154.174 1.00 38.53  0  748  HIS   A O   1 
ATOM   5375  C CB  . HIS   A 1 784  ? 113.643 131.106 153.823 1.00 31.27  0  748  HIS   A CB  1 
ATOM   5376  C CG  . HIS   A 1 784  ? 113.992 132.533 154.094 1.00 33.49  0  748  HIS   A CG  1 
ATOM   5377  N ND1 . HIS   A 1 784  ? 113.710 133.153 155.292 1.00 39.23  0  748  HIS   A ND1 1 
ATOM   5378  C CD2 . HIS   A 1 784  ? 114.612 133.460 153.328 1.00 31.86  0  748  HIS   A CD2 1 
ATOM   5379  C CE1 . HIS   A 1 784  ? 114.135 134.402 155.249 1.00 41.26  0  748  HIS   A CE1 1 
ATOM   5380  N NE2 . HIS   A 1 784  ? 114.685 134.614 154.068 1.00 38.77  0  748  HIS   A NE2 1 
ATOM   5381  N N   . ALA   A 1 785  ? 114.959 127.722 154.223 1.00 27.70  0  749  ALA   A N   1 
ATOM   5382  C CA  . ALA   A 1 785  ? 114.605 126.323 153.981 1.00 28.96  0  749  ALA   A CA  1 
ATOM   5383  C C   . ALA   A 1 785  ? 115.349 125.431 154.963 1.00 33.89  0  749  ALA   A C   1 
ATOM   5384  O O   . ALA   A 1 785  ? 116.232 124.655 154.581 1.00 32.14  0  749  ALA   A O   1 
ATOM   5385  C CB  . ALA   A 1 785  ? 114.910 125.930 152.535 1.00 26.89  0  749  ALA   A CB  1 
ATOM   5386  N N   . PRO   A 1 786  ? 115.004 125.503 156.244 1.00 29.06  0  750  PRO   A N   1 
ATOM   5387  C CA  . PRO   A 1 786  ? 115.682 124.679 157.239 1.00 29.07  0  750  PRO   A CA  1 
ATOM   5388  C C   . PRO   A 1 786  ? 115.128 123.267 157.246 1.00 30.16  0  750  PRO   A C   1 
ATOM   5389  O O   . PRO   A 1 786  ? 113.981 123.038 156.836 1.00 31.52  0  750  PRO   A O   1 
ATOM   5390  C CB  . PRO   A 1 786  ? 115.373 125.404 158.553 1.00 29.15  0  750  PRO   A CB  1 
ATOM   5391  C CG  . PRO   A 1 786  ? 114.036 125.990 158.321 1.00 31.60  0  750  PRO   A CG  1 
ATOM   5392  C CD  . PRO   A 1 786  ? 113.954 126.337 156.854 1.00 27.58  0  750  PRO   A CD  1 
ATOM   5393  N N   . PRO   A 1 787  ? 115.909 122.293 157.695 1.00 25.27  0  751  PRO   A N   1 
ATOM   5394  C CA  . PRO   A 1 787  ? 115.381 120.944 157.887 1.00 29.78  0  751  PRO   A CA  1 
ATOM   5395  C C   . PRO   A 1 787  ? 114.672 120.826 159.228 1.00 38.41  0  751  PRO   A C   1 
ATOM   5396  O O   . PRO   A 1 787  ? 114.812 121.665 160.117 1.00 45.03  0  751  PRO   A O   1 
ATOM   5397  C CB  . PRO   A 1 787  ? 116.639 120.078 157.853 1.00 28.63  0  751  PRO   A CB  1 
ATOM   5398  C CG  . PRO   A 1 787  ? 117.671 120.950 158.450 1.00 28.16  0  751  PRO   A CG  1 
ATOM   5399  C CD  . PRO   A 1 787  ? 117.347 122.357 158.004 1.00 34.88  0  751  PRO   A CD  1 
ATOM   5400  N N   . TYR   A 1 788  ? 113.899 119.754 159.364 1.00 32.92  0  752  TYR   A N   1 
ATOM   5401  C CA  . TYR   A 1 788  ? 113.269 119.421 160.637 1.00 28.65  0  752  TYR   A CA  1 
ATOM   5402  C C   . TYR   A 1 788  ? 114.264 118.600 161.445 1.00 36.34  0  752  TYR   A C   1 
ATOM   5403  O O   . TYR   A 1 788  ? 114.457 117.410 161.189 1.00 39.35  0  752  TYR   A O   1 
ATOM   5404  C CB  . TYR   A 1 788  ? 111.965 118.665 160.423 1.00 31.51  0  752  TYR   A CB  1 
ATOM   5405  C CG  . TYR   A 1 788  ? 111.227 118.388 161.710 1.00 39.74  0  752  TYR   A CG  1 
ATOM   5406  C CD1 . TYR   A 1 788  ? 110.537 119.395 162.362 1.00 38.29  0  752  TYR   A CD1 1 
ATOM   5407  C CD2 . TYR   A 1 788  ? 111.231 117.125 162.276 1.00 40.14  0  752  TYR   A CD2 1 
ATOM   5408  C CE1 . TYR   A 1 788  ? 109.867 119.151 163.536 1.00 35.98  0  752  TYR   A CE1 1 
ATOM   5409  C CE2 . TYR   A 1 788  ? 110.563 116.871 163.451 1.00 39.84  0  752  TYR   A CE2 1 
ATOM   5410  C CZ  . TYR   A 1 788  ? 109.882 117.889 164.077 1.00 41.51  0  752  TYR   A CZ  1 
ATOM   5411  O OH  . TYR   A 1 788  ? 109.211 117.645 165.251 1.00 46.34  0  752  TYR   A OH  1 
ATOM   5412  N N   . ILE   A 1 789  ? 114.901 119.235 162.421 1.00 41.93  0  753  ILE   A N   1 
ATOM   5413  C CA  . ILE   A 1 789  ? 115.901 118.576 163.251 1.00 36.49  0  753  ILE   A CA  1 
ATOM   5414  C C   . ILE   A 1 789  ? 115.196 117.947 164.443 1.00 44.39  0  753  ILE   A C   1 
ATOM   5415  O O   . ILE   A 1 789  ? 114.432 118.615 165.147 1.00 49.97  0  753  ILE   A O   1 
ATOM   5416  C CB  . ILE   A 1 789  ? 116.984 119.562 163.706 1.00 36.65  0  753  ILE   A CB  1 
ATOM   5417  C CG1 . ILE   A 1 789  ? 117.417 120.440 162.537 1.00 38.43  0  753  ILE   A CG1 1 
ATOM   5418  C CG2 . ILE   A 1 789  ? 118.179 118.819 164.257 1.00 37.62  0  753  ILE   A CG2 1 
ATOM   5419  C CD1 . ILE   A 1 789  ? 118.350 121.540 162.930 1.00 42.38  0  753  ILE   A CD1 1 
ATOM   5420  N N   . GLY   A 1 790  ? 115.456 116.667 164.671 1.00 58.35  0  754  GLY   A N   1 
ATOM   5421  C CA  . GLY   A 1 790  ? 114.759 115.940 165.708 1.00 61.42  0  754  GLY   A CA  1 
ATOM   5422  C C   . GLY   A 1 790  ? 115.184 116.353 167.102 1.00 63.32  0  754  GLY   A C   1 
ATOM   5423  O O   . GLY   A 1 790  ? 116.142 117.098 167.312 1.00 66.69  0  754  GLY   A O   1 
ATOM   5424  N N   . ASP   A 1 791  ? 114.433 115.852 168.077 1.00 62.44  0  755  ASP   A N   1 
ATOM   5425  C CA  . ASP   A 1 791  ? 114.715 116.142 169.475 1.00 61.71  0  755  ASP   A CA  1 
ATOM   5426  C C   . ASP   A 1 791  ? 116.087 115.603 169.860 1.00 58.71  0  755  ASP   A C   1 
ATOM   5427  O O   . ASP   A 1 791  ? 116.413 114.445 169.585 1.00 59.71  0  755  ASP   A O   1 
ATOM   5428  C CB  . ASP   A 1 791  ? 113.618 115.533 170.354 1.00 65.54  0  755  ASP   A CB  1 
ATOM   5429  C CG  . ASP   A 1 791  ? 114.041 115.365 171.800 1.00 67.61  0  755  ASP   A CG  1 
ATOM   5430  O OD1 . ASP   A 1 791  ? 114.679 114.341 172.122 1.00 67.32  0  755  ASP   A OD1 1 
ATOM   5431  O OD2 . ASP   A 1 791  ? 113.717 116.249 172.619 1.00 66.59  -1 755  ASP   A OD2 1 
ATOM   5432  N N   . HIS   A 1 792  ? 116.891 116.452 170.498 1.00 56.73  0  756  HIS   A N   1 
ATOM   5433  C CA  . HIS   A 1 792  ? 118.250 116.122 170.922 1.00 61.60  0  756  HIS   A CA  1 
ATOM   5434  C C   . HIS   A 1 792  ? 119.134 115.671 169.765 1.00 61.75  0  756  HIS   A C   1 
ATOM   5435  O O   . HIS   A 1 792  ? 120.005 114.814 169.946 1.00 61.96  0  756  HIS   A O   1 
ATOM   5436  C CB  . HIS   A 1 792  ? 118.252 115.057 172.025 1.00 64.84  0  756  HIS   A CB  1 
ATOM   5437  C CG  . HIS   A 1 792  ? 117.381 115.391 173.196 1.00 65.43  0  756  HIS   A CG  1 
ATOM   5438  N ND1 . HIS   A 1 792  ? 116.799 116.628 173.366 1.00 65.92  0  756  HIS   A ND1 1 
ATOM   5439  C CD2 . HIS   A 1 792  ? 116.997 114.646 174.260 1.00 66.42  0  756  HIS   A CD2 1 
ATOM   5440  C CE1 . HIS   A 1 792  ? 116.093 116.631 174.483 1.00 65.93  0  756  HIS   A CE1 1 
ATOM   5441  N NE2 . HIS   A 1 792  ? 116.196 115.439 175.044 1.00 67.30  0  756  HIS   A NE2 1 
ATOM   5442  N N   . ILE   A 1 793  ? 118.937 116.230 168.576 1.00 56.84  0  757  ILE   A N   1 
ATOM   5443  C CA  . ILE   A 1 793  ? 119.783 115.945 167.423 1.00 56.30  0  757  ILE   A CA  1 
ATOM   5444  C C   . ILE   A 1 793  ? 120.610 117.186 167.125 1.00 55.37  0  757  ILE   A C   1 
ATOM   5445  O O   . ILE   A 1 793  ? 120.060 118.264 166.873 1.00 59.30  0  757  ILE   A O   1 
ATOM   5446  C CB  . ILE   A 1 793  ? 118.955 115.528 166.198 1.00 52.30  0  757  ILE   A CB  1 
ATOM   5447  C CG1 . ILE   A 1 793  ? 118.438 114.099 166.360 1.00 52.23  0  757  ILE   A CG1 1 
ATOM   5448  C CG2 . ILE   A 1 793  ? 119.790 115.632 164.938 1.00 51.28  0  757  ILE   A CG2 1 
ATOM   5449  C CD1 . ILE   A 1 793  ? 119.530 113.062 166.377 1.00 53.08  0  757  ILE   A CD1 1 
ATOM   5450  N N   . VAL   A 1 794  ? 121.930 117.036 167.156 1.00 43.96  0  758  VAL   A N   1 
ATOM   5451  C CA  . VAL   A 1 794  ? 122.836 118.140 166.876 1.00 43.62  0  758  VAL   A CA  1 
ATOM   5452  C C   . VAL   A 1 794  ? 123.754 117.855 165.696 1.00 49.81  0  758  VAL   A C   1 
ATOM   5453  O O   . VAL   A 1 794  ? 124.341 118.802 165.150 1.00 48.74  0  758  VAL   A O   1 
ATOM   5454  C CB  . VAL   A 1 794  ? 123.669 118.501 168.121 1.00 45.85  0  758  VAL   A CB  1 
ATOM   5455  C CG1 . VAL   A 1 794  ? 122.769 119.021 169.223 1.00 46.52  0  758  VAL   A CG1 1 
ATOM   5456  C CG2 . VAL   A 1 794  ? 124.448 117.291 168.602 1.00 46.17  0  758  VAL   A CG2 1 
ATOM   5457  N N   . ASP   A 1 795  ? 123.887 116.602 165.278 1.00 51.00  0  759  ASP   A N   1 
ATOM   5458  C CA  . ASP   A 1 795  ? 124.801 116.206 164.217 1.00 43.72  0  759  ASP   A CA  1 
ATOM   5459  C C   . ASP   A 1 795  ? 124.041 116.111 162.903 1.00 43.34  0  759  ASP   A C   1 
ATOM   5460  O O   . ASP   A 1 795  ? 122.957 115.525 162.850 1.00 50.04  0  759  ASP   A O   1 
ATOM   5461  C CB  . ASP   A 1 795  ? 125.452 114.865 164.554 1.00 46.38  0  759  ASP   A CB  1 
ATOM   5462  C CG  . ASP   A 1 795  ? 126.648 114.558 163.684 1.00 52.70  0  759  ASP   A CG  1 
ATOM   5463  O OD1 . ASP   A 1 795  ? 126.793 115.187 162.616 1.00 55.15  0  759  ASP   A OD1 1 
ATOM   5464  O OD2 . ASP   A 1 795  ? 127.446 113.679 164.072 1.00 58.77  -1 759  ASP   A OD2 1 
ATOM   5465  N N   . LEU   A 1 796  ? 124.612 116.688 161.844 1.00 30.49  0  760  LEU   A N   1 
ATOM   5466  C CA  . LEU   A 1 796  ? 123.960 116.653 160.540 1.00 35.57  0  760  LEU   A CA  1 
ATOM   5467  C C   . LEU   A 1 796  ? 123.916 115.251 159.952 1.00 35.59  0  760  LEU   A C   1 
ATOM   5468  O O   . LEU   A 1 796  ? 123.025 114.955 159.150 1.00 29.47  0  760  LEU   A O   1 
ATOM   5469  C CB  . LEU   A 1 796  ? 124.667 117.601 159.572 1.00 38.16  0  760  LEU   A CB  1 
ATOM   5470  C CG  . LEU   A 1 796  ? 124.021 117.737 158.195 1.00 33.89  0  760  LEU   A CG  1 
ATOM   5471  C CD1 . LEU   A 1 796  ? 122.557 118.038 158.350 1.00 32.96  0  760  LEU   A CD1 1 
ATOM   5472  C CD2 . LEU   A 1 796  ? 124.688 118.821 157.393 1.00 29.22  0  760  LEU   A CD2 1 
ATOM   5473  N N   . ASN   A 1 797  ? 124.853 114.383 160.330 1.00 40.17  0  761  ASN   A N   1 
ATOM   5474  C CA  . ASN   A 1 797  ? 124.861 113.023 159.813 1.00 40.17  0  761  ASN   A CA  1 
ATOM   5475  C C   . ASN   A 1 797  ? 123.788 112.149 160.444 1.00 46.10  0  761  ASN   A C   1 
ATOM   5476  O O   . ASN   A 1 797  ? 123.425 111.123 159.863 1.00 47.45  0  761  ASN   A O   1 
ATOM   5477  C CB  . ASN   A 1 797  ? 126.236 112.393 160.025 1.00 37.16  0  761  ASN   A CB  1 
ATOM   5478  C CG  . ASN   A 1 797  ? 127.279 112.948 159.079 1.00 44.74  0  761  ASN   A CG  1 
ATOM   5479  O OD1 . ASN   A 1 797  ? 126.951 113.476 158.016 1.00 50.32  0  761  ASN   A OD1 1 
ATOM   5480  N ND2 . ASN   A 1 797  ? 128.543 112.837 159.463 1.00 42.64  0  761  ASN   A ND2 1 
ATOM   5481  N N   . ASN   A 1 798  ? 123.271 112.530 161.610 1.00 39.27  0  762  ASN   A N   1 
ATOM   5482  C CA  . ASN   A 1 798  ? 122.212 111.786 162.272 1.00 28.99  0  762  ASN   A CA  1 
ATOM   5483  C C   . ASN   A 1 798  ? 120.834 112.389 162.052 1.00 26.57  0  762  ASN   A C   1 
ATOM   5484  O O   . ASN   A 1 798  ? 119.852 111.864 162.585 1.00 34.14  0  762  ASN   A O   1 
ATOM   5485  C CB  . ASN   A 1 798  ? 122.495 111.686 163.773 1.00 38.65  0  762  ASN   A CB  1 
ATOM   5486  C CG  . ASN   A 1 798  ? 123.689 110.812 164.079 1.00 38.86  0  762  ASN   A CG  1 
ATOM   5487  O OD1 . ASN   A 1 798  ? 123.905 109.790 163.431 1.00 31.44  0  762  ASN   A OD1 1 
ATOM   5488  N ND2 . ASN   A 1 798  ? 124.474 111.210 165.072 1.00 40.46  0  762  ASN   A ND2 1 
ATOM   5489  N N   . VAL   A 1 799  ? 120.731 113.478 161.289 1.00 25.49  0  763  VAL   A N   1 
ATOM   5490  C CA  . VAL   A 1 799  ? 119.428 114.048 160.986 1.00 26.18  0  763  VAL   A CA  1 
ATOM   5491  C C   . VAL   A 1 799  ? 118.660 113.094 160.085 1.00 32.50  0  763  VAL   A C   1 
ATOM   5492  O O   . VAL   A 1 799  ? 119.209 112.530 159.130 1.00 36.35  0  763  VAL   A O   1 
ATOM   5493  C CB  . VAL   A 1 799  ? 119.583 115.432 160.333 1.00 25.27  0  763  VAL   A CB  1 
ATOM   5494  C CG1 . VAL   A 1 799  ? 118.241 115.964 159.875 1.00 19.98  0  763  VAL   A CG1 1 
ATOM   5495  C CG2 . VAL   A 1 799  ? 120.225 116.398 161.303 1.00 32.34  0  763  VAL   A CG2 1 
ATOM   5496  N N   . ASP   A 1 800  ? 117.385 112.894 160.401 1.00 36.23  0  764  ASP   A N   1 
ATOM   5497  C CA  . ASP   A 1 800  ? 116.538 112.017 159.605 1.00 30.86  0  764  ASP   A CA  1 
ATOM   5498  C C   . ASP   A 1 800  ? 116.399 112.559 158.187 1.00 29.27  0  764  ASP   A C   1 
ATOM   5499  O O   . ASP   A 1 800  ? 116.152 113.752 157.988 1.00 23.18  0  764  ASP   A O   1 
ATOM   5500  C CB  . ASP   A 1 800  ? 115.168 111.881 160.267 1.00 34.92  0  764  ASP   A CB  1 
ATOM   5501  C CG  . ASP   A 1 800  ? 114.140 111.241 159.361 1.00 44.31  0  764  ASP   A CG  1 
ATOM   5502  O OD1 . ASP   A 1 800  ? 114.174 110.004 159.200 1.00 47.27  0  764  ASP   A OD1 1 
ATOM   5503  O OD2 . ASP   A 1 800  ? 113.288 111.976 158.819 1.00 46.06  -1 764  ASP   A OD2 1 
ATOM   5504  N N   . GLU   A 1 801  ? 116.566 111.678 157.204 1.00 35.61  0  765  GLU   A N   1 
ATOM   5505  C CA  . GLU   A 1 801  ? 116.438 112.074 155.808 1.00 34.59  0  765  GLU   A CA  1 
ATOM   5506  C C   . GLU   A 1 801  ? 115.026 112.560 155.522 1.00 40.50  0  765  GLU   A C   1 
ATOM   5507  O O   . GLU   A 1 801  ? 114.043 112.037 156.052 1.00 46.25  0  765  GLU   A O   1 
ATOM   5508  C CB  . GLU   A 1 801  ? 116.784 110.907 154.887 1.00 35.30  0  765  GLU   A CB  1 
ATOM   5509  C CG  . GLU   A 1 801  ? 118.264 110.743 154.620 1.00 35.80  0  765  GLU   A CG  1 
ATOM   5510  C CD  . GLU   A 1 801  ? 118.561 109.560 153.727 1.00 44.23  0  765  GLU   A CD  1 
ATOM   5511  O OE1 . GLU   A 1 801  ? 118.600 108.424 154.240 1.00 49.03  0  765  GLU   A OE1 1 
ATOM   5512  O OE2 . GLU   A 1 801  ? 118.739 109.762 152.509 1.00 43.36  -1 765  GLU   A OE2 1 
ATOM   5513  N N   . GLN   A 1 802  ? 114.928 113.569 154.670 1.00 31.26  0  766  GLN   A N   1 
ATOM   5514  C CA  . GLN   A 1 802  ? 113.659 114.246 154.437 1.00 33.88  0  766  GLN   A CA  1 
ATOM   5515  C C   . GLN   A 1 802  ? 113.780 115.041 153.148 1.00 30.49  0  766  GLN   A C   1 
ATOM   5516  O O   . GLN   A 1 802  ? 114.816 115.022 152.479 1.00 35.93  0  766  GLN   A O   1 
ATOM   5517  C CB  . GLN   A 1 802  ? 113.308 115.153 155.613 1.00 34.52  0  766  GLN   A CB  1 
ATOM   5518  C CG  . GLN   A 1 802  ? 114.368 116.200 155.887 1.00 29.90  0  766  GLN   A CG  1 
ATOM   5519  C CD  . GLN   A 1 802  ? 114.401 116.625 157.331 1.00 33.95  0  766  GLN   A CD  1 
ATOM   5520  O OE1 . GLN   A 1 802  ? 113.651 117.505 157.745 1.00 37.99  0  766  GLN   A OE1 1 
ATOM   5521  N NE2 . GLN   A 1 802  ? 115.270 116.000 158.112 1.00 30.63  0  766  GLN   A NE2 1 
ATOM   5522  N N   . SER   A 1 803  ? 112.707 115.741 152.802 1.00 28.81  0  767  SER   A N   1 
ATOM   5523  C CA  . SER   A 1 803  ? 112.773 116.704 151.715 1.00 32.40  0  767  SER   A CA  1 
ATOM   5524  C C   . SER   A 1 803  ? 113.631 117.877 152.160 1.00 39.60  0  767  SER   A C   1 
ATOM   5525  O O   . SER   A 1 803  ? 113.313 118.547 153.148 1.00 44.94  0  767  SER   A O   1 
ATOM   5526  C CB  . SER   A 1 803  ? 111.375 117.170 151.325 1.00 33.95  0  767  SER   A CB  1 
ATOM   5527  O OG  . SER   A 1 803  ? 111.430 118.095 150.254 1.00 39.65  0  767  SER   A OG  1 
ATOM   5528  N N   . GLY   A 1 804  ? 114.720 118.121 151.441 1.00 25.55  0  768  GLY   A N   1 
ATOM   5529  C CA  . GLY   A 1 804  ? 115.682 119.121 151.850 1.00 25.61  0  768  GLY   A CA  1 
ATOM   5530  C C   . GLY   A 1 804  ? 116.902 118.588 152.565 1.00 28.63  0  768  GLY   A C   1 
ATOM   5531  O O   . GLY   A 1 804  ? 117.707 119.385 153.055 1.00 36.11  0  768  GLY   A O   1 
ATOM   5532  N N   . LEU   A 1 805  ? 117.060 117.267 152.654 1.00 25.42  0  769  LEU   A N   1 
ATOM   5533  C CA  . LEU   A 1 805  ? 118.231 116.665 153.282 1.00 17.25  0  769  LEU   A CA  1 
ATOM   5534  C C   . LEU   A 1 805  ? 118.335 115.187 152.933 1.00 30.84  0  769  LEU   A C   1 
ATOM   5535  O O   . LEU   A 1 805  ? 117.432 114.413 153.260 1.00 42.57  0  769  LEU   A O   1 
ATOM   5536  C CB  . LEU   A 1 805  ? 118.169 116.837 154.797 1.00 14.10  0  769  LEU   A CB  1 
ATOM   5537  C CG  . LEU   A 1 805  ? 119.471 116.678 155.569 1.00 17.25  0  769  LEU   A CG  1 
ATOM   5538  C CD1 . LEU   A 1 805  ? 119.416 117.556 156.791 1.00 28.39  0  769  LEU   A CD1 1 
ATOM   5539  C CD2 . LEU   A 1 805  ? 119.694 115.232 155.962 1.00 22.08  0  769  LEU   A CD2 1 
ATOM   5540  N N   . TYR   A 1 806  ? 119.425 114.769 152.294 1.00 28.20  0  770  TYR   A N   1 
ATOM   5541  C CA  . TYR   A 1 806  ? 119.594 113.352 152.007 1.00 34.13  0  770  TYR   A CA  1 
ATOM   5542  C C   . TYR   A 1 806  ? 121.072 112.996 151.995 1.00 31.76  0  770  TYR   A C   1 
ATOM   5543  O O   . TYR   A 1 806  ? 121.939 113.861 151.858 1.00 42.27  0  770  TYR   A O   1 
ATOM   5544  C CB  . TYR   A 1 806  ? 118.925 112.961 150.685 1.00 33.69  0  770  TYR   A CB  1 
ATOM   5545  C CG  . TYR   A 1 806  ? 119.696 113.312 149.440 1.00 26.28  0  770  TYR   A CG  1 
ATOM   5546  C CD1 . TYR   A 1 806  ? 119.539 114.542 148.833 1.00 25.89  0  770  TYR   A CD1 1 
ATOM   5547  C CD2 . TYR   A 1 806  ? 120.558 112.400 148.856 1.00 29.64  0  770  TYR   A CD2 1 
ATOM   5548  C CE1 . TYR   A 1 806  ? 120.231 114.861 147.689 1.00 38.16  0  770  TYR   A CE1 1 
ATOM   5549  C CE2 . TYR   A 1 806  ? 121.254 112.710 147.716 1.00 26.36  0  770  TYR   A CE2 1 
ATOM   5550  C CZ  . TYR   A 1 806  ? 121.088 113.941 147.135 1.00 33.75  0  770  TYR   A CZ  1 
ATOM   5551  O OH  . TYR   A 1 806  ? 121.782 114.257 145.993 1.00 29.81  0  770  TYR   A OH  1 
ATOM   5552  N N   . ARG   A 1 807  ? 121.345 111.705 152.143 1.00 21.07  0  771  ARG   A N   1 
ATOM   5553  C CA  . ARG   A 1 807  ? 122.693 111.163 152.222 1.00 21.73  0  771  ARG   A CA  1 
ATOM   5554  C C   . ARG   A 1 807  ? 122.901 110.117 151.133 1.00 33.23  0  771  ARG   A C   1 
ATOM   5555  O O   . ARG   A 1 807  ? 122.018 109.851 150.316 1.00 36.91  0  771  ARG   A O   1 
ATOM   5556  C CB  . ARG   A 1 807  ? 122.953 110.556 153.601 1.00 20.34  0  771  ARG   A CB  1 
ATOM   5557  C CG  . ARG   A 1 807  ? 123.289 111.572 154.661 1.00 29.21  0  771  ARG   A CG  1 
ATOM   5558  C CD  . ARG   A 1 807  ? 123.575 110.920 155.998 1.00 30.27  0  771  ARG   A CD  1 
ATOM   5559  N NE  . ARG   A 1 807  ? 122.359 110.459 156.655 1.00 34.07  0  771  ARG   A NE  1 
ATOM   5560  C CZ  . ARG   A 1 807  ? 121.451 111.256 157.202 1.00 30.69  0  771  ARG   A CZ  1 
ATOM   5561  N NH1 . ARG   A 1 807  ? 121.580 112.571 157.180 1.00 21.81  1  771  ARG   A NH1 1 
ATOM   5562  N NH2 . ARG   A 1 807  ? 120.386 110.718 157.786 1.00 38.51  0  771  ARG   A NH2 1 
ATOM   5563  N N   . TYR   A 1 808  ? 124.095 109.522 151.140 1.00 48.74  0  772  TYR   A N   1 
ATOM   5564  C CA  . TYR   A 1 808  ? 124.463 108.433 150.234 1.00 40.17  0  772  TYR   A CA  1 
ATOM   5565  C C   . TYR   A 1 808  ? 124.235 108.819 148.777 1.00 35.87  0  772  TYR   A C   1 
ATOM   5566  O O   . TYR   A 1 808  ? 123.610 108.098 148.000 1.00 39.50  0  772  TYR   A O   1 
ATOM   5567  C CB  . TYR   A 1 808  ? 123.715 107.154 150.599 1.00 38.41  0  772  TYR   A CB  1 
ATOM   5568  C CG  . TYR   A 1 808  ? 123.878 106.812 152.054 1.00 41.92  0  772  TYR   A CG  1 
ATOM   5569  C CD1 . TYR   A 1 808  ? 125.135 106.582 152.588 1.00 37.87  0  772  TYR   A CD1 1 
ATOM   5570  C CD2 . TYR   A 1 808  ? 122.787 106.750 152.901 1.00 41.93  0  772  TYR   A CD2 1 
ATOM   5571  C CE1 . TYR   A 1 808  ? 125.299 106.282 153.919 1.00 40.31  0  772  TYR   A CE1 1 
ATOM   5572  C CE2 . TYR   A 1 808  ? 122.941 106.452 154.234 1.00 44.52  0  772  TYR   A CE2 1 
ATOM   5573  C CZ  . TYR   A 1 808  ? 124.198 106.218 154.739 1.00 46.07  0  772  TYR   A CZ  1 
ATOM   5574  O OH  . TYR   A 1 808  ? 124.358 105.918 156.070 1.00 48.31  0  772  TYR   A OH  1 
ATOM   5575  N N   . HIS   A 1 809  ? 124.769 109.982 148.413 1.00 33.95  0  773  HIS   A N   1 
ATOM   5576  C CA  . HIS   A 1 809  ? 124.658 110.521 147.061 1.00 33.39  0  773  HIS   A CA  1 
ATOM   5577  C C   . HIS   A 1 809  ? 125.805 109.956 146.230 1.00 34.38  0  773  HIS   A C   1 
ATOM   5578  O O   . HIS   A 1 809  ? 126.903 110.507 146.159 1.00 35.05  0  773  HIS   A O   1 
ATOM   5579  C CB  . HIS   A 1 809  ? 124.665 112.042 147.117 1.00 43.25  0  773  HIS   A CB  1 
ATOM   5580  C CG  . HIS   A 1 809  ? 124.858 112.720 145.799 1.00 39.57  0  773  HIS   A CG  1 
ATOM   5581  N ND1 . HIS   A 1 809  ? 123.806 113.177 145.038 1.00 35.23  0  773  HIS   A ND1 1 
ATOM   5582  C CD2 . HIS   A 1 809  ? 125.982 113.080 145.138 1.00 36.72  0  773  HIS   A CD2 1 
ATOM   5583  C CE1 . HIS   A 1 809  ? 124.273 113.761 143.951 1.00 32.49  0  773  HIS   A CE1 1 
ATOM   5584  N NE2 . HIS   A 1 809  ? 125.590 113.711 143.984 1.00 34.88  0  773  HIS   A NE2 1 
ATOM   5585  N N   . MET   A 1 810  ? 125.542 108.809 145.610 1.00 46.24  0  774  MET   A N   1 
ATOM   5586  C CA  . MET   A 1 810  ? 126.521 108.175 144.737 1.00 43.90  0  774  MET   A CA  1 
ATOM   5587  C C   . MET   A 1 810  ? 126.426 108.796 143.354 1.00 46.25  0  774  MET   A C   1 
ATOM   5588  O O   . MET   A 1 810  ? 125.485 108.518 142.605 1.00 57.39  0  774  MET   A O   1 
ATOM   5589  C CB  . MET   A 1 810  ? 126.290 106.670 144.665 1.00 37.58  0  774  MET   A CB  1 
ATOM   5590  C CG  . MET   A 1 810  ? 125.891 106.044 145.974 1.00 40.76  0  774  MET   A CG  1 
ATOM   5591  S SD  . MET   A 1 810  ? 127.209 106.179 147.182 1.00 45.14  0  774  MET   A SD  1 
ATOM   5592  C CE  . MET   A 1 810  ? 128.566 105.496 146.244 1.00 46.30  0  774  MET   A CE  1 
ATOM   5593  N N   . GLY   A 1 811  ? 127.401 109.625 143.011 1.00 27.61  0  775  GLY   A N   1 
ATOM   5594  C CA  . GLY   A 1 811  ? 127.356 110.352 141.764 1.00 25.72  0  775  GLY   A CA  1 
ATOM   5595  C C   . GLY   A 1 811  ? 128.101 111.659 141.877 1.00 27.71  0  775  GLY   A C   1 
ATOM   5596  O O   . GLY   A 1 811  ? 128.689 111.952 142.921 1.00 33.50  0  775  GLY   A O   1 
ATOM   5597  N N   . GLY   A 1 812  ? 128.093 112.452 140.817 1.00 30.84  0  776  GLY   A N   1 
ATOM   5598  C CA  . GLY   A 1 812  ? 128.813 113.706 140.794 1.00 35.64  0  776  GLY   A CA  1 
ATOM   5599  C C   . GLY   A 1 812  ? 127.896 114.885 141.050 1.00 38.29  0  776  GLY   A C   1 
ATOM   5600  O O   . GLY   A 1 812  ? 126.698 114.827 140.795 1.00 43.65  0  776  GLY   A O   1 
ATOM   5601  N N   . ILE   A 1 813  ? 128.477 115.957 141.568 1.00 34.72  0  777  ILE   A N   1 
ATOM   5602  C CA  . ILE   A 1 813  ? 127.757 117.206 141.764 1.00 36.09  0  777  ILE   A CA  1 
ATOM   5603  C C   . ILE   A 1 813  ? 128.068 118.123 140.594 1.00 38.11  0  777  ILE   A C   1 
ATOM   5604  O O   . ILE   A 1 813  ? 129.230 118.259 140.194 1.00 37.64  0  777  ILE   A O   1 
ATOM   5605  C CB  . ILE   A 1 813  ? 128.133 117.859 143.102 1.00 37.26  0  777  ILE   A CB  1 
ATOM   5606  C CG1 . ILE   A 1 813  ? 127.585 117.036 144.266 1.00 31.77  0  777  ILE   A CG1 1 
ATOM   5607  C CG2 . ILE   A 1 813  ? 127.596 119.266 143.168 1.00 38.81  0  777  ILE   A CG2 1 
ATOM   5608  C CD1 . ILE   A 1 813  ? 128.623 116.220 144.960 1.00 34.09  0  777  ILE   A CD1 1 
ATOM   5609  N N   . GLU   A 1 814  ? 127.030 118.740 140.036 1.00 40.92  0  778  GLU   A N   1 
ATOM   5610  C CA  . GLU   A 1 814  ? 127.185 119.556 138.841 1.00 41.26  0  778  GLU   A CA  1 
ATOM   5611  C C   . GLU   A 1 814  ? 128.211 120.658 139.068 1.00 44.86  0  778  GLU   A C   1 
ATOM   5612  O O   . GLU   A 1 814  ? 128.188 121.346 140.092 1.00 45.13  0  778  GLU   A O   1 
ATOM   5613  C CB  . GLU   A 1 814  ? 125.837 120.157 138.445 1.00 43.39  0  778  GLU   A CB  1 
ATOM   5614  C CG  . GLU   A 1 814  ? 125.926 121.495 137.741 1.00 50.03  0  778  GLU   A CG  1 
ATOM   5615  C CD  . GLU   A 1 814  ? 124.695 121.797 136.915 1.00 53.81  0  778  GLU   A CD  1 
ATOM   5616  O OE1 . GLU   A 1 814  ? 124.663 122.860 136.259 1.00 54.03  0  778  GLU   A OE1 1 
ATOM   5617  O OE2 . GLU   A 1 814  ? 123.758 120.972 136.923 1.00 50.08  -1 778  GLU   A OE2 1 
ATOM   5618  N N   . GLY   A 1 815  ? 129.121 120.814 138.105 1.00 34.50  0  779  GLY   A N   1 
ATOM   5619  C CA  . GLY   A 1 815  ? 130.170 121.801 138.154 1.00 31.15  0  779  GLY   A CA  1 
ATOM   5620  C C   . GLY   A 1 815  ? 131.509 121.262 138.615 1.00 35.06  0  779  GLY   A C   1 
ATOM   5621  O O   . GLY   A 1 815  ? 132.545 121.657 138.072 1.00 38.42  0  779  GLY   A O   1 
ATOM   5622  N N   . TRP   A 1 816  ? 131.511 120.373 139.603 1.00 35.22  0  780  TRP   A N   1 
ATOM   5623  C CA  . TRP   A 1 816  ? 132.749 119.788 140.091 1.00 29.12  0  780  TRP   A CA  1 
ATOM   5624  C C   . TRP   A 1 816  ? 133.189 118.667 139.161 1.00 36.21  0  780  TRP   A C   1 
ATOM   5625  O O   . TRP   A 1 816  ? 132.369 117.868 138.705 1.00 41.32  0  780  TRP   A O   1 
ATOM   5626  C CB  . TRP   A 1 816  ? 132.567 119.246 141.508 1.00 24.88  0  780  TRP   A CB  1 
ATOM   5627  C CG  . TRP   A 1 816  ? 132.005 120.234 142.479 1.00 28.22  0  780  TRP   A CG  1 
ATOM   5628  C CD1 . TRP   A 1 816  ? 131.836 121.571 142.288 1.00 31.50  0  780  TRP   A CD1 1 
ATOM   5629  C CD2 . TRP   A 1 816  ? 131.539 119.958 143.801 1.00 25.30  0  780  TRP   A CD2 1 
ATOM   5630  N NE1 . TRP   A 1 816  ? 131.290 122.144 143.407 1.00 24.78  0  780  TRP   A NE1 1 
ATOM   5631  C CE2 . TRP   A 1 816  ? 131.101 121.172 144.352 1.00 22.91  0  780  TRP   A CE2 1 
ATOM   5632  C CE3 . TRP   A 1 816  ? 131.451 118.800 144.573 1.00 28.78  0  780  TRP   A CE3 1 
ATOM   5633  C CZ2 . TRP   A 1 816  ? 130.583 121.261 145.633 1.00 29.77  0  780  TRP   A CZ2 1 
ATOM   5634  C CZ3 . TRP   A 1 816  ? 130.938 118.891 145.843 1.00 28.92  0  780  TRP   A CZ3 1 
ATOM   5635  C CH2 . TRP   A 1 816  ? 130.509 120.111 146.362 1.00 32.42  0  780  TRP   A CH2 1 
ATOM   5636  N N   . CYS   A 1 817  ? 134.489 118.617 138.874 1.00 38.87  0  781  CYS   A N   1 
ATOM   5637  C CA  . CYS   A 1 817  ? 135.063 117.613 137.977 1.00 35.32  0  781  CYS   A CA  1 
ATOM   5638  C C   . CYS   A 1 817  ? 134.413 117.644 136.597 1.00 26.58  0  781  CYS   A C   1 
ATOM   5639  O O   . CYS   A 1 817  ? 134.270 116.610 135.946 1.00 33.41  0  781  CYS   A O   1 
ATOM   5640  C CB  . CYS   A 1 817  ? 134.962 116.208 138.575 1.00 39.18  0  781  CYS   A CB  1 
ATOM   5641  S SG  . CYS   A 1 817  ? 135.890 115.971 140.098 1.00 55.51  0  781  CYS   A SG  1 
ATOM   5642  N N   . GLN   A 1 818  ? 134.011 118.830 136.140 1.00 25.07  0  782  GLN   A N   1 
ATOM   5643  C CA  . GLN   A 1 818  ? 133.393 118.947 134.824 1.00 33.04  0  782  GLN   A CA  1 
ATOM   5644  C C   . GLN   A 1 818  ? 134.379 118.600 133.717 1.00 43.54  0  782  GLN   A C   1 
ATOM   5645  O O   . GLN   A 1 818  ? 134.012 117.963 132.721 1.00 45.50  0  782  GLN   A O   1 
ATOM   5646  C CB  . GLN   A 1 818  ? 132.842 120.359 134.632 1.00 35.58  0  782  GLN   A CB  1 
ATOM   5647  C CG  . GLN   A 1 818  ? 132.177 120.592 133.293 1.00 36.33  0  782  GLN   A CG  1 
ATOM   5648  C CD  . GLN   A 1 818  ? 130.840 119.897 133.187 1.00 47.83  0  782  GLN   A CD  1 
ATOM   5649  O OE1 . GLN   A 1 818  ? 130.050 119.901 134.131 1.00 45.77  0  782  GLN   A OE1 1 
ATOM   5650  N NE2 . GLN   A 1 818  ? 130.577 119.293 132.036 1.00 48.47  0  782  GLN   A NE2 1 
ATOM   5651  N N   . LYS   A 1 819  ? 135.636 119.024 133.868 1.00 36.61  0  783  LYS   A N   1 
ATOM   5652  C CA  . LYS   A 1 819  ? 136.650 118.721 132.863 1.00 30.89  0  783  LYS   A CA  1 
ATOM   5653  C C   . LYS   A 1 819  ? 136.893 117.223 132.757 1.00 32.03  0  783  LYS   A C   1 
ATOM   5654  O O   . LYS   A 1 819  ? 137.049 116.692 131.652 1.00 47.23  0  783  LYS   A O   1 
ATOM   5655  C CB  . LYS   A 1 819  ? 137.949 119.453 133.194 1.00 35.35  0  783  LYS   A CB  1 
ATOM   5656  C CG  . LYS   A 1 819  ? 137.827 120.965 133.188 1.00 35.17  0  783  LYS   A CG  1 
ATOM   5657  C CD  . LYS   A 1 819  ? 137.371 121.462 131.831 1.00 39.80  0  783  LYS   A CD  1 
ATOM   5658  C CE  . LYS   A 1 819  ? 137.405 122.974 131.754 1.00 39.46  0  783  LYS   A CE  1 
ATOM   5659  N NZ  . LYS   A 1 819  ? 136.931 123.454 130.427 1.00 38.67  1  783  LYS   A NZ  1 
ATOM   5660  N N   . LEU   A 1 820  ? 136.932 116.526 133.894 1.00 23.86  0  784  LEU   A N   1 
ATOM   5661  C CA  . LEU   A 1 820  ? 137.134 115.083 133.867 1.00 22.83  0  784  LEU   A CA  1 
ATOM   5662  C C   . LEU   A 1 820  ? 136.010 114.384 133.119 1.00 25.68  0  784  LEU   A C   1 
ATOM   5663  O O   . LEU   A 1 820  ? 136.256 113.474 132.321 1.00 46.07  0  784  LEU   A O   1 
ATOM   5664  C CB  . LEU   A 1 820  ? 137.245 114.543 135.289 1.00 22.35  0  784  LEU   A CB  1 
ATOM   5665  C CG  . LEU   A 1 820  ? 137.353 113.028 135.421 1.00 25.24  0  784  LEU   A CG  1 
ATOM   5666  C CD1 . LEU   A 1 820  ? 138.593 112.530 134.714 1.00 30.76  0  784  LEU   A CD1 1 
ATOM   5667  C CD2 . LEU   A 1 820  ? 137.378 112.630 136.881 1.00 29.21  0  784  LEU   A CD2 1 
ATOM   5668  N N   . TRP   A 1 821  ? 134.767 114.800 133.353 1.00 25.83  0  785  TRP   A N   1 
ATOM   5669  C CA  . TRP   A 1 821  ? 133.647 114.170 132.666 1.00 31.29  0  785  TRP   A CA  1 
ATOM   5670  C C   . TRP   A 1 821  ? 133.628 114.515 131.184 1.00 32.53  0  785  TRP   A C   1 
ATOM   5671  O O   . TRP   A 1 821  ? 133.245 113.676 130.367 1.00 43.03  0  785  TRP   A O   1 
ATOM   5672  C CB  . TRP   A 1 821  ? 132.336 114.567 133.336 1.00 34.20  0  785  TRP   A CB  1 
ATOM   5673  C CG  . TRP   A 1 821  ? 132.261 114.106 134.750 1.00 30.78  0  785  TRP   A CG  1 
ATOM   5674  C CD1 . TRP   A 1 821  ? 132.839 112.991 135.276 1.00 33.15  0  785  TRP   A CD1 1 
ATOM   5675  C CD2 . TRP   A 1 821  ? 131.590 114.757 135.830 1.00 33.35  0  785  TRP   A CD2 1 
ATOM   5676  N NE1 . TRP   A 1 821  ? 132.560 112.899 136.616 1.00 33.30  0  785  TRP   A NE1 1 
ATOM   5677  C CE2 . TRP   A 1 821  ? 131.794 113.974 136.981 1.00 35.03  0  785  TRP   A CE2 1 
ATOM   5678  C CE3 . TRP   A 1 821  ? 130.830 115.924 135.935 1.00 36.29  0  785  TRP   A CE3 1 
ATOM   5679  C CZ2 . TRP   A 1 821  ? 131.267 114.319 138.218 1.00 35.42  0  785  TRP   A CZ2 1 
ATOM   5680  C CZ3 . TRP   A 1 821  ? 130.309 116.263 137.162 1.00 35.96  0  785  TRP   A CZ3 1 
ATOM   5681  C CH2 . TRP   A 1 821  ? 130.529 115.466 138.288 1.00 30.54  0  785  TRP   A CH2 1 
ATOM   5682  N N   . THR   A 1 822  ? 134.034 115.730 130.811 1.00 25.38  0  786  THR   A N   1 
ATOM   5683  C CA  . THR   A 1 822  ? 134.147 116.052 129.390 1.00 35.35  0  786  THR   A CA  1 
ATOM   5684  C C   . THR   A 1 822  ? 135.208 115.189 128.713 1.00 37.04  0  786  THR   A C   1 
ATOM   5685  O O   . THR   A 1 822  ? 135.003 114.688 127.598 1.00 40.21  0  786  THR   A O   1 
ATOM   5686  C CB  . THR   A 1 822  ? 134.466 117.535 129.216 1.00 37.94  0  786  THR   A CB  1 
ATOM   5687  O OG1 . THR   A 1 822  ? 133.371 118.319 129.705 1.00 36.12  0  786  THR   A OG1 1 
ATOM   5688  C CG2 . THR   A 1 822  ? 134.703 117.864 127.757 1.00 32.38  0  786  THR   A CG2 1 
ATOM   5689  N N   . ILE   A 1 823  ? 136.344 114.997 129.383 1.00 31.40  0  787  ILE   A N   1 
ATOM   5690  C CA  . ILE   A 1 823  ? 137.396 114.128 128.865 1.00 24.95  0  787  ILE   A CA  1 
ATOM   5691  C C   . ILE   A 1 823  ? 136.878 112.705 128.701 1.00 31.94  0  787  ILE   A C   1 
ATOM   5692  O O   . ILE   A 1 823  ? 137.121 112.042 127.684 1.00 37.12  0  787  ILE   A O   1 
ATOM   5693  C CB  . ILE   A 1 823  ? 138.616 114.179 129.800 1.00 18.82  0  787  ILE   A CB  1 
ATOM   5694  C CG1 . ILE   A 1 823  ? 139.441 115.434 129.538 1.00 21.37  0  787  ILE   A CG1 1 
ATOM   5695  C CG2 . ILE   A 1 823  ? 139.444 112.940 129.671 1.00 31.66  0  787  ILE   A CG2 1 
ATOM   5696  C CD1 . ILE   A 1 823  ? 140.578 115.591 130.496 1.00 30.68  0  787  ILE   A CD1 1 
ATOM   5697  N N   . GLU   A 1 824  ? 136.158 112.217 129.709 1.00 32.45  0  788  GLU   A N   1 
ATOM   5698  C CA  . GLU   A 1 824  ? 135.595 110.875 129.664 1.00 28.92  0  788  GLU   A CA  1 
ATOM   5699  C C   . GLU   A 1 824  ? 134.580 110.726 128.536 1.00 38.91  0  788  GLU   A C   1 
ATOM   5700  O O   . GLU   A 1 824  ? 134.532 109.682 127.877 1.00 45.85  0  788  GLU   A O   1 
ATOM   5701  C CB  . GLU   A 1 824  ? 134.959 110.568 131.013 1.00 28.68  0  788  GLU   A CB  1 
ATOM   5702  C CG  . GLU   A 1 824  ? 134.918 109.121 131.388 1.00 42.73  0  788  GLU   A CG  1 
ATOM   5703  C CD  . GLU   A 1 824  ? 134.776 108.947 132.881 1.00 52.22  0  788  GLU   A CD  1 
ATOM   5704  O OE1 . GLU   A 1 824  ? 135.516 109.621 133.628 1.00 39.75  0  788  GLU   A OE1 1 
ATOM   5705  O OE2 . GLU   A 1 824  ? 133.910 108.159 133.309 1.00 53.52  -1 788  GLU   A OE2 1 
ATOM   5706  N N   . ALA   A 1 825  ? 133.765 111.754 128.300 1.00 30.55  0  789  ALA   A N   1 
ATOM   5707  C CA  . ALA   A 1 825  ? 132.826 111.721 127.187 1.00 30.79  0  789  ALA   A CA  1 
ATOM   5708  C C   . ALA   A 1 825  ? 133.550 111.673 125.849 1.00 35.95  0  789  ALA   A C   1 
ATOM   5709  O O   . ALA   A 1 825  ? 133.123 110.963 124.934 1.00 45.36  0  789  ALA   A O   1 
ATOM   5710  C CB  . ALA   A 1 825  ? 131.898 112.930 127.247 1.00 31.45  0  789  ALA   A CB  1 
ATOM   5711  N N   . ILE   A 1 826  ? 134.638 112.431 125.706 1.00 27.87  0  790  ILE   A N   1 
ATOM   5712  C CA  . ILE   A 1 826  ? 135.400 112.377 124.459 1.00 26.49  0  790  ILE   A CA  1 
ATOM   5713  C C   . ILE   A 1 826  ? 135.998 110.988 124.253 1.00 35.33  0  790  ILE   A C   1 
ATOM   5714  O O   . ILE   A 1 826  ? 136.001 110.452 123.134 1.00 37.97  0  790  ILE   A O   1 
ATOM   5715  C CB  . ILE   A 1 826  ? 136.479 113.472 124.441 1.00 35.48  0  790  ILE   A CB  1 
ATOM   5716  C CG1 . ILE   A 1 826  ? 135.832 114.844 124.285 1.00 38.84  0  790  ILE   A CG1 1 
ATOM   5717  C CG2 . ILE   A 1 826  ? 137.455 113.239 123.320 1.00 40.19  0  790  ILE   A CG2 1 
ATOM   5718  C CD1 . ILE   A 1 826  ? 136.812 115.975 124.335 1.00 39.22  0  790  ILE   A CD1 1 
ATOM   5719  N N   . SER   A 1 827  ? 136.507 110.381 125.326 1.00 32.95  0  791  SER   A N   1 
ATOM   5720  C CA  . SER   A 1 827  ? 137.025 109.020 125.230 1.00 30.24  0  791  SER   A CA  1 
ATOM   5721  C C   . SER   A 1 827  ? 135.934 108.050 124.793 1.00 38.18  0  791  SER   A C   1 
ATOM   5722  O O   . SER   A 1 827  ? 136.155 107.187 123.931 1.00 44.59  0  791  SER   A O   1 
ATOM   5723  C CB  . SER   A 1 827  ? 137.614 108.597 126.573 1.00 31.70  0  791  SER   A CB  1 
ATOM   5724  O OG  . SER   A 1 827  ? 138.549 109.554 127.031 1.00 36.24  0  791  SER   A OG  1 
ATOM   5725  N N   . LEU   A 1 828  ? 134.739 108.186 125.373 1.00 37.53  0  792  LEU   A N   1 
ATOM   5726  C CA  . LEU   A 1 828  ? 133.620 107.347 124.961 1.00 39.96  0  792  LEU   A CA  1 
ATOM   5727  C C   . LEU   A 1 828  ? 133.277 107.543 123.495 1.00 34.45  0  792  LEU   A C   1 
ATOM   5728  O O   . LEU   A 1 828  ? 132.938 106.582 122.799 1.00 36.84  0  792  LEU   A O   1 
ATOM   5729  C CB  . LEU   A 1 828  ? 132.382 107.637 125.798 1.00 34.36  0  792  LEU   A CB  1 
ATOM   5730  C CG  . LEU   A 1 828  ? 131.373 106.511 125.588 1.00 35.69  0  792  LEU   A CG  1 
ATOM   5731  C CD1 . LEU   A 1 828  ? 132.006 105.135 125.761 1.00 37.51  0  792  LEU   A CD1 1 
ATOM   5732  C CD2 . LEU   A 1 828  ? 130.154 106.685 126.431 1.00 38.42  0  792  LEU   A CD2 1 
ATOM   5733  N N   . LEU   A 1 829  ? 133.294 108.785 123.021 1.00 33.20  0  793  LEU   A N   1 
ATOM   5734  C CA  . LEU   A 1 829  ? 132.958 109.026 121.624 1.00 39.01  0  793  LEU   A CA  1 
ATOM   5735  C C   . LEU   A 1 829  ? 133.983 108.381 120.703 1.00 43.83  0  793  LEU   A C   1 
ATOM   5736  O O   . LEU   A 1 829  ? 133.630 107.850 119.643 1.00 42.02  0  793  LEU   A O   1 
ATOM   5737  C CB  . LEU   A 1 829  ? 132.840 110.523 121.357 1.00 40.05  0  793  LEU   A CB  1 
ATOM   5738  C CG  . LEU   A 1 829  ? 131.423 111.099 121.440 1.00 35.75  0  793  LEU   A CG  1 
ATOM   5739  C CD1 . LEU   A 1 829  ? 130.500 110.415 120.452 1.00 37.75  0  793  LEU   A CD1 1 
ATOM   5740  C CD2 . LEU   A 1 829  ? 130.853 110.999 122.842 1.00 40.59  0  793  LEU   A CD2 1 
ATOM   5741  N N   . ASP   A 1 830  ? 135.258 108.399 121.097 1.00 45.73  0  794  ASP   A N   1 
ATOM   5742  C CA  . ASP   A 1 830  ? 136.268 107.673 120.328 1.00 45.13  0  794  ASP   A CA  1 
ATOM   5743  C C   . ASP   A 1 830  ? 135.981 106.175 120.315 1.00 38.36  0  794  ASP   A C   1 
ATOM   5744  O O   . ASP   A 1 830  ? 136.094 105.518 119.271 1.00 41.44  0  794  ASP   A O   1 
ATOM   5745  C CB  . ASP   A 1 830  ? 137.659 107.937 120.900 1.00 50.24  0  794  ASP   A CB  1 
ATOM   5746  C CG  . ASP   A 1 830  ? 138.267 109.218 120.379 1.00 55.39  0  794  ASP   A CG  1 
ATOM   5747  O OD1 . ASP   A 1 830  ? 137.662 109.847 119.485 1.00 55.85  0  794  ASP   A OD1 1 
ATOM   5748  O OD2 . ASP   A 1 830  ? 139.355 109.591 120.862 1.00 52.19  -1 794  ASP   A OD2 1 
ATOM   5749  N N   . LEU   A 1 831  ? 135.610 105.618 121.469 1.00 40.79  0  795  LEU   A N   1 
ATOM   5750  C CA  . LEU   A 1 831  ? 135.300 104.192 121.537 1.00 41.80  0  795  LEU   A CA  1 
ATOM   5751  C C   . LEU   A 1 831  ? 134.100 103.840 120.662 1.00 44.00  0  795  LEU   A C   1 
ATOM   5752  O O   . LEU   A 1 831  ? 134.090 102.799 119.995 1.00 48.61  0  795  LEU   A O   1 
ATOM   5753  C CB  . LEU   A 1 831  ? 135.048 103.788 122.987 1.00 42.73  0  795  LEU   A CB  1 
ATOM   5754  C CG  . LEU   A 1 831  ? 134.402 102.433 123.240 1.00 42.54  0  795  LEU   A CG  1 
ATOM   5755  C CD1 . LEU   A 1 831  ? 135.283 101.318 122.719 1.00 40.24  0  795  LEU   A CD1 1 
ATOM   5756  C CD2 . LEU   A 1 831  ? 134.153 102.268 124.721 1.00 43.99  0  795  LEU   A CD2 1 
ATOM   5757  N N   . ILE   A 1 832  ? 133.078 104.694 120.659 1.00 46.95  0  796  ILE   A N   1 
ATOM   5758  C CA  . ILE   A 1 832  ? 131.910 104.476 119.810 1.00 38.36  0  796  ILE   A CA  1 
ATOM   5759  C C   . ILE   A 1 832  ? 132.298 104.551 118.339 1.00 41.78  0  796  ILE   A C   1 
ATOM   5760  O O   . ILE   A 1 832  ? 131.834 103.749 117.521 1.00 42.50  0  796  ILE   A O   1 
ATOM   5761  C CB  . ILE   A 1 832  ? 130.803 105.486 120.158 1.00 43.05  0  796  ILE   A CB  1 
ATOM   5762  C CG1 . ILE   A 1 832  ? 130.030 105.026 121.391 1.00 45.61  0  796  ILE   A CG1 1 
ATOM   5763  C CG2 . ILE   A 1 832  ? 129.866 105.693 118.981 1.00 45.95  0  796  ILE   A CG2 1 
ATOM   5764  C CD1 . ILE   A 1 832  ? 129.189 106.111 122.017 1.00 46.15  0  796  ILE   A CD1 1 
ATOM   5765  N N   . SER   A 1 833  ? 133.149 105.515 117.978 1.00 46.34  0  797  SER   A N   1 
ATOM   5766  C CA  . SER   A 1 833  ? 133.633 105.597 116.604 1.00 47.10  0  797  SER   A CA  1 
ATOM   5767  C C   . SER   A 1 833  ? 134.346 104.317 116.200 1.00 43.82  0  797  SER   A C   1 
ATOM   5768  O O   . SER   A 1 833  ? 134.208 103.850 115.064 1.00 38.92  0  797  SER   A O   1 
ATOM   5769  C CB  . SER   A 1 833  ? 134.567 106.794 116.446 1.00 50.01  0  797  SER   A CB  1 
ATOM   5770  O OG  . SER   A 1 833  ? 135.258 106.735 115.211 1.00 53.97  0  797  SER   A OG  1 
ATOM   5771  N N   . LEU   A 1 834  ? 135.125 103.743 117.116 1.00 51.75  0  798  LEU   A N   1 
ATOM   5772  C CA  . LEU   A 1 834  ? 135.746 102.451 116.845 1.00 45.75  0  798  LEU   A CA  1 
ATOM   5773  C C   . LEU   A 1 834  ? 134.697 101.362 116.654 1.00 46.07  0  798  LEU   A C   1 
ATOM   5774  O O   . LEU   A 1 834  ? 134.815 100.528 115.749 1.00 48.62  0  798  LEU   A O   1 
ATOM   5775  C CB  . LEU   A 1 834  ? 136.701 102.078 117.977 1.00 47.05  0  798  LEU   A CB  1 
ATOM   5776  C CG  . LEU   A 1 834  ? 137.064 100.598 118.044 1.00 44.88  0  798  LEU   A CG  1 
ATOM   5777  C CD1 . LEU   A 1 834  ? 137.971 100.244 116.890 1.00 51.21  0  798  LEU   A CD1 1 
ATOM   5778  C CD2 . LEU   A 1 834  ? 137.721 100.258 119.361 1.00 47.65  0  798  LEU   A CD2 1 
ATOM   5779  N N   . LYS   A 1 835  ? 133.660 101.355 117.494 1.00 51.52  0  799  LYS   A N   1 
ATOM   5780  C CA  . LYS   A 1 835  ? 132.639 100.314 117.428 1.00 50.75  0  799  LYS   A CA  1 
ATOM   5781  C C   . LYS   A 1 835  ? 131.645 100.516 116.291 1.00 52.57  0  799  LYS   A C   1 
ATOM   5782  O O   . LYS   A 1 835  ? 130.917 99.578  115.952 1.00 50.01  0  799  LYS   A O   1 
ATOM   5783  C CB  . LYS   A 1 835  ? 131.876 100.239 118.752 1.00 49.59  0  799  LYS   A CB  1 
ATOM   5784  C CG  . LYS   A 1 835  ? 132.715 99.774  119.925 1.00 51.65  0  799  LYS   A CG  1 
ATOM   5785  C CD  . LYS   A 1 835  ? 131.875 99.606  121.176 1.00 50.99  0  799  LYS   A CD  1 
ATOM   5786  C CE  . LYS   A 1 835  ? 131.157 98.271  121.180 1.00 48.97  0  799  LYS   A CE  1 
ATOM   5787  N NZ  . LYS   A 1 835  ? 130.600 97.948  122.522 1.00 53.55  1  799  LYS   A NZ  1 
ATOM   5788  N N   . GLY   A 1 836  ? 131.591 101.705 115.700 1.00 56.31  0  800  GLY   A N   1 
ATOM   5789  C CA  . GLY   A 1 836  ? 130.608 101.978 114.670 1.00 50.86  0  800  GLY   A CA  1 
ATOM   5790  C C   . GLY   A 1 836  ? 131.186 102.090 113.278 1.00 52.96  0  800  GLY   A C   1 
ATOM   5791  O O   . GLY   A 1 836  ? 130.444 102.252 112.306 1.00 52.64  0  800  GLY   A O   1 
ATOM   5792  N N   . LYS   A 1 837  ? 132.512 102.001 113.175 1.00 61.26  0  801  LYS   A N   1 
ATOM   5793  C CA  . LYS   A 1 837  ? 133.216 102.063 111.894 1.00 61.82  0  801  LYS   A CA  1 
ATOM   5794  C C   . LYS   A 1 837  ? 132.867 103.333 111.122 1.00 63.92  0  801  LYS   A C   1 
ATOM   5795  O O   . LYS   A 1 837  ? 132.668 103.310 109.907 1.00 66.68  0  801  LYS   A O   1 
ATOM   5796  C CB  . LYS   A 1 837  ? 132.930 100.822 111.044 1.00 59.85  0  801  LYS   A CB  1 
ATOM   5797  C CG  . LYS   A 1 837  ? 132.835 99.520  111.825 1.00 61.93  0  801  LYS   A CG  1 
ATOM   5798  C CD  . LYS   A 1 837  ? 134.155 99.163  112.483 1.00 62.26  0  801  LYS   A CD  1 
ATOM   5799  C CE  . LYS   A 1 837  ? 134.022 97.909  113.328 1.00 60.85  0  801  LYS   A CE  1 
ATOM   5800  N NZ  . LYS   A 1 837  ? 135.284 97.590  114.046 1.00 63.44  1  801  LYS   A NZ  1 
ATOM   5801  N N   . PHE   A 1 838  ? 132.787 104.457 111.833 1.00 56.26  0  802  PHE   A N   1 
ATOM   5802  C CA  . PHE   A 1 838  ? 132.565 105.747 111.196 1.00 51.07  0  802  PHE   A CA  1 
ATOM   5803  C C   . PHE   A 1 838  ? 133.523 106.781 111.766 1.00 54.65  0  802  PHE   A C   1 
ATOM   5804  O O   . PHE   A 1 838  ? 133.895 106.717 112.940 1.00 61.30  0  802  PHE   A O   1 
ATOM   5805  C CB  . PHE   A 1 838  ? 131.106 106.229 111.353 1.00 56.71  0  802  PHE   A CB  1 
ATOM   5806  C CG  . PHE   A 1 838  ? 130.554 106.117 112.752 1.00 60.33  0  802  PHE   A CG  1 
ATOM   5807  C CD1 . PHE   A 1 838  ? 131.011 106.938 113.768 1.00 56.83  0  802  PHE   A CD1 1 
ATOM   5808  C CD2 . PHE   A 1 838  ? 129.542 105.219 113.036 1.00 57.64  0  802  PHE   A CD2 1 
ATOM   5809  C CE1 . PHE   A 1 838  ? 130.493 106.842 115.040 1.00 55.94  0  802  PHE   A CE1 1 
ATOM   5810  C CE2 . PHE   A 1 838  ? 129.020 105.122 114.308 1.00 51.82  0  802  PHE   A CE2 1 
ATOM   5811  C CZ  . PHE   A 1 838  ? 129.497 105.935 115.310 1.00 52.56  0  802  PHE   A CZ  1 
ATOM   5812  N N   . SER   A 1 839  ? 133.931 107.723 110.921 1.00 58.49  0  803  SER   A N   1 
ATOM   5813  C CA  . SER   A 1 839  ? 134.734 108.846 111.381 1.00 61.35  0  803  SER   A CA  1 
ATOM   5814  C C   . SER   A 1 839  ? 133.871 109.806 112.189 1.00 57.29  0  803  SER   A C   1 
ATOM   5815  O O   . SER   A 1 839  ? 132.692 110.015 111.894 1.00 62.44  0  803  SER   A O   1 
ATOM   5816  C CB  . SER   A 1 839  ? 135.369 109.573 110.198 1.00 62.51  0  803  SER   A CB  1 
ATOM   5817  O OG  . SER   A 1 839  ? 136.069 110.727 110.628 1.00 64.84  0  803  SER   A OG  1 
ATOM   5818  N N   . ILE   A 1 840  ? 134.472 110.399 113.220 1.00 50.03  0  804  ILE   A N   1 
ATOM   5819  C CA  . ILE   A 1 840  ? 133.728 111.153 114.218 1.00 53.12  0  804  ILE   A CA  1 
ATOM   5820  C C   . ILE   A 1 840  ? 134.430 112.478 114.493 1.00 56.83  0  804  ILE   A C   1 
ATOM   5821  O O   . ILE   A 1 840  ? 135.631 112.634 114.262 1.00 59.92  0  804  ILE   A O   1 
ATOM   5822  C CB  . ILE   A 1 840  ? 133.564 110.335 115.517 1.00 51.95  0  804  ILE   A CB  1 
ATOM   5823  C CG1 . ILE   A 1 840  ? 132.310 110.756 116.269 1.00 50.50  0  804  ILE   A CG1 1 
ATOM   5824  C CG2 . ILE   A 1 840  ? 134.783 110.488 116.407 1.00 58.94  0  804  ILE   A CG2 1 
ATOM   5825  C CD1 . ILE   A 1 840  ? 131.869 109.730 117.269 1.00 52.59  0  804  ILE   A CD1 1 
ATOM   5826  N N   . THR   A 1 841  ? 133.652 113.446 114.972 1.00 56.73  0  805  THR   A N   1 
ATOM   5827  C CA  . THR   A 1 841  ? 134.187 114.757 115.339 1.00 59.79  0  805  THR   A CA  1 
ATOM   5828  C C   . THR   A 1 841  ? 133.356 115.296 116.495 1.00 61.00  0  805  THR   A C   1 
ATOM   5829  O O   . THR   A 1 841  ? 132.154 115.519 116.340 1.00 62.76  0  805  THR   A O   1 
ATOM   5830  C CB  . THR   A 1 841  ? 134.160 115.715 114.150 1.00 58.75  0  805  THR   A CB  1 
ATOM   5831  O OG1 . THR   A 1 841  ? 134.994 115.205 113.102 1.00 57.01  0  805  THR   A OG1 1 
ATOM   5832  C CG2 . THR   A 1 841  ? 134.655 117.091 114.560 1.00 56.23  0  805  THR   A CG2 1 
ATOM   5833  N N   . ALA   A 1 842  ? 133.986 115.518 117.641 1.00 52.41  0  806  ALA   A N   1 
ATOM   5834  C CA  . ALA   A 1 842  ? 133.272 115.916 118.843 1.00 54.11  0  806  ALA   A CA  1 
ATOM   5835  C C   . ALA   A 1 842  ? 133.514 117.385 119.163 1.00 59.07  0  806  ALA   A C   1 
ATOM   5836  O O   . ALA   A 1 842  ? 134.603 117.918 118.938 1.00 60.02  0  806  ALA   A O   1 
ATOM   5837  C CB  . ALA   A 1 842  ? 133.691 115.055 120.036 1.00 58.31  0  806  ALA   A CB  1 
ATOM   5838  N N   . LEU   A 1 843  ? 132.478 118.037 119.686 1.00 58.37  0  807  LEU   A N   1 
ATOM   5839  C CA  . LEU   A 1 843  ? 132.588 119.402 120.196 1.00 54.32  0  807  LEU   A CA  1 
ATOM   5840  C C   . LEU   A 1 843  ? 131.750 119.491 121.462 1.00 53.01  0  807  LEU   A C   1 
ATOM   5841  O O   . LEU   A 1 843  ? 130.520 119.542 121.383 1.00 61.84  0  807  LEU   A O   1 
ATOM   5842  C CB  . LEU   A 1 843  ? 132.119 120.426 119.163 1.00 55.56  0  807  LEU   A CB  1 
ATOM   5843  C CG  . LEU   A 1 843  ? 133.067 120.742 118.008 1.00 55.49  0  807  LEU   A CG  1 
ATOM   5844  C CD1 . LEU   A 1 843  ? 132.767 119.851 116.817 1.00 59.14  0  807  LEU   A CD1 1 
ATOM   5845  C CD2 . LEU   A 1 843  ? 132.969 122.206 117.622 1.00 52.91  0  807  LEU   A CD2 1 
ATOM   5846  N N   . ILE   A 1 844  ? 132.402 119.502 122.619 1.00 46.59  0  808  ILE   A N   1 
ATOM   5847  C CA  . ILE   A 1 844  ? 131.719 119.553 123.907 1.00 53.62  0  808  ILE   A CA  1 
ATOM   5848  C C   . ILE   A 1 844  ? 131.872 120.969 124.446 1.00 53.71  0  808  ILE   A C   1 
ATOM   5849  O O   . ILE   A 1 844  ? 132.903 121.318 125.027 1.00 57.88  0  808  ILE   A O   1 
ATOM   5850  C CB  . ILE   A 1 844  ? 132.267 118.515 124.887 1.00 50.93  0  808  ILE   A CB  1 
ATOM   5851  C CG1 . ILE   A 1 844  ? 132.139 117.111 124.302 1.00 51.06  0  808  ILE   A CG1 1 
ATOM   5852  C CG2 . ILE   A 1 844  ? 131.527 118.599 126.207 1.00 49.97  0  808  ILE   A CG2 1 
ATOM   5853  C CD1 . ILE   A 1 844  ? 132.489 116.021 125.278 1.00 50.48  0  808  ILE   A CD1 1 
ATOM   5854  N N   . ASN   A 1 845  ? 130.841 121.789 124.264 1.00 59.32  0  809  ASN   A N   1 
ATOM   5855  C CA  . ASN   A 1 845  ? 130.840 123.177 124.716 1.00 62.24  0  809  ASN   A CA  1 
ATOM   5856  C C   . ASN   A 1 845  ? 130.085 123.250 126.042 1.00 63.72  0  809  ASN   A C   1 
ATOM   5857  O O   . ASN   A 1 845  ? 128.954 123.730 126.115 1.00 63.33  0  809  ASN   A O   1 
ATOM   5858  C CB  . ASN   A 1 845  ? 130.217 124.088 123.658 1.00 64.31  0  809  ASN   A CB  1 
ATOM   5859  C CG  . ASN   A 1 845  ? 130.543 125.550 123.881 1.00 64.36  0  809  ASN   A CG  1 
ATOM   5860  O OD1 . ASN   A 1 845  ? 131.037 125.933 124.940 1.00 65.01  0  809  ASN   A OD1 1 
ATOM   5861  N ND2 . ASN   A 1 845  ? 130.271 126.376 122.878 1.00 62.52  0  809  ASN   A ND2 1 
ATOM   5862  N N   . GLY   A 1 846  ? 130.730 122.771 127.101 1.00 56.54  0  810  GLY   A N   1 
ATOM   5863  C CA  . GLY   A 1 846  ? 130.156 122.856 128.428 1.00 56.07  0  810  GLY   A CA  1 
ATOM   5864  C C   . GLY   A 1 846  ? 129.220 121.718 128.773 1.00 59.01  0  810  GLY   A C   1 
ATOM   5865  O O   . GLY   A 1 846  ? 129.665 120.611 129.089 1.00 59.32  0  810  GLY   A O   1 
ATOM   5866  N N   . ASP   A 1 847  ? 127.913 121.982 128.720 1.00 57.81  0  811  ASP   A N   1 
ATOM   5867  C CA  . ASP   A 1 847  ? 126.902 121.001 129.101 1.00 56.26  0  811  ASP   A CA  1 
ATOM   5868  C C   . ASP   A 1 847  ? 126.098 120.502 127.906 1.00 57.75  0  811  ASP   A C   1 
ATOM   5869  O O   . ASP   A 1 847  ? 125.065 119.851 128.088 1.00 60.62  0  811  ASP   A O   1 
ATOM   5870  C CB  . ASP   A 1 847  ? 125.969 121.583 130.163 1.00 56.91  0  811  ASP   A CB  1 
ATOM   5871  C CG  . ASP   A 1 847  ? 126.407 121.237 131.571 1.00 59.10  0  811  ASP   A CG  1 
ATOM   5872  O OD1 . ASP   A 1 847  ? 126.981 120.144 131.758 1.00 54.14  0  811  ASP   A OD1 1 
ATOM   5873  O OD2 . ASP   A 1 847  ? 126.180 122.054 132.488 1.00 53.90  -1 811  ASP   A OD2 1 
ATOM   5874  N N   . ASN   A 1 848  ? 126.541 120.795 126.688 1.00 57.13  0  812  ASN   A N   1 
ATOM   5875  C CA  . ASN   A 1 848  ? 125.902 120.252 125.498 1.00 60.45  0  812  ASN   A CA  1 
ATOM   5876  C C   . ASN   A 1 848  ? 126.981 119.931 124.479 1.00 55.90  0  812  ASN   A C   1 
ATOM   5877  O O   . ASN   A 1 848  ? 127.921 120.711 124.305 1.00 55.24  0  812  ASN   A O   1 
ATOM   5878  C CB  . ASN   A 1 848  ? 124.870 121.227 124.917 1.00 61.97  0  812  ASN   A CB  1 
ATOM   5879  C CG  . ASN   A 1 848  ? 125.506 122.417 124.232 1.00 60.17  0  812  ASN   A CG  1 
ATOM   5880  O OD1 . ASN   A 1 848  ? 125.747 122.396 123.028 1.00 58.02  0  812  ASN   A OD1 1 
ATOM   5881  N ND2 . ASN   A 1 848  ? 125.773 123.467 124.997 1.00 57.83  0  812  ASN   A ND2 1 
ATOM   5882  N N   . GLN   A 1 849  ? 126.851 118.785 123.819 1.00 48.63  0  813  GLN   A N   1 
ATOM   5883  C CA  . GLN   A 1 849  ? 127.860 118.317 122.884 1.00 46.04  0  813  GLN   A CA  1 
ATOM   5884  C C   . GLN   A 1 849  ? 127.250 118.086 121.512 1.00 46.88  0  813  GLN   A C   1 
ATOM   5885  O O   . GLN   A 1 849  ? 126.064 117.773 121.380 1.00 51.97  0  813  GLN   A O   1 
ATOM   5886  C CB  . GLN   A 1 849  ? 128.527 117.029 123.376 1.00 45.56  0  813  GLN   A CB  1 
ATOM   5887  C CG  . GLN   A 1 849  ? 127.735 115.767 123.116 1.00 49.27  0  813  GLN   A CG  1 
ATOM   5888  C CD  . GLN   A 1 849  ? 128.501 114.516 123.484 1.00 48.87  0  813  GLN   A CD  1 
ATOM   5889  O OE1 . GLN   A 1 849  ? 129.476 114.569 124.230 1.00 45.38  0  813  GLN   A OE1 1 
ATOM   5890  N NE2 . GLN   A 1 849  ? 128.063 113.380 122.961 1.00 48.86  0  813  GLN   A NE2 1 
ATOM   5891  N N   . SER   A 1 850  ? 128.081 118.266 120.491 1.00 48.66  0  814  SER   A N   1 
ATOM   5892  C CA  . SER   A 1 850  ? 127.721 118.002 119.108 1.00 53.36  0  814  SER   A CA  1 
ATOM   5893  C C   . SER   A 1 850  ? 128.673 116.957 118.549 1.00 55.76  0  814  SER   A C   1 
ATOM   5894  O O   . SER   A 1 850  ? 129.896 117.113 118.642 1.00 60.61  0  814  SER   A O   1 
ATOM   5895  C CB  . SER   A 1 850  ? 127.780 119.278 118.265 1.00 54.99  0  814  SER   A CB  1 
ATOM   5896  O OG  . SER   A 1 850  ? 127.738 118.975 116.882 1.00 61.31  0  814  SER   A OG  1 
ATOM   5897  N N   . ILE   A 1 851  ? 128.113 115.899 117.973 1.00 49.01  0  815  ILE   A N   1 
ATOM   5898  C CA  . ILE   A 1 851  ? 128.882 114.802 117.405 1.00 47.68  0  815  ILE   A CA  1 
ATOM   5899  C C   . ILE   A 1 851  ? 128.591 114.755 115.915 1.00 47.58  0  815  ILE   A C   1 
ATOM   5900  O O   . ILE   A 1 851  ? 127.451 114.514 115.508 1.00 49.35  0  815  ILE   A O   1 
ATOM   5901  C CB  . ILE   A 1 851  ? 128.531 113.466 118.075 1.00 43.89  0  815  ILE   A CB  1 
ATOM   5902  C CG1 . ILE   A 1 851  ? 128.840 113.530 119.567 1.00 49.00  0  815  ILE   A CG1 1 
ATOM   5903  C CG2 . ILE   A 1 851  ? 129.276 112.330 117.420 1.00 47.19  0  815  ILE   A CG2 1 
ATOM   5904  C CD1 . ILE   A 1 851  ? 130.205 114.084 119.878 1.00 48.79  0  815  ILE   A CD1 1 
ATOM   5905  N N   . ASP   A 1 852  ? 129.614 114.986 115.102 1.00 52.43  0  816  ASP   A N   1 
ATOM   5906  C CA  . ASP   A 1 852  ? 129.495 114.923 113.654 1.00 54.35  0  816  ASP   A CA  1 
ATOM   5907  C C   . ASP   A 1 852  ? 130.012 113.566 113.201 1.00 52.41  0  816  ASP   A C   1 
ATOM   5908  O O   . ASP   A 1 852  ? 131.158 113.208 113.491 1.00 51.19  0  816  ASP   A O   1 
ATOM   5909  C CB  . ASP   A 1 852  ? 130.276 116.056 112.994 1.00 55.17  0  816  ASP   A CB  1 
ATOM   5910  C CG  . ASP   A 1 852  ? 129.577 116.610 111.775 1.00 57.57  0  816  ASP   A CG  1 
ATOM   5911  O OD1 . ASP   A 1 852  ? 128.641 115.956 111.274 1.00 54.21  0  816  ASP   A OD1 1 
ATOM   5912  O OD2 . ASP   A 1 852  ? 129.957 117.710 111.322 1.00 59.13  -1 816  ASP   A OD2 1 
ATOM   5913  N N   . ILE   A 1 853  ? 129.168 112.811 112.504 1.00 52.38  0  817  ILE   A N   1 
ATOM   5914  C CA  . ILE   A 1 853  ? 129.447 111.428 112.146 1.00 50.19  0  817  ILE   A CA  1 
ATOM   5915  C C   . ILE   A 1 853  ? 129.455 111.306 110.633 1.00 55.43  0  817  ILE   A C   1 
ATOM   5916  O O   . ILE   A 1 853  ? 128.536 111.784 109.959 1.00 60.43  0  817  ILE   A O   1 
ATOM   5917  C CB  . ILE   A 1 853  ? 128.407 110.475 112.764 1.00 48.43  0  817  ILE   A CB  1 
ATOM   5918  C CG1 . ILE   A 1 853  ? 128.472 110.539 114.287 1.00 50.61  0  817  ILE   A CG1 1 
ATOM   5919  C CG2 . ILE   A 1 853  ? 128.624 109.060 112.272 1.00 56.15  0  817  ILE   A CG2 1 
ATOM   5920  C CD1 . ILE   A 1 853  ? 127.243 110.005 114.966 1.00 50.70  0  817  ILE   A CD1 1 
ATOM   5921  N N   . SER   A 1 854  ? 130.495 110.673 110.099 1.00 52.81  0  818  SER   A N   1 
ATOM   5922  C CA  . SER   A 1 854  ? 130.611 110.423 108.671 1.00 51.23  0  818  SER   A CA  1 
ATOM   5923  C C   . SER   A 1 854  ? 130.920 108.954 108.443 1.00 50.40  0  818  SER   A C   1 
ATOM   5924  O O   . SER   A 1 854  ? 131.720 108.362 109.170 1.00 52.22  0  818  SER   A O   1 
ATOM   5925  C CB  . SER   A 1 854  ? 131.703 111.288 108.041 1.00 55.32  0  818  SER   A CB  1 
ATOM   5926  O OG  . SER   A 1 854  ? 132.052 110.797 106.760 1.00 61.62  0  818  SER   A OG  1 
ATOM   5927  N N   . LYS   A 1 855  ? 130.279 108.367 107.431 1.00 59.27  0  819  LYS   A N   1 
ATOM   5928  C CA  . LYS   A 1 855  ? 130.509 106.970 107.091 1.00 63.81  0  819  LYS   A CA  1 
ATOM   5929  C C   . LYS   A 1 855  ? 130.506 106.790 105.577 1.00 66.08  0  819  LYS   A C   1 
ATOM   5930  O O   . LYS   A 1 855  ? 129.628 107.341 104.891 1.00 66.31  0  819  LYS   A O   1 
ATOM   5931  C CB  . LYS   A 1 855  ? 129.462 106.055 107.728 1.00 60.78  0  819  LYS   A CB  1 
ATOM   5932  C CG  . LYS   A 1 855  ? 129.773 104.580 107.548 1.00 60.05  0  819  LYS   A CG  1 
ATOM   5933  C CD  . LYS   A 1 855  ? 128.929 103.707 108.449 1.00 61.82  0  819  LYS   A CD  1 
ATOM   5934  C CE  . LYS   A 1 855  ? 129.415 102.272 108.412 1.00 60.80  0  819  LYS   A CE  1 
ATOM   5935  N NZ  . LYS   A 1 855  ? 128.713 101.418 109.405 1.00 62.18  1  819  LYS   A NZ  1 
ATOM   5936  N N   . PRO   A 1 856  ? 131.467 106.048 105.026 1.00 67.80  0  820  PRO   A N   1 
ATOM   5937  C CA  . PRO   A 1 856  ? 131.398 105.685 103.606 1.00 66.01  0  820  PRO   A CA  1 
ATOM   5938  C C   . PRO   A 1 856  ? 130.526 104.459 103.399 1.00 69.71  0  820  PRO   A C   1 
ATOM   5939  O O   . PRO   A 1 856  ? 130.749 103.427 104.037 1.00 71.83  0  820  PRO   A O   1 
ATOM   5940  C CB  . PRO   A 1 856  ? 132.862 105.402 103.239 1.00 69.27  0  820  PRO   A CB  1 
ATOM   5941  C CG  . PRO   A 1 856  ? 133.675 105.774 104.466 1.00 67.79  0  820  PRO   A CG  1 
ATOM   5942  C CD  . PRO   A 1 856  ? 132.749 105.651 105.621 1.00 66.25  0  820  PRO   A CD  1 
ATOM   5943  N N   . ILE   A 1 857  ? 129.533 104.550 102.516 1.00 76.06  0  821  ILE   A N   1 
ATOM   5944  C CA  . ILE   A 1 857  ? 128.588 103.465 102.304 1.00 77.31  0  821  ILE   A CA  1 
ATOM   5945  C C   . ILE   A 1 857  ? 128.485 103.169 100.816 1.00 81.75  0  821  ILE   A C   1 
ATOM   5946  O O   . ILE   A 1 857  ? 128.762 104.016 99.964  1.00 83.12  0  821  ILE   A O   1 
ATOM   5947  C CB  . ILE   A 1 857  ? 127.191 103.791 102.871 1.00 76.89  0  821  ILE   A CB  1 
ATOM   5948  C CG1 . ILE   A 1 857  ? 126.617 105.024 102.174 1.00 74.67  0  821  ILE   A CG1 1 
ATOM   5949  C CG2 . ILE   A 1 857  ? 127.253 104.001 104.372 1.00 76.87  0  821  ILE   A CG2 1 
ATOM   5950  C CD1 . ILE   A 1 857  ? 125.138 105.199 102.378 1.00 77.97  0  821  ILE   A CD1 1 
ATOM   5951  N N   . ARG   A 1 858  ? 128.083 101.937 100.516 1.00 89.80  0  822  ARG   A N   1 
ATOM   5952  C CA  . ARG   A 1 858  ? 127.705 101.555 99.161  1.00 88.97  0  822  ARG   A CA  1 
ATOM   5953  C C   . ARG   A 1 858  ? 126.240 101.924 98.969  1.00 87.08  0  822  ARG   A C   1 
ATOM   5954  O O   . ARG   A 1 858  ? 125.353 101.276 99.532  1.00 85.09  0  822  ARG   A O   1 
ATOM   5955  C CB  . ARG   A 1 858  ? 127.934 100.063 98.937  1.00 88.97  0  822  ARG   A CB  1 
ATOM   5956  C CG  . ARG   A 1 858  ? 129.375 99.614  99.120  1.00 88.79  0  822  ARG   A CG  1 
ATOM   5957  C CD  . ARG   A 1 858  ? 130.215 99.909  97.887  1.00 89.27  0  822  ARG   A CD  1 
ATOM   5958  N NE  . ARG   A 1 858  ? 131.534 99.292  97.966  1.00 88.42  0  822  ARG   A NE  1 
ATOM   5959  C CZ  . ARG   A 1 858  ? 132.462 99.387  97.024  1.00 87.99  0  822  ARG   A CZ  1 
ATOM   5960  N NH1 . ARG   A 1 858  ? 132.252 100.075 95.914  1.00 88.30  1  822  ARG   A NH1 1 
ATOM   5961  N NH2 . ARG   A 1 858  ? 133.632 98.779  97.202  1.00 87.31  0  822  ARG   A NH2 1 
ATOM   5962  N N   . LEU   A 1 859  ? 125.985 102.972 98.192  1.00 85.71  0  823  LEU   A N   1 
ATOM   5963  C CA  . LEU   A 1 859  ? 124.628 103.474 98.043  1.00 87.50  0  823  LEU   A CA  1 
ATOM   5964  C C   . LEU   A 1 859  ? 123.741 102.445 97.355  1.00 91.01  0  823  LEU   A C   1 
ATOM   5965  O O   . LEU   A 1 859  ? 124.134 101.826 96.362  1.00 93.02  0  823  LEU   A O   1 
ATOM   5966  C CB  . LEU   A 1 859  ? 124.631 104.778 97.250  1.00 86.06  0  823  LEU   A CB  1 
ATOM   5967  C CG  . LEU   A 1 859  ? 123.396 105.657 97.429  1.00 86.39  0  823  LEU   A CG  1 
ATOM   5968  C CD1 . LEU   A 1 859  ? 123.391 106.271 98.814  1.00 87.11  0  823  LEU   A CD1 1 
ATOM   5969  C CD2 . LEU   A 1 859  ? 123.350 106.735 96.363  1.00 87.07  0  823  LEU   A CD2 1 
ATOM   5970  N N   . MET   A 1 860  ? 122.537 102.264 97.890  1.00 98.64  0  824  MET   A N   1 
ATOM   5971  C CA  . MET   A 1 860  ? 121.583 101.340 97.299  1.00 97.68  0  824  MET   A CA  1 
ATOM   5972  C C   . MET   A 1 860  ? 121.025 101.913 95.998  1.00 97.62  0  824  MET   A C   1 
ATOM   5973  O O   . MET   A 1 860  ? 121.201 103.090 95.674  1.00 96.32  0  824  MET   A O   1 
ATOM   5974  C CB  . MET   A 1 860  ? 120.445 101.042 98.276  1.00 95.76  0  824  MET   A CB  1 
ATOM   5975  C CG  . MET   A 1 860  ? 120.876 100.403 99.590  1.00 95.91  0  824  MET   A CG  1 
ATOM   5976  S SD  . MET   A 1 860  ? 122.571 99.786  99.599  1.00 102.65 0  824  MET   A SD  1 
ATOM   5977  C CE  . MET   A 1 860  ? 122.377 98.206  98.774  1.00 96.87  0  824  MET   A CE  1 
ATOM   5978  N N   . GLU   A 1 861  ? 120.347 101.055 95.242  1.00 101.74 0  825  GLU   A N   1 
ATOM   5979  C CA  . GLU   A 1 861  ? 119.715 101.461 93.996  1.00 103.58 0  825  GLU   A CA  1 
ATOM   5980  C C   . GLU   A 1 861  ? 118.365 102.096 94.299  1.00 102.26 0  825  GLU   A C   1 
ATOM   5981  O O   . GLU   A 1 861  ? 117.530 101.499 94.986  1.00 99.89  0  825  GLU   A O   1 
ATOM   5982  C CB  . GLU   A 1 861  ? 119.543 100.265 93.058  1.00 103.86 0  825  GLU   A CB  1 
ATOM   5983  C CG  . GLU   A 1 861  ? 118.915 100.615 91.718  1.00 103.63 0  825  GLU   A CG  1 
ATOM   5984  C CD  . GLU   A 1 861  ? 119.720 101.645 90.947  1.00 104.04 0  825  GLU   A CD  1 
ATOM   5985  O OE1 . GLU   A 1 861  ? 120.962 101.524 90.910  1.00 102.50 0  825  GLU   A OE1 1 
ATOM   5986  O OE2 . GLU   A 1 861  ? 119.109 102.575 90.379  1.00 103.63 -1 825  GLU   A OE2 1 
ATOM   5987  N N   . GLY   A 1 862  ? 118.157 103.307 93.787  1.00 95.55  0  826  GLY   A N   1 
ATOM   5988  C CA  . GLY   A 1 862  ? 116.959 104.069 94.047  1.00 95.94  0  826  GLY   A CA  1 
ATOM   5989  C C   . GLY   A 1 862  ? 117.014 104.902 95.312  1.00 96.38  0  826  GLY   A C   1 
ATOM   5990  O O   . GLY   A 1 862  ? 116.306 105.909 95.413  1.00 94.39  0  826  GLY   A O   1 
ATOM   5991  N N   . GLN   A 1 863  ? 117.840 104.503 96.277  1.00 86.03  0  827  GLN   A N   1 
ATOM   5992  C CA  . GLN   A 1 863  ? 117.998 105.273 97.501  1.00 82.94  0  827  GLN   A CA  1 
ATOM   5993  C C   . GLN   A 1 863  ? 118.618 106.629 97.194  1.00 82.90  0  827  GLN   A C   1 
ATOM   5994  O O   . GLN   A 1 863  ? 119.421 106.775 96.268  1.00 84.06  0  827  GLN   A O   1 
ATOM   5995  C CB  . GLN   A 1 863  ? 118.870 104.509 98.495  1.00 81.86  0  827  GLN   A CB  1 
ATOM   5996  C CG  . GLN   A 1 863  ? 118.690 104.922 99.940  1.00 80.13  0  827  GLN   A CG  1 
ATOM   5997  C CD  . GLN   A 1 863  ? 119.575 104.129 100.878 1.00 81.15  0  827  GLN   A CD  1 
ATOM   5998  O OE1 . GLN   A 1 863  ? 120.741 103.877 100.582 1.00 81.26  0  827  GLN   A OE1 1 
ATOM   5999  N NE2 . GLN   A 1 863  ? 119.021 103.722 102.012 1.00 81.96  0  827  GLN   A NE2 1 
ATOM   6000  N N   . THR   A 1 864  ? 118.231 107.631 97.973  1.00 70.25  0  828  THR   A N   1 
ATOM   6001  C CA  . THR   A 1 864  ? 118.731 108.986 97.807  1.00 73.22  0  828  THR   A CA  1 
ATOM   6002  C C   . THR   A 1 864  ? 119.663 109.340 98.962  1.00 72.39  0  828  THR   A C   1 
ATOM   6003  O O   . THR   A 1 864  ? 119.882 108.551 99.885  1.00 69.22  0  828  THR   A O   1 
ATOM   6004  C CB  . THR   A 1 864  ? 117.573 109.981 97.700  1.00 71.27  0  828  THR   A CB  1 
ATOM   6005  O OG1 . THR   A 1 864  ? 118.077 111.262 97.302  1.00 70.26  0  828  THR   A OG1 1 
ATOM   6006  C CG2 . THR   A 1 864  ? 116.860 110.115 99.032  1.00 70.54  0  828  THR   A CG2 1 
ATOM   6007  N N   . HIS   A 1 865  ? 120.230 110.547 98.890  1.00 68.52  0  829  HIS   A N   1 
ATOM   6008  C CA  . HIS   A 1 865  ? 121.150 111.000 99.928  1.00 66.92  0  829  HIS   A CA  1 
ATOM   6009  C C   . HIS   A 1 865  ? 120.439 111.185 101.262 1.00 64.97  0  829  HIS   A C   1 
ATOM   6010  O O   . HIS   A 1 865  ? 120.980 110.827 102.315 1.00 69.15  0  829  HIS   A O   1 
ATOM   6011  C CB  . HIS   A 1 865  ? 121.820 112.301 99.494  1.00 66.77  0  829  HIS   A CB  1 
ATOM   6012  C CG  . HIS   A 1 865  ? 122.683 112.159 98.280  1.00 70.35  0  829  HIS   A CG  1 
ATOM   6013  N ND1 . HIS   A 1 865  ? 123.269 110.965 97.921  1.00 70.24  0  829  HIS   A ND1 1 
ATOM   6014  C CD2 . HIS   A 1 865  ? 123.052 113.058 97.338  1.00 68.87  0  829  HIS   A CD2 1 
ATOM   6015  C CE1 . HIS   A 1 865  ? 123.967 111.135 96.813  1.00 69.31  0  829  HIS   A CE1 1 
ATOM   6016  N NE2 . HIS   A 1 865  ? 123.851 112.397 96.438  1.00 71.54  0  829  HIS   A NE2 1 
ATOM   6017  N N   . ALA   A 1 866  ? 119.228 111.746 101.236 1.00 62.21  0  830  ALA   A N   1 
ATOM   6018  C CA  . ALA   A 1 866  ? 118.511 112.018 102.477 1.00 61.40  0  830  ALA   A CA  1 
ATOM   6019  C C   . ALA   A 1 866  ? 118.213 110.735 103.239 1.00 63.45  0  830  ALA   A C   1 
ATOM   6020  O O   . ALA   A 1 866  ? 118.374 110.682 104.464 1.00 70.57  0  830  ALA   A O   1 
ATOM   6021  C CB  . ALA   A 1 866  ? 117.219 112.775 102.179 1.00 62.04  0  830  ALA   A CB  1 
ATOM   6022  N N   . GLN   A 1 867  ? 117.776 109.690 102.534 1.00 63.37  0  831  GLN   A N   1 
ATOM   6023  C CA  . GLN   A 1 867  ? 117.475 108.427 103.199 1.00 62.72  0  831  GLN   A CA  1 
ATOM   6024  C C   . GLN   A 1 867  ? 118.726 107.810 103.806 1.00 57.40  0  831  GLN   A C   1 
ATOM   6025  O O   . GLN   A 1 867  ? 118.683 107.279 104.921 1.00 53.07  0  831  GLN   A O   1 
ATOM   6026  C CB  . GLN   A 1 867  ? 116.825 107.458 102.215 1.00 62.65  0  831  GLN   A CB  1 
ATOM   6027  C CG  . GLN   A 1 867  ? 115.548 107.980 101.593 1.00 59.40  0  831  GLN   A CG  1 
ATOM   6028  C CD  . GLN   A 1 867  ? 114.587 106.873 101.235 1.00 62.16  0  831  GLN   A CD  1 
ATOM   6029  O OE1 . GLN   A 1 867  ? 114.985 105.720 101.073 1.00 62.08  0  831  GLN   A OE1 1 
ATOM   6030  N NE2 . GLN   A 1 867  ? 113.312 107.215 101.111 1.00 66.17  0  831  GLN   A NE2 1 
ATOM   6031  N N   . ALA   A 1 868  ? 119.848 107.868 103.088 1.00 58.26  0  832  ALA   A N   1 
ATOM   6032  C CA  . ALA   A 1 868  ? 121.094 107.324 103.615 1.00 61.99  0  832  ALA   A CA  1 
ATOM   6033  C C   . ALA   A 1 868  ? 121.532 108.076 104.862 1.00 63.86  0  832  ALA   A C   1 
ATOM   6034  O O   . ALA   A 1 868  ? 121.944 107.469 105.859 1.00 65.16  0  832  ALA   A O   1 
ATOM   6035  C CB  . ALA   A 1 868  ? 122.181 107.380 102.543 1.00 62.26  0  832  ALA   A CB  1 
ATOM   6036  N N   . ASP   A 1 869  ? 121.443 109.407 104.825 1.00 68.73  0  833  ASP   A N   1 
ATOM   6037  C CA  . ASP   A 1 869  ? 121.829 110.212 105.978 1.00 64.10  0  833  ASP   A CA  1 
ATOM   6038  C C   . ASP   A 1 869  ? 120.934 109.917 107.174 1.00 63.76  0  833  ASP   A C   1 
ATOM   6039  O O   . ASP   A 1 869  ? 121.414 109.773 108.304 1.00 70.71  0  833  ASP   A O   1 
ATOM   6040  C CB  . ASP   A 1 869  ? 121.778 111.693 105.609 1.00 60.02  0  833  ASP   A CB  1 
ATOM   6041  C CG  . ASP   A 1 869  ? 122.900 112.093 104.678 1.00 69.48  0  833  ASP   A CG  1 
ATOM   6042  O OD1 . ASP   A 1 869  ? 123.816 111.273 104.467 1.00 70.63  0  833  ASP   A OD1 1 
ATOM   6043  O OD2 . ASP   A 1 869  ? 122.856 113.212 104.130 1.00 66.83  -1 833  ASP   A OD2 1 
ATOM   6044  N N   . TYR   A 1 870  ? 119.624 109.808 106.940 1.00 57.37  0  834  TYR   A N   1 
ATOM   6045  C CA  . TYR   A 1 870  ? 118.701 109.513 108.029 1.00 56.23  0  834  TYR   A CA  1 
ATOM   6046  C C   . TYR   A 1 870  ? 118.955 108.129 108.615 1.00 59.62  0  834  TYR   A C   1 
ATOM   6047  O O   . TYR   A 1 870  ? 118.909 107.948 109.838 1.00 68.64  0  834  TYR   A O   1 
ATOM   6048  C CB  . TYR   A 1 870  ? 117.259 109.634 107.540 1.00 58.05  0  834  TYR   A CB  1 
ATOM   6049  C CG  . TYR   A 1 870  ? 116.233 109.494 108.636 1.00 59.83  0  834  TYR   A CG  1 
ATOM   6050  C CD1 . TYR   A 1 870  ? 116.350 110.207 109.819 1.00 59.04  0  834  TYR   A CD1 1 
ATOM   6051  C CD2 . TYR   A 1 870  ? 115.147 108.647 108.489 1.00 56.23  0  834  TYR   A CD2 1 
ATOM   6052  C CE1 . TYR   A 1 870  ? 115.418 110.081 110.822 1.00 53.58  0  834  TYR   A CE1 1 
ATOM   6053  C CE2 . TYR   A 1 870  ? 114.211 108.515 109.488 1.00 60.24  0  834  TYR   A CE2 1 
ATOM   6054  C CZ  . TYR   A 1 870  ? 114.351 109.233 110.652 1.00 60.68  0  834  TYR   A CZ  1 
ATOM   6055  O OH  . TYR   A 1 870  ? 113.416 109.102 111.651 1.00 66.31  0  834  TYR   A OH  1 
ATOM   6056  N N   . LEU   A 1 871  ? 119.221 107.139 107.761 1.00 52.58  0  835  LEU   A N   1 
ATOM   6057  C CA  . LEU   A 1 871  ? 119.509 105.797 108.255 1.00 55.09  0  835  LEU   A CA  1 
ATOM   6058  C C   . LEU   A 1 871  ? 120.791 105.777 109.076 1.00 54.03  0  835  LEU   A C   1 
ATOM   6059  O O   . LEU   A 1 871  ? 120.858 105.120 110.123 1.00 53.07  0  835  LEU   A O   1 
ATOM   6060  C CB  . LEU   A 1 871  ? 119.602 104.821 107.084 1.00 59.19  0  835  LEU   A CB  1 
ATOM   6061  C CG  . LEU   A 1 871  ? 119.938 103.369 107.421 1.00 56.17  0  835  LEU   A CG  1 
ATOM   6062  C CD1 . LEU   A 1 871  ? 118.863 102.763 108.305 1.00 51.42  0  835  LEU   A CD1 1 
ATOM   6063  C CD2 . LEU   A 1 871  ? 120.120 102.558 106.151 1.00 54.65  0  835  LEU   A CD2 1 
ATOM   6064  N N   . LEU   A 1 872  ? 121.821 106.490 108.613 1.00 49.39  0  836  LEU   A N   1 
ATOM   6065  C CA  . LEU   A 1 872  ? 123.052 106.590 109.388 1.00 49.69  0  836  LEU   A CA  1 
ATOM   6066  C C   . LEU   A 1 872  ? 122.792 107.239 110.738 1.00 54.60  0  836  LEU   A C   1 
ATOM   6067  O O   . LEU   A 1 872  ? 123.313 106.787 111.766 1.00 55.82  0  836  LEU   A O   1 
ATOM   6068  C CB  . LEU   A 1 872  ? 124.100 107.385 108.612 1.00 50.77  0  836  LEU   A CB  1 
ATOM   6069  C CG  . LEU   A 1 872  ? 125.201 108.012 109.470 1.00 52.22  0  836  LEU   A CG  1 
ATOM   6070  C CD1 . LEU   A 1 872  ? 126.210 106.970 109.917 1.00 50.43  0  836  LEU   A CD1 1 
ATOM   6071  C CD2 . LEU   A 1 872  ? 125.882 109.141 108.727 1.00 52.64  0  836  LEU   A CD2 1 
ATOM   6072  N N   . ALA   A 1 873  ? 121.987 108.303 110.752 1.00 56.54  0  837  ALA   A N   1 
ATOM   6073  C CA  . ALA   A 1 873  ? 121.668 108.971 112.006 1.00 46.38  0  837  ALA   A CA  1 
ATOM   6074  C C   . ALA   A 1 873  ? 120.957 108.027 112.961 1.00 49.86  0  837  ALA   A C   1 
ATOM   6075  O O   . ALA   A 1 873  ? 121.279 107.982 114.151 1.00 53.17  0  837  ALA   A O   1 
ATOM   6076  C CB  . ALA   A 1 873  ? 120.817 110.210 111.736 1.00 45.99  0  837  ALA   A CB  1 
ATOM   6077  N N   . LEU   A 1 874  ? 119.997 107.250 112.457 1.00 56.02  0  838  LEU   A N   1 
ATOM   6078  C CA  . LEU   A 1 874  ? 119.269 106.324 113.321 1.00 56.68  0  838  LEU   A CA  1 
ATOM   6079  C C   . LEU   A 1 874  ? 120.183 105.236 113.874 1.00 63.44  0  838  LEU   A C   1 
ATOM   6080  O O   . LEU   A 1 874  ? 120.109 104.899 115.064 1.00 64.64  0  838  LEU   A O   1 
ATOM   6081  C CB  . LEU   A 1 874  ? 118.100 105.706 112.558 1.00 55.88  0  838  LEU   A CB  1 
ATOM   6082  C CG  . LEU   A 1 874  ? 117.027 106.690 112.092 1.00 56.39  0  838  LEU   A CG  1 
ATOM   6083  C CD1 . LEU   A 1 874  ? 115.948 105.972 111.308 1.00 59.72  0  838  LEU   A CD1 1 
ATOM   6084  C CD2 . LEU   A 1 874  ? 116.431 107.430 113.271 1.00 59.64  0  838  LEU   A CD2 1 
ATOM   6085  N N   . ASN   A 1 875  ? 121.052 104.673 113.029 1.00 62.91  0  839  ASN   A N   1 
ATOM   6086  C CA  . ASN   A 1 875  ? 121.949 103.620 113.499 1.00 55.97  0  839  ASN   A CA  1 
ATOM   6087  C C   . ASN   A 1 875  ? 122.935 104.149 114.532 1.00 51.95  0  839  ASN   A C   1 
ATOM   6088  O O   . ASN   A 1 875  ? 123.185 103.496 115.553 1.00 52.28  0  839  ASN   A O   1 
ATOM   6089  C CB  . ASN   A 1 875  ? 122.690 102.996 112.321 1.00 53.58  0  839  ASN   A CB  1 
ATOM   6090  C CG  . ASN   A 1 875  ? 121.753 102.398 111.300 1.00 59.05  0  839  ASN   A CG  1 
ATOM   6091  O OD1 . ASN   A 1 875  ? 121.027 101.448 111.586 1.00 60.74  0  839  ASN   A OD1 1 
ATOM   6092  N ND2 . ASN   A 1 875  ? 121.765 102.951 110.098 1.00 63.22  0  839  ASN   A ND2 1 
ATOM   6093  N N   . SER   A 1 876  ? 123.506 105.330 114.286 1.00 50.55  0  840  SER   A N   1 
ATOM   6094  C CA  . SER   A 1 876  ? 124.418 105.923 115.256 1.00 53.67  0  840  SER   A CA  1 
ATOM   6095  C C   . SER   A 1 876  ? 123.695 106.276 116.547 1.00 54.38  0  840  SER   A C   1 
ATOM   6096  O O   . SER   A 1 876  ? 124.261 106.144 117.638 1.00 59.41  0  840  SER   A O   1 
ATOM   6097  C CB  . SER   A 1 876  ? 125.087 107.154 114.654 1.00 56.49  0  840  SER   A CB  1 
ATOM   6098  O OG  . SER   A 1 876  ? 124.126 108.144 114.339 1.00 56.63  0  840  SER   A OG  1 
ATOM   6099  N N   . LEU   A 1 877  ? 122.446 106.735 116.444 1.00 52.08  0  841  LEU   A N   1 
ATOM   6100  C CA  . LEU   A 1 877  ? 121.642 106.991 117.631 1.00 49.54  0  841  LEU   A CA  1 
ATOM   6101  C C   . LEU   A 1 877  ? 121.504 105.731 118.467 1.00 52.43  0  841  LEU   A C   1 
ATOM   6102  O O   . LEU   A 1 877  ? 121.739 105.748 119.680 1.00 52.33  0  841  LEU   A O   1 
ATOM   6103  C CB  . LEU   A 1 877  ? 120.263 107.502 117.219 1.00 52.31  0  841  LEU   A CB  1 
ATOM   6104  C CG  . LEU   A 1 877  ? 119.886 108.954 117.486 1.00 55.26  0  841  LEU   A CG  1 
ATOM   6105  C CD1 . LEU   A 1 877  ? 118.587 109.270 116.773 1.00 56.23  0  841  LEU   A CD1 1 
ATOM   6106  C CD2 . LEU   A 1 877  ? 119.759 109.213 118.965 1.00 56.52  0  841  LEU   A CD2 1 
ATOM   6107  N N   . LYS   A 1 878  ? 121.130 104.622 117.826 1.00 56.37  0  842  LYS   A N   1 
ATOM   6108  C CA  . LYS   A 1 878  ? 120.986 103.365 118.551 1.00 53.35  0  842  LYS   A CA  1 
ATOM   6109  C C   . LYS   A 1 878  ? 122.304 102.945 119.186 1.00 56.09  0  842  LYS   A C   1 
ATOM   6110  O O   . LYS   A 1 878  ? 122.335 102.505 120.341 1.00 56.03  0  842  LYS   A O   1 
ATOM   6111  C CB  . LYS   A 1 878  ? 120.482 102.268 117.615 1.00 57.51  0  842  LYS   A CB  1 
ATOM   6112  C CG  . LYS   A 1 878  ? 119.119 102.522 117.004 1.00 58.74  0  842  LYS   A CG  1 
ATOM   6113  C CD  . LYS   A 1 878  ? 118.804 101.470 115.951 1.00 59.11  0  842  LYS   A CD  1 
ATOM   6114  C CE  . LYS   A 1 878  ? 117.499 101.763 115.237 1.00 59.87  0  842  LYS   A CE  1 
ATOM   6115  N NZ  . LYS   A 1 878  ? 117.206 100.740 114.196 1.00 58.47  1  842  LYS   A NZ  1 
ATOM   6116  N N   . LEU   A 1 879  ? 123.406 103.084 118.448 1.00 60.39  0  843  LEU   A N   1 
ATOM   6117  C CA  . LEU   A 1 879  ? 124.698 102.631 118.951 1.00 56.09  0  843  LEU   A CA  1 
ATOM   6118  C C   . LEU   A 1 879  ? 125.147 103.445 120.158 1.00 57.56  0  843  LEU   A C   1 
ATOM   6119  O O   . LEU   A 1 879  ? 125.592 102.883 121.168 1.00 62.22  0  843  LEU   A O   1 
ATOM   6120  C CB  . LEU   A 1 879  ? 125.742 102.696 117.840 1.00 50.24  0  843  LEU   A CB  1 
ATOM   6121  C CG  . LEU   A 1 879  ? 127.162 102.346 118.268 1.00 53.30  0  843  LEU   A CG  1 
ATOM   6122  C CD1 . LEU   A 1 879  ? 127.210 100.966 118.897 1.00 56.98  0  843  LEU   A CD1 1 
ATOM   6123  C CD2 . LEU   A 1 879  ? 128.075 102.418 117.072 1.00 58.71  0  843  LEU   A CD2 1 
ATOM   6124  N N   . LEU   A 1 880  ? 125.048 104.773 120.079 1.00 57.28  0  844  LEU   A N   1 
ATOM   6125  C CA  . LEU   A 1 880  ? 125.490 105.571 121.214 1.00 53.75  0  844  LEU   A CA  1 
ATOM   6126  C C   . LEU   A 1 880  ? 124.520 105.480 122.380 1.00 49.99  0  844  LEU   A C   1 
ATOM   6127  O O   . LEU   A 1 880  ? 124.946 105.591 123.531 1.00 55.60  0  844  LEU   A O   1 
ATOM   6128  C CB  . LEU   A 1 880  ? 125.725 107.028 120.807 1.00 52.00  0  844  LEU   A CB  1 
ATOM   6129  C CG  . LEU   A 1 880  ? 124.623 107.981 120.365 1.00 52.49  0  844  LEU   A CG  1 
ATOM   6130  C CD1 . LEU   A 1 880  ? 124.026 108.701 121.550 1.00 53.27  0  844  LEU   A CD1 1 
ATOM   6131  C CD2 . LEU   A 1 880  ? 125.226 108.981 119.409 1.00 47.29  0  844  LEU   A CD2 1 
ATOM   6132  N N   . TYR   A 1 881  ? 123.231 105.249 122.119 1.00 50.09  0  845  TYR   A N   1 
ATOM   6133  C CA  . TYR   A 1 881  ? 122.316 104.930 123.208 1.00 55.14  0  845  TYR   A CA  1 
ATOM   6134  C C   . TYR   A 1 881  ? 122.750 103.658 123.916 1.00 54.60  0  845  TYR   A C   1 
ATOM   6135  O O   . TYR   A 1 881  ? 122.785 103.604 125.151 1.00 58.74  0  845  TYR   A O   1 
ATOM   6136  C CB  . TYR   A 1 881  ? 120.895 104.778 122.669 1.00 58.80  0  845  TYR   A CB  1 
ATOM   6137  C CG  . TYR   A 1 881  ? 120.101 106.060 122.631 1.00 60.28  0  845  TYR   A CG  1 
ATOM   6138  C CD1 . TYR   A 1 881  ? 120.708 107.264 122.307 1.00 59.79  0  845  TYR   A CD1 1 
ATOM   6139  C CD2 . TYR   A 1 881  ? 118.741 106.065 122.898 1.00 59.14  0  845  TYR   A CD2 1 
ATOM   6140  C CE1 . TYR   A 1 881  ? 119.988 108.437 122.269 1.00 59.86  0  845  TYR   A CE1 1 
ATOM   6141  C CE2 . TYR   A 1 881  ? 118.012 107.234 122.857 1.00 63.48  0  845  TYR   A CE2 1 
ATOM   6142  C CZ  . TYR   A 1 881  ? 118.641 108.416 122.540 1.00 62.65  0  845  TYR   A CZ  1 
ATOM   6143  O OH  . TYR   A 1 881  ? 117.920 109.585 122.498 1.00 62.60  0  845  TYR   A OH  1 
ATOM   6144  N N   . LYS   A 1 882  ? 123.112 102.631 123.143 1.00 46.16  0  846  LYS   A N   1 
ATOM   6145  C CA  . LYS   A 1 882  ? 123.559 101.373 123.727 1.00 46.85  0  846  LYS   A CA  1 
ATOM   6146  C C   . LYS   A 1 882  ? 124.820 101.565 124.557 1.00 48.48  0  846  LYS   A C   1 
ATOM   6147  O O   . LYS   A 1 882  ? 124.927 101.033 125.664 1.00 50.25  0  846  LYS   A O   1 
ATOM   6148  C CB  . LYS   A 1 882  ? 123.792 100.345 122.623 1.00 53.74  0  846  LYS   A CB  1 
ATOM   6149  C CG  . LYS   A 1 882  ? 123.682 98.904  123.075 1.00 54.83  0  846  LYS   A CG  1 
ATOM   6150  C CD  . LYS   A 1 882  ? 123.671 97.960  121.886 1.00 51.60  0  846  LYS   A CD  1 
ATOM   6151  C CE  . LYS   A 1 882  ? 124.924 98.119  121.045 1.00 47.17  0  846  LYS   A CE  1 
ATOM   6152  N NZ  . LYS   A 1 882  ? 126.146 97.744  121.804 1.00 47.03  1  846  LYS   A NZ  1 
ATOM   6153  N N   . GLU   A 1 883  ? 125.777 102.346 124.055 1.00 52.00  0  847  GLU   A N   1 
ATOM   6154  C CA  . GLU   A 1 883  ? 127.026 102.536 124.793 1.00 48.78  0  847  GLU   A CA  1 
ATOM   6155  C C   . GLU   A 1 883  ? 126.831 103.385 126.050 1.00 53.70  0  847  GLU   A C   1 
ATOM   6156  O O   . GLU   A 1 883  ? 127.337 103.043 127.131 1.00 53.64  0  847  GLU   A O   1 
ATOM   6157  C CB  . GLU   A 1 883  ? 128.082 103.157 123.882 1.00 44.70  0  847  GLU   A CB  1 
ATOM   6158  C CG  . GLU   A 1 883  ? 129.051 102.140 123.306 1.00 52.09  0  847  GLU   A CG  1 
ATOM   6159  C CD  . GLU   A 1 883  ? 129.682 101.267 124.377 1.00 56.31  0  847  GLU   A CD  1 
ATOM   6160  O OE1 . GLU   A 1 883  ? 130.192 101.816 125.376 1.00 58.02  0  847  GLU   A OE1 1 
ATOM   6161  O OE2 . GLU   A 1 883  ? 129.667 100.028 124.221 1.00 54.41  -1 847  GLU   A OE2 1 
ATOM   6162  N N   . TYR   A 1 884  ? 126.100 104.497 125.930 1.00 53.27  0  848  TYR   A N   1 
ATOM   6163  C CA  . TYR   A 1 884  ? 125.830 105.334 127.090 1.00 44.07  0  848  TYR   A CA  1 
ATOM   6164  C C   . TYR   A 1 884  ? 125.075 104.556 128.154 1.00 47.86  0  848  TYR   A C   1 
ATOM   6165  O O   . TYR   A 1 884  ? 125.333 104.716 129.350 1.00 61.46  0  848  TYR   A O   1 
ATOM   6166  C CB  . TYR   A 1 884  ? 125.044 106.574 126.673 1.00 47.41  0  848  TYR   A CB  1 
ATOM   6167  C CG  . TYR   A 1 884  ? 125.908 107.756 126.313 1.00 48.10  0  848  TYR   A CG  1 
ATOM   6168  C CD1 . TYR   A 1 884  ? 126.700 108.376 127.264 1.00 50.39  0  848  TYR   A CD1 1 
ATOM   6169  C CD2 . TYR   A 1 884  ? 125.925 108.257 125.022 1.00 53.73  0  848  TYR   A CD2 1 
ATOM   6170  C CE1 . TYR   A 1 884  ? 127.489 109.458 126.938 1.00 52.39  0  848  TYR   A CE1 1 
ATOM   6171  C CE2 . TYR   A 1 884  ? 126.709 109.338 124.686 1.00 52.34  0  848  TYR   A CE2 1 
ATOM   6172  C CZ  . TYR   A 1 884  ? 127.489 109.935 125.646 1.00 52.09  0  848  TYR   A CZ  1 
ATOM   6173  O OH  . TYR   A 1 884  ? 128.273 111.013 125.312 1.00 48.70  0  848  TYR   A OH  1 
ATOM   6174  N N   . ALA   A 1 885  ? 124.130 103.709 127.741 1.00 42.49  0  849  ALA   A N   1 
ATOM   6175  C CA  . ALA   A 1 885  ? 123.535 102.783 128.693 1.00 46.59  0  849  ALA   A CA  1 
ATOM   6176  C C   . ALA   A 1 885  ? 124.574 101.813 129.225 1.00 50.09  0  849  ALA   A C   1 
ATOM   6177  O O   . ALA   A 1 885  ? 124.476 101.364 130.372 1.00 60.26  0  849  ALA   A O   1 
ATOM   6178  C CB  . ALA   A 1 885  ? 122.379 102.030 128.040 1.00 59.54  0  849  ALA   A CB  1 
ATOM   6179  N N   . GLY   A 1 886  ? 125.577 101.485 128.410 1.00 46.59  0  850  GLY   A N   1 
ATOM   6180  C CA  . GLY   A 1 886  ? 126.650 100.623 128.864 1.00 48.65  0  850  GLY   A CA  1 
ATOM   6181  C C   . GLY   A 1 886  ? 127.402 101.187 130.048 1.00 48.13  0  850  GLY   A C   1 
ATOM   6182  O O   . GLY   A 1 886  ? 127.821 100.437 130.933 1.00 50.27  0  850  GLY   A O   1 
ATOM   6183  N N   . ILE   A 1 887  ? 127.590 102.507 130.088 1.00 49.50  0  851  ILE   A N   1 
ATOM   6184  C CA  . ILE   A 1 887  ? 128.163 103.131 131.281 1.00 49.66  0  851  ILE   A CA  1 
ATOM   6185  C C   . ILE   A 1 887  ? 127.087 103.540 132.282 1.00 46.56  0  851  ILE   A C   1 
ATOM   6186  O O   . ILE   A 1 887  ? 127.377 104.277 133.228 1.00 41.11  0  851  ILE   A O   1 
ATOM   6187  C CB  . ILE   A 1 887  ? 129.042 104.346 130.956 1.00 44.50  0  851  ILE   A CB  1 
ATOM   6188  C CG1 . ILE   A 1 887  ? 128.422 105.200 129.862 1.00 46.81  0  851  ILE   A CG1 1 
ATOM   6189  C CG2 . ILE   A 1 887  ? 130.431 103.893 130.545 1.00 43.20  0  851  ILE   A CG2 1 
ATOM   6190  C CD1 . ILE   A 1 887  ? 129.219 106.432 129.603 1.00 42.67  0  851  ILE   A CD1 1 
ATOM   6191  N N   . GLY   A 1 888  ? 125.848 103.104 132.086 1.00 49.97  0  852  GLY   A N   1 
ATOM   6192  C CA  . GLY   A 1 888  ? 124.796 103.461 133.013 1.00 48.70  0  852  GLY   A CA  1 
ATOM   6193  C C   . GLY   A 1 888  ? 124.228 104.851 132.850 1.00 54.10  0  852  GLY   A C   1 
ATOM   6194  O O   . GLY   A 1 888  ? 123.587 105.355 133.776 1.00 62.62  0  852  GLY   A O   1 
ATOM   6195  N N   . HIS   A 1 889  ? 124.449 105.500 131.709 1.00 50.11  0  853  HIS   A N   1 
ATOM   6196  C CA  . HIS   A 1 889  ? 123.831 106.795 131.431 1.00 47.47  0  853  HIS   A CA  1 
ATOM   6197  C C   . HIS   A 1 889  ? 122.676 106.546 130.467 1.00 55.20  0  853  HIS   A C   1 
ATOM   6198  O O   . HIS   A 1 889  ? 122.826 106.574 129.247 1.00 61.28  0  853  HIS   A O   1 
ATOM   6199  C CB  . HIS   A 1 889  ? 124.850 107.777 130.861 1.00 49.35  0  853  HIS   A CB  1 
ATOM   6200  C CG  . HIS   A 1 889  ? 124.259 109.084 130.424 1.00 59.92  0  853  HIS   A CG  1 
ATOM   6201  N ND1 . HIS   A 1 889  ? 125.026 110.117 129.929 1.00 61.07  0  853  HIS   A ND1 1 
ATOM   6202  C CD2 . HIS   A 1 889  ? 122.983 109.540 130.439 1.00 59.09  0  853  HIS   A CD2 1 
ATOM   6203  C CE1 . HIS   A 1 889  ? 124.246 111.142 129.636 1.00 60.00  0  853  HIS   A CE1 1 
ATOM   6204  N NE2 . HIS   A 1 889  ? 123.002 110.819 129.938 1.00 60.93  0  853  HIS   A NE2 1 
ATOM   6205  N N   . LYS   A 1 890  ? 121.499 106.316 131.036 1.00 67.45  0  854  LYS   A N   1 
ATOM   6206  C CA  . LYS   A 1 890  ? 120.305 106.057 130.237 1.00 66.63  0  854  LYS   A CA  1 
ATOM   6207  C C   . LYS   A 1 890  ? 119.881 107.351 129.557 1.00 67.47  0  854  LYS   A C   1 
ATOM   6208  O O   . LYS   A 1 890  ? 119.219 108.199 130.159 1.00 68.68  0  854  LYS   A O   1 
ATOM   6209  C CB  . LYS   A 1 890  ? 119.191 105.497 131.113 1.00 67.12  0  854  LYS   A CB  1 
ATOM   6210  C CG  . LYS   A 1 890  ? 119.647 104.404 132.061 1.00 68.96  0  854  LYS   A CG  1 
ATOM   6211  C CD  . LYS   A 1 890  ? 118.777 104.351 133.304 1.00 70.56  0  854  LYS   A CD  1 
ATOM   6212  C CE  . LYS   A 1 890  ? 119.565 103.863 134.508 1.00 70.00  0  854  LYS   A CE  1 
ATOM   6213  N NZ  . LYS   A 1 890  ? 119.992 102.444 134.363 1.00 66.97  1  854  LYS   A NZ  1 
ATOM   6214  N N   . LEU   A 1 891  ? 120.263 107.506 128.294 1.00 66.50  0  855  LEU   A N   1 
ATOM   6215  C CA  . LEU   A 1 891  ? 119.916 108.703 127.545 1.00 64.80  0  855  LEU   A CA  1 
ATOM   6216  C C   . LEU   A 1 891  ? 118.410 108.782 127.325 1.00 67.67  0  855  LEU   A C   1 
ATOM   6217  O O   . LEU   A 1 891  ? 117.728 107.768 127.160 1.00 67.45  0  855  LEU   A O   1 
ATOM   6218  C CB  . LEU   A 1 891  ? 120.638 108.711 126.199 1.00 65.27  0  855  LEU   A CB  1 
ATOM   6219  C CG  . LEU   A 1 891  ? 122.011 109.375 126.158 1.00 63.87  0  855  LEU   A CG  1 
ATOM   6220  C CD1 . LEU   A 1 891  ? 122.483 109.503 124.728 1.00 61.20  0  855  LEU   A CD1 1 
ATOM   6221  C CD2 . LEU   A 1 891  ? 121.953 110.731 126.823 1.00 66.48  0  855  LEU   A CD2 1 
ATOM   6222  N N   . LYS   A 1 892  ? 117.894 110.006 127.325 1.00 71.50  0  856  LYS   A N   1 
ATOM   6223  C CA  . LYS   A 1 892  ? 116.482 110.269 127.096 1.00 69.84  0  856  LYS   A CA  1 
ATOM   6224  C C   . LYS   A 1 892  ? 116.302 110.941 125.744 1.00 67.99  0  856  LYS   A C   1 
ATOM   6225  O O   . LYS   A 1 892  ? 117.108 111.789 125.351 1.00 70.86  0  856  LYS   A O   1 
ATOM   6226  C CB  . LYS   A 1 892  ? 115.902 111.154 128.201 1.00 70.73  0  856  LYS   A CB  1 
ATOM   6227  C CG  . LYS   A 1 892  ? 116.500 110.901 129.573 1.00 71.14  0  856  LYS   A CG  1 
ATOM   6228  C CD  . LYS   A 1 892  ? 115.567 111.358 130.680 1.00 72.11  0  856  LYS   A CD  1 
ATOM   6229  C CE  . LYS   A 1 892  ? 115.443 112.872 130.707 1.00 71.38  0  856  LYS   A CE  1 
ATOM   6230  N NZ  . LYS   A 1 892  ? 114.586 113.337 131.832 1.00 70.46  1  856  LYS   A NZ  1 
ATOM   6231  N N   . GLY   A 1 893  ? 115.240 110.559 125.035 1.00 60.74  0  857  GLY   A N   1 
ATOM   6232  C CA  . GLY   A 1 893  ? 114.976 111.135 123.729 1.00 63.02  0  857  GLY   A CA  1 
ATOM   6233  C C   . GLY   A 1 893  ? 114.702 112.623 123.759 1.00 62.67  0  857  GLY   A C   1 
ATOM   6234  O O   . GLY   A 1 893  ? 114.837 113.290 122.729 1.00 63.10  0  857  GLY   A O   1 
ATOM   6235  N N   . THR   A 1 894  ? 114.315 113.160 124.917 1.00 64.99  0  858  THR   A N   1 
ATOM   6236  C CA  . THR   A 1 894  ? 114.076 114.593 125.024 1.00 65.44  0  858  THR   A CA  1 
ATOM   6237  C C   . THR   A 1 894  ? 115.369 115.388 124.908 1.00 64.35  0  858  THR   A C   1 
ATOM   6238  O O   . THR   A 1 894  ? 115.354 116.532 124.439 1.00 65.71  0  858  THR   A O   1 
ATOM   6239  C CB  . THR   A 1 894  ? 113.383 114.912 126.349 1.00 66.30  0  858  THR   A CB  1 
ATOM   6240  O OG1 . THR   A 1 894  ? 114.362 115.020 127.389 1.00 64.80  0  858  THR   A OG1 1 
ATOM   6241  C CG2 . THR   A 1 894  ? 112.403 113.807 126.712 1.00 61.22  0  858  THR   A CG2 1 
ATOM   6242  N N   . GLU   A 1 895  ? 116.493 114.802 125.323 1.00 64.39  0  859  GLU   A N   1 
ATOM   6243  C CA  . GLU   A 1 895  ? 117.760 115.523 125.321 1.00 65.02  0  859  GLU   A CA  1 
ATOM   6244  C C   . GLU   A 1 895  ? 118.437 115.460 123.958 1.00 67.20  0  859  GLU   A C   1 
ATOM   6245  O O   . GLU   A 1 895  ? 118.807 116.493 123.390 1.00 66.97  0  859  GLU   A O   1 
ATOM   6246  C CB  . GLU   A 1 895  ? 118.687 114.952 126.395 1.00 64.42  0  859  GLU   A CB  1 
ATOM   6247  C CG  . GLU   A 1 895  ? 117.983 114.486 127.661 1.00 66.50  0  859  GLU   A CG  1 
ATOM   6248  C CD  . GLU   A 1 895  ? 117.682 115.616 128.628 1.00 69.83  0  859  GLU   A CD  1 
ATOM   6249  O OE1 . GLU   A 1 895  ? 117.674 116.790 128.202 1.00 68.46  0  859  GLU   A OE1 1 
ATOM   6250  O OE2 . GLU   A 1 895  ? 117.455 115.329 129.822 1.00 71.47  -1 859  GLU   A OE2 1 
ATOM   6251  N N   . THR   A 1 896  ? 118.597 114.255 123.418 1.00 63.00  0  860  THR   A N   1 
ATOM   6252  C CA  . THR   A 1 896  ? 119.382 114.034 122.213 1.00 57.68  0  860  THR   A CA  1 
ATOM   6253  C C   . THR   A 1 896  ? 118.509 114.200 120.978 1.00 53.60  0  860  THR   A C   1 
ATOM   6254  O O   . THR   A 1 896  ? 117.386 113.691 120.932 1.00 58.01  0  860  THR   A O   1 
ATOM   6255  C CB  . THR   A 1 896  ? 119.990 112.634 122.228 1.00 53.99  0  860  THR   A CB  1 
ATOM   6256  O OG1 . THR   A 1 896  ? 118.960 111.668 121.995 1.00 62.41  0  860  THR   A OG1 1 
ATOM   6257  C CG2 . THR   A 1 896  ? 120.604 112.355 123.580 1.00 54.33  0  860  THR   A CG2 1 
ATOM   6258  N N   . TYR   A 1 897  ? 119.028 114.907 119.981 1.00 47.20  0  861  TYR   A N   1 
ATOM   6259  C CA  . TYR   A 1 897  ? 118.335 115.021 118.706 1.00 49.00  0  861  TYR   A CA  1 
ATOM   6260  C C   . TYR   A 1 897  ? 119.355 114.957 117.580 1.00 57.49  0  861  TYR   A C   1 
ATOM   6261  O O   . TYR   A 1 897  ? 120.564 115.048 117.802 1.00 64.34  0  861  TYR   A O   1 
ATOM   6262  C CB  . TYR   A 1 897  ? 117.477 116.294 118.632 1.00 50.42  0  861  TYR   A CB  1 
ATOM   6263  C CG  . TYR   A 1 897  ? 118.229 117.590 118.428 1.00 55.49  0  861  TYR   A CG  1 
ATOM   6264  C CD1 . TYR   A 1 897  ? 118.486 118.073 117.154 1.00 55.18  0  861  TYR   A CD1 1 
ATOM   6265  C CD2 . TYR   A 1 897  ? 118.646 118.350 119.510 1.00 54.46  0  861  TYR   A CD2 1 
ATOM   6266  C CE1 . TYR   A 1 897  ? 119.160 119.261 116.963 1.00 55.25  0  861  TYR   A CE1 1 
ATOM   6267  C CE2 . TYR   A 1 897  ? 119.319 119.540 119.329 1.00 54.87  0  861  TYR   A CE2 1 
ATOM   6268  C CZ  . TYR   A 1 897  ? 119.573 119.990 118.053 1.00 54.30  0  861  TYR   A CZ  1 
ATOM   6269  O OH  . TYR   A 1 897  ? 120.244 121.176 117.865 1.00 50.25  0  861  TYR   A OH  1 
ATOM   6270  N N   . ILE   A 1 898  ? 118.859 114.767 116.359 1.00 54.30  0  862  ILE   A N   1 
ATOM   6271  C CA  . ILE   A 1 898  ? 119.708 114.549 115.195 1.00 53.90  0  862  ILE   A CA  1 
ATOM   6272  C C   . ILE   A 1 898  ? 119.392 115.588 114.132 1.00 55.49  0  862  ILE   A C   1 
ATOM   6273  O O   . ILE   A 1 898  ? 118.230 115.956 113.928 1.00 56.69  0  862  ILE   A O   1 
ATOM   6274  C CB  . ILE   A 1 898  ? 119.544 113.127 114.623 1.00 46.59  0  862  ILE   A CB  1 
ATOM   6275  C CG1 . ILE   A 1 898  ? 118.068 112.770 114.477 1.00 49.35  0  862  ILE   A CG1 1 
ATOM   6276  C CG2 . ILE   A 1 898  ? 120.235 112.124 115.511 1.00 45.72  0  862  ILE   A CG2 1 
ATOM   6277  C CD1 . ILE   A 1 898  ? 117.832 111.454 113.775 1.00 54.47  0  862  ILE   A CD1 1 
ATOM   6278  N N   . SER   A 1 899  ? 120.437 116.059 113.459 1.00 55.74  0  863  SER   A N   1 
ATOM   6279  C CA  . SER   A 1 899  ? 120.337 117.016 112.371 1.00 52.64  0  863  SER   A CA  1 
ATOM   6280  C C   . SER   A 1 899  ? 121.208 116.535 111.222 1.00 58.19  0  863  SER   A C   1 
ATOM   6281  O O   . SER   A 1 899  ? 122.145 115.760 111.419 1.00 63.99  0  863  SER   A O   1 
ATOM   6282  C CB  . SER   A 1 899  ? 120.769 118.417 112.807 1.00 58.43  0  863  SER   A CB  1 
ATOM   6283  O OG  . SER   A 1 899  ? 121.380 119.112 111.736 1.00 63.39  0  863  SER   A OG  1 
ATOM   6284  N N   . ARG   A 1 900  ? 120.862 116.956 110.007 1.00 62.47  0  864  ARG   A N   1 
ATOM   6285  C CA  . ARG   A 1 900  ? 121.626 116.512 108.847 1.00 59.36  0  864  ARG   A CA  1 
ATOM   6286  C C   . ARG   A 1 900  ? 123.018 117.134 108.868 1.00 59.86  0  864  ARG   A C   1 
ATOM   6287  O O   . ARG   A 1 900  ? 124.027 116.427 108.955 1.00 64.22  0  864  ARG   A O   1 
ATOM   6288  C CB  . ARG   A 1 900  ? 120.878 116.875 107.561 1.00 64.41  0  864  ARG   A CB  1 
ATOM   6289  C CG  . ARG   A 1 900  ? 121.587 116.584 106.229 1.00 62.35  0  864  ARG   A CG  1 
ATOM   6290  C CD  . ARG   A 1 900  ? 122.499 115.359 106.306 1.00 61.55  0  864  ARG   A CD  1 
ATOM   6291  N NE  . ARG   A 1 900  ? 123.365 115.187 105.142 1.00 66.99  0  864  ARG   A NE  1 
ATOM   6292  C CZ  . ARG   A 1 900  ? 124.401 115.955 104.836 1.00 65.11  0  864  ARG   A CZ  1 
ATOM   6293  N NH1 . ARG   A 1 900  ? 124.751 116.979 105.592 1.00 60.25  1  864  ARG   A NH1 1 
ATOM   6294  N NH2 . ARG   A 1 900  ? 125.113 115.680 103.748 1.00 63.59  0  864  ARG   A NH2 1 
ATOM   6295  N N   . ASP   A 1 901  ? 123.085 118.464 108.800 1.00 70.67  0  865  ASP   A N   1 
ATOM   6296  C CA  . ASP   A 1 901  ? 124.357 119.179 108.716 1.00 78.58  0  865  ASP   A CA  1 
ATOM   6297  C C   . ASP   A 1 901  ? 124.467 120.450 109.549 1.00 79.59  0  865  ASP   A C   1 
ATOM   6298  O O   . ASP   A 1 901  ? 125.582 120.968 109.675 1.00 79.21  0  865  ASP   A O   1 
ATOM   6299  C CB  . ASP   A 1 901  ? 124.670 119.518 107.254 1.00 81.84  0  865  ASP   A CB  1 
ATOM   6300  C CG  . ASP   A 1 901  ? 123.662 120.472 106.648 1.00 82.49  0  865  ASP   A CG  1 
ATOM   6301  O OD1 . ASP   A 1 901  ? 122.461 120.340 106.972 1.00 73.36  0  865  ASP   A OD1 1 
ATOM   6302  O OD2 . ASP   A 1 901  ? 124.062 121.354 105.861 1.00 81.71  -1 865  ASP   A OD2 1 
ATOM   6303  N N   . MET   A 1 902  ? 123.393 120.981 110.127 1.00 80.34  0  866  MET   A N   1 
ATOM   6304  C CA  . MET   A 1 902  ? 123.476 122.238 110.866 1.00 81.40  0  866  MET   A CA  1 
ATOM   6305  C C   . MET   A 1 902  ? 124.130 122.052 112.227 1.00 79.13  0  866  MET   A C   1 
ATOM   6306  O O   . MET   A 1 902  ? 123.846 121.084 112.941 1.00 75.52  0  866  MET   A O   1 
ATOM   6307  C CB  . MET   A 1 902  ? 122.098 122.875 111.041 1.00 77.38  0  866  MET   A CB  1 
ATOM   6308  C CG  . MET   A 1 902  ? 121.129 122.582 109.936 1.00 78.09  0  866  MET   A CG  1 
ATOM   6309  S SD  . MET   A 1 902  ? 122.020 122.777 108.390 1.00 81.62  0  866  MET   A SD  1 
ATOM   6310  C CE  . MET   A 1 902  ? 122.241 124.542 108.330 1.00 72.67  0  866  MET   A CE  1 
ATOM   6311  N N   . GLN   A 1 903  ? 125.004 122.990 112.578 1.00 79.58  0  867  GLN   A N   1 
ATOM   6312  C CA  . GLN   A 1 903  ? 125.623 123.054 113.892 1.00 81.84  0  867  GLN   A CA  1 
ATOM   6313  C C   . GLN   A 1 903  ? 125.147 124.315 114.596 1.00 80.76  0  867  GLN   A C   1 
ATOM   6314  O O   . GLN   A 1 903  ? 125.224 125.413 114.033 1.00 76.69  0  867  GLN   A O   1 
ATOM   6315  C CB  . GLN   A 1 903  ? 127.148 123.054 113.789 1.00 77.80  0  867  GLN   A CB  1 
ATOM   6316  C CG  . GLN   A 1 903  ? 127.714 121.754 113.271 1.00 76.52  0  867  GLN   A CG  1 
ATOM   6317  C CD  . GLN   A 1 903  ? 127.113 120.552 113.965 1.00 80.44  0  867  GLN   A CD  1 
ATOM   6318  O OE1 . GLN   A 1 903  ? 127.150 120.441 115.191 1.00 80.33  0  867  GLN   A OE1 1 
ATOM   6319  N NE2 . GLN   A 1 903  ? 126.537 119.651 113.182 1.00 81.29  0  867  GLN   A NE2 1 
ATOM   6320  N N   . PHE   A 1 904  ? 124.663 124.156 115.822 1.00 77.54  0  868  PHE   A N   1 
ATOM   6321  C CA  . PHE   A 1 904  ? 124.145 125.258 116.621 1.00 77.68  0  868  PHE   A CA  1 
ATOM   6322  C C   . PHE   A 1 904  ? 124.941 125.392 117.907 1.00 78.77  0  868  PHE   A C   1 
ATOM   6323  O O   . PHE   A 1 904  ? 124.392 125.532 119.002 1.00 80.50  0  868  PHE   A O   1 
ATOM   6324  C CB  . PHE   A 1 904  ? 122.662 125.064 116.909 1.00 75.11  0  868  PHE   A CB  1 
ATOM   6325  C CG  . PHE   A 1 904  ? 121.834 124.836 115.678 1.00 79.69  0  868  PHE   A CG  1 
ATOM   6326  C CD1 . PHE   A 1 904  ? 121.685 125.838 114.735 1.00 78.55  0  868  PHE   A CD1 1 
ATOM   6327  C CD2 . PHE   A 1 904  ? 121.208 123.621 115.460 1.00 79.74  0  868  PHE   A CD2 1 
ATOM   6328  C CE1 . PHE   A 1 904  ? 120.925 125.635 113.602 1.00 75.43  0  868  PHE   A CE1 1 
ATOM   6329  C CE2 . PHE   A 1 904  ? 120.445 123.415 114.327 1.00 79.14  0  868  PHE   A CE2 1 
ATOM   6330  C CZ  . PHE   A 1 904  ? 120.302 124.427 113.400 1.00 77.16  0  868  PHE   A CZ  1 
ATOM   6331  N N   . MET   A 1 905  ? 126.263 125.335 117.786 1.00 79.43  0  869  MET   A N   1 
ATOM   6332  C CA  . MET   A 1 905  ? 127.122 125.531 118.939 1.00 80.90  0  869  MET   A CA  1 
ATOM   6333  C C   . MET   A 1 905  ? 127.254 127.019 119.245 1.00 78.53  0  869  MET   A C   1 
ATOM   6334  O O   . MET   A 1 905  ? 126.887 127.881 118.442 1.00 75.90  0  869  MET   A O   1 
ATOM   6335  C CB  . MET   A 1 905  ? 128.494 124.903 118.701 1.00 80.62  0  869  MET   A CB  1 
ATOM   6336  C CG  . MET   A 1 905  ? 128.599 123.372 118.871 1.00 82.35  0  869  MET   A CG  1 
ATOM   6337  S SD  . MET   A 1 905  ? 127.822 122.560 120.295 1.00 91.79  0  869  MET   A SD  1 
ATOM   6338  C CE  . MET   A 1 905  ? 126.083 122.485 119.846 1.00 81.54  0  869  MET   A CE  1 
ATOM   6339  N N   . SER   A 1 906  ? 127.776 127.315 120.436 1.00 78.49  0  870  SER   A N   1 
ATOM   6340  C CA  . SER   A 1 906  ? 127.941 128.687 120.919 1.00 77.94  0  870  SER   A CA  1 
ATOM   6341  C C   . SER   A 1 906  ? 126.609 129.428 120.984 1.00 75.98  0  870  SER   A C   1 
ATOM   6342  O O   . SER   A 1 906  ? 126.570 130.658 120.909 1.00 74.96  0  870  SER   A O   1 
ATOM   6343  C CB  . SER   A 1 906  ? 128.943 129.468 120.063 1.00 78.22  0  870  SER   A CB  1 
ATOM   6344  O OG  . SER   A 1 906  ? 130.197 128.812 120.013 1.00 79.05  0  870  SER   A OG  1 
ATOM   6345  N N   . LYS   A 1 907  ? 125.511 128.681 121.121 1.00 75.43  0  871  LYS   A N   1 
ATOM   6346  C CA  . LYS   A 1 907  ? 124.161 129.240 121.209 1.00 77.53  0  871  LYS   A CA  1 
ATOM   6347  C C   . LYS   A 1 907  ? 123.839 130.149 120.028 1.00 77.14  0  871  LYS   A C   1 
ATOM   6348  O O   . LYS   A 1 907  ? 123.052 131.092 120.160 1.00 70.83  0  871  LYS   A O   1 
ATOM   6349  C CB  . LYS   A 1 907  ? 123.955 129.993 122.529 1.00 74.97  0  871  LYS   A CB  1 
ATOM   6350  C CG  . LYS   A 1 907  ? 123.401 129.143 123.665 1.00 75.01  0  871  LYS   A CG  1 
ATOM   6351  C CD  . LYS   A 1 907  ? 121.879 129.161 123.671 1.00 77.51  0  871  LYS   A CD  1 
ATOM   6352  C CE  . LYS   A 1 907  ? 121.321 128.683 125.001 1.00 75.03  0  871  LYS   A CE  1 
ATOM   6353  N NZ  . LYS   A 1 907  ? 119.834 128.713 125.023 1.00 69.28  1  871  LYS   A NZ  1 
ATOM   6354  N N   . THR   A 1 908  ? 124.434 129.881 118.868 1.00 66.30  0  872  THR   A N   1 
ATOM   6355  C CA  . THR   A 1 908  ? 124.220 130.682 117.673 1.00 60.86  0  872  THR   A CA  1 
ATOM   6356  C C   . THR   A 1 908  ? 123.771 129.785 116.528 1.00 56.81  0  872  THR   A C   1 
ATOM   6357  O O   . THR   A 1 908  ? 124.061 128.586 116.505 1.00 57.06  0  872  THR   A O   1 
ATOM   6358  C CB  . THR   A 1 908  ? 125.490 131.457 117.279 1.00 60.79  0  872  THR   A CB  1 
ATOM   6359  O OG1 . THR   A 1 908  ? 125.157 132.474 116.327 1.00 62.28  0  872  THR   A OG1 1 
ATOM   6360  C CG2 . THR   A 1 908  ? 126.530 130.531 116.677 1.00 61.89  0  872  THR   A CG2 1 
ATOM   6361  N N   . ILE   A 1 909  ? 123.044 130.376 115.586 1.00 42.19  0  873  ILE   A N   1 
ATOM   6362  C CA  . ILE   A 1 909  ? 122.462 129.653 114.462 1.00 40.50  0  873  ILE   A CA  1 
ATOM   6363  C C   . ILE   A 1 909  ? 123.290 129.942 113.220 1.00 39.87  0  873  ILE   A C   1 
ATOM   6364  O O   . ILE   A 1 909  ? 123.588 131.103 112.918 1.00 45.74  0  873  ILE   A O   1 
ATOM   6365  C CB  . ILE   A 1 909  ? 120.991 130.046 114.247 1.00 43.72  0  873  ILE   A CB  1 
ATOM   6366  C CG1 . ILE   A 1 909  ? 120.225 130.005 115.569 1.00 41.72  0  873  ILE   A CG1 1 
ATOM   6367  C CG2 . ILE   A 1 909  ? 120.340 129.137 113.228 1.00 43.91  0  873  ILE   A CG2 1 
ATOM   6368  C CD1 . ILE   A 1 909  ? 120.246 128.665 116.244 1.00 44.15  0  873  ILE   A CD1 1 
ATOM   6369  N N   . GLN   A 1 910  ? 123.670 128.887 112.507 1.00 39.67  0  874  GLN   A N   1 
ATOM   6370  C CA  . GLN   A 1 910  ? 124.482 128.996 111.304 1.00 37.58  0  874  GLN   A CA  1 
ATOM   6371  C C   . GLN   A 1 910  ? 123.848 128.164 110.202 1.00 40.37  0  874  GLN   A C   1 
ATOM   6372  O O   . GLN   A 1 910  ? 123.688 126.950 110.352 1.00 48.89  0  874  GLN   A O   1 
ATOM   6373  C CB  . GLN   A 1 910  ? 125.913 128.530 111.574 1.00 44.04  0  874  GLN   A CB  1 
ATOM   6374  C CG  . GLN   A 1 910  ? 126.733 128.218 110.335 1.00 51.10  0  874  GLN   A CG  1 
ATOM   6375  C CD  . GLN   A 1 910  ? 127.575 129.388 109.877 1.00 51.25  0  874  GLN   A CD  1 
ATOM   6376  O OE1 . GLN   A 1 910  ? 127.279 130.540 110.188 1.00 48.48  0  874  GLN   A OE1 1 
ATOM   6377  N NE2 . GLN   A 1 910  ? 128.654 129.093 109.164 1.00 45.94  0  874  GLN   A NE2 1 
