data_9DMI
# 
_entry.id   9DMI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9DMI         pdb_00009dmi 10.2210/pdb9dmi/pdb 
WWPDB D_1000288363 ?            ?                   
EMDB  EMD-47006    ?            ?                   
# 
_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       2025-06-18 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9DMI 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB 'Focused refinement map'                                                       EMD-47004 'focused EM volume'    
EMDB 'Structure of the C-terminal half of LRRK2 bound to RN277 (Type-II inhibitor)' EMD-47006 'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              aleschziner@ucsd.edu 
_pdbx_contact_author.name_first         Andres 
_pdbx_contact_author.name_last          Leschziner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7732-7023 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Sanz-Murillo, M.' 1 0000-0002-6175-9315 
'Leschziner, A.'   2 0000-0002-7732-7023 
# 
_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            'Sci Adv' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            11 
_citation.language                  ? 
_citation.page_first                eadt2050 
_citation.page_last                 eadt2050 
_citation.title                     
;Type II kinase inhibitors that target Parkinson's disease-associated LRRK2.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/sciadv.adt2050 
_citation.pdbx_database_id_PubMed   40465731 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Raig, N.D.'          1  0000-0002-2075-7938 
primary 'Surridge, K.J.'      2  0000-0003-0048-5784 
primary 'Sanz-Murillo, M.'    3  0000-0002-6175-9315 
primary 'Dederer, V.'         4  0009-0006-7557-5388 
primary 'Kramer, A.'          5  0000-0003-3294-2660 
primary 'Schwalm, M.P.'       6  0000-0002-1252-1829 
primary 'Lattal, N.M.'        7  ?                   
primary 'Elson, L.'           8  0009-0004-6142-3653 
primary 'Chatterjee, D.'      9  ?                   
primary 'Mathea, S.'          10 0000-0001-8500-4569 
primary 'Hanke, T.'           11 0000-0001-7202-9468 
primary 'Leschziner, A.E.'    12 0000-0002-7732-7023 
primary 'Reck-Peterson, S.L.' 13 0000-0002-1553-465X 
primary 'Knapp, S.'           14 0000-0001-5995-6494 
# 
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 'Leucine-rich repeat serine/threonine-protein kinase 2' 136174.781 1 2.7.11.1,3.6.5.- ? ? ? 
2 polymer     man 'E11 DARPin' 19766.912  1 ?                ? ? 'Some loops are missing due to the lack of cryo-EM density' 
3 non-polymer syn 
;N-[3-tert-butyl-1-(4-methylphenyl)-1H-pyrazol-5-yl]-N'-{(3M)-3-[2-chloro-4-(morpholin-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-5-yl]phenyl}urea
;
585.099    1 ?                ? ? ?                                                           
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        Dardarin 
# 
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 
;NRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQR
ALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATE
ESDALAKLRKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENELPHA
VHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRRDVEKFLSKKRKFPKNYMSQYFKL
LEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRM
YWRQGIYLNWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWA
LYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEQAPEFLLGDGSFGS
VYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQH
RIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQ
QADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEKLIKQCLKENPQERPTSAQVFDIL
NSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKE
SWIVSGTQSGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLKILN
IGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAFSDSNIITVVVDTALYIAKQNSPV
VEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFC
NSVRVMMTAQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE
;
;NRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQR
ALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATE
ESDALAKLRKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENELPHA
VHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRRDVEKFLSKKRKFPKNYMSQYFKL
LEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRM
YWRQGIYLNWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWA
LYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEQAPEFLLGDGSFGS
VYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQH
RIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQ
QADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEKLIKQCLKENPQERPTSAQVFDIL
NSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKE
SWIVSGTQSGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLKILN
IGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAFSDSNIITVVVDTALYIAKQNSPV
VEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFC
NSVRVMMTAQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE
;
A ? 
2 'polypeptide(L)' no no 
;MRGSHHHHHHHHGSDLGKKLLEAARAGQDDEVRILMANGADVNATDEAGVTPLHLAADSGHLEIVEVLLKTGADVNAWDH
YGFTPLHLAAHVGHLEIVEVLLKAGADVNAQDHAGWTPLHLAALYGHLEIVEVLLKHGADVNAQDMWGETPFDLAIDNGN
EDIAEVLQKAAKLNDYKDDDDK
;
;MRGSHHHHHHHHGSDLGKKLLEAARAGQDDEVRILMANGADVNATDEAGVTPLHLAADSGHLEIVEVLLKTGADVNAWDH
YGFTPLHLAAHVGHLEIVEVLLKAGADVNAQDHAGWTPLHLAALYGHLEIVEVLLKHGADVNAQDMWGETPFDLAIDNGN
EDIAEVLQKAAKLNDYKDDDDK
;
B ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        
;N-[3-tert-butyl-1-(4-methylphenyl)-1H-pyrazol-5-yl]-N'-{(3M)-3-[2-chloro-4-(morpholin-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-5-yl]phenyl}urea
;
_pdbx_entity_nonpoly.comp_id     A1A7Q 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    ASN n 
1 2    ARG n 
1 3    MET n 
1 4    LYS n 
1 5    LEU n 
1 6    MET n 
1 7    ILE n 
1 8    VAL n 
1 9    GLY n 
1 10   ASN n 
1 11   THR n 
1 12   GLY n 
1 13   SER n 
1 14   GLY n 
1 15   LYS n 
1 16   THR n 
1 17   THR n 
1 18   LEU n 
1 19   LEU n 
1 20   GLN n 
1 21   GLN n 
1 22   LEU n 
1 23   MET n 
1 24   LYS n 
1 25   THR n 
1 26   LYS n 
1 27   LYS n 
1 28   SER n 
1 29   ASP n 
1 30   LEU n 
1 31   GLY n 
1 32   MET n 
1 33   GLN n 
1 34   SER n 
1 35   ALA n 
1 36   THR n 
1 37   VAL n 
1 38   GLY n 
1 39   ILE n 
1 40   ASP n 
1 41   VAL n 
1 42   LYS n 
1 43   ASP n 
1 44   TRP n 
1 45   PRO n 
1 46   ILE n 
1 47   GLN n 
1 48   ILE n 
1 49   ARG n 
1 50   ASP n 
1 51   LYS n 
1 52   ARG n 
1 53   LYS n 
1 54   ARG n 
1 55   ASP n 
1 56   LEU n 
1 57   VAL n 
1 58   LEU n 
1 59   ASN n 
1 60   VAL n 
1 61   TRP n 
1 62   ASP n 
1 63   PHE n 
1 64   ALA n 
1 65   GLY n 
1 66   ARG n 
1 67   GLU n 
1 68   GLU n 
1 69   PHE n 
1 70   TYR n 
1 71   SER n 
1 72   THR n 
1 73   HIS n 
1 74   PRO n 
1 75   HIS n 
1 76   PHE n 
1 77   MET n 
1 78   THR n 
1 79   GLN n 
1 80   ARG n 
1 81   ALA n 
1 82   LEU n 
1 83   TYR n 
1 84   LEU n 
1 85   ALA n 
1 86   VAL n 
1 87   TYR n 
1 88   ASP n 
1 89   LEU n 
1 90   SER n 
1 91   LYS n 
1 92   GLY n 
1 93   GLN n 
1 94   ALA n 
1 95   GLU n 
1 96   VAL n 
1 97   ASP n 
1 98   ALA n 
1 99   MET n 
1 100  LYS n 
1 101  PRO n 
1 102  TRP n 
1 103  LEU n 
1 104  PHE n 
1 105  ASN n 
1 106  ILE n 
1 107  LYS n 
1 108  ALA n 
1 109  ARG n 
1 110  ALA n 
1 111  SER n 
1 112  SER n 
1 113  SER n 
1 114  PRO n 
1 115  VAL n 
1 116  ILE n 
1 117  LEU n 
1 118  VAL n 
1 119  GLY n 
1 120  THR n 
1 121  HIS n 
1 122  LEU n 
1 123  ASP n 
1 124  VAL n 
1 125  SER n 
1 126  ASP n 
1 127  GLU n 
1 128  LYS n 
1 129  GLN n 
1 130  ARG n 
1 131  LYS n 
1 132  ALA n 
1 133  CYS n 
1 134  MET n 
1 135  SER n 
1 136  LYS n 
1 137  ILE n 
1 138  THR n 
1 139  LYS n 
1 140  GLU n 
1 141  LEU n 
1 142  LEU n 
1 143  ASN n 
1 144  LYS n 
1 145  ARG n 
1 146  GLY n 
1 147  PHE n 
1 148  PRO n 
1 149  ALA n 
1 150  ILE n 
1 151  ARG n 
1 152  ASP n 
1 153  TYR n 
1 154  HIS n 
1 155  PHE n 
1 156  VAL n 
1 157  ASN n 
1 158  ALA n 
1 159  THR n 
1 160  GLU n 
1 161  GLU n 
1 162  SER n 
1 163  ASP n 
1 164  ALA n 
1 165  LEU n 
1 166  ALA n 
1 167  LYS n 
1 168  LEU n 
1 169  ARG n 
1 170  LYS n 
1 171  THR n 
1 172  ILE n 
1 173  ILE n 
1 174  ASN n 
1 175  GLU n 
1 176  SER n 
1 177  LEU n 
1 178  ASN n 
1 179  PHE n 
1 180  LYS n 
1 181  ILE n 
1 182  ARG n 
1 183  ASP n 
1 184  GLN n 
1 185  LEU n 
1 186  VAL n 
1 187  VAL n 
1 188  GLY n 
1 189  GLN n 
1 190  LEU n 
1 191  ILE n 
1 192  PRO n 
1 193  ASP n 
1 194  CYS n 
1 195  TYR n 
1 196  VAL n 
1 197  GLU n 
1 198  LEU n 
1 199  GLU n 
1 200  LYS n 
1 201  ILE n 
1 202  ILE n 
1 203  LEU n 
1 204  SER n 
1 205  GLU n 
1 206  ARG n 
1 207  LYS n 
1 208  ASN n 
1 209  VAL n 
1 210  PRO n 
1 211  ILE n 
1 212  GLU n 
1 213  PHE n 
1 214  PRO n 
1 215  VAL n 
1 216  ILE n 
1 217  ASP n 
1 218  ARG n 
1 219  LYS n 
1 220  ARG n 
1 221  LEU n 
1 222  LEU n 
1 223  GLN n 
1 224  LEU n 
1 225  VAL n 
1 226  ARG n 
1 227  GLU n 
1 228  ASN n 
1 229  GLN n 
1 230  LEU n 
1 231  GLN n 
1 232  LEU n 
1 233  ASP n 
1 234  GLU n 
1 235  ASN n 
1 236  GLU n 
1 237  LEU n 
1 238  PRO n 
1 239  HIS n 
1 240  ALA n 
1 241  VAL n 
1 242  HIS n 
1 243  PHE n 
1 244  LEU n 
1 245  ASN n 
1 246  GLU n 
1 247  SER n 
1 248  GLY n 
1 249  VAL n 
1 250  LEU n 
1 251  LEU n 
1 252  HIS n 
1 253  PHE n 
1 254  GLN n 
1 255  ASP n 
1 256  PRO n 
1 257  ALA n 
1 258  LEU n 
1 259  GLN n 
1 260  LEU n 
1 261  SER n 
1 262  ASP n 
1 263  LEU n 
1 264  TYR n 
1 265  PHE n 
1 266  VAL n 
1 267  GLU n 
1 268  PRO n 
1 269  LYS n 
1 270  TRP n 
1 271  LEU n 
1 272  CYS n 
1 273  LYS n 
1 274  ILE n 
1 275  MET n 
1 276  ALA n 
1 277  GLN n 
1 278  ILE n 
1 279  LEU n 
1 280  THR n 
1 281  VAL n 
1 282  LYS n 
1 283  VAL n 
1 284  GLU n 
1 285  GLY n 
1 286  CYS n 
1 287  PRO n 
1 288  LYS n 
1 289  HIS n 
1 290  PRO n 
1 291  LYS n 
1 292  GLY n 
1 293  ILE n 
1 294  ILE n 
1 295  SER n 
1 296  ARG n 
1 297  ARG n 
1 298  ASP n 
1 299  VAL n 
1 300  GLU n 
1 301  LYS n 
1 302  PHE n 
1 303  LEU n 
1 304  SER n 
1 305  LYS n 
1 306  LYS n 
1 307  ARG n 
1 308  LYS n 
1 309  PHE n 
1 310  PRO n 
1 311  LYS n 
1 312  ASN n 
1 313  TYR n 
1 314  MET n 
1 315  SER n 
1 316  GLN n 
1 317  TYR n 
1 318  PHE n 
1 319  LYS n 
1 320  LEU n 
1 321  LEU n 
1 322  GLU n 
1 323  LYS n 
1 324  PHE n 
1 325  GLN n 
1 326  ILE n 
1 327  ALA n 
1 328  LEU n 
1 329  PRO n 
1 330  ILE n 
1 331  GLY n 
1 332  GLU n 
1 333  GLU n 
1 334  TYR n 
1 335  LEU n 
1 336  LEU n 
1 337  VAL n 
1 338  PRO n 
1 339  SER n 
1 340  SER n 
1 341  LEU n 
1 342  SER n 
1 343  ASP n 
1 344  HIS n 
1 345  ARG n 
1 346  PRO n 
1 347  VAL n 
1 348  ILE n 
1 349  GLU n 
1 350  LEU n 
1 351  PRO n 
1 352  HIS n 
1 353  CYS n 
1 354  GLU n 
1 355  ASN n 
1 356  SER n 
1 357  GLU n 
1 358  ILE n 
1 359  ILE n 
1 360  ILE n 
1 361  ARG n 
1 362  LEU n 
1 363  TYR n 
1 364  GLU n 
1 365  MET n 
1 366  PRO n 
1 367  TYR n 
1 368  PHE n 
1 369  PRO n 
1 370  MET n 
1 371  GLY n 
1 372  PHE n 
1 373  TRP n 
1 374  SER n 
1 375  ARG n 
1 376  LEU n 
1 377  ILE n 
1 378  ASN n 
1 379  ARG n 
1 380  LEU n 
1 381  LEU n 
1 382  GLU n 
1 383  ILE n 
1 384  SER n 
1 385  PRO n 
1 386  TYR n 
1 387  MET n 
1 388  LEU n 
1 389  SER n 
1 390  GLY n 
1 391  ARG n 
1 392  GLU n 
1 393  ARG n 
1 394  ALA n 
1 395  LEU n 
1 396  ARG n 
1 397  PRO n 
1 398  ASN n 
1 399  ARG n 
1 400  MET n 
1 401  TYR n 
1 402  TRP n 
1 403  ARG n 
1 404  GLN n 
1 405  GLY n 
1 406  ILE n 
1 407  TYR n 
1 408  LEU n 
1 409  ASN n 
1 410  TRP n 
1 411  SER n 
1 412  PRO n 
1 413  GLU n 
1 414  ALA n 
1 415  TYR n 
1 416  CYS n 
1 417  LEU n 
1 418  VAL n 
1 419  GLY n 
1 420  SER n 
1 421  GLU n 
1 422  VAL n 
1 423  LEU n 
1 424  ASP n 
1 425  ASN n 
1 426  HIS n 
1 427  PRO n 
1 428  GLU n 
1 429  SER n 
1 430  PHE n 
1 431  LEU n 
1 432  LYS n 
1 433  ILE n 
1 434  THR n 
1 435  VAL n 
1 436  PRO n 
1 437  SER n 
1 438  CYS n 
1 439  ARG n 
1 440  LYS n 
1 441  GLY n 
1 442  CYS n 
1 443  ILE n 
1 444  LEU n 
1 445  LEU n 
1 446  GLY n 
1 447  GLN n 
1 448  VAL n 
1 449  VAL n 
1 450  ASP n 
1 451  HIS n 
1 452  ILE n 
1 453  ASP n 
1 454  SER n 
1 455  LEU n 
1 456  MET n 
1 457  GLU n 
1 458  GLU n 
1 459  TRP n 
1 460  PHE n 
1 461  PRO n 
1 462  GLY n 
1 463  LEU n 
1 464  LEU n 
1 465  GLU n 
1 466  ILE n 
1 467  ASP n 
1 468  ILE n 
1 469  CYS n 
1 470  GLY n 
1 471  GLU n 
1 472  GLY n 
1 473  GLU n 
1 474  THR n 
1 475  LEU n 
1 476  LEU n 
1 477  LYS n 
1 478  LYS n 
1 479  TRP n 
1 480  ALA n 
1 481  LEU n 
1 482  TYR n 
1 483  SER n 
1 484  PHE n 
1 485  ASN n 
1 486  ASP n 
1 487  GLY n 
1 488  GLU n 
1 489  GLU n 
1 490  HIS n 
1 491  GLN n 
1 492  LYS n 
1 493  ILE n 
1 494  LEU n 
1 495  LEU n 
1 496  ASP n 
1 497  ASP n 
1 498  LEU n 
1 499  MET n 
1 500  LYS n 
1 501  LYS n 
1 502  ALA n 
1 503  GLU n 
1 504  GLU n 
1 505  GLY n 
1 506  ASP n 
1 507  LEU n 
1 508  LEU n 
1 509  VAL n 
1 510  ASN n 
1 511  PRO n 
1 512  ASP n 
1 513  GLN n 
1 514  PRO n 
1 515  ARG n 
1 516  LEU n 
1 517  THR n 
1 518  ILE n 
1 519  PRO n 
1 520  ILE n 
1 521  SER n 
1 522  GLN n 
1 523  ILE n 
1 524  ALA n 
1 525  PRO n 
1 526  ASP n 
1 527  LEU n 
1 528  ILE n 
1 529  LEU n 
1 530  ALA n 
1 531  ASP n 
1 532  LEU n 
1 533  PRO n 
1 534  ARG n 
1 535  ASN n 
1 536  ILE n 
1 537  MET n 
1 538  LEU n 
1 539  ASN n 
1 540  ASN n 
1 541  ASP n 
1 542  GLU n 
1 543  LEU n 
1 544  GLU n 
1 545  PHE n 
1 546  GLU n 
1 547  GLN n 
1 548  ALA n 
1 549  PRO n 
1 550  GLU n 
1 551  PHE n 
1 552  LEU n 
1 553  LEU n 
1 554  GLY n 
1 555  ASP n 
1 556  GLY n 
1 557  SER n 
1 558  PHE n 
1 559  GLY n 
1 560  SER n 
1 561  VAL n 
1 562  TYR n 
1 563  ARG n 
1 564  ALA n 
1 565  ALA n 
1 566  TYR n 
1 567  GLU n 
1 568  GLY n 
1 569  GLU n 
1 570  GLU n 
1 571  VAL n 
1 572  ALA n 
1 573  VAL n 
1 574  LYS n 
1 575  ILE n 
1 576  PHE n 
1 577  ASN n 
1 578  LYS n 
1 579  HIS n 
1 580  THR n 
1 581  SER n 
1 582  LEU n 
1 583  ARG n 
1 584  LEU n 
1 585  LEU n 
1 586  ARG n 
1 587  GLN n 
1 588  GLU n 
1 589  LEU n 
1 590  VAL n 
1 591  VAL n 
1 592  LEU n 
1 593  CYS n 
1 594  HIS n 
1 595  LEU n 
1 596  HIS n 
1 597  HIS n 
1 598  PRO n 
1 599  SER n 
1 600  LEU n 
1 601  ILE n 
1 602  SER n 
1 603  LEU n 
1 604  LEU n 
1 605  ALA n 
1 606  ALA n 
1 607  GLY n 
1 608  ILE n 
1 609  ARG n 
1 610  PRO n 
1 611  ARG n 
1 612  MET n 
1 613  LEU n 
1 614  VAL n 
1 615  MET n 
1 616  GLU n 
1 617  LEU n 
1 618  ALA n 
1 619  SER n 
1 620  LYS n 
1 621  GLY n 
1 622  SER n 
1 623  LEU n 
1 624  ASP n 
1 625  ARG n 
1 626  LEU n 
1 627  LEU n 
1 628  GLN n 
1 629  GLN n 
1 630  ASP n 
1 631  LYS n 
1 632  ALA n 
1 633  SER n 
1 634  LEU n 
1 635  THR n 
1 636  ARG n 
1 637  THR n 
1 638  LEU n 
1 639  GLN n 
1 640  HIS n 
1 641  ARG n 
1 642  ILE n 
1 643  ALA n 
1 644  LEU n 
1 645  HIS n 
1 646  VAL n 
1 647  ALA n 
1 648  ASP n 
1 649  GLY n 
1 650  LEU n 
1 651  ARG n 
1 652  TYR n 
1 653  LEU n 
1 654  HIS n 
1 655  SER n 
1 656  ALA n 
1 657  MET n 
1 658  ILE n 
1 659  ILE n 
1 660  TYR n 
1 661  ARG n 
1 662  ASP n 
1 663  LEU n 
1 664  LYS n 
1 665  PRO n 
1 666  HIS n 
1 667  ASN n 
1 668  VAL n 
1 669  LEU n 
1 670  LEU n 
1 671  PHE n 
1 672  THR n 
1 673  LEU n 
1 674  TYR n 
1 675  PRO n 
1 676  ASN n 
1 677  ALA n 
1 678  ALA n 
1 679  ILE n 
1 680  ILE n 
1 681  ALA n 
1 682  LYS n 
1 683  ILE n 
1 684  ALA n 
1 685  ASP n 
1 686  TYR n 
1 687  GLY n 
1 688  ILE n 
1 689  ALA n 
1 690  GLN n 
1 691  TYR n 
1 692  CYS n 
1 693  CYS n 
1 694  ARG n 
1 695  MET n 
1 696  GLY n 
1 697  ILE n 
1 698  LYS n 
1 699  THR n 
1 700  SER n 
1 701  GLU n 
1 702  GLY n 
1 703  THR n 
1 704  PRO n 
1 705  GLY n 
1 706  PHE n 
1 707  ARG n 
1 708  ALA n 
1 709  PRO n 
1 710  GLU n 
1 711  VAL n 
1 712  ALA n 
1 713  ARG n 
1 714  GLY n 
1 715  ASN n 
1 716  VAL n 
1 717  ILE n 
1 718  TYR n 
1 719  ASN n 
1 720  GLN n 
1 721  GLN n 
1 722  ALA n 
1 723  ASP n 
1 724  VAL n 
1 725  TYR n 
1 726  SER n 
1 727  PHE n 
1 728  GLY n 
1 729  LEU n 
1 730  LEU n 
1 731  LEU n 
1 732  TYR n 
1 733  ASP n 
1 734  ILE n 
1 735  LEU n 
1 736  THR n 
1 737  THR n 
1 738  GLY n 
1 739  GLY n 
1 740  ARG n 
1 741  ILE n 
1 742  VAL n 
1 743  GLU n 
1 744  GLY n 
1 745  LEU n 
1 746  LYS n 
1 747  PHE n 
1 748  PRO n 
1 749  ASN n 
1 750  GLU n 
1 751  PHE n 
1 752  ASP n 
1 753  GLU n 
1 754  LEU n 
1 755  GLU n 
1 756  ILE n 
1 757  GLN n 
1 758  GLY n 
1 759  LYS n 
1 760  LEU n 
1 761  PRO n 
1 762  ASP n 
1 763  PRO n 
1 764  VAL n 
1 765  LYS n 
1 766  GLU n 
1 767  TYR n 
1 768  GLY n 
1 769  CYS n 
1 770  ALA n 
1 771  PRO n 
1 772  TRP n 
1 773  PRO n 
1 774  MET n 
1 775  VAL n 
1 776  GLU n 
1 777  LYS n 
1 778  LEU n 
1 779  ILE n 
1 780  LYS n 
1 781  GLN n 
1 782  CYS n 
1 783  LEU n 
1 784  LYS n 
1 785  GLU n 
1 786  ASN n 
1 787  PRO n 
1 788  GLN n 
1 789  GLU n 
1 790  ARG n 
1 791  PRO n 
1 792  THR n 
1 793  SER n 
1 794  ALA n 
1 795  GLN n 
1 796  VAL n 
1 797  PHE n 
1 798  ASP n 
1 799  ILE n 
1 800  LEU n 
1 801  ASN n 
1 802  SER n 
1 803  ALA n 
1 804  GLU n 
1 805  LEU n 
1 806  VAL n 
1 807  CYS n 
1 808  LEU n 
1 809  THR n 
1 810  ARG n 
1 811  ARG n 
1 812  ILE n 
1 813  LEU n 
1 814  LEU n 
1 815  PRO n 
1 816  LYS n 
1 817  ASN n 
1 818  VAL n 
1 819  ILE n 
1 820  VAL n 
1 821  GLU n 
1 822  CYS n 
1 823  MET n 
1 824  VAL n 
1 825  ALA n 
1 826  THR n 
1 827  HIS n 
1 828  HIS n 
1 829  ASN n 
1 830  SER n 
1 831  ARG n 
1 832  ASN n 
1 833  ALA n 
1 834  SER n 
1 835  ILE n 
1 836  TRP n 
1 837  LEU n 
1 838  GLY n 
1 839  CYS n 
1 840  GLY n 
1 841  HIS n 
1 842  THR n 
1 843  ASP n 
1 844  ARG n 
1 845  GLY n 
1 846  GLN n 
1 847  LEU n 
1 848  SER n 
1 849  PHE n 
1 850  LEU n 
1 851  ASP n 
1 852  LEU n 
1 853  ASN n 
1 854  THR n 
1 855  GLU n 
1 856  GLY n 
1 857  TYR n 
1 858  THR n 
1 859  SER n 
1 860  GLU n 
1 861  GLU n 
1 862  VAL n 
1 863  ALA n 
1 864  ASP n 
1 865  SER n 
1 866  ARG n 
1 867  ILE n 
1 868  LEU n 
1 869  CYS n 
1 870  LEU n 
1 871  ALA n 
1 872  LEU n 
1 873  VAL n 
1 874  HIS n 
1 875  LEU n 
1 876  PRO n 
1 877  VAL n 
1 878  GLU n 
1 879  LYS n 
1 880  GLU n 
1 881  SER n 
1 882  TRP n 
1 883  ILE n 
1 884  VAL n 
1 885  SER n 
1 886  GLY n 
1 887  THR n 
1 888  GLN n 
1 889  SER n 
1 890  GLY n 
1 891  THR n 
1 892  LEU n 
1 893  LEU n 
1 894  VAL n 
1 895  ILE n 
1 896  ASN n 
1 897  THR n 
1 898  GLU n 
1 899  ASP n 
1 900  GLY n 
1 901  LYS n 
1 902  LYS n 
1 903  ARG n 
1 904  HIS n 
1 905  THR n 
1 906  LEU n 
1 907  GLU n 
1 908  LYS n 
1 909  MET n 
1 910  THR n 
1 911  ASP n 
1 912  SER n 
1 913  VAL n 
1 914  THR n 
1 915  CYS n 
1 916  LEU n 
1 917  TYR n 
1 918  CYS n 
1 919  ASN n 
1 920  SER n 
1 921  PHE n 
1 922  SER n 
1 923  LYS n 
1 924  GLN n 
1 925  SER n 
1 926  LYS n 
1 927  GLN n 
1 928  LYS n 
1 929  ASN n 
1 930  PHE n 
1 931  LEU n 
1 932  LEU n 
1 933  VAL n 
1 934  GLY n 
1 935  THR n 
1 936  ALA n 
1 937  ASP n 
1 938  GLY n 
1 939  LYS n 
1 940  LEU n 
1 941  ALA n 
1 942  ILE n 
1 943  PHE n 
1 944  GLU n 
1 945  ASP n 
1 946  LYS n 
1 947  THR n 
1 948  VAL n 
1 949  LYS n 
1 950  LEU n 
1 951  LYS n 
1 952  GLY n 
1 953  ALA n 
1 954  ALA n 
1 955  PRO n 
1 956  LEU n 
1 957  LYS n 
1 958  ILE n 
1 959  LEU n 
1 960  ASN n 
1 961  ILE n 
1 962  GLY n 
1 963  ASN n 
1 964  VAL n 
1 965  SER n 
1 966  THR n 
1 967  PRO n 
1 968  LEU n 
1 969  MET n 
1 970  CYS n 
1 971  LEU n 
1 972  SER n 
1 973  GLU n 
1 974  SER n 
1 975  THR n 
1 976  ASN n 
1 977  SER n 
1 978  THR n 
1 979  GLU n 
1 980  ARG n 
1 981  ASN n 
1 982  VAL n 
1 983  MET n 
1 984  TRP n 
1 985  GLY n 
1 986  GLY n 
1 987  CYS n 
1 988  GLY n 
1 989  THR n 
1 990  LYS n 
1 991  ILE n 
1 992  PHE n 
1 993  SER n 
1 994  PHE n 
1 995  SER n 
1 996  ASN n 
1 997  ASP n 
1 998  PHE n 
1 999  THR n 
1 1000 ILE n 
1 1001 GLN n 
1 1002 LYS n 
1 1003 LEU n 
1 1004 ILE n 
1 1005 GLU n 
1 1006 THR n 
1 1007 ARG n 
1 1008 THR n 
1 1009 SER n 
1 1010 GLN n 
1 1011 LEU n 
1 1012 PHE n 
1 1013 SER n 
1 1014 TYR n 
1 1015 ALA n 
1 1016 ALA n 
1 1017 PHE n 
1 1018 SER n 
1 1019 ASP n 
1 1020 SER n 
1 1021 ASN n 
1 1022 ILE n 
1 1023 ILE n 
1 1024 THR n 
1 1025 VAL n 
1 1026 VAL n 
1 1027 VAL n 
1 1028 ASP n 
1 1029 THR n 
1 1030 ALA n 
1 1031 LEU n 
1 1032 TYR n 
1 1033 ILE n 
1 1034 ALA n 
1 1035 LYS n 
1 1036 GLN n 
1 1037 ASN n 
1 1038 SER n 
1 1039 PRO n 
1 1040 VAL n 
1 1041 VAL n 
1 1042 GLU n 
1 1043 VAL n 
1 1044 TRP n 
1 1045 ASP n 
1 1046 LYS n 
1 1047 LYS n 
1 1048 THR n 
1 1049 GLU n 
1 1050 LYS n 
1 1051 LEU n 
1 1052 CYS n 
1 1053 GLY n 
1 1054 LEU n 
1 1055 ILE n 
1 1056 ASP n 
1 1057 CYS n 
1 1058 VAL n 
1 1059 HIS n 
1 1060 PHE n 
1 1061 LEU n 
1 1062 ARG n 
1 1063 GLU n 
1 1064 VAL n 
1 1065 MET n 
1 1066 VAL n 
1 1067 LYS n 
1 1068 GLU n 
1 1069 ASN n 
1 1070 LYS n 
1 1071 GLU n 
1 1072 SER n 
1 1073 LYS n 
1 1074 HIS n 
1 1075 LYS n 
1 1076 MET n 
1 1077 SER n 
1 1078 TYR n 
1 1079 SER n 
1 1080 GLY n 
1 1081 ARG n 
1 1082 VAL n 
1 1083 LYS n 
1 1084 THR n 
1 1085 LEU n 
1 1086 CYS n 
1 1087 LEU n 
1 1088 GLN n 
1 1089 LYS n 
1 1090 ASN n 
1 1091 THR n 
1 1092 ALA n 
1 1093 LEU n 
1 1094 TRP n 
1 1095 ILE n 
1 1096 GLY n 
1 1097 THR n 
1 1098 GLY n 
1 1099 GLY n 
1 1100 GLY n 
1 1101 HIS n 
1 1102 ILE n 
1 1103 LEU n 
1 1104 LEU n 
1 1105 LEU n 
1 1106 ASP n 
1 1107 LEU n 
1 1108 SER n 
1 1109 THR n 
1 1110 ARG n 
1 1111 ARG n 
1 1112 LEU n 
1 1113 ILE n 
1 1114 ARG n 
1 1115 VAL n 
1 1116 ILE n 
1 1117 TYR n 
1 1118 ASN n 
1 1119 PHE n 
1 1120 CYS n 
1 1121 ASN n 
1 1122 SER n 
1 1123 VAL n 
1 1124 ARG n 
1 1125 VAL n 
1 1126 MET n 
1 1127 MET n 
1 1128 THR n 
1 1129 ALA n 
1 1130 GLN n 
1 1131 LEU n 
1 1132 GLY n 
1 1133 SER n 
1 1134 LEU n 
1 1135 LYS n 
1 1136 ASN n 
1 1137 VAL n 
1 1138 MET n 
1 1139 LEU n 
1 1140 VAL n 
1 1141 LEU n 
1 1142 GLY n 
1 1143 TYR n 
1 1144 ASN n 
1 1145 ARG n 
1 1146 LYS n 
1 1147 ASN n 
1 1148 THR n 
1 1149 GLU n 
1 1150 GLY n 
1 1151 THR n 
1 1152 GLN n 
1 1153 LYS n 
1 1154 GLN n 
1 1155 LYS n 
1 1156 GLU n 
1 1157 ILE n 
1 1158 GLN n 
1 1159 SER n 
1 1160 CYS n 
1 1161 LEU n 
1 1162 THR n 
1 1163 VAL n 
1 1164 TRP n 
1 1165 ASP n 
1 1166 ILE n 
1 1167 ASN n 
1 1168 LEU n 
1 1169 PRO n 
1 1170 HIS n 
1 1171 GLU n 
1 1172 VAL n 
1 1173 GLN n 
1 1174 ASN n 
1 1175 LEU n 
1 1176 GLU n 
1 1177 LYS n 
1 1178 HIS n 
1 1179 ILE n 
1 1180 GLU n 
1 1181 VAL n 
1 1182 ARG n 
1 1183 LYS n 
1 1184 GLU n 
1 1185 LEU n 
1 1186 ALA n 
1 1187 GLU n 
1 1188 LYS n 
1 1189 MET n 
1 1190 ARG n 
1 1191 ARG n 
1 1192 THR n 
1 1193 SER n 
1 1194 VAL n 
1 1195 GLU n 
2 1    MET n 
2 2    ARG n 
2 3    GLY n 
2 4    SER n 
2 5    HIS n 
2 6    HIS n 
2 7    HIS n 
2 8    HIS n 
2 9    HIS n 
2 10   HIS n 
2 11   HIS n 
2 12   HIS n 
2 13   GLY n 
2 14   SER n 
2 15   ASP n 
2 16   LEU n 
2 17   GLY n 
2 18   LYS n 
2 19   LYS n 
2 20   LEU n 
2 21   LEU n 
2 22   GLU n 
2 23   ALA n 
2 24   ALA n 
2 25   ARG n 
2 26   ALA n 
2 27   GLY n 
2 28   GLN n 
2 29   ASP n 
2 30   ASP n 
2 31   GLU n 
2 32   VAL n 
2 33   ARG n 
2 34   ILE n 
2 35   LEU n 
2 36   MET n 
2 37   ALA n 
2 38   ASN n 
2 39   GLY n 
2 40   ALA n 
2 41   ASP n 
2 42   VAL n 
2 43   ASN n 
2 44   ALA n 
2 45   THR n 
2 46   ASP n 
2 47   GLU n 
2 48   ALA n 
2 49   GLY n 
2 50   VAL n 
2 51   THR n 
2 52   PRO n 
2 53   LEU n 
2 54   HIS n 
2 55   LEU n 
2 56   ALA n 
2 57   ALA n 
2 58   ASP n 
2 59   SER n 
2 60   GLY n 
2 61   HIS n 
2 62   LEU n 
2 63   GLU n 
2 64   ILE n 
2 65   VAL n 
2 66   GLU n 
2 67   VAL n 
2 68   LEU n 
2 69   LEU n 
2 70   LYS n 
2 71   THR n 
2 72   GLY n 
2 73   ALA n 
2 74   ASP n 
2 75   VAL n 
2 76   ASN n 
2 77   ALA n 
2 78   TRP n 
2 79   ASP n 
2 80   HIS n 
2 81   TYR n 
2 82   GLY n 
2 83   PHE n 
2 84   THR n 
2 85   PRO n 
2 86   LEU n 
2 87   HIS n 
2 88   LEU n 
2 89   ALA n 
2 90   ALA n 
2 91   HIS n 
2 92   VAL n 
2 93   GLY n 
2 94   HIS n 
2 95   LEU n 
2 96   GLU n 
2 97   ILE n 
2 98   VAL n 
2 99   GLU n 
2 100  VAL n 
2 101  LEU n 
2 102  LEU n 
2 103  LYS n 
2 104  ALA n 
2 105  GLY n 
2 106  ALA n 
2 107  ASP n 
2 108  VAL n 
2 109  ASN n 
2 110  ALA n 
2 111  GLN n 
2 112  ASP n 
2 113  HIS n 
2 114  ALA n 
2 115  GLY n 
2 116  TRP n 
2 117  THR n 
2 118  PRO n 
2 119  LEU n 
2 120  HIS n 
2 121  LEU n 
2 122  ALA n 
2 123  ALA n 
2 124  LEU n 
2 125  TYR n 
2 126  GLY n 
2 127  HIS n 
2 128  LEU n 
2 129  GLU n 
2 130  ILE n 
2 131  VAL n 
2 132  GLU n 
2 133  VAL n 
2 134  LEU n 
2 135  LEU n 
2 136  LYS n 
2 137  HIS n 
2 138  GLY n 
2 139  ALA n 
2 140  ASP n 
2 141  VAL n 
2 142  ASN n 
2 143  ALA n 
2 144  GLN n 
2 145  ASP n 
2 146  MET n 
2 147  TRP n 
2 148  GLY n 
2 149  GLU n 
2 150  THR n 
2 151  PRO n 
2 152  PHE n 
2 153  ASP n 
2 154  LEU n 
2 155  ALA n 
2 156  ILE n 
2 157  ASP n 
2 158  ASN n 
2 159  GLY n 
2 160  ASN n 
2 161  GLU n 
2 162  ASP n 
2 163  ILE n 
2 164  ALA n 
2 165  GLU n 
2 166  VAL n 
2 167  LEU n 
2 168  GLN n 
2 169  LYS n 
2 170  ALA n 
2 171  ALA n 
2 172  LYS n 
2 173  LEU n 
2 174  ASN n 
2 175  ASP n 
2 176  TYR n 
2 177  LYS n 
2 178  ASP n 
2 179  ASP n 
2 180  ASP n 
2 181  ASP n 
2 182  LYS 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 1195 human ? 'LRRK2, PARK8' ? ? ? ? ? ? 'Homo sapiens'        9606  ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? Baculovirus ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 182  ?     ? ?              ? ? ? ? ? ? 'synthetic construct' 32630 ? ? ? ? ? ? ? ? 
'Escherichia coli'      562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ?           ? ? ? ? ? ? 
# 
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 
A1A7Q non-polymer         . 
;N-[3-tert-butyl-1-(4-methylphenyl)-1H-pyrazol-5-yl]-N'-{(3M)-3-[2-chloro-4-(morpholin-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-5-yl]phenyl}urea
;
? 'C31 H33 Cl N8 O2' 585.099 
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    ASN 1    1333 ?    ?   ?   A . n 
A 1 2    ARG 2    1334 1334 ARG ARG A . n 
A 1 3    MET 3    1335 1335 MET MET A . n 
A 1 4    LYS 4    1336 1336 LYS LYS A . n 
A 1 5    LEU 5    1337 1337 LEU LEU A . n 
A 1 6    MET 6    1338 1338 MET MET A . n 
A 1 7    ILE 7    1339 1339 ILE ILE A . n 
A 1 8    VAL 8    1340 1340 VAL VAL A . n 
A 1 9    GLY 9    1341 1341 GLY GLY A . n 
A 1 10   ASN 10   1342 1342 ASN ASN A . n 
A 1 11   THR 11   1343 1343 THR THR A . n 
A 1 12   GLY 12   1344 1344 GLY GLY A . n 
A 1 13   SER 13   1345 1345 SER SER A . n 
A 1 14   GLY 14   1346 1346 GLY GLY A . n 
A 1 15   LYS 15   1347 1347 LYS LYS A . n 
A 1 16   THR 16   1348 1348 THR THR A . n 
A 1 17   THR 17   1349 1349 THR THR A . n 
A 1 18   LEU 18   1350 1350 LEU LEU A . n 
A 1 19   LEU 19   1351 1351 LEU LEU A . n 
A 1 20   GLN 20   1352 1352 GLN GLN A . n 
A 1 21   GLN 21   1353 1353 GLN GLN A . n 
A 1 22   LEU 22   1354 1354 LEU LEU A . n 
A 1 23   MET 23   1355 1355 MET MET A . n 
A 1 24   LYS 24   1356 ?    ?   ?   A . n 
A 1 25   THR 25   1357 ?    ?   ?   A . n 
A 1 26   LYS 26   1358 ?    ?   ?   A . n 
A 1 27   LYS 27   1359 ?    ?   ?   A . n 
A 1 28   SER 28   1360 ?    ?   ?   A . n 
A 1 29   ASP 29   1361 ?    ?   ?   A . n 
A 1 30   LEU 30   1362 ?    ?   ?   A . n 
A 1 31   GLY 31   1363 ?    ?   ?   A . n 
A 1 32   MET 32   1364 ?    ?   ?   A . n 
A 1 33   GLN 33   1365 ?    ?   ?   A . n 
A 1 34   SER 34   1366 ?    ?   ?   A . n 
A 1 35   ALA 35   1367 ?    ?   ?   A . n 
A 1 36   THR 36   1368 ?    ?   ?   A . n 
A 1 37   VAL 37   1369 ?    ?   ?   A . n 
A 1 38   GLY 38   1370 1370 GLY GLY A . n 
A 1 39   ILE 39   1371 1371 ILE ILE A . n 
A 1 40   ASP 40   1372 1372 ASP ASP A . n 
A 1 41   VAL 41   1373 1373 VAL VAL A . n 
A 1 42   LYS 42   1374 1374 LYS LYS A . n 
A 1 43   ASP 43   1375 1375 ASP ASP A . n 
A 1 44   TRP 44   1376 1376 TRP TRP A . n 
A 1 45   PRO 45   1377 1377 PRO PRO A . n 
A 1 46   ILE 46   1378 1378 ILE ILE A . n 
A 1 47   GLN 47   1379 ?    ?   ?   A . n 
A 1 48   ILE 48   1380 ?    ?   ?   A . n 
A 1 49   ARG 49   1381 ?    ?   ?   A . n 
A 1 50   ASP 50   1382 ?    ?   ?   A . n 
A 1 51   LYS 51   1383 ?    ?   ?   A . n 
A 1 52   ARG 52   1384 ?    ?   ?   A . n 
A 1 53   LYS 53   1385 ?    ?   ?   A . n 
A 1 54   ARG 54   1386 ?    ?   ?   A . n 
A 1 55   ASP 55   1387 ?    ?   ?   A . n 
A 1 56   LEU 56   1388 1388 LEU LEU A . n 
A 1 57   VAL 57   1389 1389 VAL VAL A . n 
A 1 58   LEU 58   1390 1390 LEU LEU A . n 
A 1 59   ASN 59   1391 1391 ASN ASN A . n 
A 1 60   VAL 60   1392 1392 VAL VAL A . n 
A 1 61   TRP 61   1393 1393 TRP TRP A . n 
A 1 62   ASP 62   1394 1394 ASP ASP A . n 
A 1 63   PHE 63   1395 1395 PHE PHE A . n 
A 1 64   ALA 64   1396 1396 ALA ALA A . n 
A 1 65   GLY 65   1397 1397 GLY GLY A . n 
A 1 66   ARG 66   1398 1398 ARG ARG A . n 
A 1 67   GLU 67   1399 1399 GLU GLU A . n 
A 1 68   GLU 68   1400 1400 GLU GLU A . n 
A 1 69   PHE 69   1401 1401 PHE PHE A . n 
A 1 70   TYR 70   1402 1402 TYR TYR A . n 
A 1 71   SER 71   1403 1403 SER SER A . n 
A 1 72   THR 72   1404 1404 THR THR A . n 
A 1 73   HIS 73   1405 1405 HIS HIS A . n 
A 1 74   PRO 74   1406 1406 PRO PRO A . n 
A 1 75   HIS 75   1407 ?    ?   ?   A . n 
A 1 76   PHE 76   1408 ?    ?   ?   A . n 
A 1 77   MET 77   1409 ?    ?   ?   A . n 
A 1 78   THR 78   1410 ?    ?   ?   A . n 
A 1 79   GLN 79   1411 ?    ?   ?   A . n 
A 1 80   ARG 80   1412 ?    ?   ?   A . n 
A 1 81   ALA 81   1413 ?    ?   ?   A . n 
A 1 82   LEU 82   1414 1414 LEU LEU A . n 
A 1 83   TYR 83   1415 1415 TYR TYR A . n 
A 1 84   LEU 84   1416 1416 LEU LEU A . n 
A 1 85   ALA 85   1417 1417 ALA ALA A . n 
A 1 86   VAL 86   1418 1418 VAL VAL A . n 
A 1 87   TYR 87   1419 1419 TYR TYR A . n 
A 1 88   ASP 88   1420 1420 ASP ASP A . n 
A 1 89   LEU 89   1421 1421 LEU LEU A . n 
A 1 90   SER 90   1422 1422 SER SER A . n 
A 1 91   LYS 91   1423 1423 LYS LYS A . n 
A 1 92   GLY 92   1424 1424 GLY GLY A . n 
A 1 93   GLN 93   1425 1425 GLN GLN A . n 
A 1 94   ALA 94   1426 1426 ALA ALA A . n 
A 1 95   GLU 95   1427 1427 GLU GLU A . n 
A 1 96   VAL 96   1428 1428 VAL VAL A . n 
A 1 97   ASP 97   1429 1429 ASP ASP A . n 
A 1 98   ALA 98   1430 1430 ALA ALA A . n 
A 1 99   MET 99   1431 1431 MET MET A . n 
A 1 100  LYS 100  1432 1432 LYS LYS A . n 
A 1 101  PRO 101  1433 1433 PRO PRO A . n 
A 1 102  TRP 102  1434 1434 TRP TRP A . n 
A 1 103  LEU 103  1435 1435 LEU LEU A . n 
A 1 104  PHE 104  1436 1436 PHE PHE A . n 
A 1 105  ASN 105  1437 1437 ASN ASN A . n 
A 1 106  ILE 106  1438 1438 ILE ILE A . n 
A 1 107  LYS 107  1439 1439 LYS LYS A . n 
A 1 108  ALA 108  1440 1440 ALA ALA A . n 
A 1 109  ARG 109  1441 ?    ?   ?   A . n 
A 1 110  ALA 110  1442 ?    ?   ?   A . n 
A 1 111  SER 111  1443 ?    ?   ?   A . n 
A 1 112  SER 112  1444 ?    ?   ?   A . n 
A 1 113  SER 113  1445 ?    ?   ?   A . n 
A 1 114  PRO 114  1446 1446 PRO PRO A . n 
A 1 115  VAL 115  1447 1447 VAL VAL A . n 
A 1 116  ILE 116  1448 1448 ILE ILE A . n 
A 1 117  LEU 117  1449 1449 LEU LEU A . n 
A 1 118  VAL 118  1450 1450 VAL VAL A . n 
A 1 119  GLY 119  1451 1451 GLY GLY A . n 
A 1 120  THR 120  1452 1452 THR THR A . n 
A 1 121  HIS 121  1453 1453 HIS HIS A . n 
A 1 122  LEU 122  1454 1454 LEU LEU A . n 
A 1 123  ASP 123  1455 1455 ASP ASP A . n 
A 1 124  VAL 124  1456 1456 VAL VAL A . n 
A 1 125  SER 125  1457 ?    ?   ?   A . n 
A 1 126  ASP 126  1458 ?    ?   ?   A . n 
A 1 127  GLU 127  1459 ?    ?   ?   A . n 
A 1 128  LYS 128  1460 ?    ?   ?   A . n 
A 1 129  GLN 129  1461 1461 GLN GLN A . n 
A 1 130  ARG 130  1462 1462 ARG ARG A . n 
A 1 131  LYS 131  1463 1463 LYS LYS A . n 
A 1 132  ALA 132  1464 1464 ALA ALA A . n 
A 1 133  CYS 133  1465 1465 CYS CYS A . n 
A 1 134  MET 134  1466 1466 MET MET A . n 
A 1 135  SER 135  1467 1467 SER SER A . n 
A 1 136  LYS 136  1468 1468 LYS LYS A . n 
A 1 137  ILE 137  1469 1469 ILE ILE A . n 
A 1 138  THR 138  1470 1470 THR THR A . n 
A 1 139  LYS 139  1471 1471 LYS LYS A . n 
A 1 140  GLU 140  1472 1472 GLU GLU A . n 
A 1 141  LEU 141  1473 1473 LEU LEU A . n 
A 1 142  LEU 142  1474 1474 LEU LEU A . n 
A 1 143  ASN 143  1475 1475 ASN ASN A . n 
A 1 144  LYS 144  1476 1476 LYS LYS A . n 
A 1 145  ARG 145  1477 1477 ARG ARG A . n 
A 1 146  GLY 146  1478 1478 GLY GLY A . n 
A 1 147  PHE 147  1479 1479 PHE PHE A . n 
A 1 148  PRO 148  1480 1480 PRO PRO A . n 
A 1 149  ALA 149  1481 1481 ALA ALA A . n 
A 1 150  ILE 150  1482 1482 ILE ILE A . n 
A 1 151  ARG 151  1483 1483 ARG ARG A . n 
A 1 152  ASP 152  1484 1484 ASP ASP A . n 
A 1 153  TYR 153  1485 1485 TYR TYR A . n 
A 1 154  HIS 154  1486 1486 HIS HIS A . n 
A 1 155  PHE 155  1487 1487 PHE PHE A . n 
A 1 156  VAL 156  1488 1488 VAL VAL A . n 
A 1 157  ASN 157  1489 1489 ASN ASN A . n 
A 1 158  ALA 158  1490 1490 ALA ALA A . n 
A 1 159  THR 159  1491 1491 THR THR A . n 
A 1 160  GLU 160  1492 1492 GLU GLU A . n 
A 1 161  GLU 161  1493 1493 GLU GLU A . n 
A 1 162  SER 162  1494 1494 SER SER A . n 
A 1 163  ASP 163  1495 1495 ASP ASP A . n 
A 1 164  ALA 164  1496 1496 ALA ALA A . n 
A 1 165  LEU 165  1497 1497 LEU LEU A . n 
A 1 166  ALA 166  1498 1498 ALA ALA A . n 
A 1 167  LYS 167  1499 1499 LYS LYS A . n 
A 1 168  LEU 168  1500 1500 LEU LEU A . n 
A 1 169  ARG 169  1501 1501 ARG ARG A . n 
A 1 170  LYS 170  1502 1502 LYS LYS A . n 
A 1 171  THR 171  1503 1503 THR THR A . n 
A 1 172  ILE 172  1504 1504 ILE ILE A . n 
A 1 173  ILE 173  1505 1505 ILE ILE A . n 
A 1 174  ASN 174  1506 1506 ASN ASN A . n 
A 1 175  GLU 175  1507 1507 GLU GLU A . n 
A 1 176  SER 176  1508 1508 SER SER A . n 
A 1 177  LEU 177  1509 1509 LEU LEU A . n 
A 1 178  ASN 178  1510 1510 ASN ASN A . n 
A 1 179  PHE 179  1511 ?    ?   ?   A . n 
A 1 180  LYS 180  1512 ?    ?   ?   A . n 
A 1 181  ILE 181  1513 ?    ?   ?   A . n 
A 1 182  ARG 182  1514 ?    ?   ?   A . n 
A 1 183  ASP 183  1515 ?    ?   ?   A . n 
A 1 184  GLN 184  1516 ?    ?   ?   A . n 
A 1 185  LEU 185  1517 ?    ?   ?   A . n 
A 1 186  VAL 186  1518 ?    ?   ?   A . n 
A 1 187  VAL 187  1519 ?    ?   ?   A . n 
A 1 188  GLY 188  1520 ?    ?   ?   A . n 
A 1 189  GLN 189  1521 ?    ?   ?   A . n 
A 1 190  LEU 190  1522 ?    ?   ?   A . n 
A 1 191  ILE 191  1523 ?    ?   ?   A . n 
A 1 192  PRO 192  1524 ?    ?   ?   A . n 
A 1 193  ASP 193  1525 ?    ?   ?   A . n 
A 1 194  CYS 194  1526 ?    ?   ?   A . n 
A 1 195  TYR 195  1527 ?    ?   ?   A . n 
A 1 196  VAL 196  1528 1528 VAL VAL A . n 
A 1 197  GLU 197  1529 1529 GLU GLU A . n 
A 1 198  LEU 198  1530 1530 LEU LEU A . n 
A 1 199  GLU 199  1531 1531 GLU GLU A . n 
A 1 200  LYS 200  1532 1532 LYS LYS A . n 
A 1 201  ILE 201  1533 1533 ILE ILE A . n 
A 1 202  ILE 202  1534 1534 ILE ILE A . n 
A 1 203  LEU 203  1535 1535 LEU LEU A . n 
A 1 204  SER 204  1536 1536 SER SER A . n 
A 1 205  GLU 205  1537 1537 GLU GLU A . n 
A 1 206  ARG 206  1538 1538 ARG ARG A . n 
A 1 207  LYS 207  1539 1539 LYS LYS A . n 
A 1 208  ASN 208  1540 1540 ASN ASN A . n 
A 1 209  VAL 209  1541 1541 VAL VAL A . n 
A 1 210  PRO 210  1542 ?    ?   ?   A . n 
A 1 211  ILE 211  1543 ?    ?   ?   A . n 
A 1 212  GLU 212  1544 ?    ?   ?   A . n 
A 1 213  PHE 213  1545 ?    ?   ?   A . n 
A 1 214  PRO 214  1546 ?    ?   ?   A . n 
A 1 215  VAL 215  1547 ?    ?   ?   A . n 
A 1 216  ILE 216  1548 ?    ?   ?   A . n 
A 1 217  ASP 217  1549 ?    ?   ?   A . n 
A 1 218  ARG 218  1550 ?    ?   ?   A . n 
A 1 219  LYS 219  1551 ?    ?   ?   A . n 
A 1 220  ARG 220  1552 ?    ?   ?   A . n 
A 1 221  LEU 221  1553 ?    ?   ?   A . n 
A 1 222  LEU 222  1554 ?    ?   ?   A . n 
A 1 223  GLN 223  1555 ?    ?   ?   A . n 
A 1 224  LEU 224  1556 ?    ?   ?   A . n 
A 1 225  VAL 225  1557 ?    ?   ?   A . n 
A 1 226  ARG 226  1558 ?    ?   ?   A . n 
A 1 227  GLU 227  1559 ?    ?   ?   A . n 
A 1 228  ASN 228  1560 ?    ?   ?   A . n 
A 1 229  GLN 229  1561 ?    ?   ?   A . n 
A 1 230  LEU 230  1562 ?    ?   ?   A . n 
A 1 231  GLN 231  1563 ?    ?   ?   A . n 
A 1 232  LEU 232  1564 ?    ?   ?   A . n 
A 1 233  ASP 233  1565 ?    ?   ?   A . n 
A 1 234  GLU 234  1566 ?    ?   ?   A . n 
A 1 235  ASN 235  1567 ?    ?   ?   A . n 
A 1 236  GLU 236  1568 ?    ?   ?   A . n 
A 1 237  LEU 237  1569 ?    ?   ?   A . n 
A 1 238  PRO 238  1570 ?    ?   ?   A . n 
A 1 239  HIS 239  1571 ?    ?   ?   A . n 
A 1 240  ALA 240  1572 ?    ?   ?   A . n 
A 1 241  VAL 241  1573 ?    ?   ?   A . n 
A 1 242  HIS 242  1574 ?    ?   ?   A . n 
A 1 243  PHE 243  1575 1575 PHE PHE A . n 
A 1 244  LEU 244  1576 1576 LEU LEU A . n 
A 1 245  ASN 245  1577 1577 ASN ASN A . n 
A 1 246  GLU 246  1578 1578 GLU GLU A . n 
A 1 247  SER 247  1579 1579 SER SER A . n 
A 1 248  GLY 248  1580 1580 GLY GLY A . n 
A 1 249  VAL 249  1581 1581 VAL VAL A . n 
A 1 250  LEU 250  1582 1582 LEU LEU A . n 
A 1 251  LEU 251  1583 1583 LEU LEU A . n 
A 1 252  HIS 252  1584 ?    ?   ?   A . n 
A 1 253  PHE 253  1585 ?    ?   ?   A . n 
A 1 254  GLN 254  1586 ?    ?   ?   A . n 
A 1 255  ASP 255  1587 ?    ?   ?   A . n 
A 1 256  PRO 256  1588 ?    ?   ?   A . n 
A 1 257  ALA 257  1589 ?    ?   ?   A . n 
A 1 258  LEU 258  1590 ?    ?   ?   A . n 
A 1 259  GLN 259  1591 ?    ?   ?   A . n 
A 1 260  LEU 260  1592 ?    ?   ?   A . n 
A 1 261  SER 261  1593 ?    ?   ?   A . n 
A 1 262  ASP 262  1594 1594 ASP ASP A . n 
A 1 263  LEU 263  1595 1595 LEU LEU A . n 
A 1 264  TYR 264  1596 1596 TYR TYR A . n 
A 1 265  PHE 265  1597 1597 PHE PHE A . n 
A 1 266  VAL 266  1598 1598 VAL VAL A . n 
A 1 267  GLU 267  1599 1599 GLU GLU A . n 
A 1 268  PRO 268  1600 1600 PRO PRO A . n 
A 1 269  LYS 269  1601 1601 LYS LYS A . n 
A 1 270  TRP 270  1602 1602 TRP TRP A . n 
A 1 271  LEU 271  1603 1603 LEU LEU A . n 
A 1 272  CYS 272  1604 1604 CYS CYS A . n 
A 1 273  LYS 273  1605 1605 LYS LYS A . n 
A 1 274  ILE 274  1606 1606 ILE ILE A . n 
A 1 275  MET 275  1607 1607 MET MET A . n 
A 1 276  ALA 276  1608 1608 ALA ALA A . n 
A 1 277  GLN 277  1609 1609 GLN GLN A . n 
A 1 278  ILE 278  1610 1610 ILE ILE A . n 
A 1 279  LEU 279  1611 1611 LEU LEU A . n 
A 1 280  THR 280  1612 1612 THR THR A . n 
A 1 281  VAL 281  1613 1613 VAL VAL A . n 
A 1 282  LYS 282  1614 ?    ?   ?   A . n 
A 1 283  VAL 283  1615 ?    ?   ?   A . n 
A 1 284  GLU 284  1616 ?    ?   ?   A . n 
A 1 285  GLY 285  1617 ?    ?   ?   A . n 
A 1 286  CYS 286  1618 ?    ?   ?   A . n 
A 1 287  PRO 287  1619 ?    ?   ?   A . n 
A 1 288  LYS 288  1620 ?    ?   ?   A . n 
A 1 289  HIS 289  1621 ?    ?   ?   A . n 
A 1 290  PRO 290  1622 ?    ?   ?   A . n 
A 1 291  LYS 291  1623 ?    ?   ?   A . n 
A 1 292  GLY 292  1624 ?    ?   ?   A . n 
A 1 293  ILE 293  1625 ?    ?   ?   A . n 
A 1 294  ILE 294  1626 ?    ?   ?   A . n 
A 1 295  SER 295  1627 ?    ?   ?   A . n 
A 1 296  ARG 296  1628 ?    ?   ?   A . n 
A 1 297  ARG 297  1629 ?    ?   ?   A . n 
A 1 298  ASP 298  1630 ?    ?   ?   A . n 
A 1 299  VAL 299  1631 ?    ?   ?   A . n 
A 1 300  GLU 300  1632 ?    ?   ?   A . n 
A 1 301  LYS 301  1633 ?    ?   ?   A . n 
A 1 302  PHE 302  1634 ?    ?   ?   A . n 
A 1 303  LEU 303  1635 ?    ?   ?   A . n 
A 1 304  SER 304  1636 ?    ?   ?   A . n 
A 1 305  LYS 305  1637 ?    ?   ?   A . n 
A 1 306  LYS 306  1638 ?    ?   ?   A . n 
A 1 307  ARG 307  1639 1639 ARG ARG A . n 
A 1 308  LYS 308  1640 1640 LYS LYS A . n 
A 1 309  PHE 309  1641 1641 PHE PHE A . n 
A 1 310  PRO 310  1642 1642 PRO PRO A . n 
A 1 311  LYS 311  1643 1643 LYS LYS A . n 
A 1 312  ASN 312  1644 1644 ASN ASN A . n 
A 1 313  TYR 313  1645 1645 TYR TYR A . n 
A 1 314  MET 314  1646 1646 MET MET A . n 
A 1 315  SER 315  1647 1647 SER SER A . n 
A 1 316  GLN 316  1648 1648 GLN GLN A . n 
A 1 317  TYR 317  1649 1649 TYR TYR A . n 
A 1 318  PHE 318  1650 1650 PHE PHE A . n 
A 1 319  LYS 319  1651 1651 LYS LYS A . n 
A 1 320  LEU 320  1652 1652 LEU LEU A . n 
A 1 321  LEU 321  1653 1653 LEU LEU A . n 
A 1 322  GLU 322  1654 1654 GLU GLU A . n 
A 1 323  LYS 323  1655 1655 LYS LYS A . n 
A 1 324  PHE 324  1656 1656 PHE PHE A . n 
A 1 325  GLN 325  1657 1657 GLN GLN A . n 
A 1 326  ILE 326  1658 1658 ILE ILE A . n 
A 1 327  ALA 327  1659 1659 ALA ALA A . n 
A 1 328  LEU 328  1660 1660 LEU LEU A . n 
A 1 329  PRO 329  1661 ?    ?   ?   A . n 
A 1 330  ILE 330  1662 ?    ?   ?   A . n 
A 1 331  GLY 331  1663 ?    ?   ?   A . n 
A 1 332  GLU 332  1664 ?    ?   ?   A . n 
A 1 333  GLU 333  1665 ?    ?   ?   A . n 
A 1 334  TYR 334  1666 ?    ?   ?   A . n 
A 1 335  LEU 335  1667 ?    ?   ?   A . n 
A 1 336  LEU 336  1668 1668 LEU LEU A . n 
A 1 337  VAL 337  1669 1669 VAL VAL A . n 
A 1 338  PRO 338  1670 1670 PRO PRO A . n 
A 1 339  SER 339  1671 1671 SER SER A . n 
A 1 340  SER 340  1672 1672 SER SER A . n 
A 1 341  LEU 341  1673 1673 LEU LEU A . n 
A 1 342  SER 342  1674 1674 SER SER A . n 
A 1 343  ASP 343  1675 ?    ?   ?   A . n 
A 1 344  HIS 344  1676 ?    ?   ?   A . n 
A 1 345  ARG 345  1677 ?    ?   ?   A . n 
A 1 346  PRO 346  1678 ?    ?   ?   A . n 
A 1 347  VAL 347  1679 ?    ?   ?   A . n 
A 1 348  ILE 348  1680 ?    ?   ?   A . n 
A 1 349  GLU 349  1681 ?    ?   ?   A . n 
A 1 350  LEU 350  1682 ?    ?   ?   A . n 
A 1 351  PRO 351  1683 ?    ?   ?   A . n 
A 1 352  HIS 352  1684 1684 HIS HIS A . n 
A 1 353  CYS 353  1685 1685 CYS CYS A . n 
A 1 354  GLU 354  1686 1686 GLU GLU A . n 
A 1 355  ASN 355  1687 1687 ASN ASN A . n 
A 1 356  SER 356  1688 1688 SER SER A . n 
A 1 357  GLU 357  1689 1689 GLU GLU A . n 
A 1 358  ILE 358  1690 1690 ILE ILE A . n 
A 1 359  ILE 359  1691 1691 ILE ILE A . n 
A 1 360  ILE 360  1692 1692 ILE ILE A . n 
A 1 361  ARG 361  1693 1693 ARG ARG A . n 
A 1 362  LEU 362  1694 1694 LEU LEU A . n 
A 1 363  TYR 363  1695 1695 TYR TYR A . n 
A 1 364  GLU 364  1696 1696 GLU GLU A . n 
A 1 365  MET 365  1697 1697 MET MET A . n 
A 1 366  PRO 366  1698 1698 PRO PRO A . n 
A 1 367  TYR 367  1699 1699 TYR TYR A . n 
A 1 368  PHE 368  1700 1700 PHE PHE A . n 
A 1 369  PRO 369  1701 1701 PRO PRO A . n 
A 1 370  MET 370  1702 1702 MET MET A . n 
A 1 371  GLY 371  1703 1703 GLY GLY A . n 
A 1 372  PHE 372  1704 1704 PHE PHE A . n 
A 1 373  TRP 373  1705 1705 TRP TRP A . n 
A 1 374  SER 374  1706 1706 SER SER A . n 
A 1 375  ARG 375  1707 1707 ARG ARG A . n 
A 1 376  LEU 376  1708 1708 LEU LEU A . n 
A 1 377  ILE 377  1709 1709 ILE ILE A . n 
A 1 378  ASN 378  1710 1710 ASN ASN A . n 
A 1 379  ARG 379  1711 1711 ARG ARG A . n 
A 1 380  LEU 380  1712 1712 LEU LEU A . n 
A 1 381  LEU 381  1713 1713 LEU LEU A . n 
A 1 382  GLU 382  1714 1714 GLU GLU A . n 
A 1 383  ILE 383  1715 1715 ILE ILE A . n 
A 1 384  SER 384  1716 1716 SER SER A . n 
A 1 385  PRO 385  1717 1717 PRO PRO A . n 
A 1 386  TYR 386  1718 ?    ?   ?   A . n 
A 1 387  MET 387  1719 ?    ?   ?   A . n 
A 1 388  LEU 388  1720 ?    ?   ?   A . n 
A 1 389  SER 389  1721 ?    ?   ?   A . n 
A 1 390  GLY 390  1722 ?    ?   ?   A . n 
A 1 391  ARG 391  1723 ?    ?   ?   A . n 
A 1 392  GLU 392  1724 ?    ?   ?   A . n 
A 1 393  ARG 393  1725 ?    ?   ?   A . n 
A 1 394  ALA 394  1726 ?    ?   ?   A . n 
A 1 395  LEU 395  1727 ?    ?   ?   A . n 
A 1 396  ARG 396  1728 ?    ?   ?   A . n 
A 1 397  PRO 397  1729 ?    ?   ?   A . n 
A 1 398  ASN 398  1730 ?    ?   ?   A . n 
A 1 399  ARG 399  1731 1731 ARG ARG A . n 
A 1 400  MET 400  1732 1732 MET MET A . n 
A 1 401  TYR 401  1733 1733 TYR TYR A . n 
A 1 402  TRP 402  1734 1734 TRP TRP A . n 
A 1 403  ARG 403  1735 1735 ARG ARG A . n 
A 1 404  GLN 404  1736 1736 GLN GLN A . n 
A 1 405  GLY 405  1737 1737 GLY GLY A . n 
A 1 406  ILE 406  1738 1738 ILE ILE A . n 
A 1 407  TYR 407  1739 1739 TYR TYR A . n 
A 1 408  LEU 408  1740 1740 LEU LEU A . n 
A 1 409  ASN 409  1741 1741 ASN ASN A . n 
A 1 410  TRP 410  1742 1742 TRP TRP A . n 
A 1 411  SER 411  1743 1743 SER SER A . n 
A 1 412  PRO 412  1744 1744 PRO PRO A . n 
A 1 413  GLU 413  1745 1745 GLU GLU A . n 
A 1 414  ALA 414  1746 1746 ALA ALA A . n 
A 1 415  TYR 415  1747 1747 TYR TYR A . n 
A 1 416  CYS 416  1748 1748 CYS CYS A . n 
A 1 417  LEU 417  1749 1749 LEU LEU A . n 
A 1 418  VAL 418  1750 1750 VAL VAL A . n 
A 1 419  GLY 419  1751 1751 GLY GLY A . n 
A 1 420  SER 420  1752 1752 SER SER A . n 
A 1 421  GLU 421  1753 ?    ?   ?   A . n 
A 1 422  VAL 422  1754 ?    ?   ?   A . n 
A 1 423  LEU 423  1755 ?    ?   ?   A . n 
A 1 424  ASP 424  1756 ?    ?   ?   A . n 
A 1 425  ASN 425  1757 ?    ?   ?   A . n 
A 1 426  HIS 426  1758 ?    ?   ?   A . n 
A 1 427  PRO 427  1759 ?    ?   ?   A . n 
A 1 428  GLU 428  1760 1760 GLU GLU A . n 
A 1 429  SER 429  1761 1761 SER SER A . n 
A 1 430  PHE 430  1762 1762 PHE PHE A . n 
A 1 431  LEU 431  1763 1763 LEU LEU A . n 
A 1 432  LYS 432  1764 1764 LYS LYS A . n 
A 1 433  ILE 433  1765 1765 ILE ILE A . n 
A 1 434  THR 434  1766 1766 THR THR A . n 
A 1 435  VAL 435  1767 1767 VAL VAL A . n 
A 1 436  PRO 436  1768 1768 PRO PRO A . n 
A 1 437  SER 437  1769 1769 SER SER A . n 
A 1 438  CYS 438  1770 1770 CYS CYS A . n 
A 1 439  ARG 439  1771 1771 ARG ARG A . n 
A 1 440  LYS 440  1772 1772 LYS LYS A . n 
A 1 441  GLY 441  1773 1773 GLY GLY A . n 
A 1 442  CYS 442  1774 1774 CYS CYS A . n 
A 1 443  ILE 443  1775 1775 ILE ILE A . n 
A 1 444  LEU 444  1776 1776 LEU LEU A . n 
A 1 445  LEU 445  1777 1777 LEU LEU A . n 
A 1 446  GLY 446  1778 1778 GLY GLY A . n 
A 1 447  GLN 447  1779 1779 GLN GLN A . n 
A 1 448  VAL 448  1780 1780 VAL VAL A . n 
A 1 449  VAL 449  1781 1781 VAL VAL A . n 
A 1 450  ASP 450  1782 1782 ASP ASP A . n 
A 1 451  HIS 451  1783 1783 HIS HIS A . n 
A 1 452  ILE 452  1784 1784 ILE ILE A . n 
A 1 453  ASP 453  1785 1785 ASP ASP A . n 
A 1 454  SER 454  1786 1786 SER SER A . n 
A 1 455  LEU 455  1787 1787 LEU LEU A . n 
A 1 456  MET 456  1788 1788 MET MET A . n 
A 1 457  GLU 457  1789 1789 GLU GLU A . n 
A 1 458  GLU 458  1790 1790 GLU GLU A . n 
A 1 459  TRP 459  1791 1791 TRP TRP A . n 
A 1 460  PHE 460  1792 1792 PHE PHE A . n 
A 1 461  PRO 461  1793 1793 PRO PRO A . n 
A 1 462  GLY 462  1794 1794 GLY GLY A . n 
A 1 463  LEU 463  1795 ?    ?   ?   A . n 
A 1 464  LEU 464  1796 ?    ?   ?   A . n 
A 1 465  GLU 465  1797 ?    ?   ?   A . n 
A 1 466  ILE 466  1798 ?    ?   ?   A . n 
A 1 467  ASP 467  1799 ?    ?   ?   A . n 
A 1 468  ILE 468  1800 ?    ?   ?   A . n 
A 1 469  CYS 469  1801 ?    ?   ?   A . n 
A 1 470  GLY 470  1802 ?    ?   ?   A . n 
A 1 471  GLU 471  1803 ?    ?   ?   A . n 
A 1 472  GLY 472  1804 ?    ?   ?   A . n 
A 1 473  GLU 473  1805 ?    ?   ?   A . n 
A 1 474  THR 474  1806 1806 THR THR A . n 
A 1 475  LEU 475  1807 1807 LEU LEU A . n 
A 1 476  LEU 476  1808 1808 LEU LEU A . n 
A 1 477  LYS 477  1809 1809 LYS LYS A . n 
A 1 478  LYS 478  1810 1810 LYS LYS A . n 
A 1 479  TRP 479  1811 1811 TRP TRP A . n 
A 1 480  ALA 480  1812 1812 ALA ALA A . n 
A 1 481  LEU 481  1813 1813 LEU LEU A . n 
A 1 482  TYR 482  1814 1814 TYR TYR A . n 
A 1 483  SER 483  1815 1815 SER SER A . n 
A 1 484  PHE 484  1816 1816 PHE PHE A . n 
A 1 485  ASN 485  1817 1817 ASN ASN A . n 
A 1 486  ASP 486  1818 1818 ASP ASP A . n 
A 1 487  GLY 487  1819 1819 GLY GLY A . n 
A 1 488  GLU 488  1820 1820 GLU GLU A . n 
A 1 489  GLU 489  1821 1821 GLU GLU A . n 
A 1 490  HIS 490  1822 1822 HIS HIS A . n 
A 1 491  GLN 491  1823 1823 GLN GLN A . n 
A 1 492  LYS 492  1824 1824 LYS LYS A . n 
A 1 493  ILE 493  1825 1825 ILE ILE A . n 
A 1 494  LEU 494  1826 1826 LEU LEU A . n 
A 1 495  LEU 495  1827 1827 LEU LEU A . n 
A 1 496  ASP 496  1828 1828 ASP ASP A . n 
A 1 497  ASP 497  1829 1829 ASP ASP A . n 
A 1 498  LEU 498  1830 1830 LEU LEU A . n 
A 1 499  MET 499  1831 1831 MET MET A . n 
A 1 500  LYS 500  1832 1832 LYS LYS A . n 
A 1 501  LYS 501  1833 1833 LYS LYS A . n 
A 1 502  ALA 502  1834 1834 ALA ALA A . n 
A 1 503  GLU 503  1835 1835 GLU GLU A . n 
A 1 504  GLU 504  1836 1836 GLU GLU A . n 
A 1 505  GLY 505  1837 1837 GLY GLY A . n 
A 1 506  ASP 506  1838 1838 ASP ASP A . n 
A 1 507  LEU 507  1839 1839 LEU LEU A . n 
A 1 508  LEU 508  1840 1840 LEU LEU A . n 
A 1 509  VAL 509  1841 1841 VAL VAL A . n 
A 1 510  ASN 510  1842 1842 ASN ASN A . n 
A 1 511  PRO 511  1843 1843 PRO PRO A . n 
A 1 512  ASP 512  1844 1844 ASP ASP A . n 
A 1 513  GLN 513  1845 1845 GLN GLN A . n 
A 1 514  PRO 514  1846 ?    ?   ?   A . n 
A 1 515  ARG 515  1847 ?    ?   ?   A . n 
A 1 516  LEU 516  1848 ?    ?   ?   A . n 
A 1 517  THR 517  1849 1849 THR THR A . n 
A 1 518  ILE 518  1850 1850 ILE ILE A . n 
A 1 519  PRO 519  1851 1851 PRO PRO A . n 
A 1 520  ILE 520  1852 1852 ILE ILE A . n 
A 1 521  SER 521  1853 1853 SER SER A . n 
A 1 522  GLN 522  1854 1854 GLN GLN A . n 
A 1 523  ILE 523  1855 1855 ILE ILE A . n 
A 1 524  ALA 524  1856 1856 ALA ALA A . n 
A 1 525  PRO 525  1857 1857 PRO PRO A . n 
A 1 526  ASP 526  1858 1858 ASP ASP A . n 
A 1 527  LEU 527  1859 1859 LEU LEU A . n 
A 1 528  ILE 528  1860 1860 ILE ILE A . n 
A 1 529  LEU 529  1861 1861 LEU LEU A . n 
A 1 530  ALA 530  1862 1862 ALA ALA A . n 
A 1 531  ASP 531  1863 1863 ASP ASP A . n 
A 1 532  LEU 532  1864 1864 LEU LEU A . n 
A 1 533  PRO 533  1865 1865 PRO PRO A . n 
A 1 534  ARG 534  1866 1866 ARG ARG A . n 
A 1 535  ASN 535  1867 1867 ASN ASN A . n 
A 1 536  ILE 536  1868 1868 ILE ILE A . n 
A 1 537  MET 537  1869 1869 MET MET A . n 
A 1 538  LEU 538  1870 1870 LEU LEU A . n 
A 1 539  ASN 539  1871 1871 ASN ASN A . n 
A 1 540  ASN 540  1872 1872 ASN ASN A . n 
A 1 541  ASP 541  1873 1873 ASP ASP A . n 
A 1 542  GLU 542  1874 1874 GLU GLU A . n 
A 1 543  LEU 543  1875 1875 LEU LEU A . n 
A 1 544  GLU 544  1876 1876 GLU GLU A . n 
A 1 545  PHE 545  1877 1877 PHE PHE A . n 
A 1 546  GLU 546  1878 1878 GLU GLU A . n 
A 1 547  GLN 547  1879 1879 GLN GLN A . n 
A 1 548  ALA 548  1880 1880 ALA ALA A . n 
A 1 549  PRO 549  1881 1881 PRO PRO A . n 
A 1 550  GLU 550  1882 1882 GLU GLU A . n 
A 1 551  PHE 551  1883 1883 PHE PHE A . n 
A 1 552  LEU 552  1884 1884 LEU LEU A . n 
A 1 553  LEU 553  1885 1885 LEU LEU A . n 
A 1 554  GLY 554  1886 ?    ?   ?   A . n 
A 1 555  ASP 555  1887 ?    ?   ?   A . n 
A 1 556  GLY 556  1888 ?    ?   ?   A . n 
A 1 557  SER 557  1889 ?    ?   ?   A . n 
A 1 558  PHE 558  1890 ?    ?   ?   A . n 
A 1 559  GLY 559  1891 1891 GLY GLY A . n 
A 1 560  SER 560  1892 1892 SER SER A . n 
A 1 561  VAL 561  1893 1893 VAL VAL A . n 
A 1 562  TYR 562  1894 1894 TYR TYR A . n 
A 1 563  ARG 563  1895 1895 ARG ARG A . n 
A 1 564  ALA 564  1896 1896 ALA ALA A . n 
A 1 565  ALA 565  1897 1897 ALA ALA A . n 
A 1 566  TYR 566  1898 1898 TYR TYR A . n 
A 1 567  GLU 567  1899 1899 GLU GLU A . n 
A 1 568  GLY 568  1900 1900 GLY GLY A . n 
A 1 569  GLU 569  1901 1901 GLU GLU A . n 
A 1 570  GLU 570  1902 1902 GLU GLU A . n 
A 1 571  VAL 571  1903 1903 VAL VAL A . n 
A 1 572  ALA 572  1904 1904 ALA ALA A . n 
A 1 573  VAL 573  1905 1905 VAL VAL A . n 
A 1 574  LYS 574  1906 1906 LYS LYS A . n 
A 1 575  ILE 575  1907 1907 ILE ILE A . n 
A 1 576  PHE 576  1908 1908 PHE PHE A . n 
A 1 577  ASN 577  1909 1909 ASN ASN A . n 
A 1 578  LYS 578  1910 1910 LYS LYS A . n 
A 1 579  HIS 579  1911 1911 HIS HIS A . n 
A 1 580  THR 580  1912 1912 THR THR A . n 
A 1 581  SER 581  1913 1913 SER SER A . n 
A 1 582  LEU 582  1914 1914 LEU LEU A . n 
A 1 583  ARG 583  1915 1915 ARG ARG A . n 
A 1 584  LEU 584  1916 1916 LEU LEU A . n 
A 1 585  LEU 585  1917 1917 LEU LEU A . n 
A 1 586  ARG 586  1918 1918 ARG ARG A . n 
A 1 587  GLN 587  1919 1919 GLN GLN A . n 
A 1 588  GLU 588  1920 1920 GLU GLU A . n 
A 1 589  LEU 589  1921 1921 LEU LEU A . n 
A 1 590  VAL 590  1922 1922 VAL VAL A . n 
A 1 591  VAL 591  1923 1923 VAL VAL A . n 
A 1 592  LEU 592  1924 1924 LEU LEU A . n 
A 1 593  CYS 593  1925 1925 CYS CYS A . n 
A 1 594  HIS 594  1926 1926 HIS HIS A . n 
A 1 595  LEU 595  1927 1927 LEU LEU A . n 
A 1 596  HIS 596  1928 1928 HIS HIS A . n 
A 1 597  HIS 597  1929 1929 HIS HIS A . n 
A 1 598  PRO 598  1930 1930 PRO PRO A . n 
A 1 599  SER 599  1931 1931 SER SER A . n 
A 1 600  LEU 600  1932 1932 LEU LEU A . n 
A 1 601  ILE 601  1933 1933 ILE ILE A . n 
A 1 602  SER 602  1934 1934 SER SER A . n 
A 1 603  LEU 603  1935 1935 LEU LEU A . n 
A 1 604  LEU 604  1936 1936 LEU LEU A . n 
A 1 605  ALA 605  1937 1937 ALA ALA A . n 
A 1 606  ALA 606  1938 1938 ALA ALA A . n 
A 1 607  GLY 607  1939 1939 GLY GLY A . n 