ATOM   6378  N N   . HIS   A 1 911  ? 123.492 128.815 109.100 1.00 36.54  0  875  HIS   A N   1 
ATOM   6379  C CA  . HIS   A 1 911  ? 122.854 128.151 107.970 1.00 40.03  0  875  HIS   A CA  1 
ATOM   6380  C C   . HIS   A 1 911  ? 123.665 128.432 106.717 1.00 46.97  0  875  HIS   A C   1 
ATOM   6381  O O   . HIS   A 1 911  ? 123.749 129.583 106.278 1.00 54.21  0  875  HIS   A O   1 
ATOM   6382  C CB  . HIS   A 1 911  ? 121.410 128.625 107.795 1.00 40.96  0  875  HIS   A CB  1 
ATOM   6383  C CG  . HIS   A 1 911  ? 120.658 127.899 106.723 1.00 45.35  0  875  HIS   A CG  1 
ATOM   6384  N ND1 . HIS   A 1 911  ? 120.495 126.532 106.723 1.00 40.27  0  875  HIS   A ND1 1 
ATOM   6385  C CD2 . HIS   A 1 911  ? 120.017 128.353 105.621 1.00 48.09  0  875  HIS   A CD2 1 
ATOM   6386  C CE1 . HIS   A 1 911  ? 119.793 126.172 105.664 1.00 43.53  0  875  HIS   A CE1 1 
ATOM   6387  N NE2 . HIS   A 1 911  ? 119.489 127.260 104.979 1.00 48.36  0  875  HIS   A NE2 1 
ATOM   6388  N N   . ASN   A 1 912  ? 124.269 127.383 106.156 1.00 43.06  0  876  ASN   A N   1 
ATOM   6389  C CA  . ASN   A 1 912  ? 125.015 127.474 104.902 1.00 36.21  0  876  ASN   A CA  1 
ATOM   6390  C C   . ASN   A 1 912  ? 126.059 128.584 104.952 1.00 40.53  0  876  ASN   A C   1 
ATOM   6391  O O   . ASN   A 1 912  ? 126.226 129.354 104.005 1.00 46.80  0  876  ASN   A O   1 
ATOM   6392  C CB  . ASN   A 1 912  ? 124.073 127.673 103.714 1.00 37.86  0  876  ASN   A CB  1 
ATOM   6393  C CG  . ASN   A 1 912  ? 123.368 126.396 103.313 1.00 46.78  0  876  ASN   A CG  1 
ATOM   6394  O OD1 . ASN   A 1 912  ? 123.857 125.298 103.570 1.00 51.59  0  876  ASN   A OD1 1 
ATOM   6395  N ND2 . ASN   A 1 912  ? 122.214 126.534 102.672 1.00 45.13  0  876  ASN   A ND2 1 
ATOM   6396  N N   . GLY   A 1 913  ? 126.763 128.673 106.075 1.00 34.78  0  877  GLY   A N   1 
ATOM   6397  C CA  . GLY   A 1 913  ? 127.806 129.669 106.194 1.00 42.56  0  877  GLY   A CA  1 
ATOM   6398  C C   . GLY   A 1 913  ? 127.328 131.077 106.455 1.00 41.83  0  877  GLY   A C   1 
ATOM   6399  O O   . GLY   A 1 913  ? 128.088 132.024 106.246 1.00 48.00  0  877  GLY   A O   1 
ATOM   6400  N N   . VAL   A 1 914  ? 126.087 131.248 106.896 1.00 33.58  0  878  VAL   A N   1 
ATOM   6401  C CA  . VAL   A 1 914  ? 125.551 132.549 107.273 1.00 25.85  0  878  VAL   A CA  1 
ATOM   6402  C C   . VAL   A 1 914  ? 125.159 132.489 108.739 1.00 31.61  0  878  VAL   A C   1 
ATOM   6403  O O   . VAL   A 1 914  ? 124.497 131.540 109.172 1.00 47.14  0  878  VAL   A O   1 
ATOM   6404  C CB  . VAL   A 1 914  ? 124.347 132.944 106.400 1.00 30.38  0  878  VAL   A CB  1 
ATOM   6405  C CG1 . VAL   A 1 914  ? 123.783 134.264 106.859 1.00 25.78  0  878  VAL   A CG1 1 
ATOM   6406  C CG2 . VAL   A 1 914  ? 124.753 133.015 104.947 1.00 32.32  0  878  VAL   A CG2 1 
ATOM   6407  N N   . TYR   A 1 915  ? 125.577 133.489 109.505 1.00 39.47  0  879  TYR   A N   1 
ATOM   6408  C CA  . TYR   A 1 915  ? 125.303 133.537 110.933 1.00 41.84  0  879  TYR   A CA  1 
ATOM   6409  C C   . TYR   A 1 915  ? 124.062 134.371 111.203 1.00 38.21  0  879  TYR   A C   1 
ATOM   6410  O O   . TYR   A 1 915  ? 123.926 135.486 110.691 1.00 39.88  0  879  TYR   A O   1 
ATOM   6411  C CB  . TYR   A 1 915  ? 126.490 134.110 111.705 1.00 45.44  0  879  TYR   A CB  1 
ATOM   6412  C CG  . TYR   A 1 915  ? 127.482 133.063 112.148 1.00 50.75  0  879  TYR   A CG  1 
ATOM   6413  C CD1 . TYR   A 1 915  ? 127.095 132.024 112.980 1.00 41.94  0  879  TYR   A CD1 1 
ATOM   6414  C CD2 . TYR   A 1 915  ? 128.805 133.112 111.730 1.00 51.92  0  879  TYR   A CD2 1 
ATOM   6415  C CE1 . TYR   A 1 915  ? 127.997 131.061 113.386 1.00 45.62  0  879  TYR   A CE1 1 
ATOM   6416  C CE2 . TYR   A 1 915  ? 129.713 132.155 112.131 1.00 51.23  0  879  TYR   A CE2 1 
ATOM   6417  C CZ  . TYR   A 1 915  ? 129.304 131.132 112.958 1.00 51.86  0  879  TYR   A CZ  1 
ATOM   6418  O OH  . TYR   A 1 915  ? 130.208 130.176 113.360 1.00 50.37  0  879  TYR   A OH  1 
ATOM   6419  N N   . TYR   A 1 916  ? 123.157 133.819 112.000 1.00 30.25  0  880  TYR   A N   1 
ATOM   6420  C CA  . TYR   A 1 916  ? 121.937 134.507 112.411 1.00 30.72  0  880  TYR   A CA  1 
ATOM   6421  C C   . TYR   A 1 916  ? 122.010 134.758 113.906 1.00 33.15  0  880  TYR   A C   1 
ATOM   6422  O O   . TYR   A 1 916  ? 121.865 133.809 114.699 1.00 28.06  0  880  TYR   A O   1 
ATOM   6423  C CB  . TYR   A 1 916  ? 120.706 133.679 112.055 1.00 34.21  0  880  TYR   A CB  1 
ATOM   6424  C CG  . TYR   A 1 916  ? 120.606 133.369 110.585 1.00 27.34  0  880  TYR   A CG  1 
ATOM   6425  C CD1 . TYR   A 1 916  ? 119.950 134.228 109.724 1.00 30.65  0  880  TYR   A CD1 1 
ATOM   6426  C CD2 . TYR   A 1 916  ? 121.179 132.229 110.057 1.00 25.68  0  880  TYR   A CD2 1 
ATOM   6427  C CE1 . TYR   A 1 916  ? 119.857 133.955 108.381 1.00 28.34  0  880  TYR   A CE1 1 
ATOM   6428  C CE2 . TYR   A 1 916  ? 121.095 131.950 108.716 1.00 30.85  0  880  TYR   A CE2 1 
ATOM   6429  C CZ  . TYR   A 1 916  ? 120.431 132.815 107.883 1.00 35.38  0  880  TYR   A CZ  1 
ATOM   6430  O OH  . TYR   A 1 916  ? 120.342 132.540 106.541 1.00 40.71  0  880  TYR   A OH  1 
ATOM   6431  N N   . PRO   A 1 917  ? 122.244 135.988 114.341 1.00 30.51  0  881  PRO   A N   1 
ATOM   6432  C CA  . PRO   A 1 917  ? 122.533 136.224 115.757 1.00 30.78  0  881  PRO   A CA  1 
ATOM   6433  C C   . PRO   A 1 917  ? 121.303 136.557 116.579 1.00 35.94  0  881  PRO   A C   1 
ATOM   6434  O O   . PRO   A 1 917  ? 120.350 137.161 116.079 1.00 34.31  0  881  PRO   A O   1 
ATOM   6435  C CB  . PRO   A 1 917  ? 123.498 137.409 115.703 1.00 28.62  0  881  PRO   A CB  1 
ATOM   6436  C CG  . PRO   A 1 917  ? 123.015 138.191 114.518 1.00 31.30  0  881  PRO   A CG  1 
ATOM   6437  C CD  . PRO   A 1 917  ? 122.399 137.215 113.542 1.00 26.31  0  881  PRO   A CD  1 
ATOM   6438  N N   . ALA   A 1 918  ? 121.319 136.162 117.850 1.00 31.50  0  882  ALA   A N   1 
ATOM   6439  C CA  . ALA   A 1 918  ? 120.316 136.609 118.814 1.00 20.68  0  882  ALA   A CA  1 
ATOM   6440  C C   . ALA   A 1 918  ? 120.869 137.814 119.572 1.00 25.08  0  882  ALA   A C   1 
ATOM   6441  O O   . ALA   A 1 918  ? 121.127 137.778 120.774 1.00 36.11  0  882  ALA   A O   1 
ATOM   6442  C CB  . ALA   A 1 918  ? 119.934 135.475 119.754 1.00 26.24  0  882  ALA   A CB  1 
ATOM   6443  N N   . SER   A 1 919  ? 121.073 138.897 118.819 1.00 18.97  0  883  SER   A N   1 
ATOM   6444  C CA  . SER   A 1 919  ? 121.651 140.107 119.395 1.00 28.81  0  883  SER   A CA  1 
ATOM   6445  C C   . SER   A 1 919  ? 120.729 140.720 120.442 1.00 34.98  0  883  SER   A C   1 
ATOM   6446  O O   . SER   A 1 919  ? 121.177 141.113 121.526 1.00 31.54  0  883  SER   A O   1 
ATOM   6447  C CB  . SER   A 1 919  ? 121.959 141.112 118.288 1.00 35.49  0  883  SER   A CB  1 
ATOM   6448  O OG  . SER   A 1 919  ? 120.779 141.496 117.610 1.00 32.39  0  883  SER   A OG  1 
ATOM   6449  N N   . ILE   A 1 920  ? 119.428 140.782 120.146 1.00 29.17  0  884  ILE   A N   1 
ATOM   6450  C CA  . ILE   A 1 920  ? 118.477 141.420 121.052 1.00 13.95  0  884  ILE   A CA  1 
ATOM   6451  C C   . ILE   A 1 920  ? 118.487 140.742 122.412 1.00 12.14  0  884  ILE   A C   1 
ATOM   6452  O O   . ILE   A 1 920  ? 118.273 141.394 123.440 1.00 13.23  0  884  ILE   A O   1 
ATOM   6453  C CB  . ILE   A 1 920  ? 117.069 141.422 120.426 1.00 10.84  0  884  ILE   A CB  1 
ATOM   6454  C CG1 . ILE   A 1 920  ? 117.023 142.363 119.225 1.00 23.03  0  884  ILE   A CG1 1 
ATOM   6455  C CG2 . ILE   A 1 920  ? 116.028 141.845 121.435 1.00 24.41  0  884  ILE   A CG2 1 
ATOM   6456  C CD1 . ILE   A 1 920  ? 115.632 142.586 118.681 1.00 20.96  0  884  ILE   A CD1 1 
ATOM   6457  N N   . LYS   A 1 921  ? 118.769 139.440 122.451 1.00 19.82  0  885  LYS   A N   1 
ATOM   6458  C CA  . LYS   A 1 921  ? 118.790 138.718 123.716 1.00 23.57  0  885  LYS   A CA  1 
ATOM   6459  C C   . LYS   A 1 921  ? 119.809 139.285 124.696 1.00 28.96  0  885  LYS   A C   1 
ATOM   6460  O O   . LYS   A 1 921  ? 119.651 139.106 125.908 1.00 37.30  0  885  LYS   A O   1 
ATOM   6461  C CB  . LYS   A 1 921  ? 119.083 137.238 123.469 1.00 20.22  0  885  LYS   A CB  1 
ATOM   6462  C CG  . LYS   A 1 921  ? 118.954 136.367 124.702 1.00 25.08  0  885  LYS   A CG  1 
ATOM   6463  C CD  . LYS   A 1 921  ? 119.356 134.934 124.423 1.00 29.76  0  885  LYS   A CD  1 
ATOM   6464  C CE  . LYS   A 1 921  ? 119.121 134.062 125.644 1.00 35.03  0  885  LYS   A CE  1 
ATOM   6465  N NZ  . LYS   A 1 921  ? 119.548 132.657 125.421 1.00 31.79  1  885  LYS   A NZ  1 
ATOM   6466  N N   . LYS   A 1 922  ? 120.842 139.972 124.213 1.00 22.49  0  886  LYS   A N   1 
ATOM   6467  C CA  . LYS   A 1 922  ? 121.894 140.457 125.097 1.00 20.67  0  886  LYS   A CA  1 
ATOM   6468  C C   . LYS   A 1 922  ? 121.719 141.908 125.517 1.00 27.54  0  886  LYS   A C   1 
ATOM   6469  O O   . LYS   A 1 922  ? 122.266 142.309 126.549 1.00 29.74  0  886  LYS   A O   1 
ATOM   6470  C CB  . LYS   A 1 922  ? 123.260 140.288 124.428 1.00 27.06  0  886  LYS   A CB  1 
ATOM   6471  C CG  . LYS   A 1 922  ? 123.569 138.856 124.039 1.00 25.16  0  886  LYS   A CG  1 
ATOM   6472  C CD  . LYS   A 1 922  ? 124.665 138.790 122.997 1.00 27.29  0  886  LYS   A CD  1 
ATOM   6473  C CE  . LYS   A 1 922  ? 124.081 138.728 121.604 1.00 25.86  0  886  LYS   A CE  1 
ATOM   6474  N NZ  . LYS   A 1 922  ? 123.518 137.388 121.295 1.00 27.30  1  886  LYS   A NZ  1 
ATOM   6475  N N   . VAL   A 1 923  ? 120.966 142.701 124.759 1.00 27.69  0  887  VAL   A N   1 
ATOM   6476  C CA  . VAL   A 1 923  ? 120.790 144.116 125.057 1.00 12.73  0  887  VAL   A CA  1 
ATOM   6477  C C   . VAL   A 1 923  ? 119.474 144.332 125.788 1.00 16.84  0  887  VAL   A C   1 
ATOM   6478  O O   . VAL   A 1 923  ? 118.955 145.452 125.828 1.00 33.84  0  887  VAL   A O   1 
ATOM   6479  C CB  . VAL   A 1 923  ? 120.833 144.961 123.775 1.00 17.80  0  887  VAL   A CB  1 
ATOM   6480  C CG1 . VAL   A 1 923  ? 122.188 144.864 123.127 1.00 19.70  0  887  VAL   A CG1 1 
ATOM   6481  C CG2 . VAL   A 1 923  ? 119.769 144.492 122.823 1.00 29.00  0  887  VAL   A CG2 1 
ATOM   6482  N N   . LEU   A 1 924  ? 118.914 143.262 126.353 1.00 21.91  0  888  LEU   A N   1 
ATOM   6483  C CA  . LEU   A 1 924  ? 117.649 143.382 127.072 1.00 15.31  0  888  LEU   A CA  1 
ATOM   6484  C C   . LEU   A 1 924  ? 117.809 144.211 128.337 1.00 12.02  0  888  LEU   A C   1 
ATOM   6485  O O   . LEU   A 1 924  ? 116.983 145.080 128.632 1.00 11.21  0  888  LEU   A O   1 
ATOM   6486  C CB  . LEU   A 1 924  ? 117.103 141.997 127.414 1.00 15.72  0  888  LEU   A CB  1 
ATOM   6487  C CG  . LEU   A 1 924  ? 116.612 141.131 126.260 1.00 18.04  0  888  LEU   A CG  1 
ATOM   6488  C CD1 . LEU   A 1 924  ? 115.925 139.890 126.788 1.00 15.83  0  888  LEU   A CD1 1 
ATOM   6489  C CD2 . LEU   A 1 924  ? 115.685 141.929 125.385 1.00 8.51   0  888  LEU   A CD2 1 
ATOM   6490  N N   . ARG   A 1 925  ? 118.880 143.968 129.090 1.00 22.11  0  889  ARG   A N   1 
ATOM   6491  C CA  . ARG   A 1 925  ? 119.068 144.560 130.408 1.00 28.89  0  889  ARG   A CA  1 
ATOM   6492  C C   . ARG   A 1 925  ? 119.837 145.873 130.361 1.00 28.01  0  889  ARG   A C   1 
ATOM   6493  O O   . ARG   A 1 925  ? 120.547 146.201 131.319 1.00 30.46  0  889  ARG   A O   1 
ATOM   6494  C CB  . ARG   A 1 925  ? 119.774 143.564 131.327 1.00 30.11  0  889  ARG   A CB  1 
ATOM   6495  C CG  . ARG   A 1 925  ? 118.876 142.454 131.844 1.00 31.93  0  889  ARG   A CG  1 
ATOM   6496  C CD  . ARG   A 1 925  ? 118.345 142.765 133.230 1.00 36.40  0  889  ARG   A CD  1 
ATOM   6497  N NE  . ARG   A 1 925  ? 119.324 142.469 134.268 1.00 40.43  0  889  ARG   A NE  1 
ATOM   6498  C CZ  . ARG   A 1 925  ? 119.509 141.270 134.803 1.00 33.22  0  889  ARG   A CZ  1 
ATOM   6499  N NH1 . ARG   A 1 925  ? 118.803 140.224 134.411 1.00 36.13  1  889  ARG   A NH1 1 
ATOM   6500  N NH2 . ARG   A 1 925  ? 120.422 141.119 135.758 1.00 21.49  0  889  ARG   A NH2 1 
ATOM   6501  N N   . VAL   A 1 926  ? 119.722 146.633 129.274 1.00 19.68  0  890  VAL   A N   1 
ATOM   6502  C CA  . VAL   A 1 926  ? 120.430 147.906 129.136 1.00 12.56  0  890  VAL   A CA  1 
ATOM   6503  C C   . VAL   A 1 926  ? 119.604 148.945 129.888 1.00 24.12  0  890  VAL   A C   1 
ATOM   6504  O O   . VAL   A 1 926  ? 118.698 149.572 129.343 1.00 29.87  0  890  VAL   A O   1 
ATOM   6505  C CB  . VAL   A 1 926  ? 120.657 148.282 127.675 1.00 7.97   0  890  VAL   A CB  1 
ATOM   6506  C CG1 . VAL   A 1 926  ? 121.204 149.687 127.568 1.00 15.02  0  890  VAL   A CG1 1 
ATOM   6507  C CG2 . VAL   A 1 926  ? 121.616 147.305 127.036 1.00 20.50  0  890  VAL   A CG2 1 
ATOM   6508  N N   . GLY   A 1 927  ? 119.920 149.114 131.167 1.00 30.54  0  891  GLY   A N   1 
ATOM   6509  C CA  . GLY   A 1 927  ? 119.309 150.128 131.989 1.00 23.70  0  891  GLY   A CA  1 
ATOM   6510  C C   . GLY   A 1 927  ? 120.353 151.098 132.496 1.00 23.70  0  891  GLY   A C   1 
ATOM   6511  O O   . GLY   A 1 927  ? 121.527 151.017 132.128 1.00 30.78  0  891  GLY   A O   1 
ATOM   6512  N N   . PRO   A 1 928  ? 119.948 152.045 133.334 1.00 18.53  0  892  PRO   A N   1 
ATOM   6513  C CA  . PRO   A 1 928  ? 120.900 153.056 133.812 1.00 25.36  0  892  PRO   A CA  1 
ATOM   6514  C C   . PRO   A 1 928  ? 122.086 152.511 134.601 1.00 35.51  0  892  PRO   A C   1 
ATOM   6515  O O   . PRO   A 1 928  ? 123.232 152.675 134.171 1.00 43.92  0  892  PRO   A O   1 
ATOM   6516  C CB  . PRO   A 1 928  ? 120.027 153.965 134.687 1.00 31.11  0  892  PRO   A CB  1 
ATOM   6517  C CG  . PRO   A 1 928  ? 118.823 153.156 135.014 1.00 29.42  0  892  PRO   A CG  1 
ATOM   6518  C CD  . PRO   A 1 928  ? 118.586 152.296 133.825 1.00 27.24  0  892  PRO   A CD  1 
ATOM   6519  N N   . TRP   A 1 929  ? 121.849 151.872 135.742 1.00 29.32  0  893  TRP   A N   1 
ATOM   6520  C CA  . TRP   A 1 929  ? 122.941 151.460 136.629 1.00 33.52  0  893  TRP   A CA  1 
ATOM   6521  C C   . TRP   A 1 929  ? 123.236 149.967 136.494 1.00 33.91  0  893  TRP   A C   1 
ATOM   6522  O O   . TRP   A 1 929  ? 123.094 149.198 137.442 1.00 39.94  0  893  TRP   A O   1 
ATOM   6523  C CB  . TRP   A 1 929  ? 122.614 151.827 138.074 1.00 32.28  0  893  TRP   A CB  1 
ATOM   6524  C CG  . TRP   A 1 929  ? 121.956 153.163 138.228 1.00 37.56  0  893  TRP   A CG  1 
ATOM   6525  C CD1 . TRP   A 1 929  ? 120.619 153.412 138.315 1.00 36.39  0  893  TRP   A CD1 1 
ATOM   6526  C CD2 . TRP   A 1 929  ? 122.606 154.436 138.319 1.00 37.67  0  893  TRP   A CD2 1 
ATOM   6527  N NE1 . TRP   A 1 929  ? 120.396 154.758 138.450 1.00 26.83  0  893  TRP   A NE1 1 
ATOM   6528  C CE2 . TRP   A 1 929  ? 121.600 155.409 138.454 1.00 30.16  0  893  TRP   A CE2 1 
ATOM   6529  C CE3 . TRP   A 1 929  ? 123.941 154.846 138.294 1.00 37.98  0  893  TRP   A CE3 1 
ATOM   6530  C CZ2 . TRP   A 1 929  ? 121.886 156.765 138.566 1.00 33.08  0  893  TRP   A CZ2 1 
ATOM   6531  C CZ3 . TRP   A 1 929  ? 124.222 156.193 138.406 1.00 40.35  0  893  TRP   A CZ3 1 
ATOM   6532  C CH2 . TRP   A 1 929  ? 123.200 157.135 138.540 1.00 35.38  0  893  TRP   A CH2 1 
ATOM   6533  N N   . ILE   A 1 930  ? 123.688 149.557 135.315 1.00 30.98  0  894  ILE   A N   1 
ATOM   6534  C CA  . ILE   A 1 930  ? 123.887 148.141 135.026 1.00 34.85  0  894  ILE   A CA  1 
ATOM   6535  C C   . ILE   A 1 930  ? 125.353 147.774 135.204 1.00 38.35  0  894  ILE   A C   1 
ATOM   6536  O O   . ILE   A 1 930  ? 126.248 148.514 134.779 1.00 42.30  0  894  ILE   A O   1 
ATOM   6537  C CB  . ILE   A 1 930  ? 123.398 147.788 133.612 1.00 26.70  0  894  ILE   A CB  1 
ATOM   6538  C CG1 . ILE   A 1 930  ? 124.156 148.580 132.552 1.00 26.26  0  894  ILE   A CG1 1 
ATOM   6539  C CG2 . ILE   A 1 930  ? 121.919 148.042 133.493 1.00 27.33  0  894  ILE   A CG2 1 
ATOM   6540  C CD1 . ILE   A 1 930  ? 123.671 148.313 131.155 1.00 30.05  0  894  ILE   A CD1 1 
ATOM   6541  N N   . ASN   A 1 931  ? 125.593 146.628 135.845 1.00 42.27  0  895  ASN   A N   1 
ATOM   6542  C CA  . ASN   A 1 931  ? 126.922 146.034 135.988 1.00 41.21  0  895  ASN   A CA  1 
ATOM   6543  C C   . ASN   A 1 931  ? 127.898 147.029 136.620 1.00 39.41  0  895  ASN   A C   1 
ATOM   6544  O O   . ASN   A 1 931  ? 128.889 147.449 136.023 1.00 35.54  0  895  ASN   A O   1 
ATOM   6545  C CB  . ASN   A 1 931  ? 127.444 145.536 134.636 1.00 35.62  0  895  ASN   A CB  1 
ATOM   6546  C CG  . ASN   A 1 931  ? 126.807 144.234 134.212 1.00 42.79  0  895  ASN   A CG  1 
ATOM   6547  O OD1 . ASN   A 1 931  ? 126.516 143.373 135.041 1.00 46.65  0  895  ASN   A OD1 1 
ATOM   6548  N ND2 . ASN   A 1 931  ? 126.588 144.080 132.912 1.00 45.03  0  895  ASN   A ND2 1 
ATOM   6549  N N   . THR   A 1 932  ? 127.584 147.394 137.858 1.00 39.53  0  896  THR   A N   1 
ATOM   6550  C CA  . THR   A 1 932  ? 128.347 148.417 138.550 1.00 44.17  0  896  THR   A CA  1 
ATOM   6551  C C   . THR   A 1 932  ? 128.348 148.126 140.042 1.00 45.75  0  896  THR   A C   1 
ATOM   6552  O O   . THR   A 1 932  ? 127.538 147.347 140.549 1.00 47.16  0  896  THR   A O   1 
ATOM   6553  C CB  . THR   A 1 932  ? 127.783 149.811 138.276 1.00 42.49  0  896  THR   A CB  1 
ATOM   6554  O OG1 . THR   A 1 932  ? 128.621 150.789 138.892 1.00 38.31  0  896  THR   A OG1 1 
ATOM   6555  C CG2 . THR   A 1 932  ? 126.383 149.933 138.842 1.00 45.45  0  896  THR   A CG2 1 
ATOM   6556  N N   . ILE   A 1 933  ? 129.283 148.764 140.740 1.00 43.20  0  897  ILE   A N   1 
ATOM   6557  C CA  . ILE   A 1 933  ? 129.407 148.675 142.188 1.00 45.33  0  897  ILE   A CA  1 
ATOM   6558  C C   . ILE   A 1 933  ? 129.195 150.068 142.759 1.00 48.55  0  897  ILE   A C   1 
ATOM   6559  O O   . ILE   A 1 933  ? 129.807 151.033 142.287 1.00 52.49  0  897  ILE   A O   1 
ATOM   6560  C CB  . ILE   A 1 933  ? 130.778 148.116 142.610 1.00 47.15  0  897  ILE   A CB  1 
ATOM   6561  C CG1 . ILE   A 1 933  ? 131.194 146.966 141.691 1.00 45.80  0  897  ILE   A CG1 1 
ATOM   6562  C CG2 . ILE   A 1 933  ? 130.739 147.649 144.053 1.00 49.29  0  897  ILE   A CG2 1 
ATOM   6563  C CD1 . ILE   A 1 933  ? 130.310 145.745 141.797 1.00 44.44  0  897  ILE   A CD1 1 
ATOM   6564  N N   . LEU   A 1 934  ? 128.321 150.171 143.762 1.00 45.33  0  898  LEU   A N   1 
ATOM   6565  C CA  . LEU   A 1 934  ? 127.968 151.451 144.379 1.00 41.33  0  898  LEU   A CA  1 
ATOM   6566  C C   . LEU   A 1 934  ? 127.376 152.416 143.355 1.00 43.94  0  898  LEU   A C   1 
ATOM   6567  O O   . LEU   A 1 934  ? 127.547 153.632 143.454 1.00 41.24  0  898  LEU   A O   1 
ATOM   6568  C CB  . LEU   A 1 934  ? 129.168 152.085 145.085 1.00 39.17  0  898  LEU   A CB  1 
ATOM   6569  C CG  . LEU   A 1 934  ? 129.464 151.647 146.516 1.00 41.75  0  898  LEU   A CG  1 
ATOM   6570  C CD1 . LEU   A 1 934  ? 130.131 150.291 146.534 1.00 42.43  0  898  LEU   A CD1 1 
ATOM   6571  C CD2 . LEU   A 1 934  ? 130.334 152.673 147.205 1.00 47.75  0  898  LEU   A CD2 1 
ATOM   6572  N N   . ASP   A 1 935  ? 126.668 151.866 142.369 1.00 43.89  0  899  ASP   A N   1 
ATOM   6573  C CA  . ASP   A 1 935  ? 125.995 152.657 141.338 1.00 38.00  0  899  ASP   A CA  1 
ATOM   6574  C C   . ASP   A 1 935  ? 126.958 153.626 140.661 1.00 39.54  0  899  ASP   A C   1 
ATOM   6575  O O   . ASP   A 1 935  ? 126.642 154.796 140.441 1.00 38.22  0  899  ASP   A O   1 
ATOM   6576  C CB  . ASP   A 1 935  ? 124.791 153.403 141.912 1.00 44.27  0  899  ASP   A CB  1 
ATOM   6577  C CG  . ASP   A 1 935  ? 123.686 152.469 142.358 1.00 51.04  0  899  ASP   A CG  1 
ATOM   6578  O OD1 . ASP   A 1 935  ? 123.601 151.347 141.818 1.00 51.56  0  899  ASP   A OD1 1 
ATOM   6579  O OD2 . ASP   A 1 935  ? 122.897 152.857 143.243 1.00 49.65  -1 899  ASP   A OD2 1 
ATOM   6580  N N   . ASP   A 1 936  ? 128.146 153.128 140.322 1.00 49.49  0  900  ASP   A N   1 
ATOM   6581  C CA  . ASP   A 1 936  ? 129.147 153.957 139.665 1.00 42.24  0  900  ASP   A CA  1 
ATOM   6582  C C   . ASP   A 1 936  ? 128.628 154.447 138.322 1.00 38.49  0  900  ASP   A C   1 
ATOM   6583  O O   . ASP   A 1 936  ? 127.828 153.787 137.657 1.00 49.90  0  900  ASP   A O   1 
ATOM   6584  C CB  . ASP   A 1 936  ? 130.449 153.177 139.475 1.00 42.68  0  900  ASP   A CB  1 
ATOM   6585  C CG  . ASP   A 1 936  ? 131.621 154.068 139.117 1.00 51.36  0  900  ASP   A CG  1 
ATOM   6586  O OD1 . ASP   A 1 936  ? 131.427 155.057 138.380 1.00 52.23  0  900  ASP   A OD1 1 
ATOM   6587  O OD2 . ASP   A 1 936  ? 132.746 153.775 139.575 1.00 54.88  -1 900  ASP   A OD2 1 
ATOM   6588  N N   . PHE   A 1 937  ? 129.094 155.627 137.932 1.00 24.48  0  901  PHE   A N   1 
ATOM   6589  C CA  . PHE   A 1 937  ? 128.638 156.314 136.734 1.00 32.29  0  901  PHE   A CA  1 
ATOM   6590  C C   . PHE   A 1 937  ? 129.454 155.937 135.504 1.00 38.77  0  901  PHE   A C   1 
ATOM   6591  O O   . PHE   A 1 937  ? 128.894 155.545 134.473 1.00 42.65  0  901  PHE   A O   1 
ATOM   6592  C CB  . PHE   A 1 937  ? 128.698 157.824 136.988 1.00 35.51  0  901  PHE   A CB  1 
ATOM   6593  C CG  . PHE   A 1 937  ? 128.366 158.659 135.800 1.00 40.86  0  901  PHE   A CG  1 
ATOM   6594  C CD1 . PHE   A 1 937  ? 127.080 158.698 135.304 1.00 39.64  0  901  PHE   A CD1 1 
ATOM   6595  C CD2 . PHE   A 1 937  ? 129.338 159.429 135.192 1.00 41.53  0  901  PHE   A CD2 1 
ATOM   6596  C CE1 . PHE   A 1 937  ? 126.772 159.478 134.216 1.00 37.35  0  901  PHE   A CE1 1 
ATOM   6597  C CE2 . PHE   A 1 937  ? 129.034 160.209 134.102 1.00 43.60  0  901  PHE   A CE2 1 
ATOM   6598  C CZ  . PHE   A 1 937  ? 127.750 160.234 133.614 1.00 41.43  0  901  PHE   A CZ  1 
ATOM   6599  N N   . LYS   A 1 938  ? 130.780 156.030 135.606 1.00 38.96  0  902  LYS   A N   1 
ATOM   6600  C CA  . LYS   A 1 938  ? 131.644 155.651 134.495 1.00 35.42  0  902  LYS   A CA  1 
ATOM   6601  C C   . LYS   A 1 938  ? 131.476 154.179 134.150 1.00 39.58  0  902  LYS   A C   1 
ATOM   6602  O O   . LYS   A 1 938  ? 131.396 153.812 132.974 1.00 46.13  0  902  LYS   A O   1 
ATOM   6603  C CB  . LYS   A 1 938  ? 133.099 155.963 134.846 1.00 39.95  0  902  LYS   A CB  1 
ATOM   6604  C CG  . LYS   A 1 938  ? 134.057 155.952 133.668 1.00 42.91  0  902  LYS   A CG  1 
ATOM   6605  C CD  . LYS   A 1 938  ? 135.402 156.535 134.061 1.00 42.27  0  902  LYS   A CD  1 
ATOM   6606  C CE  . LYS   A 1 938  ? 136.313 156.691 132.860 1.00 41.80  0  902  LYS   A CE  1 
ATOM   6607  N NZ  . LYS   A 1 938  ? 136.867 155.386 132.417 1.00 40.62  1  902  LYS   A NZ  1 
ATOM   6608  N N   . VAL   A 1 939  ? 131.413 153.318 135.167 1.00 33.15  0  903  VAL   A N   1 
ATOM   6609  C CA  . VAL   A 1 939  ? 131.295 151.885 134.922 1.00 29.97  0  903  VAL   A CA  1 
ATOM   6610  C C   . VAL   A 1 939  ? 129.949 151.555 134.289 1.00 29.05  0  903  VAL   A C   1 
ATOM   6611  O O   . VAL   A 1 939  ? 129.859 150.699 133.402 1.00 30.40  0  903  VAL   A O   1 
ATOM   6612  C CB  . VAL   A 1 939  ? 131.517 151.102 136.227 1.00 31.67  0  903  VAL   A CB  1 
ATOM   6613  C CG1 . VAL   A 1 939  ? 131.455 149.613 135.968 1.00 32.76  0  903  VAL   A CG1 1 
ATOM   6614  C CG2 . VAL   A 1 939  ? 132.847 151.478 136.839 1.00 25.44  0  903  VAL   A CG2 1 
ATOM   6615  N N   . SER   A 1 940  ? 128.880 152.218 134.735 1.00 29.46  0  904  SER   A N   1 
ATOM   6616  C CA  . SER   A 1 940  ? 127.574 151.990 134.128 1.00 31.26  0  904  SER   A CA  1 
ATOM   6617  C C   . SER   A 1 940  ? 127.553 152.445 132.674 1.00 25.15  0  904  SER   A C   1 
ATOM   6618  O O   . SER   A 1 940  ? 126.968 151.772 131.820 1.00 29.57  0  904  SER   A O   1 
ATOM   6619  C CB  . SER   A 1 940  ? 126.483 152.696 134.931 1.00 36.38  0  904  SER   A CB  1 
ATOM   6620  O OG  . SER   A 1 940  ? 126.273 154.015 134.464 1.00 33.76  0  904  SER   A OG  1 
ATOM   6621  N N   . LEU   A 1 941  ? 128.184 153.581 132.368 1.00 17.10  0  905  LEU   A N   1 
ATOM   6622  C CA  . LEU   A 1 941  ? 128.280 153.994 130.969 1.00 27.58  0  905  LEU   A CA  1 
ATOM   6623  C C   . LEU   A 1 941  ? 129.103 153.012 130.143 1.00 37.58  0  905  LEU   A C   1 
ATOM   6624  O O   . LEU   A 1 941  ? 128.758 152.731 128.987 1.00 38.70  0  905  LEU   A O   1 
ATOM   6625  C CB  . LEU   A 1 941  ? 128.872 155.397 130.867 1.00 29.82  0  905  LEU   A CB  1 
ATOM   6626  C CG  . LEU   A 1 941  ? 127.873 156.547 130.755 1.00 28.14  0  905  LEU   A CG  1 
ATOM   6627  C CD1 . LEU   A 1 941  ? 127.092 156.720 132.034 1.00 27.17  0  905  LEU   A CD1 1 
ATOM   6628  C CD2 . LEU   A 1 941  ? 128.584 157.828 130.381 1.00 32.63  0  905  LEU   A CD2 1 
ATOM   6629  N N   . GLU   A 1 942  ? 130.191 152.489 130.713 1.00 38.20  0  906  GLU   A N   1 
ATOM   6630  C CA  . GLU   A 1 942  ? 130.991 151.485 130.022 1.00 23.97  0  906  GLU   A CA  1 
ATOM   6631  C C   . GLU   A 1 942  ? 130.156 150.256 129.701 1.00 30.62  0  906  GLU   A C   1 
ATOM   6632  O O   . GLU   A 1 942  ? 130.200 149.733 128.582 1.00 34.84  0  906  GLU   A O   1 
ATOM   6633  C CB  . GLU   A 1 942  ? 132.194 151.092 130.879 1.00 24.96  0  906  GLU   A CB  1 
ATOM   6634  C CG  . GLU   A 1 942  ? 133.250 152.165 131.020 1.00 31.49  0  906  GLU   A CG  1 
ATOM   6635  C CD  . GLU   A 1 942  ? 134.361 151.766 131.968 1.00 34.94  0  906  GLU   A CD  1 
ATOM   6636  O OE1 . GLU   A 1 942  ? 134.355 150.609 132.434 1.00 33.74  0  906  GLU   A OE1 1 
ATOM   6637  O OE2 . GLU   A 1 942  ? 135.236 152.609 132.250 1.00 33.48  -1 906  GLU   A OE2 1 
ATOM   6638  N N   . SER   A 1 943  ? 129.391 149.777 130.683 1.00 28.09  0  907  SER   A N   1 
ATOM   6639  C CA  . SER   A 1 943  ? 128.558 148.600 130.470 1.00 16.50  0  907  SER   A CA  1 
ATOM   6640  C C   . SER   A 1 943  ? 127.476 148.868 129.438 1.00 8.19   0  907  SER   A C   1 
ATOM   6641  O O   . SER   A 1 943  ? 127.182 148.004 128.607 1.00 24.54  0  907  SER   A O   1 
ATOM   6642  C CB  . SER   A 1 943  ? 127.941 148.146 131.788 1.00 28.09  0  907  SER   A CB  1 
ATOM   6643  O OG  . SER   A 1 943  ? 128.945 147.738 132.698 1.00 37.71  0  907  SER   A OG  1 
ATOM   6644  N N   . ILE   A 1 944  ? 126.867 150.055 129.473 1.00 7.97   0  908  ILE   A N   1 
ATOM   6645  C CA  . ILE   A 1 944  ? 125.840 150.382 128.489 1.00 21.16  0  908  ILE   A CA  1 
ATOM   6646  C C   . ILE   A 1 944  ? 126.427 150.361 127.086 1.00 25.22  0  908  ILE   A C   1 
ATOM   6647  O O   . ILE   A 1 944  ? 125.847 149.775 126.164 1.00 26.82  0  908  ILE   A O   1 
ATOM   6648  C CB  . ILE   A 1 944  ? 125.196 151.742 128.810 1.00 16.19  0  908  ILE   A CB  1 
ATOM   6649  C CG1 . ILE   A 1 944  ? 124.268 151.625 130.018 1.00 13.48  0  908  ILE   A CG1 1 
ATOM   6650  C CG2 . ILE   A 1 944  ? 124.425 152.257 127.613 1.00 16.35  0  908  ILE   A CG2 1 
ATOM   6651  C CD1 . ILE   A 1 944  ? 123.652 152.930 130.438 1.00 13.82  0  908  ILE   A CD1 1 
ATOM   6652  N N   . GLY   A 1 945  ? 127.590 150.988 126.901 1.00 27.69  0  909  GLY   A N   1 
ATOM   6653  C CA  . GLY   A 1 945  ? 128.218 150.978 125.589 1.00 11.69  0  909  GLY   A CA  1 
ATOM   6654  C C   . GLY   A 1 945  ? 128.596 149.582 125.130 1.00 13.71  0  909  GLY   A C   1 
ATOM   6655  O O   . GLY   A 1 945  ? 128.336 149.202 123.985 1.00 23.31  0  909  GLY   A O   1 
ATOM   6656  N N   . SER   A 1 946  ? 129.190 148.790 126.026 1.00 15.77  0  910  SER   A N   1 
ATOM   6657  C CA  . SER   A 1 946  ? 129.591 147.433 125.671 1.00 15.63  0  910  SER   A CA  1 
ATOM   6658  C C   . SER   A 1 946  ? 128.389 146.588 125.273 1.00 29.55  0  910  SER   A C   1 
ATOM   6659  O O   . SER   A 1 946  ? 128.424 145.876 124.264 1.00 37.18  0  910  SER   A O   1 
ATOM   6660  C CB  . SER   A 1 946  ? 130.331 146.783 126.838 1.00 10.11  0  910  SER   A CB  1 
ATOM   6661  O OG  . SER   A 1 946  ? 131.566 147.427 127.074 1.00 23.46  0  910  SER   A OG  1 
ATOM   6662  N N   . LEU   A 1 947  ? 127.310 146.655 126.053 1.00 20.28  0  911  LEU   A N   1 
ATOM   6663  C CA  . LEU   A 1 947  ? 126.135 145.850 125.750 1.00 5.98   0  911  LEU   A CA  1 
ATOM   6664  C C   . LEU   A 1 947  ? 125.487 146.298 124.451 1.00 12.59  0  911  LEU   A C   1 
ATOM   6665  O O   . LEU   A 1 947  ? 125.222 145.481 123.566 1.00 28.23  0  911  LEU   A O   1 
ATOM   6666  C CB  . LEU   A 1 947  ? 125.136 145.925 126.902 1.00 16.12  0  911  LEU   A CB  1 
ATOM   6667  C CG  . LEU   A 1 947  ? 125.527 145.152 128.156 1.00 20.11  0  911  LEU   A CG  1 
ATOM   6668  C CD1 . LEU   A 1 947  ? 124.442 145.275 129.200 1.00 21.01  0  911  LEU   A CD1 1 
ATOM   6669  C CD2 . LEU   A 1 947  ? 125.788 143.701 127.819 1.00 18.88  0  911  LEU   A CD2 1 
ATOM   6670  N N   . THR   A 1 948  ? 125.247 147.592 124.304 1.00 12.38  0  912  THR   A N   1 
ATOM   6671  C CA  . THR   A 1 948  ? 124.599 148.054 123.086 1.00 15.04  0  912  THR   A CA  1 
ATOM   6672  C C   . THR   A 1 948  ? 125.487 147.951 121.875 1.00 20.22  0  912  THR   A C   1 
ATOM   6673  O O   . THR   A 1 948  ? 124.996 148.194 120.772 1.00 25.05  0  912  THR   A O   1 
ATOM   6674  C CB  . THR   A 1 948  ? 124.121 149.491 123.261 1.00 13.32  0  912  THR   A CB  1 
ATOM   6675  O OG1 . THR   A 1 948  ? 125.248 150.344 123.479 1.00 27.24  0  912  THR   A OG1 1 
ATOM   6676  C CG2 . THR   A 1 948  ? 123.187 149.589 124.444 1.00 16.29  0  912  THR   A CG2 1 
ATOM   6677  N N   . GLN   A 1 949  ? 126.771 147.634 122.017 1.00 27.04  0  913  GLN   A N   1 
ATOM   6678  C CA  . GLN   A 1 949  ? 127.609 147.357 120.860 1.00 23.26  0  913  GLN   A CA  1 
ATOM   6679  C C   . GLN   A 1 949  ? 127.316 146.007 120.211 1.00 22.83  0  913  GLN   A C   1 
ATOM   6680  O O   . GLN   A 1 949  ? 127.766 145.769 119.085 1.00 36.25  0  913  GLN   A O   1 
ATOM   6681  C CB  . GLN   A 1 949  ? 129.082 147.427 121.266 1.00 18.65  0  913  GLN   A CB  1 
ATOM   6682  C CG  . GLN   A 1 949  ? 130.040 147.585 120.117 1.00 19.64  0  913  GLN   A CG  1 
ATOM   6683  C CD  . GLN   A 1 949  ? 131.148 148.551 120.438 1.00 27.45  0  913  GLN   A CD  1 
ATOM   6684  O OE1 . GLN   A 1 949  ? 132.012 148.264 121.264 1.00 33.99  0  913  GLN   A OE1 1 
ATOM   6685  N NE2 . GLN   A 1 949  ? 131.131 149.708 119.788 1.00 26.79  0  913  GLN   A NE2 1 
ATOM   6686  N N   . GLU   A 1 950  ? 126.575 145.122 120.882 1.00 18.04  0  914  GLU   A N   1 
ATOM   6687  C CA  . GLU   A 1 950  ? 126.235 143.838 120.281 1.00 19.82  0  914  GLU   A CA  1 
ATOM   6688  C C   . GLU   A 1 950  ? 125.248 143.970 119.133 1.00 20.14  0  914  GLU   A C   1 
ATOM   6689  O O   . GLU   A 1 950  ? 125.217 143.093 118.267 1.00 31.55  0  914  GLU   A O   1 
ATOM   6690  C CB  . GLU   A 1 950  ? 125.671 142.883 121.333 1.00 26.29  0  914  GLU   A CB  1 
ATOM   6691  C CG  . GLU   A 1 950  ? 126.502 142.792 122.600 1.00 31.60  0  914  GLU   A CG  1 
ATOM   6692  C CD  . GLU   A 1 950  ? 127.821 142.077 122.395 1.00 37.46  0  914  GLU   A CD  1 
ATOM   6693  O OE1 . GLU   A 1 950  ? 128.813 142.750 122.046 1.00 34.66  0  914  GLU   A OE1 1 
ATOM   6694  O OE2 . GLU   A 1 950  ? 127.869 140.846 122.595 1.00 40.48  -1 914  GLU   A OE2 1 
ATOM   6695  N N   . LEU   A 1 951  ? 124.442 145.028 119.104 1.00 21.28  0  915  LEU   A N   1 
ATOM   6696  C CA  . LEU   A 1 951  ? 123.607 145.319 117.947 1.00 25.86  0  915  LEU   A CA  1 
ATOM   6697  C C   . LEU   A 1 951  ? 124.418 145.801 116.756 1.00 31.96  0  915  LEU   A C   1 
ATOM   6698  O O   . LEU   A 1 951  ? 123.882 145.880 115.648 1.00 33.48  0  915  LEU   A O   1 
ATOM   6699  C CB  . LEU   A 1 951  ? 122.552 146.369 118.303 1.00 27.31  0  915  LEU   A CB  1 
ATOM   6700  C CG  . LEU   A 1 951  ? 121.571 146.029 119.424 1.00 27.99  0  915  LEU   A CG  1 
ATOM   6701  C CD1 . LEU   A 1 951  ? 120.667 147.211 119.691 1.00 22.85  0  915  LEU   A CD1 1 
ATOM   6702  C CD2 . LEU   A 1 951  ? 120.758 144.804 119.068 1.00 22.35  0  915  LEU   A CD2 1 
ATOM   6703  N N   . GLU   A 1 952  ? 125.687 146.137 116.970 1.00 33.01  0  916  GLU   A N   1 
ATOM   6704  C CA  . GLU   A 1 952  ? 126.632 146.507 115.927 1.00 29.86  0  916  GLU   A CA  1 
ATOM   6705  C C   . GLU   A 1 952  ? 127.466 145.327 115.458 1.00 34.05  0  916  GLU   A C   1 
ATOM   6706  O O   . GLU   A 1 952  ? 127.538 145.044 114.260 1.00 28.26  0  916  GLU   A O   1 
ATOM   6707  C CB  . GLU   A 1 952  ? 127.568 147.600 116.451 1.00 26.89  0  916  GLU   A CB  1 
ATOM   6708  C CG  . GLU   A 1 952  ? 128.429 148.272 115.409 1.00 29.03  0  916  GLU   A CG  1 
ATOM   6709  C CD  . GLU   A 1 952  ? 128.658 149.728 115.727 1.00 42.43  0  916  GLU   A CD  1 
ATOM   6710  O OE1 . GLU   A 1 952  ? 128.123 150.591 115.009 1.00 43.79  0  916  GLU   A OE1 1 
ATOM   6711  O OE2 . GLU   A 1 952  ? 129.369 150.011 116.713 1.00 47.19  -1 916  GLU   A OE2 1 
ATOM   6712  N N   . TYR   A 1 953  ? 128.106 144.634 116.397 1.00 26.14  0  917  TYR   A N   1 
ATOM   6713  C CA  . TYR   A 1 953  ? 129.039 143.576 116.037 1.00 12.54  0  917  TYR   A CA  1 
ATOM   6714  C C   . TYR   A 1 953  ? 128.306 142.349 115.515 1.00 28.18  0  917  TYR   A C   1 
ATOM   6715  O O   . TYR   A 1 953  ? 128.697 141.764 114.500 1.00 36.07  0  917  TYR   A O   1 
ATOM   6716  C CB  . TYR   A 1 953  ? 129.904 143.222 117.243 1.00 17.77  0  917  TYR   A CB  1 
ATOM   6717  C CG  . TYR   A 1 953  ? 130.958 144.261 117.542 1.00 29.57  0  917  TYR   A CG  1 
ATOM   6718  C CD1 . TYR   A 1 953  ? 131.066 145.404 116.767 1.00 31.71  0  917  TYR   A CD1 1 
ATOM   6719  C CD2 . TYR   A 1 953  ? 131.837 144.104 118.601 1.00 31.97  0  917  TYR   A CD2 1 
ATOM   6720  C CE1 . TYR   A 1 953  ? 132.016 146.354 117.030 1.00 28.55  0  917  TYR   A CE1 1 
ATOM   6721  C CE2 . TYR   A 1 953  ? 132.795 145.053 118.871 1.00 31.06  0  917  TYR   A CE2 1 
ATOM   6722  C CZ  . TYR   A 1 953  ? 132.876 146.175 118.081 1.00 29.18  0  917  TYR   A CZ  1 
ATOM   6723  O OH  . TYR   A 1 953  ? 133.825 147.128 118.339 1.00 32.55  0  917  TYR   A OH  1 
ATOM   6724  N N   . ARG   A 1 954  ? 127.233 141.947 116.194 1.00 31.93  0  918  ARG   A N   1 
ATOM   6725  C CA  . ARG   A 1 954  ? 126.478 140.760 115.807 1.00 26.64  0  918  ARG   A CA  1 
ATOM   6726  C C   . ARG   A 1 954  ? 125.280 141.117 114.933 1.00 25.72  0  918  ARG   A C   1 
ATOM   6727  O O   . ARG   A 1 954  ? 125.127 140.585 113.831 1.00 31.80  0  918  ARG   A O   1 
ATOM   6728  C CB  . ARG   A 1 954  ? 126.028 140.003 117.058 1.00 24.39  0  918  ARG   A CB  1 
ATOM   6729  C CG  . ARG   A 1 954  ? 127.175 139.451 117.868 1.00 24.88  0  918  ARG   A CG  1 
ATOM   6730  C CD  . ARG   A 1 954  ? 126.687 138.692 119.077 1.00 31.15  0  918  ARG   A CD  1 
ATOM   6731  N NE  . ARG   A 1 954  ? 127.491 137.502 119.320 1.00 36.15  0  918  ARG   A NE  1 
ATOM   6732  C CZ  . ARG   A 1 954  ? 126.994 136.286 119.505 1.00 40.01  0  918  ARG   A CZ  1 
ATOM   6733  N NH1 . ARG   A 1 954  ? 125.690 136.062 119.486 1.00 35.88  1  918  ARG   A NH1 1 
ATOM   6734  N NH2 . ARG   A 1 954  ? 127.827 135.271 119.713 1.00 33.81  0  918  ARG   A NH2 1 
ATOM   6735  N N   . GLY   A 1 955  ? 124.433 142.029 115.406 1.00 25.70  0  919  GLY   A N   1 
ATOM   6736  C CA  . GLY   A 1 955  ? 123.240 142.401 114.668 1.00 31.94  0  919  GLY   A CA  1 
ATOM   6737  C C   . GLY   A 1 955  ? 123.505 143.129 113.368 1.00 34.11  0  919  GLY   A C   1 
ATOM   6738  O O   . GLY   A 1 955  ? 122.587 143.243 112.549 1.00 43.74  0  919  GLY   A O   1 
ATOM   6739  N N   . GLU   A 1 956  ? 124.723 143.630 113.164 1.00 26.91  0  920  GLU   A N   1 
ATOM   6740  C CA  . GLU   A 1 956  ? 125.124 144.291 111.923 1.00 32.54  0  920  GLU   A CA  1 
ATOM   6741  C C   . GLU   A 1 956  ? 124.256 145.517 111.633 1.00 40.41  0  920  GLU   A C   1 
ATOM   6742  O O   . GLU   A 1 956  ? 123.590 145.614 110.600 1.00 43.02  0  920  GLU   A O   1 
ATOM   6743  C CB  . GLU   A 1 956  ? 125.096 143.313 110.748 1.00 28.63  0  920  GLU   A CB  1 
ATOM   6744  C CG  . GLU   A 1 956  ? 126.132 142.225 110.833 1.00 33.64  0  920  GLU   A CG  1 
ATOM   6745  C CD  . GLU   A 1 956  ? 126.232 141.427 109.557 1.00 40.92  0  920  GLU   A CD  1 
ATOM   6746  O OE1 . GLU   A 1 956  ? 126.581 142.020 108.517 1.00 46.13  0  920  GLU   A OE1 1 
ATOM   6747  O OE2 . GLU   A 1 956  ? 125.964 140.209 109.593 1.00 45.39  -1 920  GLU   A OE2 1 
ATOM   6748  N N   . SER   A 1 957  ? 124.282 146.465 112.564 1.00 30.17  0  921  SER   A N   1 
ATOM   6749  C CA  . SER   A 1 957  ? 123.596 147.737 112.370 1.00 28.39  0  921  SER   A CA  1 
ATOM   6750  C C   . SER   A 1 957  ? 124.309 148.800 113.185 1.00 33.33  0  921  SER   A C   1 
ATOM   6751  O O   . SER   A 1 957  ? 124.266 148.772 114.417 1.00 41.59  0  921  SER   A O   1 
ATOM   6752  C CB  . SER   A 1 957  ? 122.128 147.644 112.772 1.00 32.85  0  921  SER   A CB  1 
ATOM   6753  O OG  . SER   A 1 957  ? 121.400 148.741 112.255 1.00 35.08  0  921  SER   A OG  1 
ATOM   6754  N N   . LEU   A 1 958  ? 124.979 149.723 112.496 1.00 36.02  0  922  LEU   A N   1 
ATOM   6755  C CA  . LEU   A 1 958  ? 125.635 150.828 113.184 1.00 26.59  0  922  LEU   A CA  1 
ATOM   6756  C C   . LEU   A 1 958  ? 124.613 151.777 113.794 1.00 28.88  0  922  LEU   A C   1 
ATOM   6757  O O   . LEU   A 1 958  ? 124.685 152.106 114.984 1.00 30.74  0  922  LEU   A O   1 
ATOM   6758  C CB  . LEU   A 1 958  ? 126.548 151.572 112.208 1.00 19.60  0  922  LEU   A CB  1 
ATOM   6759  C CG  . LEU   A 1 958  ? 127.450 152.688 112.734 1.00 21.20  0  922  LEU   A CG  1 
ATOM   6760  C CD1 . LEU   A 1 958  ? 128.799 152.624 112.048 1.00 29.22  0  922  LEU   A CD1 1 
ATOM   6761  C CD2 . LEU   A 1 958  ? 126.820 154.050 112.525 1.00 27.65  0  922  LEU   A CD2 1 
ATOM   6762  N N   . LEU   A 1 959  ? 123.634 152.202 112.996 1.00 18.58  0  923  LEU   A N   1 
ATOM   6763  C CA  . LEU   A 1 959  ? 122.739 153.268 113.427 1.00 21.46  0  923  LEU   A CA  1 
ATOM   6764  C C   . LEU   A 1 959  ? 121.787 152.799 114.518 1.00 38.51  0  923  LEU   A C   1 
ATOM   6765  O O   . LEU   A 1 959  ? 121.478 153.557 115.443 1.00 38.36  0  923  LEU   A O   1 
ATOM   6766  C CB  . LEU   A 1 959  ? 121.969 153.810 112.227 1.00 20.04  0  923  LEU   A CB  1 
ATOM   6767  C CG  . LEU   A 1 959  ? 121.326 155.178 112.418 1.00 27.37  0  923  LEU   A CG  1 
ATOM   6768  C CD1 . LEU   A 1 959  ? 122.209 156.056 113.268 1.00 22.48  0  923  LEU   A CD1 1 
ATOM   6769  C CD2 . LEU   A 1 959  ? 121.067 155.829 111.077 1.00 27.62  0  923  LEU   A CD2 1 
ATOM   6770  N N   . CYS   A 1 960  ? 121.304 151.559 114.429 1.00 35.70  0  924  CYS   A N   1 
ATOM   6771  C CA  . CYS   A 1 960  ? 120.390 151.052 115.448 1.00 22.82  0  924  CYS   A CA  1 
ATOM   6772  C C   . CYS   A 1 960  ? 121.067 150.990 116.809 1.00 22.03  0  924  CYS   A C   1 
ATOM   6773  O O   . CYS   A 1 960  ? 120.513 151.456 117.812 1.00 38.31  0  924  CYS   A O   1 
ATOM   6774  C CB  . CYS   A 1 960  ? 119.866 149.675 115.048 1.00 28.30  0  924  CYS   A CB  1 
ATOM   6775  S SG  . CYS   A 1 960  ? 118.795 148.917 116.283 1.00 55.87  0  924  CYS   A SG  1 
ATOM   6776  N N   . SER   A 1 961  ? 122.270 150.416 116.864 1.00 11.52  0  925  SER   A N   1 
ATOM   6777  C CA  . SER   A 1 961  ? 123.001 150.364 118.125 1.00 20.70  0  925  SER   A CA  1 
ATOM   6778  C C   . SER   A 1 961  ? 123.347 151.760 118.614 1.00 27.15  0  925  SER   A C   1 
ATOM   6779  O O   . SER   A 1 961  ? 123.276 152.037 119.815 1.00 33.66  0  925  SER   A O   1 
ATOM   6780  C CB  . SER   A 1 961  ? 124.267 149.529 117.972 1.00 27.57  0  925  SER   A CB  1 
ATOM   6781  O OG  . SER   A 1 961  ? 125.050 149.600 119.149 1.00 31.45  0  925  SER   A OG  1 
ATOM   6782  N N   . LEU   A 1 962  ? 123.726 152.651 117.698 1.00 24.96  0  926  LEU   A N   1 
ATOM   6783  C CA  . LEU   A 1 962  ? 124.039 154.022 118.084 1.00 21.04  0  926  LEU   A CA  1 
ATOM   6784  C C   . LEU   A 1 962  ? 122.847 154.689 118.757 1.00 22.56  0  926  LEU   A C   1 
ATOM   6785  O O   . LEU   A 1 962  ? 122.979 155.278 119.834 1.00 33.58  0  926  LEU   A O   1 
ATOM   6786  C CB  . LEU   A 1 962  ? 124.482 154.808 116.851 1.00 18.32  0  926  LEU   A CB  1 
ATOM   6787  C CG  . LEU   A 1 962  ? 124.693 156.312 116.976 1.00 12.59  0  926  LEU   A CG  1 
ATOM   6788  C CD1 . LEU   A 1 962  ? 125.842 156.614 117.905 1.00 13.35  0  926  LEU   A CD1 1 
ATOM   6789  C CD2 . LEU   A 1 962  ? 124.952 156.898 115.607 1.00 26.12  0  926  LEU   A CD2 1 
ATOM   6790  N N   . ILE   A 1 963  ? 121.664 154.581 118.149 1.00 9.87   0  927  ILE   A N   1 
ATOM   6791  C CA  . ILE   A 1 963  ? 120.489 155.264 118.684 1.00 3.55   0  927  ILE   A CA  1 
ATOM   6792  C C   . ILE   A 1 963  ? 120.026 154.619 119.984 1.00 1.74   0  927  ILE   A C   1 
ATOM   6793  O O   . ILE   A 1 963  ? 119.594 155.312 120.908 1.00 11.81  0  927  ILE   A O   1 
ATOM   6794  C CB  . ILE   A 1 963  ? 119.369 155.302 117.636 1.00 8.82   0  927  ILE   A CB  1 
ATOM   6795  C CG1 . ILE   A 1 963  ? 119.802 156.154 116.450 1.00 7.45   0  927  ILE   A CG1 1 
ATOM   6796  C CG2 . ILE   A 1 963  ? 118.105 155.870 118.236 1.00 10.19  0  927  ILE   A CG2 1 
ATOM   6797  C CD1 . ILE   A 1 963  ? 118.997 155.913 115.222 1.00 11.14  0  927  ILE   A CD1 1 
ATOM   6798  N N   . PHE   A 1 964  ? 120.092 153.291 120.077 1.00 6.59   0  928  PHE   A N   1 
ATOM   6799  C CA  . PHE   A 1 964  ? 119.736 152.627 121.328 1.00 3.56   0  928  PHE   A CA  1 
ATOM   6800  C C   . PHE   A 1 964  ? 120.667 153.049 122.460 1.00 14.05  0  928  PHE   A C   1 
ATOM   6801  O O   . PHE   A 1 964  ? 120.215 153.383 123.570 1.00 33.74  0  928  PHE   A O   1 
ATOM   6802  C CB  . PHE   A 1 964  ? 119.775 151.115 121.119 1.00 7.28   0  928  PHE   A CB  1 
ATOM   6803  C CG  . PHE   A 1 964  ? 119.211 150.323 122.253 1.00 6.28   0  928  PHE   A CG  1 
ATOM   6804  C CD1 . PHE   A 1 964  ? 117.896 150.475 122.636 1.00 7.98   0  928  PHE   A CD1 1 
ATOM   6805  C CD2 . PHE   A 1 964  ? 119.993 149.400 122.918 1.00 17.61  0  928  PHE   A CD2 1 
ATOM   6806  C CE1 . PHE   A 1 964  ? 117.380 149.736 123.673 1.00 18.12  0  928  PHE   A CE1 1 
ATOM   6807  C CE2 . PHE   A 1 964  ? 119.481 148.658 123.954 1.00 16.02  0  928  PHE   A CE2 1 
ATOM   6808  C CZ  . PHE   A 1 964  ? 118.174 148.826 124.332 1.00 17.09  0  928  PHE   A CZ  1 
ATOM   6809  N N   . ARG   A 1 965  ? 121.971 153.074 122.185 1.00 2.75   0  929  ARG   A N   1 
ATOM   6810  C CA  . ARG   A 1 965  ? 122.934 153.502 123.186 1.00 8.21   0  929  ARG   A CA  1 
ATOM   6811  C C   . ARG   A 1 965  ? 122.705 154.948 123.583 1.00 16.16  0  929  ARG   A C   1 
ATOM   6812  O O   . ARG   A 1 965  ? 122.837 155.296 124.755 1.00 25.85  0  929  ARG   A O   1 
ATOM   6813  C CB  . ARG   A 1 965  ? 124.353 153.316 122.660 1.00 17.18  0  929  ARG   A CB  1 
ATOM   6814  C CG  . ARG   A 1 965  ? 125.423 153.550 123.697 1.00 15.55  0  929  ARG   A CG  1 
ATOM   6815  C CD  . ARG   A 1 965  ? 126.790 153.297 123.115 1.00 19.19  0  929  ARG   A CD  1 
ATOM   6816  N NE  . ARG   A 1 965  ? 127.176 154.345 122.180 1.00 31.18  0  929  ARG   A NE  1 
ATOM   6817  C CZ  . ARG   A 1 965  ? 127.335 154.163 120.877 1.00 31.69  0  929  ARG   A CZ  1 
ATOM   6818  N NH1 . ARG   A 1 965  ? 127.127 152.986 120.314 1.00 17.96  1  929  ARG   A NH1 1 
ATOM   6819  N NH2 . ARG   A 1 965  ? 127.715 155.188 120.123 1.00 28.32  0  929  ARG   A NH2 1 
ATOM   6820  N N   . ASN   A 1 966  ? 122.373 155.810 122.620 1.00 14.06  0  930  ASN   A N   1 
ATOM   6821  C CA  . ASN   A 1 966  ? 122.148 157.212 122.952 1.00 5.30   0  930  ASN   A CA  1 
ATOM   6822  C C   . ASN   A 1 966  ? 120.867 157.401 123.755 1.00 1.35   0  930  ASN   A C   1 
ATOM   6823  O O   . ASN   A 1 966  ? 120.829 158.227 124.672 1.00 9.55   0  930  ASN   A O   1 
ATOM   6824  C CB  . ASN   A 1 966  ? 122.126 158.059 121.686 1.00 5.05   0  930  ASN   A CB  1 
ATOM   6825  C CG  . ASN   A 1 966  ? 123.496 158.213 121.076 1.00 14.87  0  930  ASN   A CG  1 
ATOM   6826  O OD1 . ASN   A 1 966  ? 123.685 157.996 119.885 1.00 25.34  0  930  ASN   A OD1 1 
ATOM   6827  N ND2 . ASN   A 1 966  ? 124.471 158.568 121.900 1.00 14.28  0  930  ASN   A ND2 1 
ATOM   6828  N N   . VAL   A 1 967  ? 119.817 156.636 123.444 1.00 4.03   0  931  VAL   A N   1 
ATOM   6829  C CA  . VAL   A 1 967  ? 118.598 156.685 124.248 1.00 3.94   0  931  VAL   A CA  1 
ATOM   6830  C C   . VAL   A 1 967  ? 118.926 156.376 125.697 1.00 2.80   0  931  VAL   A C   1 
ATOM   6831  O O   . VAL   A 1 967  ? 118.579 157.132 126.614 1.00 24.50  0  931  VAL   A O   1 
ATOM   6832  C CB  . VAL   A 1 967  ? 117.545 155.699 123.707 1.00 3.06   0  931  VAL   A CB  1 
ATOM   6833  C CG1 . VAL   A 1 967  ? 116.506 155.413 124.766 1.00 1.74   0  931  VAL   A CG1 1 
ATOM   6834  C CG2 . VAL   A 1 967  ? 116.876 156.226 122.463 1.00 6.50   0  931  VAL   A CG2 1 
ATOM   6835  N N   . TRP   A 1 968  ? 119.640 155.280 125.923 1.00 0.00   0  932  TRP   A N   1 
ATOM   6836  C CA  . TRP   A 1 968  ? 119.875 154.887 127.303 1.00 2.81   0  932  TRP   A CA  1 
ATOM   6837  C C   . TRP   A 1 968  ? 120.964 155.708 127.986 1.00 14.15  0  932  TRP   A C   1 
ATOM   6838  O O   . TRP   A 1 968  ? 120.911 155.881 129.206 1.00 19.29  0  932  TRP   A O   1 
ATOM   6839  C CB  . TRP   A 1 968  ? 120.156 153.392 127.355 1.00 8.78   0  932  TRP   A CB  1 
ATOM   6840  C CG  . TRP   A 1 968  ? 118.872 152.647 127.232 1.00 5.63   0  932  TRP   A CG  1 
ATOM   6841  C CD1 . TRP   A 1 968  ? 118.453 151.905 126.175 1.00 4.56   0  932  TRP   A CD1 1 
ATOM   6842  C CD2 . TRP   A 1 968  ? 117.814 152.609 128.195 1.00 13.34  0  932  TRP   A CD2 1 
ATOM   6843  N NE1 . TRP   A 1 968  ? 117.204 151.392 126.423 1.00 10.84  0  932  TRP   A NE1 1 
ATOM   6844  C CE2 . TRP   A 1 968  ? 116.792 151.811 127.659 1.00 10.98  0  932  TRP   A CE2 1 
ATOM   6845  C CE3 . TRP   A 1 968  ? 117.638 153.166 129.465 1.00 7.29   0  932  TRP   A CE3 1 
ATOM   6846  C CZ2 . TRP   A 1 968  ? 115.613 151.556 128.346 1.00 5.62   0  932  TRP   A CZ2 1 
ATOM   6847  C CZ3 . TRP   A 1 968  ? 116.470 152.914 130.141 1.00 0.51   0  932  TRP   A CZ3 1 
ATOM   6848  C CH2 . TRP   A 1 968  ? 115.472 152.116 129.583 1.00 11.13  0  932  TRP   A CH2 1 
ATOM   6849  N N   . LEU   A 1 969  ? 121.912 156.270 127.233 1.00 19.07  0  933  LEU   A N   1 
ATOM   6850  C CA  . LEU   A 1 969  ? 122.881 157.187 127.824 1.00 10.03  0  933  LEU   A CA  1 
ATOM   6851  C C   . LEU   A 1 969  ? 122.222 158.490 128.246 1.00 18.01  0  933  LEU   A C   1 
ATOM   6852  O O   . LEU   A 1 969  ? 122.517 159.018 129.324 1.00 26.91  0  933  LEU   A O   1 
ATOM   6853  C CB  . LEU   A 1 969  ? 124.014 157.469 126.841 1.00 15.09  0  933  LEU   A CB  1 
ATOM   6854  C CG  . LEU   A 1 969  ? 125.091 156.402 126.675 1.00 16.79  0  933  LEU   A CG  1 
ATOM   6855  C CD1 . LEU   A 1 969  ? 126.196 156.925 125.782 1.00 14.07  0  933  LEU   A CD1 1 
ATOM   6856  C CD2 . LEU   A 1 969  ? 125.633 155.975 128.019 1.00 20.75  0  933  LEU   A CD2 1 
ATOM   6857  N N   . TYR   A 1 970  ? 121.340 159.037 127.406 1.00 18.43  0  934  TYR   A N   1 
ATOM   6858  C CA  . TYR   A 1 970  ? 120.595 160.222 127.802 1.00 18.20  0  934  TYR   A CA  1 
ATOM   6859  C C   . TYR   A 1 970  ? 119.722 159.934 129.011 1.00 13.36  0  934  TYR   A C   1 
ATOM   6860  O O   . TYR   A 1 970  ? 119.616 160.764 129.918 1.00 14.30  0  934  TYR   A O   1 
ATOM   6861  C CB  . TYR   A 1 970  ? 119.744 160.733 126.644 1.00 15.33  0  934  TYR   A CB  1 
ATOM   6862  C CG  . TYR   A 1 970  ? 119.064 162.042 126.954 1.00 19.38  0  934  TYR   A CG  1 
ATOM   6863  C CD1 . TYR   A 1 970  ? 117.795 162.073 127.508 1.00 27.71  0  934  TYR   A CD1 1 
ATOM   6864  C CD2 . TYR   A 1 970  ? 119.696 163.246 126.706 1.00 16.65  0  934  TYR   A CD2 1 
ATOM   6865  C CE1 . TYR   A 1 970  ? 117.175 163.263 127.800 1.00 22.44  0  934  TYR   A CE1 1 
ATOM   6866  C CE2 . TYR   A 1 970  ? 119.083 164.440 126.995 1.00 23.97  0  934  TYR   A CE2 1 
ATOM   6867  C CZ  . TYR   A 1 970  ? 117.823 164.443 127.542 1.00 23.58  0  934  TYR   A CZ  1 
ATOM   6868  O OH  . TYR   A 1 970  ? 117.209 165.637 127.830 1.00 31.23  0  934  TYR   A OH  1 
ATOM   6869  N N   . ASN   A 1 971  ? 119.088 158.762 129.047 1.00 15.02  0  935  ASN   A N   1 
ATOM   6870  C CA  . ASN   A 1 971  ? 118.305 158.404 130.222 1.00 17.18  0  935  ASN   A CA  1 
ATOM   6871  C C   . ASN   A 1 971  ? 119.174 158.307 131.468 1.00 20.77  0  935  ASN   A C   1 
ATOM   6872  O O   . ASN   A 1 971  ? 118.741 158.699 132.555 1.00 39.01  0  935  ASN   A O   1 
ATOM   6873  C CB  . ASN   A 1 971  ? 117.572 157.088 129.984 1.00 28.13  0  935  ASN   A CB  1 
ATOM   6874  C CG  . ASN   A 1 971  ? 116.431 156.879 130.950 1.00 36.82  0  935  ASN   A CG  1 
ATOM   6875  O OD1 . ASN   A 1 971  ? 115.354 157.449 130.785 1.00 33.77  0  935  ASN   A OD1 1 
ATOM   6876  N ND2 . ASN   A 1 971  ? 116.661 156.062 131.971 1.00 37.87  0  935  ASN   A ND2 1 
ATOM   6877  N N   . GLN   A 1 972  ? 120.393 157.785 131.338 1.00 14.61  0  936  GLN   A N   1 
ATOM   6878  C CA  . GLN   A 1 972  ? 121.253 157.627 132.506 1.00 20.33  0  936  GLN   A CA  1 
ATOM   6879  C C   . GLN   A 1 972  ? 121.809 158.963 132.985 1.00 17.72  0  936  GLN   A C   1 
ATOM   6880  O O   . GLN   A 1 972  ? 121.949 159.184 134.192 1.00 22.26  0  936  GLN   A O   1 
ATOM   6881  C CB  . GLN   A 1 972  ? 122.388 156.654 132.184 1.00 33.99  0  936  GLN   A CB  1 
ATOM   6882  C CG  . GLN   A 1 972  ? 123.640 156.839 133.018 1.00 36.00  0  936  GLN   A CG  1 
ATOM   6883  C CD  . GLN   A 1 972  ? 123.427 156.506 134.474 1.00 28.28  0  936  GLN   A CD  1 
ATOM   6884  O OE1 . GLN   A 1 972  ? 122.936 155.435 134.808 1.00 23.70  0  936  GLN   A OE1 1 
ATOM   6885  N NE2 . GLN   A 1 972  ? 123.791 157.428 135.350 1.00 34.40  0  936  GLN   A NE2 1 
ATOM   6886  N N   . ILE   A 1 973  ? 122.126 159.869 132.063 1.00 20.67  0  937  ILE   A N   1 
ATOM   6887  C CA  . ILE   A 1 973  ? 122.850 161.087 132.415 1.00 22.51  0  937  ILE   A CA  1 
ATOM   6888  C C   . ILE   A 1 973  ? 121.893 162.239 132.683 1.00 23.71  0  937  ILE   A C   1 
ATOM   6889  O O   . ILE   A 1 973  ? 121.958 162.878 133.736 1.00 28.13  0  937  ILE   A O   1 
ATOM   6890  C CB  . ILE   A 1 973  ? 123.860 161.459 131.315 1.00 23.74  0  937  ILE   A CB  1 
ATOM   6891  C CG1 . ILE   A 1 973  ? 125.120 160.614 131.463 1.00 27.72  0  937  ILE   A CG1 1 
ATOM   6892  C CG2 . ILE   A 1 973  ? 124.211 162.931 131.376 1.00 19.08  0  937  ILE   A CG2 1 
ATOM   6893  C CD1 . ILE   A 1 973  ? 126.031 160.641 130.273 1.00 26.78  0  937  ILE   A CD1 1 
ATOM   6894  N N   . ALA   A 1 974  ? 121.004 162.524 131.733 1.00 17.87  0  938  ALA   A N   1 
ATOM   6895  C CA  . ALA   A 1 974  ? 120.142 163.690 131.872 1.00 17.19  0  938  ALA   A CA  1 
ATOM   6896  C C   . ALA   A 1 974  ? 119.064 163.470 132.925 1.00 31.87  0  938  ALA   A C   1 
ATOM   6897  O O   . ALA   A 1 974  ? 118.740 164.387 133.687 1.00 37.45  0  938  ALA   A O   1 
ATOM   6898  C CB  . ALA   A 1 974  ? 119.512 164.036 130.526 1.00 16.17  0  938  ALA   A CB  1 
ATOM   6899  N N   . LEU   A 1 975  ? 118.501 162.266 132.992 1.00 35.98  0  939  LEU   A N   1 
ATOM   6900  C CA  . LEU   A 1 975  ? 117.331 162.011 133.822 1.00 25.75  0  939  LEU   A CA  1 
ATOM   6901  C C   . LEU   A 1 975  ? 117.656 161.277 135.116 1.00 22.09  0  939  LEU   A C   1 
ATOM   6902  O O   . LEU   A 1 975  ? 117.300 161.749 136.197 1.00 36.01  0  939  LEU   A O   1 
ATOM   6903  C CB  . LEU   A 1 975  ? 116.291 161.220 133.024 1.00 33.47  0  939  LEU   A CB  1 
ATOM   6904  C CG  . LEU   A 1 975  ? 115.938 161.813 131.662 1.00 34.43  0  939  LEU   A CG  1 
ATOM   6905  C CD1 . LEU   A 1 975  ? 114.919 160.946 130.960 1.00 32.47  0  939  LEU   A CD1 1 
ATOM   6906  C CD2 . LEU   A 1 975  ? 115.419 163.228 131.812 1.00 29.24  0  939  LEU   A CD2 1 
ATOM   6907  N N   . GLN   A 1 976  ? 118.322 160.133 135.037 1.00 25.67  0  940  GLN   A N   1 
ATOM   6908  C CA  . GLN   A 1 976  ? 118.513 159.299 136.215 1.00 26.45  0  940  GLN   A CA  1 
ATOM   6909  C C   . GLN   A 1 976  ? 119.698 159.719 137.072 1.00 30.67  0  940  GLN   A C   1 
ATOM   6910  O O   . GLN   A 1 976  ? 119.914 159.115 138.126 1.00 37.99  0  940  GLN   A O   1 
ATOM   6911  C CB  . GLN   A 1 976  ? 118.679 157.837 135.803 1.00 32.04  0  940  GLN   A CB  1 
ATOM   6912  C CG  . GLN   A 1 976  ? 117.458 157.243 135.130 1.00 32.72  0  940  GLN   A CG  1 
ATOM   6913  C CD  . GLN   A 1 976  ? 116.334 156.975 136.104 1.00 41.73  0  940  GLN   A CD  1 
ATOM   6914  O OE1 . GLN   A 1 976  ? 116.490 156.207 137.052 1.00 48.35  0  940  GLN   A OE1 1 
ATOM   6915  N NE2 . GLN   A 1 976  ? 115.191 157.610 135.876 1.00 41.10  0  940  GLN   A NE2 1 
ATOM   6916  N N   . LEU   A 1 977  ? 120.473 160.720 136.658 1.00 28.19  0  941  LEU   A N   1 
ATOM   6917  C CA  . LEU   A 1 977  ? 121.633 161.115 137.449 1.00 34.93  0  941  LEU   A CA  1 
ATOM   6918  C C   . LEU   A 1 977  ? 121.226 161.869 138.708 1.00 38.59  0  941  LEU   A C   1 
ATOM   6919  O O   . LEU   A 1 977  ? 121.815 161.664 139.774 1.00 38.87  0  941  LEU   A O   1 
ATOM   6920  C CB  . LEU   A 1 977  ? 122.583 161.961 136.605 1.00 32.95  0  941  LEU   A CB  1 
ATOM   6921  C CG  . LEU   A 1 977  ? 124.024 162.082 137.095 1.00 31.80  0  941  LEU   A CG  1 
ATOM   6922  C CD1 . LEU   A 1 977  ? 124.610 160.718 137.395 1.00 35.35  0  941  LEU   A CD1 1 
ATOM   6923  C CD2 . LEU   A 1 977  ? 124.862 162.803 136.063 1.00 35.94  0  941  LEU   A CD2 1 
ATOM   6924  N N   . LYS   A 1 978  ? 120.219 162.736 138.608 1.00 33.23  0  942  LYS   A N   1 
ATOM   6925  C CA  . LYS   A 1 978  ? 119.745 163.480 139.767 1.00 24.03  0  942  LYS   A CA  1 
ATOM   6926  C C   . LYS   A 1 978  ? 118.943 162.625 140.732 1.00 27.84  0  942  LYS   A C   1 
ATOM   6927  O O   . LYS   A 1 978  ? 118.374 163.171 141.681 1.00 35.21  0  942  LYS   A O   1 
ATOM   6928  C CB  . LYS   A 1 978  ? 118.904 164.671 139.315 1.00 23.84  0  942  LYS   A CB  1 
ATOM   6929  C CG  . LYS   A 1 978  ? 117.765 164.305 138.393 1.00 31.63  0  942  LYS   A CG  1 
ATOM   6930  C CD  . LYS   A 1 978  ? 117.280 165.514 137.622 1.00 33.93  0  942  LYS   A CD  1 
ATOM   6931  C CE  . LYS   A 1 978  ? 116.348 165.113 136.497 1.00 40.80  0  942  LYS   A CE  1 
ATOM   6932  N NZ  . LYS   A 1 978  ? 116.004 166.273 135.635 1.00 43.13  1  942  LYS   A NZ  1 
ATOM   6933  N N   . ASN   A 1 979  ? 118.880 161.313 140.519 1.00 33.09  0  943  ASN   A N   1 
ATOM   6934  C CA  . ASN   A 1 979  ? 118.182 160.395 141.408 1.00 41.18  0  943  ASN   A CA  1 
ATOM   6935  C C   . ASN   A 1 979  ? 119.134 159.348 141.974 1.00 44.51  0  943  ASN   A C   1 
ATOM   6936  O O   . ASN   A 1 979  ? 118.743 158.205 142.217 1.00 42.70  0  943  ASN   A O   1 
ATOM   6937  C CB  . ASN   A 1 979  ? 117.016 159.724 140.684 1.00 40.52  0  943  ASN   A CB  1 
ATOM   6938  C CG  . ASN   A 1 979  ? 115.943 160.709 140.272 1.00 44.93  0  943  ASN   A CG  1 
ATOM   6939  O OD1 . ASN   A 1 979  ? 115.343 161.375 141.112 1.00 48.03  0  943  ASN   A OD1 1 
ATOM   6940  N ND2 . ASN   A 1 979  ? 115.690 160.799 138.974 1.00 41.56  0  943  ASN   A ND2 1 
ATOM   6941  N N   . HIS   A 1 980  ? 120.392 159.726 142.180 1.00 47.37  0  944  HIS   A N   1 
ATOM   6942  C CA  . HIS   A 1 980  ? 121.377 158.797 142.713 1.00 43.98  0  944  HIS   A CA  1 
ATOM   6943  C C   . HIS   A 1 980  ? 121.034 158.425 144.149 1.00 44.57  0  944  HIS   A C   1 
ATOM   6944  O O   . HIS   A 1 980  ? 120.393 159.185 144.877 1.00 47.62  0  944  HIS   A O   1 
ATOM   6945  C CB  . HIS   A 1 980  ? 122.775 159.411 142.643 1.00 37.16  0  944  HIS   A CB  1 
ATOM   6946  C CG  . HIS   A 1 980  ? 123.879 158.403 142.602 1.00 38.41  0  944  HIS   A CG  1 
ATOM   6947  N ND1 . HIS   A 1 980  ? 124.351 157.770 143.731 1.00 41.86  0  944  HIS   A ND1 1 
ATOM   6948  C CD2 . HIS   A 1 980  ? 124.609 157.922 141.569 1.00 43.67  0  944  HIS   A CD2 1 
ATOM   6949  C CE1 . HIS   A 1 980  ? 125.323 156.942 143.395 1.00 41.51  0  944  HIS   A CE1 1 
ATOM   6950  N NE2 . HIS   A 1 980  ? 125.499 157.015 142.089 1.00 45.09  0  944  HIS   A NE2 1 
ATOM   6951  N N   . ALA   A 1 981  ? 121.459 157.229 144.552 1.00 39.38  0  945  ALA   A N   1 
ATOM   6952  C CA  . ALA   A 1 981  ? 121.117 156.737 145.881 1.00 45.17  0  945  ALA   A CA  1 
ATOM   6953  C C   . ALA   A 1 981  ? 121.929 157.441 146.962 1.00 52.38  0  945  ALA   A C   1 
ATOM   6954  O O   . ALA   A 1 981  ? 121.394 157.801 148.017 1.00 55.24  0  945  ALA   A O   1 
ATOM   6955  C CB  . ALA   A 1 981  ? 121.326 155.225 145.948 1.00 36.02  0  945  ALA   A CB  1 
ATOM   6956  N N   . LEU   A 1 982  ? 123.221 157.656 146.716 1.00 43.76  0  946  LEU   A N   1 
ATOM   6957  C CA  . LEU   A 1 982  ? 124.138 158.105 147.756 1.00 43.31  0  946  LEU   A CA  1 
ATOM   6958  C C   . LEU   A 1 982  ? 124.498 159.580 147.668 1.00 48.41  0  946  LEU   A C   1 
ATOM   6959  O O   . LEU   A 1 982  ? 124.874 160.170 148.685 1.00 55.63  0  946  LEU   A O   1 
ATOM   6960  C CB  . LEU   A 1 982  ? 125.424 157.276 147.704 1.00 41.36  0  946  LEU   A CB  1 
ATOM   6961  C CG  . LEU   A 1 982  ? 125.200 155.809 147.337 1.00 45.37  0  946  LEU   A CG  1 
ATOM   6962  C CD1 . LEU   A 1 982  ? 126.480 155.177 146.833 1.00 45.83  0  946  LEU   A CD1 1 
ATOM   6963  C CD2 . LEU   A 1 982  ? 124.655 155.045 148.526 1.00 42.31  0  946  LEU   A CD2 1 
ATOM   6964  N N   . CYS   A 1 983  ? 124.401 160.183 146.486 1.00 50.54  0  947  CYS   A N   1 
ATOM   6965  C CA  . CYS   A 1 983  ? 124.816 161.560 146.252 1.00 48.44  0  947  CYS   A CA  1 
ATOM   6966  C C   . CYS   A 1 983  ? 123.734 162.272 145.439 1.00 46.30  0  947  CYS   A C   1 
ATOM   6967  O O   . CYS   A 1 983  ? 123.999 162.867 144.400 1.00 53.07  0  947  CYS   A O   1 
ATOM   6968  C CB  . CYS   A 1 983  ? 126.175 161.611 145.559 1.00 49.68  0  947  CYS   A CB  1 
ATOM   6969  S SG  . CYS   A 1 983  ? 126.267 160.668 144.030 1.00 64.74  0  947  CYS   A SG  1 
ATOM   6970  N N   . ASN   A 1 984  ? 122.500 162.222 145.945 1.00 39.03  0  948  ASN   A N   1 
ATOM   6971  C CA  . ASN   A 1 984  ? 121.272 162.346 145.164 1.00 46.21  0  948  ASN   A CA  1 
ATOM   6972  C C   . ASN   A 1 984  ? 121.364 163.273 143.955 1.00 46.66  0  948  ASN   A C   1 
ATOM   6973  O O   . ASN   A 1 984  ? 120.955 162.883 142.859 1.00 50.60  0  948  ASN   A O   1 
ATOM   6974  C CB  . ASN   A 1 984  ? 120.124 162.805 146.070 1.00 48.57  0  948  ASN   A CB  1 
ATOM   6975  C CG  . ASN   A 1 984  ? 120.370 164.166 146.685 1.00 55.25  0  948  ASN   A CG  1 
ATOM   6976  O OD1 . ASN   A 1 984  ? 121.497 164.661 146.696 1.00 60.85  0  948  ASN   A OD1 1 
ATOM   6977  N ND2 . ASN   A 1 984  ? 119.311 164.784 147.194 1.00 47.86  0  948  ASN   A ND2 1 
ATOM   6978  N N   . ASN   A 1 985  ? 121.901 164.482 144.112 1.00 34.47  0  949  ASN   A N   1 
ATOM   6979  C CA  . ASN   A 1 985  ? 122.060 165.325 142.933 1.00 39.05  0  949  ASN   A CA  1 
ATOM   6980  C C   . ASN   A 1 985  ? 123.412 166.024 142.908 1.00 43.43  0  949  ASN   A C   1 
ATOM   6981  O O   . ASN   A 1 985  ? 123.587 167.006 142.180 1.00 48.56  0  949  ASN   A O   1 
ATOM   6982  C CB  . ASN   A 1 985  ? 120.937 166.360 142.821 1.00 35.26  0  949  ASN   A CB  1 
ATOM   6983  C CG  . ASN   A 1 985  ? 120.920 167.332 143.974 1.00 48.60  0  949  ASN   A CG  1 
ATOM   6984  O OD1 . ASN   A 1 985  ? 121.501 167.078 145.027 1.00 57.19  0  949  ASN   A OD1 1 
ATOM   6985  N ND2 . ASN   A 1 985  ? 120.261 168.464 143.776 1.00 48.06  0  949  ASN   A ND2 1 
ATOM   6986  N N   . LYS   A 1 986  ? 124.380 165.533 143.683 1.00 39.90  0  950  LYS   A N   1 
ATOM   6987  C CA  . LYS   A 1 986  ? 125.732 166.072 143.591 1.00 42.65  0  950  LYS   A CA  1 
ATOM   6988  C C   . LYS   A 1 986  ? 126.292 165.878 142.189 1.00 42.93  0  950  LYS   A C   1 
ATOM   6989  O O   . LYS   A 1 986  ? 126.866 166.803 141.597 1.00 48.01  0  950  LYS   A O   1 
ATOM   6990  C CB  . LYS   A 1 986  ? 126.637 165.401 144.620 1.00 47.83  0  950  LYS   A CB  1 
ATOM   6991  C CG  . LYS   A 1 986  ? 126.305 165.716 146.062 1.00 52.68  0  950  LYS   A CG  1 
ATOM   6992  C CD  . LYS   A 1 986  ? 127.287 165.025 146.994 1.00 52.31  0  950  LYS   A CD  1 
ATOM   6993  C CE  . LYS   A 1 986  ? 126.841 165.114 148.441 1.00 48.80  0  950  LYS   A CE  1 
ATOM   6994  N NZ  . LYS   A 1 986  ? 127.687 164.267 149.326 1.00 47.11  1  950  LYS   A NZ  1 
ATOM   6995  N N   . LEU   A 1 987  ? 126.117 164.677 141.634 1.00 35.10  0  951  LEU   A N   1 
ATOM   6996  C CA  . LEU   A 1 987  ? 126.605 164.404 140.290 1.00 31.59  0  951  LEU   A CA  1 
ATOM   6997  C C   . LEU   A 1 987  ? 125.879 165.238 139.248 1.00 34.25  0  951  LEU   A C   1 
ATOM   6998  O O   . LEU   A 1 987  ? 126.493 165.651 138.263 1.00 49.87  0  951  LEU   A O   1 
ATOM   6999  C CB  . LEU   A 1 987  ? 126.472 162.919 139.965 1.00 32.88  0  951  LEU   A CB  1 
ATOM   7000  C CG  . LEU   A 1 987  ? 127.143 161.938 140.923 1.00 30.35  0  951  LEU   A CG  1 
ATOM   7001  C CD1 . LEU   A 1 987  ? 127.161 160.544 140.330 1.00 35.78  0  951  LEU   A CD1 1 
ATOM   7002  C CD2 . LEU   A 1 987  ? 128.545 162.386 141.257 1.00 40.47  0  951  LEU   A CD2 1 
ATOM   7003  N N   . TYR   A 1 988  ? 124.584 165.498 139.434 1.00 17.74  0  952  TYR   A N   1 
ATOM   7004  C CA  . TYR   A 1 988  ? 123.882 166.334 138.467 1.00 21.17  0  952  TYR   A CA  1 
ATOM   7005  C C   . TYR   A 1 988  ? 124.372 167.774 138.518 1.00 32.67  0  952  TYR   A C   1 
ATOM   7006  O O   . TYR   A 1 988  ? 124.504 168.427 137.477 1.00 37.40  0  952  TYR   A O   1 
ATOM   7007  C CB  . TYR   A 1 988  ? 122.377 166.283 138.696 1.00 31.11  0  952  TYR   A CB  1 
ATOM   7008  C CG  . TYR   A 1 988  ? 121.601 166.819 137.520 1.00 33.26  0  952  TYR   A CG  1 
ATOM   7009  C CD1 . TYR   A 1 988  ? 121.752 166.267 136.260 1.00 30.18  0  952  TYR   A CD1 1 
ATOM   7010  C CD2 . TYR   A 1 988  ? 120.726 167.882 137.667 1.00 36.33  0  952  TYR   A CD2 1 
ATOM   7011  C CE1 . TYR   A 1 988  ? 121.050 166.752 135.182 1.00 35.42  0  952  TYR   A CE1 1 
ATOM   7012  C CE2 . TYR   A 1 988  ? 120.019 168.374 136.593 1.00 31.49  0  952  TYR   A CE2 1 
ATOM   7013  C CZ  . TYR   A 1 988  ? 120.185 167.804 135.352 1.00 38.09  0  952  TYR   A CZ  1 
ATOM   7014  O OH  . TYR   A 1 988  ? 119.482 168.289 134.276 1.00 37.50  0  952  TYR   A OH  1 
ATOM   7015  N N   . LEU   A 1 989  ? 124.647 168.290 139.715 1.00 42.89  0  953  LEU   A N   1 
ATOM   7016  C CA  . LEU   A 1 989  ? 125.201 169.634 139.815 1.00 37.13  0  953  LEU   A CA  1 
ATOM   7017  C C   . LEU   A 1 989  ? 126.581 169.702 139.174 1.00 39.05  0  953  LEU   A C   1 
ATOM   7018  O O   . LEU   A 1 989  ? 126.911 170.680 138.492 1.00 41.99  0  953  LEU   A O   1 
ATOM   7019  C CB  . LEU   A 1 989  ? 125.254 170.071 141.277 1.00 34.14  0  953  LEU   A CB  1 
ATOM   7020  C CG  . LEU   A 1 989  ? 123.887 170.141 141.961 1.00 36.59  0  953  LEU   A CG  1 
ATOM   7021  C CD1 . LEU   A 1 989  ? 124.031 170.526 143.422 1.00 38.16  0  953  LEU   A CD1 1 
ATOM   7022  C CD2 . LEU   A 1 989  ? 122.961 171.098 141.230 1.00 35.01  0  953  LEU   A CD2 1 
ATOM   7023  N N   . ASP   A 1 990  ? 127.398 168.662 139.368 1.00 44.08  0  954  ASP   A N   1 
ATOM   7024  C CA  . ASP   A 1 990  ? 128.704 168.629 138.716 1.00 38.82  0  954  ASP   A CA  1 
ATOM   7025  C C   . ASP   A 1 990  ? 128.570 168.560 137.199 1.00 23.74  0  954  ASP   A C   1 
ATOM   7026  O O   . ASP   A 1 990  ? 129.316 169.225 136.473 1.00 37.86  0  954  ASP   A O   1 
ATOM   7027  C CB  . ASP   A 1 990  ? 129.523 167.451 139.235 1.00 42.71  0  954  ASP   A CB  1 
ATOM   7028  C CG  . ASP   A 1 990  ? 129.904 167.607 140.690 1.00 44.70  0  954  ASP   A CG  1 
ATOM   7029  O OD1 . ASP   A 1 990  ? 129.634 168.679 141.267 1.00 38.34  0  954  ASP   A OD1 1 
ATOM   7030  O OD2 . ASP   A 1 990  ? 130.481 166.660 141.256 1.00 45.18  -1 954  ASP   A OD2 1 
ATOM   7031  N N   . ILE   A 1 991  ? 127.627 167.759 136.700 1.00 11.95  0  955  ILE   A N   1 
ATOM   7032  C CA  . ILE   A 1 991  ? 127.447 167.656 135.256 1.00 31.50  0  955  ILE   A CA  1 
ATOM   7033  C C   . ILE   A 1 991  ? 126.945 168.978 134.695 1.00 36.88  0  955  ILE   A C   1 
ATOM   7034  O O   . ILE   A 1 991  ? 127.286 169.350 133.569 1.00 43.90  0  955  ILE   A O   1 
ATOM   7035  C CB  . ILE   A 1 991  ? 126.513 166.477 134.901 1.00 34.00  0  955  ILE   A CB  1 
ATOM   7036  C CG1 . ILE   A 1 991  ? 126.972 165.798 133.614 1.00 22.37  0  955  ILE   A CG1 1 
ATOM   7037  C CG2 . ILE   A 1 991  ? 125.079 166.928 134.718 1.00 38.43  0  955  ILE   A CG2 1 
ATOM   7038  C CD1 . ILE   A 1 991  ? 128.184 164.938 133.795 1.00 32.26  0  955  ILE   A CD1 1 
ATOM   7039  N N   . LEU   A 1 992  ? 126.153 169.721 135.471 1.00 37.06  0  956  LEU   A N   1 
ATOM   7040  C CA  . LEU   A 1 992  ? 125.723 171.044 135.032 1.00 35.53  0  956  LEU   A CA  1 
ATOM   7041  C C   . LEU   A 1 992  ? 126.874 172.040 135.031 1.00 37.40  0  956  LEU   A C   1 
ATOM   7042  O O   . LEU   A 1 992  ? 126.947 172.899 134.143 1.00 40.56  0  956  LEU   A O   1 
ATOM   7043  C CB  . LEU   A 1 992  ? 124.579 171.544 135.912 1.00 31.55  0  956  LEU   A CB  1 
ATOM   7044  C CG  . LEU   A 1 992  ? 123.199 171.051 135.481 1.00 37.99  0  956  LEU   A CG  1 
ATOM   7045  C CD1 . LEU   A 1 992  ? 122.104 171.761 136.252 1.00 38.70  0  956  LEU   A CD1 1 
ATOM   7046  C CD2 . LEU   A 1 992  ? 123.014 171.243 133.989 1.00 39.04  0  956  LEU   A CD2 1 
ATOM   7047  N N   . LYS   A 1 993  ? 127.781 171.937 136.004 1.00 36.74  0  957  LYS   A N   1 
ATOM   7048  C CA  . LYS   A 1 993  ? 129.005 172.731 135.963 1.00 34.27  0  957  LYS   A CA  1 
ATOM   7049  C C   . LYS   A 1 993  ? 129.792 172.437 134.694 1.00 37.50  0  957  LYS   A C   1 
ATOM   7050  O O   . LYS   A 1 993  ? 130.278 173.350 134.019 1.00 39.87  0  957  LYS   A O   1 
ATOM   7051  C CB  . LYS   A 1 993  ? 129.865 172.444 137.192 1.00 35.02  0  957  LYS   A CB  1 
ATOM   7052  C CG  . LYS   A 1 993  ? 129.492 173.229 138.428 1.00 38.92  0  957  LYS   A CG  1 
ATOM   7053  C CD  . LYS   A 1 993  ? 130.608 173.168 139.455 1.00 36.78  0  957  LYS   A CD  1 
ATOM   7054  C CE  . LYS   A 1 993  ? 130.781 171.759 139.990 1.00 38.09  0  957  LYS   A CE  1 
ATOM   7055  N NZ  . LYS   A 1 993  ? 131.732 171.698 141.132 1.00 37.25  1  957  LYS   A NZ  1 
ATOM   7056  N N   . VAL   A 1 994  ? 129.925 171.153 134.360 1.00 34.56  0  958  VAL   A N   1 
ATOM   7057  C CA  . VAL   A 1 994  ? 130.667 170.759 133.164 1.00 21.20  0  958  VAL   A CA  1 
ATOM   7058  C C   . VAL   A 1 994  ? 129.988 171.300 131.913 1.00 17.00  0  958  VAL   A C   1 
ATOM   7059  O O   . VAL   A 1 994  ? 130.652 171.755 130.978 1.00 34.08  0  958  VAL   A O   1 
ATOM   7060  C CB  . VAL   A 1 994  ? 130.823 169.228 133.109 1.00 16.04  0  958  VAL   A CB  1 
ATOM   7061  C CG1 . VAL   A 1 994  ? 131.445 168.812 131.802 1.00 27.80  0  958  VAL   A CG1 1 
ATOM   7062  C CG2 . VAL   A 1 994  ? 131.670 168.741 134.262 1.00 19.20  0  958  VAL   A CG2 1 
ATOM   7063  N N   . LEU   A 1 995  ? 128.657 171.251 131.870 1.00 18.95  0  959  LEU   A N   1 
ATOM   7064  C CA  . LEU   A 1 995  ? 127.942 171.758 130.703 1.00 26.96  0  959  LEU   A CA  1 
ATOM   7065  C C   . LEU   A 1 995  ? 128.102 173.267 130.557 1.00 32.81  0  959  LEU   A C   1 
ATOM   7066  O O   . LEU   A 1 995  ? 128.278 173.770 129.442 1.00 39.62  0  959  LEU   A O   1 
ATOM   7067  C CB  . LEU   A 1 995  ? 126.465 171.380 130.784 1.00 36.33  0  959  LEU   A CB  1 
ATOM   7068  C CG  . LEU   A 1 995  ? 126.180 169.882 130.719 1.00 37.53  0  959  LEU   A CG  1 
ATOM   7069  C CD1 . LEU   A 1 995  ? 124.692 169.618 130.713 1.00 32.72  0  959  LEU   A CD1 1 
ATOM   7070  C CD2 . LEU   A 1 995  ? 126.846 169.278 129.503 1.00 34.89  0  959  LEU   A CD2 1 
ATOM   7071  N N   . LYS   A 1 996  ? 128.039 174.009 131.664 1.00 38.49  0  960  LYS   A N   1 
ATOM   7072  C CA  . LYS   A 1 996  ? 128.280 175.448 131.592 1.00 33.21  0  960  LYS   A CA  1 
ATOM   7073  C C   . LYS   A 1 996  ? 129.704 175.742 131.138 1.00 36.77  0  960  LYS   A C   1 
ATOM   7074  O O   . LYS   A 1 996  ? 129.937 176.655 130.335 1.00 41.75  0  960  LYS   A O   1 
ATOM   7075  C CB  . LYS   A 1 996  ? 128.007 176.100 132.947 1.00 31.79  0  960  LYS   A CB  1 
ATOM   7076  C CG  . LYS   A 1 996  ? 126.552 176.058 133.376 1.00 37.42  0  960  LYS   A CG  1 
ATOM   7077  C CD  . LYS   A 1 996  ? 126.410 176.304 134.865 1.00 38.76  0  960  LYS   A CD  1 
ATOM   7078  C CE  . LYS   A 1 996  ? 124.998 176.013 135.335 1.00 40.56  0  960  LYS   A CE  1 
ATOM   7079  N NZ  . LYS   A 1 996  ? 124.879 176.110 136.814 1.00 39.38  1  960  LYS   A NZ  1 
ATOM   7080  N N   . HIS   A 1 997  ? 130.668 174.971 131.642 1.00 36.78  0  961  HIS   A N   1 
ATOM   7081  C CA  . HIS   A 1 997  ? 132.057 175.141 131.237 1.00 34.88  0  961  HIS   A CA  1 
ATOM   7082  C C   . HIS   A 1 997  ? 132.226 174.894 129.744 1.00 31.38  0  961  HIS   A C   1 
ATOM   7083  O O   . HIS   A 1 997  ? 132.935 175.635 129.059 1.00 39.77  0  961  HIS   A O   1 
ATOM   7084  C CB  . HIS   A 1 997  ? 132.942 174.198 132.051 1.00 34.42  0  961  HIS   A CB  1 
ATOM   7085  C CG  . HIS   A 1 997  ? 134.379 174.192 131.634 1.00 38.72  0  961  HIS   A CG  1 
ATOM   7086  N ND1 . HIS   A 1 997  ? 135.391 174.623 132.463 1.00 41.76  0  961  HIS   A ND1 1 
ATOM   7087  C CD2 . HIS   A 1 997  ? 134.978 173.786 130.490 1.00 35.07  0  961  HIS   A CD2 1 
ATOM   7088  C CE1 . HIS   A 1 997  ? 136.550 174.493 131.844 1.00 39.33  0  961  HIS   A CE1 1 
ATOM   7089  N NE2 . HIS   A 1 997  ? 136.327 173.993 130.643 1.00 42.06  0  961  HIS   A NE2 1 
ATOM   7090  N N   . LEU   A 1 998  ? 131.590 173.845 129.223 1.00 29.11  0  962  LEU   A N   1 
ATOM   7091  C CA  . LEU   A 1 998  ? 131.699 173.547 127.801 1.00 28.18  0  962  LEU   A CA  1 
ATOM   7092  C C   . LEU   A 1 998  ? 130.956 174.555 126.943 1.00 28.97  0  962  LEU   A C   1 
ATOM   7093  O O   . LEU   A 1 998  ? 131.350 174.780 125.796 1.00 34.64  0  962  LEU   A O   1 
ATOM   7094  C CB  . LEU   A 1 998  ? 131.181 172.143 127.503 1.00 32.83  0  962  LEU   A CB  1 
ATOM   7095  C CG  . LEU   A 1 998  ? 131.961 170.976 128.104 1.00 30.49  0  962  LEU   A CG  1 
ATOM   7096  C CD1 . LEU   A 1 998  ? 131.375 169.667 127.627 1.00 31.82  0  962  LEU   A CD1 1 
ATOM   7097  C CD2 . LEU   A 1 998  ? 133.425 171.070 127.747 1.00 28.86  0  962  LEU   A CD2 1 
ATOM   7098  N N   . LYS   A 1 999  ? 129.877 175.144 127.454 1.00 30.95  0  963  LYS   A N   1 
ATOM   7099  C CA  . LYS   A 1 999  ? 129.219 176.217 126.722 1.00 35.26  0  963  LYS   A CA  1 
ATOM   7100  C C   . LYS   A 1 999  ? 130.110 177.449 126.636 1.00 46.08  0  963  LYS   A C   1 
ATOM   7101  O O   . LYS   A 1 999  ? 130.221 178.068 125.572 1.00 50.22  0  963  LYS   A O   1 
ATOM   7102  C CB  . LYS   A 1 999  ? 127.888 176.571 127.380 1.00 35.44  0  963  LYS   A CB  1 
ATOM   7103  C CG  . LYS   A 1 999  ? 127.045 177.534 126.564 1.00 36.23  0  963  LYS   A CG  1 
ATOM   7104  C CD  . LYS   A 1 999  ? 125.700 177.787 127.216 1.00 40.30  0  963  LYS   A CD  1 
ATOM   7105  C CE  . LYS   A 1 999  ? 125.750 178.989 128.137 1.00 42.75  0  963  LYS   A CE  1 
ATOM   7106  N NZ  . LYS   A 1 999  ? 125.793 180.259 127.366 1.00 45.31  1  963  LYS   A NZ  1 
ATOM   7107  N N   . THR   A 1 1000 ? 130.746 177.818 127.750 1.00 42.94  0  964  THR   A N   1 
ATOM   7108  C CA  . THR   A 1 1000 ? 131.653 178.962 127.741 1.00 32.72  0  964  THR   A CA  1 
ATOM   7109  C C   . THR   A 1 1000 ? 132.872 178.699 126.866 1.00 30.57  0  964  THR   A C   1 
ATOM   7110  O O   . THR   A 1 1000 ? 133.319 179.586 126.130 1.00 33.97  0  964  THR   A O   1 
ATOM   7111  C CB  . THR   A 1 1000 ? 132.084 179.296 129.168 1.00 33.58  0  964  THR   A CB  1 
ATOM   7112  O OG1 . THR   A 1 1000 ? 130.926 179.399 130.004 1.00 32.34  0  964  THR   A OG1 1 
ATOM   7113  C CG2 . THR   A 1 1000 ? 132.835 180.608 129.199 1.00 39.62  0  964  THR   A CG2 1 
ATOM   7114  N N   . PHE   A 1 1001 ? 133.414 177.483 126.927 1.00 40.28  0  965  PHE   A N   1 
ATOM   7115  C CA  . PHE   A 1 1001 ? 134.651 177.158 126.224 1.00 39.50  0  965  PHE   A CA  1 
ATOM   7116  C C   . PHE   A 1 1001 ? 134.434 177.120 124.718 1.00 36.84  0  965  PHE   A C   1 
ATOM   7117  O O   . PHE   A 1 1001 ? 135.053 177.881 123.967 1.00 40.94  0  965  PHE   A O   1 
ATOM   7118  C CB  . PHE   A 1 1001 ? 135.184 175.815 126.728 1.00 34.87  0  965  PHE   A CB  1 
ATOM   7119  C CG  . PHE   A 1 1001 ? 136.577 175.497 126.274 1.00 38.24  0  965  PHE   A CG  1 
ATOM   7120  C CD1 . PHE   A 1 1001 ? 136.831 175.112 124.971 1.00 41.13  0  965  PHE   A CD1 1 
ATOM   7121  C CD2 . PHE   A 1 1001 ? 137.633 175.559 127.160 1.00 42.81  0  965  PHE   A CD2 1 
ATOM   7122  C CE1 . PHE   A 1 1001 ? 138.109 174.818 124.558 1.00 44.33  0  965  PHE   A CE1 1 
ATOM   7123  C CE2 . PHE   A 1 1001 ? 138.913 175.263 126.750 1.00 43.03  0  965  PHE   A CE2 1 
ATOM   7124  C CZ  . PHE   A 1 1001 ? 139.149 174.892 125.448 1.00 41.83  0  965  PHE   A CZ  1 
ATOM   7125  N N   . PHE   A 1 1002 ? 133.558 176.235 124.257 1.00 32.49  0  966  PHE   A N   1 
ATOM   7126  C CA  . PHE   A 1 1002 ? 133.370 176.015 122.831 1.00 33.37  0  966  PHE   A CA  1 
ATOM   7127  C C   . PHE   A 1 1002 ? 132.414 177.013 122.196 1.00 32.11  0  966  PHE   A C   1 
ATOM   7128  O O   . PHE   A 1 1002 ? 132.116 176.881 121.006 1.00 27.86  0  966  PHE   A O   1 
ATOM   7129  C CB  . PHE   A 1 1002 ? 132.867 174.592 122.584 1.00 38.89  0  966  PHE   A CB  1 
ATOM   7130  C CG  . PHE   A 1 1002 ? 133.874 173.526 122.910 1.00 34.68  0  966  PHE   A CG  1 
ATOM   7131  C CD1 . PHE   A 1 1002 ? 134.871 173.199 122.011 1.00 35.74  0  966  PHE   A CD1 1 
ATOM   7132  C CD2 . PHE   A 1 1002 ? 133.820 172.850 124.115 1.00 34.93  0  966  PHE   A CD2 1 
ATOM   7133  C CE1 . PHE   A 1 1002 ? 135.792 172.221 122.311 1.00 38.41  0  966  PHE   A CE1 1 
ATOM   7134  C CE2 . PHE   A 1 1002 ? 134.740 171.871 124.417 1.00 35.59  0  966  PHE   A CE2 1 
ATOM   7135  C CZ  . PHE   A 1 1002 ? 135.726 171.557 123.516 1.00 34.32  0  966  PHE   A CZ  1 
ATOM   7136  N N   . ASN   A 1 1003 ? 131.921 177.992 122.955 1.00 32.23  0  967  ASN   A N   1 
ATOM   7137  C CA  . ASN   A 1 1003 ? 131.014 179.017 122.441 1.00 39.36  0  967  ASN   A CA  1 
ATOM   7138  C C   . ASN   A 1 1003 ? 129.755 178.382 121.847 1.00 38.65  0  967  ASN   A C   1 
ATOM   7139  O O   . ASN   A 1 1003 ? 129.408 178.581 120.682 1.00 39.49  0  967  ASN   A O   1 
ATOM   7140  C CB  . ASN   A 1 1003 ? 131.725 179.907 121.417 1.00 41.08  0  967  ASN   A CB  1 
ATOM   7141  C CG  . ASN   A 1 1003 ? 131.030 181.232 121.218 1.00 40.19  0  967  ASN   A CG  1 
ATOM   7142  O OD1 . ASN   A 1 1003 ? 130.261 181.676 122.067 1.00 40.05  0  967  ASN   A OD1 1 
ATOM   7143  N ND2 . ASN   A 1 1003 ? 131.299 181.875 120.090 1.00 41.78  0  967  ASN   A ND2 1 
ATOM   7144  N N   . LEU   A 1 1004 ? 129.073 177.607 122.682 1.00 44.82  0  968  LEU   A N   1 
ATOM   7145  C CA  . LEU   A 1 1004 ? 127.882 176.873 122.288 1.00 46.29  0  968  LEU   A CA  1 
ATOM   7146  C C   . LEU   A 1 1004 ? 126.629 177.697 122.551 1.00 46.38  0  968  LEU   A C   1 
ATOM   7147  O O   . LEU   A 1 1004 ? 126.610 178.597 123.393 1.00 47.99  0  968  LEU   A O   1 
ATOM   7148  C CB  . LEU   A 1 1004 ? 127.804 175.539 123.032 1.00 42.39  0  968  LEU   A CB  1 
ATOM   7149  C CG  . LEU   A 1 1004 ? 128.909 174.544 122.683 1.00 44.10  0  968  LEU   A CG  1 
ATOM   7150  C CD1 . LEU   A 1 1004 ? 129.001 173.461 123.733 1.00 39.52  0  968  LEU   A CD1 1 
ATOM   7151  C CD2 . LEU   A 1 1004 ? 128.665 173.946 121.311 1.00 36.69  0  968  LEU   A CD2 1 
ATOM   7152  N N   . ASP   A 1 1005 ? 125.569 177.367 121.810 1.00 46.23  0  969  ASP   A N   1 
ATOM   7153  C CA  . ASP   A 1 1005 ? 124.345 178.160 121.857 1.00 45.39  0  969  ASP   A CA  1 
ATOM   7154  C C   . ASP   A 1 1005 ? 123.684 178.101 123.228 1.00 45.67  0  969  ASP   A C   1 
ATOM   7155  O O   . ASP   A 1 1005 ? 123.232 179.127 123.746 1.00 50.89  0  969  ASP   A O   1 
ATOM   7156  C CB  . ASP   A 1 1005 ? 123.379 177.679 120.778 1.00 45.71  0  969  ASP   A CB  1 
ATOM   7157  C CG  . ASP   A 1 1005 ? 124.071 177.406 119.462 1.00 54.53  0  969  ASP   A CG  1 
ATOM   7158  O OD1 . ASP   A 1 1005 ? 125.171 177.955 119.244 1.00 51.18  0  969  ASP   A OD1 1 
ATOM   7159  O OD2 . ASP   A 1 1005 ? 123.518 176.643 118.645 1.00 55.86  -1 969  ASP   A OD2 1 
ATOM   7160  N N   . ASN   A 1 1006 ? 123.616 176.918 123.830 1.00 48.71  0  970  ASN   A N   1 
ATOM   7161  C CA  . ASN   A 1 1006 ? 122.938 176.745 125.109 1.00 50.60  0  970  ASN   A CA  1 
ATOM   7162  C C   . ASN   A 1 1006 ? 123.434 175.456 125.754 1.00 47.69  0  970  ASN   A C   1 
ATOM   7163  O O   . ASN   A 1 1006 ? 124.400 174.841 125.292 1.00 45.95  0  970  ASN   A O   1 
ATOM   7164  C CB  . ASN   A 1 1006 ? 121.418 176.753 124.921 1.00 44.49  0  970  ASN   A CB  1 
ATOM   7165  C CG  . ASN   A 1 1006 ? 120.961 175.794 123.847 1.00 46.60  0  970  ASN   A CG  1 
ATOM   7166  O OD1 . ASN   A 1 1006 ? 121.763 175.069 123.267 1.00 45.66  0  970  ASN   A OD1 1 
ATOM   7167  N ND2 . ASN   A 1 1006 ? 119.662 175.786 123.575 1.00 49.02  0  970  ASN   A ND2 1 
ATOM   7168  N N   . ILE   A 1 1007 ? 122.772 175.050 126.838 1.00 37.90  0  971  ILE   A N   1 
ATOM   7169  C CA  . ILE   A 1 1007 ? 123.165 173.848 127.563 1.00 34.58  0  971  ILE   A CA  1 
ATOM   7170  C C   . ILE   A 1 1007 ? 122.678 172.570 126.886 1.00 45.03  0  971  ILE   A C   1 
ATOM   7171  O O   . ILE   A 1 1007 ? 123.270 171.503 127.096 1.00 49.71  0  971  ILE   A O   1 
ATOM   7172  C CB  . ILE   A 1 1007 ? 122.667 173.936 129.017 1.00 33.38  0  971  ILE   A CB  1 
ATOM   7173  C CG1 . ILE   A 1 1007 ? 123.324 175.120 129.713 1.00 43.92  0  971  ILE   A CG1 1 
ATOM   7174  C CG2 . ILE   A 1 1007 ? 123.005 172.691 129.800 1.00 39.44  0  971  ILE   A CG2 1 
ATOM   7175  C CD1 . ILE   A 1 1007 ? 124.823 174.993 129.810 1.00 42.02  0  971  ILE   A CD1 1 
ATOM   7176  N N   . ASP   A 1 1008 ? 121.632 172.645 126.063 1.00 45.21  0  972  ASP   A N   1 
ATOM   7177  C CA  . ASP   A 1 1008 ? 121.245 171.483 125.269 1.00 40.95  0  972  ASP   A CA  1 
ATOM   7178  C C   . ASP   A 1 1008 ? 122.382 171.060 124.348 1.00 38.95  0  972  ASP   A C   1 
ATOM   7179  O O   . ASP   A 1 1008 ? 122.761 169.884 124.299 1.00 42.14  0  972  ASP   A O   1 
ATOM   7180  C CB  . ASP   A 1 1008 ? 119.988 171.796 124.459 1.00 43.51  0  972  ASP   A CB  1 
ATOM   7181  C CG  . ASP   A 1 1008 ? 118.726 171.724 125.289 1.00 48.71  0  972  ASP   A CG  1 
ATOM   7182  O OD1 . ASP   A 1 1008 ? 118.701 170.953 126.272 1.00 47.51  0  972  ASP   A OD1 1 
ATOM   7183  O OD2 . ASP   A 1 1008 ? 117.756 172.437 124.957 1.00 46.85  -1 972  ASP   A OD2 1 
ATOM   7184  N N   . THR   A 1 1009 ? 122.949 172.020 123.617 1.00 32.71  0  973  THR   A N   1 
ATOM   7185  C CA  . THR   A 1 1009 ? 124.080 171.721 122.750 1.00 29.95  0  973  THR   A CA  1 
ATOM   7186  C C   . THR   A 1 1009 ? 125.300 171.300 123.554 1.00 30.89  0  973  THR   A C   1 
ATOM   7187  O O   . THR   A 1 1009 ? 126.081 170.461 123.097 1.00 38.69  0  973  THR   A O   1 
ATOM   7188  C CB  . THR   A 1 1009 ? 124.405 172.929 121.879 1.00 35.50  0  973  THR   A CB  1 
ATOM   7189  O OG1 . THR   A 1 1009 ? 123.190 173.470 121.350 1.00 41.10  0  973  THR   A OG1 1 
ATOM   7190  C CG2 . THR   A 1 1009 ? 125.294 172.522 120.728 1.00 35.68  0  973  THR   A CG2 1 
ATOM   7191  N N   . ALA   A 1 1010 ? 125.476 171.863 124.751 1.00 23.75  0  974  ALA   A N   1 
ATOM   7192  C CA  . ALA   A 1 1010 ? 126.576 171.437 125.607 1.00 26.18  0  974  ALA   A CA  1 
ATOM   7193  C C   . ALA   A 1 1010 ? 126.439 169.977 126.002 1.00 29.51  0  974  ALA   A C   1 
ATOM   7194  O O   . ALA   A 1 1010 ? 127.430 169.248 126.014 1.00 32.23  0  974  ALA   A O   1 
ATOM   7195  C CB  . ALA   A 1 1010 ? 126.651 172.315 126.852 1.00 32.60  0  974  ALA   A CB  1 
ATOM   7196  N N   . LEU   A 1 1011 ? 125.224 169.534 126.329 1.00 32.84  0  975  LEU   A N   1 
ATOM   7197  C CA  . LEU   A 1 1011 ? 125.007 168.126 126.649 1.00 24.95  0  975  LEU   A CA  1 
ATOM   7198  C C   . LEU   A 1 1011 ? 125.201 167.246 125.423 1.00 27.07  0  975  LEU   A C   1 
ATOM   7199  O O   . LEU   A 1 1011 ? 125.774 166.155 125.519 1.00 34.71  0  975  LEU   A O   1 
ATOM   7200  C CB  . LEU   A 1 1011 ? 123.611 167.930 127.234 1.00 19.04  0  975  LEU   A CB  1 
ATOM   7201  C CG  . LEU   A 1 1011 ? 123.277 166.516 127.699 1.00 21.84  0  975  LEU   A CG  1 
ATOM   7202  C CD1 . LEU   A 1 1011 ? 124.257 166.060 128.761 1.00 26.32  0  975  LEU   A CD1 1 
ATOM   7203  C CD2 . LEU   A 1 1011 ? 121.863 166.459 128.223 1.00 20.36  0  975  LEU   A CD2 1 
ATOM   7204  N N   . THR   A 1 1012 ? 124.734 167.706 124.262 1.00 28.51  0  976  THR   A N   1 
ATOM   7205  C CA  . THR   A 1 1012 ? 124.928 166.939 123.036 1.00 17.62  0  976  THR   A CA  1 
ATOM   7206  C C   . THR   A 1 1012 ? 126.408 166.742 122.741 1.00 18.98  0  976  THR   A C   1 
ATOM   7207  O O   . THR   A 1 1012 ? 126.832 165.644 122.367 1.00 29.04  0  976  THR   A O   1 
ATOM   7208  C CB  . THR   A 1 1012 ? 124.237 167.638 121.866 1.00 24.19  0  976  THR   A CB  1 
ATOM   7209  O OG1 . THR   A 1 1012 ? 122.818 167.587 122.047 1.00 30.67  0  976  THR   A OG1 1 
ATOM   7210  C CG2 . THR   A 1 1012 ? 124.597 166.974 120.557 1.00 25.68  0  976  THR   A CG2 1 
ATOM   7211  N N   . LEU   A 1 1013 ? 127.212 167.792 122.914 1.00 25.91  0  977  LEU   A N   1 
ATOM   7212  C CA  . LEU   A 1 1013 ? 128.649 167.686 122.686 1.00 28.41  0  977  LEU   A CA  1 
ATOM   7213  C C   . LEU   A 1 1013 ? 129.338 166.870 123.773 1.00 28.63  0  977  LEU   A C   1 
ATOM   7214  O O   . LEU   A 1 1013 ? 130.263 166.106 123.482 1.00 40.75  0  977  LEU   A O   1 
ATOM   7215  C CB  . LEU   A 1 1013 ? 129.269 169.079 122.595 1.00 30.65  0  977  LEU   A CB  1 
ATOM   7216  C CG  . LEU   A 1 1013 ? 130.787 169.180 122.738 1.00 29.34  0  977  LEU   A CG  1 
ATOM   7217  C CD1 . LEU   A 1 1013 ? 131.478 168.511 121.567 1.00 28.26  0  977  LEU   A CD1 1 
ATOM   7218  C CD2 . LEU   A 1 1013 ? 131.208 170.627 122.852 1.00 27.53  0  977  LEU   A CD2 1 
ATOM   7219  N N   . TYR   A 1 1014 ? 128.912 167.019 125.027 1.00 19.33  0  978  TYR   A N   1 
ATOM   7220  C CA  . TYR   A 1 1014 ? 129.506 166.242 126.107 1.00 25.52  0  978  TYR   A CA  1 
ATOM   7221  C C   . TYR   A 1 1014 ? 129.277 164.758 125.893 1.00 25.04  0  978  TYR   A C   1 
ATOM   7222  O O   . TYR   A 1 1014 ? 130.166 163.942 126.154 1.00 28.65  0  978  TYR   A O   1 
ATOM   7223  C CB  . TYR   A 1 1014 ? 128.928 166.683 127.451 1.00 27.79  0  978  TYR   A CB  1 
ATOM   7224  C CG  . TYR   A 1 1014 ? 129.282 165.778 128.606 1.00 22.03  0  978  TYR   A CG  1 
ATOM   7225  C CD1 . TYR   A 1 1014 ? 130.495 165.900 129.256 1.00 23.18  0  978  TYR   A CD1 1 
ATOM   7226  C CD2 . TYR   A 1 1014 ? 128.399 164.808 129.051 1.00 24.20  0  978  TYR   A CD2 1 
ATOM   7227  C CE1 . TYR   A 1 1014 ? 130.822 165.081 130.311 1.00 30.32  0  978  TYR   A CE1 1 
ATOM   7228  C CE2 . TYR   A 1 1014 ? 128.720 163.982 130.106 1.00 29.87  0  978  TYR   A CE2 1 
ATOM   7229  C CZ  . TYR   A 1 1014 ? 129.933 164.124 130.732 1.00 27.84  0  978  TYR   A CZ  1 
ATOM   7230  O OH  . TYR   A 1 1014 ? 130.261 163.304 131.785 1.00 23.82  0  978  TYR   A OH  1 
ATOM   7231  N N   . MET   A 1 1015 ? 128.091 164.391 125.409 1.00 23.41  0  979  MET   A N   1 
ATOM   7232  C CA  . MET   A 1 1015 ? 127.761 162.997 125.152 1.00 14.53  0  979  MET   A CA  1 
ATOM   7233  C C   . MET   A 1 1015 ? 128.615 162.376 124.058 1.00 19.57  0  979  MET   A C   1 
ATOM   7234  O O   . MET   A 1 1015 ? 128.662 161.146 123.965 1.00 28.08  0  979  MET   A O   1 
ATOM   7235  C CB  . MET   A 1 1015 ? 126.288 162.879 124.773 1.00 25.60  0  979  MET   A CB  1 
ATOM   7236  C CG  . MET   A 1 1015 ? 125.583 161.695 125.389 1.00 32.08  0  979  MET   A CG  1 
ATOM   7237  S SD  . MET   A 1 1015 ? 125.382 161.898 127.158 1.00 43.11  0  979  MET   A SD  1 
ATOM   7238  C CE  . MET   A 1 1015 ? 123.807 162.735 127.219 1.00 25.22  0  979  MET   A CE  1 
ATOM   7239  N N   . ASN   A 1 1016 ? 129.282 163.183 123.233 1.00 20.94  0  980  ASN   A N   1 
ATOM   7240  C CA  . ASN   A 1 1016 ? 130.107 162.680 122.143 1.00 11.69  0  980  ASN   A CA  1 
ATOM   7241  C C   . ASN   A 1 1016 ? 131.591 162.947 122.359 1.00 25.04  0  980  ASN   A C   1 
ATOM   7242  O O   . ASN   A 1 1016 ? 132.361 162.946 121.395 1.00 38.14  0  980  ASN   A O   1 
ATOM   7243  C CB  . ASN   A 1 1016 ? 129.653 163.283 120.816 1.00 11.83  0  980  ASN   A CB  1 
ATOM   7244  C CG  . ASN   A 1 1016 ? 128.332 162.728 120.354 1.00 20.90  0  980  ASN   A CG  1 
ATOM   7245  O OD1 . ASN   A 1 1016 ? 128.247 161.591 119.900 1.00 34.47  0  980  ASN   A OD1 1 
ATOM   7246  N ND2 . ASN   A 1 1016 ? 127.286 163.529 120.468 1.00 26.57  0  980  ASN   A ND2 1 
ATOM   7247  N N   . LEU   A 1 1017 ? 132.011 163.184 123.595 1.00 31.77  0  981  LEU   A N   1 
ATOM   7248  C CA  . LEU   A 1 1017 ? 133.433 163.347 123.837 1.00 33.96  0  981  LEU   A CA  1 
ATOM   7249  C C   . LEU   A 1 1017 ? 133.998 162.100 124.502 1.00 33.61  0  981  LEU   A C   1 
ATOM   7250  O O   . LEU   A 1 1017 ? 133.310 161.468 125.307 1.00 42.91  0  981  LEU   A O   1 
ATOM   7251  C CB  . LEU   A 1 1017 ? 133.717 164.566 124.722 1.00 28.36  0  981  LEU   A CB  1 
ATOM   7252  C CG  . LEU   A 1 1017 ? 133.703 165.927 124.023 1.00 26.88  0  981  LEU   A CG  1 
ATOM   7253  C CD1 . LEU   A 1 1017 ? 133.951 167.035 125.023 1.00 23.60  0  981  LEU   A CD1 1 
ATOM   7254  C CD2 . LEU   A 1 1017 ? 134.728 165.974 122.903 1.00 24.82  0  981  LEU   A CD2 1 
ATOM   7255  N N   . PRO   A 1 1018 ? 135.233 161.722 124.184 1.00 19.64  0  982  PRO   A N   1 
ATOM   7256  C CA  . PRO   A 1 1018 ? 135.784 160.477 124.723 1.00 18.50  0  982  PRO   A CA  1 
ATOM   7257  C C   . PRO   A 1 1018 ? 135.854 160.496 126.238 1.00 19.99  0  982  PRO   A C   1 
ATOM   7258  O O   . PRO   A 1 1018 ? 136.074 161.535 126.860 1.00 16.28  0  982  PRO   A O   1 
ATOM   7259  C CB  . PRO   A 1 1018 ? 137.183 160.414 124.105 1.00 28.14  0  982  PRO   A CB  1 
ATOM   7260  C CG  . PRO   A 1 1018 ? 137.089 161.247 122.886 1.00 31.38  0  982  PRO   A CG  1 
ATOM   7261  C CD  . PRO   A 1 1018 ? 136.144 162.351 123.218 1.00 25.33  0  982  PRO   A CD  1 
ATOM   7262  N N   . MET   A 1 1019 ? 135.660 159.320 126.833 1.00 31.16  0  983  MET   A N   1 
ATOM   7263  C CA  . MET   A 1 1019 ? 135.755 159.190 128.280 1.00 32.61  0  983  MET   A CA  1 
ATOM   7264  C C   . MET   A 1 1019 ? 137.178 159.352 128.790 1.00 38.65  0  983  MET   A C   1 
ATOM   7265  O O   . MET   A 1 1019 ? 137.374 159.454 130.005 1.00 37.83  0  983  MET   A O   1 
ATOM   7266  C CB  . MET   A 1 1019 ? 135.189 157.843 128.722 1.00 32.19  0  983  MET   A CB  1 
ATOM   7267  C CG  . MET   A 1 1019 ? 133.710 157.683 128.432 1.00 38.49  0  983  MET   A CG  1 
ATOM   7268  S SD  . MET   A 1 1019 ? 132.808 156.967 129.810 1.00 48.68  0  983  MET   A SD  1 
ATOM   7269  C CE  . MET   A 1 1019 ? 133.777 155.496 130.082 1.00 31.76  0  983  MET   A CE  1 
ATOM   7270  N N   . LEU   A 1 1020 ? 138.170 159.356 127.898 1.00 37.48  0  984  LEU   A N   1 
ATOM   7271  C CA  . LEU   A 1 1020 ? 139.535 159.673 128.301 1.00 33.11  0  984  LEU   A CA  1 
ATOM   7272  C C   . LEU   A 1 1020 ? 139.637 161.115 128.782 1.00 32.99  0  984  LEU   A C   1 
ATOM   7273  O O   . LEU   A 1 1020 ? 140.273 161.401 129.802 1.00 33.09  0  984  LEU   A O   1 
ATOM   7274  C CB  . LEU   A 1 1020 ? 140.489 159.423 127.134 1.00 28.48  0  984  LEU   A CB  1 
ATOM   7275  C CG  . LEU   A 1 1020 ? 141.941 159.093 127.465 1.00 22.25  0  984  LEU   A CG  1 
ATOM   7276  C CD1 . LEU   A 1 1020 ? 142.057 157.658 127.931 1.00 26.79  0  984  LEU   A CD1 1 
ATOM   7277  C CD2 . LEU   A 1 1020 ? 142.818 159.340 126.258 1.00 21.99  0  984  LEU   A CD2 1 
ATOM   7278  N N   . PHE   A 1 1021 ? 139.006 162.039 128.058 1.00 30.24  0  985  PHE   A N   1 
ATOM   7279  C CA  . PHE   A 1 1021 ? 139.018 163.459 128.427 1.00 26.60  0  985  PHE   A CA  1 
ATOM   7280  C C   . PHE   A 1 1021 ? 137.754 163.821 129.200 1.00 32.70  0  985  PHE   A C   1 
ATOM   7281  O O   . PHE   A 1 1021 ? 137.820 164.336 130.319 1.00 36.56  0  985  PHE   A O   1 
ATOM   7282  C CB  . PHE   A 1 1021 ? 139.153 164.331 127.178 1.00 24.34  0  985  PHE   A CB  1 
ATOM   7283  C CG  . PHE   A 1 1021 ? 140.205 163.868 126.219 1.00 23.99  0  985  PHE   A CG  1 
ATOM   7284  C CD1 . PHE   A 1 1021 ? 141.441 163.450 126.672 1.00 28.45  0  985  PHE   A CD1 1 
ATOM   7285  C CD2 . PHE   A 1 1021 ? 139.966 163.874 124.861 1.00 22.37  0  985  PHE   A CD2 1 
ATOM   7286  C CE1 . PHE   A 1 1021 ? 142.408 163.037 125.790 1.00 29.97  0  985  PHE   A CE1 1 
ATOM   7287  C CE2 . PHE   A 1 1021 ? 140.931 163.462 123.977 1.00 25.41  0  985  PHE   A CE2 1 
ATOM   7288  C CZ  . PHE   A 1 1021 ? 142.153 163.042 124.441 1.00 31.03  0  985  PHE   A CZ  1 
ATOM   7289  N N   . GLY   A 1 1022 ? 136.599 163.527 128.615 1.00 45.08  0  986  GLY   A N   1 
ATOM   7290  C CA  . GLY   A 1 1022 ? 135.297 163.948 129.085 1.00 42.81  0  986  GLY   A CA  1 
ATOM   7291  C C   . GLY   A 1 1022 ? 134.634 162.821 129.849 1.00 45.09  0  986  GLY   A C   1 
ATOM   7292  O O   . GLY   A 1 1022 ? 134.849 162.655 131.064 1.00 38.28  0  986  GLY   A O   1 
ATOM   7293  N N   . GLY   A 1 1023 ? 133.824 162.024 129.162 1.00 44.19  0  987  GLY   A N   1 
ATOM   7294  C CA  . GLY   A 1 1023 ? 133.089 160.961 129.811 1.00 39.25  0  987  GLY   A CA  1 
ATOM   7295  C C   . GLY   A 1 1023 ? 131.717 160.735 129.223 1.00 40.93  0  987  GLY   A C   1 
ATOM   7296  O O   . GLY   A 1 1023 ? 130.939 159.931 129.741 1.00 53.05  0  987  GLY   A O   1 
ATOM   7297  N N   . GLY   A 1 1024 ? 131.405 161.431 128.139 1.00 29.15  0  988  GLY   A N   1 
ATOM   7298  C CA  . GLY   A 1 1024 ? 130.143 161.192 127.477 1.00 35.40  0  988  GLY   A CA  1 
ATOM   7299  C C   . GLY   A 1 1024 ? 130.118 159.900 126.692 1.00 21.61  0  988  GLY   A C   1 
ATOM   7300  O O   . GLY   A 1 1024 ? 129.417 158.957 127.064 1.00 26.05  0  988  GLY   A O   1 
ATOM   7301  N N   . ASP   A 1 1025 ? 130.900 159.835 125.619 1.00 19.52  0  989  ASP   A N   1 
ATOM   7302  C CA  . ASP   A 1 1025 ? 130.837 158.717 124.689 1.00 22.99  0  989  ASP   A CA  1 
ATOM   7303  C C   . ASP   A 1 1025 ? 131.720 157.572 125.163 1.00 27.87  0  989  ASP   A C   1 
ATOM   7304  O O   . ASP   A 1 1025 ? 132.946 157.718 125.226 1.00 26.06  0  989  ASP   A O   1 
ATOM   7305  C CB  . ASP   A 1 1025 ? 131.265 159.166 123.292 1.00 16.51  0  989  ASP   A CB  1 
ATOM   7306  C CG  . ASP   A 1 1025 ? 130.445 158.520 122.197 1.00 29.52  0  989  ASP   A CG  1 
ATOM   7307  O OD1 . ASP   A 1 1025 ? 129.337 158.028 122.496 1.00 36.81  0  989  ASP   A OD1 1 
ATOM   7308  O OD2 . ASP   A 1 1025 ? 130.904 158.503 121.036 1.00 21.75  -1 989  ASP   A OD2 1 
ATOM   7309  N N   . PRO   A 1 1026 ? 131.141 156.414 125.491 1.00 32.02  0  990  PRO   A N   1 
ATOM   7310  C CA  . PRO   A 1 1026 ? 131.961 155.275 125.915 1.00 31.68  0  990  PRO   A CA  1 
ATOM   7311  C C   . PRO   A 1 1026 ? 132.476 154.436 124.763 1.00 37.06  0  990  PRO   A C   1 
ATOM   7312  O O   . PRO   A 1 1026 ? 133.386 153.623 124.973 1.00 43.88  0  990  PRO   A O   1 
ATOM   7313  C CB  . PRO   A 1 1026 ? 130.997 154.470 126.788 1.00 31.48  0  990  PRO   A CB  1 
ATOM   7314  C CG  . PRO   A 1 1026 ? 129.668 154.713 126.160 1.00 31.96  0  990  PRO   A CG  1 
ATOM   7315  C CD  . PRO   A 1 1026 ? 129.705 156.094 125.531 1.00 34.41  0  990  PRO   A CD  1 
ATOM   7316  N N   . ASN   A 1 1027 ? 131.927 154.602 123.563 1.00 26.94  0  991  ASN   A N   1 
ATOM   7317  C CA  . ASN   A 1 1027 ? 132.327 153.831 122.390 1.00 22.88  0  991  ASN   A CA  1 
ATOM   7318  C C   . ASN   A 1 1027 ? 132.939 154.788 121.375 1.00 25.45  0  991  ASN   A C   1 
ATOM   7319  O O   . ASN   A 1 1027 ? 132.222 155.555 120.727 1.00 32.87  0  991  ASN   A O   1 
ATOM   7320  C CB  . ASN   A 1 1027 ? 131.141 153.081 121.799 1.00 23.82  0  991  ASN   A CB  1 
ATOM   7321  C CG  . ASN   A 1 1027 ? 130.776 151.856 122.601 1.00 33.47  0  991  ASN   A CG  1 
ATOM   7322  O OD1 . ASN   A 1 1027 ? 129.601 151.583 122.837 1.00 30.67  0  991  ASN   A OD1 1 
ATOM   7323  N ND2 . ASN   A 1 1027 ? 131.786 151.114 123.037 1.00 34.65  0  991  ASN   A ND2 1 
ATOM   7324  N N   . LEU   A 1 1028 ? 134.259 154.731 121.231 1.00 26.19  0  992  LEU   A N   1 
ATOM   7325  C CA  . LEU   A 1 1028 ? 134.949 155.581 120.276 1.00 25.97  0  992  LEU   A CA  1 
ATOM   7326  C C   . LEU   A 1 1028 ? 134.617 155.158 118.850 1.00 26.33  0  992  LEU   A C   1 
ATOM   7327  O O   . LEU   A 1 1028 ? 134.157 154.044 118.594 1.00 30.22  0  992  LEU   A O   1 
ATOM   7328  C CB  . LEU   A 1 1028 ? 136.456 155.525 120.507 1.00 22.32  0  992  LEU   A CB  1 
ATOM   7329  C CG  . LEU   A 1 1028 ? 136.912 156.015 121.878 1.00 15.90  0  992  LEU   A CG  1 
ATOM   7330  C CD1 . LEU   A 1 1028 ? 138.360 155.658 122.120 1.00 16.79  0  992  LEU   A CD1 1 
ATOM   7331  C CD2 . LEU   A 1 1028 ? 136.702 157.505 121.974 1.00 16.26  0  992  LEU   A CD2 1 
ATOM   7332  N N   . LEU   A 1 1029 ? 134.858 156.074 117.910 1.00 19.45  0  993  LEU   A N   1 
ATOM   7333  C CA  . LEU   A 1 1029 ? 134.511 155.813 116.518 1.00 16.83  0  993  LEU   A CA  1 
ATOM   7334  C C   . LEU   A 1 1029 ? 135.288 154.636 115.949 1.00 19.32  0  993  LEU   A C   1 
ATOM   7335  O O   . LEU   A 1 1029 ? 134.765 153.901 115.104 1.00 29.15  0  993  LEU   A O   1 
ATOM   7336  C CB  . LEU   A 1 1029 ? 134.754 157.061 115.672 1.00 16.30  0  993  LEU   A CB  1 
ATOM   7337  C CG  . LEU   A 1 1029 ? 133.510 157.872 115.330 1.00 13.84  0  993  LEU   A CG  1 
ATOM   7338  C CD1 . LEU   A 1 1029 ? 133.850 159.003 114.383 1.00 17.03  0  993  LEU   A CD1 1 
ATOM   7339  C CD2 . LEU   A 1 1029 ? 132.462 156.966 114.728 1.00 12.40  0  993  LEU   A CD2 1 
ATOM   7340  N N   . TYR   A 1 1030 ? 136.528 154.433 116.396 1.00 9.10   0  994  TYR   A N   1 
ATOM   7341  C CA  . TYR   A 1 1030 ? 137.316 153.324 115.873 1.00 16.28  0  994  TYR   A CA  1 
ATOM   7342  C C   . TYR   A 1 1030 ? 136.657 151.985 116.161 1.00 25.37  0  994  TYR   A C   1 
ATOM   7343  O O   . TYR   A 1 1030 ? 136.854 151.024 115.410 1.00 28.57  0  994  TYR   A O   1 
ATOM   7344  C CB  . TYR   A 1 1030 ? 138.729 153.360 116.451 1.00 25.94  0  994  TYR   A CB  1 
ATOM   7345  C CG  . TYR   A 1 1030 ? 138.908 152.602 117.746 1.00 20.61  0  994  TYR   A CG  1 
ATOM   7346  C CD1 . TYR   A 1 1030 ? 139.287 151.271 117.748 1.00 17.28  0  994  TYR   A CD1 1 
ATOM   7347  C CD2 . TYR   A 1 1030 ? 138.732 153.229 118.964 1.00 20.19  0  994  TYR   A CD2 1 
ATOM   7348  C CE1 . TYR   A 1 1030 ? 139.455 150.584 118.922 1.00 22.03  0  994  TYR   A CE1 1 
ATOM   7349  C CE2 . TYR   A 1 1030 ? 138.904 152.547 120.146 1.00 22.78  0  994  TYR   A CE2 1 
ATOM   7350  C CZ  . TYR   A 1 1030 ? 139.266 151.226 120.118 1.00 23.52  0  994  TYR   A CZ  1 
ATOM   7351  O OH  . TYR   A 1 1030 ? 139.441 150.539 121.295 1.00 26.55  0  994  TYR   A OH  1 
ATOM   7352  N N   . ARG   A 1 1031 ? 135.875 151.896 117.235 1.00 30.28  0  995  ARG   A N   1 
ATOM   7353  C CA  . ARG   A 1 1031 ? 135.202 150.646 117.556 1.00 20.19  0  995  ARG   A CA  1 
ATOM   7354  C C   . ARG   A 1 1031 ? 134.138 150.288 116.530 1.00 20.63  0  995  ARG   A C   1 
ATOM   7355  O O   . ARG   A 1 1031 ? 133.733 149.124 116.457 1.00 27.22  0  995  ARG   A O   1 
ATOM   7356  C CB  . ARG   A 1 1031 ? 134.591 150.730 118.951 1.00 16.50  0  995  ARG   A CB  1 
ATOM   7357  C CG  . ARG   A 1 1031 ? 135.525 150.269 120.045 1.00 18.36  0  995  ARG   A CG  1 
ATOM   7358  C CD  . ARG   A 1 1031 ? 135.135 148.898 120.537 1.00 25.36  0  995  ARG   A CD  1 
ATOM   7359  N NE  . ARG   A 1 1031 ? 136.248 148.183 121.145 1.00 31.37  0  995  ARG   A NE  1 
ATOM   7360  C CZ  . ARG   A 1 1031 ? 136.239 146.886 121.421 1.00 34.35  0  995  ARG   A CZ  1 
ATOM   7361  N NH1 . ARG   A 1 1031 ? 135.188 146.130 121.154 1.00 30.60  1  995  ARG   A NH1 1 
ATOM   7362  N NH2 . ARG   A 1 1031 ? 137.312 146.334 121.980 1.00 34.86  0  995  ARG   A NH2 1 
ATOM   7363  N N   . SER   A 1 1032 ? 133.682 151.255 115.736 1.00 14.45  0  996  SER   A N   1 
ATOM   7364  C CA  . SER   A 1 1032 ? 132.729 150.973 114.673 1.00 10.34  0  996  SER   A CA  1 
ATOM   7365  C C   . SER   A 1 1032 ? 133.388 150.401 113.429 1.00 32.93  0  996  SER   A C   1 
ATOM   7366  O O   . SER   A 1 1032 ? 132.678 150.009 112.498 1.00 41.25  0  996  SER   A O   1 
ATOM   7367  C CB  . SER   A 1 1032 ? 131.965 152.242 114.300 1.00 5.93   0  996  SER   A CB  1 
ATOM   7368  O OG  . SER   A 1 1032 ? 131.245 152.743 115.408 1.00 20.63  0  996  SER   A OG  1 
ATOM   7369  N N   . PHE   A 1 1033 ? 134.719 150.345 113.388 1.00 32.34  0  997  PHE   A N   1 
ATOM   7370  C CA  . PHE   A 1 1033 ? 135.443 149.879 112.214 1.00 16.61  0  997  PHE   A CA  1 
ATOM   7371  C C   . PHE   A 1 1033 ? 136.487 148.812 112.502 1.00 11.12  0  997  PHE   A C   1 
ATOM   7372  O O   . PHE   A 1 1033 ? 136.857 148.086 111.576 1.00 19.59  0  997  PHE   A O   1 
ATOM   7373  C CB  . PHE   A 1 1033 ? 136.123 151.057 111.511 1.00 24.86  0  997  PHE   A CB  1 
ATOM   7374  C CG  . PHE   A 1 1033 ? 135.173 152.138 111.089 1.00 23.96  0  997  PHE   A CG  1 
ATOM   7375  C CD1 . PHE   A 1 1033 ? 134.497 152.052 109.888 1.00 24.11  0  997  PHE   A CD1 1 
ATOM   7376  C CD2 . PHE   A 1 1033 ? 134.960 153.241 111.890 1.00 17.09  0  997  PHE   A CD2 1 
ATOM   7377  C CE1 . PHE   A 1 1033 ? 133.630 153.046 109.496 1.00 20.65  0  997  PHE   A CE1 1 
ATOM   7378  C CE2 . PHE   A 1 1033 ? 134.092 154.235 111.501 1.00 22.86  0  997  PHE   A CE2 1 
ATOM   7379  C CZ  . PHE   A 1 1033 ? 133.427 154.138 110.304 1.00 17.00  0  997  PHE   A CZ  1 
ATOM   7380  N N   . TYR   A 1 1034 ? 136.987 148.697 113.728 1.00 22.11  0  998  TYR   A N   1 