A 1 608  ILE 608  1940 1940 ILE ILE A . n 
A 1 609  ARG 609  1941 1941 ARG ARG A . n 
A 1 610  PRO 610  1942 1942 PRO PRO A . n 
A 1 611  ARG 611  1943 1943 ARG ARG A . n 
A 1 612  MET 612  1944 1944 MET MET A . n 
A 1 613  LEU 613  1945 1945 LEU LEU A . n 
A 1 614  VAL 614  1946 1946 VAL VAL A . n 
A 1 615  MET 615  1947 1947 MET MET A . n 
A 1 616  GLU 616  1948 1948 GLU GLU A . n 
A 1 617  LEU 617  1949 1949 LEU LEU A . n 
A 1 618  ALA 618  1950 1950 ALA ALA A . n 
A 1 619  SER 619  1951 1951 SER SER A . n 
A 1 620  LYS 620  1952 1952 LYS LYS A . n 
A 1 621  GLY 621  1953 1953 GLY GLY A . n 
A 1 622  SER 622  1954 1954 SER SER A . n 
A 1 623  LEU 623  1955 1955 LEU LEU A . n 
A 1 624  ASP 624  1956 1956 ASP ASP A . n 
A 1 625  ARG 625  1957 1957 ARG ARG A . n 
A 1 626  LEU 626  1958 1958 LEU LEU A . n 
A 1 627  LEU 627  1959 1959 LEU LEU A . n 
A 1 628  GLN 628  1960 1960 GLN GLN A . n 
A 1 629  GLN 629  1961 1961 GLN GLN A . n 
A 1 630  ASP 630  1962 1962 ASP ASP A . n 
A 1 631  LYS 631  1963 1963 LYS LYS A . n 
A 1 632  ALA 632  1964 1964 ALA ALA A . n 
A 1 633  SER 633  1965 1965 SER SER A . n 
A 1 634  LEU 634  1966 1966 LEU LEU A . n 
A 1 635  THR 635  1967 1967 THR THR A . n 
A 1 636  ARG 636  1968 1968 ARG ARG A . n 
A 1 637  THR 637  1969 1969 THR THR A . n 
A 1 638  LEU 638  1970 1970 LEU LEU A . n 
A 1 639  GLN 639  1971 1971 GLN GLN A . n 
A 1 640  HIS 640  1972 1972 HIS HIS A . n 
A 1 641  ARG 641  1973 1973 ARG ARG A . n 
A 1 642  ILE 642  1974 1974 ILE ILE A . n 
A 1 643  ALA 643  1975 1975 ALA ALA A . n 
A 1 644  LEU 644  1976 1976 LEU LEU A . n 
A 1 645  HIS 645  1977 1977 HIS HIS A . n 
A 1 646  VAL 646  1978 1978 VAL VAL A . n 
A 1 647  ALA 647  1979 1979 ALA ALA A . n 
A 1 648  ASP 648  1980 1980 ASP ASP A . n 
A 1 649  GLY 649  1981 1981 GLY GLY A . n 
A 1 650  LEU 650  1982 1982 LEU LEU A . n 
A 1 651  ARG 651  1983 1983 ARG ARG A . n 
A 1 652  TYR 652  1984 1984 TYR TYR A . n 
A 1 653  LEU 653  1985 1985 LEU LEU A . n 
A 1 654  HIS 654  1986 1986 HIS HIS A . n 
A 1 655  SER 655  1987 1987 SER SER A . n 
A 1 656  ALA 656  1988 1988 ALA ALA A . n 
A 1 657  MET 657  1989 1989 MET MET A . n 
A 1 658  ILE 658  1990 1990 ILE ILE A . n 
A 1 659  ILE 659  1991 1991 ILE ILE A . n 
A 1 660  TYR 660  1992 1992 TYR TYR A . n 
A 1 661  ARG 661  1993 1993 ARG ARG A . n 
A 1 662  ASP 662  1994 1994 ASP ASP A . n 
A 1 663  LEU 663  1995 1995 LEU LEU A . n 
A 1 664  LYS 664  1996 1996 LYS LYS A . n 
A 1 665  PRO 665  1997 1997 PRO PRO A . n 
A 1 666  HIS 666  1998 1998 HIS HIS A . n 
A 1 667  ASN 667  1999 1999 ASN ASN A . n 
A 1 668  VAL 668  2000 2000 VAL VAL A . n 
A 1 669  LEU 669  2001 2001 LEU LEU A . n 
A 1 670  LEU 670  2002 2002 LEU LEU A . n 
A 1 671  PHE 671  2003 2003 PHE PHE A . n 
A 1 672  THR 672  2004 2004 THR THR A . n 
A 1 673  LEU 673  2005 2005 LEU LEU A . n 
A 1 674  TYR 674  2006 2006 TYR TYR A . n 
A 1 675  PRO 675  2007 2007 PRO PRO A . n 
A 1 676  ASN 676  2008 2008 ASN ASN A . n 
A 1 677  ALA 677  2009 2009 ALA ALA A . n 
A 1 678  ALA 678  2010 2010 ALA ALA A . n 
A 1 679  ILE 679  2011 2011 ILE ILE A . n 
A 1 680  ILE 680  2012 2012 ILE ILE A . n 
A 1 681  ALA 681  2013 2013 ALA ALA A . n 
A 1 682  LYS 682  2014 2014 LYS LYS A . n 
A 1 683  ILE 683  2015 2015 ILE ILE A . n 
A 1 684  ALA 684  2016 2016 ALA ALA A . n 
A 1 685  ASP 685  2017 2017 ASP ASP A . n 
A 1 686  TYR 686  2018 2018 TYR TYR A . n 
A 1 687  GLY 687  2019 2019 GLY GLY A . n 
A 1 688  ILE 688  2020 2020 ILE ILE A . n 
A 1 689  ALA 689  2021 ?    ?   ?   A . n 
A 1 690  GLN 690  2022 ?    ?   ?   A . n 
A 1 691  TYR 691  2023 ?    ?   ?   A . n 
A 1 692  CYS 692  2024 ?    ?   ?   A . n 
A 1 693  CYS 693  2025 ?    ?   ?   A . n 
A 1 694  ARG 694  2026 ?    ?   ?   A . n 
A 1 695  MET 695  2027 ?    ?   ?   A . n 
A 1 696  GLY 696  2028 ?    ?   ?   A . n 
A 1 697  ILE 697  2029 ?    ?   ?   A . n 
A 1 698  LYS 698  2030 ?    ?   ?   A . n 
A 1 699  THR 699  2031 ?    ?   ?   A . n 
A 1 700  SER 700  2032 ?    ?   ?   A . n 
A 1 701  GLU 701  2033 2033 GLU GLU A . n 
A 1 702  GLY 702  2034 2034 GLY GLY A . n 
A 1 703  THR 703  2035 2035 THR THR A . n 
A 1 704  PRO 704  2036 2036 PRO PRO A . n 
A 1 705  GLY 705  2037 2037 GLY GLY A . n 
A 1 706  PHE 706  2038 2038 PHE PHE A . n 
A 1 707  ARG 707  2039 2039 ARG ARG A . n 
A 1 708  ALA 708  2040 2040 ALA ALA A . n 
A 1 709  PRO 709  2041 2041 PRO PRO A . n 
A 1 710  GLU 710  2042 2042 GLU GLU A . n 
A 1 711  VAL 711  2043 2043 VAL VAL A . n 
A 1 712  ALA 712  2044 ?    ?   ?   A . n 
A 1 713  ARG 713  2045 ?    ?   ?   A . n 
A 1 714  GLY 714  2046 ?    ?   ?   A . n 
A 1 715  ASN 715  2047 ?    ?   ?   A . n 
A 1 716  VAL 716  2048 ?    ?   ?   A . n 
A 1 717  ILE 717  2049 ?    ?   ?   A . n 
A 1 718  TYR 718  2050 2050 TYR TYR A . n 
A 1 719  ASN 719  2051 2051 ASN ASN A . n 
A 1 720  GLN 720  2052 2052 GLN GLN A . n 
A 1 721  GLN 721  2053 2053 GLN GLN A . n 
A 1 722  ALA 722  2054 2054 ALA ALA A . n 
A 1 723  ASP 723  2055 2055 ASP ASP A . n 
A 1 724  VAL 724  2056 2056 VAL VAL A . n 
A 1 725  TYR 725  2057 2057 TYR TYR A . n 
A 1 726  SER 726  2058 2058 SER SER A . n 
A 1 727  PHE 727  2059 2059 PHE PHE A . n 
A 1 728  GLY 728  2060 2060 GLY GLY A . n 
A 1 729  LEU 729  2061 2061 LEU LEU A . n 
A 1 730  LEU 730  2062 2062 LEU LEU A . n 
A 1 731  LEU 731  2063 2063 LEU LEU A . n 
A 1 732  TYR 732  2064 2064 TYR TYR A . n 
A 1 733  ASP 733  2065 2065 ASP ASP A . n 
A 1 734  ILE 734  2066 2066 ILE ILE A . n 
A 1 735  LEU 735  2067 2067 LEU LEU A . n 
A 1 736  THR 736  2068 2068 THR THR A . n 
A 1 737  THR 737  2069 2069 THR THR A . n 
A 1 738  GLY 738  2070 2070 GLY GLY A . n 
A 1 739  GLY 739  2071 2071 GLY GLY A . n 
A 1 740  ARG 740  2072 2072 ARG ARG A . n 
A 1 741  ILE 741  2073 2073 ILE ILE A . n 
A 1 742  VAL 742  2074 2074 VAL VAL A . n 
A 1 743  GLU 743  2075 ?    ?   ?   A . n 
A 1 744  GLY 744  2076 ?    ?   ?   A . n 
A 1 745  LEU 745  2077 ?    ?   ?   A . n 
A 1 746  LYS 746  2078 ?    ?   ?   A . n 
A 1 747  PHE 747  2079 ?    ?   ?   A . n 
A 1 748  PRO 748  2080 ?    ?   ?   A . n 
A 1 749  ASN 749  2081 ?    ?   ?   A . n 
A 1 750  GLU 750  2082 ?    ?   ?   A . n 
A 1 751  PHE 751  2083 ?    ?   ?   A . n 
A 1 752  ASP 752  2084 ?    ?   ?   A . n 
A 1 753  GLU 753  2085 ?    ?   ?   A . n 
A 1 754  LEU 754  2086 ?    ?   ?   A . n 
A 1 755  GLU 755  2087 ?    ?   ?   A . n 
A 1 756  ILE 756  2088 ?    ?   ?   A . n 
A 1 757  GLN 757  2089 2089 GLN GLN A . n 
A 1 758  GLY 758  2090 2090 GLY GLY A . n 
A 1 759  LYS 759  2091 2091 LYS LYS A . n 
A 1 760  LEU 760  2092 2092 LEU LEU A . n 
A 1 761  PRO 761  2093 2093 PRO PRO A . n 
A 1 762  ASP 762  2094 2094 ASP ASP A . n 
A 1 763  PRO 763  2095 2095 PRO PRO A . n 
A 1 764  VAL 764  2096 2096 VAL VAL A . n 
A 1 765  LYS 765  2097 2097 LYS LYS A . n 
A 1 766  GLU 766  2098 2098 GLU GLU A . n 
A 1 767  TYR 767  2099 2099 TYR TYR A . n 
A 1 768  GLY 768  2100 2100 GLY GLY A . n 
A 1 769  CYS 769  2101 2101 CYS CYS A . n 
A 1 770  ALA 770  2102 2102 ALA ALA A . n 
A 1 771  PRO 771  2103 2103 PRO PRO A . n 
A 1 772  TRP 772  2104 2104 TRP TRP A . n 
A 1 773  PRO 773  2105 2105 PRO PRO A . n 
A 1 774  MET 774  2106 2106 MET MET A . n 
A 1 775  VAL 775  2107 2107 VAL VAL A . n 
A 1 776  GLU 776  2108 2108 GLU GLU A . n 
A 1 777  LYS 777  2109 2109 LYS LYS A . n 
A 1 778  LEU 778  2110 2110 LEU LEU A . n 
A 1 779  ILE 779  2111 2111 ILE ILE A . n 
A 1 780  LYS 780  2112 2112 LYS LYS A . n 
A 1 781  GLN 781  2113 2113 GLN GLN A . n 
A 1 782  CYS 782  2114 2114 CYS CYS A . n 
A 1 783  LEU 783  2115 2115 LEU LEU A . n 
A 1 784  LYS 784  2116 2116 LYS LYS A . n 
A 1 785  GLU 785  2117 2117 GLU GLU A . n 
A 1 786  ASN 786  2118 2118 ASN ASN A . n 
A 1 787  PRO 787  2119 2119 PRO PRO A . n 
A 1 788  GLN 788  2120 2120 GLN GLN A . n 
A 1 789  GLU 789  2121 2121 GLU GLU A . n 
A 1 790  ARG 790  2122 2122 ARG ARG A . n 
A 1 791  PRO 791  2123 2123 PRO PRO A . n 
A 1 792  THR 792  2124 2124 THR THR A . n 
A 1 793  SER 793  2125 2125 SER SER A . n 
A 1 794  ALA 794  2126 2126 ALA ALA A . n 
A 1 795  GLN 795  2127 2127 GLN GLN A . n 
A 1 796  VAL 796  2128 2128 VAL VAL A . n 
A 1 797  PHE 797  2129 2129 PHE PHE A . n 
A 1 798  ASP 798  2130 2130 ASP ASP A . n 
A 1 799  ILE 799  2131 2131 ILE ILE A . n 
A 1 800  LEU 800  2132 2132 LEU LEU A . n 
A 1 801  ASN 801  2133 2133 ASN ASN A . n 
A 1 802  SER 802  2134 2134 SER SER A . n 
A 1 803  ALA 803  2135 2135 ALA ALA A . n 
A 1 804  GLU 804  2136 2136 GLU GLU A . n 
A 1 805  LEU 805  2137 2137 LEU LEU A . n 
A 1 806  VAL 806  2138 2138 VAL VAL A . n 
A 1 807  CYS 807  2139 2139 CYS CYS A . n 
A 1 808  LEU 808  2140 2140 LEU LEU A . n 
A 1 809  THR 809  2141 2141 THR THR A . n 
A 1 810  ARG 810  2142 2142 ARG ARG A . n 
A 1 811  ARG 811  2143 2143 ARG ARG A . n 
A 1 812  ILE 812  2144 2144 ILE ILE A . n 
A 1 813  LEU 813  2145 2145 LEU LEU A . n 
A 1 814  LEU 814  2146 2146 LEU LEU A . n 
A 1 815  PRO 815  2147 2147 PRO PRO A . n 
A 1 816  LYS 816  2148 2148 LYS LYS A . n 
A 1 817  ASN 817  2149 2149 ASN ASN A . n 
A 1 818  VAL 818  2150 2150 VAL VAL A . n 
A 1 819  ILE 819  2151 2151 ILE ILE A . n 
A 1 820  VAL 820  2152 2152 VAL VAL A . n 
A 1 821  GLU 821  2153 2153 GLU GLU A . n 
A 1 822  CYS 822  2154 2154 CYS CYS A . n 
A 1 823  MET 823  2155 2155 MET MET A . n 
A 1 824  VAL 824  2156 2156 VAL VAL A . n 
A 1 825  ALA 825  2157 2157 ALA ALA A . n 
A 1 826  THR 826  2158 2158 THR THR A . n 
A 1 827  HIS 827  2159 2159 HIS HIS A . n 
A 1 828  HIS 828  2160 2160 HIS HIS A . n 
A 1 829  ASN 829  2161 ?    ?   ?   A . n 
A 1 830  SER 830  2162 ?    ?   ?   A . n 
A 1 831  ARG 831  2163 ?    ?   ?   A . n 
A 1 832  ASN 832  2164 2164 ASN ASN A . n 
A 1 833  ALA 833  2165 2165 ALA ALA A . n 
A 1 834  SER 834  2166 2166 SER SER A . n 
A 1 835  ILE 835  2167 2167 ILE ILE A . n 
A 1 836  TRP 836  2168 2168 TRP TRP A . n 
A 1 837  LEU 837  2169 2169 LEU LEU A . n 
A 1 838  GLY 838  2170 2170 GLY GLY A . n 
A 1 839  CYS 839  2171 2171 CYS CYS A . n 
A 1 840  GLY 840  2172 2172 GLY GLY A . n 
A 1 841  HIS 841  2173 2173 HIS HIS A . n 
A 1 842  THR 842  2174 2174 THR THR A . n 
A 1 843  ASP 843  2175 2175 ASP ASP A . n 
A 1 844  ARG 844  2176 2176 ARG ARG A . n 
A 1 845  GLY 845  2177 2177 GLY GLY A . n 
A 1 846  GLN 846  2178 2178 GLN GLN A . n 
A 1 847  LEU 847  2179 2179 LEU LEU A . n 
A 1 848  SER 848  2180 2180 SER SER A . n 
A 1 849  PHE 849  2181 2181 PHE PHE A . n 
A 1 850  LEU 850  2182 2182 LEU LEU A . n 
A 1 851  ASP 851  2183 2183 ASP ASP A . n 
A 1 852  LEU 852  2184 2184 LEU LEU A . n 
A 1 853  ASN 853  2185 2185 ASN ASN A . n 
A 1 854  THR 854  2186 2186 THR THR A . n 
A 1 855  GLU 855  2187 2187 GLU GLU A . n 
A 1 856  GLY 856  2188 2188 GLY GLY A . n 
A 1 857  TYR 857  2189 2189 TYR TYR A . n 
A 1 858  THR 858  2190 2190 THR THR A . n 
A 1 859  SER 859  2191 2191 SER SER A . n 
A 1 860  GLU 860  2192 2192 GLU GLU A . n 
A 1 861  GLU 861  2193 2193 GLU GLU A . n 
A 1 862  VAL 862  2194 2194 VAL VAL A . n 
A 1 863  ALA 863  2195 2195 ALA ALA A . n 
A 1 864  ASP 864  2196 2196 ASP ASP A . n 
A 1 865  SER 865  2197 2197 SER SER A . n 
A 1 866  ARG 866  2198 2198 ARG ARG A . n 
A 1 867  ILE 867  2199 2199 ILE ILE A . n 
A 1 868  LEU 868  2200 2200 LEU LEU A . n 
A 1 869  CYS 869  2201 2201 CYS CYS A . n 
A 1 870  LEU 870  2202 2202 LEU LEU A . n 
A 1 871  ALA 871  2203 2203 ALA ALA A . n 
A 1 872  LEU 872  2204 2204 LEU LEU A . n 
A 1 873  VAL 873  2205 2205 VAL VAL A . n 
A 1 874  HIS 874  2206 2206 HIS HIS A . n 
A 1 875  LEU 875  2207 2207 LEU LEU A . n 
A 1 876  PRO 876  2208 2208 PRO PRO A . n 
A 1 877  VAL 877  2209 ?    ?   ?   A . n 
A 1 878  GLU 878  2210 ?    ?   ?   A . n 
A 1 879  LYS 879  2211 ?    ?   ?   A . n 
A 1 880  GLU 880  2212 ?    ?   ?   A . n 
A 1 881  SER 881  2213 2213 SER SER A . n 
A 1 882  TRP 882  2214 2214 TRP TRP A . n 
A 1 883  ILE 883  2215 2215 ILE ILE A . n 
A 1 884  VAL 884  2216 2216 VAL VAL A . n 
A 1 885  SER 885  2217 2217 SER SER A . n 
A 1 886  GLY 886  2218 2218 GLY GLY A . n 
A 1 887  THR 887  2219 2219 THR THR A . n 
A 1 888  GLN 888  2220 2220 GLN GLN A . n 
A 1 889  SER 889  2221 2221 SER SER A . n 
A 1 890  GLY 890  2222 2222 GLY GLY A . n 
A 1 891  THR 891  2223 2223 THR THR A . n 
A 1 892  LEU 892  2224 2224 LEU LEU A . n 
A 1 893  LEU 893  2225 2225 LEU LEU A . n 
A 1 894  VAL 894  2226 2226 VAL VAL A . n 
A 1 895  ILE 895  2227 2227 ILE ILE A . n 
A 1 896  ASN 896  2228 2228 ASN ASN A . n 
A 1 897  THR 897  2229 2229 THR THR A . n 
A 1 898  GLU 898  2230 2230 GLU GLU A . n 
A 1 899  ASP 899  2231 2231 ASP ASP A . n 
A 1 900  GLY 900  2232 2232 GLY GLY A . n 
A 1 901  LYS 901  2233 2233 LYS LYS A . n 
A 1 902  LYS 902  2234 2234 LYS LYS A . n 
A 1 903  ARG 903  2235 2235 ARG ARG A . n 
A 1 904  HIS 904  2236 2236 HIS HIS A . n 
A 1 905  THR 905  2237 2237 THR THR A . n 
A 1 906  LEU 906  2238 2238 LEU LEU A . n 
A 1 907  GLU 907  2239 2239 GLU GLU A . n 
A 1 908  LYS 908  2240 2240 LYS LYS A . n 
A 1 909  MET 909  2241 2241 MET MET A . n 
A 1 910  THR 910  2242 2242 THR THR A . n 
A 1 911  ASP 911  2243 2243 ASP ASP A . n 
A 1 912  SER 912  2244 2244 SER SER A . n 
A 1 913  VAL 913  2245 2245 VAL VAL A . n 
A 1 914  THR 914  2246 2246 THR THR A . n 
A 1 915  CYS 915  2247 2247 CYS CYS A . n 
A 1 916  LEU 916  2248 2248 LEU LEU A . n 
A 1 917  TYR 917  2249 2249 TYR TYR A . n 
A 1 918  CYS 918  2250 2250 CYS CYS A . n 
A 1 919  ASN 919  2251 2251 ASN ASN A . n 
A 1 920  SER 920  2252 ?    ?   ?   A . n 
A 1 921  PHE 921  2253 ?    ?   ?   A . n 
A 1 922  SER 922  2254 ?    ?   ?   A . n 
A 1 923  LYS 923  2255 ?    ?   ?   A . n 
A 1 924  GLN 924  2256 ?    ?   ?   A . n 
A 1 925  SER 925  2257 ?    ?   ?   A . n 
A 1 926  LYS 926  2258 ?    ?   ?   A . n 
A 1 927  GLN 927  2259 ?    ?   ?   A . n 
A 1 928  LYS 928  2260 ?    ?   ?   A . n 
A 1 929  ASN 929  2261 ?    ?   ?   A . n 
A 1 930  PHE 930  2262 2262 PHE PHE A . n 
A 1 931  LEU 931  2263 2263 LEU LEU A . n 
A 1 932  LEU 932  2264 2264 LEU LEU A . n 
A 1 933  VAL 933  2265 2265 VAL VAL A . n 
A 1 934  GLY 934  2266 2266 GLY GLY A . n 
A 1 935  THR 935  2267 2267 THR THR A . n 
A 1 936  ALA 936  2268 2268 ALA ALA A . n 
A 1 937  ASP 937  2269 2269 ASP ASP A . n 
A 1 938  GLY 938  2270 2270 GLY GLY A . n 
A 1 939  LYS 939  2271 2271 LYS LYS A . n 
A 1 940  LEU 940  2272 2272 LEU LEU A . n 
A 1 941  ALA 941  2273 2273 ALA ALA A . n 
A 1 942  ILE 942  2274 2274 ILE ILE A . n 
A 1 943  PHE 943  2275 2275 PHE PHE A . n 
A 1 944  GLU 944  2276 2276 GLU GLU A . n 
A 1 945  ASP 945  2277 2277 ASP ASP A . n 
A 1 946  LYS 946  2278 2278 LYS LYS A . n 
A 1 947  THR 947  2279 2279 THR THR A . n 
A 1 948  VAL 948  2280 2280 VAL VAL A . n 
A 1 949  LYS 949  2281 2281 LYS LYS A . n 
A 1 950  LEU 950  2282 2282 LEU LEU A . n 
A 1 951  LYS 951  2283 2283 LYS LYS A . n 
A 1 952  GLY 952  2284 2284 GLY GLY A . n 
A 1 953  ALA 953  2285 2285 ALA ALA A . n 
A 1 954  ALA 954  2286 2286 ALA ALA A . n 
A 1 955  PRO 955  2287 2287 PRO PRO A . n 
A 1 956  LEU 956  2288 2288 LEU LEU A . n 
A 1 957  LYS 957  2289 2289 LYS LYS A . n 
A 1 958  ILE 958  2290 2290 ILE ILE A . n 
A 1 959  LEU 959  2291 2291 LEU LEU A . n 
A 1 960  ASN 960  2292 2292 ASN ASN A . n 
A 1 961  ILE 961  2293 2293 ILE ILE A . n 
A 1 962  GLY 962  2294 2294 GLY GLY A . n 
A 1 963  ASN 963  2295 2295 ASN ASN A . n 
A 1 964  VAL 964  2296 2296 VAL VAL A . n 
A 1 965  SER 965  2297 2297 SER SER A . n 
A 1 966  THR 966  2298 2298 THR THR A . n 
A 1 967  PRO 967  2299 2299 PRO PRO A . n 
A 1 968  LEU 968  2300 2300 LEU LEU A . n 
A 1 969  MET 969  2301 2301 MET MET A . n 
A 1 970  CYS 970  2302 2302 CYS CYS A . n 
A 1 971  LEU 971  2303 2303 LEU LEU A . n 
A 1 972  SER 972  2304 2304 SER SER A . n 
A 1 973  GLU 973  2305 2305 GLU GLU A . n 
A 1 974  SER 974  2306 2306 SER SER A . n 
A 1 975  THR 975  2307 ?    ?   ?   A . n 
A 1 976  ASN 976  2308 ?    ?   ?   A . n 
A 1 977  SER 977  2309 ?    ?   ?   A . n 
A 1 978  THR 978  2310 ?    ?   ?   A . n 
A 1 979  GLU 979  2311 ?    ?   ?   A . n 
A 1 980  ARG 980  2312 2312 ARG ARG A . n 
A 1 981  ASN 981  2313 2313 ASN ASN A . n 
A 1 982  VAL 982  2314 2314 VAL VAL A . n 
A 1 983  MET 983  2315 2315 MET MET A . n 
A 1 984  TRP 984  2316 2316 TRP TRP A . n 
A 1 985  GLY 985  2317 2317 GLY GLY A . n 
A 1 986  GLY 986  2318 2318 GLY GLY A . n 
A 1 987  CYS 987  2319 2319 CYS CYS A . n 
A 1 988  GLY 988  2320 2320 GLY GLY A . n 
A 1 989  THR 989  2321 2321 THR THR A . n 
A 1 990  LYS 990  2322 2322 LYS LYS A . n 
A 1 991  ILE 991  2323 2323 ILE ILE A . n 
A 1 992  PHE 992  2324 2324 PHE PHE A . n 
A 1 993  SER 993  2325 2325 SER SER A . n 
A 1 994  PHE 994  2326 2326 PHE PHE A . n 
A 1 995  SER 995  2327 2327 SER SER A . n 
A 1 996  ASN 996  2328 2328 ASN ASN A . n 
A 1 997  ASP 997  2329 2329 ASP ASP A . n 
A 1 998  PHE 998  2330 2330 PHE PHE A . n 
A 1 999  THR 999  2331 2331 THR THR A . n 
A 1 1000 ILE 1000 2332 2332 ILE ILE A . n 
A 1 1001 GLN 1001 2333 2333 GLN GLN A . n 
A 1 1002 LYS 1002 2334 2334 LYS LYS A . n 
A 1 1003 LEU 1003 2335 2335 LEU LEU A . n 
A 1 1004 ILE 1004 2336 2336 ILE ILE A . n 
A 1 1005 GLU 1005 2337 2337 GLU GLU A . n 
A 1 1006 THR 1006 2338 2338 THR THR A . n 
A 1 1007 ARG 1007 2339 2339 ARG ARG A . n 
A 1 1008 THR 1008 2340 2340 THR THR A . n 
A 1 1009 SER 1009 2341 2341 SER SER A . n 
A 1 1010 GLN 1010 2342 2342 GLN GLN A . n 
A 1 1011 LEU 1011 2343 2343 LEU LEU A . n 
A 1 1012 PHE 1012 2344 2344 PHE PHE A . n 
A 1 1013 SER 1013 2345 2345 SER SER A . n 
A 1 1014 TYR 1014 2346 2346 TYR TYR A . n 
A 1 1015 ALA 1015 2347 2347 ALA ALA A . n 
A 1 1016 ALA 1016 2348 2348 ALA ALA A . n 
A 1 1017 PHE 1017 2349 2349 PHE PHE A . n 
A 1 1018 SER 1018 2350 2350 SER SER A . n 
A 1 1019 ASP 1019 2351 2351 ASP ASP A . n 
A 1 1020 SER 1020 2352 2352 SER SER A . n 
A 1 1021 ASN 1021 2353 2353 ASN ASN A . n 
A 1 1022 ILE 1022 2354 2354 ILE ILE A . n 
A 1 1023 ILE 1023 2355 2355 ILE ILE A . n 
A 1 1024 THR 1024 2356 2356 THR THR A . n 
A 1 1025 VAL 1025 2357 2357 VAL VAL A . n 
A 1 1026 VAL 1026 2358 2358 VAL VAL A . n 
A 1 1027 VAL 1027 2359 2359 VAL VAL A . n 
A 1 1028 ASP 1028 2360 2360 ASP ASP A . n 
A 1 1029 THR 1029 2361 2361 THR THR A . n 
A 1 1030 ALA 1030 2362 2362 ALA ALA A . n 
A 1 1031 LEU 1031 2363 2363 LEU LEU A . n 
A 1 1032 TYR 1032 2364 2364 TYR TYR A . n 
A 1 1033 ILE 1033 2365 2365 ILE ILE A . n 
A 1 1034 ALA 1034 2366 2366 ALA ALA A . n 
A 1 1035 LYS 1035 2367 2367 LYS LYS A . n 
A 1 1036 GLN 1036 2368 2368 GLN GLN A . n 
A 1 1037 ASN 1037 2369 2369 ASN ASN A . n 
A 1 1038 SER 1038 2370 2370 SER SER A . n 
A 1 1039 PRO 1039 2371 2371 PRO PRO A . n 
A 1 1040 VAL 1040 2372 2372 VAL VAL A . n 
A 1 1041 VAL 1041 2373 2373 VAL VAL A . n 
A 1 1042 GLU 1042 2374 2374 GLU GLU A . n 
A 1 1043 VAL 1043 2375 2375 VAL VAL A . n 
A 1 1044 TRP 1044 2376 2376 TRP TRP A . n 
A 1 1045 ASP 1045 2377 2377 ASP ASP A . n 
A 1 1046 LYS 1046 2378 2378 LYS LYS A . n 
A 1 1047 LYS 1047 2379 2379 LYS LYS A . n 
A 1 1048 THR 1048 2380 2380 THR THR A . n 
A 1 1049 GLU 1049 2381 2381 GLU GLU A . n 
A 1 1050 LYS 1050 2382 2382 LYS LYS A . n 
A 1 1051 LEU 1051 2383 2383 LEU LEU A . n 
A 1 1052 CYS 1052 2384 2384 CYS CYS A . n 
A 1 1053 GLY 1053 2385 2385 GLY GLY A . n 
A 1 1054 LEU 1054 2386 2386 LEU LEU A . n 
A 1 1055 ILE 1055 2387 2387 ILE ILE A . n 
A 1 1056 ASP 1056 2388 2388 ASP ASP A . n 
A 1 1057 CYS 1057 2389 2389 CYS CYS A . n 
A 1 1058 VAL 1058 2390 2390 VAL VAL A . n 
A 1 1059 HIS 1059 2391 2391 HIS HIS A . n 
A 1 1060 PHE 1060 2392 2392 PHE PHE A . n 
A 1 1061 LEU 1061 2393 2393 LEU LEU A . n 
A 1 1062 ARG 1062 2394 2394 ARG ARG A . n 
A 1 1063 GLU 1063 2395 2395 GLU GLU A . n 
A 1 1064 VAL 1064 2396 2396 VAL VAL A . n 
A 1 1065 MET 1065 2397 ?    ?   ?   A . n 
A 1 1066 VAL 1066 2398 ?    ?   ?   A . n 
A 1 1067 LYS 1067 2399 ?    ?   ?   A . n 
A 1 1068 GLU 1068 2400 ?    ?   ?   A . n 
A 1 1069 ASN 1069 2401 ?    ?   ?   A . n 
A 1 1070 LYS 1070 2402 ?    ?   ?   A . n 
A 1 1071 GLU 1071 2403 ?    ?   ?   A . n 
A 1 1072 SER 1072 2404 ?    ?   ?   A . n 
A 1 1073 LYS 1073 2405 ?    ?   ?   A . n 
A 1 1074 HIS 1074 2406 ?    ?   ?   A . n 
A 1 1075 LYS 1075 2407 ?    ?   ?   A . n 
A 1 1076 MET 1076 2408 ?    ?   ?   A . n 
A 1 1077 SER 1077 2409 ?    ?   ?   A . n 
A 1 1078 TYR 1078 2410 2410 TYR TYR A . n 
A 1 1079 SER 1079 2411 2411 SER SER A . n 
A 1 1080 GLY 1080 2412 2412 GLY GLY A . n 
A 1 1081 ARG 1081 2413 2413 ARG ARG A . n 
A 1 1082 VAL 1082 2414 2414 VAL VAL A . n 
A 1 1083 LYS 1083 2415 2415 LYS LYS A . n 
A 1 1084 THR 1084 2416 2416 THR THR A . n 
A 1 1085 LEU 1085 2417 2417 LEU LEU A . n 
A 1 1086 CYS 1086 2418 2418 CYS CYS A . n 
A 1 1087 LEU 1087 2419 2419 LEU LEU A . n 
A 1 1088 GLN 1088 2420 2420 GLN GLN A . n 
A 1 1089 LYS 1089 2421 2421 LYS LYS A . n 
A 1 1090 ASN 1090 2422 2422 ASN ASN A . n 
A 1 1091 THR 1091 2423 2423 THR THR A . n 
A 1 1092 ALA 1092 2424 2424 ALA ALA A . n 
A 1 1093 LEU 1093 2425 2425 LEU LEU A . n 
A 1 1094 TRP 1094 2426 2426 TRP TRP A . n 
A 1 1095 ILE 1095 2427 2427 ILE ILE A . n 
A 1 1096 GLY 1096 2428 2428 GLY GLY A . n 
A 1 1097 THR 1097 2429 2429 THR THR A . n 
A 1 1098 GLY 1098 2430 2430 GLY GLY A . n 
A 1 1099 GLY 1099 2431 2431 GLY GLY A . n 
A 1 1100 GLY 1100 2432 2432 GLY GLY A . n 
A 1 1101 HIS 1101 2433 2433 HIS HIS A . n 
A 1 1102 ILE 1102 2434 2434 ILE ILE A . n 
A 1 1103 LEU 1103 2435 2435 LEU LEU A . n 
A 1 1104 LEU 1104 2436 2436 LEU LEU A . n 
A 1 1105 LEU 1105 2437 2437 LEU LEU A . n 
A 1 1106 ASP 1106 2438 2438 ASP ASP A . n 
A 1 1107 LEU 1107 2439 2439 LEU LEU A . n 
A 1 1108 SER 1108 2440 2440 SER SER A . n 
A 1 1109 THR 1109 2441 2441 THR THR A . n 
A 1 1110 ARG 1110 2442 2442 ARG ARG A . n 
A 1 1111 ARG 1111 2443 2443 ARG ARG A . n 
A 1 1112 LEU 1112 2444 2444 LEU LEU A . n 
A 1 1113 ILE 1113 2445 2445 ILE ILE A . n 
A 1 1114 ARG 1114 2446 2446 ARG ARG A . n 
A 1 1115 VAL 1115 2447 2447 VAL VAL A . n 
A 1 1116 ILE 1116 2448 2448 ILE ILE A . n 
A 1 1117 TYR 1117 2449 2449 TYR TYR A . n 
A 1 1118 ASN 1118 2450 2450 ASN ASN A . n 
A 1 1119 PHE 1119 2451 2451 PHE PHE A . n 
A 1 1120 CYS 1120 2452 2452 CYS CYS A . n 
A 1 1121 ASN 1121 2453 2453 ASN ASN A . n 
A 1 1122 SER 1122 2454 2454 SER SER A . n 
A 1 1123 VAL 1123 2455 2455 VAL VAL A . n 
A 1 1124 ARG 1124 2456 2456 ARG ARG A . n 
A 1 1125 VAL 1125 2457 2457 VAL VAL A . n 
A 1 1126 MET 1126 2458 2458 MET MET A . n 
A 1 1127 MET 1127 2459 2459 MET MET A . n 
A 1 1128 THR 1128 2460 2460 THR THR A . n 
A 1 1129 ALA 1129 2461 2461 ALA ALA A . n 
A 1 1130 GLN 1130 2462 2462 GLN GLN A . n 
A 1 1131 LEU 1131 2463 2463 LEU LEU A . n 
A 1 1132 GLY 1132 2464 2464 GLY GLY A . n 
A 1 1133 SER 1133 2465 ?    ?   ?   A . n 
A 1 1134 LEU 1134 2466 ?    ?   ?   A . n 
A 1 1135 LYS 1135 2467 2467 LYS LYS A . n 
A 1 1136 ASN 1136 2468 2468 ASN ASN A . n 
A 1 1137 VAL 1137 2469 2469 VAL VAL A . n 
A 1 1138 MET 1138 2470 2470 MET MET A . n 
A 1 1139 LEU 1139 2471 2471 LEU LEU A . n 
A 1 1140 VAL 1140 2472 2472 VAL VAL A . n 
A 1 1141 LEU 1141 2473 2473 LEU LEU A . n 
A 1 1142 GLY 1142 2474 2474 GLY GLY A . n 
A 1 1143 TYR 1143 2475 2475 TYR TYR A . n 
A 1 1144 ASN 1144 2476 2476 ASN ASN A . n 
A 1 1145 ARG 1145 2477 ?    ?   ?   A . n 
A 1 1146 LYS 1146 2478 ?    ?   ?   A . n 
A 1 1147 ASN 1147 2479 ?    ?   ?   A . n 
A 1 1148 THR 1148 2480 ?    ?   ?   A . n 
A 1 1149 GLU 1149 2481 ?    ?   ?   A . n 
A 1 1150 GLY 1150 2482 ?    ?   ?   A . n 
A 1 1151 THR 1151 2483 ?    ?   ?   A . n 
A 1 1152 GLN 1152 2484 ?    ?   ?   A . n 
A 1 1153 LYS 1153 2485 ?    ?   ?   A . n 
A 1 1154 GLN 1154 2486 ?    ?   ?   A . n 
A 1 1155 LYS 1155 2487 ?    ?   ?   A . n 
A 1 1156 GLU 1156 2488 ?    ?   ?   A . n 
A 1 1157 ILE 1157 2489 2489 ILE ILE A . n 
A 1 1158 GLN 1158 2490 2490 GLN GLN A . n 
A 1 1159 SER 1159 2491 2491 SER SER A . n 
A 1 1160 CYS 1160 2492 2492 CYS CYS A . n 
A 1 1161 LEU 1161 2493 2493 LEU LEU A . n 
A 1 1162 THR 1162 2494 2494 THR THR A . n 
A 1 1163 VAL 1163 2495 2495 VAL VAL A . n 
A 1 1164 TRP 1164 2496 2496 TRP TRP A . n 
A 1 1165 ASP 1165 2497 2497 ASP ASP A . n 
A 1 1166 ILE 1166 2498 2498 ILE ILE A . n 
A 1 1167 ASN 1167 2499 2499 ASN ASN A . n 
A 1 1168 LEU 1168 2500 2500 LEU LEU A . n 
A 1 1169 PRO 1169 2501 2501 PRO PRO A . n 
A 1 1170 HIS 1170 2502 2502 HIS HIS A . n 
A 1 1171 GLU 1171 2503 2503 GLU GLU A . n 
A 1 1172 VAL 1172 2504 2504 VAL VAL A . n 
A 1 1173 GLN 1173 2505 2505 GLN GLN A . n 
A 1 1174 ASN 1174 2506 2506 ASN ASN A . n 
A 1 1175 LEU 1175 2507 2507 LEU LEU A . n 
A 1 1176 GLU 1176 2508 2508 GLU GLU A . n 
A 1 1177 LYS 1177 2509 2509 LYS LYS A . n 
A 1 1178 HIS 1178 2510 2510 HIS HIS A . n 
A 1 1179 ILE 1179 2511 2511 ILE ILE A . n 
A 1 1180 GLU 1180 2512 2512 GLU GLU A . n 
A 1 1181 VAL 1181 2513 2513 VAL VAL A . n 
A 1 1182 ARG 1182 2514 2514 ARG ARG A . n 
A 1 1183 LYS 1183 2515 2515 LYS LYS A . n 
A 1 1184 GLU 1184 2516 2516 GLU GLU A . n 
A 1 1185 LEU 1185 2517 2517 LEU LEU A . n 
A 1 1186 ALA 1186 2518 2518 ALA ALA A . n 
A 1 1187 GLU 1187 2519 2519 GLU GLU A . n 
A 1 1188 LYS 1188 2520 2520 LYS LYS A . n 
A 1 1189 MET 1189 2521 2521 MET MET A . n 
A 1 1190 ARG 1190 2522 2522 ARG ARG A . n 
A 1 1191 ARG 1191 2523 2523 ARG ARG A . n 
A 1 1192 THR 1192 2524 2524 THR THR A . n 
A 1 1193 SER 1193 2525 2525 SER SER A . n 
A 1 1194 VAL 1194 2526 2526 VAL VAL A . n 
A 1 1195 GLU 1195 2527 ?    ?   ?   A . n 
B 2 1    MET 1    1    ?    ?   ?   B . n 
B 2 2    ARG 2    2    ?    ?   ?   B . n 
B 2 3    GLY 3    3    ?    ?   ?   B . n 
B 2 4    SER 4    4    ?    ?   ?   B . n 
B 2 5    HIS 5    5    ?    ?   ?   B . n 
B 2 6    HIS 6    6    ?    ?   ?   B . n 
B 2 7    HIS 7    7    ?    ?   ?   B . n 
B 2 8    HIS 8    8    ?    ?   ?   B . n 
B 2 9    HIS 9    9    ?    ?   ?   B . n 
B 2 10   HIS 10   10   ?    ?   ?   B . n 
B 2 11   HIS 11   11   ?    ?   ?   B . n 
B 2 12   HIS 12   12   ?    ?   ?   B . n 
B 2 13   GLY 13   13   ?    ?   ?   B . n 
B 2 14   SER 14   14   ?    ?   ?   B . n 
B 2 15   ASP 15   15   ?    ?   ?   B . n 
B 2 16   LEU 16   16   ?    ?   ?   B . n 
B 2 17   GLY 17   17   ?    ?   ?   B . n 
B 2 18   LYS 18   18   ?    ?   ?   B . n 
B 2 19   LYS 19   19   ?    ?   ?   B . n 
B 2 20   LEU 20   20   ?    ?   ?   B . n 
B 2 21   LEU 21   21   ?    ?   ?   B . n 
B 2 22   GLU 22   22   ?    ?   ?   B . n 
B 2 23   ALA 23   23   ?    ?   ?   B . n 
B 2 24   ALA 24   24   ?    ?   ?   B . n 
B 2 25   ARG 25   25   ?    ?   ?   B . n 
B 2 26   ALA 26   26   ?    ?   ?   B . n 
B 2 27   GLY 27   27   ?    ?   ?   B . n 
B 2 28   GLN 28   28   ?    ?   ?   B . n 
B 2 29   ASP 29   29   ?    ?   ?   B . n 
B 2 30   ASP 30   30   ?    ?   ?   B . n 
B 2 31   GLU 31   31   ?    ?   ?   B . n 
B 2 32   VAL 32   32   ?    ?   ?   B . n 
B 2 33   ARG 33   33   ?    ?   ?   B . n 
B 2 34   ILE 34   34   ?    ?   ?   B . n 
B 2 35   LEU 35   35   ?    ?   ?   B . n 
B 2 36   MET 36   36   ?    ?   ?   B . n 
B 2 37   ALA 37   37   ?    ?   ?   B . n 
B 2 38   ASN 38   38   ?    ?   ?   B . n 
B 2 39   GLY 39   39   ?    ?   ?   B . n 
B 2 40   ALA 40   40   ?    ?   ?   B . n 
B 2 41   ASP 41   41   ?    ?   ?   B . n 
B 2 42   VAL 42   42   ?    ?   ?   B . n 
B 2 43   ASN 43   43   ?    ?   ?   B . n 
B 2 44   ALA 44   44   ?    ?   ?   B . n 
B 2 45   THR 45   45   ?    ?   ?   B . n 
B 2 46   ASP 46   46   ?    ?   ?   B . n 
B 2 47   GLU 47   47   ?    ?   ?   B . n 
B 2 48   ALA 48   48   ?    ?   ?   B . n 
B 2 49   GLY 49   49   ?    ?   ?   B . n 
B 2 50   VAL 50   50   ?    ?   ?   B . n 
B 2 51   THR 51   51   ?    ?   ?   B . n 
B 2 52   PRO 52   52   52   PRO PRO B . n 
B 2 53   LEU 53   53   53   LEU LEU B . n 
B 2 54   HIS 54   54   54   HIS HIS B . n 
B 2 55   LEU 55   55   55   LEU LEU B . n 
B 2 56   ALA 56   56   56   ALA ALA B . n 
B 2 57   ALA 57   57   57   ALA ALA B . n 
B 2 58   ASP 58   58   58   ASP ASP B . n 
B 2 59   SER 59   59   59   SER SER B . n 
B 2 60   GLY 60   60   60   GLY GLY B . n 
B 2 61   HIS 61   61   61   HIS HIS B . n 
B 2 62   LEU 62   62   62   LEU LEU B . n 
B 2 63   GLU 63   63   63   GLU GLU B . n 
B 2 64   ILE 64   64   64   ILE ILE B . n 
B 2 65   VAL 65   65   65   VAL VAL B . n 
B 2 66   GLU 66   66   66   GLU GLU B . n 
B 2 67   VAL 67   67   67   VAL VAL B . n 
B 2 68   LEU 68   68   68   LEU LEU B . n 
B 2 69   LEU 69   69   69   LEU LEU B . n 
B 2 70   LYS 70   70   70   LYS LYS B . n 
B 2 71   THR 71   71   71   THR THR B . n 
B 2 72   GLY 72   72   72   GLY GLY B . n 
B 2 73   ALA 73   73   73   ALA ALA B . n 
B 2 74   ASP 74   74   74   ASP ASP B . n 
B 2 75   VAL 75   75   75   VAL VAL B . n 
B 2 76   ASN 76   76   76   ASN ASN B . n 
B 2 77   ALA 77   77   77   ALA ALA B . n 
B 2 78   TRP 78   78   78   TRP TRP B . n 
B 2 79   ASP 79   79   79   ASP ASP B . n 
B 2 80   HIS 80   80   80   HIS HIS B . n 
B 2 81   TYR 81   81   81   TYR TYR B . n 
B 2 82   GLY 82   82   82   GLY GLY B . n 
B 2 83   PHE 83   83   83   PHE PHE B . n 
B 2 84   THR 84   84   84   THR THR B . n 
B 2 85   PRO 85   85   85   PRO PRO B . n 
B 2 86   LEU 86   86   86   LEU LEU B . n 
B 2 87   HIS 87   87   87   HIS HIS B . n 
B 2 88   LEU 88   88   88   LEU LEU B . n 
B 2 89   ALA 89   89   89   ALA ALA B . n 
B 2 90   ALA 90   90   90   ALA ALA B . n 
B 2 91   HIS 91   91   91   HIS HIS B . n 
B 2 92   VAL 92   92   92   VAL VAL B . n 
B 2 93   GLY 93   93   93   GLY GLY B . n 
B 2 94   HIS 94   94   94   HIS HIS B . n 
B 2 95   LEU 95   95   95   LEU LEU B . n 
B 2 96   GLU 96   96   96   GLU GLU B . n 
B 2 97   ILE 97   97   97   ILE ILE B . n 
B 2 98   VAL 98   98   98   VAL VAL B . n 
B 2 99   GLU 99   99   99   GLU GLU B . n 
B 2 100  VAL 100  100  100  VAL VAL B . n 
B 2 101  LEU 101  101  101  LEU LEU B . n 
B 2 102  LEU 102  102  102  LEU LEU B . n 
B 2 103  LYS 103  103  103  LYS LYS B . n 
B 2 104  ALA 104  104  104  ALA ALA B . n 
B 2 105  GLY 105  105  105  GLY GLY B . n 
B 2 106  ALA 106  106  106  ALA ALA B . n 
B 2 107  ASP 107  107  107  ASP ASP B . n 
B 2 108  VAL 108  108  108  VAL VAL B . n 
B 2 109  ASN 109  109  109  ASN ASN B . n 
B 2 110  ALA 110  110  110  ALA ALA B . n 
B 2 111  GLN 111  111  111  GLN GLN B . n 
B 2 112  ASP 112  112  112  ASP ASP B . n 
B 2 113  HIS 113  113  113  HIS HIS B . n 
B 2 114  ALA 114  114  114  ALA ALA B . n 
B 2 115  GLY 115  115  115  GLY GLY B . n 
B 2 116  TRP 116  116  116  TRP TRP B . n 
B 2 117  THR 117  117  117  THR THR B . n 
B 2 118  PRO 118  118  118  PRO PRO B . n 
B 2 119  LEU 119  119  119  LEU LEU B . n 
B 2 120  HIS 120  120  120  HIS HIS B . n 
B 2 121  LEU 121  121  121  LEU LEU B . n 
B 2 122  ALA 122  122  122  ALA ALA B . n 
B 2 123  ALA 123  123  123  ALA ALA B . n 
B 2 124  LEU 124  124  124  LEU LEU B . n 
B 2 125  TYR 125  125  125  TYR TYR B . n 
B 2 126  GLY 126  126  126  GLY GLY B . n 
B 2 127  HIS 127  127  127  HIS HIS B . n 
B 2 128  LEU 128  128  128  LEU LEU B . n 
B 2 129  GLU 129  129  129  GLU GLU B . n 
B 2 130  ILE 130  130  130  ILE ILE B . n 
B 2 131  VAL 131  131  131  VAL VAL B . n 
B 2 132  GLU 132  132  132  GLU GLU B . n 
B 2 133  VAL 133  133  133  VAL VAL B . n 
B 2 134  LEU 134  134  134  LEU LEU B . n 
B 2 135  LEU 135  135  135  LEU LEU B . n 
B 2 136  LYS 136  136  136  LYS LYS B . n 
B 2 137  HIS 137  137  137  HIS HIS B . n 
B 2 138  GLY 138  138  138  GLY GLY B . n 
B 2 139  ALA 139  139  139  ALA ALA B . n 
B 2 140  ASP 140  140  140  ASP ASP B . n 
B 2 141  VAL 141  141  141  VAL VAL B . n 
B 2 142  ASN 142  142  142  ASN ASN B . n 
B 2 143  ALA 143  143  143  ALA ALA B . n 
B 2 144  GLN 144  144  144  GLN GLN B . n 
B 2 145  ASP 145  145  145  ASP ASP B . n 
B 2 146  MET 146  146  146  MET MET B . n 
B 2 147  TRP 147  147  147  TRP TRP B . n 
B 2 148  GLY 148  148  148  GLY GLY B . n 
B 2 149  GLU 149  149  149  GLU GLU B . n 
B 2 150  THR 150  150  150  THR THR B . n 
B 2 151  PRO 151  151  151  PRO PRO B . n 
B 2 152  PHE 152  152  152  PHE PHE B . n 
B 2 153  ASP 153  153  153  ASP ASP B . n 
B 2 154  LEU 154  154  154  LEU LEU B . n 
B 2 155  ALA 155  155  155  ALA ALA B . n 
B 2 156  ILE 156  156  ?    ?   ?   B . n 
B 2 157  ASP 157  157  ?    ?   ?   B . n 
B 2 158  ASN 158  158  ?    ?   ?   B . n 
B 2 159  GLY 159  159  ?    ?   ?   B . n 
B 2 160  ASN 160  160  ?    ?   ?   B . n 
B 2 161  GLU 161  161  ?    ?   ?   B . n 
B 2 162  ASP 162  162  162  ASP ASP B . n 
B 2 163  ILE 163  163  163  ILE ILE B . n 
B 2 164  ALA 164  164  164  ALA ALA B . n 
B 2 165  GLU 165  165  165  GLU GLU B . n 
B 2 166  VAL 166  166  166  VAL VAL B . n 
B 2 167  LEU 167  167  167  LEU LEU B . n 
B 2 168  GLN 168  168  168  GLN GLN B . n 
B 2 169  LYS 169  169  169  LYS LYS B . n 
B 2 170  ALA 170  170  170  ALA ALA B . n 
B 2 171  ALA 171  171  171  ALA ALA B . n 
B 2 172  LYS 172  172  ?    ?   ?   B . n 
B 2 173  LEU 173  173  ?    ?   ?   B . n 
B 2 174  ASN 174  174  ?    ?   ?   B . n 
B 2 175  ASP 175  175  ?    ?   ?   B . n 
B 2 176  TYR 176  176  ?    ?   ?   B . n 
B 2 177  LYS 177  177  ?    ?   ?   B . n 
B 2 178  ASP 178  178  ?    ?   ?   B . n 
B 2 179  ASP 179  179  ?    ?   ?   B . n 
B 2 180  ASP 180  180  ?    ?   ?   B . n 
B 2 181  ASP 181  181  ?    ?   ?   B . n 
B 2 182  LYS 182  182  ?    ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A7Q 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A7Q 
_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         C 
_pdbx_nonpoly_scheme.entity_id       3 
_pdbx_nonpoly_scheme.mon_id          A1A7Q 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     2601 
_pdbx_nonpoly_scheme.auth_seq_num    1 
_pdbx_nonpoly_scheme.pdb_mon_id      A1A7Q 
_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 ARG 1334 ? CG  ? A ARG 2    CG  
2   1 Y 1 A ARG 1334 ? CD  ? A ARG 2    CD  
3   1 Y 1 A ARG 1334 ? NE  ? A ARG 2    NE  
4   1 Y 1 A ARG 1334 ? CZ  ? A ARG 2    CZ  
5   1 Y 1 A ARG 1334 ? NH1 ? A ARG 2    NH1 
6   1 Y 1 A ARG 1334 ? NH2 ? A ARG 2    NH2 
7   1 Y 1 A LYS 1336 ? CG  ? A LYS 4    CG  
8   1 Y 1 A LYS 1336 ? CD  ? A LYS 4    CD  
9   1 Y 1 A LYS 1336 ? CE  ? A LYS 4    CE  
10  1 Y 1 A LYS 1336 ? NZ  ? A LYS 4    NZ  
11  1 Y 1 A ARG 1398 ? CG  ? A ARG 66   CG  
12  1 Y 1 A ARG 1398 ? CD  ? A ARG 66   CD  
13  1 Y 1 A ARG 1398 ? NE  ? A ARG 66   NE  
14  1 Y 1 A ARG 1398 ? CZ  ? A ARG 66   CZ  
15  1 Y 1 A ARG 1398 ? NH1 ? A ARG 66   NH1 
16  1 Y 1 A ARG 1398 ? NH2 ? A ARG 66   NH2 
17  1 Y 1 A GLU 1400 ? CG  ? A GLU 68   CG  
18  1 Y 1 A GLU 1400 ? CD  ? A GLU 68   CD  
19  1 Y 1 A GLU 1400 ? OE1 ? A GLU 68   OE1 
20  1 Y 1 A GLU 1400 ? OE2 ? A GLU 68   OE2 
21  1 Y 1 A PHE 1401 ? CG  ? A PHE 69   CG  
22  1 Y 1 A PHE 1401 ? CD1 ? A PHE 69   CD1 
23  1 Y 1 A PHE 1401 ? CD2 ? A PHE 69   CD2 
24  1 Y 1 A PHE 1401 ? CE1 ? A PHE 69   CE1 
25  1 Y 1 A PHE 1401 ? CE2 ? A PHE 69   CE2 
26  1 Y 1 A PHE 1401 ? CZ  ? A PHE 69   CZ  
27  1 Y 1 A LYS 1432 ? CG  ? A LYS 100  CG  
28  1 Y 1 A LYS 1432 ? CD  ? A LYS 100  CD  
29  1 Y 1 A LYS 1432 ? CE  ? A LYS 100  CE  
30  1 Y 1 A LYS 1432 ? NZ  ? A LYS 100  NZ  
31  1 Y 1 A LEU 1449 ? CG  ? A LEU 117  CG  
32  1 Y 1 A LEU 1449 ? CD1 ? A LEU 117  CD1 
33  1 Y 1 A LEU 1449 ? CD2 ? A LEU 117  CD2 
34  1 Y 1 A GLN 1461 ? CG  ? A GLN 129  CG  
35  1 Y 1 A GLN 1461 ? CD  ? A GLN 129  CD  
36  1 Y 1 A GLN 1461 ? OE1 ? A GLN 129  OE1 
37  1 Y 1 A GLN 1461 ? NE2 ? A GLN 129  NE2 
38  1 Y 1 A ARG 1462 ? CG  ? A ARG 130  CG  
39  1 Y 1 A ARG 1462 ? CD  ? A ARG 130  CD  
40  1 Y 1 A ARG 1462 ? NE  ? A ARG 130  NE  
41  1 Y 1 A ARG 1462 ? CZ  ? A ARG 130  CZ  
42  1 Y 1 A ARG 1462 ? NH1 ? A ARG 130  NH1 
43  1 Y 1 A ARG 1462 ? NH2 ? A ARG 130  NH2 
44  1 Y 1 A LYS 1463 ? CG  ? A LYS 131  CG  
45  1 Y 1 A LYS 1463 ? CD  ? A LYS 131  CD  
46  1 Y 1 A LYS 1463 ? CE  ? A LYS 131  CE  
47  1 Y 1 A LYS 1463 ? NZ  ? A LYS 131  NZ  
48  1 Y 1 A CYS 1465 ? SG  ? A CYS 133  SG  
49  1 Y 1 A MET 1466 ? CG  ? A MET 134  CG  
50  1 Y 1 A MET 1466 ? SD  ? A MET 134  SD  
51  1 Y 1 A MET 1466 ? CE  ? A MET 134  CE  
52  1 Y 1 A LYS 1468 ? CG  ? A LYS 136  CG  
53  1 Y 1 A LYS 1468 ? CD  ? A LYS 136  CD  
54  1 Y 1 A LYS 1468 ? CE  ? A LYS 136  CE  
55  1 Y 1 A LYS 1468 ? NZ  ? A LYS 136  NZ  
56  1 Y 1 A ILE 1469 ? CG1 ? A ILE 137  CG1 
57  1 Y 1 A ILE 1469 ? CG2 ? A ILE 137  CG2 
58  1 Y 1 A ILE 1469 ? CD1 ? A ILE 137  CD1 
59  1 Y 1 A THR 1470 ? OG1 ? A THR 138  OG1 
60  1 Y 1 A THR 1470 ? CG2 ? A THR 138  CG2 
61  1 Y 1 A LYS 1471 ? CG  ? A LYS 139  CG  
62  1 Y 1 A LYS 1471 ? CD  ? A LYS 139  CD  
63  1 Y 1 A LYS 1471 ? CE  ? A LYS 139  CE  
64  1 Y 1 A LYS 1471 ? NZ  ? A LYS 139  NZ  
65  1 Y 1 A GLU 1472 ? CG  ? A GLU 140  CG  
66  1 Y 1 A GLU 1472 ? CD  ? A GLU 140  CD  
67  1 Y 1 A GLU 1472 ? OE1 ? A GLU 140  OE1 
68  1 Y 1 A GLU 1472 ? OE2 ? A GLU 140  OE2 
69  1 Y 1 A LEU 1473 ? CG  ? A LEU 141  CG  
70  1 Y 1 A LEU 1473 ? CD1 ? A LEU 141  CD1 
71  1 Y 1 A LEU 1473 ? CD2 ? A LEU 141  CD2 
72  1 Y 1 A LEU 1474 ? CG  ? A LEU 142  CG  
73  1 Y 1 A LEU 1474 ? CD1 ? A LEU 142  CD1 
74  1 Y 1 A LEU 1474 ? CD2 ? A LEU 142  CD2 
75  1 Y 1 A ASN 1475 ? CG  ? A ASN 143  CG  
76  1 Y 1 A ASN 1475 ? OD1 ? A ASN 143  OD1 
77  1 Y 1 A ASN 1475 ? ND2 ? A ASN 143  ND2 
78  1 Y 1 A LYS 1476 ? CG  ? A LYS 144  CG  
79  1 Y 1 A LYS 1476 ? CD  ? A LYS 144  CD  
80  1 Y 1 A LYS 1476 ? CE  ? A LYS 144  CE  
81  1 Y 1 A LYS 1476 ? NZ  ? A LYS 144  NZ  
82  1 Y 1 A ARG 1477 ? CG  ? A ARG 145  CG  
83  1 Y 1 A ARG 1477 ? CD  ? A ARG 145  CD  
84  1 Y 1 A ARG 1477 ? NE  ? A ARG 145  NE  
85  1 Y 1 A ARG 1477 ? CZ  ? A ARG 145  CZ  
86  1 Y 1 A ARG 1477 ? NH1 ? A ARG 145  NH1 
87  1 Y 1 A ARG 1477 ? NH2 ? A ARG 145  NH2 
88  1 Y 1 A ARG 1483 ? CG  ? A ARG 151  CG  
89  1 Y 1 A ARG 1483 ? CD  ? A ARG 151  CD  
90  1 Y 1 A ARG 1483 ? NE  ? A ARG 151  NE  
91  1 Y 1 A ARG 1483 ? CZ  ? A ARG 151  CZ  
92  1 Y 1 A ARG 1483 ? NH1 ? A ARG 151  NH1 
93  1 Y 1 A ARG 1483 ? NH2 ? A ARG 151  NH2 
94  1 Y 1 A TYR 1485 ? CG  ? A TYR 153  CG  
95  1 Y 1 A TYR 1485 ? CD1 ? A TYR 153  CD1 
96  1 Y 1 A TYR 1485 ? CD2 ? A TYR 153  CD2 
97  1 Y 1 A TYR 1485 ? CE1 ? A TYR 153  CE1 
98  1 Y 1 A TYR 1485 ? CE2 ? A TYR 153  CE2 
99  1 Y 1 A TYR 1485 ? CZ  ? A TYR 153  CZ  
100 1 Y 1 A TYR 1485 ? OH  ? A TYR 153  OH  
101 1 Y 1 A ASN 1489 ? CG  ? A ASN 157  CG  
102 1 Y 1 A ASN 1489 ? OD1 ? A ASN 157  OD1 
103 1 Y 1 A ASN 1489 ? ND2 ? A ASN 157  ND2 
104 1 Y 1 A GLU 1492 ? CG  ? A GLU 160  CG  
105 1 Y 1 A GLU 1492 ? CD  ? A GLU 160  CD  
106 1 Y 1 A GLU 1492 ? OE1 ? A GLU 160  OE1 
107 1 Y 1 A GLU 1492 ? OE2 ? A GLU 160  OE2 
108 1 Y 1 A ASN 1510 ? CG  ? A ASN 178  CG  
109 1 Y 1 A ASN 1510 ? OD1 ? A ASN 178  OD1 
110 1 Y 1 A ASN 1510 ? ND2 ? A ASN 178  ND2 
111 1 Y 1 A LYS 1532 ? CG  ? A LYS 200  CG  
112 1 Y 1 A LYS 1532 ? CD  ? A LYS 200  CD  
113 1 Y 1 A LYS 1532 ? CE  ? A LYS 200  CE  
114 1 Y 1 A LYS 1532 ? NZ  ? A LYS 200  NZ  
115 1 Y 1 A ILE 1533 ? CG1 ? A ILE 201  CG1 
116 1 Y 1 A ILE 1533 ? CG2 ? A ILE 201  CG2 
117 1 Y 1 A ILE 1533 ? CD1 ? A ILE 201  CD1 
118 1 Y 1 A ILE 1534 ? CG1 ? A ILE 202  CG1 
119 1 Y 1 A ILE 1534 ? CG2 ? A ILE 202  CG2 
120 1 Y 1 A ILE 1534 ? CD1 ? A ILE 202  CD1 
121 1 Y 1 A LEU 1535 ? CG  ? A LEU 203  CG  
122 1 Y 1 A LEU 1535 ? CD1 ? A LEU 203  CD1 
123 1 Y 1 A LEU 1535 ? CD2 ? A LEU 203  CD2 
124 1 Y 1 A GLU 1537 ? CG  ? A GLU 205  CG  
125 1 Y 1 A GLU 1537 ? CD  ? A GLU 205  CD  
126 1 Y 1 A GLU 1537 ? OE1 ? A GLU 205  OE1 
127 1 Y 1 A GLU 1537 ? OE2 ? A GLU 205  OE2 
128 1 Y 1 A ASN 1540 ? CG  ? A ASN 208  CG  
129 1 Y 1 A ASN 1540 ? OD1 ? A ASN 208  OD1 
130 1 Y 1 A ASN 1540 ? ND2 ? A ASN 208  ND2 
131 1 Y 1 A VAL 1541 ? CG1 ? A VAL 209  CG1 
132 1 Y 1 A VAL 1541 ? CG2 ? A VAL 209  CG2 
133 1 Y 1 A PHE 1575 ? CG  ? A PHE 243  CG  
134 1 Y 1 A PHE 1575 ? CD1 ? A PHE 243  CD1 
135 1 Y 1 A PHE 1575 ? CD2 ? A PHE 243  CD2 
136 1 Y 1 A PHE 1575 ? CE1 ? A PHE 243  CE1 
137 1 Y 1 A PHE 1575 ? CE2 ? A PHE 243  CE2 
138 1 Y 1 A PHE 1575 ? CZ  ? A PHE 243  CZ  
139 1 Y 1 A LEU 1576 ? CG  ? A LEU 244  CG  
140 1 Y 1 A LEU 1576 ? CD1 ? A LEU 244  CD1 
141 1 Y 1 A LEU 1576 ? CD2 ? A LEU 244  CD2 
142 1 Y 1 A LEU 1583 ? CG  ? A LEU 251  CG  
143 1 Y 1 A LEU 1583 ? CD1 ? A LEU 251  CD1 
144 1 Y 1 A LEU 1583 ? CD2 ? A LEU 251  CD2 
145 1 Y 1 A TYR 1596 ? CG  ? A TYR 264  CG  
146 1 Y 1 A TYR 1596 ? CD1 ? A TYR 264  CD1 
147 1 Y 1 A TYR 1596 ? CD2 ? A TYR 264  CD2 
148 1 Y 1 A TYR 1596 ? CE1 ? A TYR 264  CE1 
149 1 Y 1 A TYR 1596 ? CE2 ? A TYR 264  CE2 
150 1 Y 1 A TYR 1596 ? CZ  ? A TYR 264  CZ  
151 1 Y 1 A TYR 1596 ? OH  ? A TYR 264  OH  
152 1 Y 1 A VAL 1598 ? CG1 ? A VAL 266  CG1 
153 1 Y 1 A VAL 1598 ? CG2 ? A VAL 266  CG2 
154 1 Y 1 A GLU 1599 ? CG  ? A GLU 267  CG  
155 1 Y 1 A GLU 1599 ? CD  ? A GLU 267  CD  
156 1 Y 1 A GLU 1599 ? OE1 ? A GLU 267  OE1 
157 1 Y 1 A GLU 1599 ? OE2 ? A GLU 267  OE2 
158 1 Y 1 A LEU 1603 ? CG  ? A LEU 271  CG  
159 1 Y 1 A LEU 1603 ? CD1 ? A LEU 271  CD1 
160 1 Y 1 A LEU 1603 ? CD2 ? A LEU 271  CD2 
161 1 Y 1 A LYS 1605 ? CG  ? A LYS 273  CG  
162 1 Y 1 A LYS 1605 ? CD  ? A LYS 273  CD  
163 1 Y 1 A LYS 1605 ? CE  ? A LYS 273  CE  
164 1 Y 1 A LYS 1605 ? NZ  ? A LYS 273  NZ  
165 1 Y 1 A MET 1607 ? CG  ? A MET 275  CG  
166 1 Y 1 A MET 1607 ? SD  ? A MET 275  SD  
167 1 Y 1 A MET 1607 ? CE  ? A MET 275  CE  
168 1 Y 1 A LEU 1611 ? CG  ? A LEU 279  CG  
169 1 Y 1 A LEU 1611 ? CD1 ? A LEU 279  CD1 
170 1 Y 1 A LEU 1611 ? CD2 ? A LEU 279  CD2 
171 1 Y 1 A ARG 1639 ? CG  ? A ARG 307  CG  
172 1 Y 1 A ARG 1639 ? CD  ? A ARG 307  CD  
173 1 Y 1 A ARG 1639 ? NE  ? A ARG 307  NE  
174 1 Y 1 A ARG 1639 ? CZ  ? A ARG 307  CZ  
175 1 Y 1 A ARG 1639 ? NH1 ? A ARG 307  NH1 
176 1 Y 1 A ARG 1639 ? NH2 ? A ARG 307  NH2 
177 1 Y 1 A LYS 1640 ? CG  ? A LYS 308  CG  
178 1 Y 1 A LYS 1640 ? CD  ? A LYS 308  CD  
179 1 Y 1 A LYS 1640 ? CE  ? A LYS 308  CE  
180 1 Y 1 A LYS 1640 ? NZ  ? A LYS 308  NZ  
181 1 Y 1 A PHE 1641 ? CG  ? A PHE 309  CG  
182 1 Y 1 A PHE 1641 ? CD1 ? A PHE 309  CD1 
183 1 Y 1 A PHE 1641 ? CD2 ? A PHE 309  CD2 
184 1 Y 1 A PHE 1641 ? CE1 ? A PHE 309  CE1 
185 1 Y 1 A PHE 1641 ? CE2 ? A PHE 309  CE2 
186 1 Y 1 A PHE 1641 ? CZ  ? A PHE 309  CZ  
187 1 Y 1 A LYS 1643 ? CG  ? A LYS 311  CG  
188 1 Y 1 A LYS 1643 ? CD  ? A LYS 311  CD  
189 1 Y 1 A LYS 1643 ? CE  ? A LYS 311  CE  
190 1 Y 1 A LYS 1643 ? NZ  ? A LYS 311  NZ  
191 1 Y 1 A LYS 1651 ? CG  ? A LYS 319  CG  
192 1 Y 1 A LYS 1651 ? CD  ? A LYS 319  CD  
193 1 Y 1 A LYS 1651 ? CE  ? A LYS 319  CE  
194 1 Y 1 A LYS 1651 ? NZ  ? A LYS 319  NZ  
195 1 Y 1 A LEU 1652 ? CG  ? A LEU 320  CG  
196 1 Y 1 A LEU 1652 ? CD1 ? A LEU 320  CD1 
197 1 Y 1 A LEU 1652 ? CD2 ? A LEU 320  CD2 
198 1 Y 1 A LEU 1653 ? CG  ? A LEU 321  CG  
199 1 Y 1 A LEU 1653 ? CD1 ? A LEU 321  CD1 
200 1 Y 1 A LEU 1653 ? CD2 ? A LEU 321  CD2 
201 1 Y 1 A GLU 1654 ? CG  ? A GLU 322  CG  
202 1 Y 1 A GLU 1654 ? CD  ? A GLU 322  CD  
203 1 Y 1 A GLU 1654 ? OE1 ? A GLU 322  OE1 
204 1 Y 1 A GLU 1654 ? OE2 ? A GLU 322  OE2 
205 1 Y 1 A LYS 1655 ? CG  ? A LYS 323  CG  
206 1 Y 1 A LYS 1655 ? CD  ? A LYS 323  CD  
207 1 Y 1 A LYS 1655 ? CE  ? A LYS 323  CE  
208 1 Y 1 A LYS 1655 ? NZ  ? A LYS 323  NZ  
209 1 Y 1 A GLN 1657 ? CG  ? A GLN 325  CG  
210 1 Y 1 A GLN 1657 ? CD  ? A GLN 325  CD  
211 1 Y 1 A GLN 1657 ? OE1 ? A GLN 325  OE1 
212 1 Y 1 A GLN 1657 ? NE2 ? A GLN 325  NE2 
213 1 Y 1 A LEU 1668 ? CG  ? A LEU 336  CG  
214 1 Y 1 A LEU 1668 ? CD1 ? A LEU 336  CD1 
215 1 Y 1 A LEU 1668 ? CD2 ? A LEU 336  CD2 
216 1 Y 1 A VAL 1669 ? CG1 ? A VAL 337  CG1 
217 1 Y 1 A VAL 1669 ? CG2 ? A VAL 337  CG2 
218 1 Y 1 A HIS 1684 ? CG  ? A HIS 352  CG  
219 1 Y 1 A HIS 1684 ? ND1 ? A HIS 352  ND1 
220 1 Y 1 A HIS 1684 ? CD2 ? A HIS 352  CD2 
221 1 Y 1 A HIS 1684 ? CE1 ? A HIS 352  CE1 
222 1 Y 1 A HIS 1684 ? NE2 ? A HIS 352  NE2 
223 1 Y 1 A CYS 1685 ? SG  ? A CYS 353  SG  
224 1 Y 1 A GLU 1686 ? CG  ? A GLU 354  CG  
225 1 Y 1 A GLU 1686 ? CD  ? A GLU 354  CD  
226 1 Y 1 A GLU 1686 ? OE1 ? A GLU 354  OE1 
227 1 Y 1 A GLU 1686 ? OE2 ? A GLU 354  OE2 
228 1 Y 1 A MET 1702 ? CG  ? A MET 370  CG  
229 1 Y 1 A MET 1702 ? SD  ? A MET 370  SD  
230 1 Y 1 A MET 1702 ? CE  ? A MET 370  CE  
231 1 Y 1 A MET 1732 ? CG  ? A MET 400  CG  
232 1 Y 1 A MET 1732 ? SD  ? A MET 400  SD  
233 1 Y 1 A MET 1732 ? CE  ? A MET 400  CE  
234 1 Y 1 A GLU 1760 ? CG  ? A GLU 428  CG  
235 1 Y 1 A GLU 1760 ? CD  ? A GLU 428  CD  
236 1 Y 1 A GLU 1760 ? OE1 ? A GLU 428  OE1 
237 1 Y 1 A GLU 1760 ? OE2 ? A GLU 428  OE2 
238 1 Y 1 A GLU 1789 ? CG  ? A GLU 457  CG  
239 1 Y 1 A GLU 1789 ? CD  ? A GLU 457  CD  
240 1 Y 1 A GLU 1789 ? OE1 ? A GLU 457  OE1 
241 1 Y 1 A GLU 1789 ? OE2 ? A GLU 457  OE2 
242 1 Y 1 A GLU 1790 ? CG  ? A GLU 458  CG  
243 1 Y 1 A GLU 1790 ? CD  ? A GLU 458  CD  
244 1 Y 1 A GLU 1790 ? OE1 ? A GLU 458  OE1 
245 1 Y 1 A GLU 1790 ? OE2 ? A GLU 458  OE2 
246 1 Y 1 A LEU 1807 ? CG  ? A LEU 475  CG  
247 1 Y 1 A LEU 1807 ? CD1 ? A LEU 475  CD1 
248 1 Y 1 A LEU 1807 ? CD2 ? A LEU 475  CD2 
249 1 Y 1 A LYS 1809 ? CG  ? A LYS 477  CG  
250 1 Y 1 A LYS 1809 ? CD  ? A LYS 477  CD  
251 1 Y 1 A LYS 1809 ? CE  ? A LYS 477  CE  
252 1 Y 1 A LYS 1809 ? NZ  ? A LYS 477  NZ  
253 1 Y 1 A GLU 1820 ? CG  ? A GLU 488  CG  
254 1 Y 1 A GLU 1820 ? CD  ? A GLU 488  CD  
255 1 Y 1 A GLU 1820 ? OE1 ? A GLU 488  OE1 
256 1 Y 1 A GLU 1820 ? OE2 ? A GLU 488  OE2 
257 1 Y 1 A LYS 1824 ? CG  ? A LYS 492  CG  
258 1 Y 1 A LYS 1824 ? CD  ? A LYS 492  CD  
259 1 Y 1 A LYS 1824 ? CE  ? A LYS 492  CE  
260 1 Y 1 A LYS 1824 ? NZ  ? A LYS 492  NZ  
261 1 Y 1 A MET 1831 ? CG  ? A MET 499  CG  
262 1 Y 1 A MET 1831 ? SD  ? A MET 499  SD  
263 1 Y 1 A MET 1831 ? CE  ? A MET 499  CE  
264 1 Y 1 A ASN 1842 ? CG  ? A ASN 510  CG  
265 1 Y 1 A ASN 1842 ? OD1 ? A ASN 510  OD1 
266 1 Y 1 A ASN 1842 ? ND2 ? A ASN 510  ND2 
267 1 Y 1 A ASP 1844 ? CG  ? A ASP 512  CG  
268 1 Y 1 A ASP 1844 ? OD1 ? A ASP 512  OD1 
269 1 Y 1 A ASP 1844 ? OD2 ? A ASP 512  OD2 
270 1 Y 1 A GLN 1845 ? CG  ? A GLN 513  CG  
271 1 Y 1 A GLN 1845 ? CD  ? A GLN 513  CD  
272 1 Y 1 A GLN 1845 ? OE1 ? A GLN 513  OE1 
273 1 Y 1 A GLN 1845 ? NE2 ? A GLN 513  NE2 
274 1 Y 1 A ARG 1866 ? CG  ? A ARG 534  CG  
275 1 Y 1 A ARG 1866 ? CD  ? A ARG 534  CD  
276 1 Y 1 A ARG 1866 ? NE  ? A ARG 534  NE  
277 1 Y 1 A ARG 1866 ? CZ  ? A ARG 534  CZ  
278 1 Y 1 A ARG 1866 ? NH1 ? A ARG 534  NH1 
279 1 Y 1 A ARG 1866 ? NH2 ? A ARG 534  NH2 
280 1 Y 1 A GLU 1874 ? CG  ? A GLU 542  CG  
281 1 Y 1 A GLU 1874 ? CD  ? A GLU 542  CD  
282 1 Y 1 A GLU 1874 ? OE1 ? A GLU 542  OE1 
283 1 Y 1 A GLU 1874 ? OE2 ? A GLU 542  OE2 
284 1 Y 1 A GLU 1882 ? CG  ? A GLU 550  CG  
285 1 Y 1 A GLU 1882 ? CD  ? A GLU 550  CD  
286 1 Y 1 A GLU 1882 ? OE1 ? A GLU 550  OE1 
287 1 Y 1 A GLU 1882 ? OE2 ? A GLU 550  OE2 
288 1 Y 1 A HIS 1911 ? CG  ? A HIS 579  CG  
289 1 Y 1 A HIS 1911 ? ND1 ? A HIS 579  ND1 
290 1 Y 1 A HIS 1911 ? CD2 ? A HIS 579  CD2 
291 1 Y 1 A HIS 1911 ? CE1 ? A HIS 579  CE1 
292 1 Y 1 A HIS 1911 ? NE2 ? A HIS 579  NE2 
293 1 Y 1 A ARG 1943 ? CG  ? A ARG 611  CG  
294 1 Y 1 A ARG 1943 ? CD  ? A ARG 611  CD  
295 1 Y 1 A ARG 1943 ? NE  ? A ARG 611  NE  
296 1 Y 1 A ARG 1943 ? CZ  ? A ARG 611  CZ  
297 1 Y 1 A ARG 1943 ? NH1 ? A ARG 611  NH1 
298 1 Y 1 A ARG 1943 ? NH2 ? A ARG 611  NH2 
299 1 Y 1 A MET 1989 ? CG  ? A MET 657  CG  
300 1 Y 1 A MET 1989 ? SD  ? A MET 657  SD  
301 1 Y 1 A MET 1989 ? CE  ? A MET 657  CE  
302 1 Y 1 A LYS 2091 ? CG  ? A LYS 759  CG  
303 1 Y 1 A LYS 2091 ? CD  ? A LYS 759  CD  
304 1 Y 1 A LYS 2091 ? CE  ? A LYS 759  CE  
305 1 Y 1 A LYS 2091 ? NZ  ? A LYS 759  NZ  
306 1 Y 1 A LYS 2097 ? CG  ? A LYS 765  CG  
307 1 Y 1 A LYS 2097 ? CD  ? A LYS 765  CD  
308 1 Y 1 A LYS 2097 ? CE  ? A LYS 765  CE  
309 1 Y 1 A LYS 2097 ? NZ  ? A LYS 765  NZ  
310 1 Y 1 A GLN 2120 ? CG  ? A GLN 788  CG  
311 1 Y 1 A GLN 2120 ? CD  ? A GLN 788  CD  
312 1 Y 1 A GLN 2120 ? OE1 ? A GLN 788  OE1 
313 1 Y 1 A GLN 2120 ? NE2 ? A GLN 788  NE2 
314 1 Y 1 A GLU 2121 ? CG  ? A GLU 789  CG  
315 1 Y 1 A GLU 2121 ? CD  ? A GLU 789  CD  
316 1 Y 1 A GLU 2121 ? OE1 ? A GLU 789  OE1 
317 1 Y 1 A GLU 2121 ? OE2 ? A GLU 789  OE2 
318 1 Y 1 A LYS 2148 ? CG  ? A LYS 816  CG  
319 1 Y 1 A LYS 2148 ? CD  ? A LYS 816  CD  
320 1 Y 1 A LYS 2148 ? CE  ? A LYS 816  CE  
321 1 Y 1 A LYS 2148 ? NZ  ? A LYS 816  NZ  
322 1 Y 1 A ASN 2164 ? CG  ? A ASN 832  CG  
323 1 Y 1 A ASN 2164 ? OD1 ? A ASN 832  OD1 
324 1 Y 1 A ASN 2164 ? ND2 ? A ASN 832  ND2 
325 1 Y 1 A ASN 2228 ? CG  ? A ASN 896  CG  
326 1 Y 1 A ASN 2228 ? OD1 ? A ASN 896  OD1 
327 1 Y 1 A ASN 2228 ? ND2 ? A ASN 896  ND2 
328 1 Y 1 A GLU 2230 ? CG  ? A GLU 898  CG  
329 1 Y 1 A GLU 2230 ? CD  ? A GLU 898  CD  
330 1 Y 1 A GLU 2230 ? OE1 ? A GLU 898  OE1 
331 1 Y 1 A GLU 2230 ? OE2 ? A GLU 898  OE2 
332 1 Y 1 A ASP 2231 ? CG  ? A ASP 899  CG  
333 1 Y 1 A ASP 2231 ? OD1 ? A ASP 899  OD1 
334 1 Y 1 A ASP 2231 ? OD2 ? A ASP 899  OD2 
335 1 Y 1 A LYS 2233 ? CG  ? A LYS 901  CG  
336 1 Y 1 A LYS 2233 ? CD  ? A LYS 901  CD  
337 1 Y 1 A LYS 2233 ? CE  ? A LYS 901  CE  
338 1 Y 1 A LYS 2233 ? NZ  ? A LYS 901  NZ  
339 1 Y 1 A LYS 2234 ? CG  ? A LYS 902  CG  
340 1 Y 1 A LYS 2234 ? CD  ? A LYS 902  CD  
341 1 Y 1 A LYS 2234 ? CE  ? A LYS 902  CE  
342 1 Y 1 A LYS 2234 ? NZ  ? A LYS 902  NZ  
343 1 Y 1 A GLU 2276 ? CG  ? A GLU 944  CG  
344 1 Y 1 A GLU 2276 ? CD  ? A GLU 944  CD  
345 1 Y 1 A GLU 2276 ? OE1 ? A GLU 944  OE1 
346 1 Y 1 A GLU 2276 ? OE2 ? A GLU 944  OE2 
347 1 Y 1 A LYS 2278 ? CG  ? A LYS 946  CG  
348 1 Y 1 A LYS 2278 ? CD  ? A LYS 946  CD  
349 1 Y 1 A LYS 2278 ? CE  ? A LYS 946  CE  
350 1 Y 1 A LYS 2278 ? NZ  ? A LYS 946  NZ  
351 1 Y 1 A LYS 2281 ? CG  ? A LYS 949  CG  
352 1 Y 1 A LYS 2281 ? CD  ? A LYS 949  CD  
353 1 Y 1 A LYS 2281 ? CE  ? A LYS 949  CE  
354 1 Y 1 A LYS 2281 ? NZ  ? A LYS 949  NZ  
355 1 Y 1 A ASP 2438 ? CG  ? A ASP 1106 CG  
356 1 Y 1 A ASP 2438 ? OD1 ? A ASP 1106 OD1 
357 1 Y 1 A ASP 2438 ? OD2 ? A ASP 1106 OD2 
358 1 Y 1 A ARG 2443 ? CG  ? A ARG 1111 CG  
359 1 Y 1 A ARG 2443 ? CD  ? A ARG 1111 CD  
360 1 Y 1 A ARG 2443 ? NE  ? A ARG 1111 NE  
361 1 Y 1 A ARG 2443 ? CZ  ? A ARG 1111 CZ  
362 1 Y 1 A ARG 2443 ? NH1 ? A ARG 1111 NH1 
363 1 Y 1 A ARG 2443 ? NH2 ? A ARG 1111 NH2 
364 1 Y 1 A PHE 2451 ? CG  ? A PHE 1119 CG  
365 1 Y 1 A PHE 2451 ? CD1 ? A PHE 1119 CD1 
366 1 Y 1 A PHE 2451 ? CD2 ? A PHE 1119 CD2 
367 1 Y 1 A PHE 2451 ? CE1 ? A PHE 1119 CE1 
368 1 Y 1 A PHE 2451 ? CE2 ? A PHE 1119 CE2 
369 1 Y 1 A PHE 2451 ? CZ  ? A PHE 1119 CZ  
370 1 Y 1 A ASN 2453 ? CG  ? A ASN 1121 CG  
371 1 Y 1 A ASN 2453 ? OD1 ? A ASN 1121 OD1 
372 1 Y 1 A ASN 2453 ? ND2 ? A ASN 1121 ND2 
373 1 Y 1 A ARG 2456 ? CG  ? A ARG 1124 CG  
374 1 Y 1 A ARG 2456 ? CD  ? A ARG 1124 CD  
375 1 Y 1 A ARG 2456 ? NE  ? A ARG 1124 NE  
376 1 Y 1 A ARG 2456 ? CZ  ? A ARG 1124 CZ  
377 1 Y 1 A ARG 2456 ? NH1 ? A ARG 1124 NH1 
378 1 Y 1 A ARG 2456 ? NH2 ? A ARG 1124 NH2 
379 1 Y 1 B GLU 63   ? CG  ? B GLU 63   CG  
380 1 Y 1 B GLU 63   ? CD  ? B GLU 63   CD  
381 1 Y 1 B GLU 63   ? OE1 ? B GLU 63   OE1 
382 1 Y 1 B GLU 63   ? OE2 ? B GLU 63   OE2 
383 1 Y 1 B ILE 64   ? CG1 ? B ILE 64   CG1 
384 1 Y 1 B ILE 64   ? CG2 ? B ILE 64   CG2 
385 1 Y 1 B ILE 64   ? CD1 ? B ILE 64   CD1 
386 1 Y 1 B GLU 66   ? CG  ? B GLU 66   CG  
387 1 Y 1 B GLU 66   ? CD  ? B GLU 66   CD  
388 1 Y 1 B GLU 66   ? OE1 ? B GLU 66   OE1 
389 1 Y 1 B GLU 66   ? OE2 ? B GLU 66   OE2 
390 1 Y 1 B VAL 67   ? CG1 ? B VAL 67   CG1 
391 1 Y 1 B VAL 67   ? CG2 ? B VAL 67   CG2 
392 1 Y 1 B LEU 69   ? CG  ? B LEU 69   CG  
393 1 Y 1 B LEU 69   ? CD1 ? B LEU 69   CD1 
394 1 Y 1 B LEU 69   ? CD2 ? B LEU 69   CD2 
395 1 Y 1 B LYS 70   ? CG  ? B LYS 70   CG  
396 1 Y 1 B LYS 70   ? CD  ? B LYS 70   CD  
397 1 Y 1 B LYS 70   ? CE  ? B LYS 70   CE  
398 1 Y 1 B LYS 70   ? NZ  ? B LYS 70   NZ  
399 1 Y 1 B ASN 76   ? CG  ? B ASN 76   CG  
400 1 Y 1 B ASN 76   ? OD1 ? B ASN 76   OD1 
401 1 Y 1 B ASN 76   ? ND2 ? B ASN 76   ND2 
402 1 Y 1 B TRP 78   ? CG  ? B TRP 78   CG  
403 1 Y 1 B TRP 78   ? CD1 ? B TRP 78   CD1 
404 1 Y 1 B TRP 78   ? CD2 ? B TRP 78   CD2 
405 1 Y 1 B TRP 78   ? NE1 ? B TRP 78   NE1 
406 1 Y 1 B TRP 78   ? CE2 ? B TRP 78   CE2 
407 1 Y 1 B TRP 78   ? CE3 ? B TRP 78   CE3 
408 1 Y 1 B TRP 78   ? CZ2 ? B TRP 78   CZ2 
409 1 Y 1 B TRP 78   ? CZ3 ? B TRP 78   CZ3 
410 1 Y 1 B TRP 78   ? CH2 ? B TRP 78   CH2 
411 1 Y 1 B GLN 111  ? CG  ? B GLN 111  CG  
412 1 Y 1 B GLN 111  ? CD  ? B GLN 111  CD  
413 1 Y 1 B GLN 111  ? OE1 ? B GLN 111  OE1 
414 1 Y 1 B GLN 111  ? NE2 ? B GLN 111  NE2 
415 1 Y 1 B LEU 124  ? CG  ? B LEU 124  CG  
416 1 Y 1 B LEU 124  ? CD1 ? B LEU 124  CD1 
417 1 Y 1 B LEU 124  ? CD2 ? B LEU 124  CD2 
418 1 Y 1 B LEU 128  ? CG  ? B LEU 128  CG  
419 1 Y 1 B LEU 128  ? CD1 ? B LEU 128  CD1 
420 1 Y 1 B LEU 128  ? CD2 ? B LEU 128  CD2 
421 1 Y 1 B GLU 129  ? CG  ? B GLU 129  CG  
422 1 Y 1 B GLU 129  ? CD  ? B GLU 129  CD  
423 1 Y 1 B GLU 129  ? OE1 ? B GLU 129  OE1 
424 1 Y 1 B GLU 129  ? OE2 ? B GLU 129  OE2 
425 1 Y 1 B GLU 132  ? CG  ? B GLU 132  CG  