ATOM   7381  C CA  . TYR   A 1 1034 ? 137.828 147.570 114.102 1.00 20.40  0  998  TYR   A CA  1 
ATOM   7382  C C   . TYR   A 1 1034 ? 137.824 147.449 115.616 1.00 28.56  0  998  TYR   A C   1 
ATOM   7383  O O   . TYR   A 1 1034 ? 137.779 148.456 116.323 1.00 36.91  0  998  TYR   A O   1 
ATOM   7384  C CB  . TYR   A 1 1034 ? 139.261 147.703 113.565 1.00 17.69  0  998  TYR   A CB  1 
ATOM   7385  C CG  . TYR   A 1 1034 ? 139.864 149.088 113.623 1.00 19.07  0  998  TYR   A CG  1 
ATOM   7386  C CD1 . TYR   A 1 1034 ? 139.646 150.002 112.606 1.00 21.72  0  998  TYR   A CD1 1 
ATOM   7387  C CD2 . TYR   A 1 1034 ? 140.686 149.467 114.672 1.00 21.01  0  998  TYR   A CD2 1 
ATOM   7388  C CE1 . TYR   A 1 1034 ? 140.199 151.258 112.648 1.00 23.20  0  998  TYR   A CE1 1 
ATOM   7389  C CE2 . TYR   A 1 1034 ? 141.243 150.722 114.718 1.00 14.02  0  998  TYR   A CE2 1 
ATOM   7390  C CZ  . TYR   A 1 1034 ? 140.996 151.610 113.703 1.00 16.98  0  998  TYR   A CZ  1 
ATOM   7391  O OH  . TYR   A 1 1034 ? 141.548 152.863 113.739 1.00 26.74  0  998  TYR   A OH  1 
ATOM   7392  N N   . ARG   A 1 1035 ? 137.869 146.210 116.102 1.00 31.42  0  999  ARG   A N   1 
ATOM   7393  C CA  . ARG   A 1 1035 ? 137.656 145.959 117.522 1.00 29.12  0  999  ARG   A CA  1 
ATOM   7394  C C   . ARG   A 1 1035 ? 138.809 146.493 118.363 1.00 30.30  0  999  ARG   A C   1 
ATOM   7395  O O   . ARG   A 1 1035 ? 138.616 147.358 119.222 1.00 42.61  0  999  ARG   A O   1 
ATOM   7396  C CB  . ARG   A 1 1035 ? 137.461 144.463 117.763 1.00 33.73  0  999  ARG   A CB  1 
ATOM   7397  C CG  . ARG   A 1 1035 ? 136.065 143.944 117.458 1.00 32.36  0  999  ARG   A CG  1 
ATOM   7398  C CD  . ARG   A 1 1035 ? 135.901 142.521 117.977 1.00 40.50  0  999  ARG   A CD  1 
ATOM   7399  N NE  . ARG   A 1 1035 ? 134.544 142.006 117.834 1.00 44.11  0  999  ARG   A NE  1 
ATOM   7400  C CZ  . ARG   A 1 1035 ? 134.016 141.579 116.695 1.00 44.05  0  999  ARG   A CZ  1 
ATOM   7401  N NH1 . ARG   A 1 1035 ? 134.687 141.633 115.557 1.00 32.49  1  999  ARG   A NH1 1 
ATOM   7402  N NH2 . ARG   A 1 1035 ? 132.781 141.087 116.698 1.00 42.77  0  999  ARG   A NH2 1 
ATOM   7403  N N   . ARG   A 1 1036 ? 140.015 145.989 118.134 1.00 25.24  0  1000 ARG   A N   1 
ATOM   7404  C CA  . ARG   A 1 1036 ? 141.150 146.282 118.995 1.00 28.03  0  1000 ARG   A CA  1 
ATOM   7405  C C   . ARG   A 1 1036 ? 142.040 147.355 118.384 1.00 36.20  0  1000 ARG   A C   1 
ATOM   7406  O O   . ARG   A 1 1036 ? 142.171 147.460 117.163 1.00 43.16  0  1000 ARG   A O   1 
ATOM   7407  C CB  . ARG   A 1 1036 ? 141.976 145.023 119.255 1.00 34.07  0  1000 ARG   A CB  1 
ATOM   7408  C CG  . ARG   A 1 1036 ? 141.168 143.813 119.677 1.00 35.93  0  1000 ARG   A CG  1 
ATOM   7409  C CD  . ARG   A 1 1036 ? 140.451 144.056 120.987 1.00 45.45  0  1000 ARG   A CD  1 
ATOM   7410  N NE  . ARG   A 1 1036 ? 141.368 144.425 122.057 1.00 51.41  0  1000 ARG   A NE  1 
ATOM   7411  C CZ  . ARG   A 1 1036 ? 142.131 143.568 122.721 1.00 50.13  0  1000 ARG   A CZ  1 
ATOM   7412  N NH1 . ARG   A 1 1036 ? 142.127 142.276 122.437 1.00 44.87  1  1000 ARG   A NH1 1 
ATOM   7413  N NH2 . ARG   A 1 1036 ? 142.917 144.018 123.695 1.00 40.48  0  1000 ARG   A NH2 1 
ATOM   7414  N N   . THR   A 1 1037 ? 142.649 148.157 119.254 1.00 37.68  0  1001 THR   A N   1 
ATOM   7415  C CA  . THR   A 1 1037 ? 143.643 149.144 118.861 1.00 36.65  0  1001 THR   A CA  1 
ATOM   7416  C C   . THR   A 1 1037 ? 144.746 149.140 119.907 1.00 30.68  0  1001 THR   A C   1 
ATOM   7417  O O   . THR   A 1 1037 ? 144.485 148.837 121.077 1.00 33.01  0  1001 THR   A O   1 
ATOM   7418  C CB  . THR   A 1 1037 ? 143.033 150.548 118.725 1.00 31.60  0  1001 THR   A CB  1 
ATOM   7419  O OG1 . THR   A 1 1037 ? 143.910 151.387 117.965 1.00 23.80  0  1001 THR   A OG1 1 
ATOM   7420  C CG2 . THR   A 1 1037 ? 142.805 151.174 120.086 1.00 32.22  0  1001 THR   A CG2 1 
ATOM   7421  N N   . PRO   A 1 1038 ? 145.986 149.435 119.519 1.00 26.03  0  1002 PRO   A N   1 
ATOM   7422  C CA  . PRO   A 1 1038 ? 147.090 149.460 120.485 1.00 32.45  0  1002 PRO   A CA  1 
ATOM   7423  C C   . PRO   A 1 1038 ? 147.382 150.823 121.094 1.00 36.77  0  1002 PRO   A C   1 
ATOM   7424  O O   . PRO   A 1 1038 ? 148.271 150.917 121.947 1.00 33.31  0  1002 PRO   A O   1 
ATOM   7425  C CB  . PRO   A 1 1038 ? 148.271 148.992 119.630 1.00 29.94  0  1002 PRO   A CB  1 
ATOM   7426  C CG  . PRO   A 1 1038 ? 147.970 149.545 118.282 1.00 27.27  0  1002 PRO   A CG  1 
ATOM   7427  C CD  . PRO   A 1 1038 ? 146.471 149.549 118.132 1.00 21.38  0  1002 PRO   A CD  1 
ATOM   7428  N N   . ASP   A 1 1039 ? 146.666 151.871 120.688 1.00 36.39  0  1003 ASP   A N   1 
ATOM   7429  C CA  . ASP   A 1 1039 ? 146.902 153.230 121.176 1.00 25.40  0  1003 ASP   A CA  1 
ATOM   7430  C C   . ASP   A 1 1039 ? 145.545 153.888 121.400 1.00 28.21  0  1003 ASP   A C   1 
ATOM   7431  O O   . ASP   A 1 1039 ? 144.908 154.341 120.446 1.00 31.58  0  1003 ASP   A O   1 
ATOM   7432  C CB  . ASP   A 1 1039 ? 147.741 154.028 120.188 1.00 24.92  0  1003 ASP   A CB  1 
ATOM   7433  C CG  . ASP   A 1 1039 ? 148.220 155.339 120.762 1.00 36.30  0  1003 ASP   A CG  1 
ATOM   7434  O OD1 . ASP   A 1 1039 ? 148.102 155.531 121.988 1.00 49.04  0  1003 ASP   A OD1 1 
ATOM   7435  O OD2 . ASP   A 1 1039 ? 148.708 156.186 119.988 1.00 41.61  -1 1003 ASP   A OD2 1 
ATOM   7436  N N   . PHE   A 1 1040 ? 145.108 153.941 122.659 1.00 29.16  0  1004 PHE   A N   1 
ATOM   7437  C CA  . PHE   A 1 1040 ? 143.811 154.536 122.962 1.00 30.46  0  1004 PHE   A CA  1 
ATOM   7438  C C   . PHE   A 1 1040 ? 143.839 156.053 122.847 1.00 27.66  0  1004 PHE   A C   1 
ATOM   7439  O O   . PHE   A 1 1040 ? 142.829 156.660 122.476 1.00 16.75  0  1004 PHE   A O   1 
ATOM   7440  C CB  . PHE   A 1 1040 ? 143.359 154.132 124.362 1.00 29.89  0  1004 PHE   A CB  1 
ATOM   7441  C CG  . PHE   A 1 1040 ? 142.921 152.705 124.467 1.00 26.74  0  1004 PHE   A CG  1 
ATOM   7442  C CD1 . PHE   A 1 1040 ? 141.929 152.212 123.646 1.00 25.28  0  1004 PHE   A CD1 1 
ATOM   7443  C CD2 . PHE   A 1 1040 ? 143.499 151.859 125.394 1.00 27.12  0  1004 PHE   A CD2 1 
ATOM   7444  C CE1 . PHE   A 1 1040 ? 141.526 150.903 123.743 1.00 27.09  0  1004 PHE   A CE1 1 
ATOM   7445  C CE2 . PHE   A 1 1040 ? 143.097 150.549 125.494 1.00 27.86  0  1004 PHE   A CE2 1 
ATOM   7446  C CZ  . PHE   A 1 1040 ? 142.110 150.070 124.669 1.00 27.63  0  1004 PHE   A CZ  1 
ATOM   7447  N N   . LEU   A 1 1041 ? 144.971 156.682 123.171 1.00 24.42  0  1005 LEU   A N   1 
ATOM   7448  C CA  . LEU   A 1 1041 ? 145.039 158.139 123.151 1.00 27.33  0  1005 LEU   A CA  1 
ATOM   7449  C C   . LEU   A 1 1041 ? 144.854 158.688 121.743 1.00 23.87  0  1005 LEU   A C   1 
ATOM   7450  O O   . LEU   A 1 1041 ? 144.134 159.672 121.545 1.00 26.68  0  1005 LEU   A O   1 
ATOM   7451  C CB  . LEU   A 1 1041 ? 146.367 158.610 123.737 1.00 23.95  0  1005 LEU   A CB  1 
ATOM   7452  C CG  . LEU   A 1 1041 ? 146.653 160.108 123.647 1.00 20.41  0  1005 LEU   A CG  1 
ATOM   7453  C CD1 . LEU   A 1 1041 ? 145.624 160.902 124.422 1.00 17.58  0  1005 LEU   A CD1 1 
ATOM   7454  C CD2 . LEU   A 1 1041 ? 148.044 160.404 124.157 1.00 28.99  0  1005 LEU   A CD2 1 
ATOM   7455  N N   . THR   A 1 1042 ? 145.501 158.073 120.753 1.00 22.32  0  1006 THR   A N   1 
ATOM   7456  C CA  . THR   A 1 1042 ? 145.365 158.554 119.382 1.00 20.85  0  1006 THR   A CA  1 
ATOM   7457  C C   . THR   A 1 1042 ? 143.943 158.376 118.873 1.00 26.49  0  1006 THR   A C   1 
ATOM   7458  O O   . THR   A 1 1042 ? 143.408 159.257 118.189 1.00 28.14  0  1006 THR   A O   1 
ATOM   7459  C CB  . THR   A 1 1042 ? 146.352 157.834 118.469 1.00 16.84  0  1006 THR   A CB  1 
ATOM   7460  O OG1 . THR   A 1 1042 ? 147.647 157.832 119.077 1.00 29.06  0  1006 THR   A OG1 1 
ATOM   7461  C CG2 . THR   A 1 1042 ? 146.437 158.542 117.133 1.00 25.64  0  1006 THR   A CG2 1 
ATOM   7462  N N   . GLU   A 1 1043 ? 143.315 157.243 119.191 1.00 30.24  0  1007 GLU   A N   1 
ATOM   7463  C CA  . GLU   A 1 1043 ? 141.930 157.034 118.787 1.00 23.32  0  1007 GLU   A CA  1 
ATOM   7464  C C   . GLU   A 1 1043 ? 141.013 158.052 119.446 1.00 35.74  0  1007 GLU   A C   1 
ATOM   7465  O O   . GLU   A 1 1043 ? 140.095 158.575 118.806 1.00 42.42  0  1007 GLU   A O   1 
ATOM   7466  C CB  . GLU   A 1 1043 ? 141.484 155.613 119.125 1.00 21.18  0  1007 GLU   A CB  1 
ATOM   7467  C CG  . GLU   A 1 1043 ? 142.365 154.512 118.554 1.00 32.12  0  1007 GLU   A CG  1 
ATOM   7468  C CD  . GLU   A 1 1043 ? 142.458 154.532 117.038 1.00 36.64  0  1007 GLU   A CD  1 
ATOM   7469  O OE1 . GLU   A 1 1043 ? 141.551 155.083 116.380 1.00 36.34  0  1007 GLU   A OE1 1 
ATOM   7470  O OE2 . GLU   A 1 1043 ? 143.442 153.981 116.502 1.00 28.34  -1 1007 GLU   A OE2 1 
ATOM   7471  N N   . ALA   A 1 1044 ? 141.250 158.353 120.726 1.00 30.38  0  1008 ALA   A N   1 
ATOM   7472  C CA  . ALA   A 1 1044 ? 140.444 159.356 121.413 1.00 20.48  0  1008 ALA   A CA  1 
ATOM   7473  C C   . ALA   A 1 1044 ? 140.614 160.733 120.784 1.00 21.92  0  1008 ALA   A C   1 
ATOM   7474  O O   . ALA   A 1 1044 ? 139.636 161.464 120.598 1.00 19.35  0  1008 ALA   A O   1 
ATOM   7475  C CB  . ALA   A 1 1044 ? 140.809 159.395 122.894 1.00 16.95  0  1008 ALA   A CB  1 
ATOM   7476  N N   . ILE   A 1 1045 ? 141.848 161.103 120.442 1.00 22.27  0  1009 ILE   A N   1 
ATOM   7477  C CA  . ILE   A 1 1045 ? 142.083 162.423 119.865 1.00 24.21  0  1009 ILE   A CA  1 
ATOM   7478  C C   . ILE   A 1 1045 ? 141.470 162.520 118.474 1.00 34.10  0  1009 ILE   A C   1 
ATOM   7479  O O   . ILE   A 1 1045 ? 140.908 163.556 118.101 1.00 38.27  0  1009 ILE   A O   1 
ATOM   7480  C CB  . ILE   A 1 1045 ? 143.587 162.744 119.851 1.00 20.14  0  1009 ILE   A CB  1 
ATOM   7481  C CG1 . ILE   A 1 1045 ? 144.122 162.827 121.278 1.00 19.16  0  1009 ILE   A CG1 1 
ATOM   7482  C CG2 . ILE   A 1 1045 ? 143.842 164.055 119.146 1.00 21.25  0  1009 ILE   A CG2 1 
ATOM   7483  C CD1 . ILE   A 1 1045 ? 145.618 162.928 121.355 1.00 24.12  0  1009 ILE   A CD1 1 
ATOM   7484  N N   . VAL   A 1 1046 ? 141.554 161.447 117.685 1.00 27.27  0  1010 VAL   A N   1 
ATOM   7485  C CA  . VAL   A 1 1046 ? 140.935 161.460 116.362 1.00 25.56  0  1010 VAL   A CA  1 
ATOM   7486  C C   . VAL   A 1 1046 ? 139.416 161.507 116.482 1.00 31.46  0  1010 VAL   A C   1 
ATOM   7487  O O   . VAL   A 1 1046 ? 138.737 162.186 115.701 1.00 36.98  0  1010 VAL   A O   1 
ATOM   7488  C CB  . VAL   A 1 1046 ? 141.408 160.249 115.542 1.00 29.03  0  1010 VAL   A CB  1 
ATOM   7489  C CG1 . VAL   A 1 1046 ? 140.557 160.086 114.300 1.00 33.41  0  1010 VAL   A CG1 1 
ATOM   7490  C CG2 . VAL   A 1 1046 ? 142.865 160.411 115.169 1.00 33.06  0  1010 VAL   A CG2 1 
ATOM   7491  N N   . HIS   A 1 1047 ? 138.858 160.794 117.463 1.00 27.87  0  1011 HIS   A N   1 
ATOM   7492  C CA  . HIS   A 1 1047 ? 137.425 160.861 117.718 1.00 21.49  0  1011 HIS   A CA  1 
ATOM   7493  C C   . HIS   A 1 1047 ? 137.011 162.280 118.070 1.00 29.66  0  1011 HIS   A C   1 
ATOM   7494  O O   . HIS   A 1 1047 ? 135.992 162.780 117.587 1.00 36.48  0  1011 HIS   A O   1 
ATOM   7495  C CB  . HIS   A 1 1047 ? 137.057 159.894 118.845 1.00 25.94  0  1011 HIS   A CB  1 
ATOM   7496  C CG  . HIS   A 1 1047 ? 135.632 159.991 119.295 1.00 25.74  0  1011 HIS   A CG  1 
ATOM   7497  N ND1 . HIS   A 1 1047 ? 134.694 159.026 119.003 1.00 21.64  0  1011 HIS   A ND1 1 
ATOM   7498  C CD2 . HIS   A 1 1047 ? 134.989 160.928 120.030 1.00 21.90  0  1011 HIS   A CD2 1 
ATOM   7499  C CE1 . HIS   A 1 1047 ? 133.532 159.369 119.529 1.00 24.90  0  1011 HIS   A CE1 1 
ATOM   7500  N NE2 . HIS   A 1 1047 ? 133.684 160.520 120.156 1.00 29.06  0  1011 HIS   A NE2 1 
ATOM   7501  N N   . SER   A 1 1048 ? 137.797 162.945 118.918 1.00 30.05  0  1012 SER   A N   1 
ATOM   7502  C CA  . SER   A 1 1048 ? 137.496 164.324 119.286 1.00 27.86  0  1012 SER   A CA  1 
ATOM   7503  C C   . SER   A 1 1048 ? 137.579 165.248 118.080 1.00 31.17  0  1012 SER   A C   1 
ATOM   7504  O O   . SER   A 1 1048 ? 136.751 166.150 117.928 1.00 30.03  0  1012 SER   A O   1 
ATOM   7505  C CB  . SER   A 1 1048 ? 138.445 164.789 120.383 1.00 25.31  0  1012 SER   A CB  1 
ATOM   7506  O OG  . SER   A 1 1048 ? 138.301 163.994 121.543 1.00 30.36  0  1012 SER   A OG  1 
ATOM   7507  N N   . VAL   A 1 1049 ? 138.575 165.042 117.216 1.00 39.23  0  1013 VAL   A N   1 
ATOM   7508  C CA  . VAL   A 1 1049 ? 138.701 165.852 116.007 1.00 41.35  0  1013 VAL   A CA  1 
ATOM   7509  C C   . VAL   A 1 1049 ? 137.465 165.692 115.131 1.00 46.17  0  1013 VAL   A C   1 
ATOM   7510  O O   . VAL   A 1 1049 ? 136.867 166.675 114.674 1.00 47.01  0  1013 VAL   A O   1 
ATOM   7511  C CB  . VAL   A 1 1049 ? 139.981 165.469 115.244 1.00 26.56  0  1013 VAL   A CB  1 
ATOM   7512  C CG1 . VAL   A 1 1049 ? 139.965 166.056 113.848 1.00 34.02  0  1013 VAL   A CG1 1 
ATOM   7513  C CG2 . VAL   A 1 1049 ? 141.208 165.925 116.005 1.00 34.18  0  1013 VAL   A CG2 1 
ATOM   7514  N N   . PHE   A 1 1050 ? 137.053 164.443 114.905 1.00 36.50  0  1014 PHE   A N   1 
ATOM   7515  C CA  . PHE   A 1 1050 ? 135.888 164.183 114.067 1.00 28.61  0  1014 PHE   A CA  1 
ATOM   7516  C C   . PHE   A 1 1050 ? 134.623 164.763 114.685 1.00 39.03  0  1014 PHE   A C   1 
ATOM   7517  O O   . PHE   A 1 1050 ? 133.781 165.328 113.978 1.00 44.84  0  1014 PHE   A O   1 
ATOM   7518  C CB  . PHE   A 1 1050 ? 135.737 162.681 113.842 1.00 28.17  0  1014 PHE   A CB  1 
ATOM   7519  C CG  . PHE   A 1 1050 ? 136.734 162.110 112.876 1.00 38.04  0  1014 PHE   A CG  1 
ATOM   7520  C CD1 . PHE   A 1 1050 ? 137.476 162.938 112.056 1.00 42.71  0  1014 PHE   A CD1 1 
ATOM   7521  C CD2 . PHE   A 1 1050 ? 136.943 160.748 112.803 1.00 33.87  0  1014 PHE   A CD2 1 
ATOM   7522  C CE1 . PHE   A 1 1050 ? 138.392 162.417 111.173 1.00 37.84  0  1014 PHE   A CE1 1 
ATOM   7523  C CE2 . PHE   A 1 1050 ? 137.859 160.224 111.925 1.00 30.85  0  1014 PHE   A CE2 1 
ATOM   7524  C CZ  . PHE   A 1 1050 ? 138.584 161.059 111.109 1.00 35.25  0  1014 PHE   A CZ  1 
ATOM   7525  N N   . ILE   A 1 1051 ? 134.472 164.632 116.004 1.00 34.25  0  1015 ILE   A N   1 
ATOM   7526  C CA  . ILE   A 1 1051 ? 133.281 165.137 116.680 1.00 23.13  0  1015 ILE   A CA  1 
ATOM   7527  C C   . ILE   A 1 1051 ? 133.219 166.655 116.587 1.00 37.70  0  1015 ILE   A C   1 
ATOM   7528  O O   . ILE   A 1 1051 ? 132.182 167.231 116.244 1.00 42.30  0  1015 ILE   A O   1 
ATOM   7529  C CB  . ILE   A 1 1051 ? 133.257 164.661 118.143 1.00 32.34  0  1015 ILE   A CB  1 
ATOM   7530  C CG1 . ILE   A 1 1051 ? 132.952 163.164 118.211 1.00 26.36  0  1015 ILE   A CG1 1 
ATOM   7531  C CG2 . ILE   A 1 1051 ? 132.259 165.466 118.954 1.00 42.18  0  1015 ILE   A CG2 1 
ATOM   7532  C CD1 . ILE   A 1 1051 ? 131.795 162.736 117.353 1.00 24.97  0  1015 ILE   A CD1 1 
ATOM   7533  N N   . LEU   A 1 1052 ? 134.332 167.327 116.885 1.00 43.58  0  1016 LEU   A N   1 
ATOM   7534  C CA  . LEU   A 1 1052 ? 134.359 168.782 116.836 1.00 39.75  0  1016 LEU   A CA  1 
ATOM   7535  C C   . LEU   A 1 1052 ? 134.261 169.312 115.414 1.00 43.52  0  1016 LEU   A C   1 
ATOM   7536  O O   . LEU   A 1 1052 ? 133.929 170.488 115.228 1.00 48.09  0  1016 LEU   A O   1 
ATOM   7537  C CB  . LEU   A 1 1052 ? 135.626 169.300 117.510 1.00 37.69  0  1016 LEU   A CB  1 
ATOM   7538  C CG  . LEU   A 1 1052 ? 135.630 169.094 119.023 1.00 38.00  0  1016 LEU   A CG  1 
ATOM   7539  C CD1 . LEU   A 1 1052 ? 137.001 169.357 119.608 1.00 39.32  0  1016 LEU   A CD1 1 
ATOM   7540  C CD2 . LEU   A 1 1052 ? 134.589 169.983 119.671 1.00 40.88  0  1016 LEU   A CD2 1 
ATOM   7541  N N   . SER   A 1 1053 ? 134.543 168.479 114.410 1.00 39.64  0  1017 SER   A N   1 
ATOM   7542  C CA  . SER   A 1 1053 ? 134.262 168.878 113.037 1.00 43.87  0  1017 SER   A CA  1 
ATOM   7543  C C   . SER   A 1 1053 ? 132.775 169.109 112.802 1.00 44.57  0  1017 SER   A C   1 
ATOM   7544  O O   . SER   A 1 1053 ? 132.409 169.804 111.849 1.00 44.51  0  1017 SER   A O   1 
ATOM   7545  C CB  . SER   A 1 1053 ? 134.785 167.823 112.064 1.00 44.32  0  1017 SER   A CB  1 
ATOM   7546  O OG  . SER   A 1 1053 ? 133.973 166.664 112.090 1.00 43.07  0  1017 SER   A OG  1 
ATOM   7547  N N   . TYR   A 1 1054 ? 131.914 168.535 113.645 1.00 40.35  0  1018 TYR   A N   1 
ATOM   7548  C CA  . TYR   A 1 1054 ? 130.482 168.790 113.534 1.00 36.99  0  1018 TYR   A CA  1 
ATOM   7549  C C   . TYR   A 1 1054 ? 130.173 170.260 113.781 1.00 38.19  0  1018 TYR   A C   1 
ATOM   7550  O O   . TYR   A 1 1054 ? 129.359 170.862 113.072 1.00 43.54  0  1018 TYR   A O   1 
ATOM   7551  C CB  . TYR   A 1 1054 ? 129.723 167.912 114.530 1.00 41.35  0  1018 TYR   A CB  1 
ATOM   7552  C CG  . TYR   A 1 1054 ? 128.220 168.066 114.512 1.00 42.70  0  1018 TYR   A CG  1 
ATOM   7553  C CD1 . TYR   A 1 1054 ? 127.545 168.375 113.343 1.00 40.16  0  1018 TYR   A CD1 1 
ATOM   7554  C CD2 . TYR   A 1 1054 ? 127.479 167.925 115.673 1.00 42.86  0  1018 TYR   A CD2 1 
ATOM   7555  C CE1 . TYR   A 1 1054 ? 126.179 168.513 113.329 1.00 35.91  0  1018 TYR   A CE1 1 
ATOM   7556  C CE2 . TYR   A 1 1054 ? 126.114 168.070 115.668 1.00 43.72  0  1018 TYR   A CE2 1 
ATOM   7557  C CZ  . TYR   A 1 1054 ? 125.469 168.365 114.493 1.00 42.89  0  1018 TYR   A CZ  1 
ATOM   7558  O OH  . TYR   A 1 1054 ? 124.105 168.510 114.482 1.00 50.50  0  1018 TYR   A OH  1 
ATOM   7559  N N   . TYR   A 1 1055 ? 130.819 170.854 114.783 1.00 43.26  0  1019 TYR   A N   1 
ATOM   7560  C CA  . TYR   A 1 1055 ? 130.569 172.241 115.148 1.00 50.08  0  1019 TYR   A CA  1 
ATOM   7561  C C   . TYR   A 1 1055 ? 131.442 173.224 114.384 1.00 54.34  0  1019 TYR   A C   1 
ATOM   7562  O O   . TYR   A 1 1055 ? 131.011 174.355 114.135 1.00 52.95  0  1019 TYR   A O   1 
ATOM   7563  C CB  . TYR   A 1 1055 ? 130.788 172.434 116.648 1.00 46.10  0  1019 TYR   A CB  1 
ATOM   7564  C CG  . TYR   A 1 1055 ? 129.879 171.591 117.506 1.00 48.72  0  1019 TYR   A CG  1 
ATOM   7565  C CD1 . TYR   A 1 1055 ? 128.558 171.952 117.709 1.00 50.41  0  1019 TYR   A CD1 1 
ATOM   7566  C CD2 . TYR   A 1 1055 ? 130.342 170.437 118.113 1.00 50.03  0  1019 TYR   A CD2 1 
ATOM   7567  C CE1 . TYR   A 1 1055 ? 127.724 171.186 118.492 1.00 52.05  0  1019 TYR   A CE1 1 
ATOM   7568  C CE2 . TYR   A 1 1055 ? 129.515 169.665 118.898 1.00 48.12  0  1019 TYR   A CE2 1 
ATOM   7569  C CZ  . TYR   A 1 1055 ? 128.208 170.046 119.084 1.00 48.60  0  1019 TYR   A CZ  1 
ATOM   7570  O OH  . TYR   A 1 1055 ? 127.379 169.281 119.866 1.00 48.30  0  1019 TYR   A OH  1 
ATOM   7571  N N   . THR   A 1 1056 ? 132.655 172.826 114.006 1.00 57.44  0  1020 THR   A N   1 
ATOM   7572  C CA  . THR   A 1 1056 ? 133.575 173.731 113.332 1.00 55.42  0  1020 THR   A CA  1 
ATOM   7573  C C   . THR   A 1 1056 ? 133.393 173.770 111.822 1.00 56.07  0  1020 THR   A C   1 
ATOM   7574  O O   . THR   A 1 1056 ? 134.079 174.553 111.158 1.00 61.99  0  1020 THR   A O   1 
ATOM   7575  C CB  . THR   A 1 1056 ? 135.023 173.350 113.648 1.00 59.73  0  1020 THR   A CB  1 
ATOM   7576  O OG1 . THR   A 1 1056 ? 135.291 172.035 113.149 1.00 57.74  0  1020 THR   A OG1 1 
ATOM   7577  C CG2 . THR   A 1 1056 ? 135.266 173.378 115.143 1.00 57.03  0  1020 THR   A CG2 1 
ATOM   7578  N N   . ASN   A 1 1057 ? 132.493 172.956 111.269 1.00 56.20  0  1021 ASN   A N   1 
ATOM   7579  C CA  . ASN   A 1 1057 ? 132.249 172.903 109.824 1.00 60.91  0  1021 ASN   A CA  1 
ATOM   7580  C C   . ASN   A 1 1057 ? 133.531 172.599 109.050 1.00 59.64  0  1021 ASN   A C   1 
ATOM   7581  O O   . ASN   A 1 1057 ? 133.799 173.188 108.002 1.00 56.75  0  1021 ASN   A O   1 
ATOM   7582  C CB  . ASN   A 1 1057 ? 131.612 174.201 109.321 1.00 61.39  0  1021 ASN   A CB  1 
ATOM   7583  C CG  . ASN   A 1 1057 ? 130.476 174.676 110.204 1.00 63.36  0  1021 ASN   A CG  1 
ATOM   7584  O OD1 . ASN   A 1 1057 ? 129.338 174.224 110.071 1.00 61.19  0  1021 ASN   A OD1 1 
ATOM   7585  N ND2 . ASN   A 1 1057 ? 130.779 175.597 111.113 1.00 58.36  0  1021 ASN   A ND2 1 
ATOM   7586  N N   . HIS   A 1 1058 ? 134.327 171.668 109.568 1.00 61.32  0  1022 HIS   A N   1 
ATOM   7587  C CA  . HIS   A 1 1058 ? 135.574 171.272 108.930 1.00 61.77  0  1022 HIS   A CA  1 
ATOM   7588  C C   . HIS   A 1 1058 ? 135.352 170.047 108.054 1.00 64.48  0  1022 HIS   A C   1 
ATOM   7589  O O   . HIS   A 1 1058 ? 134.692 169.088 108.463 1.00 64.82  0  1022 HIS   A O   1 
ATOM   7590  C CB  . HIS   A 1 1058 ? 136.647 170.967 109.976 1.00 62.31  0  1022 HIS   A CB  1 
ATOM   7591  C CG  . HIS   A 1 1058 ? 137.435 172.165 110.407 1.00 66.13  0  1022 HIS   A CG  1 
ATOM   7592  N ND1 . HIS   A 1 1058 ? 137.901 173.110 109.519 1.00 67.55  0  1022 HIS   A ND1 1 
ATOM   7593  C CD2 . HIS   A 1 1058 ? 137.847 172.565 111.633 1.00 65.61  0  1022 HIS   A CD2 1 
ATOM   7594  C CE1 . HIS   A 1 1058 ? 138.561 174.044 110.180 1.00 66.35  0  1022 HIS   A CE1 1 
ATOM   7595  N NE2 . HIS   A 1 1058 ? 138.543 173.738 111.465 1.00 66.39  0  1022 HIS   A NE2 1 
ATOM   7596  N N   . ASP   A 1 1059 ? 135.906 170.085 106.846 1.00 65.11  0  1023 ASP   A N   1 
ATOM   7597  C CA  . ASP   A 1 1059 ? 135.836 168.942 105.948 1.00 65.96  0  1023 ASP   A CA  1 
ATOM   7598  C C   . ASP   A 1 1059 ? 136.833 167.874 106.380 1.00 65.95  0  1023 ASP   A C   1 
ATOM   7599  O O   . ASP   A 1 1059 ? 137.996 168.168 106.669 1.00 67.11  0  1023 ASP   A O   1 
ATOM   7600  C CB  . ASP   A 1 1059 ? 136.115 169.372 104.509 1.00 67.66  0  1023 ASP   A CB  1 
ATOM   7601  C CG  . ASP   A 1 1059 ? 135.586 168.380 103.490 1.00 67.06  0  1023 ASP   A CG  1 
ATOM   7602  O OD1 . ASP   A 1 1059 ? 135.228 167.251 103.887 1.00 63.83  0  1023 ASP   A OD1 1 
ATOM   7603  O OD2 . ASP   A 1 1059 ? 135.528 168.727 102.292 1.00 67.42  -1 1023 ASP   A OD2 1 
ATOM   7604  N N   . LEU   A 1 1060 ? 136.368 166.626 106.424 1.00 59.89  0  1024 LEU   A N   1 
ATOM   7605  C CA  . LEU   A 1 1060 ? 137.184 165.511 106.881 1.00 61.35  0  1024 LEU   A CA  1 
ATOM   7606  C C   . LEU   A 1 1060 ? 137.821 164.718 105.751 1.00 59.33  0  1024 LEU   A C   1 
ATOM   7607  O O   . LEU   A 1 1060 ? 138.604 163.804 106.027 1.00 59.03  0  1024 LEU   A O   1 
ATOM   7608  C CB  . LEU   A 1 1060 ? 136.345 164.566 107.751 1.00 60.71  0  1024 LEU   A CB  1 
ATOM   7609  C CG  . LEU   A 1 1060 ? 135.804 165.184 109.039 1.00 58.32  0  1024 LEU   A CG  1 
ATOM   7610  C CD1 . LEU   A 1 1060 ? 135.070 164.145 109.866 1.00 51.77  0  1024 LEU   A CD1 1 
ATOM   7611  C CD2 . LEU   A 1 1060 ? 136.939 165.806 109.831 1.00 57.20  0  1024 LEU   A CD2 1 
ATOM   7612  N N   . LYS   A 1 1061 ? 137.507 165.032 104.498 1.00 64.30  0  1025 LYS   A N   1 
ATOM   7613  C CA  . LYS   A 1 1061 ? 138.135 164.374 103.361 1.00 66.55  0  1025 LYS   A CA  1 
ATOM   7614  C C   . LYS   A 1 1061 ? 139.410 165.071 102.910 1.00 70.11  0  1025 LYS   A C   1 
ATOM   7615  O O   . LYS   A 1 1061 ? 140.057 164.599 101.969 1.00 68.46  0  1025 LYS   A O   1 
ATOM   7616  C CB  . LYS   A 1 1061 ? 137.155 164.297 102.189 1.00 66.09  0  1025 LYS   A CB  1 
ATOM   7617  C CG  . LYS   A 1 1061 ? 135.890 163.514 102.480 1.00 66.07  0  1025 LYS   A CG  1 
ATOM   7618  C CD  . LYS   A 1 1061 ? 134.913 163.618 101.323 1.00 68.75  0  1025 LYS   A CD  1 
ATOM   7619  C CE  . LYS   A 1 1061 ? 134.323 165.013 101.228 1.00 65.71  0  1025 LYS   A CE  1 
ATOM   7620  N NZ  . LYS   A 1 1061 ? 133.272 165.102 100.178 1.00 67.42  1  1025 LYS   A NZ  1 
ATOM   7621  N N   . ASP   A 1 1062 ? 139.782 166.170 103.553 1.00 83.47  0  1026 ASP   A N   1 
ATOM   7622  C CA  . ASP   A 1 1062 ? 140.935 166.967 103.167 1.00 86.27  0  1026 ASP   A CA  1 
ATOM   7623  C C   . ASP   A 1 1062 ? 141.941 166.998 104.319 1.00 85.67  0  1026 ASP   A C   1 
ATOM   7624  O O   . ASP   A 1 1062 ? 141.790 166.302 105.326 1.00 86.10  0  1026 ASP   A O   1 
ATOM   7625  C CB  . ASP   A 1 1062 ? 140.491 168.373 102.756 1.00 83.78  0  1026 ASP   A CB  1 
ATOM   7626  C CG  . ASP   A 1 1062 ? 141.412 168.998 101.729 1.00 87.99  0  1026 ASP   A CG  1 
ATOM   7627  O OD1 . ASP   A 1 1062 ? 142.343 168.306 101.265 1.00 86.36  0  1026 ASP   A OD1 1 
ATOM   7628  O OD2 . ASP   A 1 1062 ? 141.208 170.181 101.388 1.00 89.63  -1 1026 ASP   A OD2 1 
ATOM   7629  N N   . LYS   A 1 1063 ? 142.976 167.815 104.158 1.00 85.80  0  1027 LYS   A N   1 
ATOM   7630  C CA  . LYS   A 1 1063 ? 144.028 167.942 105.152 1.00 87.05  0  1027 LYS   A CA  1 
ATOM   7631  C C   . LYS   A 1 1063 ? 143.559 168.796 106.329 1.00 91.60  0  1027 LYS   A C   1 
ATOM   7632  O O   . LYS   A 1 1063 ? 142.486 169.405 106.307 1.00 88.42  0  1027 LYS   A O   1 
ATOM   7633  C CB  . LYS   A 1 1063 ? 145.278 168.554 104.524 1.00 85.98  0  1027 LYS   A CB  1 
ATOM   7634  C CG  . LYS   A 1 1063 ? 145.078 169.989 104.073 1.00 87.46  0  1027 LYS   A CG  1 
ATOM   7635  C CD  . LYS   A 1 1063 ? 146.320 170.556 103.416 1.00 86.05  0  1027 LYS   A CD  1 
ATOM   7636  C CE  . LYS   A 1 1063 ? 146.125 172.023 103.069 1.00 85.63  0  1027 LYS   A CE  1 
ATOM   7637  N NZ  . LYS   A 1 1063 ? 147.320 172.604 102.400 1.00 88.85  1  1027 LYS   A NZ  1 
ATOM   7638  N N   . LEU   A 1 1064 ? 144.384 168.831 107.374 1.00 88.00  0  1028 LEU   A N   1 
ATOM   7639  C CA  . LEU   A 1 1064 ? 144.138 169.718 108.502 1.00 82.62  0  1028 LEU   A CA  1 
ATOM   7640  C C   . LEU   A 1 1064 ? 144.738 171.087 108.220 1.00 83.63  0  1028 LEU   A C   1 
ATOM   7641  O O   . LEU   A 1 1064 ? 145.922 171.199 107.889 1.00 84.90  0  1028 LEU   A O   1 
ATOM   7642  C CB  . LEU   A 1 1064 ? 144.728 169.143 109.789 1.00 83.68  0  1028 LEU   A CB  1 
ATOM   7643  C CG  . LEU   A 1 1064 ? 143.757 168.406 110.711 1.00 86.09  0  1028 LEU   A CG  1 
ATOM   7644  C CD1 . LEU   A 1 1064 ? 144.368 168.212 112.092 1.00 83.60  0  1028 LEU   A CD1 1 
ATOM   7645  C CD2 . LEU   A 1 1064 ? 142.429 169.142 110.801 1.00 83.14  0  1028 LEU   A CD2 1 
ATOM   7646  N N   . GLN   A 1 1065 ? 143.920 172.127 108.356 1.00 89.79  0  1029 GLN   A N   1 
ATOM   7647  C CA  . GLN   A 1 1065 ? 144.359 173.491 108.106 1.00 92.19  0  1029 GLN   A CA  1 
ATOM   7648  C C   . GLN   A 1 1065 ? 143.697 174.425 109.107 1.00 90.26  0  1029 GLN   A C   1 
ATOM   7649  O O   . GLN   A 1 1065 ? 142.695 174.084 109.741 1.00 88.34  0  1029 GLN   A O   1 
ATOM   7650  C CB  . GLN   A 1 1065 ? 144.043 173.932 106.671 1.00 92.87  0  1029 GLN   A CB  1 
ATOM   7651  C CG  . GLN   A 1 1065 ? 142.607 173.690 106.248 1.00 91.07  0  1029 GLN   A CG  1 
ATOM   7652  C CD  . GLN   A 1 1065 ? 142.401 173.892 104.761 1.00 93.17  0  1029 GLN   A CD  1 
ATOM   7653  O OE1 . GLN   A 1 1065 ? 142.082 174.992 104.312 1.00 93.09  0  1029 GLN   A OE1 1 
ATOM   7654  N NE2 . GLN   A 1 1065 ? 142.582 172.828 103.988 1.00 90.36  0  1029 GLN   A NE2 1 
ATOM   7655  N N   . ASP   A 1 1066 ? 144.281 175.612 109.247 1.00 86.74  0  1030 ASP   A N   1 
ATOM   7656  C CA  . ASP   A 1 1066 ? 143.758 176.635 110.147 1.00 89.70  0  1030 ASP   A CA  1 
ATOM   7657  C C   . ASP   A 1 1066 ? 142.694 177.442 109.415 1.00 88.37  0  1030 ASP   A C   1 
ATOM   7658  O O   . ASP   A 1 1066 ? 142.990 178.122 108.427 1.00 87.22  0  1030 ASP   A O   1 
ATOM   7659  C CB  . ASP   A 1 1066 ? 144.884 177.537 110.642 1.00 86.99  0  1030 ASP   A CB  1 
ATOM   7660  C CG  . ASP   A 1 1066 ? 145.542 177.014 111.902 1.00 85.33  0  1030 ASP   A CG  1 
ATOM   7661  O OD1 . ASP   A 1 1066 ? 144.829 176.446 112.754 1.00 90.76  0  1030 ASP   A OD1 1 
ATOM   7662  O OD2 . ASP   A 1 1066 ? 146.771 177.173 112.044 1.00 81.20  -1 1030 ASP   A OD2 1 
ATOM   7663  N N   . LEU   A 1 1067 ? 141.457 177.368 109.892 1.00 86.92  0  1031 LEU   A N   1 
ATOM   7664  C CA  . LEU   A 1 1067 ? 140.357 178.153 109.355 1.00 87.82  0  1031 LEU   A CA  1 
ATOM   7665  C C   . LEU   A 1 1067 ? 139.802 179.070 110.441 1.00 86.13  0  1031 LEU   A C   1 
ATOM   7666  O O   . LEU   A 1 1067 ? 140.339 179.157 111.549 1.00 84.94  0  1031 LEU   A O   1 
ATOM   7667  C CB  . LEU   A 1 1067 ? 139.273 177.242 108.775 1.00 86.61  0  1031 LEU   A CB  1 
ATOM   7668  C CG  . LEU   A 1 1067 ? 139.727 176.340 107.624 1.00 87.29  0  1031 LEU   A CG  1 
ATOM   7669  C CD1 . LEU   A 1 1067 ? 138.584 175.470 107.126 1.00 86.68  0  1031 LEU   A CD1 1 
ATOM   7670  C CD2 . LEU   A 1 1067 ? 140.315 177.162 106.487 1.00 83.73  0  1031 LEU   A CD2 1 
ATOM   7671  N N   . SER   A 1 1068 ? 138.711 179.764 110.105 1.00 86.76  0  1032 SER   A N   1 
ATOM   7672  C CA  . SER   A 1 1068 ? 138.179 180.794 110.994 1.00 87.93  0  1032 SER   A CA  1 
ATOM   7673  C C   . SER   A 1 1068 ? 137.726 180.220 112.331 1.00 88.85  0  1032 SER   A C   1 
ATOM   7674  O O   . SER   A 1 1068 ? 137.997 180.813 113.381 1.00 84.49  0  1032 SER   A O   1 
ATOM   7675  C CB  . SER   A 1 1068 ? 137.025 181.528 110.313 1.00 85.85  0  1032 SER   A CB  1 
ATOM   7676  O OG  . SER   A 1 1068 ? 135.941 180.651 110.062 1.00 87.97  0  1032 SER   A OG  1 
ATOM   7677  N N   . ASP   A 1 1069 ? 137.043 179.079 112.319 1.00 83.55  0  1033 ASP   A N   1 
ATOM   7678  C CA  . ASP   A 1 1069 ? 136.551 178.456 113.543 1.00 78.20  0  1033 ASP   A CA  1 
ATOM   7679  C C   . ASP   A 1 1069 ? 137.697 177.683 114.187 1.00 79.64  0  1033 ASP   A C   1 
ATOM   7680  O O   . ASP   A 1 1069 ? 138.167 176.682 113.636 1.00 82.06  0  1033 ASP   A O   1 
ATOM   7681  C CB  . ASP   A 1 1069 ? 135.366 177.543 113.247 1.00 77.38  0  1033 ASP   A CB  1 
ATOM   7682  C CG  . ASP   A 1 1069 ? 134.439 177.392 114.433 1.00 79.60  0  1033 ASP   A CG  1 
ATOM   7683  O OD1 . ASP   A 1 1069 ? 134.882 177.643 115.573 1.00 78.04  0  1033 ASP   A OD1 1 
ATOM   7684  O OD2 . ASP   A 1 1069 ? 133.266 177.020 114.228 1.00 82.12  -1 1033 ASP   A OD2 1 
ATOM   7685  N N   . ASP   A 1 1070 ? 138.142 178.142 115.355 1.00 69.17  0  1034 ASP   A N   1 
ATOM   7686  C CA  . ASP   A 1 1070 ? 139.305 177.578 116.026 1.00 67.61  0  1034 ASP   A CA  1 
ATOM   7687  C C   . ASP   A 1 1070 ? 138.934 176.813 117.292 1.00 69.03  0  1034 ASP   A C   1 
ATOM   7688  O O   . ASP   A 1 1070 ? 139.715 176.765 118.243 1.00 69.75  0  1034 ASP   A O   1 
ATOM   7689  C CB  . ASP   A 1 1070 ? 140.314 178.677 116.350 1.00 71.66  0  1034 ASP   A CB  1 
ATOM   7690  C CG  . ASP   A 1 1070 ? 139.674 179.869 117.024 1.00 74.94  0  1034 ASP   A CG  1 
ATOM   7691  O OD1 . ASP   A 1 1070 ? 138.428 179.933 117.057 1.00 72.56  0  1034 ASP   A OD1 1 
ATOM   7692  O OD2 . ASP   A 1 1070 ? 140.416 180.741 117.523 1.00 75.13  -1 1034 ASP   A OD2 1 
ATOM   7693  N N   . ARG   A 1 1071 ? 137.741 176.216 117.323 1.00 63.23  0  1035 ARG   A N   1 
ATOM   7694  C CA  . ARG   A 1 1071 ? 137.378 175.366 118.452 1.00 60.67  0  1035 ARG   A CA  1 
ATOM   7695  C C   . ARG   A 1 1071 ? 138.302 174.159 118.540 1.00 61.82  0  1035 ARG   A C   1 
ATOM   7696  O O   . ARG   A 1 1071 ? 138.762 173.793 119.629 1.00 55.21  0  1035 ARG   A O   1 
ATOM   7697  C CB  . ARG   A 1 1071 ? 135.926 174.915 118.319 1.00 60.26  0  1035 ARG   A CB  1 
ATOM   7698  C CG  . ARG   A 1 1071 ? 134.944 175.717 119.140 1.00 59.45  0  1035 ARG   A CG  1 
ATOM   7699  C CD  . ARG   A 1 1071 ? 133.534 175.535 118.612 1.00 63.25  0  1035 ARG   A CD  1 
ATOM   7700  N NE  . ARG   A 1 1071 ? 133.215 176.495 117.564 1.00 62.68  0  1035 ARG   A NE  1 
ATOM   7701  C CZ  . ARG   A 1 1071 ? 131.984 176.808 117.188 1.00 61.41  0  1035 ARG   A CZ  1 
ATOM   7702  N NH1 . ARG   A 1 1071 ? 130.926 176.262 117.764 1.00 59.12  1  1035 ARG   A NH1 1 
ATOM   7703  N NH2 . ARG   A 1 1071 ? 131.808 177.693 116.213 1.00 62.42  0  1035 ARG   A NH2 1 
ATOM   7704  N N   . LEU   A 1 1072 ? 138.584 173.531 117.398 1.00 58.85  0  1036 LEU   A N   1 
ATOM   7705  C CA  . LEU   A 1 1072 ? 139.511 172.406 117.374 1.00 55.00  0  1036 LEU   A CA  1 
ATOM   7706  C C   . LEU   A 1 1072 ? 140.921 172.846 117.742 1.00 62.28  0  1036 LEU   A C   1 
ATOM   7707  O O   . LEU   A 1 1072 ? 141.641 172.120 118.436 1.00 64.99  0  1036 LEU   A O   1 
ATOM   7708  C CB  . LEU   A 1 1072 ? 139.488 171.749 115.996 1.00 54.98  0  1036 LEU   A CB  1 
ATOM   7709  C CG  . LEU   A 1 1072 ? 140.164 170.388 115.856 1.00 57.09  0  1036 LEU   A CG  1 
ATOM   7710  C CD1 . LEU   A 1 1072 ? 139.815 169.493 117.024 1.00 57.86  0  1036 LEU   A CD1 1 
ATOM   7711  C CD2 . LEU   A 1 1072 ? 139.739 169.748 114.552 1.00 58.02  0  1036 LEU   A CD2 1 
ATOM   7712  N N   . ASN   A 1 1073 ? 141.334 174.029 117.281 1.00 64.28  0  1037 ASN   A N   1 
ATOM   7713  C CA  . ASN   A 1 1073 ? 142.644 174.553 117.653 1.00 59.31  0  1037 ASN   A CA  1 
ATOM   7714  C C   . ASN   A 1 1073 ? 142.749 174.757 119.156 1.00 55.97  0  1037 ASN   A C   1 
ATOM   7715  O O   . ASN   A 1 1073 ? 143.756 174.389 119.770 1.00 55.80  0  1037 ASN   A O   1 
ATOM   7716  C CB  . ASN   A 1 1073 ? 142.909 175.865 116.922 1.00 60.37  0  1037 ASN   A CB  1 
ATOM   7717  C CG  . ASN   A 1 1073 ? 143.472 175.653 115.542 1.00 66.35  0  1037 ASN   A CG  1 
ATOM   7718  O OD1 . ASN   A 1 1073 ? 144.410 174.883 115.361 1.00 67.09  0  1037 ASN   A OD1 1 
ATOM   7719  N ND2 . ASN   A 1 1073 ? 142.900 176.332 114.556 1.00 68.06  0  1037 ASN   A ND2 1 
ATOM   7720  N N   . LYS   A 1 1074 ? 141.716 175.342 119.766 1.00 46.80  0  1038 LYS   A N   1 
ATOM   7721  C CA  . LYS   A 1 1074 ? 141.725 175.540 121.210 1.00 50.53  0  1038 LYS   A CA  1 
ATOM   7722  C C   . LYS   A 1 1074 ? 141.728 174.209 121.948 1.00 50.58  0  1038 LYS   A C   1 
ATOM   7723  O O   . LYS   A 1 1074 ? 142.423 174.054 122.960 1.00 52.74  0  1038 LYS   A O   1 
ATOM   7724  C CB  . LYS   A 1 1074 ? 140.525 176.387 121.631 1.00 49.34  0  1038 LYS   A CB  1 
ATOM   7725  C CG  . LYS   A 1 1074 ? 140.574 177.819 121.123 1.00 52.22  0  1038 LYS   A CG  1 
ATOM   7726  C CD  . LYS   A 1 1074 ? 139.317 178.602 121.481 1.00 50.86  0  1038 LYS   A CD  1 
ATOM   7727  C CE  . LYS   A 1 1074 ? 138.727 178.160 122.808 1.00 51.13  0  1038 LYS   A CE  1 
ATOM   7728  N NZ  . LYS   A 1 1074 ? 137.538 178.971 123.175 1.00 49.67  1  1038 LYS   A NZ  1 
ATOM   7729  N N   . PHE   A 1 1075 ? 140.960 173.234 121.458 1.00 45.34  0  1039 PHE   A N   1 
ATOM   7730  C CA  . PHE   A 1 1075 ? 140.946 171.920 122.091 1.00 46.28  0  1039 PHE   A CA  1 
ATOM   7731  C C   . PHE   A 1 1075 ? 142.325 171.271 122.042 1.00 46.19  0  1039 PHE   A C   1 
ATOM   7732  O O   . PHE   A 1 1075 ? 142.823 170.765 123.054 1.00 43.98  0  1039 PHE   A O   1 
ATOM   7733  C CB  . PHE   A 1 1075 ? 139.905 171.026 121.418 1.00 41.77  0  1039 PHE   A CB  1 
ATOM   7734  C CG  . PHE   A 1 1075 ? 139.928 169.609 121.901 1.00 38.67  0  1039 PHE   A CG  1 
ATOM   7735  C CD1 . PHE   A 1 1075 ? 139.411 169.278 123.138 1.00 39.29  0  1039 PHE   A CD1 1 
ATOM   7736  C CD2 . PHE   A 1 1075 ? 140.470 168.608 121.120 1.00 42.45  0  1039 PHE   A CD2 1 
ATOM   7737  C CE1 . PHE   A 1 1075 ? 139.435 167.978 123.587 1.00 37.95  0  1039 PHE   A CE1 1 
ATOM   7738  C CE2 . PHE   A 1 1075 ? 140.500 167.309 121.564 1.00 43.55  0  1039 PHE   A CE2 1 
ATOM   7739  C CZ  . PHE   A 1 1075 ? 139.981 166.993 122.799 1.00 41.02  0  1039 PHE   A CZ  1 
ATOM   7740  N N   . LEU   A 1 1076 ? 142.965 171.292 120.871 1.00 50.58  0  1040 LEU   A N   1 
ATOM   7741  C CA  . LEU   A 1 1076 ? 144.284 170.681 120.738 1.00 45.42  0  1040 LEU   A CA  1 
ATOM   7742  C C   . LEU   A 1 1076 ? 145.320 171.413 121.580 1.00 54.38  0  1040 LEU   A C   1 
ATOM   7743  O O   . LEU   A 1 1076 ? 146.190 170.781 122.193 1.00 57.12  0  1040 LEU   A O   1 
ATOM   7744  C CB  . LEU   A 1 1076 ? 144.702 170.653 119.270 1.00 42.00  0  1040 LEU   A CB  1 
ATOM   7745  C CG  . LEU   A 1 1076 ? 143.864 169.769 118.346 1.00 43.71  0  1040 LEU   A CG  1 
ATOM   7746  C CD1 . LEU   A 1 1076 ? 144.420 169.794 116.936 1.00 48.22  0  1040 LEU   A CD1 1 
ATOM   7747  C CD2 . LEU   A 1 1076 ? 143.801 168.349 118.869 1.00 48.27  0  1040 LEU   A CD2 1 
ATOM   7748  N N   . THR   A 1 1077 ? 145.247 172.746 121.623 1.00 51.72  0  1041 THR   A N   1 
ATOM   7749  C CA  . THR   A 1 1077 ? 146.174 173.510 122.448 1.00 43.44  0  1041 THR   A CA  1 
ATOM   7750  C C   . THR   A 1 1077 ? 146.010 173.166 123.920 1.00 47.02  0  1041 THR   A C   1 
ATOM   7751  O O   . THR   A 1 1077 ? 146.999 172.957 124.628 1.00 49.83  0  1041 THR   A O   1 
ATOM   7752  C CB  . THR   A 1 1077 ? 145.963 175.005 122.227 1.00 50.13  0  1041 THR   A CB  1 
ATOM   7753  O OG1 . THR   A 1 1077 ? 146.242 175.329 120.861 1.00 55.59  0  1041 THR   A OG1 1 
ATOM   7754  C CG2 . THR   A 1 1077 ? 146.878 175.806 123.128 1.00 53.35  0  1041 THR   A CG2 1 
ATOM   7755  N N   . CYS   A 1 1078 ? 144.767 173.088 124.399 1.00 40.57  0  1042 CYS   A N   1 
ATOM   7756  C CA  . CYS   A 1 1078 ? 144.540 172.677 125.778 1.00 41.06  0  1042 CYS   A CA  1 
ATOM   7757  C C   . CYS   A 1 1078 ? 144.975 171.241 126.022 1.00 42.56  0  1042 CYS   A C   1 
ATOM   7758  O O   . CYS   A 1 1078 ? 145.303 170.888 127.159 1.00 37.66  0  1042 CYS   A O   1 
ATOM   7759  C CB  . CYS   A 1 1078 ? 143.069 172.844 126.142 1.00 41.95  0  1042 CYS   A CB  1 
ATOM   7760  S SG  . CYS   A 1 1078 ? 142.514 174.551 126.162 1.00 65.11  0  1042 CYS   A SG  1 
ATOM   7761  N N   . ILE   A 1 1079 ? 144.965 170.406 124.983 1.00 46.67  0  1043 ILE   A N   1 
ATOM   7762  C CA  . ILE   A 1 1079 ? 145.449 169.037 125.123 1.00 45.22  0  1043 ILE   A CA  1 
ATOM   7763  C C   . ILE   A 1 1079 ? 146.961 169.020 125.319 1.00 43.49  0  1043 ILE   A C   1 
ATOM   7764  O O   . ILE   A 1 1079 ? 147.477 168.344 126.217 1.00 45.62  0  1043 ILE   A O   1 
ATOM   7765  C CB  . ILE   A 1 1079 ? 145.023 168.193 123.908 1.00 43.55  0  1043 ILE   A CB  1 
ATOM   7766  C CG1 . ILE   A 1 1079 ? 143.584 167.709 124.076 1.00 44.52  0  1043 ILE   A CG1 1 
ATOM   7767  C CG2 . ILE   A 1 1079 ? 145.949 167.013 123.717 1.00 41.52  0  1043 ILE   A CG2 1 
ATOM   7768  C CD1 . ILE   A 1 1079 ? 143.395 166.781 125.248 1.00 34.89  0  1043 ILE   A CD1 1 
ATOM   7769  N N   . ILE   A 1 1080 ? 147.693 169.773 124.499 1.00 39.55  0  1044 ILE   A N   1 
ATOM   7770  C CA  . ILE   A 1 1080 ? 149.147 169.639 124.493 1.00 39.41  0  1044 ILE   A CA  1 
ATOM   7771  C C   . ILE   A 1 1080 ? 149.840 170.560 125.498 1.00 42.99  0  1044 ILE   A C   1 
ATOM   7772  O O   . ILE   A 1 1080 ? 150.923 170.224 125.987 1.00 46.51  0  1044 ILE   A O   1 
ATOM   7773  C CB  . ILE   A 1 1080 ? 149.706 169.856 123.077 1.00 39.31  0  1044 ILE   A CB  1 
ATOM   7774  C CG1 . ILE   A 1 1080 ? 149.697 171.335 122.706 1.00 41.39  0  1044 ILE   A CG1 1 
ATOM   7775  C CG2 . ILE   A 1 1080 ? 148.917 169.054 122.069 1.00 39.76  0  1044 ILE   A CG2 1 
ATOM   7776  C CD1 . ILE   A 1 1080 ? 150.680 171.690 121.622 1.00 42.49  0  1044 ILE   A CD1 1 
ATOM   7777  N N   . THR   A 1 1081 ? 149.256 171.711 125.826 1.00 43.58  0  1045 THR   A N   1 
ATOM   7778  C CA  . THR   A 1 1081 ? 149.837 172.627 126.804 1.00 42.29  0  1045 THR   A CA  1 
ATOM   7779  C C   . THR   A 1 1081 ? 149.163 172.406 128.151 1.00 41.10  0  1045 THR   A C   1 
ATOM   7780  O O   . THR   A 1 1081 ? 147.994 172.757 128.336 1.00 42.90  0  1045 THR   A O   1 
ATOM   7781  C CB  . THR   A 1 1081 ? 149.700 174.084 126.367 1.00 41.94  0  1045 THR   A CB  1 
ATOM   7782  O OG1 . THR   A 1 1081 ? 148.449 174.609 126.827 1.00 42.96  0  1045 THR   A OG1 1 
ATOM   7783  C CG2 . THR   A 1 1081 ? 149.804 174.220 124.862 1.00 47.52  0  1045 THR   A CG2 1 
ATOM   7784  N N   . PHE   A 1 1082 ? 149.905 171.828 129.090 1.00 40.43  0  1046 PHE   A N   1 
ATOM   7785  C CA  . PHE   A 1 1082 ? 149.408 171.622 130.439 1.00 42.19  0  1046 PHE   A CA  1 
ATOM   7786  C C   . PHE   A 1 1082 ? 150.594 171.535 131.385 1.00 43.83  0  1046 PHE   A C   1 
ATOM   7787  O O   . PHE   A 1 1082 ? 151.700 171.172 130.980 1.00 49.15  0  1046 PHE   A O   1 
ATOM   7788  C CB  . PHE   A 1 1082 ? 148.549 170.360 130.535 1.00 37.57  0  1046 PHE   A CB  1 
ATOM   7789  C CG  . PHE   A 1 1082 ? 149.260 169.103 130.123 1.00 47.87  0  1046 PHE   A CG  1 
ATOM   7790  C CD1 . PHE   A 1 1082 ? 149.226 168.673 128.809 1.00 46.75  0  1046 PHE   A CD1 1 
ATOM   7791  C CD2 . PHE   A 1 1082 ? 149.945 168.340 131.052 1.00 44.44  0  1046 PHE   A CD2 1 
ATOM   7792  C CE1 . PHE   A 1 1082 ? 149.866 167.519 128.428 1.00 36.57  0  1046 PHE   A CE1 1 
ATOM   7793  C CE2 . PHE   A 1 1082 ? 150.588 167.184 130.675 1.00 38.39  0  1046 PHE   A CE2 1 
ATOM   7794  C CZ  . PHE   A 1 1082 ? 150.548 166.774 129.362 1.00 35.77  0  1046 PHE   A CZ  1 
ATOM   7795  N N   . ASP   A 1 1083 ? 150.353 171.874 132.646 1.00 43.54  0  1047 ASP   A N   1 
ATOM   7796  C CA  . ASP   A 1 1083 ? 151.404 171.779 133.647 1.00 42.41  0  1047 ASP   A CA  1 
ATOM   7797  C C   . ASP   A 1 1083 ? 151.686 170.317 133.957 1.00 47.63  0  1047 ASP   A C   1 
ATOM   7798  O O   . ASP   A 1 1083 ? 150.782 169.568 134.333 1.00 54.53  0  1047 ASP   A O   1 
ATOM   7799  C CB  . ASP   A 1 1083 ? 150.996 172.521 134.916 1.00 50.92  0  1047 ASP   A CB  1 
ATOM   7800  C CG  . ASP   A 1 1083 ? 150.867 174.014 134.701 1.00 56.31  0  1047 ASP   A CG  1 
ATOM   7801  O OD1 . ASP   A 1 1083 ? 151.557 174.547 133.807 1.00 53.42  0  1047 ASP   A OD1 1 
ATOM   7802  O OD2 . ASP   A 1 1083 ? 150.076 174.654 135.424 1.00 56.18  -1 1047 ASP   A OD2 1 
ATOM   7803  N N   . LYS   A 1 1084 ? 152.942 169.910 133.802 1.00 42.47  0  1048 LYS   A N   1 
ATOM   7804  C CA  . LYS   A 1 1084 ? 153.320 168.517 133.981 1.00 41.96  0  1048 LYS   A CA  1 
ATOM   7805  C C   . LYS   A 1 1084 ? 153.614 168.241 135.448 1.00 38.85  0  1048 LYS   A C   1 
ATOM   7806  O O   . LYS   A 1 1084 ? 154.381 168.968 136.085 1.00 48.55  0  1048 LYS   A O   1 
ATOM   7807  C CB  . LYS   A 1 1084 ? 154.527 168.165 133.111 1.00 42.80  0  1048 LYS   A CB  1 
ATOM   7808  C CG  . LYS   A 1 1084 ? 155.745 169.035 133.322 1.00 42.53  0  1048 LYS   A CG  1 
ATOM   7809  C CD  . LYS   A 1 1084 ? 156.865 168.645 132.379 1.00 45.11  0  1048 LYS   A CD  1 
ATOM   7810  C CE  . LYS   A 1 1084 ? 156.662 169.240 131.002 1.00 43.05  0  1048 LYS   A CE  1 
ATOM   7811  N NZ  . LYS   A 1 1084 ? 157.862 169.043 130.146 1.00 43.86  1  1048 LYS   A NZ  1 
ATOM   7812  N N   . ASN   A 1 1085 ? 152.984 167.200 135.984 1.00 44.40  0  1049 ASN   A N   1 
ATOM   7813  C CA  . ASN   A 1 1085 ? 153.163 166.795 137.378 1.00 51.54  0  1049 ASN   A CA  1 
ATOM   7814  C C   . ASN   A 1 1085 ? 153.408 165.291 137.451 1.00 55.38  0  1049 ASN   A C   1 
ATOM   7815  O O   . ASN   A 1 1085 ? 152.574 164.532 137.953 1.00 52.42  0  1049 ASN   A O   1 
ATOM   7816  C CB  . ASN   A 1 1085 ? 151.945 167.197 138.208 1.00 48.94  0  1049 ASN   A CB  1 
ATOM   7817  C CG  . ASN   A 1 1085 ? 152.109 166.881 139.678 1.00 53.89  0  1049 ASN   A CG  1 
ATOM   7818  O OD1 . ASN   A 1 1085 ? 153.225 166.776 140.183 1.00 56.35  0  1049 ASN   A OD1 1 
ATOM   7819  N ND2 . ASN   A 1 1085 ? 150.991 166.721 140.373 1.00 52.39  0  1049 ASN   A ND2 1 
ATOM   7820  N N   . PRO   A 1 1086 ? 154.548 164.824 136.948 1.00 48.44  0  1050 PRO   A N   1 
ATOM   7821  C CA  . PRO   A 1 1086 ? 154.826 163.387 136.983 1.00 45.97  0  1050 PRO   A CA  1 
ATOM   7822  C C   . PRO   A 1 1086 ? 155.022 162.892 138.404 1.00 49.28  0  1050 PRO   A C   1 
ATOM   7823  O O   . PRO   A 1 1086 ? 155.546 163.597 139.270 1.00 51.36  0  1050 PRO   A O   1 
ATOM   7824  C CB  . PRO   A 1 1086 ? 156.117 163.252 136.167 1.00 42.21  0  1050 PRO   A CB  1 
ATOM   7825  C CG  . PRO   A 1 1086 ? 156.271 164.549 135.456 1.00 42.44  0  1050 PRO   A CG  1 
ATOM   7826  C CD  . PRO   A 1 1086 ? 155.654 165.571 136.335 1.00 42.36  0  1050 PRO   A CD  1 
ATOM   7827  N N   . ASN   A 1 1087 ? 154.597 161.654 138.633 1.00 49.00  0  1051 ASN   A N   1 
ATOM   7828  C CA  . ASN   A 1 1087 ? 154.742 161.015 139.933 1.00 47.74  0  1051 ASN   A CA  1 
ATOM   7829  C C   . ASN   A 1 1087 ? 154.530 159.524 139.750 1.00 47.38  0  1051 ASN   A C   1 
ATOM   7830  O O   . ASN   A 1 1087 ? 153.496 159.110 139.218 1.00 49.91  0  1051 ASN   A O   1 
ATOM   7831  C CB  . ASN   A 1 1087 ? 153.741 161.579 140.947 1.00 45.53  0  1051 ASN   A CB  1 
ATOM   7832  C CG  . ASN   A 1 1087 ? 154.013 161.105 142.361 1.00 43.52  0  1051 ASN   A CG  1 
ATOM   7833  O OD1 . ASN   A 1 1087 ? 155.043 160.489 142.636 1.00 42.79  0  1051 ASN   A OD1 1 
ATOM   7834  N ND2 . ASN   A 1 1087 ? 153.086 161.389 143.267 1.00 43.58  0  1051 ASN   A ND2 1 
ATOM   7835  N N   . ALA   A 1 1088 ? 155.501 158.728 140.192 1.00 45.02  0  1052 ALA   A N   1 
ATOM   7836  C CA  . ALA   A 1 1088 ? 155.449 157.275 140.063 1.00 41.83  0  1052 ALA   A CA  1 
ATOM   7837  C C   . ALA   A 1 1088 ? 155.184 156.870 138.617 1.00 42.02  0  1052 ALA   A C   1 
ATOM   7838  O O   . ALA   A 1 1088 ? 154.263 156.110 138.315 1.00 45.58  0  1052 ALA   A O   1 
ATOM   7839  C CB  . ALA   A 1 1088 ? 154.399 156.683 141.003 1.00 40.30  0  1052 ALA   A CB  1 
ATOM   7840  N N   . GLU   A 1 1089 ? 156.004 157.406 137.709 1.00 37.65  0  1053 GLU   A N   1 
ATOM   7841  C CA  . GLU   A 1 1089 ? 155.805 157.153 136.287 1.00 34.88  0  1053 GLU   A CA  1 
ATOM   7842  C C   . GLU   A 1 1089 ? 155.971 155.681 135.943 1.00 38.82  0  1053 GLU   A C   1 
ATOM   7843  O O   . GLU   A 1 1089 ? 155.191 155.135 135.156 1.00 38.63  0  1053 GLU   A O   1 
ATOM   7844  C CB  . GLU   A 1 1089 ? 156.782 157.987 135.458 1.00 39.91  0  1053 GLU   A CB  1 
ATOM   7845  C CG  . GLU   A 1 1089 ? 156.951 159.421 135.928 1.00 49.29  0  1053 GLU   A CG  1 
ATOM   7846  C CD  . GLU   A 1 1089 ? 158.181 159.616 136.790 1.00 55.40  0  1053 GLU   A CD  1 
ATOM   7847  O OE1 . GLU   A 1 1089 ? 158.913 158.632 137.020 1.00 57.41  0  1053 GLU   A OE1 1 
ATOM   7848  O OE2 . GLU   A 1 1089 ? 158.419 160.756 137.239 1.00 51.71  -1 1053 GLU   A OE2 1 
ATOM   7849  N N   . PHE   A 1 1090 ? 156.974 155.025 136.516 1.00 40.08  0  1054 PHE   A N   1 
ATOM   7850  C CA  . PHE   A 1 1090 ? 157.352 153.699 136.051 1.00 33.96  0  1054 PHE   A CA  1 
ATOM   7851  C C   . PHE   A 1 1090 ? 156.449 152.597 136.586 1.00 40.52  0  1054 PHE   A C   1 
ATOM   7852  O O   . PHE   A 1 1090 ? 156.124 151.668 135.844 1.00 46.11  0  1054 PHE   A O   1 
ATOM   7853  C CB  . PHE   A 1 1090 ? 158.818 153.440 136.394 1.00 34.64  0  1054 PHE   A CB  1 
ATOM   7854  C CG  . PHE   A 1 1090 ? 159.751 154.376 135.689 1.00 43.88  0  1054 PHE   A CG  1 
ATOM   7855  C CD1 . PHE   A 1 1090 ? 160.055 154.190 134.354 1.00 40.12  0  1054 PHE   A CD1 1 
ATOM   7856  C CD2 . PHE   A 1 1090 ? 160.277 155.472 136.341 1.00 45.26  0  1054 PHE   A CD2 1 
ATOM   7857  C CE1 . PHE   A 1 1090 ? 160.890 155.059 133.693 1.00 37.80  0  1054 PHE   A CE1 1 
ATOM   7858  C CE2 . PHE   A 1 1090 ? 161.114 156.346 135.684 1.00 40.91  0  1054 PHE   A CE2 1 
ATOM   7859  C CZ  . PHE   A 1 1090 ? 161.421 156.138 134.358 1.00 38.94  0  1054 PHE   A CZ  1 
ATOM   7860  N N   . VAL   A 1 1091 ? 155.999 152.679 137.839 1.00 36.52  0  1055 VAL   A N   1 
ATOM   7861  C CA  . VAL   A 1 1091 ? 155.034 151.692 138.316 1.00 28.27  0  1055 VAL   A CA  1 
ATOM   7862  C C   . VAL   A 1 1091 ? 153.701 151.864 137.603 1.00 31.79  0  1055 VAL   A C   1 
ATOM   7863  O O   . VAL   A 1 1091 ? 153.024 150.881 137.279 1.00 45.15  0  1055 VAL   A O   1 
ATOM   7864  C CB  . VAL   A 1 1091 ? 154.875 151.771 139.843 1.00 33.95  0  1055 VAL   A CB  1 
ATOM   7865  C CG1 . VAL   A 1 1091 ? 156.140 151.314 140.515 1.00 45.72  0  1055 VAL   A CG1 1 
ATOM   7866  C CG2 . VAL   A 1 1091 ? 154.535 153.177 140.272 1.00 40.52  0  1055 VAL   A CG2 1 
ATOM   7867  N N   . THR   A 1 1092 ? 153.303 153.109 137.340 1.00 24.23  0  1056 THR   A N   1 
ATOM   7868  C CA  . THR   A 1 1092 ? 152.069 153.352 136.604 1.00 29.59  0  1056 THR   A CA  1 
ATOM   7869  C C   . THR   A 1 1092 ? 152.155 152.829 135.179 1.00 39.06  0  1056 THR   A C   1 
ATOM   7870  O O   . THR   A 1 1092 ? 151.179 152.276 134.664 1.00 47.31  0  1056 THR   A O   1 
ATOM   7871  C CB  . THR   A 1 1092 ? 151.746 154.841 136.599 1.00 26.57  0  1056 THR   A CB  1 
ATOM   7872  O OG1 . THR   A 1 1092 ? 151.709 155.322 137.946 1.00 30.13  0  1056 THR   A OG1 1 
ATOM   7873  C CG2 . THR   A 1 1092 ? 150.401 155.081 135.953 1.00 32.84  0  1056 THR   A CG2 1 
ATOM   7874  N N   . LEU   A 1 1093 ? 153.304 152.993 134.525 1.00 26.62  0  1057 LEU   A N   1 
ATOM   7875  C CA  . LEU   A 1 1093 ? 153.468 152.448 133.185 1.00 17.19  0  1057 LEU   A CA  1 
ATOM   7876  C C   . LEU   A 1 1093 ? 153.575 150.930 133.198 1.00 25.25  0  1057 LEU   A C   1 
ATOM   7877  O O   . LEU   A 1 1093 ? 153.188 150.280 132.225 1.00 38.36  0  1057 LEU   A O   1 
ATOM   7878  C CB  . LEU   A 1 1093 ? 154.694 153.060 132.520 1.00 27.10  0  1057 LEU   A CB  1 
ATOM   7879  C CG  . LEU   A 1 1093 ? 154.488 154.484 132.015 1.00 24.38  0  1057 LEU   A CG  1 
ATOM   7880  C CD1 . LEU   A 1 1093 ? 155.824 155.129 131.736 1.00 33.58  0  1057 LEU   A CD1 1 
ATOM   7881  C CD2 . LEU   A 1 1093 ? 153.621 154.487 130.776 1.00 27.58  0  1057 LEU   A CD2 1 
ATOM   7882  N N   . MET   A 1 1094 ? 154.104 150.349 134.273 1.00 21.72  0  1058 MET   A N   1 
ATOM   7883  C CA  . MET   A 1 1094 ? 154.069 148.899 134.406 1.00 22.88  0  1058 MET   A CA  1 
ATOM   7884  C C   . MET   A 1 1094 ? 152.645 148.389 134.553 1.00 26.88  0  1058 MET   A C   1 
ATOM   7885  O O   . MET   A 1 1094 ? 152.298 147.352 133.981 1.00 35.60  0  1058 MET   A O   1 
ATOM   7886  C CB  . MET   A 1 1094 ? 154.909 148.457 135.602 1.00 24.45  0  1058 MET   A CB  1 
ATOM   7887  C CG  . MET   A 1 1094 ? 156.404 148.570 135.396 1.00 28.65  0  1058 MET   A CG  1 
ATOM   7888  S SD  . MET   A 1 1094 ? 157.284 148.571 136.963 1.00 54.98  0  1058 MET   A SD  1 
ATOM   7889  C CE  . MET   A 1 1094 ? 158.789 147.719 136.512 1.00 36.02  0  1058 MET   A CE  1 
ATOM   7890  N N   . ARG   A 1 1095 ? 151.808 149.094 135.309 1.00 28.03  0  1059 ARG   A N   1 
ATOM   7891  C CA  . ARG   A 1 1095 ? 150.438 148.652 135.535 1.00 32.47  0  1059 ARG   A CA  1 
ATOM   7892  C C   . ARG   A 1 1095 ? 149.540 148.907 134.329 1.00 34.65  0  1059 ARG   A C   1 
ATOM   7893  O O   . ARG   A 1 1095 ? 148.809 148.011 133.898 1.00 42.56  0  1059 ARG   A O   1 
ATOM   7894  C CB  . ARG   A 1 1095 ? 149.875 149.339 136.778 1.00 29.26  0  1059 ARG   A CB  1 
ATOM   7895  C CG  . ARG   A 1 1095 ? 150.528 148.870 138.056 1.00 29.40  0  1059 ARG   A CG  1 
ATOM   7896  C CD  . ARG   A 1 1095 ? 149.684 149.217 139.253 1.00 33.83  0  1059 ARG   A CD  1 
ATOM   7897  N NE  . ARG   A 1 1095 ? 149.830 150.614 139.628 1.00 34.47  0  1059 ARG   A NE  1 
ATOM   7898  C CZ  . ARG   A 1 1095 ? 150.494 151.029 140.696 1.00 34.76  0  1059 ARG   A CZ  1 
ATOM   7899  N NH1 . ARG   A 1 1095 ? 151.085 150.175 141.514 1.00 30.52  1  1059 ARG   A NH1 1 
ATOM   7900  N NH2 . ARG   A 1 1095 ? 150.564 152.331 140.951 1.00 38.90  0  1059 ARG   A NH2 1 
ATOM   7901  N N   . ASP   A 1 1096 ? 149.572 150.117 133.779 1.00 27.99  0  1060 ASP   A N   1 
ATOM   7902  C CA  . ASP   A 1 1096 ? 148.836 150.453 132.563 1.00 29.96  0  1060 ASP   A CA  1 
ATOM   7903  C C   . ASP   A 1 1096 ? 149.816 151.101 131.597 1.00 37.94  0  1060 ASP   A C   1 
ATOM   7904  O O   . ASP   A 1 1096 ? 150.078 152.308 131.679 1.00 35.36  0  1060 ASP   A O   1 
ATOM   7905  C CB  . ASP   A 1 1096 ? 147.654 151.372 132.859 1.00 40.54  0  1060 ASP   A CB  1 
ATOM   7906  C CG  . ASP   A 1 1096 ? 146.757 151.583 131.649 1.00 43.02  0  1060 ASP   A CG  1 
ATOM   7907  O OD1 . ASP   A 1 1096 ? 146.968 150.910 130.620 1.00 33.31  0  1060 ASP   A OD1 1 
ATOM   7908  O OD2 . ASP   A 1 1096 ? 145.837 152.426 131.724 1.00 40.30  -1 1060 ASP   A OD2 1 
ATOM   7909  N N   . PRO   A 1 1097 ? 150.381 150.329 130.666 1.00 38.26  0  1061 PRO   A N   1 
ATOM   7910  C CA  . PRO   A 1 1097 ? 151.354 150.895 129.722 1.00 27.58  0  1061 PRO   A CA  1 
ATOM   7911  C C   . PRO   A 1 1097 ? 150.769 151.953 128.802 1.00 29.75  0  1061 PRO   A C   1 
ATOM   7912  O O   . PRO   A 1 1097 ? 151.510 152.642 128.098 1.00 37.73  0  1061 PRO   A O   1 
ATOM   7913  C CB  . PRO   A 1 1097 ? 151.825 149.667 128.936 1.00 17.14  0  1061 PRO   A CB  1 
ATOM   7914  C CG  . PRO   A 1 1097 ? 151.577 148.524 129.850 1.00 23.61  0  1061 PRO   A CG  1 
ATOM   7915  C CD  . PRO   A 1 1097 ? 150.312 148.864 130.566 1.00 35.62  0  1061 PRO   A CD  1 
ATOM   7916  N N   . GLN   A 1 1098 ? 149.446 152.089 128.791 1.00 25.25  0  1062 GLN   A N   1 
ATOM   7917  C CA  . GLN   A 1 1098 ? 148.775 153.124 128.018 1.00 24.68  0  1062 GLN   A CA  1 
ATOM   7918  C C   . GLN   A 1 1098 ? 148.413 154.342 128.860 1.00 39.09  0  1062 GLN   A C   1 
ATOM   7919  O O   . GLN   A 1 1098 ? 147.743 155.250 128.361 1.00 42.44  0  1062 GLN   A O   1 
ATOM   7920  C CB  . GLN   A 1 1098 ? 147.520 152.555 127.357 1.00 27.90  0  1062 GLN   A CB  1 
ATOM   7921  C CG  . GLN   A 1 1098 ? 147.785 151.434 126.375 1.00 30.92  0  1062 GLN   A CG  1 
ATOM   7922  C CD  . GLN   A 1 1098 ? 147.676 151.890 124.939 1.00 37.22  0  1062 GLN   A CD  1 
ATOM   7923  O OE1 . GLN   A 1 1098 ? 146.694 152.516 124.547 1.00 28.95  0  1062 GLN   A OE1 1 
ATOM   7924  N NE2 . GLN   A 1 1098 ? 148.689 151.579 124.142 1.00 39.64  0  1062 GLN   A NE2 1 
ATOM   7925  N N   . ALA   A 1 1099 ? 148.839 154.383 130.120 1.00 36.93  0  1063 ALA   A N   1 
ATOM   7926  C CA  . ALA   A 1 1099 ? 148.478 155.478 131.009 1.00 28.15  0  1063 ALA   A CA  1 
ATOM   7927  C C   . ALA   A 1 1099 ? 149.110 156.785 130.549 1.00 32.11  0  1063 ALA   A C   1 
ATOM   7928  O O   . ALA   A 1 1099 ? 150.181 156.804 129.941 1.00 46.24  0  1063 ALA   A O   1 
ATOM   7929  C CB  . ALA   A 1 1099 ? 148.912 155.169 132.440 1.00 26.61  0  1063 ALA   A CB  1 
ATOM   7930  N N   . LEU   A 1 1100 ? 148.430 157.892 130.849 1.00 23.16  0  1064 LEU   A N   1 
ATOM   7931  C CA  . LEU   A 1 1100 ? 148.937 159.210 130.484 1.00 20.90  0  1064 LEU   A CA  1 
ATOM   7932  C C   . LEU   A 1 1100 ? 149.753 159.833 131.612 1.00 30.55  0  1064 LEU   A C   1 
ATOM   7933  O O   . LEU   A 1 1100 ? 150.953 160.074 131.456 1.00 39.33  0  1064 LEU   A O   1 
ATOM   7934  C CB  . LEU   A 1 1100 ? 147.780 160.130 130.092 1.00 23.13  0  1064 LEU   A CB  1 
ATOM   7935  C CG  . LEU   A 1 1100 ? 147.281 159.968 128.664 1.00 20.45  0  1064 LEU   A CG  1 
ATOM   7936  C CD1 . LEU   A 1 1100 ? 146.392 161.130 128.288 1.00 22.46  0  1064 LEU   A CD1 1 
ATOM   7937  C CD2 . LEU   A 1 1100 ? 148.457 159.867 127.728 1.00 27.75  0  1064 LEU   A CD2 1 
ATOM   7938  N N   . GLY   A 1 1101 ? 149.127 160.075 132.758 1.00 37.80  0  1065 GLY   A N   1 
ATOM   7939  C CA  . GLY   A 1 1101 ? 149.825 160.687 133.867 1.00 43.88  0  1065 GLY   A CA  1 
ATOM   7940  C C   . GLY   A 1 1101 ? 149.662 162.194 133.907 1.00 41.34  0  1065 GLY   A C   1 
ATOM   7941  O O   . GLY   A 1 1101 ? 148.991 162.808 133.078 1.00 44.54  0  1065 GLY   A O   1 
ATOM   7942  N N   . SER   A 1 1102 ? 150.306 162.796 134.911 1.00 38.30  0  1066 SER   A N   1 
ATOM   7943  C CA  . SER   A 1 1102 ? 150.165 164.221 135.216 1.00 42.33  0  1066 SER   A CA  1 
ATOM   7944  C C   . SER   A 1 1102 ? 148.719 164.589 135.524 1.00 47.61  0  1066 SER   A C   1 
ATOM   7945  O O   . SER   A 1 1102 ? 148.296 165.724 135.290 1.00 51.52  0  1066 SER   A O   1 
ATOM   7946  C CB  . SER   A 1 1102 ? 150.703 165.102 134.084 1.00 42.23  0  1066 SER   A CB  1 
ATOM   7947  O OG  . SER   A 1 1102 ? 152.110 165.235 134.162 1.00 44.04  0  1066 SER   A OG  1 
ATOM   7948  N N   . GLU   A 1 1103 ? 147.957 163.629 136.055 1.00 47.09  0  1067 GLU   A N   1 
ATOM   7949  C CA  . GLU   A 1 1103 ? 146.539 163.817 136.365 1.00 47.42  0  1067 GLU   A CA  1 
ATOM   7950  C C   . GLU   A 1 1103 ? 145.761 164.282 135.137 1.00 50.76  0  1067 GLU   A C   1 
ATOM   7951  O O   . GLU   A 1 1103 ? 144.857 165.114 135.230 1.00 47.63  0  1067 GLU   A O   1 
ATOM   7952  C CB  . GLU   A 1 1103 ? 146.351 164.787 137.532 1.00 48.13  0  1067 GLU   A CB  1 
ATOM   7953  C CG  . GLU   A 1 1103 ? 146.342 164.121 138.898 1.00 54.63  0  1067 GLU   A CG  1 
ATOM   7954  C CD  . GLU   A 1 1103 ? 147.586 163.296 139.155 1.00 56.39  0  1067 GLU   A CD  1 
ATOM   7955  O OE1 . GLU   A 1 1103 ? 148.688 163.752 138.787 1.00 59.05  0  1067 GLU   A OE1 1 
ATOM   7956  O OE2 . GLU   A 1 1103 ? 147.463 162.192 139.725 1.00 53.47  -1 1067 GLU   A OE2 1 
ATOM   7957  N N   . ARG   A 1 1104 ? 146.122 163.743 133.975 1.00 43.22  0  1068 ARG   A N   1 
ATOM   7958  C CA  . ARG   A 1 1104 ? 145.455 164.048 132.719 1.00 38.88  0  1068 ARG   A CA  1 
ATOM   7959  C C   . ARG   A 1 1104 ? 144.482 162.959 132.299 1.00 41.14  0  1068 ARG   A C   1 
ATOM   7960  O O   . ARG   A 1 1104 ? 143.948 163.012 131.187 1.00 42.34  0  1068 ARG   A O   1 
ATOM   7961  C CB  . ARG   A 1 1104 ? 146.487 164.274 131.616 1.00 32.64  0  1068 ARG   A CB  1 
ATOM   7962  C CG  . ARG   A 1 1104 ? 147.453 165.388 131.918 1.00 36.37  0  1068 ARG   A CG  1 
ATOM   7963  C CD  . ARG   A 1 1104 ? 146.734 166.717 131.953 1.00 38.29  0  1068 ARG   A CD  1 
ATOM   7964  N NE  . ARG   A 1 1104 ? 146.245 167.092 130.633 1.00 43.04  0  1068 ARG   A NE  1 
ATOM   7965  C CZ  . ARG   A 1 1104 ? 145.644 168.240 130.358 1.00 46.67  0  1068 ARG   A CZ  1 
ATOM   7966  N NH1 . ARG   A 1 1104 ? 145.433 169.149 131.294 1.00 45.69  1  1068 ARG   A NH1 1 
ATOM   7967  N NH2 . ARG   A 1 1104 ? 145.250 168.483 129.113 1.00 47.28  0  1068 ARG   A NH2 1 
ATOM   7968  N N   . GLN   A 1 1105 ? 144.241 161.975 133.159 1.00 40.30  0  1069 GLN   A N   1 
ATOM   7969  C CA  . GLN   A 1 1105 ? 143.380 160.855 132.829 1.00 37.26  0  1069 GLN   A CA  1 
ATOM   7970  C C   . GLN   A 1 1105 ? 142.456 160.581 134.007 1.00 46.30  0  1069 GLN   A C   1 
ATOM   7971  O O   . GLN   A 1 1105 ? 142.766 160.908 135.155 1.00 46.19  0  1069 GLN   A O   1 
ATOM   7972  C CB  . GLN   A 1 1105 ? 144.204 159.611 132.489 1.00 26.19  0  1069 GLN   A CB  1 
ATOM   7973  C CG  . GLN   A 1 1105 ? 143.609 158.740 131.409 1.00 33.27  0  1069 GLN   A CG  1 
ATOM   7974  C CD  . GLN   A 1 1105 ? 144.376 157.451 131.239 1.00 44.87  0  1069 GLN   A CD  1 
ATOM   7975  O OE1 . GLN   A 1 1105 ? 144.294 156.797 130.201 1.00 44.17  0  1069 GLN   A OE1 1 
ATOM   7976  N NE2 . GLN   A 1 1105 ? 145.118 157.068 132.271 1.00 47.37  0  1069 GLN   A NE2 1 
ATOM   7977  N N   . ALA   A 1 1106 ? 141.310 159.977 133.710 1.00 51.62  0  1070 ALA   A N   1 
ATOM   7978  C CA  . ALA   A 1 1106 ? 140.336 159.663 134.746 1.00 45.02  0  1070 ALA   A CA  1 
ATOM   7979  C C   . ALA   A 1 1106 ? 140.817 158.476 135.570 1.00 48.18  0  1070 ALA   A C   1 
ATOM   7980  O O   . ALA   A 1 1106 ? 141.103 157.407 135.023 1.00 50.97  0  1070 ALA   A O   1 
ATOM   7981  C CB  . ALA   A 1 1106 ? 138.978 159.365 134.119 1.00 45.12  0  1070 ALA   A CB  1 
ATOM   7982  N N   . LYS   A 1 1107 ? 140.903 158.662 136.883 1.00 50.94  0  1071 LYS   A N   1 
ATOM   7983  C CA  . LYS   A 1 1107 ? 141.334 157.585 137.761 1.00 56.16  0  1071 LYS   A CA  1 
ATOM   7984  C C   . LYS   A 1 1107 ? 140.280 156.486 137.813 1.00 61.04  0  1071 LYS   A C   1 
ATOM   7985  O O   . LYS   A 1 1107 ? 139.077 156.754 137.778 1.00 59.75  0  1071 LYS   A O   1 
ATOM   7986  C CB  . LYS   A 1 1107 ? 141.610 158.119 139.165 1.00 54.30  0  1071 LYS   A CB  1 
ATOM   7987  C CG  . LYS   A 1 1107 ? 142.798 159.062 139.242 1.00 54.39  0  1071 LYS   A CG  1 
ATOM   7988  C CD  . LYS   A 1 1107 ? 143.297 159.203 140.668 1.00 57.18  0  1071 LYS   A CD  1 
ATOM   7989  C CE  . LYS   A 1 1107 ? 144.310 160.329 140.792 1.00 57.03  0  1071 LYS   A CE  1 
ATOM   7990  N NZ  . LYS   A 1 1107 ? 145.537 160.073 139.988 1.00 59.05  1  1071 LYS   A NZ  1 
ATOM   7991  N N   . ILE   A 1 1108 ? 140.740 155.245 137.900 1.00 60.04  0  1072 ILE   A N   1 
ATOM   7992  C CA  . ILE   A 1 1108 ? 139.866 154.093 137.860 1.00 56.09  0  1072 ILE   A CA  1 
ATOM   7993  C C   . ILE   A 1 1108 ? 139.614 153.600 139.280 1.00 53.21  0  1072 ILE   A C   1 
ATOM   7994  O O   . ILE   A 1 1108 ? 140.258 154.026 140.235 1.00 54.74  0  1072 ILE   A O   1 
ATOM   7995  C CB  . ILE   A 1 1108 ? 140.437 152.969 136.964 1.00 52.47  0  1072 ILE   A CB  1 
ATOM   7996  C CG1 . ILE   A 1 1108 ? 141.950 152.866 137.139 1.00 57.29  0  1072 ILE   A CG1 1 
ATOM   7997  C CG2 . ILE   A 1 1108 ? 140.081 153.216 135.512 1.00 50.83  0  1072 ILE   A CG2 1 
ATOM   7998  C CD1 . ILE   A 1 1108 ? 142.505 151.499 136.831 1.00 59.70  0  1072 ILE   A CD1 1 
ATOM   7999  N N   . THR   A 1 1109 ? 138.651 152.687 139.419 1.00 50.83  0  1073 THR   A N   1 
ATOM   8000  C CA  . THR   A 1 1109 ? 138.225 152.230 140.738 1.00 51.42  0  1073 THR   A CA  1 
ATOM   8001  C C   . THR   A 1 1109 ? 139.351 151.523 141.482 1.00 54.25  0  1073 THR   A C   1 
ATOM   8002  O O   . THR   A 1 1109 ? 139.495 151.685 142.699 1.00 57.80  0  1073 THR   A O   1 
ATOM   8003  C CB  . THR   A 1 1109 ? 137.018 151.305 140.599 1.00 55.05  0  1073 THR   A CB  1 
ATOM   8004  O OG1 . THR   A 1 1109 ? 136.081 151.879 139.680 1.00 56.97  0  1073 THR   A OG1 1 
ATOM   8005  C CG2 . THR   A 1 1109 ? 136.344 151.105 141.942 1.00 53.30  0  1073 THR   A CG2 1 
ATOM   8006  N N   . SER   A 1 1110 ? 140.150 150.719 140.777 1.00 49.30  0  1074 SER   A N   1 
ATOM   8007  C CA  . SER   A 1 1110 ? 141.249 150.020 141.432 1.00 49.31  0  1074 SER   A CA  1 
ATOM   8008  C C   . SER   A 1 1110 ? 142.337 150.972 141.905 1.00 49.72  0  1074 SER   A C   1 
ATOM   8009  O O   . SER   A 1 1110 ? 142.981 150.699 142.923 1.00 49.59  0  1074 SER   A O   1 
ATOM   8010  C CB  . SER   A 1 1110 ? 141.849 148.972 140.495 1.00 49.50  0  1074 SER   A CB  1 
ATOM   8011  O OG  . SER   A 1 1110 ? 142.593 149.580 139.457 1.00 48.98  0  1074 SER   A OG  1 
ATOM   8012  N N   . GLU   A 1 1111 ? 142.564 152.072 141.185 1.00 52.58  0  1075 GLU   A N   1 
ATOM   8013  C CA  . GLU   A 1 1111 ? 143.554 153.053 141.618 1.00 55.27  0  1075 GLU   A CA  1 
ATOM   8014  C C   . GLU   A 1 1111 ? 143.129 153.738 142.910 1.00 54.00  0  1075 GLU   A C   1 
ATOM   8015  O O   . GLU   A 1 1111 ? 143.955 153.964 143.801 1.00 54.79  0  1075 GLU   A O   1 
ATOM   8016  C CB  . GLU   A 1 1111 ? 143.780 154.087 140.517 1.00 53.76  0  1075 GLU   A CB  1 
ATOM   8017  C CG  . GLU   A 1 1111 ? 144.704 153.622 139.411 1.00 56.11  0  1075 GLU   A CG  1 
ATOM   8018  C CD  . GLU   A 1 1111 ? 145.447 154.767 138.753 1.00 62.35  0  1075 GLU   A CD  1 
ATOM   8019  O OE1 . GLU   A 1 1111 ? 144.827 155.497 137.952 1.00 65.20  0  1075 GLU   A OE1 1 
ATOM   8020  O OE2 . GLU   A 1 1111 ? 146.652 154.936 139.036 1.00 56.60  -1 1075 GLU   A OE2 1 
ATOM   8021  N N   . ILE   A 1 1112 ? 141.844 154.079 143.025 1.00 50.72  0  1076 ILE   A N   1 
ATOM   8022  C CA  . ILE   A 1 1112 ? 141.366 154.830 144.180 1.00 47.18  0  1076 ILE   A CA  1 
ATOM   8023  C C   . ILE   A 1 1112 ? 141.398 153.974 145.437 1.00 47.89  0  1076 ILE   A C   1 
ATOM   8024  O O   . ILE   A 1 1112 ? 141.831 154.427 146.503 1.00 47.61  0  1076 ILE   A O   1 
ATOM   8025  C CB  . ILE   A 1 1112 ? 139.954 155.372 143.904 1.00 44.28  0  1076 ILE   A CB  1 
ATOM   8026  C CG1 . ILE   A 1 1112 ? 139.978 156.338 142.721 1.00 50.54  0  1076 ILE   A CG1 1 
ATOM   8027  C CG2 . ILE   A 1 1112 ? 139.387 156.039 145.137 1.00 45.48  0  1076 ILE   A CG2 1 
ATOM   8028  C CD1 . ILE   A 1 1112 ? 140.949 157.479 142.895 1.00 52.43  0  1076 ILE   A CD1 1 
ATOM   8029  N N   . ASN   A 1 1113 ? 140.945 152.730 145.338 1.00 49.20  0  1077 ASN   A N   1 
ATOM   8030  C CA  . ASN   A 1 1113 ? 140.772 151.876 146.502 1.00 49.11  0  1077 ASN   A CA  1 
ATOM   8031  C C   . ASN   A 1 1113 ? 142.016 151.075 146.853 1.00 51.35  0  1077 ASN   A C   1 
ATOM   8032  O O   . ASN   A 1 1113 ? 141.993 150.333 147.839 1.00 48.56  0  1077 ASN   A O   1 
ATOM   8033  C CB  . ASN   A 1 1113 ? 139.598 150.925 146.276 1.00 43.72  0  1077 ASN   A CB  1 
ATOM   8034  C CG  . ASN   A 1 1113 ? 138.319 151.657 145.945 1.00 51.18  0  1077 ASN   A CG  1 
ATOM   8035  O OD1 . ASN   A 1 1113 ? 137.647 152.193 146.825 1.00 54.43  0  1077 ASN   A OD1 1 
ATOM   8036  N ND2 . ASN   A 1 1113 ? 137.980 151.698 144.665 1.00 51.70  0  1077 ASN   A ND2 1 
ATOM   8037  N N   . ARG   A 1 1114 ? 143.096 151.205 146.081 1.00 48.47  0  1078 ARG   A N   1 
ATOM   8038  C CA  . ARG   A 1 1114 ? 144.294 150.414 146.345 1.00 43.89  0  1078 ARG   A CA  1 
ATOM   8039  C C   . ARG   A 1 1114 ? 144.863 150.714 147.726 1.00 41.21  0  1078 ARG   A C   1 
ATOM   8040  O O   . ARG   A 1 1114 ? 145.221 149.795 148.474 1.00 42.15  0  1078 ARG   A O   1 
ATOM   8041  C CB  . ARG   A 1 1114 ? 145.340 150.679 145.265 1.00 40.60  0  1078 ARG   A CB  1 
ATOM   8042  C CG  . ARG   A 1 1114 ? 146.691 150.048 145.536 1.00 44.01  0  1078 ARG   A CG  1 
ATOM   8043  C CD  . ARG   A 1 1114 ? 147.713 150.478 144.500 1.00 40.27  0  1078 ARG   A CD  1 
ATOM   8044  N NE  . ARG   A 1 1114 ? 147.398 149.947 143.180 1.00 45.18  0  1078 ARG   A NE  1 
ATOM   8045  C CZ  . ARG   A 1 1114 ? 147.017 150.687 142.149 1.00 47.31  0  1078 ARG   A CZ  1 
ATOM   8046  N NH1 . ARG   A 1 1114 ? 146.904 152.000 142.247 1.00 47.00  1  1078 ARG   A NH1 1 
ATOM   8047  N NH2 . ARG   A 1 1114 ? 146.745 150.094 140.991 1.00 44.15  0  1078 ARG   A NH2 1 
ATOM   8048  N N   . LEU   A 1 1115 ? 144.945 151.995 148.086 1.00 41.71  0  1079 LEU   A N   1 
ATOM   8049  C CA  . LEU   A 1 1115 ? 145.450 152.354 149.405 1.00 45.41  0  1079 LEU   A CA  1 
ATOM   8050  C C   . LEU   A 1 1115 ? 144.533 151.839 150.506 1.00 49.64  0  1079 LEU   A C   1 
ATOM   8051  O O   . LEU   A 1 1115 ? 145.007 151.307 151.515 1.00 54.42  0  1079 LEU   A O   1 
ATOM   8052  C CB  . LEU   A 1 1115 ? 145.617 153.868 149.507 1.00 45.09  0  1079 LEU   A CB  1 
ATOM   8053  C CG  . LEU   A 1 1115 ? 146.390 154.370 150.727 1.00 47.72  0  1079 LEU   A CG  1 
ATOM   8054  C CD1 . LEU   A 1 1115 ? 147.618 153.511 150.979 1.00 43.58  0  1079 LEU   A CD1 1 
ATOM   8055  C CD2 . LEU   A 1 1115 ? 146.778 155.827 150.547 1.00 50.97  0  1079 LEU   A CD2 1 
ATOM   8056  N N   . ALA   A 1 1116 ? 143.218 151.979 150.327 1.00 46.39  0  1080 ALA   A N   1 
ATOM   8057  C CA  . ALA   A 1 1116 ? 142.280 151.471 151.322 1.00 39.50  0  1080 ALA   A CA  1 
ATOM   8058  C C   . ALA   A 1 1116 ? 142.377 149.958 151.446 1.00 47.52  0  1080 ALA   A C   1 
ATOM   8059  O O   . ALA   A 1 1116 ? 142.324 149.414 152.555 1.00 52.09  0  1080 ALA   A O   1 
ATOM   8060  C CB  . ALA   A 1 1116 ? 140.856 151.888 150.965 1.00 40.59  0  1080 ALA   A CB  1 
ATOM   8061  N N   . VAL   A 1 1117 ? 142.522 149.259 150.317 1.00 51.31  0  1081 VAL   A N   1 
ATOM   8062  C CA  . VAL   A 1 1117 ? 142.660 147.807 150.362 1.00 48.02  0  1081 VAL   A CA  1 
ATOM   8063  C C   . VAL   A 1 1117 ? 143.918 147.418 151.122 1.00 45.68  0  1081 VAL   A C   1 
ATOM   8064  O O   . VAL   A 1 1117 ? 143.906 146.478 151.921 1.00 35.20  0  1081 VAL   A O   1 
ATOM   8065  C CB  . VAL   A 1 1117 ? 142.655 147.216 148.941 1.00 36.05  0  1081 VAL   A CB  1 
ATOM   8066  C CG1 . VAL   A 1 1117 ? 143.063 145.762 148.981 1.00 33.49  0  1081 VAL   A CG1 1 
ATOM   8067  C CG2 . VAL   A 1 1117 ? 141.288 147.345 148.331 1.00 41.50  0  1081 VAL   A CG2 1 
ATOM   8068  N N   . THR   A 1 1118 ? 145.025 148.123 150.880 1.00 50.76  0  1082 THR   A N   1 
ATOM   8069  C CA  . THR   A 1 1118 ? 146.255 147.804 151.597 1.00 47.58  0  1082 THR   A CA  1 
ATOM   8070  C C   . THR   A 1 1118 ? 146.117 148.074 153.091 1.00 51.83  0  1082 THR   A C   1 
ATOM   8071  O O   . THR   A 1 1118 ? 146.599 147.285 153.911 1.00 58.47  0  1082 THR   A O   1 
ATOM   8072  C CB  . THR   A 1 1118 ? 147.430 148.586 151.017 1.00 36.34  0  1082 THR   A CB  1 
ATOM   8073  O OG1 . THR   A 1 1118 ? 147.101 149.977 150.965 1.00 47.70  0  1082 THR   A OG1 1 
ATOM   8074  C CG2 . THR   A 1 1118 ? 147.748 148.092 149.622 1.00 33.95  0  1082 THR   A CG2 1 
ATOM   8075  N N   . GLU   A 1 1119 ? 145.469 149.181 153.469 1.00 49.85  0  1083 GLU   A N   1 
ATOM   8076  C CA  . GLU   A 1 1119 ? 145.271 149.448 154.893 1.00 45.14  0  1083 GLU   A CA  1 
ATOM   8077  C C   . GLU   A 1 1119 ? 144.357 148.420 155.542 1.00 50.15  0  1083 GLU   A C   1 
ATOM   8078  O O   . GLU   A 1 1119 ? 144.518 148.116 156.728 1.00 55.55  0  1083 GLU   A O   1 
ATOM   8079  C CB  . GLU   A 1 1119 ? 144.716 150.854 155.122 1.00 49.37  0  1083 GLU   A CB  1 
ATOM   8080  C CG  . GLU   A 1 1119 ? 145.450 151.965 154.395 1.00 58.46  0  1083 GLU   A CG  1 
ATOM   8081  C CD  . GLU   A 1 1119 ? 146.788 152.292 155.025 1.00 61.05  0  1083 GLU   A CD  1 
ATOM   8082  O OE1 . GLU   A 1 1119 ? 146.923 152.128 156.256 1.00 61.44  0  1083 GLU   A OE1 1 
ATOM   8083  O OE2 . GLU   A 1 1119 ? 147.704 152.716 154.289 1.00 55.36  -1 1083 GLU   A OE2 1 
ATOM   8084  N N   . VAL   A 1 1120 ? 143.387 147.889 154.797 1.00 53.08  0  1084 VAL   A N   1 
ATOM   8085  C CA  . VAL   A 1 1120 ? 142.540 146.828 155.336 1.00 54.92  0  1084 VAL   A CA  1 
ATOM   8086  C C   . VAL   A 1 1120 ? 143.333 145.533 155.481 1.00 52.36  0  1084 VAL   A C   1 
ATOM   8087  O O   . VAL   A 1 1120 ? 143.250 144.845 156.505 1.00 43.16  0  1084 VAL   A O   1 
ATOM   8088  C CB  . VAL   A 1 1120 ? 141.297 146.631 154.449 1.00 52.27  0  1084 VAL   A CB  1 
ATOM   8089  C CG1 . VAL   A 1 1120 ? 140.556 145.368 154.847 1.00 51.30  0  1084 VAL   A CG1 1 
ATOM   8090  C CG2 . VAL   A 1 1120 ? 140.380 147.835 154.550 1.00 48.99  0  1084 VAL   A CG2 1 
ATOM   8091  N N   . LEU   A 1 1121 ? 144.126 145.193 154.462 1.00 48.14  0  1085 LEU   A N   1 
ATOM   8092  C CA  . LEU   A 1 1121 ? 144.828 143.915 154.443 1.00 50.76  0  1085 LEU   A CA  1 
ATOM   8093  C C   . LEU   A 1 1121 ? 145.987 143.883 155.426 1.00 54.18  0  1085 LEU   A C   1 
ATOM   8094  O O   . LEU   A 1 1121 ? 146.370 142.804 155.889 1.00 56.83  0  1085 LEU   A O   1 
ATOM   8095  C CB  . LEU   A 1 1121 ? 145.339 143.612 153.034 1.00 47.44  0  1085 LEU   A CB  1 
ATOM   8096  C CG  . LEU   A 1 1121 ? 144.322 143.342 151.924 1.00 48.39  0  1085 LEU   A CG  1 
ATOM   8097  C CD1 . LEU   A 1 1121 ? 145.033 143.029 150.621 1.00 47.55  0  1085 LEU   A CD1 1 
ATOM   8098  C CD2 . LEU   A 1 1121 ? 143.386 142.215 152.304 1.00 49.15  0  1085 LEU   A CD2 1 
ATOM   8099  N N   . SER   A 1 1122 ? 146.565 145.041 155.749 1.00 51.10  0  1086 SER   A N   1 
ATOM   8100  C CA  . SER   A 1 1122 ? 147.713 145.065 156.645 1.00 47.08  0  1086 SER   A CA  1 
ATOM   8101  C C   . SER   A 1 1122 ? 147.377 144.545 158.034 1.00 51.30  0  1086 SER   A C   1 
ATOM   8102  O O   . SER   A 1 1122 ? 148.270 144.051 158.730 1.00 54.71  0  1086 SER   A O   1 
ATOM   8103  C CB  . SER   A 1 1122 ? 148.270 146.483 156.739 1.00 46.46  0  1086 SER   A CB  1 
ATOM   8104  O OG  . SER   A 1 1122 ? 147.306 147.366 157.281 1.00 52.15  0  1086 SER   A OG  1 
ATOM   8105  N N   . THR   A 1 1123 ? 146.117 144.634 158.449 1.00 50.87  0  1087 THR   A N   1 
ATOM   8106  C CA  . THR   A 1 1123 ? 145.690 144.170 159.762 1.00 55.22  0  1087 THR   A CA  1 
ATOM   8107  C C   . THR   A 1 1123 ? 145.091 142.771 159.736 1.00 58.91  0  1087 THR   A C   1 
ATOM   8108  O O   . THR   A 1 1123 ? 144.600 142.307 160.768 1.00 56.73  0  1087 THR   A O   1 
ATOM   8109  C CB  . THR   A 1 1123 ? 144.676 145.145 160.363 1.00 52.74  0  1087 THR   A CB  1 
ATOM   8110  O OG1 . THR   A 1 1123 ? 143.540 145.245 159.497 1.00 54.46  0  1087 THR   A OG1 1 
ATOM   8111  C CG2 . THR   A 1 1123 ? 145.301 146.519 160.533 1.00 49.19  0  1087 THR   A CG2 1 
ATOM   8112  N N   . ALA   A 1 1124 ? 145.114 142.095 158.589 1.00 53.74  0  1088 ALA   A N   1 
ATOM   8113  C CA  . ALA   A 1 1124 ? 144.533 140.767 158.495 1.00 45.80  0  1088 ALA   A CA  1 
ATOM   8114  C C   . ALA   A 1 1124 ? 145.326 139.780 159.349 1.00 47.02  0  1088 ALA   A C   1 
ATOM   8115  O O   . ALA   A 1 1124 ? 146.548 139.898 159.477 1.00 51.85  0  1088 ALA   A O   1 
ATOM   8116  C CB  . ALA   A 1 1124 ? 144.506 140.299 157.043 1.00 44.29  0  1088 ALA   A CB  1 
ATOM   8117  N N   . PRO   A 1 1125 ? 144.653 138.804 159.963 1.00 48.89  0  1089 PRO   A N   1 
ATOM   8118  C CA  . PRO   A 1 1125 ? 145.376 137.813 160.775 1.00 48.20  0  1089 PRO   A CA  1 
ATOM   8119  C C   . PRO   A 1 1125 ? 146.360 136.976 159.985 1.00 44.38  0  1089 PRO   A C   1 
ATOM   8120  O O   . PRO   A 1 1125 ? 147.302 136.435 160.576 1.00 45.92  0  1089 PRO   A O   1 
ATOM   8121  C CB  . PRO   A 1 1125 ? 144.250 136.949 161.357 1.00 48.40  0  1089 PRO   A CB  1 
ATOM   8122  C CG  . PRO   A 1 1125 ? 143.044 137.817 161.309 1.00 50.67  0  1089 PRO   A CG  1 
ATOM   8123  C CD  . PRO   A 1 1125 ? 143.195 138.648 160.072 1.00 49.74  0  1089 PRO   A CD  1 
ATOM   8124  N N   . ASN   A 1 1126 ? 146.177 136.849 158.674 1.00 46.37  0  1090 ASN   A N   1 
ATOM   8125  C CA  . ASN   A 1 1126 ? 147.071 136.042 157.854 1.00 49.68  0  1090 ASN   A CA  1 
ATOM   8126  C C   . ASN   A 1 1126 ? 148.385 136.781 157.649 1.00 56.19  0  1090 ASN   A C   1 
ATOM   8127  O O   . ASN   A 1 1126 ? 148.398 137.909 157.146 1.00 63.45  0  1090 ASN   A O   1 
ATOM   8128  C CB  . ASN   A 1 1126 ? 146.424 135.724 156.510 1.00 50.38  0  1090 ASN   A CB  1 
ATOM   8129  C CG  . ASN   A 1 1126 ? 147.118 134.594 155.791 1.00 49.42  0  1090 ASN   A CG  1 
ATOM   8130  O OD1 . ASN   A 1 1126 ? 148.153 134.107 156.239 1.00 51.11  0  1090 ASN   A OD1 1 
ATOM   8131  N ND2 . ASN   A 1 1126 ? 146.555 134.169 154.669 1.00 53.24  0  1090 ASN   A ND2 1 
ATOM   8132  N N   . LYS   A 1 1127 ? 149.492 136.142 158.029 1.00 59.68  0  1091 LYS   A N   1 
ATOM   8133  C CA  . LYS   A 1 1127 ? 150.793 136.782 157.887 1.00 54.43  0  1091 LYS   A CA  1 
ATOM   8134  C C   . LYS   A 1 1127 ? 151.169 136.970 156.426 1.00 50.82  0  1091 LYS   A C   1 
ATOM   8135  O O   . LYS   A 1 1127 ? 151.850 137.940 156.085 1.00 57.64  0  1091 LYS   A O   1 
ATOM   8136  C CB  . LYS   A 1 1127 ? 151.861 135.966 158.611 1.00 55.48  0  1091 LYS   A CB  1 
ATOM   8137  C CG  . LYS   A 1 1127 ? 151.681 135.929 160.116 1.00 59.97  0  1091 LYS   A CG  1 
ATOM   8138  C CD  . LYS   A 1 1127 ? 152.766 135.111 160.791 1.00 59.47  0  1091 LYS   A CD  1 
ATOM   8139  C CE  . LYS   A 1 1127 ? 152.614 135.144 162.303 1.00 59.27  0  1091 LYS   A CE  1 
ATOM   8140  N NZ  . LYS   A 1 1127 ? 151.370 134.459 162.751 1.00 56.63  1  1091 LYS   A NZ  1 
ATOM   8141  N N   . ILE   A 1 1128 ? 150.732 136.063 155.551 1.00 43.93  0  1092 ILE   A N   1 
ATOM   8142  C CA  . ILE   A 1 1128 ? 151.096 136.158 154.141 1.00 43.87  0  1092 ILE   A CA  1 
ATOM   8143  C C   . ILE   A 1 1128 ? 150.532 137.430 153.524 1.00 48.52  0  1092 ILE   A C   1 
ATOM   8144  O O   . ILE   A 1 1128 ? 151.215 138.119 152.759 1.00 56.69  0  1092 ILE   A O   1 
ATOM   8145  C CB  . ILE   A 1 1128 ? 150.624 134.906 153.381 1.00 51.72  0  1092 ILE   A CB  1 
ATOM   8146  C CG1 . ILE   A 1 1128 ? 151.070 133.635 154.105 1.00 53.71  0  1092 ILE   A CG1 1 
ATOM   8147  C CG2 . ILE   A 1 1128 ? 151.145 134.922 151.959 1.00 50.21  0  1092 ILE   A CG2 1 
ATOM   8148  C CD1 . ILE   A 1 1128 ? 152.550 133.563 154.373 1.00 48.36  0  1092 ILE   A CD1 1 
ATOM   8149  N N   . PHE   A 1 1129 ? 149.280 137.758 153.832 1.00 44.74  0  1093 PHE   A N   1 
ATOM   8150  C CA  . PHE   A 1 1129 ? 148.661 138.959 153.287 1.00 49.09  0  1093 PHE   A CA  1 
ATOM   8151  C C   . PHE   A 1 1129 ? 149.064 140.215 154.047 1.00 52.62  0  1093 PHE   A C   1 
ATOM   8152  O O   . PHE   A 1 1129 ? 149.316 141.256 153.431 1.00 55.23  0  1093 PHE   A O   1 
ATOM   8153  C CB  . PHE   A 1 1129 ? 147.137 138.820 153.296 1.00 52.78  0  1093 PHE   A CB  1 
ATOM   8154  C CG  . PHE   A 1 1129 ? 146.615 137.805 152.324 1.00 51.03  0  1093 PHE   A CG  1 
ATOM   8155  C CD1 . PHE   A 1 1129 ? 146.664 138.041 150.963 1.00 51.50  0  1093 PHE   A CD1 1 
ATOM   8156  C CD2 . PHE   A 1 1129 ? 146.070 136.616 152.772 1.00 49.97  0  1093 PHE   A CD2 1 
ATOM   8157  C CE1 . PHE   A 1 1129 ? 146.181 137.110 150.068 1.00 54.02  0  1093 PHE   A CE1 1 
ATOM   8158  C CE2 . PHE   A 1 1129 ? 145.587 135.680 151.883 1.00 49.29  0  1093 PHE   A CE2 1 
ATOM   8159  C CZ  . PHE   A 1 1129 ? 145.642 135.927 150.529 1.00 53.63  0  1093 PHE   A CZ  1 
ATOM   8160  N N   . SER   A 1 1130 ? 149.127 140.142 155.378 1.00 47.85  0  1094 SER   A N   1 
ATOM   8161  C CA  . SER   A 1 1130 ? 149.503 141.313 156.162 1.00 46.74  0  1094 SER   A CA  1 
ATOM   8162  C C   . SER   A 1 1130 ? 150.929 141.751 155.854 1.00 54.19  0  1094 SER   A C   1 
ATOM   8163  O O   . SER   A 1 1130 ? 151.201 142.949 155.721 1.00 56.39  0  1094 SER   A O   1 
ATOM   8164  C CB  . SER   A 1 1130 ? 149.341 141.024 157.652 1.00 45.34  0  1094 SER   A CB  1 
ATOM   8165  O OG  . SER   A 1 1130 ? 150.383 140.190 158.124 1.00 47.42  0  1094 SER   A OG  1 
ATOM   8166  N N   . LYS   A 1 1131 ? 151.855 140.797 155.741 1.00 53.20  0  1095 LYS   A N   1 
ATOM   8167  C CA  . LYS   A 1 1131 ? 153.242 141.138 155.448 1.00 44.42  0  1095 LYS   A CA  1 
ATOM   8168  C C   . LYS   A 1 1131 ? 153.365 141.797 154.083 1.00 44.22  0  1095 LYS   A C   1 
ATOM   8169  O O   . LYS   A 1 1131 ? 154.079 142.792 153.924 1.00 59.04  0  1095 LYS   A O   1 
ATOM   8170  C CB  . LYS   A 1 1131 ? 154.114 139.888 155.523 1.00 42.94  0  1095 LYS   A CB  1 
ATOM   8171  C CG  . LYS   A 1 1131 ? 155.555 140.170 155.891 1.00 50.91  0  1095 LYS   A CG  1 
ATOM   8172  C CD  . LYS   A 1 1131 ? 155.678 140.628 157.333 1.00 53.79  0  1095 LYS   A CD  1 
ATOM   8173  C CE  . LYS   A 1 1131 ? 155.407 139.490 158.300 1.00 53.11  0  1095 LYS   A CE  1 
ATOM   8174  N NZ  . LYS   A 1 1131 ? 155.196 139.983 159.688 1.00 49.72  1  1095 LYS   A NZ  1 
ATOM   8175  N N   . SER   A 1 1132 ? 152.670 141.260 153.084 1.00 43.69  0  1096 SER   A N   1 
ATOM   8176  C CA  . SER   A 1 1132 ? 152.720 141.848 151.754 1.00 51.26  0  1096 SER   A CA  1 
ATOM   8177  C C   . SER   A 1 1132 ? 152.003 143.186 151.675 1.00 51.61  0  1096 SER   A C   1 
ATOM   8178  O O   . SER   A 1 1132 ? 152.333 143.990 150.799 1.00 54.06  0  1096 SER   A O   1 
ATOM   8179  C CB  . SER   A 1 1132 ? 152.124 140.890 150.727 1.00 52.42  0  1096 SER   A CB  1 
ATOM   8180  O OG  . SER   A 1 1132 ? 152.092 141.492 149.447 1.00 48.58  0  1096 SER   A OG  1 
ATOM   8181  N N   . ALA   A 1 1133 ? 151.028 143.438 152.547 1.00 40.43  0  1097 ALA   A N   1 
ATOM   8182  C CA  . ALA   A 1 1133 ? 150.368 144.734 152.576 1.00 40.91  0  1097 ALA   A CA  1 
ATOM   8183  C C   . ALA   A 1 1133 ? 151.158 145.785 153.339 1.00 51.37  0  1097 ALA   A C   1 
ATOM   8184  O O   . ALA   A 1 1133 ? 151.054 146.973 153.018 1.00 55.34  0  1097 ALA   A O   1 
ATOM   8185  C CB  . ALA   A 1 1133 ? 148.973 144.605 153.190 1.00 40.33  0  1097 ALA   A CB  1 
ATOM   8186  N N   . GLN   A 1 1134 ? 151.938 145.379 154.342 1.00 54.05  0  1098 GLN   A N   1 
ATOM   8187  C CA  . GLN   A 1 1134 ? 152.756 146.336 155.077 1.00 48.67  0  1098 GLN   A CA  1 
ATOM   8188  C C   . GLN   A 1 1134 ? 153.861 146.910 154.200 1.00 52.23  0  1098 GLN   A C   1 
ATOM   8189  O O   . GLN   A 1 1134 ? 154.170 148.103 154.284 1.00 56.15  0  1098 GLN   A O   1 
ATOM   8190  C CB  . GLN   A 1 1134 ? 153.348 145.672 156.317 1.00 47.52  0  1098 GLN   A CB  1 
ATOM   8191  C CG  . GLN   A 1 1134 ? 152.346 145.446 157.429 1.00 53.40  0  1098 GLN   A CG  1 
ATOM   8192  C CD  . GLN   A 1 1134 ? 152.852 144.470 158.466 1.00 57.84  0  1098 GLN   A CD  1 
ATOM   8193  O OE1 . GLN   A 1 1134 ? 154.040 144.158 158.511 1.00 56.42  0  1098 GLN   A OE1 1 
ATOM   8194  N NE2 . GLN   A 1 1134 ? 151.951 143.982 159.309 1.00 55.93  0  1098 GLN   A NE2 1 
ATOM   8195  N N   . HIS   A 1 1135 ? 154.464 146.079 153.355 1.00 47.19  0  1099 HIS   A N   1 
ATOM   8196  C CA  . HIS   A 1 1135 ? 155.546 146.495 152.476 1.00 40.22  0  1099 HIS   A CA  1 
ATOM   8197  C C   . HIS   A 1 1135 ? 155.054 146.987 151.127 1.00 36.82  0  1099 HIS   A C   1 
ATOM   8198  O O   . HIS   A 1 1135 ? 155.872 147.217 150.235 1.00 48.71  0  1099 HIS   A O   1 
ATOM   8199  C CB  . HIS   A 1 1135 ? 156.528 145.343 152.258 1.00 43.27  0  1099 HIS   A CB  1 
ATOM   8200  C CG  . HIS   A 1 1135 ? 157.112 144.796 153.520 1.00 50.28  0  1099 HIS   A CG  1 
ATOM   8201  N ND1 . HIS   A 1 1135 ? 157.853 145.564 154.391 1.00 50.83  0  1099 HIS   A ND1 1 
ATOM   8202  C CD2 . HIS   A 1 1135 ? 157.080 143.551 154.050 1.00 49.64  0  1099 HIS   A CD2 1 
ATOM   8203  C CE1 . HIS   A 1 1135 ? 158.242 144.819 155.409 1.00 51.28  0  1099 HIS   A CE1 1 
ATOM   8204  N NE2 . HIS   A 1 1135 ? 157.786 143.594 155.227 1.00 54.38  0  1099 HIS   A NE2 1 
ATOM   8205  N N   . TYR   A 1 1136 ? 153.743 147.141 150.953 1.00 41.15  0  1100 TYR   A N   1 
ATOM   8206  C CA  . TYR   A 1 1136 ? 153.202 147.422 149.628 1.00 41.50  0  1100 TYR   A CA  1 
ATOM   8207  C C   . TYR   A 1 1136 ? 153.685 148.764 149.095 1.00 50.89  0  1100 TYR   A C   1 
ATOM   8208  O O   . TYR   A 1 1136 ? 154.146 148.857 147.952 1.00 56.50  0  1100 TYR   A O   1 
ATOM   8209  C CB  . TYR   A 1 1136 ? 151.679 147.380 149.672 1.00 47.38  0  1100 TYR   A CB  1 
ATOM   8210  C CG  . TYR   A 1 1136 ? 151.040 147.346 148.310 1.00 45.24  0  1100 TYR   A CG  1 
ATOM   8211  C CD1 . TYR   A 1 1136 ? 150.774 148.515 147.618 1.00 44.95  0  1100 TYR   A CD1 1 
ATOM   8212  C CD2 . TYR   A 1 1136 ? 150.700 146.143 147.718 1.00 47.59  0  1100 TYR   A CD2 1 
ATOM   8213  C CE1 . TYR   A 1 1136 ? 150.192 148.486 146.378 1.00 46.28  0  1100 TYR   A CE1 1 
ATOM   8214  C CE2 . TYR   A 1 1136 ? 150.116 146.106 146.477 1.00 47.29  0  1100 TYR   A CE2 1 
ATOM   8215  C CZ  . TYR   A 1 1136 ? 149.865 147.280 145.814 1.00 47.04  0  1100 TYR   A CZ  1 
ATOM   8216  O OH  . TYR   A 1 1136 ? 149.280 147.245 144.577 1.00 54.26  0  1100 TYR   A OH  1 
ATOM   8217  N N   . THR   A 1 1137 ? 153.581 149.822 149.902 1.00 48.65  0  1101 THR   A N   1 
ATOM   8218  C CA  . THR   A 1 1137 ? 153.995 151.140 149.430 1.00 46.32  0  1101 THR   A CA  1 
ATOM   8219  C C   . THR   A 1 1137 ? 155.501 151.206 149.193 1.00 48.63  0  1101 THR   A C   1 
ATOM   8220  O O   . THR   A 1 1137 ? 155.950 151.743 148.174 1.00 47.45  0  1101 THR   A O   1 
ATOM   8221  C CB  . THR   A 1 1137 ? 153.549 152.218 150.419 1.00 45.62  0  1101 THR   A CB  1 
ATOM   8222  O OG1 . THR   A 1 1137 ? 154.117 153.477 150.043 1.00 48.38  0  1101 THR   A OG1 1 
ATOM   8223  C CG2 . THR   A 1 1137 ? 153.957 151.867 151.841 1.00 45.54  0  1101 THR   A CG2 1 
ATOM   8224  N N   . THR   A 1 1138 ? 156.295 150.657 150.115 1.00 47.78  0  1102 THR   A N   1 
ATOM   8225  C CA  . THR   A 1 1138 ? 157.743 150.672 149.945 1.00 50.04  0  1102 THR   A CA  1 
ATOM   8226  C C   . THR   A 1 1138 ? 158.162 149.843 148.739 1.00 44.96  0  1102 THR   A C   1 
ATOM   8227  O O   . THR   A 1 1138 ? 159.073 150.230 147.997 1.00 41.40  0  1102 THR   A O   1 
ATOM   8228  C CB  . THR   A 1 1138 ? 158.423 150.165 151.212 1.00 48.18  0  1102 THR   A CB  1 
ATOM   8229  O OG1 . THR   A 1 1138 ? 158.118 148.778 151.392 1.00 46.86  0  1102 THR   A OG1 1 
ATOM   8230  C CG2 . THR   A 1 1138 ? 157.928 150.937 152.420 1.00 46.64  0  1102 THR   A CG2 1 
ATOM   8231  N N   . THR   A 1 1139 ? 157.512 148.697 148.528 1.00 47.67  0  1103 THR   A N   1 
ATOM   8232  C CA  . THR   A 1 1139 ? 157.793 147.909 147.334 1.00 41.81  0  1103 THR   A CA  1 
ATOM   8233  C C   . THR   A 1 1139 ? 157.401 148.660 146.072 1.00 40.28  0  1103 THR   A C   1 
ATOM   8234  O O   . THR   A 1 1139 ? 158.083 148.544 145.053 1.00 54.81  0  1103 THR   A O   1 
ATOM   8235  C CB  . THR   A 1 1139 ? 157.075 146.564 147.397 1.00 42.30  0  1103 THR   A CB  1 
ATOM   8236  O OG1 . THR   A 1 1139 ? 157.538 145.832 148.535 1.00 49.76  0  1103 THR   A OG1 1 
ATOM   8237  C CG2 . THR   A 1 1139 ? 157.363 145.752 146.159 1.00 44.56  0  1103 THR   A CG2 1 
ATOM   8238  N N   . GLU   A 1 1140 ? 156.320 149.438 146.115 1.00 29.67  0  1104 GLU   A N   1 
ATOM   8239  C CA  . GLU   A 1 1140 ? 155.971 150.255 144.958 1.00 34.75  0  1104 GLU   A CA  1 
ATOM   8240  C C   . GLU   A 1 1140 ? 157.051 151.289 144.667 1.00 47.53  0  1104 GLU   A C   1 
ATOM   8241  O O   . GLU   A 1 1140 ? 157.423 151.500 143.506 1.00 50.08  0  1104 GLU   A O   1 
ATOM   8242  C CB  . GLU   A 1 1140 ? 154.625 150.936 145.186 1.00 39.67  0  1104 GLU   A CB  1 
ATOM   8243  C CG  . GLU   A 1 1140 ? 153.934 151.363 143.910 1.00 41.27  0  1104 GLU   A CG  1 
ATOM   8244  C CD  . GLU   A 1 1140 ? 152.477 151.700 144.127 1.00 50.61  0  1104 GLU   A CD  1 
ATOM   8245  O OE1 . GLU   A 1 1140 ? 152.190 152.618 144.921 1.00 53.71  0  1104 GLU   A OE1 1 
ATOM   8246  O OE2 . GLU   A 1 1140 ? 151.616 151.042 143.509 1.00 51.38  -1 1104 GLU   A OE2 1 
ATOM   8247  N N   . ILE   A 1 1141 ? 157.570 151.943 145.710 1.00 52.29  0  1105 ILE   A N   1 
ATOM   8248  C CA  . ILE   A 1 1141 ? 158.640 152.922 145.506 1.00 49.80  0  1105 ILE   A CA  1 
ATOM   8249  C C   . ILE   A 1 1141 ? 159.884 152.253 144.936 1.00 48.56  0  1105 ILE   A C   1 
ATOM   8250  O O   . ILE   A 1 1141 ? 160.539 152.794 144.038 1.00 46.73  0  1105 ILE   A O   1 
ATOM   8251  C CB  . ILE   A 1 1141 ? 158.960 153.680 146.808 1.00 49.13  0  1105 ILE   A CB  1 
ATOM   8252  C CG1 . ILE   A 1 1141 ? 157.685 154.066 147.550 1.00 45.77  0  1105 ILE   A CG1 1 
ATOM   8253  C CG2 . ILE   A 1 1141 ? 159.792 154.911 146.511 1.00 49.53  0  1105 ILE   A CG2 1 
ATOM   8254  C CD1 . ILE   A 1 1141 ? 157.892 154.303 149.025 1.00 46.72  0  1105 ILE   A CD1 1 
ATOM   8255  N N   . ASP   A 1 1142 ? 160.241 151.077 145.458 1.00 48.54  0  1106 ASP   A N   1 
ATOM   8256  C CA  . ASP   A 1 1142 ? 161.401 150.360 144.934 1.00 46.69  0  1106 ASP   A CA  1 
ATOM   8257  C C   . ASP   A 1 1142 ? 161.186 149.946 143.483 1.00 42.57  0  1106 ASP   A C   1 
ATOM   8258  O O   . ASP   A 1 1142 ? 162.096 150.051 142.654 1.00 43.83  0  1106 ASP   A O   1 
ATOM   8259  C CB  . ASP   A 1 1142 ? 161.700 149.142 145.803 1.00 46.91  0  1106 ASP   A CB  1 
ATOM   8260  C CG  . ASP   A 1 1142 ? 162.198 149.523 147.175 1.00 55.39  0  1106 ASP   A CG  1 
ATOM   8261  O OD1 . ASP   A 1 1142 ? 161.850 150.627 147.643 1.00 55.13  0  1106 ASP   A OD1 1 
ATOM   8262  O OD2 . ASP   A 1 1142 ? 162.941 148.727 147.785 1.00 51.07  -1 1106 ASP   A OD2 1 
ATOM   8263  N N   . LEU   A 1 1143 ? 159.982 149.476 143.159 1.00 42.20  0  1107 LEU   A N   1 
ATOM   8264  C CA  . LEU   A 1 1143 ? 159.666 149.080 141.794 1.00 44.86  0  1107 LEU   A CA  1 
ATOM   8265  C C   . LEU   A 1 1143 ? 159.717 150.267 140.844 1.00 41.97  0  1107 LEU   A C   1 
ATOM   8266  O O   . LEU   A 1 1143 ? 160.042 150.105 139.663 1.00 44.75  0  1107 LEU   A O   1 
ATOM   8267  C CB  . LEU   A 1 1143 ? 158.289 148.417 141.762 1.00 45.13  0  1107 LEU   A CB  1 
ATOM   8268  C CG  . LEU   A 1 1143 ? 157.756 147.886 140.435 1.00 44.08  0  1107 LEU   A CG  1 
ATOM   8269  C CD1 . LEU   A 1 1143 ? 158.467 146.610 140.042 1.00 47.76  0  1107 LEU   A CD1 1 
ATOM   8270  C CD2 . LEU   A 1 1143 ? 156.259 147.660 140.528 1.00 37.99  0  1107 LEU   A CD2 1 
ATOM   8271  N N   . ASN   A 1 1144 ? 159.391 151.464 141.331 1.00 31.34  0  1108 ASN   A N   1 
ATOM   8272  C CA  . ASN   A 1 1144 ? 159.583 152.650 140.508 1.00 43.96  0  1108 ASN   A CA  1 
ATOM   8273  C C   . ASN   A 1 1144 ? 161.062 152.958 140.312 1.00 49.79  0  1108 ASN   A C   1 
ATOM   8274  O O   . ASN   A 1 1144 ? 161.442 153.537 139.288 1.00 51.27  0  1108 ASN   A O   1 
ATOM   8275  C CB  . ASN   A 1 1144 ? 158.867 153.849 141.130 1.00 50.73  0  1108 ASN   A CB  1 
ATOM   8276  C CG  . ASN   A 1 1144 ? 158.882 155.067 140.229 1.00 50.92  0  1108 ASN   A CG  1 
ATOM   8277  O OD1 . ASN   A 1 1144 ? 158.232 155.090 139.186 1.00 47.71  0  1108 ASN   A OD1 1 
ATOM   8278  N ND2 . ASN   A 1 1144 ? 159.627 156.089 140.628 1.00 41.95  0  1108 ASN   A ND2 1 
ATOM   8279  N N   . ASP   A 1 1145 ? 161.909 152.576 141.269 1.00 50.46  0  1109 ASP   A N   1 
ATOM   8280  C CA  . ASP   A 1 1145 ? 163.326 152.911 141.221 1.00 47.59  0  1109 ASP   A CA  1 
ATOM   8281  C C   . ASP   A 1 1145 ? 164.165 151.901 140.452 1.00 50.27  0  1109 ASP   A C   1 
ATOM   8282  O O   . ASP   A 1 1145 ? 165.365 152.135 140.278 1.00 54.38  0  1109 ASP   A O   1 
ATOM   8283  C CB  . ASP   A 1 1145 ? 163.888 153.040 142.639 1.00 49.38  0  1109 ASP   A CB  1 
ATOM   8284  C CG  . ASP   A 1 1145 ? 163.290 154.204 143.400 1.00 57.08  0  1109 ASP   A CG  1 
ATOM   8285  O OD1 . ASP   A 1 1145 ? 162.609 155.041 142.774 1.00 54.68  0  1109 ASP   A OD1 1 
ATOM   8286  O OD2 . ASP   A 1 1145 ? 163.507 154.283 144.627 1.00 58.27  -1 1109 ASP   A OD2 1 
ATOM   8287  N N   . ILE   A 1 1146 ? 163.581 150.794 139.994 1.00 52.51  0  1110 ILE   A N   1 
ATOM   8288  C CA  . ILE   A 1 1146 ? 164.370 149.756 139.334 1.00 50.82  0  1110 ILE   A CA  1 
ATOM   8289  C C   . ILE   A 1 1146 ? 164.842 150.229 137.966 1.00 44.97  0  1110 ILE   A C   1 
ATOM   8290  O O   . ILE   A 1 1146 ? 166.039 150.212 137.661 1.00 43.72  0  1110 ILE   A O   1 
ATOM   8291  C CB  . ILE   A 1 1146 ? 163.564 148.451 139.216 1.00 44.91  0  1110 ILE   A CB  1 
ATOM   8292  C CG1 . ILE   A 1 1146 ? 163.385 147.797 140.580 1.00 45.29  0  1110 ILE   A CG1 1 
ATOM   8293  C CG2 . ILE   A 1 1146 ? 164.262 147.482 138.292 1.00 43.81  0  1110 ILE   A CG2 1 
ATOM   8294  C CD1 . ILE   A 1 1146 ? 162.555 146.545 140.516 1.00 49.73  0  1110 ILE   A CD1 1 
ATOM   8295  N N   . MET   A 1 1147 ? 163.909 150.664 137.123 1.00 43.19  0  1111 MET   A N   1 
ATOM   8296  C CA  . MET   A 1 1147 ? 164.191 150.918 135.718 1.00 46.34  0  1111 MET   A CA  1 
ATOM   8297  C C   . MET   A 1 1147 ? 164.051 152.390 135.350 1.00 50.05  0  1111 MET   A C   1 
ATOM   8298  O O   . MET   A 1 1147 ? 163.638 152.720 134.236 1.00 49.98  0  1111 MET   A O   1 
ATOM   8299  C CB  . MET   A 1 1147 ? 163.279 150.074 134.836 1.00 47.90  0  1111 MET   A CB  1 
ATOM   8300  C CG  . MET   A 1 1147 ? 163.396 148.591 135.076 1.00 48.95  0  1111 MET   A CG  1 
ATOM   8301  S SD  . MET   A 1 1147 ? 164.562 147.875 133.925 1.00 64.36  0  1111 MET   A SD  1 
ATOM   8302  C CE  . MET   A 1 1147 ? 163.585 148.015 132.450 1.00 48.48  0  1111 MET   A CE  1 
ATOM   8303  N N   . GLN   A 1 1148 ? 164.390 153.284 136.273 1.00 49.88  0  1112 GLN   A N   1 
ATOM   8304  C CA  . GLN   A 1 1148 ? 164.290 154.708 135.993 1.00 48.93  0  1112 GLN   A CA  1 
ATOM   8305  C C   . GLN   A 1 1148 ? 165.448 155.224 135.152 1.00 48.58  0  1112 GLN   A C   1 
ATOM   8306  O O   . GLN   A 1 1148 ? 165.347 156.318 134.588 1.00 49.73  0  1112 GLN   A O   1 
ATOM   8307  C CB  . GLN   A 1 1148 ? 164.214 155.486 137.306 1.00 46.33  0  1112 GLN   A CB  1 
ATOM   8308  C CG  . GLN   A 1 1148 ? 165.492 155.437 138.113 1.00 53.60  0  1112 GLN   A CG  1 
ATOM   8309  C CD  . GLN   A 1 1148 ? 165.324 156.008 139.500 1.00 53.02  0  1112 GLN   A CD  1 
ATOM   8310  O OE1 . GLN   A 1 1148 ? 164.644 157.015 139.690 1.00 54.14  0  1112 GLN   A OE1 1 
ATOM   8311  N NE2 . GLN   A 1 1148 ? 165.949 155.370 140.481 1.00 51.87  0  1112 GLN   A NE2 1 
ATOM   8312  N N   . ASN   A 1 1149 ? 166.532 154.458 135.039 1.00 46.75  0  1113 ASN   A N   1 
ATOM   8313  C CA  . ASN   A 1 1149 ? 167.744 154.939 134.392 1.00 45.75  0  1113 ASN   A CA  1 
ATOM   8314  C C   . ASN   A 1 1149 ? 167.825 154.596 132.911 1.00 50.72  0  1113 ASN   A C   1 
ATOM   8315  O O   . ASN   A 1 1149 ? 168.668 155.165 132.209 1.00 56.48  0  1113 ASN   A O   1 
ATOM   8316  C CB  . ASN   A 1 1149 ? 168.973 154.377 135.108 1.00 51.02  0  1113 ASN   A CB  1 
ATOM   8317  C CG  . ASN   A 1 1149 ? 169.043 154.805 136.558 1.00 53.40  0  1113 ASN   A CG  1 
ATOM   8318  O OD1 . ASN   A 1 1149 ? 168.666 155.923 136.905 1.00 48.87  0  1113 ASN   A OD1 1 
ATOM   8319  N ND2 . ASN   A 1 1149 ? 169.525 153.915 137.416 1.00 58.31  0  1113 ASN   A ND2 1 
ATOM   8320  N N   . ILE   A 1 1150 ? 166.981 153.690 132.418 1.00 46.24  0  1114 ILE   A N   1 
ATOM   8321  C CA  . ILE   A 1 1150 ? 166.978 153.370 130.995 1.00 42.16  0  1114 ILE   A CA  1 
ATOM   8322  C C   . ILE   A 1 1150 ? 166.309 154.502 130.230 1.00 46.69  0  1114 ILE   A C   1 
ATOM   8323  O O   . ILE   A 1 1150 ? 165.168 154.881 130.522 1.00 52.29  0  1114 ILE   A O   1 
ATOM   8324  C CB  . ILE   A 1 1150 ? 166.274 152.030 130.743 1.00 38.56  0  1114 ILE   A CB  1 
ATOM   8325  C CG1 . ILE   A 1 1150 ? 167.105 150.877 131.300 1.00 36.05  0  1114 ILE   A CG1 1 
ATOM   8326  C CG2 . ILE   A 1 1150 ? 166.032 151.832 129.264 1.00 41.04  0  1114 ILE   A CG2 1 
ATOM   8327  C CD1 . ILE   A 1 1150 ? 166.746 150.481 132.703 1.00 39.02  0  1114 ILE   A CD1 1 
ATOM   8328  N N   . GLU   A 1 1151 ? 167.017 155.052 129.248 1.00 50.27  0  1115 GLU   A N   1 
ATOM   8329  C CA  . GLU   A 1 1151 ? 166.547 156.270 128.600 1.00 52.46  0  1115 GLU   A CA  1 
ATOM   8330  C C   . GLU   A 1 1151 ? 165.346 156.021 127.689 1.00 56.36  0  1115 GLU   A C   1 
ATOM   8331  O O   . GLU   A 1 1151 ? 164.281 156.604 127.932 1.00 56.28  0  1115 GLU   A O   1 
ATOM   8332  C CB  . GLU   A 1 1151 ? 167.686 156.950 127.831 1.00 51.05  0  1115 GLU   A CB  1 
ATOM   8333  C CG  . GLU   A 1 1151 ? 167.219 157.869 126.708 1.00 53.02  0  1115 GLU   A CG  1 
ATOM   8334  C CD  . GLU   A 1 1151 ? 166.396 159.042 127.205 1.00 56.49  0  1115 GLU   A CD  1 
ATOM   8335  O OE1 . GLU   A 1 1151 ? 166.573 159.454 128.370 1.00 56.69  0  1115 GLU   A OE1 1 
ATOM   8336  O OE2 . GLU   A 1 1151 ? 165.562 159.546 126.426 1.00 55.36  -1 1115 GLU   A OE2 1 
ATOM   8337  N N   . PRO   A 1 1152 ? 165.442 155.182 126.639 1.00 42.71  0  1116 PRO   A N   1 
ATOM   8338  C CA  . PRO   A 1 1152 ? 164.286 155.037 125.747 1.00 33.13  0  1116 PRO   A CA  1 
ATOM   8339  C C   . PRO   A 1 1152 ? 163.224 154.152 126.373 1.00 37.34  0  1116 PRO   A C   1 
ATOM   8340  O O   . PRO   A 1 1152 ? 163.187 152.945 126.126 1.00 50.29  0  1116 PRO   A O   1 
ATOM   8341  C CB  . PRO   A 1 1152 ? 164.889 154.417 124.485 1.00 29.24  0  1116 PRO   A CB  1 
ATOM   8342  C CG  . PRO   A 1 1152 ? 166.044 153.640 124.975 1.00 36.02  0  1116 PRO   A CG  1 
ATOM   8343  C CD  . PRO   A 1 1152 ? 166.520 154.245 126.271 1.00 38.12  0  1116 PRO   A CD  1 
ATOM   8344  N N   . THR   A 1 1153 ? 162.369 154.745 127.201 1.00 29.64  0  1117 THR   A N   1 
ATOM   8345  C CA  . THR   A 1 1153 ? 161.424 153.974 127.998 1.00 30.69  0  1117 THR   A CA  1 
ATOM   8346  C C   . THR   A 1 1153 ? 160.468 153.188 127.109 1.00 36.72  0  1117 THR   A C   1 
ATOM   8347  O O   . THR   A 1 1153 ? 159.777 153.760 126.261 1.00 30.19  0  1117 THR   A O   1 
ATOM   8348  C CB  . THR   A 1 1153 ? 160.646 154.907 128.923 1.00 31.47  0  1117 THR   A CB  1 
ATOM   8349  O OG1 . THR   A 1 1153 ? 161.559 155.573 129.803 1.00 36.56  0  1117 THR   A OG1 1 
ATOM   8350  C CG2 . THR   A 1 1153 ? 159.642 154.127 129.749 1.00 29.89  0  1117 THR   A CG2 1 
ATOM   8351  N N   . TYR   A 1 1154 ? 160.435 151.870 127.311 1.00 34.46  0  1118 TYR   A N   1 
ATOM   8352  C CA  . TYR   A 1 1154 ? 159.498 150.999 126.622 1.00 29.44  0  1118 TYR   A CA  1 
ATOM   8353  C C   . TYR   A 1 1154 ? 158.470 150.522 127.633 1.00 32.49  0  1118 TYR   A C   1 
ATOM   8354  O O   . TYR   A 1 1154 ? 158.789 149.655 128.460 1.00 33.34  0  1118 TYR   A O   1 
ATOM   8355  C CB  . TYR   A 1 1154 ? 160.226 149.811 125.996 1.00 31.88  0  1118 TYR   A CB  1 
ATOM   8356  C CG  . TYR   A 1 1154 ? 159.365 148.949 125.100 1.00 35.51  0  1118 TYR   A CG  1 
ATOM   8357  C CD1 . TYR   A 1 1154 ? 158.327 149.497 124.370 1.00 24.27  0  1118 TYR   A CD1 1 
ATOM   8358  C CD2 . TYR   A 1 1154 ? 159.597 147.587 124.985 1.00 31.49  0  1118 TYR   A CD2 1 
ATOM   8359  C CE1 . TYR   A 1 1154 ? 157.540 148.717 123.555 1.00 28.87  0  1118 TYR   A CE1 1 
ATOM   8360  C CE2 . TYR   A 1 1154 ? 158.816 146.799 124.171 1.00 22.12  0  1118 TYR   A CE2 1 
ATOM   8361  C CZ  . TYR   A 1 1154 ? 157.789 147.370 123.458 1.00 29.41  0  1118 TYR   A CZ  1 
ATOM   8362  O OH  . TYR   A 1 1154 ? 157.003 146.593 122.643 1.00 27.16  0  1118 TYR   A OH  1 
ATOM   8363  N N   . PRO   A 1 1155 ? 157.249 151.062 127.631 1.00 29.74  0  1119 PRO   A N   1 
ATOM   8364  C CA  . PRO   A 1 1155 ? 156.275 150.670 128.660 1.00 24.73  0  1119 PRO   A CA  1 
ATOM   8365  C C   . PRO   A 1 1155 ? 155.928 149.194 128.638 1.00 38.34  0  1119 PRO   A C   1 
ATOM   8366  O O   . PRO   A 1 1155 ? 155.682 148.611 129.700 1.00 37.66  0  1119 PRO   A O   1 
ATOM   8367  C CB  . PRO   A 1 1155 ? 155.057 151.541 128.330 1.00 21.69  0  1119 PRO   A CB  1 
ATOM   8368  C CG  . PRO   A 1 1155 ? 155.602 152.675 127.541 1.00 16.41  0  1119 PRO   A CG  1 
ATOM   8369  C CD  . PRO   A 1 1155 ? 156.713 152.098 126.737 1.00 32.16  0  1119 PRO   A CD  1 
ATOM   8370  N N   . HIS   A 1 1156 ? 155.896 148.568 127.462 1.00 30.11  0  1120 HIS   A N   1 
ATOM   8371  C CA  . HIS   A 1 1156 ? 155.576 147.147 127.400 1.00 24.35  0  1120 HIS   A CA  1 
ATOM   8372  C C   . HIS   A 1 1156 ? 156.715 146.300 127.954 1.00 29.96  0  1120 HIS   A C   1 
ATOM   8373  O O   . HIS   A 1 1156 ? 156.477 145.278 128.607 1.00 43.86  0  1120 HIS   A O   1 
ATOM   8374  C CB  . HIS   A 1 1156 ? 155.241 146.753 125.966 1.00 23.48  0  1120 HIS   A CB  1 
ATOM   8375  C CG  . HIS   A 1 1156 ? 154.029 147.443 125.422 1.00 16.08  0  1120 HIS   A CG  1 
ATOM   8376  N ND1 . HIS   A 1 1156 ? 152.788 147.339 126.010 1.00 25.06  0  1120 HIS   A ND1 1 
ATOM   8377  C CD2 . HIS   A 1 1156 ? 153.868 148.245 124.345 1.00 26.19  0  1120 HIS   A CD2 1 
ATOM   8378  C CE1 . HIS   A 1 1156 ? 151.914 148.048 125.317 1.00 25.31  0  1120 HIS   A CE1 1 
ATOM   8379  N NE2 . HIS   A 1 1156 ? 152.544 148.606 124.301 1.00 17.55  0  1120 HIS   A NE2 1 
ATOM   8380  N N   . GLY   A 1 1157 ? 157.960 146.708 127.714 1.00 24.11  0  1121 GLY   A N   1 
ATOM   8381  C CA  . GLY   A 1 1157 ? 159.072 146.059 128.384 1.00 23.51  0  1121 GLY   A CA  1 
ATOM   8382  C C   . GLY   A 1 1157 ? 159.011 146.227 129.886 1.00 21.00  0  1121 GLY   A C   1 
ATOM   8383  O O   . GLY   A 1 1157 ? 159.359 145.310 130.636 1.00 28.79  0  1121 GLY   A O   1 
ATOM   8384  N N   . LEU   A 1 1158 ? 158.560 147.393 130.349 1.00 23.47  0  1122 LEU   A N   1 