426 1 Y 1 B GLU 132  ? CD  ? B GLU 132  CD  
427 1 Y 1 B GLU 132  ? OE1 ? B GLU 132  OE1 
428 1 Y 1 B GLU 132  ? OE2 ? B GLU 132  OE2 
429 1 Y 1 B LYS 136  ? CG  ? B LYS 136  CG  
430 1 Y 1 B LYS 136  ? CD  ? B LYS 136  CD  
431 1 Y 1 B LYS 136  ? CE  ? B LYS 136  CE  
432 1 Y 1 B LYS 136  ? NZ  ? B LYS 136  NZ  
433 1 Y 1 B GLU 149  ? CG  ? B GLU 149  CG  
434 1 Y 1 B GLU 149  ? CD  ? B GLU 149  CD  
435 1 Y 1 B GLU 149  ? OE1 ? B GLU 149  OE1 
436 1 Y 1 B GLU 149  ? OE2 ? B GLU 149  OE2 
437 1 Y 1 B PHE 152  ? CG  ? B PHE 152  CG  
438 1 Y 1 B PHE 152  ? CD1 ? B PHE 152  CD1 
439 1 Y 1 B PHE 152  ? CD2 ? B PHE 152  CD2 
440 1 Y 1 B PHE 152  ? CE1 ? B PHE 152  CE1 
441 1 Y 1 B PHE 152  ? CE2 ? B PHE 152  CE2 
442 1 Y 1 B PHE 152  ? CZ  ? B PHE 152  CZ  
443 1 Y 1 B ASP 153  ? CG  ? B ASP 153  CG  
444 1 Y 1 B ASP 153  ? OD1 ? B ASP 153  OD1 
445 1 Y 1 B ASP 153  ? OD2 ? B ASP 153  OD2 
# 
_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                     9DMI 
_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                         9DMI 
_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                   9DMI 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DMI 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.35 
_refine.ls_d_res_low                             ? 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.006 ? 8105  ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.897 ? 11026 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 6.070 ? 1104  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.054 ? 1316  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.007 ? 1376  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9DMI 
_struct.title                        'Structure of the C-terminal half of LRRK2 bound to RN277 (Type-II inhibitor)' 
_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        9DMI 
_struct_keywords.text            'GTPase, Kinase, inhibitors, PROTEIN BINDING' 
_struct_keywords.pdbx_keywords   'PROTEIN BINDING' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
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 LRRK2_HUMAN Q5S007 ? 1 
;NRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQR
ALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATE
ESDALAKLRKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENELPHA
VHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRRDVEKFLSKKRKFPKNYMSQYFKL
LEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRM
YWRQGIYLNWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWA
LYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEQAPEFLLGDGSFGS
VYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQH
RIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQ
QADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEKLIKQCLKENPQERPTSAQVFDIL
NSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKE
SWIVSGTQSGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLKILN
IGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAFSDSNIITVVVDTALYIAKQNSPV
VEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFC
NSVRVMMTAQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE
;
1333 
2 PDB 9DMI        9DMI   ? 2 ? 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 9DMI A 1 ? 1195 ? Q5S007 1333 ? 2527 ? 1333 2527 
2 2 9DMI B 1 ? 182  ? 9DMI   1    ? 182  ? 1    182  
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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 GLY A 12   ? MET A 23   ? GLY A 1344 MET A 1355 1 ? 12 
HELX_P HELX_P2  AA2 MET A 99   ? ALA A 108  ? MET A 1431 ALA A 1440 1 ? 10 
HELX_P HELX_P3  AA3 ARG A 130  ? ASN A 143  ? ARG A 1462 ASN A 1475 1 ? 14 
HELX_P HELX_P4  AA4 SER A 162  ? LEU A 177  ? SER A 1494 LEU A 1509 1 ? 16 
HELX_P HELX_P5  AA5 GLU A 197  ? VAL A 209  ? GLU A 1529 VAL A 1541 1 ? 13 
HELX_P HELX_P6  AA6 LEU A 244  ? GLY A 248  ? LEU A 1576 GLY A 1580 5 ? 5  
HELX_P HELX_P7  AA7 GLU A 267  ? VAL A 281  ? GLU A 1599 VAL A 1613 1 ? 15 
HELX_P HELX_P8  AA8 TYR A 313  ? LYS A 323  ? TYR A 1645 LYS A 1655 1 ? 11 
HELX_P HELX_P9  AA9 GLY A 371  ? LEU A 380  ? GLY A 1703 LEU A 1712 1 ? 10 
HELX_P HELX_P10 AB1 CYS A 438  ? TRP A 459  ? CYS A 1770 TRP A 1791 1 ? 22 
HELX_P HELX_P11 AB2 LEU A 495  ? GLU A 504  ? LEU A 1827 GLU A 1836 1 ? 10 
HELX_P HELX_P12 AB3 SER A 521  ? ILE A 523  ? SER A 1853 ILE A 1855 5 ? 3  
HELX_P HELX_P13 AB4 ALA A 524  ? ILE A 528  ? ALA A 1856 ILE A 1860 5 ? 5  
HELX_P HELX_P14 AB5 ALA A 548  ? LEU A 552  ? ALA A 1880 LEU A 1884 5 ? 5  
HELX_P HELX_P15 AB6 ARG A 583  ? CYS A 593  ? ARG A 1915 CYS A 1925 1 ? 11 
HELX_P HELX_P16 AB7 LEU A 623  ? ASP A 630  ? LEU A 1955 ASP A 1962 1 ? 8  
HELX_P HELX_P17 AB8 LYS A 631  ? LEU A 634  ? LYS A 1963 LEU A 1966 5 ? 4  
HELX_P HELX_P18 AB9 THR A 635  ? ALA A 656  ? THR A 1967 ALA A 1988 1 ? 22 
HELX_P HELX_P19 AC1 ASN A 719  ? THR A 737  ? ASN A 2051 THR A 2069 1 ? 19 
HELX_P HELX_P20 AC2 ASP A 762  ? GLY A 768  ? ASP A 2094 GLY A 2100 1 ? 7  
HELX_P HELX_P21 AC3 VAL A 775  ? LEU A 783  ? VAL A 2107 LEU A 2115 1 ? 9  
HELX_P HELX_P22 AC4 THR A 792  ? ASN A 801  ? THR A 2124 ASN A 2133 1 ? 10 
HELX_P HELX_P23 AC5 SER A 802  ? LEU A 808  ? SER A 2134 LEU A 2140 1 ? 7  
HELX_P HELX_P24 AC6 LYS A 946  ? LEU A 950  ? LYS A 2278 LEU A 2282 5 ? 5  
HELX_P HELX_P25 AC7 ARG A 1007 ? PHE A 1012 ? ARG A 2339 PHE A 2344 5 ? 6  
HELX_P HELX_P26 AC8 TYR A 1014 ? ASP A 1019 ? TYR A 2346 ASP A 2351 1 ? 6  
HELX_P HELX_P27 AC9 CYS A 1057 ? ARG A 1062 ? CYS A 2389 ARG A 2394 1 ? 6  
HELX_P HELX_P28 AD1 ASN A 1167 ? VAL A 1194 ? ASN A 2499 VAL A 2526 1 ? 28 
HELX_P HELX_P29 AD2 LEU B 53   ? GLY B 60   ? LEU B 53   GLY B 60   1 ? 8  
HELX_P HELX_P30 AD3 HIS B 61   ? THR B 71   ? HIS B 61   THR B 71   1 ? 11 
HELX_P HELX_P31 AD4 THR B 84   ? GLY B 93   ? THR B 84   GLY B 93   1 ? 10 
HELX_P HELX_P32 AD5 LEU B 95   ? ALA B 106  ? LEU B 95   ALA B 106  1 ? 12 
HELX_P HELX_P33 AD6 THR B 117  ? TYR B 125  ? THR B 117  TYR B 125  1 ? 9  
HELX_P HELX_P34 AD7 GLU B 129  ? HIS B 137  ? GLU B 129  HIS B 137  1 ? 9  
HELX_P HELX_P35 AD8 THR B 150  ? ALA B 155  ? THR B 150  ALA B 155  1 ? 6  
HELX_P HELX_P36 AD9 ILE B 163  ? ALA B 171  ? ILE B 163  ALA B 171  1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            1120 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           A 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            1160 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             2452 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             2492 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.036 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       1120 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      1160 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        2452 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       2492 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 3 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASP A 40   ? TRP A 44   ? ASP A 1372 TRP A 1376 
AA1 2 LEU A 58   ? ASP A 62   ? LEU A 1390 ASP A 1394 
AA1 3 MET A 3    ? GLY A 9    ? MET A 1335 GLY A 1341 
AA1 4 TYR A 83   ? TYR A 87   ? TYR A 1415 TYR A 1419 
AA1 5 VAL A 115  ? GLY A 119  ? VAL A 1447 GLY A 1451 
AA1 6 ILE A 150  ? HIS A 154  ? ILE A 1482 HIS A 1486 
AA2 1 SER A 429  ? PRO A 436  ? SER A 1761 PRO A 1768 
AA2 2 ILE A 358  ? MET A 365  ? ILE A 1690 MET A 1697 
AA2 3 LYS A 477  ? TYR A 482  ? LYS A 1809 TYR A 1814 
AA2 4 GLN A 491  ? LEU A 494  ? GLN A 1823 LEU A 1826 
AA3 1 LEU A 507  ? LEU A 508  ? LEU A 1839 LEU A 1840 
AA3 2 ILE A 518  ? PRO A 519  ? ILE A 1850 PRO A 1851 
AA4 1 VAL A 561  ? TYR A 566  ? VAL A 1893 TYR A 1898 
AA4 2 GLU A 569  ? ILE A 575  ? GLU A 1901 ILE A 1907 
AA4 3 MET A 612  ? GLU A 616  ? MET A 1944 GLU A 1948 
AA4 4 LEU A 603  ? GLY A 607  ? LEU A 1935 GLY A 1939 
AA5 1 GLY A 621  ? SER A 622  ? GLY A 1953 SER A 1954 
AA5 2 VAL A 668  ? LEU A 670  ? VAL A 2000 LEU A 2002 
AA5 3 ALA A 681  ? ILE A 683  ? ALA A 2013 ILE A 2015 
AA6 1 ARG A 810  ? LEU A 813  ? ARG A 2142 LEU A 2145 
AA6 2 SER A 1159 ? ASP A 1165 ? SER A 2491 ASP A 2497 
AA6 3 VAL A 1137 ? TYR A 1143 ? VAL A 2469 TYR A 2475 
AA6 4 SER A 1122 ? ALA A 1129 ? SER A 2454 ALA A 2461 
AA7 1 VAL A 820  ? ALA A 825  ? VAL A 2152 ALA A 2157 
AA7 2 SER A 834  ? CYS A 839  ? SER A 2166 CYS A 2171 
AA7 3 GLN A 846  ? ASP A 851  ? GLN A 2178 ASP A 2183 
AA7 4 THR A 858  ? GLU A 861  ? THR A 2190 GLU A 2193 
AA8 1 ILE A 867  ? VAL A 873  ? ILE A 2199 VAL A 2205 
AA8 2 TRP A 882  ? THR A 887  ? TRP A 2214 THR A 2219 
AA8 3 LEU A 892  ? ASN A 896  ? LEU A 2224 ASN A 2228 
AA8 4 HIS A 904  ? THR A 905  ? HIS A 2236 THR A 2237 
AA9 1 VAL A 913  ? LEU A 916  ? VAL A 2245 LEU A 2248 
AA9 2 LEU A 932  ? THR A 935  ? LEU A 2264 THR A 2267 
AA9 3 LYS A 939  ? ILE A 942  ? LYS A 2271 ILE A 2274 
AA9 4 ILE A 958  ? ASN A 960  ? ILE A 2290 ASN A 2292 
AB1 1 LEU A 968  ? GLU A 973  ? LEU A 2300 GLU A 2305 
AB1 2 MET A 983  ? CYS A 987  ? MET A 2315 CYS A 2319 
AB1 3 LYS A 990  ? PHE A 994  ? LYS A 2322 PHE A 2326 
AB1 4 ILE A 1000 ? GLU A 1005 ? ILE A 2332 GLU A 2337 
AB2 1 ILE A 1022 ? VAL A 1027 ? ILE A 2354 VAL A 2359 
AB2 2 LEU A 1031 ? LYS A 1035 ? LEU A 2363 LYS A 2367 
AB2 3 VAL A 1040 ? TRP A 1044 ? VAL A 2372 TRP A 2376 
AB2 4 LEU A 1051 ? ASP A 1056 ? LEU A 2383 ASP A 2388 
AB3 1 VAL A 1082 ? GLN A 1088 ? VAL A 2414 GLN A 2420 
AB3 2 ALA A 1092 ? THR A 1097 ? ALA A 2424 THR A 2429 
AB3 3 HIS A 1101 ? ASP A 1106 ? HIS A 2433 ASP A 2438 
AB3 4 ARG A 1111 ? TYR A 1117 ? ARG A 2443 TYR A 2449 
# 
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 TRP A 44   ? N TRP A 1376 O LEU A 58   ? O LEU A 1390 
AA1 2 3 O TRP A 61   ? O TRP A 1393 N ILE A 7    ? N ILE A 1339 
AA1 3 4 N VAL A 8    ? N VAL A 1340 O VAL A 86   ? O VAL A 1418 
AA1 4 5 N ALA A 85   ? N ALA A 1417 O VAL A 118  ? O VAL A 1450 
AA1 5 6 N VAL A 115  ? N VAL A 1447 O ARG A 151  ? O ARG A 1483 
AA2 1 2 O LEU A 431  ? O LEU A 1763 N TYR A 363  ? N TYR A 1695 
AA2 2 3 N LEU A 362  ? N LEU A 1694 O TRP A 479  ? O TRP A 1811 
AA2 3 4 N ALA A 480  ? N ALA A 1812 O ILE A 493  ? O ILE A 1825 
AA3 1 2 N LEU A 508  ? N LEU A 1840 O ILE A 518  ? O ILE A 1850 
AA4 1 2 N TYR A 562  ? N TYR A 1894 O VAL A 573  ? O VAL A 1905 
AA4 2 3 N ALA A 572  ? N ALA A 1904 O MET A 615  ? O MET A 1947 
AA4 3 4 O MET A 612  ? O MET A 1944 N GLY A 607  ? N GLY A 1939 
AA5 1 2 N GLY A 621  ? N GLY A 1953 O LEU A 670  ? O LEU A 2002 
AA5 2 3 N LEU A 669  ? N LEU A 2001 O LYS A 682  ? O LYS A 2014 
AA6 1 2 N ILE A 812  ? N ILE A 2144 O LEU A 1161 ? O LEU A 2493 
AA6 2 3 O THR A 1162 ? O THR A 2494 N VAL A 1140 ? N VAL A 2472 
AA6 3 4 O TYR A 1143 ? O TYR A 2475 N SER A 1122 ? N SER A 2454 
AA7 1 2 N CYS A 822  ? N CYS A 2154 O GLY A 838  ? O GLY A 2170 
AA7 2 3 N ILE A 835  ? N ILE A 2167 O LEU A 850  ? O LEU A 2182 
AA7 3 4 N LEU A 847  ? N LEU A 2179 O GLU A 860  ? O GLU A 2192 
AA8 1 2 N LEU A 868  ? N LEU A 2200 O GLY A 886  ? O GLY A 2218 
AA8 2 3 N SER A 885  ? N SER A 2217 O LEU A 893  ? O LEU A 2225 
AA8 3 4 N VAL A 894  ? N VAL A 2226 O HIS A 904  ? O HIS A 2236 
AA9 1 2 N THR A 914  ? N THR A 2246 O GLY A 934  ? O GLY A 2266 
AA9 2 3 N VAL A 933  ? N VAL A 2265 O ALA A 941  ? O ALA A 2273 
AA9 3 4 N LEU A 940  ? N LEU A 2272 O LEU A 959  ? O LEU A 2291 
AB1 1 2 N SER A 972  ? N SER A 2304 O TRP A 984  ? O TRP A 2316 
AB1 2 3 N CYS A 987  ? N CYS A 2319 O LYS A 990  ? O LYS A 2322 
AB1 3 4 N SER A 993  ? N SER A 2325 O GLN A 1001 ? O GLN A 2333 
AB2 1 2 N VAL A 1026 ? N VAL A 2358 O TYR A 1032 ? O TYR A 2364 
AB2 2 3 N LEU A 1031 ? N LEU A 2363 O TRP A 1044 ? O TRP A 2376 
AB2 3 4 N VAL A 1043 ? N VAL A 2375 O GLY A 1053 ? O GLY A 2385 
AB3 1 2 N CYS A 1086 ? N CYS A 2418 O TRP A 1094 ? O TRP A 2426 
AB3 2 3 N LEU A 1093 ? N LEU A 2425 O LEU A 1105 ? O LEU A 2437 
AB3 3 4 N ASP A 1106 ? N ASP A 2438 O ARG A 1111 ? O ARG A 2443 
# 
_pdbx_entry_details.entry_id                   9DMI 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A THR 2321 ? ? OG1 A THR 2338 ? ? 2.13 
2 1 O A VAL 2205 ? ? OG  A SER 2213 ? ? 2.17 
3 1 O B TYR 81   ? ? ND1 B HIS 113  ? B 2.18 
4 1 O A LYS 1336 ? ? N   A LEU 1414 ? ? 2.18 
# 
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 ARG A 1398 ? ? -97.35  30.16   
2  1 GLU A 1400 ? ? -121.74 -56.46  
3  1 TYR A 1402 ? ? -142.47 11.16   
4  1 SER A 1403 ? ? -69.96  12.16   
5  1 THR A 1452 ? ? -91.36  -159.76 
6  1 LEU A 1454 ? ? 68.08   -4.69   
7  1 LYS A 1476 ? ? 57.60   -141.54 
8  1 ARG A 1477 ? ? -161.80 -160.71 
9  1 ALA A 1490 ? ? 66.18   169.36  
10 1 VAL A 1598 ? ? 55.03   -147.56 
11 1 LEU A 1712 ? ? -90.52  35.18   
12 1 TRP A 1742 ? ? 52.31   -114.22 
13 1 LEU A 1749 ? ? -91.77  59.30   
14 1 LEU A 1807 ? ? 58.00   -128.48 
15 1 SER A 1815 ? ? -160.45 113.75  
16 1 LEU A 1870 ? ? -65.90  88.55   
17 1 ASN A 1872 ? ? -67.16  89.61   
18 1 GLN A 1879 ? ? 85.49   3.69    
19 1 SER A 1913 ? ? 51.63   10.52   
20 1 ALA A 1937 ? ? 55.71   82.44   
21 1 ARG A 1943 ? ? 60.31   66.46   
22 1 MET A 2106 ? ? 51.81   19.49   
23 1 LEU A 2140 ? ? -69.45  91.06   
24 1 ALA A 2195 ? ? 74.24   154.33  
25 1 GLU A 2230 ? ? -94.01  -63.05  
26 1 TYR A 2249 ? ? 65.79   -117.72 
27 1 LEU A 2263 ? ? 29.97   61.20   
28 1 SER A 2341 ? ? -67.81  4.93    
29 1 SER A 2345 ? ? 58.25   -139.78 
30 1 ASP A 2360 ? ? -134.36 -39.96  
31 1 LEU A 2417 ? ? -161.56 117.36  
32 1 LYS A 2421 ? ? 51.04   -128.29 
33 1 ILE A 2448 ? ? -39.73  139.78  
34 1 PHE A 2451 ? ? 76.43   -8.23   
35 1 LEU A 2463 ? ? 58.97   -115.05 
36 1 ALA B 139  ? ? 63.05   -159.94 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9DMI 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'AB INITIO MODEL' 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  6VP7 
_em_3d_fitting_list.pdb_chain_id                  A 
_em_3d_fitting_list.pdb_chain_residue_range       1333-2527 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      A 
_em_3d_fitting_list.chain_residue_range           1333-2527 
_em_3d_fitting_list.source_name                   PDB 
_em_3d_fitting_list.type                          'experimental model' 
_em_3d_fitting_list.accession_code                6VP7 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9DMI 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   'FOURIER SPACE' 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.35 
_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               226172 
_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            7.4 
# 
_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                 'C-terminal half of LRRK2 bound to RN277' 
_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                        9DMI 
_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           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1000 
_em_imaging.nominal_defocus_max             4000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           130000 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    GOLD 
_em_sample_support.grid_mesh_size   200 
_em_sample_support.grid_type        'UltrAuFoil R2/2' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9DMI 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              95 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277.15 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               
;Blot time 4s
Blot force 5 
Waiting time 20s
;
# 
_em_experiment.entry_id                9DMI 
_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 ASN 1333 ? A ASN 1    
2   1 Y 1 A LYS 1356 ? A LYS 24   
3   1 Y 1 A THR 1357 ? A THR 25   
4   1 Y 1 A LYS 1358 ? A LYS 26   
5   1 Y 1 A LYS 1359 ? A LYS 27   
6   1 Y 1 A SER 1360 ? A SER 28   
7   1 Y 1 A ASP 1361 ? A ASP 29   
8   1 Y 1 A LEU 1362 ? A LEU 30   
9   1 Y 1 A GLY 1363 ? A GLY 31   
10  1 Y 1 A MET 1364 ? A MET 32   
11  1 Y 1 A GLN 1365 ? A GLN 33   
12  1 Y 1 A SER 1366 ? A SER 34   
13  1 Y 1 A ALA 1367 ? A ALA 35   
14  1 Y 1 A THR 1368 ? A THR 36   
15  1 Y 1 A VAL 1369 ? A VAL 37   
16  1 Y 1 A GLN 1379 ? A GLN 47   
17  1 Y 1 A ILE 1380 ? A ILE 48   
18  1 Y 1 A ARG 1381 ? A ARG 49   
19  1 Y 1 A ASP 1382 ? A ASP 50   
20  1 Y 1 A LYS 1383 ? A LYS 51   
21  1 Y 1 A ARG 1384 ? A ARG 52   
22  1 Y 1 A LYS 1385 ? A LYS 53   
23  1 Y 1 A ARG 1386 ? A ARG 54   
24  1 Y 1 A ASP 1387 ? A ASP 55   
25  1 Y 1 A HIS 1407 ? A HIS 75   
26  1 Y 1 A PHE 1408 ? A PHE 76   
27  1 Y 1 A MET 1409 ? A MET 77   
28  1 Y 1 A THR 1410 ? A THR 78   
29  1 Y 1 A GLN 1411 ? A GLN 79   
30  1 Y 1 A ARG 1412 ? A ARG 80   
31  1 Y 1 A ALA 1413 ? A ALA 81   
32  1 Y 1 A ARG 1441 ? A ARG 109  
33  1 Y 1 A ALA 1442 ? A ALA 110  
34  1 Y 1 A SER 1443 ? A SER 111  
35  1 Y 1 A SER 1444 ? A SER 112  
36  1 Y 1 A SER 1445 ? A SER 113  
37  1 Y 1 A SER 1457 ? A SER 125  
38  1 Y 1 A ASP 1458 ? A ASP 126  
39  1 Y 1 A GLU 1459 ? A GLU 127  
40  1 Y 1 A LYS 1460 ? A LYS 128  
41  1 Y 1 A PHE 1511 ? A PHE 179  
42  1 Y 1 A LYS 1512 ? A LYS 180  
43  1 Y 1 A ILE 1513 ? A ILE 181  
44  1 Y 1 A ARG 1514 ? A ARG 182  
45  1 Y 1 A ASP 1515 ? A ASP 183  
46  1 Y 1 A GLN 1516 ? A GLN 184  
47  1 Y 1 A LEU 1517 ? A LEU 185  
48  1 Y 1 A VAL 1518 ? A VAL 186  
49  1 Y 1 A VAL 1519 ? A VAL 187  
50  1 Y 1 A GLY 1520 ? A GLY 188  
51  1 Y 1 A GLN 1521 ? A GLN 189  
52  1 Y 1 A LEU 1522 ? A LEU 190  
53  1 Y 1 A ILE 1523 ? A ILE 191  
54  1 Y 1 A PRO 1524 ? A PRO 192  
55  1 Y 1 A ASP 1525 ? A ASP 193  
56  1 Y 1 A CYS 1526 ? A CYS 194  
57  1 Y 1 A TYR 1527 ? A TYR 195  
58  1 Y 1 A PRO 1542 ? A PRO 210  
59  1 Y 1 A ILE 1543 ? A ILE 211  
60  1 Y 1 A GLU 1544 ? A GLU 212  
61  1 Y 1 A PHE 1545 ? A PHE 213  
62  1 Y 1 A PRO 1546 ? A PRO 214  
63  1 Y 1 A VAL 1547 ? A VAL 215  
64  1 Y 1 A ILE 1548 ? A ILE 216  
65  1 Y 1 A ASP 1549 ? A ASP 217  
66  1 Y 1 A ARG 1550 ? A ARG 218  
67  1 Y 1 A LYS 1551 ? A LYS 219  
68  1 Y 1 A ARG 1552 ? A ARG 220  
69  1 Y 1 A LEU 1553 ? A LEU 221  
70  1 Y 1 A LEU 1554 ? A LEU 222  
71  1 Y 1 A GLN 1555 ? A GLN 223  
72  1 Y 1 A LEU 1556 ? A LEU 224  
73  1 Y 1 A VAL 1557 ? A VAL 225  
74  1 Y 1 A ARG 1558 ? A ARG 226  
75  1 Y 1 A GLU 1559 ? A GLU 227  
76  1 Y 1 A ASN 1560 ? A ASN 228  
77  1 Y 1 A GLN 1561 ? A GLN 229  
78  1 Y 1 A LEU 1562 ? A LEU 230  
79  1 Y 1 A GLN 1563 ? A GLN 231  
80  1 Y 1 A LEU 1564 ? A LEU 232  
81  1 Y 1 A ASP 1565 ? A ASP 233  
82  1 Y 1 A GLU 1566 ? A GLU 234  
83  1 Y 1 A ASN 1567 ? A ASN 235  
84  1 Y 1 A GLU 1568 ? A GLU 236  
85  1 Y 1 A LEU 1569 ? A LEU 237  
86  1 Y 1 A PRO 1570 ? A PRO 238  
87  1 Y 1 A HIS 1571 ? A HIS 239  
88  1 Y 1 A ALA 1572 ? A ALA 240  
89  1 Y 1 A VAL 1573 ? A VAL 241  
90  1 Y 1 A HIS 1574 ? A HIS 242  
91  1 Y 1 A HIS 1584 ? A HIS 252  
92  1 Y 1 A PHE 1585 ? A PHE 253  
93  1 Y 1 A GLN 1586 ? A GLN 254  
94  1 Y 1 A ASP 1587 ? A ASP 255  
95  1 Y 1 A PRO 1588 ? A PRO 256  
96  1 Y 1 A ALA 1589 ? A ALA 257  
97  1 Y 1 A LEU 1590 ? A LEU 258  
98  1 Y 1 A GLN 1591 ? A GLN 259  
99  1 Y 1 A LEU 1592 ? A LEU 260  
100 1 Y 1 A SER 1593 ? A SER 261  
101 1 Y 1 A LYS 1614 ? A LYS 282  
102 1 Y 1 A VAL 1615 ? A VAL 283  
103 1 Y 1 A GLU 1616 ? A GLU 284  
104 1 Y 1 A GLY 1617 ? A GLY 285  
105 1 Y 1 A CYS 1618 ? A CYS 286  
106 1 Y 1 A PRO 1619 ? A PRO 287  
107 1 Y 1 A LYS 1620 ? A LYS 288  
108 1 Y 1 A HIS 1621 ? A HIS 289  
109 1 Y 1 A PRO 1622 ? A PRO 290  
110 1 Y 1 A LYS 1623 ? A LYS 291  
111 1 Y 1 A GLY 1624 ? A GLY 292  
112 1 Y 1 A ILE 1625 ? A ILE 293  
113 1 Y 1 A ILE 1626 ? A ILE 294  
114 1 Y 1 A SER 1627 ? A SER 295  
115 1 Y 1 A ARG 1628 ? A ARG 296  
116 1 Y 1 A ARG 1629 ? A ARG 297  
117 1 Y 1 A ASP 1630 ? A ASP 298  
118 1 Y 1 A VAL 1631 ? A VAL 299  
119 1 Y 1 A GLU 1632 ? A GLU 300  
120 1 Y 1 A LYS 1633 ? A LYS 301  
121 1 Y 1 A PHE 1634 ? A PHE 302  
122 1 Y 1 A LEU 1635 ? A LEU 303  
123 1 Y 1 A SER 1636 ? A SER 304  
124 1 Y 1 A LYS 1637 ? A LYS 305  
125 1 Y 1 A LYS 1638 ? A LYS 306  
126 1 Y 1 A PRO 1661 ? A PRO 329  
127 1 Y 1 A ILE 1662 ? A ILE 330  
128 1 Y 1 A GLY 1663 ? A GLY 331  
129 1 Y 1 A GLU 1664 ? A GLU 332  
130 1 Y 1 A GLU 1665 ? A GLU 333  
131 1 Y 1 A TYR 1666 ? A TYR 334  
132 1 Y 1 A LEU 1667 ? A LEU 335  
133 1 Y 1 A ASP 1675 ? A ASP 343  
134 1 Y 1 A HIS 1676 ? A HIS 344  
135 1 Y 1 A ARG 1677 ? A ARG 345  
136 1 Y 1 A PRO 1678 ? A PRO 346  
137 1 Y 1 A VAL 1679 ? A VAL 347  
138 1 Y 1 A ILE 1680 ? A ILE 348  
139 1 Y 1 A GLU 1681 ? A GLU 349  
140 1 Y 1 A LEU 1682 ? A LEU 350  
141 1 Y 1 A PRO 1683 ? A PRO 351  
142 1 Y 1 A TYR 1718 ? A TYR 386  
143 1 Y 1 A MET 1719 ? A MET 387  
144 1 Y 1 A LEU 1720 ? A LEU 388  
145 1 Y 1 A SER 1721 ? A SER 389  
146 1 Y 1 A GLY 1722 ? A GLY 390  
147 1 Y 1 A ARG 1723 ? A ARG 391  
148 1 Y 1 A GLU 1724 ? A GLU 392  
149 1 Y 1 A ARG 1725 ? A ARG 393  
150 1 Y 1 A ALA 1726 ? A ALA 394  
151 1 Y 1 A LEU 1727 ? A LEU 395  
152 1 Y 1 A ARG 1728 ? A ARG 396  
153 1 Y 1 A PRO 1729 ? A PRO 397  
154 1 Y 1 A ASN 1730 ? A ASN 398  
155 1 Y 1 A GLU 1753 ? A GLU 421  
156 1 Y 1 A VAL 1754 ? A VAL 422  
157 1 Y 1 A LEU 1755 ? A LEU 423  
158 1 Y 1 A ASP 1756 ? A ASP 424  
159 1 Y 1 A ASN 1757 ? A ASN 425  
160 1 Y 1 A HIS 1758 ? A HIS 426  
161 1 Y 1 A PRO 1759 ? A PRO 427  
162 1 Y 1 A LEU 1795 ? A LEU 463  
163 1 Y 1 A LEU 1796 ? A LEU 464  
164 1 Y 1 A GLU 1797 ? A GLU 465  
165 1 Y 1 A ILE 1798 ? A ILE 466  
166 1 Y 1 A ASP 1799 ? A ASP 467  
167 1 Y 1 A ILE 1800 ? A ILE 468  
168 1 Y 1 A CYS 1801 ? A CYS 469  
169 1 Y 1 A GLY 1802 ? A GLY 470  
170 1 Y 1 A GLU 1803 ? A GLU 471  
171 1 Y 1 A GLY 1804 ? A GLY 472  
172 1 Y 1 A GLU 1805 ? A GLU 473  
173 1 Y 1 A PRO 1846 ? A PRO 514  
174 1 Y 1 A ARG 1847 ? A ARG 515  
175 1 Y 1 A LEU 1848 ? A LEU 516  
176 1 Y 1 A GLY 1886 ? A GLY 554  
177 1 Y 1 A ASP 1887 ? A ASP 555  
178 1 Y 1 A GLY 1888 ? A GLY 556  
179 1 Y 1 A SER 1889 ? A SER 557  
180 1 Y 1 A PHE 1890 ? A PHE 558  
181 1 Y 1 A ALA 2021 ? A ALA 689  
182 1 Y 1 A GLN 2022 ? A GLN 690  
183 1 Y 1 A TYR 2023 ? A TYR 691  
184 1 Y 1 A CYS 2024 ? A CYS 692  
185 1 Y 1 A CYS 2025 ? A CYS 693  
186 1 Y 1 A ARG 2026 ? A ARG 694  
187 1 Y 1 A MET 2027 ? A MET 695  
188 1 Y 1 A GLY 2028 ? A GLY 696  
189 1 Y 1 A ILE 2029 ? A ILE 697  
190 1 Y 1 A LYS 2030 ? A LYS 698  
191 1 Y 1 A THR 2031 ? A THR 699  
192 1 Y 1 A SER 2032 ? A SER 700  
193 1 Y 1 A ALA 2044 ? A ALA 712  
194 1 Y 1 A ARG 2045 ? A ARG 713  
195 1 Y 1 A GLY 2046 ? A GLY 714  
196 1 Y 1 A ASN 2047 ? A ASN 715  
197 1 Y 1 A VAL 2048 ? A VAL 716  
198 1 Y 1 A ILE 2049 ? A ILE 717  
199 1 Y 1 A GLU 2075 ? A GLU 743  
200 1 Y 1 A GLY 2076 ? A GLY 744  
201 1 Y 1 A LEU 2077 ? A LEU 745  
202 1 Y 1 A LYS 2078 ? A LYS 746  
203 1 Y 1 A PHE 2079 ? A PHE 747  
204 1 Y 1 A PRO 2080 ? A PRO 748  
205 1 Y 1 A ASN 2081 ? A ASN 749  
206 1 Y 1 A GLU 2082 ? A GLU 750  
207 1 Y 1 A PHE 2083 ? A PHE 751  
208 1 Y 1 A ASP 2084 ? A ASP 752  
209 1 Y 1 A GLU 2085 ? A GLU 753  
210 1 Y 1 A LEU 2086 ? A LEU 754  
211 1 Y 1 A GLU 2087 ? A GLU 755  
212 1 Y 1 A ILE 2088 ? A ILE 756  
213 1 Y 1 A ASN 2161 ? A ASN 829  
214 1 Y 1 A SER 2162 ? A SER 830  
215 1 Y 1 A ARG 2163 ? A ARG 831  
216 1 Y 1 A VAL 2209 ? A VAL 877  
217 1 Y 1 A GLU 2210 ? A GLU 878  
218 1 Y 1 A LYS 2211 ? A LYS 879  
219 1 Y 1 A GLU 2212 ? A GLU 880  
220 1 Y 1 A SER 2252 ? A SER 920  
221 1 Y 1 A PHE 2253 ? A PHE 921  
222 1 Y 1 A SER 2254 ? A SER 922  
223 1 Y 1 A LYS 2255 ? A LYS 923  
224 1 Y 1 A GLN 2256 ? A GLN 924  
225 1 Y 1 A SER 2257 ? A SER 925  
226 1 Y 1 A LYS 2258 ? A LYS 926  
227 1 Y 1 A GLN 2259 ? A GLN 927  
228 1 Y 1 A LYS 2260 ? A LYS 928  
229 1 Y 1 A ASN 2261 ? A ASN 929  
230 1 Y 1 A THR 2307 ? A THR 975  
231 1 Y 1 A ASN 2308 ? A ASN 976  
232 1 Y 1 A SER 2309 ? A SER 977  
233 1 Y 1 A THR 2310 ? A THR 978  
234 1 Y 1 A GLU 2311 ? A GLU 979  
235 1 Y 1 A MET 2397 ? A MET 1065 
236 1 Y 1 A VAL 2398 ? A VAL 1066 
237 1 Y 1 A LYS 2399 ? A LYS 1067 
238 1 Y 1 A GLU 2400 ? A GLU 1068 
239 1 Y 1 A ASN 2401 ? A ASN 1069 
240 1 Y 1 A LYS 2402 ? A LYS 1070 
241 1 Y 1 A GLU 2403 ? A GLU 1071 
242 1 Y 1 A SER 2404 ? A SER 1072 
243 1 Y 1 A LYS 2405 ? A LYS 1073 
244 1 Y 1 A HIS 2406 ? A HIS 1074 
245 1 Y 1 A LYS 2407 ? A LYS 1075 
246 1 Y 1 A MET 2408 ? A MET 1076 
247 1 Y 1 A SER 2409 ? A SER 1077 
248 1 Y 1 A SER 2465 ? A SER 1133 
249 1 Y 1 A LEU 2466 ? A LEU 1134 
250 1 Y 1 A ARG 2477 ? A ARG 1145 
251 1 Y 1 A LYS 2478 ? A LYS 1146 
252 1 Y 1 A ASN 2479 ? A ASN 1147 
253 1 Y 1 A THR 2480 ? A THR 1148 
254 1 Y 1 A GLU 2481 ? A GLU 1149 
255 1 Y 1 A GLY 2482 ? A GLY 1150 
256 1 Y 1 A THR 2483 ? A THR 1151 
257 1 Y 1 A GLN 2484 ? A GLN 1152 
258 1 Y 1 A LYS 2485 ? A LYS 1153 
259 1 Y 1 A GLN 2486 ? A GLN 1154 
260 1 Y 1 A LYS 2487 ? A LYS 1155 
261 1 Y 1 A GLU 2488 ? A GLU 1156 
262 1 Y 1 A GLU 2527 ? A GLU 1195 
263 1 Y 1 B MET 1    ? B MET 1    
264 1 Y 1 B ARG 2    ? B ARG 2    
265 1 Y 1 B GLY 3    ? B GLY 3    
266 1 Y 1 B SER 4    ? B SER 4    
267 1 Y 1 B HIS 5    ? B HIS 5    
268 1 Y 1 B HIS 6    ? B HIS 6    
269 1 Y 1 B HIS 7    ? B HIS 7    
270 1 Y 1 B HIS 8    ? B HIS 8    
271 1 Y 1 B HIS 9    ? B HIS 9    
272 1 Y 1 B HIS 10   ? B HIS 10   
273 1 Y 1 B HIS 11   ? B HIS 11   
274 1 Y 1 B HIS 12   ? B HIS 12   
275 1 Y 1 B GLY 13   ? B GLY 13   
276 1 Y 1 B SER 14   ? B SER 14   
277 1 Y 1 B ASP 15   ? B ASP 15   
278 1 Y 1 B LEU 16   ? B LEU 16   
279 1 Y 1 B GLY 17   ? B GLY 17   
280 1 Y 1 B LYS 18   ? B LYS 18   
281 1 Y 1 B LYS 19   ? B LYS 19   
282 1 Y 1 B LEU 20   ? B LEU 20   
283 1 Y 1 B LEU 21   ? B LEU 21   
284 1 Y 1 B GLU 22   ? B GLU 22   
285 1 Y 1 B ALA 23   ? B ALA 23   
286 1 Y 1 B ALA 24   ? B ALA 24   
287 1 Y 1 B ARG 25   ? B ARG 25   
288 1 Y 1 B ALA 26   ? B ALA 26   
289 1 Y 1 B GLY 27   ? B GLY 27   
290 1 Y 1 B GLN 28   ? B GLN 28   
291 1 Y 1 B ASP 29   ? B ASP 29   
292 1 Y 1 B ASP 30   ? B ASP 30   
293 1 Y 1 B GLU 31   ? B GLU 31   
294 1 Y 1 B VAL 32   ? B VAL 32   
295 1 Y 1 B ARG 33   ? B ARG 33   
296 1 Y 1 B ILE 34   ? B ILE 34   
297 1 Y 1 B LEU 35   ? B LEU 35   
298 1 Y 1 B MET 36   ? B MET 36   
299 1 Y 1 B ALA 37   ? B ALA 37   
300 1 Y 1 B ASN 38   ? B ASN 38   
301 1 Y 1 B GLY 39   ? B GLY 39   
302 1 Y 1 B ALA 40   ? B ALA 40   
303 1 Y 1 B ASP 41   ? B ASP 41   
304 1 Y 1 B VAL 42   ? B VAL 42   
305 1 Y 1 B ASN 43   ? B ASN 43   
306 1 Y 1 B ALA 44   ? B ALA 44   
307 1 Y 1 B THR 45   ? B THR 45   
308 1 Y 1 B ASP 46   ? B ASP 46   
309 1 Y 1 B GLU 47   ? B GLU 47   
310 1 Y 1 B ALA 48   ? B ALA 48   
311 1 Y 1 B GLY 49   ? B GLY 49   
312 1 Y 1 B VAL 50   ? B VAL 50   
313 1 Y 1 B THR 51   ? B THR 51   
314 1 Y 1 B ILE 156  ? B ILE 156  
315 1 Y 1 B ASP 157  ? B ASP 157  
316 1 Y 1 B ASN 158  ? B ASN 158  
317 1 Y 1 B GLY 159  ? B GLY 159  
318 1 Y 1 B ASN 160  ? B ASN 160  
319 1 Y 1 B GLU 161  ? B GLU 161  
320 1 Y 1 B LYS 172  ? B LYS 172  
321 1 Y 1 B LEU 173  ? B LEU 173  
322 1 Y 1 B ASN 174  ? B ASN 174  
323 1 Y 1 B ASP 175  ? B ASP 175  
324 1 Y 1 B TYR 176  ? B TYR 176  
325 1 Y 1 B LYS 177  ? B LYS 177  
326 1 Y 1 B ASP 178  ? B ASP 178  
327 1 Y 1 B ASP 179  ? B ASP 179  
328 1 Y 1 B ASP 180  ? B ASP 180  
329 1 Y 1 B ASP 181  ? B ASP 181  
330 1 Y 1 B LYS 182  ? B LYS 182  
# 
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 
A1A7Q C13  C  Y N 1   
A1A7Q C15  C  Y N 2   
A1A7Q C17  C  Y N 3   
A1A7Q C21  C  N N 4   
A1A7Q C22  C  N N 5   
A1A7Q C24  C  N N 6   
A1A7Q C01  C  N N 7   
A1A7Q C02  C  Y N 8   
A1A7Q C03  C  Y N 9   
A1A7Q C04  C  Y N 10  
A1A7Q C05  C  Y N 11  
A1A7Q C07  C  Y N 12  
A1A7Q C09  C  N N 13  
A1A7Q C11  C  Y N 14  
A1A7Q C12  C  Y N 15  
A1A7Q C14  C  Y N 16  
A1A7Q C18  C  Y N 17  
A1A7Q C19  C  Y N 18  
A1A7Q C25  C  N N 19  
A1A7Q C27  C  Y N 20  
A1A7Q C30  C  Y N 21  
A1A7Q C31  C  Y N 22  
A1A7Q C32  C  Y N 23  
A1A7Q C34  C  Y N 24  
A1A7Q C35  C  Y N 25  
A1A7Q C36  C  N N 26  
A1A7Q C37  C  N N 27  
A1A7Q C38  C  N N 28  
A1A7Q C39  C  N N 29  
A1A7Q C41  C  Y N 30  
A1A7Q C42  C  Y N 31  
A1A7Q N06  N  Y N 32  
A1A7Q N08  N  N N 33  
A1A7Q N10  N  N N 34  
A1A7Q N16  N  Y N 35  
A1A7Q N20  N  N N 36  
A1A7Q N26  N  Y N 37  
A1A7Q N29  N  Y N 38  
A1A7Q N40  N  Y N 39  
A1A7Q O23  O  N N 40  
A1A7Q O33  O  N N 41  
A1A7Q CL28 CL N N 42  
A1A7Q H1   H  N N 43  
A1A7Q H2   H  N N 44  
A1A7Q H3   H  N N 45  
A1A7Q H4   H  N N 46  
A1A7Q H5   H  N N 47  
A1A7Q H6   H  N N 48  
A1A7Q H7   H  N N 49  
A1A7Q H8   H  N N 50  
A1A7Q H9   H  N N 51  
A1A7Q H10  H  N N 52  
A1A7Q H11  H  N N 53  
A1A7Q H12  H  N N 54  
A1A7Q H13  H  N N 55  
A1A7Q H14  H  N N 56  
A1A7Q H15  H  N N 57  
A1A7Q H16  H  N N 58  
A1A7Q H17  H  N N 59  
A1A7Q H18  H  N N 60  
A1A7Q H19  H  N N 61  
A1A7Q H20  H  N N 62  
A1A7Q H21  H  N N 63  
A1A7Q H22  H  N N 64  
A1A7Q H23  H  N N 65  
A1A7Q H24  H  N N 66  
A1A7Q H25  H  N N 67  
A1A7Q H26  H  N N 68  
A1A7Q H27  H  N N 69  
A1A7Q H28  H  N N 70  
A1A7Q H29  H  N N 71  
A1A7Q H30  H  N N 72  
A1A7Q H31  H  N N 73  
A1A7Q H32  H  N N 74  
A1A7Q H33  H  N N 75  
ALA   N    N  N N 76  
ALA   CA   C  N S 77  
ALA   C    C  N N 78  
ALA   O    O  N N 79  
ALA   CB   C  N N 80  
ALA   OXT  O  N N 81  
ALA   H    H  N N 82  
ALA   H2   H  N N 83  
ALA   HA   H  N N 84  
ALA   HB1  H  N N 85  
ALA   HB2  H  N N 86  
ALA   HB3  H  N N 87  
ALA   HXT  H  N N 88  
ARG   N    N  N N 89  
ARG   CA   C  N S 90  
ARG   C    C  N N 91  
ARG   O    O  N N 92  
ARG   CB   C  N N 93  
ARG   CG   C  N N 94  
ARG   CD   C  N N 95  
ARG   NE   N  N N 96  
ARG   CZ   C  N N 97  
ARG   NH1  N  N N 98  
ARG   NH2  N  N N 99  
ARG   OXT  O  N N 100 
ARG   H    H  N N 101 
ARG   H2   H  N N 102 
ARG   HA   H  N N 103 
ARG   HB2  H  N N 104 
ARG   HB3  H  N N 105 
ARG   HG2  H  N N 106 
ARG   HG3  H  N N 107 
ARG   HD2  H  N N 108 
ARG   HD3  H  N N 109 
ARG   HE   H  N N 110 
ARG   HH11 H  N N 111 
ARG   HH12 H  N N 112 
ARG   HH21 H  N N 113 
ARG   HH22 H  N N 114 
ARG   HXT  H  N N 115 
ASN   N    N  N N 116 
ASN   CA   C  N S 117 
ASN   C    C  N N 118 
ASN   O    O  N N 119 
ASN   CB   C  N N 120 
ASN   CG   C  N N 121 
ASN   OD1  O  N N 122 
ASN   ND2  N  N N 123 
ASN   OXT  O  N N 124 
ASN   H    H  N N 125 
ASN   H2   H  N N 126 
ASN   HA   H  N N 127 
ASN   HB2  H  N N 128 
ASN   HB3  H  N N 129 
ASN   HD21 H  N N 130 
ASN   HD22 H  N N 131 
ASN   HXT  H  N N 132 
ASP   N    N  N N 133 
ASP   CA   C  N S 134 
ASP   C    C  N N 135 
ASP   O    O  N N 136 
ASP   CB   C  N N 137 
ASP   CG   C  N N 138 
ASP   OD1  O  N N 139 
ASP   OD2  O  N N 140 
ASP   OXT  O  N N 141 
ASP   H    H  N N 142 
ASP   H2   H  N N 143 
ASP   HA   H  N N 144 
ASP   HB2  H  N N 145 
ASP   HB3  H  N N 146 
ASP   HD2  H  N N 147 
ASP   HXT  H  N N 148 
CYS   N    N  N N 149 
CYS   CA   C  N R 150 
CYS   C    C  N N 151 
CYS   O    O  N N 152 
CYS   CB   C  N N 153 
CYS   SG   S  N N 154 
CYS   OXT  O  N N 155 
CYS   H    H  N N 156 
CYS   H2   H  N N 157 
CYS   HA   H  N N 158 
CYS   HB2  H  N N 159 
CYS   HB3  H  N N 160 
CYS   HG   H  N N 161 
CYS   HXT  H  N N 162 
GLN   N    N  N N 163 
GLN   CA   C  N S 164 
GLN   C    C  N N 165 
GLN   O    O  N N 166 
GLN   CB   C  N N 167 
GLN   CG   C  N N 168 
GLN   CD   C  N N 169 
GLN   OE1  O  N N 170 
GLN   NE2  N  N N 171 
GLN   OXT  O  N N 172 
GLN   H    H  N N 173 
GLN   H2   H  N N 174 
GLN   HA   H  N N 175 
GLN   HB2  H  N N 176 
GLN   HB3  H  N N 177 
GLN   HG2  H  N N 178 
GLN   HG3  H  N N 179 
GLN   HE21 H  N N 180 
GLN   HE22 H  N N 181 
GLN   HXT  H  N N 182 
GLU   N    N  N N 183 
GLU   CA   C  N S 184 
GLU   C    C  N N 185 
GLU   O    O  N N 186 
GLU   CB   C  N N 187 
GLU   CG   C  N N 188 
GLU   CD   C  N N 189 
GLU   OE1  O  N N 190 
GLU   OE2  O  N N 191 
GLU   OXT  O  N N 192 
GLU   H    H  N N 193 
GLU   H2   H  N N 194 
GLU   HA   H  N N 195 
GLU   HB2  H  N N 196 
GLU   HB3  H  N N 197 
GLU   HG2  H  N N 198 
GLU   HG3  H  N N 199 
GLU   HE2  H  N N 200 
GLU   HXT  H  N N 201 
GLY   N    N  N N 202 
GLY   CA   C  N N 203 
GLY   C    C  N N 204 
GLY   O    O  N N 205 
GLY   OXT  O  N N 206 
GLY   H    H  N N 207 
GLY   H2   H  N N 208 
GLY   HA2  H  N N 209 
GLY   HA3  H  N N 210 
GLY   HXT  H  N N 211 
HIS   N    N  N N 212 
HIS   CA   C  N S 213 
HIS   C    C  N N 214 
HIS   O    O  N N 215 
HIS   CB   C  N N 216 
HIS   CG   C  Y N 217 
HIS   ND1  N  Y N 218 
HIS   CD2  C  Y N 219 
HIS   CE1  C  Y N 220 
HIS   NE2  N  Y N 221 
HIS   OXT  O  N N 222 
HIS   H    H  N N 223 
HIS   H2   H  N N 224 
HIS   HA   H  N N 225 
HIS   HB2  H  N N 226 
HIS   HB3  H  N N 227 
HIS   HD1  H  N N 228 
HIS   HD2  H  N N 229 
HIS   HE1  H  N N 230 
HIS   HE2  H  N N 231 
HIS   HXT  H  N N 232 
ILE   N    N  N N 233 
ILE   CA   C  N S 234 
ILE   C    C  N N 235 
ILE   O    O  N N 236 
ILE   CB   C  N S 237 
ILE   CG1  C  N N 238 
ILE   CG2  C  N N 239 
ILE   CD1  C  N N 240 
ILE   OXT  O  N N 241 
ILE   H    H  N N 242 
ILE   H2   H  N N 243 
ILE   HA   H  N N 244 
ILE   HB   H  N N 245 
ILE   HG12 H  N N 246 
ILE   HG13 H  N N 247 
ILE   HG21 H  N N 248 
ILE   HG22 H  N N 249 
ILE   HG23 H  N N 250 
ILE   HD11 H  N N 251 
ILE   HD12 H  N N 252 
ILE   HD13 H  N N 253 
ILE   HXT  H  N N 254 
LEU   N    N  N N 255 
LEU   CA   C  N S 256 
LEU   C    C  N N 257 
LEU   O    O  N N 258 
LEU   CB   C  N N 259 
LEU   CG   C  N N 260 
LEU   CD1  C  N N 261 
LEU   CD2  C  N N 262 
LEU   OXT  O  N N 263 
LEU   H    H  N N 264 
LEU   H2   H  N N 265 
LEU   HA   H  N N 266 
LEU   HB2  H  N N 267 
LEU   HB3  H  N N 268 
LEU   HG   H  N N 269 
LEU   HD11 H  N N 270 
LEU   HD12 H  N N 271 
LEU   HD13 H  N N 272 
LEU   HD21 H  N N 273 
LEU   HD22 H  N N 274 
LEU   HD23 H  N N 275 
LEU   HXT  H  N N 276 
LYS   N    N  N N 277 
LYS   CA   C  N S 278 
LYS   C    C  N N 279 
LYS   O    O  N N 280 
LYS   CB   C  N N 281 
LYS   CG   C  N N 282 
LYS   CD   C  N N 283 
LYS   CE   C  N N 284 
LYS   NZ   N  N N 285 
LYS   OXT  O  N N 286 
LYS   H    H  N N 287 
LYS   H2   H  N N 288 
LYS   HA   H  N N 289 
LYS   HB2  H  N N 290 
LYS   HB3  H  N N 291 
LYS   HG2  H  N N 292 
LYS   HG3  H  N N 293 
LYS   HD2  H  N N 294 
LYS   HD3  H  N N 295 
LYS   HE2  H  N N 296 
LYS   HE3  H  N N 297 
LYS   HZ1  H  N N 298 
LYS   HZ2  H  N N 299 
LYS   HZ3  H  N N 300 
LYS   HXT  H  N N 301 
MET   N    N  N N 302 
MET   CA   C  N S 303 
MET   C    C  N N 304 
MET   O    O  N N 305 
MET   CB   C  N N 306 
MET   CG   C  N N 307 
MET   SD   S  N N 308 
MET   CE   C  N N 309 
MET   OXT  O  N N 310 
MET   H    H  N N 311 
MET   H2   H  N N 312 
MET   HA   H  N N 313 
MET   HB2  H  N N 314 
MET   HB3  H  N N 315 
MET   HG2  H  N N 316 
MET   HG3  H  N N 317 
MET   HE1  H  N N 318 
MET   HE2  H  N N 319 
MET   HE3  H  N N 320 
MET   HXT  H  N N 321 
PHE   N    N  N N 322 
PHE   CA   C  N S 323 
PHE   C    C  N N 324 
PHE   O    O  N N 325 
PHE   CB   C  N N 326 
PHE   CG   C  Y N 327 
PHE   CD1  C  Y N 328 
PHE   CD2  C  Y N 329 
PHE   CE1  C  Y N 330 
PHE   CE2  C  Y N 331 
PHE   CZ   C  Y N 332 
PHE   OXT  O  N N 333 
PHE   H    H  N N 334 
PHE   H2   H  N N 335 
PHE   HA   H  N N 336 
PHE   HB2  H  N N 337 
PHE   HB3  H  N N 338 
PHE   HD1  H  N N 339 
PHE   HD2  H  N N 340 
PHE   HE1  H  N N 341 
PHE   HE2  H  N N 342 
PHE   HZ   H  N N 343 
PHE   HXT  H  N N 344 
PRO   N    N  N N 345 
PRO   CA   C  N S 346 
PRO   C    C  N N 347 
PRO   O    O  N N 348 
PRO   CB   C  N N 349 
PRO   CG   C  N N 350 
PRO   CD   C  N N 351 
PRO   OXT  O  N N 352 
PRO   H    H  N N 353 
PRO   HA   H  N N 354 
PRO   HB2  H  N N 355 
PRO   HB3  H  N N 356 
PRO   HG2  H  N N 357 
PRO   HG3  H  N N 358 
PRO   HD2  H  N N 359 
PRO   HD3  H  N N 360 
PRO   HXT  H  N N 361 
SER   N    N  N N 362 
SER   CA   C  N S 363 
SER   C    C  N N 364 
SER   O    O  N N 365 
SER   CB   C  N N 366 
SER   OG   O  N N 367 
SER   OXT  O  N N 368 
SER   H    H  N N 369 
SER   H2   H  N N 370 
SER   HA   H  N N 371 
SER   HB2  H  N N 372 
SER   HB3  H  N N 373 
SER   HG   H  N N 374 
SER   HXT  H  N N 375 
THR   N    N  N N 376 
THR   CA   C  N S 377 
THR   C    C  N N 378 
THR   O    O  N N 379 
THR   CB   C  N R 380 
THR   OG1  O  N N 381 
THR   CG2  C  N N 382 
THR   OXT  O  N N 383 
THR   H    H  N N 384 
THR   H2   H  N N 385 
THR   HA   H  N N 386 
THR   HB   H  N N 387 
THR   HG1  H  N N 388 
THR   HG21 H  N N 389 
THR   HG22 H  N N 390 
THR   HG23 H  N N 391 
THR   HXT  H  N N 392 
TRP   N    N  N N 393 
TRP   CA   C  N S 394 
TRP   C    C  N N 395 
TRP   O    O  N N 396 
TRP   CB   C  N N 397 
TRP   CG   C  Y N 398 
TRP   CD1  C  Y N 399 
TRP   CD2  C  Y N 400 
TRP   NE1  N  Y N 401 
TRP   CE2  C  Y N 402 
TRP   CE3  C  Y N 403 
TRP   CZ2  C  Y N 404 
TRP   CZ3  C  Y N 405 
TRP   CH2  C  Y N 406 
TRP   OXT  O  N N 407 
TRP   H    H  N N 408 
TRP   H2   H  N N 409 
TRP   HA   H  N N 410 
TRP   HB2  H  N N 411 
TRP   HB3  H  N N 412 
TRP   HD1  H  N N 413 
TRP   HE1  H  N N 414 
TRP   HE3  H  N N 415 
TRP   HZ2  H  N N 416 
TRP   HZ3  H  N N 417 
TRP   HH2  H  N N 418 
TRP   HXT  H  N N 419 
TYR   N    N  N N 420 
TYR   CA   C  N S 421 
TYR   C    C  N N 422 
TYR   O    O  N N 423 
TYR   CB   C  N N 424 
TYR   CG   C  Y N 425 
TYR   CD1  C  Y N 426 
TYR   CD2  C  Y N 427 
TYR   CE1  C  Y N 428 
TYR   CE2  C  Y N 429 
TYR   CZ   C  Y N 430 
TYR   OH   O  N N 431 
TYR   OXT  O  N N 432 
TYR   H    H  N N 433 
TYR   H2   H  N N 434 
TYR   HA   H  N N 435 
TYR   HB2  H  N N 436 
TYR   HB3  H  N N 437 
TYR   HD1  H  N N 438 
TYR   HD2  H  N N 439 
TYR   HE1  H  N N 440 
TYR   HE2  H  N N 441 
TYR   HH   H  N N 442 
TYR   HXT  H  N N 443 
VAL   N    N  N N 444 
VAL   CA   C  N S 445 
VAL   C    C  N N 446 
VAL   O    O  N N 447 
VAL   CB   C  N N 448 
VAL   CG1  C  N N 449 
VAL   CG2  C  N N 450 
VAL   OXT  O  N N 451 
VAL   H    H  N N 452 
VAL   H2   H  N N 453 
VAL   HA   H  N N 454 
VAL   HB   H  N N 455 
VAL   HG11 H  N N 456 
VAL   HG12 H  N N 457 
VAL   HG13 H  N N 458 
VAL   HG21 H  N N 459 
VAL   HG22 H  N N 460 
VAL   HG23 H  N N 461 
VAL   HXT  H  N N 462 
# 
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 
A1A7Q CL28 C27  sing N N 1   
A1A7Q C27  N29  doub Y N 2   
A1A7Q C27  N26  sing Y N 3   
A1A7Q N29  C17  sing Y N 4   
A1A7Q N26  C19  doub Y N 5   
A1A7Q C17  N16  sing Y N 6   
A1A7Q C17  C18  doub Y N 7   
A1A7Q N16  C15  sing Y N 8   
A1A7Q O23  C22  sing N N 9   
A1A7Q O23  C24  sing N N 10  
A1A7Q C19  C18  sing Y N 11  
A1A7Q C19  N20  sing N N 12  
A1A7Q C18  C14  sing Y N 13  
A1A7Q C22  C21  sing N N 14  
A1A7Q C24  C25  sing N N 15  
A1A7Q C15  C14  doub Y N 16  
A1A7Q N20  C25  sing N N 17  
A1A7Q N20  C21  sing N N 18  
A1A7Q C14  C13  sing N N 19  
A1A7Q C38  C36  sing N N 20  
A1A7Q C13  C12  doub Y N 21  
A1A7Q C13  C30  sing Y N 22  
A1A7Q C37  C36  sing N N 23  
A1A7Q C36  C39  sing N N 24  
A1A7Q C36  C35  sing N N 25  
A1A7Q C12  C11  sing Y N 26  
A1A7Q C30  C31  doub Y N 27  
A1A7Q O33  C09  doub N N 28  
A1A7Q C34  C35  sing Y N 29  
A1A7Q C34  C07  doub Y N 30  
A1A7Q C35  N40  doub Y N 31  
A1A7Q C11  N10  sing N N 32  
A1A7Q C11  C32  doub Y N 33  
A1A7Q C09  N10  sing N N 34  
A1A7Q C09  N08  sing N N 35  
A1A7Q C31  C32  sing Y N 36  
A1A7Q C07  N08  sing N N 37  
A1A7Q C07  N06  sing Y N 38  
A1A7Q N40  N06  sing Y N 39  
A1A7Q N06  C05  sing N N 40  
A1A7Q C05  C41  doub Y N 41  
A1A7Q C05  C04  sing Y N 42  
A1A7Q C41  C42  sing Y N 43  
A1A7Q C04  C03  doub Y N 44  
A1A7Q C42  C02  doub Y N 45  
A1A7Q C03  C02  sing Y N 46  
A1A7Q C02  C01  sing N N 47  
A1A7Q C15  H1   sing N N 48  
A1A7Q C21  H2   sing N N 49  
A1A7Q C21  H3   sing N N 50  
A1A7Q C22  H4   sing N N 51  
A1A7Q C22  H5   sing N N 52  
A1A7Q C24  H6   sing N N 53  
A1A7Q C24  H7   sing N N 54  
A1A7Q C01  H8   sing N N 55  
A1A7Q C01  H9   sing N N 56  
A1A7Q C01  H10  sing N N 57  
A1A7Q C03  H11  sing N N 58  
A1A7Q C04  H12  sing N N 59  
A1A7Q C12  H13  sing N N 60  
A1A7Q C25  H14  sing N N 61  
A1A7Q C25  H15  sing N N 62  
A1A7Q C30  H16  sing N N 63  
A1A7Q C31  H17  sing N N 64  
A1A7Q C32  H18  sing N N 65  
A1A7Q C34  H19  sing N N 66  
A1A7Q C37  H20  sing N N 67  
A1A7Q C37  H21  sing N N 68  
A1A7Q C37  H22  sing N N 69  
A1A7Q C38  H23  sing N N 70  
A1A7Q C38  H24  sing N N 71  
A1A7Q C38  H25  sing N N 72  
A1A7Q C39  H26  sing N N 73  
A1A7Q C39  H27  sing N N 74  
A1A7Q C39  H28  sing N N 75  
A1A7Q C41  H29  sing N N 76  
A1A7Q C42  H30  sing N N 77  
A1A7Q N08  H31  sing N N 78  
A1A7Q N10  H32  sing N N 79  
A1A7Q N16  H33  sing N N 80  
ALA   N    CA   sing N N 81  
ALA   N    H    sing N N 82  
ALA   N    H2   sing N N 83  
ALA   CA   C    sing N N 84  
ALA   CA   CB   sing N N 85  
ALA   CA   HA   sing N N 86  
ALA   C    O    doub N N 87  
ALA   C    OXT  sing N N 88  
ALA   CB   HB1  sing N N 89  
ALA   CB   HB2  sing N N 90  
ALA   CB   HB3  sing N N 91  
ALA   OXT  HXT  sing N N 92  
ARG   N    CA   sing N N 93  
ARG   N    H    sing N N 94  
ARG   N    H2   sing N N 95  
ARG   CA   C    sing N N 96  
ARG   CA   CB   sing N N 97  
ARG   CA   HA   sing N N 98  
ARG   C    O    doub N N 99  
ARG   C    OXT  sing N N 100 
ARG   CB   CG   sing N N 101 
ARG   CB   HB2  sing N N 102 
ARG   CB   HB3  sing N N 103 
ARG   CG   CD   sing N N 104 
ARG   CG   HG2  sing N N 105 
ARG   CG   HG3  sing N N 106 
ARG   CD   NE   sing N N 107 
ARG   CD   HD2  sing N N 108 
ARG   CD   HD3  sing N N 109 
ARG   NE   CZ   sing N N 110 
ARG   NE   HE   sing N N 111 
ARG   CZ   NH1  sing N N 112 
ARG   CZ   NH2  doub N N 113 
ARG   NH1  HH11 sing N N 114 
ARG   NH1  HH12 sing N N 115 
ARG   NH2  HH21 sing N N 116 
ARG   NH2  HH22 sing N N 117 
ARG   OXT  HXT  sing N N 118 
ASN   N    CA   sing N N 119 
ASN   N    H    sing N N 120 
ASN   N    H2   sing N N 121 
ASN   CA   C    sing N N 122 
ASN   CA   CB   sing N N 123 
ASN   CA   HA   sing N N 124 
ASN   C    O    doub N N 125 
ASN   C    OXT  sing N N 126 
ASN   CB   CG   sing N N 127 
ASN   CB   HB2  sing N N 128 
ASN   CB   HB3  sing N N 129 
ASN   CG   OD1  doub N N 130 
ASN   CG   ND2  sing N N 131 
ASN   ND2  HD21 sing N N 132 
ASN   ND2  HD22 sing N N 133 
ASN   OXT  HXT  sing N N 134 
ASP   N    CA   sing N N 135 
ASP   N    H    sing N N 136 
ASP   N    H2   sing N N 137 
ASP   CA   C    sing N N 138 
ASP   CA   CB   sing N N 139 
ASP   CA   HA   sing N N 140 
ASP   C    O    doub N N 141 
ASP   C    OXT  sing N N 142 
ASP   CB   CG   sing N N 143 
ASP   CB   HB2  sing N N 144 
ASP   CB   HB3  sing N N 145 
ASP   CG   OD1  doub N N 146 
ASP   CG   OD2  sing N N 147 
ASP   OD2  HD2  sing N N 148 
ASP   OXT  HXT  sing N N 149 
CYS   N    CA   sing N N 150 
CYS   N    H    sing N N 151 
CYS   N    H2   sing N N 152 
CYS   CA   C    sing N N 153 
CYS   CA   CB   sing N N 154 
CYS   CA   HA   sing N N 155 
CYS   C    O    doub N N 156 
CYS   C    OXT  sing N N 157 
CYS   CB   SG   sing N N 158 
CYS   CB   HB2  sing N N 159 
CYS   CB   HB3  sing N N 160 
CYS   SG   HG   sing N N 161 
CYS   OXT  HXT  sing N N 162 
GLN   N    CA   sing N N 163 
GLN   N    H    sing N N 164 
GLN   N    H2   sing N N 165 
GLN   CA   C    sing N N 166 
GLN   CA   CB   sing N N 167 
GLN   CA   HA   sing N N 168 
GLN   C    O    doub N N 169 
GLN   C    OXT  sing N N 170 
GLN   CB   CG   sing N N 171 
GLN   CB   HB2  sing N N 172 
GLN   CB   HB3  sing N N 173 
GLN   CG   CD   sing N N 174 
GLN   CG   HG2  sing N N 175 
GLN   CG   HG3  sing N N 176 
GLN   CD   OE1  doub N N 177 
GLN   CD   NE2  sing N N 178 
GLN   NE2  HE21 sing N N 179 
GLN   NE2  HE22 sing N N 180 
GLN   OXT  HXT  sing N N 181 
GLU   N    CA   sing N N 182 
GLU   N    H    sing N N 183 
GLU   N    H2   sing N N 184 
GLU   CA   C    sing N N 185 
GLU   CA   CB   sing N N 186 
GLU   CA   HA   sing N N 187 
GLU   C    O    doub N N 188 
GLU   C    OXT  sing N N 189 
GLU   CB   CG   sing N N 190 
GLU   CB   HB2  sing N N 191 
GLU   CB   HB3  sing N N 192 
GLU   CG   CD   sing N N 193 
GLU   CG   HG2  sing N N 194 
GLU   CG   HG3  sing N N 195 
GLU   CD   OE1  doub N N 196 
GLU   CD   OE2  sing N N 197 
GLU   OE2  HE2  sing N N 198 
GLU   OXT  HXT  sing N N 199 
GLY   N    CA   sing N N 200 
GLY   N    H    sing N N 201 
GLY   N    H2   sing N N 202 
GLY   CA   C    sing N N 203 
GLY   CA   HA2  sing N N 204 
GLY   CA   HA3  sing N N 205 
GLY   C    O    doub N N 206 
GLY   C    OXT  sing N N 207 
GLY   OXT  HXT  sing N N 208 
HIS   N    CA   sing N N 209 
HIS   N    H    sing N N 210 
HIS   N    H2   sing N N 211 
HIS   CA   C    sing N N 212 
HIS   CA   CB   sing N N 213 
HIS   CA   HA   sing N N 214 
HIS   C    O    doub N N 215 
HIS   C    OXT  sing N N 216 
HIS   CB   CG   sing N N 217 
HIS   CB   HB2  sing N N 218 
HIS   CB   HB3  sing N N 219 
HIS   CG   ND1  sing Y N 220 
HIS   CG   CD2  doub Y N 221 
HIS   ND1  CE1  doub Y N 222 
HIS   ND1  HD1  sing N N 223 
HIS   CD2  NE2  sing Y N 224 
HIS   CD2  HD2  sing N N 225 
HIS   CE1  NE2  sing Y N 226 
HIS   CE1  HE1  sing N N 227 
HIS   NE2  HE2  sing N N 228 
HIS   OXT  HXT  sing N N 229 
ILE   N    CA   sing N N 230 
ILE   N    H    sing N N 231 
ILE   N    H2   sing N N 232 
ILE   CA   C    sing N N 233 
ILE   CA   CB   sing N N 234 
ILE   CA   HA   sing N N 235 
ILE   C    O    doub N N 236 
ILE   C    OXT  sing N N 237 
ILE   CB   CG1  sing N N 238 
ILE   CB   CG2  sing N N 239 
ILE   CB   HB   sing N N 240 
ILE   CG1  CD1  sing N N 241 
ILE   CG1  HG12 sing N N 242 
ILE   CG1  HG13 sing N N 243 
ILE   CG2  HG21 sing N N 244 
ILE   CG2  HG22 sing N N 245 
ILE   CG2  HG23 sing N N 246 
ILE   CD1  HD11 sing N N 247 
ILE   CD1  HD12 sing N N 248 
ILE   CD1  HD13 sing N N 249 
ILE   OXT  HXT  sing N N 250 
LEU   N    CA   sing N N 251 
LEU   N    H    sing N N 252 
LEU   N    H2   sing N N 253 
LEU   CA   C    sing N N 254 
LEU   CA   CB   sing N N 255 
LEU   CA   HA   sing N N 256 
LEU   C    O    doub N N 257 
LEU   C    OXT  sing N N 258 
LEU   CB   CG   sing N N 259 
LEU   CB   HB2  sing N N 260 
LEU   CB   HB3  sing N N 261 
LEU   CG   CD1  sing N N 262 
LEU   CG   CD2  sing N N 263 
LEU   CG   HG   sing N N 264 
LEU   CD1  HD11 sing N N 265 
LEU   CD1  HD12 sing N N 266 
LEU   CD1  HD13 sing N N 267 
LEU   CD2  HD21 sing N N 268 
LEU   CD2  HD22 sing N N 269 
LEU   CD2  HD23 sing N N 270 
LEU   OXT  HXT  sing N N 271 
LYS   N    CA   sing N N 272 
LYS   N    H    sing N N 273 
LYS   N    H2   sing N N 274 
LYS   CA   C    sing N N 275 
LYS   CA   CB   sing N N 276 
LYS   CA   HA   sing N N 277 
LYS   C    O    doub N N 278 
LYS   C    OXT  sing N N 279 
LYS   CB   CG   sing N N 280 
LYS   CB   HB2  sing N N 281 
LYS   CB   HB3  sing N N 282 
LYS   CG   CD   sing N N 283 
LYS   CG   HG2  sing N N 284 
LYS   CG   HG3  sing N N 285 
LYS   CD   CE   sing N N 286 
LYS   CD   HD2  sing N N 287 
LYS   CD   HD3  sing N N 288 
LYS   CE   NZ   sing N N 289 
LYS   CE   HE2  sing N N 290 
LYS   CE   HE3  sing N N 291 
LYS   NZ   HZ1  sing N N 292 
LYS   NZ   HZ2  sing N N 293 
LYS   NZ   HZ3  sing N N 294 
LYS   OXT  HXT  sing N N 295 
MET   N    CA   sing N N 296 
MET   N    H    sing N N 297 
MET   N    H2   sing N N 298 
MET   CA   C    sing N N 299 
MET   CA   CB   sing N N 300 
MET   CA   HA   sing N N 301 
MET   C    O    doub N N 302 
MET   C    OXT  sing N N 303 
MET   CB   CG   sing N N 304 
MET   CB   HB2  sing N N 305 
MET   CB   HB3  sing N N 306 
MET   CG   SD   sing N N 307 
MET   CG   HG2  sing N N 308 
MET   CG   HG3  sing N N 309 
MET   SD   CE   sing N N 310 
MET   CE   HE1  sing N N 311 
MET   CE   HE2  sing N N 312 
MET   CE   HE3  sing N N 313 
MET   OXT  HXT  sing N N 314 
PHE   N    CA   sing N N 315 
PHE   N    H    sing N N 316 
PHE   N    H2   sing N N 317 
PHE   CA   C    sing N N 318 
PHE   CA   CB   sing N N 319 
PHE   CA   HA   sing N N 320 
PHE   C    O    doub N N 321 
PHE   C    OXT  sing N N 322 
PHE   CB   CG   sing N N 323 
PHE   CB   HB2  sing N N 324 
PHE   CB   HB3  sing N N 325 
PHE   CG   CD1  doub Y N 326 
PHE   CG   CD2  sing Y N 327 
PHE   CD1  CE1  sing Y N 328 
PHE   CD1  HD1  sing N N 329 
PHE   CD2  CE2  doub Y N 330 
PHE   CD2  HD2  sing N N 331 
PHE   CE1  CZ   doub Y N 332 
PHE   CE1  HE1  sing N N 333 
PHE   CE2  CZ   sing Y N 334 
PHE   CE2  HE2  sing N N 335 
PHE   CZ   HZ   sing N N 336 
PHE   OXT  HXT  sing N N 337 
PRO   N    CA   sing N N 338 
PRO   N    CD   sing N N 339 
PRO   N    H    sing N N 340 
PRO   CA   C    sing N N 341 
PRO   CA   CB   sing N N 342 
PRO   CA   HA   sing N N 343 
PRO   C    O    doub N N 344 
PRO   C    OXT  sing N N 345 
PRO   CB   CG   sing N N 346 
PRO   CB   HB2  sing N N 347 
PRO   CB   HB3  sing N N 348 
PRO   CG   CD   sing N N 349 
PRO   CG   HG2  sing N N 350 
PRO   CG   HG3  sing N N 351 
PRO   CD   HD2  sing N N 352 
PRO   CD   HD3  sing N N 353 
PRO   OXT  HXT  sing N N 354 
SER   N    CA   sing N N 355 
SER   N    H    sing N N 356 
SER   N    H2   sing N N 357 
SER   CA   C    sing N N 358 
SER   CA   CB   sing N N 359 
SER   CA   HA   sing N N 360 
SER   C    O    doub N N 361 
SER   C    OXT  sing N N 362 
SER   CB   OG   sing N N 363 
SER   CB   HB2  sing N N 364 
SER   CB   HB3  sing N N 365 
SER   OG   HG   sing N N 366 
SER   OXT  HXT  sing N N 367 
THR   N    CA   sing N N 368 
THR   N    H    sing N N 369 
THR   N    H2   sing N N 370 
THR   CA   C    sing N N 371 
THR   CA   CB   sing N N 372 
THR   CA   HA   sing N N 373 
THR   C    O    doub N N 374 
THR   C    OXT  sing N N 375 
THR   CB   OG1  sing N N 376 
THR   CB   CG2  sing N N 377 
THR   CB   HB   sing N N 378 
THR   OG1  HG1  sing N N 379 
THR   CG2  HG21 sing N N 380 
THR   CG2  HG22 sing N N 381 
THR   CG2  HG23 sing N N 382 
THR   OXT  HXT  sing N N 383 
TRP   N    CA   sing N N 384 
TRP   N    H    sing N N 385 
TRP   N    H2   sing N N 386 
TRP   CA   C    sing N N 387 
TRP   CA   CB   sing N N 388 
TRP   CA   HA   sing N N 389 
TRP   C    O    doub N N 390 
TRP   C    OXT  sing N N 391 
TRP   CB   CG   sing N N 392 
TRP   CB   HB2  sing N N 393 
TRP   CB   HB3  sing N N 394 
TRP   CG   CD1  doub Y N 395 
TRP   CG   CD2  sing Y N 396 
TRP   CD1  NE1  sing Y N 397 
TRP   CD1  HD1  sing N N 398 
TRP   CD2  CE2  doub Y N 399 
TRP   CD2  CE3  sing Y N 400 
TRP   NE1  CE2  sing Y N 401 
TRP   NE1  HE1  sing N N 402 
TRP   CE2  CZ2  sing Y N 403 
TRP   CE3  CZ3  doub Y N 404 
TRP   CE3  HE3  sing N N 405 
TRP   CZ2  CH2  doub Y N 406 
TRP   CZ2  HZ2  sing N N 407 
TRP   CZ3  CH2  sing Y N 408 
TRP   CZ3  HZ3  sing N N 409 
TRP   CH2  HH2  sing N N 410 
TRP   OXT  HXT  sing N N 411 
TYR   N    CA   sing N N 412 
TYR   N    H    sing N N 413 
TYR   N    H2   sing N N 414 
TYR   CA   C    sing N N 415 
TYR   CA   CB   sing N N 416 
TYR   CA   HA   sing N N 417 
TYR   C    O    doub N N 418 
TYR   C    OXT  sing N N 419 
TYR   CB   CG   sing N N 420 
TYR   CB   HB2  sing N N 421 
TYR   CB   HB3  sing N N 422 
TYR   CG   CD1  doub Y N 423 
TYR   CG   CD2  sing Y N 424 
TYR   CD1  CE1  sing Y N 425 
TYR   CD1  HD1  sing N N 426 
TYR   CD2  CE2  doub Y N 427 
TYR   CD2  HD2  sing N N 428 
TYR   CE1  CZ   doub Y N 429 
TYR   CE1  HE1  sing N N 430 
TYR   CE2  CZ   sing Y N 431 
TYR   CE2  HE2  sing N N 432 
TYR   CZ   OH   sing N N 433 
TYR   OH   HH   sing N N 434 
TYR   OXT  HXT  sing N N 435 
VAL   N    CA   sing N N 436 
VAL   N    H    sing N N 437 
VAL   N    H2   sing N N 438 
VAL   CA   C    sing N N 439 
VAL   CA   CB   sing N N 440 
VAL   CA   HA   sing N N 441 
VAL   C    O    doub N N 442 
VAL   C    OXT  sing N N 443 
VAL   CB   CG1  sing N N 444 
VAL   CB   CG2  sing N N 445 
VAL   CB   HB   sing N N 446 
VAL   CG1  HG11 sing N N 447 
VAL   CG1  HG12 sing N N 448 
VAL   CG1  HG13 sing N N 449 
VAL   CG2  HG21 sing N N 450 
VAL   CG2  HG22 sing N N 451 
VAL   CG2  HG23 sing N N 452 
VAL   OXT  HXT  sing N N 453 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-09-13 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9DMI 
_em_admin.last_update        2025-06-18 
_em_admin.map_release_date   2025-06-18 
_em_admin.title              'Structure of the C-terminal half of LRRK2 bound to RN277 (Type-II inhibitor)' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 20  mM ?     1 HEPES                
1 150 mM NaCl  2 'Sodium Chloride'    
1 2.5 mM MgCl2 3 'Magnesium Chloride' 
1 5   %  GlyOH 4 Glycerol             
1 20  uM ?     5 GDP                  
1 0.5 mM ?     6 TCEP                 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    YES 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.137 
# 
_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          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_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         55 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'FEI FALCON IV (4k 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                    1 
_em_image_recording.num_real_images                     13972 
# 
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 ? ? Topaz           0.2.5 
'IMAGE ACQUISITION'             ? 2  ? ? 1 cryoSPARC       4.5   
MASKING                         ? 3  ? ? ? ?               ?     