ATOM   8385  C CA  . LEU   A 1 1158 ? 158.326 147.579 131.775 1.00 28.04  0  1122 LEU   A CA  1 
ATOM   8386  C C   . LEU   A 1 1158 ? 157.252 146.625 132.272 1.00 27.68  0  1122 LEU   A C   1 
ATOM   8387  O O   . LEU   A 1 1158 ? 157.347 146.098 133.383 1.00 39.65  0  1122 LEU   A O   1 
ATOM   8388  C CB  . LEU   A 1 1158 ? 157.936 149.028 132.059 1.00 36.46  0  1122 LEU   A CB  1 
ATOM   8389  C CG  . LEU   A 1 1158 ? 158.999 150.094 131.798 1.00 33.50  0  1122 LEU   A CG  1 
ATOM   8390  C CD1 . LEU   A 1 1158 ? 158.428 151.476 132.030 1.00 30.79  0  1122 LEU   A CD1 1 
ATOM   8391  C CD2 . LEU   A 1 1158 ? 160.211 149.859 132.679 1.00 32.33  0  1122 LEU   A CD2 1 
ATOM   8392  N N   . ARG   A 1 1159 ? 156.224 146.383 131.458 1.00 24.78  0  1123 ARG   A N   1 
ATOM   8393  C CA  . ARG   A 1 1159 ? 155.207 145.402 131.822 1.00 26.78  0  1123 ARG   A CA  1 
ATOM   8394  C C   . ARG   A 1 1159 ? 155.807 144.007 131.944 1.00 28.31  0  1123 ARG   A C   1 
ATOM   8395  O O   . ARG   A 1 1159 ? 155.467 143.255 132.865 1.00 30.38  0  1123 ARG   A O   1 
ATOM   8396  C CB  . ARG   A 1 1159 ? 154.078 145.420 130.793 1.00 28.27  0  1123 ARG   A CB  1 
ATOM   8397  C CG  . ARG   A 1 1159 ? 152.987 144.404 131.052 1.00 26.22  0  1123 ARG   A CG  1 
ATOM   8398  C CD  . ARG   A 1 1159 ? 152.325 144.645 132.389 1.00 26.22  0  1123 ARG   A CD  1 
ATOM   8399  N NE  . ARG   A 1 1159 ? 151.109 143.861 132.554 1.00 30.98  0  1123 ARG   A NE  1 
ATOM   8400  C CZ  . ARG   A 1 1159 ? 150.265 144.001 133.566 1.00 36.79  0  1123 ARG   A CZ  1 
ATOM   8401  N NH1 . ARG   A 1 1159 ? 150.473 144.893 134.519 1.00 33.06  1  1123 ARG   A NH1 1 
ATOM   8402  N NH2 . ARG   A 1 1159 ? 149.189 143.224 133.625 1.00 33.02  0  1123 ARG   A NH2 1 
ATOM   8403  N N   . VAL   A 1 1160 ? 156.697 143.643 131.019 1.00 39.89  0  1124 VAL   A N   1 
ATOM   8404  C CA  . VAL   A 1 1160 ? 157.367 142.344 131.099 1.00 35.20  0  1124 VAL   A CA  1 
ATOM   8405  C C   . VAL   A 1 1160 ? 158.160 142.243 132.394 1.00 32.11  0  1124 VAL   A C   1 
ATOM   8406  O O   . VAL   A 1 1160 ? 158.144 141.213 133.076 1.00 31.60  0  1124 VAL   A O   1 
ATOM   8407  C CB  . VAL   A 1 1160 ? 158.274 142.117 129.877 1.00 30.11  0  1124 VAL   A CB  1 
ATOM   8408  C CG1 . VAL   A 1 1160 ? 158.810 140.701 129.888 1.00 28.24  0  1124 VAL   A CG1 1 
ATOM   8409  C CG2 . VAL   A 1 1160 ? 157.527 142.376 128.597 1.00 22.28  0  1124 VAL   A CG2 1 
ATOM   8410  N N   . VAL   A 1 1161 ? 158.878 143.313 132.742 1.00 32.37  0  1125 VAL   A N   1 
ATOM   8411  C CA  . VAL   A 1 1161 ? 159.603 143.344 134.009 1.00 30.92  0  1125 VAL   A CA  1 
ATOM   8412  C C   . VAL   A 1 1161 ? 158.636 143.196 135.172 1.00 38.37  0  1125 VAL   A C   1 
ATOM   8413  O O   . VAL   A 1 1161 ? 158.959 142.573 136.190 1.00 46.01  0  1125 VAL   A O   1 
ATOM   8414  C CB  . VAL   A 1 1161 ? 160.425 144.642 134.126 1.00 28.00  0  1125 VAL   A CB  1 
ATOM   8415  C CG1 . VAL   A 1 1161 ? 161.180 144.677 135.437 1.00 37.80  0  1125 VAL   A CG1 1 
ATOM   8416  C CG2 . VAL   A 1 1161 ? 161.386 144.764 132.972 1.00 25.89  0  1125 VAL   A CG2 1 
ATOM   8417  N N   . TYR   A 1 1162 ? 157.443 143.770 135.042 1.00 35.54  0  1126 TYR   A N   1 
ATOM   8418  C CA  . TYR   A 1 1162 ? 156.451 143.715 136.108 1.00 29.63  0  1126 TYR   A CA  1 
ATOM   8419  C C   . TYR   A 1 1162 ? 155.960 142.293 136.340 1.00 33.77  0  1126 TYR   A C   1 
ATOM   8420  O O   . TYR   A 1 1162 ? 155.950 141.807 137.476 1.00 32.07  0  1126 TYR   A O   1 
ATOM   8421  C CB  . TYR   A 1 1162 ? 155.285 144.635 135.756 1.00 28.18  0  1126 TYR   A CB  1 
ATOM   8422  C CG  . TYR   A 1 1162 ? 154.344 144.891 136.894 1.00 31.65  0  1126 TYR   A CG  1 
ATOM   8423  C CD1 . TYR   A 1 1162 ? 154.801 144.909 138.199 1.00 39.99  0  1126 TYR   A CD1 1 
ATOM   8424  C CD2 . TYR   A 1 1162 ? 152.998 145.123 136.667 1.00 31.51  0  1126 TYR   A CD2 1 
ATOM   8425  C CE1 . TYR   A 1 1162 ? 153.950 145.146 139.242 1.00 38.02  0  1126 TYR   A CE1 1 
ATOM   8426  C CE2 . TYR   A 1 1162 ? 152.138 145.360 137.709 1.00 36.42  0  1126 TYR   A CE2 1 
ATOM   8427  C CZ  . TYR   A 1 1162 ? 152.622 145.371 138.994 1.00 36.48  0  1126 TYR   A CZ  1 
ATOM   8428  O OH  . TYR   A 1 1162 ? 151.781 145.610 140.046 1.00 26.84  0  1126 TYR   A OH  1 
ATOM   8429  N N   . GLU   A 1 1163 ? 155.554 141.605 135.270 1.00 39.36  0  1127 GLU   A N   1 
ATOM   8430  C CA  . GLU   A 1 1163 ? 154.977 140.273 135.412 1.00 31.04  0  1127 GLU   A CA  1 
ATOM   8431  C C   . GLU   A 1 1163 ? 155.994 139.239 135.867 1.00 34.52  0  1127 GLU   A C   1 
ATOM   8432  O O   . GLU   A 1 1163 ? 155.600 138.193 136.392 1.00 42.76  0  1127 GLU   A O   1 
ATOM   8433  C CB  . GLU   A 1 1163 ? 154.348 139.819 134.096 1.00 26.76  0  1127 GLU   A CB  1 
ATOM   8434  C CG  . GLU   A 1 1163 ? 153.544 140.878 133.378 1.00 30.37  0  1127 GLU   A CG  1 
ATOM   8435  C CD  . GLU   A 1 1163 ? 152.725 140.309 132.236 1.00 45.30  0  1127 GLU   A CD  1 
ATOM   8436  O OE1 . GLU   A 1 1163 ? 151.562 139.925 132.470 1.00 44.96  0  1127 GLU   A OE1 1 
ATOM   8437  O OE2 . GLU   A 1 1163 ? 153.243 140.244 131.101 1.00 46.87  -1 1127 GLU   A OE2 1 
ATOM   8438  N N   . SER   A 1 1164 ? 157.282 139.497 135.679 1.00 31.55  0  1128 SER   A N   1 
ATOM   8439  C CA  . SER   A 1 1164 ? 158.326 138.558 136.055 1.00 29.98  0  1128 SER   A CA  1 
ATOM   8440  C C   . SER   A 1 1164 ? 158.740 138.695 137.511 1.00 28.95  0  1128 SER   A C   1 
ATOM   8441  O O   . SER   A 1 1164 ? 159.635 137.973 137.957 1.00 32.68  0  1128 SER   A O   1 
ATOM   8442  C CB  . SER   A 1 1164 ? 159.543 138.737 135.150 1.00 36.96  0  1128 SER   A CB  1 
ATOM   8443  O OG  . SER   A 1 1164 ? 160.278 139.888 135.516 1.00 30.72  0  1128 SER   A OG  1 
ATOM   8444  N N   . LEU   A 1 1165 ? 158.118 139.602 138.252 1.00 30.97  0  1129 LEU   A N   1 
ATOM   8445  C CA  . LEU   A 1 1165 ? 158.388 139.840 139.658 1.00 33.66  0  1129 LEU   A CA  1 
ATOM   8446  C C   . LEU   A 1 1165 ? 157.189 139.424 140.503 1.00 33.18  0  1129 LEU   A C   1 
ATOM   8447  O O   . LEU   A 1 1165 ? 156.052 139.441 140.026 1.00 35.69  0  1129 LEU   A O   1 
ATOM   8448  C CB  . LEU   A 1 1165 ? 158.702 141.319 139.909 1.00 32.24  0  1129 LEU   A CB  1 
ATOM   8449  C CG  . LEU   A 1 1165 ? 159.998 141.835 139.287 1.00 31.46  0  1129 LEU   A CG  1 
ATOM   8450  C CD1 . LEU   A 1 1165 ? 159.990 143.344 139.217 1.00 30.65  0  1129 LEU   A CD1 1 
ATOM   8451  C CD2 . LEU   A 1 1165 ? 161.187 141.350 140.084 1.00 34.24  0  1129 LEU   A CD2 1 
ATOM   8452  N N   . PRO   A 1 1166 ? 157.404 139.036 141.764 1.00 34.79  0  1130 PRO   A N   1 
ATOM   8453  C CA  . PRO   A 1 1166 ? 156.282 138.581 142.595 1.00 37.99  0  1130 PRO   A CA  1 
ATOM   8454  C C   . PRO   A 1 1166 ? 155.285 139.670 142.947 1.00 43.79  0  1130 PRO   A C   1 
ATOM   8455  O O   . PRO   A 1 1166 ? 154.223 139.353 143.493 1.00 50.75  0  1130 PRO   A O   1 
ATOM   8456  C CB  . PRO   A 1 1166 ? 156.978 138.048 143.853 1.00 41.38  0  1130 PRO   A CB  1 
ATOM   8457  C CG  . PRO   A 1 1166 ? 158.265 138.763 143.898 1.00 42.66  0  1130 PRO   A CG  1 
ATOM   8458  C CD  . PRO   A 1 1166 ? 158.687 138.929 142.474 1.00 42.43  0  1130 PRO   A CD  1 
ATOM   8459  N N   . PHE   A 1 1167 ? 155.587 140.938 142.668 1.00 50.26  0  1131 PHE   A N   1 
ATOM   8460  C CA  . PHE   A 1 1167 ? 154.633 142.003 142.945 1.00 46.47  0  1131 PHE   A CA  1 
ATOM   8461  C C   . PHE   A 1 1167 ? 153.401 141.917 142.057 1.00 42.08  0  1131 PHE   A C   1 
ATOM   8462  O O   . PHE   A 1 1167 ? 152.357 142.468 142.416 1.00 47.79  0  1131 PHE   A O   1 
ATOM   8463  C CB  . PHE   A 1 1167 ? 155.306 143.365 142.778 1.00 43.00  0  1131 PHE   A CB  1 
ATOM   8464  C CG  . PHE   A 1 1167 ? 154.517 144.506 143.350 1.00 42.19  0  1131 PHE   A CG  1 
ATOM   8465  C CD1 . PHE   A 1 1167 ? 154.167 144.520 144.685 1.00 41.08  0  1131 PHE   A CD1 1 
ATOM   8466  C CD2 . PHE   A 1 1167 ? 154.135 145.570 142.554 1.00 45.56  0  1131 PHE   A CD2 1 
ATOM   8467  C CE1 . PHE   A 1 1167 ? 153.448 145.566 145.212 1.00 45.65  0  1131 PHE   A CE1 1 
ATOM   8468  C CE2 . PHE   A 1 1167 ? 153.414 146.618 143.077 1.00 43.73  0  1131 PHE   A CE2 1 
ATOM   8469  C CZ  . PHE   A 1 1167 ? 153.071 146.616 144.406 1.00 42.73  0  1131 PHE   A CZ  1 
ATOM   8470  N N   . TYR   A 1 1168 ? 153.495 141.239 140.912 1.00 35.74  0  1132 TYR   A N   1 
ATOM   8471  C CA  . TYR   A 1 1168 ? 152.342 141.107 140.028 1.00 33.20  0  1132 TYR   A CA  1 
ATOM   8472  C C   . TYR   A 1 1168 ? 151.213 140.339 140.700 1.00 41.54  0  1132 TYR   A C   1 
ATOM   8473  O O   . TYR   A 1 1168 ? 150.043 140.723 140.596 1.00 42.05  0  1132 TYR   A O   1 
ATOM   8474  C CB  . TYR   A 1 1168 ? 152.761 140.417 138.733 1.00 37.54  0  1132 TYR   A CB  1 
ATOM   8475  C CG  . TYR   A 1 1168 ? 151.696 140.401 137.666 1.00 41.96  0  1132 TYR   A CG  1 
ATOM   8476  C CD1 . TYR   A 1 1168 ? 151.124 141.577 137.215 1.00 41.15  0  1132 TYR   A CD1 1 
ATOM   8477  C CD2 . TYR   A 1 1168 ? 151.275 139.209 137.098 1.00 42.10  0  1132 TYR   A CD2 1 
ATOM   8478  C CE1 . TYR   A 1 1168 ? 150.158 141.567 136.238 1.00 40.76  0  1132 TYR   A CE1 1 
ATOM   8479  C CE2 . TYR   A 1 1168 ? 150.308 139.190 136.120 1.00 42.97  0  1132 TYR   A CE2 1 
ATOM   8480  C CZ  . TYR   A 1 1168 ? 149.753 140.373 135.693 1.00 44.14  0  1132 TYR   A CZ  1 
ATOM   8481  O OH  . TYR   A 1 1168 ? 148.785 140.364 134.715 1.00 46.29  0  1132 TYR   A OH  1 
ATOM   8482  N N   . LYS   A 1 1169 ? 151.543 139.248 141.393 1.00 54.32  0  1133 LYS   A N   1 
ATOM   8483  C CA  . LYS   A 1 1169 ? 150.525 138.453 142.072 1.00 52.25  0  1133 LYS   A CA  1 
ATOM   8484  C C   . LYS   A 1 1169 ? 149.863 139.238 143.199 1.00 50.35  0  1133 LYS   A C   1 
ATOM   8485  O O   . LYS   A 1 1169 ? 148.636 139.190 143.362 1.00 52.04  0  1133 LYS   A O   1 
ATOM   8486  C CB  . LYS   A 1 1169 ? 151.153 137.168 142.605 1.00 47.74  0  1133 LYS   A CB  1 
ATOM   8487  C CG  . LYS   A 1 1169 ? 150.164 136.122 143.072 1.00 56.49  0  1133 LYS   A CG  1 
ATOM   8488  C CD  . LYS   A 1 1169 ? 150.891 134.832 143.407 1.00 56.69  0  1133 LYS   A CD  1 
ATOM   8489  C CE  . LYS   A 1 1169 ? 149.955 133.785 143.967 1.00 57.01  0  1133 LYS   A CE  1 
ATOM   8490  N NZ  . LYS   A 1 1169 ? 150.703 132.565 144.376 1.00 53.41  1  1133 LYS   A NZ  1 
ATOM   8491  N N   . ALA   A 1 1170 ? 150.658 139.963 143.988 1.00 43.24  0  1134 ALA   A N   1 
ATOM   8492  C CA  . ALA   A 1 1170 ? 150.092 140.789 145.048 1.00 39.00  0  1134 ALA   A CA  1 
ATOM   8493  C C   . ALA   A 1 1170 ? 149.195 141.871 144.473 1.00 40.16  0  1134 ALA   A C   1 
ATOM   8494  O O   . ALA   A 1 1170 ? 148.116 142.147 145.010 1.00 55.98  0  1134 ALA   A O   1 
ATOM   8495  C CB  . ALA   A 1 1170 ? 151.208 141.411 145.883 1.00 44.79  0  1134 ALA   A CB  1 
ATOM   8496  N N   . GLU   A 1 1171 ? 149.622 142.492 143.375 1.00 37.14  0  1135 GLU   A N   1 
ATOM   8497  C CA  . GLU   A 1 1171 ? 148.800 143.511 142.738 1.00 32.51  0  1135 GLU   A CA  1 
ATOM   8498  C C   . GLU   A 1 1171 ? 147.492 142.928 142.232 1.00 35.77  0  1135 GLU   A C   1 
ATOM   8499  O O   . GLU   A 1 1171 ? 146.442 143.562 142.348 1.00 48.17  0  1135 GLU   A O   1 
ATOM   8500  C CB  . GLU   A 1 1171 ? 149.561 144.157 141.588 1.00 46.20  0  1135 GLU   A CB  1 
ATOM   8501  C CG  . GLU   A 1 1171 ? 148.853 145.349 140.995 1.00 43.26  0  1135 GLU   A CG  1 
ATOM   8502  C CD  . GLU   A 1 1171 ? 149.152 146.615 141.754 1.00 49.97  0  1135 GLU   A CD  1 
ATOM   8503  O OE1 . GLU   A 1 1171 ? 150.195 146.658 142.437 1.00 48.84  0  1135 GLU   A OE1 1 
ATOM   8504  O OE2 . GLU   A 1 1171 ? 148.340 147.561 141.684 1.00 55.54  -1 1135 GLU   A OE2 1 
ATOM   8505  N N   . LYS   A 1 1172 ? 147.537 141.733 141.646 1.00 37.81  0  1136 LYS   A N   1 
ATOM   8506  C CA  . LYS   A 1 1172 ? 146.313 141.120 141.142 1.00 42.09  0  1136 LYS   A CA  1 
ATOM   8507  C C   . LYS   A 1 1172 ? 145.356 140.773 142.277 1.00 41.59  0  1136 LYS   A C   1 
ATOM   8508  O O   . LYS   A 1 1172 ? 144.143 140.983 142.157 1.00 43.96  0  1136 LYS   A O   1 
ATOM   8509  C CB  . LYS   A 1 1172 ? 146.651 139.887 140.307 1.00 41.85  0  1136 LYS   A CB  1 
ATOM   8510  C CG  . LYS   A 1 1172 ? 146.911 140.213 138.843 1.00 43.76  0  1136 LYS   A CG  1 
ATOM   8511  C CD  . LYS   A 1 1172 ? 147.203 138.977 138.007 1.00 42.29  0  1136 LYS   A CD  1 
ATOM   8512  C CE  . LYS   A 1 1172 ? 147.873 137.887 138.818 1.00 44.34  0  1136 LYS   A CE  1 
ATOM   8513  N NZ  . LYS   A 1 1172 ? 147.930 136.604 138.070 1.00 45.65  1  1136 LYS   A NZ  1 
ATOM   8514  N N   . ILE   A 1 1173 ? 145.879 140.258 143.391 1.00 39.43  0  1137 ILE   A N   1 
ATOM   8515  C CA  . ILE   A 1 1173 ? 145.021 139.972 144.540 1.00 33.57  0  1137 ILE   A CA  1 
ATOM   8516  C C   . ILE   A 1 1173 ? 144.399 141.257 145.078 1.00 29.31  0  1137 ILE   A C   1 
ATOM   8517  O O   . ILE   A 1 1173 ? 143.199 141.306 145.384 1.00 35.82  0  1137 ILE   A O   1 
ATOM   8518  C CB  . ILE   A 1 1173 ? 145.816 139.226 145.626 1.00 41.25  0  1137 ILE   A CB  1 
ATOM   8519  C CG1 . ILE   A 1 1173 ? 145.955 137.748 145.259 1.00 43.94  0  1137 ILE   A CG1 1 
ATOM   8520  C CG2 . ILE   A 1 1173 ? 145.158 139.383 146.985 1.00 39.31  0  1137 ILE   A CG2 1 
ATOM   8521  C CD1 . ILE   A 1 1173 ? 146.889 136.981 146.160 1.00 38.51  0  1137 ILE   A CD1 1 
ATOM   8522  N N   . VAL   A 1 1174 ? 145.199 142.318 145.192 1.00 34.32  0  1138 VAL   A N   1 
ATOM   8523  C CA  . VAL   A 1 1174 ? 144.693 143.584 145.710 1.00 28.92  0  1138 VAL   A CA  1 
ATOM   8524  C C   . VAL   A 1 1174 ? 143.651 144.177 144.767 1.00 32.86  0  1138 VAL   A C   1 
ATOM   8525  O O   . VAL   A 1 1174 ? 142.643 144.737 145.210 1.00 41.83  0  1138 VAL   A O   1 
ATOM   8526  C CB  . VAL   A 1 1174 ? 145.864 144.550 145.961 1.00 31.53  0  1138 VAL   A CB  1 
ATOM   8527  C CG1 . VAL   A 1 1174 ? 145.373 145.978 146.091 1.00 40.03  0  1138 VAL   A CG1 1 
ATOM   8528  C CG2 . VAL   A 1 1174 ? 146.629 144.131 147.203 1.00 26.88  0  1138 VAL   A CG2 1 
ATOM   8529  N N   . ASN   A 1 1175 ? 143.869 144.063 143.456 1.00 32.74  0  1139 ASN   A N   1 
ATOM   8530  C CA  . ASN   A 1 1175 ? 142.893 144.561 142.495 1.00 28.54  0  1139 ASN   A CA  1 
ATOM   8531  C C   . ASN   A 1 1175 ? 141.602 143.760 142.537 1.00 37.86  0  1139 ASN   A C   1 
ATOM   8532  O O   . ASN   A 1 1175 ? 140.521 144.324 142.340 1.00 43.45  0  1139 ASN   A O   1 
ATOM   8533  C CB  . ASN   A 1 1175 ? 143.476 144.536 141.084 1.00 35.01  0  1139 ASN   A CB  1 
ATOM   8534  C CG  . ASN   A 1 1175 ? 144.631 145.493 140.915 1.00 44.32  0  1139 ASN   A CG  1 
ATOM   8535  O OD1 . ASN   A 1 1175 ? 144.962 146.252 141.824 1.00 41.83  0  1139 ASN   A OD1 1 
ATOM   8536  N ND2 . ASN   A 1 1175 ? 145.253 145.466 139.744 1.00 46.45  0  1139 ASN   A ND2 1 
ATOM   8537  N N   . LEU   A 1 1176 ? 141.692 142.449 142.760 1.00 39.97  0  1140 LEU   A N   1 
ATOM   8538  C CA  . LEU   A 1 1176 ? 140.486 141.644 142.923 1.00 38.99  0  1140 LEU   A CA  1 
ATOM   8539  C C   . LEU   A 1 1176 ? 139.707 142.084 144.155 1.00 36.07  0  1140 LEU   A C   1 
ATOM   8540  O O   . LEU   A 1 1176 ? 138.480 142.229 144.114 1.00 38.05  0  1140 LEU   A O   1 
ATOM   8541  C CB  . LEU   A 1 1176 ? 140.855 140.165 143.017 1.00 40.07  0  1140 LEU   A CB  1 
ATOM   8542  C CG  . LEU   A 1 1176 ? 139.913 139.278 143.829 1.00 39.32  0  1140 LEU   A CG  1 
ATOM   8543  C CD1 . LEU   A 1 1176 ? 138.617 139.035 143.076 1.00 41.03  0  1140 LEU   A CD1 1 
ATOM   8544  C CD2 . LEU   A 1 1176 ? 140.589 137.969 144.171 1.00 42.48  0  1140 LEU   A CD2 1 
ATOM   8545  N N   . ILE   A 1 1177 ? 140.411 142.306 145.267 1.00 36.68  0  1141 ILE   A N   1 
ATOM   8546  C CA  . ILE   A 1 1177 ? 139.744 142.734 146.491 1.00 28.92  0  1141 ILE   A CA  1 
ATOM   8547  C C   . ILE   A 1 1177 ? 139.146 144.128 146.355 1.00 27.94  0  1141 ILE   A C   1 
ATOM   8548  O O   . ILE   A 1 1177 ? 138.077 144.395 146.913 1.00 35.55  0  1141 ILE   A O   1 
ATOM   8549  C CB  . ILE   A 1 1177 ? 140.720 142.653 147.678 1.00 29.55  0  1141 ILE   A CB  1 
ATOM   8550  C CG1 . ILE   A 1 1177 ? 141.116 141.199 147.929 1.00 31.22  0  1141 ILE   A CG1 1 
ATOM   8551  C CG2 . ILE   A 1 1177 ? 140.108 143.244 148.926 1.00 30.59  0  1141 ILE   A CG2 1 
ATOM   8552  C CD1 . ILE   A 1 1177 ? 142.197 141.032 148.957 1.00 31.63  0  1141 ILE   A CD1 1 
ATOM   8553  N N   . SER   A 1 1178 ? 139.793 145.024 145.612 1.00 40.39  0  1142 SER   A N   1 
ATOM   8554  C CA  . SER   A 1 1178 ? 139.317 146.394 145.463 1.00 43.30  0  1142 SER   A CA  1 
ATOM   8555  C C   . SER   A 1 1178 ? 138.066 146.508 144.606 1.00 42.14  0  1142 SER   A C   1 
ATOM   8556  O O   . SER   A 1 1178 ? 137.463 147.585 144.566 1.00 41.24  0  1142 SER   A O   1 
ATOM   8557  C CB  . SER   A 1 1178 ? 140.415 147.276 144.864 1.00 45.16  0  1142 SER   A CB  1 
ATOM   8558  O OG  . SER   A 1 1178 ? 140.631 146.969 143.500 1.00 45.31  0  1142 SER   A OG  1 
ATOM   8559  N N   . GLY   A 1 1179 ? 137.668 145.446 143.912 1.00 41.10  0  1143 GLY   A N   1 
ATOM   8560  C CA  . GLY   A 1 1179 ? 136.465 145.489 143.107 1.00 41.94  0  1143 GLY   A CA  1 
ATOM   8561  C C   . GLY   A 1 1179 ? 135.178 145.256 143.858 1.00 49.21  0  1143 GLY   A C   1 
ATOM   8562  O O   . GLY   A 1 1179 ? 134.098 145.446 143.295 1.00 50.61  0  1143 GLY   A O   1 
ATOM   8563  N N   . THR   A 1 1180 ? 135.265 144.857 145.123 1.00 52.06  0  1144 THR   A N   1 
ATOM   8564  C CA  . THR   A 1 1180 ? 134.079 144.575 145.910 1.00 46.29  0  1144 THR   A CA  1 
ATOM   8565  C C   . THR   A 1 1180 ? 133.484 145.866 146.465 1.00 44.63  0  1144 THR   A C   1 
ATOM   8566  O O   . THR   A 1 1180 ? 134.071 146.947 146.383 1.00 44.14  0  1144 THR   A O   1 
ATOM   8567  C CB  . THR   A 1 1180 ? 134.412 143.624 147.059 1.00 45.93  0  1144 THR   A CB  1 
ATOM   8568  O OG1 . THR   A 1 1180 ? 135.292 144.278 147.979 1.00 48.64  0  1144 THR   A OG1 1 
ATOM   8569  C CG2 . THR   A 1 1180 ? 135.086 142.369 146.537 1.00 43.06  0  1144 THR   A CG2 1 
ATOM   8570  N N   . LYS   A 1 1181 ? 132.289 145.739 147.029 1.00 59.57  0  1145 LYS   A N   1 
ATOM   8571  C CA  . LYS   A 1 1181 ? 131.671 146.817 147.783 1.00 61.38  0  1145 LYS   A CA  1 
ATOM   8572  C C   . LYS   A 1 1181 ? 132.008 146.665 149.259 1.00 61.89  0  1145 LYS   A C   1 
ATOM   8573  O O   . LYS   A 1 1181 ? 132.207 145.554 149.758 1.00 63.75  0  1145 LYS   A O   1 
ATOM   8574  C CB  . LYS   A 1 1181 ? 130.153 146.823 147.590 1.00 59.87  0  1145 LYS   A CB  1 
ATOM   8575  C CG  . LYS   A 1 1181 ? 129.424 145.712 148.335 1.00 59.73  0  1145 LYS   A CG  1 
ATOM   8576  C CD  . LYS   A 1 1181 ? 128.000 146.110 148.681 1.00 56.50  0  1145 LYS   A CD  1 
ATOM   8577  C CE  . LYS   A 1 1181 ? 127.126 146.158 147.443 1.00 56.89  0  1145 LYS   A CE  1 
ATOM   8578  N NZ  . LYS   A 1 1181 ? 125.699 145.900 147.768 1.00 57.55  1  1145 LYS   A NZ  1 
ATOM   8579  N N   . SER   A 1 1182 ? 132.087 147.800 149.953 1.00 61.25  0  1146 SER   A N   1 
ATOM   8580  C CA  . SER   A 1 1182 ? 132.350 147.834 151.391 1.00 65.38  0  1146 SER   A CA  1 
ATOM   8581  C C   . SER   A 1 1182 ? 133.674 147.136 151.720 1.00 61.36  0  1146 SER   A C   1 
ATOM   8582  O O   . SER   A 1 1182 ? 133.721 146.085 152.362 1.00 57.98  0  1146 SER   A O   1 
ATOM   8583  C CB  . SER   A 1 1182 ? 131.186 147.211 152.170 1.00 64.85  0  1146 SER   A CB  1 
ATOM   8584  O OG  . SER   A 1 1182 ? 131.356 147.386 153.564 1.00 67.85  0  1146 SER   A OG  1 
ATOM   8585  N N   . ILE   A 1 1183 ? 134.754 147.752 151.236 1.00 55.65  0  1147 ILE   A N   1 
ATOM   8586  C CA  . ILE   A 1 1183 ? 136.093 147.233 151.508 1.00 59.66  0  1147 ILE   A CA  1 
ATOM   8587  C C   . ILE   A 1 1183 ? 136.356 147.208 153.008 1.00 62.58  0  1147 ILE   A C   1 
ATOM   8588  O O   . ILE   A 1 1183 ? 136.828 146.207 153.559 1.00 68.00  0  1147 ILE   A O   1 
ATOM   8589  C CB  . ILE   A 1 1183 ? 137.153 148.072 150.773 1.00 56.40  0  1147 ILE   A CB  1 
ATOM   8590  C CG1 . ILE   A 1 1183 ? 136.696 148.403 149.354 1.00 55.84  0  1147 ILE   A CG1 1 
ATOM   8591  C CG2 . ILE   A 1 1183 ? 138.482 147.346 150.760 1.00 51.02  0  1147 ILE   A CG2 1 
ATOM   8592  C CD1 . ILE   A 1 1183 ? 136.765 147.242 148.407 1.00 54.35  0  1147 ILE   A CD1 1 
ATOM   8593  N N   . THR   A 1 1184 ? 136.029 148.306 153.692 1.00 56.60  0  1148 THR   A N   1 
ATOM   8594  C CA  . THR   A 1 1184 ? 136.371 148.438 155.104 1.00 55.48  0  1148 THR   A CA  1 
ATOM   8595  C C   . THR   A 1 1184 ? 135.739 147.332 155.937 1.00 57.51  0  1148 THR   A C   1 
ATOM   8596  O O   . THR   A 1 1184 ? 136.378 146.787 156.846 1.00 59.23  0  1148 THR   A O   1 
ATOM   8597  C CB  . THR   A 1 1184 ? 135.933 149.807 155.616 1.00 57.95  0  1148 THR   A CB  1 
ATOM   8598  O OG1 . THR   A 1 1184 ? 136.494 150.828 154.782 1.00 60.43  0  1148 THR   A OG1 1 
ATOM   8599  C CG2 . THR   A 1 1184 ? 136.393 150.012 157.049 1.00 56.30  0  1148 THR   A CG2 1 
ATOM   8600  N N   . ASN   A 1 1185 ? 134.495 146.974 155.636 1.00 60.48  0  1149 ASN   A N   1 
ATOM   8601  C CA  . ASN   A 1 1185 ? 133.789 145.949 156.392 1.00 62.58  0  1149 ASN   A CA  1 
ATOM   8602  C C   . ASN   A 1 1185 ? 134.111 144.537 155.928 1.00 62.10  0  1149 ASN   A C   1 
ATOM   8603  O O   . ASN   A 1 1185 ? 133.410 143.604 156.333 1.00 64.93  0  1149 ASN   A O   1 
ATOM   8604  C CB  . ASN   A 1 1185 ? 132.278 146.177 156.312 1.00 62.01  0  1149 ASN   A CB  1 
ATOM   8605  C CG  . ASN   A 1 1185 ? 131.880 147.584 156.698 1.00 60.90  0  1149 ASN   A CG  1 
ATOM   8606  O OD1 . ASN   A 1 1185 ? 131.989 147.975 157.858 1.00 64.60  0  1149 ASN   A OD1 1 
ATOM   8607  N ND2 . ASN   A 1 1185 ? 131.412 148.353 155.724 1.00 59.53  0  1149 ASN   A ND2 1 
ATOM   8608  N N   . ILE   A 1 1186 ? 135.153 144.357 155.109 1.00 53.65  0  1150 ILE   A N   1 
ATOM   8609  C CA  . ILE   A 1 1186 ? 135.486 143.022 154.616 1.00 54.36  0  1150 ILE   A CA  1 
ATOM   8610  C C   . ILE   A 1 1186 ? 135.723 142.062 155.771 1.00 59.58  0  1150 ILE   A C   1 
ATOM   8611  O O   . ILE   A 1 1186 ? 135.289 140.905 155.726 1.00 60.57  0  1150 ILE   A O   1 
ATOM   8612  C CB  . ILE   A 1 1186 ? 136.699 143.086 153.667 1.00 51.64  0  1150 ILE   A CB  1 
ATOM   8613  C CG1 . ILE   A 1 1186 ? 136.242 143.386 152.242 1.00 53.98  0  1150 ILE   A CG1 1 
ATOM   8614  C CG2 . ILE   A 1 1186 ? 137.486 141.792 153.696 1.00 50.22  0  1150 ILE   A CG2 1 
ATOM   8615  C CD1 . ILE   A 1 1186 ? 137.376 143.594 151.284 1.00 52.97  0  1150 ILE   A CD1 1 
ATOM   8616  N N   . LEU   A 1 1187 ? 136.390 142.519 156.825 1.00 62.13  0  1151 LEU   A N   1 
ATOM   8617  C CA  . LEU   A 1 1187 ? 136.623 141.701 158.005 1.00 62.98  0  1151 LEU   A CA  1 
ATOM   8618  C C   . LEU   A 1 1187 ? 135.636 141.990 159.130 1.00 64.07  0  1151 LEU   A C   1 
ATOM   8619  O O   . LEU   A 1 1187 ? 135.815 141.479 160.239 1.00 66.87  0  1151 LEU   A O   1 
ATOM   8620  C CB  . LEU   A 1 1187 ? 138.053 141.899 158.506 1.00 58.93  0  1151 LEU   A CB  1 
ATOM   8621  C CG  . LEU   A 1 1187 ? 139.151 141.355 157.596 1.00 60.45  0  1151 LEU   A CG  1 
ATOM   8622  C CD1 . LEU   A 1 1187 ? 140.515 141.690 158.160 1.00 60.29  0  1151 LEU   A CD1 1 
ATOM   8623  C CD2 . LEU   A 1 1187 ? 138.993 139.859 157.423 1.00 59.63  0  1151 LEU   A CD2 1 
ATOM   8624  N N   . GLU   A 1 1188 ? 134.605 142.795 158.878 1.00 66.47  0  1152 GLU   A N   1 
ATOM   8625  C CA  . GLU   A 1 1188 ? 133.672 143.189 159.925 1.00 62.55  0  1152 GLU   A CA  1 
ATOM   8626  C C   . GLU   A 1 1188 ? 132.412 142.335 159.966 1.00 64.20  0  1152 GLU   A C   1 
ATOM   8627  O O   . GLU   A 1 1188 ? 131.561 142.560 160.832 1.00 65.79  0  1152 GLU   A O   1 
ATOM   8628  C CB  . GLU   A 1 1188 ? 133.294 144.665 159.766 1.00 61.22  0  1152 GLU   A CB  1 
ATOM   8629  C CG  . GLU   A 1 1188 ? 134.465 145.622 159.927 1.00 66.61  0  1152 GLU   A CG  1 
ATOM   8630  C CD  . GLU   A 1 1188 ? 135.215 145.416 161.229 1.00 66.37  0  1152 GLU   A CD  1 
ATOM   8631  O OE1 . GLU   A 1 1188 ? 134.560 145.325 162.287 1.00 65.22  0  1152 GLU   A OE1 1 
ATOM   8632  O OE2 . GLU   A 1 1188 ? 136.461 145.342 161.194 1.00 67.08  -1 1152 GLU   A OE2 1 
ATOM   8633  N N   . LYS   A 1 1189 ? 132.278 141.361 159.064 1.00 63.44  0  1153 LYS   A N   1 
ATOM   8634  C CA  . LYS   A 1 1189 ? 131.141 140.436 159.050 1.00 63.22  0  1153 LYS   A CA  1 
ATOM   8635  C C   . LYS   A 1 1189 ? 129.810 141.173 158.912 1.00 59.64  0  1153 LYS   A C   1 
ATOM   8636  O O   . LYS   A 1 1189 ? 128.811 140.809 159.533 1.00 56.24  0  1153 LYS   A O   1 
ATOM   8637  C CB  . LYS   A 1 1189 ? 131.137 139.544 160.293 1.00 63.05  0  1153 LYS   A CB  1 
ATOM   8638  C CG  . LYS   A 1 1189 ? 131.924 138.257 160.136 1.00 63.13  0  1153 LYS   A CG  1 
ATOM   8639  C CD  . LYS   A 1 1189 ? 132.043 137.519 161.456 1.00 63.48  0  1153 LYS   A CD  1 
ATOM   8640  C CE  . LYS   A 1 1189 ? 132.533 138.440 162.559 1.00 66.64  0  1153 LYS   A CE  1 
ATOM   8641  N NZ  . LYS   A 1 1189 ? 134.013 138.596 162.542 1.00 64.20  1  1153 LYS   A NZ  1 
ATOM   8642  N N   . THR   A 1 1190 ? 129.795 142.219 158.090 1.00 66.63  0  1154 THR   A N   1 
ATOM   8643  C CA  . THR   A 1 1190 ? 128.572 142.936 157.765 1.00 66.15  0  1154 THR   A CA  1 
ATOM   8644  C C   . THR   A 1 1190 ? 128.420 143.003 156.254 1.00 65.62  0  1154 THR   A C   1 
ATOM   8645  O O   . THR   A 1 1190 ? 129.391 142.887 155.504 1.00 66.95  0  1154 THR   A O   1 
ATOM   8646  C CB  . THR   A 1 1190 ? 128.553 144.364 158.336 1.00 70.93  0  1154 THR   A CB  1 
ATOM   8647  O OG1 . THR   A 1 1190 ? 129.149 145.266 157.397 1.00 67.75  0  1154 THR   A OG1 1 
ATOM   8648  C CG2 . THR   A 1 1190 ? 129.305 144.440 159.654 1.00 70.10  0  1154 THR   A CG2 1 
ATOM   8649  N N   . SER   A 1 1191 ? 127.176 143.185 155.814 1.00 65.42  0  1155 SER   A N   1 
ATOM   8650  C CA  . SER   A 1 1191 ? 126.865 143.379 154.404 1.00 66.29  0  1155 SER   A CA  1 
ATOM   8651  C C   . SER   A 1 1191 ? 126.580 144.839 154.081 1.00 67.85  0  1155 SER   A C   1 
ATOM   8652  O O   . SER   A 1 1191 ? 126.029 145.142 153.019 1.00 66.39  0  1155 SER   A O   1 
ATOM   8653  C CB  . SER   A 1 1191 ? 125.682 142.503 153.995 1.00 64.10  0  1155 SER   A CB  1 
ATOM   8654  O OG  . SER   A 1 1191 ? 125.879 141.160 154.400 1.00 67.17  0  1155 SER   A OG  1 
ATOM   8655  N N   . ALA   A 1 1192 ? 126.944 145.749 154.978 1.00 61.04  0  1156 ALA   A N   1 
ATOM   8656  C CA  . ALA   A 1 1192 ? 126.674 147.167 154.814 1.00 58.04  0  1156 ALA   A CA  1 
ATOM   8657  C C   . ALA   A 1 1192 ? 127.898 147.888 154.270 1.00 58.72  0  1156 ALA   A C   1 
ATOM   8658  O O   . ALA   A 1 1192 ? 129.039 147.501 154.532 1.00 59.85  0  1156 ALA   A O   1 
ATOM   8659  C CB  . ALA   A 1 1192 ? 126.254 147.796 156.141 1.00 56.36  0  1156 ALA   A CB  1 
ATOM   8660  N N   . ILE   A 1 1193 ? 127.647 148.952 153.516 1.00 60.06  0  1157 ILE   A N   1 
ATOM   8661  C CA  . ILE   A 1 1193 ? 128.710 149.758 152.931 1.00 59.36  0  1157 ILE   A CA  1 
ATOM   8662  C C   . ILE   A 1 1193 ? 129.100 150.819 153.952 1.00 62.17  0  1157 ILE   A C   1 
ATOM   8663  O O   . ILE   A 1 1193 ? 128.262 151.611 154.386 1.00 62.13  0  1157 ILE   A O   1 
ATOM   8664  C CB  . ILE   A 1 1193 ? 128.271 150.401 151.613 1.00 60.07  0  1157 ILE   A CB  1 
ATOM   8665  C CG1 . ILE   A 1 1193 ? 127.701 149.353 150.667 1.00 57.86  0  1157 ILE   A CG1 1 
ATOM   8666  C CG2 . ILE   A 1 1193 ? 129.444 151.086 150.950 1.00 62.22  0  1157 ILE   A CG2 1 
ATOM   8667  C CD1 . ILE   A 1 1193 ? 127.063 149.954 149.448 1.00 54.88  0  1157 ILE   A CD1 1 
ATOM   8668  N N   . ASP   A 1 1194 ? 130.373 150.838 154.333 1.00 57.75  0  1158 ASP   A N   1 
ATOM   8669  C CA  . ASP   A 1 1194 ? 130.847 151.838 155.277 1.00 55.78  0  1158 ASP   A CA  1 
ATOM   8670  C C   . ASP   A 1 1194 ? 130.739 153.227 154.666 1.00 57.68  0  1158 ASP   A C   1 
ATOM   8671  O O   . ASP   A 1 1194 ? 130.829 153.403 153.448 1.00 57.27  0  1158 ASP   A O   1 
ATOM   8672  C CB  . ASP   A 1 1194 ? 132.292 151.551 155.678 1.00 59.88  0  1158 ASP   A CB  1 
ATOM   8673  C CG  . ASP   A 1 1194 ? 132.695 152.265 156.948 1.00 62.53  0  1158 ASP   A CG  1 
ATOM   8674  O OD1 . ASP   A 1 1194 ? 132.813 153.508 156.922 1.00 61.34  0  1158 ASP   A OD1 1 
ATOM   8675  O OD2 . ASP   A 1 1194 ? 132.901 151.582 157.974 1.00 65.12  -1 1158 ASP   A OD2 1 
ATOM   8676  N N   . LEU   A 1 1195 ? 130.524 154.225 155.526 1.00 60.49  0  1159 LEU   A N   1 
ATOM   8677  C CA  . LEU   A 1 1195 ? 130.409 155.593 155.036 1.00 61.68  0  1159 LEU   A CA  1 
ATOM   8678  C C   . LEU   A 1 1195 ? 131.720 156.091 154.443 1.00 64.97  0  1159 LEU   A C   1 
ATOM   8679  O O   . LEU   A 1 1195 ? 131.707 156.953 153.557 1.00 66.71  0  1159 LEU   A O   1 
ATOM   8680  C CB  . LEU   A 1 1195 ? 129.943 156.520 156.156 1.00 62.58  0  1159 LEU   A CB  1 
ATOM   8681  C CG  . LEU   A 1 1195 ? 128.461 156.902 156.137 1.00 65.46  0  1159 LEU   A CG  1 
ATOM   8682  C CD1 . LEU   A 1 1195 ? 128.249 158.241 156.821 1.00 64.44  0  1159 LEU   A CD1 1 
ATOM   8683  C CD2 . LEU   A 1 1195 ? 127.921 156.938 154.715 1.00 64.41  0  1159 LEU   A CD2 1 
ATOM   8684  N N   . THR   A 1 1196 ? 132.854 155.565 154.910 1.00 64.07  0  1160 THR   A N   1 
ATOM   8685  C CA  . THR   A 1 1196 ? 134.139 155.949 154.336 1.00 61.75  0  1160 THR   A CA  1 
ATOM   8686  C C   . THR   A 1 1196 ? 134.204 155.590 152.857 1.00 58.69  0  1160 THR   A C   1 
ATOM   8687  O O   . THR   A 1 1196 ? 134.581 156.417 152.019 1.00 58.89  0  1160 THR   A O   1 
ATOM   8688  C CB  . THR   A 1 1196 ? 135.276 155.270 155.099 1.00 60.35  0  1160 THR   A CB  1 
ATOM   8689  O OG1 . THR   A 1 1196 ? 135.192 155.611 156.487 1.00 60.66  0  1160 THR   A OG1 1 
ATOM   8690  C CG2 . THR   A 1 1196 ? 136.618 155.713 154.551 1.00 58.45  0  1160 THR   A CG2 1 
ATOM   8691  N N   . ASP   A 1 1197 ? 133.819 154.358 152.520 1.00 54.98  0  1161 ASP   A N   1 
ATOM   8692  C CA  . ASP   A 1 1197 ? 133.818 153.930 151.126 1.00 57.72  0  1161 ASP   A CA  1 
ATOM   8693  C C   . ASP   A 1 1197 ? 132.801 154.714 150.311 1.00 56.78  0  1161 ASP   A C   1 
ATOM   8694  O O   . ASP   A 1 1197 ? 133.047 155.035 149.143 1.00 55.38  0  1161 ASP   A O   1 
ATOM   8695  C CB  . ASP   A 1 1197 ? 133.534 152.433 151.043 1.00 60.05  0  1161 ASP   A CB  1 
ATOM   8696  C CG  . ASP   A 1 1197 ? 134.337 151.632 152.044 1.00 59.31  0  1161 ASP   A CG  1 
ATOM   8697  O OD1 . ASP   A 1 1197 ? 135.419 152.100 152.456 1.00 53.68  0  1161 ASP   A OD1 1 
ATOM   8698  O OD2 . ASP   A 1 1197 ? 133.887 150.533 152.422 1.00 61.98  -1 1161 ASP   A OD2 1 
ATOM   8699  N N   . ILE   A 1 1198 ? 131.652 155.027 150.910 1.00 57.01  0  1162 ILE   A N   1 
ATOM   8700  C CA  . ILE   A 1 1198 ? 130.628 155.800 150.215 1.00 56.49  0  1162 ILE   A CA  1 
ATOM   8701  C C   . ILE   A 1 1198 ? 131.174 157.169 149.833 1.00 60.49  0  1162 ILE   A C   1 
ATOM   8702  O O   . ILE   A 1 1198 ? 131.050 157.616 148.685 1.00 63.37  0  1162 ILE   A O   1 
ATOM   8703  C CB  . ILE   A 1 1198 ? 129.373 155.924 151.096 1.00 60.79  0  1162 ILE   A CB  1 
ATOM   8704  C CG1 . ILE   A 1 1198 ? 128.642 154.586 151.179 1.00 60.27  0  1162 ILE   A CG1 1 
ATOM   8705  C CG2 . ILE   A 1 1198 ? 128.454 157.009 150.564 1.00 61.04  0  1162 ILE   A CG2 1 
ATOM   8706  C CD1 . ILE   A 1 1198 ? 127.869 154.234 149.951 1.00 57.60  0  1162 ILE   A CD1 1 
ATOM   8707  N N   . ASP   A 1 1199 ? 131.803 157.849 150.795 1.00 61.86  0  1163 ASP   A N   1 
ATOM   8708  C CA  . ASP   A 1 1199 ? 132.367 159.169 150.536 1.00 57.21  0  1163 ASP   A CA  1 
ATOM   8709  C C   . ASP   A 1 1199 ? 133.500 159.097 149.522 1.00 59.72  0  1163 ASP   A C   1 
ATOM   8710  O O   . ASP   A 1 1199 ? 133.612 159.963 148.646 1.00 61.39  0  1163 ASP   A O   1 
ATOM   8711  C CB  . ASP   A 1 1199 ? 132.858 159.793 151.841 1.00 56.98  0  1163 ASP   A CB  1 
ATOM   8712  C CG  . ASP   A 1 1199 ? 131.779 159.850 152.902 1.00 63.19  0  1163 ASP   A CG  1 
ATOM   8713  O OD1 . ASP   A 1 1199 ? 130.588 159.714 152.553 1.00 62.11  0  1163 ASP   A OD1 1 
ATOM   8714  O OD2 . ASP   A 1 1199 ? 132.121 160.025 154.090 1.00 64.20  -1 1163 ASP   A OD2 1 
ATOM   8715  N N   . ARG   A 1 1200 ? 134.353 158.077 149.629 1.00 61.06  0  1164 ARG   A N   1 
ATOM   8716  C CA  . ARG   A 1 1200 ? 135.461 157.940 148.691 1.00 56.69  0  1164 ARG   A CA  1 
ATOM   8717  C C   . ARG   A 1 1200 ? 134.954 157.750 147.269 1.00 53.19  0  1164 ARG   A C   1 
ATOM   8718  O O   . ARG   A 1 1200 ? 135.442 158.393 146.332 1.00 56.38  0  1164 ARG   A O   1 
ATOM   8719  C CB  . ARG   A 1 1200 ? 136.352 156.772 149.106 1.00 50.86  0  1164 ARG   A CB  1 
ATOM   8720  C CG  . ARG   A 1 1200 ? 137.578 156.611 148.243 1.00 49.21  0  1164 ARG   A CG  1 
ATOM   8721  C CD  . ARG   A 1 1200 ? 138.545 155.620 148.847 1.00 51.23  0  1164 ARG   A CD  1 
ATOM   8722  N NE  . ARG   A 1 1200 ? 137.974 154.283 148.918 1.00 49.80  0  1164 ARG   A NE  1 
ATOM   8723  C CZ  . ARG   A 1 1200 ? 137.828 153.594 150.039 1.00 52.27  0  1164 ARG   A CZ  1 
ATOM   8724  N NH1 . ARG   A 1 1200 ? 138.205 154.088 151.205 1.00 58.66  1  1164 ARG   A NH1 1 
ATOM   8725  N NH2 . ARG   A 1 1200 ? 137.294 152.378 149.988 1.00 51.23  0  1164 ARG   A NH2 1 
ATOM   8726  N N   . ALA   A 1 1201 ? 133.960 156.877 147.089 1.00 44.27  0  1165 ALA   A N   1 
ATOM   8727  C CA  . ALA   A 1 1201 ? 133.398 156.661 145.762 1.00 45.18  0  1165 ALA   A CA  1 
ATOM   8728  C C   . ALA   A 1 1201 ? 132.718 157.918 145.239 1.00 53.38  0  1165 ALA   A C   1 
ATOM   8729  O O   . ALA   A 1 1201 ? 132.805 158.229 144.045 1.00 56.77  0  1165 ALA   A O   1 
ATOM   8730  C CB  . ALA   A 1 1201 ? 132.417 155.492 145.793 1.00 48.54  0  1165 ALA   A CB  1 
ATOM   8731  N N   . THR   A 1 1202 ? 132.028 158.653 146.116 1.00 54.83  0  1166 THR   A N   1 
ATOM   8732  C CA  . THR   A 1 1202 ? 131.377 159.887 145.691 1.00 49.08  0  1166 THR   A CA  1 
ATOM   8733  C C   . THR   A 1 1202 ? 132.399 160.899 145.190 1.00 52.94  0  1166 THR   A C   1 
ATOM   8734  O O   . THR   A 1 1202 ? 132.222 161.509 144.128 1.00 52.79  0  1166 THR   A O   1 
ATOM   8735  C CB  . THR   A 1 1202 ? 130.566 160.475 146.843 1.00 54.19  0  1166 THR   A CB  1 
ATOM   8736  O OG1 . THR   A 1 1202 ? 129.702 159.469 147.383 1.00 55.92  0  1166 THR   A OG1 1 
ATOM   8737  C CG2 . THR   A 1 1202 ? 129.733 161.643 146.355 1.00 58.90  0  1166 THR   A CG2 1 
ATOM   8738  N N   . GLU   A 1 1203 ? 133.483 161.085 145.946 1.00 54.42  0  1167 GLU   A N   1 
ATOM   8739  C CA  . GLU   A 1 1203 ? 134.524 162.014 145.521 1.00 54.83  0  1167 GLU   A CA  1 
ATOM   8740  C C   . GLU   A 1 1203 ? 135.174 161.552 144.225 1.00 57.26  0  1167 GLU   A C   1 
ATOM   8741  O O   . GLU   A 1 1203 ? 135.496 162.373 143.358 1.00 60.20  0  1167 GLU   A O   1 
ATOM   8742  C CB  . GLU   A 1 1203 ? 135.570 162.177 146.621 1.00 53.41  0  1167 GLU   A CB  1 
ATOM   8743  C CG  . GLU   A 1 1203 ? 135.008 162.690 147.934 1.00 60.17  0  1167 GLU   A CG  1 
ATOM   8744  C CD  . GLU   A 1 1203 ? 134.036 163.839 147.745 1.00 62.03  0  1167 GLU   A CD  1 
ATOM   8745  O OE1 . GLU   A 1 1203 ? 134.408 164.831 147.082 1.00 61.18  0  1167 GLU   A OE1 1 
ATOM   8746  O OE2 . GLU   A 1 1203 ? 132.902 163.753 148.260 1.00 55.88  -1 1167 GLU   A OE2 1 
ATOM   8747  N N   . MET   A 1 1204 ? 135.383 160.242 144.077 1.00 54.53  0  1168 MET   A N   1 
ATOM   8748  C CA  . MET   A 1 1204 ? 135.931 159.711 142.835 1.00 49.18  0  1168 MET   A CA  1 
ATOM   8749  C C   . MET   A 1 1204 ? 135.045 160.071 141.651 1.00 50.31  0  1168 MET   A C   1 
ATOM   8750  O O   . MET   A 1 1204 ? 135.527 160.546 140.616 1.00 55.76  0  1168 MET   A O   1 
ATOM   8751  C CB  . MET   A 1 1204 ? 136.093 158.195 142.949 1.00 52.91  0  1168 MET   A CB  1 
ATOM   8752  C CG  . MET   A 1 1204 ? 136.245 157.475 141.620 1.00 63.11  0  1168 MET   A CG  1 
ATOM   8753  S SD  . MET   A 1 1204 ? 135.480 155.843 141.621 1.00 73.96  0  1168 MET   A SD  1 
ATOM   8754  C CE  . MET   A 1 1204 ? 136.336 155.073 142.991 1.00 57.01  0  1168 MET   A CE  1 
ATOM   8755  N N   . MET   A 1 1205 ? 133.735 159.859 141.794 1.00 49.42  0  1169 MET   A N   1 
ATOM   8756  C CA  . MET   A 1 1205 ? 132.816 160.161 140.701 1.00 50.98  0  1169 MET   A CA  1 
ATOM   8757  C C   . MET   A 1 1205 ? 132.800 161.650 140.382 1.00 50.57  0  1169 MET   A C   1 
ATOM   8758  O O   . MET   A 1 1205 ? 132.771 162.042 139.209 1.00 49.41  0  1169 MET   A O   1 
ATOM   8759  C CB  . MET   A 1 1205 ? 131.408 159.675 141.043 1.00 52.20  0  1169 MET   A CB  1 
ATOM   8760  C CG  . MET   A 1 1205 ? 131.259 158.168 141.101 1.00 48.00  0  1169 MET   A CG  1 
ATOM   8761  S SD  . MET   A 1 1205 ? 129.745 157.677 141.936 1.00 49.66  0  1169 MET   A SD  1 
ATOM   8762  C CE  . MET   A 1 1205 ? 130.290 156.190 142.761 1.00 48.94  0  1169 MET   A CE  1 
ATOM   8763  N N   . ARG   A 1 1206 ? 132.817 162.499 141.413 1.00 42.21  0  1170 ARG   A N   1 
ATOM   8764  C CA  . ARG   A 1 1206 ? 132.804 163.940 141.174 1.00 45.26  0  1170 ARG   A CA  1 
ATOM   8765  C C   . ARG   A 1 1206 ? 134.077 164.405 140.474 1.00 49.89  0  1170 ARG   A C   1 
ATOM   8766  O O   . ARG   A 1 1206 ? 134.023 165.220 139.542 1.00 55.58  0  1170 ARG   A O   1 
ATOM   8767  C CB  . ARG   A 1 1206 ? 132.609 164.686 142.491 1.00 48.03  0  1170 ARG   A CB  1 
ATOM   8768  C CG  . ARG   A 1 1206 ? 131.327 164.328 143.220 1.00 47.98  0  1170 ARG   A CG  1 
ATOM   8769  C CD  . ARG   A 1 1206 ? 131.184 165.128 144.495 1.00 49.14  0  1170 ARG   A CD  1 
ATOM   8770  N NE  . ARG   A 1 1206 ? 130.624 166.448 144.242 1.00 50.76  0  1170 ARG   A NE  1 
ATOM   8771  C CZ  . ARG   A 1 1206 ? 130.624 167.441 145.118 1.00 52.47  0  1170 ARG   A CZ  1 
ATOM   8772  N NH1 . ARG   A 1 1206 ? 131.168 167.304 146.316 1.00 54.11  1  1170 ARG   A NH1 1 
ATOM   8773  N NH2 . ARG   A 1 1206 ? 130.063 168.600 144.786 1.00 51.92  0  1170 ARG   A NH2 1 
ATOM   8774  N N   . LYS   A 1 1207 ? 135.233 163.901 140.909 1.00 45.22  0  1171 LYS   A N   1 
ATOM   8775  C CA  . LYS   A 1 1207 ? 136.489 164.254 140.261 1.00 41.94  0  1171 LYS   A CA  1 
ATOM   8776  C C   . LYS   A 1 1207 ? 136.494 163.802 138.808 1.00 42.36  0  1171 LYS   A C   1 
ATOM   8777  O O   . LYS   A 1 1207 ? 136.929 164.538 137.915 1.00 43.05  0  1171 LYS   A O   1 
ATOM   8778  C CB  . LYS   A 1 1207 ? 137.662 163.633 141.022 1.00 42.82  0  1171 LYS   A CB  1 
ATOM   8779  C CG  . LYS   A 1 1207 ? 137.951 164.276 142.367 1.00 39.32  0  1171 LYS   A CG  1 
ATOM   8780  C CD  . LYS   A 1 1207 ? 138.852 165.488 142.216 1.00 43.17  0  1171 LYS   A CD  1 
ATOM   8781  C CE  . LYS   A 1 1207 ? 140.046 165.174 141.334 1.00 49.03  0  1171 LYS   A CE  1 
ATOM   8782  N NZ  . LYS   A 1 1207 ? 141.044 166.278 141.314 1.00 45.32  1  1171 LYS   A NZ  1 
ATOM   8783  N N   . ASN   A 1 1208 ? 136.002 162.589 138.550 1.00 41.25  0  1172 ASN   A N   1 
ATOM   8784  C CA  . ASN   A 1 1208 ? 135.954 162.098 137.178 1.00 36.59  0  1172 ASN   A CA  1 
ATOM   8785  C C   . ASN   A 1 1208 ? 135.029 162.951 136.321 1.00 35.46  0  1172 ASN   A C   1 
ATOM   8786  O O   . ASN   A 1 1208 ? 135.322 163.213 135.150 1.00 41.25  0  1172 ASN   A O   1 
ATOM   8787  C CB  . ASN   A 1 1208 ? 135.510 160.639 137.160 1.00 39.67  0  1172 ASN   A CB  1 
ATOM   8788  C CG  . ASN   A 1 1208 ? 136.478 159.734 137.876 1.00 40.37  0  1172 ASN   A CG  1 
ATOM   8789  O OD1 . ASN   A 1 1208 ? 137.572 160.152 138.248 1.00 35.88  0  1172 ASN   A OD1 1 
ATOM   8790  N ND2 . ASN   A 1 1208 ? 136.081 158.485 138.080 1.00 47.15  0  1172 ASN   A ND2 1 
ATOM   8791  N N   . ILE   A 1 1209 ? 133.901 163.386 136.884 1.00 33.24  0  1173 ILE   A N   1 
ATOM   8792  C CA  . ILE   A 1 1209 ? 132.965 164.209 136.124 1.00 30.36  0  1173 ILE   A CA  1 
ATOM   8793  C C   . ILE   A 1 1209 ? 133.591 165.555 135.779 1.00 34.88  0  1173 ILE   A C   1 
ATOM   8794  O O   . ILE   A 1 1209 ? 133.475 166.036 134.645 1.00 30.80  0  1173 ILE   A O   1 
ATOM   8795  C CB  . ILE   A 1 1209 ? 131.648 164.375 136.905 1.00 40.64  0  1173 ILE   A CB  1 
ATOM   8796  C CG1 . ILE   A 1 1209 ? 130.750 163.158 136.699 1.00 42.83  0  1173 ILE   A CG1 1 
ATOM   8797  C CG2 . ILE   A 1 1209 ? 130.920 165.620 136.458 1.00 45.32  0  1173 ILE   A CG2 1 
ATOM   8798  C CD1 . ILE   A 1 1209 ? 129.327 163.375 137.136 1.00 42.08  0  1173 ILE   A CD1 1 
ATOM   8799  N N   . THR   A 1 1210 ? 134.273 166.177 136.740 1.00 44.88  0  1174 THR   A N   1 
ATOM   8800  C CA  . THR   A 1 1210 ? 134.879 167.491 136.537 1.00 37.23  0  1174 THR   A CA  1 
ATOM   8801  C C   . THR   A 1 1210 ? 136.246 167.423 135.858 1.00 38.26  0  1174 THR   A C   1 
ATOM   8802  O O   . THR   A 1 1210 ? 136.879 168.468 135.633 1.00 40.92  0  1174 THR   A O   1 
ATOM   8803  C CB  . THR   A 1 1210 ? 134.990 168.215 137.878 1.00 41.32  0  1174 THR   A CB  1 
ATOM   8804  O OG1 . THR   A 1 1210 ? 135.290 167.264 138.906 1.00 44.87  0  1174 THR   A OG1 1 
ATOM   8805  C CG2 . THR   A 1 1210 ? 133.679 168.898 138.213 1.00 34.71  0  1174 THR   A CG2 1 
ATOM   8806  N N   . LEU   A 1 1211 ? 136.721 166.217 135.542 1.00 35.52  0  1175 LEU   A N   1 
ATOM   8807  C CA  . LEU   A 1 1211 ? 137.936 166.084 134.748 1.00 29.49  0  1175 LEU   A CA  1 
ATOM   8808  C C   . LEU   A 1 1211 ? 137.844 166.839 133.431 1.00 20.32  0  1175 LEU   A C   1 
ATOM   8809  O O   . LEU   A 1 1211 ? 138.861 167.309 132.919 1.00 22.81  0  1175 LEU   A O   1 
ATOM   8810  C CB  . LEU   A 1 1211 ? 138.224 164.609 134.479 1.00 33.81  0  1175 LEU   A CB  1 
ATOM   8811  C CG  . LEU   A 1 1211 ? 139.484 164.314 133.671 1.00 34.92  0  1175 LEU   A CG  1 
ATOM   8812  C CD1 . LEU   A 1 1211 ? 140.712 164.495 134.537 1.00 36.15  0  1175 LEU   A CD1 1 
ATOM   8813  C CD2 . LEU   A 1 1211 ? 139.433 162.919 133.088 1.00 31.93  0  1175 LEU   A CD2 1 
ATOM   8814  N N   . LEU   A 1 1212 ? 136.649 166.969 132.863 1.00 23.01  0  1176 LEU   A N   1 
ATOM   8815  C CA  . LEU   A 1 1212 ? 136.522 167.690 131.604 1.00 25.80  0  1176 LEU   A CA  1 
ATOM   8816  C C   . LEU   A 1 1212 ? 136.736 169.190 131.756 1.00 29.32  0  1176 LEU   A C   1 
ATOM   8817  O O   . LEU   A 1 1212 ? 137.238 169.824 130.824 1.00 31.10  0  1176 LEU   A O   1 
ATOM   8818  C CB  . LEU   A 1 1212 ? 135.158 167.422 130.971 1.00 34.60  0  1176 LEU   A CB  1 
ATOM   8819  C CG  . LEU   A 1 1212 ? 134.987 167.901 129.529 1.00 32.57  0  1176 LEU   A CG  1 
ATOM   8820  C CD1 . LEU   A 1 1212 ? 136.193 167.540 128.688 1.00 30.46  0  1176 LEU   A CD1 1 
ATOM   8821  C CD2 . LEU   A 1 1212 ? 133.736 167.300 128.932 1.00 28.92  0  1176 LEU   A CD2 1 
ATOM   8822  N N   . ILE   A 1 1213 ? 136.359 169.779 132.891 1.00 40.77  0  1177 ILE   A N   1 
ATOM   8823  C CA  . ILE   A 1 1213 ? 136.675 171.185 133.116 1.00 35.35  0  1177 ILE   A CA  1 
ATOM   8824  C C   . ILE   A 1 1213 ? 138.122 171.368 133.550 1.00 34.07  0  1177 ILE   A C   1 
ATOM   8825  O O   . ILE   A 1 1213 ? 138.681 172.458 133.361 1.00 34.62  0  1177 ILE   A O   1 
ATOM   8826  C CB  . ILE   A 1 1213 ? 135.737 171.836 134.150 1.00 34.71  0  1177 ILE   A CB  1 
ATOM   8827  C CG1 . ILE   A 1 1213 ? 136.132 171.458 135.574 1.00 33.81  0  1177 ILE   A CG1 1 
ATOM   8828  C CG2 . ILE   A 1 1213 ? 134.307 171.421 133.904 1.00 40.72  0  1177 ILE   A CG2 1 
ATOM   8829  C CD1 . ILE   A 1 1213 ? 135.288 172.119 136.629 1.00 37.04  0  1177 ILE   A CD1 1 
ATOM   8830  N N   . ARG   A 1 1214 ? 138.744 170.339 134.131 1.00 45.01  0  1178 ARG   A N   1 
ATOM   8831  C CA  . ARG   A 1 1214 ? 140.169 170.446 134.439 1.00 41.04  0  1178 ARG   A CA  1 
ATOM   8832  C C   . ARG   A 1 1214 ? 141.025 170.314 133.182 1.00 44.30  0  1178 ARG   A C   1 
ATOM   8833  O O   . ARG   A 1 1214 ? 142.071 170.962 133.065 1.00 40.56  0  1178 ARG   A O   1 
ATOM   8834  C CB  . ARG   A 1 1214 ? 140.574 169.397 135.469 1.00 36.24  0  1178 ARG   A CB  1 
ATOM   8835  C CG  . ARG   A 1 1214 ? 140.200 169.763 136.883 1.00 40.81  0  1178 ARG   A CG  1 
ATOM   8836  C CD  . ARG   A 1 1214 ? 139.576 168.587 137.598 1.00 46.97  0  1178 ARG   A CD  1 
ATOM   8837  N NE  . ARG   A 1 1214 ? 140.529 167.495 137.750 1.00 50.97  0  1178 ARG   A NE  1 
ATOM   8838  C CZ  . ARG   A 1 1214 ? 140.200 166.252 138.071 1.00 47.72  0  1178 ARG   A CZ  1 
ATOM   8839  N NH1 . ARG   A 1 1214 ? 138.941 165.901 138.270 1.00 42.70  1  1178 ARG   A NH1 1 
ATOM   8840  N NH2 . ARG   A 1 1214 ? 141.158 165.339 138.196 1.00 44.69  0  1178 ARG   A NH2 1 
ATOM   8841  N N   . ILE   A 1 1215 ? 140.597 169.478 132.233 1.00 46.36  0  1179 ILE   A N   1 
ATOM   8842  C CA  . ILE   A 1 1215 ? 141.381 169.208 131.031 1.00 30.07  0  1179 ILE   A CA  1 
ATOM   8843  C C   . ILE   A 1 1215 ? 141.433 170.427 130.120 1.00 31.40  0  1179 ILE   A C   1 
ATOM   8844  O O   . ILE   A 1 1215 ? 142.469 170.707 129.508 1.00 40.24  0  1179 ILE   A O   1 
ATOM   8845  C CB  . ILE   A 1 1215 ? 140.811 167.977 130.299 1.00 30.44  0  1179 ILE   A CB  1 
ATOM   8846  C CG1 . ILE   A 1 1215 ? 141.231 166.685 130.998 1.00 31.00  0  1179 ILE   A CG1 1 
ATOM   8847  C CG2 . ILE   A 1 1215 ? 141.254 167.944 128.852 1.00 26.41  0  1179 ILE   A CG2 1 
ATOM   8848  C CD1 . ILE   A 1 1215 ? 142.678 166.346 130.839 1.00 32.41  0  1179 ILE   A CD1 1 
ATOM   8849  N N   . LEU   A 1 1216 ? 140.338 171.182 130.022 1.00 31.50  0  1180 LEU   A N   1 
ATOM   8850  C CA  . LEU   A 1 1216 ? 140.216 172.291 129.077 1.00 32.28  0  1180 LEU   A CA  1 
ATOM   8851  C C   . LEU   A 1 1216 ? 139.927 173.588 129.826 1.00 40.94  0  1180 LEU   A C   1 
ATOM   8852  O O   . LEU   A 1 1216 ? 138.779 174.050 129.860 1.00 54.28  0  1180 LEU   A O   1 
ATOM   8853  C CB  . LEU   A 1 1216 ? 139.112 172.024 128.057 1.00 24.46  0  1180 LEU   A CB  1 
ATOM   8854  C CG  . LEU   A 1 1216 ? 139.066 170.665 127.372 1.00 36.92  0  1180 LEU   A CG  1 
ATOM   8855  C CD1 . LEU   A 1 1216 ? 137.796 170.552 126.554 1.00 34.60  0  1180 LEU   A CD1 1 
ATOM   8856  C CD2 . LEU   A 1 1216 ? 140.279 170.487 126.494 1.00 44.09  0  1180 LEU   A CD2 1 
ATOM   8857  N N   . PRO   A 1 1217 ? 140.943 174.207 130.424 1.00 39.63  0  1181 PRO   A N   1 
ATOM   8858  C CA  . PRO   A 1 1217 ? 140.716 175.477 131.118 1.00 44.36  0  1181 PRO   A CA  1 
ATOM   8859  C C   . PRO   A 1 1217 ? 140.310 176.569 130.140 1.00 46.44  0  1181 PRO   A C   1 
ATOM   8860  O O   . PRO   A 1 1217 ? 140.687 176.553 128.967 1.00 41.92  0  1181 PRO   A O   1 
ATOM   8861  C CB  . PRO   A 1 1217 ? 142.071 175.777 131.768 1.00 45.17  0  1181 PRO   A CB  1 
ATOM   8862  C CG  . PRO   A 1 1217 ? 142.792 174.470 131.781 1.00 38.20  0  1181 PRO   A CG  1 
ATOM   8863  C CD  . PRO   A 1 1217 ? 142.340 173.766 130.547 1.00 40.07  0  1181 PRO   A CD  1 
ATOM   8864  N N   . LEU   A 1 1218 ? 139.523 177.524 130.640 1.00 47.08  0  1182 LEU   A N   1 
ATOM   8865  C CA  . LEU   A 1 1218 ? 138.986 178.576 129.783 1.00 47.85  0  1182 LEU   A CA  1 
ATOM   8866  C C   . LEU   A 1 1218 ? 140.070 179.476 129.207 1.00 54.38  0  1182 LEU   A C   1 
ATOM   8867  O O   . LEU   A 1 1218 ? 139.853 180.087 128.156 1.00 55.26  0  1182 LEU   A O   1 
ATOM   8868  C CB  . LEU   A 1 1218 ? 137.982 179.434 130.556 1.00 52.61  0  1182 LEU   A CB  1 
ATOM   8869  C CG  . LEU   A 1 1218 ? 136.559 178.919 130.796 1.00 55.90  0  1182 LEU   A CG  1 
ATOM   8870  C CD1 . LEU   A 1 1218 ? 135.927 178.438 129.504 1.00 53.23  0  1182 LEU   A CD1 1 
ATOM   8871  C CD2 . LEU   A 1 1218 ? 136.529 177.837 131.857 1.00 49.69  0  1182 LEU   A CD2 1 
ATOM   8872  N N   . ASP   A 1 1219 ? 141.224 179.574 129.868 1.00 56.88  0  1183 ASP   A N   1 
ATOM   8873  C CA  . ASP   A 1 1219 ? 142.280 180.504 129.485 1.00 56.08  0  1183 ASP   A CA  1 
ATOM   8874  C C   . ASP   A 1 1219 ? 143.432 179.811 128.762 1.00 55.40  0  1183 ASP   A C   1 
ATOM   8875  O O   . ASP   A 1 1219 ? 144.585 180.234 128.872 1.00 51.92  0  1183 ASP   A O   1 
ATOM   8876  C CB  . ASP   A 1 1219 ? 142.794 181.250 130.714 1.00 56.03  0  1183 ASP   A CB  1 
ATOM   8877  C CG  . ASP   A 1 1219 ? 142.992 180.336 131.906 1.00 55.57  0  1183 ASP   A CG  1 
ATOM   8878  O OD1 . ASP   A 1 1219 ? 142.676 179.135 131.791 1.00 54.92  0  1183 ASP   A OD1 1 
ATOM   8879  O OD2 . ASP   A 1 1219 ? 143.460 180.817 132.958 1.00 53.38  -1 1183 ASP   A OD2 1 
ATOM   8880  N N   . CYS   A 1 1220 ? 143.138 178.749 128.020 1.00 51.93  0  1184 CYS   A N   1 
ATOM   8881  C CA  . CYS   A 1 1220 ? 144.163 178.047 127.258 1.00 53.23  0  1184 CYS   A CA  1 
ATOM   8882  C C   . CYS   A 1 1220 ? 143.651 177.688 125.867 1.00 52.14  0  1184 CYS   A C   1 
ATOM   8883  O O   . CYS   A 1 1220 ? 142.780 178.365 125.323 1.00 51.35  0  1184 CYS   A O   1 
ATOM   8884  C CB  . CYS   A 1 1220 ? 144.619 176.799 127.999 1.00 50.18  0  1184 CYS   A CB  1 
ATOM   8885  N N   . GLU   A 1 1226 ? 149.551 181.819 122.369 1.00 77.40  0  1190 GLU   A N   1 
ATOM   8886  C CA  . GLU   A 1 1226 ? 150.010 180.696 121.561 1.00 77.00  0  1190 GLU   A CA  1 
ATOM   8887  C C   . GLU   A 1 1226 ? 148.858 179.755 121.233 1.00 78.89  0  1190 GLU   A C   1 
ATOM   8888  O O   . GLU   A 1 1226 ? 148.153 179.290 122.127 1.00 78.68  0  1190 GLU   A O   1 
ATOM   8889  C CB  . GLU   A 1 1226 ? 151.121 179.945 122.277 1.00 73.79  0  1190 GLU   A CB  1 
ATOM   8890  N N   . ILE   A 1 1227 ? 148.668 179.483 119.945 1.00 75.10  0  1191 ILE   A N   1 
ATOM   8891  C CA  . ILE   A 1 1227 ? 147.631 178.572 119.477 1.00 73.03  0  1191 ILE   A CA  1 
ATOM   8892  C C   . ILE   A 1 1227 ? 148.261 177.590 118.501 1.00 70.48  0  1191 ILE   A C   1 
ATOM   8893  O O   . ILE   A 1 1227 ? 148.988 177.994 117.588 1.00 70.52  0  1191 ILE   A O   1 
ATOM   8894  C CB  . ILE   A 1 1227 ? 146.457 179.326 118.820 1.00 72.58  0  1191 ILE   A CB  1 
ATOM   8895  C CG1 . ILE   A 1 1227 ? 145.509 179.863 119.894 1.00 70.43  0  1191 ILE   A CG1 1 
ATOM   8896  C CG2 . ILE   A 1 1227 ? 145.705 178.428 117.852 1.00 70.65  0  1191 ILE   A CG2 1 
ATOM   8897  C CD1 . ILE   A 1 1227 ? 144.905 178.785 120.767 1.00 66.56  0  1191 ILE   A CD1 1 
ATOM   8898  N N   . LEU   A 1 1228 ? 147.992 176.303 118.705 1.00 67.54  0  1192 LEU   A N   1 
ATOM   8899  C CA  . LEU   A 1 1228 ? 148.510 175.267 117.823 1.00 69.56  0  1192 LEU   A CA  1 
ATOM   8900  C C   . LEU   A 1 1228 ? 148.036 175.496 116.392 1.00 70.89  0  1192 LEU   A C   1 
ATOM   8901  O O   . LEU   A 1 1228 ? 146.879 175.849 116.152 1.00 69.29  0  1192 LEU   A O   1 
ATOM   8902  C CB  . LEU   A 1 1228 ? 148.062 173.894 118.325 1.00 67.00  0  1192 LEU   A CB  1 
ATOM   8903  C CG  . LEU   A 1 1228 ? 148.456 172.639 117.552 1.00 66.24  0  1192 LEU   A CG  1 
ATOM   8904  C CD1 . LEU   A 1 1228 ? 148.832 171.543 118.522 1.00 64.68  0  1192 LEU   A CD1 1 
ATOM   8905  C CD2 . LEU   A 1 1228 ? 147.313 172.183 116.667 1.00 65.15  0  1192 LEU   A CD2 1 
ATOM   8906  N N   . SER   A 1 1229 ? 148.941 175.297 115.438 1.00 80.48  0  1193 SER   A N   1 
ATOM   8907  C CA  . SER   A 1 1229 ? 148.661 175.511 114.024 1.00 80.43  0  1193 SER   A CA  1 
ATOM   8908  C C   . SER   A 1 1229 ? 148.514 174.168 113.324 1.00 79.15  0  1193 SER   A C   1 
ATOM   8909  O O   . SER   A 1 1229 ? 149.388 173.304 113.444 1.00 77.77  0  1193 SER   A O   1 
ATOM   8910  C CB  . SER   A 1 1229 ? 149.772 176.333 113.367 1.00 81.76  0  1193 SER   A CB  1 
ATOM   8911  O OG  . SER   A 1 1229 ? 149.578 176.422 111.966 1.00 83.30  0  1193 SER   A OG  1 
ATOM   8912  N N   . MET   A 1 1230 ? 147.420 174.006 112.578 1.00 77.07  0  1194 MET   A N   1 
ATOM   8913  C CA  . MET   A 1 1230 ? 147.110 172.736 111.933 1.00 77.84  0  1194 MET   A CA  1 
ATOM   8914  C C   . MET   A 1 1230 ? 147.898 172.498 110.654 1.00 81.25  0  1194 MET   A C   1 
ATOM   8915  O O   . MET   A 1 1230 ? 147.808 171.402 110.090 1.00 81.86  0  1194 MET   A O   1 
ATOM   8916  C CB  . MET   A 1 1230 ? 145.617 172.651 111.617 1.00 78.69  0  1194 MET   A CB  1 
ATOM   8917  C CG  . MET   A 1 1230 ? 144.726 173.242 112.685 1.00 80.26  0  1194 MET   A CG  1 
ATOM   8918  S SD  . MET   A 1 1230 ? 144.416 172.086 114.029 1.00 90.29  0  1194 MET   A SD  1 
ATOM   8919  C CE  . MET   A 1 1230 ? 142.811 171.458 113.555 1.00 77.64  0  1194 MET   A CE  1 
ATOM   8920  N N   . GLU   A 1 1231 ? 148.654 173.482 110.177 1.00 76.55  0  1195 GLU   A N   1 
ATOM   8921  C CA  . GLU   A 1 1231 ? 149.441 173.299 108.966 1.00 73.83  0  1195 GLU   A CA  1 
ATOM   8922  C C   . GLU   A 1 1231 ? 150.530 172.264 109.218 1.00 75.56  0  1195 GLU   A C   1 
ATOM   8923  O O   . GLU   A 1 1231 ? 151.379 172.449 110.096 1.00 77.89  0  1195 GLU   A O   1 
ATOM   8924  C CB  . GLU   A 1 1231 ? 150.048 174.628 108.525 1.00 76.55  0  1195 GLU   A CB  1 
ATOM   8925  C CG  . GLU   A 1 1231 ? 150.997 174.526 107.343 1.00 80.55  0  1195 GLU   A CG  1 
ATOM   8926  C CD  . GLU   A 1 1231 ? 152.452 174.551 107.763 1.00 79.34  0  1195 GLU   A CD  1 
ATOM   8927  O OE1 . GLU   A 1 1231 ? 152.768 175.200 108.782 1.00 78.01  0  1195 GLU   A OE1 1 
ATOM   8928  O OE2 . GLU   A 1 1231 ? 153.282 173.927 107.070 1.00 76.88  -1 1195 GLU   A OE2 1 
ATOM   8929  N N   . ASN   A 1 1232 ? 150.498 171.174 108.450 1.00 72.49  0  1196 ASN   A N   1 
ATOM   8930  C CA  . ASN   A 1 1232 ? 151.442 170.065 108.588 1.00 75.32  0  1196 ASN   A CA  1 
ATOM   8931  C C   . ASN   A 1 1232 ? 151.418 169.497 110.009 1.00 73.30  0  1196 ASN   A C   1 
ATOM   8932  O O   . ASN   A 1 1232 ? 152.429 169.449 110.712 1.00 71.67  0  1196 ASN   A O   1 
ATOM   8933  C CB  . ASN   A 1 1232 ? 152.857 170.494 108.186 1.00 76.68  0  1196 ASN   A CB  1 
ATOM   8934  C CG  . ASN   A 1 1232 ? 152.962 170.841 106.716 1.00 76.79  0  1196 ASN   A CG  1 
ATOM   8935  O OD1 . ASN   A 1 1232 ? 152.272 170.260 105.879 1.00 77.46  0  1196 ASN   A OD1 1 
ATOM   8936  N ND2 . ASN   A 1 1232 ? 153.832 171.789 106.392 1.00 74.91  0  1196 ASN   A ND2 1 
ATOM   8937  N N   . LEU   A 1 1233 ? 150.233 169.059 110.420 1.00 61.74  0  1197 LEU   A N   1 
ATOM   8938  C CA  . LEU   A 1 1233 ? 150.018 168.477 111.738 1.00 59.88  0  1197 LEU   A CA  1 
ATOM   8939  C C   . LEU   A 1 1233 ? 149.751 166.987 111.597 1.00 61.23  0  1197 LEU   A C   1 
ATOM   8940  O O   . LEU   A 1 1233 ? 148.852 166.581 110.852 1.00 64.50  0  1197 LEU   A O   1 
ATOM   8941  C CB  . LEU   A 1 1233 ? 148.857 169.157 112.460 1.00 62.07  0  1197 LEU   A CB  1 
ATOM   8942  C CG  . LEU   A 1 1233 ? 148.977 169.160 113.983 1.00 62.68  0  1197 LEU   A CG  1 
ATOM   8943  C CD1 . LEU   A 1 1233 ? 149.801 170.338 114.466 1.00 64.08  0  1197 LEU   A CD1 1 
ATOM   8944  C CD2 . LEU   A 1 1233 ? 147.602 169.162 114.623 1.00 62.01  0  1197 LEU   A CD2 1 
ATOM   8945  N N   . SER   A 1 1234 ? 150.528 166.180 112.311 1.00 47.02  0  1198 SER   A N   1 
ATOM   8946  C CA  . SER   A 1 1234 ? 150.313 164.744 112.390 1.00 48.49  0  1198 SER   A CA  1 
ATOM   8947  C C   . SER   A 1 1234 ? 149.868 164.409 113.805 1.00 42.37  0  1198 SER   A C   1 
ATOM   8948  O O   . SER   A 1 1234 ? 150.596 164.676 114.767 1.00 44.09  0  1198 SER   A O   1 
ATOM   8949  C CB  . SER   A 1 1234 ? 151.579 163.974 112.029 1.00 49.22  0  1198 SER   A CB  1 
ATOM   8950  O OG  . SER   A 1 1234 ? 152.493 163.985 113.106 1.00 47.11  0  1198 SER   A OG  1 
ATOM   8951  N N   . ILE   A 1 1235 ? 148.676 163.822 113.926 1.00 29.46  0  1199 ILE   A N   1 
ATOM   8952  C CA  . ILE   A 1 1235 ? 148.128 163.508 115.237 1.00 34.46  0  1199 ILE   A CA  1 
ATOM   8953  C C   . ILE   A 1 1235 ? 148.932 162.423 115.936 1.00 37.57  0  1199 ILE   A C   1 
ATOM   8954  O O   . ILE   A 1 1235 ? 148.885 162.319 117.165 1.00 42.82  0  1199 ILE   A O   1 
ATOM   8955  C CB  . ILE   A 1 1235 ? 146.646 163.115 115.099 1.00 37.43  0  1199 ILE   A CB  1 
ATOM   8956  C CG1 . ILE   A 1 1235 ? 145.897 164.179 114.301 1.00 38.20  0  1199 ILE   A CG1 1 
ATOM   8957  C CG2 . ILE   A 1 1235 ? 145.996 162.962 116.455 1.00 32.45  0  1199 ILE   A CG2 1 
ATOM   8958  C CD1 . ILE   A 1 1235 ? 145.961 165.558 114.899 1.00 35.20  0  1199 ILE   A CD1 1 
ATOM   8959  N N   . THR   A 1 1236 ? 149.679 161.609 115.190 1.00 34.35  0  1200 THR   A N   1 
ATOM   8960  C CA  . THR   A 1 1236 ? 150.539 160.618 115.830 1.00 33.70  0  1200 THR   A CA  1 
ATOM   8961  C C   . THR   A 1 1236 ? 151.645 161.291 116.633 1.00 41.72  0  1200 THR   A C   1 
ATOM   8962  O O   . THR   A 1 1236 ? 151.891 160.935 117.792 1.00 45.47  0  1200 THR   A O   1 
ATOM   8963  C CB  . THR   A 1 1236 ? 151.134 159.685 114.781 1.00 42.15  0  1200 THR   A CB  1 
ATOM   8964  O OG1 . THR   A 1 1236 ? 150.129 159.350 113.818 1.00 48.64  0  1200 THR   A OG1 1 
ATOM   8965  C CG2 . THR   A 1 1236 ? 151.635 158.419 115.438 1.00 46.29  0  1200 THR   A CG2 1 
ATOM   8966  N N   . GLU   A 1 1237 ? 152.317 162.278 116.033 1.00 42.38  0  1201 GLU   A N   1 
ATOM   8967  C CA  . GLU   A 1 1237 ? 153.332 163.033 116.761 1.00 37.76  0  1201 GLU   A CA  1 
ATOM   8968  C C   . GLU   A 1 1237 ? 152.717 163.796 117.923 1.00 38.29  0  1201 GLU   A C   1 
ATOM   8969  O O   . GLU   A 1 1237 ? 153.319 163.898 118.995 1.00 42.80  0  1201 GLU   A O   1 
ATOM   8970  C CB  . GLU   A 1 1237 ? 154.053 163.995 115.818 1.00 39.39  0  1201 GLU   A CB  1 
ATOM   8971  C CG  . GLU   A 1 1237 ? 155.193 163.368 115.038 1.00 48.17  0  1201 GLU   A CG  1 
ATOM   8972  C CD  . GLU   A 1 1237 ? 155.871 164.350 114.104 1.00 47.60  0  1201 GLU   A CD  1 
ATOM   8973  O OE1 . GLU   A 1 1237 ? 155.366 165.481 113.958 1.00 50.55  0  1201 GLU   A OE1 1 
ATOM   8974  O OE2 . GLU   A 1 1237 ? 156.912 163.991 113.516 1.00 41.14  -1 1201 GLU   A OE2 1 
ATOM   8975  N N   . LEU   A 1 1238 ? 151.521 164.351 117.723 1.00 36.43  0  1202 LEU   A N   1 
ATOM   8976  C CA  . LEU   A 1 1238 ? 150.851 165.081 118.794 1.00 26.20  0  1202 LEU   A CA  1 
ATOM   8977  C C   . LEU   A 1 1238 ? 150.554 164.171 119.978 1.00 22.10  0  1202 LEU   A C   1 
ATOM   8978  O O   . LEU   A 1 1238 ? 150.793 164.542 121.131 1.00 36.55  0  1202 LEU   A O   1 
ATOM   8979  C CB  . LEU   A 1 1238 ? 149.567 165.709 118.255 1.00 26.97  0  1202 LEU   A CB  1 
ATOM   8980  C CG  . LEU   A 1 1238 ? 148.856 166.794 119.056 1.00 25.97  0  1202 LEU   A CG  1 
ATOM   8981  C CD1 . LEU   A 1 1238 ? 148.223 167.779 118.100 1.00 34.79  0  1202 LEU   A CD1 1 
ATOM   8982  C CD2 . LEU   A 1 1238 ? 147.804 166.188 119.956 1.00 29.68  0  1202 LEU   A CD2 1 
ATOM   8983  N N   . SER   A 1 1239 ? 150.042 162.970 119.711 1.00 20.08  0  1203 SER   A N   1 
ATOM   8984  C CA  . SER   A 1 1239 ? 149.757 162.029 120.787 1.00 21.91  0  1203 SER   A CA  1 
ATOM   8985  C C   . SER   A 1 1239 ? 151.036 161.555 121.460 1.00 29.80  0  1203 SER   A C   1 
ATOM   8986  O O   . SER   A 1 1239 ? 151.069 161.373 122.682 1.00 33.98  0  1203 SER   A O   1 
ATOM   8987  C CB  . SER   A 1 1239 ? 148.970 160.841 120.249 1.00 35.44  0  1203 SER   A CB  1 
ATOM   8988  O OG  . SER   A 1 1239 ? 149.298 159.668 120.968 1.00 39.31  0  1203 SER   A OG  1 
ATOM   8989  N N   . LYS   A 1 1240 ? 152.097 161.337 120.680 1.00 34.03  0  1204 LYS   A N   1 
ATOM   8990  C CA  . LYS   A 1 1240 ? 153.375 160.958 121.271 1.00 32.49  0  1204 LYS   A CA  1 
ATOM   8991  C C   . LYS   A 1 1240 ? 153.894 162.051 122.193 1.00 37.38  0  1204 LYS   A C   1 
ATOM   8992  O O   . LYS   A 1 1240 ? 154.372 161.769 123.298 1.00 40.51  0  1204 LYS   A O   1 
ATOM   8993  C CB  . LYS   A 1 1240 ? 154.389 160.659 120.170 1.00 29.12  0  1204 LYS   A CB  1 
ATOM   8994  C CG  . LYS   A 1 1240 ? 155.668 160.020 120.664 1.00 30.90  0  1204 LYS   A CG  1 
ATOM   8995  C CD  . LYS   A 1 1240 ? 156.591 159.678 119.509 1.00 35.97  0  1204 LYS   A CD  1 
ATOM   8996  C CE  . LYS   A 1 1240 ? 157.928 159.171 120.009 1.00 40.61  0  1204 LYS   A CE  1 
ATOM   8997  N NZ  . LYS   A 1 1240 ? 157.776 157.901 120.766 1.00 45.04  1  1204 LYS   A NZ  1 
ATOM   8998  N N   . TYR   A 1 1241 ? 153.796 163.308 121.758 1.00 38.55  0  1205 TYR   A N   1 
ATOM   8999  C CA  . TYR   A 1 1241 ? 154.241 164.424 122.581 1.00 32.90  0  1205 TYR   A CA  1 
ATOM   9000  C C   . TYR   A 1 1241 ? 153.401 164.548 123.843 1.00 32.33  0  1205 TYR   A C   1 
ATOM   9001  O O   . TYR   A 1 1241 ? 153.935 164.818 124.920 1.00 37.73  0  1205 TYR   A O   1 
ATOM   9002  C CB  . TYR   A 1 1241 ? 154.195 165.718 121.772 1.00 33.06  0  1205 TYR   A CB  1 
ATOM   9003  C CG  . TYR   A 1 1241 ? 154.547 166.958 122.561 1.00 37.09  0  1205 TYR   A CG  1 
ATOM   9004  C CD1 . TYR   A 1 1241 ? 155.618 166.964 123.444 1.00 42.97  0  1205 TYR   A CD1 1 
ATOM   9005  C CD2 . TYR   A 1 1241 ? 153.822 168.129 122.406 1.00 35.90  0  1205 TYR   A CD2 1 
ATOM   9006  C CE1 . TYR   A 1 1241 ? 155.944 168.094 124.163 1.00 41.84  0  1205 TYR   A CE1 1 
ATOM   9007  C CE2 . TYR   A 1 1241 ? 154.143 169.265 123.118 1.00 41.50  0  1205 TYR   A CE2 1 
ATOM   9008  C CZ  . TYR   A 1 1241 ? 155.205 169.241 123.995 1.00 42.10  0  1205 TYR   A CZ  1 
ATOM   9009  O OH  . TYR   A 1 1241 ? 155.528 170.372 124.707 1.00 39.52  0  1205 TYR   A OH  1 
ATOM   9010  N N   . VAL   A 1 1242 ? 152.087 164.357 123.732 1.00 31.08  0  1206 VAL   A N   1 
ATOM   9011  C CA  . VAL   A 1 1242 ? 151.231 164.419 124.913 1.00 25.51  0  1206 VAL   A CA  1 
ATOM   9012  C C   . VAL   A 1 1242 ? 151.605 163.324 125.901 1.00 25.43  0  1206 VAL   A C   1 
ATOM   9013  O O   . VAL   A 1 1242 ? 151.728 163.571 127.108 1.00 38.34  0  1206 VAL   A O   1 
ATOM   9014  C CB  . VAL   A 1 1242 ? 149.751 164.329 124.503 1.00 22.25  0  1206 VAL   A CB  1 
ATOM   9015  C CG1 . VAL   A 1 1242 ? 148.885 164.070 125.715 1.00 25.15  0  1206 VAL   A CG1 1 
ATOM   9016  C CG2 . VAL   A 1 1242 ? 149.325 165.598 123.800 1.00 24.31  0  1206 VAL   A CG2 1 
ATOM   9017  N N   . ARG   A 1 1243 ? 151.809 162.101 125.408 1.00 20.90  0  1207 ARG   A N   1 
ATOM   9018  C CA  . ARG   A 1 1243 ? 152.152 160.999 126.299 1.00 21.91  0  1207 ARG   A CA  1 
ATOM   9019  C C   . ARG   A 1 1243 ? 153.508 161.213 126.958 1.00 28.32  0  1207 ARG   A C   1 
ATOM   9020  O O   . ARG   A 1 1243 ? 153.681 160.902 128.142 1.00 32.80  0  1207 ARG   A O   1 
ATOM   9021  C CB  . ARG   A 1 1243 ? 152.135 159.678 125.536 1.00 30.95  0  1207 ARG   A CB  1 
ATOM   9022  C CG  . ARG   A 1 1243 ? 152.322 158.460 126.425 1.00 35.40  0  1207 ARG   A CG  1 
ATOM   9023  C CD  . ARG   A 1 1243 ? 152.125 157.175 125.647 1.00 29.34  0  1207 ARG   A CD  1 
ATOM   9024  N NE  . ARG   A 1 1243 ? 150.822 156.579 125.903 1.00 20.39  0  1207 ARG   A NE  1 
ATOM   9025  C CZ  . ARG   A 1 1243 ? 149.872 156.451 124.989 1.00 27.58  0  1207 ARG   A CZ  1 
ATOM   9026  N NH1 . ARG   A 1 1243 ? 150.048 156.870 123.748 1.00 22.05  1  1207 ARG   A NH1 1 
ATOM   9027  N NH2 . ARG   A 1 1243 ? 148.715 155.893 125.330 1.00 32.79  0  1207 ARG   A NH2 1 
ATOM   9028  N N   . GLU   A 1 1244 ? 154.486 161.729 126.210 1.00 34.68  0  1208 GLU   A N   1 
ATOM   9029  C CA  . GLU   A 1 1244 ? 155.803 161.976 126.790 1.00 33.93  0  1208 GLU   A CA  1 
ATOM   9030  C C   . GLU   A 1 1244 ? 155.752 163.109 127.807 1.00 36.29  0  1208 GLU   A C   1 
ATOM   9031  O O   . GLU   A 1 1244 ? 156.316 163.000 128.901 1.00 36.33  0  1208 GLU   A O   1 
ATOM   9032  C CB  . GLU   A 1 1244 ? 156.814 162.297 125.692 1.00 32.28  0  1208 GLU   A CB  1 
ATOM   9033  C CG  . GLU   A 1 1244 ? 157.082 161.169 124.723 1.00 34.51  0  1208 GLU   A CG  1 
ATOM   9034  C CD  . GLU   A 1 1244 ? 158.014 161.591 123.609 1.00 46.46  0  1208 GLU   A CD  1 
ATOM   9035  O OE1 . GLU   A 1 1244 ? 157.716 162.596 122.933 1.00 47.63  0  1208 GLU   A OE1 1 
ATOM   9036  O OE2 . GLU   A 1 1244 ? 159.048 160.922 123.409 1.00 43.95  -1 1208 GLU   A OE2 1 
ATOM   9037  N N   . ARG   A 1 1245 ? 155.076 164.205 127.460 1.00 35.31  0  1209 ARG   A N   1 
ATOM   9038  C CA  . ARG   A 1 1245 ? 155.008 165.362 128.343 1.00 35.41  0  1209 ARG   A CA  1 
ATOM   9039  C C   . ARG   A 1 1245 ? 154.274 165.031 129.631 1.00 33.83  0  1209 ARG   A C   1 
ATOM   9040  O O   . ARG   A 1 1245 ? 154.623 165.543 130.700 1.00 40.70  0  1209 ARG   A O   1 
ATOM   9041  C CB  . ARG   A 1 1245 ? 154.324 166.517 127.618 1.00 37.67  0  1209 ARG   A CB  1 
ATOM   9042  C CG  . ARG   A 1 1245 ? 154.085 167.740 128.469 1.00 38.97  0  1209 ARG   A CG  1 
ATOM   9043  C CD  . ARG   A 1 1245 ? 153.359 168.806 127.681 1.00 35.26  0  1209 ARG   A CD  1 
ATOM   9044  N NE  . ARG   A 1 1245 ? 153.110 169.990 128.491 1.00 33.16  0  1209 ARG   A NE  1 
ATOM   9045  C CZ  . ARG   A 1 1245 ? 153.907 171.047 128.531 1.00 38.19  0  1209 ARG   A CZ  1 
ATOM   9046  N NH1 . ARG   A 1 1245 ? 155.005 171.112 127.798 1.00 41.13  1  1209 ARG   A NH1 1 
ATOM   9047  N NH2 . ARG   A 1 1245 ? 153.594 172.065 129.325 1.00 44.54  0  1209 ARG   A NH2 1 
ATOM   9048  N N   . SER   A 1 1246 ? 153.255 164.175 129.550 1.00 31.49  0  1210 SER   A N   1 
ATOM   9049  C CA  . SER   A 1 1246 ? 152.479 163.841 130.737 1.00 27.87  0  1210 SER   A CA  1 
ATOM   9050  C C   . SER   A 1 1246 ? 153.359 163.208 131.805 1.00 31.58  0  1210 SER   A C   1 
ATOM   9051  O O   . SER   A 1 1246 ? 153.255 163.544 132.989 1.00 40.29  0  1210 SER   A O   1 
ATOM   9052  C CB  . SER   A 1 1246 ? 151.330 162.914 130.357 1.00 27.65  0  1210 SER   A CB  1 
ATOM   9053  O OG  . SER   A 1 1246 ? 150.513 163.510 129.369 1.00 36.45  0  1210 SER   A OG  1 
ATOM   9054  N N   . TRP   A 1 1247 ? 154.237 162.294 131.409 1.00 29.95  0  1211 TRP   A N   1 
ATOM   9055  C CA  . TRP   A 1 1247 ? 155.204 161.730 132.338 1.00 32.20  0  1211 TRP   A CA  1 
ATOM   9056  C C   . TRP   A 1 1247 ? 156.513 162.502 132.370 1.00 39.06  0  1211 TRP   A C   1 
ATOM   9057  O O   . TRP   A 1 1247 ? 157.374 162.190 133.201 1.00 42.27  0  1211 TRP   A O   1 
ATOM   9058  C CB  . TRP   A 1 1247 ? 155.496 160.271 131.986 1.00 33.30  0  1211 TRP   A CB  1 
ATOM   9059  C CG  . TRP   A 1 1247 ? 154.338 159.358 132.162 1.00 30.77  0  1211 TRP   A CG  1 
ATOM   9060  C CD1 . TRP   A 1 1247 ? 153.761 158.579 131.208 1.00 33.44  0  1211 TRP   A CD1 1 
ATOM   9061  C CD2 . TRP   A 1 1247 ? 153.618 159.109 133.373 1.00 30.14  0  1211 TRP   A CD2 1 
ATOM   9062  N NE1 . TRP   A 1 1247 ? 152.721 157.867 131.745 1.00 36.77  0  1211 TRP   A NE1 1 
ATOM   9063  C CE2 . TRP   A 1 1247 ? 152.614 158.174 133.075 1.00 34.85  0  1211 TRP   A CE2 1 
ATOM   9064  C CE3 . TRP   A 1 1247 ? 153.722 159.590 134.679 1.00 35.48  0  1211 TRP   A CE3 1 
ATOM   9065  C CZ2 . TRP   A 1 1247 ? 151.723 157.712 134.032 1.00 34.43  0  1211 TRP   A CZ2 1 
ATOM   9066  C CZ3 . TRP   A 1 1247 ? 152.837 159.130 135.625 1.00 33.21  0  1211 TRP   A CZ3 1 
ATOM   9067  C CH2 . TRP   A 1 1247 ? 151.851 158.201 135.299 1.00 31.92  0  1211 TRP   A CH2 1 
ATOM   9068  N N   . SER   A 1 1248 ? 156.676 163.496 131.496 1.00 41.17  0  1212 SER   A N   1 
ATOM   9069  C CA  . SER   A 1 1248 ? 157.927 164.241 131.365 1.00 38.83  0  1212 SER   A CA  1 
ATOM   9070  C C   . SER   A 1 1248 ? 159.097 163.301 131.100 1.00 39.01  0  1212 SER   A C   1 
ATOM   9071  O O   . SER   A 1 1248 ? 160.206 163.493 131.602 1.00 41.27  0  1212 SER   A O   1 
ATOM   9072  C CB  . SER   A 1 1248 ? 158.193 165.103 132.596 1.00 32.93  0  1212 SER   A CB  1 
ATOM   9073  O OG  . SER   A 1 1248 ? 158.855 164.349 133.593 1.00 36.26  0  1212 SER   A OG  1 
ATOM   9074  N N   . LEU   A 1 1249 ? 158.841 162.263 130.311 1.00 32.91  0  1213 LEU   A N   1 
ATOM   9075  C CA  . LEU   A 1 1249 ? 159.888 161.357 129.870 1.00 34.89  0  1213 LEU   A CA  1 
ATOM   9076  C C   . LEU   A 1 1249 ? 160.420 161.825 128.525 1.00 36.32  0  1213 LEU   A C   1 
ATOM   9077  O O   . LEU   A 1 1249 ? 159.656 162.263 127.661 1.00 39.69  0  1213 LEU   A O   1 
ATOM   9078  C CB  . LEU   A 1 1249 ? 159.364 159.925 129.769 1.00 35.91  0  1213 LEU   A CB  1 
ATOM   9079  C CG  . LEU   A 1 1249 ? 159.038 159.257 131.107 1.00 37.21  0  1213 LEU   A CG  1 
ATOM   9080  C CD1 . LEU   A 1 1249 ? 158.583 157.828 130.905 1.00 36.23  0  1213 LEU   A CD1 1 
ATOM   9081  C CD2 . LEU   A 1 1249 ? 160.233 159.307 132.038 1.00 36.00  0  1213 LEU   A CD2 1 
ATOM   9082  N N   . SER   A 1 1250 ? 161.741 161.750 128.361 1.00 43.20  0  1214 SER   A N   1 
ATOM   9083  C CA  . SER   A 1 1250 ? 162.363 162.261 127.145 1.00 42.78  0  1214 SER   A CA  1 
ATOM   9084  C C   . SER   A 1 1250 ? 161.886 161.495 125.919 1.00 43.21  0  1214 SER   A C   1 
ATOM   9085  O O   . SER   A 1 1250 ? 161.543 162.093 124.893 1.00 43.04  0  1214 SER   A O   1 
ATOM   9086  C CB  . SER   A 1 1250 ? 163.885 162.192 127.267 1.00 40.59  0  1214 SER   A CB  1 
ATOM   9087  O OG  . SER   A 1 1250 ? 164.348 163.010 128.326 1.00 43.69  0  1214 SER   A OG  1 
ATOM   9088  N N   . ASN   A 1 1251 ? 161.845 160.167 126.009 1.00 39.15  0  1215 ASN   A N   1 
ATOM   9089  C CA  . ASN   A 1 1251 ? 161.431 159.341 124.884 1.00 35.90  0  1215 ASN   A CA  1 
ATOM   9090  C C   . ASN   A 1 1251 ? 160.667 158.128 125.387 1.00 33.69  0  1215 ASN   A C   1 
ATOM   9091  O O   . ASN   A 1 1251 ? 161.154 157.398 126.255 1.00 37.31  0  1215 ASN   A O   1 
ATOM   9092  C CB  . ASN   A 1 1251 ? 162.637 158.896 124.052 1.00 38.06  0  1215 ASN   A CB  1 
ATOM   9093  C CG  . ASN   A 1 1251 ? 162.234 158.305 122.720 1.00 45.85  0  1215 ASN   A CG  1 
ATOM   9094  O OD1 . ASN   A 1 1251 ? 161.087 158.431 122.298 1.00 41.50  0  1215 ASN   A OD1 1 
ATOM   9095  N ND2 . ASN   A 1 1251 ? 163.177 157.657 122.049 1.00 43.34  0  1215 ASN   A ND2 1 
ATOM   9096  N N   . ILE   A 1 1252 ? 159.470 157.926 124.844 1.00 31.89  0  1216 ILE   A N   1 
ATOM   9097  C CA  . ILE   A 1 1252 ? 158.658 156.743 125.098 1.00 34.00  0  1216 ILE   A CA  1 
ATOM   9098  C C   . ILE   A 1 1252 ? 158.362 156.106 123.750 1.00 36.57  0  1216 ILE   A C   1 
ATOM   9099  O O   . ILE   A 1 1252 ? 157.850 156.775 122.844 1.00 47.38  0  1216 ILE   A O   1 
ATOM   9100  C CB  . ILE   A 1 1252 ? 157.357 157.084 125.840 1.00 35.11  0  1216 ILE   A CB  1 
ATOM   9101  C CG1 . ILE   A 1 1252 ? 157.652 157.580 127.255 1.00 41.85  0  1216 ILE   A CG1 1 
ATOM   9102  C CG2 . ILE   A 1 1252 ? 156.449 155.877 125.894 1.00 28.57  0  1216 ILE   A CG2 1 
ATOM   9103  C CD1 . ILE   A 1 1252 ? 156.410 157.895 128.051 1.00 31.34  0  1216 ILE   A CD1 1 
ATOM   9104  N N   . VAL   A 1 1253 ? 158.676 154.823 123.615 1.00 33.30  0  1217 VAL   A N   1 
ATOM   9105  C CA  . VAL   A 1 1253 ? 158.577 154.139 122.334 1.00 36.95  0  1217 VAL   A CA  1 
ATOM   9106  C C   . VAL   A 1 1253 ? 157.730 152.888 122.492 1.00 37.48  0  1217 VAL   A C   1 
ATOM   9107  O O   . VAL   A 1 1253 ? 157.628 152.314 123.580 1.00 40.68  0  1217 VAL   A O   1 
ATOM   9108  C CB  . VAL   A 1 1253 ? 159.967 153.775 121.774 1.00 36.66  0  1217 VAL   A CB  1 
ATOM   9109  C CG1 . VAL   A 1 1253 ? 160.683 155.017 121.283 1.00 32.47  0  1217 VAL   A CG1 1 
ATOM   9110  C CG2 . VAL   A 1 1253 ? 160.789 153.058 122.834 1.00 32.57  0  1217 VAL   A CG2 1 
ATOM   9111  N N   . GLY   A 1 1254 ? 157.122 152.464 121.388 1.00 35.50  0  1218 GLY   A N   1 
ATOM   9112  C CA  . GLY   A 1 1254 ? 156.431 151.194 121.355 1.00 31.72  0  1218 GLY   A CA  1 
ATOM   9113  C C   . GLY   A 1 1254 ? 155.007 151.199 121.851 1.00 30.14  0  1218 GLY   A C   1 
ATOM   9114  O O   . GLY   A 1 1254 ? 154.416 150.126 121.991 1.00 46.10  0  1218 GLY   A O   1 
ATOM   9115  N N   . VAL   A 1 1255 ? 154.430 152.368 122.126 1.00 16.75  0  1219 VAL   A N   1 
ATOM   9116  C CA  . VAL   A 1 1255 ? 153.042 152.463 122.559 1.00 34.19  0  1219 VAL   A CA  1 
ATOM   9117  C C   . VAL   A 1 1255 ? 152.224 153.410 121.701 1.00 33.79  0  1219 VAL   A C   1 
ATOM   9118  O O   . VAL   A 1 1255 ? 151.011 153.510 121.900 1.00 30.14  0  1219 VAL   A O   1 
ATOM   9119  C CB  . VAL   A 1 1255 ? 152.937 152.871 124.043 1.00 32.35  0  1219 VAL   A CB  1 
ATOM   9120  C CG1 . VAL   A 1 1255 ? 153.396 151.743 124.934 1.00 26.99  0  1219 VAL   A CG1 1 
ATOM   9121  C CG2 . VAL   A 1 1255 ? 153.752 154.111 124.304 1.00 36.66  0  1219 VAL   A CG2 1 
ATOM   9122  N N   . THR   A 1 1256 ? 152.841 154.103 120.753 1.00 26.05  0  1220 THR   A N   1 
ATOM   9123  C CA  . THR   A 1 1256 ? 152.146 155.053 119.897 1.00 27.52  0  1220 THR   A CA  1 
ATOM   9124  C C   . THR   A 1 1256 ? 151.976 154.461 118.507 1.00 31.03  0  1220 THR   A C   1 
ATOM   9125  O O   . THR   A 1 1256 ? 152.960 154.094 117.860 1.00 43.13  0  1220 THR   A O   1 
ATOM   9126  C CB  . THR   A 1 1256 ? 152.906 156.375 119.813 1.00 29.80  0  1220 THR   A CB  1 
ATOM   9127  O OG1 . THR   A 1 1256 ? 152.899 157.011 121.096 1.00 42.20  0  1220 THR   A OG1 1 
ATOM   9128  C CG2 . THR   A 1 1256 ? 152.260 157.292 118.796 1.00 26.27  0  1220 THR   A CG2 1 
ATOM   9129  N N   . SER   A 1 1257 ? 150.726 154.375 118.052 1.00 23.44  0  1221 SER   A N   1 
ATOM   9130  C CA  . SER   A 1 1257 ? 150.404 153.876 116.732 1.00 20.04  0  1221 SER   A CA  1 
ATOM   9131  C C   . SER   A 1 1257 ? 149.339 154.784 116.143 1.00 25.43  0  1221 SER   A C   1 
ATOM   9132  O O   . SER   A 1 1257 ? 148.441 155.219 116.876 1.00 40.75  0  1221 SER   A O   1 
ATOM   9133  C CB  . SER   A 1 1257 ? 149.902 152.433 116.777 1.00 27.46  0  1221 SER   A CB  1 
ATOM   9134  O OG  . SER   A 1 1257 ? 149.547 151.978 115.486 1.00 32.76  0  1221 SER   A OG  1 
ATOM   9135  N N   . PRO   A 1 1258 ? 149.399 155.087 114.851 1.00 18.99  0  1222 PRO   A N   1 
ATOM   9136  C CA  . PRO   A 1 1258 ? 148.405 155.985 114.258 1.00 22.78  0  1222 PRO   A CA  1 
ATOM   9137  C C   . PRO   A 1 1258 ? 147.025 155.351 114.246 1.00 30.65  0  1222 PRO   A C   1 
ATOM   9138  O O   . PRO   A 1 1258 ? 146.861 154.132 114.312 1.00 34.86  0  1222 PRO   A O   1 
ATOM   9139  C CB  . PRO   A 1 1258 ? 148.930 156.214 112.838 1.00 24.99  0  1222 PRO   A CB  1 
ATOM   9140  C CG  . PRO   A 1 1258 ? 149.777 155.040 112.560 1.00 27.60  0  1222 PRO   A CG  1 
ATOM   9141  C CD  . PRO   A 1 1258 ? 150.398 154.649 113.866 1.00 24.72  0  1222 PRO   A CD  1 
ATOM   9142  N N   . SER   A 1 1259 ? 146.013 156.209 114.178 1.00 28.99  0  1223 SER   A N   1 
ATOM   9143  C CA  . SER   A 1 1259 ? 144.635 155.761 114.045 1.00 24.64  0  1223 SER   A CA  1 
ATOM   9144  C C   . SER   A 1 1259 ? 144.371 155.439 112.581 1.00 28.62  0  1223 SER   A C   1 
ATOM   9145  O O   . SER   A 1 1259 ? 144.550 156.296 111.710 1.00 32.85  0  1223 SER   A O   1 
ATOM   9146  C CB  . SER   A 1 1259 ? 143.660 156.821 114.549 1.00 30.40  0  1223 SER   A CB  1 
ATOM   9147  O OG  . SER   A 1 1259 ? 142.330 156.333 114.528 1.00 35.50  0  1223 SER   A OG  1 
ATOM   9148  N N   . ILE   A 1 1260 ? 143.949 154.202 112.315 1.00 22.36  0  1224 ILE   A N   1 
ATOM   9149  C CA  . ILE   A 1 1260 ? 143.737 153.767 110.940 1.00 20.00  0  1224 ILE   A CA  1 
ATOM   9150  C C   . ILE   A 1 1260 ? 142.604 154.549 110.300 1.00 27.36  0  1224 ILE   A C   1 
ATOM   9151  O O   . ILE   A 1 1260 ? 142.647 154.859 109.104 1.00 29.92  0  1224 ILE   A O   1 
ATOM   9152  C CB  . ILE   A 1 1260 ? 143.456 152.257 110.897 1.00 21.30  0  1224 ILE   A CB  1 
ATOM   9153  C CG1 . ILE   A 1 1260 ? 144.304 151.520 111.934 1.00 19.61  0  1224 ILE   A CG1 1 
ATOM   9154  C CG2 . ILE   A 1 1260 ? 143.716 151.726 109.511 1.00 31.05  0  1224 ILE   A CG2 1 
ATOM   9155  C CD1 . ILE   A 1 1260 ? 145.779 151.626 111.719 1.00 19.08  0  1224 ILE   A CD1 1 
ATOM   9156  N N   . MET   A 1 1261 ? 141.570 154.868 111.077 1.00 35.50  0  1225 MET   A N   1 
ATOM   9157  C CA  . MET   A 1 1261 ? 140.419 155.584 110.547 1.00 34.74  0  1225 MET   A CA  1 
ATOM   9158  C C   . MET   A 1 1261 ? 140.783 156.987 110.084 1.00 25.53  0  1225 MET   A C   1 
ATOM   9159  O O   . MET   A 1 1261 ? 140.149 157.506 109.162 1.00 26.63  0  1225 MET   A O   1 
ATOM   9160  C CB  . MET   A 1 1261 ? 139.314 155.614 111.607 1.00 34.43  0  1225 MET   A CB  1 
ATOM   9161  C CG  . MET   A 1 1261 ? 138.232 156.649 111.403 1.00 39.38  0  1225 MET   A CG  1 
ATOM   9162  S SD  . MET   A 1 1261 ? 137.231 156.835 112.884 1.00 58.52  0  1225 MET   A SD  1 
ATOM   9163  C CE  . MET   A 1 1261 ? 138.506 156.913 114.138 1.00 35.76  0  1225 MET   A CE  1 
ATOM   9164  N N   . TYR   A 1 1262 ? 141.802 157.601 110.681 1.00 25.70  0  1226 TYR   A N   1 
ATOM   9165  C CA  . TYR   A 1 1262 ? 142.255 158.912 110.236 1.00 32.62  0  1226 TYR   A CA  1 
ATOM   9166  C C   . TYR   A 1 1262 ? 143.343 158.802 109.173 1.00 41.12  0  1226 TYR   A C   1 
ATOM   9167  O O   . TYR   A 1 1262 ? 143.378 159.604 108.234 1.00 41.55  0  1226 TYR   A O   1 
ATOM   9168  C CB  . TYR   A 1 1262 ? 142.781 159.719 111.426 1.00 30.69  0  1226 TYR   A CB  1 
ATOM   9169  C CG  . TYR   A 1 1262 ? 142.963 161.195 111.146 1.00 41.75  0  1226 TYR   A CG  1 
ATOM   9170  C CD1 . TYR   A 1 1262 ? 142.464 161.772 109.984 1.00 41.91  0  1226 TYR   A CD1 1 
ATOM   9171  C CD2 . TYR   A 1 1262 ? 143.651 162.008 112.029 1.00 38.61  0  1226 TYR   A CD2 1 
ATOM   9172  C CE1 . TYR   A 1 1262 ? 142.631 163.112 109.722 1.00 41.95  0  1226 TYR   A CE1 1 
ATOM   9173  C CE2 . TYR   A 1 1262 ? 143.823 163.350 111.771 1.00 39.99  0  1226 TYR   A CE2 1 
ATOM   9174  C CZ  . TYR   A 1 1262 ? 143.312 163.895 110.617 1.00 40.95  0  1226 TYR   A CZ  1 
ATOM   9175  O OH  . TYR   A 1 1262 ? 143.481 165.231 110.356 1.00 41.01  0  1226 TYR   A OH  1 
ATOM   9176  N N   . THR   A 1 1263 ? 144.229 157.813 109.299 1.00 36.13  0  1227 THR   A N   1 
ATOM   9177  C CA  . THR   A 1 1263 ? 145.354 157.700 108.378 1.00 24.50  0  1227 THR   A CA  1 
ATOM   9178  C C   . THR   A 1 1263 ? 144.881 157.481 106.948 1.00 28.27  0  1227 THR   A C   1 
ATOM   9179  O O   . THR   A 1 1263 ? 145.399 158.097 106.011 1.00 34.33  0  1227 THR   A O   1 
ATOM   9180  C CB  . THR   A 1 1263 ? 146.271 156.559 108.813 1.00 24.69  0  1227 THR   A CB  1 
ATOM   9181  O OG1 . THR   A 1 1263 ? 146.672 156.756 110.173 1.00 33.02  0  1227 THR   A OG1 1 
ATOM   9182  C CG2 . THR   A 1 1263 ? 147.503 156.507 107.937 1.00 30.01  0  1227 THR   A CG2 1 
ATOM   9183  N N   . MET   A 1 1264 ? 143.890 156.614 106.760 1.00 39.67  0  1228 MET   A N   1 
ATOM   9184  C CA  . MET   A 1 1264 ? 143.505 156.150 105.429 1.00 32.79  0  1228 MET   A CA  1 
ATOM   9185  C C   . MET   A 1 1264 ? 142.312 156.946 104.922 1.00 30.52  0  1228 MET   A C   1 
ATOM   9186  O O   . MET   A 1 1264 ? 141.187 156.766 105.388 1.00 42.73  0  1228 MET   A O   1 
ATOM   9187  C CB  . MET   A 1 1264 ? 143.191 154.660 105.457 1.00 26.96  0  1228 MET   A CB  1 
ATOM   9188  C CG  . MET   A 1 1264 ? 144.291 153.812 106.048 1.00 30.21  0  1228 MET   A CG  1 
ATOM   9189  S SD  . MET   A 1 1264 ? 145.530 153.430 104.804 1.00 49.39  0  1228 MET   A SD  1 
ATOM   9190  C CE  . MET   A 1 1264 ? 146.379 152.073 105.587 1.00 41.77  0  1228 MET   A CE  1 
ATOM   9191  N N   . ASP   A 1 1265 ? 142.556 157.823 103.955 1.00 28.30  0  1229 ASP   A N   1 
ATOM   9192  C CA  . ASP   A 1 1265 ? 141.465 158.407 103.194 1.00 30.64  0  1229 ASP   A CA  1 
ATOM   9193  C C   . ASP   A 1 1265 ? 140.824 157.336 102.321 1.00 41.47  0  1229 ASP   A C   1 
ATOM   9194  O O   . ASP   A 1 1265 ? 141.474 156.377 101.902 1.00 52.17  0  1229 ASP   A O   1 
ATOM   9195  C CB  . ASP   A 1 1265 ? 141.973 159.560 102.334 1.00 42.00  0  1229 ASP   A CB  1 
ATOM   9196  C CG  . ASP   A 1 1265 ? 140.859 160.268 101.595 1.00 51.57  0  1229 ASP   A CG  1 
ATOM   9197  O OD1 . ASP   A 1 1265 ? 139.681 160.063 101.954 1.00 49.36  0  1229 ASP   A OD1 1 
ATOM   9198  O OD2 . ASP   A 1 1265 ? 141.160 161.027 100.649 1.00 54.37  -1 1229 ASP   A OD2 1 
ATOM   9199  N N   . ILE   A 1 1266 ? 139.536 157.505 102.043 1.00 40.38  0  1230 ILE   A N   1 
ATOM   9200  C CA  . ILE   A 1 1266 ? 138.729 156.473 101.402 1.00 39.12  0  1230 ILE   A CA  1 
ATOM   9201  C C   . ILE   A 1 1266 ? 138.327 156.964 100.020 1.00 38.54  0  1230 ILE   A C   1 
ATOM   9202  O O   . ILE   A 1 1266 ? 137.752 158.050 99.887  1.00 36.75  0  1230 ILE   A O   1 
ATOM   9203  C CB  . ILE   A 1 1266 ? 137.493 156.128 102.244 1.00 38.55  0  1230 ILE   A CB  1 
ATOM   9204  C CG1 . ILE   A 1 1266 ? 137.891 155.271 103.444 1.00 39.38  0  1230 ILE   A CG1 1 
ATOM   9205  C CG2 . ILE   A 1 1266 ? 136.482 155.387 101.414 1.00 34.06  0  1230 ILE   A CG2 1 
ATOM   9206  C CD1 . ILE   A 1 1266 ? 137.324 155.762 104.758 1.00 36.42  0  1230 ILE   A CD1 1 
ATOM   9207  N N   . LYS   A 1 1267 ? 138.621 156.165 98.994  1.00 47.43  0  1231 LYS   A N   1 
ATOM   9208  C CA  . LYS   A 1 1267 ? 138.253 156.479 97.621  1.00 47.71  0  1231 LYS   A CA  1 
ATOM   9209  C C   . LYS   A 1 1267 ? 137.427 155.342 97.037  1.00 49.92  0  1231 LYS   A C   1 
ATOM   9210  O O   . LYS   A 1 1267 ? 137.660 154.170 97.340  1.00 47.48  0  1231 LYS   A O   1 
ATOM   9211  C CB  . LYS   A 1 1267 ? 139.492 156.715 96.754  1.00 50.93  0  1231 LYS   A CB  1 
ATOM   9212  C CG  . LYS   A 1 1267 ? 140.267 157.963 97.118  1.00 50.91  0  1231 LYS   A CG  1 
ATOM   9213  C CD  . LYS   A 1 1267 ? 139.511 159.214 96.723  1.00 48.55  0  1231 LYS   A CD  1 
ATOM   9214  C CE  . LYS   A 1 1267 ? 140.329 160.451 97.028  1.00 46.69  0  1231 LYS   A CE  1 
ATOM   9215  N NZ  . LYS   A 1 1267 ? 140.557 160.600 98.489  1.00 48.47  1  1231 LYS   A NZ  1 
ATOM   9216  N N   . TYR   A 1 1268 ? 136.462 155.692 96.188  1.00 46.05  0  1232 TYR   A N   1 
ATOM   9217  C CA  . TYR   A 1 1268 ? 135.546 154.709 95.623  1.00 45.50  0  1232 TYR   A CA  1 
ATOM   9218  C C   . TYR   A 1 1268 ? 135.681 154.558 94.113  1.00 50.79  0  1232 TYR   A C   1 
ATOM   9219  O O   . TYR   A 1 1268 ? 134.944 153.768 93.515  1.00 48.70  0  1232 TYR   A O   1 
ATOM   9220  C CB  . TYR   A 1 1268 ? 134.102 155.065 95.983  1.00 48.36  0  1232 TYR   A CB  1 
ATOM   9221  C CG  . TYR   A 1 1268 ? 133.842 155.134 97.471  1.00 47.62  0  1232 TYR   A CG  1 
ATOM   9222  C CD1 . TYR   A 1 1268 ? 133.801 153.984 98.241  1.00 43.04  0  1232 TYR   A CD1 1 
ATOM   9223  C CD2 . TYR   A 1 1268 ? 133.632 156.350 98.102  1.00 45.87  0  1232 TYR   A CD2 1 
ATOM   9224  C CE1 . TYR   A 1 1268 ? 133.567 154.044 99.594  1.00 40.82  0  1232 TYR   A CE1 1 
ATOM   9225  C CE2 . TYR   A 1 1268 ? 133.397 156.417 99.454  1.00 41.63  0  1232 TYR   A CE2 1 
ATOM   9226  C CZ  . TYR   A 1 1268 ? 133.363 155.262 100.194 1.00 42.37  0  1232 TYR   A CZ  1 
ATOM   9227  O OH  . TYR   A 1 1268 ? 133.131 155.326 101.545 1.00 53.51  0  1232 TYR   A OH  1 
ATOM   9228  N N   . THR   A 1 1269 ? 136.602 155.277 93.482  1.00 70.26  0  1233 THR   A N   1 
ATOM   9229  C CA  . THR   A 1 1269 ? 136.781 155.224 92.037  1.00 67.69  0  1233 THR   A CA  1 
ATOM   9230  C C   . THR   A 1 1269 ? 138.078 154.486 91.709  1.00 64.35  0  1233 THR   A C   1 
ATOM   9231  O O   . THR   A 1 1269 ? 138.755 153.960 92.592  1.00 60.44  0  1233 THR   A O   1 
ATOM   9232  C CB  . THR   A 1 1269 ? 136.770 156.631 91.434  1.00 69.51  0  1233 THR   A CB  1 
ATOM   9233  O OG1 . THR   A 1 1269 ? 137.851 157.396 91.981  1.00 68.24  0  1233 THR   A OG1 1 
ATOM   9234  C CG2 . THR   A 1 1269 ? 135.450 157.329 91.730  1.00 66.27  0  1233 THR   A CG2 1 
ATOM   9235  N N   . THR   A 1 1270 ? 138.413 154.447 90.422  1.00 78.15  0  1234 THR   A N   1 
ATOM   9236  C CA  . THR   A 1 1270 ? 139.602 153.735 89.971  1.00 79.14  0  1234 THR   A CA  1 
ATOM   9237  C C   . THR   A 1 1270 ? 140.867 154.405 90.494  1.00 77.11  0  1234 THR   A C   1 
ATOM   9238  O O   . THR   A 1 1270 ? 140.995 155.632 90.476  1.00 76.54  0  1234 THR   A O   1 
ATOM   9239  C CB  . THR   A 1 1270 ? 139.633 153.674 88.443  1.00 79.24  0  1234 THR   A CB  1 
ATOM   9240  O OG1 . THR   A 1 1270 ? 138.438 153.044 87.965  1.00 79.31  0  1234 THR   A OG1 1 
ATOM   9241  C CG2 . THR   A 1 1270 ? 140.843 152.887 87.956  1.00 77.08  0  1234 THR   A CG2 1 
ATOM   9242  N N   . SER   A 1 1271 ? 141.809 153.588 90.959  1.00 85.24  0  1235 SER   A N   1 
ATOM   9243  C CA  . SER   A 1 1271 ? 143.067 154.082 91.518  1.00 89.33  0  1235 SER   A CA  1 
ATOM   9244  C C   . SER   A 1 1271 ? 143.989 154.466 90.368  1.00 91.09  0  1235 SER   A C   1 
ATOM   9245  O O   . SER   A 1 1271 ? 144.687 153.630 89.792  1.00 90.39  0  1235 SER   A O   1 
ATOM   9246  C CB  . SER   A 1 1271 ? 143.702 153.030 92.420  1.00 87.66  0  1235 SER   A CB  1 
ATOM   9247  O OG  . SER   A 1 1271 ? 144.914 153.498 92.987  1.00 85.74  0  1235 SER   A OG  1 
ATOM   9248  N N   . THR   A 1 1272 ? 143.994 155.756 90.029  1.00 90.25  0  1236 THR   A N   1 
ATOM   9249  C CA  . THR   A 1 1272 ? 144.845 156.241 88.950  1.00 92.38  0  1236 THR   A CA  1 
ATOM   9250  C C   . THR   A 1 1272 ? 146.292 156.433 89.381  1.00 91.82  0  1236 THR   A C   1 
ATOM   9251  O O   . THR   A 1 1272 ? 147.145 156.697 88.526  1.00 90.16  0  1236 THR   A O   1 
ATOM   9252  C CB  . THR   A 1 1272 ? 144.297 157.559 88.395  1.00 91.38  0  1236 THR   A CB  1 
ATOM   9253  O OG1 . THR   A 1 1272 ? 144.452 158.595 89.372  1.00 87.46  0  1236 THR   A OG1 1 
ATOM   9254  C CG2 . THR   A 1 1272 ? 142.824 157.418 88.049  1.00 88.94  0  1236 THR   A CG2 1 
ATOM   9255  N N   . ILE   A 1 1273 ? 146.589 156.308 90.675  1.00 90.26  0  1237 ILE   A N   1 
ATOM   9256  C CA  . ILE   A 1 1273 ? 147.928 156.533 91.202  1.00 90.11  0  1237 ILE   A CA  1 
ATOM   9257  C C   . ILE   A 1 1273 ? 148.568 155.265 91.742  1.00 88.12  0  1237 ILE   A C   1 
ATOM   9258  O O   . ILE   A 1 1273 ? 149.731 155.304 92.158  1.00 84.18  0  1237 ILE   A O   1 
ATOM   9259  C CB  . ILE   A 1 1273 ? 147.924 157.629 92.288  1.00 89.76  0  1237 ILE   A CB  1 
ATOM   9260  C CG1 . ILE   A 1 1273 ? 146.924 157.283 93.393  1.00 87.41  0  1237 ILE   A CG1 1 
ATOM   9261  C CG2 . ILE   A 1 1273 ? 147.603 158.983 91.675  1.00 86.42  0  1237 ILE   A CG2 1 
ATOM   9262  C CD1 . ILE   A 1 1273 ? 147.012 158.190 94.599  1.00 86.16  0  1237 ILE   A CD1 1 
ATOM   9263  N N   . SER   A 1 1274 ? 147.848 154.141 91.746  1.00 87.91  0  1238 SER   A N   1 
ATOM   9264  C CA  . SER   A 1 1274 ? 148.365 152.864 92.243  1.00 87.14  0  1238 SER   A CA  1 
ATOM   9265  C C   . SER   A 1 1274 ? 148.872 152.986 93.679  1.00 88.03  0  1238 SER   A C   1 
ATOM   9266  O O   . SER   A 1 1274 ? 149.979 152.553 94.005  1.00 87.65  0  1238 SER   A O   1 
ATOM   9267  C CB  . SER   A 1 1274 ? 149.461 152.315 91.327  1.00 83.14  0  1238 SER   A CB  1 
ATOM   9268  O OG  . SER   A 1 1274 ? 148.945 152.014 90.042  1.00 84.19  0  1238 SER   A OG  1 
ATOM   9269  N N   . SER   A 1 1275 ? 148.059 153.586 94.546  1.00 76.39  0  1239 SER   A N   1 
ATOM   9270  C CA  . SER   A 1 1275 ? 148.401 153.755 95.950  1.00 72.16  0  1239 SER   A CA  1 
ATOM   9271  C C   . SER   A 1 1275 ? 147.205 153.397 96.818  1.00 71.80  0  1239 SER   A C   1 
ATOM   9272  O O   . SER   A 1 1275 ? 146.068 153.748 96.496  1.00 69.76  0  1239 SER   A O   1 
ATOM   9273  C CB  . SER   A 1 1275 ? 148.847 155.190 96.243  1.00 68.13  0  1239 SER   A CB  1 
ATOM   9274  O OG  . SER   A 1 1275 ? 149.213 155.342 97.602  1.00 68.53  0  1239 SER   A OG  1 
ATOM   9275  N N   . GLY   A 1 1276 ? 147.468 152.697 97.915  1.00 55.23  0  1240 GLY   A N   1 
ATOM   9276  C CA  . GLY   A 1 1276 ? 146.446 152.376 98.887  1.00 52.67  0  1240 GLY   A CA  1 
ATOM   9277  C C   . GLY   A 1 1276 ? 145.960 150.940 98.774  1.00 46.92  0  1240 GLY   A C   1 
ATOM   9278  O O   . GLY   A 1 1276 ? 146.063 150.292 97.731  1.00 50.06  0  1240 GLY   A O   1 
ATOM   9279  N N   . ILE   A 1 1277 ? 145.411 150.442 99.884  1.00 44.97  0  1241 ILE   A N   1 
ATOM   9280  C CA  . ILE   A 1 1277 ? 144.863 149.090 99.918  1.00 46.51  0  1241 ILE   A CA  1 
ATOM   9281  C C   . ILE   A 1 1277 ? 143.576 149.041 99.107  1.00 44.49  0  1241 ILE   A C   1 
ATOM   9282  O O   . ILE   A 1 1277 ? 142.751 149.956 99.174  1.00 38.83  0  1241 ILE   A O   1 
ATOM   9283  C CB  . ILE   A 1 1277 ? 144.614 148.649 101.370 1.00 45.81  0  1241 ILE   A CB  1 
ATOM   9284  C CG1 . ILE   A 1 1277 ? 145.889 148.773 102.197 1.00 47.04  0  1241 ILE   A CG1 1 
ATOM   9285  C CG2 . ILE   A 1 1277 ? 144.101 147.227 101.418 1.00 44.07  0  1241 ILE   A CG2 1 
ATOM   9286  C CD1 . ILE   A 1 1277 ? 145.728 148.316 103.624 1.00 45.82  0  1241 ILE   A CD1 1 
ATOM   9287  N N   . ILE   A 1 1278 ? 143.390 147.970 98.340  1.00 45.08  0  1242 ILE   A N   1 
ATOM   9288  C CA  . ILE   A 1 1278 ? 142.212 147.805 97.496  1.00 39.34  0  1242 ILE   A CA  1 
ATOM   9289  C C   . ILE   A 1 1278 ? 141.346 146.704 98.089  1.00 39.88  0  1242 ILE   A C   1 
ATOM   9290  O O   . ILE   A 1 1278 ? 141.772 145.547 98.166  1.00 43.04  0  1242 ILE   A O   1 
ATOM   9291  C CB  . ILE   A 1 1278 ? 142.594 147.471 96.047  1.00 35.09  0  1242 ILE   A CB  1 
ATOM   9292  C CG1 . ILE   A 1 1278 ? 143.471 148.569 95.452  1.00 43.53  0  1242 ILE   A CG1 1 
ATOM   9293  C CG2 . ILE   A 1 1278 ? 141.353 147.295 95.206  1.00 40.33  0  1242 ILE   A CG2 1 
ATOM   9294  C CD1 . ILE   A 1 1278 ? 144.414 148.069 94.382  1.00 43.89  0  1242 ILE   A CD1 1 
ATOM   9295  N N   . ILE   A 1 1279 ? 140.127 147.051 98.492  1.00 40.02  0  1243 ILE   A N   1 
ATOM   9296  C CA  . ILE   A 1 1279 ? 139.156 146.079 98.980  1.00 39.92  0  1243 ILE   A CA  1 
ATOM   9297  C C   . ILE   A 1 1279 ? 138.052 145.962 97.939  1.00 44.82  0  1243 ILE   A C   1 
ATOM   9298  O O   . ILE   A 1 1279 ? 137.388 146.953 97.612  1.00 37.66  0  1243 ILE   A O   1 
ATOM   9299  C CB  . ILE   A 1 1279 ? 138.585 146.473 100.349 1.00 35.68  0  1243 ILE   A CB  1 
ATOM   9300  C CG1 . ILE   A 1 1279 ? 139.671 147.086 101.232 1.00 36.10  0  1243 ILE   A CG1 1 
ATOM   9301  C CG2 . ILE   A 1 1279 ? 137.981 145.266 101.037 1.00 41.46  0  1243 ILE   A CG2 1 
ATOM   9302  C CD1 . ILE   A 1 1279 ? 140.649 146.090 101.781 1.00 41.98  0  1243 ILE   A CD1 1 
ATOM   9303  N N   . GLU   A 1 1280 ? 137.853 144.752 97.423  1.00 43.28  0  1244 GLU   A N   1 
ATOM   9304  C CA  . GLU   A 1 1280 ? 136.915 144.489 96.345  1.00 42.40  0  1244 GLU   A CA  1 
ATOM   9305  C C   . GLU   A 1 1280 ? 135.843 143.513 96.808  1.00 48.10  0  1244 GLU   A C   1 
ATOM   9306  O O   . GLU   A 1 1280 ? 136.064 142.685 97.695  1.00 47.21  0  1244 GLU   A O   1 
ATOM   9307  C CB  . GLU   A 1 1280 ? 137.631 143.921 95.115  1.00 42.71  0  1244 GLU   A CB  1 
ATOM   9308  C CG  . GLU   A 1 1280 ? 138.781 144.771 94.621  1.00 45.31  0  1244 GLU   A CG  1 
ATOM   9309  C CD  . GLU   A 1 1280 ? 139.763 143.985 93.782  1.00 47.67  0  1244 GLU   A CD  1 
ATOM   9310  O OE1 . GLU   A 1 1280 ? 139.544 142.771 93.599  1.00 49.85  0  1244 GLU   A OE1 1 
ATOM   9311  O OE2 . GLU   A 1 1280 ? 140.753 144.579 93.308  1.00 41.70  -1 1244 GLU   A OE2 1 
ATOM   9312  N N   . LYS   A 1 1281 ? 134.674 143.619 96.185  1.00 51.20  0  1245 LYS   A N   1 
ATOM   9313  C CA  . LYS   A 1 1281 ? 133.534 142.767 96.491  1.00 49.42  0  1245 LYS   A CA  1 
ATOM   9314  C C   . LYS   A 1 1281 ? 133.482 141.625 95.484  1.00 48.44  0  1245 LYS   A C   1 
ATOM   9315  O O   . LYS   A 1 1281 ? 133.223 141.851 94.297  1.00 44.25  0  1245 LYS   A O   1 
ATOM   9316  C CB  . LYS   A 1 1281 ? 132.236 143.574 96.462  1.00 52.20  0  1245 LYS   A CB  1 
ATOM   9317  C CG  . LYS   A 1 1281 ? 130.973 142.739 96.500  1.00 50.77  0  1245 LYS   A CG  1 
ATOM   9318  C CD  . LYS   A 1 1281 ? 129.755 143.608 96.744  1.00 47.68  0  1245 LYS   A CD  1 
ATOM   9319  C CE  . LYS   A 1 1281 ? 129.469 144.515 95.557  1.00 48.12  0  1245 LYS   A CE  1 
ATOM   9320  N NZ  . LYS   A 1 1281 ? 128.550 143.894 94.567  1.00 44.85  1  1245 LYS   A NZ  1 
ATOM   9321  N N   . TYR   A 1 1282 ? 133.730 140.404 95.957  1.00 52.41  0  1246 TYR   A N   1 
ATOM   9322  C CA  . TYR   A 1 1282 ? 133.688 139.235 95.088  1.00 50.87  0  1246 TYR   A CA  1 
ATOM   9323  C C   . TYR   A 1 1282 ? 132.277 138.707 94.881  1.00 49.83  0  1246 TYR   A C   1 
ATOM   9324  O O   . TYR   A 1 1282 ? 132.010 138.058 93.863  1.00 52.25  0  1246 TYR   A O   1 
ATOM   9325  C CB  . TYR   A 1 1282 ? 134.574 138.124 95.652  1.00 46.10  0  1246 TYR   A CB  1 
ATOM   9326  C CG  . TYR   A 1 1282 ? 136.017 138.248 95.231  1.00 51.25  0  1246 TYR   A CG  1 
ATOM   9327  C CD1 . TYR   A 1 1282 ? 136.428 139.283 94.404  1.00 50.32  0  1246 TYR   A CD1 1 
ATOM   9328  C CD2 . TYR   A 1 1282 ? 136.963 137.331 95.651  1.00 52.04  0  1246 TYR   A CD2 1 
ATOM   9329  C CE1 . TYR   A 1 1282 ? 137.742 139.405 94.015  1.00 50.59  0  1246 TYR   A CE1 1 
ATOM   9330  C CE2 . TYR   A 1 1282 ? 138.281 137.442 95.267  1.00 50.88  0  1246 TYR   A CE2 1 
ATOM   9331  C CZ  . TYR   A 1 1282 ? 138.666 138.482 94.449  1.00 52.04  0  1246 TYR   A CZ  1 
ATOM   9332  O OH  . TYR   A 1 1282 ? 139.980 138.598 94.060  1.00 54.21  0  1246 TYR   A OH  1 
ATOM   9333  N N   . ASN   A 1 1283 ? 131.372 138.974 95.818  1.00 53.64  0  1247 ASN   A N   1 
ATOM   9334  C CA  . ASN   A 1 1283 ? 129.970 138.612 95.667  1.00 55.80  0  1247 ASN   A CA  1 
ATOM   9335  C C   . ASN   A 1 1283 ? 129.362 139.378 94.499  1.00 56.89  0  1247 ASN   A C   1 
ATOM   9336  O O   . ASN   A 1 1283 ? 129.814 140.479 94.170  1.00 54.30  0  1247 ASN   A O   1 
ATOM   9337  C CB  . ASN   A 1 1283 ? 129.215 138.901 96.966  1.00 55.43  0  1247 ASN   A CB  1 
ATOM   9338  C CG  . ASN   A 1 1283 ? 127.817 138.325 96.975  1.00 55.25  0  1247 ASN   A CG  1 
ATOM   9339  O OD1 . ASN   A 1 1283 ? 126.965 138.715 96.178  1.00 48.97  0  1247 ASN   A OD1 1 
ATOM   9340  N ND2 . ASN   A 1 1283 ? 127.570 137.395 97.889  1.00 57.99  0  1247 ASN   A ND2 1 
ATOM   9341  N N   . VAL   A 1 1284 ? 128.351 138.801 93.853  1.00 57.54  0  1248 VAL   A N   1 
ATOM   9342  C CA  . VAL   A 1 1284 ? 127.712 139.453 92.718  1.00 57.37  0  1248 VAL   A CA  1 
ATOM   9343  C C   . VAL   A 1 1284 ? 126.460 140.232 93.109  1.00 60.52  0  1248 VAL   A C   1 
ATOM   9344  O O   . VAL   A 1 1284 ? 126.011 141.086 92.329  1.00 62.43  0  1248 VAL   A O   1 
ATOM   9345  C CB  . VAL   A 1 1284 ? 127.373 138.427 91.618  1.00 57.55  0  1248 VAL   A CB  1 
ATOM   9346  C CG1 . VAL   A 1 1284 ? 128.627 138.042 90.853  1.00 58.21  0  1248 VAL   A CG1 1 
ATOM   9347  C CG2 . VAL   A 1 1284 ? 126.725 137.197 92.230  1.00 57.34  0  1248 VAL   A CG2 1 
ATOM   9348  N N   . ASN   A 1 1285 ? 125.888 139.969 94.280  1.00 58.51  0  1249 ASN   A N   1 
ATOM   9349  C CA  . ASN   A 1 1285 ? 124.690 140.668 94.717  1.00 55.17  0  1249 ASN   A CA  1 
ATOM   9350  C C   . ASN   A 1 1285 ? 125.029 142.077 95.187  1.00 57.03  0  1249 ASN   A C   1 
ATOM   9351  O O   . ASN   A 1 1285 ? 126.112 142.335 95.718  1.00 60.10  0  1249 ASN   A O   1 
ATOM   9352  C CB  . ASN   A 1 1285 ? 124.003 139.898 95.842  1.00 54.48  0  1249 ASN   A CB  1 
ATOM   9353  C CG  . ASN   A 1 1285 ? 123.541 138.526 95.409  1.00 59.80  0  1249 ASN   A CG  1 
ATOM   9354  O OD1 . ASN   A 1 1285 ? 122.971 138.364 94.331  1.00 61.95  0  1249 ASN   A OD1 1 
ATOM   9355  N ND2 . ASN   A 1 1285 ? 123.787 137.527 96.247  1.00 58.95  0  1249 ASN   A ND2 1 
ATOM   9356  N N   . SER   A 1 1286 ? 124.082 142.995 94.986  1.00 53.04  0  1250 SER   A N   1 
ATOM   9357  C CA  . SER   A 1 1286 ? 124.285 144.366 95.440  1.00 55.49  0  1250 SER   A CA  1 
ATOM   9358  C C   . SER   A 1 1286 ? 124.350 144.448 96.958  1.00 53.15  0  1250 SER   A C   1 
ATOM   9359  O O   . SER   A 1 1286 ? 125.081 145.281 97.502  1.00 55.06  0  1250 SER   A O   1 
ATOM   9360  C CB  . SER   A 1 1286 ? 123.174 145.269 94.907  1.00 55.38  0  1250 SER   A CB  1 
ATOM   9361  O OG  . SER   A 1 1286 ? 123.316 145.479 93.514  1.00 55.94  0  1250 SER   A OG  1 
ATOM   9362  N N   . LEU   A 1 1287 ? 123.600 143.601 97.655  1.00 48.95  0  1251 LEU   A N   1 
ATOM   9363  C CA  . LEU   A 1 1287 ? 123.585 143.570 99.112  1.00 49.91  0  1251 LEU   A CA  1 
ATOM   9364  C C   . LEU   A 1 1287 ? 124.283 142.301 99.570  1.00 48.33  0  1251 LEU   A C   1 
ATOM   9365  O O   . LEU   A 1 1287 ? 123.934 141.204 99.126  1.00 49.68  0  1251 LEU   A O   1 
ATOM   9366  C CB  . LEU   A 1 1287 ? 122.156 143.623 99.652  1.00 53.52  0  1251 LEU   A CB  1 
ATOM   9367  C CG  . LEU   A 1 1287 ? 121.572 145.016 99.886  1.00 48.35  0  1251 LEU   A CG  1 
ATOM   9368  C CD1 . LEU   A 1 1287 ? 122.474 145.809 100.812 1.00 41.49  0  1251 LEU   A CD1 1 
ATOM   9369  C CD2 . LEU   A 1 1287 ? 121.354 145.755 98.575  1.00 46.12  0  1251 LEU   A CD2 1 
ATOM   9370  N N   . THR   A 1 1288 ? 125.261 142.450 100.460 1.00 38.02  0  1252 THR   A N   1 
ATOM   9371  C CA  . THR   A 1 1288 ? 126.096 141.340 100.894 1.00 36.42  0  1252 THR   A CA  1 
ATOM   9372  C C   . THR   A 1 1288 ? 125.905 141.008 102.370 1.00 41.51  0  1252 THR   A C   1 
ATOM   9373  O O   . THR   A 1 1288 ? 126.735 140.317 102.962 1.00 48.07  0  1252 THR   A O   1 
ATOM   9374  C CB  . THR   A 1 1288 ? 127.565 141.642 100.612 1.00 47.53  0  1252 THR   A CB  1 
ATOM   9375  O OG1 . THR   A 1 1288 ? 127.816 143.035 100.829 1.00 50.80  0  1252 THR   A OG1 1 
ATOM   9376  C CG2 . THR   A 1 1288 ? 127.907 141.301 99.180  1.00 47.89  0  1252 THR   A CG2 1 
ATOM   9377  N N   . ARG   A 1 1289 ? 124.822 141.485 102.979 1.00 37.55  0  1253 ARG   A N   1 
ATOM   9378  C CA  . ARG   A 1 1289 ? 124.536 141.168 104.372 1.00 29.42  0  1253 ARG   A CA  1 
ATOM   9379  C C   . ARG   A 1 1289 ? 123.784 139.848 104.455 1.00 32.70  0  1253 ARG   A C   1 
ATOM   9380  O O   . ARG   A 1 1289 ? 122.785 139.650 103.757 1.00 33.49  0  1253 ARG   A O   1 
ATOM   9381  C CB  . ARG   A 1 1289 ? 123.723 142.271 105.046 1.00 27.98  0  1253 ARG   A CB  1 
ATOM   9382  C CG  . ARG   A 1 1289 ? 123.548 142.040 106.542 1.00 33.67  0  1253 ARG   A CG  1 
ATOM   9383  C CD  . ARG   A 1 1289 ? 123.183 143.313 107.279 1.00 33.48  0  1253 ARG   A CD  1 
ATOM   9384  N NE  . ARG   A 1 1289 ? 121.842 143.773 106.947 1.00 30.59  0  1253 ARG   A NE  1 
ATOM   9385  C CZ  . ARG   A 1 1289 ? 121.280 144.861 107.454 1.00 20.81  0  1253 ARG   A CZ  1 
ATOM   9386  N NH1 . ARG   A 1 1289 ? 121.916 145.622 108.327 1.00 21.77  1  1253 ARG   A NH1 1 
ATOM   9387  N NH2 . ARG   A 1 1289 ? 120.052 145.194 107.072 1.00 23.83  0  1253 ARG   A NH2 1 
ATOM   9388  N N   . GLY   A 1 1290 ? 124.262 138.956 105.315 1.00 32.90  0  1254 GLY   A N   1 
ATOM   9389  C CA  . GLY   A 1 1290 ? 123.670 137.641 105.421 1.00 37.18  0  1254 GLY   A CA  1 
ATOM   9390  C C   . GLY   A 1 1290 ? 124.008 136.706 104.288 1.00 34.34  0  1254 GLY   A C   1 
ATOM   9391  O O   . GLY   A 1 1290 ? 123.258 135.759 104.039 1.00 40.44  0  1254 GLY   A O   1 
ATOM   9392  N N   . GLU   A 1 1291 ? 125.109 136.949 103.583 1.00 34.64  0  1255 GLU   A N   1 
ATOM   9393  C CA  . GLU   A 1 1291 ? 125.553 136.102 102.488 1.00 36.81  0  1255 GLU   A CA  1 
ATOM   9394  C C   . GLU   A 1 1291 ? 127.024 135.770 102.676 1.00 43.21  0  1255 GLU   A C   1 
ATOM   9395  O O   . GLU   A 1 1291 ? 127.810 136.621 103.099 1.00 45.40  0  1255 GLU   A O   1 
ATOM   9396  C CB  . GLU   A 1 1291 ? 125.344 136.784 101.138 1.00 38.11  0  1255 GLU   A CB  1 
ATOM   9397  C CG  . GLU   A 1 1291 ? 123.929 137.263 100.909 1.00 44.90  0  1255 GLU   A CG  1 
ATOM   9398  C CD  . GLU   A 1 1291 ? 123.765 137.961 99.581  1.00 53.93  0  1255 GLU   A CD  1 
ATOM   9399  O OE1 . GLU   A 1 1291 ? 124.772 138.093 98.857  1.00 56.28  0  1255 GLU   A OE1 1 
ATOM   9400  O OE2 . GLU   A 1 1291 ? 122.631 138.376 99.261  1.00 53.57  -1 1255 GLU   A OE2 1 
ATOM   9401  N N   . ARG   A 1 1292 ? 127.393 134.534 102.359 1.00 37.27  0  1256 ARG   A N   1 
ATOM   9402  C CA  . ARG   A 1 1292 ? 128.772 134.082 102.466 1.00 38.29  0  1256 ARG   A CA  1 
ATOM   9403  C C   . ARG   A 1 1292 ? 129.404 134.040 101.083 1.00 42.78  0  1256 ARG   A C   1 
ATOM   9404  O O   . ARG   A 1 1292 ? 128.803 133.525 100.135 1.00 45.98  0  1256 ARG   A O   1 
ATOM   9405  C CB  . ARG   A 1 1292 ? 128.853 132.707 103.124 1.00 34.05  0  1256 ARG   A CB  1 
ATOM   9406  C CG  . ARG   A 1 1292 ? 130.265 132.166 103.198 1.00 38.90  0  1256 ARG   A CG  1 
ATOM   9407  C CD  . ARG   A 1 1292 ? 130.356 130.974 104.117 1.00 35.58  0  1256 ARG   A CD  1 
ATOM   9408  N NE  . ARG   A 1 1292 ? 130.657 131.362 105.489 1.00 39.50  0  1256 ARG   A NE  1 
ATOM   9409  C CZ  . ARG   A 1 1292 ? 131.730 130.964 106.159 1.00 43.86  0  1256 ARG   A CZ  1 
ATOM   9410  N NH1 . ARG   A 1 1292 ? 132.636 130.176 105.606 1.00 40.51  1  1256 ARG   A NH1 1 
ATOM   9411  N NH2 . ARG   A 1 1292 ? 131.893 131.362 107.417 1.00 42.36  0  1256 ARG   A NH2 1 
ATOM   9412  N N   . GLY   A 1 1293 ? 130.611 134.585 100.971 1.00 36.89  0  1257 GLY   A N   1 
ATOM   9413  C CA  . GLY   A 1 1293 ? 131.317 134.630 99.715  1.00 36.32  0  1257 GLY   A CA  1 
ATOM   9414  C C   . GLY   A 1 1293 ? 132.364 133.542 99.598  1.00 36.58  0  1257 GLY   A C   1 
ATOM   9415  O O   . GLY   A 1 1293 ? 132.417 132.605 100.400 1.00 39.12  0  1257 GLY   A O   1 
ATOM   9416  N N   . PRO   A 1 1294 ? 133.217 133.647 98.587  1.00 26.08  0  1258 PRO   A N   1 
ATOM   9417  C CA  . PRO   A 1 1294 ? 134.219 132.601 98.354  1.00 28.02  0  1258 PRO   A CA  1 
ATOM   9418  C C   . PRO   A 1 1294 ? 135.435 132.680 99.263  1.00 34.29  0  1258 PRO   A C   1 
ATOM   9419  O O   . PRO   A 1 1294 ? 135.974 131.645 99.665  1.00 37.62  0  1258 PRO   A O   1 
ATOM   9420  C CB  . PRO   A 1 1294 ? 134.616 132.833 96.893  1.00 32.30  0  1258 PRO   A CB  1 
ATOM   9421  C CG  . PRO   A 1 1294 ? 134.390 134.284 96.684  1.00 33.44  0  1258 PRO   A CG  1 
ATOM   9422  C CD  . PRO   A 1 1294 ? 133.192 134.643 97.504  1.00 31.49  0  1258 PRO   A CD  1 
ATOM   9423  N N   . THR   A 1 1295 ? 135.874 133.891 99.599  1.00 39.45  0  1259 THR   A N   1 
ATOM   9424  C CA  . THR   A 1 1295 ? 137.180 134.075 100.215 1.00 40.10  0  1259 THR   A CA  1 
ATOM   9425  C C   . THR   A 1 1295 ? 137.202 133.534 101.643 1.00 41.88  0  1259 THR   A C   1 
ATOM   9426  O O   . THR   A 1 1295 ? 136.169 133.293 102.269 1.00 41.95  0  1259 THR   A O   1 
ATOM   9427  C CB  . THR   A 1 1295 ? 137.575 135.550 100.207 1.00 40.26  0  1259 THR   A CB  1 
ATOM   9428  O OG1 . THR   A 1 1295 ? 136.668 136.294 101.024 1.00 32.69  0  1259 THR   A OG1 1 
ATOM   9429  C CG2 . THR   A 1 1295 ? 137.524 136.096 98.801  1.00 42.81  0  1259 THR   A CG2 1 
ATOM   9430  N N   . LYS   A 1 1296 ? 138.415 133.334 102.150 1.00 45.17  0  1260 LYS   A N   1 
ATOM   9431  C CA  . LYS   A 1 1296 ? 138.604 132.836 103.501 1.00 42.85  0  1260 LYS   A CA  1 
ATOM   9432  C C   . LYS   A 1 1296 ? 138.223 133.907 104.523 1.00 49.79  0  1260 LYS   A C   1 
ATOM   9433  O O   . LYS   A 1 1296 ? 138.343 135.105 104.252 1.00 55.00  0  1260 LYS   A O   1 
ATOM   9434  C CB  . LYS   A 1 1296 ? 140.055 132.415 103.707 1.00 41.66  0  1260 LYS   A CB  1 
ATOM   9435  C CG  . LYS   A 1 1296 ? 141.042 133.572 103.639 1.00 42.00  0  1260 LYS   A CG  1 
ATOM   9436  C CD  . LYS   A 1 1296 ? 142.483 133.092 103.669 1.00 47.30  0  1260 LYS   A CD  1 
ATOM   9437  C CE  . LYS   A 1 1296 ? 142.938 132.629 102.294 1.00 51.44  0  1260 LYS   A CE  1 
ATOM   9438  N NZ  . LYS   A 1 1296 ? 143.001 133.754 101.322 1.00 49.63  1  1260 LYS   A NZ  1 
ATOM   9439  N N   . PRO   A 1 1297 ? 137.756 133.504 105.703 1.00 48.63  0  1261 PRO   A N   1 
ATOM   9440  C CA  . PRO   A 1 1297 ? 137.367 134.492 106.714 1.00 42.47  0  1261 PRO   A CA  1 
ATOM   9441  C C   . PRO   A 1 1297 ? 138.570 135.233 107.276 1.00 39.52  0  1261 PRO   A C   1 
ATOM   9442  O O   . PRO   A 1 1297 ? 139.681 134.704 107.346 1.00 45.41  0  1261 PRO   A O   1 
ATOM   9443  C CB  . PRO   A 1 1297 ? 136.684 133.646 107.793 1.00 39.17  0  1261 PRO   A CB  1 
ATOM   9444  C CG  . PRO   A 1 1297 ? 137.291 132.303 107.646 1.00 48.32  0  1261 PRO   A CG  1 
ATOM   9445  C CD  . PRO   A 1 1297 ? 137.556 132.125 106.176 1.00 45.86  0  1261 PRO   A CD  1 
ATOM   9446  N N   . TRP   A 1 1298 ? 138.328 136.475 107.689 1.00 36.84  0  1262 TRP   A N   1 
ATOM   9447  C CA  . TRP   A 1 1298 ? 139.354 137.335 108.275 1.00 34.78  0  1262 TRP   A CA  1 
ATOM   9448  C C   . TRP   A 1 1298 ? 139.200 137.287 109.790 1.00 38.53  0  1262 TRP   A C   1 
ATOM   9449  O O   . TRP   A 1 1298 ? 138.334 137.953 110.360 1.00 33.25  0  1262 TRP   A O   1 
ATOM   9450  C CB  . TRP   A 1 1298 ? 139.236 138.756 107.734 1.00 33.25  0  1262 TRP   A CB  1 
ATOM   9451  C CG  . TRP   A 1 1298 ? 140.250 139.708 108.278 1.00 33.22  0  1262 TRP   A CG  1 
ATOM   9452  C CD1 . TRP   A 1 1298 ? 140.019 140.744 109.129 1.00 39.53  0  1262 TRP   A CD1 1 
ATOM   9453  C CD2 . TRP   A 1 1298 ? 141.659 139.712 108.016 1.00 41.03  0  1262 TRP   A CD2 1 
ATOM   9454  N NE1 . TRP   A 1 1298 ? 141.193 141.395 109.413 1.00 39.89  0  1262 TRP   A NE1 1 
ATOM   9455  C CE2 . TRP   A 1 1298 ? 142.215 140.780 108.742 1.00 37.89  0  1262 TRP   A CE2 1 
ATOM   9456  C CE3 . TRP   A 1 1298 ? 142.503 138.914 107.241 1.00 43.01  0  1262 TRP   A CE3 1 
ATOM   9457  C CZ2 . TRP   A 1 1298 ? 143.574 141.072 108.714 1.00 33.14  0  1262 TRP   A CZ2 1 
ATOM   9458  C CZ3 . TRP   A 1 1298 ? 143.851 139.206 107.216 1.00 38.95  0  1262 TRP   A CZ3 1 
ATOM   9459  C CH2 . TRP   A 1 1298 ? 144.372 140.276 107.946 1.00 32.99  0  1262 TRP   A CH2 1 
ATOM   9460  N N   . VAL   A 1 1299 ? 140.052 136.499 110.440 1.00 41.99  0  1263 VAL   A N   1 
ATOM   9461  C CA  . VAL   A 1 1299 ? 140.005 136.305 111.885 1.00 47.29  0  1263 VAL   A CA  1 
ATOM   9462  C C   . VAL   A 1 1299 ? 140.709 137.488 112.538 1.00 49.79  0  1263 VAL   A C   1 
ATOM   9463  O O   . VAL   A 1 1299 ? 140.512 137.780 113.724 1.00 44.24  0  1263 VAL   A O   1 
ATOM   9464  C CB  . VAL   A 1 1299 ? 140.644 134.949 112.261 1.00 43.50  0  1263 VAL   A CB  1 
ATOM   9465  C CG1 . VAL   A 1 1299 ? 141.229 134.950 113.664 1.00 44.47  0  1263 VAL   A CG1 1 
ATOM   9466  C CG2 . VAL   A 1 1299 ? 139.630 133.827 112.111 1.00 44.07  0  1263 VAL   A CG2 1 
ATOM   9467  N N   . GLY   A 1 1300 ? 141.462 138.222 111.744 1.00 50.51  0  1264 GLY   A N   1 
ATOM   9468  C CA  . GLY   A 1 1300 ? 142.321 139.295 112.224 1.00 37.20  0  1264 GLY   A CA  1 
ATOM   9469  C C   . GLY   A 1 1300 ? 143.771 138.975 111.985 1.00 42.80  0  1264 GLY   A C   1 
ATOM   9470  O O   . GLY   A 1 1300 ? 144.534 139.838 111.559 1.00 46.92  0  1264 GLY   A O   1 
ATOM   9471  N N   . SER   A 1 1301 ? 144.161 137.727 112.248 1.00 58.03  0  1265 SER   A N   1 
ATOM   9472  C CA  . SER   A 1 1301 ? 145.451 137.186 111.836 1.00 62.82  0  1265 SER   A CA  1 
ATOM   9473  C C   . SER   A 1 1301 ? 146.631 137.983 112.380 1.00 62.57  0  1265 SER   A C   1 
ATOM   9474  O O   . SER   A 1 1301 ? 147.388 138.580 111.608 1.00 63.01  0  1265 SER   A O   1 
ATOM   9475  C CB  . SER   A 1 1301 ? 145.529 137.119 110.308 1.00 59.19  0  1265 SER   A CB  1 
ATOM   9476  O OG  . SER   A 1 1301 ? 144.441 136.385 109.770 1.00 58.80  0  1265 SER   A OG  1 
ATOM   9477  N N   . SER   A 1 1302 ? 146.797 138.002 113.699 1.00 61.41  0  1266 SER   A N   1 
ATOM   9478  C CA  . SER   A 1 1302 ? 147.968 138.642 114.282 1.00 67.59  0  1266 SER   A CA  1 
ATOM   9479  C C   . SER   A 1 1302 ? 149.221 137.831 113.982 1.00 67.96  0  1266 SER   A C   1 
ATOM   9480  O O   . SER   A 1 1302 ? 149.211 136.598 114.037 1.00 70.16  0  1266 SER   A O   1 
ATOM   9481  C CB  . SER   A 1 1302 ? 147.798 138.799 115.789 1.00 69.10  0  1266 SER   A CB  1 
ATOM   9482  O OG  . SER   A 1 1302 ? 148.963 139.348 116.379 1.00 68.97  0  1266 SER   A OG  1 
ATOM   9483  N N   . THR   A 1 1303 ? 150.309 138.530 113.673 1.00 67.92  0  1267 THR   A N   1 
ATOM   9484  C CA  . THR   A 1 1303 ? 151.575 137.884 113.354 1.00 72.09  0  1267 THR   A CA  1 
ATOM   9485  C C   . THR   A 1 1303 ? 152.368 137.680 114.639 1.00 77.05  0  1267 THR   A C   1 
ATOM   9486  O O   . THR   A 1 1303 ? 152.711 138.648 115.326 1.00 75.65  0  1267 THR   A O   1 
ATOM   9487  C CB  . THR   A 1 1303 ? 152.377 138.711 112.353 1.00 74.58  0  1267 THR   A CB  1 
ATOM   9488  O OG1 . THR   A 1 1303 ? 151.551 139.031 111.228 1.00 78.42  0  1267 THR   A OG1 1 
ATOM   9489  C CG2 . THR   A 1 1303 ? 153.577 137.921 111.869 1.00 73.26  0  1267 THR   A CG2 1 
ATOM   9490  N N   . GLN   A 1 1304 ? 152.664 136.422 114.953 1.00 83.34  0  1268 GLN   A N   1 
ATOM   9491  C CA  . GLN   A 1 1304 ? 153.302 136.059 116.206 1.00 81.85  0  1268 GLN   A CA  1 
ATOM   9492  C C   . GLN   A 1 1304 ? 154.823 136.112 116.073 1.00 81.31  0  1268 GLN   A C   1 
ATOM   9493  O O   . GLN   A 1 1304 ? 155.377 136.332 114.993 1.00 79.14  0  1268 GLN   A O   1 
ATOM   9494  C CB  . GLN   A 1 1304 ? 152.834 134.673 116.645 1.00 79.49  0  1268 GLN   A CB  1 
ATOM   9495  C CG  . GLN   A 1 1304 ? 153.325 133.541 115.755 1.00 79.99  0  1268 GLN   A CG  1 
ATOM   9496  C CD  . GLN   A 1 1304 ? 152.444 133.322 114.539 1.00 83.47  0  1268 GLN   A CD  1 
ATOM   9497  O OE1 . GLN   A 1 1304 ? 151.978 134.273 113.913 1.00 83.26  0  1268 GLN   A OE1 1 
ATOM   9498  N NE2 . GLN   A 1 1304 ? 152.206 132.060 114.202 1.00 82.59  0  1268 GLN   A NE2 1 
ATOM   9499  N N   . GLU   A 1 1305 ? 155.505 135.902 117.193 1.00 75.15  0  1269 GLU   A N   1 
ATOM   9500  C CA  . GLU   A 1 1305 ? 156.957 135.943 117.245 1.00 72.78  0  1269 GLU   A CA  1 
ATOM   9501  C C   . GLU   A 1 1305 ? 157.552 134.581 116.905 1.00 75.09  0  1269 GLU   A C   1 
ATOM   9502  O O   . GLU   A 1 1305 ? 156.911 133.540 117.069 1.00 74.94  0  1269 GLU   A O   1 
ATOM   9503  C CB  . GLU   A 1 1305 ? 157.424 136.386 118.631 1.00 71.74  0  1269 GLU   A CB  1 
ATOM   9504  C CG  . GLU   A 1 1305 ? 156.868 135.542 119.762 1.00 71.81  0  1269 GLU   A CG  1 
ATOM   9505  C CD  . GLU   A 1 1305 ? 157.181 136.119 121.125 1.00 75.24  0  1269 GLU   A CD  1 
ATOM   9506  O OE1 . GLU   A 1 1305 ? 157.822 137.187 121.184 1.00 72.48  0  1269 GLU   A OE1 1 
ATOM   9507  O OE2 . GLU   A 1 1305 ? 156.791 135.505 122.139 1.00 79.05  -1 1269 GLU   A OE2 1 
ATOM   9508  N N   . LYS   A 1 1306 ? 158.794 134.603 116.428 1.00 72.41  0  1270 LYS   A N   1 
ATOM   9509  C CA  . LYS   A 1 1306 ? 159.517 133.397 116.048 1.00 72.67  0  1270 LYS   A CA  1 
ATOM   9510  C C   . LYS   A 1 1306 ? 160.557 133.080 117.112 1.00 71.23  0  1270 LYS   A C   1 
ATOM   9511  O O   . LYS   A 1 1306 ? 161.371 133.939 117.463 1.00 71.25  0  1270 LYS   A O   1 
ATOM   9512  C CB  . LYS   A 1 1306 ? 160.195 133.578 114.690 1.00 69.81  0  1270 LYS   A CB  1 
ATOM   9513  C CG  . LYS   A 1 1306 ? 159.325 134.261 113.657 1.00 72.37  0  1270 LYS   A CG  1 
ATOM   9514  C CD  . LYS   A 1 1306 ? 160.023 134.346 112.315 1.00 71.30  0  1270 LYS   A CD  1 
ATOM   9515  C CE  . LYS   A 1 1306 ? 159.575 135.578 111.547 1.00 73.63  0  1270 LYS   A CE  1 
ATOM   9516  N NZ  . LYS   A 1 1306 ? 158.139 135.505 111.162 1.00 70.19  1  1270 LYS   A NZ  1 
ATOM   9517  N N   . LYS   A 1 1307 ? 160.531 131.852 117.621 1.00 62.56  0  1271 LYS   A N   1 
ATOM   9518  C CA  . LYS   A 1 1307 ? 161.445 131.463 118.683 1.00 61.38  0  1271 LYS   A CA  1 
ATOM   9519  C C   . LYS   A 1 1307 ? 161.807 129.994 118.537 1.00 68.21  0  1271 LYS   A C   1 
ATOM   9520  O O   . LYS   A 1 1307 ? 160.941 129.156 118.274 1.00 67.96  0  1271 LYS   A O   1 
ATOM   9521  C CB  . LYS   A 1 1307 ? 160.833 131.723 120.064 1.00 61.81  0  1271 LYS   A CB  1 
ATOM   9522  C CG  . LYS   A 1 1307 ? 159.376 131.315 120.188 1.00 65.45  0  1271 LYS   A CG  1 
ATOM   9523  C CD  . LYS   A 1 1307 ? 159.041 130.896 121.607 1.00 66.00  0  1271 LYS   A CD  1 
ATOM   9524  C CE  . LYS   A 1 1307 ? 157.542 130.891 121.845 1.00 63.53  0  1271 LYS   A CE  1 
ATOM   9525  N NZ  . LYS   A 1 1307 ? 157.196 130.343 123.186 1.00 62.88  1  1271 LYS   A NZ  1 
ATOM   9526  N N   . THR   A 1 1308 ? 163.091 129.690 118.712 1.00 70.11  0  1272 THR   A N   1 
ATOM   9527  C CA  . THR   A 1 1308 ? 163.573 128.312 118.688 1.00 65.05  0  1272 THR   A CA  1 
ATOM   9528  C C   . THR   A 1 1308 ? 163.561 127.787 120.116 1.00 65.30  0  1272 THR   A C   1 
ATOM   9529  O O   . THR   A 1 1308 ? 164.429 128.126 120.924 1.00 67.33  0  1272 THR   A O   1 
ATOM   9530  C CB  . THR   A 1 1308 ? 164.966 128.227 118.076 1.00 64.23  0  1272 THR   A CB  1 
ATOM   9531  O OG1 . THR   A 1 1308 ? 165.914 128.857 118.945 1.00 67.62  0  1272 THR   A OG1 1 
ATOM   9532  C CG2 . THR   A 1 1308 ? 164.990 128.904 116.726 1.00 61.52  0  1272 THR   A CG2 1 
ATOM   9533  N N   . MET   A 1 1309 ? 162.579 126.957 120.423 1.00 66.39  0  1273 MET   A N   1 
ATOM   9534  C CA  . MET   A 1 1309 ? 162.455 126.417 121.767 1.00 68.91  0  1273 MET   A CA  1 
ATOM   9535  C C   . MET   A 1 1309 ? 163.541 125.371 121.992 1.00 69.43  0  1273 MET   A C   1 
ATOM   9536  O O   . MET   A 1 1309 ? 163.632 124.408 121.223 1.00 70.17  0  1273 MET   A O   1 
ATOM   9537  C CB  . MET   A 1 1309 ? 161.074 125.793 121.958 1.00 71.30  0  1273 MET   A CB  1 
ATOM   9538  C CG  . MET   A 1 1309 ? 159.982 126.751 122.421 1.00 69.62  0  1273 MET   A CG  1 
ATOM   9539  S SD  . MET   A 1 1309 ? 160.066 127.246 124.151 1.00 80.90  0  1273 MET   A SD  1 
ATOM   9540  C CE  . MET   A 1 1309 ? 160.760 125.794 124.923 1.00 69.81  0  1273 MET   A CE  1 
ATOM   9541  N N   . PRO   A 1 1310 ? 164.384 125.526 123.009 1.00 71.50  0  1274 PRO   A N   1 
ATOM   9542  C CA  . PRO   A 1 1310 ? 165.402 124.507 123.279 1.00 71.89  0  1274 PRO   A CA  1 
ATOM   9543  C C   . PRO   A 1 1310 ? 164.770 123.197 123.714 1.00 75.03  0  1274 PRO   A C   1 
ATOM   9544  O O   . PRO   A 1 1310 ? 163.682 123.166 124.295 1.00 75.50  0  1274 PRO   A O   1 
ATOM   9545  C CB  . PRO   A 1 1310 ? 166.238 125.124 124.406 1.00 70.21  0  1274 PRO   A CB  1 
ATOM   9546  C CG  . PRO   A 1 1310 ? 165.924 126.583 124.370 1.00 70.62  0  1274 PRO   A CG  1 
ATOM   9547  C CD  . PRO   A 1 1310 ? 164.510 126.683 123.905 1.00 71.82  0  1274 PRO   A CD  1 
ATOM   9548  N N   . VAL   A 1 1311 ? 165.471 122.104 123.423 1.00 76.07  0  1275 VAL   A N   1 
ATOM   9549  C CA  . VAL   A 1 1311 ? 164.942 120.762 123.633 1.00 75.71  0  1275 VAL   A CA  1 
ATOM   9550  C C   . VAL   A 1 1311 ? 165.305 120.281 125.031 1.00 76.56  0  1275 VAL   A C   1 
ATOM   9551  O O   . VAL   A 1 1311 ? 166.485 120.249 125.403 1.00 74.80  0  1275 VAL   A O   1 
ATOM   9552  C CB  . VAL   A 1 1311 ? 165.461 119.791 122.559 1.00 74.15  0  1275 VAL   A CB  1 
ATOM   9553  C CG1 . VAL   A 1 1311 ? 166.968 119.935 122.373 1.00 75.25  0  1275 VAL   A CG1 1 
ATOM   9554  C CG2 . VAL   A 1 1311 ? 165.101 118.360 122.922 1.00 73.08  0  1275 VAL   A CG2 1 
ATOM   9555  N N   . TYR   A 1 1312 ? 164.290 119.911 125.805 1.00 74.19  0  1276 TYR   A N   1 
ATOM   9556  C CA  . TYR   A 1 1312 ? 164.472 119.332 127.132 1.00 72.33  0  1276 TYR   A CA  1 
ATOM   9557  C C   . TYR   A 1 1312 ? 163.136 118.740 127.566 1.00 73.39  0  1276 TYR   A C   1 
ATOM   9558  O O   . TYR   A 1 1312 ? 162.118 118.890 126.884 1.00 74.29  0  1276 TYR   A O   1 
ATOM   9559  C CB  . TYR   A 1 1312 ? 164.986 120.353 128.152 1.00 74.70  0  1276 TYR   A CB  1 
ATOM   9560  C CG  . TYR   A 1 1312 ? 164.171 121.622 128.271 1.00 73.70  0  1276 TYR   A CG  1 
ATOM   9561  C CD1 . TYR   A 1 1312 ? 164.148 122.561 127.252 1.00 73.05  0  1276 TYR   A CD1 1 
ATOM   9562  C CD2 . TYR   A 1 1312 ? 163.431 121.882 129.414 1.00 72.67  0  1276 TYR   A CD2 1 
ATOM   9563  C CE1 . TYR   A 1 1312 ? 163.405 123.716 127.366 1.00 76.01  0  1276 TYR   A CE1 1 
ATOM   9564  C CE2 . TYR   A 1 1312 ? 162.687 123.034 129.537 1.00 74.37  0  1276 TYR   A CE2 1 
ATOM   9565  C CZ  . TYR   A 1 1312 ? 162.677 123.948 128.509 1.00 78.65  0  1276 TYR   A CZ  1 
ATOM   9566  O OH  . TYR   A 1 1312 ? 161.937 125.100 128.622 1.00 76.72  0  1276 TYR   A OH  1 
ATOM   9567  N N   . ASN   A 1 1313 ? 163.149 118.064 128.715 1.00 73.92  0  1277 ASN   A N   1 
ATOM   9568  C CA  . ASN   A 1 1313 ? 161.948 117.430 129.258 1.00 71.69  0  1277 ASN   A CA  1 
ATOM   9569  C C   . ASN   A 1 1313 ? 161.049 118.517 129.836 1.00 73.62  0  1277 ASN   A C   1 
ATOM   9570  O O   . ASN   A 1 1313 ? 161.098 118.854 131.022 1.00 76.14  0  1277 ASN   A O   1 
ATOM   9571  C CB  . ASN   A 1 1313 ? 162.314 116.384 130.301 1.00 72.71  0  1277 ASN   A CB  1 
ATOM   9572  C CG  . ASN   A 1 1313 ? 162.840 115.105 129.684 1.00 75.62  0  1277 ASN   A CG  1 
ATOM   9573  O OD1 . ASN   A 1 1313 ? 163.551 115.135 128.680 1.00 76.26  0  1277 ASN   A OD1 1 
ATOM   9574  N ND2 . ASN   A 1 1313 ? 162.483 113.971 130.275 1.00 72.97  0  1277 ASN   A ND2 1 
ATOM   9575  N N   . ARG   A 1 1314 ? 160.201 119.069 128.967 1.00 72.99  0  1278 ARG   A N   1 
ATOM   9576  C CA  . ARG   A 1 1314 ? 159.381 120.216 129.337 1.00 76.14  0  1278 ARG   A CA  1 
ATOM   9577  C C   . ARG   A 1 1314 ? 158.343 119.866 130.394 1.00 72.75  0  1278 ARG   A C   1 
ATOM   9578  O O   . ARG   A 1 1314 ? 157.899 120.753 131.130 1.00 68.74  0  1278 ARG   A O   1 
ATOM   9579  C CB  . ARG   A 1 1314 ? 158.685 120.768 128.098 1.00 73.92  0  1278 ARG   A CB  1 
ATOM   9580  C CG  . ARG   A 1 1314 ? 159.273 122.060 127.584 1.00 70.63  0  1278 ARG   A CG  1 
ATOM   9581  C CD  . ARG   A 1 1314 ? 159.019 122.175 126.094 1.00 72.19  0  1278 ARG   A CD  1 
ATOM   9582  N NE  . ARG   A 1 1314 ? 160.171 122.702 125.377 1.00 75.12  0  1278 ARG   A NE  1 
ATOM   9583  C CZ  . ARG   A 1 1314 ? 160.482 122.376 124.130 1.00 76.31  0  1278 ARG   A CZ  1 
ATOM   9584  N NH1 . ARG   A 1 1314 ? 159.728 121.550 123.425 1.00 75.70  1  1278 ARG   A NH1 1 
ATOM   9585  N NH2 . ARG   A 1 1314 ? 161.577 122.890 123.578 1.00 75.40  0  1278 ARG   A NH2 1 
ATOM   9586  N N   . GLN   A 1 1315 ? 157.952 118.597 130.491 1.00 63.77  0  1279 GLN   A N   1 
ATOM   9587  C CA  . GLN   A 1 1315 ? 156.965 118.178 131.477 1.00 62.88  0  1279 GLN   A CA  1 
ATOM   9588  C C   . GLN   A 1 1315 ? 157.505 118.197 132.900 1.00 60.61  0  1279 GLN   A C   1 
ATOM   9589  O O   . GLN   A 1 1315 ? 156.726 118.005 133.839 1.00 54.14  0  1279 GLN   A O   1 
ATOM   9590  C CB  . GLN   A 1 1315 ? 156.437 116.784 131.125 1.00 58.83  0  1279 GLN   A CB  1 
ATOM   9591  C CG  . GLN   A 1 1315 ? 157.506 115.777 130.744 1.00 59.00  0  1279 GLN   A CG  1 
ATOM   9592  C CD  . GLN   A 1 1315 ? 158.054 115.032 131.939 1.00 63.92  0  1279 GLN   A CD  1 
ATOM   9593  O OE1 . GLN   A 1 1315 ? 157.545 115.163 133.051 1.00 65.22  0  1279 GLN   A OE1 1 
ATOM   9594  N NE2 . GLN   A 1 1315 ? 159.098 114.245 131.718 1.00 61.04  0  1279 GLN   A NE2 1 
ATOM   9595  N N   . VAL   A 1 1316 ? 158.809 118.412 133.082 1.00 65.17  0  1280 VAL   A N   1 
ATOM   9596  C CA  . VAL   A 1 1316 ? 159.375 118.509 134.423 1.00 68.77  0  1280 VAL   A CA  1 
ATOM   9597  C C   . VAL   A 1 1316 ? 159.110 119.875 135.048 1.00 76.71  0  1280 VAL   A C   1 
ATOM   9598  O O   . VAL   A 1 1316 ? 159.204 120.021 136.274 1.00 74.62  0  1280 VAL   A O   1 
ATOM   9599  C CB  . VAL   A 1 1316 ? 160.880 118.194 134.371 1.00 67.44  0  1280 VAL   A CB  1 
ATOM   9600  C CG1 . VAL   A 1 1316 ? 161.472 118.099 135.762 1.00 68.26  0  1280 VAL   A CG1 1 
ATOM   9601  C CG2 . VAL   A 1 1316 ? 161.110 116.897 133.628 1.00 71.45  0  1280 VAL   A CG2 1 
ATOM   9602  N N   . LEU   A 1 1317 ? 158.756 120.874 134.246 1.00 72.14  0  1281 LEU   A N   1 
ATOM   9603  C CA  . LEU   A 1 1317 ? 158.455 122.209 134.741 1.00 60.73  0  1281 LEU   A CA  1 
ATOM   9604  C C   . LEU   A 1 1317 ? 156.947 122.413 134.786 1.00 61.20  0  1281 LEU   A C   1 
ATOM   9605  O O   . LEU   A 1 1317 ? 156.242 122.058 133.837 1.00 64.92  0  1281 LEU   A O   1 
ATOM   9606  C CB  . LEU   A 1 1317 ? 159.096 123.275 133.854 1.00 56.38  0  1281 LEU   A CB  1 
ATOM   9607  C CG  . LEU   A 1 1317 ? 160.607 123.195 133.664 1.00 61.37  0  1281 LEU   A CG  1 
ATOM   9608  C CD1 . LEU   A 1 1317 ? 161.022 124.086 132.517 1.00 63.76  0  1281 LEU   A CD1 1 
ATOM   9609  C CD2 . LEU   A 1 1317 ? 161.328 123.586 134.936 1.00 61.00  0  1281 LEU   A CD2 1 
ATOM   9610  N N   . THR   A 1 1318 ? 156.461 122.993 135.880 1.00 59.18  0  1282 THR   A N   1 
ATOM   9611  C CA  . THR   A 1 1318 ? 155.047 123.315 135.994 1.00 58.48  0  1282 THR   A CA  1 
ATOM   9612  C C   . THR   A 1 1318 ? 154.695 124.471 135.058 1.00 58.80  0  1282 THR   A C   1 
ATOM   9613  O O   . THR   A 1 1318 ? 155.545 125.029 134.361 1.00 64.31  0  1282 THR   A O   1 
ATOM   9614  C CB  . THR   A 1 1318 ? 154.696 123.662 137.437 1.00 56.98  0  1282 THR   A CB  1 
ATOM   9615  O OG1 . THR   A 1 1318 ? 155.070 125.017 137.706 1.00 57.93  0  1282 THR   A OG1 1 
ATOM   9616  C CG2 . THR   A 1 1318 ? 155.439 122.750 138.391 1.00 56.89  0  1282 THR   A CG2 1 
ATOM   9617  N N   . LYS   A 1 1319 ? 153.411 124.831 135.035 1.00 53.95  0  1283 LYS   A N   1 
ATOM   9618  C CA  . LYS   A 1 1319 ? 152.974 125.928 134.177 1.00 57.74  0  1283 LYS   A CA  1 
ATOM   9619  C C   . LYS   A 1 1319 ? 153.581 127.253 134.616 1.00 61.26  0  1283 LYS   A C   1 
ATOM   9620  O O   . LYS   A 1 1319 ? 153.979 128.068 133.776 1.00 66.26  0  1283 LYS   A O   1 
ATOM   9621  C CB  . LYS   A 1 1319 ? 151.451 126.019 134.170 1.00 59.34  0  1283 LYS   A CB  1 
ATOM   9622  C CG  . LYS   A 1 1319 ? 150.907 127.045 133.195 1.00 61.50  0  1283 LYS   A CG  1 
ATOM   9623  C CD  . LYS   A 1 1319 ? 151.122 126.601 131.763 1.00 59.23  0  1283 LYS   A CD  1 
ATOM   9624  C CE  . LYS   A 1 1319 ? 150.378 127.500 130.799 1.00 62.69  0  1283 LYS   A CE  1 
ATOM   9625  N NZ  . LYS   A 1 1319 ? 151.037 128.829 130.681 1.00 62.38  1  1283 LYS   A NZ  1 
ATOM   9626  N N   . LYS   A 1 1320 ? 153.649 127.490 135.927 1.00 57.03  0  1284 LYS   A N   1 
ATOM   9627  C CA  . LYS   A 1 1320 ? 154.217 128.740 136.423 1.00 56.91  0  1284 LYS   A CA  1 
ATOM   9628  C C   . LYS   A 1 1320 ? 155.684 128.869 136.037 1.00 56.65  0  1284 LYS   A C   1 
ATOM   9629  O O   . LYS   A 1 1320 ? 156.136 129.947 135.636 1.00 57.97  0  1284 LYS   A O   1 
ATOM   9630  C CB  . LYS   A 1 1320 ? 154.053 128.826 137.939 1.00 56.69  0  1284 LYS   A CB  1 
ATOM   9631  C CG  . LYS   A 1 1320 ? 152.641 128.562 138.434 1.00 54.78  0  1284 LYS   A CG  1 
ATOM   9632  C CD  . LYS   A 1 1320 ? 152.525 128.826 139.927 1.00 57.41  0  1284 LYS   A CD  1 
ATOM   9633  C CE  . LYS   A 1 1320 ? 152.491 127.527 140.716 1.00 58.21  0  1284 LYS   A CE  1 
ATOM   9634  N NZ  . LYS   A 1 1320 ? 151.940 127.718 142.087 1.00 58.69  1  1284 LYS   A NZ  1 
ATOM   9635  N N   . GLN   A 1 1321 ? 156.443 127.779 136.151 1.00 49.70  0  1285 GLN   A N   1 
ATOM   9636  C CA  . GLN   A 1 1321 ? 157.857 127.823 135.802 1.00 51.30  0  1285 GLN   A CA  1 
ATOM   9637  C C   . GLN   A 1 1321 ? 158.056 128.057 134.310 1.00 46.80  0  1285 GLN   A C   1 
ATOM   9638  O O   . GLN   A 1 1321 ? 158.948 128.812 133.910 1.00 57.69  0  1285 GLN   A O   1 
ATOM   9639  C CB  . GLN   A 1 1321 ? 158.539 126.535 136.251 1.00 54.42  0  1285 GLN   A CB  1 
ATOM   9640  C CG  . GLN   A 1 1321 ? 158.598 126.395 137.759 1.00 53.41  0  1285 GLN   A CG  1 
ATOM   9641  C CD  . GLN   A 1 1321 ? 158.968 125.002 138.204 1.00 55.78  0  1285 GLN   A CD  1 
ATOM   9642  O OE1 . GLN   A 1 1321 ? 158.539 124.015 137.613 1.00 60.60  0  1285 GLN   A OE1 1 
ATOM   9643  N NE2 . GLN   A 1 1321 ? 159.764 124.912 139.258 1.00 52.45  0  1285 GLN   A NE2 1 
ATOM   9644  N N   . ARG   A 1 1322 ? 157.234 127.427 133.471 1.00 41.08  0  1286 ARG   A N   1 
ATOM   9645  C CA  . ARG   A 1 1322 ? 157.324 127.672 132.035 1.00 44.48  0  1286 ARG   A CA  1 
ATOM   9646  C C   . ARG   A 1 1322 ? 156.978 129.116 131.698 1.00 47.05  0  1286 ARG   A C   1 
ATOM   9647  O O   . ARG   A 1 1322 ? 157.630 129.734 130.848 1.00 57.30  0  1286 ARG   A O   1 
ATOM   9648  C CB  . ARG   A 1 1322 ? 156.408 126.712 131.279 1.00 53.83  0  1286 ARG   A CB  1 
ATOM   9649  C CG  . ARG   A 1 1322 ? 156.989 125.327 131.086 1.00 53.97  0  1286 ARG   A CG  1 
ATOM   9650  C CD  . ARG   A 1 1322 ? 156.269 124.582 129.978 1.00 50.24  0  1286 ARG   A CD  1 
ATOM   9651  N NE  . ARG   A 1 1322 ? 154.888 124.283 130.336 1.00 55.48  0  1286 ARG   A NE  1 
ATOM   9652  C CZ  . ARG   A 1 1322 ? 154.523 123.290 131.135 1.00 55.51  0  1286 ARG   A CZ  1 
ATOM   9653  N NH1 . ARG   A 1 1322 ? 155.414 122.483 131.684 1.00 54.74  1  1286 ARG   A NH1 1 
ATOM   9654  N NH2 . ARG   A 1 1322 ? 153.231 123.104 131.389 1.00 52.74  0  1286 ARG   A NH2 1 
ATOM   9655  N N   . ASP   A 1 1323 ? 155.957 129.672 132.353 1.00 48.22  0  1287 ASP   A N   1 
ATOM   9656  C CA  . ASP   A 1 1323 ? 155.602 131.066 132.111 1.00 50.11  0  1287 ASP   A CA  1 
ATOM   9657  C C   . ASP   A 1 1323 ? 156.721 132.003 132.547 1.00 49.71  0  1287 ASP   A C   1 
ATOM   9658  O O   . ASP   A 1 1323 ? 157.026 132.983 131.858 1.00 55.14  0  1287 ASP   A O   1 
ATOM   9659  C CB  . ASP   A 1 1323 ? 154.301 131.409 132.833 1.00 56.84  0  1287 ASP   A CB  1 
ATOM   9660  C CG  . ASP   A 1 1323 ? 153.101 130.699 132.238 1.00 61.54  0  1287 ASP   A CG  1 
ATOM   9661  O OD1 . ASP   A 1 1323 ? 153.211 130.188 131.104 1.00 56.44  0  1287 ASP   A OD1 1 
ATOM   9662  O OD2 . ASP   A 1 1323 ? 152.047 130.650 132.905 1.00 61.23  -1 1287 ASP   A OD2 1 
ATOM   9663  N N   . GLN   A 1 1324 ? 157.346 131.719 133.692 1.00 44.74  0  1288 GLN   A N   1 
ATOM   9664  C CA  . GLN   A 1 1324 ? 158.457 132.545 134.152 1.00 38.74  0  1288 GLN   A CA  1 
ATOM   9665  C C   . GLN   A 1 1324 ? 159.639 132.464 133.198 1.00 40.97  0  1288 GLN   A C   1 
ATOM   9666  O O   . GLN   A 1 1324 ? 160.294 133.475 132.922 1.00 44.49  0  1288 GLN   A O   1 
ATOM   9667  C CB  . GLN   A 1 1324 ? 158.877 132.127 135.558 1.00 35.11  0  1288 GLN   A CB  1 
ATOM   9668  C CG  . GLN   A 1 1324 ? 159.903 133.048 136.181 1.00 43.62  0  1288 GLN   A CG  1 
ATOM   9669  C CD  . GLN   A 1 1324 ? 159.305 134.355 136.648 1.00 49.36  0  1288 GLN   A CD  1 
ATOM   9670  O OE1 . GLN   A 1 1324 ? 158.093 134.551 136.592 1.00 52.96  0  1288 GLN   A OE1 1 
ATOM   9671  N NE2 . GLN   A 1 1324 ? 160.156 135.265 137.105 1.00 38.21  0  1288 GLN   A NE2 1 
ATOM   9672  N N   . ILE   A 1 1325 ? 159.935 131.267 132.694 1.00 43.45  0  1289 ILE   A N   1 
ATOM   9673  C CA  . ILE   A 1 1325 ? 161.023 131.112 131.735 1.00 34.26  0  1289 ILE   A CA  1 
ATOM   9674  C C   . ILE   A 1 1325 ? 160.724 131.890 130.463 1.00 33.64  0  1289 ILE   A C   1 
ATOM   9675  O O   . ILE   A 1 1325 ? 161.608 132.538 129.892 1.00 41.86  0  1289 ILE   A O   1 
ATOM   9676  C CB  . ILE   A 1 1325 ? 161.267 129.620 131.451 1.00 37.04  0  1289 ILE   A CB  1 
ATOM   9677  C CG1 . ILE   A 1 1325 ? 162.142 129.017 132.546 1.00 39.07  0  1289 ILE   A CG1 1 
ATOM   9678  C CG2 . ILE   A 1 1325 ? 161.908 129.427 130.098 1.00 43.63  0  1289 ILE   A CG2 1 
ATOM   9679  C CD1 . ILE   A 1 1325 ? 162.103 127.522 132.588 1.00 41.01  0  1289 ILE   A CD1 1 
ATOM   9680  N N   . ASP   A 1 1326 ? 159.473 131.844 130.000 1.00 35.14  0  1290 ASP   A N   1 
ATOM   9681  C CA  . ASP   A 1 1326 ? 159.099 132.609 128.816 1.00 41.49  0  1290 ASP   A CA  1 
ATOM   9682  C C   . ASP   A 1 1326 ? 159.250 134.107 129.059 1.00 44.96  0  1290 ASP   A C   1 
ATOM   9683  O O   . ASP   A 1 1326 ? 159.723 134.839 128.183 1.00 49.03  0  1290 ASP   A O   1 
ATOM   9684  C CB  . ASP   A 1 1326 ? 157.669 132.262 128.405 1.00 47.21  0  1290 ASP   A CB  1 
ATOM   9685  C CG  . ASP   A 1 1326 ? 157.329 132.721 126.996 1.00 53.29  0  1290 ASP   A CG  1 
ATOM   9686  O OD1 . ASP   A 1 1326 ? 156.616 131.977 126.289 1.00 52.78  0  1290 ASP   A OD1 1 
ATOM   9687  O OD2 . ASP   A 1 1326 ? 157.761 133.818 126.588 1.00 51.96  -1 1290 ASP   A OD2 1 
ATOM   9688  N N   . LEU   A 1 1327 ? 158.858 134.581 130.242 1.00 42.51  0  1291 LEU   A N   1 
ATOM   9689  C CA  . LEU   A 1 1327 ? 158.992 136.003 130.553 1.00 38.19  0  1291 LEU   A CA  1 
ATOM   9690  C C   . LEU   A 1 1327 ? 160.457 136.426 130.596 1.00 38.88  0  1291 LEU   A C   1 
ATOM   9691  O O   . LEU   A 1 1327 ? 160.829 137.478 130.061 1.00 41.30  0  1291 LEU   A O   1 
ATOM   9692  C CB  . LEU   A 1 1327 ? 158.304 136.312 131.881 1.00 35.58  0  1291 LEU   A CB  1 
ATOM   9693  C CG  . LEU   A 1 1327 ? 156.782 136.413 131.834 1.00 36.29  0  1291 LEU   A CG  1 
ATOM   9694  C CD1 . LEU   A 1 1327 ? 156.215 136.412 133.237 1.00 37.57  0  1291 LEU   A CD1 1 
ATOM   9695  C CD2 . LEU   A 1 1327 ? 156.360 137.658 131.080 1.00 34.62  0  1291 LEU   A CD2 1 
ATOM   9696  N N   . LEU   A 1 1328 ? 161.304 135.617 131.233 1.00 36.74  0  1292 LEU   A N   1 
ATOM   9697  C CA  . LEU   A 1 1328 ? 162.726 135.938 131.294 1.00 40.12  0  1292 LEU   A CA  1 
ATOM   9698  C C   . LEU   A 1 1328 ? 163.366 135.907 129.912 1.00 40.24  0  1292 LEU   A C   1 
ATOM   9699  O O   . LEU   A 1 1328 ? 164.242 136.726 129.616 1.00 43.68  0  1292 LEU   A O   1 
ATOM   9700  C CB  . LEU   A 1 1328 ? 163.437 134.973 132.240 1.00 41.61  0  1292 LEU   A CB  1 
ATOM   9701  C CG  . LEU   A 1 1328 ? 163.615 135.439 133.682 1.00 35.36  0  1292 LEU   A CG  1 
ATOM   9702  C CD1 . LEU   A 1 1328 ? 162.278 135.625 134.352 1.00 37.64  0  1292 LEU   A CD1 1 
ATOM   9703  C CD2 . LEU   A 1 1328 ? 164.444 134.435 134.449 1.00 35.08  0  1292 LEU   A CD2 1 
ATOM   9704  N N   . ALA   A 1 1329 ? 162.950 134.975 129.056 1.00 41.56  0  1293 ALA   A N   1 
ATOM   9705  C CA  . ALA   A 1 1329 ? 163.449 134.959 127.687 1.00 40.44  0  1293 ALA   A CA  1 
ATOM   9706  C C   . ALA   A 1 1329 ? 163.000 136.195 126.923 1.00 43.32  0  1293 ALA   A C   1 
ATOM   9707  O O   . ALA   A 1 1329 ? 163.764 136.752 126.126 1.00 60.04  0  1293 ALA   A O   1 
ATOM   9708  C CB  . ALA   A 1 1329 ? 162.983 133.697 126.974 1.00 42.72  0  1293 ALA   A CB  1 
ATOM   9709  N N   . LYS   A 1 1330 ? 161.759 136.632 127.139 1.00 33.72  0  1294 LYS   A N   1 
ATOM   9710  C CA  . LYS   A 1 1330 ? 161.302 137.869 126.518 1.00 35.66  0  1294 LYS   A CA  1 
ATOM   9711  C C   . LYS   A 1 1330 ? 162.149 139.046 126.973 1.00 39.01  0  1294 LYS   A C   1 
ATOM   9712  O O   . LYS   A 1 1330 ? 162.476 139.931 126.176 1.00 44.38  0  1294 LYS   A O   1 
ATOM   9713  C CB  . LYS   A 1 1330 ? 159.831 138.115 126.843 1.00 46.49  0  1294 LYS   A CB  1 
ATOM   9714  C CG  . LYS   A 1 1330 ? 158.868 137.254 126.058 1.00 46.03  0  1294 LYS   A CG  1 
ATOM   9715  C CD  . LYS   A 1 1330 ? 157.447 137.466 126.527 1.00 36.72  0  1294 LYS   A CD  1 
ATOM   9716  C CE  . LYS   A 1 1330 ? 156.470 136.706 125.661 1.00 37.96  0  1294 LYS   A CE  1 
ATOM   9717  N NZ  . LYS   A 1 1330 ? 155.096 136.773 126.219 1.00 51.73  1  1294 LYS   A NZ  1 
ATOM   9718  N N   . LEU   A 1 1331 ? 162.508 139.075 128.257 1.00 44.68  0  1295 LEU   A N   1 
ATOM   9719  C CA  . LEU   A 1 1331 ? 163.391 140.124 128.756 1.00 47.52  0  1295 LEU   A CA  1 
ATOM   9720  C C   . LEU   A 1 1331 ? 164.754 140.063 128.078 1.00 43.08  0  1295 LEU   A C   1 
ATOM   9721  O O   . LEU   A 1 1331 ? 165.294 141.088 127.647 1.00 44.15  0  1295 LEU   A O   1 
ATOM   9722  C CB  . LEU   A 1 1331 ? 163.542 140.006 130.271 1.00 40.67  0  1295 LEU   A CB  1 
ATOM   9723  C CG  . LEU   A 1 1331 ? 162.402 140.577 131.103 1.00 35.23  0  1295 LEU   A CG  1 
ATOM   9724  C CD1 . LEU   A 1 1331 ? 162.673 140.379 132.577 1.00 37.49  0  1295 LEU   A CD1 1 
ATOM   9725  C CD2 . LEU   A 1 1331 ? 162.225 142.041 130.775 1.00 38.94  0  1295 LEU   A CD2 1 
ATOM   9726  N N   . ASP   A 1 1332 ? 165.321 138.861 127.965 1.00 44.32  0  1296 ASP   A N   1 
ATOM   9727  C CA  . ASP   A 1 1332 ? 166.625 138.708 127.325 1.00 41.20  0  1296 ASP   A CA  1 
ATOM   9728  C C   . ASP   A 1 1332 ? 166.578 139.137 125.871 1.00 38.14  0  1296 ASP   A C   1 
ATOM   9729  O O   . ASP   A 1 1332 ? 167.579 139.615 125.329 1.00 50.12  0  1296 ASP   A O   1 
ATOM   9730  C CB  . ASP   A 1 1332 ? 167.093 137.258 127.437 1.00 46.32  0  1296 ASP   A CB  1 
ATOM   9731  C CG  . ASP   A 1 1332 ? 168.580 137.105 127.206 1.00 52.33  0  1296 ASP   A CG  1 
ATOM   9732  O OD1 . ASP   A 1 1332 ? 169.365 137.454 128.112 1.00 56.98  0  1296 ASP   A OD1 1 
ATOM   9733  O OD2 . ASP   A 1 1332 ? 168.965 136.633 126.117 1.00 48.73  -1 1296 ASP   A OD2 1 
ATOM   9734  N N   . TRP   A 1 1333 ? 165.431 138.965 125.226 1.00 36.05  0  1297 TRP   A N   1 
ATOM   9735  C CA  . TRP   A 1 1333 ? 165.274 139.411 123.851 1.00 39.35  0  1297 TRP   A CA  1 
ATOM   9736  C C   . TRP   A 1 1333 ? 165.139 140.925 123.762 1.00 47.24  0  1297 TRP   A C   1 
ATOM   9737  O O   . TRP   A 1 1333 ? 165.717 141.550 122.868 1.00 50.04  0  1297 TRP   A O   1 
ATOM   9738  C CB  . TRP   A 1 1333 ? 164.060 138.732 123.230 1.00 41.05  0  1297 TRP   A CB  1 
ATOM   9739  C CG  . TRP   A 1 1333 ? 163.724 139.219 121.875 1.00 42.28  0  1297 TRP   A CG  1 
ATOM   9740  C CD1 . TRP   A 1 1333 ? 164.593 139.590 120.898 1.00 50.23  0  1297 TRP   A CD1 1 
ATOM   9741  C CD2 . TRP   A 1 1333 ? 162.414 139.377 121.330 1.00 40.04  0  1297 TRP   A CD2 1 
ATOM   9742  N NE1 . TRP   A 1 1333 ? 163.907 139.976 119.777 1.00 54.33  0  1297 TRP   A NE1 1 
ATOM   9743  C CE2 . TRP   A 1 1333 ? 162.564 139.852 120.017 1.00 44.56  0  1297 TRP   A CE2 1 
ATOM   9744  C CE3 . TRP   A 1 1333 ? 161.127 139.162 121.825 1.00 44.85  0  1297 TRP   A CE3 1 
ATOM   9745  C CZ2 . TRP   A 1 1333 ? 161.480 140.116 119.194 1.00 46.05  0  1297 TRP   A CZ2 1 
ATOM   9746  C CZ3 . TRP   A 1 1333 ? 160.054 139.426 121.008 1.00 49.39  0  1297 TRP   A CZ3 1 
ATOM   9747  C CH2 . TRP   A 1 1333 ? 160.234 139.897 119.708 1.00 46.98  0  1297 TRP   A CH2 1 
ATOM   9748  N N   . VAL   A 1 1334 ? 164.384 141.533 124.674 1.00 48.97  0  1298 VAL   A N   1 
ATOM   9749  C CA  . VAL   A 1 1334 ? 164.102 142.962 124.575 1.00 42.62  0  1298 VAL   A CA  1 
ATOM   9750  C C   . VAL   A 1 1334 ? 165.186 143.792 125.249 1.00 45.78  0  1298 VAL   A C   1 
ATOM   9751  O O   . VAL   A 1 1334 ? 165.481 144.907 124.814 1.00 49.52  0  1298 VAL   A O   1 
ATOM   9752  C CB  . VAL   A 1 1334 ? 162.703 143.273 125.150 1.00 46.62  0  1298 VAL   A CB  1 
ATOM   9753  C CG1 . VAL   A 1 1334 ? 162.649 143.000 126.637 1.00 43.18  0  1298 VAL   A CG1 1 
ATOM   9754  C CG2 . VAL   A 1 1334 ? 162.304 144.707 124.849 1.00 45.16  0  1298 VAL   A CG2 1 
ATOM   9755  N N   . TYR   A 1 1335 ? 165.812 143.267 126.298 1.00 51.23  0  1299 TYR   A N   1 
ATOM   9756  C CA  . TYR   A 1 1335 ? 166.803 144.011 127.071 1.00 45.95  0  1299 TYR   A CA  1 
ATOM   9757  C C   . TYR   A 1 1335 ? 168.211 143.500 126.817 1.00 50.82  0  1299 TYR   A C   1 
ATOM   9758  O O   . TYR   A 1 1335 ? 169.033 143.413 127.732 1.00 51.83  0  1299 TYR   A O   1 
ATOM   9759  C CB  . TYR   A 1 1335 ? 166.450 143.952 128.551 1.00 42.07  0  1299 TYR   A CB  1 
ATOM   9760  C CG  . TYR   A 1 1335 ? 165.356 144.927 128.877 1.00 46.28  0  1299 TYR   A CG  1 
ATOM   9761  C CD1 . TYR   A 1 1335 ? 165.163 146.046 128.087 1.00 47.80  0  1299 TYR   A CD1 1 
ATOM   9762  C CD2 . TYR   A 1 1335 ? 164.473 144.700 129.916 1.00 45.35  0  1299 TYR   A CD2 1 
ATOM   9763  C CE1 . TYR   A 1 1335 ? 164.157 146.938 128.347 1.00 48.59  0  1299 TYR   A CE1 1 
ATOM   9764  C CE2 . TYR   A 1 1335 ? 163.454 145.584 130.178 1.00 48.19  0  1299 TYR   A CE2 1 
ATOM   9765  C CZ  . TYR   A 1 1335 ? 163.304 146.706 129.389 1.00 48.85  0  1299 TYR   A CZ  1 
ATOM   9766  O OH  . TYR   A 1 1335 ? 162.299 147.610 129.632 1.00 48.92  0  1299 TYR   A OH  1 
ATOM   9767  N N   . ALA   A 1 1336 ? 168.502 143.141 125.567 1.00 51.07  0  1300 ALA   A N   1 
ATOM   9768  C CA  . ALA   A 1 1336 ? 169.837 142.691 125.208 1.00 47.02  0  1300 ALA   A CA  1 
ATOM   9769  C C   . ALA   A 1 1336 ? 170.839 143.834 125.169 1.00 50.33  0  1300 ALA   A C   1 
ATOM   9770  O O   . ALA   A 1 1336 ? 172.047 143.582 125.119 1.00 53.97  0  1300 ALA   A O   1 
ATOM   9771  C CB  . ALA   A 1 1336 ? 169.804 141.977 123.857 1.00 45.36  0  1300 ALA   A CB  1 
ATOM   9772  N N   . SER   A 1 1337 ? 170.370 145.079 125.187 1.00 46.44  0  1301 SER   A N   1 
ATOM   9773  C CA  . SER   A 1 1337 ? 171.248 146.236 125.122 1.00 44.84  0  1301 SER   A CA  1 
ATOM   9774  C C   . SER   A 1 1337 ? 171.564 146.829 126.488 1.00 50.94  0  1301 SER   A C   1 
ATOM   9775  O O   . SER   A 1 1337 ? 172.285 147.828 126.559 1.00 53.06  0  1301 SER   A O   1 
ATOM   9776  C CB  . SER   A 1 1337 ? 170.620 147.310 124.234 1.00 50.52  0  1301 SER   A CB  1 
ATOM   9777  O OG  . SER   A 1 1337 ? 170.259 146.777 122.973 1.00 52.10  0  1301 SER   A OG  1 
ATOM   9778  N N   . ILE   A 1 1338 ? 171.047 146.240 127.569 1.00 55.05  0  1302 ILE   A N   1 
ATOM   9779  C CA  . ILE   A 1 1338 ? 171.278 146.783 128.901 1.00 48.22  0  1302 ILE   A CA  1 
ATOM   9780  C C   . ILE   A 1 1338 ? 172.749 146.657 129.267 1.00 53.72  0  1302 ILE   A C   1 
ATOM   9781  O O   . ILE   A 1 1338 ? 173.382 145.618 129.043 1.00 55.46  0  1302 ILE   A O   1 
ATOM   9782  C CB  . ILE   A 1 1338 ? 170.378 146.074 129.925 1.00 46.64  0  1302 ILE   A CB  1 
ATOM   9783  C CG1 . ILE   A 1 1338 ? 168.937 146.545 129.769 1.00 49.57  0  1302 ILE   A CG1 1 
ATOM   9784  C CG2 . ILE   A 1 1338 ? 170.848 146.338 131.336 1.00 49.97  0  1302 ILE   A CG2 1 
ATOM   9785  C CD1 . ILE   A 1 1338 ? 168.803 148.043 129.758 1.00 51.79  0  1302 ILE   A CD1 1 
ATOM   9786  N N   . ASP   A 1 1339 ? 173.302 147.731 129.835 1.00 53.70  0  1303 ASP   A N   1 
ATOM   9787  C CA  . ASP   A 1 1339 ? 174.723 147.774 130.153 1.00 54.38  0  1303 ASP   A CA  1 
ATOM   9788  C C   . ASP   A 1 1339 ? 175.115 146.798 131.254 1.00 52.98  0  1303 ASP   A C   1 
ATOM   9789  O O   . ASP   A 1 1339 ? 176.254 146.319 131.258 1.00 54.95  0  1303 ASP   A O   1 
ATOM   9790  C CB  . ASP   A 1 1339 ? 175.120 149.195 130.542 1.00 54.84  0  1303 ASP   A CB  1 
ATOM   9791  C CG  . ASP   A 1 1339 ? 174.964 150.169 129.395 1.00 56.80  0  1303 ASP   A CG  1 
ATOM   9792  O OD1 . ASP   A 1 1339 ? 173.840 150.669 129.188 1.00 54.48  0  1303 ASP   A OD1 1 
ATOM   9793  O OD2 . ASP   A 1 1339 ? 175.963 150.430 128.694 1.00 59.96  -1 1303 ASP   A OD2 1 
ATOM   9794  N N   . ASN   A 1 1340 ? 174.213 146.490 132.182 1.00 51.95  0  1304 ASN   A N   1 
ATOM   9795  C CA  . ASN   A 1 1340 ? 174.516 145.507 133.215 1.00 52.53  0  1304 ASN   A CA  1 
ATOM   9796  C C   . ASN   A 1 1340 ? 173.551 144.333 133.126 1.00 55.01  0  1304 ASN   A C   1 
ATOM   9797  O O   . ASN   A 1 1340 ? 172.977 143.911 134.134 1.00 51.32  0  1304 ASN   A O   1 
ATOM   9798  C CB  . ASN   A 1 1340 ? 174.477 146.138 134.608 1.00 50.53  0  1304 ASN   A CB  1 
ATOM   9799  C CG  . ASN   A 1 1340 ? 173.158 146.799 134.912 1.00 53.80  0  1304 ASN   A CG  1 
ATOM   9800  O OD1 . ASN   A 1 1340 ? 172.434 147.210 134.008 1.00 57.27  0  1304 ASN   A OD1 1 
ATOM   9801  N ND2 . ASN   A 1 1340 ? 172.835 146.909 136.194 1.00 54.08  0  1304 ASN   A ND2 1 
ATOM   9802  N N   . LYS   A 1 1341 ? 173.367 143.809 131.912 1.00 54.20  0  1305 LYS   A N   1 
ATOM   9803  C CA  . LYS   A 1 1341 ? 172.451 142.692 131.710 1.00 50.54  0  1305 LYS   A CA  1 
ATOM   9804  C C   . LYS   A 1 1341 ? 172.875 141.471 132.513 1.00 50.83  0  1305 LYS   A C   1 
ATOM   9805  O O   . LYS   A 1 1341 ? 172.028 140.746 133.041 1.00 59.40  0  1305 LYS   A O   1 
ATOM   9806  C CB  . LYS   A 1 1341 ? 172.379 142.328 130.231 1.00 49.64  0  1305 LYS   A CB  1 
ATOM   9807  C CG  . LYS   A 1 1341 ? 171.609 141.046 129.964 1.00 50.39  0  1305 LYS   A CG  1 
ATOM   9808  C CD  . LYS   A 1 1341 ? 171.118 140.975 128.537 1.00 47.79  0  1305 LYS   A CD  1 
ATOM   9809  C CE  . LYS   A 1 1341 ? 172.100 141.651 127.600 1.00 54.00  0  1305 LYS   A CE  1 
ATOM   9810  N NZ  . LYS   A 1 1341 ? 173.139 140.709 127.100 1.00 56.10  1  1305 LYS   A NZ  1 
ATOM   9811  N N   . ASP   A 1 1342 ? 174.179 141.212 132.593 1.00 53.60  0  1306 ASP   A N   1 
ATOM   9812  C CA  . ASP   A 1 1342 ? 174.648 139.991 133.239 1.00 53.80  0  1306 ASP   A CA  1 
ATOM   9813  C C   . ASP   A 1 1342 ? 174.223 139.941 134.701 1.00 56.67  0  1306 ASP   A C   1 
ATOM   9814  O O   . ASP   A 1 1342 ? 173.606 138.968 135.145 1.00 64.55  0  1306 ASP   A O   1 
ATOM   9815  C CB  . ASP   A 1 1342 ? 176.166 139.886 133.110 1.00 58.76  0  1306 ASP   A CB  1 
ATOM   9816  C CG  . ASP   A 1 1342 ? 176.604 139.493 131.714 1.00 65.03  0  1306 ASP   A CG  1 
ATOM   9817  O OD1 . ASP   A 1 1342 ? 175.861 138.744 131.046 1.00 64.34  0  1306 ASP   A OD1 1 
ATOM   9818  O OD2 . ASP   A 1 1342 ? 177.685 139.941 131.280 1.00 62.54  -1 1306 ASP   A OD2 1 
ATOM   9819  N N   . GLU   A 1 1343 ? 174.526 140.997 135.459 1.00 54.37  0  1307 GLU   A N   1 
ATOM   9820  C CA  . GLU   A 1 1343 ? 174.152 141.030 136.870 1.00 58.82  0  1307 GLU   A CA  1 
ATOM   9821  C C   . GLU   A 1 1343 ? 172.639 141.047 137.038 1.00 59.85  0  1307 GLU   A C   1 
ATOM   9822  O O   . GLU   A 1 1343 ? 172.093 140.382 137.925 1.00 60.68  0  1307 GLU   A O   1 
ATOM   9823  C CB  . GLU   A 1 1343 ? 174.776 142.251 137.543 1.00 56.62  0  1307 GLU   A CB  1 
ATOM   9824  C CG  . GLU   A 1 1343 ? 176.112 142.663 136.950 1.00 57.17  0  1307 GLU   A CG  1 
ATOM   9825  C CD  . GLU   A 1 1343 ? 176.479 144.093 137.288 1.00 61.32  0  1307 GLU   A CD  1 
ATOM   9826  O OE1 . GLU   A 1 1343 ? 177.688 144.400 137.355 1.00 58.61  0  1307 GLU   A OE1 1 
ATOM   9827  O OE2 . GLU   A 1 1343 ? 175.558 144.912 137.486 1.00 62.16  -1 1307 GLU   A OE2 1 
ATOM   9828  N N   . PHE   A 1 1344 ? 171.948 141.805 136.187 1.00 53.63  0  1308 PHE   A N   1 
ATOM   9829  C CA  . PHE   A 1 1344 ? 170.498 141.939 136.282 1.00 53.72  0  1308 PHE   A CA  1 
ATOM   9830  C C   . PHE   A 1 1344 ? 169.804 140.595 136.091 1.00 51.47  0  1308 PHE   A C   1 
ATOM   9831  O O   . PHE   A 1 1344 ? 168.952 140.198 136.897 1.00 52.99  0  1308 PHE   A O   1 
ATOM   9832  C CB  . PHE   A 1 1344 ? 170.045 142.981 135.254 1.00 52.27  0  1308 PHE   A CB  1 
ATOM   9833  C CG  . PHE   A 1 1344 ? 168.624 142.851 134.801 1.00 52.70  0  1308 PHE   A CG  1 
ATOM   9834  C CD1 . PHE   A 1 1344 ? 167.575 142.964 135.694 1.00 52.84  0  1308 PHE   A CD1 1 
ATOM   9835  C CD2 . PHE   A 1 1344 ? 168.337 142.694 133.458 1.00 48.01  0  1308 PHE   A CD2 1 
ATOM   9836  C CE1 . PHE   A 1 1344 ? 166.269 142.872 135.257 1.00 48.27  0  1308 PHE   A CE1 1 
ATOM   9837  C CE2 . PHE   A 1 1344 ? 167.038 142.605 133.018 1.00 50.31  0  1308 PHE   A CE2 1 
ATOM   9838  C CZ  . PHE   A 1 1344 ? 166.002 142.694 133.918 1.00 54.65  0  1308 PHE   A CZ  1 
ATOM   9839  N N   . MET   A 1 1345 ? 170.195 139.851 135.058 1.00 45.74  0  1309 MET   A N   1 
ATOM   9840  C CA  . MET   A 1 1345 ? 169.572 138.559 134.819 1.00 41.17  0  1309 MET   A CA  1 
ATOM   9841  C C   . MET   A 1 1345 ? 170.065 137.495 135.783 1.00 44.36  0  1309 MET   A C   1 
ATOM   9842  O O   . MET   A 1 1345 ? 169.312 136.574 136.106 1.00 55.34  0  1309 MET   A O   1 
ATOM   9843  C CB  . MET   A 1 1345 ? 169.792 138.121 133.380 1.00 45.16  0  1309 MET   A CB  1 
ATOM   9844  C CG  . MET   A 1 1345 ? 169.024 138.977 132.430 1.00 47.42  0  1309 MET   A CG  1 
ATOM   9845  S SD  . MET   A 1 1345 ? 167.348 138.348 132.365 1.00 55.02  0  1309 MET   A SD  1 
ATOM   9846  C CE  . MET   A 1 1345 ? 166.893 138.871 130.736 1.00 49.42  0  1309 MET   A CE  1 
ATOM   9847  N N   . GLU   A 1 1346 ? 171.306 137.594 136.261 1.00 49.09  0  1310 GLU   A N   1 
ATOM   9848  C CA  . GLU   A 1 1346 ? 171.737 136.682 137.310 1.00 54.82  0  1310 GLU   A CA  1 
ATOM   9849  C C   . GLU   A 1 1346 ? 170.873 136.850 138.548 1.00 57.13  0  1310 GLU   A C   1 
ATOM   9850  O O   . GLU   A 1 1346 ? 170.422 135.863 139.140 1.00 57.76  0  1310 GLU   A O   1 
ATOM   9851  C CB  . GLU   A 1 1346 ? 173.210 136.914 137.644 1.00 53.46  0  1310 GLU   A CB  1 
ATOM   9852  C CG  . GLU   A 1 1346 ? 173.683 136.198 138.899 1.00 57.20  0  1310 GLU   A CG  1 
ATOM   9853  C CD  . GLU   A 1 1346 ? 174.082 134.755 138.649 1.00 63.72  0  1310 GLU   A CD  1 
ATOM   9854  O OE1 . GLU   A 1 1346 ? 174.789 134.179 139.501 1.00 61.62  0  1310 GLU   A OE1 1 
ATOM   9855  O OE2 . GLU   A 1 1346 ? 173.696 134.195 137.603 1.00 64.51  -1 1310 GLU   A OE2 1 
ATOM   9856  N N   . GLU   A 1 1347 ? 170.603 138.100 138.932 1.00 56.85  0  1311 GLU   A N   1 
ATOM   9857  C CA  . GLU   A 1 1347 ? 169.743 138.354 140.081 1.00 56.56  0  1311 GLU   A CA  1 
ATOM   9858  C C   . GLU   A 1 1347 ? 168.331 137.841 139.824 1.00 53.39  0  1311 GLU   A C   1 
ATOM   9859  O O   . GLU   A 1 1347 ? 167.747 137.171 140.681 1.00 54.36  0  1311 GLU   A O   1 
ATOM   9860  C CB  . GLU   A 1 1347 ? 169.732 139.851 140.394 1.00 55.99  0  1311 GLU   A CB  1 
ATOM   9861  C CG  . GLU   A 1 1347 ? 168.728 140.312 141.447 1.00 61.28  0  1311 GLU   A CG  1 
ATOM   9862  C CD  . GLU   A 1 1347 ? 168.535 139.311 142.573 1.00 64.38  0  1311 GLU   A CD  1 
ATOM   9863  O OE1 . GLU   A 1 1347 ? 167.394 138.844 142.771 1.00 60.14  0  1311 GLU   A OE1 1 
ATOM   9864  O OE2 . GLU   A 1 1347 ? 169.528 138.988 143.259 1.00 63.62  -1 1311 GLU   A OE2 1 
ATOM   9865  N N   . LEU   A 1 1348 ? 167.779 138.122 138.640 1.00 47.07  0  1312 LEU   A N   1 
ATOM   9866  C CA  . LEU   A 1 1348 ? 166.422 137.674 138.335 1.00 42.41  0  1312 LEU   A CA  1 
ATOM   9867  C C   . LEU   A 1 1348 ? 166.303 136.156 138.395 1.00 40.82  0  1312 LEU   A C   1 
ATOM   9868  O O   . LEU   A 1 1348 ? 165.377 135.622 139.017 1.00 44.37  0  1312 LEU   A O   1 
ATOM   9869  C CB  . LEU   A 1 1348 ? 165.998 138.177 136.958 1.00 40.34  0  1312 LEU   A CB  1 
ATOM   9870  C CG  . LEU   A 1 1348 ? 165.102 139.409 136.909 1.00 34.74  0  1312 LEU   A CG  1 
ATOM   9871  C CD1 . LEU   A 1 1348 ? 164.686 139.684 135.484 1.00 35.55  0  1312 LEU   A CD1 1 
ATOM   9872  C CD2 . LEU   A 1 1348 ? 163.890 139.199 137.784 1.00 43.41  0  1312 LEU   A CD2 1 
ATOM   9873  N N   . SER   A 1 1349 ? 167.230 135.442 137.758 1.00 43.79  0  1313 SER   A N   1 
ATOM   9874  C CA  . SER   A 1 1349 ? 167.149 133.989 137.713 1.00 38.00  0  1313 SER   A CA  1 
ATOM   9875  C C   . SER   A 1 1349 ? 167.437 133.361 139.070 1.00 42.69  0  1313 SER   A C   1 
ATOM   9876  O O   . SER   A 1 1349 ? 166.827 132.346 139.422 1.00 45.68  0  1313 SER   A O   1 
ATOM   9877  C CB  . SER   A 1 1349 ? 168.106 133.446 136.655 1.00 45.51  0  1313 SER   A CB  1 
ATOM   9878  O OG  . SER   A 1 1349 ? 167.718 133.873 135.362 1.00 47.52  0  1313 SER   A OG  1 
ATOM   9879  N N   . ILE   A 1 1350 ? 168.365 133.931 139.842 1.00 48.30  0  1314 ILE   A N   1 
ATOM   9880  C CA  . ILE   A 1 1350 ? 168.639 133.396 141.170 1.00 50.23  0  1314 ILE   A CA  1 
ATOM   9881  C C   . ILE   A 1 1350 ? 167.442 133.611 142.088 1.00 58.54  0  1314 ILE   A C   1 
ATOM   9882  O O   . ILE   A 1 1350 ? 167.087 132.733 142.883 1.00 60.88  0  1314 ILE   A O   1 
ATOM   9883  C CB  . ILE   A 1 1350 ? 169.921 134.024 141.742 1.00 49.56  0  1314 ILE   A CB  1 
ATOM   9884  C CG1 . ILE   A 1 1350 ? 171.147 133.243 141.272 1.00 53.35  0  1314 ILE   A CG1 1 
ATOM   9885  C CG2 . ILE   A 1 1350 ? 169.877 134.058 143.260 1.00 51.98  0  1314 ILE   A CG2 1 
ATOM   9886  C CD1 . ILE   A 1 1350 ? 171.326 131.914 141.969 1.00 54.46  0  1314 ILE   A CD1 1 
ATOM   9887  N N   . GLY   A 1 1351 ? 166.796 134.770 141.990 1.00 57.63  0  1315 GLY   A N   1 
ATOM   9888  C CA  . GLY   A 1 1351 ? 165.658 135.065 142.832 1.00 48.36  0  1315 GLY   A CA  1 
ATOM   9889  C C   . GLY   A 1 1351 ? 164.418 134.276 142.476 1.00 50.98  0  1315 GLY   A C   1 
ATOM   9890  O O   . GLY   A 1 1351 ? 163.906 133.519 143.304 1.00 58.29  0  1315 GLY   A O   1 
ATOM   9891  N N   . THR   A 1 1352 ? 163.926 134.432 141.246 1.00 43.75  0  1316 THR   A N   1 
ATOM   9892  C CA  . THR   A 1 1352 ? 162.663 133.801 140.880 1.00 48.04  0  1316 THR   A CA  1 
ATOM   9893  C C   . THR   A 1 1352 ? 162.837 132.310 140.606 1.00 48.37  0  1316 THR   A C   1 
ATOM   9894  O O   . THR   A 1 1352 ? 162.253 131.469 141.296 1.00 50.51  0  1316 THR   A O   1 
ATOM   9895  C CB  . THR   A 1 1352 ? 162.054 134.502 139.663 1.00 43.36  0  1316 THR   A CB  1 
ATOM   9896  O OG1 . THR   A 1 1352 ? 162.764 134.119 138.482 1.00 48.33  0  1316 THR   A OG1 1 
ATOM   9897  C CG2 . THR   A 1 1352 ? 162.129 136.009 139.825 1.00 43.69  0  1316 THR   A CG2 1 
ATOM   9898  N N   . LEU   A 1 1353 ? 163.646 131.962 139.603 1.00 48.52  0  1317 LEU   A N   1 
ATOM   9899  C CA  . LEU   A 1 1353 ? 163.774 130.570 139.189 1.00 45.83  0  1317 LEU   A CA  1 
ATOM   9900  C C   . LEU   A 1 1353 ? 164.703 129.758 140.081 1.00 50.80  0  1317 LEU   A C   1 
ATOM   9901  O O   . LEU   A 1 1353 ? 164.661 128.526 140.028 1.00 51.30  0  1317 LEU   A O   1 
ATOM   9902  C CB  . LEU   A 1 1353 ? 164.271 130.491 137.746 1.00 47.91  0  1317 LEU   A CB  1 
ATOM   9903  C CG  . LEU   A 1 1353 ? 163.282 130.921 136.667 1.00 48.57  0  1317 LEU   A CG  1 
ATOM   9904  C CD1 . LEU   A 1 1353 ? 163.880 130.710 135.290 1.00 48.48  0  1317 LEU   A CD1 1 
ATOM   9905  C CD2 . LEU   A 1 1353 ? 161.987 130.153 136.814 1.00 46.06  0  1317 LEU   A CD2 1 
ATOM   9906  N N   . GLY   A 1 1354 ? 165.536 130.405 140.888 1.00 49.82  0  1318 GLY   A N   1 
ATOM   9907  C CA  . GLY   A 1 1354 ? 166.451 129.675 141.738 1.00 46.62  0  1318 GLY   A CA  1 
ATOM   9908  C C   . GLY   A 1 1354 ? 167.659 129.101 141.037 1.00 56.74  0  1318 GLY   A C   1 
ATOM   9909  O O   . GLY   A 1 1354 ? 168.387 128.309 141.644 1.00 60.31  0  1318 GLY   A O   1 
ATOM   9910  N N   . LEU   A 1 1355 ? 167.898 129.472 139.782 1.00 62.84  0  1319 LEU   A N   1 
ATOM   9911  C CA  . LEU   A 1 1355 ? 169.029 128.986 139.007 1.00 57.20  0  1319 LEU   A CA  1 
ATOM   9912  C C   . LEU   A 1 1355 ? 169.951 130.137 138.628 1.00 58.59  0  1319 LEU   A C   1 
ATOM   9913  O O   . LEU   A 1 1355 ? 169.549 131.303 138.626 1.00 63.56  0  1319 LEU   A O   1 
ATOM   9914  C CB  . LEU   A 1 1355 ? 168.562 128.278 137.736 1.00 54.40  0  1319 LEU   A CB  1 
ATOM   9915  C CG  . LEU   A 1 1355 ? 167.622 127.092 137.912 1.00 57.89  0  1319 LEU   A CG  1 
ATOM   9916  C CD1 . LEU   A 1 1355 ? 167.192 126.570 136.556 1.00 58.72  0  1319 LEU   A CD1 1 
ATOM   9917  C CD2 . LEU   A 1 1355 ? 168.305 126.006 138.715 1.00 60.99  0  1319 LEU   A CD2 1 
ATOM   9918  N N   . THR   A 1 1356 ? 171.194 129.798 138.304 1.00 62.03  0  1320 THR   A N   1 
ATOM   9919  C CA  . THR   A 1 1356 ? 172.114 130.788 137.772 1.00 65.95  0  1320 THR   A CA  1 
ATOM   9920  C C   . THR   A 1 1356 ? 171.706 131.170 136.352 1.00 64.92  0  1320 THR   A C   1 
ATOM   9921  O O   . THR   A 1 1356 ? 170.933 130.473 135.692 1.00 63.64  0  1320 THR   A O   1 
ATOM   9922  C CB  . THR   A 1 1356 ? 173.546 130.256 137.781 1.00 64.95  0  1320 THR   A CB  1 
ATOM   9923  O OG1 . THR   A 1 1356 ? 173.728 129.360 136.680 1.00 66.43  0  1320 THR   A OG1 1 
ATOM   9924  C CG2 . THR   A 1 1356 ? 173.826 129.511 139.077 1.00 63.17  0  1320 THR   A CG2 1 
ATOM   9925  N N   . TYR   A 1 1357 ? 172.239 132.300 135.882 1.00 58.15  0  1321 TYR   A N   1 
ATOM   9926  C CA  . TYR   A 1 1357 ? 171.835 132.813 134.575 1.00 59.88  0  1321 TYR   A CA  1 
ATOM   9927  C C   . TYR   A 1 1357 ? 172.197 131.847 133.455 1.00 64.91  0  1321 TYR   A C   1 
ATOM   9928  O O   . TYR   A 1 1357 ? 171.402 131.633 132.534 1.00 66.05  0  1321 TYR   A O   1 
ATOM   9929  C CB  . TYR   A 1 1357 ? 172.467 134.179 134.321 1.00 58.36  0  1321 TYR   A CB  1 
ATOM   9930  C CG  . TYR   A 1 1357 ? 172.130 134.750 132.962 1.00 61.64  0  1321 TYR   A CG  1 
ATOM   9931  C CD1 . TYR   A 1 1357 ? 170.838 134.689 132.463 1.00 62.61  0  1321 TYR   A CD1 1 
ATOM   9932  C CD2 . TYR   A 1 1357 ? 173.103 135.358 132.183 1.00 64.09  0  1321 TYR   A CD2 1 
ATOM   9933  C CE1 . TYR   A 1 1357 ? 170.525 135.208 131.224 1.00 62.92  0  1321 TYR   A CE1 1 
ATOM   9934  C CE2 . TYR   A 1 1357 ? 172.798 135.883 130.941 1.00 65.02  0  1321 TYR   A CE2 1 
ATOM   9935  C CZ  . TYR   A 1 1357 ? 171.507 135.805 130.468 1.00 65.83  0  1321 TYR   A CZ  1 
ATOM   9936  O OH  . TYR   A 1 1357 ? 171.195 136.326 129.233 1.00 67.05  0  1321 TYR   A OH  1 
ATOM   9937  N N   . GLU   A 1 1358 ? 173.393 131.260 133.505 1.00 67.72  0  1322 GLU   A N   1 
ATOM   9938  C CA  . GLU   A 1 1358 ? 173.801 130.348 132.442 1.00 64.20  0  1322 GLU   A CA  1 
ATOM   9939  C C   . GLU   A 1 1358 ? 173.029 129.035 132.484 1.00 62.73  0  1322 GLU   A C   1 
ATOM   9940  O O   . GLU   A 1 1358 ? 172.765 128.447 131.431 1.00 65.36  0  1322 GLU   A O   1 
ATOM   9941  C CB  . GLU   A 1 1358 ? 175.306 130.085 132.515 1.00 62.09  0  1322 GLU   A CB  1 
ATOM   9942  C CG  . GLU   A 1 1358 ? 175.750 129.309 133.738 1.00 61.64  0  1322 GLU   A CG  1 
ATOM   9943  C CD  . GLU   A 1 1358 ? 176.068 130.210 134.907 1.00 64.36  0  1322 GLU   A CD  1 
ATOM   9944  O OE1 . GLU   A 1 1358 ? 175.947 131.444 134.757 1.00 63.80  0  1322 GLU   A OE1 1 
ATOM   9945  O OE2 . GLU   A 1 1358 ? 176.434 129.684 135.978 1.00 66.19  -1 1322 GLU   A OE2 1 
ATOM   9946  N N   . LYS   A 1 1359 ? 172.665 128.558 133.676 1.00 56.13  0  1323 LYS   A N   1 
ATOM   9947  C CA  . LYS   A 1 1359 ? 171.849 127.353 133.763 1.00 59.85  0  1323 LYS   A CA  1 
ATOM   9948  C C   . LYS   A 1 1359 ? 170.454 127.594 133.204 1.00 64.54  0  1323 LYS   A C   1 
ATOM   9949  O O   . LYS   A 1 1359 ? 169.898 126.732 132.516 1.00 66.00  0  1323 LYS   A O   1 
ATOM   9950  C CB  . LYS   A 1 1359 ? 171.770 126.868 135.209 1.00 61.23  0  1323 LYS   A CB  1 
ATOM   9951  C CG  . LYS   A 1 1359 ? 173.085 126.362 135.763 1.00 61.89  0  1323 LYS   A CG  1 
ATOM   9952  C CD  . LYS   A 1 1359 ? 173.539 125.114 135.030 1.00 62.09  0  1323 LYS   A CD  1 
ATOM   9953  C CE  . LYS   A 1 1359 ? 174.843 124.584 135.597 1.00 61.60  0  1323 LYS   A CE  1 
ATOM   9954  N NZ  . LYS   A 1 1359 ? 175.331 123.408 134.830 1.00 63.27  1  1323 LYS   A NZ  1 
ATOM   9955  N N   . ALA   A 1 1360 ? 169.875 128.760 133.489 1.00 66.73  0  1324 ALA   A N   1 
ATOM   9956  C CA  . ALA   A 1 1360 ? 168.537 129.060 132.994 1.00 65.22  0  1324 ALA   A CA  1 
ATOM   9957  C C   . ALA   A 1 1360 ? 168.557 129.388 131.508 1.00 61.73  0  1324 ALA   A C   1 
ATOM   9958  O O   . ALA   A 1 1360 ? 167.562 129.171 130.807 1.00 64.09  0  1324 ALA   A O   1 
ATOM   9959  C CB  . ALA   A 1 1360 ? 167.930 130.212 133.790 1.00 59.52  0  1324 ALA   A CB  1 
ATOM   9960  N N   . LYS   A 1 1361 ? 169.679 129.907 131.007 1.00 61.81  0  1325 LYS   A N   1 
ATOM   9961  C CA  . LYS   A 1 1361 ? 169.764 130.289 129.604 1.00 63.56  0  1325 LYS   A CA  1 
ATOM   9962  C C   . LYS   A 1 1361 ? 169.613 129.095 128.676 1.00 60.57  0  1325 LYS   A C   1 
ATOM   9963  O O   . LYS   A 1 1361 ? 169.240 129.270 127.512 1.00 62.41  0  1325 LYS   A O   1 
ATOM   9964  C CB  . LYS   A 1 1361 ? 171.089 131.002 129.337 1.00 65.64  0  1325 LYS   A CB  1 
ATOM   9965  C CG  . LYS   A 1 1361 ? 171.172 131.665 127.974 1.00 65.20  0  1325 LYS   A CG  1 
ATOM   9966  C CD  . LYS   A 1 1361 ? 172.049 132.902 128.012 1.00 65.01  0  1325 LYS   A CD  1 
ATOM   9967  C CE  . LYS   A 1 1361 ? 172.042 133.618 126.674 1.00 65.73  0  1325 LYS   A CE  1 
ATOM   9968  N NZ  . LYS   A 1 1361 ? 171.030 133.042 125.746 1.00 62.47  1  1325 LYS   A NZ  1 
ATOM   9969  N N   . LYS   A 1 1362 ? 169.888 127.886 129.165 1.00 63.18  0  1326 LYS   A N   1 
ATOM   9970  C CA  . LYS   A 1 1362 ? 169.677 126.693 128.357 1.00 67.73  0  1326 LYS   A CA  1 
ATOM   9971  C C   . LYS   A 1 1362 ? 168.204 126.452 128.061 1.00 66.63  0  1326 LYS   A C   1 
ATOM   9972  O O   . LYS   A 1 1362 ? 167.887 125.698 127.136 1.00 65.90  0  1326 LYS   A O   1 
ATOM   9973  C CB  . LYS   A 1 1362 ? 170.272 125.473 129.060 1.00 67.28  0  1326 LYS   A CB  1 
ATOM   9974  C CG  . LYS   A 1 1362 ? 171.743 125.620 129.410 1.00 67.42  0  1326 LYS   A CG  1 
ATOM   9975  C CD  . LYS   A 1 1362 ? 172.237 124.433 130.217 1.00 68.30  0  1326 LYS   A CD  1 
ATOM   9976  C CE  . LYS   A 1 1362 ? 173.730 124.524 130.475 1.00 64.80  0  1326 LYS   A CE  1 
ATOM   9977  N NZ  . LYS   A 1 1362 ? 174.214 123.384 131.296 1.00 65.97  1  1326 LYS   A NZ  1 
ATOM   9978  N N   . LEU   A 1 1363 ? 167.303 127.077 128.819 1.00 61.52  0  1327 LEU   A N   1 
ATOM   9979  C CA  . LEU   A 1 1363 ? 165.869 126.876 128.666 1.00 59.06  0  1327 LEU   A CA  1 
ATOM   9980  C C   . LEU   A 1 1363 ? 165.168 128.047 127.998 1.00 56.59  0  1327 LEU   A C   1 
ATOM   9981  O O   . LEU   A 1 1363 ? 164.004 127.911 127.609 1.00 52.12  0  1327 LEU   A O   1 
ATOM   9982  C CB  . LEU   A 1 1363 ? 165.222 126.623 130.032 1.00 56.63  0  1327 LEU   A CB  1 
ATOM   9983  C CG  . LEU   A 1 1363 ? 166.055 125.842 131.046 1.00 57.29  0  1327 LEU   A CG  1 
ATOM   9984  C CD1 . LEU   A 1 1363 ? 165.275 125.637 132.329 1.00 61.20  0  1327 LEU   A CD1 1 
ATOM   9985  C CD2 . LEU   A 1 1363 ? 166.475 124.512 130.461 1.00 56.57  0  1327 LEU   A CD2 1 
ATOM   9986  N N   . PHE   A 1 1364 ? 165.834 129.181 127.863 1.00 54.03  0  1328 PHE   A N   1 
ATOM   9987  C CA  . PHE   A 1 1364 ? 165.195 130.360 127.303 1.00 50.52  0  1328 PHE   A CA  1 
ATOM   9988  C C   . PHE   A 1 1364 ? 164.942 130.152 125.816 1.00 53.56  0  1328 PHE   A C   1 
ATOM   9989  O O   . PHE   A 1 1364 ? 165.866 129.780 125.085 1.00 61.54  0  1328 PHE   A O   1 
ATOM   9990  C CB  . PHE   A 1 1364 ? 166.069 131.594 127.505 1.00 52.16  0  1328 PHE   A CB  1 
ATOM   9991  C CG  . PHE   A 1 1364 ? 166.190 132.034 128.934 1.00 54.11  0  1328 PHE   A CG  1 
ATOM   9992  C CD1 . PHE   A 1 1364 ? 165.500 131.387 129.941 1.00 54.01  0  1328 PHE   A CD1 1 
ATOM   9993  C CD2 . PHE   A 1 1364 ? 167.007 133.095 129.269 1.00 58.05  0  1328 PHE   A CD2 1 
ATOM   9994  C CE1 . PHE   A 1 1364 ? 165.621 131.791 131.250 1.00 53.21  0  1328 PHE   A CE1 1 
ATOM   9995  C CE2 . PHE   A 1 1364 ? 167.130 133.503 130.576 1.00 55.86  0  1328 PHE   A CE2 1 
ATOM   9996  C CZ  . PHE   A 1 1364 ? 166.436 132.850 131.569 1.00 53.13  0  1328 PHE   A CZ  1 
ATOM   9997  N N   . PRO   A 1 1365 ? 163.719 130.357 125.336 1.00 49.52  0  1329 PRO   A N   1 
ATOM   9998  C CA  . PRO   A 1 1365 ? 163.504 130.414 123.889 1.00 50.47  0  1329 PRO   A CA  1 
ATOM   9999  C C   . PRO   A 1 1365 ? 164.367 131.495 123.261 1.00 56.23  0  1329 PRO   A C   1 
ATOM   10000 O O   . PRO   A 1 1365 ? 164.533 132.583 123.815 1.00 57.55  0  1329 PRO   A O   1 
ATOM   10001 C CB  . PRO   A 1 1365 ? 162.015 130.745 123.765 1.00 49.18  0  1329 PRO   A CB  1 
ATOM   10002 C CG  . PRO   A 1 1365 ? 161.421 130.242 125.019 1.00 50.49  0  1329 PRO   A CG  1 
ATOM   10003 C CD  . PRO   A 1 1365 ? 162.455 130.376 126.088 1.00 52.47  0  1329 PRO   A CD  1 
ATOM   10004 N N   . GLN   A 1 1366 ? 164.924 131.183 122.099 1.00 61.67  0  1330 GLN   A N   1 
ATOM   10005 C CA  . GLN   A 1 1366 ? 165.791 132.100 121.369 1.00 62.42  0  1330 GLN   A CA  1 
ATOM   10006 C C   . GLN   A 1 1366 ? 164.963 132.766 120.278 1.00 62.78  0  1330 GLN   A C   1 
ATOM   10007 O O   . GLN   A 1 1366 ? 164.596 132.124 119.290 1.00 65.47  0  1330 GLN   A O   1 
ATOM   10008 C CB  . GLN   A 1 1366 ? 166.989 131.358 120.785 1.00 63.01  0  1330 GLN   A CB  1 
ATOM   10009 C CG  . GLN   A 1 1366 ? 167.700 130.457 121.779 1.00 60.63  0  1330 GLN   A CG  1 
ATOM   10010 C CD  . GLN   A 1 1366 ? 168.204 131.215 122.989 1.00 63.95  0  1330 GLN   A CD  1 
ATOM   10011 O OE1 . GLN   A 1 1366 ? 168.850 132.253 122.858 1.00 64.16  0  1330 GLN   A OE1 1 
ATOM   10012 N NE2 . GLN   A 1 1366 ? 167.915 130.697 124.175 1.00 64.36  0  1330 GLN   A NE2 1 
ATOM   10013 N N   . TYR   A 1 1367 ? 164.675 134.050 120.454 1.00 53.04  0  1331 TYR   A N   1 
ATOM   10014 C CA  . TYR   A 1 1367 ? 163.791 134.772 119.543 1.00 50.64  0  1331 TYR   A CA  1 
ATOM   10015 C C   . TYR   A 1 1367 ? 164.587 135.199 118.319 1.00 53.53  0  1331 TYR   A C   1 
ATOM   10016 O O   . TYR   A 1 1367 ? 165.385 136.136 118.374 1.00 55.66  0  1331 TYR   A O   1 
ATOM   10017 C CB  . TYR   A 1 1367 ? 163.156 135.960 120.251 1.00 47.15  0  1331 TYR   A CB  1 
ATOM   10018 C CG  . TYR   A 1 1367 ? 162.254 135.550 121.391 1.00 50.51  0  1331 TYR   A CG  1 
ATOM   10019 C CD1 . TYR   A 1 1367 ? 162.763 135.334 122.661 1.00 50.97  0  1331 TYR   A CD1 1 
ATOM   10020 C CD2 . TYR   A 1 1367 ? 160.897 135.370 121.192 1.00 53.37  0  1331 TYR   A CD2 1 
ATOM   10021 C CE1 . TYR   A 1 1367 ? 161.944 134.953 123.700 1.00 49.57  0  1331 TYR   A CE1 1 
ATOM   10022 C CE2 . TYR   A 1 1367 ? 160.073 134.991 122.225 1.00 50.57  0  1331 TYR   A CE2 1 
ATOM   10023 C CZ  . TYR   A 1 1367 ? 160.600 134.783 123.475 1.00 49.07  0  1331 TYR   A CZ  1 
ATOM   10024 O OH  . TYR   A 1 1367 ? 159.776 134.404 124.506 1.00 52.08  0  1331 TYR   A OH  1 
ATOM   10025 N N   . LEU   A 1 1368 ? 164.365 134.502 117.203 1.00 61.91  0  1332 LEU   A N   1 
ATOM   10026 C CA  . LEU   A 1 1368 ? 165.086 134.813 115.974 1.00 61.94  0  1332 LEU   A CA  1 
ATOM   10027 C C   . LEU   A 1 1368 ? 164.748 136.204 115.462 1.00 65.28  0  1332 LEU   A C   1 
ATOM   10028 O O   . LEU   A 1 1368 ? 165.561 136.825 114.768 1.00 63.24  0  1332 LEU   A O   1 
ATOM   10029 C CB  . LEU   A 1 1368 ? 164.769 133.772 114.902 1.00 61.19  0  1332 LEU   A CB  1 
ATOM   10030 C CG  . LEU   A 1 1368 ? 165.032 132.313 115.264 1.00 61.42  0  1332 LEU   A CG  1 
ATOM   10031 C CD1 . LEU   A 1 1368 ? 164.530 131.399 114.160 1.00 59.73  0  1332 LEU   A CD1 1 
ATOM   10032 C CD2 . LEU   A 1 1368 ? 166.510 132.090 115.520 1.00 62.75  0  1332 LEU   A CD2 1 
ATOM   10033 N N   . SER   A 1 1369 ? 163.561 136.704 115.785 1.00 59.22  0  1333 SER   A N   1 
ATOM   10034 C CA  . SER   A 1 1369 ? 163.134 138.003 115.293 1.00 54.27  0  1333 SER   A CA  1 
ATOM   10035 C C   . SER   A 1 1369 ? 163.995 139.115 115.880 1.00 56.71  0  1333 SER   A C   1 
ATOM   10036 O O   . SER   A 1 1369 ? 164.428 139.057 117.032 1.00 54.90  0  1333 SER   A O   1 
ATOM   10037 C CB  . SER   A 1 1369 ? 161.667 138.236 115.631 1.00 53.01  0  1333 SER   A CB  1 
ATOM   10038 O OG  . SER   A 1 1369 ? 161.422 137.981 116.999 1.00 56.87  0  1333 SER   A OG  1 
ATOM   10039 N N   . VAL   A 1 1370 ? 164.244 140.135 115.061 1.00 64.15  0  1334 VAL   A N   1 
ATOM   10040 C CA  . VAL   A 1 1370 ? 165.089 141.244 115.485 1.00 61.74  0  1334 VAL   A CA  1 
ATOM   10041 C C   . VAL   A 1 1370 ? 164.273 142.297 116.220 1.00 59.48  0  1334 VAL   A C   1 
ATOM   10042 O O   . VAL   A 1 1370 ? 164.706 142.828 117.248 1.00 58.52  0  1334 VAL   A O   1 
ATOM   10043 C CB  . VAL   A 1 1370 ? 165.817 141.845 114.268 1.00 58.68  0  1334 VAL   A CB  1 
ATOM   10044 C CG1 . VAL   A 1 1370 ? 166.820 142.896 114.713 1.00 56.23  0  1334 VAL   A CG1 1 
ATOM   10045 C CG2 . VAL   A 1 1370 ? 166.496 140.752 113.463 1.00 58.18  0  1334 VAL   A CG2 1 
ATOM   10046 N N   . ASN   A 1 1371 ? 163.084 142.611 115.713 1.00 51.89  0  1335 ASN   A N   1 
ATOM   10047 C CA  . ASN   A 1 1371 ? 162.274 143.709 116.224 1.00 53.84  0  1335 ASN   A CA  1 
ATOM   10048 C C   . ASN   A 1 1371 ? 161.348 143.190 117.315 1.00 55.78  0  1335 ASN   A C   1 
ATOM   10049 O O   . ASN   A 1 1371 ? 160.494 142.335 117.061 1.00 58.25  0  1335 ASN   A O   1 
ATOM   10050 C CB  . ASN   A 1 1371 ? 161.476 144.358 115.099 1.00 53.38  0  1335 ASN   A CB  1 
ATOM   10051 C CG  . ASN   A 1 1371 ? 160.880 145.680 115.506 1.00 55.07  0  1335 ASN   A CG  1 
ATOM   10052 O OD1 . ASN   A 1 1371 ? 161.055 146.129 116.635 1.00 58.70  0  1335 ASN   A OD1 1 
ATOM   10053 N ND2 . ASN   A 1 1371 ? 160.177 146.316 114.589 1.00 53.15  0  1335 ASN   A ND2 1 
ATOM   10054 N N   . TYR   A 1 1372 ? 161.515 143.715 118.525 1.00 50.11  0  1336 TYR   A N   1 
ATOM   10055 C CA  . TYR   A 1 1372 ? 160.643 143.389 119.643 1.00 40.83  0  1336 TYR   A CA  1 
ATOM   10056 C C   . TYR   A 1 1372 ? 159.528 144.401 119.844 1.00 40.05  0  1336 TYR   A C   1 
ATOM   10057 O O   . TYR   A 1 1372 ? 158.645 144.164 120.672 1.00 51.59  0  1336 TYR   A O   1 
ATOM   10058 C CB  . TYR   A 1 1372 ? 161.477 143.249 120.921 1.00 41.44  0  1336 TYR   A CB  1 
ATOM   10059 C CG  . TYR   A 1 1372 ? 162.427 144.398 121.196 1.00 44.72  0  1336 TYR   A CG  1 
ATOM   10060 C CD1 . TYR   A 1 1372 ? 163.763 144.157 121.464 1.00 47.05  0  1336 TYR   A CD1 1 
ATOM   10061 C CD2 . TYR   A 1 1372 ? 161.990 145.715 121.211 1.00 43.98  0  1336 TYR   A CD2 1 
ATOM   10062 C CE1 . TYR   A 1 1372 ? 164.639 145.187 121.720 1.00 47.57  0  1336 TYR   A CE1 1 
ATOM   10063 C CE2 . TYR   A 1 1372 ? 162.859 146.753 121.466 1.00 48.66  0  1336 TYR   A CE2 1 
ATOM   10064 C CZ  . TYR   A 1 1372 ? 164.183 146.483 121.720 1.00 52.28  0  1336 TYR   A CZ  1 
ATOM   10065 O OH  . TYR   A 1 1372 ? 165.056 147.515 121.975 1.00 55.18  0  1336 TYR   A OH  1 
ATOM   10066 N N   . LEU   A 1 1373 ? 159.540 145.508 119.110 1.00 35.82  0  1337 LEU   A N   1 
ATOM   10067 C CA  . LEU   A 1 1373 ? 158.549 146.552 119.315 1.00 37.87  0  1337 LEU   A CA  1 
ATOM   10068 C C   . LEU   A 1 1373 ? 157.223 146.253 118.632 1.00 41.02  0  1337 LEU   A C   1 
ATOM   10069 O O   . LEU   A 1 1373 ? 156.265 147.005 118.829 1.00 49.40  0  1337 LEU   A O   1 
ATOM   10070 C CB  . LEU   A 1 1373 ? 159.086 147.897 118.828 1.00 34.45  0  1337 LEU   A CB  1 
ATOM   10071 C CG  . LEU   A 1 1373 ? 160.258 148.506 119.594 1.00 34.71  0  1337 LEU   A CG  1 
ATOM   10072 C CD1 . LEU   A 1 1373 ? 160.645 149.831 118.983 1.00 37.74  0  1337 LEU   A CD1 1 
ATOM   10073 C CD2 . LEU   A 1 1373 ? 159.930 148.672 121.052 1.00 40.53  0  1337 LEU   A CD2 1 
ATOM   10074 N N   . HIS   A 1 1374 ? 157.141 145.193 117.833 1.00 45.77  0  1338 HIS   A N   1 
ATOM   10075 C CA  . HIS   A 1 1374 ? 155.859 144.766 117.297 1.00 48.64  0  1338 HIS   A CA  1 
ATOM   10076 C C   . HIS   A 1 1374 ? 155.676 143.257 117.331 1.00 50.29  0  1338 HIS   A C   1 
ATOM   10077 O O   . HIS   A 1 1374 ? 154.651 142.770 116.848 1.00 46.22  0  1338 HIS   A O   1 
ATOM   10078 C CB  . HIS   A 1 1374 ? 155.678 145.260 115.857 1.00 46.15  0  1338 HIS   A CB  1 
ATOM   10079 C CG  . HIS   A 1 1374 ? 156.325 144.385 114.833 1.00 50.85  0  1338 HIS   A CG  1 
ATOM   10080 N ND1 . HIS   A 1 1374 ? 155.654 143.358 114.206 1.00 51.63  0  1338 HIS   A ND1 1 
ATOM   10081 C CD2 . HIS   A 1 1374 ? 157.579 144.380 114.326 1.00 49.40  0  1338 HIS   A CD2 1 
ATOM   10082 C CE1 . HIS   A 1 1374 ? 156.466 142.760 113.354 1.00 51.95  0  1338 HIS   A CE1 1 
ATOM   10083 N NE2 . HIS   A 1 1374 ? 157.641 143.361 113.407 1.00 50.45  0  1338 HIS   A NE2 1 
ATOM   10084 N N   . ARG   A 1 1375 ? 156.631 142.505 117.877 1.00 56.81  0  1339 ARG   A N   1 
ATOM   10085 C CA  . ARG   A 1 1375 ? 156.512 141.062 118.004 1.00 51.70  0  1339 ARG   A CA  1 
ATOM   10086 C C   . ARG   A 1 1375 ? 156.462 140.590 119.446 1.00 51.60  0  1339 ARG   A C   1 
ATOM   10087 O O   . ARG   A 1 1375 ? 156.216 139.403 119.679 1.00 53.32  0  1339 ARG   A O   1 
ATOM   10088 C CB  . ARG   A 1 1375 ? 157.675 140.366 117.287 1.00 49.54  0  1339 ARG   A CB  1 
ATOM   10089 C CG  . ARG   A 1 1375 ? 157.690 140.603 115.795 1.00 53.03  0  1339 ARG   A CG  1 
ATOM   10090 C CD  . ARG   A 1 1375 ? 158.439 139.505 115.076 1.00 56.93  0  1339 ARG   A CD  1 
ATOM   10091 N NE  . ARG   A 1 1375 ? 158.088 139.444 113.664 1.00 58.75  0  1339 ARG   A NE  1 
ATOM   10092 C CZ  . ARG   A 1 1375 ? 156.960 138.929 113.197 1.00 62.69  0  1339 ARG   A CZ  1 
ATOM   10093 N NH1 . ARG   A 1 1375 ? 156.054 138.404 114.005 1.00 60.00  1  1339 ARG   A NH1 1 
ATOM   10094 N NH2 . ARG   A 1 1375 ? 156.737 138.937 111.886 1.00 61.06  0  1339 ARG   A NH2 1 
ATOM   10095 N N   . LEU   A 1 1376 ? 156.700 141.472 120.410 1.00 46.46  0  1340 LEU   A N   1 
ATOM   10096 C CA  . LEU   A 1 1376 ? 156.537 141.102 121.806 1.00 45.66  0  1340 LEU   A CA  1 
ATOM   10097 C C   . LEU   A 1 1376 ? 155.076 140.782 122.087 1.00 49.84  0  1340 LEU   A C   1 
ATOM   10098 O O   . LEU   A 1 1376 ? 154.165 141.368 121.497 1.00 56.26  0  1340 LEU   A O   1 
ATOM   10099 C CB  . LEU   A 1 1376 ? 157.018 142.229 122.717 1.00 33.12  0  1340 LEU   A CB  1 
ATOM   10100 C CG  . LEU   A 1 1376 ? 156.971 141.960 124.217 1.00 32.98  0  1340 LEU   A CG  1 
ATOM   10101 C CD1 . LEU   A 1 1376 ? 157.946 140.865 124.584 1.00 37.29  0  1340 LEU   A CD1 1 
ATOM   10102 C CD2 . LEU   A 1 1376 ? 157.280 143.222 124.978 1.00 43.38  0  1340 LEU   A CD2 1 
ATOM   10103 N N   . THR   A 1 1377 ? 154.853 139.828 122.985 1.00 48.36  0  1341 THR   A N   1 
ATOM   10104 C CA  . THR   A 1 1377 ? 153.507 139.374 123.319 1.00 47.85  0  1341 THR   A CA  1 
ATOM   10105 C C   . THR   A 1 1377 ? 153.321 139.459 124.830 1.00 43.40  0  1341 THR   A C   1 
ATOM   10106 O O   . THR   A 1 1377 ? 153.805 138.601 125.573 1.00 49.40  0  1341 THR   A O   1 
ATOM   10107 C CB  . THR   A 1 1377 ? 153.268 137.959 122.809 1.00 51.32  0  1341 THR   A CB  1 
ATOM   10108 O OG1 . THR   A 1 1377 ? 154.381 137.130 123.164 1.00 51.07  0  1341 THR   A OG1 1 
ATOM   10109 C CG2 . THR   A 1 1377 ? 153.113 137.964 121.299 1.00 46.97  0  1341 THR   A CG2 1 
ATOM   10110 N N   . VAL   A 1 1378 ? 152.623 140.499 125.280 1.00 35.17  0  1342 VAL   A N   1 
ATOM   10111 C CA  . VAL   A 1 1378 ? 152.210 140.631 126.667 1.00 42.39  0  1342 VAL   A CA  1 
ATOM   10112 C C   . VAL   A 1 1378 ? 150.713 140.907 126.704 1.00 45.34  0  1342 VAL   A C   1 
ATOM   10113 O O   . VAL   A 1 1378 ? 150.068 141.106 125.676 1.00 48.34  0  1342 VAL   A O   1 
ATOM   10114 C CB  . VAL   A 1 1378 ? 152.991 141.726 127.415 1.00 47.58  0  1342 VAL   A CB  1 
ATOM   10115 C CG1 . VAL   A 1 1378 ? 154.326 141.193 127.858 1.00 48.40  0  1342 VAL   A CG1 1 
ATOM   10116 C CG2 . VAL   A 1 1378 ? 153.186 142.934 126.524 1.00 41.40  0  1342 VAL   A CG2 1 
ATOM   10117 N N   . SER   A 1 1379 ? 150.164 140.910 127.919 1.00 39.19  0  1343 SER   A N   1 
ATOM   10118 C CA  . SER   A 1 1379 ? 148.732 141.115 128.087 1.00 41.37  0  1343 SER   A CA  1 
ATOM   10119 C C   . SER   A 1 1379 ? 148.296 142.523 127.706 1.00 43.61  0  1343 SER   A C   1 
ATOM   10120 O O   . SER   A 1 1379 ? 147.097 142.757 127.524 1.00 50.43  0  1343 SER   A O   1 
ATOM   10121 C CB  . SER   A 1 1379 ? 148.328 140.819 129.530 1.00 43.69  0  1343 SER   A CB  1 
ATOM   10122 O OG  . SER   A 1 1379 ? 148.963 141.712 130.424 1.00 42.74  0  1343 SER   A OG  1 
ATOM   10123 N N   . SER   A 1 1380 ? 149.230 143.457 127.571 1.00 34.16  0  1344 SER   A N   1 
ATOM   10124 C CA  . SER   A 1 1380 ? 148.899 144.836 127.246 1.00 34.32  0  1344 SER   A CA  1 
ATOM   10125 C C   . SER   A 1 1380 ? 148.783 145.080 125.752 1.00 36.98  0  1344 SER   A C   1 
ATOM   10126 O O   . SER   A 1 1380 ? 148.568 146.226 125.344 1.00 42.53  0  1344 SER   A O   1 
ATOM   10127 C CB  . SER   A 1 1380 ? 149.943 145.783 127.840 1.00 36.70  0  1344 SER   A CB  1 
ATOM   10128 O OG  . SER   A 1 1380 ? 151.168 145.690 127.140 1.00 45.37  0  1344 SER   A OG  1 
ATOM   10129 N N   . ARG   A 1 1381 ? 148.921 144.044 124.929 1.00 31.28  0  1345 ARG   A N   1 
ATOM   10130 C CA  . ARG   A 1 1381 ? 148.843 144.205 123.492 1.00 36.89  0  1345 ARG   A CA  1 
ATOM   10131 C C   . ARG   A 1 1381 ? 147.712 143.361 122.921 1.00 39.81  0  1345 ARG   A C   1 
ATOM   10132 O O   . ARG   A 1 1381 ? 147.443 142.265 123.423 1.00 41.96  0  1345 ARG   A O   1 
ATOM   10133 C CB  . ARG   A 1 1381 ? 150.162 143.803 122.826 1.00 32.76  0  1345 ARG   A CB  1 
ATOM   10134 C CG  . ARG   A 1 1381 ? 151.381 144.103 123.662 1.00 33.06  0  1345 ARG   A CG  1 
ATOM   10135 C CD  . ARG   A 1 1381 ? 152.643 143.982 122.843 1.00 38.60  0  1345 ARG   A CD  1 
ATOM   10136 N NE  . ARG   A 1 1381 ? 152.651 144.928 121.737 1.00 38.53  0  1345 ARG   A NE  1 
ATOM   10137 C CZ  . ARG   A 1 1381 ? 153.748 145.362 121.134 1.00 38.62  0  1345 ARG   A CZ  1 
ATOM   10138 N NH1 . ARG   A 1 1381 ? 154.948 144.957 121.509 1.00 37.51  1  1345 ARG   A NH1 1 
ATOM   10139 N NH2 . ARG   A 1 1381 ? 153.636 146.230 120.134 1.00 39.49  0  1345 ARG   A NH2 1 
ATOM   10140 N N   . PRO   A 1 1382 ? 147.032 143.840 121.879 1.00 37.91  0  1346 PRO   A N   1 
ATOM   10141 C CA  . PRO   A 1 1382 ? 145.920 143.074 121.300 1.00 46.04  0  1346 PRO   A CA  1 
ATOM   10142 C C   . PRO   A 1 1382 ? 146.425 141.808 120.625 1.00 47.77  0  1346 PRO   A C   1 
ATOM   10143 O O   . PRO   A 1 1382 ? 147.242 141.863 119.704 1.00 46.39  0  1346 PRO   A O   1 
ATOM   10144 C CB  . PRO   A 1 1382 ? 145.305 144.049 120.289 1.00 41.55  0  1346 PRO   A CB  1 
ATOM   10145 C CG  . PRO   A 1 1382 ? 145.820 145.392 120.673 1.00 33.95  0  1346 PRO   A CG  1 
ATOM   10146 C CD  . PRO   A 1 1382 ? 147.173 145.161 121.250 1.00 34.16  0  1346 PRO   A CD  1 
ATOM   10147 N N   . CYS   A 1 1383 ? 145.929 140.662 121.088 1.00 48.89  0  1347 CYS   A N   1 
ATOM   10148 C CA  . CYS   A 1 1383 ? 146.295 139.377 120.513 1.00 49.75  0  1347 CYS   A CA  1 
ATOM   10149 C C   . CYS   A 1 1383 ? 145.664 139.134 119.150 1.00 50.14  0  1347 CYS   A C   1 
ATOM   10150 O O   . CYS   A 1 1383 ? 146.198 138.339 118.372 1.00 45.31  0  1347 CYS   A O   1 
ATOM   10151 C CB  . CYS   A 1 1383 ? 145.906 138.245 121.470 1.00 50.40  0  1347 CYS   A CB  1 
ATOM   10152 S SG  . CYS   A 1 1383 ? 144.230 138.371 122.131 1.00 61.98  0  1347 CYS   A SG  1 
ATOM   10153 N N   . GLU   A 1 1384 ? 144.545 139.788 118.849 1.00 49.74  0  1348 GLU   A N   1 
ATOM   10154 C CA  . GLU   A 1 1384 ? 143.912 139.710 117.541 1.00 41.93  0  1348 GLU   A CA  1 
ATOM   10155 C C   . GLU   A 1 1384 ? 143.421 141.100 117.170 1.00 39.79  0  1348 GLU   A C   1 
ATOM   10156 O O   . GLU   A 1 1384 ? 143.181 141.941 118.038 1.00 49.84  0  1348 GLU   A O   1 
ATOM   10157 C CB  . GLU   A 1 1384 ? 142.744 138.717 117.525 1.00 43.03  0  1348 GLU   A CB  1 
ATOM   10158 C CG  . GLU   A 1 1384 ? 143.101 137.300 117.108 1.00 51.70  0  1348 GLU   A CG  1 
ATOM   10159 C CD  . GLU   A 1 1384 ? 143.724 136.491 118.228 1.00 51.58  0  1348 GLU   A CD  1 
ATOM   10160 O OE1 . GLU   A 1 1384 ? 143.083 136.360 119.291 1.00 49.18  0  1348 GLU   A OE1 1 
ATOM   10161 O OE2 . GLU   A 1 1384 ? 144.844 135.973 118.041 1.00 52.05  -1 1348 GLU   A OE2 1 
ATOM   10162 N N   . PHE   A 1 1385 ? 143.264 141.336 115.873 1.00 28.10  0  1349 PHE   A N   1 
ATOM   10163 C CA  . PHE   A 1 1385 ? 142.779 142.619 115.363 1.00 28.51  0  1349 PHE   A CA  1 
ATOM   10164 C C   . PHE   A 1 1385 ? 141.628 142.393 114.392 1.00 41.75  0  1349 PHE   A C   1 
ATOM   10165 O O   . PHE   A 1 1385 ? 141.751 142.645 113.190 1.00 50.94  0  1349 PHE   A O   1 
ATOM   10166 C CB  . PHE   A 1 1385 ? 143.910 143.396 114.695 1.00 32.13  0  1349 PHE   A CB  1 
ATOM   10167 C CG  . PHE   A 1 1385 ? 145.016 143.779 115.629 1.00 32.99  0  1349 PHE   A CG  1 
ATOM   10168 C CD1 . PHE   A 1 1385 ? 146.004 142.872 115.959 1.00 33.75  0  1349 PHE   A CD1 1 
ATOM   10169 C CD2 . PHE   A 1 1385 ? 145.073 145.047 116.169 1.00 33.37  0  1349 PHE   A CD2 1 
ATOM   10170 C CE1 . PHE   A 1 1385 ? 147.019 143.219 116.815 1.00 32.08  0  1349 PHE   A CE1 1 
ATOM   10171 C CE2 . PHE   A 1 1385 ? 146.085 145.399 117.023 1.00 35.22  0  1349 PHE   A CE2 1 
ATOM   10172 C CZ  . PHE   A 1 1385 ? 147.062 144.484 117.345 1.00 38.62  0  1349 PHE   A CZ  1 
ATOM   10173 N N   . PRO   A 1 1386 ? 140.483 141.931 114.884 1.00 35.72  0  1350 PRO   A N   1 
ATOM   10174 C CA  . PRO   A 1 1386 ? 139.367 141.620 113.989 1.00 29.63  0  1350 PRO   A CA  1 
ATOM   10175 C C   . PRO   A 1 1386 ? 138.636 142.881 113.560 1.00 31.72  0  1350 PRO   A C   1 
ATOM   10176 O O   . PRO   A 1 1386 ? 138.859 143.976 114.075 1.00 39.13  0  1350 PRO   A O   1 
ATOM   10177 C CB  . PRO   A 1 1386 ? 138.480 140.721 114.845 1.00 26.25  0  1350 PRO   A CB  1 
ATOM   10178 C CG  . PRO   A 1 1386 ? 138.714 141.202 116.222 1.00 27.86  0  1350 PRO   A CG  1 
ATOM   10179 C CD  . PRO   A 1 1386 ? 140.136 141.684 116.293 1.00 29.38  0  1350 PRO   A CD  1 
ATOM   10180 N N   . ALA   A 1 1387 ? 137.757 142.709 112.579 1.00 21.48  0  1351 ALA   A N   1 
ATOM   10181 C CA  . ALA   A 1 1387 ? 136.928 143.801 112.100 1.00 26.04  0  1351 ALA   A CA  1 
ATOM   10182 C C   . ALA   A 1 1387 ? 135.688 143.932 112.979 1.00 42.14  0  1351 ALA   A C   1 
ATOM   10183 O O   . ALA   A 1 1387 ? 135.451 143.133 113.889 1.00 42.87  0  1351 ALA   A O   1 
ATOM   10184 C CB  . ALA   A 1 1387 ? 136.553 143.579 110.639 1.00 17.95  0  1351 ALA   A CB  1 
ATOM   10185 N N   . SER   A 1 1388 ? 134.895 144.966 112.731 1.00 37.33  0  1352 SER   A N   1 
ATOM   10186 C CA  . SER   A 1 1388 ? 133.611 145.117 113.418 1.00 24.00  0  1352 SER   A CA  1 
ATOM   10187 C C   . SER   A 1 1388 ? 132.481 144.515 112.597 1.00 30.36  0  1352 SER   A C   1 
ATOM   10188 O O   . SER   A 1 1388 ? 131.444 145.138 112.382 1.00 41.11  0  1352 SER   A O   1 
ATOM   10189 C CB  . SER   A 1 1388 ? 133.341 146.583 113.717 1.00 33.53  0  1352 SER   A CB  1 
ATOM   10190 O OG  . SER   A 1 1388 ? 132.499 147.146 112.729 1.00 38.93  0  1352 SER   A OG  1 
ATOM   10191 N N   . ILE   A 1 1389 ? 132.679 143.284 112.134 1.00 25.86  0  1353 ILE   A N   1 
ATOM   10192 C CA  . ILE   A 1 1389 ? 131.642 142.537 111.421 1.00 23.03  0  1353 ILE   A CA  1 
ATOM   10193 C C   . ILE   A 1 1389 ? 131.778 141.067 111.760 1.00 33.77  0  1353 ILE   A C   1 
ATOM   10194 O O   . ILE   A 1 1389 ? 132.849 140.596 112.164 1.00 31.30  0  1353 ILE   A O   1 
ATOM   10195 C CB  . ILE   A 1 1389 ? 131.737 142.724 109.889 1.00 22.40  0  1353 ILE   A CB  1 
ATOM   10196 C CG1 . ILE   A 1 1389 ? 133.182 142.629 109.408 1.00 27.44  0  1353 ILE   A CG1 1 
ATOM   10197 C CG2 . ILE   A 1 1389 ? 131.117 144.039 109.461 1.00 16.22  0  1353 ILE   A CG2 1 
ATOM   10198 C CD1 . ILE   A 1 1389 ? 133.321 142.761 107.908 1.00 27.83  0  1353 ILE   A CD1 1 
ATOM   10199 N N   . PRO   A 1 1390 ? 130.689 140.311 111.620 1.00 34.67  0  1354 PRO   A N   1 
ATOM   10200 C CA  . PRO   A 1 1390 ? 130.778 138.868 111.856 1.00 32.51  0  1354 PRO   A CA  1 
ATOM   10201 C C   . PRO   A 1 1390 ? 131.755 138.228 110.883 1.00 35.32  0  1354 PRO   A C   1 
ATOM   10202 O O   . PRO   A 1 1390 ? 131.928 138.689 109.753 1.00 27.95  0  1354 PRO   A O   1 
ATOM   10203 C CB  . PRO   A 1 1390 ? 129.345 138.380 111.626 1.00 27.10  0  1354 PRO   A CB  1 
ATOM   10204 C CG  . PRO   A 1 1390 ? 128.501 139.581 111.846 1.00 21.59  0  1354 PRO   A CG  1 
ATOM   10205 C CD  . PRO   A 1 1390 ? 129.307 140.735 111.349 1.00 22.55  0  1354 PRO   A CD  1 
ATOM   10206 N N   . ALA   A 1 1391 ? 132.404 137.157 111.345 1.00 36.10  0  1355 ALA   A N   1 
ATOM   10207 C CA  . ALA   A 1 1391 ? 133.489 136.551 110.579 1.00 31.44  0  1355 ALA   A CA  1 
ATOM   10208 C C   . ALA   A 1 1391 ? 133.034 136.162 109.179 1.00 27.10  0  1355 ALA   A C   1 
ATOM   10209 O O   . ALA   A 1 1391 ? 133.712 136.464 108.190 1.00 34.28  0  1355 ALA   A O   1 
ATOM   10210 C CB  . ALA   A 1 1391 ? 134.036 135.335 111.326 1.00 24.51  0  1355 ALA   A CB  1 
ATOM   10211 N N   . TYR   A 1 1392 ? 131.867 135.521 109.075 1.00 24.96  0  1356 TYR   A N   1 
ATOM   10212 C CA  . TYR   A 1 1392 ? 131.367 135.085 107.775 1.00 30.67  0  1356 TYR   A CA  1 
ATOM   10213 C C   . TYR   A 1 1392 ? 131.325 136.239 106.783 1.00 31.98  0  1356 TYR   A C   1 
ATOM   10214 O O   . TYR   A 1 1392 ? 131.632 136.065 105.598 1.00 47.15  0  1356 TYR   A O   1 
ATOM   10215 C CB  . TYR   A 1 1392 ? 129.976 134.458 107.927 1.00 31.89  0  1356 TYR   A CB  1 
ATOM   10216 C CG  . TYR   A 1 1392 ? 128.841 135.459 107.899 1.00 27.97  0  1356 TYR   A CG  1 
ATOM   10217 C CD1 . TYR   A 1 1392 ? 128.223 135.807 106.706 1.00 28.49  0  1356 TYR   A CD1 1 
ATOM   10218 C CD2 . TYR   A 1 1392 ? 128.386 136.052 109.064 1.00 27.93  0  1356 TYR   A CD2 1 
ATOM   10219 C CE1 . TYR   A 1 1392 ? 127.200 136.724 106.675 1.00 28.95  0  1356 TYR   A CE1 1 
ATOM   10220 C CE2 . TYR   A 1 1392 ? 127.358 136.968 109.040 1.00 31.18  0  1356 TYR   A CE2 1 
ATOM   10221 C CZ  . TYR   A 1 1392 ? 126.772 137.299 107.843 1.00 29.82  0  1356 TYR   A CZ  1 
ATOM   10222 O OH  . TYR   A 1 1392 ? 125.748 138.210 107.812 1.00 28.10  0  1356 TYR   A OH  1 
ATOM   10223 N N   . ARG   A 1 1393 ? 130.973 137.433 107.258 1.00 18.52  0  1357 ARG   A N   1 
ATOM   10224 C CA  . ARG   A 1 1393 ? 130.821 138.575 106.367 1.00 21.23  0  1357 ARG   A CA  1 
ATOM   10225 C C   . ARG   A 1 1393 ? 132.131 138.906 105.670 1.00 34.21  0  1357 ARG   A C   1 
ATOM   10226 O O   . ARG   A 1 1393 ? 132.139 139.305 104.499 1.00 33.65  0  1357 ARG   A O   1 
ATOM   10227 C CB  . ARG   A 1 1393 ? 130.309 139.774 107.156 1.00 21.74  0  1357 ARG   A CB  1 
ATOM   10228 C CG  . ARG   A 1 1393 ? 129.977 140.963 106.307 1.00 27.27  0  1357 ARG   A CG  1 
ATOM   10229 C CD  . ARG   A 1 1393 ? 128.648 140.787 105.634 1.00 22.03  0  1357 ARG   A CD  1 
ATOM   10230 N NE  . ARG   A 1 1393 ? 128.297 141.979 104.878 1.00 22.83  0  1357 ARG   A NE  1 
ATOM   10231 C CZ  . ARG   A 1 1393 ? 127.794 143.078 105.417 1.00 30.20  0  1357 ARG   A CZ  1 
ATOM   10232 N NH1 . ARG   A 1 1393 ? 127.534 143.157 106.710 1.00 35.65  1  1357 ARG   A NH1 1 
ATOM   10233 N NH2 . ARG   A 1 1393 ? 127.546 144.124 104.640 1.00 30.93  0  1357 ARG   A NH2 1 
ATOM   10234 N N   . THR   A 1 1394 ? 133.254 138.722 106.368 1.00 32.71  0  1358 THR   A N   1 
ATOM   10235 C CA  . THR   A 1 1394 ? 134.544 139.045 105.776 1.00 24.84  0  1358 THR   A CA  1 
ATOM   10236 C C   . THR   A 1 1394 ? 134.815 138.208 104.537 1.00 26.29  0  1358 THR   A C   1 
ATOM   10237 O O   . THR   A 1 1394 ? 135.630 138.595 103.693 1.00 31.53  0  1358 THR   A O   1 
ATOM   10238 C CB  . THR   A 1 1394 ? 135.654 138.843 106.800 1.00 29.83  0  1358 THR   A CB  1 
ATOM   10239 O OG1 . THR   A 1 1394 ? 135.828 137.443 107.038 1.00 30.80  0  1358 THR   A OG1 1 
ATOM   10240 C CG2 . THR   A 1 1394 ? 135.292 139.524 108.103 1.00 31.44  0  1358 THR   A CG2 1 
ATOM   10241 N N   . THR   A 1 1395 ? 134.138 137.064 104.403 1.00 34.75  0  1359 THR   A N   1 
ATOM   10242 C CA  . THR   A 1 1395 ? 134.339 136.223 103.232 1.00 28.45  0  1359 THR   A CA  1 
ATOM   10243 C C   . THR   A 1 1395 ? 133.834 136.877 101.955 1.00 34.78  0  1359 THR   A C   1 
ATOM   10244 O O   . THR   A 1 1395 ? 134.253 136.479 100.865 1.00 43.83  0  1359 THR   A O   1 
ATOM   10245 C CB  . THR   A 1 1395 ? 133.653 134.874 103.427 1.00 17.53  0  1359 THR   A CB  1 
ATOM   10246 O OG1 . THR   A 1 1395 ? 132.238 135.065 103.496 1.00 25.67  0  1359 THR   A OG1 1 
ATOM   10247 C CG2 . THR   A 1 1395 ? 134.128 134.224 104.707 1.00 22.00  0  1359 THR   A CG2 1 
ATOM   10248 N N   . ASN   A 1 1396 ? 132.960 137.879 102.055 1.00 30.69  0  1360 ASN   A N   1 
ATOM   10249 C CA  . ASN   A 1 1396 ? 132.416 138.487 100.846 1.00 26.34  0  1360 ASN   A CA  1 
ATOM   10250 C C   . ASN   A 1 1396 ? 133.421 139.381 100.133 1.00 39.27  0  1360 ASN   A C   1 
ATOM   10251 O O   . ASN   A 1 1396 ? 133.185 139.750 98.978  1.00 42.66  0  1360 ASN   A O   1 
ATOM   10252 C CB  . ASN   A 1 1396 ? 131.169 139.302 101.179 1.00 37.05  0  1360 ASN   A CB  1 
ATOM   10253 C CG  . ASN   A 1 1396 ? 130.180 138.537 102.022 1.00 44.73  0  1360 ASN   A CG  1 
ATOM   10254 O OD1 . ASN   A 1 1396 ? 130.560 137.722 102.858 1.00 47.92  0  1360 ASN   A OD1 1 
ATOM   10255 N ND2 . ASN   A 1 1396 ? 128.899 138.807 101.819 1.00 45.54  0  1360 ASN   A ND2 1 
ATOM   10256 N N   . TYR   A 1 1397 ? 134.529 139.734 100.782 1.00 47.12  0  1361 TYR   A N   1 
ATOM   10257 C CA  . TYR   A 1 1397 ? 135.436 140.760 100.288 1.00 41.42  0  1361 TYR   A CA  1 
ATOM   10258 C C   . TYR   A 1 1397 ? 136.861 140.231 100.190 1.00 39.16  0  1361 TYR   A C   1 
ATOM   10259 O O   . TYR   A 1 1397 ? 137.261 139.326 100.928 1.00 38.42  0  1361 TYR   A O   1 
ATOM   10260 C CB  . TYR   A 1 1397 ? 135.409 141.996 101.193 1.00 34.53  0  1361 TYR   A CB  1 
ATOM   10261 C CG  . TYR   A 1 1397 ? 134.025 142.363 101.667 1.00 36.84  0  1361 TYR   A CG  1 
ATOM   10262 C CD1 . TYR   A 1 1397 ? 133.091 142.887 100.789 1.00 39.06  0  1361 TYR   A CD1 1 
ATOM   10263 C CD2 . TYR   A 1 1397 ? 133.649 142.178 102.989 1.00 37.26  0  1361 TYR   A CD2 1 
ATOM   10264 C CE1 . TYR   A 1 1397 ? 131.825 143.224 101.211 1.00 45.00  0  1361 TYR   A CE1 1 
ATOM   10265 C CE2 . TYR   A 1 1397 ? 132.382 142.511 103.419 1.00 41.20  0  1361 TYR   A CE2 1 
ATOM   10266 C CZ  . TYR   A 1 1397 ? 131.475 143.032 102.525 1.00 43.54  0  1361 TYR   A CZ  1 
ATOM   10267 O OH  . TYR   A 1 1397 ? 130.210 143.367 102.943 1.00 39.91  0  1361 TYR   A OH  1 
ATOM   10268 N N   . HIS   A 1 1398 ? 137.623 140.816 99.270  1.00 31.46  0  1362 HIS   A N   1 
ATOM   10269 C CA  . HIS   A 1 1398 ? 139.015 140.458 99.036  1.00 34.03  0  1362 HIS   A CA  1 
ATOM   10270 C C   . HIS   A 1 1398 ? 139.884 141.700 99.157  1.00 40.16  0  1362 HIS   A C   1 
ATOM   10271 O O   . HIS   A 1 1398 ? 139.572 142.738 98.566  1.00 38.23  0  1362 HIS   A O   1 
ATOM   10272 C CB  . HIS   A 1 1398 ? 139.190 139.824 97.657  1.00 40.60  0  1362 HIS   A CB  1 
ATOM   10273 C CG  . HIS   A 1 1398 ? 140.596 139.414 97.355  1.00 42.24  0  1362 HIS   A CG  1 
ATOM   10274 N ND1 . HIS   A 1 1398 ? 141.326 139.964 96.323  1.00 41.55  0  1362 HIS   A ND1 1 
ATOM   10275 C CD2 . HIS   A 1 1398 ? 141.408 138.508 97.949  1.00 41.43  0  1362 HIS   A CD2 1 
ATOM   10276 C CE1 . HIS   A 1 1398 ? 142.527 139.417 96.295  1.00 41.70  0  1362 HIS   A CE1 1 
ATOM   10277 N NE2 . HIS   A 1 1398 ? 142.603 138.530 97.271  1.00 46.50  0  1362 HIS   A NE2 1 
ATOM   10278 N N   . PHE   A 1 1399 ? 140.980 141.589 99.902  1.00 41.64  0  1363 PHE   A N   1 
ATOM   10279 C CA  . PHE   A 1 1399 ? 141.878 142.706 100.158 1.00 34.57  0  1363 PHE   A CA  1 
ATOM   10280 C C   . PHE   A 1 1399 ? 143.205 142.492 99.441  1.00 39.20  0  1363 PHE   A C   1 
ATOM   10281 O O   . PHE   A 1 1399 ? 143.734 141.377 99.420  1.00 42.22  0  1363 PHE   A O   1 
ATOM   10282 C CB  . PHE   A 1 1399 ? 142.089 142.900 101.663 1.00 33.62  0  1363 PHE   A CB  1 
ATOM   10283 C CG  . PHE   A 1 1399 ? 142.498 141.655 102.399 1.00 41.46  0  1363 PHE   A CG  1 
ATOM   10284 C CD1 . PHE   A 1 1399 ? 143.794 141.177 102.332 1.00 41.31  0  1363 PHE   A CD1 1 
ATOM   10285 C CD2 . PHE   A 1 1399 ? 141.576 140.959 103.157 1.00 44.95  0  1363 PHE   A CD2 1 
ATOM   10286 C CE1 . PHE   A 1 1399 ? 144.163 140.033 103.012 1.00 41.75  0  1363 PHE   A CE1 1 
ATOM   10287 C CE2 . PHE   A 1 1399 ? 141.940 139.815 103.838 1.00 41.28  0  1363 PHE   A CE2 1 
ATOM   10288 C CZ  . PHE   A 1 1399 ? 143.234 139.352 103.764 1.00 38.77  0  1363 PHE   A CZ  1 
ATOM   10289 N N   . ASP   A 1 1400 ? 143.722 143.556 98.834  1.00 50.07  0  1364 ASP   A N   1 
ATOM   10290 C CA  . ASP   A 1 1400 ? 144.992 143.538 98.118  1.00 46.50  0  1364 ASP   A CA  1 
ATOM   10291 C C   . ASP   A 1 1400 ? 145.822 144.714 98.614  1.00 48.15  0  1364 ASP   A C   1 
ATOM   10292 O O   . ASP   A 1 1400 ? 145.413 145.872 98.474  1.00 49.40  0  1364 ASP   A O   1 
ATOM   10293 C CB  . ASP   A 1 1400 ? 144.769 143.617 96.609  1.00 49.90  0  1364 ASP   A CB  1 
ATOM   10294 C CG  . ASP   A 1 1400 ? 146.047 143.437 95.818  1.00 56.60  0  1364 ASP   A CG  1 
ATOM   10295 O OD1 . ASP   A 1 1400 ? 146.520 142.288 95.697  1.00 55.07  0  1364 ASP   A OD1 1 
ATOM   10296 O OD2 . ASP   A 1 1400 ? 146.579 144.446 95.313  1.00 59.86  -1 1364 ASP   A OD2 1 
ATOM   10297 N N   . THR   A 1 1401 ? 146.980 144.418 99.195  1.00 52.72  0  1365 THR   A N   1 
ATOM   10298 C CA  . THR   A 1 1401 ? 147.856 145.423 99.784  1.00 53.96  0  1365 THR   A CA  1 
ATOM   10299 C C   . THR   A 1 1401 ? 149.223 145.413 99.117  1.00 52.92  0  1365 THR   A C   1 
ATOM   10300 O O   . THR   A 1 1401 ? 150.254 145.529 99.776  1.00 51.62  0  1365 THR   A O   1 
ATOM   10301 C CB  . THR   A 1 1401 ? 148.009 145.201 101.283 1.00 52.10  0  1365 THR   A CB  1 
ATOM   10302 O OG1 . THR   A 1 1401 ? 149.001 144.195 101.512 1.00 56.29  0  1365 THR   A OG1 1 
ATOM   10303 C CG2 . THR   A 1 1401 ? 146.707 144.732 101.872 1.00 47.76  0  1365 THR   A CG2 1 
ATOM   10304 N N   . SER   A 1 1402 ? 149.247 145.252 97.802  1.00 47.97  0  1366 SER   A N   1 
ATOM   10305 C CA  . SER   A 1 1402 ? 150.503 145.250 97.065  1.00 45.66  0  1366 SER   A CA  1 
ATOM   10306 C C   . SER   A 1 1402 ? 151.021 146.665 96.809  1.00 52.53  0  1366 SER   A C   1 
ATOM   10307 O O   . SER   A 1 1402 ? 152.201 146.929 97.078  1.00 53.63  0  1366 SER   A O   1 
ATOM   10308 C CB  . SER   A 1 1402 ? 150.346 144.488 95.747  1.00 49.13  0  1366 SER   A CB  1 
ATOM   10309 O OG  . SER   A 1 1402 ? 151.549 144.512 94.999  1.00 52.63  0  1366 SER   A OG  1 
ATOM   10310 N N   . PRO   A 1 1403 ? 150.208 147.600 96.290  1.00 51.33  0  1367 PRO   A N   1 
ATOM   10311 C CA  . PRO   A 1 1403 ? 150.762 148.938 96.010  1.00 51.05  0  1367 PRO   A CA  1 
ATOM   10312 C C   . PRO   A 1 1403 ? 151.241 149.667 97.252  1.00 48.29  0  1367 PRO   A C   1 
ATOM   10313 O O   . PRO   A 1 1403 ? 152.324 150.269 97.241  1.00 47.49  0  1367 PRO   A O   1 
ATOM   10314 C CB  . PRO   A 1 1403 ? 149.592 149.667 95.334  1.00 46.35  0  1367 PRO   A CB  1 
ATOM   10315 C CG  . PRO   A 1 1403 ? 148.387 148.944 95.766  1.00 43.82  0  1367 PRO   A CG  1 
ATOM   10316 C CD  . PRO   A 1 1403 ? 148.791 147.517 95.891  1.00 44.60  0  1367 PRO   A CD  1 
ATOM   10317 N N   . ILE   A 1 1404 ? 150.465 149.621 98.335  1.00 49.51  0  1368 ILE   A N   1 
ATOM   10318 C CA  . ILE   A 1 1404 ? 150.897 150.283 99.556  1.00 46.87  0  1368 ILE   A CA  1 
ATOM   10319 C C   . ILE   A 1 1404 ? 152.123 149.595 100.134 1.00 46.15  0  1368 ILE   A C   1 
ATOM   10320 O O   . ILE   A 1 1404 ? 153.013 150.260 100.671 1.00 57.42  0  1368 ILE   A O   1 
ATOM   10321 C CB  . ILE   A 1 1404 ? 149.743 150.350 100.573 1.00 52.23  0  1368 ILE   A CB  1 
ATOM   10322 C CG1 . ILE   A 1 1404 ? 150.200 151.056 101.852 1.00 49.99  0  1368 ILE   A CG1 1 
ATOM   10323 C CG2 . ILE   A 1 1404 ? 149.206 148.964 100.866 1.00 50.86  0  1368 ILE   A CG2 1 
ATOM   10324 C CD1 . ILE   A 1 1404 ? 149.081 151.382 102.811 1.00 46.48  0  1368 ILE   A CD1 1 
ATOM   10325 N N   . ASN   A 1 1405 ? 152.208 148.267 100.036 1.00 39.03  0  1369 ASN   A N   1 
ATOM   10326 C CA  . ASN   A 1 1405 ? 153.400 147.585 100.524 1.00 40.83  0  1369 ASN   A CA  1 
ATOM   10327 C C   . ASN   A 1 1405 ? 154.631 148.009 99.742  1.00 47.54  0  1369 ASN   A C   1 
ATOM   10328 O O   . ASN   A 1 1405 ? 155.692 148.249 100.327 1.00 52.82  0  1369 ASN   A O   1 
ATOM   10329 C CB  . ASN   A 1 1405 ? 153.230 146.071 100.449 1.00 46.96  0  1369 ASN   A CB  1 
ATOM   10330 C CG  . ASN   A 1 1405 ? 154.270 145.332 101.264 1.00 44.21  0  1369 ASN   A CG  1 
ATOM   10331 O OD1 . ASN   A 1 1405 ? 154.162 145.230 102.483 1.00 44.67  0  1369 ASN   A OD1 1 
ATOM   10332 N ND2 . ASN   A 1 1405 ? 155.293 144.824 100.593 1.00 42.21  0  1369 ASN   A ND2 1 
ATOM   10333 N N   . ARG   A 1 1406 ? 154.513 148.111 98.416  1.00 52.68  0  1370 ARG   A N   1 
ATOM   10334 C CA  . ARG   A 1 1406 ? 155.664 148.527 97.622  1.00 54.05  0  1370 ARG   A CA  1 
ATOM   10335 C C   . ARG   A 1 1406 ? 156.064 149.963 97.943  1.00 51.38  0  1370 ARG   A C   1 
ATOM   10336 O O   . ARG   A 1 1406 ? 157.256 150.260 98.079  1.00 52.81  0  1370 ARG   A O   1 
ATOM   10337 C CB  . ARG   A 1 1406 ? 155.383 148.337 96.127  1.00 52.58  0  1370 ARG   A CB  1 
ATOM   10338 C CG  . ARG   A 1 1406 ? 154.758 149.517 95.402  1.00 49.53  0  1370 ARG   A CG  1 
ATOM   10339 C CD  . ARG   A 1 1406 ? 154.280 149.122 94.016  1.00 51.57  0  1370 ARG   A CD  1 
ATOM   10340 N NE  . ARG   A 1 1406 ? 153.477 147.906 94.041  1.00 54.01  0  1370 ARG   A NE  1 
ATOM   10341 C CZ  . ARG   A 1 1406 ? 152.556 147.597 93.139  1.00 54.32  0  1370 ARG   A CZ  1 
ATOM   10342 N NH1 . ARG   A 1 1406 ? 152.282 148.404 92.127  1.00 57.40  1  1370 ARG   A NH1 1 
ATOM   10343 N NH2 . ARG   A 1 1406 ? 151.892 146.451 93.255  1.00 50.78  0  1370 ARG   A NH2 1 
ATOM   10344 N N   . ILE   A 1 1407 ? 155.088 150.860 98.115  1.00 45.56  0  1371 ILE   A N   1 
ATOM   10345 C CA  . ILE   A 1 1407 ? 155.421 152.246 98.438  1.00 46.35  0  1371 ILE   A CA  1 
ATOM   10346 C C   . ILE   A 1 1407 ? 156.077 152.341 99.810  1.00 43.20  0  1371 ILE   A C   1 
ATOM   10347 O O   . ILE   A 1 1407 ? 157.079 153.045 99.987  1.00 48.39  0  1371 ILE   A O   1 
ATOM   10348 C CB  . ILE   A 1 1407 ? 154.172 153.140 98.336  1.00 45.88  0  1371 ILE   A CB  1 
ATOM   10349 C CG1 . ILE   A 1 1407 ? 153.791 153.349 96.870  1.00 47.41  0  1371 ILE   A CG1 1 
ATOM   10350 C CG2 . ILE   A 1 1407 ? 154.405 154.471 99.023  1.00 42.91  0  1371 ILE   A CG2 1 
ATOM   10351 C CD1 . ILE   A 1 1407 ? 152.487 154.080 96.674  1.00 47.64  0  1371 ILE   A CD1 1 
ATOM   10352 N N   . LEU   A 1 1408 ? 155.541 151.626 100.799 1.00 42.02  0  1372 LEU   A N   1 
ATOM   10353 C CA  . LEU   A 1 1408 ? 156.090 151.709 102.145 1.00 44.10  0  1372 LEU   A CA  1 
ATOM   10354 C C   . LEU   A 1 1408 ? 157.461 151.057 102.242 1.00 45.39  0  1372 LEU   A C   1 
ATOM   10355 O O   . LEU   A 1 1408 ? 158.318 151.546 102.984 1.00 52.66  0  1372 LEU   A O   1 
ATOM   10356 C CB  . LEU   A 1 1408 ? 155.125 151.081 103.149 1.00 44.22  0  1372 LEU   A CB  1 
ATOM   10357 C CG  . LEU   A 1 1408 ? 153.821 151.854 103.359 1.00 41.46  0  1372 LEU   A CG  1 
ATOM   10358 C CD1 . LEU   A 1 1408 ? 152.937 151.149 104.366 1.00 40.04  0  1372 LEU   A CD1 1 
ATOM   10359 C CD2 . LEU   A 1 1408 ? 154.098 153.282 103.791 1.00 41.75  0  1372 LEU   A CD2 1 
ATOM   10360 N N   . THR   A 1 1409 ? 157.698 149.963 101.516 1.00 48.73  0  1373 THR   A N   1 
ATOM   10361 C CA  . THR   A 1 1409 ? 159.022 149.353 101.536 1.00 53.38  0  1373 THR   A CA  1 
ATOM   10362 C C   . THR   A 1 1409 ? 160.022 150.104 100.667 1.00 54.00  0  1373 THR   A C   1 
ATOM   10363 O O   . THR   A 1 1409 ? 161.229 149.924 100.844 1.00 55.02  0  1373 THR   A O   1 
ATOM   10364 C CB  . THR   A 1 1409 ? 158.949 147.889 101.097 1.00 47.93  0  1373 THR   A CB  1 
ATOM   10365 O OG1 . THR   A 1 1409 ? 160.164 147.223 101.457 1.00 47.07  0  1373 THR   A OG1 1 
ATOM   10366 C CG2 . THR   A 1 1409 ? 158.761 147.789 99.595  1.00 49.03  0  1373 THR   A CG2 1 
ATOM   10367 N N   . GLU   A 1 1410 ? 159.554 150.931 99.729  1.00 56.12  0  1374 GLU   A N   1 
ATOM   10368 C CA  . GLU   A 1 1410 ? 160.456 151.853 99.049  1.00 56.11  0  1374 GLU   A CA  1 
ATOM   10369 C C   . GLU   A 1 1410 ? 160.843 153.003 99.968  1.00 56.96  0  1374 GLU   A C   1 
ATOM   10370 O O   . GLU   A 1 1410 ? 162.011 153.400 100.032 1.00 57.62  0  1374 GLU   A O   1 
ATOM   10371 C CB  . GLU   A 1 1410 ? 159.799 152.382 97.774  1.00 53.66  0  1374 GLU   A CB  1 
ATOM   10372 C CG  . GLU   A 1 1410 ? 160.540 153.535 97.109  1.00 57.84  0  1374 GLU   A CG  1 
ATOM   10373 C CD  . GLU   A 1 1410 ? 161.980 153.197 96.766  1.00 62.80  0  1374 GLU   A CD  1 
ATOM   10374 O OE1 . GLU   A 1 1410 ? 162.200 152.410 95.822  1.00 61.44  0  1374 GLU   A OE1 1 
ATOM   10375 O OE2 . GLU   A 1 1410 ? 162.893 153.727 97.432  1.00 58.06  -1 1374 GLU   A OE2 1 
ATOM   10376 N N   . LYS   A 1 1411 ? 159.868 153.543 100.701 1.00 54.00  0  1375 LYS   A N   1 
ATOM   10377 C CA  . LYS   A 1 1411 ? 160.131 154.709 101.537 1.00 51.26  0  1375 LYS   A CA  1 
ATOM   10378 C C   . LYS   A 1 1411 ? 160.934 154.342 102.780 1.00 50.35  0  1375 LYS   A C   1 
ATOM   10379 O O   . LYS   A 1 1411 ? 161.809 155.105 103.202 1.00 57.49  0  1375 LYS   A O   1 
ATOM   10380 C CB  . LYS   A 1 1411 ? 158.815 155.381 101.923 1.00 52.47  0  1375 LYS   A CB  1 
ATOM   10381 C CG  . LYS   A 1 1411 ? 158.968 156.576 102.842 1.00 50.65  0  1375 LYS   A CG  1 
ATOM   10382 C CD  . LYS   A 1 1411 ? 157.663 157.343 102.959 1.00 54.94  0  1375 LYS   A CD  1 
ATOM   10383 C CE  . LYS   A 1 1411 ? 157.648 158.225 104.194 1.00 53.92  0  1375 LYS   A CE  1 
ATOM   10384 N NZ  . LYS   A 1 1411 ? 158.672 159.298 104.121 1.00 60.62  1  1375 LYS   A NZ  1 
ATOM   10385 N N   . TYR   A 1 1412 ? 160.658 153.186 103.384 1.00 44.41  0  1376 TYR   A N   1 
ATOM   10386 C CA  . TYR   A 1 1412 ? 161.322 152.809 104.622 1.00 49.26  0  1376 TYR   A CA  1 
ATOM   10387 C C   . TYR   A 1 1412 ? 162.348 151.701 104.450 1.00 46.58  0  1376 TYR   A C   1 
ATOM   10388 O O   . TYR   A 1 1412 ? 163.162 151.494 105.355 1.00 51.48  0  1376 TYR   A O   1 
ATOM   10389 C CB  . TYR   A 1 1412 ? 160.302 152.373 105.687 1.00 54.11  0  1376 TYR   A CB  1 
ATOM   10390 C CG  . TYR   A 1 1412 ? 159.374 153.469 106.161 1.00 48.49  0  1376 TYR   A CG  1 
ATOM   10391 C CD1 . TYR   A 1 1412 ? 158.517 154.114 105.283 1.00 48.44  0  1376 TYR   A CD1 1 