'CTF CORRECTION'                ? 4  1 ? ? cryoSPARC       4.3   
'LAYERLINE INDEXING'            ? 5  ? ? ? ?               ?     
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?               ?     
'MODEL FITTING'                 ? 7  ? 1 ? 'UCSF ChimeraX' 1.7   
OTHER                           ? 8  ? ? ? ?               ?     
'INITIAL EULER ASSIGNMENT'      ? 9  1 ? ? ?               ?     
'FINAL EULER ASSIGNMENT'        ? 10 1 ? ? ?               ?     
CLASSIFICATION                  ? 11 1 ? ? ?               ?     
RECONSTRUCTION                  ? 12 1 ? ? cryoSPARC       4.4   
'MODEL REFINEMENT'              ? 13 ? 1 ? PHENIX          1.21  
'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           616.5 
_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   'Michael J. Fox Foundation' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ASAP-000519 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6VP7 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DMI 
_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  
CL 
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    . ARG   A 1 2    ? 169.851 160.861 218.517 1.00 196.15 ? 1334 ARG   A N    1 
ATOM   2    C  CA   . ARG   A 1 2    ? 171.186 161.449 218.499 1.00 199.43 ? 1334 ARG   A CA   1 
ATOM   3    C  C    . ARG   A 1 2    ? 171.135 162.947 218.784 1.00 203.14 ? 1334 ARG   A C    1 
ATOM   4    O  O    . ARG   A 1 2    ? 171.799 163.737 218.114 1.00 204.69 ? 1334 ARG   A O    1 
ATOM   5    C  CB   . ARG   A 1 2    ? 171.866 161.192 217.154 1.00 193.27 ? 1334 ARG   A CB   1 
ATOM   6    N  N    . MET   A 1 3    ? 170.338 163.332 219.780 1.00 200.41 ? 1335 MET   A N    1 
ATOM   7    C  CA   . MET   A 1 3    ? 170.218 164.737 220.147 1.00 199.26 ? 1335 MET   A CA   1 
ATOM   8    C  C    . MET   A 1 3    ? 171.535 165.236 220.735 1.00 198.78 ? 1335 MET   A C    1 
ATOM   9    O  O    . MET   A 1 3    ? 172.225 164.505 221.451 1.00 199.19 ? 1335 MET   A O    1 
ATOM   10   C  CB   . MET   A 1 3    ? 169.067 164.921 221.140 1.00 198.46 ? 1335 MET   A CB   1 
ATOM   11   C  CG   . MET   A 1 3    ? 168.957 166.307 221.760 1.00 202.28 ? 1335 MET   A CG   1 
ATOM   12   S  SD   . MET   A 1 3    ? 168.838 167.629 220.537 1.00 201.60 ? 1335 MET   A SD   1 
ATOM   13   C  CE   . MET   A 1 3    ? 168.067 168.921 221.508 1.00 180.60 ? 1335 MET   A CE   1 
ATOM   14   N  N    . LYS   A 1 4    ? 171.880 166.484 220.429 1.00 198.06 ? 1336 LYS   A N    1 
ATOM   15   C  CA   . LYS   A 1 4    ? 173.191 167.042 220.730 1.00 196.48 ? 1336 LYS   A CA   1 
ATOM   16   C  C    . LYS   A 1 4    ? 173.281 167.493 222.184 1.00 198.63 ? 1336 LYS   A C    1 
ATOM   17   O  O    . LYS   A 1 4    ? 172.566 168.404 222.605 1.00 192.45 ? 1336 LYS   A O    1 
ATOM   18   C  CB   . LYS   A 1 4    ? 173.487 168.228 219.808 1.00 190.80 ? 1336 LYS   A CB   1 
ATOM   19   N  N    . LEU   A 1 5    ? 174.189 166.871 222.938 1.00 199.80 ? 1337 LEU   A N    1 
ATOM   20   C  CA   . LEU   A 1 5    ? 174.426 167.221 224.336 1.00 197.01 ? 1337 LEU   A CA   1 
ATOM   21   C  C    . LEU   A 1 5    ? 175.907 167.519 224.521 1.00 192.16 ? 1337 LEU   A C    1 
ATOM   22   O  O    . LEU   A 1 5    ? 176.758 166.756 224.053 1.00 188.36 ? 1337 LEU   A O    1 
ATOM   23   C  CB   . LEU   A 1 5    ? 173.978 166.092 225.273 1.00 196.22 ? 1337 LEU   A CB   1 
ATOM   24   C  CG   . LEU   A 1 5    ? 173.968 166.334 226.790 1.00 191.39 ? 1337 LEU   A CG   1 
ATOM   25   C  CD1  . LEU   A 1 5    ? 172.938 165.436 227.453 1.00 191.06 ? 1337 LEU   A CD1  1 
ATOM   26   C  CD2  . LEU   A 1 5    ? 175.328 166.134 227.440 1.00 189.01 ? 1337 LEU   A CD2  1 
ATOM   27   N  N    . MET   A 1 6    ? 176.214 168.618 225.205 1.00 190.01 ? 1338 MET   A N    1 
ATOM   28   C  CA   . MET   A 1 6    ? 177.590 169.029 225.447 1.00 181.43 ? 1338 MET   A CA   1 
ATOM   29   C  C    . MET   A 1 6    ? 177.787 169.339 226.924 1.00 171.98 ? 1338 MET   A C    1 
ATOM   30   O  O    . MET   A 1 6    ? 177.126 170.230 227.468 1.00 169.39 ? 1338 MET   A O    1 
ATOM   31   C  CB   . MET   A 1 6    ? 177.950 170.254 224.604 1.00 182.32 ? 1338 MET   A CB   1 
ATOM   32   C  CG   . MET   A 1 6    ? 177.970 169.989 223.111 1.00 182.86 ? 1338 MET   A CG   1 
ATOM   33   S  SD   . MET   A 1 6    ? 178.465 171.415 222.135 1.00 182.12 ? 1338 MET   A SD   1 
ATOM   34   C  CE   . MET   A 1 6    ? 177.003 172.429 222.247 1.00 175.22 ? 1338 MET   A CE   1 
ATOM   35   N  N    . ILE   A 1 7    ? 178.701 168.618 227.561 1.00 171.96 ? 1339 ILE   A N    1 
ATOM   36   C  CA   . ILE   A 1 7    ? 179.092 168.905 228.935 1.00 173.22 ? 1339 ILE   A CA   1 
ATOM   37   C  C    . ILE   A 1 7    ? 180.120 170.036 228.916 1.00 179.35 ? 1339 ILE   A C    1 
ATOM   38   O  O    . ILE   A 1 7    ? 181.208 169.898 228.350 1.00 179.62 ? 1339 ILE   A O    1 
ATOM   39   C  CB   . ILE   A 1 7    ? 179.618 167.639 229.642 1.00 169.62 ? 1339 ILE   A CB   1 
ATOM   40   C  CG1  . ILE   A 1 7    ? 179.636 167.813 231.163 1.00 160.63 ? 1339 ILE   A CG1  1 
ATOM   41   C  CG2  . ILE   A 1 7    ? 180.953 167.135 229.087 1.00 176.60 ? 1339 ILE   A CG2  1 
ATOM   42   C  CD1  . ILE   A 1 7    ? 178.326 168.217 231.743 1.00 160.42 ? 1339 ILE   A CD1  1 
ATOM   43   N  N    . VAL   A 1 8    ? 179.755 171.180 229.493 1.00 181.78 ? 1340 VAL   A N    1 
ATOM   44   C  CA   . VAL   A 1 8    ? 180.638 172.345 229.508 1.00 174.60 ? 1340 VAL   A CA   1 
ATOM   45   C  C    . VAL   A 1 8    ? 181.379 172.458 230.840 1.00 174.46 ? 1340 VAL   A C    1 
ATOM   46   O  O    . VAL   A 1 8    ? 180.843 172.951 231.839 1.00 173.56 ? 1340 VAL   A O    1 
ATOM   47   C  CB   . VAL   A 1 8    ? 179.858 173.629 229.150 1.00 164.98 ? 1340 VAL   A CB   1 
ATOM   48   C  CG1  . VAL   A 1 8    ? 179.207 173.469 227.800 1.00 163.40 ? 1340 VAL   A CG1  1 
ATOM   49   C  CG2  . VAL   A 1 8    ? 178.760 173.922 230.159 1.00 165.79 ? 1340 VAL   A CG2  1 
ATOM   50   N  N    . GLY   A 1 9    ? 182.622 171.983 230.866 1.00 171.60 ? 1341 GLY   A N    1 
ATOM   51   C  CA   . GLY   A 1 9    ? 183.439 172.080 232.062 1.00 169.95 ? 1341 GLY   A CA   1 
ATOM   52   C  C    . GLY   A 1 9    ? 184.671 172.940 231.862 1.00 164.33 ? 1341 GLY   A C    1 
ATOM   53   O  O    . GLY   A 1 9    ? 185.204 173.009 230.752 1.00 163.94 ? 1341 GLY   A O    1 
ATOM   54   N  N    . ASN   A 1 10   ? 185.128 173.616 232.918 1.00 162.93 ? 1342 ASN   A N    1 
ATOM   55   C  CA   . ASN   A 1 10   ? 186.323 174.444 232.791 1.00 162.66 ? 1342 ASN   A CA   1 
ATOM   56   C  C    . ASN   A 1 10   ? 187.593 173.613 232.932 1.00 160.35 ? 1342 ASN   A C    1 
ATOM   57   O  O    . ASN   A 1 10   ? 188.396 173.523 231.997 1.00 163.46 ? 1342 ASN   A O    1 
ATOM   58   C  CB   . ASN   A 1 10   ? 186.292 175.570 233.821 1.00 167.73 ? 1342 ASN   A CB   1 
ATOM   59   C  CG   . ASN   A 1 10   ? 185.046 176.417 233.707 1.00 167.18 ? 1342 ASN   A CG   1 
ATOM   60   O  OD1  . ASN   A 1 10   ? 184.136 176.098 232.940 1.00 164.12 ? 1342 ASN   A OD1  1 
ATOM   61   N  ND2  . ASN   A 1 10   ? 184.998 177.504 234.464 1.00 169.68 ? 1342 ASN   A ND2  1 
ATOM   62   N  N    . THR   A 1 11   ? 187.793 172.999 234.095 1.00 161.75 ? 1343 THR   A N    1 
ATOM   63   C  CA   . THR   A 1 11   ? 188.921 172.105 234.312 1.00 165.41 ? 1343 THR   A CA   1 
ATOM   64   C  C    . THR   A 1 11   ? 188.636 170.694 233.819 1.00 166.72 ? 1343 THR   A C    1 
ATOM   65   O  O    . THR   A 1 11   ? 189.416 169.777 234.098 1.00 168.72 ? 1343 THR   A O    1 
ATOM   66   C  CB   . THR   A 1 11   ? 189.304 172.081 235.795 1.00 155.66 ? 1343 THR   A CB   1 
ATOM   67   O  OG1  . THR   A 1 11   ? 190.512 171.329 235.969 1.00 145.36 ? 1343 THR   A OG1  1 
ATOM   68   C  CG2  . THR   A 1 11   ? 188.199 171.459 236.629 1.00 151.68 ? 1343 THR   A CG2  1 
ATOM   69   N  N    . GLY   A 1 12   ? 187.540 170.506 233.088 1.00 162.49 ? 1344 GLY   A N    1 
ATOM   70   C  CA   . GLY   A 1 12   ? 187.156 169.187 232.642 1.00 159.38 ? 1344 GLY   A CA   1 
ATOM   71   C  C    . GLY   A 1 12   ? 186.808 168.228 233.751 1.00 159.43 ? 1344 GLY   A C    1 
ATOM   72   O  O    . GLY   A 1 12   ? 187.185 167.055 233.674 1.00 156.52 ? 1344 GLY   A O    1 
ATOM   73   N  N    . SER   A 1 13   ? 186.092 168.690 234.782 1.00 164.20 ? 1345 SER   A N    1 
ATOM   74   C  CA   . SER   A 1 13   ? 185.733 167.818 235.898 1.00 168.03 ? 1345 SER   A CA   1 
ATOM   75   C  C    . SER   A 1 13   ? 184.926 166.625 235.414 1.00 173.32 ? 1345 SER   A C    1 
ATOM   76   O  O    . SER   A 1 13   ? 184.863 165.588 236.085 1.00 178.64 ? 1345 SER   A O    1 
ATOM   77   C  CB   . SER   A 1 13   ? 184.952 168.599 236.953 1.00 160.54 ? 1345 SER   A CB   1 
ATOM   78   O  OG   . SER   A 1 13   ? 185.691 169.710 237.422 1.00 152.06 ? 1345 SER   A OG   1 
ATOM   79   N  N    . GLY   A 1 14   ? 184.291 166.761 234.255 1.00 165.91 ? 1346 GLY   A N    1 
ATOM   80   C  CA   . GLY   A 1 14   ? 183.643 165.638 233.620 1.00 173.98 ? 1346 GLY   A CA   1 
ATOM   81   C  C    . GLY   A 1 14   ? 184.611 164.499 233.389 1.00 176.60 ? 1346 GLY   A C    1 
ATOM   82   O  O    . GLY   A 1 14   ? 184.421 163.407 233.931 1.00 179.00 ? 1346 GLY   A O    1 
ATOM   83   N  N    . LYS   A 1 15   ? 185.670 164.739 232.610 1.00 172.22 ? 1347 LYS   A N    1 
ATOM   84   C  CA   . LYS   A 1 15   ? 186.561 163.639 232.265 1.00 175.45 ? 1347 LYS   A CA   1 
ATOM   85   C  C    . LYS   A 1 15   ? 187.412 163.203 233.448 1.00 175.66 ? 1347 LYS   A C    1 
ATOM   86   O  O    . LYS   A 1 15   ? 188.063 162.155 233.376 1.00 174.86 ? 1347 LYS   A O    1 
ATOM   87   C  CB   . LYS   A 1 15   ? 187.465 164.001 231.081 1.00 176.64 ? 1347 LYS   A CB   1 
ATOM   88   C  CG   . LYS   A 1 15   ? 188.478 165.116 231.300 1.00 170.95 ? 1347 LYS   A CG   1 
ATOM   89   C  CD   . LYS   A 1 15   ? 188.711 165.891 230.008 1.00 169.60 ? 1347 LYS   A CD   1 
ATOM   90   C  CE   . LYS   A 1 15   ? 189.761 166.979 230.172 1.00 172.50 ? 1347 LYS   A CE   1 
ATOM   91   N  NZ   . LYS   A 1 15   ? 189.587 167.814 231.380 1.00 169.45 ? 1347 LYS   A NZ   1 
ATOM   92   N  N    . THR   A 1 16   ? 187.421 163.976 234.534 1.00 174.74 ? 1348 THR   A N    1 
ATOM   93   C  CA   . THR   A 1 16   ? 188.144 163.555 235.728 1.00 178.64 ? 1348 THR   A CA   1 
ATOM   94   C  C    . THR   A 1 16   ? 187.461 162.368 236.396 1.00 179.07 ? 1348 THR   A C    1 
ATOM   95   O  O    . THR   A 1 16   ? 188.036 161.278 236.492 1.00 181.69 ? 1348 THR   A O    1 
ATOM   96   C  CB   . THR   A 1 16   ? 188.275 164.723 236.707 1.00 171.91 ? 1348 THR   A CB   1 
ATOM   97   O  OG1  . THR   A 1 16   ? 187.002 164.987 237.312 1.00 168.01 ? 1348 THR   A OG1  1 
ATOM   98   C  CG2  . THR   A 1 16   ? 188.810 165.968 236.011 1.00 160.44 ? 1348 THR   A CG2  1 
ATOM   99   N  N    . THR   A 1 17   ? 186.231 162.561 236.872 1.00 177.69 ? 1349 THR   A N    1 
ATOM   100  C  CA   . THR   A 1 17   ? 185.528 161.507 237.602 1.00 185.24 ? 1349 THR   A CA   1 
ATOM   101  C  C    . THR   A 1 17   ? 184.076 161.307 237.191 1.00 188.93 ? 1349 THR   A C    1 
ATOM   102  O  O    . THR   A 1 17   ? 183.457 160.349 237.666 1.00 186.58 ? 1349 THR   A O    1 
ATOM   103  C  CB   . THR   A 1 17   ? 185.571 161.779 239.115 1.00 180.45 ? 1349 THR   A CB   1 
ATOM   104  O  OG1  . THR   A 1 17   ? 184.857 162.986 239.408 1.00 176.23 ? 1349 THR   A OG1  1 
ATOM   105  C  CG2  . THR   A 1 17   ? 187.006 161.906 239.619 1.00 169.42 ? 1349 THR   A CG2  1 
ATOM   106  N  N    . LEU   A 1 18   ? 183.504 162.151 236.332 1.00 188.59 ? 1350 LEU   A N    1 
ATOM   107  C  CA   . LEU   A 1 18   ? 182.061 162.191 236.132 1.00 192.63 ? 1350 LEU   A CA   1 
ATOM   108  C  C    . LEU   A 1 18   ? 181.574 161.317 234.977 1.00 195.23 ? 1350 LEU   A C    1 
ATOM   109  O  O    . LEU   A 1 18   ? 180.387 160.974 234.945 1.00 199.22 ? 1350 LEU   A O    1 
ATOM   110  C  CB   . LEU   A 1 18   ? 181.619 163.644 235.906 1.00 183.90 ? 1350 LEU   A CB   1 
ATOM   111  C  CG   . LEU   A 1 18   ? 180.162 163.994 235.598 1.00 179.21 ? 1350 LEU   A CG   1 
ATOM   112  C  CD1  . LEU   A 1 18   ? 179.228 163.366 236.617 1.00 187.57 ? 1350 LEU   A CD1  1 
ATOM   113  C  CD2  . LEU   A 1 18   ? 179.974 165.498 235.554 1.00 167.33 ? 1350 LEU   A CD2  1 
ATOM   114  N  N    . LEU   A 1 19   ? 182.451 160.932 234.046 1.00 191.82 ? 1351 LEU   A N    1 
ATOM   115  C  CA   . LEU   A 1 19   ? 182.016 160.164 232.880 1.00 194.98 ? 1351 LEU   A CA   1 
ATOM   116  C  C    . LEU   A 1 19   ? 181.317 158.872 233.290 1.00 201.86 ? 1351 LEU   A C    1 
ATOM   117  O  O    . LEU   A 1 19   ? 180.143 158.659 232.969 1.00 201.53 ? 1351 LEU   A O    1 
ATOM   118  C  CB   . LEU   A 1 19   ? 183.206 159.867 231.966 1.00 191.63 ? 1351 LEU   A CB   1 
ATOM   119  C  CG   . LEU   A 1 19   ? 184.159 161.011 231.633 1.00 181.98 ? 1351 LEU   A CG   1 
ATOM   120  C  CD1  . LEU   A 1 19   ? 185.082 160.599 230.506 1.00 178.01 ? 1351 LEU   A CD1  1 
ATOM   121  C  CD2  . LEU   A 1 19   ? 183.354 162.224 231.207 1.00 179.69 ? 1351 LEU   A CD2  1 
ATOM   122  N  N    . GLN   A 1 20   ? 182.027 157.993 234.000 1.00 205.04 ? 1352 GLN   A N    1 
ATOM   123  C  CA   . GLN   A 1 20   ? 181.410 156.745 234.439 1.00 204.32 ? 1352 GLN   A CA   1 
ATOM   124  C  C    . GLN   A 1 20   ? 180.255 157.012 235.396 1.00 205.91 ? 1352 GLN   A C    1 
ATOM   125  O  O    . GLN   A 1 20   ? 179.301 156.228 235.462 1.00 207.21 ? 1352 GLN   A O    1 
ATOM   126  C  CB   . GLN   A 1 20   ? 182.455 155.836 235.088 1.00 197.36 ? 1352 GLN   A CB   1 
ATOM   127  C  CG   . GLN   A 1 20   ? 183.398 155.100 234.120 1.00 191.10 ? 1352 GLN   A CG   1 
ATOM   128  C  CD   . GLN   A 1 20   ? 182.716 154.413 232.932 1.00 191.30 ? 1352 GLN   A CD   1 
ATOM   129  O  OE1  . GLN   A 1 20   ? 181.493 154.283 232.867 1.00 192.71 ? 1352 GLN   A OE1  1 
ATOM   130  N  NE2  . GLN   A 1 20   ? 183.528 153.972 231.977 1.00 193.36 ? 1352 GLN   A NE2  1 
ATOM   131  N  N    . GLN   A 1 21   ? 180.327 158.112 236.149 1.00 204.91 ? 1353 GLN   A N    1 
ATOM   132  C  CA   . GLN   A 1 21   ? 179.198 158.516 236.978 1.00 202.22 ? 1353 GLN   A CA   1 
ATOM   133  C  C    . GLN   A 1 21   ? 177.990 158.887 236.127 1.00 201.56 ? 1353 GLN   A C    1 
ATOM   134  O  O    . GLN   A 1 21   ? 176.858 158.496 236.435 1.00 200.08 ? 1353 GLN   A O    1 
ATOM   135  C  CB   . GLN   A 1 21   ? 179.597 159.690 237.870 1.00 199.56 ? 1353 GLN   A CB   1 
ATOM   136  C  CG   . GLN   A 1 21   ? 178.436 160.283 238.635 1.00 199.67 ? 1353 GLN   A CG   1 
ATOM   137  C  CD   . GLN   A 1 21   ? 178.815 160.746 240.023 1.00 199.61 ? 1353 GLN   A CD   1 
ATOM   138  O  OE1  . GLN   A 1 21   ? 179.715 160.192 240.651 1.00 199.89 ? 1353 GLN   A OE1  1 
ATOM   139  N  NE2  . GLN   A 1 21   ? 178.119 161.763 240.516 1.00 199.01 ? 1353 GLN   A NE2  1 
ATOM   140  N  N    . LEU   A 1 22   ? 178.210 159.647 235.051 1.00 201.00 ? 1354 LEU   A N    1 
ATOM   141  C  CA   . LEU   A 1 22   ? 177.097 160.070 234.210 1.00 202.04 ? 1354 LEU   A CA   1 
ATOM   142  C  C    . LEU   A 1 22   ? 176.546 158.919 233.378 1.00 203.69 ? 1354 LEU   A C    1 
ATOM   143  O  O    . LEU   A 1 22   ? 175.334 158.854 233.141 1.00 202.85 ? 1354 LEU   A O    1 
ATOM   144  C  CB   . LEU   A 1 22   ? 177.528 161.222 233.303 1.00 198.35 ? 1354 LEU   A CB   1 
ATOM   145  C  CG   . LEU   A 1 22   ? 176.396 162.094 232.753 1.00 190.90 ? 1354 LEU   A CG   1 
ATOM   146  C  CD1  . LEU   A 1 22   ? 175.820 162.986 233.845 1.00 184.37 ? 1354 LEU   A CD1  1 
ATOM   147  C  CD2  . LEU   A 1 22   ? 176.872 162.922 231.569 1.00 175.71 ? 1354 LEU   A CD2  1 
ATOM   148  N  N    . MET   A 1 23   ? 177.408 158.012 232.926 1.00 204.00 ? 1355 MET   A N    1 
ATOM   149  C  CA   . MET   A 1 23   ? 176.969 156.875 232.124 1.00 201.02 ? 1355 MET   A CA   1 
ATOM   150  C  C    . MET   A 1 23   ? 176.092 155.937 232.947 1.00 197.17 ? 1355 MET   A C    1 
ATOM   151  O  O    . MET   A 1 23   ? 175.156 155.328 232.428 1.00 191.83 ? 1355 MET   A O    1 
ATOM   152  C  CB   . MET   A 1 23   ? 178.170 156.110 231.562 1.00 202.22 ? 1355 MET   A CB   1 
ATOM   153  C  CG   . MET   A 1 23   ? 179.024 156.886 230.565 1.00 201.58 ? 1355 MET   A CG   1 
ATOM   154  S  SD   . MET   A 1 23   ? 178.152 157.395 229.070 1.00 202.90 ? 1355 MET   A SD   1 
ATOM   155  C  CE   . MET   A 1 23   ? 177.857 159.128 229.418 1.00 198.10 ? 1355 MET   A CE   1 
ATOM   156  N  N    . GLY   A 1 38   ? 191.259 167.671 225.516 1.00 182.33 ? 1370 GLY   A N    1 
ATOM   157  C  CA   . GLY   A 1 38   ? 190.829 166.989 224.311 1.00 185.35 ? 1370 GLY   A CA   1 
ATOM   158  C  C    . GLY   A 1 38   ? 189.338 166.754 224.274 1.00 186.06 ? 1370 GLY   A C    1 
ATOM   159  O  O    . GLY   A 1 38   ? 188.715 166.523 225.307 1.00 182.23 ? 1370 GLY   A O    1 
ATOM   160  N  N    . ILE   A 1 39   ? 188.764 166.811 223.077 1.00 192.08 ? 1371 ILE   A N    1 
ATOM   161  C  CA   . ILE   A 1 39   ? 187.328 166.623 222.905 1.00 193.84 ? 1371 ILE   A CA   1 
ATOM   162  C  C    . ILE   A 1 39   ? 187.044 165.130 222.806 1.00 193.00 ? 1371 ILE   A C    1 
ATOM   163  O  O    . ILE   A 1 39   ? 187.631 164.430 221.974 1.00 189.79 ? 1371 ILE   A O    1 
ATOM   164  C  CB   . ILE   A 1 39   ? 186.815 167.364 221.663 1.00 190.83 ? 1371 ILE   A CB   1 
ATOM   165  C  CG1  . ILE   A 1 39   ? 187.122 168.862 221.754 1.00 188.89 ? 1371 ILE   A CG1  1 
ATOM   166  C  CG2  . ILE   A 1 39   ? 185.321 167.140 221.495 1.00 187.60 ? 1371 ILE   A CG2  1 
ATOM   167  C  CD1  . ILE   A 1 39   ? 186.493 169.565 222.925 1.00 177.08 ? 1371 ILE   A CD1  1 
ATOM   168  N  N    . ASP   A 1 40   ? 186.141 164.640 223.650 1.00 195.21 ? 1372 ASP   A N    1 
ATOM   169  C  CA   . ASP   A 1 40   ? 185.776 163.231 223.677 1.00 197.77 ? 1372 ASP   A CA   1 
ATOM   170  C  C    . ASP   A 1 40   ? 184.329 163.070 223.232 1.00 197.71 ? 1372 ASP   A C    1 
ATOM   171  O  O    . ASP   A 1 40   ? 183.454 163.846 223.632 1.00 192.30 ? 1372 ASP   A O    1 
ATOM   172  C  CB   . ASP   A 1 40   ? 185.967 162.638 225.077 1.00 198.01 ? 1372 ASP   A CB   1 
ATOM   173  C  CG   . ASP   A 1 40   ? 186.161 161.133 225.052 1.00 198.01 ? 1372 ASP   A CG   1 
ATOM   174  O  OD1  . ASP   A 1 40   ? 185.809 160.463 226.046 1.00 193.18 ? 1372 ASP   A OD1  1 
ATOM   175  O  OD2  . ASP   A 1 40   ? 186.673 160.620 224.035 1.00 198.65 ? 1372 ASP   A OD2  1 
ATOM   176  N  N    . VAL   A 1 41   ? 184.083 162.061 222.400 1.00 202.35 ? 1373 VAL   A N    1 
ATOM   177  C  CA   . VAL   A 1 41   ? 182.761 161.798 221.844 1.00 200.89 ? 1373 VAL   A CA   1 
ATOM   178  C  C    . VAL   A 1 41   ? 182.395 160.361 222.182 1.00 201.65 ? 1373 VAL   A C    1 
ATOM   179  O  O    . VAL   A 1 41   ? 183.173 159.439 221.907 1.00 201.70 ? 1373 VAL   A O    1 
ATOM   180  C  CB   . VAL   A 1 41   ? 182.725 162.012 220.321 1.00 199.92 ? 1373 VAL   A CB   1 
ATOM   181  C  CG1  . VAL   A 1 41   ? 181.357 161.644 219.756 1.00 197.39 ? 1373 VAL   A CG1  1 
ATOM   182  C  CG2  . VAL   A 1 41   ? 183.124 163.433 219.961 1.00 198.15 ? 1373 VAL   A CG2  1 
ATOM   183  N  N    . LYS   A 1 42   ? 181.218 160.167 222.772 1.00 202.96 ? 1374 LYS   A N    1 
ATOM   184  C  CA   . LYS   A 1 42   ? 180.706 158.831 223.034 1.00 207.75 ? 1374 LYS   A CA   1 
ATOM   185  C  C    . LYS   A 1 42   ? 179.188 158.879 223.122 1.00 210.51 ? 1374 LYS   A C    1 
ATOM   186  O  O    . LYS   A 1 42   ? 178.597 159.924 223.407 1.00 203.76 ? 1374 LYS   A O    1 
ATOM   187  C  CB   . LYS   A 1 42   ? 181.299 158.229 224.316 1.00 203.83 ? 1374 LYS   A CB   1 
ATOM   188  C  CG   . LYS   A 1 42   ? 180.758 158.809 225.610 1.00 197.42 ? 1374 LYS   A CG   1 
ATOM   189  C  CD   . LYS   A 1 42   ? 181.827 158.801 226.694 1.00 188.48 ? 1374 LYS   A CD   1 
ATOM   190  C  CE   . LYS   A 1 42   ? 181.495 159.763 227.821 1.00 176.83 ? 1374 LYS   A CE   1 
ATOM   191  N  NZ   . LYS   A 1 42   ? 181.548 161.180 227.374 1.00 175.92 ? 1374 LYS   A NZ   1 
ATOM   192  N  N    . ASP   A 1 43   ? 178.565 157.732 222.873 1.00 218.06 ? 1375 ASP   A N    1 
ATOM   193  C  CA   . ASP   A 1 43   ? 177.116 157.635 222.810 1.00 218.19 ? 1375 ASP   A CA   1 
ATOM   194  C  C    . ASP   A 1 43   ? 176.543 157.239 224.164 1.00 219.91 ? 1375 ASP   A C    1 
ATOM   195  O  O    . ASP   A 1 43   ? 177.067 156.358 224.852 1.00 219.14 ? 1375 ASP   A O    1 
ATOM   196  C  CB   . ASP   A 1 43   ? 176.695 156.621 221.746 1.00 214.75 ? 1375 ASP   A CB   1 
ATOM   197  C  CG   . ASP   A 1 43   ? 175.510 157.092 220.933 1.00 210.12 ? 1375 ASP   A CG   1 
ATOM   198  O  OD1  . ASP   A 1 43   ? 175.281 156.543 219.835 1.00 207.92 ? 1375 ASP   A OD1  1 
ATOM   199  O  OD2  . ASP   A 1 43   ? 174.810 158.015 221.395 1.00 209.22 ? 1375 ASP   A OD2  1 
ATOM   200  N  N    . TRP   A 1 44   ? 175.447 157.897 224.537 1.00 218.23 ? 1376 TRP   A N    1 
ATOM   201  C  CA   . TRP   A 1 44   ? 174.800 157.683 225.829 1.00 218.02 ? 1376 TRP   A CA   1 
ATOM   202  C  C    . TRP   A 1 44   ? 173.317 157.430 225.599 1.00 217.84 ? 1376 TRP   A C    1 
ATOM   203  O  O    . TRP   A 1 44   ? 172.515 158.385 225.636 1.00 216.32 ? 1376 TRP   A O    1 
ATOM   204  C  CB   . TRP   A 1 44   ? 175.015 158.886 226.751 1.00 214.40 ? 1376 TRP   A CB   1 
ATOM   205  C  CG   . TRP   A 1 44   ? 174.408 158.727 228.109 1.00 210.74 ? 1376 TRP   A CG   1 
ATOM   206  C  CD1  . TRP   A 1 44   ? 174.760 157.822 229.066 1.00 206.25 ? 1376 TRP   A CD1  1 
ATOM   207  C  CD2  . TRP   A 1 44   ? 173.337 159.499 228.661 1.00 206.37 ? 1376 TRP   A CD2  1 
ATOM   208  N  NE1  . TRP   A 1 44   ? 173.976 157.985 230.182 1.00 202.26 ? 1376 TRP   A NE1  1 
ATOM   209  C  CE2  . TRP   A 1 44   ? 173.092 159.008 229.958 1.00 203.56 ? 1376 TRP   A CE2  1 
ATOM   210  C  CE3  . TRP   A 1 44   ? 172.559 160.559 228.183 1.00 202.89 ? 1376 TRP   A CE3  1 
ATOM   211  C  CZ2  . TRP   A 1 44   ? 172.104 159.539 230.783 1.00 201.51 ? 1376 TRP   A CZ2  1 
ATOM   212  C  CZ3  . TRP   A 1 44   ? 171.579 161.085 229.003 1.00 200.76 ? 1376 TRP   A CZ3  1 
ATOM   213  C  CH2  . TRP   A 1 44   ? 171.359 160.574 230.288 1.00 200.45 ? 1376 TRP   A CH2  1 
ATOM   214  N  N    . PRO   A 1 45   ? 172.905 156.190 225.353 1.00 217.54 ? 1377 PRO   A N    1 
ATOM   215  C  CA   . PRO   A 1 45   ? 171.482 155.891 225.178 1.00 217.74 ? 1377 PRO   A CA   1 
ATOM   216  C  C    . PRO   A 1 45   ? 170.704 156.004 226.483 1.00 219.99 ? 1377 PRO   A C    1 
ATOM   217  O  O    . PRO   A 1 45   ? 171.258 155.957 227.583 1.00 219.03 ? 1377 PRO   A O    1 
ATOM   218  C  CB   . PRO   A 1 45   ? 171.488 154.437 224.679 1.00 218.58 ? 1377 PRO   A CB   1 
ATOM   219  C  CG   . PRO   A 1 45   ? 172.849 154.236 224.099 1.00 217.92 ? 1377 PRO   A CG   1 
ATOM   220  C  CD   . PRO   A 1 45   ? 173.761 155.059 224.957 1.00 216.34 ? 1377 PRO   A CD   1 
ATOM   221  N  N    . ILE   A 1 46   ? 169.391 156.153 226.334 1.00 220.20 ? 1378 ILE   A N    1 
ATOM   222  C  CA   . ILE   A 1 46   ? 168.489 156.187 227.480 1.00 214.60 ? 1378 ILE   A CA   1 
ATOM   223  C  C    . ILE   A 1 46   ? 167.634 154.924 227.512 1.00 209.62 ? 1378 ILE   A C    1 
ATOM   224  O  O    . ILE   A 1 46   ? 166.621 154.830 226.818 1.00 207.06 ? 1378 ILE   A O    1 
ATOM   225  C  CB   . ILE   A 1 46   ? 167.599 157.442 227.461 1.00 208.17 ? 1378 ILE   A CB   1 
ATOM   226  C  CG1  . ILE   A 1 46   ? 168.452 158.703 227.317 1.00 200.77 ? 1378 ILE   A CG1  1 
ATOM   227  C  CG2  . ILE   A 1 46   ? 166.748 157.513 228.721 1.00 200.03 ? 1378 ILE   A CG2  1 
ATOM   228  C  CD1  . ILE   A 1 46   ? 167.636 159.962 227.158 1.00 188.89 ? 1378 ILE   A CD1  1 
ATOM   229  N  N    . LEU   A 1 56   ? 166.342 157.039 224.234 1.00 207.98 ? 1388 LEU   A N    1 
ATOM   230  C  CA   . LEU   A 1 56   ? 166.704 158.087 223.288 1.00 206.73 ? 1388 LEU   A CA   1 
ATOM   231  C  C    . LEU   A 1 56   ? 168.226 158.185 223.201 1.00 208.54 ? 1388 LEU   A C    1 
ATOM   232  O  O    . LEU   A 1 56   ? 168.919 158.136 224.216 1.00 207.12 ? 1388 LEU   A O    1 
ATOM   233  C  CB   . LEU   A 1 56   ? 166.088 159.426 223.711 1.00 206.75 ? 1388 LEU   A CB   1 
ATOM   234  C  CG   . LEU   A 1 56   ? 166.504 160.727 223.017 1.00 207.05 ? 1388 LEU   A CG   1 
ATOM   235  C  CD1  . LEU   A 1 56   ? 166.497 160.590 221.499 1.00 208.12 ? 1388 LEU   A CD1  1 
ATOM   236  C  CD2  . LEU   A 1 56   ? 165.609 161.876 223.458 1.00 198.94 ? 1388 LEU   A CD2  1 
ATOM   237  N  N    . VAL   A 1 57   ? 168.740 158.322 221.983 1.00 211.32 ? 1389 VAL   A N    1 
ATOM   238  C  CA   . VAL   A 1 57   ? 170.174 158.371 221.727 1.00 211.08 ? 1389 VAL   A CA   1 
ATOM   239  C  C    . VAL   A 1 57   ? 170.661 159.797 221.939 1.00 209.64 ? 1389 VAL   A C    1 
ATOM   240  O  O    . VAL   A 1 57   ? 170.083 160.747 221.396 1.00 208.69 ? 1389 VAL   A O    1 
ATOM   241  C  CB   . VAL   A 1 57   ? 170.500 157.884 220.304 1.00 209.47 ? 1389 VAL   A CB   1 
ATOM   242  C  CG1  . VAL   A 1 57   ? 171.982 158.042 220.012 1.00 209.30 ? 1389 VAL   A CG1  1 
ATOM   243  C  CG2  . VAL   A 1 57   ? 170.072 156.437 220.130 1.00 204.71 ? 1389 VAL   A CG2  1 
ATOM   244  N  N    . LEU   A 1 58   ? 171.709 159.951 222.746 1.00 208.61 ? 1390 LEU   A N    1 
ATOM   245  C  CA   . LEU   A 1 58   ? 172.351 161.237 222.976 1.00 207.12 ? 1390 LEU   A CA   1 
ATOM   246  C  C    . LEU   A 1 58   ? 173.841 161.112 222.696 1.00 206.39 ? 1390 LEU   A C    1 
ATOM   247  O  O    . LEU   A 1 58   ? 174.490 160.157 223.129 1.00 206.17 ? 1390 LEU   A O    1 
ATOM   248  C  CB   . LEU   A 1 58   ? 172.141 161.746 224.416 1.00 204.66 ? 1390 LEU   A CB   1 
ATOM   249  C  CG   . LEU   A 1 58   ? 170.826 162.408 224.850 1.00 203.24 ? 1390 LEU   A CG   1 
ATOM   250  C  CD1  . LEU   A 1 58   ? 170.630 163.741 224.145 1.00 197.07 ? 1390 LEU   A CD1  1 
ATOM   251  C  CD2  . LEU   A 1 58   ? 169.624 161.508 224.637 1.00 206.79 ? 1390 LEU   A CD2  1 
ATOM   252  N  N    . ASN   A 1 59   ? 174.380 162.092 221.976 1.00 203.77 ? 1391 ASN   A N    1 
ATOM   253  C  CA   . ASN   A 1 59   ? 175.796 162.125 221.614 1.00 200.95 ? 1391 ASN   A CA   1 
ATOM   254  C  C    . ASN   A 1 59   ? 176.451 163.208 222.468 1.00 197.09 ? 1391 ASN   A C    1 
ATOM   255  O  O    . ASN   A 1 59   ? 176.315 164.402 222.198 1.00 195.36 ? 1391 ASN   A O    1 
ATOM   256  C  CB   . ASN   A 1 59   ? 175.981 162.385 220.119 1.00 193.99 ? 1391 ASN   A CB   1 
ATOM   257  C  CG   . ASN   A 1 59   ? 177.437 162.327 219.689 1.00 191.52 ? 1391 ASN   A CG   1 
ATOM   258  O  OD1  . ASN   A 1 59   ? 178.297 163.005 220.253 1.00 191.41 ? 1391 ASN   A OD1  1 
ATOM   259  N  ND2  . ASN   A 1 59   ? 177.719 161.510 218.681 1.00 187.72 ? 1391 ASN   A ND2  1 
ATOM   260  N  N    . VAL   A 1 60   ? 177.161 162.778 223.509 1.00 196.91 ? 1392 VAL   A N    1 
ATOM   261  C  CA   . VAL   A 1 60   ? 177.765 163.713 224.451 1.00 194.76 ? 1392 VAL   A CA   1 
ATOM   262  C  C    . VAL   A 1 60   ? 179.151 164.112 223.956 1.00 193.64 ? 1392 VAL   A C    1 
ATOM   263  O  O    . VAL   A 1 60   ? 179.926 163.274 223.480 1.00 194.46 ? 1392 VAL   A O    1 
ATOM   264  C  CB   . VAL   A 1 60   ? 177.814 163.113 225.864 1.00 192.53 ? 1392 VAL   A CB   1 
ATOM   265  C  CG1  . VAL   A 1 60   ? 178.720 161.897 225.913 1.00 191.24 ? 1392 VAL   A CG1  1 
ATOM   266  C  CG2  . VAL   A 1 60   ? 178.281 164.153 226.862 1.00 188.60 ? 1392 VAL   A CG2  1 
ATOM   267  N  N    . TRP   A 1 61   ? 179.451 165.407 224.027 1.00 190.70 ? 1393 TRP   A N    1 
ATOM   268  C  CA   . TRP   A 1 61   ? 180.783 165.930 223.761 1.00 189.61 ? 1393 TRP   A CA   1 
ATOM   269  C  C    . TRP   A 1 61   ? 181.376 166.515 225.035 1.00 188.52 ? 1393 TRP   A C    1 
ATOM   270  O  O    . TRP   A 1 61   ? 180.667 167.134 225.835 1.00 183.13 ? 1393 TRP   A O    1 