ATOM   10392 C CD2 . TYR   A 1 1412 ? 159.391 153.892 107.480 1.00 44.81  0  1376 TYR   A CD2 1 
ATOM   10393 C CE1 . TYR   A 1 1412 ? 157.677 155.114 105.712 1.00 45.32  0  1376 TYR   A CE1 1 
ATOM   10394 C CE2 . TYR   A 1 1412 ? 158.558 154.899 107.915 1.00 52.18  0  1376 TYR   A CE2 1 
ATOM   10395 C CZ  . TYR   A 1 1412 ? 157.704 155.507 107.025 1.00 52.59  0  1376 TYR   A CZ  1 
ATOM   10396 O OH  . TYR   A 1 1412 ? 156.869 156.513 107.448 1.00 57.86  0  1376 TYR   A OH  1 
ATOM   10397 N N   . GLY   A 1 1413 ? 162.327 150.981 103.333 1.00 52.73  0  1377 GLY   A N   1 
ATOM   10398 C CA  . GLY   A 1 1413 ? 163.348 149.991 103.053 1.00 64.93  0  1377 GLY   A CA  1 
ATOM   10399 C C   . GLY   A 1 1413 ? 163.412 148.836 104.029 1.00 66.08  0  1377 GLY   A C   1 
ATOM   10400 O O   . GLY   A 1 1413 ? 164.422 148.655 104.713 1.00 64.81  0  1377 GLY   A O   1 
ATOM   10401 N N   . ASP   A 1 1414 ? 162.342 148.043 104.088 1.00 62.77  0  1378 ASP   A N   1 
ATOM   10402 C CA  . ASP   A 1 1414 ? 162.281 146.851 104.933 1.00 62.75  0  1378 ASP   A CA  1 
ATOM   10403 C C   . ASP   A 1 1414 ? 162.578 147.259 106.377 1.00 64.70  0  1378 ASP   A C   1 
ATOM   10404 O O   . ASP   A 1 1414 ? 163.658 147.013 106.915 1.00 61.93  0  1378 ASP   A O   1 
ATOM   10405 C CB  . ASP   A 1 1414 ? 163.233 145.761 104.407 1.00 62.60  0  1378 ASP   A CB  1 
ATOM   10406 C CG  . ASP   A 1 1414 ? 163.396 144.545 105.346 1.00 65.56  0  1378 ASP   A CG  1 
ATOM   10407 O OD1 . ASP   A 1 1414 ? 163.699 143.462 104.802 1.00 63.92  0  1378 ASP   A OD1 1 
ATOM   10408 O OD2 . ASP   A 1 1414 ? 163.184 144.603 106.573 1.00 67.35  -1 1378 ASP   A OD2 1 
ATOM   10409 N N   . GLU   A 1 1415 ? 161.655 148.015 106.962 1.00 54.22  0  1379 GLU   A N   1 
ATOM   10410 C CA  . GLU   A 1 1415 ? 161.742 148.415 108.357 1.00 49.16  0  1379 GLU   A CA  1 
ATOM   10411 C C   . GLU   A 1 1415 ? 160.336 148.573 108.907 1.00 48.87  0  1379 GLU   A C   1 
ATOM   10412 O O   . GLU   A 1 1415 ? 159.486 149.202 108.270 1.00 54.11  0  1379 GLU   A O   1 
ATOM   10413 C CB  . GLU   A 1 1415 ? 162.529 149.715 108.518 1.00 50.95  0  1379 GLU   A CB  1 
ATOM   10414 C CG  . GLU   A 1 1415 ? 162.929 149.989 109.948 1.00 53.68  0  1379 GLU   A CG  1 
ATOM   10415 C CD  . GLU   A 1 1415 ? 163.493 148.761 110.630 1.00 56.38  0  1379 GLU   A CD  1 
ATOM   10416 O OE1 . GLU   A 1 1415 ? 164.619 148.350 110.282 1.00 56.79  0  1379 GLU   A OE1 1 
ATOM   10417 O OE2 . GLU   A 1 1415 ? 162.804 148.201 111.508 1.00 55.69  -1 1379 GLU   A OE2 1 
ATOM   10418 N N   . ASP   A 1 1416 ? 160.099 148.011 110.089 1.00 41.87  0  1380 ASP   A N   1 
ATOM   10419 C CA  . ASP   A 1 1416 ? 158.760 148.002 110.661 1.00 40.70  0  1380 ASP   A CA  1 
ATOM   10420 C C   . ASP   A 1 1416 ? 158.280 149.416 110.945 1.00 42.72  0  1380 ASP   A C   1 
ATOM   10421 O O   . ASP   A 1 1416 ? 159.031 150.250 111.455 1.00 52.44  0  1380 ASP   A O   1 
ATOM   10422 C CB  . ASP   A 1 1416 ? 158.753 147.185 111.946 1.00 37.47  0  1380 ASP   A CB  1 
ATOM   10423 C CG  . ASP   A 1 1416 ? 159.040 145.727 111.704 1.00 48.38  0  1380 ASP   A CG  1 
ATOM   10424 O OD1 . ASP   A 1 1416 ? 158.510 145.172 110.721 1.00 52.36  0  1380 ASP   A OD1 1 
ATOM   10425 O OD2 . ASP   A 1 1416 ? 159.811 145.139 112.486 1.00 49.50  -1 1380 ASP   A OD2 1 
ATOM   10426 N N   . ILE   A 1 1417 ? 157.023 149.678 110.620 1.00 30.82  0  1381 ILE   A N   1 
ATOM   10427 C CA  . ILE   A 1 1417 ? 156.409 150.954 110.890 1.00 32.51  0  1381 ILE   A CA  1 
ATOM   10428 C C   . ILE   A 1 1417 ? 155.406 150.778 112.023 1.00 42.32  0  1381 ILE   A C   1 
ATOM   10429 O O   . ILE   A 1 1417 ? 155.182 149.677 112.519 1.00 49.66  0  1381 ILE   A O   1 
ATOM   10430 C CB  . ILE   A 1 1417 ? 155.759 151.553 109.627 1.00 29.41  0  1381 ILE   A CB  1 
ATOM   10431 C CG1 . ILE   A 1 1417 ? 154.807 150.555 108.990 1.00 38.01  0  1381 ILE   A CG1 1 
ATOM   10432 C CG2 . ILE   A 1 1417 ? 156.817 151.905 108.620 1.00 32.19  0  1381 ILE   A CG2 1 
ATOM   10433 C CD1 . ILE   A 1 1417 ? 154.287 151.018 107.659 1.00 39.47  0  1381 ILE   A CD1 1 
ATOM   10434 N N   . ASP   A 1 1418 ? 154.809 151.884 112.463 1.00 38.49  0  1382 ASP   A N   1 
ATOM   10435 C CA  . ASP   A 1 1418 ? 153.944 151.874 113.634 1.00 35.43  0  1382 ASP   A CA  1 
ATOM   10436 C C   . ASP   A 1 1418 ? 152.475 151.640 113.312 1.00 36.46  0  1382 ASP   A C   1 
ATOM   10437 O O   . ASP   A 1 1418 ? 151.673 151.500 114.239 1.00 35.55  0  1382 ASP   A O   1 
ATOM   10438 C CB  . ASP   A 1 1418 ? 154.107 153.181 114.417 1.00 35.56  0  1382 ASP   A CB  1 
ATOM   10439 C CG  . ASP   A 1 1418 ? 153.811 154.404 113.580 1.00 42.74  0  1382 ASP   A CG  1 
ATOM   10440 O OD1 . ASP   A 1 1418 ? 153.577 154.257 112.364 1.00 43.96  0  1382 ASP   A OD1 1 
ATOM   10441 O OD2 . ASP   A 1 1418 ? 153.819 155.520 114.141 1.00 40.29  -1 1382 ASP   A OD2 1 
ATOM   10442 N N   . ILE   A 1 1419 ? 152.100 151.575 112.039 1.00 29.65  0  1383 ILE   A N   1 
ATOM   10443 C CA  . ILE   A 1 1419 ? 150.711 151.349 111.658 1.00 27.93  0  1383 ILE   A CA  1 
ATOM   10444 C C   . ILE   A 1 1419 ? 150.475 149.849 111.542 1.00 27.03  0  1383 ILE   A C   1 
ATOM   10445 O O   . ILE   A 1 1419 ? 151.307 149.117 110.996 1.00 23.90  0  1383 ILE   A O   1 
ATOM   10446 C CB  . ILE   A 1 1419 ? 150.368 152.085 110.352 1.00 20.94  0  1383 ILE   A CB  1 
ATOM   10447 C CG1 . ILE   A 1 1419 ? 148.875 151.999 110.065 1.00 18.04  0  1383 ILE   A CG1 1 
ATOM   10448 C CG2 . ILE   A 1 1419 ? 151.139 151.527 109.188 1.00 34.94  0  1383 ILE   A CG2 1 
ATOM   10449 C CD1 . ILE   A 1 1419 ? 148.383 153.061 109.121 1.00 24.16  0  1383 ILE   A CD1 1 
ATOM   10450 N N   . VAL   A 1 1420 ? 149.353 149.384 112.084 1.00 35.42  0  1384 VAL   A N   1 
ATOM   10451 C CA  . VAL   A 1 1420 ? 149.078 147.954 112.167 1.00 35.32  0  1384 VAL   A CA  1 
ATOM   10452 C C   . VAL   A 1 1420 ? 148.419 147.498 110.872 1.00 37.44  0  1384 VAL   A C   1 
ATOM   10453 O O   . VAL   A 1 1420 ? 147.365 148.011 110.486 1.00 45.82  0  1384 VAL   A O   1 
ATOM   10454 C CB  . VAL   A 1 1420 ? 148.199 147.630 113.381 1.00 29.71  0  1384 VAL   A CB  1 
ATOM   10455 C CG1 . VAL   A 1 1420 ? 148.199 146.141 113.647 1.00 28.69  0  1384 VAL   A CG1 1 
ATOM   10456 C CG2 . VAL   A 1 1420 ? 148.689 148.381 114.599 1.00 34.55  0  1384 VAL   A CG2 1 
ATOM   10457 N N   . PHE   A 1 1421 ? 149.039 146.524 110.205 1.00 24.75  0  1385 PHE   A N   1 
ATOM   10458 C CA  . PHE   A 1 1421 ? 148.524 146.016 108.937 1.00 31.73  0  1385 PHE   A CA  1 
ATOM   10459 C C   . PHE   A 1 1421 ? 147.144 145.387 109.110 1.00 38.03  0  1385 PHE   A C   1 
ATOM   10460 O O   . PHE   A 1 1421 ? 146.207 145.673 108.346 1.00 36.45  0  1385 PHE   A O   1 
ATOM   10461 C CB  . PHE   A 1 1421 ? 149.525 145.005 108.378 1.00 37.46  0  1385 PHE   A CB  1 
ATOM   10462 C CG  . PHE   A 1 1421 ? 149.098 144.351 107.103 1.00 39.22  0  1385 PHE   A CG  1 
ATOM   10463 C CD1 . PHE   A 1 1421 ? 148.957 145.086 105.946 1.00 39.17  0  1385 PHE   A CD1 1 
ATOM   10464 C CD2 . PHE   A 1 1421 ? 148.859 142.992 107.060 1.00 35.41  0  1385 PHE   A CD2 1 
ATOM   10465 C CE1 . PHE   A 1 1421 ? 148.574 144.485 104.774 1.00 38.48  0  1385 PHE   A CE1 1 
ATOM   10466 C CE2 . PHE   A 1 1421 ? 148.475 142.385 105.889 1.00 38.84  0  1385 PHE   A CE2 1 
ATOM   10467 C CZ  . PHE   A 1 1421 ? 148.332 143.134 104.743 1.00 39.99  0  1385 PHE   A CZ  1 
ATOM   10468 N N   . GLN   A 1 1422 ? 146.998 144.539 110.131 1.00 37.51  0  1386 GLN   A N   1 
ATOM   10469 C CA  . GLN   A 1 1422 ? 145.731 143.860 110.372 1.00 28.47  0  1386 GLN   A CA  1 
ATOM   10470 C C   . GLN   A 1 1422 ? 144.609 144.862 110.583 1.00 25.69  0  1386 GLN   A C   1 
ATOM   10471 O O   . GLN   A 1 1422 ? 143.491 144.675 110.093 1.00 38.18  0  1386 GLN   A O   1 
ATOM   10472 C CB  . GLN   A 1 1422 ? 145.857 142.936 111.582 1.00 25.33  0  1386 GLN   A CB  1 
ATOM   10473 C CG  . GLN   A 1 1422 ? 146.892 141.847 111.428 1.00 24.28  0  1386 GLN   A CG  1 
ATOM   10474 C CD  . GLN   A 1 1422 ? 148.257 142.267 111.910 1.00 34.85  0  1386 GLN   A CD  1 
ATOM   10475 O OE1 . GLN   A 1 1422 ? 148.845 143.216 111.395 1.00 42.15  0  1386 GLN   A OE1 1 
ATOM   10476 N NE2 . GLN   A 1 1422 ? 148.774 141.560 112.905 1.00 35.76  0  1386 GLN   A NE2 1 
ATOM   10477 N N   . ASN   A 1 1423 ? 144.889 145.935 111.321 1.00 27.07  0  1387 ASN   A N   1 
ATOM   10478 C CA  . ASN   A 1 1423 ? 143.872 146.952 111.541 1.00 35.08  0  1387 ASN   A CA  1 
ATOM   10479 C C   . ASN   A 1 1423 ? 143.519 147.679 110.252 1.00 33.65  0  1387 ASN   A C   1 
ATOM   10480 O O   . ASN   A 1 1423 ? 142.368 148.083 110.076 1.00 26.87  0  1387 ASN   A O   1 
ATOM   10481 C CB  . ASN   A 1 1423 ? 144.334 147.936 112.612 1.00 36.22  0  1387 ASN   A CB  1 
ATOM   10482 C CG  . ASN   A 1 1423 ? 143.936 147.499 114.007 1.00 33.14  0  1387 ASN   A CG  1 
ATOM   10483 O OD1 . ASN   A 1 1423 ? 143.071 146.644 114.176 1.00 30.33  0  1387 ASN   A OD1 1 
ATOM   10484 N ND2 . ASN   A 1 1423 ? 144.567 148.085 115.014 1.00 30.55  0  1387 ASN   A ND2 1 
ATOM   10485 N N   . CYS   A 1 1424 ? 144.476 147.844 109.337 1.00 29.02  0  1388 CYS   A N   1 
ATOM   10486 C CA  . CYS   A 1 1424 ? 144.157 148.435 108.039 1.00 31.95  0  1388 CYS   A CA  1 
ATOM   10487 C C   . CYS   A 1 1424 ? 143.179 147.556 107.269 1.00 42.37  0  1388 CYS   A C   1 
ATOM   10488 O O   . CYS   A 1 1424 ? 142.182 148.041 106.712 1.00 47.65  0  1388 CYS   A O   1 
ATOM   10489 C CB  . CYS   A 1 1424 ? 145.436 148.648 107.229 1.00 27.64  0  1388 CYS   A CB  1 
ATOM   10490 S SG  . CYS   A 1 1424 ? 146.692 149.653 108.034 1.00 29.46  0  1388 CYS   A SG  1 
ATOM   10491 N N   . ILE   A 1 1425 ? 143.442 146.247 107.247 1.00 39.36  0  1389 ILE   A N   1 
ATOM   10492 C CA  . ILE   A 1 1425 ? 142.549 145.320 106.552 1.00 29.03  0  1389 ILE   A CA  1 
ATOM   10493 C C   . ILE   A 1 1425 ? 141.166 145.326 107.195 1.00 34.87  0  1389 ILE   A C   1 
ATOM   10494 O O   . ILE   A 1 1425 ? 140.134 145.378 106.508 1.00 40.14  0  1389 ILE   A O   1 
ATOM   10495 C CB  . ILE   A 1 1425 ? 143.154 143.907 106.543 1.00 28.33  0  1389 ILE   A CB  1 
ATOM   10496 C CG1 . ILE   A 1 1425 ? 144.433 143.889 105.712 1.00 38.15  0  1389 ILE   A CG1 1 
ATOM   10497 C CG2 . ILE   A 1 1425 ? 142.150 142.911 106.016 1.00 30.81  0  1389 ILE   A CG2 1 
ATOM   10498 C CD1 . ILE   A 1 1425 ? 144.277 144.545 104.376 1.00 37.18  0  1389 ILE   A CD1 1 
ATOM   10499 N N   . SER   A 1 1426 ? 141.131 145.264 108.528 1.00 29.49  0  1390 SER   A N   1 
ATOM   10500 C CA  . SER   A 1 1426 ? 139.864 145.239 109.246 1.00 16.30  0  1390 SER   A CA  1 
ATOM   10501 C C   . SER   A 1 1426 ? 139.074 146.515 109.011 1.00 17.70  0  1390 SER   A C   1 
ATOM   10502 O O   . SER   A 1 1426 ? 137.853 146.473 108.831 1.00 40.09  0  1390 SER   A O   1 
ATOM   10503 C CB  . SER   A 1 1426 ? 140.119 145.033 110.734 1.00 21.44  0  1390 SER   A CB  1 
ATOM   10504 O OG  . SER   A 1 1426 ? 140.724 143.777 110.971 1.00 21.98  0  1390 SER   A OG  1 
ATOM   10505 N N   . PHE   A 1 1427 ? 139.753 147.662 109.014 1.00 8.91   0  1391 PHE   A N   1 
ATOM   10506 C CA  . PHE   A 1 1427 ? 139.083 148.925 108.741 1.00 23.05  0  1391 PHE   A CA  1 
ATOM   10507 C C   . PHE   A 1 1427 ? 138.488 148.932 107.342 1.00 27.59  0  1391 PHE   A C   1 
ATOM   10508 O O   . PHE   A 1 1427 ? 137.359 149.395 107.146 1.00 34.14  0  1391 PHE   A O   1 
ATOM   10509 C CB  . PHE   A 1 1427 ? 140.068 150.078 108.923 1.00 23.62  0  1391 PHE   A CB  1 
ATOM   10510 C CG  . PHE   A 1 1427 ? 139.541 151.411 108.482 1.00 22.51  0  1391 PHE   A CG  1 
ATOM   10511 C CD1 . PHE   A 1 1427 ? 138.472 151.992 109.126 1.00 21.00  0  1391 PHE   A CD1 1 
ATOM   10512 C CD2 . PHE   A 1 1427 ? 140.136 152.094 107.441 1.00 27.26  0  1391 PHE   A CD2 1 
ATOM   10513 C CE1 . PHE   A 1 1427 ? 137.994 153.219 108.730 1.00 27.92  0  1391 PHE   A CE1 1 
ATOM   10514 C CE2 . PHE   A 1 1427 ? 139.664 153.324 107.045 1.00 19.02  0  1391 PHE   A CE2 1 
ATOM   10515 C CZ  . PHE   A 1 1427 ? 138.590 153.886 107.689 1.00 21.04  0  1391 PHE   A CZ  1 
ATOM   10516 N N   . GLY   A 1 1428 ? 139.223 148.412 106.358 1.00 26.98  0  1392 GLY   A N   1 
ATOM   10517 C CA  . GLY   A 1 1428 ? 138.677 148.352 105.011 1.00 23.35  0  1392 GLY   A CA  1 
ATOM   10518 C C   . GLY   A 1 1428 ? 137.418 147.510 104.929 1.00 28.23  0  1392 GLY   A C   1 
ATOM   10519 O O   . GLY   A 1 1428 ? 136.397 147.939 104.376 1.00 38.10  0  1392 GLY   A O   1 
ATOM   10520 N N   . LEU   A 1 1429 ? 137.464 146.306 105.505 1.00 25.46  0  1393 LEU   A N   1 
ATOM   10521 C CA  . LEU   A 1 1429 ? 136.295 145.427 105.466 1.00 20.39  0  1393 LEU   A CA  1 
ATOM   10522 C C   . LEU   A 1 1429 ? 135.103 146.066 106.171 1.00 26.34  0  1393 LEU   A C   1 
ATOM   10523 O O   . LEU   A 1 1429 ? 133.986 146.117 105.629 1.00 37.36  0  1393 LEU   A O   1 
ATOM   10524 C CB  . LEU   A 1 1429 ? 136.629 144.079 106.107 1.00 21.87  0  1393 LEU   A CB  1 
ATOM   10525 C CG  . LEU   A 1 1429 ? 137.800 143.273 105.544 1.00 27.42  0  1393 LEU   A CG  1 
ATOM   10526 C CD1 . LEU   A 1 1429 ? 138.014 142.010 106.354 1.00 20.64  0  1393 LEU   A CD1 1 
ATOM   10527 C CD2 . LEU   A 1 1429 ? 137.582 142.936 104.084 1.00 28.21  0  1393 LEU   A CD2 1 
ATOM   10528 N N   . SER   A 1 1430 ? 135.329 146.578 107.382 1.00 25.95  0  1394 SER   A N   1 
ATOM   10529 C CA  . SER   A 1 1430 ? 134.236 147.144 108.155 1.00 22.89  0  1394 SER   A CA  1 
ATOM   10530 C C   . SER   A 1 1430 ? 133.647 148.368 107.483 1.00 23.96  0  1394 SER   A C   1 
ATOM   10531 O O   . SER   A 1 1430 ? 132.433 148.577 107.548 1.00 36.45  0  1394 SER   A O   1 
ATOM   10532 C CB  . SER   A 1 1430 ? 134.706 147.495 109.557 1.00 21.38  0  1394 SER   A CB  1 
ATOM   10533 O OG  . SER   A 1 1430 ? 135.063 146.329 110.271 1.00 22.94  0  1394 SER   A OG  1 
ATOM   10534 N N   . LEU   A 1 1431 ? 134.469 149.198 106.840 1.00 30.20  0  1395 LEU   A N   1 
ATOM   10535 C CA  . LEU   A 1 1431 ? 133.878 150.362 106.204 1.00 39.59  0  1395 LEU   A CA  1 
ATOM   10536 C C   . LEU   A 1 1431 ? 133.151 149.981 104.928 1.00 28.17  0  1395 LEU   A C   1 
ATOM   10537 O O   . LEU   A 1 1431 ? 132.216 150.680 104.541 1.00 32.78  0  1395 LEU   A O   1 
ATOM   10538 C CB  . LEU   A 1 1431 ? 134.925 151.440 105.910 1.00 26.80  0  1395 LEU   A CB  1 
ATOM   10539 C CG  . LEU   A 1 1431 ? 135.969 151.299 104.807 1.00 35.51  0  1395 LEU   A CG  1 
ATOM   10540 C CD1 . LEU   A 1 1431 ? 135.374 151.727 103.474 1.00 38.19  0  1395 LEU   A CD1 1 
ATOM   10541 C CD2 . LEU   A 1 1431 ? 137.181 152.110 105.112 1.00 39.23  0  1395 LEU   A CD2 1 
ATOM   10542 N N   . MET   A 1 1432 ? 133.556 148.899 104.258 1.00 23.87  0  1396 MET   A N   1 
ATOM   10543 C CA  . MET   A 1 1432 ? 132.723 148.393 103.171 1.00 35.27  0  1396 MET   A CA  1 
ATOM   10544 C C   . MET   A 1 1432 ? 131.342 148.017 103.689 1.00 32.62  0  1396 MET   A C   1 
ATOM   10545 O O   . MET   A 1 1432 ? 130.316 148.392 103.100 1.00 35.89  0  1396 MET   A O   1 
ATOM   10546 C CB  . MET   A 1 1432 ? 133.390 147.194 102.499 1.00 38.84  0  1396 MET   A CB  1 
ATOM   10547 C CG  . MET   A 1 1432 ? 134.434 147.572 101.468 1.00 44.20  0  1396 MET   A CG  1 
ATOM   10548 S SD  . MET   A 1 1432 ? 133.750 147.694 99.806  1.00 53.06  0  1396 MET   A SD  1 
ATOM   10549 C CE  . MET   A 1 1432 ? 133.528 145.972 99.404  1.00 36.98  0  1396 MET   A CE  1 
ATOM   10550 N N   . SER   A 1 1433 ? 131.300 147.315 104.823 1.00 31.50  0  1397 SER   A N   1 
ATOM   10551 C CA  . SER   A 1 1433 ? 130.017 146.980 105.439 1.00 30.53  0  1397 SER   A CA  1 
ATOM   10552 C C   . SER   A 1 1433 ? 129.219 148.236 105.786 1.00 29.42  0  1397 SER   A C   1 
ATOM   10553 O O   . SER   A 1 1433 ? 128.011 148.314 105.530 1.00 25.20  0  1397 SER   A O   1 
ATOM   10554 C CB  . SER   A 1 1433 ? 130.250 146.129 106.685 1.00 24.08  0  1397 SER   A CB  1 
ATOM   10555 O OG  . SER   A 1 1433 ? 129.097 146.100 107.501 1.00 35.82  0  1397 SER   A OG  1 
ATOM   10556 N N   . VAL   A 1 1434 ? 129.885 149.239 106.361 1.00 28.36  0  1398 VAL   A N   1 
ATOM   10557 C CA  . VAL   A 1 1434 ? 129.195 150.448 106.808 1.00 22.61  0  1398 VAL   A CA  1 
ATOM   10558 C C   . VAL   A 1 1434 ? 128.689 151.272 105.626 1.00 24.59  0  1398 VAL   A C   1 
ATOM   10559 O O   . VAL   A 1 1434 ? 127.606 151.867 105.696 1.00 28.50  0  1398 VAL   A O   1 
ATOM   10560 C CB  . VAL   A 1 1434 ? 130.115 151.273 107.727 1.00 12.83  0  1398 VAL   A CB  1 
ATOM   10561 C CG1 . VAL   A 1 1434 ? 129.504 152.624 108.018 1.00 24.09  0  1398 VAL   A CG1 1 
ATOM   10562 C CG2 . VAL   A 1 1434 ? 130.367 150.529 109.021 1.00 13.37  0  1398 VAL   A CG2 1 
ATOM   10563 N N   . VAL   A 1 1435 ? 129.451 151.340 104.534 1.00 34.57  0  1399 VAL   A N   1 
ATOM   10564 C CA  . VAL   A 1 1435 ? 128.973 152.048 103.352 1.00 32.61  0  1399 VAL   A CA  1 
ATOM   10565 C C   . VAL   A 1 1435 ? 127.778 151.324 102.752 1.00 33.40  0  1399 VAL   A C   1 
ATOM   10566 O O   . VAL   A 1 1435 ? 126.841 151.956 102.252 1.00 29.23  0  1399 VAL   A O   1 
ATOM   10567 C CB  . VAL   A 1 1435 ? 130.104 152.228 102.323 1.00 31.21  0  1399 VAL   A CB  1 
ATOM   10568 C CG1 . VAL   A 1 1435 ? 129.571 152.897 101.076 1.00 29.69  0  1399 VAL   A CG1 1 
ATOM   10569 C CG2 . VAL   A 1 1435 ? 131.216 153.066 102.909 1.00 36.65  0  1399 VAL   A CG2 1 
ATOM   10570 N N   . GLU   A 1 1436 ? 127.778 149.989 102.804 1.00 37.61  0  1400 GLU   A N   1 
ATOM   10571 C CA  . GLU   A 1 1436 ? 126.582 149.259 102.396 1.00 28.58  0  1400 GLU   A CA  1 
ATOM   10572 C C   . GLU   A 1 1436 ? 125.391 149.637 103.270 1.00 36.40  0  1400 GLU   A C   1 
ATOM   10573 O O   . GLU   A 1 1436 ? 124.281 149.848 102.769 1.00 44.26  0  1400 GLU   A O   1 
ATOM   10574 C CB  . GLU   A 1 1436 ? 126.827 147.755 102.463 1.00 31.51  0  1400 GLU   A CB  1 
ATOM   10575 C CG  . GLU   A 1 1436 ? 125.546 146.948 102.470 1.00 41.25  0  1400 GLU   A CG  1 
ATOM   10576 C CD  . GLU   A 1 1436 ? 125.780 145.487 102.753 1.00 44.67  0  1400 GLU   A CD  1 
ATOM   10577 O OE1 . GLU   A 1 1436 ? 126.912 145.013 102.531 1.00 42.05  0  1400 GLU   A OE1 1 
ATOM   10578 O OE2 . GLU   A 1 1436 ? 124.837 144.809 103.210 1.00 39.92  -1 1400 GLU   A OE2 1 
ATOM   10579 N N   . GLN   A 1 1437 ? 125.610 149.729 104.584 1.00 37.47  0  1401 GLN   A N   1 
ATOM   10580 C CA  . GLN   A 1 1437 ? 124.530 150.076 105.506 1.00 24.30  0  1401 GLN   A CA  1 
ATOM   10581 C C   . GLN   A 1 1437 ? 123.953 151.450 105.197 1.00 24.73  0  1401 GLN   A C   1 
ATOM   10582 O O   . GLN   A 1 1437 ? 122.733 151.624 105.122 1.00 25.88  0  1401 GLN   A O   1 
ATOM   10583 C CB  . GLN   A 1 1437 ? 125.036 150.045 106.944 1.00 18.01  0  1401 GLN   A CB  1 
ATOM   10584 C CG  . GLN   A 1 1437 ? 125.135 148.674 107.552 1.00 29.75  0  1401 GLN   A CG  1 
ATOM   10585 C CD  . GLN   A 1 1437 ? 125.709 148.719 108.944 1.00 30.16  0  1401 GLN   A CD  1 
ATOM   10586 O OE1 . GLN   A 1 1437 ? 125.471 149.664 109.690 1.00 38.62  0  1401 GLN   A OE1 1 
ATOM   10587 N NE2 . GLN   A 1 1437 ? 126.471 147.697 109.306 1.00 22.99  0  1401 GLN   A NE2 1 
ATOM   10588 N N   . PHE   A 1 1438 ? 124.819 152.442 105.017 1.00 30.02  0  1402 PHE   A N   1 
ATOM   10589 C CA  . PHE   A 1 1438 ? 124.370 153.820 104.869 1.00 29.94  0  1402 PHE   A CA  1 
ATOM   10590 C C   . PHE   A 1 1438 ? 124.024 154.190 103.435 1.00 34.95  0  1402 PHE   A C   1 
ATOM   10591 O O   . PHE   A 1 1438 ? 123.502 155.286 103.209 1.00 37.40  0  1402 PHE   A O   1 
ATOM   10592 C CB  . PHE   A 1 1438 ? 125.439 154.781 105.392 1.00 30.46  0  1402 PHE   A CB  1 
ATOM   10593 C CG  . PHE   A 1 1438 ? 125.387 154.993 106.874 1.00 36.28  0  1402 PHE   A CG  1 
ATOM   10594 C CD1 . PHE   A 1 1438 ? 124.508 155.904 107.427 1.00 36.22  0  1402 PHE   A CD1 1 
ATOM   10595 C CD2 . PHE   A 1 1438 ? 126.211 154.273 107.717 1.00 36.21  0  1402 PHE   A CD2 1 
ATOM   10596 C CE1 . PHE   A 1 1438 ? 124.458 156.096 108.789 1.00 31.60  0  1402 PHE   A CE1 1 
ATOM   10597 C CE2 . PHE   A 1 1438 ? 126.163 154.460 109.078 1.00 29.36  0  1402 PHE   A CE2 1 
ATOM   10598 C CZ  . PHE   A 1 1438 ? 125.285 155.373 109.614 1.00 33.93  0  1402 PHE   A CZ  1 
ATOM   10599 N N   . THR   A 1 1439 ? 124.291 153.313 102.467 1.00 35.67  0  1403 THR   A N   1 
ATOM   10600 C CA  . THR   A 1 1439 ? 124.083 153.628 101.061 1.00 31.37  0  1403 THR   A CA  1 
ATOM   10601 C C   . THR   A 1 1439 ? 123.041 152.754 100.386 1.00 36.39  0  1403 THR   A C   1 
ATOM   10602 O O   . THR   A 1 1439 ? 122.479 153.165 99.370  1.00 40.63  0  1403 THR   A O   1 
ATOM   10603 C CB  . THR   A 1 1439 ? 125.404 153.496 100.293 1.00 31.73  0  1403 THR   A CB  1 
ATOM   10604 O OG1 . THR   A 1 1439 ? 126.475 153.985 101.106 1.00 34.29  0  1403 THR   A OG1 1 
ATOM   10605 C CG2 . THR   A 1 1439 ? 125.365 154.305 99.011  1.00 38.75  0  1403 THR   A CG2 1 
ATOM   10606 N N   . ASN   A 1 1440 ? 122.774 151.566 100.927 1.00 38.03  0  1404 ASN   A N   1 
ATOM   10607 C CA  . ASN   A 1 1440 ? 121.898 150.525 100.392 1.00 36.05  0  1404 ASN   A CA  1 
ATOM   10608 C C   . ASN   A 1 1440 ? 122.536 149.821 99.197  1.00 43.85  0  1404 ASN   A C   1 
ATOM   10609 O O   . ASN   A 1 1440 ? 121.917 148.912 98.637  1.00 54.82  0  1404 ASN   A O   1 
ATOM   10610 C CB  . ASN   A 1 1440 ? 120.509 151.051 99.990  1.00 31.08  0  1404 ASN   A CB  1 
ATOM   10611 C CG  . ASN   A 1 1440 ? 119.466 149.956 99.923  1.00 40.88  0  1404 ASN   A CG  1 
ATOM   10612 O OD1 . ASN   A 1 1440 ? 119.480 149.018 100.718 1.00 44.90  0  1404 ASN   A OD1 1 
ATOM   10613 N ND2 . ASN   A 1 1440 ? 118.551 150.071 98.970  1.00 40.15  0  1404 ASN   A ND2 1 
ATOM   10614 N N   . VAL   A 1 1441 ? 123.745 150.202 98.787  1.00 39.70  0  1405 VAL   A N   1 
ATOM   10615 C CA  . VAL   A 1 1441 ? 124.457 149.547 97.695  1.00 42.62  0  1405 VAL   A CA  1 
ATOM   10616 C C   . VAL   A 1 1441 ? 125.885 149.307 98.165  1.00 46.47  0  1405 VAL   A C   1 
ATOM   10617 O O   . VAL   A 1 1441 ? 126.631 150.265 98.395  1.00 53.91  0  1405 VAL   A O   1 
ATOM   10618 C CB  . VAL   A 1 1441 ? 124.451 150.377 96.405  1.00 41.06  0  1405 VAL   A CB  1 
ATOM   10619 C CG1 . VAL   A 1 1441 ? 125.208 149.651 95.307  1.00 41.76  0  1405 VAL   A CG1 1 
ATOM   10620 C CG2 . VAL   A 1 1441 ? 123.030 150.675 95.968  1.00 44.35  0  1405 VAL   A CG2 1 
ATOM   10621 N N   . CYS   A 1 1442 ? 126.269 148.045 98.303  1.00 43.14  0  1406 CYS   A N   1 
ATOM   10622 C CA  . CYS   A 1 1442 ? 127.628 147.723 98.713  1.00 41.15  0  1406 CYS   A CA  1 
ATOM   10623 C C   . CYS   A 1 1442 ? 128.607 148.217 97.652  1.00 44.01  0  1406 CYS   A C   1 
ATOM   10624 O O   . CYS   A 1 1442 ? 128.362 148.022 96.454  1.00 47.53  0  1406 CYS   A O   1 
ATOM   10625 C CB  . CYS   A 1 1442 ? 127.779 146.218 98.918  1.00 45.16  0  1406 CYS   A CB  1 
ATOM   10626 S SG  . CYS   A 1 1442 ? 129.291 145.701 99.753  1.00 59.44  0  1406 CYS   A SG  1 
ATOM   10627 N N   . PRO   A 1 1443 ? 129.700 148.871 98.037  1.00 37.17  0  1407 PRO   A N   1 
ATOM   10628 C CA  . PRO   A 1 1443 ? 130.617 149.420 97.035  1.00 40.85  0  1407 PRO   A CA  1 
ATOM   10629 C C   . PRO   A 1 1443 ? 131.272 148.324 96.217  1.00 44.24  0  1407 PRO   A C   1 
ATOM   10630 O O   . PRO   A 1 1443 ? 131.582 147.240 96.717  1.00 44.06  0  1407 PRO   A O   1 
ATOM   10631 C CB  . PRO   A 1 1443 ? 131.658 150.175 97.873  1.00 40.40  0  1407 PRO   A CB  1 
ATOM   10632 C CG  . PRO   A 1 1443 ? 131.079 150.282 99.233  1.00 43.80  0  1407 PRO   A CG  1 
ATOM   10633 C CD  . PRO   A 1 1443 ? 130.180 149.109 99.405  1.00 40.87  0  1407 PRO   A CD  1 
ATOM   10634 N N   . ASN   A 1 1444 ? 131.485 148.623 94.935  1.00 47.72  0  1408 ASN   A N   1 
ATOM   10635 C CA  . ASN   A 1 1444 ? 132.208 147.694 94.077  1.00 43.37  0  1408 ASN   A CA  1 
ATOM   10636 C C   . ASN   A 1 1444 ? 133.645 147.529 94.547  1.00 46.44  0  1408 ASN   A C   1 
ATOM   10637 O O   . ASN   A 1 1444 ? 134.176 146.413 94.567  1.00 44.48  0  1408 ASN   A O   1 
ATOM   10638 C CB  . ASN   A 1 1444 ? 132.171 148.181 92.632  1.00 44.10  0  1408 ASN   A CB  1 
ATOM   10639 C CG  . ASN   A 1 1444 ? 130.783 148.130 92.036  1.00 49.14  0  1408 ASN   A CG  1 
ATOM   10640 O OD1 . ASN   A 1 1444 ? 129.993 147.239 92.347  1.00 50.96  0  1408 ASN   A OD1 1 
ATOM   10641 N ND2 . ASN   A 1 1444 ? 130.475 149.091 91.175  1.00 52.32  0  1408 ASN   A ND2 1 
ATOM   10642 N N   . ARG   A 1 1445 ? 134.284 148.628 94.940  1.00 45.94  0  1409 ARG   A N   1 
ATOM   10643 C CA  . ARG   A 1 1445 ? 135.683 148.607 95.336  1.00 41.26  0  1409 ARG   A CA  1 
ATOM   10644 C C   . ARG   A 1 1445 ? 136.003 149.885 96.094  1.00 45.45  0  1409 ARG   A C   1 
ATOM   10645 O O   . ARG   A 1 1445 ? 135.506 150.958 95.746  1.00 46.45  0  1409 ARG   A O   1 
ATOM   10646 C CB  . ARG   A 1 1445 ? 136.595 148.471 94.114  1.00 39.58  0  1409 ARG   A CB  1 
ATOM   10647 C CG  . ARG   A 1 1445 ? 138.071 148.608 94.406  1.00 41.67  0  1409 ARG   A CG  1 
ATOM   10648 C CD  . ARG   A 1 1445 ? 138.844 148.962 93.148  1.00 39.88  0  1409 ARG   A CD  1 
ATOM   10649 N NE  . ARG   A 1 1445 ? 138.687 147.954 92.108  1.00 44.02  0  1409 ARG   A NE  1 
ATOM   10650 C CZ  . ARG   A 1 1445 ? 137.885 148.077 91.061  1.00 45.29  0  1409 ARG   A CZ  1 
ATOM   10651 N NH1 . ARG   A 1 1445 ? 137.150 149.161 90.878  1.00 41.81  1  1409 ARG   A NH1 1 
ATOM   10652 N NH2 . ARG   A 1 1445 ? 137.815 147.086 90.177  1.00 51.39  0  1409 ARG   A NH2 1 
ATOM   10653 N N   . ILE   A 1 1446 ? 136.830 149.758 97.126  1.00 40.17  0  1410 ILE   A N   1 
ATOM   10654 C CA  . ILE   A 1 1446 ? 137.338 150.896 97.881  1.00 40.86  0  1410 ILE   A CA  1 
ATOM   10655 C C   . ILE   A 1 1446 ? 138.857 150.850 97.857  1.00 45.14  0  1410 ILE   A C   1 
ATOM   10656 O O   . ILE   A 1 1446 ? 139.468 149.785 97.720  1.00 49.78  0  1410 ILE   A O   1 
ATOM   10657 C CB  . ILE   A 1 1446 ? 136.843 150.919 99.342  1.00 42.67  0  1410 ILE   A CB  1 
ATOM   10658 C CG1 . ILE   A 1 1446 ? 137.452 149.743 100.096 1.00 42.38  0  1410 ILE   A CG1 1 
ATOM   10659 C CG2 . ILE   A 1 1446 ? 135.330 150.900 99.409  1.00 40.60  0  1410 ILE   A CG2 1 
ATOM   10660 C CD1 . ILE   A 1 1446 ? 137.429 149.875 101.576 1.00 39.90  0  1410 ILE   A CD1 1 
ATOM   10661 N N   . ILE   A 1 1447 ? 139.466 152.024 97.989  1.00 40.79  0  1411 ILE   A N   1 
ATOM   10662 C CA  . ILE   A 1 1447 ? 140.909 152.155 98.124  1.00 44.26  0  1411 ILE   A CA  1 
ATOM   10663 C C   . ILE   A 1 1447 ? 141.207 153.027 99.333  1.00 43.24  0  1411 ILE   A C   1 
ATOM   10664 O O   . ILE   A 1 1447 ? 140.665 154.130 99.465  1.00 38.90  0  1411 ILE   A O   1 
ATOM   10665 C CB  . ILE   A 1 1447 ? 141.564 152.733 96.856  1.00 48.17  0  1411 ILE   A CB  1 
ATOM   10666 C CG1 . ILE   A 1 1447 ? 141.279 151.833 95.658  1.00 47.87  0  1411 ILE   A CG1 1 
ATOM   10667 C CG2 . ILE   A 1 1447 ? 143.057 152.869 97.045  1.00 45.68  0  1411 ILE   A CG2 1 
ATOM   10668 C CD1 . ILE   A 1 1447 ? 140.390 152.453 94.643  1.00 51.28  0  1411 ILE   A CD1 1 
ATOM   10669 N N   . LEU   A 1 1448 ? 142.061 152.519 100.214 1.00 40.81  0  1412 LEU   A N   1 
ATOM   10670 C CA  . LEU   A 1 1448 ? 142.527 153.237 101.395 1.00 37.40  0  1412 LEU   A CA  1 
ATOM   10671 C C   . LEU   A 1 1448 ? 143.881 153.848 101.060 1.00 40.44  0  1412 LEU   A C   1 
ATOM   10672 O O   . LEU   A 1 1448 ? 144.884 153.139 100.942 1.00 46.29  0  1412 LEU   A O   1 
ATOM   10673 C CB  . LEU   A 1 1448 ? 142.614 152.298 102.591 1.00 37.54  0  1412 LEU   A CB  1 
ATOM   10674 C CG  . LEU   A 1 1448 ? 141.358 151.477 102.874 1.00 36.27  0  1412 LEU   A CG  1 
ATOM   10675 C CD1 . LEU   A 1 1448 ? 141.511 150.670 104.151 1.00 31.18  0  1412 LEU   A CD1 1 
ATOM   10676 C CD2 . LEU   A 1 1448 ? 140.153 152.390 102.958 1.00 32.95  0  1412 LEU   A CD2 1 
ATOM   10677 N N   . ILE   A 1 1449 ? 143.900 155.167 100.894 1.00 38.82  0  1413 ILE   A N   1 
ATOM   10678 C CA  . ILE   A 1 1449 ? 145.123 155.910 100.600 1.00 32.44  0  1413 ILE   A CA  1 
ATOM   10679 C C   . ILE   A 1 1449 ? 145.672 156.436 101.922 1.00 38.61  0  1413 ILE   A C   1 
ATOM   10680 O O   . ILE   A 1 1449 ? 145.017 157.278 102.556 1.00 47.69  0  1413 ILE   A O   1 
ATOM   10681 C CB  . ILE   A 1 1449 ? 144.850 157.060 99.625  1.00 34.45  0  1413 ILE   A CB  1 
ATOM   10682 C CG1 . ILE   A 1 1449 ? 144.272 156.525 98.318  1.00 37.61  0  1413 ILE   A CG1 1 
ATOM   10683 C CG2 . ILE   A 1 1449 ? 146.113 157.852 99.370  1.00 44.08  0  1413 ILE   A CG2 1 
ATOM   10684 C CD1 . ILE   A 1 1449 ? 143.860 157.607 97.358  1.00 41.15  0  1413 ILE   A CD1 1 
ATOM   10685 N N   . PRO   A 1 1450 ? 146.835 155.982 102.373 1.00 37.54  0  1414 PRO   A N   1 
ATOM   10686 C CA  . PRO   A 1 1450 ? 147.335 156.417 103.679 1.00 35.00  0  1414 PRO   A CA  1 
ATOM   10687 C C   . PRO   A 1 1450 ? 147.829 157.854 103.649 1.00 36.53  0  1414 PRO   A C   1 
ATOM   10688 O O   . PRO   A 1 1450 ? 148.139 158.418 102.598 1.00 40.71  0  1414 PRO   A O   1 
ATOM   10689 C CB  . PRO   A 1 1450 ? 148.482 155.442 103.958 1.00 37.75  0  1414 PRO   A CB  1 
ATOM   10690 C CG  . PRO   A 1 1450 ? 148.960 155.053 102.615 1.00 41.74  0  1414 PRO   A CG  1 
ATOM   10691 C CD  . PRO   A 1 1450 ? 147.752 155.035 101.720 1.00 39.49  0  1414 PRO   A CD  1 
ATOM   10692 N N   . LYS   A 1 1451 ? 147.881 158.451 104.836 1.00 39.46  0  1415 LYS   A N   1 
ATOM   10693 C CA  . LYS   A 1 1451 ? 148.565 159.718 105.054 1.00 41.05  0  1415 LYS   A CA  1 
ATOM   10694 C C   . LYS   A 1 1451 ? 149.987 159.408 105.497 1.00 46.56  0  1415 LYS   A C   1 
ATOM   10695 O O   . LYS   A 1 1451 ? 150.193 158.822 106.565 1.00 45.73  0  1415 LYS   A O   1 
ATOM   10696 C CB  . LYS   A 1 1451 ? 147.847 160.565 106.103 1.00 40.66  0  1415 LYS   A CB  1 
ATOM   10697 C CG  . LYS   A 1 1451 ? 146.578 161.231 105.611 1.00 42.85  0  1415 LYS   A CG  1 
ATOM   10698 C CD  . LYS   A 1 1451 ? 145.859 161.932 106.751 1.00 40.91  0  1415 LYS   A CD  1 
ATOM   10699 C CE  . LYS   A 1 1451 ? 144.661 162.718 106.250 1.00 44.53  0  1415 LYS   A CE  1 
ATOM   10700 N NZ  . LYS   A 1 1451 ? 143.616 161.836 105.667 1.00 46.82  1  1415 LYS   A NZ  1 
ATOM   10701 N N   . LEU   A 1 1452 ? 150.964 159.793 104.674 1.00 49.42  0  1416 LEU   A N   1 
ATOM   10702 C CA  . LEU   A 1 1452 ? 152.338 159.360 104.910 1.00 49.50  0  1416 LEU   A CA  1 
ATOM   10703 C C   . LEU   A 1 1452 ? 152.912 159.972 106.183 1.00 48.84  0  1416 LEU   A C   1 
ATOM   10704 O O   . LEU   A 1 1452 ? 153.625 159.296 106.932 1.00 48.11  0  1416 LEU   A O   1 
ATOM   10705 C CB  . LEU   A 1 1452 ? 153.212 159.704 103.705 1.00 45.69  0  1416 LEU   A CB  1 
ATOM   10706 C CG  . LEU   A 1 1452 ? 153.241 158.688 102.559 1.00 46.72  0  1416 LEU   A CG  1 
ATOM   10707 C CD1 . LEU   A 1 1452 ? 153.668 157.325 103.074 1.00 49.46  0  1416 LEU   A CD1 1 
ATOM   10708 C CD2 . LEU   A 1 1452 ? 151.908 158.605 101.829 1.00 45.44  0  1416 LEU   A CD2 1 
ATOM   10709 N N   . ASN   A 1 1453 ? 152.613 161.247 106.447 1.00 46.46  0  1417 ASN   A N   1 
ATOM   10710 C CA  . ASN   A 1 1453 ? 153.162 161.906 107.627 1.00 47.94  0  1417 ASN   A CA  1 
ATOM   10711 C C   . ASN   A 1 1453 ? 152.661 161.289 108.924 1.00 44.38  0  1417 ASN   A C   1 
ATOM   10712 O O   . ASN   A 1 1453 ? 153.296 161.466 109.968 1.00 45.76  0  1417 ASN   A O   1 
ATOM   10713 C CB  . ASN   A 1 1453 ? 152.834 163.399 107.600 1.00 49.70  0  1417 ASN   A CB  1 
ATOM   10714 C CG  . ASN   A 1 1453 ? 151.354 163.668 107.460 1.00 47.47  0  1417 ASN   A CG  1 
ATOM   10715 O OD1 . ASN   A 1 1453 ? 150.546 162.744 107.417 1.00 50.24  0  1417 ASN   A OD1 1 
ATOM   10716 N ND2 . ASN   A 1 1453 ? 150.989 164.940 107.392 1.00 44.86  0  1417 ASN   A ND2 1 
ATOM   10717 N N   . GLU   A 1 1454 ? 151.539 160.573 108.885 1.00 41.72  0  1418 GLU   A N   1 
ATOM   10718 C CA  . GLU   A 1 1454 ? 151.028 159.909 110.075 1.00 45.00  0  1418 GLU   A CA  1 
ATOM   10719 C C   . GLU   A 1 1454 ? 151.770 158.619 110.391 1.00 45.02  0  1418 GLU   A C   1 
ATOM   10720 O O   . GLU   A 1 1454 ? 151.657 158.114 111.513 1.00 36.82  0  1418 GLU   A O   1 
ATOM   10721 C CB  . GLU   A 1 1454 ? 149.537 159.615 109.904 1.00 38.40  0  1418 GLU   A CB  1 
ATOM   10722 C CG  . GLU   A 1 1454 ? 148.653 160.846 109.933 1.00 39.47  0  1418 GLU   A CG  1 
ATOM   10723 C CD  . GLU   A 1 1454 ? 148.020 161.072 111.289 1.00 45.91  0  1418 GLU   A CD  1 
ATOM   10724 O OE1 . GLU   A 1 1454 ? 148.258 160.253 112.201 1.00 45.96  0  1418 GLU   A OE1 1 
ATOM   10725 O OE2 . GLU   A 1 1454 ? 147.280 162.064 111.443 1.00 47.37  -1 1418 GLU   A OE2 1 
ATOM   10726 N N   . ILE   A 1 1455 ? 152.525 158.081 109.439 1.00 42.35  0  1419 ILE   A N   1 
ATOM   10727 C CA  . ILE   A 1 1455 ? 153.212 156.803 109.590 1.00 43.43  0  1419 ILE   A CA  1 
ATOM   10728 C C   . ILE   A 1 1455 ? 154.680 157.091 109.856 1.00 40.13  0  1419 ILE   A C   1 
ATOM   10729 O O   . ILE   A 1 1455 ? 155.329 157.809 109.087 1.00 38.15  0  1419 ILE   A O   1 
ATOM   10730 C CB  . ILE   A 1 1455 ? 153.037 155.916 108.348 1.00 39.33  0  1419 ILE   A CB  1 
ATOM   10731 C CG1 . ILE   A 1 1455 ? 151.599 155.996 107.838 1.00 37.90  0  1419 ILE   A CG1 1 
ATOM   10732 C CG2 . ILE   A 1 1455 ? 153.399 154.480 108.668 1.00 37.20  0  1419 ILE   A CG2 1 
ATOM   10733 C CD1 . ILE   A 1 1455 ? 151.382 155.307 106.523 1.00 31.60  0  1419 ILE   A CD1 1 
ATOM   10734 N N   . HIS   A 1 1456 ? 155.204 156.531 110.941 1.00 44.83  0  1420 HIS   A N   1 
ATOM   10735 C CA  . HIS   A 1 1456 ? 156.573 156.774 111.361 1.00 38.58  0  1420 HIS   A CA  1 
ATOM   10736 C C   . HIS   A 1 1456 ? 157.313 155.455 111.517 1.00 35.53  0  1420 HIS   A C   1 
ATOM   10737 O O   . HIS   A 1 1456 ? 156.733 154.436 111.899 1.00 38.35  0  1420 HIS   A O   1 
ATOM   10738 C CB  . HIS   A 1 1456 ? 156.622 157.560 112.677 1.00 45.57  0  1420 HIS   A CB  1 
ATOM   10739 C CG  . HIS   A 1 1456 ? 156.096 158.957 112.565 1.00 52.14  0  1420 HIS   A CG  1 
ATOM   10740 N ND1 . HIS   A 1 1456 ? 156.382 159.775 111.494 1.00 50.20  0  1420 HIS   A ND1 1 
ATOM   10741 C CD2 . HIS   A 1 1456 ? 155.294 159.676 113.385 1.00 46.76  0  1420 HIS   A CD2 1 
ATOM   10742 C CE1 . HIS   A 1 1456 ? 155.782 160.941 111.661 1.00 48.83  0  1420 HIS   A CE1 1 
ATOM   10743 N NE2 . HIS   A 1 1456 ? 155.114 160.906 112.799 1.00 46.61  0  1420 HIS   A NE2 1 
ATOM   10744 N N   . LEU   A 1 1457 ? 158.606 155.492 111.218 1.00 40.38  0  1421 LEU   A N   1 
ATOM   10745 C CA  . LEU   A 1 1457 ? 159.442 154.308 111.296 1.00 43.07  0  1421 LEU   A CA  1 
ATOM   10746 C C   . LEU   A 1 1457 ? 159.582 153.847 112.744 1.00 36.12  0  1421 LEU   A C   1 
ATOM   10747 O O   . LEU   A 1 1457 ? 159.470 154.632 113.689 1.00 34.57  0  1421 LEU   A O   1 
ATOM   10748 C CB  . LEU   A 1 1457 ? 160.808 154.604 110.677 1.00 40.00  0  1421 LEU   A CB  1 
ATOM   10749 C CG  . LEU   A 1 1457 ? 161.838 153.488 110.546 1.00 41.01  0  1421 LEU   A CG  1 
ATOM   10750 C CD1 . LEU   A 1 1457 ? 162.557 153.602 109.220 1.00 45.15  0  1421 LEU   A CD1 1 
ATOM   10751 C CD2 . LEU   A 1 1457 ? 162.821 153.591 111.684 1.00 42.37  0  1421 LEU   A CD2 1 
ATOM   10752 N N   . MET   A 1 1458 ? 159.819 152.546 112.915 1.00 29.21  0  1422 MET   A N   1 
ATOM   10753 C CA  . MET   A 1 1458 ? 159.964 151.975 114.252 1.00 30.59  0  1422 MET   A CA  1 
ATOM   10754 C C   . MET   A 1 1458 ? 161.094 150.952 114.209 1.00 35.14  0  1422 MET   A C   1 
ATOM   10755 O O   . MET   A 1 1458 ? 160.968 149.913 113.556 1.00 39.60  0  1422 MET   A O   1 
ATOM   10756 C CB  . MET   A 1 1458 ? 158.666 151.338 114.727 1.00 38.82  0  1422 MET   A CB  1 
ATOM   10757 C CG  . MET   A 1 1458 ? 158.866 150.363 115.874 1.00 41.04  0  1422 MET   A CG  1 
ATOM   10758 S SD  . MET   A 1 1458 ? 157.404 150.139 116.897 1.00 36.59  0  1422 MET   A SD  1 
ATOM   10759 C CE  . MET   A 1 1458 ? 156.128 150.180 115.661 1.00 27.80  0  1422 MET   A CE  1 
ATOM   10760 N N   . LYS   A 1 1459 ? 162.188 151.251 114.904 1.00 43.36  0  1423 LYS   A N   1 
ATOM   10761 C CA  . LYS   A 1 1459 ? 163.278 150.308 115.080 1.00 47.64  0  1423 LYS   A CA  1 
ATOM   10762 C C   . LYS   A 1 1459 ? 163.474 149.992 116.555 1.00 46.49  0  1423 LYS   A C   1 
ATOM   10763 O O   . LYS   A 1 1459 ? 163.263 150.854 117.411 1.00 49.66  0  1423 LYS   A O   1 
ATOM   10764 C CB  . LYS   A 1 1459 ? 164.600 150.844 114.519 1.00 53.69  0  1423 LYS   A CB  1 
ATOM   10765 C CG  . LYS   A 1 1459 ? 164.643 150.985 113.015 1.00 49.90  0  1423 LYS   A CG  1 
ATOM   10766 C CD  . LYS   A 1 1459 ? 165.920 151.670 112.569 1.00 49.77  0  1423 LYS   A CD  1 
ATOM   10767 C CE  . LYS   A 1 1459 ? 167.136 151.064 113.248 1.00 52.66  0  1423 LYS   A CE  1 
ATOM   10768 N NZ  . LYS   A 1 1459 ? 167.230 149.598 113.008 1.00 52.03  1  1423 LYS   A NZ  1 
ATOM   10769 N N   . PRO   A 1 1460 ? 163.886 148.773 116.884 1.00 46.08  0  1424 PRO   A N   1 
ATOM   10770 C CA  . PRO   A 1 1460 ? 164.220 148.453 118.271 1.00 51.50  0  1424 PRO   A CA  1 
ATOM   10771 C C   . PRO   A 1 1460 ? 165.445 149.228 118.718 1.00 49.99  0  1424 PRO   A C   1 
ATOM   10772 O O   . PRO   A 1 1460 ? 166.547 149.027 118.187 1.00 50.85  0  1424 PRO   A O   1 
ATOM   10773 C CB  . PRO   A 1 1460 ? 164.495 146.943 118.234 1.00 46.99  0  1424 PRO   A CB  1 
ATOM   10774 C CG  . PRO   A 1 1460 ? 164.824 146.651 116.816 1.00 48.50  0  1424 PRO   A CG  1 
ATOM   10775 C CD  . PRO   A 1 1460 ? 164.020 147.608 115.996 1.00 46.06  0  1424 PRO   A CD  1 
ATOM   10776 N N   . PRO   A 1 1461 ? 165.295 150.129 119.681 1.00 48.75  0  1425 PRO   A N   1 
ATOM   10777 C CA  . PRO   A 1 1461 ? 166.410 150.979 120.095 1.00 49.32  0  1425 PRO   A CA  1 
ATOM   10778 C C   . PRO   A 1 1461 ? 167.340 150.264 121.068 1.00 55.75  0  1425 PRO   A C   1 
ATOM   10779 O O   . PRO   A 1 1461 ? 167.043 149.184 121.582 1.00 53.34  0  1425 PRO   A O   1 
ATOM   10780 C CB  . PRO   A 1 1461 ? 165.702 152.152 120.779 1.00 46.45  0  1425 PRO   A CB  1 
ATOM   10781 C CG  . PRO   A 1 1461 ? 164.492 151.529 121.375 1.00 52.41  0  1425 PRO   A CG  1 
ATOM   10782 C CD  . PRO   A 1 1461 ? 164.073 150.411 120.453 1.00 46.09  0  1425 PRO   A CD  1 
ATOM   10783 N N   . ILE   A 1 1462 ? 168.481 150.898 121.312 1.00 51.85  0  1426 ILE   A N   1 
ATOM   10784 C CA  . ILE   A 1 1462 ? 169.479 150.408 122.253 1.00 44.44  0  1426 ILE   A CA  1 
ATOM   10785 C C   . ILE   A 1 1462 ? 169.186 151.035 123.607 1.00 46.32  0  1426 ILE   A C   1 
ATOM   10786 O O   . ILE   A 1 1462 ? 169.197 152.263 123.746 1.00 51.70  0  1426 ILE   A O   1 
ATOM   10787 C CB  . ILE   A 1 1462 ? 170.902 150.742 121.781 1.00 48.75  0  1426 ILE   A CB  1 
ATOM   10788 C CG1 . ILE   A 1 1462 ? 171.204 150.032 120.461 1.00 46.36  0  1426 ILE   A CG1 1 
ATOM   10789 C CG2 . ILE   A 1 1462 ? 171.921 150.368 122.843 1.00 49.52  0  1426 ILE   A CG2 1 
ATOM   10790 C CD1 . ILE   A 1 1462 ? 172.463 150.518 119.783 1.00 48.48  0  1426 ILE   A CD1 1 
ATOM   10791 N N   . PHE   A 1 1463 ? 168.925 150.197 124.604 1.00 41.96  0  1427 PHE   A N   1 
ATOM   10792 C CA  . PHE   A 1 1463 ? 168.499 150.671 125.918 1.00 49.55  0  1427 PHE   A CA  1 
ATOM   10793 C C   . PHE   A 1 1463 ? 169.726 151.086 126.715 1.00 54.29  0  1427 PHE   A C   1 
ATOM   10794 O O   . PHE   A 1 1463 ? 170.255 150.328 127.528 1.00 55.15  0  1427 PHE   A O   1 
ATOM   10795 C CB  . PHE   A 1 1463 ? 167.699 149.596 126.641 1.00 44.95  0  1427 PHE   A CB  1 
ATOM   10796 C CG  . PHE   A 1 1463 ? 166.350 149.357 126.043 1.00 44.16  0  1427 PHE   A CG  1 
ATOM   10797 C CD1 . PHE   A 1 1463 ? 165.462 150.398 125.879 1.00 43.37  0  1427 PHE   A CD1 1 
ATOM   10798 C CD2 . PHE   A 1 1463 ? 165.981 148.100 125.620 1.00 47.42  0  1427 PHE   A CD2 1 
ATOM   10799 C CE1 . PHE   A 1 1463 ? 164.230 150.189 125.319 1.00 39.91  0  1427 PHE   A CE1 1 
ATOM   10800 C CE2 . PHE   A 1 1463 ? 164.744 147.887 125.062 1.00 49.52  0  1427 PHE   A CE2 1 
ATOM   10801 C CZ  . PHE   A 1 1463 ? 163.870 148.934 124.910 1.00 43.58  0  1427 PHE   A CZ  1 
ATOM   10802 N N   . THR   A 1 1464 ? 170.184 152.311 126.480 1.00 49.83  0  1428 THR   A N   1 
ATOM   10803 C CA  . THR   A 1 1464 ? 171.298 152.846 127.246 1.00 46.09  0  1428 THR   A CA  1 
ATOM   10804 C C   . THR   A 1 1464 ? 170.865 153.109 128.683 1.00 45.18  0  1428 THR   A C   1 
ATOM   10805 O O   . THR   A 1 1464 ? 169.776 153.633 128.931 1.00 41.58  0  1428 THR   A O   1 
ATOM   10806 C CB  . THR   A 1 1464 ? 171.829 154.124 126.597 1.00 49.03  0  1428 THR   A CB  1 
ATOM   10807 O OG1 . THR   A 1 1464 ? 172.821 154.720 127.443 1.00 49.63  0  1428 THR   A OG1 1 
ATOM   10808 C CG2 . THR   A 1 1464 ? 170.704 155.117 126.341 1.00 51.25  0  1428 THR   A CG2 1 
ATOM   10809 N N   . GLY   A 1 1465 ? 171.712 152.729 129.629 1.00 48.57  0  1429 GLY   A N   1 
ATOM   10810 C CA  . GLY   A 1 1465 ? 171.418 152.877 131.039 1.00 49.07  0  1429 GLY   A CA  1 
ATOM   10811 C C   . GLY   A 1 1465 ? 171.621 151.578 131.792 1.00 50.53  0  1429 GLY   A C   1 
ATOM   10812 O O   . GLY   A 1 1465 ? 171.855 150.517 131.219 1.00 54.79  0  1429 GLY   A O   1 
ATOM   10813 N N   . ASP   A 1 1466 ? 171.522 151.691 133.110 1.00 56.45  0  1430 ASP   A N   1 
ATOM   10814 C CA  . ASP   A 1 1466 ? 171.707 150.565 134.009 1.00 55.39  0  1430 ASP   A CA  1 
ATOM   10815 C C   . ASP   A 1 1466 ? 170.388 150.220 134.684 1.00 60.83  0  1430 ASP   A C   1 
ATOM   10816 O O   . ASP   A 1 1466 ? 169.441 151.010 134.691 1.00 62.14  0  1430 ASP   A O   1 
ATOM   10817 C CB  . ASP   A 1 1466 ? 172.771 150.868 135.071 1.00 58.87  0  1430 ASP   A CB  1 
ATOM   10818 C CG  . ASP   A 1 1466 ? 174.160 151.007 134.484 1.00 61.95  0  1430 ASP   A CG  1 
ATOM   10819 O OD1 . ASP   A 1 1466 ? 174.272 151.158 133.251 1.00 60.08  0  1430 ASP   A OD1 1 
ATOM   10820 O OD2 . ASP   A 1 1466 ? 175.140 150.967 135.257 1.00 62.31  -1 1430 ASP   A OD2 1 
ATOM   10821 N N   . VAL   A 1 1467 ? 170.335 149.020 135.251 1.00 58.78  0  1431 VAL   A N   1 
ATOM   10822 C CA  . VAL   A 1 1467 ? 169.182 148.551 136.008 1.00 60.27  0  1431 VAL   A CA  1 
ATOM   10823 C C   . VAL   A 1 1467 ? 169.574 148.486 137.476 1.00 58.09  0  1431 VAL   A C   1 
ATOM   10824 O O   . VAL   A 1 1467 ? 170.624 147.931 137.821 1.00 60.95  0  1431 VAL   A O   1 
ATOM   10825 C CB  . VAL   A 1 1467 ? 168.703 147.182 135.501 1.00 50.60  0  1431 VAL   A CB  1 
ATOM   10826 C CG1 . VAL   A 1 1467 ? 167.563 146.669 136.356 1.00 52.36  0  1431 VAL   A CG1 1 
ATOM   10827 C CG2 . VAL   A 1 1467 ? 168.285 147.278 134.046 1.00 47.43  0  1431 VAL   A CG2 1 
ATOM   10828 N N   . ASP   A 1 1468 ? 168.742 149.057 138.342 1.00 52.37  0  1432 ASP   A N   1 
ATOM   10829 C CA  . ASP   A 1 1468 ? 169.051 149.119 139.768 1.00 52.93  0  1432 ASP   A CA  1 
ATOM   10830 C C   . ASP   A 1 1468 ? 168.940 147.722 140.360 1.00 55.99  0  1432 ASP   A C   1 
ATOM   10831 O O   . ASP   A 1 1468 ? 167.843 147.230 140.627 1.00 57.11  0  1432 ASP   A O   1 
ATOM   10832 C CB  . ASP   A 1 1468 ? 168.118 150.095 140.473 1.00 55.36  0  1432 ASP   A CB  1 
ATOM   10833 C CG  . ASP   A 1 1468 ? 168.718 150.652 141.743 1.00 56.99  0  1432 ASP   A CG  1 
ATOM   10834 O OD1 . ASP   A 1 1468 ? 169.412 149.896 142.454 1.00 56.84  0  1432 ASP   A OD1 1 
ATOM   10835 O OD2 . ASP   A 1 1468 ? 168.500 151.847 142.029 1.00 60.77  -1 1432 ASP   A OD2 1 
ATOM   10836 N N   . ILE   A 1 1469 ? 170.087 147.076 140.568 1.00 56.98  0  1433 ILE   A N   1 
ATOM   10837 C CA  . ILE   A 1 1469 ? 170.089 145.691 141.027 1.00 53.46  0  1433 ILE   A CA  1 
ATOM   10838 C C   . ILE   A 1 1469 ? 169.633 145.597 142.476 1.00 55.97  0  1433 ILE   A C   1 
ATOM   10839 O O   . ILE   A 1 1469 ? 168.898 144.676 142.847 1.00 59.56  0  1433 ILE   A O   1 
ATOM   10840 C CB  . ILE   A 1 1469 ? 171.478 145.066 140.828 1.00 55.55  0  1433 ILE   A CB  1 
ATOM   10841 C CG1 . ILE   A 1 1469 ? 171.934 145.260 139.384 1.00 56.74  0  1433 ILE   A CG1 1 
ATOM   10842 C CG2 . ILE   A 1 1469 ? 171.452 143.592 141.186 1.00 58.26  0  1433 ILE   A CG2 1 
ATOM   10843 C CD1 . ILE   A 1 1469 ? 170.930 144.788 138.370 1.00 52.81  0  1433 ILE   A CD1 1 
ATOM   10844 N N   . HIS   A 1 1470 ? 170.073 146.528 143.324 1.00 48.20  0  1434 HIS   A N   1 
ATOM   10845 C CA  . HIS   A 1 1470 ? 169.671 146.482 144.726 1.00 50.04  0  1434 HIS   A CA  1 
ATOM   10846 C C   . HIS   A 1 1470 ? 168.171 146.695 144.881 1.00 55.84  0  1434 HIS   A C   1 
ATOM   10847 O O   . HIS   A 1 1470 ? 167.522 146.017 145.687 1.00 54.45  0  1434 HIS   A O   1 
ATOM   10848 C CB  . HIS   A 1 1470 ? 170.444 147.521 145.533 1.00 51.86  0  1434 HIS   A CB  1 
ATOM   10849 C CG  . HIS   A 1 1470 ? 169.905 147.732 146.912 1.00 57.94  0  1434 HIS   A CG  1 
ATOM   10850 N ND1 . HIS   A 1 1470 ? 169.914 146.744 147.873 1.00 55.38  0  1434 HIS   A ND1 1 
ATOM   10851 C CD2 . HIS   A 1 1470 ? 169.340 148.816 147.493 1.00 57.46  0  1434 HIS   A CD2 1 
ATOM   10852 C CE1 . HIS   A 1 1470 ? 169.377 147.211 148.986 1.00 55.54  0  1434 HIS   A CE1 1 
ATOM   10853 N NE2 . HIS   A 1 1470 ? 169.020 148.466 148.782 1.00 55.89  0  1434 HIS   A NE2 1 
ATOM   10854 N N   . LYS   A 1 1471 ? 167.600 147.630 144.118 1.00 55.28  0  1435 LYS   A N   1 
ATOM   10855 C CA  . LYS   A 1 1471 ? 166.158 147.846 144.174 1.00 50.60  0  1435 LYS   A CA  1 
ATOM   10856 C C   . LYS   A 1 1471 ? 165.400 146.624 143.672 1.00 51.30  0  1435 LYS   A C   1 
ATOM   10857 O O   . LYS   A 1 1471 ? 164.352 146.266 144.220 1.00 53.45  0  1435 LYS   A O   1 
ATOM   10858 C CB  . LYS   A 1 1471 ? 165.780 149.086 143.366 1.00 48.20  0  1435 LYS   A CB  1 
ATOM   10859 C CG  . LYS   A 1 1471 ? 166.229 150.391 143.996 1.00 48.27  0  1435 LYS   A CG  1 
ATOM   10860 C CD  . LYS   A 1 1471 ? 165.876 150.440 145.471 1.00 50.37  0  1435 LYS   A CD  1 
ATOM   10861 C CE  . LYS   A 1 1471 ? 166.070 151.831 146.041 1.00 47.70  0  1435 LYS   A CE  1 
ATOM   10862 N NZ  . LYS   A 1 1471 ? 165.935 151.835 147.522 1.00 52.85  1  1435 LYS   A NZ  1 
ATOM   10863 N N   . LEU   A 1 1472 ? 165.911 145.974 142.626 1.00 49.88  0  1436 LEU   A N   1 
ATOM   10864 C CA  . LEU   A 1 1472 ? 165.274 144.759 142.130 1.00 45.84  0  1436 LEU   A CA  1 
ATOM   10865 C C   . LEU   A 1 1472 ? 165.321 143.650 143.172 1.00 44.19  0  1436 LEU   A C   1 
ATOM   10866 O O   . LEU   A 1 1472 ? 164.340 142.921 143.363 1.00 51.72  0  1436 LEU   A O   1 
ATOM   10867 C CB  . LEU   A 1 1472 ? 165.952 144.314 140.836 1.00 44.80  0  1436 LEU   A CB  1 
ATOM   10868 C CG  . LEU   A 1 1472 ? 165.184 143.338 139.954 1.00 44.99  0  1436 LEU   A CG  1 
ATOM   10869 C CD1 . LEU   A 1 1472 ? 165.386 143.705 138.503 1.00 48.87  0  1436 LEU   A CD1 1 
ATOM   10870 C CD2 . LEU   A 1 1472 ? 165.652 141.926 140.211 1.00 53.32  0  1436 LEU   A CD2 1 
ATOM   10871 N N   . LYS   A 1 1473 ? 166.456 143.510 143.857 1.00 44.81  0  1437 LYS   A N   1 
ATOM   10872 C CA  . LYS   A 1 1473 ? 166.564 142.522 144.922 1.00 48.42  0  1437 LYS   A CA  1 
ATOM   10873 C C   . LYS   A 1 1473 ? 165.599 142.835 146.057 1.00 56.10  0  1437 LYS   A C   1 
ATOM   10874 O O   . LYS   A 1 1473 ? 164.999 141.927 146.641 1.00 63.81  0  1437 LYS   A O   1 
ATOM   10875 C CB  . LYS   A 1 1473 ? 168.001 142.466 145.434 1.00 49.23  0  1437 LYS   A CB  1 
ATOM   10876 C CG  . LYS   A 1 1473 ? 168.492 141.070 145.745 1.00 50.30  0  1437 LYS   A CG  1 
ATOM   10877 C CD  . LYS   A 1 1473 ? 169.994 141.056 145.962 1.00 56.04  0  1437 LYS   A CD  1 
ATOM   10878 C CE  . LYS   A 1 1473 ? 170.404 142.031 147.051 1.00 56.51  0  1437 LYS   A CE  1 
ATOM   10879 N NZ  . LYS   A 1 1473 ? 171.831 141.858 147.440 1.00 54.69  1  1437 LYS   A NZ  1 
ATOM   10880 N N   . GLN   A 1 1474 ? 165.440 144.119 146.384 1.00 52.49  0  1438 GLN   A N   1 
ATOM   10881 C CA  . GLN   A 1 1474 ? 164.476 144.506 147.409 1.00 48.81  0  1438 GLN   A CA  1 
ATOM   10882 C C   . GLN   A 1 1474 ? 163.050 144.178 146.984 1.00 48.96  0  1438 GLN   A C   1 
ATOM   10883 O O   . GLN   A 1 1474 ? 162.246 143.717 147.800 1.00 52.26  0  1438 GLN   A O   1 
ATOM   10884 C CB  . GLN   A 1 1474 ? 164.612 145.995 147.722 1.00 51.45  0  1438 GLN   A CB  1 
ATOM   10885 C CG  . GLN   A 1 1474 ? 165.875 146.351 148.479 1.00 55.36  0  1438 GLN   A CG  1 
ATOM   10886 C CD  . GLN   A 1 1474 ? 165.843 145.875 149.913 1.00 60.61  0  1438 GLN   A CD  1 
ATOM   10887 O OE1 . GLN   A 1 1474 ? 165.017 146.320 150.708 1.00 62.66  0  1438 GLN   A OE1 1 
ATOM   10888 N NE2 . GLN   A 1 1474 ? 166.743 144.960 150.253 1.00 55.15  0  1438 GLN   A NE2 1 
ATOM   10889 N N   . VAL   A 1 1475 ? 162.714 144.420 145.715 1.00 41.74  0  1439 VAL   A N   1 
ATOM   10890 C CA  . VAL   A 1 1475 ? 161.374 144.104 145.226 1.00 40.11  0  1439 VAL   A CA  1 
ATOM   10891 C C   . VAL   A 1 1475 ? 161.120 142.606 145.304 1.00 36.57  0  1439 VAL   A C   1 
ATOM   10892 O O   . VAL   A 1 1475 ? 160.036 142.163 145.699 1.00 47.27  0  1439 VAL   A O   1 
ATOM   10893 C CB  . VAL   A 1 1475 ? 161.181 144.636 143.794 1.00 36.58  0  1439 VAL   A CB  1 
ATOM   10894 C CG1 . VAL   A 1 1475 ? 159.951 144.018 143.159 1.00 31.33  0  1439 VAL   A CG1 1 
ATOM   10895 C CG2 . VAL   A 1 1475 ? 161.058 146.145 143.803 1.00 34.98  0  1439 VAL   A CG2 1 
ATOM   10896 N N   . ILE   A 1 1476 ? 162.113 141.802 144.925 1.00 40.47  0  1440 ILE   A N   1 
ATOM   10897 C CA  . ILE   A 1 1476 ? 161.958 140.353 145.005 1.00 39.90  0  1440 ILE   A CA  1 
ATOM   10898 C C   . ILE   A 1 1476 ? 161.804 139.904 146.453 1.00 43.19  0  1440 ILE   A C   1 
ATOM   10899 O O   . ILE   A 1 1476 ? 160.951 139.066 146.768 1.00 50.20  0  1440 ILE   A O   1 
ATOM   10900 C CB  . ILE   A 1 1476 ? 163.138 139.648 144.315 1.00 42.14  0  1440 ILE   A CB  1 
ATOM   10901 C CG1 . ILE   A 1 1476 ? 163.010 139.761 142.798 1.00 41.51  0  1440 ILE   A CG1 1 
ATOM   10902 C CG2 . ILE   A 1 1476 ? 163.218 138.197 144.737 1.00 43.43  0  1440 ILE   A CG2 1 
ATOM   10903 C CD1 . ILE   A 1 1476 ? 164.176 139.179 142.053 1.00 41.94  0  1440 ILE   A CD1 1 
ATOM   10904 N N   . GLN   A 1 1477 ? 162.615 140.453 147.359 1.00 50.64  0  1441 GLN   A N   1 
ATOM   10905 C CA  . GLN   A 1 1477 ? 162.607 139.977 148.738 1.00 55.20  0  1441 GLN   A CA  1 
ATOM   10906 C C   . GLN   A 1 1477 ? 161.345 140.404 149.479 1.00 56.37  0  1441 GLN   A C   1 
ATOM   10907 O O   . GLN   A 1 1477 ? 160.781 139.622 150.253 1.00 55.04  0  1441 GLN   A O   1 
ATOM   10908 C CB  . GLN   A 1 1477 ? 163.855 140.475 149.467 1.00 52.20  0  1441 GLN   A CB  1 
ATOM   10909 C CG  . GLN   A 1 1477 ? 164.070 139.867 150.845 1.00 51.51  0  1441 GLN   A CG  1 
ATOM   10910 C CD  . GLN   A 1 1477 ? 163.170 140.477 151.901 1.00 57.54  0  1441 GLN   A CD  1 
ATOM   10911 O OE1 . GLN   A 1 1477 ? 163.236 141.674 152.174 1.00 59.83  0  1441 GLN   A OE1 1 
ATOM   10912 N NE2 . GLN   A 1 1477 ? 162.306 139.657 152.485 1.00 54.24  0  1441 GLN   A NE2 1 
ATOM   10913 N N   . LYS   A 1 1478 ? 160.896 141.645 149.274 1.00 49.58  0  1442 LYS   A N   1 
ATOM   10914 C CA  . LYS   A 1 1478 ? 159.786 142.169 150.062 1.00 48.34  0  1442 LYS   A CA  1 
ATOM   10915 C C   . LYS   A 1 1478 ? 158.512 141.373 149.823 1.00 52.41  0  1442 LYS   A C   1 
ATOM   10916 O O   . LYS   A 1 1478 ? 157.773 141.071 150.767 1.00 54.32  0  1442 LYS   A O   1 
ATOM   10917 C CB  . LYS   A 1 1478 ? 159.566 143.644 149.736 1.00 44.80  0  1442 LYS   A CB  1 
ATOM   10918 C CG  . LYS   A 1 1478 ? 160.249 144.587 150.700 1.00 47.58  0  1442 LYS   A CG  1 
ATOM   10919 C CD  . LYS   A 1 1478 ? 160.413 145.963 150.097 1.00 45.18  0  1442 LYS   A CD  1 
ATOM   10920 C CE  . LYS   A 1 1478 ? 160.726 146.987 151.168 1.00 49.48  0  1442 LYS   A CE  1 
ATOM   10921 N NZ  . LYS   A 1 1478 ? 161.124 148.290 150.576 1.00 54.27  1  1442 LYS   A NZ  1 
ATOM   10922 N N   . GLN   A 1 1479 ? 158.241 141.023 148.569 1.00 50.47  0  1443 GLN   A N   1 
ATOM   10923 C CA  . GLN   A 1 1479 ? 157.089 140.207 148.200 1.00 47.62  0  1443 GLN   A CA  1 
ATOM   10924 C C   . GLN   A 1 1479 ? 157.501 138.783 147.869 1.00 48.54  0  1443 GLN   A C   1 
ATOM   10925 O O   . GLN   A 1 1479 ? 156.965 138.172 146.944 1.00 55.44  0  1443 GLN   A O   1 
ATOM   10926 C CB  . GLN   A 1 1479 ? 156.348 140.839 147.029 1.00 42.75  0  1443 GLN   A CB  1 
ATOM   10927 C CG  . GLN   A 1 1479 ? 156.315 142.348 147.087 1.00 43.23  0  1443 GLN   A CG  1 
ATOM   10928 C CD  . GLN   A 1 1479 ? 155.161 142.871 147.915 1.00 54.86  0  1443 GLN   A CD  1 
ATOM   10929 O OE1 . GLN   A 1 1479 ? 154.593 142.153 148.736 1.00 53.50  0  1443 GLN   A OE1 1 
ATOM   10930 N NE2 . GLN   A 1 1479 ? 154.816 144.131 147.712 1.00 57.67  0  1443 GLN   A NE2 1 
ATOM   10931 N N   . HIS   A 1 1480 ? 158.462 138.237 148.615 1.00 46.82  0  1444 HIS   A N   1 
ATOM   10932 C CA  . HIS   A 1 1480 ? 158.987 136.913 148.298 1.00 53.93  0  1444 HIS   A CA  1 
ATOM   10933 C C   . HIS   A 1 1480 ? 157.923 135.834 148.452 1.00 56.95  0  1444 HIS   A C   1 
ATOM   10934 O O   . HIS   A 1 1480 ? 158.008 134.780 147.812 1.00 56.90  0  1444 HIS   A O   1 
ATOM   10935 C CB  . HIS   A 1 1480 ? 160.189 136.605 149.185 1.00 54.90  0  1444 HIS   A CB  1 
ATOM   10936 C CG  . HIS   A 1 1480 ? 159.827 136.300 150.603 1.00 57.26  0  1444 HIS   A CG  1 
ATOM   10937 N ND1 . HIS   A 1 1480 ? 159.659 135.014 151.067 1.00 58.12  0  1444 HIS   A ND1 1 
ATOM   10938 C CD2 . HIS   A 1 1480 ? 159.598 137.114 151.659 1.00 56.23  0  1444 HIS   A CD2 1 
ATOM   10939 C CE1 . HIS   A 1 1480 ? 159.344 135.049 152.349 1.00 60.23  0  1444 HIS   A CE1 1 
ATOM   10940 N NE2 . HIS   A 1 1480 ? 159.300 136.311 152.733 1.00 59.43  0  1444 HIS   A NE2 1 
ATOM   10941 N N   . MET   A 1 1481 ? 156.910 136.076 149.285 1.00 53.36  0  1445 MET   A N   1 
ATOM   10942 C CA  . MET   A 1 1481 ? 155.899 135.057 149.541 1.00 52.08  0  1445 MET   A CA  1 
ATOM   10943 C C   . MET   A 1 1481 ? 155.084 134.706 148.305 1.00 53.55  0  1445 MET   A C   1 
ATOM   10944 O O   . MET   A 1 1481 ? 154.423 133.663 148.299 1.00 57.92  0  1445 MET   A O   1 
ATOM   10945 C CB  . MET   A 1 1481 ? 154.967 135.509 150.664 1.00 51.23  0  1445 MET   A CB  1 
ATOM   10946 C CG  . MET   A 1 1481 ? 154.098 136.698 150.314 1.00 50.46  0  1445 MET   A CG  1 
ATOM   10947 S SD  . MET   A 1 1481 ? 154.905 138.265 150.681 1.00 57.66  0  1445 MET   A SD  1 
ATOM   10948 C CE  . MET   A 1 1481 ? 155.143 138.102 152.446 1.00 55.10  0  1445 MET   A CE  1 
ATOM   10949 N N   . PHE   A 1 1482 ? 155.109 135.540 147.269 1.00 51.44  0  1446 PHE   A N   1 
ATOM   10950 C CA  . PHE   A 1 1482 ? 154.406 135.263 146.024 1.00 51.53  0  1446 PHE   A CA  1 
ATOM   10951 C C   . PHE   A 1 1482 ? 155.339 134.768 144.929 1.00 51.71  0  1446 PHE   A C   1 
ATOM   10952 O O   . PHE   A 1 1482 ? 154.921 134.667 143.771 1.00 54.27  0  1446 PHE   A O   1 
ATOM   10953 C CB  . PHE   A 1 1482 ? 153.658 136.509 145.552 1.00 47.54  0  1446 PHE   A CB  1 
ATOM   10954 C CG  . PHE   A 1 1482 ? 152.640 137.000 146.530 1.00 47.62  0  1446 PHE   A CG  1 
ATOM   10955 C CD1 . PHE   A 1 1482 ? 151.607 136.180 146.938 1.00 55.13  0  1446 PHE   A CD1 1 
ATOM   10956 C CD2 . PHE   A 1 1482 ? 152.723 138.274 147.052 1.00 45.65  0  1446 PHE   A CD2 1 
ATOM   10957 C CE1 . PHE   A 1 1482 ? 150.669 136.624 147.843 1.00 56.66  0  1446 PHE   A CE1 1 
ATOM   10958 C CE2 . PHE   A 1 1482 ? 151.791 138.720 147.957 1.00 49.83  0  1446 PHE   A CE2 1 
ATOM   10959 C CZ  . PHE   A 1 1482 ? 150.760 137.894 148.353 1.00 55.23  0  1446 PHE   A CZ  1 
ATOM   10960 N N   . LEU   A 1 1483 ? 156.589 134.467 145.264 1.00 50.66  0  1447 LEU   A N   1 
ATOM   10961 C CA  . LEU   A 1 1483 ? 157.537 134.021 144.258 1.00 53.82  0  1447 LEU   A CA  1 
ATOM   10962 C C   . LEU   A 1 1483 ? 157.108 132.668 143.696 1.00 57.59  0  1447 LEU   A C   1 
ATOM   10963 O O   . LEU   A 1 1483 ? 156.640 131.804 144.444 1.00 56.36  0  1447 LEU   A O   1 
ATOM   10964 C CB  . LEU   A 1 1483 ? 158.942 133.921 144.848 1.00 52.50  0  1447 LEU   A CB  1 
ATOM   10965 C CG  . LEU   A 1 1483 ? 159.754 135.215 144.893 1.00 48.04  0  1447 LEU   A CG  1 
ATOM   10966 C CD1 . LEU   A 1 1483 ? 160.986 135.044 145.759 1.00 51.13  0  1447 LEU   A CD1 1 
ATOM   10967 C CD2 . LEU   A 1 1483 ? 160.143 135.643 143.493 1.00 47.00  0  1447 LEU   A CD2 1 
ATOM   10968 N N   . PRO   A 1 1484 ? 157.251 132.455 142.390 1.00 64.00  0  1448 PRO   A N   1 
ATOM   10969 C CA  . PRO   A 1 1484 ? 156.892 131.157 141.807 1.00 60.99  0  1448 PRO   A CA  1 
ATOM   10970 C C   . PRO   A 1 1484 ? 157.786 130.050 142.342 1.00 59.42  0  1448 PRO   A C   1 
ATOM   10971 O O   . PRO   A 1 1484 ? 158.777 130.284 143.035 1.00 61.72  0  1448 PRO   A O   1 
ATOM   10972 C CB  . PRO   A 1 1484 ? 157.093 131.369 140.303 1.00 58.30  0  1448 PRO   A CB  1 
ATOM   10973 C CG  . PRO   A 1 1484 ? 158.012 132.542 140.199 1.00 58.58  0  1448 PRO   A CG  1 
ATOM   10974 C CD  . PRO   A 1 1484 ? 157.702 133.417 141.371 1.00 56.51  0  1448 PRO   A CD  1 
ATOM   10975 N N   . ASP   A 1 1485 ? 157.411 128.816 142.013 1.00 59.41  0  1449 ASP   A N   1 
ATOM   10976 C CA  . ASP   A 1 1485 ? 158.147 127.659 142.501 1.00 62.01  0  1449 ASP   A CA  1 
ATOM   10977 C C   . ASP   A 1 1485 ? 159.589 127.684 142.010 1.00 62.98  0  1449 ASP   A C   1 
ATOM   10978 O O   . ASP   A 1 1485 ? 159.859 127.921 140.830 1.00 61.95  0  1449 ASP   A O   1 
ATOM   10979 C CB  . ASP   A 1 1485 ? 157.463 126.370 142.048 1.00 61.39  0  1449 ASP   A CB  1 
ATOM   10980 C CG  . ASP   A 1 1485 ? 156.208 126.074 142.831 1.00 61.74  0  1449 ASP   A CG  1 
ATOM   10981 O OD1 . ASP   A 1 1485 ? 156.009 126.705 143.887 1.00 61.68  0  1449 ASP   A OD1 1 
ATOM   10982 O OD2 . ASP   A 1 1485 ? 155.423 125.209 142.391 1.00 63.22  -1 1449 ASP   A OD2 1 
ATOM   10983 N N   . LYS   A 1 1486 ? 160.518 127.443 142.929 1.00 61.07  0  1450 LYS   A N   1 
ATOM   10984 C CA  . LYS   A 1 1486 ? 161.923 127.361 142.564 1.00 60.64  0  1450 LYS   A CA  1 
ATOM   10985 C C   . LYS   A 1 1486 ? 162.204 126.054 141.834 1.00 67.53  0  1450 LYS   A C   1 
ATOM   10986 O O   . LYS   A 1 1486 ? 161.564 125.029 142.078 1.00 70.67  0  1450 LYS   A O   1 
ATOM   10987 C CB  . LYS   A 1 1486 ? 162.805 127.469 143.807 1.00 59.96  0  1450 LYS   A CB  1 
ATOM   10988 C CG  . LYS   A 1 1486 ? 162.767 128.833 144.470 1.00 67.88  0  1450 LYS   A CG  1 
ATOM   10989 C CD  . LYS   A 1 1486 ? 163.707 128.898 145.660 1.00 67.51  0  1450 LYS   A CD  1 
ATOM   10990 C CE  . LYS   A 1 1486 ? 163.706 130.282 146.287 1.00 62.96  0  1450 LYS   A CE  1 
ATOM   10991 N NZ  . LYS   A 1 1486 ? 164.552 130.338 147.510 1.00 62.05  1  1450 LYS   A NZ  1 
ATOM   10992 N N   . ILE   A 1 1487 ? 163.172 126.099 140.922 1.00 63.40  0  1451 ILE   A N   1 
ATOM   10993 C CA  . ILE   A 1 1487 ? 163.592 124.917 140.179 1.00 59.60  0  1451 ILE   A CA  1 
ATOM   10994 C C   . ILE   A 1 1487 ? 164.665 124.225 141.014 1.00 64.71  0  1451 ILE   A C   1 
ATOM   10995 O O   . ILE   A 1 1487 ? 165.813 124.667 141.067 1.00 63.05  0  1451 ILE   A O   1 
ATOM   10996 C CB  . ILE   A 1 1487 ? 164.094 125.272 138.780 1.00 58.55  0  1451 ILE   A CB  1 
ATOM   10997 C CG1 . ILE   A 1 1487 ? 162.951 125.838 137.938 1.00 58.50  0  1451 ILE   A CG1 1 
ATOM   10998 C CG2 . ILE   A 1 1487 ? 164.686 124.052 138.107 1.00 62.68  0  1451 ILE   A CG2 1 
ATOM   10999 C CD1 . ILE   A 1 1487 ? 163.364 126.241 136.547 1.00 62.32  0  1451 ILE   A CD1 1 
ATOM   11000 N N   . SER   A 1 1488 ? 164.283 123.133 141.671 1.00 76.16  0  1452 SER   A N   1 
ATOM   11001 C CA  . SER   A 1 1488 ? 165.191 122.428 142.560 1.00 74.25  0  1452 SER   A CA  1 
ATOM   11002 C C   . SER   A 1 1488 ? 166.305 121.754 141.762 1.00 74.99  0  1452 SER   A C   1 
ATOM   11003 O O   . SER   A 1 1488 ? 166.250 121.633 140.537 1.00 76.29  0  1452 SER   A O   1 
ATOM   11004 C CB  . SER   A 1 1488 ? 164.428 121.394 143.386 1.00 73.73  0  1452 SER   A CB  1 
ATOM   11005 O OG  . SER   A 1 1488 ? 163.828 120.419 142.552 1.00 71.63  0  1452 SER   A OG  1 
ATOM   11006 N N   . LEU   A 1 1489 ? 167.339 121.321 142.485 1.00 79.79  0  1453 LEU   A N   1 
ATOM   11007 C CA  . LEU   A 1 1489 ? 168.473 120.670 141.837 1.00 78.89  0  1453 LEU   A CA  1 
ATOM   11008 C C   . LEU   A 1 1489 ? 168.050 119.371 141.162 1.00 78.51  0  1453 LEU   A C   1 
ATOM   11009 O O   . LEU   A 1 1489 ? 168.457 119.088 140.030 1.00 77.78  0  1453 LEU   A O   1 
ATOM   11010 C CB  . LEU   A 1 1489 ? 169.581 120.415 142.858 1.00 78.02  0  1453 LEU   A CB  1 
ATOM   11011 C CG  . LEU   A 1 1489 ? 170.912 119.923 142.290 1.00 81.09  0  1453 LEU   A CG  1 
ATOM   11012 C CD1 . LEU   A 1 1489 ? 171.324 120.763 141.090 1.00 80.27  0  1453 LEU   A CD1 1 
ATOM   11013 C CD2 . LEU   A 1 1489 ? 171.992 119.947 143.362 1.00 81.72  0  1453 LEU   A CD2 1 
ATOM   11014 N N   . THR   A 1 1490 ? 167.227 118.569 141.843 1.00 78.87  0  1454 THR   A N   1 
ATOM   11015 C CA  . THR   A 1 1490 ? 166.746 117.326 141.249 1.00 78.64  0  1454 THR   A CA  1 
ATOM   11016 C C   . THR   A 1 1490 ? 165.861 117.600 140.041 1.00 78.20  0  1454 THR   A C   1 
ATOM   11017 O O   . THR   A 1 1490 ? 165.912 116.869 139.046 1.00 78.35  0  1454 THR   A O   1 
ATOM   11018 C CB  . THR   A 1 1490 ? 165.982 116.508 142.286 1.00 77.42  0  1454 THR   A CB  1 
ATOM   11019 O OG1 . THR   A 1 1490 ? 164.633 116.981 142.361 1.00 77.19  0  1454 THR   A OG1 1 
ATOM   11020 C CG2 . THR   A 1 1490 ? 166.633 116.649 143.648 1.00 79.88  0  1454 THR   A CG2 1 
ATOM   11021 N N   . GLN   A 1 1491 ? 165.026 118.638 140.119 1.00 69.79  0  1455 GLN   A N   1 
ATOM   11022 C CA  . GLN   A 1 1491 ? 164.182 118.994 138.985 1.00 68.91  0  1455 GLN   A CA  1 
ATOM   11023 C C   . GLN   A 1 1491 ? 165.021 119.403 137.781 1.00 71.73  0  1455 GLN   A C   1 
ATOM   11024 O O   . GLN   A 1 1491 ? 164.729 119.008 136.646 1.00 73.11  0  1455 GLN   A O   1 
ATOM   11025 C CB  . GLN   A 1 1491 ? 163.224 120.114 139.385 1.00 66.04  0  1455 GLN   A CB  1 
ATOM   11026 C CG  . GLN   A 1 1491 ? 162.259 120.525 138.297 1.00 68.65  0  1455 GLN   A CG  1 
ATOM   11027 C CD  . GLN   A 1 1491 ? 161.065 121.270 138.844 1.00 70.63  0  1455 GLN   A CD  1 
ATOM   11028 O OE1 . GLN   A 1 1491 ? 161.104 121.793 139.956 1.00 70.01  0  1455 GLN   A OE1 1 
ATOM   11029 N NE2 . GLN   A 1 1491 ? 159.993 121.322 138.065 1.00 70.30  0  1455 GLN   A NE2 1 
ATOM   11030 N N   . TYR   A 1 1492 ? 166.075 120.188 138.011 1.00 70.65  0  1456 TYR   A N   1 
ATOM   11031 C CA  . TYR   A 1 1492 ? 166.971 120.557 136.921 1.00 65.86  0  1456 TYR   A CA  1 
ATOM   11032 C C   . TYR   A 1 1492 ? 167.685 119.335 136.363 1.00 68.68  0  1456 TYR   A C   1 
ATOM   11033 O O   . TYR   A 1 1492 ? 167.891 119.225 135.149 1.00 69.27  0  1456 TYR   A O   1 
ATOM   11034 C CB  . TYR   A 1 1492 ? 167.984 121.595 137.399 1.00 68.30  0  1456 TYR   A CB  1 
ATOM   11035 C CG  . TYR   A 1 1492 ? 168.717 122.282 136.273 1.00 72.46  0  1456 TYR   A CG  1 
ATOM   11036 C CD1 . TYR   A 1 1492 ? 168.055 123.154 135.423 1.00 72.81  0  1456 TYR   A CD1 1 
ATOM   11037 C CD2 . TYR   A 1 1492 ? 170.066 122.050 136.052 1.00 72.96  0  1456 TYR   A CD2 1 
ATOM   11038 C CE1 . TYR   A 1 1492 ? 168.716 123.783 134.390 1.00 73.32  0  1456 TYR   A CE1 1 
ATOM   11039 C CE2 . TYR   A 1 1492 ? 170.736 122.674 135.019 1.00 70.56  0  1456 TYR   A CE2 1 
ATOM   11040 C CZ  . TYR   A 1 1492 ? 170.055 123.539 134.192 1.00 72.54  0  1456 TYR   A CZ  1 
ATOM   11041 O OH  . TYR   A 1 1492 ? 170.715 124.166 133.162 1.00 72.96  0  1456 TYR   A OH  1 
ATOM   11042 N N   . VAL   A 1 1493 ? 168.075 118.406 137.238 1.00 74.39  0  1457 VAL   A N   1 
ATOM   11043 C CA  . VAL   A 1 1493 ? 168.761 117.195 136.793 1.00 72.40  0  1457 VAL   A CA  1 
ATOM   11044 C C   . VAL   A 1 1493 ? 167.856 116.380 135.877 1.00 74.21  0  1457 VAL   A C   1 
ATOM   11045 O O   . VAL   A 1 1493 ? 168.248 115.990 134.772 1.00 75.98  0  1457 VAL   A O   1 
ATOM   11046 C CB  . VAL   A 1 1493 ? 169.227 116.370 138.004 1.00 70.65  0  1457 VAL   A CB  1 
ATOM   11047 C CG1 . VAL   A 1 1493 ? 169.359 114.913 137.629 1.00 74.41  0  1457 VAL   A CG1 1 
ATOM   11048 C CG2 . VAL   A 1 1493 ? 170.543 116.907 138.532 1.00 72.49  0  1457 VAL   A CG2 1 
ATOM   11049 N N   . GLU   A 1 1494 ? 166.622 116.124 136.321 1.00 80.10  0  1458 GLU   A N   1 
ATOM   11050 C CA  . GLU   A 1 1494 ? 165.670 115.399 135.485 1.00 77.18  0  1458 GLU   A CA  1 
ATOM   11051 C C   . GLU   A 1 1494 ? 165.291 116.183 134.238 1.00 78.90  0  1458 GLU   A C   1 
ATOM   11052 O O   . GLU   A 1 1494 ? 164.825 115.588 133.261 1.00 76.76  0  1458 GLU   A O   1 
ATOM   11053 C CB  . GLU   A 1 1494 ? 164.405 115.060 136.275 1.00 77.35  0  1458 GLU   A CB  1 
ATOM   11054 C CG  . GLU   A 1 1494 ? 164.651 114.426 137.629 1.00 80.87  0  1458 GLU   A CG  1 
ATOM   11055 C CD  . GLU   A 1 1494 ? 163.605 113.388 137.982 1.00 86.61  0  1458 GLU   A CD  1 
ATOM   11056 O OE1 . GLU   A 1 1494 ? 162.684 113.170 137.167 1.00 86.93  0  1458 GLU   A OE1 1 
ATOM   11057 O OE2 . GLU   A 1 1494 ? 163.697 112.796 139.077 1.00 86.23  -1 1458 GLU   A OE2 1 
ATOM   11058 N N   . LEU   A 1 1495 ? 165.477 117.504 134.254 1.00 83.07  0  1459 LEU   A N   1 
ATOM   11059 C CA  . LEU   A 1 1495 ? 165.110 118.320 133.104 1.00 81.29  0  1459 LEU   A CA  1 
ATOM   11060 C C   . LEU   A 1 1495 ? 166.056 118.108 131.928 1.00 79.06  0  1459 LEU   A C   1 
ATOM   11061 O O   . LEU   A 1 1495 ? 165.656 118.308 130.776 1.00 81.46  0  1459 LEU   A O   1 
ATOM   11062 C CB  . LEU   A 1 1495 ? 165.076 119.792 133.517 1.00 78.88  0  1459 LEU   A CB  1 
ATOM   11063 C CG  . LEU   A 1 1495 ? 164.932 120.865 132.442 1.00 76.15  0  1459 LEU   A CG  1 
ATOM   11064 C CD1 . LEU   A 1 1495 ? 164.033 121.979 132.929 1.00 75.90  0  1459 LEU   A CD1 1 
ATOM   11065 C CD2 . LEU   A 1 1495 ? 166.297 121.407 132.072 1.00 78.37  0  1459 LEU   A CD2 1 
ATOM   11066 N N   . PHE   A 1 1496 ? 167.296 117.706 132.195 1.00 71.89  0  1460 PHE   A N   1 
ATOM   11067 C CA  . PHE   A 1 1496 ? 168.342 117.626 131.174 1.00 74.19  0  1460 PHE   A CA  1 
ATOM   11068 C C   . PHE   A 1 1496 ? 168.543 118.989 130.518 1.00 74.95  0  1460 PHE   A C   1 
ATOM   11069 O O   . PHE   A 1 1496 ? 169.109 119.906 131.114 1.00 72.90  0  1460 PHE   A O   1 
ATOM   11070 C CB  . PHE   A 1 1496 ? 168.013 116.574 130.106 1.00 73.77  0  1460 PHE   A CB  1 
ATOM   11071 C CG  . PHE   A 1 1496 ? 168.011 115.159 130.615 1.00 74.63  0  1460 PHE   A CG  1 
ATOM   11072 C CD1 . PHE   A 1 1496 ? 167.537 114.130 129.821 1.00 73.06  0  1460 PHE   A CD1 1 
ATOM   11073 C CD2 . PHE   A 1 1496 ? 168.493 114.855 131.875 1.00 76.63  0  1460 PHE   A CD2 1 
ATOM   11074 C CE1 . PHE   A 1 1496 ? 167.532 112.830 130.280 1.00 73.94  0  1460 PHE   A CE1 1 
ATOM   11075 C CE2 . PHE   A 1 1496 ? 168.489 113.554 132.338 1.00 72.09  0  1460 PHE   A CE2 1 
ATOM   11076 C CZ  . PHE   A 1 1496 ? 168.008 112.542 131.540 1.00 71.68  0  1460 PHE   A CZ  1 
ATOM   11077 N N   . ASN   B 2 128  ? 155.697 65.751  117.540 1.00 128.93 0  128  ASN   B N   1 
ATOM   11078 C CA  . ASN   B 2 128  ? 155.403 66.985  118.258 1.00 129.86 0  128  ASN   B CA  1 
ATOM   11079 C C   . ASN   B 2 128  ? 153.920 67.083  118.593 1.00 130.71 0  128  ASN   B C   1 
ATOM   11080 O O   . ASN   B 2 128  ? 153.365 68.177  118.686 1.00 131.46 0  128  ASN   B O   1 
ATOM   11081 C CB  . ASN   B 2 128  ? 155.839 68.200  117.436 1.00 130.23 0  128  ASN   B CB  1 
ATOM   11082 C CG  . ASN   B 2 128  ? 157.337 68.427  117.482 1.00 131.31 0  128  ASN   B CG  1 
ATOM   11083 O OD1 . ASN   B 2 128  ? 158.000 68.076  118.457 1.00 130.99 0  128  ASN   B OD1 1 
ATOM   11084 N ND2 . ASN   B 2 128  ? 157.878 69.017  116.423 1.00 131.75 0  128  ASN   B ND2 1 
ATOM   11085 N N   . ASP   B 2 129  ? 153.279 65.926  118.770 1.00 128.71 0  129  ASP   B N   1 
ATOM   11086 C CA  . ASP   B 2 129  ? 151.853 65.907  119.077 1.00 127.56 0  129  ASP   B CA  1 
ATOM   11087 C C   . ASP   B 2 129  ? 151.582 66.283  120.529 1.00 126.95 0  129  ASP   B C   1 
ATOM   11088 O O   . ASP   B 2 129  ? 150.579 66.943  120.822 1.00 126.85 0  129  ASP   B O   1 
ATOM   11089 C CB  . ASP   B 2 129  ? 151.266 64.530  118.766 1.00 127.58 0  129  ASP   B CB  1 
ATOM   11090 C CG  . ASP   B 2 129  ? 151.138 64.275  117.276 1.00 127.47 0  129  ASP   B CG  1 
ATOM   11091 O OD1 . ASP   B 2 129  ? 151.268 65.239  116.493 1.00 128.49 0  129  ASP   B OD1 1 
ATOM   11092 O OD2 . ASP   B 2 129  ? 150.907 63.110  116.889 1.00 126.39 -1 129  ASP   B OD2 1 
ATOM   11093 N N   . ASN   B 2 130  ? 152.454 65.867  121.451 1.00 127.45 0  130  ASN   B N   1 
ATOM   11094 C CA  . ASN   B 2 130  ? 152.234 66.170  122.862 1.00 128.41 0  130  ASN   B CA  1 
ATOM   11095 C C   . ASN   B 2 130  ? 152.356 67.661  123.149 1.00 127.75 0  130  ASN   B C   1 
ATOM   11096 O O   . ASN   B 2 130  ? 151.607 68.194  123.977 1.00 126.76 0  130  ASN   B O   1 
ATOM   11097 C CB  . ASN   B 2 130  ? 153.209 65.377  123.730 1.00 127.55 0  130  ASN   B CB  1 
ATOM   11098 C CG  . ASN   B 2 130  ? 152.663 64.019  124.122 1.00 128.30 0  130  ASN   B CG  1 
ATOM   11099 O OD1 . ASN   B 2 130  ? 151.455 63.785  124.071 1.00 127.23 0  130  ASN   B OD1 1 
ATOM   11100 N ND2 . ASN   B 2 130  ? 153.551 63.116  124.519 1.00 128.31 0  130  ASN   B ND2 1 
ATOM   11101 N N   . ILE   B 2 131  ? 153.289 68.346  122.487 1.00 121.37 0  131  ILE   B N   1 
ATOM   11102 C CA  . ILE   B 2 131  ? 153.395 69.793  122.647 1.00 119.77 0  131  ILE   B CA  1 
ATOM   11103 C C   . ILE   B 2 131  ? 152.123 70.471  122.158 1.00 119.68 0  131  ILE   B C   1 
ATOM   11104 O O   . ILE   B 2 131  ? 151.608 71.397  122.796 1.00 122.03 0  131  ILE   B O   1 
ATOM   11105 C CB  . ILE   B 2 131  ? 154.641 70.321  121.913 1.00 120.20 0  131  ILE   B CB  1 
ATOM   11106 C CG1 . ILE   B 2 131  ? 155.911 69.778  122.568 1.00 121.77 0  131  ILE   B CG1 1 
ATOM   11107 C CG2 . ILE   B 2 131  ? 154.657 71.838  121.907 1.00 119.19 0  131  ILE   B CG2 1 
ATOM   11108 C CD1 . ILE   B 2 131  ? 157.138 69.860  121.683 1.00 120.63 0  131  ILE   B CD1 1 
ATOM   11109 N N   . THR   B 2 132  ? 151.593 70.016  121.021 1.00 115.96 0  132  THR   B N   1 
ATOM   11110 C CA  . THR   B 2 132  ? 150.344 70.573  120.512 1.00 117.20 0  132  THR   B CA  1 
ATOM   11111 C C   . THR   B 2 132  ? 149.191 70.312  121.474 1.00 117.64 0  132  THR   B C   1 
ATOM   11112 O O   . THR   B 2 132  ? 148.338 71.180  121.679 1.00 117.50 0  132  THR   B O   1 
ATOM   11113 C CB  . THR   B 2 132  ? 150.036 69.997  119.130 1.00 115.32 0  132  THR   B CB  1 
ATOM   11114 O OG1 . THR   B 2 132  ? 151.139 70.250  118.251 1.00 114.22 0  132  THR   B OG1 1 
ATOM   11115 C CG2 . THR   B 2 132  ? 148.784 70.636  118.552 1.00 114.77 0  132  THR   B CG2 1 
ATOM   11116 N N   . ALA   B 2 133  ? 149.148 69.121  122.077 1.00 118.38 0  133  ALA   B N   1 
ATOM   11117 C CA  . ALA   B 2 133  ? 148.095 68.819  123.042 1.00 117.81 0  133  ALA   B CA  1 
ATOM   11118 C C   . ALA   B 2 133  ? 148.199 69.706  124.278 1.00 118.63 0  133  ALA   B C   1 
ATOM   11119 O O   . ALA   B 2 133  ? 147.181 70.192  124.789 1.00 118.49 0  133  ALA   B O   1 
ATOM   11120 C CB  . ALA   B 2 133  ? 148.148 67.343  123.434 1.00 117.01 0  133  ALA   B CB  1 
ATOM   11121 N N   . ARG   B 2 134  ? 149.418 69.922  124.777 1.00 116.90 0  134  ARG   B N   1 
ATOM   11122 C CA  . ARG   B 2 134  ? 149.607 70.812  125.920 1.00 117.00 0  134  ARG   B CA  1 
ATOM   11123 C C   . ARG   B 2 134  ? 149.176 72.235  125.579 1.00 116.52 0  134  ARG   B C   1 
ATOM   11124 O O   . ARG   B 2 134  ? 148.499 72.905  126.373 1.00 117.00 0  134  ARG   B O   1 
ATOM   11125 C CB  . ARG   B 2 134  ? 151.069 70.788  126.365 1.00 116.92 0  134  ARG   B CB  1 
ATOM   11126 C CG  . ARG   B 2 134  ? 151.499 69.515  127.072 1.00 116.61 0  134  ARG   B CG  1 
ATOM   11127 C CD  . ARG   B 2 134  ? 151.274 69.621  128.570 1.00 116.01 0  134  ARG   B CD  1 
ATOM   11128 N NE  . ARG   B 2 134  ? 152.229 68.821  129.326 1.00 116.42 0  134  ARG   B NE  1 
ATOM   11129 C CZ  . ARG   B 2 134  ? 152.106 67.519  129.548 1.00 117.66 0  134  ARG   B CZ  1 
ATOM   11130 N NH1 . ARG   B 2 134  ? 151.077 66.832  129.079 1.00 118.16 1  134  ARG   B NH1 1 
ATOM   11131 N NH2 . ARG   B 2 134  ? 153.037 66.892  130.261 1.00 117.02 0  134  ARG   B NH2 1 
ATOM   11132 N N   . LEU   B 2 135  ? 149.561 72.710  124.392 1.00 110.98 0  135  LEU   B N   1 
ATOM   11133 C CA  . LEU   B 2 135  ? 149.165 74.047  123.970 1.00 109.70 0  135  LEU   B CA  1 
ATOM   11134 C C   . LEU   B 2 135  ? 147.657 74.156  123.815 1.00 110.51 0  135  LEU   B C   1 
ATOM   11135 O O   . LEU   B 2 135  ? 147.076 75.195  124.139 1.00 111.69 0  135  LEU   B O   1 
ATOM   11136 C CB  . LEU   B 2 135  ? 149.868 74.419  122.666 1.00 108.96 0  135  LEU   B CB  1 
ATOM   11137 C CG  . LEU   B 2 135  ? 151.372 74.679  122.778 1.00 109.28 0  135  LEU   B CG  1 
ATOM   11138 C CD1 . LEU   B 2 135  ? 151.966 75.009  121.419 1.00 109.43 0  135  LEU   B CD1 1 
ATOM   11139 C CD2 . LEU   B 2 135  ? 151.654 75.788  123.775 1.00 107.49 0  135  LEU   B CD2 1 
ATOM   11140 N N   . ASP   B 2 136  ? 147.003 73.098  123.332 1.00 110.55 0  136  ASP   B N   1 
ATOM   11141 C CA  . ASP   B 2 136  ? 145.551 73.120  123.204 1.00 111.86 0  136  ASP   B CA  1 
ATOM   11142 C C   . ASP   B 2 136  ? 144.864 73.118  124.562 1.00 110.47 0  136  ASP   B C   1 
ATOM   11143 O O   . ASP   B 2 136  ? 143.834 73.778  124.732 1.00 110.09 0  136  ASP   B O   1 
ATOM   11144 C CB  . ASP   B 2 136  ? 145.080 71.934  122.364 1.00 113.30 0  136  ASP   B CB  1 
ATOM   11145 C CG  . ASP   B 2 136  ? 145.393 72.106  120.892 1.00 113.10 0  136  ASP   B CG  1 
ATOM   11146 O OD1 . ASP   B 2 136  ? 145.791 73.223  120.497 1.00 112.03 0  136  ASP   B OD1 1 
ATOM   11147 O OD2 . ASP   B 2 136  ? 145.244 71.127  120.131 1.00 110.39 -1 136  ASP   B OD2 1 
ATOM   11148 N N   . ARG   B 2 137  ? 145.408 72.389  125.537 1.00 106.40 0  137  ARG   B N   1 
ATOM   11149 C CA  . ARG   B 2 137  ? 144.850 72.433  126.887 1.00 107.98 0  137  ARG   B CA  1 
ATOM   11150 C C   . ARG   B 2 137  ? 144.982 73.829  127.487 1.00 109.46 0  137  ARG   B C   1 
ATOM   11151 O O   . ARG   B 2 137  ? 144.041 74.353  128.102 1.00 107.07 0  137  ARG   B O   1 
ATOM   11152 C CB  . ARG   B 2 137  ? 145.538 71.395  127.773 1.00 107.44 0  137  ARG   B CB  1 
ATOM   11153 C CG  . ARG   B 2 137  ? 145.164 69.962  127.440 1.00 108.02 0  137  ARG   B CG  1 
ATOM   11154 C CD  . ARG   B 2 137  ? 143.657 69.777  127.454 1.00 107.72 0  137  ARG   B CD  1 
ATOM   11155 N NE  . ARG   B 2 137  ? 143.272 68.395  127.198 1.00 108.79 0  137  ARG   B NE  1 
ATOM   11156 C CZ  . ARG   B 2 137  ? 142.037 68.002  126.918 1.00 107.10 0  137  ARG   B CZ  1 
ATOM   11157 N NH1 . ARG   B 2 137  ? 141.036 68.865  126.850 1.00 105.67 1  137  ARG   B NH1 1 
ATOM   11158 N NH2 . ARG   B 2 137  ? 141.801 66.711  126.698 1.00 106.35 0  137  ARG   B NH2 1 
ATOM   11159 N N   . ILE   B 2 138  ? 146.150 74.451  127.310 1.00 106.59 0  138  ILE   B N   1 
ATOM   11160 C CA  . ILE   B 2 138  ? 146.347 75.814  127.796 1.00 100.76 0  138  ILE   B CA  1 
ATOM   11161 C C   . ILE   B 2 138  ? 145.397 76.774  127.091 1.00 102.82 0  138  ILE   B C   1 
ATOM   11162 O O   . ILE   B 2 138  ? 144.826 77.677  127.714 1.00 107.02 0  138  ILE   B O   1 
ATOM   11163 C CB  . ILE   B 2 138  ? 147.819 76.232  127.624 1.00 101.06 0  138  ILE   B CB  1 
ATOM   11164 C CG1 . ILE   B 2 138  ? 148.681 75.572  128.701 1.00 103.76 0  138  ILE   B CG1 1 
ATOM   11165 C CG2 . ILE   B 2 138  ? 147.964 77.742  127.662 1.00 102.61 0  138  ILE   B CG2 1 
ATOM   11166 C CD1 . ILE   B 2 138  ? 150.163 75.681  128.443 1.00 106.28 0  138  ILE   B CD1 1 
ATOM   11167 N N   . ASP   B 2 139  ? 145.210 76.592  125.782 1.00 100.23 0  139  ASP   B N   1 
ATOM   11168 C CA  . ASP   B 2 139  ? 144.289 77.439  125.035 1.00 101.14 0  139  ASP   B CA  1 
ATOM   11169 C C   . ASP   B 2 139  ? 142.858 77.274  125.528 1.00 101.30 0  139  ASP   B C   1 
ATOM   11170 O O   . ASP   B 2 139  ? 142.110 78.251  125.612 1.00 102.55 0  139  ASP   B O   1 
ATOM   11171 C CB  . ASP   B 2 139  ? 144.380 77.125  123.544 1.00 100.60 0  139  ASP   B CB  1 
ATOM   11172 C CG  . ASP   B 2 139  ? 143.437 77.971  122.715 1.00 101.79 0  139  ASP   B CG  1 
ATOM   11173 O OD1 . ASP   B 2 139  ? 143.668 79.194  122.610 1.00 101.51 0  139  ASP   B OD1 1 
ATOM   11174 O OD2 . ASP   B 2 139  ? 142.463 77.414  122.169 1.00 102.70 -1 139  ASP   B OD2 1 
ATOM   11175 N N   . GLU   B 2 140  ? 142.454 76.044  125.848 1.00 97.67  0  140  GLU   B N   1 
ATOM   11176 C CA  . GLU   B 2 140  ? 141.111 75.825  126.375 1.00 96.94  0  140  GLU   B CA  1 
ATOM   11177 C C   . GLU   B 2 140  ? 140.933 76.500  127.729 1.00 96.28  0  140  GLU   B C   1 
ATOM   11178 O O   . GLU   B 2 140  ? 139.884 77.098  127.998 1.00 97.26  0  140  GLU   B O   1 
ATOM   11179 C CB  . GLU   B 2 140  ? 140.821 74.328  126.479 1.00 98.72  0  140  GLU   B CB  1 
ATOM   11180 C CG  . GLU   B 2 140  ? 139.406 74.008  126.932 1.00 98.46  0  140  GLU   B CG  1 
ATOM   11181 C CD  . GLU   B 2 140  ? 138.842 72.774  126.258 1.00 99.90  0  140  GLU   B CD  1 
ATOM   11182 O OE1 . GLU   B 2 140  ? 139.350 72.397  125.181 1.00 98.86  0  140  GLU   B OE1 1 
ATOM   11183 O OE2 . GLU   B 2 140  ? 137.890 72.180  126.805 1.00 98.73  -1 140  GLU   B OE2 1 
ATOM   11184 N N   . LYS   B 2 141  ? 141.943 76.411  128.597 1.00 97.50  0  141  LYS   B N   1 
ATOM   11185 C CA  . LYS   B 2 141  ? 141.855 77.092  129.888 1.00 99.08  0  141  LYS   B CA  1 
ATOM   11186 C C   . LYS   B 2 141  ? 141.764 78.606  129.710 1.00 98.01  0  141  LYS   B C   1 
ATOM   11187 O O   . LYS   B 2 141  ? 140.968 79.276  130.385 1.00 96.19  0  141  LYS   B O   1 
ATOM   11188 C CB  . LYS   B 2 141  ? 143.052 76.721  130.761 1.00 100.86 0  141  LYS   B CB  1 
ATOM   11189 C CG  . LYS   B 2 141  ? 142.813 75.527  131.670 1.00 101.06 0  141  LYS   B CG  1 
ATOM   11190 C CD  . LYS   B 2 141  ? 143.991 75.302  132.605 1.00 100.09 0  141  LYS   B CD  1 
ATOM   11191 C CE  . LYS   B 2 141  ? 143.590 74.496  133.830 1.00 97.78  0  141  LYS   B CE  1 
ATOM   11192 N NZ  . LYS   B 2 141  ? 143.068 73.150  133.472 1.00 97.17  1  141  LYS   B NZ  1 
ATOM   11193 N N   . LEU   B 2 142  ? 142.568 79.160  128.799 1.00 93.12  0  142  LEU   B N   1 
ATOM   11194 C CA  . LEU   B 2 142  ? 142.500 80.591  128.517 1.00 89.52  0  142  LEU   B CA  1 
ATOM   11195 C C   . LEU   B 2 142  ? 141.136 80.981  127.967 1.00 89.64  0  142  LEU   B C   1 
ATOM   11196 O O   . LEU   B 2 142  ? 140.590 82.030  128.326 1.00 91.44  0  142  LEU   B O   1 
ATOM   11197 C CB  . LEU   B 2 142  ? 143.596 80.983  127.529 1.00 88.09  0  142  LEU   B CB  1 
ATOM   11198 C CG  . LEU   B 2 142  ? 144.848 81.633  128.107 1.00 87.91  0  142  LEU   B CG  1 
ATOM   11199 C CD1 . LEU   B 2 142  ? 145.620 80.634  128.929 1.00 87.68  0  142  LEU   B CD1 1 
ATOM   11200 C CD2 . LEU   B 2 142  ? 145.711 82.176  126.989 1.00 90.76  0  142  LEU   B CD2 1 
ATOM   11201 N N   . SER   B 2 143  ? 140.580 80.154  127.080 1.00 85.43  0  143  SER   B N   1 
ATOM   11202 C CA  . SER   B 2 143  ? 139.263 80.432  126.523 1.00 84.88  0  143  SER   B CA  1 
ATOM   11203 C C   . SER   B 2 143  ? 138.196 80.415  127.605 1.00 85.94  0  143  SER   B C   1 
ATOM   11204 O O   . SER   B 2 143  ? 137.290 81.252  127.602 1.00 86.12  0  143  SER   B O   1 
ATOM   11205 C CB  . SER   B 2 143  ? 138.934 79.419  125.428 1.00 85.95  0  143  SER   B CB  1 
ATOM   11206 O OG  . SER   B 2 143  ? 137.604 79.580  124.971 1.00 88.09  0  143  SER   B OG  1 
ATOM   11207 N N   . GLU   B 2 144  ? 138.283 79.467  128.539 1.00 89.67  0  144  GLU   B N   1 
ATOM   11208 C CA  . GLU   B 2 144  ? 137.324 79.433  129.640 1.00 87.67  0  144  GLU   B CA  1 
ATOM   11209 C C   . GLU   B 2 144  ? 137.435 80.680  130.510 1.00 88.76  0  144  GLU   B C   1 
ATOM   11210 O O   . GLU   B 2 144  ? 136.415 81.280  130.878 1.00 89.23  0  144  GLU   B O   1 
ATOM   11211 C CB  . GLU   B 2 144  ? 137.529 78.172  130.476 1.00 90.28  0  144  GLU   B CB  1 
ATOM   11212 C CG  . GLU   B 2 144  ? 136.637 78.091  131.703 1.00 90.10  0  144  GLU   B CG  1 
ATOM   11213 C CD  . GLU   B 2 144  ? 136.543 76.686  132.261 1.00 92.06  0  144  GLU   B CD  1 
ATOM   11214 O OE1 . GLU   B 2 144  ? 136.906 75.733  131.541 1.00 91.06  0  144  GLU   B OE1 1 
ATOM   11215 O OE2 . GLU   B 2 144  ? 136.104 76.532  133.420 1.00 92.33  -1 144  GLU   B OE2 1 
ATOM   11216 N N   . ILE   B 2 145  ? 138.663 81.097  130.833 1.00 88.47  0  145  ILE   B N   1 
ATOM   11217 C CA  . ILE   B 2 145  ? 138.845 82.290  131.660 1.00 85.39  0  145  ILE   B CA  1 
ATOM   11218 C C   . ILE   B 2 145  ? 138.294 83.522  130.951 1.00 82.03  0  145  ILE   B C   1 
ATOM   11219 O O   . ILE   B 2 145  ? 137.581 84.337  131.548 1.00 84.43  0  145  ILE   B O   1 
ATOM   11220 C CB  . ILE   B 2 145  ? 140.327 82.472  132.032 1.00 82.91  0  145  ILE   B CB  1 
ATOM   11221 C CG1 . ILE   B 2 145  ? 140.717 81.515  133.155 1.00 84.86  0  145  ILE   B CG1 1 
ATOM   11222 C CG2 . ILE   B 2 145  ? 140.600 83.901  132.458 1.00 78.87  0  145  ILE   B CG2 1 
ATOM   11223 C CD1 . ILE   B 2 145  ? 142.205 81.354  133.323 1.00 86.83  0  145  ILE   B CD1 1 
ATOM   11224 N N   . LEU   B 2 146  ? 138.614 83.674  129.664 1.00 71.76  0  146  LEU   B N   1 
ATOM   11225 C CA  . LEU   B 2 146  ? 138.146 84.841  128.926 1.00 72.21  0  146  LEU   B CA  1 
ATOM   11226 C C   . LEU   B 2 146  ? 136.633 84.826  128.757 1.00 76.15  0  146  LEU   B C   1 
ATOM   11227 O O   . LEU   B 2 146  ? 135.986 85.875  128.844 1.00 84.01  0  146  LEU   B O   1 
ATOM   11228 C CB  . LEU   B 2 146  ? 138.835 84.922  127.566 1.00 71.76  0  146  LEU   B CB  1 
ATOM   11229 C CG  . LEU   B 2 146  ? 140.093 85.788  127.526 1.00 71.34  0  146  LEU   B CG  1 
ATOM   11230 C CD1 . LEU   B 2 146  ? 140.673 85.815  126.128 1.00 74.70  0  146  LEU   B CD1 1 
ATOM   11231 C CD2 . LEU   B 2 146  ? 139.783 87.191  128.002 1.00 74.18  0  146  LEU   B CD2 1 
ATOM   11232 N N   . GLY   B 2 147  ? 136.048 83.654  128.507 1.00 77.08  0  147  GLY   B N   1 
ATOM   11233 C CA  . GLY   B 2 147  ? 134.606 83.568  128.395 1.00 78.99  0  147  GLY   B CA  1 
ATOM   11234 C C   . GLY   B 2 147  ? 133.894 83.894  129.688 1.00 77.71  0  147  GLY   B C   1 
ATOM   11235 O O   . GLY   B 2 147  ? 132.812 84.486  129.671 1.00 77.73  0  147  GLY   B O   1 
ATOM   11236 N N   . MET   B 2 148  ? 134.479 83.514  130.825 1.00 78.12  0  148  MET   B N   1 
ATOM   11237 C CA  . MET   B 2 148  ? 133.875 83.895  132.093 1.00 77.55  0  148  MET   B CA  1 
ATOM   11238 C C   . MET   B 2 148  ? 134.031 85.387  132.363 1.00 82.55  0  148  MET   B C   1 
ATOM   11239 O O   . MET   B 2 148  ? 133.084 86.030  132.831 1.00 83.72  0  148  MET   B O   1 
ATOM   11240 C CB  . MET   B 2 148  ? 134.491 83.105  133.242 1.00 79.74  0  148  MET   B CB  1 
ATOM   11241 C CG  . MET   B 2 148  ? 134.240 83.746  134.586 1.00 83.42  0  148  MET   B CG  1 
ATOM   11242 S SD  . MET   B 2 148  ? 135.473 83.331  135.814 1.00 92.72  0  148  MET   B SD  1 
ATOM   11243 C CE  . MET   B 2 148  ? 136.477 84.799  135.656 1.00 78.85  0  148  MET   B CE  1 
ATOM   11244 N N   . LEU   B 2 149  ? 135.209 85.952  132.080 1.00 79.29  0  149  LEU   B N   1 
ATOM   11245 C CA  . LEU   B 2 149  ? 135.457 87.366  132.353 1.00 75.18  0  149  LEU   B CA  1 
ATOM   11246 C C   . LEU   B 2 149  ? 134.602 88.274  131.477 1.00 75.17  0  149  LEU   B C   1 
ATOM   11247 O O   . LEU   B 2 149  ? 134.049 89.268  131.958 1.00 78.72  0  149  LEU   B O   1 
ATOM   11248 C CB  . LEU   B 2 149  ? 136.937 87.694  132.154 1.00 70.30  0  149  LEU   B CB  1 
ATOM   11249 C CG  . LEU   B 2 149  ? 137.891 87.453  133.322 1.00 72.89  0  149  LEU   B CG  1 
ATOM   11250 C CD1 . LEU   B 2 149  ? 139.307 87.795  132.909 1.00 71.28  0  149  LEU   B CD1 1 
ATOM   11251 C CD2 . LEU   B 2 149  ? 137.479 88.257  134.537 1.00 75.01  0  149  LEU   B CD2 1 
ATOM   11252 N N   . HIS   B 2 150  ? 134.484 87.950  130.188 1.00 74.93  0  150  HIS   B N   1 
ATOM   11253 C CA  . HIS   B 2 150  ? 133.776 88.825  129.261 1.00 74.31  0  150  HIS   B CA  1 
ATOM   11254 C C   . HIS   B 2 150  ? 132.303 88.977  129.613 1.00 78.63  0  150  HIS   B C   1 
ATOM   11255 O O   . HIS   B 2 150  ? 131.669 89.939  129.168 1.00 81.76  0  150  HIS   B O   1 
ATOM   11256 C CB  . HIS   B 2 150  ? 133.915 88.298  127.834 1.00 78.68  0  150  HIS   B CB  1 
ATOM   11257 C CG  . HIS   B 2 150  ? 133.861 89.367  126.787 1.00 82.89  0  150  HIS   B CG  1 
ATOM   11258 N ND1 . HIS   B 2 150  ? 134.994 89.931  126.240 1.00 81.98  0  150  HIS   B ND1 1 
ATOM   11259 C CD2 . HIS   B 2 150  ? 132.811 89.977  126.188 1.00 79.12  0  150  HIS   B CD2 1 
ATOM   11260 C CE1 . HIS   B 2 150  ? 134.645 90.841  125.349 1.00 81.66  0  150  HIS   B CE1 1 
ATOM   11261 N NE2 . HIS   B 2 150  ? 133.326 90.889  125.298 1.00 83.27  0  150  HIS   B NE2 1 
ATOM   11262 N N   . THR   B 2 151  ? 131.745 88.055  130.395 1.00 77.64  0  151  THR   B N   1 
ATOM   11263 C CA  . THR   B 2 151  ? 130.350 88.109  130.804 1.00 78.31  0  151  THR   B CA  1 
ATOM   11264 C C   . THR   B 2 151  ? 130.176 88.583  132.241 1.00 76.67  0  151  THR   B C   1 
ATOM   11265 O O   . THR   B 2 151  ? 129.105 88.387  132.821 1.00 79.18  0  151  THR   B O   1 
ATOM   11266 C CB  . THR   B 2 151  ? 129.695 86.738  130.633 1.00 78.08  0  151  THR   B CB  1 
ATOM   11267 O OG1 . THR   B 2 151  ? 130.163 85.853  131.658 1.00 79.43  0  151  THR   B OG1 1 
ATOM   11268 C CG2 . THR   B 2 151  ? 130.038 86.152  129.275 1.00 78.02  0  151  THR   B CG2 1 
ATOM   11269 N N   . LEU   B 2 152  ? 131.200 89.194  132.828 1.00 63.58  0  152  LEU   B N   1 
ATOM   11270 C CA  . LEU   B 2 152  ? 131.149 89.623  134.219 1.00 66.88  0  152  LEU   B CA  1 
ATOM   11271 C C   . LEU   B 2 152  ? 130.450 90.972  134.322 1.00 68.86  0  152  LEU   B C   1 
ATOM   11272 O O   . LEU   B 2 152  ? 130.801 91.916  133.607 1.00 64.32  0  152  LEU   B O   1 
ATOM   11273 C CB  . LEU   B 2 152  ? 132.558 89.709  134.803 1.00 64.09  0  152  LEU   B CB  1 
ATOM   11274 C CG  . LEU   B 2 152  ? 132.674 89.557  136.317 1.00 65.01  0  152  LEU   B CG  1 
ATOM   11275 C CD1 . LEU   B 2 152  ? 132.473 88.110  136.702 1.00 68.31  0  152  LEU   B CD1 1 
ATOM   11276 C CD2 . LEU   B 2 152  ? 134.018 90.054  136.803 1.00 67.91  0  152  LEU   B CD2 1 
ATOM   11277 N N   . VAL   B 2 153  ? 129.467 91.060  135.215 1.00 72.99  0  153  VAL   B N   1 
ATOM   11278 C CA  . VAL   B 2 153  ? 128.691 92.274  135.433 1.00 68.61  0  153  VAL   B CA  1 
ATOM   11279 C C   . VAL   B 2 153  ? 129.114 92.886  136.761 1.00 70.50  0  153  VAL   B C   1 
ATOM   11280 O O   . VAL   B 2 153  ? 129.146 92.199  137.793 1.00 68.85  0  153  VAL   B O   1 
ATOM   11281 C CB  . VAL   B 2 153  ? 127.179 91.993  135.409 1.00 66.12  0  153  VAL   B CB  1 
ATOM   11282 C CG1 . VAL   B 2 153  ? 126.432 93.020  136.236 1.00 65.94  0  153  VAL   B CG1 1 
ATOM   11283 C CG2 . VAL   B 2 153  ? 126.668 91.998  133.984 1.00 68.69  0  153  VAL   B CG2 1 
ATOM   11284 N N   . VAL   B 2 154  ? 129.439 94.178  136.728 1.00 68.64  0  154  VAL   B N   1 
ATOM   11285 C CA  . VAL   B 2 154  ? 129.858 94.938  137.899 1.00 67.15  0  154  VAL   B CA  1 
ATOM   11286 C C   . VAL   B 2 154  ? 128.689 95.797  138.355 1.00 66.58  0  154  VAL   B C   1 
ATOM   11287 O O   . VAL   B 2 154  ? 128.088 96.519  137.550 1.00 68.02  0  154  VAL   B O   1 
ATOM   11288 C CB  . VAL   B 2 154  ? 131.084 95.812  137.584 1.00 57.39  0  154  VAL   B CB  1 
ATOM   11289 C CG1 . VAL   B 2 154  ? 131.621 96.453  138.849 1.00 59.39  0  154  VAL   B CG1 1 
ATOM   11290 C CG2 . VAL   B 2 154  ? 132.157 94.996  136.887 1.00 56.36  0  154  VAL   B CG2 1 
ATOM   11291 N N   . ALA   B 2 155  ? 128.362 95.721  139.640 1.00 59.49  0  155  ALA   B N   1 
ATOM   11292 C CA  . ALA   B 2 155  ? 127.310 96.537  140.225 1.00 54.18  0  155  ALA   B CA  1 
ATOM   11293 C C   . ALA   B 2 155  ? 127.925 97.723  140.953 1.00 57.47  0  155  ALA   B C   1 
ATOM   11294 O O   . ALA   B 2 155  ? 128.950 97.586  141.625 1.00 60.16  0  155  ALA   B O   1 
ATOM   11295 C CB  . ALA   B 2 155  ? 126.452 95.718  141.189 1.00 58.72  0  155  ALA   B CB  1 
ATOM   11296 N N   . SER   B 2 156  ? 127.293 98.885  140.814 1.00 58.14  0  156  SER   B N   1 
ATOM   11297 C CA  . SER   B 2 156  ? 127.796 100.097 141.440 1.00 57.53  0  156  SER   B CA  1 
ATOM   11298 C C   . SER   B 2 156  ? 127.751 99.975  142.962 1.00 57.44  0  156  SER   B C   1 
ATOM   11299 O O   . SER   B 2 156  ? 127.007 99.175  143.533 1.00 58.77  0  156  SER   B O   1 
ATOM   11300 C CB  . SER   B 2 156  ? 126.989 101.309 140.982 1.00 57.07  0  156  SER   B CB  1 
ATOM   11301 O OG  . SER   B 2 156  ? 127.014 102.337 141.956 1.00 55.99  0  156  SER   B OG  1 
ATOM   11302 N N   . ALA   B 2 157  ? 128.571 100.787 143.620 1.00 55.56  0  157  ALA   B N   1 
ATOM   11303 C CA  . ALA   B 2 157  ? 128.694 100.759 145.077 1.00 59.61  0  157  ALA   B CA  1 
ATOM   11304 C C   . ALA   B 2 157  ? 127.657 101.651 145.750 1.00 58.04  0  157  ALA   B C   1 
ATOM   11305 O O   . ALA   B 2 157  ? 127.985 102.497 146.575 1.00 54.82  0  157  ALA   B O   1 
ATOM   11306 C CB  . ALA   B 2 157  ? 130.105 101.164 145.484 1.00 58.58  0  157  ALA   B CB  1 
ATOM   11307 N N   . GLY   B 2 158  ? 126.386 101.441 145.424 1.00 61.80  0  158  GLY   B N   1 
ATOM   11308 C CA  . GLY   B 2 158  ? 125.324 102.288 145.911 1.00 63.86  0  158  GLY   B CA  1 
ATOM   11309 C C   . GLY   B 2 158  ? 125.041 102.113 147.390 1.00 66.53  0  158  GLY   B C   1 
ATOM   11310 O O   . GLY   B 2 158  ? 125.749 101.399 148.106 1.00 67.30  0  158  GLY   B O   1 
ATOM   11311 N N   . PRO   B 2 159  ? 124.002 102.785 147.877 1.00 64.98  0  159  PRO   B N   1 
ATOM   11312 C CA  . PRO   B 2 159  ? 123.643 102.673 149.293 1.00 60.67  0  159  PRO   B CA  1 
ATOM   11313 C C   . PRO   B 2 159  ? 123.107 101.290 149.628 1.00 66.99  0  159  PRO   B C   1 
ATOM   11314 O O   . PRO   B 2 159  ? 122.573 100.571 148.781 1.00 65.57  0  159  PRO   B O   1 
ATOM   11315 C CB  . PRO   B 2 159  ? 122.560 103.742 149.479 1.00 61.00  0  159  PRO   B CB  1 
ATOM   11316 C CG  . PRO   B 2 159  ? 122.595 104.577 148.232 1.00 62.56  0  159  PRO   B CG  1 
ATOM   11317 C CD  . PRO   B 2 159  ? 123.103 103.693 147.150 1.00 62.20  0  159  PRO   B CD  1 
ATOM   11318 N N   . THR   B 2 160  ? 123.257 100.927 150.898 1.00 74.43  0  160  THR   B N   1 
ATOM   11319 C CA  . THR   B 2 160  ? 122.796 99.638  151.385 1.00 76.79  0  160  THR   B CA  1 
ATOM   11320 C C   . THR   B 2 160  ? 121.292 99.684  151.650 1.00 73.92  0  160  THR   B C   1 
ATOM   11321 O O   . THR   B 2 160  ? 120.633 100.713 151.482 1.00 72.16  0  160  THR   B O   1 
ATOM   11322 C CB  . THR   B 2 160  ? 123.562 99.242  152.646 1.00 73.99  0  160  THR   B CB  1 
ATOM   11323 O OG1 . THR   B 2 160  ? 123.319 97.862  152.945 1.00 77.10  0  160  THR   B OG1 1 
ATOM   11324 C CG2 . THR   B 2 160  ? 123.121 100.090 153.823 1.00 67.82  0  160  THR   B CG2 1 
ATOM   11325 N N   . SER   B 2 161  ? 120.738 98.546  152.058 1.00 75.48  0  161  SER   B N   1 
ATOM   11326 C CA  . SER   B 2 161  ? 119.338 98.498  152.446 1.00 74.89  0  161  SER   B CA  1 
ATOM   11327 C C   . SER   B 2 161  ? 119.114 99.315  153.713 1.00 74.52  0  161  SER   B C   1 
ATOM   11328 O O   . SER   B 2 161  ? 120.004 99.450  154.558 1.00 74.40  0  161  SER   B O   1 
ATOM   11329 C CB  . SER   B 2 161  ? 118.890 97.052  152.662 1.00 75.45  0  161  SER   B CB  1 
ATOM   11330 O OG  . SER   B 2 161  ? 118.924 96.322  151.447 1.00 75.68  0  161  SER   B OG  1 
ATOM   11331 N N   . ALA   B 2 162  ? 117.913 99.880  153.827 1.00 67.27  0  162  ALA   B N   1 
ATOM   11332 C CA  . ALA   B 2 162  ? 117.509 100.778 154.906 1.00 68.95  0  162  ALA   B CA  1 
ATOM   11333 C C   . ALA   B 2 162  ? 118.303 102.078 154.918 1.00 71.14  0  162  ALA   B C   1 
ATOM   11334 O O   . ALA   B 2 162  ? 118.116 102.900 155.824 1.00 68.41  0  162  ALA   B O   1 
ATOM   11335 C CB  . ALA   B 2 162  ? 117.600 100.100 156.279 1.00 67.77  0  162  ALA   B CB  1 
ATOM   11336 N N   . ARG   B 2 163  ? 119.180 102.283 153.934 1.00 65.86  0  163  ARG   B N   1 
ATOM   11337 C CA  . ARG   B 2 163  ? 119.936 103.522 153.768 1.00 58.26  0  163  ARG   B CA  1 
ATOM   11338 C C   . ARG   B 2 163  ? 120.668 103.910 155.050 1.00 61.07  0  163  ARG   B C   1 
ATOM   11339 O O   . ARG   B 2 163  ? 120.626 105.056 155.499 1.00 59.75  0  163  ARG   B O   1 
ATOM   11340 C CB  . ARG   B 2 163  ? 119.026 104.653 153.291 1.00 60.26  0  163  ARG   B CB  1 
ATOM   11341 C CG  . ARG   B 2 163  ? 118.377 104.392 151.945 1.00 60.80  0  163  ARG   B CG  1 
ATOM   11342 C CD  . ARG   B 2 163  ? 117.529 105.571 151.508 1.00 62.30  0  163  ARG   B CD  1 
ATOM   11343 N NE  . ARG   B 2 163  ? 118.338 106.740 151.187 1.00 64.02  0  163  ARG   B NE  1 
ATOM   11344 C CZ  . ARG   B 2 163  ? 118.792 107.026 149.975 1.00 62.58  0  163  ARG   B CZ  1 
ATOM   11345 N NH1 . ARG   B 2 163  ? 118.531 106.247 148.938 1.00 64.16  1  163  ARG   B NH1 1 
ATOM   11346 N NH2 . ARG   B 2 163  ? 119.521 108.124 149.797 1.00 56.18  0  163  ARG   B NH2 1 
ATOM   11347 N N   . ASP   B 2 164  ? 121.325 102.924 155.662 1.00 66.01  0  164  ASP   B N   1 
ATOM   11348 C CA  . ASP   B 2 164  ? 122.212 103.148 156.806 1.00 64.78  0  164  ASP   B CA  1 
ATOM   11349 C C   . ASP   B 2 164  ? 123.506 102.394 156.518 1.00 64.03  0  164  ASP   B C   1 
ATOM   11350 O O   . ASP   B 2 164  ? 123.685 101.252 156.945 1.00 69.65  0  164  ASP   B O   1 
ATOM   11351 C CB  . ASP   B 2 164  ? 121.563 102.702 158.110 1.00 61.43  0  164  ASP   B CB  1 
ATOM   11352 C CG  . ASP   B 2 164  ? 122.170 103.381 159.320 1.00 62.77  0  164  ASP   B CG  1 
ATOM   11353 O OD1 . ASP   B 2 164  ? 123.270 103.954 159.188 1.00 62.09  0  164  ASP   B OD1 1 
ATOM   11354 O OD2 . ASP   B 2 164  ? 121.546 103.349 160.402 1.00 63.28  -1 164  ASP   B OD2 1 
ATOM   11355 N N   . GLY   B 2 165  ? 124.410 103.044 155.799 1.00 54.95  0  165  GLY   B N   1 
ATOM   11356 C CA  . GLY   B 2 165  ? 125.655 102.436 155.375 1.00 55.63  0  165  GLY   B CA  1 
ATOM   11357 C C   . GLY   B 2 165  ? 125.800 102.450 153.867 1.00 57.17  0  165  GLY   B C   1 
ATOM   11358 O O   . GLY   B 2 165  ? 124.875 102.760 153.120 1.00 60.49  0  165  GLY   B O   1 
ATOM   11359 N N   . ILE   B 2 166  ? 127.003 102.096 153.432 1.00 62.92  0  166  ILE   B N   1 
ATOM   11360 C CA  . ILE   B 2 166  ? 127.364 102.082 152.021 1.00 64.60  0  166  ILE   B CA  1 
ATOM   11361 C C   . ILE   B 2 166  ? 127.887 100.696 151.670 1.00 68.47  0  166  ILE   B C   1 
ATOM   11362 O O   . ILE   B 2 166  ? 128.647 100.096 152.439 1.00 68.51  0  166  ILE   B O   1 
ATOM   11363 C CB  . ILE   B 2 166  ? 128.401 103.180 151.699 1.00 65.24  0  166  ILE   B CB  1 
ATOM   11364 C CG1 . ILE   B 2 166  ? 128.791 103.150 150.223 1.00 66.86  0  166  ILE   B CG1 1 
ATOM   11365 C CG2 . ILE   B 2 166  ? 129.627 103.054 152.594 1.00 63.39  0  166  ILE   B CG2 1 
ATOM   11366 C CD1 . ILE   B 2 166  ? 129.509 104.398 149.775 1.00 65.54  0  166  ILE   B CD1 1 
ATOM   11367 N N   . ARG   B 2 167  ? 127.459 100.177 150.525 1.00 77.99  0  167  ARG   B N   1 
ATOM   11368 C CA  . ARG   B 2 167  ? 127.812 98.830  150.105 1.00 77.36  0  167  ARG   B CA  1 
ATOM   11369 C C   . ARG   B 2 167  ? 129.035 98.844  149.196 1.00 80.25  0  167  ARG   B C   1 
ATOM   11370 O O   . ARG   B 2 167  ? 129.439 99.877  148.656 1.00 81.14  0  167  ARG   B O   1 
ATOM   11371 C CB  . ARG   B 2 167  ? 126.634 98.156  149.399 1.00 72.76  0  167  ARG   B CB  1 
ATOM   11372 C CG  . ARG   B 2 167  ? 125.731 97.386  150.336 1.00 74.58  0  167  ARG   B CG  1 
ATOM   11373 C CD  . ARG   B 2 167  ? 124.872 96.379  149.592 1.00 80.75  0  167  ARG   B CD  1 
ATOM   11374 N NE  . ARG   B 2 167  ? 123.726 97.003  148.943 1.00 81.54  0  167  ARG   B NE  1 
ATOM   11375 C CZ  . ARG   B 2 167  ? 122.567 96.396  148.733 1.00 82.23  0  167  ARG   B CZ  1 
ATOM   11376 N NH1 . ARG   B 2 167  ? 122.358 95.151  149.129 1.00 80.87  1  167  ARG   B NH1 1 
ATOM   11377 N NH2 . ARG   B 2 167  ? 121.591 97.055  148.115 1.00 81.20  0  167  ARG   B NH2 1 
ATOM   11378 N N   . ASP   B 2 168  ? 129.625 97.664  149.033 1.00 75.98  0  168  ASP   B N   1 
ATOM   11379 C CA  . ASP   B 2 168  ? 130.806 97.487  148.207 1.00 72.48  0  168  ASP   B CA  1 
ATOM   11380 C C   . ASP   B 2 168  ? 130.412 97.335  146.739 1.00 70.88  0  168  ASP   B C   1 
ATOM   11381 O O   . ASP   B 2 168  ? 129.248 97.119  146.394 1.00 69.54  0  168  ASP   B O   1 
ATOM   11382 C CB  . ASP   B 2 168  ? 131.603 96.273  148.681 1.00 77.04  0  168  ASP   B CB  1 
ATOM   11383 C CG  . ASP   B 2 168  ? 133.071 96.357  148.318 1.00 78.65  0  168  ASP   B CG  1 
ATOM   11384 O OD1 . ASP   B 2 168  ? 133.462 97.329  147.639 1.00 78.80  0  168  ASP   B OD1 1 
ATOM   11385 O OD2 . ASP   B 2 168  ? 133.834 95.449  148.710 1.00 79.35  -1 168  ASP   B OD2 1 
ATOM   11386 N N   . ALA   B 2 169  ? 131.411 97.452  145.864 1.00 72.05  0  169  ALA   B N   1 
ATOM   11387 C CA  . ALA   B 2 169  ? 131.208 97.312  144.423 1.00 72.56  0  169  ALA   B CA  1 
ATOM   11388 C C   . ALA   B 2 169  ? 131.230 95.828  144.072 1.00 75.76  0  169  ALA   B C   1 
ATOM   11389 O O   . ALA   B 2 169  ? 132.210 95.288  143.554 1.00 75.79  0  169  ALA   B O   1 
ATOM   11390 C CB  . ALA   B 2 169  ? 132.269 98.086  143.654 1.00 72.18  0  169  ALA   B CB  1 
ATOM   11391 N N   . MET   B 2 170  ? 130.118 95.160  144.363 1.00 81.74  0  170  MET   B N   1 
ATOM   11392 C CA  . MET   B 2 170  ? 130.030 93.724  144.143 1.00 82.09  0  170  MET   B CA  1 
ATOM   11393 C C   . MET   B 2 170  ? 130.017 93.402  142.652 1.00 83.54  0  170  MET   B C   1 
ATOM   11394 O O   . MET   B 2 170  ? 129.609 94.215  141.819 1.00 82.50  0  170  MET   B O   1 
ATOM   11395 C CB  . MET   B 2 170  ? 128.778 93.156  144.812 1.00 81.61  0  170  MET   B CB  1 
ATOM   11396 C CG  . MET   B 2 170  ? 127.482 93.786  144.341 1.00 81.82  0  170  MET   B CG  1 
ATOM   11397 S SD  . MET   B 2 170  ? 126.034 92.961  145.022 1.00 85.69  0  170  MET   B SD  1 
ATOM   11398 C CE  . MET   B 2 170  ? 126.431 92.980  146.768 1.00 82.49  0  170  MET   B CE  1 
ATOM   11399 N N   . ILE   B 2 171  ? 130.478 92.195  142.322 1.00 89.41  0  171  ILE   B N   1 
ATOM   11400 C CA  . ILE   B 2 171  ? 130.528 91.716  140.948 1.00 87.68  0  171  ILE   B CA  1 
ATOM   11401 C C   . ILE   B 2 171  ? 129.880 90.341  140.886 1.00 88.68  0  171  ILE   B C   1 
ATOM   11402 O O   . ILE   B 2 171  ? 129.732 89.650  141.896 1.00 88.87  0  171  ILE   B O   1 
ATOM   11403 C CB  . ILE   B 2 171  ? 131.968 91.648  140.401 1.00 85.61  0  171  ILE   B CB  1 
ATOM   11404 C CG1 . ILE   B 2 171  ? 132.924 91.153  141.485 1.00 86.25  0  171  ILE   B CG1 1 
ATOM   11405 C CG2 . ILE   B 2 171  ? 132.406 93.004  139.901 1.00 86.50  0  171  ILE   B CG2 1 
ATOM   11406 C CD1 . ILE   B 2 171  ? 134.157 90.477  140.945 1.00 85.60  0  171  ILE   B CD1 1 
ATOM   11407 N N   . GLY   B 2 172  ? 129.494 89.948  139.678 1.00 86.71  0  172  GLY   B N   1 
ATOM   11408 C CA  . GLY   B 2 172  ? 128.916 88.628  139.504 1.00 86.18  0  172  GLY   B CA  1 
ATOM   11409 C C   . GLY   B 2 172  ? 128.863 88.266  138.040 1.00 84.23  0  172  GLY   B C   1 
ATOM   11410 O O   . GLY   B 2 172  ? 129.391 88.974  137.181 1.00 85.15  0  172  GLY   B O   1 
ATOM   11411 N N   . LEU   B 2 173  ? 128.230 87.133  137.762 1.00 87.87  0  173  LEU   B N   1 
ATOM   11412 C CA  . LEU   B 2 173  ? 127.995 86.765  136.378 1.00 88.68  0  173  LEU   B CA  1 
ATOM   11413 C C   . LEU   B 2 173  ? 126.771 87.504  135.846 1.00 88.86  0  173  LEU   B C   1 
ATOM   11414 O O   . LEU   B 2 173  ? 125.997 88.101  136.597 1.00 91.47  0  173  LEU   B O   1 
ATOM   11415 C CB  . LEU   B 2 173  ? 127.827 85.253  136.243 1.00 92.89  0  173  LEU   B CB  1 
ATOM   11416 C CG  . LEU   B 2 173  ? 129.116 84.430  136.350 1.00 93.96  0  173  LEU   B CG  1 
ATOM   11417 C CD1 . LEU   B 2 173  ? 128.815 82.941  136.282 1.00 91.78  0  173  LEU   B CD1 1 
ATOM   11418 C CD2 . LEU   B 2 173  ? 130.105 84.828  135.265 1.00 90.44  0  173  LEU   B CD2 1 
ATOM   11419 N N   . ARG   B 2 174  ? 126.605 87.468  134.523 1.00 88.51  0  174  ARG   B N   1 
ATOM   11420 C CA  . ARG   B 2 174  ? 125.528 88.224  133.891 1.00 90.78  0  174  ARG   B CA  1 
ATOM   11421 C C   . ARG   B 2 174  ? 124.161 87.734  134.354 1.00 93.67  0  174  ARG   B C   1 
ATOM   11422 O O   . ARG   B 2 174  ? 123.329 88.523  134.819 1.00 94.71  0  174  ARG   B O   1 
ATOM   11423 C CB  . ARG   B 2 174  ? 125.651 88.125  132.372 1.00 90.41  0  174  ARG   B CB  1 
ATOM   11424 C CG  . ARG   B 2 174  ? 124.811 89.127  131.610 1.00 89.85  0  174  ARG   B CG  1 
ATOM   11425 C CD  . ARG   B 2 174  ? 124.961 88.926  130.115 1.00 93.15  0  174  ARG   B CD  1 
ATOM   11426 N NE  . ARG   B 2 174  ? 126.345 89.063  129.679 1.00 93.41  0  174  ARG   B NE  1 
ATOM   11427 C CZ  . ARG   B 2 174  ? 126.827 88.563  128.550 1.00 92.06  0  174  ARG   B CZ  1 
ATOM   11428 N NH1 . ARG   B 2 174  ? 126.062 87.883  127.713 1.00 91.25  1  174  ARG   B NH1 1 
ATOM   11429 N NH2 . ARG   B 2 174  ? 128.110 88.749  128.253 1.00 90.68  0  174  ARG   B NH2 1 
ATOM   11430 N N   . GLU   B 2 175  ? 123.916 86.426  134.247 1.00 100.99 0  175  GLU   B N   1 
ATOM   11431 C CA  . GLU   B 2 175  ? 122.622 85.878  134.642 1.00 100.34 0  175  GLU   B CA  1 
ATOM   11432 C C   . GLU   B 2 175  ? 122.397 85.986  136.144 1.00 99.86  0  175  GLU   B C   1 
ATOM   11433 O O   . GLU   B 2 175  ? 121.268 86.235  136.584 1.00 100.97 0  175  GLU   B O   1 
ATOM   11434 C CB  . GLU   B 2 175  ? 122.508 84.422  134.193 1.00 100.64 0  175  GLU   B CB  1 
ATOM   11435 C CG  . GLU   B 2 175  ? 122.656 84.217  132.694 1.00 100.74 0  175  GLU   B CG  1 
ATOM   11436 C CD  . GLU   B 2 175  ? 124.079 83.885  132.290 1.00 100.06 0  175  GLU   B CD  1 
ATOM   11437 O OE1 . GLU   B 2 175  ? 124.921 83.684  133.189 1.00 101.41 0  175  GLU   B OE1 1 
ATOM   11438 O OE2 . GLU   B 2 175  ? 124.357 83.827  131.074 1.00 99.80  -1 175  GLU   B OE2 1 
ATOM   11439 N N   . GLU   B 2 176  ? 123.450 85.799  136.942 1.00 103.02 0  176  GLU   B N   1 
ATOM   11440 C CA  . GLU   B 2 176  ? 123.310 85.914  138.390 1.00 104.06 0  176  GLU   B CA  1 
ATOM   11441 C C   . GLU   B 2 176  ? 122.901 87.325  138.788 1.00 104.05 0  176  GLU   B C   1 
ATOM   11442 O O   . GLU   B 2 176  ? 122.019 87.515  139.632 1.00 104.36 0  176  GLU   B O   1 
ATOM   11443 C CB  . GLU   B 2 176  ? 124.617 85.521  139.075 1.00 104.65 0  176  GLU   B CB  1 
ATOM   11444 C CG  . GLU   B 2 176  ? 124.432 85.009  140.487 1.00 105.66 0  176  GLU   B CG  1 
ATOM   11445 C CD  . GLU   B 2 176  ? 125.716 85.025  141.285 1.00 106.10 0  176  GLU   B CD  1 
ATOM   11446 O OE1 . GLU   B 2 176  ? 126.795 85.198  140.680 1.00 104.99 0  176  GLU   B OE1 1 
ATOM   11447 O OE2 . GLU   B 2 176  ? 125.644 84.859  142.519 1.00 104.98 -1 176  GLU   B OE2 1 
ATOM   11448 N N   . MET   B 2 177  ? 123.522 88.334  138.177 1.00 99.16  0  177  MET   B N   1 
ATOM   11449 C CA  . MET   B 2 177  ? 123.157 89.711  138.490 1.00 98.27  0  177  MET   B CA  1 
ATOM   11450 C C   . MET   B 2 177  ? 121.776 90.056  137.945 1.00 101.32 0  177  MET   B C   1 
ATOM   11451 O O   . MET   B 2 177  ? 121.040 90.835  138.561 1.00 104.92 0  177  MET   B O   1 
ATOM   11452 C CB  . MET   B 2 177  ? 124.213 90.671  137.950 1.00 99.54  0  177  MET   B CB  1 
ATOM   11453 C CG  . MET   B 2 177  ? 125.511 90.641  138.736 1.00 101.35 0  177  MET   B CG  1 
ATOM   11454 S SD  . MET   B 2 177  ? 125.316 91.245  140.422 1.00 103.32 0  177  MET   B SD  1 
ATOM   11455 C CE  . MET   B 2 177  ? 126.010 89.882  141.355 1.00 98.37  0  177  MET   B CE  1 
ATOM   11456 N N   . ILE   B 2 178  ? 121.401 89.485  136.798 1.00 103.28 0  178  ILE   B N   1 
ATOM   11457 C CA  . ILE   B 2 178  ? 120.050 89.697  136.284 1.00 103.14 0  178  ILE   B CA  1 
ATOM   11458 C C   . ILE   B 2 178  ? 119.018 89.158  137.267 1.00 104.18 0  178  ILE   B C   1 
ATOM   11459 O O   . ILE   B 2 178  ? 118.011 89.815  137.560 1.00 104.47 0  178  ILE   B O   1 
ATOM   11460 C CB  . ILE   B 2 178  ? 119.899 89.059  134.891 1.00 103.20 0  178  ILE   B CB  1 
ATOM   11461 C CG1 . ILE   B 2 178  ? 120.612 89.906  133.837 1.00 104.16 0  178  ILE   B CG1 1 
ATOM   11462 C CG2 . ILE   B 2 178  ? 118.434 88.897  134.530 1.00 103.14 0  178  ILE   B CG2 1 
ATOM   11463 C CD1 . ILE   B 2 178  ? 120.927 89.155  132.564 1.00 103.32 0  178  ILE   B CD1 1 
ATOM   11464 N N   . GLU   B 2 179  ? 119.257 87.959  137.802 1.00 109.05 0  179  GLU   B N   1 
ATOM   11465 C CA  . GLU   B 2 179  ? 118.348 87.403  138.799 1.00 108.46 0  179  GLU   B CA  1 
ATOM   11466 C C   . GLU   B 2 179  ? 118.378 88.202  140.096 1.00 108.50 0  179  GLU   B C   1 
ATOM   11467 O O   . GLU   B 2 179  ? 117.351 88.322  140.772 1.00 108.04 0  179  GLU   B O   1 
ATOM   11468 C CB  . GLU   B 2 179  ? 118.687 85.938  139.065 1.00 106.84 0  179  GLU   B CB  1 
ATOM   11469 C CG  . GLU   B 2 179  ? 118.294 85.012  137.930 1.00 107.12 0  179  GLU   B CG  1 
ATOM   11470 C CD  . GLU   B 2 179  ? 116.828 85.135  137.564 1.00 107.99 0  179  GLU   B CD  1 
ATOM   11471 O OE1 . GLU   B 2 179  ? 115.974 84.733  138.381 1.00 108.61 0  179  GLU   B OE1 1 
ATOM   11472 O OE2 . GLU   B 2 179  ? 116.530 85.637  136.461 1.00 108.80 -1 179  GLU   B OE2 1 
ATOM   11473 N N   . LYS   B 2 180  ? 119.542 88.743  140.463 1.00 106.34 0  180  LYS   B N   1 
ATOM   11474 C CA  . LYS   B 2 180  ? 119.620 89.611  141.634 1.00 106.88 0  180  LYS   B CA  1 
ATOM   11475 C C   . LYS   B 2 180  ? 118.753 90.850  141.452 1.00 106.27 0  180  LYS   B C   1 
ATOM   11476 O O   . LYS   B 2 180  ? 118.092 91.303  142.394 1.00 105.87 0  180  LYS   B O   1 
ATOM   11477 C CB  . LYS   B 2 180  ? 121.073 90.004  141.895 1.00 106.58 0  180  LYS   B CB  1 
ATOM   11478 C CG  . LYS   B 2 180  ? 121.858 88.990  142.707 1.00 106.91 0  180  LYS   B CG  1 
ATOM   11479 C CD  . LYS   B 2 180  ? 121.910 89.397  144.165 1.00 106.85 0  180  LYS   B CD  1 
ATOM   11480 C CE  . LYS   B 2 180  ? 123.104 88.785  144.867 1.00 108.22 0  180  LYS   B CE  1 
ATOM   11481 N NZ  . LYS   B 2 180  ? 123.325 89.392  146.208 1.00 106.02 1  180  LYS   B NZ  1 
ATOM   11482 N N   . ILE   B 2 181  ? 118.758 91.418  140.246 1.00 104.01 0  181  ILE   B N   1 
ATOM   11483 C CA  . ILE   B 2 181  ? 117.840 92.506  139.926 1.00 104.29 0  181  ILE   B CA  1 
ATOM   11484 C C   . ILE   B 2 181  ? 116.397 92.021  140.010 1.00 106.45 0  181  ILE   B C   1 
ATOM   11485 O O   . ILE   B 2 181  ? 115.510 92.745  140.478 1.00 108.39 0  181  ILE   B O   1 
ATOM   11486 C CB  . ILE   B 2 181  ? 118.165 93.084  138.536 1.00 103.03 0  181  ILE   B CB  1 
ATOM   11487 C CG1 . ILE   B 2 181  ? 119.570 93.683  138.521 1.00 101.28 0  181  ILE   B CG1 1 
ATOM   11488 C CG2 . ILE   B 2 181  ? 117.147 94.139  138.141 1.00 103.35 0  181  ILE   B CG2 1 
ATOM   11489 C CD1 . ILE   B 2 181  ? 120.128 93.881  137.133 1.00 101.35 0  181  ILE   B CD1 1 
ATOM   11490 N N   . ARG   B 2 182  ? 116.142 90.788  139.564 1.00 109.90 0  182  ARG   B N   1 
ATOM   11491 C CA  . ARG   B 2 182  ? 114.794 90.231  139.640 1.00 109.71 0  182  ARG   B CA  1 
ATOM   11492 C C   . ARG   B 2 182  ? 114.329 90.090  141.084 1.00 109.70 0  182  ARG   B C   1 
ATOM   11493 O O   . ARG   B 2 182  ? 113.150 90.308  141.385 1.00 108.75 0  182  ARG   B O   1 
ATOM   11494 C CB  . ARG   B 2 182  ? 114.739 88.881  138.928 1.00 108.98 0  182  ARG   B CB  1 
ATOM   11495 C CG  . ARG   B 2 182  ? 113.330 88.381  138.662 1.00 109.50 0  182  ARG   B CG  1 
ATOM   11496 C CD  . ARG   B 2 182  ? 113.335 86.922  138.241 1.00 110.05 0  182  ARG   B CD  1 
ATOM   11497 N NE  . ARG   B 2 182  ? 113.813 86.053  139.310 1.00 110.70 0  182  ARG   B NE  1 
ATOM   11498 C CZ  . ARG   B 2 182  ? 113.089 85.678  140.355 1.00 109.83 0  182  ARG   B CZ  1 
ATOM   11499 N NH1 . ARG   B 2 182  ? 111.832 86.063  140.501 1.00 109.04 1  182  ARG   B NH1 1 
ATOM   11500 N NH2 . ARG   B 2 182  ? 113.641 84.896  141.279 1.00 108.62 0  182  ARG   B NH2 1 
ATOM   11501 N N   . THR   B 2 183  ? 115.232 89.715  141.988 1.00 108.22 0  183  THR   B N   1 
ATOM   11502 C CA  . THR   B 2 183  ? 114.907 89.586  143.404 1.00 108.51 0  183  THR   B CA  1 
ATOM   11503 C C   . THR   B 2 183  ? 115.058 90.895  144.170 1.00 110.10 0  183  THR   B C   1 
ATOM   11504 O O   . THR   B 2 183  ? 115.198 90.857  145.399 1.00 109.73 0  183  THR   B O   1 
ATOM   11505 C CB  . THR   B 2 183  ? 115.781 88.510  144.053 1.00 106.66 0  183  THR   B CB  1 
ATOM   11506 O OG1 . THR   B 2 183  ? 117.152 88.924  144.028 1.00 108.79 0  183  THR   B OG1 1 
ATOM   11507 C CG2 . THR   B 2 183  ? 115.639 87.192  143.311 1.00 106.56 0  183  THR   B CG2 1 
ATOM   11508 N N   . GLU   B 2 184  ? 115.025 92.036  143.471 1.00 108.61 0  184  GLU   B N   1 
ATOM   11509 C CA  . GLU   B 2 184  ? 115.233 93.377  144.020 1.00 106.74 0  184  GLU   B CA  1 
ATOM   11510 C C   . GLU   B 2 184  ? 116.332 93.413  145.076 1.00 107.47 0  184  GLU   B C   1 
ATOM   11511 O O   . GLU   B 2 184  ? 116.230 94.159  146.055 1.00 106.80 0  184  GLU   B O   1 
ATOM   11512 C CB  . GLU   B 2 184  ? 113.943 93.984  144.607 1.00 107.93 0  184  GLU   B CB  1 
ATOM   11513 C CG  . GLU   B 2 184  ? 113.013 93.085  145.425 1.00 107.56 0  184  GLU   B CG  1 
ATOM   11514 C CD  . GLU   B 2 184  ? 112.010 92.317  144.580 1.00 109.04 0  184  GLU   B CD  1 
ATOM   11515 O OE1 . GLU   B 2 184  ? 110.802 92.394  144.888 1.00 108.99 0  184  GLU   B OE1 1 
ATOM   11516 O OE2 . GLU   B 2 184  ? 112.407 91.660  143.601 1.00 108.39 -1 184  GLU   B OE2 1 
ATOM   11517 N N   . ALA   B 2 185  ? 117.391 92.623  144.886 1.00 107.05 0  185  ALA   B N   1 
ATOM   11518 C CA  . ALA   B 2 185  ? 118.479 92.592  145.856 1.00 107.55 0  185  ALA   B CA  1 
ATOM   11519 C C   . ALA   B 2 185  ? 119.386 93.810  145.757 1.00 108.11 0  185  ALA   B C   1 
ATOM   11520 O O   . ALA   B 2 185  ? 120.123 94.091  146.708 1.00 106.45 0  185  ALA   B O   1 
ATOM   11521 C CB  . ALA   B 2 185  ? 119.301 91.314  145.684 1.00 104.81 0  185  ALA   B CB  1 
ATOM   11522 N N   . LEU   B 2 186  ? 119.353 94.528  144.638 1.00 101.06 0  186  LEU   B N   1 
ATOM   11523 C CA  . LEU   B 2 186  ? 120.115 95.758  144.451 1.00 98.51  0  186  LEU   B CA  1 
ATOM   11524 C C   . LEU   B 2 186  ? 119.135 96.848  144.038 1.00 98.62  0  186  LEU   B C   1 
ATOM   11525 O O   . LEU   B 2 186  ? 118.585 96.807  142.932 1.00 97.83  0  186  LEU   B O   1 
ATOM   11526 C CB  . LEU   B 2 186  ? 121.216 95.569  143.410 1.00 96.61  0  186  LEU   B CB  1 
ATOM   11527 C CG  . LEU   B 2 186  ? 122.273 94.532  143.789 1.00 96.66  0  186  LEU   B CG  1 
ATOM   11528 C CD1 . LEU   B 2 186  ? 123.331 94.422  142.711 1.00 94.98  0  186  LEU   B CD1 1 
ATOM   11529 C CD2 . LEU   B 2 186  ? 122.904 94.875  145.129 1.00 95.15  0  186  LEU   B CD2 1 
ATOM   11530 N N   . MET   B 2 187  ? 118.919 97.816  144.926 1.00 93.48  0  187  MET   B N   1 
ATOM   11531 C CA  . MET   B 2 187  ? 117.877 98.811  144.711 1.00 92.74  0  187  MET   B CA  1 
ATOM   11532 C C   . MET   B 2 187  ? 118.189 99.679  143.498 1.00 92.40  0  187  MET   B C   1 
ATOM   11533 O O   . MET   B 2 187  ? 119.270 100.263 143.393 1.00 87.44  0  187  MET   B O   1 
ATOM   11534 C CB  . MET   B 2 187  ? 117.711 99.671  145.966 1.00 90.65  0  187  MET   B CB  1 
ATOM   11535 C CG  . MET   B 2 187  ? 119.007 99.965  146.718 1.00 91.08  0  187  MET   B CG  1 
ATOM   11536 S SD  . MET   B 2 187  ? 119.895 101.425 146.138 1.00 88.01  0  187  MET   B SD  1 
ATOM   11537 C CE  . MET   B 2 187  ? 118.662 102.697 146.394 1.00 88.49  0  187  MET   B CE  1 
ATOM   11538 N N   . THR   B 2 188  ? 117.234 99.745  142.571 1.00 93.71  0  188  THR   B N   1 
ATOM   11539 C CA  . THR   B 2 188  ? 117.344 100.580 141.384 1.00 93.85  0  188  THR   B CA  1 
ATOM   11540 C C   . THR   B 2 188  ? 115.994 101.223 141.107 1.00 94.69  0  188  THR   B C   1 
ATOM   11541 O O   . THR   B 2 188  ? 114.946 100.718 141.517 1.00 91.69  0  188  THR   B O   1 
ATOM   11542 C CB  . THR   B 2 188  ? 117.788 99.788  140.145 1.00 91.12  0  188  THR   B CB  1 
ATOM   11543 O OG1 . THR   B 2 188  ? 116.797 98.806  139.820 1.00 91.58  0  188  THR   B OG1 1 
ATOM   11544 C CG2 . THR   B 2 188  ? 119.116 99.099  140.389 1.00 90.75  0  188  THR   B CG2 1 
ATOM   11545 N N   . ASN   B 2 189  ? 116.033 102.349 140.397 1.00 95.80  0  189  ASN   B N   1 
ATOM   11546 C CA  . ASN   B 2 189  ? 114.810 103.029 139.993 1.00 94.56  0  189  ASN   B CA  1 
ATOM   11547 C C   . ASN   B 2 189  ? 114.172 102.407 138.759 1.00 96.19  0  189  ASN   B C   1 
ATOM   11548 O O   . ASN   B 2 189  ? 113.047 102.779 138.409 1.00 94.73  0  189  ASN   B O   1 
ATOM   11549 C CB  . ASN   B 2 189  ? 115.097 104.509 139.733 1.00 91.61  0  189  ASN   B CB  1 
ATOM   11550 C CG  . ASN   B 2 189  ? 115.873 105.157 140.864 1.00 93.17  0  189  ASN   B CG  1 
ATOM   11551 O OD1 . ASN   B 2 189  ? 115.824 104.703 142.007 1.00 92.66  0  189  ASN   B OD1 1 
ATOM   11552 N ND2 . ASN   B 2 189  ? 116.595 106.225 140.548 1.00 94.41  0  189  ASN   B ND2 1 
ATOM   11553 N N   . ASP   B 2 190  ? 114.857 101.476 138.101 1.00 110.09 0  190  ASP   B N   1 
ATOM   11554 C CA  . ASP   B 2 190  ? 114.356 100.843 136.891 1.00 110.20 0  190  ASP   B CA  1 
ATOM   11555 C C   . ASP   B 2 190  ? 114.862 99.410  136.854 1.00 109.87 0  190  ASP   B C   1 
ATOM   11556 O O   . ASP   B 2 190  ? 116.006 99.142  137.230 1.00 111.01 0  190  ASP   B O   1 
ATOM   11557 C CB  . ASP   B 2 190  ? 114.807 101.611 135.644 1.00 109.42 0  190  ASP   B CB  1 
ATOM   11558 C CG  . ASP   B 2 190  ? 114.039 101.214 134.405 1.00 110.60 0  190  ASP   B CG  1 
ATOM   11559 O OD1 . ASP   B 2 190  ? 113.289 100.217 134.458 1.00 110.33 0  190  ASP   B OD1 1 
ATOM   11560 O OD2 . ASP   B 2 190  ? 114.174 101.913 133.378 1.00 111.56 -1 190  ASP   B OD2 1 
ATOM   11561 N N   . ARG   B 2 191  ? 114.006 98.492  136.405 1.00 114.21 0  191  ARG   B N   1 
ATOM   11562 C CA  . ARG   B 2 191  ? 114.356 97.076  136.366 1.00 115.55 0  191  ARG   B CA  1 
ATOM   11563 C C   . ARG   B 2 191  ? 114.439 96.537  134.945 1.00 115.87 0  191  ARG   B C   1 
ATOM   11564 O O   . ARG   B 2 191  ? 115.493 96.034  134.545 1.00 114.83 0  191  ARG   B O   1 
ATOM   11565 C CB  . ARG   B 2 191  ? 113.344 96.260  137.180 1.00 116.37 0  191  ARG   B CB  1 
ATOM   11566 C CG  . ARG   B 2 191  ? 113.219 96.667  138.636 1.00 115.25 0  191  ARG   B CG  1 
ATOM   11567 C CD  . ARG   B 2 191  ? 112.372 95.659  139.386 1.00 114.05 0  191  ARG   B CD  1 
ATOM   11568 N NE  . ARG   B 2 191  ? 111.115 95.408  138.692 1.00 114.27 0  191  ARG   B NE  1 
ATOM   11569 C CZ  . ARG   B 2 191  ? 110.466 94.253  138.714 1.00 114.98 0  191  ARG   B CZ  1 
ATOM   11570 N NH1 . ARG   B 2 191  ? 110.933 93.210  139.381 1.00 114.27 1  191  ARG   B NH1 1 
ATOM   11571 N NH2 . ARG   B 2 191  ? 109.322 94.138  138.044 1.00 115.43 0  191  ARG   B NH2 1 
ATOM   11572 N N   . LEU   B 2 192  ? 113.360 96.639  134.165 1.00 112.90 0  192  LEU   B N   1 
ATOM   11573 C CA  . LEU   B 2 192  ? 113.315 95.981  132.863 1.00 111.47 0  192  LEU   B CA  1 
ATOM   11574 C C   . LEU   B 2 192  ? 114.332 96.568  131.895 1.00 112.12 0  192  LEU   B C   1 
ATOM   11575 O O   . LEU   B 2 192  ? 114.842 95.853  131.027 1.00 112.88 0  192  LEU   B O   1 
ATOM   11576 C CB  . LEU   B 2 192  ? 111.906 96.071  132.282 1.00 111.32 0  192  LEU   B CB  1 
ATOM   11577 C CG  . LEU   B 2 192  ? 110.796 95.530  133.187 1.00 110.98 0  192  LEU   B CG  1 
ATOM   11578 C CD1 . LEU   B 2 192  ? 109.456 95.546  132.469 1.00 110.93 0  192  LEU   B CD1 1 
ATOM   11579 C CD2 . LEU   B 2 192  ? 111.135 94.125  133.670 1.00 109.44 0  192  LEU   B CD2 1 
ATOM   11580 N N   . GLU   B 2 193  ? 114.633 97.860  132.024 1.00 108.73 0  193  GLU   B N   1 
ATOM   11581 C CA  . GLU   B 2 193  ? 115.679 98.466  131.207 1.00 108.42 0  193  GLU   B CA  1 
ATOM   11582 C C   . GLU   B 2 193  ? 117.025 97.811  131.482 1.00 109.19 0  193  GLU   B C   1 
ATOM   11583 O O   . GLU   B 2 193  ? 117.753 97.442  130.552 1.00 107.83 0  193  GLU   B O   1 
ATOM   11584 C CB  . GLU   B 2 193  ? 115.731 99.972  131.473 1.00 109.06 0  193  GLU   B CB  1 
ATOM   11585 C CG  . GLU   B 2 193  ? 116.383 100.815 130.379 1.00 111.10 0  193  GLU   B CG  1 
ATOM   11586 C CD  . GLU   B 2 193  ? 117.901 100.901 130.490 1.00 110.76 0  193  GLU   B CD  1 
ATOM   11587 O OE1 . GLU   B 2 193  ? 118.516 101.569 129.630 1.00 107.68 0  193  GLU   B OE1 1 
ATOM   11588 O OE2 . GLU   B 2 193  ? 118.474 100.344 131.450 1.00 111.37 -1 193  GLU   B OE2 1 
ATOM   11589 N N   . ALA   B 2 194  ? 117.365 97.644  132.763 1.00 105.85 0  194  ALA   B N   1 
ATOM   11590 C CA  . ALA   B 2 194  ? 118.632 97.017  133.119 1.00 104.10 0  194  ALA   B CA  1 
ATOM   11591 C C   . ALA   B 2 194  ? 118.681 95.567  132.657 1.00 107.54 0  194  ALA   B C   1 
ATOM   11592 O O   . ALA   B 2 194  ? 119.708 95.104  132.148 1.00 107.67 0  194  ALA   B O   1 
ATOM   11593 C CB  . ALA   B 2 194  ? 118.859 97.112  134.628 1.00 101.77 0  194  ALA   B CB  1 
ATOM   11594 N N   . MET   B 2 195  ? 117.578 94.832  132.825 1.00 111.60 0  195  MET   B N   1 
ATOM   11595 C CA  . MET   B 2 195  ? 117.541 93.444  132.377 1.00 109.76 0  195  MET   B CA  1 
ATOM   11596 C C   . MET   B 2 195  ? 117.735 93.348  130.870 1.00 110.96 0  195  MET   B C   1 
ATOM   11597 O O   . MET   B 2 195  ? 118.555 92.558  130.389 1.00 112.89 0  195  MET   B O   1 
ATOM   11598 C CB  . MET   B 2 195  ? 116.221 92.792  132.789 1.00 109.62 0  195  MET   B CB  1 
ATOM   11599 C CG  . MET   B 2 195  ? 115.877 92.940  134.256 1.00 110.71 0  195  MET   B CG  1 
ATOM   11600 S SD  . MET   B 2 195  ? 114.535 91.842  134.737 1.00 115.36 0  195  MET   B SD  1 
ATOM   11601 C CE  . MET   B 2 195  ? 114.644 91.946  136.517 1.00 110.26 0  195  MET   B CE  1 
ATOM   11602 N N   . ALA   B 2 196  ? 116.997 94.157  130.108 1.00 108.23 0  196  ALA   B N   1 
ATOM   11603 C CA  . ALA   B 2 196  ? 117.124 94.123  128.655 1.00 108.90 0  196  ALA   B CA  1 
ATOM   11604 C C   . ALA   B 2 196  ? 118.521 94.524  128.207 1.00 106.57 0  196  ALA   B C   1 
ATOM   11605 O O   . ALA   B 2 196  ? 119.047 93.961  127.240 1.00 104.26 0  196  ALA   B O   1 
ATOM   11606 C CB  . ALA   B 2 196  ? 116.078 95.031  128.013 1.00 107.23 0  196  ALA   B CB  1 
ATOM   11607 N N   . ARG   B 2 197  ? 119.134 95.493  128.887 1.00 98.77  0  197  ARG   B N   1 
ATOM   11608 C CA  . ARG   B 2 197  ? 120.496 95.884  128.546 1.00 100.21 0  197  ARG   B CA  1 
ATOM   11609 C C   . ARG   B 2 197  ? 121.477 94.750  128.812 1.00 99.70  0  197  ARG   B C   1 
ATOM   11610 O O   . ARG   B 2 197  ? 122.327 94.441  127.968 1.00 100.35 0  197  ARG   B O   1 
ATOM   11611 C CB  . ARG   B 2 197  ? 120.892 97.133  129.331 1.00 98.79  0  197  ARG   B CB  1 
ATOM   11612 C CG  . ARG   B 2 197  ? 122.247 97.689  128.952 1.00 96.37  0  197  ARG   B CG  1 
ATOM   11613 C CD  . ARG   B 2 197  ? 122.592 98.892  129.797 1.00 96.10  0  197  ARG   B CD  1 
ATOM   11614 N NE  . ARG   B 2 197  ? 123.328 98.534  131.003 1.00 96.02  0  197  ARG   B NE  1 
ATOM   11615 C CZ  . ARG   B 2 197  ? 122.843 98.639  132.231 1.00 97.27  0  197  ARG   B CZ  1 
ATOM   11616 N NH1 . ARG   B 2 197  ? 121.613 99.070  132.453 1.00 98.38  1  197  ARG   B NH1 1 
ATOM   11617 N NH2 . ARG   B 2 197  ? 123.612 98.306  133.263 1.00 93.70  0  197  ARG   B NH2 1 
ATOM   11618 N N   . LEU   B 2 198  ? 121.381 94.121  129.985 1.00 102.95 0  198  LEU   B N   1 
ATOM   11619 C CA  . LEU   B 2 198  ? 122.293 93.030  130.311 1.00 103.48 0  198  LEU   B CA  1 
ATOM   11620 C C   . LEU   B 2 198  ? 122.069 91.830  129.398 1.00 104.15 0  198  LEU   B C   1 
ATOM   11621 O O   . LEU   B 2 198  ? 123.028 91.192  128.950 1.00 101.88 0  198  LEU   B O   1 
ATOM   11622 C CB  . LEU   B 2 198  ? 122.135 92.637  131.778 1.00 103.40 0  198  LEU   B CB  1 
ATOM   11623 C CG  . LEU   B 2 198  ? 122.556 93.708  132.785 1.00 98.98  0  198  LEU   B CG  1 
ATOM   11624 C CD1 . LEU   B 2 198  ? 122.303 93.241  134.208 1.00 98.97  0  198  LEU   B CD1 1 
ATOM   11625 C CD2 . LEU   B 2 198  ? 124.014 94.082  132.588 1.00 97.94  0  198  LEU   B CD2 1 
ATOM   11626 N N   . ARG   B 2 199  ? 120.808 91.513  129.102 1.00 110.24 0  199  ARG   B N   1 
ATOM   11627 C CA  . ARG   B 2 199  ? 120.491 90.430  128.179 1.00 111.04 0  199  ARG   B CA  1 
ATOM   11628 C C   . ARG   B 2 199  ? 120.731 90.805  126.724 1.00 113.67 0  199  ARG   B C   1 
ATOM   11629 O O   . ARG   B 2 199  ? 120.458 89.979  125.846 1.00 114.85 0  199  ARG   B O   1 
ATOM   11630 C CB  . ARG   B 2 199  ? 119.036 89.995  128.357 1.00 110.37 0  199  ARG   B CB  1 
ATOM   11631 C CG  . ARG   B 2 199  ? 118.700 89.477  129.740 1.00 110.06 0  199  ARG   B CG  1 
ATOM   11632 C CD  . ARG   B 2 199  ? 117.198 89.446  129.961 1.00 108.86 0  199  ARG   B CD  1 
ATOM   11633 N NE  . ARG   B 2 199  ? 116.856 89.293  131.370 1.00 109.19 0  199  ARG   B NE  1 
ATOM   11634 C CZ  . ARG   B 2 199  ? 115.625 89.383  131.854 1.00 110.48 0  199  ARG   B CZ  1 
ATOM   11635 N NH1 . ARG   B 2 199  ? 114.590 89.625  131.068 1.00 111.31 1  199  ARG   B NH1 1 
ATOM   11636 N NH2 . ARG   B 2 199  ? 115.429 89.226  133.160 1.00 110.24 0  199  ARG   B NH2 1 
ATOM   11637 N N   . ASN   B 2 200  ? 121.217 92.019  126.455 1.00 118.61 0  200  ASN   B N   1 
ATOM   11638 C CA  . ASN   B 2 200  ? 121.410 92.526  125.096 1.00 117.87 0  200  ASN   B CA  1 
ATOM   11639 C C   . ASN   B 2 200  ? 120.100 92.551  124.314 1.00 118.72 0  200  ASN   B C   1 
ATOM   11640 O O   . ASN   B 2 200  ? 120.086 92.364  123.096 1.00 118.40 0  200  ASN   B O   1 
ATOM   11641 C CB  . ASN   B 2 200  ? 122.472 91.717  124.342 1.00 116.38 0  200  ASN   B CB  1 
ATOM   11642 C CG  . ASN   B 2 200  ? 123.174 92.530  123.275 1.00 117.67 0  200  ASN   B CG  1 
ATOM   11643 O OD1 . ASN   B 2 200  ? 123.409 93.726  123.443 1.00 118.60 0  200  ASN   B OD1 1 
ATOM   11644 N ND2 . ASN   B 2 200  ? 123.515 91.883  122.167 1.00 117.57 0  200  ASN   B ND2 1 
ATOM   11645 N N   . GLU   B 2 201  ? 118.993 92.786  125.009 1.00 122.18 0  201  GLU   B N   1 
ATOM   11646 C CA  . GLU   B 2 201  ? 117.674 92.834  124.398 1.00 123.34 0  201  GLU   B CA  1 
ATOM   11647 C C   . GLU   B 2 201  ? 117.269 94.276  124.111 1.00 125.23 0  201  GLU   B C   1 
ATOM   11648 O O   . GLU   B 2 201  ? 117.901 95.234  124.562 1.00 122.48 0  201  GLU   B O   1 
ATOM   11649 C CB  . GLU   B 2 201  ? 116.634 92.166  125.302 1.00 122.36 0  201  GLU   B CB  1 
ATOM   11650 C CG  . GLU   B 2 201  ? 116.859 90.686  125.539 1.00 121.81 0  201  GLU   B CG  1 
ATOM   11651 C CD  . GLU   B 2 201  ? 115.835 90.092  126.485 1.00 121.97 0  201  GLU   B CD  1 
ATOM   11652 O OE1 . GLU   B 2 201  ? 114.850 90.788  126.808 1.00 120.52 0  201  GLU   B OE1 1 
ATOM   11653 O OE2 . GLU   B 2 201  ? 116.014 88.930  126.905 1.00 121.87 -1 201  GLU   B OE2 1 
ATOM   11654 N N   . GLU   B 2 202  ? 116.190 94.418  123.347 1.00 137.75 0  202  GLU   B N   1 
ATOM   11655 C CA  . GLU   B 2 202  ? 115.615 95.721  123.027 1.00 137.02 0  202  GLU   B CA  1 
ATOM   11656 C C   . GLU   B 2 202  ? 114.323 95.867  123.822 1.00 135.94 0  202  GLU   B C   1 
ATOM   11657 O O   . GLU   B 2 202  ? 113.284 95.318  123.446 1.00 135.51 0  202  GLU   B O   1 
ATOM   11658 C CB  . GLU   B 2 202  ? 115.366 95.855  121.529 1.00 137.29 0  202  GLU   B CB  1 
ATOM   11659 C CG  . GLU   B 2 202  ? 114.814 97.211  121.112 1.00 137.55 0  202  GLU   B CG  1 
ATOM   11660 C CD  . GLU   B 2 202  ? 114.343 97.233  119.670 1.00 137.41 0  202  GLU   B CD  1 
ATOM   11661 O OE1 . GLU   B 2 202  ? 114.196 96.145  119.074 1.00 137.80 0  202  GLU   B OE1 1 
ATOM   11662 O OE2 . GLU   B 2 202  ? 114.123 98.339  119.133 1.00 136.47 -1 202  GLU   B OE2 1 
ATOM   11663 N N   . SER   B 2 203  ? 114.389 96.610  124.923 1.00 131.16 0  203  SER   B N   1 
ATOM   11664 C CA  . SER   B 2 203  ? 113.198 96.864  125.713 1.00 132.13 0  203  SER   B CA  1 
ATOM   11665 C C   . SER   B 2 203  ? 112.274 97.834  124.979 1.00 132.53 0  203  SER   B C   1 
ATOM   11666 O O   . SER   B 2 203  ? 112.638 98.450  123.973 1.00 132.52 0  203  SER   B O   1 
ATOM   11667 C CB  . SER   B 2 203  ? 113.569 97.417  127.088 1.00 132.36 0  203  SER   B CB  1 
ATOM   11668 O OG  . SER   B 2 203  ? 114.116 98.720  126.988 1.00 132.28 0  203  SER   B OG  1 
ATOM   11669 N N   . GLU   B 2 204  ? 111.053 97.961  125.502 1.00 127.08 0  204  GLU   B N   1 
ATOM   11670 C CA  . GLU   B 2 204  ? 110.065 98.837  124.881 1.00 126.49 0  204  GLU   B CA  1 
ATOM   11671 C C   . GLU   B 2 204  ? 110.525 100.290 124.892 1.00 127.07 0  204  GLU   B C   1 
ATOM   11672 O O   . GLU   B 2 204  ? 110.311 101.024 123.919 1.00 127.02 0  204  GLU   B O   1 
ATOM   11673 C CB  . GLU   B 2 204  ? 108.719 98.693  125.591 1.00 126.63 0  204  GLU   B CB  1 
ATOM   11674 C CG  . GLU   B 2 204  ? 108.167 97.274  125.600 1.00 126.84 0  204  GLU   B CG  1 
ATOM   11675 C CD  . GLU   B 2 204  ? 108.654 96.463  126.786 1.00 127.13 0  204  GLU   B CD  1 
ATOM   11676 O OE1 . GLU   B 2 204  ? 109.385 97.024  127.630 1.00 125.97 0  204  GLU   B OE1 1 
ATOM   11677 O OE2 . GLU   B 2 204  ? 108.310 95.265  126.872 1.00 126.83 -1 204  GLU   B OE2 1 
ATOM   11678 N N   . LYS   B 2 205  ? 111.149 100.727 125.989 1.00 126.62 0  205  LYS   B N   1 
ATOM   11679 C CA  . LYS   B 2 205  ? 111.584 102.116 126.092 1.00 126.05 0  205  LYS   B CA  1 
ATOM   11680 C C   . LYS   B 2 205  ? 112.623 102.449 125.028 1.00 126.24 0  205  LYS   B C   1 
ATOM   11681 O O   . LYS   B 2 205  ? 112.529 103.482 124.356 1.00 126.70 0  205  LYS   B O   1 
ATOM   11682 C CB  . LYS   B 2 205  ? 112.127 102.391 127.494 1.00 124.80 0  205  LYS   B CB  1 
ATOM   11683 C CG  . LYS   B 2 205  ? 111.072 102.308 128.586 1.00 124.48 0  205  LYS   B CG  1 
ATOM   11684 C CD  . LYS   B 2 205  ? 111.682 102.465 129.968 1.00 125.59 0  205  LYS   B CD  1 
ATOM   11685 C CE  . LYS   B 2 205  ? 110.608 102.438 131.041 1.00 123.61 0  205  LYS   B CE  1 
ATOM   11686 N NZ  . LYS   B 2 205  ? 111.177 102.577 132.408 1.00 121.84 1  205  LYS   B NZ  1 
ATOM   11687 N N   . MET   B 2 206  ? 113.616 101.574 124.847 1.00 123.74 0  206  MET   B N   1 
ATOM   11688 C CA  . MET   B 2 206  ? 114.594 101.783 123.782 1.00 122.66 0  206  MET   B CA  1 
ATOM   11689 C C   . MET   B 2 206  ? 113.935 101.728 122.412 1.00 122.61 0  206  MET   B C   1 
ATOM   11690 O O   . MET   B 2 206  ? 114.279 102.507 121.516 1.00 121.69 0  206  MET   B O   1 
ATOM   11691 C CB  . MET   B 2 206  ? 115.704 100.738 123.861 1.00 123.72 0  206  MET   B CB  1 
ATOM   11692 C CG  . MET   B 2 206  ? 116.251 100.486 125.248 1.00 125.32 0  206  MET   B CG  1 
ATOM   11693 S SD  . MET   B 2 206  ? 117.967 99.944  125.151 1.00 128.19 0  206  MET   B SD  1 
ATOM   11694 C CE  . MET   B 2 206  ? 118.599 100.511 126.721 1.00 121.24 0  206  MET   B CE  1 
ATOM   11695 N N   . ALA   B 2 207  ? 112.992 100.801 122.231 1.00 123.66 0  207  ALA   B N   1 
ATOM   11696 C CA  . ALA   B 2 207  ? 112.356 100.630 120.930 1.00 124.47 0  207  ALA   B CA  1 
ATOM   11697 C C   . ALA   B 2 207  ? 111.592 101.880 120.521 1.00 123.45 0  207  ALA   B C   1 
ATOM   11698 O O   . ALA   B 2 207  ? 111.645 102.295 119.357 1.00 122.66 0  207  ALA   B O   1 
ATOM   11699 C CB  . ALA   B 2 207  ? 111.426 99.418  120.957 1.00 123.64 0  207  ALA   B CB  1 
ATOM   11700 N N   . LYS   B 2 208  ? 110.875 102.494 121.461 1.00 119.78 0  208  LYS   B N   1 
ATOM   11701 C CA  . LYS   B 2 208  ? 110.084 103.675 121.142 1.00 119.16 0  208  LYS   B CA  1 
ATOM   11702 C C   . LYS   B 2 208  ? 110.882 104.971 121.203 1.00 118.59 0  208  LYS   B C   1 
ATOM   11703 O O   . LYS   B 2 208  ? 110.478 105.955 120.573 1.00 118.88 0  208  LYS   B O   1 
ATOM   11704 C CB  . LYS   B 2 208  ? 108.870 103.771 122.075 1.00 119.26 0  208  LYS   B CB  1 
ATOM   11705 C CG  . LYS   B 2 208  ? 109.151 104.390 123.434 1.00 119.24 0  208  LYS   B CG  1 
ATOM   11706 C CD  . LYS   B 2 208  ? 107.867 104.551 124.234 1.00 118.94 0  208  LYS   B CD  1 
ATOM   11707 C CE  . LYS   B 2 208  ? 108.139 105.179 125.589 1.00 119.09 0  208  LYS   B CE  1 
ATOM   11708 N NZ  . LYS   B 2 208  ? 108.567 106.601 125.471 1.00 118.54 1  208  LYS   B NZ  1 
ATOM   11709 N N   . ASP   B 2 209  ? 111.999 105.000 121.936 1.00 112.42 0  209  ASP   B N   1 
ATOM   11710 C CA  . ASP   B 2 209  ? 112.799 106.219 122.005 1.00 111.30 0  209  ASP   B CA  1 
ATOM   11711 C C   . ASP   B 2 209  ? 113.408 106.567 120.653 1.00 110.26 0  209  ASP   B C   1 
ATOM   11712 O O   . ASP   B 2 209  ? 113.400 107.734 120.244 1.00 111.87 0  209  ASP   B O   1 
ATOM   11713 C CB  . ASP   B 2 209  ? 113.895 106.074 123.061 1.00 110.18 0  209  ASP   B CB  1 
ATOM   11714 C CG  . ASP   B 2 209  ? 113.410 106.413 124.454 1.00 111.14 0  209  ASP   B CG  1 
ATOM   11715 O OD1 . ASP   B 2 209  ? 112.250 106.853 124.591 1.00 111.39 0  209  ASP   B OD1 1 
ATOM   11716 O OD2 . ASP   B 2 209  ? 114.190 106.240 125.413 1.00 111.29 -1 209  ASP   B OD2 1 
ATOM   11717 N N   . THR   B 2 210  ? 113.939 105.570 119.941 1.00 94.75  0  210  THR   B N   1 
ATOM   11718 C CA  . THR   B 2 210  ? 114.633 105.787 118.668 1.00 92.95  0  210  THR   B CA  1 
ATOM   11719 C C   . THR   B 2 210  ? 114.019 104.867 117.618 1.00 93.73  0  210  THR   B C   1 
ATOM   11720 O O   . THR   B 2 210  ? 114.496 103.753 117.393 1.00 93.47  0  210  THR   B O   1 
ATOM   11721 C CB  . THR   B 2 210  ? 116.130 105.550 118.815 1.00 92.34  0  210  THR   B CB  1 
ATOM   11722 O OG1 . THR   B 2 210  ? 116.609 106.232 119.981 1.00 90.71  0  210  THR   B OG1 1 
ATOM   11723 C CG2 . THR   B 2 210  ? 116.866 106.070 117.593 1.00 90.39  0  210  THR   B CG2 1 
ATOM   11724 N N   . SER   B 2 211  ? 112.965 105.343 116.967 1.00 91.29  0  211  SER   B N   1 
ATOM   11725 C CA  . SER   B 2 211  ? 112.290 104.611 115.909 1.00 93.21  0  211  SER   B CA  1 
ATOM   11726 C C   . SER   B 2 211  ? 112.369 105.404 114.609 1.00 93.07  0  211  SER   B C   1 
ATOM   11727 O O   . SER   B 2 211  ? 112.917 106.507 114.558 1.00 91.77  0  211  SER   B O   1 
ATOM   11728 C CB  . SER   B 2 211  ? 110.838 104.324 116.297 1.00 92.54  0  211  SER   B CB  1 
ATOM   11729 O OG  . SER   B 2 211  ? 110.210 103.483 115.345 1.00 93.00  0  211  SER   B OG  1 
ATOM   11730 N N   . ASP   B 2 212  ? 111.813 104.821 113.543 1.00 95.65  0  212  ASP   B N   1 
ATOM   11731 C CA  . ASP   B 2 212  ? 111.759 105.526 112.267 1.00 94.42  0  212  ASP   B CA  1 
ATOM   11732 C C   . ASP   B 2 212  ? 110.916 106.787 112.369 1.00 95.77  0  212  ASP   B C   1 
ATOM   11733 O O   . ASP   B 2 212  ? 111.203 107.785 111.698 1.00 96.15  0  212  ASP   B O   1 
ATOM   11734 C CB  . ASP   B 2 212  ? 111.210 104.604 111.177 1.00 93.72  0  212  ASP   B CB  1 
ATOM   11735 C CG  . ASP   B 2 212  ? 112.152 103.459 110.855 1.00 97.59  0  212  ASP   B CG  1 
ATOM   11736 O OD1 . ASP   B 2 212  ? 113.317 103.503 111.302 1.00 96.92  0  212  ASP   B OD1 1 
ATOM   11737 O OD2 . ASP   B 2 212  ? 111.729 102.515 110.155 1.00 99.35  -1 212  ASP   B OD2 1 
ATOM   11738 N N   . GLU   B 2 213  ? 109.878 106.763 113.200 1.00 83.99  0  213  GLU   B N   1 
ATOM   11739 C CA  . GLU   B 2 213  ? 109.061 107.933 113.471 1.00 84.10  0  213  GLU   B CA  1 
ATOM   11740 C C   . GLU   B 2 213  ? 108.809 108.015 114.968 1.00 84.85  0  213  GLU   B C   1 
ATOM   11741 O O   . GLU   B 2 213  ? 108.855 107.010 115.682 1.00 85.47  0  213  GLU   B O   1 
ATOM   11742 C CB  . GLU   B 2 213  ? 107.730 107.888 112.709 1.00 81.38  0  213  GLU   B CB  1 
ATOM   11743 C CG  . GLU   B 2 213  ? 107.875 108.010 111.203 1.00 82.12  0  213  GLU   B CG  1 
ATOM   11744 C CD  . GLU   B 2 213  ? 106.541 108.088 110.496 1.00 83.76  0  213  GLU   B CD  1 
ATOM   11745 O OE1 . GLU   B 2 213  ? 105.501 108.005 111.181 1.00 82.80  0  213  GLU   B OE1 1 
ATOM   11746 O OE2 . GLU   B 2 213  ? 106.532 108.233 109.256 1.00 86.66  -1 213  GLU   B OE2 1 
ATOM   11747 N N   . VAL   B 2 214  ? 108.548 109.229 115.441 1.00 62.76  0  214  VAL   B N   1 
ATOM   11748 C CA  . VAL   B 2 214  ? 108.229 109.471 116.842 1.00 56.94  0  214  VAL   B CA  1 
ATOM   11749 C C   . VAL   B 2 214  ? 106.717 109.606 116.960 1.00 58.90  0  214  VAL   B C   1 
ATOM   11750 O O   . VAL   B 2 214  ? 106.106 110.458 116.303 1.00 59.72  0  214  VAL   B O   1 
ATOM   11751 C CB  . VAL   B 2 214  ? 108.950 110.718 117.378 1.00 57.98  0  214  VAL   B CB  1 
ATOM   11752 C CG1 . VAL   B 2 214  ? 108.195 111.304 118.555 1.00 60.36  0  214  VAL   B CG1 1 
ATOM   11753 C CG2 . VAL   B 2 214  ? 110.366 110.367 117.788 1.00 59.63  0  214  VAL   B CG2 1 
ATOM   11754 N N   . SER   B 2 215  ? 106.114 108.752 117.782 1.00 58.18  0  215  SER   B N   1 
ATOM   11755 C CA  . SER   B 2 215  ? 104.671 108.752 117.961 1.00 62.07  0  215  SER   B CA  1 
ATOM   11756 C C   . SER   B 2 215  ? 104.233 109.969 118.761 1.00 62.07  0  215  SER   B C   1 
ATOM   11757 O O   . SER   B 2 215  ? 104.915 110.395 119.697 1.00 61.00  0  215  SER   B O   1 
ATOM   11758 C CB  . SER   B 2 215  ? 104.225 107.476 118.673 1.00 61.43  0  215  SER   B CB  1 
ATOM   11759 O OG  . SER   B 2 215  ? 104.761 107.419 119.984 1.00 62.35  0  215  SER   B OG  1 
ATOM   11760 N N   . LEU   B 2 216  ? 103.083 110.524 118.394 1.00 51.76  0  216  LEU   B N   1 
ATOM   11761 C CA  . LEU   B 2 216  ? 102.552 111.690 119.085 1.00 51.65  0  216  LEU   B CA  1 
ATOM   11762 C C   . LEU   B 2 216  ? 101.750 111.253 120.305 1.00 53.24  0  216  LEU   B C   1 
ATOM   11763 O O   . LEU   B 2 216  ? 100.836 110.428 120.197 1.00 48.58  0  216  LEU   B O   1 
ATOM   11764 C CB  . LEU   B 2 216  ? 101.686 112.521 118.143 1.00 55.18  0  216  LEU   B CB  1 
ATOM   11765 C CG  . LEU   B 2 216  ? 102.415 113.524 117.250 1.00 53.94  0  216  LEU   B CG  1 
ATOM   11766 C CD1 . LEU   B 2 216  ? 101.427 114.310 116.404 1.00 51.54  0  216  LEU   B CD1 1 
ATOM   11767 C CD2 . LEU   B 2 216  ? 103.259 114.460 118.091 1.00 51.14  0  216  LEU   B CD2 1 
ATOM   11768 N N   . ASN   B 2 217  ? 102.099 111.804 121.459 1.00 65.55  0  217  ASN   B N   1 
ATOM   11769 C CA  . ASN   B 2 217  ? 101.294 111.629 122.656 1.00 68.46  0  217  ASN   B CA  1 
ATOM   11770 C C   . ASN   B 2 217  ? 99.907  112.222 122.398 1.00 68.02  0  217  ASN   B C   1 
ATOM   11771 O O   . ASN   B 2 217  ? 99.795  113.218 121.671 1.00 67.40  0  217  ASN   B O   1 
ATOM   11772 C CB  . ASN   B 2 217  ? 101.977 112.341 123.831 1.00 65.46  0  217  ASN   B CB  1 
ATOM   11773 C CG  . ASN   B 2 217  ? 101.759 111.650 125.162 1.00 70.56  0  217  ASN   B CG  1 
ATOM   11774 O OD1 . ASN   B 2 217  ? 101.293 110.516 125.226 1.00 70.32  0  217  ASN   B OD1 1 
ATOM   11775 N ND2 . ASN   B 2 217  ? 102.096 112.345 126.242 1.00 66.81  0  217  ASN   B ND2 1 
ATOM   11776 N N   . PRO   B 2 218  ? 98.833  111.637 122.944 1.00 60.57  0  218  PRO   B N   1 
ATOM   11777 C CA  . PRO   B 2 218  ? 97.485  112.138 122.608 1.00 59.16  0  218  PRO   B CA  1 
ATOM   11778 C C   . PRO   B 2 218  ? 97.297  113.631 122.830 1.00 63.37  0  218  PRO   B C   1 
ATOM   11779 O O   . PRO   B 2 218  ? 96.630  114.299 122.026 1.00 59.99  0  218  PRO   B O   1 
ATOM   11780 C CB  . PRO   B 2 218  ? 96.583  111.311 123.529 1.00 56.81  0  218  PRO   B CB  1 
ATOM   11781 C CG  . PRO   B 2 218  ? 97.304  110.036 123.700 1.00 61.06  0  218  PRO   B CG  1 
ATOM   11782 C CD  . PRO   B 2 218  ? 98.773  110.353 123.662 1.00 55.45  0  218  PRO   B CD  1 
ATOM   11783 N N   . THR   B 2 219  ? 97.872  114.179 123.902 1.00 65.74  0  219  THR   B N   1 
ATOM   11784 C CA  . THR   B 2 219  ? 97.775  115.617 124.121 1.00 59.28  0  219  THR   B CA  1 
ATOM   11785 C C   . THR   B 2 219  ? 98.496  116.379 123.018 1.00 58.75  0  219  THR   B C   1 
ATOM   11786 O O   . THR   B 2 219  ? 97.994  117.397 122.524 1.00 63.38  0  219  THR   B O   1 
ATOM   11787 C CB  . THR   B 2 219  ? 98.346  115.984 125.488 1.00 55.91  0  219  THR   B CB  1 
ATOM   11788 O OG1 . THR   B 2 219  ? 97.749  115.156 126.490 1.00 58.32  0  219  THR   B OG1 1 
ATOM   11789 C CG2 . THR   B 2 219  ? 98.028  117.430 125.810 1.00 51.17  0  219  THR   B CG2 1 
ATOM   11790 N N   . SER   B 2 220  ? 99.671  115.895 122.608 1.00 52.28  0  220  SER   B N   1 
ATOM   11791 C CA  . SER   B 2 220  ? 100.360 116.506 121.479 1.00 54.66  0  220  SER   B CA  1 
ATOM   11792 C C   . SER   B 2 220  ? 99.586  116.307 120.191 1.00 56.32  0  220  SER   B C   1 
ATOM   11793 O O   . SER   B 2 220  ? 99.635  117.164 119.306 1.00 56.59  0  220  SER   B O   1 
ATOM   11794 C CB  . SER   B 2 220  ? 101.765 115.935 121.336 1.00 55.70  0  220  SER   B CB  1 
ATOM   11795 O OG  . SER   B 2 220  ? 101.789 114.576 121.706 1.00 53.32  0  220  SER   B OG  1 
ATOM   11796 N N   . GLU   B 2 221  ? 98.855  115.198 120.071 1.00 59.79  0  221  GLU   B N   1 
ATOM   11797 C CA  . GLU   B 2 221  ? 97.972  115.035 118.923 1.00 61.69  0  221  GLU   B CA  1 
ATOM   11798 C C   . GLU   B 2 221  ? 96.939  116.152 118.872 1.00 62.26  0  221  GLU   B C   1 
ATOM   11799 O O   . GLU   B 2 221  ? 96.799  116.828 117.845 1.00 59.83  0  221  GLU   B O   1 
ATOM   11800 C CB  . GLU   B 2 221  ? 97.286  113.671 118.979 1.00 59.90  0  221  GLU   B CB  1 
ATOM   11801 C CG  . GLU   B 2 221  ? 96.433  113.353 117.763 1.00 60.00  0  221  GLU   B CG  1 
ATOM   11802 C CD  . GLU   B 2 221  ? 97.256  113.073 116.525 1.00 64.49  0  221  GLU   B CD  1 
ATOM   11803 O OE1 . GLU   B 2 221  ? 98.427  112.666 116.667 1.00 64.00  0  221  GLU   B OE1 1 
ATOM   11804 O OE2 . GLU   B 2 221  ? 96.734  113.260 115.406 1.00 66.08  -1 221  GLU   B OE2 1 
ATOM   11805 N N   . LYS   B 2 222  ? 96.238  116.384 119.986 1.00 58.33  0  222  LYS   B N   1 
ATOM   11806 C CA  . LYS   B 2 222  ? 95.230  117.440 120.034 1.00 55.84  0  222  LYS   B CA  1 
ATOM   11807 C C   . LYS   B 2 222  ? 95.852  118.800 119.750 1.00 59.53  0  222  LYS   B C   1 
ATOM   11808 O O   . LYS   B 2 222  ? 95.295  119.611 118.999 1.00 64.70  0  222  LYS   B O   1 
ATOM   11809 C CB  . LYS   B 2 222  ? 94.543  117.452 121.398 1.00 54.26  0  222  LYS   B CB  1 
ATOM   11810 C CG  . LYS   B 2 222  ? 93.714  116.218 121.704 1.00 60.81  0  222  LYS   B CG  1 
ATOM   11811 C CD  . LYS   B 2 222  ? 93.200  116.196 123.146 1.00 62.22  0  222  LYS   B CD  1 
ATOM   11812 C CE  . LYS   B 2 222  ? 92.932  117.585 123.725 1.00 61.16  0  222  LYS   B CE  1 
ATOM   11813 N NZ  . LYS   B 2 222  ? 92.034  118.432 122.884 1.00 58.67  1  222  LYS   B NZ  1 
ATOM   11814 N N   . LEU   B 2 223  ? 97.016  119.063 120.345 1.00 59.24  0  223  LEU   B N   1 
ATOM   11815 C CA  . LEU   B 2 223  ? 97.725  120.306 120.069 1.00 55.12  0  223  LEU   B CA  1 
ATOM   11816 C C   . LEU   B 2 223  ? 98.090  120.422 118.598 1.00 50.67  0  223  LEU   B C   1 
ATOM   11817 O O   . LEU   B 2 223  ? 98.146  121.530 118.060 1.00 53.94  0  223  LEU   B O   1 
ATOM   11818 C CB  . LEU   B 2 223  ? 98.975  120.398 120.944 1.00 57.68  0  223  LEU   B CB  1 
ATOM   11819 C CG  . LEU   B 2 223  ? 99.824  121.669 120.882 1.00 60.96  0  223  LEU   B CG  1 
ATOM   11820 C CD1 . LEU   B 2 223  ? 98.976  122.899 121.093 1.00 54.56  0  223  LEU   B CD1 1 
ATOM   11821 C CD2 . LEU   B 2 223  ? 100.923 121.608 121.923 1.00 57.71  0  223  LEU   B CD2 1 
ATOM   11822 N N   . ASN   B 2 224  ? 98.336  119.294 117.929 1.00 53.56  0  224  ASN   B N   1 
ATOM   11823 C CA  . ASN   B 2 224  ? 98.693  119.344 116.517 1.00 61.87  0  224  ASN   B CA  1 
ATOM   11824 C C   . ASN   B 2 224  ? 97.493  119.658 115.634 1.00 63.75  0  224  ASN   B C   1 
ATOM   11825 O O   . ASN   B 2 224  ? 97.624  120.442 114.689 1.00 63.68  0  224  ASN   B O   1 
ATOM   11826 C CB  . ASN   B 2 224  ? 99.340  118.033 116.083 1.00 60.35  0  224  ASN   B CB  1 
ATOM   11827 C CG  . ASN   B 2 224  ? 99.729  118.042 114.623 1.00 56.67  0  224  ASN   B CG  1 
ATOM   11828 O OD1 . ASN   B 2 224  ? 100.386 118.968 114.152 1.00 53.23  0  224  ASN   B OD1 1 
ATOM   11829 N ND2 . ASN   B 2 224  ? 99.327  117.007 113.897 1.00 58.81  0  224  ASN   B ND2 1 
ATOM   11830 N N   . ASN   B 2 225  ? 96.325  119.060 115.900 1.00 63.26  0  225  ASN   B N   1 
ATOM   11831 C CA  . ASN   B 2 225  ? 95.148  119.495 115.139 1.00 60.55  0  225  ASN   B CA  1 
ATOM   11832 C C   . ASN   B 2 225  ? 94.816  120.953 115.429 1.00 63.36  0  225  ASN   B C   1 
ATOM   11833 O O   . ASN   B 2 225  ? 94.370  121.682 114.537 1.00 64.06  0  225  ASN   B O   1 
ATOM   11834 C CB  . ASN   B 2 225  ? 93.897  118.631 115.365 1.00 60.35  0  225  ASN   B CB  1 
ATOM   11835 C CG  . ASN   B 2 225  ? 94.194  117.166 115.569 1.00 65.29  0  225  ASN   B CG  1 
ATOM   11836 O OD1 . ASN   B 2 225  ? 94.860  116.781 116.506 1.00 64.83  0  225  ASN   B OD1 1 
ATOM   11837 N ND2 . ASN   B 2 225  ? 93.682  116.335 114.673 1.00 65.94  0  225  ASN   B ND2 1 
ATOM   11838 N N   . LEU   B 2 226  ? 95.016  121.399 116.670 1.00 60.96  0  226  LEU   B N   1 
ATOM   11839 C CA  . LEU   B 2 226  ? 94.734  122.795 116.988 1.00 56.00  0  226  LEU   B CA  1 
ATOM   11840 C C   . LEU   B 2 226  ? 95.691  123.734 116.265 1.00 53.20  0  226  LEU   B C   1 
ATOM   11841 O O   . LEU   B 2 226  ? 95.277  124.786 115.767 1.00 53.94  0  226  LEU   B O   1 
ATOM   11842 C CB  . LEU   B 2 226  ? 94.802  123.009 118.495 1.00 52.96  0  226  LEU   B CB  1 
ATOM   11843 C CG  . LEU   B 2 226  ? 93.489  122.768 119.233 1.00 51.17  0  226  LEU   B CG  1 
ATOM   11844 C CD1 . LEU   B 2 226  ? 93.709  122.842 120.725 1.00 54.67  0  226  LEU   B CD1 1 
ATOM   11845 C CD2 . LEU   B 2 226  ? 92.445  123.772 118.794 1.00 52.25  0  226  LEU   B CD2 1 
ATOM   11846 N N   . LEU   B 2 227  ? 96.973  123.371 116.197 1.00 52.87  0  227  LEU   B N   1 
ATOM   11847 C CA  . LEU   B 2 227  ? 97.963  124.235 115.563 1.00 51.98  0  227  LEU   B CA  1 
ATOM   11848 C C   . LEU   B 2 227  ? 97.752  124.307 114.057 1.00 54.76  0  227  LEU   B C   1 
ATOM   11849 O O   . LEU   B 2 227  ? 97.777  125.395 113.471 1.00 55.49  0  227  LEU   B O   1 
ATOM   11850 C CB  . LEU   B 2 227  ? 99.370  123.736 115.886 1.00 48.87  0  227  LEU   B CB  1 
ATOM   11851 C CG  . LEU   B 2 227  ? 99.916  124.182 117.241 1.00 47.81  0  227  LEU   B CG  1 
ATOM   11852 C CD1 . LEU   B 2 227  ? 101.119 123.351 117.649 1.00 45.60  0  227  LEU   B CD1 1 
ATOM   11853 C CD2 . LEU   B 2 227  ? 100.272 125.651 117.190 1.00 50.47  0  227  LEU   B CD2 1 
ATOM   11854 N N   . GLU   B 2 228  ? 97.548  123.163 113.414 1.00 67.95  0  228  GLU   B N   1 
ATOM   11855 C CA  . GLU   B 2 228  ? 97.261  123.157 111.990 1.00 69.55  0  228  GLU   B CA  1 
ATOM   11856 C C   . GLU   B 2 228  ? 95.832  123.629 111.744 1.00 76.08  0  228  GLU   B C   1 
ATOM   11857 O O   . GLU   B 2 228  ? 94.983  123.621 112.639 1.00 74.97  0  228  GLU   B O   1 
ATOM   11858 C CB  . GLU   B 2 228  ? 97.476  121.763 111.401 1.00 65.28  0  228  GLU   B CB  1 
ATOM   11859 C CG  . GLU   B 2 228  ? 96.426  120.745 111.802 1.00 71.83  0  228  GLU   B CG  1 
ATOM   11860 C CD  . GLU   B 2 228  ? 96.778  119.340 111.354 1.00 75.09  0  228  GLU   B CD  1 
ATOM   11861 O OE1 . GLU   B 2 228  ? 97.828  119.170 110.699 1.00 73.97  0  228  GLU   B OE1 1 
ATOM   11862 O OE2 . GLU   B 2 228  ? 96.008  118.405 111.659 1.00 73.70  -1 228  GLU   B OE2 1 
ATOM   11863 N N   . GLY   B 2 229  ? 95.572  124.051 110.511 1.00 83.11  0  229  GLY   B N   1 
ATOM   11864 C CA  . GLY   B 2 229  ? 94.265  124.605 110.195 1.00 80.20  0  229  GLY   B CA  1 
ATOM   11865 C C   . GLY   B 2 229  ? 93.967  125.885 110.944 1.00 81.52  0  229  GLY   B C   1 
ATOM   11866 O O   . GLY   B 2 229  ? 92.866  126.047 111.483 1.00 81.69  0  229  GLY   B O   1 
ATOM   11867 N N   . ASN   B 2 230  ? 94.937  126.796 111.000 1.00 86.24  0  230  ASN   B N   1 
ATOM   11868 C CA  . ASN   B 2 230  ? 94.769  128.070 111.692 1.00 86.02  0  230  ASN   B CA  1 
ATOM   11869 C C   . ASN   B 2 230  ? 93.714  128.900 110.971 1.00 87.25  0  230  ASN   B C   1 
ATOM   11870 O O   . ASN   B 2 230  ? 93.954  129.402 109.869 1.00 85.42  0  230  ASN   B O   1 
ATOM   11871 C CB  . ASN   B 2 230  ? 96.105  128.805 111.753 1.00 84.66  0  230  ASN   B CB  1 
ATOM   11872 C CG  . ASN   B 2 230  ? 96.036  130.077 112.571 1.00 84.44  0  230  ASN   B CG  1 
ATOM   11873 O OD1 . ASN   B 2 230  ? 95.088  130.294 113.326 1.00 85.13  0  230  ASN   B OD1 1 
ATOM   11874 N ND2 . ASN   B 2 230  ? 97.046  130.928 112.426 1.00 81.04  0  230  ASN   B ND2 1 
ATOM   11875 N N   . ASP   B 2 231  ? 92.538  129.045 111.592 1.00 95.45  0  231  ASP   B N   1 
ATOM   11876 C CA  . ASP   B 2 231  ? 91.430  129.742 110.950 1.00 95.87  0  231  ASP   B CA  1 
ATOM   11877 C C   . ASP   B 2 231  ? 90.675  130.660 111.908 1.00 94.52  0  231  ASP   B C   1 
ATOM   11878 O O   . ASP   B 2 231  ? 89.526  131.022 111.623 1.00 93.32  0  231  ASP   B O   1 
ATOM   11879 C CB  . ASP   B 2 231  ? 90.457  128.737 110.324 1.00 94.38  0  231  ASP   B CB  1 
ATOM   11880 C CG  . ASP   B 2 231  ? 91.118  127.864 109.274 1.00 92.63  0  231  ASP   B CG  1 
ATOM   11881 O OD1 . ASP   B 2 231  ? 91.788  128.415 108.377 1.00 90.06  0  231  ASP   B OD1 1 
ATOM   11882 O OD2 . ASP   B 2 231  ? 90.972  126.625 109.347 1.00 93.47  -1 231  ASP   B OD2 1 
ATOM   11883 N N   . SER   B 2 232  ? 91.290  131.047 113.030 1.00 105.41 0  232  SER   B N   1 
ATOM   11884 C CA  . SER   B 2 232  ? 90.666  131.932 114.020 1.00 108.60 0  232  SER   B CA  1 
ATOM   11885 C C   . SER   B 2 232  ? 89.341  131.365 114.525 1.00 107.68 0  232  SER   B C   1 
ATOM   11886 O O   . SER   B 2 232  ? 88.354  132.088 114.683 1.00 105.20 0  232  SER   B O   1 
ATOM   11887 C CB  . SER   B 2 232  ? 90.471  133.344 113.460 1.00 107.62 0  232  SER   B CB  1 
ATOM   11888 O OG  . SER   B 2 232  ? 91.715  133.977 113.219 1.00 107.12 0  232  SER   B OG  1 
ATOM   11889 N N   . ASP   B 2 233  ? 89.317  130.056 114.787 1.00 109.41 0  233  ASP   B N   1 
ATOM   11890 C CA  . ASP   B 2 233  ? 88.109  129.386 115.257 1.00 110.00 0  233  ASP   B CA  1 
ATOM   11891 C C   . ASP   B 2 233  ? 88.374  128.520 116.484 1.00 109.16 0  233  ASP   B C   1 
ATOM   11892 O O   . ASP   B 2 233  ? 87.660  127.536 116.707 1.00 107.46 0  233  ASP   B O   1 
ATOM   11893 C CB  . ASP   B 2 233  ? 87.491  128.545 114.137 1.00 108.35 0  233  ASP   B CB  1 
ATOM   11894 C CG  . ASP   B 2 233  ? 88.480  127.575 113.523 1.00 108.37 0  233  ASP   B CG  1 
ATOM   11895 O OD1 . ASP   B 2 233  ? 89.672  127.627 113.890 1.00 108.11 0  233  ASP   B OD1 1 
ATOM   11896 O OD2 . ASP   B 2 233  ? 88.065  126.763 112.670 1.00 108.17 -1 233  ASP   B OD2 1 
ATOM   11897 N N   . ASN   B 2 234  ? 89.381  128.865 117.286 1.00 107.42 0  234  ASN   B N   1 
ATOM   11898 C CA  . ASN   B 2 234  ? 89.721  128.082 118.466 1.00 106.85 0  234  ASN   B CA  1 
ATOM   11899 C C   . ASN   B 2 234  ? 88.835  128.388 119.667 1.00 108.82 0  234  ASN   B C   1 
ATOM   11900 O O   . ASN   B 2 234  ? 88.907  127.660 120.663 1.00 107.55 0  234  ASN   B O   1 
ATOM   11901 C CB  . ASN   B 2 234  ? 91.193  128.303 118.830 1.00 107.41 0  234  ASN   B CB  1 
ATOM   11902 C CG  . ASN   B 2 234  ? 91.553  129.774 118.948 1.00 109.78 0  234  ASN   B CG  1 
ATOM   11903 O OD1 . ASN   B 2 234  ? 90.693  130.648 118.836 1.00 109.05 0  234  ASN   B OD1 1 
ATOM   11904 N ND2 . ASN   B 2 234  ? 92.834  130.054 119.171 1.00 105.71 0  234  ASN   B ND2 1 
ATOM   11905 N N   . ASP   B 2 235  ? 88.005  129.433 119.596 1.00 111.03 0  235  ASP   B N   1 
ATOM   11906 C CA  . ASP   B 2 235  ? 87.051  129.785 120.650 1.00 109.18 0  235  ASP   B CA  1 
ATOM   11907 C C   . ASP   B 2 235  ? 87.768  130.036 121.981 1.00 108.23 0  235  ASP   B C   1 
ATOM   11908 O O   . ASP   B 2 235  ? 87.605  129.314 122.967 1.00 109.32 0  235  ASP   B O   1 
ATOM   11909 C CB  . ASP   B 2 235  ? 85.974  128.702 120.794 1.00 108.77 0  235  ASP   B CB  1 
ATOM   11910 C CG  . ASP   B 2 235  ? 85.014  128.677 119.621 1.00 108.88 0  235  ASP   B CG  1 
ATOM   11911 O OD1 . ASP   B 2 235  ? 84.663  129.763 119.114 1.00 108.33 0  235  ASP   B OD1 1 
ATOM   11912 O OD2 . ASP   B 2 235  ? 84.613  127.570 119.203 1.00 108.88 -1 235  ASP   B OD2 1 
ATOM   11913 N N   . LEU   B 2 236  ? 88.576  131.092 121.975 1.00 98.08  0  236  LEU   B N   1 
ATOM   11914 C CA  . LEU   B 2 236  ? 89.374  131.492 123.127 1.00 100.48 0  236  LEU   B CA  1 
ATOM   11915 C C   . LEU   B 2 236  ? 88.783  132.752 123.748 1.00 99.31  0  236  LEU   B C   1 
ATOM   11916 O O   . LEU   B 2 236  ? 88.502  133.725 123.040 1.00 99.75  0  236  LEU   B O   1 
ATOM   11917 C CB  . LEU   B 2 236  ? 90.829  131.725 122.716 1.00 102.25 0  236  LEU   B CB  1 
ATOM   11918 C CG  . LEU   B 2 236  ? 91.824  132.214 123.766 1.00 101.23 0  236  LEU   B CG  1 
ATOM   11919 C CD1 . LEU   B 2 236  ? 91.767  131.355 125.018 1.00 100.19 0  236  LEU   B CD1 1 
ATOM   11920 C CD2 . LEU   B 2 236  ? 93.219  132.199 123.175 1.00 95.53  0  236  LEU   B CD2 1 
ATOM   11921 N N   . SER   B 2 237  ? 88.596  132.730 125.069 1.00 99.93  0  237  SER   B N   1 
ATOM   11922 C CA  . SER   B 2 237  ? 88.016  133.846 125.821 1.00 101.30 0  237  SER   B CA  1 
ATOM   11923 C C   . SER   B 2 237  ? 88.975  134.193 126.958 1.00 100.01 0  237  SER   B C   1 
ATOM   11924 O O   . SER   B 2 237  ? 88.971  133.545 128.008 1.00 99.44  0  237  SER   B O   1 
ATOM   11925 C CB  . SER   B 2 237  ? 86.623  133.491 126.339 1.00 100.69 0  237  SER   B CB  1 
ATOM   11926 O OG  . SER   B 2 237  ? 86.098  134.524 127.155 1.00 101.79 0  237  SER   B OG  1 
ATOM   11927 N N   . LEU   B 2 238  ? 89.795  135.225 126.744 1.00 94.86  0  238  LEU   B N   1 
ATOM   11928 C CA  . LEU   B 2 238  ? 90.828  135.567 127.718 1.00 95.66  0  238  LEU   B CA  1 
ATOM   11929 C C   . LEU   B 2 238  ? 90.240  136.249 128.947 1.00 94.52  0  238  LEU   B C   1 
ATOM   11930 O O   . LEU   B 2 238  ? 90.706  136.023 130.070 1.00 93.24  0  238  LEU   B O   1 
ATOM   11931 C CB  . LEU   B 2 238  ? 91.886  136.463 127.073 1.00 94.12  0  238  LEU   B CB  1 
ATOM   11932 C CG  . LEU   B 2 238  ? 92.898  135.821 126.124 1.00 92.78  0  238  LEU   B CG  1 
ATOM   11933 C CD1 . LEU   B 2 238  ? 92.325  135.703 124.723 1.00 90.43  0  238  LEU   B CD1 1 
ATOM   11934 C CD2 . LEU   B 2 238  ? 94.194  136.618 126.111 1.00 91.55  0  238  LEU   B CD2 1 
ATOM   11935 N N   . GLU   B 2 239  ? 89.222  137.089 128.756 1.00 105.71 0  239  GLU   B N   1 
ATOM   11936 C CA  . GLU   B 2 239  ? 88.697  137.901 129.848 1.00 107.16 0  239  GLU   B CA  1 
ATOM   11937 C C   . GLU   B 2 239  ? 87.970  137.084 130.909 1.00 106.88 0  239  GLU   B C   1 
ATOM   11938 O O   . GLU   B 2 239  ? 87.698  137.615 131.991 1.00 104.91 0  239  GLU   B O   1 
ATOM   11939 C CB  . GLU   B 2 239  ? 87.770  138.982 129.290 1.00 106.89 0  239  GLU   B CB  1 
ATOM   11940 C CG  . GLU   B 2 239  ? 88.501  140.240 128.843 1.00 106.05 0  239  GLU   B CG  1 
ATOM   11941 C CD  . GLU   B 2 239  ? 89.329  140.025 127.589 1.00 107.35 0  239  GLU   B CD  1 
ATOM   11942 O OE1 . GLU   B 2 239  ? 89.066  139.047 126.858 1.00 108.42 0  239  GLU   B OE1 1 
ATOM   11943 O OE2 . GLU   B 2 239  ? 90.250  140.830 127.337 1.00 105.09 -1 239  GLU   B OE2 1 
ATOM   11944 N N   . ASP   B 2 240  ? 87.653  135.819 130.633 1.00 104.36 0  240  ASP   B N   1 
ATOM   11945 C CA  . ASP   B 2 240  ? 87.052  134.952 131.638 1.00 102.94 0  240  ASP   B CA  1 
ATOM   11946 C C   . ASP   B 2 240  ? 88.085  134.250 132.508 1.00 102.95 0  240  ASP   B C   1 
ATOM   11947 O O   . ASP   B 2 240  ? 87.702  133.541 133.445 1.00 100.95 0  240  ASP   B O   1 
ATOM   11948 C CB  . ASP   B 2 240  ? 86.157  133.908 130.966 1.00 102.42 0  240  ASP   B CB  1 
ATOM   11949 C CG  . ASP   B 2 240  ? 84.846  134.490 130.480 1.00 102.40 0  240  ASP   B CG  1 
ATOM   11950 O OD1 . ASP   B 2 240  ? 84.211  135.246 131.245 1.00 101.80 0  240  ASP   B OD1 1 
ATOM   11951 O OD2 . ASP   B 2 240  ? 84.454  134.196 129.331 1.00 102.42 -1 240  ASP   B OD2 1 
ATOM   11952 N N   . PHE   B 2 241  ? 89.372  134.432 132.227 1.00 96.10  0  241  PHE   B N   1 
ATOM   11953 C CA  . PHE   B 2 241  ? 90.432  133.775 132.984 1.00 91.12  0  241  PHE   B CA  1 
ATOM   11954 C C   . PHE   B 2 241  ? 90.491  134.288 134.418 1.00 90.80  0  241  PHE   B C   1 
ATOM   11955 O O   . PHE   B 2 241  ? 90.172  135.444 134.693 1.00 92.21  0  241  PHE   B O   1 
ATOM   11956 C CB  . PHE   B 2 241  ? 91.784  133.981 132.297 1.00 89.15  0  241  PHE   B CB  1 
ATOM   11957 C CG  . PHE   B 2 241  ? 91.918  133.253 130.987 1.00 92.14  0  241  PHE   B CG  1 
ATOM   11958 C CD1 . PHE   B 2 241  ? 91.099  132.179 130.686 1.00 90.98  0  241  PHE   B CD1 1 
ATOM   11959 C CD2 . PHE   B 2 241  ? 92.864  133.646 130.056 1.00 89.84  0  241  PHE   B CD2 1 
ATOM   11960 C CE1 . PHE   B 2 241  ? 91.223  131.510 129.483 1.00 88.31  0  241  PHE   B CE1 1 
ATOM   11961 C CE2 . PHE   B 2 241  ? 92.991  132.981 128.853 1.00 89.19  0  241  PHE   B CE2 1 
ATOM   11962 C CZ  . PHE   B 2 241  ? 92.169  131.912 128.567 1.00 86.26  0  241  PHE   B CZ  1 
ATOM   11963 N N   . ASN   C 2 130  ? 154.376 76.974  113.493 1.00 100.90 0  130  ASN   C N   1 
ATOM   11964 C CA  . ASN   C 2 130  ? 153.163 77.579  114.029 1.00 102.46 0  130  ASN   C CA  1 
ATOM   11965 C C   . ASN   C 2 130  ? 153.182 77.602  115.552 1.00 101.36 0  130  ASN   C C   1 
ATOM   11966 O O   . ASN   C 2 130  ? 152.243 78.087  116.182 1.00 102.35 0  130  ASN   C O   1 
ATOM   11967 C CB  . ASN   C 2 130  ? 151.923 76.831  113.534 1.00 103.03 0  130  ASN   C CB  1 
ATOM   11968 C CG  . ASN   C 2 130  ? 151.552 77.193  112.109 1.00 102.37 0  130  ASN   C CG  1 
ATOM   11969 O OD1 . ASN   C 2 130  ? 151.819 78.302  111.647 1.00 101.27 0  130  ASN   C OD1 1 
ATOM   11970 N ND2 . ASN   C 2 130  ? 150.927 76.256  111.405 1.00 102.52 0  130  ASN   C ND2 1 
ATOM   11971 N N   . ILE   C 2 131  ? 154.252 77.066  116.141 1.00 99.24  0  131  ILE   C N   1 
ATOM   11972 C CA  . ILE   C 2 131  ? 154.383 77.091  117.595 1.00 101.93 0  131  ILE   C CA  1 
ATOM   11973 C C   . ILE   C 2 131  ? 154.482 78.526  118.093 1.00 104.75 0  131  ILE   C C   1 
ATOM   11974 O O   . ILE   C 2 131  ? 153.854 78.900  119.092 1.00 103.70 0  131  ILE   C O   1 
ATOM   11975 C CB  . ILE   C 2 131  ? 155.594 76.249  118.038 1.00 100.35 0  131  ILE   C CB  1 
ATOM   11976 C CG1 . ILE   C 2 131  ? 155.440 74.811  117.545 1.00 101.95 0  131  ILE   C CG1 1 
ATOM   11977 C CG2 . ILE   C 2 131  ? 155.740 76.278  119.549 1.00 98.81  0  131  ILE   C CG2 1 
ATOM   11978 C CD1 . ILE   C 2 131  ? 154.130 74.167  117.943 1.00 101.76 0  131  ILE   C CD1 1 
ATOM   11979 N N   . THR   C 2 132  ? 155.269 79.354  117.403 1.00 106.09 0  132  THR   C N   1 
ATOM   11980 C CA  . THR   C 2 132  ? 155.365 80.761  117.776 1.00 103.90 0  132  THR   C CA  1 
ATOM   11981 C C   . THR   C 2 132  ? 154.034 81.477  117.594 1.00 102.12 0  132  THR   C C   1 
ATOM   11982 O O   . THR   C 2 132  ? 153.694 82.359  118.389 1.00 101.91 0  132  THR   C O   1 
ATOM   11983 C CB  . THR   C 2 132  ? 156.457 81.452  116.961 1.00 101.65 0  132  THR   C CB  1 
ATOM   11984 O OG1 . THR   C 2 132  ? 156.257 81.185  115.567 1.00 104.11 0  132  THR   C OG1 1 
ATOM   11985 C CG2 . THR   C 2 132  ? 157.831 80.946  117.379 1.00 99.92  0  132  THR   C CG2 1 
ATOM   11986 N N   . ALA   C 2 133  ? 153.268 81.117  116.562 1.00 98.85  0  133  ALA   C N   1 
ATOM   11987 C CA  . ALA   C 2 133  ? 151.948 81.715  116.383 1.00 98.55  0  133  ALA   C CA  1 
ATOM   11988 C C   . ALA   C 2 133  ? 151.018 81.357  117.537 1.00 98.18  0  133  ALA   C C   1 
ATOM   11989 O O   . ALA   C 2 133  ? 150.278 82.213  118.038 1.00 98.79  0  133  ALA   C O   1 
ATOM   11990 C CB  . ALA   C 2 133  ? 151.347 81.275  115.049 1.00 97.87  0  133  ALA   C CB  1 
ATOM   11991 N N   . ARG   C 2 134  ? 151.039 80.093  117.970 1.00 96.08  0  134  ARG   C N   1 
ATOM   11992 C CA  . ARG   C 2 134  ? 150.232 79.694  119.118 1.00 97.24  0  134  ARG   C CA  1 
ATOM   11993 C C   . ARG   C 2 134  ? 150.670 80.429  120.375 1.00 97.00  0  134  ARG   C C   1 
ATOM   11994 O O   . ARG   C 2 134  ? 149.832 80.867  121.173 1.00 97.55  0  134  ARG   C O   1 
ATOM   11995 C CB  . ARG   C 2 134  ? 150.318 78.183  119.329 1.00 96.33  0  134  ARG   C CB  1 
ATOM   11996 C CG  . ARG   C 2 134  ? 149.288 77.378  118.557 1.00 94.64  0  134  ARG   C CG  1 
ATOM   11997 C CD  . ARG   C 2 134  ? 149.148 75.981  119.141 1.00 95.71  0  134  ARG   C CD  1 
ATOM   11998 N NE  . ARG   C 2 134  ? 148.260 75.139  118.350 1.00 99.89  0  134  ARG   C NE  1 
ATOM   11999 C CZ  . ARG   C 2 134  ? 148.654 74.377  117.339 1.00 100.20 0  134  ARG   C CZ  1 
ATOM   12000 N NH1 . ARG   C 2 134  ? 149.921 74.334  116.959 1.00 98.51  1  134  ARG   C NH1 1 
ATOM   12001 N NH2 . ARG   C 2 134  ? 147.756 73.639  116.692 1.00 97.01  0  134  ARG   C NH2 1 
ATOM   12002 N N   . LEU   C 2 135  ? 151.983 80.574  120.569 1.00 90.80  0  135  LEU   C N   1 
ATOM   12003 C CA  . LEU   C 2 135  ? 152.478 81.303  121.731 1.00 94.50  0  135  LEU   C CA  1 
ATOM   12004 C C   . LEU   C 2 135  ? 152.037 82.760  121.694 1.00 94.97  0  135  LEU   C C   1 
ATOM   12005 O O   . LEU   C 2 135  ? 151.678 83.333  122.727 1.00 92.82  0  135  LEU   C O   1 
ATOM   12006 C CB  . LEU   C 2 135  ? 154.000 81.200  121.807 1.00 93.37  0  135  LEU   C CB  1 
ATOM   12007 C CG  . LEU   C 2 135  ? 154.559 79.880  122.339 1.00 91.95  0  135  LEU   C CG  1 
ATOM   12008 C CD1 . LEU   C 2 135  ? 156.070 79.848  122.203 1.00 92.63  0  135  LEU   C CD1 1 
ATOM   12009 C CD2 . LEU   C 2 135  ? 154.144 79.662  123.785 1.00 90.18  0  135  LEU   C CD2 1 
ATOM   12010 N N   . ASP   C 2 136  ? 152.051 83.375  120.510 1.00 90.75  0  136  ASP   C N   1 
ATOM   12011 C CA  . ASP   C 2 136  ? 151.625 84.766  120.390 1.00 88.95  0  136  ASP   C CA  1 
ATOM   12012 C C   . ASP   C 2 136  ? 150.132 84.919  120.656 1.00 92.66  0  136  ASP   C C   1 
ATOM   12013 O O   . ASP   C 2 136  ? 149.708 85.885  121.301 1.00 93.37  0  136  ASP   C O   1 
ATOM   12014 C CB  . ASP   C 2 136  ? 151.984 85.303  119.006 1.00 87.96  0  136  ASP   C CB  1 
ATOM   12015 C CG  . ASP   C 2 136  ? 153.440 85.700  118.900 1.00 89.69  0  136  ASP   C CG  1 
ATOM   12016 O OD1 . ASP   C 2 136  ? 154.102 85.812  119.952 1.00 89.09  0  136  ASP   C OD1 1 
ATOM   12017 O OD2 . ASP   C 2 136  ? 153.924 85.896  117.766 1.00 92.01  -1 136  ASP   C OD2 1 
ATOM   12018 N N   . ARG   C 2 137  ? 149.317 83.987  120.156 1.00 89.01  0  137  ARG   C N   1 
ATOM   12019 C CA  . ARG   C 2 137  ? 147.886 84.041  120.440 1.00 85.72  0  137  ARG   C CA  1 
ATOM   12020 C C   . ARG   C 2 137  ? 147.617 83.873  121.929 1.00 86.97  0  137  ARG   C C   1 
ATOM   12021 O O   . ARG   C 2 137  ? 146.788 84.591  122.507 1.00 88.50  0  137  ARG   C O   1 
ATOM   12022 C CB  . ARG   C 2 137  ? 147.150 82.972  119.635 1.00 84.03  0  137  ARG   C CB  1 
ATOM   12023 C CG  . ARG   C 2 137  ? 146.756 83.420  118.242 1.00 85.52  0  137  ARG   C CG  1 
ATOM   12024 C CD  . ARG   C 2 137  ? 145.939 82.357  117.531 1.00 89.81  0  137  ARG   C CD  1 
ATOM   12025 N NE  . ARG   C 2 137  ? 146.779 81.286  117.009 1.00 90.02  0  137  ARG   C NE  1 
ATOM   12026 C CZ  . ARG   C 2 137  ? 147.328 81.283  115.802 1.00 87.16  0  137  ARG   C CZ  1 
ATOM   12027 N NH1 . ARG   C 2 137  ? 147.143 82.283  114.956 1.00 85.81  1  137  ARG   C NH1 1 
ATOM   12028 N NH2 . ARG   C 2 137  ? 148.082 80.251  115.435 1.00 86.88  0  137  ARG   C NH2 1 
ATOM   12029 N N   . ILE   C 2 138  ? 148.318 82.937  122.570 1.00 85.07  0  138  ILE   C N   1 
ATOM   12030 C CA  . ILE   C 2 138  ? 148.166 82.745  124.008 1.00 85.88  0  138  ILE   C CA  1 
ATOM   12031 C C   . ILE   C 2 138  ? 148.601 83.997  124.757 1.00 84.71  0  138  ILE   C C   1 
ATOM   12032 O O   . ILE   C 2 138  ? 147.971 84.401  125.741 1.00 84.11  0  138  ILE   C O   1 
ATOM   12033 C CB  . ILE   C 2 138  ? 148.952 81.500  124.461 1.00 85.19  0  138  ILE   C CB  1 
ATOM   12034 C CG1 . ILE   C 2 138  ? 148.203 80.230  124.060 1.00 84.35  0  138  ILE   C CG1 1 
ATOM   12035 C CG2 . ILE   C 2 138  ? 149.198 81.524  125.960 1.00 83.98  0  138  ILE   C CG2 1 
ATOM   12036 C CD1 . ILE   C 2 138  ? 149.037 78.977  124.157 1.00 85.79  0  138  ILE   C CD1 1 
ATOM   12037 N N   . ASP   C 2 139  ? 149.676 84.637  124.296 1.00 82.82  0  139  ASP   C N   1 
ATOM   12038 C CA  . ASP   C 2 139  ? 150.157 85.851  124.944 1.00 85.04  0  139  ASP   C CA  1 
ATOM   12039 C C   . ASP   C 2 139  ? 149.153 86.989  124.810 1.00 86.74  0  139  ASP   C C   1 
ATOM   12040 O O   . ASP   C 2 139  ? 148.934 87.742  125.764 1.00 88.76  0  139  ASP   C O   1 
ATOM   12041 C CB  . ASP   C 2 139  ? 151.509 86.252  124.358 1.00 86.41  0  139  ASP   C CB  1 
ATOM   12042 C CG  . ASP   C 2 139  ? 152.335 87.079  125.317 1.00 87.59  0  139  ASP   C CG  1 
ATOM   12043 O OD1 . ASP   C 2 139  ? 152.626 86.588  126.428 1.00 85.53  0  139  ASP   C OD1 1 
ATOM   12044 O OD2 . ASP   C 2 139  ? 152.700 88.217  124.958 1.00 88.07  -1 139  ASP   C OD2 1 
ATOM   12045 N N   . GLU   C 2 140  ? 148.534 87.137  123.637 1.00 78.07  0  140  GLU   C N   1 
ATOM   12046 C CA  . GLU   C 2 140  ? 147.526 88.180  123.473 1.00 80.28  0  140  GLU   C CA  1 
ATOM   12047 C C   . GLU   C 2 140  ? 146.290 87.911  124.324 1.00 78.07  0  140  GLU   C C   1 
ATOM   12048 O O   . GLU   C 2 140  ? 145.709 88.848  124.887 1.00 76.05  0  140  GLU   C O   1 
ATOM   12049 C CB  . GLU   C 2 140  ? 147.140 88.322  122.003 1.00 76.88  0  140  GLU   C CB  1 
ATOM   12050 C CG  . GLU   C 2 140  ? 146.114 89.412  121.756 1.00 77.59  0  140  GLU   C CG  1 
ATOM   12051 C CD  . GLU   C 2 140  ? 146.414 90.230  120.521 1.00 79.23  0  140  GLU   C CD  1 
ATOM   12052 O OE1 . GLU   C 2 140  ? 147.578 90.225  120.070 1.00 74.36  0  140  GLU   C OE1 1 
ATOM   12053 O OE2 . GLU   C 2 140  ? 145.487 90.887  120.005 1.00 82.68  -1 140  GLU   C OE2 1 
ATOM   12054 N N   . LYS   C 2 141  ? 145.868 86.651  124.430 1.00 73.27  0  141  LYS   C N   1 
ATOM   12055 C CA  . LYS   C 2 141  ? 144.750 86.338  125.316 1.00 73.79  0  141  LYS   C CA  1 
ATOM   12056 C C   . LYS   C 2 141  ? 145.107 86.619  126.772 1.00 72.37  0  141  LYS   C C   1 
ATOM   12057 O O   . LYS   C 2 141  ? 144.276 87.122  127.539 1.00 77.50  0  141  LYS   C O   1 
ATOM   12058 C CB  . LYS   C 2 141  ? 144.323 84.886  125.127 1.00 75.93  0  141  LYS   C CB  1 
ATOM   12059 C CG  . LYS   C 2 141  ? 143.446 84.669  123.909 1.00 74.65  0  141  LYS   C CG  1 
ATOM   12060 C CD  . LYS   C 2 141  ? 143.136 83.200  123.699 1.00 75.84  0  141  LYS   C CD  1 
ATOM   12061 C CE  . LYS   C 2 141  ? 142.444 82.977  122.364 1.00 77.31  0  141  LYS   C CE  1 
ATOM   12062 N NZ  . LYS   C 2 141  ? 142.305 81.531  122.040 1.00 78.23  1  141  LYS   C NZ  1 
ATOM   12063 N N   . LEU   C 2 142  ? 146.342 86.310  127.170 1.00 68.14  0  142  LEU   C N   1 
ATOM   12064 C CA  . LEU   C 2 142  ? 146.791 86.648  128.516 1.00 70.22  0  142  LEU   C CA  1 
ATOM   12065 C C   . LEU   C 2 142  ? 146.805 88.155  128.724 1.00 71.91  0  142  LEU   C C   1 
ATOM   12066 O O   . LEU   C 2 142  ? 146.501 88.642  129.817 1.00 75.44  0  142  LEU   C O   1 
ATOM   12067 C CB  . LEU   C 2 142  ? 148.177 86.060  128.766 1.00 70.16  0  142  LEU   C CB  1 
ATOM   12068 C CG  . LEU   C 2 142  ? 148.212 84.562  129.052 1.00 70.56  0  142  LEU   C CG  1 
ATOM   12069 C CD1 . LEU   C 2 142  ? 149.575 83.993  128.715 1.00 73.74  0  142  LEU   C CD1 1 
ATOM   12070 C CD2 . LEU   C 2 142  ? 147.862 84.304  130.504 1.00 69.93  0  142  LEU   C CD2 1 
ATOM   12071 N N   . SER   C 2 143  ? 147.169 88.907  127.687 1.00 63.48  0  143  SER   C N   1 
ATOM   12072 C CA  . SER   C 2 143  ? 147.150 90.362  127.781 1.00 62.36  0  143  SER   C CA  1 
ATOM   12073 C C   . SER   C 2 143  ? 145.732 90.883  127.974 1.00 66.70  0  143  SER   C C   1 
ATOM   12074 O O   . SER   C 2 143  ? 145.504 91.808  128.762 1.00 66.75  0  143  SER   C O   1 
ATOM   12075 C CB  . SER   C 2 143  ? 147.782 90.967  126.532 1.00 60.47  0  143  SER   C CB  1 
ATOM   12076 O OG  . SER   C 2 143  ? 148.120 92.323  126.740 1.00 68.48  0  143  SER   C OG  1 
ATOM   12077 N N   . GLU   C 2 144  ? 144.766 90.307  127.254 1.00 69.53  0  144  GLU   C N   1 
ATOM   12078 C CA  . GLU   C 2 144  ? 143.369 90.688  127.461 1.00 63.91  0  144  GLU   C CA  1 
ATOM   12079 C C   . GLU   C 2 144  ? 142.918 90.370  128.880 1.00 59.54  0  144  GLU   C C   1 
ATOM   12080 O O   . GLU   C 2 144  ? 142.201 91.162  129.506 1.00 63.43  0  144  GLU   C O   1 
ATOM   12081 C CB  . GLU   C 2 144  ? 142.460 89.976  126.464 1.00 65.39  0  144  GLU   C CB  1 
ATOM   12082 C CG  . GLU   C 2 144  ? 141.026 90.470  126.520 1.00 66.10  0  144  GLU   C CG  1 
ATOM   12083 C CD  . GLU   C 2 144  ? 140.106 89.723  125.578 1.00 72.92  0  144  GLU   C CD  1 
ATOM   12084 O OE1 . GLU   C 2 144  ? 140.591 89.215  124.551 1.00 74.71  0  144  GLU   C OE1 1 
ATOM   12085 O OE2 . GLU   C 2 144  ? 138.891 89.652  125.862 1.00 68.81  -1 144  GLU   C OE2 1 
ATOM   12086 N N   . ILE   C 2 145  ? 143.307 89.201  129.392 1.00 59.64  0  145  ILE   C N   1 
ATOM   12087 C CA  . ILE   C 2 145  ? 142.966 88.837  130.766 1.00 60.09  0  145  ILE   C CA  1 
ATOM   12088 C C   . ILE   C 2 145  ? 143.559 89.844  131.741 1.00 63.73  0  145  ILE   C C   1 
ATOM   12089 O O   . ILE   C 2 145  ? 142.900 90.268  132.698 1.00 67.33  0  145  ILE   C O   1 
ATOM   12090 C CB  . ILE   C 2 145  ? 143.444 87.407  131.075 1.00 60.72  0  145  ILE   C CB  1 
ATOM   12091 C CG1 . ILE   C 2 145  ? 142.685 86.392  130.224 1.00 62.27  0  145  ILE   C CG1 1 
ATOM   12092 C CG2 . ILE   C 2 145  ? 143.275 87.090  132.548 1.00 62.61  0  145  ILE   C CG2 1 
ATOM   12093 C CD1 . ILE   C 2 145  ? 143.334 85.036  130.188 1.00 65.61  0  145  ILE   C CD1 1 
ATOM   12094 N N   . LEU   C 2 146  ? 144.812 90.240  131.513 1.00 59.27  0  146  LEU   C N   1 
ATOM   12095 C CA  . LEU   C 2 146  ? 145.456 91.225  132.375 1.00 60.78  0  146  LEU   C CA  1 
ATOM   12096 C C   . LEU   C 2 146  ? 144.733 92.564  132.326 1.00 60.72  0  146  LEU   C C   1 
ATOM   12097 O O   . LEU   C 2 146  ? 144.527 93.199  133.364 1.00 63.65  0  146  LEU   C O   1 
ATOM   12098 C CB  . LEU   C 2 146  ? 146.917 91.395  131.970 1.00 62.88  0  146  LEU   C CB  1 
ATOM   12099 C CG  . LEU   C 2 146  ? 147.920 90.471  132.653 1.00 63.77  0  146  LEU   C CG  1 
ATOM   12100 C CD1 . LEU   C 2 146  ? 149.155 90.321  131.795 1.00 65.81  0  146  LEU   C CD1 1 
ATOM   12101 C CD2 . LEU   C 2 146  ? 148.282 91.009  134.023 1.00 62.91  0  146  LEU   C CD2 1 
ATOM   12102 N N   . GLY   C 2 147  ? 144.339 93.007  131.132 1.00 52.91  0  147  GLY   C N   1 
ATOM   12103 C CA  . GLY   C 2 147  ? 143.617 94.264  131.025 1.00 49.85  0  147  GLY   C CA  1 
ATOM   12104 C C   . GLY   C 2 147  ? 142.287 94.232  131.754 1.00 58.78  0  147  GLY   C C   1 
ATOM   12105 O O   . GLY   C 2 147  ? 141.946 95.156  132.499 1.00 62.53  0  147  GLY   C O   1 
ATOM   12106 N N   . MET   C 2 148  ? 141.519 93.158  131.556 1.00 63.84  0  148  MET   C N   1 
ATOM   12107 C CA  . MET   C 2 148  ? 140.226 93.051  132.226 1.00 53.85  0  148  MET   C CA  1 
ATOM   12108 C C   . MET   C 2 148  ? 140.388 92.995  133.738 1.00 48.47  0  148  MET   C C   1 
ATOM   12109 O O   . MET   C 2 148  ? 139.652 93.665  134.471 1.00 59.46  0  148  MET   C O   1 
ATOM   12110 C CB  . MET   C 2 148  ? 139.471 91.822  131.727 1.00 55.81  0  148  MET   C CB  1 
ATOM   12111 C CG  . MET   C 2 148  ? 138.603 92.076  130.515 1.00 57.76  0  148  MET   C CG  1 
ATOM   12112 S SD  . MET   C 2 148  ? 137.245 90.903  130.417 1.00 77.74  0  148  MET   C SD  1 
ATOM   12113 C CE  . MET   C 2 148  ? 136.976 90.850  128.651 1.00 64.41  0  148  MET   C CE  1 
ATOM   12114 N N   . LEU   C 2 149  ? 141.350 92.210  134.226 1.00 45.67  0  149  LEU   C N   1 
ATOM   12115 C CA  . LEU   C 2 149  ? 141.541 92.109  135.666 1.00 49.83  0  149  LEU   C CA  1 
ATOM   12116 C C   . LEU   C 2 149  ? 142.045 93.418  136.256 1.00 55.33  0  149  LEU   C C   1 
ATOM   12117 O O   . LEU   C 2 149  ? 141.673 93.771  137.380 1.00 64.03  0  149  LEU   C O   1 
ATOM   12118 C CB  . LEU   C 2 149  ? 142.497 90.965  135.988 1.00 55.93  0  149  LEU   C CB  1 
ATOM   12119 C CG  . LEU   C 2 149  ? 141.965 89.560  135.706 1.00 63.42  0  149  LEU   C CG  1 
ATOM   12120 C CD1 . LEU   C 2 149  ? 143.027 88.521  136.005 1.00 65.45  0  149  LEU   C CD1 1 
ATOM   12121 C CD2 . LEU   C 2 149  ? 140.702 89.285  136.503 1.00 58.66  0  149  LEU   C CD2 1 
ATOM   12122 N N   . HIS   C 2 150  ? 142.875 94.161  135.520 1.00 49.29  0  150  HIS   C N   1 
ATOM   12123 C CA  . HIS   C 2 150  ? 143.322 95.460  136.012 1.00 49.14  0  150  HIS   C CA  1 
ATOM   12124 C C   . HIS   C 2 150  ? 142.169 96.449  136.087 1.00 49.72  0  150  HIS   C C   1 
ATOM   12125 O O   . HIS   C 2 150  ? 142.062 97.217  137.051 1.00 51.18  0  150  HIS   C O   1 
ATOM   12126 C CB  . HIS   C 2 150  ? 144.433 96.018  135.127 1.00 45.75  0  150  HIS   C CB  1 
ATOM   12127 C CG  . HIS   C 2 150  ? 145.010 97.300  135.636 1.00 45.60  0  150  HIS   C CG  1 
ATOM   12128 N ND1 . HIS   C 2 150  ? 145.364 98.340  134.806 1.00 45.69  0  150  HIS   C ND1 1 
ATOM   12129 C CD2 . HIS   C 2 150  ? 145.282 97.715  136.896 1.00 48.02  0  150  HIS   C CD2 1 
ATOM   12130 C CE1 . HIS   C 2 150  ? 145.834 99.338  135.531 1.00 45.58  0  150  HIS   C CE1 1 
ATOM   12131 N NE2 . HIS   C 2 150  ? 145.796 98.984  136.802 1.00 47.08  0  150  HIS   C NE2 1 
ATOM   12132 N N   . THR   C 2 151  ? 141.308 96.468  135.068 1.00 46.54  0  151  THR   C N   1 
ATOM   12133 C CA  . THR   C 2 151  ? 140.151 97.354  135.126 1.00 41.66  0  151  THR   C CA  1 
ATOM   12134 C C   . THR   C 2 151  ? 139.228 96.977  136.275 1.00 37.37  0  151  THR   C C   1 
ATOM   12135 O O   . THR   C 2 151  ? 138.668 97.856  136.937 1.00 39.54  0  151  THR   C O   1 
ATOM   12136 C CB  . THR   C 2 151  ? 139.397 97.332  133.800 1.00 42.32  0  151  THR   C CB  1 
ATOM   12137 O OG1 . THR   C 2 151  ? 140.285 97.706  132.742 1.00 41.46  0  151  THR   C OG1 1 
ATOM   12138 C CG2 . THR   C 2 151  ? 138.240 98.309  133.834 1.00 40.59  0  151  THR   C CG2 1 
ATOM   12139 N N   . LEU   C 2 152  ? 139.066 95.679  136.534 1.00 46.03  0  152  LEU   C N   1 
ATOM   12140 C CA  . LEU   C 2 152  ? 138.287 95.248  137.689 1.00 44.32  0  152  LEU   C CA  1 
ATOM   12141 C C   . LEU   C 2 152  ? 138.933 95.700  138.994 1.00 47.29  0  152  LEU   C C   1 
ATOM   12142 O O   . LEU   C 2 152  ? 138.233 96.086  139.936 1.00 54.75  0  152  LEU   C O   1 
ATOM   12143 C CB  . LEU   C 2 152  ? 138.118 93.730  137.668 1.00 42.53  0  152  LEU   C CB  1 
ATOM   12144 C CG  . LEU   C 2 152  ? 137.276 93.108  138.779 1.00 41.77  0  152  LEU   C CG  1 
ATOM   12145 C CD1 . LEU   C 2 152  ? 135.880 93.687  138.767 1.00 47.28  0  152  LEU   C CD1 1 
ATOM   12146 C CD2 . LEU   C 2 152  ? 137.226 91.606  138.612 1.00 48.26  0  152  LEU   C CD2 1 
ATOM   12147 N N   . VAL   C 2 153  ? 140.264 95.651  139.073 1.00 39.62  0  153  VAL   C N   1 
ATOM   12148 C CA  . VAL   C 2 153  ? 140.955 96.121  140.271 1.00 38.60  0  153  VAL   C CA  1 
ATOM   12149 C C   . VAL   C 2 153  ? 140.730 97.614  140.471 1.00 43.41  0  153  VAL   C C   1 
ATOM   12150 O O   . VAL   C 2 153  ? 140.463 98.071  141.588 1.00 49.73  0  153  VAL   C O   1 
ATOM   12151 C CB  . VAL   C 2 153  ? 142.454 95.781  140.192 1.00 39.71  0  153  VAL   C CB  1 
ATOM   12152 C CG1 . VAL   C 2 153  ? 143.240 96.615  141.178 1.00 44.16  0  153  VAL   C CG1 1 
ATOM   12153 C CG2 . VAL   C 2 153  ? 142.675 94.313  140.471 1.00 49.32  0  153  VAL   C CG2 1 
ATOM   12154 N N   . VAL   C 2 154  ? 140.835 98.396  139.397 1.00 40.74  0  154  VAL   C N   1 
ATOM   12155 C CA  . VAL   C 2 154  ? 140.643 99.843  139.500 1.00 34.44  0  154  VAL   C CA  1 
ATOM   12156 C C   . VAL   C 2 154  ? 139.212 100.163 139.917 1.00 38.65  0  154  VAL   C C   1 
ATOM   12157 O O   . VAL   C 2 154  ? 138.975 100.980 140.813 1.00 47.20  0  154  VAL   C O   1 
ATOM   12158 C CB  . VAL   C 2 154  ? 141.007 100.536 138.177 1.00 35.78  0  154  VAL   C CB  1 
ATOM   12159 C CG1 . VAL   C 2 154  ? 140.490 101.956 138.171 1.00 29.46  0  154  VAL   C CG1 1 
ATOM   12160 C CG2 . VAL   C 2 154  ? 142.505 100.531 137.980 1.00 40.58  0  154  VAL   C CG2 1 
ATOM   12161 N N   . ALA   C 2 155  ? 138.236 99.512  139.281 1.00 42.11  0  155  ALA   C N   1 
ATOM   12162 C CA  . ALA   C 2 155  ? 136.835 99.790  139.567 1.00 36.74  0  155  ALA   C CA  1 
ATOM   12163 C C   . ALA   C 2 155  ? 136.367 99.201  140.889 1.00 34.01  0  155  ALA   C C   1 
ATOM   12164 O O   . ALA   C 2 155  ? 135.307 99.600  141.380 1.00 36.31  0  155  ALA   C O   1 
ATOM   12165 C CB  . ALA   C 2 155  ? 135.954 99.267  138.433 1.00 31.79  0  155  ALA   C CB  1 
ATOM   12166 N N   . SER   C 2 156  ? 137.114 98.270  141.472 1.00 37.12  0  156  SER   C N   1 
ATOM   12167 C CA  . SER   C 2 156  ? 136.750 97.667  142.744 1.00 42.02  0  156  SER   C CA  1 
ATOM   12168 C C   . SER   C 2 156  ? 137.366 98.379  143.939 1.00 44.45  0  156  SER   C C   1 
ATOM   12169 O O   . SER   C 2 156  ? 137.103 97.987  145.079 1.00 51.03  0  156  SER   C O   1 
ATOM   12170 C CB  . SER   C 2 156  ? 137.158 96.194  142.761 1.00 38.96  0  156  SER   C CB  1 
ATOM   12171 O OG  . SER   C 2 156  ? 138.566 96.066  142.701 1.00 43.11  0  156  SER   C OG  1 
ATOM   12172 N N   . ALA   C 2 157  ? 138.183 99.404  143.709 1.00 36.41  0  157  ALA   C N   1 
ATOM   12173 C CA  . ALA   C 2 157  ? 138.800 100.164 144.795 1.00 37.77  0  157  ALA   C CA  1 
ATOM   12174 C C   . ALA   C 2 157  ? 137.990 101.433 145.053 1.00 47.15  0  157  ALA   C C   1 
ATOM   12175 O O   . ALA   C 2 157  ? 138.462 102.557 144.898 1.00 49.43  0  157  ALA   C O   1 
ATOM   12176 C CB  . ALA   C 2 157  ? 140.252 100.482 144.458 1.00 35.97  0  157  ALA   C CB  1 
ATOM   12177 N N   . GLY   C 2 158  ? 136.746 101.225 145.479 1.00 48.08  0  158  GLY   C N   1 
ATOM   12178 C CA  . GLY   C 2 158  ? 135.775 102.291 145.553 1.00 48.46  0  158  GLY   C CA  1 
ATOM   12179 C C   . GLY   C 2 158  ? 135.754 103.059 146.858 1.00 47.18  0  158  GLY   C C   1 
ATOM   12180 O O   . GLY   C 2 158  ? 136.652 102.943 147.698 1.00 43.18  0  158  GLY   C O   1 
ATOM   12181 N N   . PRO   C 2 159  ? 134.710 103.873 147.041 1.00 47.89  0  159  PRO   C N   1 
ATOM   12182 C CA  . PRO   C 2 159  ? 134.586 104.643 148.287 1.00 46.06  0  159  PRO   C CA  1 
ATOM   12183 C C   . PRO   C 2 159  ? 134.524 103.783 149.531 1.00 46.44  0  159  PRO   C C   1 
ATOM   12184 O O   . PRO   C 2 159  ? 134.893 104.255 150.613 1.00 54.37  0  159  PRO   C O   1 
ATOM   12185 C CB  . PRO   C 2 159  ? 133.285 105.433 148.083 1.00 44.56  0  159  PRO   C CB  1 
ATOM   12186 C CG  . PRO   C 2 159  ? 132.597 104.791 146.928 1.00 40.41  0  159  PRO   C CG  1 
ATOM   12187 C CD  . PRO   C 2 159  ? 133.668 104.228 146.067 1.00 47.31  0  159  PRO   C CD  1 
ATOM   12188 N N   . THR   C 2 160  ? 134.060 102.538 149.422 1.00 48.44  0  160  THR   C N   1 
ATOM   12189 C CA  . THR   C 2 160  ? 134.107 101.642 150.572 1.00 52.37  0  160  THR   C CA  1 
ATOM   12190 C C   . THR   C 2 160  ? 135.546 101.382 150.999 1.00 52.61  0  160  THR   C C   1 
ATOM   12191 O O   . THR   C 2 160  ? 135.849 101.337 152.196 1.00 50.60  0  160  THR   C O   1 
ATOM   12192 C CB  . THR   C 2 160  ? 133.400 100.329 150.248 1.00 54.64  0  160  THR   C CB  1 
ATOM   12193 O OG1 . THR   C 2 160  ? 132.297 100.586 149.370 1.00 53.82  0  160  THR   C OG1 1 
ATOM   12194 C CG2 . THR   C 2 160  ? 132.884 99.685  151.522 1.00 58.01  0  160  THR   C CG2 1 
ATOM   12195 N N   . SER   C 2 161  ? 136.447 101.212 150.030 1.00 60.69  0  161  SER   C N   1 
ATOM   12196 C CA  . SER   C 2 161  ? 137.862 101.044 150.343 1.00 62.73  0  161  SER   C CA  1 
ATOM   12197 C C   . SER   C 2 161  ? 138.439 102.299 150.985 1.00 60.20  0  161  SER   C C   1 
ATOM   12198 O O   . SER   C 2 161  ? 139.199 102.217 151.957 1.00 61.41  0  161  SER   C O   1 
ATOM   12199 C CB  . SER   C 2 161  ? 138.634 100.690 149.075 1.00 57.65  0  161  SER   C CB  1 
ATOM   12200 O OG  . SER   C 2 161  ? 138.531 101.731 148.122 1.00 59.53  0  161  SER   C OG  1 
ATOM   12201 N N   . ALA   C 2 162  ? 138.092 103.474 150.451 1.00 57.49  0  162  ALA   C N   1 
ATOM   12202 C CA  . ALA   C 2 162  ? 138.601 104.721 151.012 1.00 58.51  0  162  ALA   C CA  1 
ATOM   12203 C C   . ALA   C 2 162  ? 138.119 104.921 152.442 1.00 57.39  0  162  ALA   C C   1 
ATOM   12204 O O   . ALA   C 2 162  ? 138.880 105.379 153.303 1.00 55.73  0  162  ALA   C O   1 
ATOM   12205 C CB  . ALA   C 2 162  ? 138.188 105.902 150.137 1.00 54.93  0  162  ALA   C CB  1 
ATOM   12206 N N   . ARG   C 2 163  ? 136.854 104.595 152.714 1.00 55.48  0  163  ARG   C N   1 
ATOM   12207 C CA  . ARG   C 2 163  ? 136.375 104.620 154.091 1.00 54.24  0  163  ARG   C CA  1 
ATOM   12208 C C   . ARG   C 2 163  ? 137.129 103.610 154.941 1.00 63.71  0  163  ARG   C C   1 
ATOM   12209 O O   . ARG   C 2 163  ? 137.455 103.883 156.101 1.00 66.20  0  163  ARG   C O   1 
ATOM   12210 C CB  . ARG   C 2 163  ? 134.872 104.347 154.133 1.00 54.66  0  163  ARG   C CB  1 
ATOM   12211 C CG  . ARG   C 2 163  ? 134.226 104.609 155.488 1.00 57.02  0  163  ARG   C CG  1 
ATOM   12212 C CD  . ARG   C 2 163  ? 134.047 103.327 156.283 1.00 59.86  0  163  ARG   C CD  1 
ATOM   12213 N NE  . ARG   C 2 163  ? 133.381 102.297 155.497 1.00 62.75  0  163  ARG   C NE  1 
ATOM   12214 C CZ  . ARG   C 2 163  ? 132.068 102.115 155.464 1.00 61.57  0  163  ARG   C CZ  1 
ATOM   12215 N NH1 . ARG   C 2 163  ? 131.248 102.867 156.179 1.00 60.40  1  163  ARG   C NH1 1 
ATOM   12216 N NH2 . ARG   C 2 163  ? 131.566 101.153 154.695 1.00 57.57  0  163  ARG   C NH2 1 
ATOM   12217 N N   . ASP   C 2 164  ? 137.405 102.433 154.380 1.00 73.57  0  164  ASP   C N   1 
ATOM   12218 C CA  . ASP   C 2 164  ? 138.206 101.440 155.087 1.00 72.71  0  164  ASP   C CA  1 
ATOM   12219 C C   . ASP   C 2 164  ? 139.639 101.916 155.286 1.00 68.74  0  164  ASP   C C   1 
ATOM   12220 O O   . ASP   C 2 164  ? 140.229 101.701 156.351 1.00 68.20  0  164  ASP   C O   1 
ATOM   12221 C CB  . ASP   C 2 164  ? 138.189 100.121 154.321 1.00 73.37  0  164  ASP   C CB  1 
ATOM   12222 C CG  . ASP   C 2 164  ? 138.235 98.923  155.232 1.00 74.93  0  164  ASP   C CG  1 
ATOM   12223 O OD1 . ASP   C 2 164  ? 138.412 97.800  154.717 1.00 75.84  0  164  ASP   C OD1 1 
ATOM   12224 O OD2 . ASP   C 2 164  ? 138.093 99.104  156.459 1.00 75.16  -1 164  ASP   C OD2 1 
ATOM   12225 N N   . GLY   C 2 165  ? 140.214 102.560 154.275 1.00 68.60  0  165  GLY   C N   1 
ATOM   12226 C CA  . GLY   C 2 165  ? 141.607 102.950 154.323 1.00 76.00  0  165  GLY   C CA  1 
ATOM   12227 C C   . GLY   C 2 165  ? 142.514 101.869 153.773 1.00 78.08  0  165  GLY   C C   1 
ATOM   12228 O O   . GLY   C 2 165  ? 143.639 101.685 154.246 1.00 80.79  0  165  GLY   C O   1 
ATOM   12229 N N   . ILE   C 2 166  ? 142.025 101.141 152.772 1.00 65.80  0  166  ILE   C N   1 
ATOM   12230 C CA  . ILE   C 2 166  ? 142.759 100.027 152.184 1.00 65.10  0  166  ILE   C CA  1 
ATOM   12231 C C   . ILE   C 2 166  ? 142.892 100.218 150.677 1.00 69.33  0  166  ILE   C C   1 
ATOM   12232 O O   . ILE   C 2 166  ? 143.336 99.313  149.962 1.00 73.28  0  166  ILE   C O   1 
ATOM   12233 C CB  . ILE   C 2 166  ? 142.082 98.686  152.529 1.00 66.53  0  166  ILE   C CB  1 
ATOM   12234 C CG1 . ILE   C 2 166  ? 140.970 98.355  151.532 1.00 64.09  0  166  ILE   C CG1 1 
ATOM   12235 C CG2 . ILE   C 2 166  ? 141.541 98.702  153.949 1.00 68.92  0  166  ILE   C CG2 1 
ATOM   12236 C CD1 . ILE   C 2 166  ? 140.163 97.130  151.896 1.00 67.23  0  166  ILE   C CD1 1 
ATOM   12237 N N   . ARG   C 2 167  ? 142.543 101.411 150.188 1.00 55.94  0  167  ARG   C N   1 
ATOM   12238 C CA  . ARG   C 2 167  ? 142.601 101.665 148.751 1.00 57.67  0  167  ARG   C CA  1 
ATOM   12239 C C   . ARG   C 2 167  ? 144.019 101.545 148.212 1.00 60.03  0  167  ARG   C C   1 
ATOM   12240 O O   . ARG   C 2 167  ? 144.218 101.059 147.092 1.00 58.56  0  167  ARG   C O   1 
ATOM   12241 C CB  . ARG   C 2 167  ? 142.035 103.048 148.434 1.00 50.03  0  167  ARG   C CB  1 
ATOM   12242 C CG  . ARG   C 2 167  ? 141.910 103.338 146.950 1.00 50.62  0  167  ARG   C CG  1 
ATOM   12243 C CD  . ARG   C 2 167  ? 141.273 104.690 146.707 1.00 46.24  0  167  ARG   C CD  1 
ATOM   12244 N NE  . ARG   C 2 167  ? 140.909 104.880 145.309 1.00 47.84  0  167  ARG   C NE  1 
ATOM   12245 C CZ  . ARG   C 2 167  ? 141.726 105.350 144.377 1.00 51.41  0  167  ARG   C CZ  1 
ATOM   12246 N NH1 . ARG   C 2 167  ? 142.969 105.697 144.660 1.00 52.84  1  167  ARG   C NH1 1 
ATOM   12247 N NH2 . ARG   C 2 167  ? 141.284 105.474 143.129 1.00 48.32  0  167  ARG   C NH2 1 
ATOM   12248 N N   . ASP   C 2 168  ? 145.015 101.980 148.985 1.00 64.73  0  168  ASP   C N   1 
ATOM   12249 C CA  . ASP   C 2 168  ? 146.399 101.917 148.536 1.00 61.94  0  168  ASP   C CA  1 
ATOM   12250 C C   . ASP   C 2 168  ? 146.915 100.491 148.408 1.00 65.34  0  168  ASP   C C   1 
ATOM   12251 O O   . ASP   C 2 168  ? 147.982 100.291 147.820 1.00 70.42  0  168  ASP   C O   1 
ATOM   12252 C CB  . ASP   C 2 168  ? 147.292 102.710 149.486 1.00 68.07  0  168  ASP   C CB  1 
ATOM   12253 C CG  . ASP   C 2 168  ? 146.902 104.170 149.560 1.00 72.95  0  168  ASP   C CG  1 
ATOM   12254 O OD1 . ASP   C 2 168  ? 146.302 104.674 148.587 1.00 69.09  0  168  ASP   C OD1 1 
ATOM   12255 O OD2 . ASP   C 2 168  ? 147.190 104.813 150.591 1.00 72.21  -1 168  ASP   C OD2 1 
ATOM   12256 N N   . ALA   C 2 169  ? 146.202 99.504  148.950 1.00 70.85  0  169  ALA   C N   1 
ATOM   12257 C CA  . ALA   C 2 169  ? 146.568 98.116  148.696 1.00 71.66  0  169  ALA   C CA  1 
ATOM   12258 C C   . ALA   C 2 169  ? 146.264 97.728  147.256 1.00 74.97  0  169  ALA   C C   1 
ATOM   12259 O O   . ALA   C 2 169  ? 147.092 97.097  146.590 1.00 78.17  0  169  ALA   C O   1 
ATOM   12260 C CB  . ALA   C 2 169  ? 145.841 97.190  149.669 1.00 71.13  0  169  ALA   C CB  1 
ATOM   12261 N N   . MET   C 2 170  ? 145.081 98.096  146.757 1.00 65.21  0  170  MET   C N   1 
ATOM   12262 C CA  . MET   C 2 170  ? 144.749 97.804  145.367 1.00 67.33  0  170  MET   C CA  1 
ATOM   12263 C C   . MET   C 2 170  ? 145.451 98.751  144.407 1.00 65.72  0  170  MET   C C   1 
ATOM   12264 O O   . MET   C 2 170  ? 145.756 98.367  143.274 1.00 63.97  0  170  MET   C O   1 
ATOM   12265 C CB  . MET   C 2 170  ? 143.237 97.870  145.150 1.00 63.12  0  170  MET   C CB  1 
ATOM   12266 C CG  . MET   C 2 170  ? 142.440 96.879  145.974 1.00 64.73  0  170  MET   C CG  1 
ATOM   12267 S SD  . MET   C 2 170  ? 140.777 97.454  146.343 1.00 66.04  0  170  MET   C SD  1 
ATOM   12268 C CE  . MET   C 2 170  ? 140.976 97.975  148.038 1.00 64.57  0  170  MET   C CE  1 
ATOM   12269 N N   . ILE   C 2 171  ? 145.716 99.981  144.835 1.00 62.43  0  171  ILE   C N   1 
ATOM   12270 C CA  . ILE   C 2 171  ? 146.270 101.006 143.968 1.00 63.83  0  171  ILE   C CA  1 
ATOM   12271 C C   . ILE   C 2 171  ? 147.793 101.027 144.012 1.00 64.64  0  171  ILE   C C   1 
ATOM   12272 O O   . ILE   C 2 171  ? 148.445 101.076 142.967 1.00 61.09  0  171  ILE   C O   1 
ATOM   12273 C CB  . ILE   C 2 171  ? 145.682 102.386 144.329 1.00 64.12  0  171  ILE   C CB  1 
ATOM   12274 C CG1 . ILE   C 2 171  ? 144.282 102.526 143.730 1.00 62.35  0  171  ILE   C CG1 1 
ATOM   12275 C CG2 . ILE   C 2 171  ? 146.586 103.503 143.851 1.00 64.30  0  171  ILE   C CG2 1 
ATOM   12276 C CD1 . ILE   C 2 171  ? 144.185 102.073 142.292 1.00 57.63  0  171  ILE   C CD1 1 
ATOM   12277 N N   . GLY   C 2 172  ? 148.379 100.983 145.204 1.00 70.82  0  172  GLY   C N   1 
ATOM   12278 C CA  . GLY   C 2 172  ? 149.822 100.945 145.328 1.00 66.67  0  172  GLY   C CA  1 
ATOM   12279 C C   . GLY   C 2 172  ? 150.440 102.302 145.578 1.00 66.19  0  172  GLY   C C   1 
ATOM   12280 O O   . GLY   C 2 172  ? 149.948 103.317 145.077 1.00 63.63  0  172  GLY   C O   1 
ATOM   12281 N N   . LEU   C 2 173  ? 151.525 102.330 146.348 1.00 68.40  0  173  LEU   C N   1 
ATOM   12282 C CA  . LEU   C 2 173  ? 152.198 103.586 146.645 1.00 65.18  0  173  LEU   C CA  1 
ATOM   12283 C C   . LEU   C 2 173  ? 152.798 104.170 145.373 1.00 68.95  0  173  LEU   C C   1 
ATOM   12284 O O   . LEU   C 2 173  ? 153.363 103.450 144.546 1.00 71.56  0  173  LEU   C O   1 
ATOM   12285 C CB  . LEU   C 2 173  ? 153.291 103.370 147.692 1.00 67.53  0  173  LEU   C CB  1 
ATOM   12286 C CG  . LEU   C 2 173  ? 152.891 103.298 149.169 1.00 68.14  0  173  LEU   C CG  1 
ATOM   12287 C CD1 . LEU   C 2 173  ? 152.125 104.539 149.579 1.00 68.29  0  173  LEU   C CD1 1 
ATOM   12288 C CD2 . LEU   C 2 173  ? 152.099 102.038 149.490 1.00 69.35  0  173  LEU   C CD2 1 
ATOM   12289 N N   . ARG   C 2 174  ? 152.675 105.482 145.218 1.00 55.97  0  174  ARG   C N   1 
ATOM   12290 C CA  . ARG   C 2 174  ? 153.147 106.178 144.029 1.00 54.62  0  174  ARG   C CA  1 
ATOM   12291 C C   . ARG   C 2 174  ? 154.234 107.177 144.415 1.00 56.31  0  174  ARG   C C   1 
ATOM   12292 O O   . ARG   C 2 174  ? 154.680 107.230 145.562 1.00 60.62  0  174  ARG   C O   1 
ATOM   12293 C CB  . ARG   C 2 174  ? 151.979 106.845 143.303 1.00 45.78  0  174  ARG   C CB  1 
ATOM   12294 C CG  . ARG   C 2 174  ? 151.042 105.823 142.694 1.00 53.05  0  174  ARG   C CG  1 
ATOM   12295 C CD  . ARG   C 2 174  ? 149.768 106.426 142.153 1.00 52.75  0  174  ARG   C CD  1 
ATOM   12296 N NE  . ARG   C 2 174  ? 148.886 105.388 141.633 1.00 49.89  0  174  ARG   C NE  1 
ATOM   12297 C CZ  . ARG   C 2 174  ? 147.628 105.585 141.266 1.00 51.79  0  174  ARG   C CZ  1 
ATOM   12298 N NH1 . ARG   C 2 174  ? 147.064 106.776 141.349 1.00 50.02  1  174  ARG   C NH1 1 
ATOM   12299 N NH2 . ARG   C 2 174  ? 146.919 104.560 140.806 1.00 56.58  0  174  ARG   C NH2 1 
ATOM   12300 N N   . GLU   C 2 175  ? 154.660 107.973 143.433 1.00 63.53  0  175  GLU   C N   1 
ATOM   12301 C CA  . GLU   C 2 175  ? 155.862 108.785 143.600 1.00 67.43  0  175  GLU   C CA  1 
ATOM   12302 C C   . GLU   C 2 175  ? 155.727 109.776 144.749 1.00 69.24  0  175  GLU   C C   1 
ATOM   12303 O O   . GLU   C 2 175  ? 156.674 109.971 145.517 1.00 68.68  0  175  GLU   C O   1 
ATOM   12304 C CB  . GLU   C 2 175  ? 156.184 109.522 142.303 1.00 66.55  0  175  GLU   C CB  1 
ATOM   12305 C CG  . GLU   C 2 175  ? 157.106 108.761 141.370 1.00 61.71  0  175  GLU   C CG  1 
ATOM   12306 C CD  . GLU   C 2 175  ? 156.365 107.786 140.484 1.00 67.03  0  175  GLU   C CD  1 
ATOM   12307 O OE1 . GLU   C 2 175  ? 155.119 107.762 140.536 1.00 71.20  0  175  GLU   C OE1 1 
ATOM   12308 O OE2 . GLU   C 2 175  ? 157.032 107.050 139.729 1.00 67.80  -1 175  GLU   C OE2 1 
ATOM   12309 N N   . GLU   C 2 176  ? 154.566 110.418 144.881 1.00 66.51  0  176  GLU   C N   1 
ATOM   12310 C CA  . GLU   C 2 176  ? 154.415 111.461 145.891 1.00 62.22  0  176  GLU   C CA  1 
ATOM   12311 C C   . GLU   C 2 176  ? 154.504 110.888 147.300 1.00 63.86  0  176  GLU   C C   1 
ATOM   12312 O O   . GLU   C 2 176  ? 155.258 111.391 148.140 1.00 70.96  0  176  GLU   C O   1 
ATOM   12313 C CB  . GLU   C 2 176  ? 153.091 112.192 145.692 1.00 59.73  0  176  GLU   C CB  1 
ATOM   12314 C CG  . GLU   C 2 176  ? 153.000 112.935 144.380 1.00 60.17  0  176  GLU   C CG  1 
ATOM   12315 C CD  . GLU   C 2 176  ? 154.042 114.019 144.255 1.00 61.65  0  176  GLU   C CD  1 
ATOM   12316 O OE1 . GLU   C 2 176  ? 154.444 114.582 145.294 1.00 63.67  0  176  GLU   C OE1 1 
ATOM   12317 O OE2 . GLU   C 2 176  ? 154.458 114.312 143.116 1.00 67.46  -1 176  GLU   C OE2 1 
ATOM   12318 N N   . MET   C 2 177  ? 153.737 109.833 147.578 1.00 71.71  0  177  MET   C N   1 
ATOM   12319 C CA  . MET   C 2 177  ? 153.753 109.248 148.915 1.00 76.51  0  177  MET   C CA  1 
ATOM   12320 C C   . MET   C 2 177  ? 155.115 108.648 149.238 1.00 78.90  0  177  MET   C C   1 
ATOM   12321 O O   . MET   C 2 177  ? 155.603 108.768 150.368 1.00 78.42  0  177  MET   C O   1 
ATOM   12322 C CB  . MET   C 2 177  ? 152.655 108.194 149.038 1.00 71.60  0  177  MET   C CB  1 
ATOM   12323 C CG  . MET   C 2 177  ? 152.125 108.018 150.448 1.00 72.92  0  177  MET   C CG  1 
ATOM   12324 S SD  . MET   C 2 177  ? 151.539 109.562 151.165 1.00 79.39  0  177  MET   C SD  1 
ATOM   12325 C CE  . MET   C 2 177  ? 152.408 109.556 152.732 1.00 74.36  0  177  MET   C CE  1 
ATOM   12326 N N   . ILE   C 2 178  ? 155.743 108.000 148.255 1.00 83.20  0  178  ILE   C N   1 
ATOM   12327 C CA  . ILE   C 2 178  ? 157.053 107.397 148.474 1.00 81.46  0  178  ILE   C CA  1 
ATOM   12328 C C   . ILE   C 2 178  ? 158.099 108.469 148.751 1.00 83.90  0  178  ILE   C C   1 
ATOM   12329 O O   . ILE   C 2 178  ? 158.945 108.312 149.637 1.00 85.89  0  178  ILE   C O   1 
ATOM   12330 C CB  . ILE   C 2 178  ? 157.431 106.515 147.271 1.00 80.40  0  178  ILE   C CB  1 
ATOM   12331 C CG1 . ILE   C 2 178  ? 156.665 105.195 147.343 1.00 80.16  0  178  ILE   C CG1 1 
ATOM   12332 C CG2 . ILE   C 2 178  ? 158.925 106.266 147.232 1.00 83.02  0  178  ILE   C CG2 1 
ATOM   12333 C CD1 . ILE   C 2 178  ? 156.646 104.431 146.055 1.00 80.69  0  178  ILE   C CD1 1 
ATOM   12334 N N   . GLU   C 2 179  ? 158.056 109.577 148.006 1.00 89.83  0  179  GLU   C N   1 
ATOM   12335 C CA  . GLU   C 2 179  ? 158.970 110.685 148.267 1.00 91.11  0  179  GLU   C CA  1 
ATOM   12336 C C   . GLU   C 2 179  ? 158.738 111.280 149.648 1.00 92.18  0  179  GLU   C C   1 
ATOM   12337 O O   . GLU   C 2 179  ? 159.695 111.601 150.362 1.00 93.74  0  179  GLU   C O   1 
ATOM   12338 C CB  . GLU   C 2 179  ? 158.808 111.763 147.196 1.00 90.87  0  179  GLU   C CB  1 
ATOM   12339 C CG  . GLU   C 2 179  ? 159.655 111.548 145.962 1.00 91.97  0  179  GLU   C CG  1 
ATOM   12340 C CD  . GLU   C 2 179  ? 159.745 112.790 145.102 1.00 95.79  0  179  GLU   C CD  1 
ATOM   12341 O OE1 . GLU   C 2 179  ? 158.860 113.664 145.225 1.00 92.18  0  179  GLU   C OE1 1 
ATOM   12342 O OE2 . GLU   C 2 179  ? 160.700 112.891 144.304 1.00 96.13  -1 179  GLU   C OE2 1 
ATOM   12343 N N   . LYS   C 2 180  ? 157.473 111.444 150.040 1.00 87.94  0  180  LYS   C N   1 
ATOM   12344 C CA  . LYS   C 2 180  ? 157.176 111.992 151.359 1.00 86.19  0  180  LYS   C CA  1 
ATOM   12345 C C   . LYS   C 2 180  ? 157.701 111.083 152.461 1.00 88.33  0  180  LYS   C C   1 
ATOM   12346 O O   . LYS   C 2 180  ? 158.244 111.559 153.464 1.00 89.12  0  180  LYS   C O   1 
ATOM   12347 C CB  . LYS   C 2 180  ? 155.670 112.207 151.509 1.00 87.64  0  180  LYS   C CB  1 
ATOM   12348 C CG  . LYS   C 2 180  ? 155.275 113.045 152.715 1.00 88.96  0  180  LYS   C CG  1 
ATOM   12349 C CD  . LYS   C 2 180  ? 154.698 112.178 153.825 1.00 90.90  0  180  LYS   C CD  1 
ATOM   12350 C CE  . LYS   C 2 180  ? 154.079 113.023 154.926 1.00 88.33  0  180  LYS   C CE  1 
ATOM   12351 N NZ  . LYS   C 2 180  ? 153.466 112.183 155.991 1.00 86.49  1  180  LYS   C NZ  1 
ATOM   12352 N N   . ILE   C 2 181  ? 157.551 109.769 152.291 1.00 102.64 0  181  ILE   C N   1 
ATOM   12353 C CA  . ILE   C 2 181  ? 158.036 108.832 153.300 1.00 105.48 0  181  ILE   C CA  1 
ATOM   12354 C C   . ILE   C 2 181  ? 159.561 108.832 153.340 1.00 104.22 0  181  ILE   C C   1 
ATOM   12355 O O   . ILE   C 2 181  ? 160.171 108.811 154.415 1.00 103.75 0  181  ILE   C O   1 
ATOM   12356 C CB  . ILE   C 2 181  ? 157.466 107.427 153.040 1.00 103.39 0  181  ILE   C CB  1 
ATOM   12357 C CG1 . ILE   C 2 181  ? 156.109 107.290 153.730 1.00 103.02 0  181  ILE   C CG1 1 
ATOM   12358 C CG2 . ILE   C 2 181  ? 158.425 106.347 153.514 1.00 102.08 0  181  ILE   C CG2 1 
ATOM   12359 C CD1 . ILE   C 2 181  ? 156.198 107.323 155.233 1.00 102.77 0  181  ILE   C CD1 1 
ATOM   12360 N N   . ARG   C 2 182  ? 160.199 108.871 152.168 1.00 101.87 0  182  ARG   C N   1 
ATOM   12361 C CA  . ARG   C 2 182  ? 161.656 108.902 152.114 1.00 100.68 0  182  ARG   C CA  1 
ATOM   12362 C C   . ARG   C 2 182  ? 162.202 110.156 152.783 1.00 102.60 0  182  ARG   C C   1 
ATOM   12363 O O   . ARG   C 2 182  ? 163.220 110.103 153.482 1.00 104.74 0  182  ARG   C O   1 
ATOM   12364 C CB  . ARG   C 2 182  ? 162.119 108.811 150.660 1.00 99.86  0  182  ARG   C CB  1 
ATOM   12365 C CG  . ARG   C 2 182  ? 163.610 108.962 150.449 1.00 100.06 0  182  ARG   C CG  1 
ATOM   12366 C CD  . ARG   C 2 182  ? 163.975 108.663 149.004 1.00 101.39 0  182  ARG   C CD  1 
ATOM   12367 N NE  . ARG   C 2 182  ? 165.259 109.243 148.627 1.00 102.44 0  182  ARG   C NE  1 
ATOM   12368 C CZ  . ARG   C 2 182  ? 165.408 110.443 148.084 1.00 102.39 0  182  ARG   C CZ  1 
ATOM   12369 N NH1 . ARG   C 2 182  ? 164.369 111.225 147.839 1.00 102.95 1  182  ARG   C NH1 1 
ATOM   12370 N NH2 . ARG   C 2 182  ? 166.629 110.870 147.777 1.00 102.21 0  182  ARG   C NH2 1 
ATOM   12371 N N   . THR   C 2 183  ? 161.539 111.296 152.581 1.00 108.84 0  183  THR   C N   1 
ATOM   12372 C CA  . THR   C 2 183  ? 161.899 112.501 153.321 1.00 110.02 0  183  THR   C CA  1 
ATOM   12373 C C   . THR   C 2 183  ? 161.685 112.307 154.818 1.00 109.65 0  183  THR   C C   1 
ATOM   12374 O O   . THR   C 2 183  ? 162.528 112.710 155.629 1.00 108.12 0  183  THR   C O   1 
ATOM   12375 C CB  . THR   C 2 183  ? 161.092 113.694 152.805 1.00 109.83 0  183  THR   C CB  1 
ATOM   12376 O OG1 . THR   C 2 183  ? 161.594 114.092 151.523 1.00 108.90 0  183  THR   C OG1 1 
ATOM   12377 C CG2 . THR   C 2 183  ? 161.181 114.871 153.768 1.00 106.76 0  183  THR   C CG2 1 
ATOM   12378 N N   . GLU   C 2 184  ? 160.570 111.682 155.203 1.00 113.16 0  184  GLU   C N   1 
ATOM   12379 C CA  . GLU   C 2 184  ? 160.341 111.360 156.606 1.00 111.75 0  184  GLU   C CA  1 
ATOM   12380 C C   . GLU   C 2 184  ? 161.327 110.322 157.124 1.00 113.59 0  184  GLU   C C   1 
ATOM   12381 O O   . GLU   C 2 184  ? 161.557 110.254 158.336 1.00 113.33 0  184  GLU   C O   1 
ATOM   12382 C CB  . GLU   C 2 184  ? 158.907 110.866 156.808 1.00 111.72 0  184  GLU   C CB  1 
ATOM   12383 C CG  . GLU   C 2 184  ? 158.451 110.837 158.260 1.00 113.07 0  184  GLU   C CG  1 
ATOM   12384 C CD  . GLU   C 2 184  ? 156.945 110.720 158.400 1.00 114.70 0  184  GLU   C CD  1 
ATOM   12385 O OE1 . GLU   C 2 184  ? 156.265 110.513 157.373 1.00 116.13 0  184  GLU   C OE1 1 
ATOM   12386 O OE2 . GLU   C 2 184  ? 156.439 110.837 159.535 1.00 111.84 -1 184  GLU   C OE2 1 
ATOM   12387 N N   . ALA   C 2 185  ? 161.912 109.520 156.240 1.00 119.85 0  185  ALA   C N   1 
ATOM   12388 C CA  . ALA   C 2 185  ? 162.910 108.524 156.630 1.00 119.87 0  185  ALA   C CA  1 
ATOM   12389 C C   . ALA   C 2 185  ? 164.323 109.092 156.559 1.00 119.63 0  185  ALA   C C   1 
ATOM   12390 O O   . ALA   C 2 185  ? 165.214 108.521 155.933 1.00 118.16 0  185  ALA   C O   1 
ATOM   12391 C CB  . ALA   C 2 185  ? 162.775 107.284 155.755 1.00 117.94 0  185  ALA   C CB  1 
ATOM   12392 N N   . LEU   C 2 186  ? 164.534 110.232 157.208 1.00 115.85 0  186  LEU   C N   1 
ATOM   12393 C CA  . LEU   C 2 186  ? 165.842 110.875 157.235 1.00 115.21 0  186  LEU   C CA  1 
ATOM   12394 C C   . LEU   C 2 186  ? 166.020 111.664 158.528 1.00 115.60 0  186  LEU   C C   1 
ATOM   12395 O O   . LEU   C 2 186  ? 165.111 111.737 159.354 1.00 114.16 0  186  LEU   C O   1 
ATOM   12396 C CB  . LEU   C 2 186  ? 166.024 111.799 156.026 1.00 115.57 0  186  LEU   C CB  1 
ATOM   12397 C CG  . LEU   C 2 186  ? 166.378 111.168 154.676 1.00 116.19 0  186  LEU   C CG  1 
ATOM   12398 C CD1 . LEU   C 2 186  ? 166.323 112.209 153.567 1.00 115.02 0  186  LEU   C CD1 1 
ATOM   12399 C CD2 . LEU   C 2 186  ? 167.742 110.497 154.723 1.00 113.31 0  186  LEU   C CD2 1 
ATOM   12400 N N   . ASN   D 2 130  ? 162.983 83.521  120.980 1.00 102.91 0  130  ASN   D N   1 
ATOM   12401 C CA  . ASN   D 2 130  ? 162.794 82.077  120.919 1.00 104.12 0  130  ASN   D CA  1 
ATOM   12402 C C   . ASN   D 2 130  ? 161.627 81.631  121.793 1.00 104.09 0  130  ASN   D C   1 
ATOM   12403 O O   . ASN   D 2 130  ? 160.833 82.450  122.253 1.00 102.47 0  130  ASN   D O   1 
ATOM   12404 C CB  . ASN   D 2 130  ? 164.072 81.353  121.345 1.00 103.74 0  130  ASN   D CB  1 
ATOM   12405 C CG  . ASN   D 2 130  ? 164.652 81.900  122.635 1.00 103.62 0  130  ASN   D CG  1 
ATOM   12406 O OD1 . ASN   D 2 130  ? 164.006 82.672  123.342 1.00 103.16 0  130  ASN   D OD1 1 
ATOM   12407 N ND2 . ASN   D 2 130  ? 165.877 81.496  122.949 1.00 103.24 0  130  ASN   D ND2 1 
ATOM   12408 N N   . ILE   D 2 131  ? 161.532 80.319  122.015 1.00 102.94 0  131  ILE   D N   1 
ATOM   12409 C CA  . ILE   D 2 131  ? 160.460 79.780  122.845 1.00 102.72 0  131  ILE   D CA  1 
ATOM   12410 C C   . ILE   D 2 131  ? 160.652 80.186  124.300 1.00 103.54 0  131  ILE   D C   1 
ATOM   12411 O O   . ILE   D 2 131  ? 159.684 80.499  125.005 1.00 102.03 0  131  ILE   D O   1 
ATOM   12412 C CB  . ILE   D 2 131  ? 160.385 78.251  122.684 1.00 103.08 0  131  ILE   D CB  1 
ATOM   12413 C CG1 . ILE   D 2 131  ? 159.990 77.886  121.253 1.00 102.90 0  131  ILE   D CG1 1 
ATOM   12414 C CG2 . ILE   D 2 131  ? 159.400 77.649  123.673 1.00 101.46 0  131  ILE   D CG2 1 
ATOM   12415 C CD1 . ILE   D 2 131  ? 160.224 76.432  120.909 1.00 103.00 0  131  ILE   D CD1 1 
ATOM   12416 N N   . THR   D 2 132  ? 161.900 80.194  124.774 1.00 105.25 0  132  THR   D N   1 
ATOM   12417 C CA  . THR   D 2 132  ? 162.162 80.505  126.176 1.00 105.43 0  132  THR   D CA  1 
ATOM   12418 C C   . THR   D 2 132  ? 161.773 81.937  126.526 1.00 105.16 0  132  THR   D C   1 
ATOM   12419 O O   . THR   D 2 132  ? 161.274 82.187  127.629 1.00 106.04 0  132  THR   D O   1 
ATOM   12420 C CB  . THR   D 2 132  ? 163.635 80.260  126.504 1.00 103.97 0  132  THR   D CB  1 
ATOM   12421 O OG1 . THR   D 2 132  ? 164.014 78.956  126.050 1.00 104.81 0  132  THR   D OG1 1 
ATOM   12422 C CG2 . THR   D 2 132  ? 163.867 80.347  128.003 1.00 102.29 0  132  THR   D CG2 1 
ATOM   12423 N N   . ALA   D 2 133  ? 161.990 82.886  125.613 1.00 103.21 0  133  ALA   D N   1 
ATOM   12424 C CA  . ALA   D 2 133  ? 161.600 84.268  125.880 1.00 103.94 0  133  ALA   D CA  1 
ATOM   12425 C C   . ALA   D 2 133  ? 160.091 84.386  126.059 1.00 103.62 0  133  ALA   D C   1 
ATOM   12426 O O   . ALA   D 2 133  ? 159.611 85.042  126.993 1.00 102.43 0  133  ALA   D O   1 
ATOM   12427 C CB  . ALA   D 2 133  ? 162.082 85.177  124.750 1.00 102.67 0  133  ALA   D CB  1 
ATOM   12428 N N   . ARG   D 2 134  ? 159.324 83.750  125.172 1.00 96.24  0  134  ARG   D N   1 
ATOM   12429 C CA  . ARG   D 2 134  ? 157.872 83.783  125.297 1.00 94.21  0  134  ARG   D CA  1 
ATOM   12430 C C   . ARG   D 2 134  ? 157.403 83.063  126.553 1.00 94.80  0  134  ARG   D C   1 
ATOM   12431 O O   . ARG   D 2 134  ? 156.439 83.498  127.192 1.00 96.89  0  134  ARG   D O   1 
ATOM   12432 C CB  . ARG   D 2 134  ? 157.225 83.177  124.054 1.00 95.88  0  134  ARG   D CB  1 
ATOM   12433 C CG  . ARG   D 2 134  ? 157.172 84.131  122.875 1.00 94.84  0  134  ARG   D CG  1 
ATOM   12434 C CD  . ARG   D 2 134  ? 156.989 83.388  121.564 1.00 97.49  0  134  ARG   D CD  1 
ATOM   12435 N NE  . ARG   D 2 134  ? 156.511 84.262  120.500 1.00 97.26  0  134  ARG   D NE  1 
ATOM   12436 C CZ  . ARG   D 2 134  ? 157.262 85.149  119.863 1.00 96.01  0  134  ARG   D CZ  1 
ATOM   12437 N NH1 . ARG   D 2 134  ? 158.540 85.315  120.162 1.00 95.17  1  134  ARG   D NH1 1 
ATOM   12438 N NH2 . ARG   D 2 134  ? 156.717 85.888  118.902 1.00 96.11  0  134  ARG   D NH2 1 
ATOM   12439 N N   . LEU   D 2 135  ? 158.066 81.967  126.923 1.00 98.52  0  135  LEU   D N   1 
ATOM   12440 C CA  . LEU   D 2 135  ? 157.706 81.278  128.158 1.00 99.76  0  135  LEU   D CA  1 
ATOM   12441 C C   . LEU   D 2 135  ? 157.965 82.158  129.375 1.00 101.07 0  135  LEU   D C   1 
ATOM   12442 O O   . LEU   D 2 135  ? 157.161 82.180  130.313 1.00 102.70 0  135  LEU   D O   1 
ATOM   12443 C CB  . LEU   D 2 135  ? 158.470 79.960  128.264 1.00 98.90  0  135  LEU   D CB  1 
ATOM   12444 C CG  . LEU   D 2 135  ? 158.048 78.887  127.259 1.00 98.81  0  135  LEU   D CG  1 
ATOM   12445 C CD1 . LEU   D 2 135  ? 158.922 77.655  127.397 1.00 99.90  0  135  LEU   D CD1 1 
ATOM   12446 C CD2 . LEU   D 2 135  ? 156.583 78.533  127.439 1.00 99.31  0  135  LEU   D CD2 1 
ATOM   12447 N N   . ASP   D 2 136  ? 159.078 82.895  129.376 1.00 99.70  0  136  ASP   D N   1 
ATOM   12448 C CA  . ASP   D 2 136  ? 159.353 83.819  130.473 1.00 99.98  0  136  ASP   D CA  1 
ATOM   12449 C C   . ASP   D 2 136  ? 158.327 84.946  130.522 1.00 98.86  0  136  ASP   D C   1 
ATOM   12450 O O   . ASP   D 2 136  ? 157.887 85.350  131.607 1.00 97.54  0  136  ASP   D O   1 
ATOM   12451 C CB  . ASP   D 2 136  ? 160.766 84.384  130.340 1.00 99.01  0  136  ASP   D CB  1 
ATOM   12452 C CG  . ASP   D 2 136  ? 161.832 83.370  130.701 1.00 101.29 0  136  ASP   D CG  1 
ATOM   12453 O OD1 . ASP   D 2 136  ? 161.505 82.388  131.399 1.00 99.74  0  136  ASP   D OD1 1 
ATOM   12454 O OD2 . ASP   D 2 136  ? 162.995 83.553  130.285 1.00 103.64 -1 136  ASP   D OD2 1 
ATOM   12455 N N   . ARG   D 2 137  ? 157.941 85.472  129.357 1.00 95.64  0  137  ARG   D N   1 
ATOM   12456 C CA  . ARG   D 2 137  ? 156.918 86.513  129.325 1.00 94.71  0  137  ARG   D CA  1 
ATOM   12457 C C   . ARG   D 2 137  ? 155.591 85.996  129.868 1.00 94.47  0  137  ARG   D C   1 
ATOM   12458 O O   . ARG   D 2 137  ? 154.907 86.692  130.629 1.00 96.21  0  137  ARG   D O   1 
ATOM   12459 C CB  . ARG   D 2 137  ? 156.747 87.042  127.902 1.00 93.90  0  137  ARG   D CB  1 
ATOM   12460 C CG  . ARG   D 2 137  ? 157.928 87.851  127.400 1.00 95.96  0  137  ARG   D CG  1 
ATOM   12461 C CD  . ARG   D 2 137  ? 157.973 89.220  128.056 1.00 96.32  0  137  ARG   D CD  1 
ATOM   12462 N NE  . ARG   D 2 137  ? 158.876 89.250  129.200 1.00 97.09  0  137  ARG   D NE  1 
ATOM   12463 C CZ  . ARG   D 2 137  ? 160.185 89.443  129.118 1.00 94.78  0  137  ARG   D CZ  1 
ATOM   12464 N NH1 . ARG   D 2 137  ? 160.784 89.630  127.953 1.00 92.24  1  137  ARG   D NH1 1 
ATOM   12465 N NH2 . ARG   D 2 137  ? 160.911 89.450  130.231 1.00 94.13  0  137  ARG   D NH2 1 
ATOM   12466 N N   . ILE   D 2 138  ? 155.213 84.774  129.490 1.00 85.71  0  138  ILE   D N   1 
ATOM   12467 C CA  . ILE   D 2 138  ? 153.982 84.187  130.004 1.00 82.66  0  138  ILE   D CA  1 
ATOM   12468 C C   . ILE   D 2 138  ? 154.086 83.949  131.504 1.00 82.63  0  138  ILE   D C   1 
ATOM   12469 O O   . ILE   D 2 138  ? 153.105 84.124  132.233 1.00 84.20  0  138  ILE   D O   1 
ATOM   12470 C CB  . ILE   D 2 138  ? 153.651 82.895  129.237 1.00 84.91  0  138  ILE   D CB  1 
ATOM   12471 C CG1 . ILE   D 2 138  ? 153.192 83.235  127.819 1.00 85.46  0  138  ILE   D CG1 1 
ATOM   12472 C CG2 . ILE   D 2 138  ? 152.584 82.095  129.960 1.00 87.51  0  138  ILE   D CG2 1 
ATOM   12473 C CD1 . ILE   D 2 138  ? 153.088 82.040  126.907 1.00 86.29  0  138  ILE   D CD1 1 
ATOM   12474 N N   . ASP   D 2 139  ? 155.264 83.561  131.993 1.00 84.51  0  139  ASP   D N   1 
ATOM   12475 C CA  . ASP   D 2 139  ? 155.453 83.404  133.432 1.00 87.48  0  139  ASP   D CA  1 
ATOM   12476 C C   . ASP   D 2 139  ? 155.248 84.725  134.164 1.00 90.97  0  139  ASP   D C   1 
ATOM   12477 O O   . ASP   D 2 139  ? 154.583 84.772  135.207 1.00 92.43  0  139  ASP   D O   1 
ATOM   12478 C CB  . ASP   D 2 139  ? 156.847 82.845  133.712 1.00 89.02  0  139  ASP   D CB  1 
ATOM   12479 C CG  . ASP   D 2 139  ? 157.034 82.440  135.158 1.00 90.63  0  139  ASP   D CG  1 
ATOM   12480 O OD1 . ASP   D 2 139  ? 156.406 81.449  135.582 1.00 91.71  0  139  ASP   D OD1 1 
ATOM   12481 O OD2 . ASP   D 2 139  ? 157.810 83.112  135.869 1.00 89.62  -1 139  ASP   D OD2 1 
ATOM   12482 N N   . GLU   D 2 140  ? 155.810 85.812  133.628 1.00 88.32  0  140  GLU   D N   1 
ATOM   12483 C CA  . GLU   D 2 140  ? 155.628 87.124  134.245 1.00 84.58  0  140  GLU   D CA  1 
ATOM   12484 C C   . GLU   D 2 140  ? 154.160 87.538  134.232 1.00 84.30  0  140  GLU   D C   1 
ATOM   12485 O O   . GLU   D 2 140  ? 153.634 88.046  135.232 1.00 85.63  0  140  GLU   D O   1 
ATOM   12486 C CB  . GLU   D 2 140  ? 156.483 88.166  133.524 1.00 87.21  0  140  GLU   D CB  1 
ATOM   12487 C CG  . GLU   D 2 140  ? 157.973 87.876  133.541 1.00 89.30  0  140  GLU   D CG  1 
ATOM   12488 C CD  . GLU   D 2 140  ? 158.724 88.622  132.456 1.00 88.92  0  140  GLU   D CD  1 
ATOM   12489 O OE1 . GLU   D 2 140  ? 158.069 89.301  131.636 1.00 88.85  0  140  GLU   D OE1 1 
ATOM   12490 O OE2 . GLU   D 2 140  ? 159.969 88.529  132.421 1.00 88.64  -1 140  GLU   D OE2 1 
ATOM   12491 N N   . LYS   D 2 141  ? 153.484 87.327  133.100 1.00 76.50  0  141  LYS   D N   1 
ATOM   12492 C CA  . LYS   D 2 141  ? 152.072 87.682  133.000 1.00 75.58  0  141  LYS   D CA  1 
ATOM   12493 C C   . LYS   D 2 141  ? 151.233 86.886  133.989 1.00 78.84  0  141  LYS   D C   1 
ATOM   12494 O O   . LYS   D 2 141  ? 150.320 87.429  134.620 1.00 78.19  0  141  LYS   D O   1 
ATOM   12495 C CB  . LYS   D 2 141  ? 151.571 87.454  131.576 1.00 75.69  0  141  LYS   D CB  1 
ATOM   12496 C CG  . LYS   D 2 141  ? 152.086 88.456  130.564 1.00 73.09  0  141  LYS   D CG  1 
ATOM   12497 C CD  . LYS   D 2 141  ? 151.463 88.211  129.203 1.00 75.59  0  141  LYS   D CD  1 
ATOM   12498 C CE  . LYS   D 2 141  ? 151.709 89.376  128.267 1.00 75.61  0  141  LYS   D CE  1 
ATOM   12499 N NZ  . LYS   D 2 141  ? 153.160 89.601  128.039 1.00 79.50  1  141  LYS   D NZ  1 
ATOM   12500 N N   . LEU   D 2 142  ? 151.526 85.592  134.136 1.00 87.00  0  142  LEU   D N   1 
ATOM   12501 C CA  . LEU   D 2 142  ? 150.794 84.770  135.090 1.00 84.28  0  142  LEU   D CA  1 
ATOM   12502 C C   . LEU   D 2 142  ? 151.060 85.202  136.524 1.00 83.28  0  142  LEU   D C   1 
ATOM   12503 O O   . LEU   D 2 142  ? 150.145 85.176  137.353 1.00 84.68  0  142  LEU   D O   1 
ATOM   12504 C CB  . LEU   D 2 142  ? 151.155 83.298  134.903 1.00 82.30  0  142  LEU   D CB  1 
ATOM   12505 C CG  . LEU   D 2 142  ? 150.670 82.665  133.601 1.00 80.59  0  142  LEU   D CG  1 
ATOM   12506 C CD1 . LEU   D 2 142  ? 151.128 81.225  133.509 1.00 85.30  0  142  LEU   D CD1 1 
ATOM   12507 C CD2 . LEU   D 2 142  ? 149.166 82.756  133.496 1.00 84.62  0  142  LEU   D CD2 1 
ATOM   12508 N N   . SER   D 2 143  ? 152.295 85.599  136.838 1.00 85.19  0  143  SER   D N   1 
ATOM   12509 C CA  . SER   D 2 143  ? 152.573 86.121  138.172 1.00 87.66  0  143  SER   D CA  1 
ATOM   12510 C C   . SER   D 2 143  ? 151.773 87.389  138.443 1.00 89.03  0  143  SER   D C   1 
ATOM   12511 O O   . SER   D 2 143  ? 151.199 87.554  139.529 1.00 87.59  0  143  SER   D O   1 
ATOM   12512 C CB  . SER   D 2 143  ? 154.068 86.389  138.331 1.00 88.51  0  143  SER   D CB  1 
ATOM   12513 O OG  . SER   D 2 143  ? 154.346 86.973  139.591 1.00 86.88  0  143  SER   D OG  1 
ATOM   12514 N N   . GLU   D 2 144  ? 151.715 88.292  137.460 1.00 90.02  0  144  GLU   D N   1 
ATOM   12515 C CA  . GLU   D 2 144  ? 150.927 89.511  137.619 1.00 86.19  0  144  GLU   D CA  1 
ATOM   12516 C C   . GLU   D 2 144  ? 149.453 89.184  137.826 1.00 86.71  0  144  GLU   D C   1 
ATOM   12517 O O   . GLU   D 2 144  ? 148.791 89.757  138.703 1.00 89.34  0  144  GLU   D O   1 
ATOM   12518 C CB  . GLU   D 2 144  ? 151.108 90.414  136.399 1.00 86.56  0  144  GLU   D CB  1 
ATOM   12519 C CG  . GLU   D 2 144  ? 152.474 91.070  136.297 1.00 89.34  0  144  GLU   D CG  1 
ATOM   12520 C CD  . GLU   D 2 144  ? 152.652 92.205  137.283 1.00 90.88  0  144  GLU   D CD  1 
ATOM   12521 O OE1 . GLU   D 2 144  ? 151.661 92.907  137.569 1.00 93.39  0  144  GLU   D OE1 1 
ATOM   12522 O OE2 . GLU   D 2 144  ? 153.785 92.399  137.770 1.00 89.80  -1 144  GLU   D OE2 1 
ATOM   12523 N N   . ILE   D 2 145  ? 148.923 88.257  137.023 1.00 84.75  0  145  ILE   D N   1 
ATOM   12524 C CA  . ILE   D 2 145  ? 147.514 87.889  137.129 1.00 82.44  0  145  ILE   D CA  1 
ATOM   12525 C C   . ILE   D 2 145  ? 147.222 87.291  138.495 1.00 79.92  0  145  ILE   D C   1 
ATOM   12526 O O   . ILE   D 2 145  ? 146.211 87.617  139.125 1.00 78.75  0  145  ILE   D O   1 
ATOM   12527 C CB  . ILE   D 2 145  ? 147.121 86.924  135.997 1.00 79.74  0  145  ILE   D CB  1 
ATOM   12528 C CG1 . ILE   D 2 145  ? 146.952 87.681  134.683 1.00 81.43  0  145  ILE   D CG1 1 
ATOM   12529 C CG2 . ILE   D 2 145  ? 145.838 86.197  136.338 1.00 77.98  0  145  ILE   D CG2 1 
ATOM   12530 C CD1 . ILE   D 2 145  ? 146.954 86.793  133.466 1.00 78.99  0  145  ILE   D CD1 1 
ATOM   12531 N N   . LEU   D 2 146  ? 148.101 86.412  138.978 1.00 87.20  0  146  LEU   D N   1 
ATOM   12532 C CA  . LEU   D 2 146  ? 147.896 85.807  140.288 1.00 88.62  0  146  LEU   D CA  1 
ATOM   12533 C C   . LEU   D 2 146  ? 147.930 86.855  141.393 1.00 90.07  0  146  LEU   D C   1 
ATOM   12534 O O   . LEU   D 2 146  ? 147.113 86.814  142.321 1.00 92.38  0  146  LEU   D O   1 
ATOM   12535 C CB  . LEU   D 2 146  ? 148.945 84.725  140.534 1.00 89.19  0  146  LEU   D CB  1 
ATOM   12536 C CG  . LEU   D 2 146  ? 148.717 83.417  139.775 1.00 88.74  0  146  LEU   D CG  1 
ATOM   12537 C CD1 . LEU   D 2 146  ? 149.981 82.573  139.757 1.00 90.23  0  146  LEU   D CD1 1 
ATOM   12538 C CD2 . LEU   D 2 146  ? 147.564 82.645  140.390 1.00 88.77  0  146  LEU   D CD2 1 
ATOM   12539 N N   . GLY   D 2 147  ? 148.862 87.807  141.310 1.00 91.09  0  147  GLY   D N   1 
ATOM   12540 C CA  . GLY   D 2 147  ? 148.922 88.850  142.324 1.00 92.36  0  147  GLY   D CA  1 
ATOM   12541 C C   . GLY   D 2 147  ? 147.672 89.711  142.359 1.00 91.87  0  147  GLY   D C   1 
ATOM   12542 O O   . GLY   D 2 147  ? 147.108 89.965  143.430 1.00 89.59  0  147  GLY   D O   1 
ATOM   12543 N N   . MET   D 2 148  ? 147.209 90.158  141.188 1.00 91.48  0  148  MET   D N   1 
ATOM   12544 C CA  . MET   D 2 148  ? 146.011 90.993  141.154 1.00 87.15  0  148  MET   D CA  1 
ATOM   12545 C C   . MET   D 2 148  ? 144.768 90.202  141.548 1.00 87.99  0  148  MET   D C   1 
ATOM   12546 O O   . MET   D 2 148  ? 143.851 90.746  142.174 1.00 90.30  0  148  MET   D O   1 
ATOM   12547 C CB  . MET   D 2 148  ? 145.846 91.636  139.776 1.00 86.30  0  148  MET   D CB  1 
ATOM   12548 C CG  . MET   D 2 148  ? 147.136 92.242  139.242 1.00 90.93  0  148  MET   D CG  1 
ATOM   12549 S SD  . MET   D 2 148  ? 146.984 93.132  137.683 1.00 93.93  0  148  MET   D SD  1 
ATOM   12550 C CE  . MET   D 2 148  ? 145.483 92.429  137.030 1.00 83.71  0  148  MET   D CE  1 
ATOM   12551 N N   . LEU   D 2 149  ? 144.724 88.911  141.209 1.00 92.24  0  149  LEU   D N   1 
ATOM   12552 C CA  . LEU   D 2 149  ? 143.608 88.079  141.642 1.00 92.19  0  149  LEU   D CA  1 
ATOM   12553 C C   . LEU   D 2 149  ? 143.591 87.924  143.154 1.00 92.37  0  149  LEU   D C   1 
ATOM   12554 O O   . LEU   D 2 149  ? 142.523 87.955  143.770 1.00 93.19  0  149  LEU   D O   1 
ATOM   12555 C CB  . LEU   D 2 149  ? 143.670 86.712  140.970 1.00 92.14  0  149  LEU   D CB  1 
ATOM   12556 C CG  . LEU   D 2 149  ? 143.145 86.680  139.539 1.00 91.97  0  149  LEU   D CG  1 
ATOM   12557 C CD1 . LEU   D 2 149  ? 142.959 85.248  139.085 1.00 91.66  0  149  LEU   D CD1 1 
ATOM   12558 C CD2 . LEU   D 2 149  ? 141.850 87.460  139.446 1.00 89.81  0  149  LEU   D CD2 1 
ATOM   12559 N N   . HIS   D 2 150  ? 144.761 87.739  143.769 1.00 101.33 0  150  HIS   D N   1 
ATOM   12560 C CA  . HIS   D 2 150  ? 144.812 87.674  145.225 1.00 102.21 0  150  HIS   D CA  1 
ATOM   12561 C C   . HIS   D 2 150  ? 144.350 88.986  145.843 1.00 101.55 0  150  HIS   D C   1 
ATOM   12562 O O   . HIS   D 2 150  ? 143.607 88.990  146.836 1.00 102.06 0  150  HIS   D O   1 
ATOM   12563 C CB  . HIS   D 2 150  ? 146.224 87.322  145.690 1.00 103.40 0  150  HIS   D CB  1 
ATOM   12564 C CG  . HIS   D 2 150  ? 146.452 85.853  145.866 1.00 106.00 0  150  HIS   D CG  1 
ATOM   12565 N ND1 . HIS   D 2 150  ? 145.774 85.103  146.803 1.00 104.95 0  150  HIS   D ND1 1 
ATOM   12566 C CD2 . HIS   D 2 150  ? 147.276 84.994  145.221 1.00 104.13 0  150  HIS   D CD2 1 
ATOM   12567 C CE1 . HIS   D 2 150  ? 146.172 83.846  146.728 1.00 103.04 0  150  HIS   D CE1 1 
ATOM   12568 N NE2 . HIS   D 2 150  ? 147.083 83.753  145.776 1.00 103.31 0  150  HIS   D NE2 1 
ATOM   12569 N N   . THR   D 2 151  ? 144.775 90.111  145.260 1.00 101.57 0  151  THR   D N   1 
ATOM   12570 C CA  . THR   D 2 151  ? 144.333 91.413  145.754 1.00 103.60 0  151  THR   D CA  1 
ATOM   12571 C C   . THR   D 2 151  ? 142.814 91.531  145.697 1.00 102.13 0  151  THR   D C   1 
ATOM   12572 O O   . THR   D 2 151  ? 142.176 91.937  146.675 1.00 101.14 0  151  THR   D O   1 
ATOM   12573 C CB  . THR   D 2 151  ? 144.988 92.537  144.947 1.00 102.23 0  151  THR   D CB  1 
ATOM   12574 O OG1 . THR   D 2 151  ? 146.356 92.681  145.345 1.00 103.35 0  151  THR   D OG1 1 
ATOM   12575 C CG2 . THR   D 2 151  ? 144.271 93.851  145.188 1.00 98.58  0  151  THR   D CG2 1 
ATOM   12576 N N   . LEU   D 2 152  ? 142.216 91.157  144.564 1.00 91.23  0  152  LEU   D N   1 
ATOM   12577 C CA  . LEU   D 2 152  ? 140.761 91.212  144.437 1.00 89.23  0  152  LEU   D CA  1 
ATOM   12578 C C   . LEU   D 2 152  ? 140.078 90.285  145.435 1.00 92.68  0  152  LEU   D C   1 
ATOM   12579 O O   . LEU   D 2 152  ? 139.096 90.666  146.082 1.00 90.74  0  152  LEU   D O   1 
ATOM   12580 C CB  . LEU   D 2 152  ? 140.340 90.849  143.015 1.00 90.20  0  152  LEU   D CB  1 
ATOM   12581 C CG  . LEU   D 2 152  ? 140.470 91.904  141.926 1.00 88.36  0  152  LEU   D CG  1 
ATOM   12582 C CD1 . LEU   D 2 152  ? 140.251 91.275  140.566 1.00 87.28  0  152  LEU   D CD1 1 
ATOM   12583 C CD2 . LEU   D 2 152  ? 139.462 93.002  142.164 1.00 88.54  0  152  LEU   D CD2 1 
ATOM   12584 N N   . VAL   D 2 153  ? 140.583 89.057  145.567 1.00 104.85 0  153  VAL   D N   1 
ATOM   12585 C CA  . VAL   D 2 153  ? 139.899 88.047  146.369 1.00 103.64 0  153  VAL   D CA  1 
ATOM   12586 C C   . VAL   D 2 153  ? 139.909 88.426  147.842 1.00 103.91 0  153  VAL   D C   1 
ATOM   12587 O O   . VAL   D 2 153  ? 138.869 88.381  148.511 1.00 104.34 0  153  VAL   D O   1 
ATOM   12588 C CB  . VAL   D 2 153  ? 140.530 86.663  146.135 1.00 102.12 0  153  VAL   D CB  1 
ATOM   12589 C CG1 . VAL   D 2 153  ? 140.082 85.687  147.209 1.00 102.36 0  153  VAL   D CG1 1 
ATOM   12590 C CG2 . VAL   D 2 153  ? 140.152 86.141  144.761 1.00 101.89 0  153  VAL   D CG2 1 
ATOM   12591 N N   . VAL   D 2 154  ? 141.068 88.810  148.377 1.00 110.86 0  154  VAL   D N   1 
ATOM   12592 C CA  . VAL   D 2 154  ? 141.093 89.122  149.803 1.00 112.67 0  154  VAL   D CA  1 
ATOM   12593 C C   . VAL   D 2 154  ? 140.668 90.564  150.064 1.00 114.29 0  154  VAL   D C   1 
ATOM   12594 O O   . VAL   D 2 154  ? 140.414 90.938  151.215 1.00 113.52 0  154  VAL   D O   1 
ATOM   12595 C CB  . VAL   D 2 154  ? 142.474 88.826  150.405 1.00 112.34 0  154  VAL   D CB  1 
ATOM   12596 C CG1 . VAL   D 2 154  ? 142.893 87.399  150.090 1.00 113.52 0  154  VAL   D CG1 1 
ATOM   12597 C CG2 . VAL   D 2 154  ? 143.486 89.809  149.895 1.00 110.78 0  154  VAL   D CG2 1 
ATOM   12598 N N   . ALA   D 2 155  ? 140.580 91.395  149.021 1.00 114.79 0  155  ALA   D N   1 
ATOM   12599 C CA  . ALA   D 2 155  ? 140.047 92.741  149.200 1.00 113.74 0  155  ALA   D CA  1 
ATOM   12600 C C   . ALA   D 2 155  ? 138.533 92.726  149.351 1.00 114.47 0  155  ALA   D C   1 
ATOM   12601 O O   . ALA   D 2 155  ? 137.957 93.664  149.913 1.00 112.39 0  155  ALA   D O   1 
ATOM   12602 C CB  . ALA   D 2 155  ? 140.455 93.630  148.028 1.00 111.60 0  155  ALA   D CB  1 
ATOM   12603 N N   . SER   D 2 156  ? 137.876 91.677  148.861 1.00 123.54 0  156  SER   D N   1 
ATOM   12604 C CA  . SER   D 2 156  ? 136.433 91.494  148.988 1.00 123.58 0  156  SER   D CA  1 
ATOM   12605 C C   . SER   D 2 156  ? 136.024 90.994  150.358 1.00 123.00 0  156  SER   D C   1 
ATOM   12606 O O   . SER   D 2 156  ? 134.883 90.541  150.525 1.00 121.71 0  156  SER   D O   1 
ATOM   12607 C CB  . SER   D 2 156  ? 135.930 90.532  147.910 1.00 122.36 0  156  SER   D CB  1 
ATOM   12608 O OG  . SER   D 2 156  ? 136.141 91.060  146.611 1.00 122.63 0  156  SER   D OG  1 
ATOM   12609 N N   . ALA   D 2 157  ? 136.930 91.057  151.330 1.00 133.20 0  157  ALA   D N   1 
ATOM   12610 C CA  . ALA   D 2 157  ? 136.626 90.605  152.680 1.00 133.92 0  157  ALA   D CA  1 
ATOM   12611 C C   . ALA   D 2 157  ? 135.601 91.524  153.334 1.00 135.43 0  157  ALA   D C   1 
ATOM   12612 O O   . ALA   D 2 157  ? 135.661 92.749  153.188 1.00 134.35 0  157  ALA   D O   1 
ATOM   12613 C CB  . ALA   D 2 157  ? 137.901 90.548  153.518 1.00 131.43 0  157  ALA   D CB  1 
ATOM   12614 N N   . GLY   D 2 158  ? 134.660 90.925  154.056 1.00 141.52 0  158  GLY   D N   1 
ATOM   12615 C CA  . GLY   D 2 158  ? 133.608 91.654  154.725 1.00 140.28 0  158  GLY   D CA  1 
ATOM   12616 C C   . GLY   D 2 158  ? 133.901 92.043  156.165 1.00 141.65 0  158  GLY   D C   1 
ATOM   12617 O O   . GLY   D 2 158  ? 133.782 93.215  156.535 1.00 140.94 0  158  GLY   D O   1 
ATOM   12618 N N   . PRO   D 2 159  ? 134.280 91.077  157.011 1.00 146.88 0  159  PRO   D N   1 
ATOM   12619 C CA  . PRO   D 2 159  ? 134.401 91.368  158.446 1.00 146.03 0  159  PRO   D CA  1 
ATOM   12620 C C   . PRO   D 2 159  ? 135.470 92.407  158.750 1.00 145.05 0  159  PRO   D C   1 
ATOM   12621 O O   . PRO   D 2 159  ? 136.450 92.562  158.018 1.00 144.72 0  159  PRO   D O   1 
ATOM   12622 C CB  . PRO   D 2 159  ? 134.760 90.008  159.056 1.00 146.22 0  159  PRO   D CB  1 
ATOM   12623 C CG  . PRO   D 2 159  ? 135.326 89.222  157.929 1.00 145.40 0  159  PRO   D CG  1 
ATOM   12624 C CD  . PRO   D 2 159  ? 134.544 89.654  156.735 1.00 145.34 0  159  PRO   D CD  1 
ATOM   12625 N N   . THR   D 2 160  ? 135.259 93.125  159.858 1.00 143.75 0  160  THR   D N   1 
ATOM   12626 C CA  . THR   D 2 160  ? 136.175 94.188  160.263 1.00 144.95 0  160  THR   D CA  1 
ATOM   12627 C C   . THR   D 2 160  ? 137.563 93.651  160.590 1.00 143.90 0  160  THR   D C   1 
ATOM   12628 O O   . THR   D 2 160  ? 138.549 94.392  160.502 1.00 143.18 0  160  THR   D O   1 
ATOM   12629 C CB  . THR   D 2 160  ? 135.601 94.937  161.470 1.00 144.83 0  160  THR   D CB  1 
ATOM   12630 O OG1 . THR   D 2 160  ? 134.221 95.243  161.234 1.00 143.98 0  160  THR   D OG1 1 
ATOM   12631 C CG2 . THR   D 2 160  ? 136.360 96.234  161.718 1.00 143.64 0  160  THR   D CG2 1 
ATOM   12632 N N   . SER   D 2 161  ? 137.664 92.376  160.973 1.00 145.54 0  161  SER   D N   1 
ATOM   12633 C CA  . SER   D 2 161  ? 138.960 91.814  161.341 1.00 146.35 0  161  SER   D CA  1 
ATOM   12634 C C   . SER   D 2 161  ? 139.934 91.863  160.170 1.00 146.99 0  161  SER   D C   1 
ATOM   12635 O O   . SER   D 2 161  ? 141.086 92.285  160.324 1.00 146.30 0  161  SER   D O   1 
ATOM   12636 C CB  . SER   D 2 161  ? 138.786 90.379  161.838 1.00 146.13 0  161  SER   D CB  1 
ATOM   12637 O OG  . SER   D 2 161  ? 138.394 89.519  160.782 1.00 144.97 0  161  SER   D OG  1 
ATOM   12638 N N   . ALA   D 2 162  ? 139.482 91.448  158.985 1.00 144.48 0  162  ALA   D N   1 
ATOM   12639 C CA  . ALA   D 2 162  ? 140.351 91.470  157.812 1.00 143.49 0  162  ALA   D CA  1 
ATOM   12640 C C   . ALA   D 2 162  ? 140.710 92.897  157.416 1.00 143.44 0  162  ALA   D C   1 
ATOM   12641 O O   . ALA   D 2 162  ? 141.845 93.170  157.008 1.00 141.65 0  162  ALA   D O   1 
ATOM   12642 C CB  . ALA   D 2 162  ? 139.680 90.740  156.650 1.00 141.77 0  162  ALA   D CB  1 
ATOM   12643 N N   . ARG   D 2 163  ? 139.752 93.819  157.523 1.00 136.92 0  163  ARG   D N   1 
ATOM   12644 C CA  . ARG   D 2 163  ? 140.017 95.215  157.194 1.00 134.54 0  163  ARG   D CA  1 
ATOM   12645 C C   . ARG   D 2 163  ? 141.093 95.799  158.104 1.00 135.65 0  163  ARG   D C   1 
ATOM   12646 O O   . ARG   D 2 163  ? 142.045 96.441  157.638 1.00 134.49 0  163  ARG   D O   1 
ATOM   12647 C CB  . ARG   D 2 163  ? 138.720 96.019  157.303 1.00 134.31 0  163  ARG   D CB  1 
ATOM   12648 C CG  . ARG   D 2 163  ? 137.507 95.318  156.702 1.00 134.22 0  163  ARG   D CG  1 
ATOM   12649 C CD  . ARG   D 2 163  ? 136.340 96.277  156.504 1.00 135.12 0  163  ARG   D CD  1 
ATOM   12650 N NE  . ARG   D 2 163  ? 135.590 96.519  157.732 1.00 134.96 0  163  ARG   D NE  1 
ATOM   12651 C CZ  . ARG   D 2 163  ? 134.328 96.159  157.919 1.00 134.84 0  163  ARG   D CZ  1 
ATOM   12652 N NH1 . ARG   D 2 163  ? 133.637 95.546  156.973 1.00 135.17 1  163  ARG   D NH1 1 
ATOM   12653 N NH2 . ARG   D 2 163  ? 133.742 96.428  159.082 1.00 134.98 0  163  ARG   D NH2 1 
ATOM   12654 N N   . ASP   D 2 164  ? 140.959 95.572  159.413 1.00 138.83 0  164  ASP   D N   1 
ATOM   12655 C CA  . ASP   D 2 164  ? 141.946 96.071  160.362 1.00 137.21 0  164  ASP   D CA  1 
ATOM   12656 C C   . ASP   D 2 164  ? 143.296 95.400  160.151 1.00 137.10 0  164  ASP   D C   1 
ATOM   12657 O O   . ASP   D 2 164  ? 144.344 96.040  160.291 1.00 136.24 0  164  ASP   D O   1 
ATOM   12658 C CB  . ASP   D 2 164  ? 141.451 95.855  161.792 1.00 137.49 0  164  ASP   D CB  1 
ATOM   12659 C CG  . ASP   D 2 164  ? 140.078 96.453  162.028 1.00 136.08 0  164  ASP   D CG  1 
ATOM   12660 O OD1 . ASP   D 2 164  ? 139.602 97.213  161.159 1.00 135.10 0  164  ASP   D OD1 1 
ATOM   12661 O OD2 . ASP   D 2 164  ? 139.472 96.160  163.079 1.00 135.10 -1 164  ASP   D OD2 1 
ATOM   12662 N N   . GLY   D 2 165  ? 143.291 94.108  159.816 1.00 140.34 0  165  GLY   D N   1 
ATOM   12663 C CA  . GLY   D 2 165  ? 144.540 93.432  159.513 1.00 140.14 0  165  GLY   D CA  1 
ATOM   12664 C C   . GLY   D 2 165  ? 145.246 94.026  158.311 1.00 139.96 0  165  GLY   D C   1 
ATOM   12665 O O   . GLY   D 2 165  ? 146.462 94.216  158.327 1.00 139.07 0  165  GLY   D O   1 
ATOM   12666 N N   . ILE   D 2 166  ? 144.491 94.337  157.254 1.00 136.36 0  166  ILE   D N   1 
ATOM   12667 C CA  . ILE   D 2 166  ? 145.086 94.957  156.073 1.00 136.34 0  166  ILE   D CA  1 
ATOM   12668 C C   . ILE   D 2 166  ? 145.635 96.338  156.412 1.00 137.05 0  166  ILE   D C   1 
ATOM   12669 O O   . ILE   D 2 166  ? 146.732 96.710  155.975 1.00 137.41 0  166  ILE   D O   1 
ATOM   12670 C CB  . ILE   D 2 166  ? 144.064 95.015  154.923 1.00 134.94 0  166  ILE   D CB  1 
ATOM   12671 C CG1 . ILE   D 2 166  ? 143.711 93.605  154.450 1.00 134.86 0  166  ILE   D CG1 1 
ATOM   12672 C CG2 . ILE   D 2 166  ? 144.612 95.823  153.758 1.00 133.52 0  166  ILE   D CG2 1 
ATOM   12673 C CD1 . ILE   D 2 166  ? 142.548 93.559  153.486 1.00 134.81 0  166  ILE   D CD1 1 
ATOM   12674 N N   . ARG   D 2 167  ? 144.886 97.121  157.193 1.00 137.00 0  167  ARG   D N   1 
ATOM   12675 C CA  . ARG   D 2 167  ? 145.352 98.456  157.564 1.00 136.36 0  167  ARG   D CA  1 
ATOM   12676 C C   . ARG   D 2 167  ? 146.638 98.388  158.386 1.00 137.60 0  167  ARG   D C   1 
ATOM   12677 O O   . ARG   D 2 167  ? 147.592 99.139  158.140 1.00 136.48 0  167  ARG   D O   1 
ATOM   12678 C CB  . ARG   D 2 167  ? 144.253 99.190  158.332 1.00 135.09 0  167  ARG   D CB  1 
ATOM   12679 C CG  . ARG   D 2 167  ? 144.527 100.661 158.584 1.00 135.22 0  167  ARG   D CG  1 
ATOM   12680 C CD  . ARG   D 2 167  ? 143.443 101.257 159.462 1.00 135.68 0  167  ARG   D CD  1 
ATOM   12681 N NE  . ARG   D 2 167  ? 143.428 100.645 160.785 1.00 137.29 0  167  ARG   D NE  1 
ATOM   12682 C CZ  . ARG   D 2 167  ? 142.328 100.368 161.471 1.00 137.54 0  167  ARG   D CZ  1 
ATOM   12683 N NH1 . ARG   D 2 167  ? 141.125 100.623 160.982 1.00 136.95 1  167  ARG   D NH1 1 
ATOM   12684 N NH2 . ARG   D 2 167  ? 142.438 99.818  162.677 1.00 136.86 0  167  ARG   D NH2 1 
ATOM   12685 N N   . ASP   D 2 168  ? 146.688 97.479  159.364 1.00 139.35 0  168  ASP   D N   1 
ATOM   12686 C CA  . ASP   D 2 168  ? 147.892 97.338  160.178 1.00 139.08 0  168  ASP   D CA  1 
ATOM   12687 C C   . ASP   D 2 168  ? 149.059 96.785  159.370 1.00 137.95 0  168  ASP   D C   1 
ATOM   12688 O O   . ASP   D 2 168  ? 150.211 97.170  159.605 1.00 136.77 0  168  ASP   D O   1 
ATOM   12689 C CB  . ASP   D 2 168  ? 147.608 96.447  161.387 1.00 138.83 0  168  ASP   D CB  1 
ATOM   12690 C CG  . ASP   D 2 168  ? 146.952 97.203  162.527 1.00 137.60 0  168  ASP   D CG  1 
ATOM   12691 O OD1 . ASP   D 2 168  ? 146.988 98.451  162.514 1.00 136.91 0  168  ASP   D OD1 1 
ATOM   12692 O OD2 . ASP   D 2 168  ? 146.401 96.549  163.436 1.00 137.03 -1 168  ASP   D OD2 1 
ATOM   12693 N N   . ALA   D 2 169  ? 148.788 95.886  158.419 1.00 135.16 0  169  ALA   D N   1 
ATOM   12694 C CA  . ALA   D 2 169  ? 149.841 95.396  157.538 1.00 134.59 0  169  ALA   D CA  1 
ATOM   12695 C C   . ALA   D 2 169  ? 150.412 96.523  156.691 1.00 134.58 0  169  ALA   D C   1 
ATOM   12696 O O   . ALA   D 2 169  ? 151.626 96.596  156.479 1.00 133.49 0  169  ALA   D O   1 
ATOM   12697 C CB  . ALA   D 2 169  ? 149.303 94.276  156.649 1.00 133.08 0  169  ALA   D CB  1 
ATOM   12698 N N   . MET   D 2 170  ? 149.549 97.413  156.195 1.00 135.77 0  170  MET   D N   1 
ATOM   12699 C CA  . MET   D 2 170  ? 150.030 98.571  155.449 1.00 135.57 0  170  MET   D CA  1 
ATOM   12700 C C   . MET   D 2 170  ? 150.843 99.512  156.331 1.00 136.34 0  170  MET   D C   1 
ATOM   12701 O O   . MET   D 2 170  ? 151.844 100.075 155.873 1.00 137.08 0  170  MET   D O   1 
ATOM   12702 C CB  . MET   D 2 170  ? 148.854 99.313  154.815 1.00 135.19 0  170  MET   D CB  1 
ATOM   12703 C CG  . MET   D 2 170  ? 148.169 98.547  153.691 1.00 135.23 0  170  MET   D CG  1 
ATOM   12704 S SD  . MET   D 2 170  ? 149.294 98.024  152.380 1.00 132.83 0  170  MET   D SD  1 
ATOM   12705 C CE  . MET   D 2 170  ? 150.102 99.570  151.973 1.00 132.41 0  170  MET   D CE  1 
ATOM   12706 N N   . ILE   D 2 171  ? 150.432 99.700  157.587 1.00 136.06 0  171  ILE   D N   1 
ATOM   12707 C CA  . ILE   D 2 171  ? 151.209 100.534 158.505 1.00 136.34 0  171  ILE   D CA  1 
ATOM   12708 C C   . ILE   D 2 171  ? 152.594 99.933  158.729 1.00 136.33 0  171  ILE   D C   1 
ATOM   12709 O O   . ILE   D 2 171  ? 153.617 100.635 158.699 1.00 135.11 0  171  ILE   D O   1 
ATOM   12710 C CB  . ILE   D 2 171  ? 150.450 100.717 159.833 1.00 135.66 0  171  ILE   D CB  1 
ATOM   12711 C CG1 . ILE   D 2 171  ? 149.348 101.767 159.677 1.00 135.66 0  171  ILE   D CG1 1 
ATOM   12712 C CG2 . ILE   D 2 171  ? 151.405 101.103 160.953 1.00 135.83 0  171  ILE   D CG2 1 
ATOM   12713 C CD1 . ILE   D 2 171  ? 148.466 101.911 160.898 1.00 134.81 0  171  ILE   D CD1 1 
ATOM   12714 N N   . GLY   D 2 172  ? 152.645 98.620  158.961 1.00 138.85 0  172  GLY   D N   1 
ATOM   12715 C CA  . GLY   D 2 172  ? 153.927 97.955  159.121 1.00 138.39 0  172  GLY   D CA  1 
ATOM   12716 C C   . GLY   D 2 172  ? 154.778 98.032  157.870 1.00 137.91 0  172  GLY   D C   1 
ATOM   12717 O O   . GLY   D 2 172  ? 155.999 98.177  157.947 1.00 138.58 0  172  GLY   D O   1 
ATOM   12718 N N   . LEU   D 2 173  ? 154.144 97.935  156.699 1.00 133.92 0  173  LEU   D N   1 
ATOM   12719 C CA  . LEU   D 2 173  ? 154.866 98.091  155.442 1.00 133.67 0  173  LEU   D CA  1 
ATOM   12720 C C   . LEU   D 2 173  ? 155.460 99.488  155.322 1.00 133.69 0  173  LEU   D C   1 
ATOM   12721 O O   . LEU   D 2 173  ? 156.593 99.650  154.861 1.00 133.24 0  173  LEU   D O   1 
ATOM   12722 C CB  . LEU   D 2 173  ? 153.933 97.797  154.266 1.00 133.07 0  173  LEU   D CB  1 
ATOM   12723 C CG  . LEU   D 2 173  ? 154.532 97.807  152.858 1.00 133.05 0  173  LEU   D CG  1 
ATOM   12724 C CD1 . LEU   D 2 173  ? 153.966 96.670  152.031 1.00 132.69 0  173  LEU   D CD1 1 
ATOM   12725 C CD2 . LEU   D 2 173  ? 154.264 99.135  152.174 1.00 133.85 0  173  LEU   D CD2 1 
ATOM   12726 N N   . ARG   D 2 174  ? 154.703 100.509 155.728 1.00 137.03 0  174  ARG   D N   1 
ATOM   12727 C CA  . ARG   D 2 174  ? 155.216 101.876 155.693 1.00 138.01 0  174  ARG   D CA  1 
ATOM   12728 C C   . ARG   D 2 174  ? 156.421 102.039 156.612 1.00 139.29 0  174  ARG   D C   1 
ATOM   12729 O O   . ARG   D 2 174  ? 157.431 102.645 156.229 1.00 138.89 0  174  ARG   D O   1 
ATOM   12730 C CB  . ARG   D 2 174  ? 154.110 102.855 156.082 1.00 137.92 0  174  ARG   D CB  1 
ATOM   12731 C CG  . ARG   D 2 174  ? 154.529 104.311 156.036 1.00 137.66 0  174  ARG   D CG  1 
ATOM   12732 C CD  . ARG   D 2 174  ? 153.364 105.238 156.350 1.00 137.18 0  174  ARG   D CD  1 
ATOM   12733 N NE  . ARG   D 2 174  ? 153.024 105.233 157.768 1.00 138.30 0  174  ARG   D NE  1 
ATOM   12734 C CZ  . ARG   D 2 174  ? 153.639 105.965 158.687 1.00 138.17 0  174  ARG   D CZ  1 
ATOM   12735 N NH1 . ARG   D 2 174  ? 154.640 106.770 158.374 1.00 136.56 1  174  ARG   D NH1 1 
ATOM   12736 N NH2 . ARG   D 2 174  ? 153.238 105.887 159.953 1.00 138.20 0  174  ARG   D NH2 1 
ATOM   12737 N N   . GLU   D 2 175  ? 156.335 101.498 157.830 1.00 140.20 0  175  GLU   D N   1 
ATOM   12738 C CA  . GLU   D 2 175  ? 157.464 101.588 158.755 1.00 137.18 0  175  GLU   D CA  1 
ATOM   12739 C C   . GLU   D 2 175  ? 158.679 100.831 158.223 1.00 135.63 0  175  GLU   D C   1 
ATOM   12740 O O   . GLU   D 2 175  ? 159.818 101.309 158.329 1.00 134.99 0  175  GLU   D O   1 
ATOM   12741 C CB  . GLU   D 2 175  ? 157.057 101.066 160.132 1.00 137.24 0  175  GLU   D CB  1 
ATOM   12742 C CG  . GLU   D 2 175  ? 155.981 101.902 160.809 1.00 136.56 0  175  GLU   D CG  1 
ATOM   12743 C CD  . GLU   D 2 175  ? 155.528 101.318 162.133 1.00 136.86 0  175  GLU   D CD  1 
ATOM   12744 O OE1 . GLU   D 2 175  ? 156.051 100.255 162.529 1.00 137.30 0  175  GLU   D OE1 1 
ATOM   12745 O OE2 . GLU   D 2 175  ? 154.646 101.924 162.778 1.00 136.00 -1 175  GLU   D OE2 1 
ATOM   12746 N N   . GLU   D 2 176  ? 158.454 99.648  157.644 1.00 139.61 0  176  GLU   D N   1 
ATOM   12747 C CA  . GLU   D 2 176  ? 159.550 98.884  157.059 1.00 140.97 0  176  GLU   D CA  1 
ATOM   12748 C C   . GLU   D 2 176  ? 160.189 99.638  155.903 1.00 140.67 0  176  GLU   D C   1 
ATOM   12749 O O   . GLU   D 2 176  ? 161.411 99.602  155.731 1.00 139.85 0  176  GLU   D O   1 
ATOM   12750 C CB  . GLU   D 2 176  ? 159.050 97.518  156.591 1.00 139.96 0  176  GLU   D CB  1 
ATOM   12751 C CG  . GLU   D 2 176  ? 158.768 96.537  157.712 1.00 139.90 0  176  GLU   D CG  1 
ATOM   12752 C CD  . GLU   D 2 176  ? 158.060 95.289  157.225 1.00 140.44 0  176  GLU   D CD  1 
ATOM   12753 O OE1 . GLU   D 2 176  ? 157.571 95.291  156.076 1.00 140.64 0  176  GLU   D OE1 1 
ATOM   12754 O OE2 . GLU   D 2 176  ? 157.993 94.304  157.992 1.00 141.35 -1 176  GLU   D OE2 1 
ATOM   12755 N N   . MET   D 2 177  ? 159.375 100.308 155.085 1.00 136.56 0  177  MET   D N   1 
ATOM   12756 C CA  . MET   D 2 177  ? 159.916 101.108 153.992 1.00 136.59 0  177  MET   D CA  1 
ATOM   12757 C C   . MET   D 2 177  ? 160.755 102.261 154.522 1.00 135.49 0  177  MET   D C   1 
ATOM   12758 O O   . MET   D 2 177  ? 161.824 102.560 153.978 1.00 134.44 0  177  MET   D O   1 
ATOM   12759 C CB  . MET   D 2 177  ? 158.783 101.625 153.107 1.00 136.12 0  177  MET   D CB  1 
ATOM   12760 C CG  . MET   D 2 177  ? 158.156 100.560 152.222 1.00 135.93 0  177  MET   D CG  1 
ATOM   12761 S SD  . MET   D 2 177  ? 159.337 99.307  151.691 1.00 137.19 0  177  MET   D SD  1 
ATOM   12762 C CE  . MET   D 2 177  ? 160.311 100.235 150.508 1.00 133.48 0  177  MET   D CE  1 
ATOM   12763 N N   . ILE   D 2 178  ? 160.290 102.914 155.590 1.00 135.51 0  178  ILE   D N   1 
ATOM   12764 C CA  . ILE   D 2 178  ? 161.076 103.979 156.212 1.00 136.02 0  178  ILE   D CA  1 
ATOM   12765 C C   . ILE   D 2 178  ? 162.438 103.446 156.643 1.00 136.56 0  178  ILE   D C   1 
ATOM   12766 O O   . ILE   D 2 178  ? 163.488 104.021 156.319 1.00 135.42 0  178  ILE   D O   1 
ATOM   12767 C CB  . ILE   D 2 178  ? 160.310 104.585 157.403 1.00 134.79 0  178  ILE   D CB  1 
ATOM   12768 C CG1 . ILE   D 2 178  ? 159.266 105.591 156.918 1.00 134.69 0  178  ILE   D CG1 1 
ATOM   12769 C CG2 . ILE   D 2 178  ? 161.266 105.242 158.387 1.00 133.38 0  178  ILE   D CG2 1 
ATOM   12770 C CD1 . ILE   D 2 178  ? 158.309 106.043 157.999 1.00 134.05 0  178  ILE   D CD1 1 
ATOM   12771 N N   . GLU   D 2 179  ? 162.437 102.323 157.366 1.00 141.20 0  179  GLU   D N   1 
ATOM   12772 C CA  . GLU   D 2 179  ? 163.690 101.779 157.882 1.00 139.68 0  179  GLU   D CA  1 
ATOM   12773 C C   . GLU   D 2 179  ? 164.615 101.332 156.755 1.00 140.04 0  179  GLU   D C   1 
ATOM   12774 O O   . GLU   D 2 179  ? 165.823 101.594 156.796 1.00 140.29 0  179  GLU   D O   1 
ATOM   12775 C CB  . GLU   D 2 179  ? 163.407 100.622 158.838 1.00 138.68 0  179  GLU   D CB  1 
ATOM   12776 C CG  . GLU   D 2 179  ? 164.633 100.142 159.596 1.00 139.77 0  179  GLU   D CG  1 
ATOM   12777 C CD  . GLU   D 2 179  ? 165.219 101.213 160.498 1.00 141.96 0  179  GLU   D CD  1 
ATOM   12778 O OE1 . GLU   D 2 179  ? 164.454 102.075 160.979 1.00 142.79 0  179  GLU   D OE1 1 
ATOM   12779 O OE2 . GLU   D 2 179  ? 166.448 101.194 160.722 1.00 141.46 -1 179  GLU   D OE2 1 
ATOM   12780 N N   . LYS   D 2 180  ? 164.069 100.665 155.736 1.00 136.87 0  180  LYS   D N   1 
ATOM   12781 C CA  . LYS   D 2 180  ? 164.894 100.169 154.641 1.00 135.85 0  180  LYS   D CA  1 
ATOM   12782 C C   . LYS   D 2 180  ? 165.445 101.306 153.794 1.00 135.64 0  180  LYS   D C   1 
ATOM   12783 O O   . LYS   D 2 180  ? 166.553 101.195 153.258 1.00 134.62 0  180  LYS   D O   1 
ATOM   12784 C CB  . LYS   D 2 180  ? 164.084 99.200  153.781 1.00 135.32 0  180  LYS   D CB  1 
ATOM   12785 C CG  . LYS   D 2 180  ? 164.860 98.569  152.638 1.00 135.78 0  180  LYS   D CG  1 
ATOM   12786 C CD  . LYS   D 2 180  ? 164.109 97.381  152.058 1.00 135.59 0  180  LYS   D CD  1 
ATOM   12787 C CE  . LYS   D 2 180  ? 164.708 96.943  150.735 1.00 135.27 0  180  LYS   D CE  1 
ATOM   12788 N NZ  . LYS   D 2 180  ? 166.160 96.643  150.861 1.00 135.38 1  180  LYS   D NZ  1 
ATOM   12789 N N   . ILE   D 2 181  ? 164.694 102.400 153.654 1.00 135.52 0  181  ILE   D N   1 
ATOM   12790 C CA  . ILE   D 2 181  ? 165.204 103.557 152.930 1.00 135.71 0  181  ILE   D CA  1 
ATOM   12791 C C   . ILE   D 2 181  ? 166.319 104.231 153.719 1.00 136.18 0  181  ILE   D C   1 
ATOM   12792 O O   . ILE   D 2 181  ? 167.354 104.608 153.154 1.00 134.13 0  181  ILE   D O   1 
ATOM   12793 C CB  . ILE   D 2 181  ? 164.058 104.533 152.611 1.00 134.75 0  181  ILE   D CB  1 
ATOM   12794 C CG1 . ILE   D 2 181  ? 163.297 104.070 151.366 1.00 134.32 0  181  ILE   D CG1 1 
ATOM   12795 C CG2 . ILE   D 2 181  ? 164.589 105.947 152.423 1.00 133.53 0  181  ILE   D CG2 1 
ATOM   12796 C CD1 . ILE   D 2 181  ? 161.949 104.734 151.188 1.00 134.90 0  181  ILE   D CD1 1 
ATOM   12797 N N   . ARG   D 2 182  ? 166.144 104.378 155.033 1.00 138.72 0  182  ARG   D N   1 
ATOM   12798 C CA  . ARG   D 2 182  ? 167.118 105.104 155.839 1.00 138.16 0  182  ARG   D CA  1 
ATOM   12799 C C   . ARG   D 2 182  ? 168.245 104.221 156.363 1.00 135.56 0  182  ARG   D C   1 
ATOM   12800 O O   . ARG   D 2 182  ? 169.106 104.713 157.100 1.00 134.57 0  182  ARG   D O   1 
ATOM   12801 C CB  . ARG   D 2 182  ? 166.423 105.815 157.003 1.00 137.73 0  182  ARG   D CB  1 
ATOM   12802 C CG  . ARG   D 2 182  ? 166.089 104.949 158.202 1.00 136.06 0  182  ARG   D CG  1 
ATOM   12803 C CD  . ARG   D 2 182  ? 165.491 105.812 159.302 1.00 135.11 0  182  ARG   D CD  1 
ATOM   12804 N NE  . ARG   D 2 182  ? 165.052 105.037 160.455 1.00 136.61 0  182  ARG   D NE  1 
ATOM   12805 C CZ  . ARG   D 2 182  ? 164.566 105.571 161.568 1.00 136.56 0  182  ARG   D CZ  1 
ATOM   12806 N NH1 . ARG   D 2 182  ? 164.450 106.881 161.713 1.00 135.80 1  182  ARG   D NH1 1 
ATOM   12807 N NH2 . ARG   D 2 182  ? 164.187 104.770 162.560 1.00 136.43 0  182  ARG   D NH2 1 
ATOM   12808 N N   . THR   D 2 183  ? 168.268 102.937 156.000 1.00 138.73 0  183  THR   D N   1 
ATOM   12809 C CA  . THR   D 2 183  ? 169.360 102.072 156.435 1.00 140.61 0  183  THR   D CA  1 
ATOM   12810 C C   . THR   D 2 183  ? 170.694 102.465 155.812 1.00 141.07 0  183  THR   D C   1 
ATOM   12811 O O   . THR   D 2 183  ? 171.745 102.075 156.333 1.00 141.55 0  183  THR   D O   1 
ATOM   12812 C CB  . THR   D 2 183  ? 169.050 100.608 156.109 1.00 140.22 0  183  THR   D CB  1 
ATOM   12813 O OG1 . THR   D 2 183  ? 169.884 99.754  156.902 1.00 138.93 0  183  THR   D OG1 1 
ATOM   12814 C CG2 . THR   D 2 183  ? 169.309 100.317 154.638 1.00 139.43 0  183  THR   D CG2 1 
ATOM   12815 N N   . GLU   D 2 184  ? 170.682 103.225 154.721 1.00 137.00 0  184  GLU   D N   1 
ATOM   12816 C CA  . GLU   D 2 184  ? 171.919 103.625 154.059 1.00 137.03 0  184  GLU   D CA  1 
ATOM   12817 C C   . GLU   D 2 184  ? 172.093 105.141 154.078 1.00 135.83 0  184  GLU   D C   1 
ATOM   12818 O O   . GLU   D 2 184  ? 171.126 105.894 153.957 1.00 135.51 0  184  GLU   D O   1 
ATOM   12819 C CB  . GLU   D 2 184  ? 171.944 103.108 152.619 1.00 135.97 0  184  GLU   D CB  1 
ATOM   12820 C CG  . GLU   D 2 184  ? 173.204 103.468 151.849 1.00 134.48 0  184  GLU   D CG  1 
ATOM   12821 C CD  . GLU   D 2 184  ? 173.255 102.816 150.483 1.00 134.49 0  184  GLU   D CD  1 
ATOM   12822 O OE1 . GLU   D 2 184  ? 172.366 101.993 150.182 1.00 135.15 0  184  GLU   D OE1 1 
ATOM   12823 O OE2 . GLU   D 2 184  ? 174.183 103.128 149.709 1.00 134.93 -1 184  GLU   D OE2 1 
ATOM   12824 N N   . ILE   E 2 131  ? 161.276 72.002  128.351 1.00 102.09 0  131  ILE   E N   1 
ATOM   12825 C CA  . ILE   E 2 131  ? 160.294 72.916  127.782 1.00 102.02 0  131  ILE   E CA  1 
ATOM   12826 C C   . ILE   E 2 131  ? 158.885 72.539  128.235 1.00 104.71 0  131  ILE   E C   1 
ATOM   12827 O O   . ILE   E 2 131  ? 158.075 73.409  128.550 1.00 105.95 0  131  ILE   E O   1 
ATOM   12828 C CB  . ILE   E 2 131  ? 160.399 72.952  126.240 1.00 101.69 0  131  ILE   E CB  1 
ATOM   12829 C CG1 . ILE   E 2 131  ? 159.271 73.795  125.640 1.00 101.45 0  131  ILE   E CG1 1 
ATOM   12830 C CG2 . ILE   E 2 131  ? 160.411 71.544  125.658 1.00 103.28 0  131  ILE   E CG2 1 
ATOM   12831 C CD1 . ILE   E 2 131  ? 159.326 73.901  124.134 1.00 101.15 0  131  ILE   E CD1 1 
ATOM   12832 N N   . THR   E 2 132  ? 158.599 71.235  128.281 1.00 109.05 0  132  THR   E N   1 
ATOM   12833 C CA  . THR   E 2 132  ? 157.281 70.779  128.707 1.00 108.42 0  132  THR   E CA  1 
ATOM   12834 C C   . THR   E 2 132  ? 157.030 71.036  130.186 1.00 108.41 0  132  THR   E C   1 
ATOM   12835 O O   . THR   E 2 132  ? 155.870 71.168  130.590 1.00 109.57 0  132  THR   E O   1 
ATOM   12836 C CB  . THR   E 2 132  ? 157.110 69.291  128.402 1.00 107.96 0  132  THR   E CB  1 
ATOM   12837 O OG1 . THR   E 2 132  ? 158.204 68.557  128.965 1.00 109.86 0  132  THR   E OG1 1 
ATOM   12838 C CG2 . THR   E 2 132  ? 157.069 69.061  126.899 1.00 106.03 0  132  THR   E CG2 1 
ATOM   12839 N N   . ALA   E 2 133  ? 158.085 71.106  131.001 1.00 108.79 0  133  ALA   E N   1 
ATOM   12840 C CA  . ALA   E 2 133  ? 157.907 71.476  132.402 1.00 110.18 0  133  ALA   E CA  1 
ATOM   12841 C C   . ALA   E 2 133  ? 157.362 72.893  132.526 1.00 109.81 0  133  ALA   E C   1 
ATOM   12842 O O   . ALA   E 2 133  ? 156.520 73.171  133.390 1.00 107.47 0  133  ALA   E O   1 
ATOM   12843 C CB  . ALA   E 2 133  ? 159.229 71.338  133.155 1.00 108.80 0  133  ALA   E CB  1 
ATOM   12844 N N   . ARG   E 2 134  ? 157.833 73.803  131.671 1.00 110.47 0  134  ARG   E N   1 
ATOM   12845 C CA  . ARG   E 2 134  ? 157.306 75.162  131.670 1.00 110.06 0  134  ARG   E CA  1 
ATOM   12846 C C   . ARG   E 2 134  ? 155.819 75.170  131.337 1.00 111.67 0  134  ARG   E C   1 
ATOM   12847 O O   . ARG   E 2 134  ? 155.032 75.875  131.977 1.00 115.34 0  134  ARG   E O   1 
ATOM   12848 C CB  . ARG   E 2 134  ? 158.086 76.025  130.678 1.00 109.01 0  134  ARG   E CB  1 
ATOM   12849 C CG  . ARG   E 2 134  ? 159.448 76.474  131.180 1.00 109.02 0  134  ARG   E CG  1 
ATOM   12850 C CD  . ARG   E 2 134  ? 159.316 77.516  132.278 1.00 109.56 0  134  ARG   E CD  1 
ATOM   12851 N NE  . ARG   E 2 134  ? 160.584 78.177  132.562 1.00 111.69 0  134  ARG   E NE  1 
ATOM   12852 C CZ  . ARG   E 2 134  ? 160.999 79.289  131.971 1.00 110.76 0  134  ARG   E CZ  1 
ATOM   12853 N NH1 . ARG   E 2 134  ? 160.270 79.894  131.048 1.00 109.65 1  134  ARG   E NH1 1 
ATOM   12854 N NH2 . ARG   E 2 134  ? 162.175 79.806  132.314 1.00 109.54 0  134  ARG   E NH2 1 
ATOM   12855 N N   . LEU   E 2 135  ? 155.415 74.381  130.339 1.00 105.90 0  135  LEU   E N   1 
ATOM   12856 C CA  . LEU   E 2 135  ? 154.002 74.314  129.979 1.00 107.23 0  135  LEU   E CA  1 
ATOM   12857 C C   . LEU   E 2 135  ? 153.171 73.706  131.102 1.00 107.64 0  135  LEU   E C   1 
ATOM   12858 O O   . LEU   E 2 135  ? 152.039 74.136  131.347 1.00 107.97 0  135  LEU   E O   1 
ATOM   12859 C CB  . LEU   E 2 135  ? 153.828 73.522  128.685 1.00 106.22 0  135  LEU   E CB  1 
ATOM   12860 C CG  . LEU   E 2 135  ? 154.436 74.163  127.437 1.00 105.55 0  135  LEU   E CG  1 
ATOM   12861 C CD1 . LEU   E 2 135  ? 154.482 73.171  126.290 1.00 107.76 0  135  LEU   E CD1 1 
ATOM   12862 C CD2 . LEU   E 2 135  ? 153.656 75.401  127.039 1.00 106.28 0  135  LEU   E CD2 1 
ATOM   12863 N N   . ASP   E 2 136  ? 153.712 72.702  131.794 1.00 107.82 0  136  ASP   E N   1 
ATOM   12864 C CA  . ASP   E 2 136  ? 152.993 72.113  132.919 1.00 108.56 0  136  ASP   E CA  1 
ATOM   12865 C C   . ASP   E 2 136  ? 152.812 73.119  134.050 1.00 108.74 0  136  ASP   E C   1 
ATOM   12866 O O   . ASP   E 2 136  ? 151.730 73.207  134.645 1.00 108.03 0  136  ASP   E O   1 
ATOM   12867 C CB  . ASP   E 2 136  ? 153.727 70.869  133.415 1.00 107.35 0  136  ASP   E CB  1 
ATOM   12868 C CG  . ASP   E 2 136  ? 153.703 69.741  132.405 1.00 108.23 0  136  ASP   E CG  1 
ATOM   12869 O OD1 . ASP   E 2 136  ? 152.945 69.843  131.418 1.00 105.37 0  136  ASP   E OD1 1 
ATOM   12870 O OD2 . ASP   E 2 136  ? 154.442 68.754  132.596 1.00 109.61 -1 136  ASP   E OD2 1 
ATOM   12871 N N   . ARG   E 2 137  ? 153.858 73.888  134.362 1.00 109.29 0  137  ARG   E N   1 
ATOM   12872 C CA  . ARG   E 2 137  ? 153.726 74.920  135.386 1.00 108.17 0  137  ARG   E CA  1 
ATOM   12873 C C   . ARG   E 2 137  ? 152.736 75.994  134.955 1.00 106.87 0  137  ARG   E C   1 
ATOM   12874 O O   . ARG   E 2 137  ? 151.974 76.515  135.778 1.00 108.82 0  137  ARG   E O   1 
ATOM   12875 C CB  . ARG   E 2 137  ? 155.089 75.538  135.700 1.00 107.59 0  137  ARG   E CB  1 
ATOM   12876 C CG  . ARG   E 2 137  ? 156.127 74.545  136.200 1.00 108.39 0  137  ARG   E CG  1 
ATOM   12877 C CD  . ARG   E 2 137  ? 155.726 73.928  137.532 1.00 108.28 0  137  ARG   E CD  1 
ATOM   12878 N NE  . ARG   E 2 137  ? 154.985 72.682  137.365 1.00 111.39 0  137  ARG   E NE  1 
ATOM   12879 C CZ  . ARG   E 2 137  ? 155.532 71.519  137.040 1.00 109.41 0  137  ARG   E CZ  1 
ATOM   12880 N NH1 . ARG   E 2 137  ? 156.835 71.397  136.843 1.00 109.28 1  137  ARG   E NH1 1 
ATOM   12881 N NH2 . ARG   E 2 137  ? 154.752 70.450  136.909 1.00 107.15 0  137  ARG   E NH2 1 
ATOM   12882 N N   . ILE   E 2 138  ? 152.729 76.334  133.664 1.00 102.55 0  138  ILE   E N   1 
ATOM   12883 C CA  . ILE   E 2 138  ? 151.764 77.301  133.151 1.00 103.58 0  138  ILE   E CA  1 
ATOM   12884 C C   . ILE   E 2 138  ? 150.344 76.781  133.331 1.00 106.04 0  138  ILE   E C   1 
ATOM   12885 O O   . ILE   E 2 138  ? 149.443 77.524  133.735 1.00 107.35 0  138  ILE   E O   1 
ATOM   12886 C CB  . ILE   E 2 138  ? 152.071 77.625  131.677 1.00 101.74 0  138  ILE   E CB  1 
ATOM   12887 C CG1 . ILE   E 2 138  ? 153.265 78.575  131.580 1.00 101.80 0  138  ILE   E CG1 1 
ATOM   12888 C CG2 . ILE   E 2 138  ? 150.857 78.220  130.988 1.00 103.23 0  138  ILE   E CG2 1 
ATOM   12889 C CD1 . ILE   E 2 138  ? 153.882 78.641  130.203 1.00 103.20 0  138  ILE   E CD1 1 
ATOM   12890 N N   . ASP   E 2 139  ? 150.123 75.499  133.037 1.00 104.11 0  139  ASP   E N   1 
ATOM   12891 C CA  . ASP   E 2 139  ? 148.797 74.914  133.221 1.00 102.02 0  139  ASP   E CA  1 
ATOM   12892 C C   . ASP   E 2 139  ? 148.394 74.899  134.690 1.00 102.52 0  139  ASP   E C   1 
ATOM   12893 O O   . ASP   E 2 139  ? 147.226 75.140  135.021 1.00 103.36 0  139  ASP   E O   1 
ATOM   12894 C CB  . ASP   E 2 139  ? 148.760 73.503  132.642 1.00 102.27 0  139  ASP   E CB  1 
ATOM   12895 C CG  . ASP   E 2 139  ? 147.351 72.971  132.505 1.00 104.97 0  139  ASP   E CG  1 
ATOM   12896 O OD1 . ASP   E 2 139  ? 146.589 73.518  131.681 1.00 106.92 0  139  ASP   E OD1 1 
ATOM   12897 O OD2 . ASP   E 2 139  ? 147.005 72.008  133.220 1.00 104.73 -1 139  ASP   E OD2 1 
ATOM   12898 N N   . GLU   E 2 140  ? 149.340 74.606  135.585 1.00 104.11 0  140  GLU   E N   1 
ATOM   12899 C CA  . GLU   E 2 140  ? 149.039 74.666  137.014 1.00 105.80 0  140  GLU   E CA  1 
ATOM   12900 C C   . GLU   E 2 140  ? 148.645 76.079  137.431 1.00 106.35 0  140  GLU   E C   1 
ATOM   12901 O O   . GLU   E 2 140  ? 147.690 76.271  138.197 1.00 105.29 0  140  GLU   E O   1 
ATOM   12902 C CB  . GLU   E 2 140  ? 150.240 74.186  137.829 1.00 105.95 0  140  GLU   E CB  1 
ATOM   12903 C CG  . GLU   E 2 140  ? 150.571 72.714  137.655 1.00 106.17 0  140  GLU   E CG  1 
ATOM   12904 C CD  . GLU   E 2 140  ? 151.788 72.297  138.458 1.00 105.97 0  140  GLU   E CD  1 
ATOM   12905 O OE1 . GLU   E 2 140  ? 152.359 73.156  139.161 1.00 103.65 0  140  GLU   E OE1 1 
ATOM   12906 O OE2 . GLU   E 2 140  ? 152.174 71.111  138.384 1.00 106.84 -1 140  GLU   E OE2 1 
ATOM   12907 N N   . LYS   E 2 141  ? 149.370 77.081  136.930 1.00 100.62 0  141  LYS   E N   1 
ATOM   12908 C CA  . LYS   E 2 141  ? 149.034 78.466  137.239 1.00 97.79  0  141  LYS   E CA  1 
ATOM   12909 C C   . LYS   E 2 141  ? 147.659 78.833  136.698 1.00 99.57  0  141  LYS   E C   1 
ATOM   12910 O O   . LYS   E 2 141  ? 146.900 79.552  137.353 1.00 103.05 0  141  LYS   E O   1 
ATOM   12911 C CB  . LYS   E 2 141  ? 150.099 79.405  136.676 1.00 96.78  0  141  LYS   E CB  1 
ATOM   12912 C CG  . LYS   E 2 141  ? 151.363 79.476  137.511 1.00 99.16  0  141  LYS   E CG  1 
ATOM   12913 C CD  . LYS   E 2 141  ? 152.382 80.406  136.879 1.00 100.51 0  141  LYS   E CD  1 
ATOM   12914 C CE  . LYS   E 2 141  ? 153.643 80.500  137.720 1.00 100.30 0  141  LYS   E CE  1 
ATOM   12915 N NZ  . LYS   E 2 141  ? 154.635 81.431  137.119 1.00 98.75  1  141  LYS   E NZ  1 
ATOM   12916 N N   . LEU   E 2 142  ? 147.322 78.357  135.499 1.00 98.43  0  142  LEU   E N   1 
ATOM   12917 C CA  . LEU   E 2 142  ? 146.012 78.656  134.929 1.00 98.58  0  142  LEU   E CA  1 
ATOM   12918 C C   . LEU   E 2 142  ? 144.897 77.996  135.729 1.00 99.64  0  142  LEU   E C   1 
ATOM   12919 O O   . LEU   E 2 142  ? 143.815 78.571  135.891 1.00 102.27 0  142  LEU   E O   1 
ATOM   12920 C CB  . LEU   E 2 142  ? 145.958 78.216  133.471 1.00 97.56  0  142  LEU   E CB  1 
ATOM   12921 C CG  . LEU   E 2 142  ? 146.911 78.972  132.554 1.00 98.51  0  142  LEU   E CG  1 
ATOM   12922 C CD1 . LEU   E 2 142  ? 147.022 78.268  131.217 1.00 100.19 0  142  LEU   E CD1 1 
ATOM   12923 C CD2 . LEU   E 2 142  ? 146.452 80.405  132.385 1.00 98.16  0  142  LEU   E CD2 1 
ATOM   12924 N N   . SER   E 2 143  ? 145.133 76.780  136.223 1.00 102.17 0  143  SER   E N   1 
ATOM   12925 C CA  . SER   E 2 143  ? 144.154 76.148  137.101 1.00 102.57 0  143  SER   E CA  1 
ATOM   12926 C C   . SER   E 2 143  ? 143.979 76.949  138.387 1.00 103.01 0  143  SER   E C   1 
ATOM   12927 O O   . SER   E 2 143  ? 142.852 77.145  138.862 1.00 101.09 0  143  SER   E O   1 
ATOM   12928 C CB  . SER   E 2 143  ? 144.575 74.712  137.410 1.00 103.23 0  143  SER   E CB  1 
ATOM   12929 O OG  . SER   E 2 143  ? 143.577 74.038  138.156 1.00 102.53 0  143  SER   E OG  1 
ATOM   12930 N N   . GLU   E 2 144  ? 145.089 77.426  138.959 1.00 102.03 0  144  GLU   E N   1 
ATOM   12931 C CA  . GLU   E 2 144  ? 144.997 78.278  140.141 1.00 101.99 0  144  GLU   E CA  1 
ATOM   12932 C C   . GLU   E 2 144  ? 144.224 79.554  139.839 1.00 103.23 0  144  GLU   E C   1 
ATOM   12933 O O   . GLU   E 2 144  ? 143.460 80.038  140.678 1.00 104.42 0  144  GLU   E O   1 
ATOM   12934 C CB  . GLU   E 2 144  ? 146.392 78.613  140.668 1.00 101.44 0  144  GLU   E CB  1 
ATOM   12935 C CG  . GLU   E 2 144  ? 147.019 77.516  141.509 1.00 103.12 0  144  GLU   E CG  1 
ATOM   12936 C CD  . GLU   E 2 144  ? 148.022 78.053  142.511 1.00 105.40 0  144  GLU   E CD  1 
ATOM   12937 O OE1 . GLU   E 2 144  ? 148.225 79.285  142.547 1.00 103.74 0  144  GLU   E OE1 1 
ATOM   12938 O OE2 . GLU   E 2 144  ? 148.606 77.244  143.262 1.00 105.23 -1 144  GLU   E OE2 1 
ATOM   12939 N N   . ILE   E 2 145  ? 144.419 80.116  138.646 1.00 98.20  0  145  ILE   E N   1 
ATOM   12940 C CA  . ILE   E 2 145  ? 143.718 81.336  138.259 1.00 94.93  0  145  ILE   E CA  1 
ATOM   12941 C C   . ILE   E 2 145  ? 142.224 81.077  138.109 1.00 97.21  0  145  ILE   E C   1 
ATOM   12942 O O   . ILE   E 2 145  ? 141.395 81.894  138.526 1.00 101.12 0  145  ILE   E O   1 
ATOM   12943 C CB  . ILE   E 2 145  ? 144.335 81.906  136.969 1.00 95.00  0  145  ILE   E CB  1 
ATOM   12944 C CG1 . ILE   E 2 145  ? 145.700 82.524  137.272 1.00 97.07  0  145  ILE   E CG1 1 
ATOM   12945 C CG2 . ILE   E 2 145  ? 143.415 82.928  136.330 1.00 96.07  0  145  ILE   E CG2 1 
ATOM   12946 C CD1 . ILE   E 2 145  ? 146.616 82.591  136.078 1.00 95.58  0  145  ILE   E CD1 1 
ATOM   12947 N N   . LEU   E 2 146  ? 141.854 79.945  137.505 1.00 96.28  0  146  LEU   E N   1 
ATOM   12948 C CA  . LEU   E 2 146  ? 140.443 79.576  137.421 1.00 95.01  0  146  LEU   E CA  1 
ATOM   12949 C C   . LEU   E 2 146  ? 139.827 79.445  138.806 1.00 96.10  0  146  LEU   E C   1 
ATOM   12950 O O   . LEU   E 2 146  ? 138.725 79.954  139.058 1.00 98.09  0  146  LEU   E O   1 
ATOM   12951 C CB  . LEU   E 2 146  ? 140.283 78.270  136.644 1.00 96.22  0  146  LEU   E CB  1 
ATOM   12952 C CG  . LEU   E 2 146  ? 140.295 78.338  135.118 1.00 98.08  0  146  LEU   E CG  1 
ATOM   12953 C CD1 . LEU   E 2 146  ? 140.551 76.967  134.523 1.00 96.36  0  146  LEU   E CD1 1 
ATOM   12954 C CD2 . LEU   E 2 146  ? 138.960 78.871  134.635 1.00 96.11  0  146  LEU   E CD2 1 
ATOM   12955 N N   . GLY   E 2 147  ? 140.523 78.766  139.718 1.00 96.68  0  147  GLY   E N   1 
ATOM   12956 C CA  . GLY   E 2 147  ? 140.015 78.653  141.076 1.00 98.44  0  147  GLY   E CA  1 
ATOM   12957 C C   . GLY   E 2 147  ? 139.876 80.004  141.750 1.00 99.07  0  147  GLY   E C   1 
ATOM   12958 O O   . GLY   E 2 147  ? 138.866 80.289  142.399 1.00 97.56  0  147  GLY   E O   1 
ATOM   12959 N N   . MET   E 2 148  ? 140.888 80.859  141.588 1.00 103.50 0  148  MET   E N   1 
ATOM   12960 C CA  . MET   E 2 148  ? 140.860 82.188  142.187 1.00 101.62 0  148  MET   E CA  1 
ATOM   12961 C C   . MET   E 2 148  ? 139.672 82.987  141.681 1.00 101.71 0  148  MET   E C   1 
ATOM   12962 O O   . MET   E 2 148  ? 138.957 83.620  142.464 1.00 104.07 0  148  MET   E O   1 
ATOM   12963 C CB  . MET   E 2 148  ? 142.160 82.929  141.868 1.00 102.80 0  148  MET   E CB  1 
ATOM   12964 C CG  . MET   E 2 148  ? 143.258 82.917  142.935 1.00 102.79 0  148  MET   E CG  1 
ATOM   12965 S SD  . MET   E 2 148  ? 142.784 83.332  144.625 1.00 107.20 0  148  MET   E SD  1 
ATOM   12966 C CE  . MET   E 2 148  ? 142.306 81.730  145.259 1.00 101.43 0  148  MET   E CE  1 
ATOM   12967 N N   . LEU   E 2 149  ? 139.441 82.959  140.369 1.00 98.16  0  149  LEU   E N   1 
ATOM   12968 C CA  . LEU   E 2 149  ? 138.364 83.739  139.773 1.00 96.32  0  149  LEU   E CA  1 
ATOM   12969 C C   . LEU   E 2 149  ? 136.998 83.222  140.208 1.00 98.56  0  149  LEU   E C   1 
ATOM   12970 O O   . LEU   E 2 149  ? 136.095 84.010  140.520 1.00 102.40 0  149  LEU   E O   1 
ATOM   12971 C CB  . LEU   E 2 149  ? 138.502 83.715  138.255 1.00 94.83  0  149  LEU   E CB  1 
ATOM   12972 C CG  . LEU   E 2 149  ? 139.541 84.694  137.709 1.00 99.13  0  149  LEU   E CG  1 
ATOM   12973 C CD1 . LEU   E 2 149  ? 139.936 84.344  136.284 1.00 101.59 0  149  LEU   E CD1 1 
ATOM   12974 C CD2 . LEU   E 2 149  ? 139.009 86.114  137.780 1.00 99.06  0  149  LEU   E CD2 1 
ATOM   12975 N N   . HIS   E 2 150  ? 136.824 81.899  140.235 1.00 102.29 0  150  HIS   E N   1 
ATOM   12976 C CA  . HIS   E 2 150  ? 135.541 81.353  140.666 1.00 103.01 0  150  HIS   E CA  1 
ATOM   12977 C C   . HIS   E 2 150  ? 135.273 81.666  142.134 1.00 104.33 0  150  HIS   E C   1 
ATOM   12978 O O   . HIS   E 2 150  ? 134.145 82.019  142.503 1.00 103.27 0  150  HIS   E O   1 
ATOM   12979 C CB  . HIS   E 2 150  ? 135.493 79.849  140.406 1.00 101.57 0  150  HIS   E CB  1 
ATOM   12980 C CG  . HIS   E 2 150  ? 135.010 79.495  139.035 1.00 103.19 0  150  HIS   E CG  1 
ATOM   12981 N ND1 . HIS   E 2 150  ? 133.763 79.853  138.570 1.00 102.57 0  150  HIS   E ND1 1 
ATOM   12982 C CD2 . HIS   E 2 150  ? 135.607 78.820  138.024 1.00 105.26 0  150  HIS   E CD2 1 
ATOM   12983 C CE1 . HIS   E 2 150  ? 133.612 79.413  137.334 1.00 104.41 0  150  HIS   E CE1 1 
ATOM   12984 N NE2 . HIS   E 2 150  ? 134.716 78.782  136.979 1.00 105.51 0  150  HIS   E NE2 1 
ATOM   12985 N N   . THR   E 2 151  ? 136.297 81.559  142.986 1.00 108.02 0  151  THR   E N   1 
ATOM   12986 C CA  . THR   E 2 151  ? 136.121 81.918  144.389 1.00 107.12 0  151  THR   E CA  1 
ATOM   12987 C C   . THR   E 2 151  ? 135.817 83.402  144.546 1.00 106.93 0  151  THR   E C   1 
ATOM   12988 O O   . THR   E 2 151  ? 135.015 83.788  145.403 1.00 107.35 0  151  THR   E O   1 
ATOM   12989 C CB  . THR   E 2 151  ? 137.359 81.533  145.200 1.00 108.13 0  151  THR   E CB  1 
ATOM   12990 O OG1 . THR   E 2 151  ? 138.516 82.176  144.651 1.00 106.93 0  151  THR   E OG1 1 
ATOM   12991 C CG2 . THR   E 2 151  ? 137.554 80.022  145.209 1.00 107.41 0  151  THR   E CG2 1 
ATOM   12992 N N   . LEU   E 2 152  ? 136.445 84.249  143.729 1.00 104.58 0  152  LEU   E N   1 
ATOM   12993 C CA  . LEU   E 2 152  ? 136.157 85.679  143.777 1.00 102.69 0  152  LEU   E CA  1 
ATOM   12994 C C   . LEU   E 2 152  ? 134.703 85.956  143.424 1.00 102.28 0  152  LEU   E C   1 
ATOM   12995 O O   . LEU   E 2 152  ? 134.024 86.736  144.102 1.00 104.27 0  152  LEU   E O   1 
ATOM   12996 C CB  . LEU   E 2 152  ? 137.088 86.432  142.827 1.00 102.40 0  152  LEU   E CB  1 
ATOM   12997 C CG  . LEU   E 2 152  ? 136.710 87.881  142.510 1.00 101.43 0  152  LEU   E CG  1 
ATOM   12998 C CD1 . LEU   E 2 152  ? 137.130 88.810  143.637 1.00 102.56 0  152  LEU   E CD1 1 
ATOM   12999 C CD2 . LEU   E 2 152  ? 137.313 88.318  141.188 1.00 98.91  0  152  LEU   E CD2 1 
ATOM   13000 N N   . VAL   E 2 153  ? 134.209 85.325  142.356 1.00 106.09 0  153  VAL   E N   1 
ATOM   13001 C CA  . VAL   E 2 153  ? 132.822 85.538  141.947 1.00 107.89 0  153  VAL   E CA  1 
ATOM   13002 C C   . VAL   E 2 153  ? 131.867 85.047  143.028 1.00 110.59 0  153  VAL   E C   1 
ATOM   13003 O O   . VAL   E 2 153  ? 130.879 85.716  143.357 1.00 109.42 0  153  VAL   E O   1 
ATOM   13004 C CB  . VAL   E 2 153  ? 132.554 84.857  140.592 1.00 107.63 0  153  VAL   E CB  1 
ATOM   13005 C CG1 . VAL   E 2 153  ? 131.093 84.461  140.469 1.00 107.32 0  153  VAL   E CG1 1 
ATOM   13006 C CG2 . VAL   E 2 153  ? 132.950 85.779  139.456 1.00 107.10 0  153  VAL   E CG2 1 
ATOM   13007 N N   . VAL   E 2 154  ? 132.153 83.879  143.610 1.00 118.88 0  154  VAL   E N   1 
ATOM   13008 C CA  . VAL   E 2 154  ? 131.297 83.343  144.666 1.00 117.63 0  154  VAL   E CA  1 
ATOM   13009 C C   . VAL   E 2 154  ? 131.288 84.274  145.874 1.00 117.70 0  154  VAL   E C   1 
ATOM   13010 O O   . VAL   E 2 154  ? 130.233 84.533  146.468 1.00 116.41 0  154  VAL   E O   1 
ATOM   13011 C CB  . VAL   E 2 154  ? 131.749 81.921  145.047 1.00 116.92 0  154  VAL   E CB  1 
ATOM   13012 C CG1 . VAL   E 2 154  ? 131.204 81.533  146.411 1.00 117.43 0  154  VAL   E CG1 1 
ATOM   13013 C CG2 . VAL   E 2 154  ? 131.304 80.925  143.986 1.00 115.79 0  154  VAL   E CG2 1 
ATOM   13014 N N   . ALA   E 2 155  ? 132.458 84.790  146.258 1.00 123.01 0  155  ALA   E N   1 
ATOM   13015 C CA  . ALA   E 2 155  ? 132.534 85.692  147.402 1.00 122.66 0  155  ALA   E CA  1 
ATOM   13016 C C   . ALA   E 2 155  ? 131.785 86.991  147.139 1.00 122.77 0  155  ALA   E C   1 
ATOM   13017 O O   . ALA   E 2 155  ? 131.080 87.496  148.021 1.00 124.32 0  155  ALA   E O   1 
ATOM   13018 C CB  . ALA   E 2 155  ? 133.994 85.977  147.751 1.00 122.29 0  155  ALA   E CB  1 
ATOM   13019 N N   . SER   E 2 156  ? 131.924 87.549  145.936 1.00 116.83 0  156  SER   E N   1 
ATOM   13020 C CA  . SER   E 2 156  ? 131.236 88.786  145.593 1.00 116.98 0  156  SER   E CA  1 
ATOM   13021 C C   . SER   E 2 156  ? 129.756 88.581  145.299 1.00 116.92 0  156  SER   E C   1 
ATOM   13022 O O   . SER   E 2 156  ? 129.030 89.569  145.149 1.00 114.54 0  156  SER   E O   1 
ATOM   13023 C CB  . SER   E 2 156  ? 131.909 89.449  144.391 1.00 115.09 0  156  SER   E CB  1 
ATOM   13024 O OG  . SER   E 2 156  ? 133.089 90.132  144.778 1.00 112.73 0  156  SER   E OG  1 
ATOM   13025 N N   . ALA   E 2 157  ? 129.298 87.330  145.203 1.00 128.88 0  157  ALA   E N   1 
ATOM   13026 C CA  . ALA   E 2 157  ? 127.873 87.081  145.020 1.00 128.67 0  157  ALA   E CA  1 
ATOM   13027 C C   . ALA   E 2 157  ? 127.064 87.626  146.190 1.00 128.60 0  157  ALA   E C   1 
ATOM   13028 O O   . ALA   E 2 157  ? 126.001 88.226  145.995 1.00 127.75 0  157  ALA   E O   1 
ATOM   13029 C CB  . ALA   E 2 157  ? 127.621 85.584  144.844 1.00 127.00 0  157  ALA   E CB  1 
ATOM   13030 N N   . GLY   E 2 158  ? 127.552 87.433  147.412 1.00 144.99 0  158  GLY   E N   1 
ATOM   13031 C CA  . GLY   E 2 158  ? 126.883 87.935  148.586 1.00 145.81 0  158  GLY   E CA  1 
ATOM   13032 C C   . GLY   E 2 158  ? 126.334 86.827  149.460 1.00 146.96 0  158  GLY   E C   1 
ATOM   13033 O O   . GLY   E 2 158  ? 126.432 85.640  149.136 1.00 146.32 0  158  GLY   E O   1 
ATOM   13034 N N   . PRO   E 2 159  ? 125.740 87.197  150.587 1.00 159.90 0  159  PRO   E N   1 
ATOM   13035 C CA  . PRO   E 2 159  ? 125.206 86.205  151.524 1.00 160.06 0  159  PRO   E CA  1 
ATOM   13036 C C   . PRO   E 2 159  ? 123.883 85.635  151.022 1.00 159.70 0  159  PRO   E C   1 
ATOM   13037 O O   . PRO   E 2 159  ? 123.404 85.963  149.938 1.00 159.91 0  159  PRO   E O   1 
ATOM   13038 C CB  . PRO   E 2 159  ? 125.020 87.010  152.811 1.00 159.93 0  159  PRO   E CB  1 
ATOM   13039 C CG  . PRO   E 2 159  ? 124.757 88.398  152.337 1.00 159.36 0  159  PRO   E CG  1 
ATOM   13040 C CD  . PRO   E 2 159  ? 125.566 88.576  151.079 1.00 159.02 0  159  PRO   E CD  1 
ATOM   13041 N N   . THR   E 2 160  ? 123.313 84.741  151.835 1.00 162.07 0  160  THR   E N   1 
ATOM   13042 C CA  . THR   E 2 160  ? 122.014 84.111  151.604 1.00 162.51 0  160  THR   E CA  1 
ATOM   13043 C C   . THR   E 2 160  ? 122.017 83.210  150.373 1.00 162.72 0  160  THR   E C   1 
ATOM   13044 O O   . THR   E 2 160  ? 120.999 82.584  150.057 1.00 162.39 0  160  THR   E O   1 
ATOM   13045 C CB  . THR   E 2 160  ? 120.899 85.160  151.481 1.00 162.12 0  160  THR   E CB  1 
ATOM   13046 O OG1 . THR   E 2 160  ? 121.036 85.876  150.246 1.00 162.29 0  160  THR   E OG1 1 
ATOM   13047 C CG2 . THR   E 2 160  ? 120.948 86.142  152.646 1.00 161.06 0  160  THR   E CG2 1 
ATOM   13048 N N   . SER   E 2 161  ? 123.148 83.129  149.671 1.00 158.36 0  161  SER   E N   1 
ATOM   13049 C CA  . SER   E 2 161  ? 123.273 82.256  148.509 1.00 157.38 0  161  SER   E CA  1 
ATOM   13050 C C   . SER   E 2 161  ? 124.305 81.160  148.733 1.00 158.29 0  161  SER   E C   1 
ATOM   13051 O O   . SER   E 2 161  ? 123.976 79.976  148.607 1.00 158.14 0  161  SER   E O   1 
ATOM   13052 C CB  . SER   E 2 161  ? 123.625 83.084  147.267 1.00 157.11 0  161  SER   E CB  1 
ATOM   13053 O OG  . SER   E 2 161  ? 123.692 82.264  146.114 1.00 158.22 0  161  SER   E OG  1 
ATOM   13054 N N   . ALA   E 2 162  ? 125.543 81.517  149.060 1.00 158.27 0  162  ALA   E N   1 
ATOM   13055 C CA  . ALA   E 2 162  ? 126.600 80.547  149.330 1.00 157.99 0  162  ALA   E CA  1 
ATOM   13056 C C   . ALA   E 2 162  ? 127.422 81.007  150.527 1.00 157.65 0  162  ALA   E C   1 
ATOM   13057 O O   . ALA   E 2 162  ? 128.653 80.959  150.527 1.00 156.59 0  162  ALA   E O   1 
ATOM   13058 C CB  . ALA   E 2 162  ? 127.482 80.336  148.101 1.00 156.71 0  162  ALA   E CB  1 
ATOM   13059 N N   . ARG   E 2 163  ? 126.734 81.469  151.570 1.00 155.49 0  163  ARG   E N   1 
ATOM   13060 C CA  . ARG   E 2 163  ? 127.389 81.977  152.772 1.00 155.19 0  163  ARG   E CA  1 
ATOM   13061 C C   . ARG   E 2 163  ? 126.674 81.413  153.993 1.00 155.38 0  163  ARG   E C   1 
ATOM   13062 O O   . ARG   E 2 163  ? 125.505 81.733  154.233 1.00 154.27 0  163  ARG   E O   1 
ATOM   13063 C CB  . ARG   E 2 163  ? 127.384 83.506  152.798 1.00 154.59 0  163  ARG   E CB  1 
ATOM   13064 C CG  . ARG   E 2 163  ? 128.486 84.114  153.645 1.00 154.54 0  163  ARG   E CG  1 
ATOM   13065 C CD  . ARG   E 2 163  ? 129.820 84.081  152.924 1.00 154.07 0  163  ARG   E CD  1 
ATOM   13066 N NE  . ARG   E 2 163  ? 129.919 85.141  151.929 1.00 154.01 0  163  ARG   E NE  1 
ATOM   13067 C CZ  . ARG   E 2 163  ? 130.903 85.256  151.048 1.00 153.97 0  163  ARG   E CZ  1 
ATOM   13068 N NH1 . ARG   E 2 163  ? 131.895 84.382  151.001 1.00 154.27 1  163  ARG   E NH1 1 
ATOM   13069 N NH2 . ARG   E 2 163  ? 130.894 86.277  150.195 1.00 152.85 0  163  ARG   E NH2 1 
ATOM   13070 N N   . ASP   E 2 164  ? 127.372 80.575  154.760 1.00 162.84 0  164  ASP   E N   1 
ATOM   13071 C CA  . ASP   E 2 164  ? 126.882 80.109  156.055 1.00 162.76 0  164  ASP   E CA  1 
ATOM   13072 C C   . ASP   E 2 164  ? 127.503 80.903  157.199 1.00 162.47 0  164  ASP   E C   1 
ATOM   13073 O O   . ASP   E 2 164  ? 126.787 81.454  158.039 1.00 161.86 0  164  ASP   E O   1 
ATOM   13074 C CB  . ASP   E 2 164  ? 127.163 78.609  156.227 1.00 162.70 0  164  ASP   E CB  1 
ATOM   13075 C CG  . ASP   E 2 164  ? 126.111 77.740  155.568 1.00 162.27 0  164  ASP   E CG  1 
ATOM   13076 O OD1 . ASP   E 2 164  ? 124.949 77.763  156.025 1.00 162.11 0  164  ASP   E OD1 1 
ATOM   13077 O OD2 . ASP   E 2 164  ? 126.445 77.033  154.594 1.00 161.86 -1 164  ASP   E OD2 1 
ATOM   13078 N N   . GLY   E 2 165  ? 128.832 80.975  157.241 1.00 163.60 0  165  GLY   E N   1 
ATOM   13079 C CA  . GLY   E 2 165  ? 129.516 81.793  158.216 1.00 163.64 0  165  GLY   E CA  1 
ATOM   13080 C C   . GLY   E 2 165  ? 129.521 83.255  157.817 1.00 163.80 0  165  GLY   E C   1 
ATOM   13081 O O   . GLY   E 2 165  ? 128.934 83.667  156.817 1.00 163.84 0  165  GLY   E O   1 
ATOM   13082 N N   . ILE   E 2 166  ? 130.204 84.057  158.627 1.00 161.56 0  166  ILE   E N   1 
ATOM   13083 C CA  . ILE   E 2 166  ? 130.291 85.506  158.378 1.00 161.04 0  166  ILE   E CA  1 
ATOM   13084 C C   . ILE   E 2 166  ? 131.506 85.711  157.482 1.00 161.84 0  166  ILE   E C   1 
ATOM   13085 O O   . ILE   E 2 166  ? 132.613 86.028  157.924 1.00 161.80 0  166  ILE   E O   1 
ATOM   13086 C CB  . ILE   E 2 166  ? 130.365 86.315  159.676 1.00 160.56 0  166  ILE   E CB  1 
ATOM   13087 C CG1 . ILE   E 2 166  ? 129.212 85.941  160.608 1.00 160.12 0  166  ILE   E CG1 1 
ATOM   13088 C CG2 . ILE   E 2 166  ? 130.334 87.804  159.374 1.00 160.28 0  166  ILE   E CG2 1 
ATOM   13089 C CD1 . ILE   E 2 166  ? 129.332 86.538  161.993 1.00 160.03 0  166  ILE   E CD1 1 
ATOM   13090 N N   . ARG   E 2 167  ? 131.287 85.528  156.177 1.00 159.49 0  167  ARG   E N   1 
ATOM   13091 C CA  . ARG   E 2 167  ? 132.269 85.826  155.132 1.00 158.49 0  167  ARG   E CA  1 
ATOM   13092 C C   . ARG   E 2 167  ? 133.594 85.105  155.404 1.00 158.55 0  167  ARG   E C   1 
ATOM   13093 O O   . ARG   E 2 167  ? 134.634 85.714  155.665 1.00 157.95 0  167  ARG   E O   1 
ATOM   13094 C CB  . ARG   E 2 167  ? 132.471 87.340  154.991 1.00 158.20 0  167  ARG   E CB  1 
ATOM   13095 C CG  . ARG   E 2 167  ? 131.198 88.159  155.170 1.00 158.09 0  167  ARG   E CG  1 
ATOM   13096 C CD  . ARG   E 2 167  ? 130.126 87.756  154.173 1.00 158.58 0  167  ARG   E CD  1 
ATOM   13097 N NE  . ARG   E 2 167  ? 128.942 88.600  154.278 1.00 158.13 0  167  ARG   E NE  1 
ATOM   13098 C CZ  . ARG   E 2 167  ? 127.879 88.307  155.014 1.00 157.89 0  167  ARG   E CZ  1 
ATOM   13099 N NH1 . ARG   E 2 167  ? 127.814 87.193  155.723 1.00 158.18 1  167  ARG   E NH1 1 
ATOM   13100 N NH2 . ARG   E 2 167  ? 126.853 89.155  155.039 1.00 157.57 0  167  ARG   E NH2 1 
ATOM   13101 N N   . ASP   E 2 168  ? 133.514 83.777  155.349 1.00 158.46 0  168  ASP   E N   1 
ATOM   13102 C CA  . ASP   E 2 168  ? 134.665 82.936  155.653 1.00 158.75 0  168  ASP   E CA  1 
ATOM   13103 C C   . ASP   E 2 168  ? 135.832 83.245  154.723 1.00 157.61 0  168  ASP   E C   1 
ATOM   13104 O O   . ASP   E 2 168  ? 135.660 83.401  153.510 1.00 157.01 0  168  ASP   E O   1 
ATOM   13105 C CB  . ASP   E 2 168  ? 134.283 81.459  155.528 1.00 158.03 0  168  ASP   E CB  1 
ATOM   13106 C CG  . ASP   E 2 168  ? 133.113 81.080  156.415 1.00 157.36 0  168  ASP   E CG  1 
ATOM   13107 O OD1 . ASP   E 2 168  ? 133.061 81.549  157.570 1.00 157.22 0  168  ASP   E OD1 1 
ATOM   13108 O OD2 . ASP   E 2 168  ? 132.243 80.311  155.953 1.00 156.76 -1 168  ASP   E OD2 1 
ATOM   13109 N N   . ALA   E 2 169  ? 137.028 83.337  155.300 1.00 152.45 0  169  ALA   E N   1 
ATOM   13110 C CA  . ALA   E 2 169  ? 138.242 83.481  154.509 1.00 152.50 0  169  ALA   E CA  1 
ATOM   13111 C C   . ALA   E 2 169  ? 138.531 82.169  153.790 1.00 153.38 0  169  ALA   E C   1 
ATOM   13112 O O   . ALA   E 2 169  ? 138.569 81.104  154.414 1.00 153.64 0  169  ALA   E O   1 
ATOM   13113 C CB  . ALA   E 2 169  ? 139.420 83.878  155.397 1.00 151.87 0  169  ALA   E CB  1 
ATOM   13114 N N   . MET   E 2 170  ? 138.736 82.248  152.478 1.00 151.24 0  170  MET   E N   1 
ATOM   13115 C CA  . MET   E 2 170  ? 138.778 81.046  151.655 1.00 150.46 0  170  MET   E CA  1 
ATOM   13116 C C   . MET   E 2 170  ? 140.189 80.470  151.555 1.00 150.37 0  170  MET   E C   1 
ATOM   13117 O O   . MET   E 2 170  ? 140.340 79.246  151.460 1.00 151.62 0  170  MET   E O   1 
ATOM   13118 C CB  . MET   E 2 170  ? 138.129 81.372  150.295 1.00 150.19 0  170  MET   E CB  1 
ATOM   13119 C CG  . MET   E 2 170  ? 137.989 80.280  149.218 1.00 149.72 0  170  MET   E CG  1 
ATOM   13120 S SD  . MET   E 2 170  ? 139.408 79.362  148.623 1.00 153.19 0  170  MET   E SD  1 
ATOM   13121 C CE  . MET   E 2 170  ? 140.312 80.727  147.920 1.00 150.13 0  170  MET   E CE  1 
ATOM   13122 N N   . ILE   E 2 171  ? 141.227 81.305  151.638 1.00 144.24 0  171  ILE   E N   1 
ATOM   13123 C CA  . ILE   E 2 171  ? 142.589 80.818  151.855 1.00 144.51 0  171  ILE   E CA  1 
ATOM   13124 C C   . ILE   E 2 171  ? 143.150 81.412  153.142 1.00 144.80 0  171  ILE   E C   1 
ATOM   13125 O O   . ILE   E 2 171  ? 143.562 80.680  154.048 1.00 144.45 0  171  ILE   E O   1 
ATOM   13126 C CB  . ILE   E 2 171  ? 143.519 81.131  150.668 1.00 144.39 0  171  ILE   E CB  1 
ATOM   13127 C CG1 . ILE   E 2 171  ? 143.240 80.190  149.499 1.00 144.39 0  171  ILE   E CG1 1 
ATOM   13128 C CG2 . ILE   E 2 171  ? 144.974 81.015  151.088 1.00 143.96 0  171  ILE   E CG2 1 
ATOM   13129 C CD1 . ILE   E 2 171  ? 143.433 78.725  149.828 1.00 143.91 0  171  ILE   E CD1 1 
ATOM   13130 N N   . GLY   E 2 172  ? 143.175 82.739  153.228 1.00 143.69 0  172  GLY   E N   1 
ATOM   13131 C CA  . GLY   E 2 172  ? 143.701 83.438  154.389 1.00 142.86 0  172  GLY   E CA  1 
ATOM   13132 C C   . GLY   E 2 172  ? 145.021 84.146  154.167 1.00 142.71 0  172  GLY   E C   1 
ATOM   13133 O O   . GLY   E 2 172  ? 145.493 84.839  155.081 1.00 140.83 0  172  GLY   E O   1 
ATOM   13134 N N   . LEU   E 2 173  ? 145.644 84.011  152.999 1.00 139.40 0  173  LEU   E N   1 
ATOM   13135 C CA  . LEU   E 2 173  ? 146.914 84.668  152.710 1.00 137.06 0  173  LEU   E CA  1 
ATOM   13136 C C   . LEU   E 2 173  ? 146.633 86.068  152.179 1.00 137.12 0  173  LEU   E C   1 
ATOM   13137 O O   . LEU   E 2 173  ? 146.273 86.236  151.009 1.00 135.49 0  173  LEU   E O   1 
ATOM   13138 C CB  . LEU   E 2 173  ? 147.727 83.857  151.704 1.00 136.38 0  173  LEU   E CB  1 
ATOM   13139 C CG  . LEU   E 2 173  ? 148.227 82.480  152.145 1.00 135.74 0  173  LEU   E CG  1 
ATOM   13140 C CD1 . LEU   E 2 173  ? 148.687 81.669  150.942 1.00 135.64 0  173  LEU   E CD1 1 
ATOM   13141 C CD2 . LEU   E 2 173  ? 149.348 82.613  153.164 1.00 135.98 0  173  LEU   E CD2 1 
ATOM   13142 N N   . ARG   E 2 174  ? 146.792 87.074  153.038 1.00 140.60 0  174  ARG   E N   1 
ATOM   13143 C CA  . ARG   E 2 174  ? 146.668 88.468  152.636 1.00 140.01 0  174  ARG   E CA  1 
ATOM   13144 C C   . ARG   E 2 174  ? 148.017 89.157  152.492 1.00 138.56 0  174  ARG   E C   1 
ATOM   13145 O O   . ARG   E 2 174  ? 148.057 90.352  152.184 1.00 137.06 0  174  ARG   E O   1 
ATOM   13146 C CB  . ARG   E 2 174  ? 145.797 89.238  153.635 1.00 136.83 0  174  ARG   E CB  1 
ATOM   13147 C CG  . ARG   E 2 174  ? 146.425 89.420  155.005 1.00 137.17 0  174  ARG   E CG  1 
ATOM   13148 C CD  . ARG   E 2 174  ? 145.624 90.395  155.853 1.00 138.91 0  174  ARG   E CD  1 
ATOM   13149 N NE  . ARG   E 2 174  ? 146.237 90.627  157.155 1.00 139.06 0  174  ARG   E NE  1 
ATOM   13150 C CZ  . ARG   E 2 174  ? 145.811 90.090  158.291 1.00 138.28 0  174  ARG   E CZ  1 
ATOM   13151 N NH1 . ARG   E 2 174  ? 144.764 89.282  158.324 1.00 137.79 1  174  ARG   E NH1 1 
ATOM   13152 N NH2 . ARG   E 2 174  ? 146.451 90.372  159.422 1.00 137.57 0  174  ARG   E NH2 1 
ATOM   13153 N N   . GLU   E 2 175  ? 149.119 88.439  152.707 1.00 139.27 0  175  GLU   E N   1 
ATOM   13154 C CA  . GLU   E 2 175  ? 150.449 89.018  152.579 1.00 139.40 0  175  GLU   E CA  1 
ATOM   13155 C C   . GLU   E 2 175  ? 150.988 88.961  151.156 1.00 140.10 0  175  GLU   E C   1 
ATOM   13156 O O   . GLU   E 2 175  ? 152.054 89.530  150.895 1.00 139.59 0  175  GLU   E O   1 
ATOM   13157 C CB  . GLU   E 2 175  ? 151.421 88.314  153.529 1.00 139.68 0  175  GLU   E CB  1 
ATOM   13158 C CG  . GLU   E 2 175  ? 151.226 88.678  154.995 1.00 139.66 0  175  GLU   E CG  1 
ATOM   13159 C CD  . GLU   E 2 175  ? 150.176 87.823  155.680 1.00 140.65 0  175  GLU   E CD  1 
ATOM   13160 O OE1 . GLU   E 2 175  ? 149.733 86.824  155.077 1.00 140.65 0  175  GLU   E OE1 1 
ATOM   13161 O OE2 . GLU   E 2 175  ? 149.791 88.152  156.822 1.00 139.90 -1 175  GLU   E OE2 1 
ATOM   13162 N N   . GLU   E 2 176  ? 150.287 88.294  150.237 1.00 135.26 0  176  GLU   E N   1 
ATOM   13163 C CA  . GLU   E 2 176  ? 150.728 88.268  148.845 1.00 134.93 0  176  GLU   E CA  1 
ATOM   13164 C C   . GLU   E 2 176  ? 150.680 89.663  148.233 1.00 134.97 0  176  GLU   E C   1 
ATOM   13165 O O   . GLU   E 2 176  ? 151.649 90.117  147.608 1.00 134.30 0  176  GLU   E O   1 
ATOM   13166 C CB  . GLU   E 2 176  ? 149.869 87.292  148.042 1.00 133.05 0  176  GLU   E CB  1 
ATOM   13167 C CG  . GLU   E 2 176  ? 150.272 87.161  146.583 1.00 132.58 0  176  GLU   E CG  1 
ATOM   13168 C CD  . GLU   E 2 176  ? 151.473 86.257  146.392 1.00 133.51 0  176  GLU   E CD  1 
ATOM   13169 O OE1 . GLU   E 2 176  ? 151.792 85.487  147.322 1.00 133.63 0  176  GLU   E OE1 1 
ATOM   13170 O OE2 . GLU   E 2 176  ? 152.097 86.313  145.311 1.00 133.05 -1 176  GLU   E OE2 1 
ATOM   13171 N N   . MET   E 2 177  ? 149.563 90.374  148.419 1.00 131.35 0  177  MET   E N   1 
ATOM   13172 C CA  . MET   E 2 177  ? 149.512 91.748  147.939 1.00 131.04 0  177  MET   E CA  1 
ATOM   13173 C C   . MET   E 2 177  ? 150.435 92.648  148.741 1.00 130.62 0  177  MET   E C   1 
ATOM   13174 O O   . MET   E 2 177  ? 150.908 93.658  148.219 1.00 129.69 0  177  MET   E O   1 
ATOM   13175 C CB  . MET   E 2 177  ? 148.097 92.318  147.992 1.00 129.31 0  177  MET   E CB  1 
ATOM   13176 C CG  . MET   E 2 177  ? 147.382 92.150  149.310 1.00 129.48 0  177  MET   E CG  1 
ATOM   13177 S SD  . MET   E 2 177  ? 145.608 92.275  149.063 1.00 131.44 0  177  MET   E SD  1 
ATOM   13178 C CE  . MET   E 2 177  ? 145.157 93.388  150.391 1.00 130.57 0  177  MET   E CE  1 
ATOM   13179 N N   . ILE   E 2 178  ? 150.694 92.315  150.006 1.00 131.09 0  178  ILE   E N   1 
ATOM   13180 C CA  . ILE   E 2 178  ? 151.651 93.098  150.780 1.00 129.93 0  178  ILE   E CA  1 
ATOM   13181 C C   . ILE   E 2 178  ? 153.031 93.018  150.142 1.00 130.95 0  178  ILE   E C   1 
ATOM   13182 O O   . ILE   E 2 178  ? 153.704 94.039  149.952 1.00 131.80 0  178  ILE   E O   1 
ATOM   13183 C CB  . ILE   E 2 178  ? 151.670 92.628  152.246 1.00 130.66 0  178  ILE   E CB  1 
ATOM   13184 C CG1 . ILE   E 2 178  ? 150.280 92.775  152.867 1.00 131.22 0  178  ILE   E CG1 1 
ATOM   13185 C CG2 . ILE   E 2 178  ? 152.693 93.412  153.047 1.00 130.06 0  178  ILE   E CG2 1 
ATOM   13186 C CD1 . ILE   E 2 178  ? 149.809 94.206  152.965 1.00 129.79 0  178  ILE   E CD1 1 
ATOM   13187 N N   . GLU   E 2 179  ? 153.461 91.810  149.772 1.00 133.63 0  179  GLU   E N   1 
ATOM   13188 C CA  . GLU   E 2 179  ? 154.743 91.658  149.091 1.00 133.93 0  179  GLU   E CA  1 
ATOM   13189 C C   . GLU   E 2 179  ? 154.729 92.334  147.724 1.00 133.42 0  179  GLU   E C   1 
ATOM   13190 O O   . GLU   E 2 179  ? 155.720 92.951  147.321 1.00 133.66 0  179  GLU   E O   1 
ATOM   13191 C CB  . GLU   E 2 179  ? 155.098 90.177  148.955 1.00 134.48 0  179  GLU   E CB  1 
ATOM   13192 C CG  . GLU   E 2 179  ? 155.494 89.511  150.263 1.00 134.64 0  179  GLU   E CG  1 
ATOM   13193 C CD  . GLU   E 2 179  ? 155.805 88.034  150.097 1.00 134.53 0  179  GLU   E CD  1 
ATOM   13194 O OE1 . GLU   E 2 179  ? 155.680 87.520  148.964 1.00 134.18 0  179  GLU   E OE1 1 
ATOM   13195 O OE2 . GLU   E 2 179  ? 156.173 87.386  151.100 1.00 134.28 -1 179  GLU   E OE2 1 
ATOM   13196 N N   . LYS   E 2 180  ? 153.616 92.223  146.992 1.00 124.56 0  180  LYS   E N   1 
ATOM   13197 C CA  . LYS   E 2 180  ? 153.537 92.854  145.676 1.00 124.05 0  180  LYS   E CA  1 
ATOM   13198 C C   . LYS   E 2 180  ? 153.634 94.374  145.779 1.00 124.24 0  180  LYS   E C   1 
ATOM   13199 O O   . LYS   E 2 180  ? 154.348 95.018  144.998 1.00 123.64 0  180  LYS   E O   1 
ATOM   13200 C CB  . LYS   E 2 180  ? 152.240 92.442  144.980 1.00 123.96 0  180  LYS   E CB  1 
ATOM   13201 C CG  . LYS   E 2 180  ? 152.051 93.038  143.595 1.00 125.16 0  180  LYS   E CG  1 
ATOM   13202 C CD  . LYS   E 2 180  ? 150.736 92.585  142.981 1.00 123.37 0  180  LYS   E CD  1 
ATOM   13203 C CE  . LYS   E 2 180  ? 150.470 93.287  141.662 1.00 122.58 0  180  LYS   E CE  1 
ATOM   13204 N NZ  . LYS   E 2 180  ? 151.510 92.960  140.648 1.00 123.13 1  180  LYS   E NZ  1 
ATOM   13205 N N   . ILE   E 2 181  ? 152.924 94.964  146.742 1.00 122.54 0  181  ILE   E N   1 
ATOM   13206 C CA  . ILE   E 2 181  ? 152.965 96.407  146.944 1.00 122.11 0  181  ILE   E CA  1 
ATOM   13207 C C   . ILE   E 2 181  ? 154.346 96.837  147.411 1.00 120.79 0  181  ILE   E C   1 
ATOM   13208 O O   . ILE   E 2 181  ? 154.856 97.885  147.000 1.00 120.09 0  181  ILE   E O   1 
ATOM   13209 C CB  . ILE   E 2 181  ? 151.867 96.836  147.937 1.00 121.09 0  181  ILE   E CB  1 
ATOM   13210 C CG1 . ILE   E 2 181  ? 150.485 96.692  147.297 1.00 119.53 0  181  ILE   E CG1 1 
ATOM   13211 C CG2 . ILE   E 2 181  ? 152.091 98.261  148.418 1.00 118.69 0  181  ILE   E CG2 1 
ATOM   13212 C CD1 . ILE   E 2 181  ? 150.368 97.349  145.938 1.00 118.37 0  181  ILE   E CD1 1 
ATOM   13213 N N   . ARG   E 2 182  ? 154.975 96.037  148.277 1.00 124.28 0  182  ARG   E N   1 
ATOM   13214 C CA  . ARG   E 2 182  ? 156.334 96.344  148.704 1.00 124.43 0  182  ARG   E CA  1 
ATOM   13215 C C   . ARG   E 2 182  ? 157.292 96.334  147.522 1.00 125.17 0  182  ARG   E C   1 
ATOM   13216 O O   . ARG   E 2 182  ? 158.159 97.203  147.413 1.00 124.65 0  182  ARG   E O   1 
ATOM   13217 C CB  . ARG   E 2 182  ? 156.787 95.352  149.774 1.00 125.65 0  182  ARG   E CB  1 
ATOM   13218 C CG  . ARG   E 2 182  ? 158.090 95.738  150.459 1.00 126.11 0  182  ARG   E CG  1 
ATOM   13219 C CD  . ARG   E 2 182  ? 158.474 94.734  151.534 1.00 125.77 0  182  ARG   E CD  1 
ATOM   13220 N NE  . ARG   E 2 182  ? 158.785 93.429  150.966 1.00 125.86 0  182  ARG   E NE  1 
ATOM   13221 C CZ  . ARG   E 2 182  ? 158.789 92.295  151.652 1.00 125.41 0  182  ARG   E CZ  1 
ATOM   13222 N NH1 . ARG   E 2 182  ? 158.511 92.269  152.945 1.00 125.05 1  182  ARG   E NH1 1 
ATOM   13223 N NH2 . ARG   E 2 182  ? 159.079 91.158  151.025 1.00 125.22 0  182  ARG   E NH2 1 
ATOM   13224 N N   . THR   E 2 183  ? 157.137 95.366  146.615 1.00 121.04 0  183  THR   E N   1 
ATOM   13225 C CA  . THR   E 2 183  ? 157.990 95.307  145.430 1.00 120.15 0  183  THR   E CA  1 
ATOM   13226 C C   . THR   E 2 183  ? 157.771 96.516  144.527 1.00 119.90 0  183  THR   E C   1 
ATOM   13227 O O   . THR   E 2 183  ? 158.731 97.120  144.032 1.00 118.45 0  183  THR   E O   1 
ATOM   13228 C CB  . THR   E 2 183  ? 157.724 94.011  144.662 1.00 118.62 0  183  THR   E CB  1 
ATOM   13229 O OG1 . THR   E 2 183  ? 158.028 92.887  145.497 1.00 118.66 0  183  THR   E OG1 1 
ATOM   13230 C CG2 . THR   E 2 183  ? 158.580 93.951  143.407 1.00 117.87 0  183  THR   E CG2 1 
ATOM   13231 N N   . GLU   E 2 184  ? 156.508 96.881  144.294 1.00 116.00 0  184  GLU   E N   1 
ATOM   13232 C CA  . GLU   E 2 184  ? 156.216 98.021  143.427 1.00 115.21 0  184  GLU   E CA  1 
ATOM   13233 C C   . GLU   E 2 184  ? 156.745 99.320  144.027 1.00 116.46 0  184  GLU   E C   1 
ATOM   13234 O O   . GLU   E 2 184  ? 157.358 100.142 143.330 1.00 115.26 0  184  GLU   E O   1 
ATOM   13235 C CB  . GLU   E 2 184  ? 154.712 98.116  143.176 1.00 112.32 0  184  GLU   E CB  1 
ATOM   13236 C CG  . GLU   E 2 184  ? 154.160 97.028  142.274 1.00 111.49 0  184  GLU   E CG  1 
ATOM   13237 C CD  . GLU   E 2 184  ? 152.734 97.303  141.841 1.00 113.13 0  184  GLU   E CD  1 
ATOM   13238 O OE1 . GLU   E 2 184  ? 152.143 98.291  142.328 1.00 113.55 0  184  GLU   E OE1 1 
ATOM   13239 O OE2 . GLU   E 2 184  ? 152.203 96.535  141.013 1.00 113.59 -1 184  GLU   E OE2 1 
ATOM   13240 N N   . ALA   E 2 185  ? 156.516 99.521  145.327 1.00 115.91 0  185  ALA   E N   1 
ATOM   13241 C CA  . ALA   E 2 185  ? 157.028 100.706 145.999 1.00 112.30 0  185  ALA   E CA  1 
ATOM   13242 C C   . ALA   E 2 185  ? 158.547 100.716 146.020 1.00 113.25 0  185  ALA   E C   1 
ATOM   13243 O O   . ALA   E 2 185  ? 159.158 101.782 145.913 1.00 114.19 0  185  ALA   E O   1 
ATOM   13244 C CB  . ALA   E 2 185  ? 156.472 100.788 147.420 1.00 109.97 0  185  ALA   E CB  1 
ATOM   13245 N N   . LEU   E 2 186  ? 159.175 99.547  146.152 1.00 119.34 0  186  LEU   E N   1 
ATOM   13246 C CA  . LEU   E 2 186  ? 160.629 99.479  146.088 1.00 121.51 0  186  LEU   E CA  1 
ATOM   13247 C C   . LEU   E 2 186  ? 161.134 99.883  144.713 1.00 119.79 0  186  LEU   E C   1 
ATOM   13248 O O   . LEU   E 2 186  ? 162.132 100.598 144.602 1.00 120.17 0  186  LEU   E O   1 
ATOM   13249 C CB  . LEU   E 2 186  ? 161.107 98.072  146.443 1.00 120.80 0  186  LEU   E CB  1 
ATOM   13250 C CG  . LEU   E 2 186  ? 161.557 97.883  147.890 1.00 121.17 0  186  LEU   E CG  1 
ATOM   13251 C CD1 . LEU   E 2 186  ? 161.820 96.416  148.183 1.00 119.98 0  186  LEU   E CD1 1 
ATOM   13252 C CD2 . LEU   E 2 186  ? 162.790 98.726  148.171 1.00 120.21 0  186  LEU   E CD2 1 
ATOM   13253 N N   . MET   E 2 187  ? 160.460 99.436  143.653 1.00 110.64 0  187  MET   E N   1 
ATOM   13254 C CA  . MET   E 2 187  ? 160.874 99.830  142.310 1.00 112.54 0  187  MET   E CA  1 
ATOM   13255 C C   . MET   E 2 187  ? 160.733 101.335 142.109 1.00 112.95 0  187  MET   E C   1 
ATOM   13256 O O   . MET   E 2 187  ? 161.631 101.984 141.557 1.00 113.08 0  187  MET   E O   1 
ATOM   13257 C CB  . MET   E 2 187  ? 160.063 99.068  141.263 1.00 112.52 0  187  MET   E CB  1 
ATOM   13258 C CG  . MET   E 2 187  ? 160.873 98.038  140.491 1.00 114.00 0  187  MET   E CG  1 
ATOM   13259 S SD  . MET   E 2 187  ? 162.182 98.777  139.494 1.00 113.81 0  187  MET   E SD  1 
ATOM   13260 C CE  . MET   E 2 187  ? 162.745 97.353  138.568 1.00 110.72 0  187  MET   E CE  1 
ATOM   13261 N N   . THR   E 2 188  ? 159.613 101.909 142.558 1.00 107.17 0  188  THR   E N   1 
ATOM   13262 C CA  . THR   E 2 188  ? 159.417 103.351 142.410 1.00 107.37 0  188  THR   E CA  1 
ATOM   13263 C C   . THR   E 2 188  ? 160.437 104.140 143.228 1.00 106.51 0  188  THR   E C   1 
ATOM   13264 O O   . THR   E 2 188  ? 160.994 105.136 142.746 1.00 106.38 0  188  THR   E O   1 
ATOM   13265 C CB  . THR   E 2 188  ? 157.994 103.737 142.811 1.00 105.59 0  188  THR   E CB  1 
ATOM   13266 O OG1 . THR   E 2 188  ? 157.056 103.074 141.954 1.00 105.34 0  188  THR   E OG1 1 
ATOM   13267 C CG2 . THR   E 2 188  ? 157.799 105.238 142.692 1.00 102.74 0  188  THR   E CG2 1 
ATOM   13268 N N   . ASN   E 2 189  ? 160.696 103.707 144.464 1.00 111.92 0  189  ASN   E N   1 
ATOM   13269 C CA  . ASN   E 2 189  ? 161.693 104.368 145.298 1.00 112.49 0  189  ASN   E CA  1 
ATOM   13270 C C   . ASN   E 2 189  ? 163.083 104.239 144.693 1.00 113.01 0  189  ASN   E C   1 
ATOM   13271 O O   . ASN   E 2 189  ? 163.889 105.172 144.769 1.00 112.52 0  189  ASN   E O   1 
ATOM   13272 C CB  . ASN   E 2 189  ? 161.659 103.780 146.709 1.00 111.54 0  189  ASN   E CB  1 
ATOM   13273 C CG  . ASN   E 2 189  ? 162.603 104.485 147.661 1.00 112.59 0  189  ASN   E CG  1 
ATOM   13274 O OD1 . ASN   E 2 189  ? 162.348 105.611 148.086 1.00 113.33 0  189  ASN   E OD1 1 
ATOM   13275 N ND2 . ASN   E 2 189  ? 163.700 103.820 148.005 1.00 113.09 0  189  ASN   E ND2 1 
ATOM   13276 N N   . ASP   E 2 190  ? 163.383 103.087 144.091 1.00 113.74 0  190  ASP   E N   1 
ATOM   13277 C CA  . ASP   E 2 190  ? 164.663 102.904 143.420 1.00 115.08 0  190  ASP   E CA  1 
ATOM   13278 C C   . ASP   E 2 190  ? 164.806 103.855 142.244 1.00 116.11 0  190  ASP   E C   1 
ATOM   13279 O O   . ASP   E 2 190  ? 165.873 104.441 142.042 1.00 115.66 0  190  ASP   E O   1 
ATOM   13280 C CB  . ASP   E 2 190  ? 164.808 101.455 142.958 1.00 114.59 0  190  ASP   E CB  1 
ATOM   13281 C CG  . ASP   E 2 190  ? 166.104 101.209 142.220 1.00 115.95 0  190  ASP   E CG  1 
ATOM   13282 O OD1 . ASP   E 2 190  ? 167.175 101.320 142.850 1.00 118.45 0  190  ASP   E OD1 1 
ATOM   13283 O OD2 . ASP   E 2 190  ? 166.052 100.906 141.010 1.00 113.22 -1 190  ASP   E OD2 1 
ATOM   13284 N N   . ARG   E 2 191  ? 163.743 104.022 141.455 1.00 105.42 0  191  ARG   E N   1 
ATOM   13285 C CA  . ARG   E 2 191  ? 163.797 104.973 140.347 1.00 104.33 0  191  ARG   E CA  1 
ATOM   13286 C C   . ARG   E 2 191  ? 164.005 106.397 140.850 1.00 104.10 0  191  ARG   E C   1 
ATOM   13287 O O   . ARG   E 2 191  ? 164.824 107.148 140.301 1.00 103.44 0  191  ARG   E O   1 
ATOM   13288 C CB  . ARG   E 2 191  ? 162.521 104.884 139.512 1.00 102.93 0  191  ARG   E CB  1 
ATOM   13289 C CG  . ARG   E 2 191  ? 162.674 104.101 138.224 1.00 100.84 0  191  ARG   E CG  1 
ATOM   13290 C CD  . ARG   E 2 191  ? 161.383 104.117 137.429 1.00 101.83 0  191  ARG   E CD  1 
ATOM   13291 N NE  . ARG   E 2 191  ? 160.841 105.464 137.288 1.00 100.74 0  191  ARG   E NE  1 
ATOM   13292 C CZ  . ARG   E 2 191  ? 161.022 106.240 136.228 1.00 100.04 0  191  ARG   E CZ  1 
ATOM   13293 N NH1 . ARG   E 2 191  ? 161.725 105.831 135.184 1.00 101.22 1  191  ARG   E NH1 1 
ATOM   13294 N NH2 . ARG   E 2 191  ? 160.482 107.454 136.213 1.00 98.61  0  191  ARG   E NH2 1 
ATOM   13295 N N   . LEU   E 2 192  ? 163.275 106.784 141.899 1.00 106.59 0  192  LEU   E N   1 
ATOM   13296 C CA  . LEU   E 2 192  ? 163.408 108.134 142.442 1.00 105.23 0  192  LEU   E CA  1 
ATOM   13297 C C   . LEU   E 2 192  ? 164.817 108.376 142.973 1.00 108.29 0  192  LEU   E C   1 
ATOM   13298 O O   . LEU   E 2 192  ? 165.425 109.421 142.709 1.00 108.15 0  192  LEU   E O   1 
ATOM   13299 C CB  . LEU   E 2 192  ? 162.373 108.356 143.543 1.00 105.79 0  192  LEU   E CB  1 
ATOM   13300 C CG  . LEU   E 2 192  ? 160.916 108.428 143.088 1.00 107.71 0  192  LEU   E CG  1 
ATOM   13301 C CD1 . LEU   E 2 192  ? 159.981 108.280 144.275 1.00 106.35 0  192  LEU   E CD1 1 
ATOM   13302 C CD2 . LEU   E 2 192  ? 160.650 109.729 142.344 1.00 105.40 0  192  LEU   E CD2 1 
ATOM   13303 N N   . GLU   E 2 193  ? 165.358 107.408 143.715 1.00 119.81 0  193  GLU   E N   1 
ATOM   13304 C CA  . GLU   E 2 193  ? 166.700 107.556 144.262 1.00 120.68 0  193  GLU   E CA  1 
ATOM   13305 C C   . GLU   E 2 193  ? 167.757 107.524 143.167 1.00 118.93 0  193  GLU   E C   1 
ATOM   13306 O O   . GLU   E 2 193  ? 168.774 108.211 143.277 1.00 116.69 0  193  GLU   E O   1 
ATOM   13307 C CB  . GLU   E 2 193  ? 166.966 106.467 145.299 1.00 120.77 0  193  GLU   E CB  1 
ATOM   13308 C CG  . GLU   E 2 193  ? 168.200 106.707 146.149 1.00 120.29 0  193  GLU   E CG  1 
ATOM   13309 C CD  . GLU   E 2 193  ? 168.296 105.744 147.315 1.00 120.40 0  193  GLU   E CD  1 
ATOM   13310 O OE1 . GLU   E 2 193  ? 167.237 105.311 147.817 1.00 119.93 0  193  GLU   E OE1 1 
ATOM   13311 O OE2 . GLU   E 2 193  ? 169.429 105.419 147.729 1.00 120.29 -1 193  GLU   E OE2 1 
ATOM   13312 N N   . ALA   E 2 194  ? 167.535 106.749 142.104 1.00 115.60 0  194  ALA   E N   1 
ATOM   13313 C CA  . ALA   E 2 194  ? 168.465 106.749 140.981 1.00 116.10 0  194  ALA   E CA  1 
ATOM   13314 C C   . ALA   E 2 194  ? 168.491 108.108 140.298 1.00 116.74 0  194  ALA   E C   1 
ATOM   13315 O O   . ALA   E 2 194  ? 169.559 108.617 139.940 1.00 114.10 0  194  ALA   E O   1 
ATOM   13316 C CB  . ALA   E 2 194  ? 168.085 105.650 139.988 1.00 113.08 0  194  ALA   E CB  1 
ATOM   13317 N N   . MET   E 2 195  ? 167.317 108.714 140.108 1.00 120.08 0  195  MET   E N   1 
ATOM   13318 C CA  . MET   E 2 195  ? 167.278 110.040 139.501 1.00 118.00 0  195  MET   E CA  1 
ATOM   13319 C C   . MET   E 2 195  ? 167.873 111.099 140.422 1.00 119.12 0  195  MET   E C   1 
ATOM   13320 O O   . MET   E 2 195  ? 168.461 112.074 139.941 1.00 121.57 0  195  MET   E O   1 
ATOM   13321 C CB  . MET   E 2 195  ? 165.845 110.405 139.116 1.00 116.45 0  195  MET   E CB  1 
ATOM   13322 C CG  . MET   E 2 195  ? 165.405 109.820 137.784 1.00 117.50 0  195  MET   E CG  1 
ATOM   13323 S SD  . MET   E 2 195  ? 163.691 109.267 137.779 1.00 119.26 0  195  MET   E SD  1 
ATOM   13324 C CE  . MET   E 2 195  ? 163.497 108.822 136.056 1.00 116.28 0  195  MET   E CE  1 
ATOM   13325 N N   . ALA   E 2 196  ? 167.735 110.929 141.739 1.00 115.81 0  196  ALA   E N   1 
ATOM   13326 C CA  . ALA   E 2 196  ? 168.353 111.864 142.674 1.00 113.54 0  196  ALA   E CA  1 
ATOM   13327 C C   . ALA   E 2 196  ? 169.862 111.667 142.779 1.00 112.47 0  196  ALA   E C   1 
ATOM   13328 O O   . ALA   E 2 196  ? 170.582 112.615 143.111 1.00 109.79 0  196  ALA   E O   1 
ATOM   13329 C CB  . ALA   E 2 196  ? 167.710 111.732 144.055 1.00 112.27 0  196  ALA   E CB  1 
ATOM   13330 N N   . ARG   E 2 197  ? 170.354 110.454 142.509 1.00 120.27 0  197  ARG   E N   1 
ATOM   13331 C CA  . ARG   E 2 197  ? 171.784 110.173 142.597 1.00 122.06 0  197  ARG   E CA  1 
ATOM   13332 C C   . ARG   E 2 197  ? 172.594 110.954 141.574 1.00 121.93 0  197  ARG   E C   1 
ATOM   13333 O O   . ARG   E 2 197  ? 173.814 111.077 141.730 1.00 120.64 0  197  ARG   E O   1 
ATOM   13334 C CB  . ARG   E 2 197  ? 172.047 108.677 142.408 1.00 121.55 0  197  ARG   E CB  1 
ATOM   13335 C CG  . ARG   E 2 197  ? 171.892 107.830 143.661 1.00 121.22 0  197  ARG   E CG  1 
ATOM   13336 C CD  . ARG   E 2 197  ? 171.833 106.353 143.300 1.00 120.11 0  197  ARG   E CD  1 
ATOM   13337 N NE  . ARG   E 2 197  ? 171.213 105.548 144.346 1.00 121.18 0  197  ARG   E NE  1 
ATOM   13338 C CZ  . ARG   E 2 197  ? 170.553 104.419 144.127 1.00 120.82 0  197  ARG   E CZ  1 
ATOM   13339 N NH1 . ARG   E 2 197  ? 170.399 103.934 142.906 1.00 120.56 1  197  ARG   E NH1 1 
ATOM   13340 N NH2 . ARG   E 2 197  ? 170.032 103.761 145.160 1.00 119.55 0  197  ARG   E NH2 1 
ATOM   13341 N N   . LEU   E 2 198  ? 171.951 111.472 140.528 1.00 115.18 0  198  LEU   E N   1 
ATOM   13342 C CA  . LEU   E 2 198  ? 172.655 112.270 139.535 1.00 112.99 0  198  LEU   E CA  1 
ATOM   13343 C C   . LEU   E 2 198  ? 173.075 113.632 140.073 1.00 111.67 0  198  LEU   E C   1 
ATOM   13344 O O   . LEU   E 2 198  ? 173.819 114.345 139.391 1.00 111.99 0  198  LEU   E O   1 
ATOM   13345 C CB  . LEU   E 2 198  ? 171.783 112.437 138.291 1.00 112.11 0  198  LEU   E CB  1 
ATOM   13346 C CG  . LEU   E 2 198  ? 171.118 111.156 137.782 1.00 111.20 0  198  LEU   E CG  1 
ATOM   13347 C CD1 . LEU   E 2 198  ? 170.112 111.465 136.687 1.00 110.46 0  198  LEU   E CD1 1 
ATOM   13348 C CD2 . LEU   E 2 198  ? 172.160 110.163 137.288 1.00 111.77 0  198  LEU   E CD2 1 
ATOM   13349 N N   . ARG   E 2 199  ? 172.615 114.007 141.263 1.00 109.80 0  199  ARG   E N   1 
ATOM   13350 C CA  . ARG   E 2 199  ? 173.062 115.229 141.922 1.00 110.99 0  199  ARG   E CA  1 
ATOM   13351 C C   . ARG   E 2 199  ? 174.546 115.153 142.268 1.00 110.82 0  199  ARG   E C   1 
ATOM   13352 O O   . ARG   E 2 199  ? 175.152 114.082 142.248 1.00 110.33 0  199  ARG   E O   1 
ATOM   13353 C CB  . ARG   E 2 199  ? 172.246 115.486 143.192 1.00 108.71 0  199  ARG   E CB  1 
ATOM   13354 C CG  . ARG   E 2 199  ? 170.902 116.151 142.950 1.00 108.01 0  199  ARG   E CG  1 
ATOM   13355 C CD  . ARG   E 2 199  ? 170.353 116.767 144.227 1.00 106.79 0  199  ARG   E CD  1 
ATOM   13356 N NE  . ARG   E 2 199  ? 169.732 115.775 145.096 1.00 108.40 0  199  ARG   E NE  1 
ATOM   13357 C CZ  . ARG   E 2 199  ? 169.256 116.033 146.306 1.00 107.69 0  199  ARG   E CZ  1 
ATOM   13358 N NH1 . ARG   E 2 199  ? 169.324 117.245 146.832 1.00 108.01 1  199  ARG   E NH1 1 
ATOM   13359 N NH2 . ARG   E 2 199  ? 168.694 115.051 147.005 1.00 106.55 0  199  ARG   E NH2 1 
HETATM 13360 N N1  . A1AWZ F 3 .    ? 152.039 148.135 119.158 1.00 43.70  0  2201 A1AWZ A N1  1 
HETATM 13361 N N3  . A1AWZ F 3 .    ? 153.709 146.943 107.612 1.00 33.46  0  2201 A1AWZ A N3  1 
HETATM 13362 C C4  . A1AWZ F 3 .    ? 152.562 147.014 115.183 1.00 36.35  0  2201 A1AWZ A C4  1 
HETATM 13363 C C5  . A1AWZ F 3 .    ? 152.777 148.339 115.550 1.00 41.23  0  2201 A1AWZ A C5  1 
HETATM 13364 C C6  . A1AWZ F 3 .    ? 152.613 148.753 116.882 1.00 43.69  0  2201 A1AWZ A C6  1 
HETATM 13365 C C7  . A1AWZ F 3 .    ? 152.828 150.084 117.293 1.00 40.88  0  2201 A1AWZ A C7  1 
HETATM 13366 C C8  . A1AWZ F 3 .    ? 152.647 150.401 118.600 1.00 33.52  0  2201 A1AWZ A C8  1 
HETATM 13367 C C10 . A1AWZ F 3 .    ? 152.217 147.803 117.848 1.00 42.41  0  2201 A1AWZ A C10 1 
HETATM 13368 C C13 . A1AWZ F 3 .    ? 153.264 146.665 110.237 1.00 43.31  0  2201 A1AWZ A C13 1 
HETATM 13369 C C15 . A1AWZ F 3 .    ? 154.831 146.652 108.286 1.00 32.88  0  2201 A1AWZ A C15 1 
HETATM 13370 C C17 . A1AWZ F 3 .    ? 156.182 147.091 106.357 1.00 40.60  0  2201 A1AWZ A C17 1 
HETATM 13371 C C20 . A1AWZ F 3 .    ? 152.481 147.601 105.672 1.00 40.38  0  2201 A1AWZ A C20 1 
HETATM 13372 C C21 . A1AWZ F 3 .    ? 152.339 147.607 104.288 1.00 41.11  0  2201 A1AWZ A C21 1 
HETATM 13373 C C22 . A1AWZ F 3 .    ? 151.121 147.886 103.692 1.00 40.19  0  2201 A1AWZ A C22 1 
HETATM 13374 C C24 . A1AWZ F 3 .    ? 150.144 148.181 105.866 1.00 46.83  0  2201 A1AWZ A C24 1 
HETATM 13375 C C26 . A1AWZ F 3 .    ? 157.556 147.175 105.684 1.00 35.95  0  2201 A1AWZ A C26 1 
HETATM 13376 C C28 . A1AWZ F 3 .    ? 158.594 146.333 106.417 1.00 37.81  0  2201 A1AWZ A C28 1 
HETATM 13377 C C1  . A1AWZ F 3 .    ? 151.313 144.270 118.094 1.00 48.06  0  2201 A1AWZ A C1  1 
HETATM 13378 O O1  . A1AWZ F 3 .    ? 151.615 145.621 118.449 1.00 39.19  0  2201 A1AWZ A O1  1 
HETATM 13379 C C2  . A1AWZ F 3 .    ? 151.996 146.461 117.450 1.00 37.59  0  2201 A1AWZ A C2  1 
HETATM 13380 N N2  . A1AWZ F 3 .    ? 153.033 146.432 111.657 1.00 39.95  0  2201 A1AWZ A N2  1 
HETATM 13381 O O2  . A1AWZ F 3 .    ? 155.632 146.913 110.541 1.00 38.25  0  2201 A1AWZ A O2  1 
HETATM 13382 C C3  . A1AWZ F 3 .    ? 152.165 146.091 116.147 1.00 37.52  0  2201 A1AWZ A C3  1 
HETATM 13383 O O3  . A1AWZ F 3 .    ? 157.464 146.663 104.344 1.00 42.35  0  2201 A1AWZ A O3  1 
HETATM 13384 N N4  . A1AWZ F 3 .    ? 152.785 145.192 112.115 1.00 43.57  0  2201 A1AWZ A N4  1 
HETATM 13385 N N5  . A1AWZ F 3 .    ? 152.604 145.293 113.415 1.00 45.17  0  2201 A1AWZ A N5  1 
HETATM 13386 C C9  . A1AWZ F 3 .    ? 152.251 149.391 119.496 1.00 36.93  0  2201 A1AWZ A C9  1 
HETATM 13387 C C11 . A1AWZ F 3 .    ? 152.728 146.595 113.787 1.00 35.45  0  2201 A1AWZ A C11 1 
HETATM 13388 C C12 . A1AWZ F 3 .    ? 153.002 147.322 112.660 1.00 33.34  0  2201 A1AWZ A C12 1 
HETATM 13389 C C14 . A1AWZ F 3 .    ? 154.663 146.260 109.729 1.00 36.96  0  2201 A1AWZ A C14 1 
HETATM 13390 C C16 . A1AWZ F 3 .    ? 156.076 146.726 107.694 1.00 38.90  0  2201 A1AWZ A C16 1 
HETATM 13391 C C18 . A1AWZ F 3 .    ? 155.017 147.385 105.674 1.00 47.21  0  2201 A1AWZ A C18 1 
HETATM 13392 C C19 . A1AWZ F 3 .    ? 153.788 147.310 106.318 1.00 43.46  0  2201 A1AWZ A C19 1 
HETATM 13393 C C23 . A1AWZ F 3 .    ? 150.056 148.165 104.502 1.00 46.79  0  2201 A1AWZ A C23 1 
HETATM 13394 C C25 . A1AWZ F 3 .    ? 151.366 147.896 106.449 1.00 38.56  0  2201 A1AWZ A C25 1 
HETATM 13395 C C27 . A1AWZ F 3 .    ? 158.033 148.618 105.576 1.00 36.34  0  2201 A1AWZ A C27 1 
HETATM 13396 C C29 . A1AWZ F 3 .    ? 154.861 144.742 109.921 1.00 41.24  0  2201 A1AWZ A C29 1 
HETATM 13397 F F1  . A1AWZ F 3 .    ? 155.096 147.756 104.383 1.00 48.43  0  2201 A1AWZ A F1  1 
HETATM 13398 F F2  . A1AWZ F 3 .    ? 148.856 148.441 103.925 1.00 43.94  0  2201 A1AWZ A F2  1 
HETATM 13399 F F3  . A1AWZ F 3 .    ? 153.960 144.034 109.236 1.00 44.08  0  2201 A1AWZ A F3  1 
HETATM 13400 F F4  . A1AWZ F 3 .    ? 154.751 144.378 111.201 1.00 46.31  0  2201 A1AWZ A F4  1 
HETATM 13401 F F5  . A1AWZ F 3 .    ? 156.066 144.342 109.509 1.00 43.66  0  2201 A1AWZ A F5  1 
# 