ATOM   271  C  CB   . TRP   A 1 61   ? 180.774 166.992 222.656 1.00 186.78 ? 1393 TRP   A CB   1 
ATOM   272  C  CG   . TRP   A 1 61   ? 180.276 166.506 221.329 1.00 187.79 ? 1393 TRP   A CG   1 
ATOM   273  C  CD1  . TRP   A 1 61   ? 180.995 165.825 220.399 1.00 187.01 ? 1393 TRP   A CD1  1 
ATOM   274  C  CD2  . TRP   A 1 61   ? 178.975 166.708 220.760 1.00 187.93 ? 1393 TRP   A CD2  1 
ATOM   275  N  NE1  . TRP   A 1 61   ? 180.221 165.560 219.296 1.00 186.00 ? 1393 TRP   A NE1  1 
ATOM   276  C  CE2  . TRP   A 1 61   ? 178.977 166.097 219.492 1.00 186.66 ? 1393 TRP   A CE2  1 
ATOM   277  C  CE3  . TRP   A 1 61   ? 177.807 167.330 221.202 1.00 186.92 ? 1393 TRP   A CE3  1 
ATOM   278  C  CZ2  . TRP   A 1 61   ? 177.861 166.096 218.665 1.00 184.77 ? 1393 TRP   A CZ2  1 
ATOM   279  C  CZ3  . TRP   A 1 61   ? 176.705 167.331 220.377 1.00 187.07 ? 1393 TRP   A CZ3  1 
ATOM   280  C  CH2  . TRP   A 1 61   ? 176.736 166.716 219.125 1.00 186.11 ? 1393 TRP   A CH2  1 
ATOM   281  N  N    . ASP   A 1 62   ? 182.677 166.300 225.219 1.00 189.44 ? 1394 ASP   A N    1 
ATOM   282  C  CA   . ASP   A 1 62   ? 183.426 166.802 226.364 1.00 185.18 ? 1394 ASP   A CA   1 
ATOM   283  C  C    . ASP   A 1 62   ? 184.445 167.832 225.899 1.00 181.87 ? 1394 ASP   A C    1 
ATOM   284  O  O    . ASP   A 1 62   ? 185.113 167.636 224.883 1.00 185.55 ? 1394 ASP   A O    1 
ATOM   285  C  CB   . ASP   A 1 62   ? 184.152 165.669 227.092 1.00 186.15 ? 1394 ASP   A CB   1 
ATOM   286  C  CG   . ASP   A 1 62   ? 184.772 166.118 228.404 1.00 181.84 ? 1394 ASP   A CG   1 
ATOM   287  O  OD1  . ASP   A 1 62   ? 184.664 167.314 228.746 1.00 185.42 ? 1394 ASP   A OD1  1 
ATOM   288  O  OD2  . ASP   A 1 62   ? 185.384 165.274 229.088 1.00 175.91 ? 1394 ASP   A OD2  1 
ATOM   289  N  N    . PHE   A 1 63   ? 184.560 168.930 226.647 1.00 178.21 ? 1395 PHE   A N    1 
ATOM   290  C  CA   . PHE   A 1 63   ? 185.575 169.941 226.373 1.00 178.26 ? 1395 PHE   A CA   1 
ATOM   291  C  C    . PHE   A 1 63   ? 186.727 169.813 227.361 1.00 178.72 ? 1395 PHE   A C    1 
ATOM   292  O  O    . PHE   A 1 63   ? 186.784 168.837 228.114 1.00 182.70 ? 1395 PHE   A O    1 
ATOM   293  C  CB   . PHE   A 1 63   ? 184.956 171.336 226.409 1.00 178.47 ? 1395 PHE   A CB   1 
ATOM   294  C  CG   . PHE   A 1 63   ? 183.655 171.433 225.664 1.00 173.91 ? 1395 PHE   A CG   1 
ATOM   295  C  CD1  . PHE   A 1 63   ? 183.628 171.410 224.283 1.00 166.27 ? 1395 PHE   A CD1  1 
ATOM   296  C  CD2  . PHE   A 1 63   ? 182.463 171.540 226.344 1.00 168.50 ? 1395 PHE   A CD2  1 
ATOM   297  C  CE1  . PHE   A 1 63   ? 182.429 171.495 223.598 1.00 159.14 ? 1395 PHE   A CE1  1 
ATOM   298  C  CE2  . PHE   A 1 63   ? 181.264 171.611 225.667 1.00 164.11 ? 1395 PHE   A CE2  1 
ATOM   299  C  CZ   . PHE   A 1 63   ? 181.249 171.596 224.294 1.00 160.07 ? 1395 PHE   A CZ   1 
ATOM   300  N  N    . ALA   A 1 64   ? 187.652 170.771 227.373 1.00 180.29 ? 1396 ALA   A N    1 
ATOM   301  C  CA   . ALA   A 1 64   ? 188.868 170.604 228.160 1.00 181.85 ? 1396 ALA   A CA   1 
ATOM   302  C  C    . ALA   A 1 64   ? 189.269 171.930 228.791 1.00 174.02 ? 1396 ALA   A C    1 
ATOM   303  O  O    . ALA   A 1 64   ? 188.603 172.955 228.622 1.00 169.35 ? 1396 ALA   A O    1 
ATOM   304  C  CB   . ALA   A 1 64   ? 190.010 170.046 227.307 1.00 181.78 ? 1396 ALA   A CB   1 
ATOM   305  N  N    . GLY   A 1 65   ? 190.380 171.886 229.526 1.00 172.76 ? 1397 GLY   A N    1 
ATOM   306  C  CA   . GLY   A 1 65   ? 190.923 173.018 230.240 1.00 168.59 ? 1397 GLY   A CA   1 
ATOM   307  C  C    . GLY   A 1 65   ? 192.014 173.782 229.531 1.00 165.25 ? 1397 GLY   A C    1 
ATOM   308  O  O    . GLY   A 1 65   ? 192.442 174.827 230.031 1.00 165.74 ? 1397 GLY   A O    1 
ATOM   309  N  N    . ARG   A 1 66   ? 192.492 173.296 228.386 1.00 162.54 ? 1398 ARG   A N    1 
ATOM   310  C  CA   . ARG   A 1 66   ? 193.455 174.026 227.574 1.00 164.06 ? 1398 ARG   A CA   1 
ATOM   311  C  C    . ARG   A 1 66   ? 192.786 174.787 226.439 1.00 168.61 ? 1398 ARG   A C    1 
ATOM   312  O  O    . ARG   A 1 66   ? 193.400 174.977 225.385 1.00 169.06 ? 1398 ARG   A O    1 
ATOM   313  C  CB   . ARG   A 1 66   ? 194.512 173.073 227.012 1.00 158.62 ? 1398 ARG   A CB   1 
ATOM   314  N  N    . GLU   A 1 67   ? 191.544 175.225 226.632 1.00 168.51 ? 1399 GLU   A N    1 
ATOM   315  C  CA   . GLU   A 1 67   ? 190.765 175.844 225.567 1.00 163.98 ? 1399 GLU   A CA   1 
ATOM   316  C  C    . GLU   A 1 67   ? 191.367 177.182 225.152 1.00 163.94 ? 1399 GLU   A C    1 
ATOM   317  O  O    . GLU   A 1 67   ? 191.827 177.955 225.999 1.00 163.73 ? 1399 GLU   A O    1 
ATOM   318  C  CB   . GLU   A 1 67   ? 189.318 176.020 226.028 1.00 162.77 ? 1399 GLU   A CB   1 
ATOM   319  C  CG   . GLU   A 1 67   ? 189.122 176.907 227.257 1.00 156.72 ? 1399 GLU   A CG   1 
ATOM   320  C  CD   . GLU   A 1 67   ? 189.019 178.382 226.924 1.00 153.95 ? 1399 GLU   A CD   1 
ATOM   321  O  OE1  . GLU   A 1 67   ? 188.916 178.717 225.727 1.00 155.68 ? 1399 GLU   A OE1  1 
ATOM   322  O  OE2  . GLU   A 1 67   ? 189.038 179.207 227.861 1.00 150.91 ? 1399 GLU   A OE2  1 
ATOM   323  N  N    . GLU   A 1 68   ? 191.402 177.435 223.843 1.00 163.44 ? 1400 GLU   A N    1 
ATOM   324  C  CA   . GLU   A 1 68   ? 191.684 178.763 223.309 1.00 159.17 ? 1400 GLU   A CA   1 
ATOM   325  C  C    . GLU   A 1 68   ? 190.566 179.295 222.424 1.00 155.82 ? 1400 GLU   A C    1 
ATOM   326  O  O    . GLU   A 1 68   ? 190.030 180.373 222.694 1.00 153.03 ? 1400 GLU   A O    1 
ATOM   327  C  CB   . GLU   A 1 68   ? 192.994 178.753 222.517 1.00 149.04 ? 1400 GLU   A CB   1 
ATOM   328  N  N    . PHE   A 1 69   ? 190.194 178.560 221.372 1.00 159.68 ? 1401 PHE   A N    1 
ATOM   329  C  CA   . PHE   A 1 69   ? 189.140 178.984 220.458 1.00 161.19 ? 1401 PHE   A CA   1 
ATOM   330  C  C    . PHE   A 1 69   ? 188.587 177.752 219.738 1.00 168.98 ? 1401 PHE   A C    1 
ATOM   331  O  O    . PHE   A 1 69   ? 189.174 177.215 218.801 1.00 171.22 ? 1401 PHE   A O    1 
ATOM   332  C  CB   . PHE   A 1 69   ? 189.654 180.026 219.461 1.00 152.05 ? 1401 PHE   A CB   1 
ATOM   333  N  N    . TYR   A 1 70   ? 187.427 177.274 220.188 1.00 169.58 ? 1402 TYR   A N    1 
ATOM   334  C  CA   . TYR   A 1 70   ? 186.698 176.231 219.474 1.00 173.23 ? 1402 TYR   A CA   1 
ATOM   335  C  C    . TYR   A 1 70   ? 185.192 176.436 219.523 1.00 176.39 ? 1402 TYR   A C    1 
ATOM   336  O  O    . TYR   A 1 70   ? 184.443 175.524 219.153 1.00 179.03 ? 1402 TYR   A O    1 
ATOM   337  C  CB   . TYR   A 1 70   ? 187.041 174.843 220.017 1.00 176.66 ? 1402 TYR   A CB   1 
ATOM   338  C  CG   . TYR   A 1 70   ? 186.831 174.682 221.500 1.00 172.38 ? 1402 TYR   A CG   1 
ATOM   339  C  CD1  . TYR   A 1 70   ? 187.908 174.537 222.355 1.00 166.93 ? 1402 TYR   A CD1  1 
ATOM   340  C  CD2  . TYR   A 1 70   ? 185.548 174.659 222.047 1.00 168.13 ? 1402 TYR   A CD2  1 
ATOM   341  C  CE1  . TYR   A 1 70   ? 187.722 174.377 223.699 1.00 164.78 ? 1402 TYR   A CE1  1 
ATOM   342  C  CE2  . TYR   A 1 70   ? 185.353 174.509 223.398 1.00 161.60 ? 1402 TYR   A CE2  1 
ATOM   343  C  CZ   . TYR   A 1 70   ? 186.446 174.375 224.221 1.00 163.79 ? 1402 TYR   A CZ   1 
ATOM   344  O  OH   . TYR   A 1 70   ? 186.268 174.214 225.571 1.00 165.35 ? 1402 TYR   A OH   1 
ATOM   345  N  N    . SER   A 1 71   ? 184.725 177.597 219.977 1.00 171.51 ? 1403 SER   A N    1 
ATOM   346  C  CA   . SER   A 1 71   ? 183.312 177.790 220.280 1.00 173.86 ? 1403 SER   A CA   1 
ATOM   347  C  C    . SER   A 1 71   ? 182.425 177.816 219.042 1.00 178.79 ? 1403 SER   A C    1 
ATOM   348  O  O    . SER   A 1 71   ? 181.262 178.218 219.153 1.00 177.12 ? 1403 SER   A O    1 
ATOM   349  C  CB   . SER   A 1 71   ? 183.125 179.081 221.077 1.00 164.12 ? 1403 SER   A CB   1 
ATOM   350  O  OG   . SER   A 1 71   ? 184.073 179.169 222.125 1.00 150.88 ? 1403 SER   A OG   1 
ATOM   351  N  N    . THR   A 1 72   ? 182.942 177.426 217.875 1.00 178.53 ? 1404 THR   A N    1 
ATOM   352  C  CA   . THR   A 1 72   ? 182.105 177.343 216.684 1.00 178.89 ? 1404 THR   A CA   1 
ATOM   353  C  C    . THR   A 1 72   ? 180.980 176.330 216.867 1.00 181.03 ? 1404 THR   A C    1 
ATOM   354  O  O    . THR   A 1 72   ? 179.851 176.559 216.418 1.00 177.21 ? 1404 THR   A O    1 
ATOM   355  C  CB   . THR   A 1 72   ? 182.954 176.976 215.468 1.00 178.95 ? 1404 THR   A CB   1 
ATOM   356  O  OG1  . THR   A 1 72   ? 183.288 175.584 215.522 1.00 180.08 ? 1404 THR   A OG1  1 
ATOM   357  C  CG2  . THR   A 1 72   ? 184.232 177.796 215.445 1.00 175.90 ? 1404 THR   A CG2  1 
ATOM   358  N  N    . HIS   A 1 73   ? 181.275 175.196 217.505 1.00 181.24 ? 1405 HIS   A N    1 
ATOM   359  C  CA   . HIS   A 1 73   ? 180.245 174.181 217.718 1.00 180.42 ? 1405 HIS   A CA   1 
ATOM   360  C  C    . HIS   A 1 73   ? 179.069 174.668 218.559 1.00 181.15 ? 1405 HIS   A C    1 
ATOM   361  O  O    . HIS   A 1 73   ? 177.923 174.375 218.178 1.00 180.00 ? 1405 HIS   A O    1 
ATOM   362  C  CB   . HIS   A 1 73   ? 180.872 172.919 218.328 1.00 176.96 ? 1405 HIS   A CB   1 
ATOM   363  C  CG   . HIS   A 1 73   ? 180.065 171.677 218.112 1.00 180.31 ? 1405 HIS   A CG   1 
ATOM   364  N  ND1  . HIS   A 1 73   ? 178.695 171.643 218.264 1.00 183.37 ? 1405 HIS   A ND1  1 
ATOM   365  C  CD2  . HIS   A 1 73   ? 180.435 170.420 217.772 1.00 178.04 ? 1405 HIS   A CD2  1 
ATOM   366  C  CE1  . HIS   A 1 73   ? 178.255 170.422 218.020 1.00 181.43 ? 1405 HIS   A CE1  1 
ATOM   367  N  NE2  . HIS   A 1 73   ? 179.291 169.660 217.719 1.00 179.37 ? 1405 HIS   A NE2  1 
ATOM   368  N  N    . PRO   A 1 74   ? 179.257 175.365 219.700 1.00 182.08 ? 1406 PRO   A N    1 
ATOM   369  C  CA   . PRO   A 1 74   ? 178.094 175.884 220.431 1.00 183.61 ? 1406 PRO   A CA   1 
ATOM   370  C  C    . PRO   A 1 74   ? 177.116 176.670 219.563 1.00 182.29 ? 1406 PRO   A C    1 
ATOM   371  O  O    . PRO   A 1 74   ? 176.050 176.142 219.250 1.00 179.67 ? 1406 PRO   A O    1 
ATOM   372  C  CB   . PRO   A 1 74   ? 178.724 176.805 221.475 1.00 179.56 ? 1406 PRO   A CB   1 
ATOM   373  C  CG   . PRO   A 1 74   ? 180.082 176.245 221.719 1.00 173.05 ? 1406 PRO   A CG   1 
ATOM   374  C  CD   . PRO   A 1 74   ? 180.469 175.387 220.541 1.00 175.43 ? 1406 PRO   A CD   1 
ATOM   375  N  N    . LEU   A 1 82   ? 172.681 170.151 223.909 1.00 171.48 ? 1414 LEU   A N    1 
ATOM   376  C  CA   . LEU   A 1 82   ? 172.416 170.442 225.312 1.00 175.31 ? 1414 LEU   A CA   1 
ATOM   377  C  C    . LEU   A 1 82   ? 173.646 170.974 226.036 1.00 177.58 ? 1414 LEU   A C    1 
ATOM   378  O  O    . LEU   A 1 82   ? 174.764 170.906 225.531 1.00 180.52 ? 1414 LEU   A O    1 
ATOM   379  C  CB   . LEU   A 1 82   ? 171.894 169.198 226.037 1.00 179.35 ? 1414 LEU   A CB   1 
ATOM   380  C  CG   . LEU   A 1 82   ? 170.433 168.771 225.869 1.00 185.14 ? 1414 LEU   A CG   1 
ATOM   381  C  CD1  . LEU   A 1 82   ? 170.151 168.211 224.496 1.00 188.11 ? 1414 LEU   A CD1  1 
ATOM   382  C  CD2  . LEU   A 1 82   ? 170.082 167.744 226.929 1.00 194.13 ? 1414 LEU   A CD2  1 
ATOM   383  N  N    . TYR   A 1 83   ? 173.418 171.507 227.231 1.00 172.46 ? 1415 TYR   A N    1 
ATOM   384  C  CA   . TYR   A 1 83   ? 174.461 172.088 228.058 1.00 172.61 ? 1415 TYR   A CA   1 
ATOM   385  C  C    . TYR   A 1 83   ? 174.279 171.632 229.497 1.00 176.62 ? 1415 TYR   A C    1 
ATOM   386  O  O    . TYR   A 1 83   ? 173.162 171.318 229.921 1.00 175.00 ? 1415 TYR   A O    1 
ATOM   387  C  CB   . TYR   A 1 83   ? 174.424 173.614 227.984 1.00 171.46 ? 1415 TYR   A CB   1 
ATOM   388  C  CG   . TYR   A 1 83   ? 174.527 174.152 226.579 1.00 170.21 ? 1415 TYR   A CG   1 
ATOM   389  C  CD1  . TYR   A 1 83   ? 175.724 174.099 225.885 1.00 169.04 ? 1415 TYR   A CD1  1 
ATOM   390  C  CD2  . TYR   A 1 83   ? 173.421 174.697 225.940 1.00 170.63 ? 1415 TYR   A CD2  1 
ATOM   391  C  CE1  . TYR   A 1 83   ? 175.824 174.588 224.599 1.00 173.56 ? 1415 TYR   A CE1  1 
ATOM   392  C  CE2  . TYR   A 1 83   ? 173.509 175.184 224.650 1.00 174.24 ? 1415 TYR   A CE2  1 
ATOM   393  C  CZ   . TYR   A 1 83   ? 174.714 175.127 223.984 1.00 178.08 ? 1415 TYR   A CZ   1 
ATOM   394  O  OH   . TYR   A 1 83   ? 174.811 175.611 222.699 1.00 179.00 ? 1415 TYR   A OH   1 
ATOM   395  N  N    . LEU   A 1 84   ? 175.385 171.583 230.240 1.00 179.53 ? 1416 LEU   A N    1 
ATOM   396  C  CA   . LEU   A 1 84   ? 175.344 171.312 231.677 1.00 177.11 ? 1416 LEU   A CA   1 
ATOM   397  C  C    . LEU   A 1 84   ? 176.588 171.941 232.296 1.00 174.43 ? 1416 LEU   A C    1 
ATOM   398  O  O    . LEU   A 1 84   ? 177.690 171.403 232.163 1.00 172.80 ? 1416 LEU   A O    1 
ATOM   399  C  CB   . LEU   A 1 84   ? 175.267 169.820 231.970 1.00 171.30 ? 1416 LEU   A CB   1 
ATOM   400  C  CG   . LEU   A 1 84   ? 175.166 169.458 233.454 1.00 170.67 ? 1416 LEU   A CG   1 
ATOM   401  C  CD1  . LEU   A 1 84   ? 173.894 170.017 234.058 1.00 176.36 ? 1416 LEU   A CD1  1 
ATOM   402  C  CD2  . LEU   A 1 84   ? 175.236 167.954 233.658 1.00 171.45 ? 1416 LEU   A CD2  1 
ATOM   403  N  N    . ALA   A 1 85   ? 176.403 173.070 232.970 1.00 174.58 ? 1417 ALA   A N    1 
ATOM   404  C  CA   . ALA   A 1 85   ? 177.534 173.797 233.525 1.00 173.64 ? 1417 ALA   A CA   1 
ATOM   405  C  C    . ALA   A 1 85   ? 178.068 173.102 234.770 1.00 174.78 ? 1417 ALA   A C    1 
ATOM   406  O  O    . ALA   A 1 85   ? 177.317 172.795 235.699 1.00 171.49 ? 1417 ALA   A O    1 
ATOM   407  C  CB   . ALA   A 1 85   ? 177.128 175.233 233.855 1.00 175.89 ? 1417 ALA   A CB   1 
ATOM   408  N  N    . VAL   A 1 86   ? 179.380 172.883 234.795 1.00 174.24 ? 1418 VAL   A N    1 
ATOM   409  C  CA   . VAL   A 1 86   ? 180.054 172.188 235.884 1.00 171.41 ? 1418 VAL   A CA   1 
ATOM   410  C  C    . VAL   A 1 86   ? 181.067 173.135 236.505 1.00 168.22 ? 1418 VAL   A C    1 
ATOM   411  O  O    . VAL   A 1 86   ? 181.856 173.762 235.791 1.00 161.72 ? 1418 VAL   A O    1 
ATOM   412  C  CB   . VAL   A 1 86   ? 180.753 170.902 235.405 1.00 174.58 ? 1418 VAL   A CB   1 
ATOM   413  C  CG1  . VAL   A 1 86   ? 181.537 170.267 236.545 1.00 169.44 ? 1418 VAL   A CG1  1 
ATOM   414  C  CG2  . VAL   A 1 86   ? 179.735 169.922 234.856 1.00 179.50 ? 1418 VAL   A CG2  1 
ATOM   415  N  N    . TYR   A 1 87   ? 181.046 173.235 237.831 1.00 173.64 ? 1419 TYR   A N    1 
ATOM   416  C  CA   . TYR   A 1 87   ? 181.943 174.131 238.541 1.00 171.42 ? 1419 TYR   A CA   1 
ATOM   417  C  C    . TYR   A 1 87   ? 182.106 173.658 239.976 1.00 169.27 ? 1419 TYR   A C    1 
ATOM   418  O  O    . TYR   A 1 87   ? 181.213 173.023 240.540 1.00 171.75 ? 1419 TYR   A O    1 
ATOM   419  C  CB   . TYR   A 1 87   ? 181.421 175.569 238.482 1.00 168.55 ? 1419 TYR   A CB   1 
ATOM   420  C  CG   . TYR   A 1 87   ? 179.985 175.750 238.938 1.00 167.96 ? 1419 TYR   A CG   1 
ATOM   421  C  CD1  . TYR   A 1 87   ? 179.628 175.622 240.274 1.00 167.00 ? 1419 TYR   A CD1  1 
ATOM   422  C  CD2  . TYR   A 1 87   ? 178.986 176.042 238.024 1.00 165.39 ? 1419 TYR   A CD2  1 
ATOM   423  C  CE1  . TYR   A 1 87   ? 178.326 175.790 240.680 1.00 167.07 ? 1419 TYR   A CE1  1 
ATOM   424  C  CE2  . TYR   A 1 87   ? 177.684 176.209 238.423 1.00 169.30 ? 1419 TYR   A CE2  1 
ATOM   425  C  CZ   . TYR   A 1 87   ? 177.361 176.084 239.751 1.00 171.49 ? 1419 TYR   A CZ   1 
ATOM   426  O  OH   . TYR   A 1 87   ? 176.061 176.252 240.155 1.00 174.04 ? 1419 TYR   A OH   1 
ATOM   427  N  N    . ASP   A 1 88   ? 183.256 173.974 240.559 1.00 163.05 ? 1420 ASP   A N    1 
ATOM   428  C  CA   . ASP   A 1 88   ? 183.547 173.637 241.943 1.00 162.97 ? 1420 ASP   A CA   1 
ATOM   429  C  C    . ASP   A 1 88   ? 183.240 174.818 242.850 1.00 167.65 ? 1420 ASP   A C    1 
ATOM   430  O  O    . ASP   A 1 88   ? 183.267 175.973 242.416 1.00 173.51 ? 1420 ASP   A O    1 
ATOM   431  C  CB   . ASP   A 1 88   ? 185.006 173.218 242.117 1.00 162.10 ? 1420 ASP   A CB   1 
ATOM   432  C  CG   . ASP   A 1 88   ? 185.185 172.183 243.206 1.00 161.74 ? 1420 ASP   A CG   1 
ATOM   433  O  OD1  . ASP   A 1 88   ? 186.233 171.503 243.229 1.00 159.11 ? 1420 ASP   A OD1  1 
ATOM   434  O  OD2  . ASP   A 1 88   ? 184.274 172.053 244.050 1.00 161.38 ? 1420 ASP   A OD2  1 
ATOM   435  N  N    . LEU   A 1 89   ? 182.937 174.514 244.112 1.00 167.74 ? 1421 LEU   A N    1 
ATOM   436  C  CA   . LEU   A 1 89   ? 182.668 175.531 245.114 1.00 170.59 ? 1421 LEU   A CA   1 
ATOM   437  C  C    . LEU   A 1 89   ? 183.671 175.533 246.256 1.00 172.49 ? 1421 LEU   A C    1 
ATOM   438  O  O    . LEU   A 1 89   ? 183.867 176.580 246.880 1.00 179.40 ? 1421 LEU   A O    1 
ATOM   439  C  CB   . LEU   A 1 89   ? 181.261 175.348 245.708 1.00 171.30 ? 1421 LEU   A CB   1 
ATOM   440  C  CG   . LEU   A 1 89   ? 180.010 175.790 244.942 1.00 168.32 ? 1421 LEU   A CG   1 
ATOM   441  C  CD1  . LEU   A 1 89   ? 179.716 174.881 243.759 1.00 166.16 ? 1421 LEU   A CD1  1 
ATOM   442  C  CD2  . LEU   A 1 89   ? 178.817 175.844 245.881 1.00 166.26 ? 1421 LEU   A CD2  1 
ATOM   443  N  N    . SER   A 1 90   ? 184.316 174.398 246.534 1.00 168.13 ? 1422 SER   A N    1 
ATOM   444  C  CA   . SER   A 1 90   ? 185.104 174.257 247.753 1.00 170.96 ? 1422 SER   A CA   1 
ATOM   445  C  C    . SER   A 1 90   ? 186.307 175.191 247.794 1.00 176.46 ? 1422 SER   A C    1 
ATOM   446  O  O    . SER   A 1 90   ? 186.753 175.556 248.888 1.00 177.39 ? 1422 SER   A O    1 
ATOM   447  C  CB   . SER   A 1 90   ? 185.567 172.807 247.903 1.00 169.21 ? 1422 SER   A CB   1 
ATOM   448  O  OG   . SER   A 1 90   ? 184.531 171.995 248.424 1.00 170.32 ? 1422 SER   A OG   1 
ATOM   449  N  N    . LYS   A 1 91   ? 186.843 175.589 246.639 1.00 176.37 ? 1423 LYS   A N    1 
ATOM   450  C  CA   . LYS   A 1 91   ? 188.017 176.454 246.633 1.00 175.45 ? 1423 LYS   A CA   1 
ATOM   451  C  C    . LYS   A 1 91   ? 187.687 177.891 247.016 1.00 179.38 ? 1423 LYS   A C    1 
ATOM   452  O  O    . LYS   A 1 91   ? 188.591 178.637 247.406 1.00 178.27 ? 1423 LYS   A O    1 
ATOM   453  C  CB   . LYS   A 1 91   ? 188.691 176.428 245.261 1.00 172.99 ? 1423 LYS   A CB   1 
ATOM   454  C  CG   . LYS   A 1 91   ? 189.254 175.078 244.860 1.00 169.66 ? 1423 LYS   A CG   1 
ATOM   455  C  CD   . LYS   A 1 91   ? 189.955 175.179 243.521 1.00 161.27 ? 1423 LYS   A CD   1 
ATOM   456  C  CE   . LYS   A 1 91   ? 188.953 175.378 242.405 1.00 157.70 ? 1423 LYS   A CE   1 
ATOM   457  N  NZ   . LYS   A 1 91   ? 188.109 174.168 242.269 1.00 155.66 ? 1423 LYS   A NZ   1 
ATOM   458  N  N    . GLY   A 1 92   ? 186.423 178.295 246.914 1.00 182.66 ? 1424 GLY   A N    1 
ATOM   459  C  CA   . GLY   A 1 92   ? 186.030 179.653 247.239 1.00 180.92 ? 1424 GLY   A CA   1 
ATOM   460  C  C    . GLY   A 1 92   ? 184.969 180.205 246.309 1.00 181.95 ? 1424 GLY   A C    1 
ATOM   461  O  O    . GLY   A 1 92   ? 183.981 179.526 246.018 1.00 187.35 ? 1424 GLY   A O    1 
ATOM   462  N  N    . GLN   A 1 93   ? 185.163 181.435 245.830 1.00 181.42 ? 1425 GLN   A N    1 
ATOM   463  C  CA   . GLN   A 1 93   ? 184.202 182.077 244.942 1.00 180.68 ? 1425 GLN   A CA   1 
ATOM   464  C  C    . GLN   A 1 93   ? 184.808 182.616 243.655 1.00 180.74 ? 1425 GLN   A C    1 
ATOM   465  O  O    . GLN   A 1 93   ? 184.051 182.929 242.730 1.00 177.20 ? 1425 GLN   A O    1 
ATOM   466  C  CB   . GLN   A 1 93   ? 183.481 183.227 245.668 1.00 174.92 ? 1425 GLN   A CB   1 
ATOM   467  C  CG   . GLN   A 1 93   ? 182.226 182.828 246.457 1.00 169.22 ? 1425 GLN   A CG   1 
ATOM   468  C  CD   . GLN   A 1 93   ? 181.270 181.926 245.688 1.00 169.84 ? 1425 GLN   A CD   1 
ATOM   469  O  OE1  . GLN   A 1 93   ? 181.170 181.998 244.464 1.00 174.31 ? 1425 GLN   A OE1  1 
ATOM   470  N  NE2  . GLN   A 1 93   ? 180.559 181.072 246.413 1.00 168.38 ? 1425 GLN   A NE2  1 
ATOM   471  N  N    . ALA   A 1 94   ? 186.134 182.740 243.561 1.00 182.61 ? 1426 ALA   A N    1 
ATOM   472  C  CA   . ALA   A 1 94   ? 186.744 183.209 242.320 1.00 179.99 ? 1426 ALA   A CA   1 
ATOM   473  C  C    . ALA   A 1 94   ? 186.517 182.220 241.184 1.00 187.37 ? 1426 ALA   A C    1 
ATOM   474  O  O    . ALA   A 1 94   ? 186.295 182.624 240.036 1.00 186.15 ? 1426 ALA   A O    1 
ATOM   475  C  CB   . ALA   A 1 94   ? 188.237 183.456 242.527 1.00 177.28 ? 1426 ALA   A CB   1 
ATOM   476  N  N    . GLU   A 1 95   ? 186.577 180.920 241.482 1.00 191.07 ? 1427 GLU   A N    1 
ATOM   477  C  CA   . GLU   A 1 95   ? 186.349 179.906 240.458 1.00 188.41 ? 1427 GLU   A CA   1 
ATOM   478  C  C    . GLU   A 1 95   ? 184.886 179.838 240.037 1.00 185.85 ? 1427 GLU   A C    1 
ATOM   479  O  O    . GLU   A 1 95   ? 184.594 179.522 238.879 1.00 179.08 ? 1427 GLU   A O    1 
ATOM   480  C  CB   . GLU   A 1 95   ? 186.822 178.536 240.955 1.00 180.71 ? 1427 GLU   A CB   1 
ATOM   481  C  CG   . GLU   A 1 95   ? 185.983 177.944 242.079 1.00 175.66 ? 1427 GLU   A CG   1 
ATOM   482  C  CD   . GLU   A 1 95   ? 186.396 178.432 243.454 1.00 173.43 ? 1427 GLU   A CD   1 
ATOM   483  O  OE1  . GLU   A 1 95   ? 187.125 179.442 243.543 1.00 176.12 ? 1427 GLU   A OE1  1 
ATOM   484  O  OE2  . GLU   A 1 95   ? 185.975 177.809 244.450 1.00 173.86 ? 1427 GLU   A OE2  1 
ATOM   485  N  N    . VAL   A 1 96   ? 183.960 180.127 240.954 1.00 186.70 ? 1428 VAL   A N    1 
ATOM   486  C  CA   . VAL   A 1 96   ? 182.542 180.094 240.615 1.00 184.55 ? 1428 VAL   A CA   1 
ATOM   487  C  C    . VAL   A 1 96   ? 182.192 181.216 239.645 1.00 182.63 ? 1428 VAL   A C    1 
ATOM   488  O  O    . VAL   A 1 96   ? 181.390 181.022 238.724 1.00 177.17 ? 1428 VAL   A O    1 
ATOM   489  C  CB   . VAL   A 1 96   ? 181.695 180.159 241.900 1.00 179.49 ? 1428 VAL   A CB   1 
ATOM   490  C  CG1  . VAL   A 1 96   ? 180.235 180.402 241.572 1.00 174.44 ? 1428 VAL   A CG1  1 
ATOM   491  C  CG2  . VAL   A 1 96   ? 181.852 178.878 242.696 1.00 173.74 ? 1428 VAL   A CG2  1 
ATOM   492  N  N    . ASP   A 1 97   ? 182.779 182.393 239.821 1.00 180.83 ? 1429 ASP   A N    1 
ATOM   493  C  CA   . ASP   A 1 97   ? 182.540 183.517 238.917 1.00 181.71 ? 1429 ASP   A CA   1 
ATOM   494  C  C    . ASP   A 1 97   ? 183.529 183.486 237.751 1.00 180.74 ? 1429 ASP   A C    1 
ATOM   495  O  O    . ASP   A 1 97   ? 184.297 184.421 237.523 1.00 184.31 ? 1429 ASP   A O    1 
ATOM   496  C  CB   . ASP   A 1 97   ? 182.619 184.835 239.682 1.00 181.37 ? 1429 ASP   A CB   1 
ATOM   497  C  CG   . ASP   A 1 97   ? 181.376 185.106 240.501 1.00 177.16 ? 1429 ASP   A CG   1 
ATOM   498  O  OD1  . ASP   A 1 97   ? 180.389 184.360 240.339 1.00 179.32 ? 1429 ASP   A OD1  1 
ATOM   499  O  OD2  . ASP   A 1 97   ? 181.381 186.063 241.303 1.00 173.20 ? 1429 ASP   A OD2  1 
ATOM   500  N  N    . ALA   A 1 98   ? 183.501 182.383 236.999 1.00 175.07 ? 1430 ALA   A N    1 
ATOM   501  C  CA   . ALA   A 1 98   ? 184.444 182.212 235.899 1.00 175.57 ? 1430 ALA   A CA   1 
ATOM   502  C  C    . ALA   A 1 98   ? 183.831 181.778 234.576 1.00 174.61 ? 1430 ALA   A C    1 
ATOM   503  O  O    . ALA   A 1 98   ? 184.524 181.862 233.558 1.00 171.33 ? 1430 ALA   A O    1 
ATOM   504  C  CB   . ALA   A 1 98   ? 185.528 181.197 236.289 1.00 178.37 ? 1430 ALA   A CB   1 
ATOM   505  N  N    . MET   A 1 99   ? 182.576 181.333 234.534 1.00 176.41 ? 1431 MET   A N    1 
ATOM   506  C  CA   . MET   A 1 99   ? 181.962 180.885 233.290 1.00 170.09 ? 1431 MET   A CA   1 
ATOM   507  C  C    . MET   A 1 99   ? 181.305 182.009 232.505 1.00 162.57 ? 1431 MET   A C    1 
ATOM   508  O  O    . MET   A 1 99   ? 180.454 181.733 231.657 1.00 161.49 ? 1431 MET   A O    1 
ATOM   509  C  CB   . MET   A 1 99   ? 180.921 179.789 233.558 1.00 169.61 ? 1431 MET   A CB   1 
ATOM   510  C  CG   . MET   A 1 99   ? 181.494 178.460 234.023 1.00 173.33 ? 1431 MET   A CG   1 
ATOM   511  S  SD   . MET   A 1 99   ? 180.589 177.738 235.402 1.00 172.06 ? 1431 MET   A SD   1 
ATOM   512  C  CE   . MET   A 1 99   ? 181.315 178.632 236.767 1.00 168.22 ? 1431 MET   A CE   1 
ATOM   513  N  N    . LYS   A 1 100  ? 181.675 183.260 232.757 1.00 158.49 ? 1432 LYS   A N    1 
ATOM   514  C  CA   . LYS   A 1 100  ? 181.079 184.363 232.009 1.00 158.15 ? 1432 LYS   A CA   1 
ATOM   515  C  C    . LYS   A 1 100  ? 181.259 184.231 230.500 1.00 164.85 ? 1432 LYS   A C    1 
ATOM   516  O  O    . LYS   A 1 100  ? 180.259 184.380 229.778 1.00 164.47 ? 1432 LYS   A O    1 
ATOM   517  C  CB   . LYS   A 1 100  ? 181.644 185.697 232.517 1.00 156.41 ? 1432 LYS   A CB   1 
ATOM   518  N  N    . PRO   A 1 101  ? 182.452 183.952 229.958 1.00 168.08 ? 1433 PRO   A N    1 
ATOM   519  C  CA   . PRO   A 1 101  ? 182.525 183.706 228.509 1.00 166.45 ? 1433 PRO   A CA   1 
ATOM   520  C  C    . PRO   A 1 101  ? 181.842 182.417 228.098 1.00 170.46 ? 1433 PRO   A C    1 
ATOM   521  O  O    . PRO   A 1 101  ? 181.450 182.267 226.934 1.00 167.31 ? 1433 PRO   A O    1 
ATOM   522  C  CB   . PRO   A 1 101  ? 184.034 183.665 228.237 1.00 159.52 ? 1433 PRO   A CB   1 
ATOM   523  C  CG   . PRO   A 1 101  ? 184.629 183.223 229.518 1.00 164.26 ? 1433 PRO   A CG   1 
ATOM   524  C  CD   . PRO   A 1 101  ? 183.777 183.823 230.597 1.00 164.34 ? 1433 PRO   A CD   1 
ATOM   525  N  N    . TRP   A 1 102  ? 181.685 181.478 229.037 1.00 171.61 ? 1434 TRP   A N    1 
ATOM   526  C  CA   . TRP   A 1 102  ? 181.094 180.184 228.712 1.00 166.48 ? 1434 TRP   A CA   1 
ATOM   527  C  C    . TRP   A 1 102  ? 179.651 180.337 228.262 1.00 164.14 ? 1434 TRP   A C    1 
ATOM   528  O  O    . TRP   A 1 102  ? 179.225 179.719 227.279 1.00 160.09 ? 1434 TRP   A O    1 
ATOM   529  C  CB   . TRP   A 1 102  ? 181.161 179.258 229.925 1.00 164.61 ? 1434 TRP   A CB   1 
ATOM   530  C  CG   . TRP   A 1 102  ? 182.433 178.502 230.056 1.00 164.00 ? 1434 TRP   A CG   1 
ATOM   531  C  CD1  . TRP   A 1 102  ? 183.294 178.540 231.109 1.00 163.35 ? 1434 TRP   A CD1  1 
ATOM   532  C  CD2  . TRP   A 1 102  ? 183.005 177.606 229.100 1.00 162.83 ? 1434 TRP   A CD2  1 
ATOM   533  N  NE1  . TRP   A 1 102  ? 184.363 177.714 230.875 1.00 166.07 ? 1434 TRP   A NE1  1 
ATOM   534  C  CE2  . TRP   A 1 102  ? 184.209 177.129 229.647 1.00 166.88 ? 1434 TRP   A CE2  1 
ATOM   535  C  CE3  . TRP   A 1 102  ? 182.615 177.156 227.838 1.00 155.01 ? 1434 TRP   A CE3  1 
ATOM   536  C  CZ2  . TRP   A 1 102  ? 185.026 176.228 228.977 1.00 165.55 ? 1434 TRP   A CZ2  1 
ATOM   537  C  CZ3  . TRP   A 1 102  ? 183.428 176.261 227.174 1.00 152.42 ? 1434 TRP   A CZ3  1 
ATOM   538  C  CH2  . TRP   A 1 102  ? 184.618 175.806 227.744 1.00 159.80 ? 1434 TRP   A CH2  1 
ATOM   539  N  N    . LEU   A 1 103  ? 178.879 181.150 228.980 1.00 166.83 ? 1435 LEU   A N    1 
ATOM   540  C  CA   . LEU   A 1 103  ? 177.464 181.292 228.666 1.00 171.38 ? 1435 LEU   A CA   1 
ATOM   541  C  C    . LEU   A 1 103  ? 177.249 182.176 227.443 1.00 169.73 ? 1435 LEU   A C    1 
ATOM   542  O  O    . LEU   A 1 103  ? 176.305 181.959 226.675 1.00 172.76 ? 1435 LEU   A O    1 
ATOM   543  C  CB   . LEU   A 1 103  ? 176.713 181.844 229.879 1.00 171.54 ? 1435 LEU   A CB   1 
ATOM   544  C  CG   . LEU   A 1 103  ? 176.380 180.892 231.035 1.00 163.36 ? 1435 LEU   A CG   1 
ATOM   545  C  CD1  . LEU   A 1 103  ? 177.610 180.503 231.840 1.00 160.84 ? 1435 LEU   A CD1  1 
ATOM   546  C  CD2  . LEU   A 1 103  ? 175.314 181.482 231.945 1.00 162.58 ? 1435 LEU   A CD2  1 
ATOM   547  N  N    . PHE   A 1 104  ? 178.108 183.179 227.241 1.00 163.05 ? 1436 PHE   A N    1 
ATOM   548  C  CA   . PHE   A 1 104  ? 177.926 184.058 226.091 1.00 165.53 ? 1436 PHE   A CA   1 
ATOM   549  C  C    . PHE   A 1 104  ? 178.282 183.365 224.783 1.00 171.07 ? 1436 PHE   A C    1 
ATOM   550  O  O    . PHE   A 1 104  ? 177.805 183.773 223.719 1.00 172.94 ? 1436 PHE   A O    1 
ATOM   551  C  CB   . PHE   A 1 104  ? 178.734 185.342 226.262 1.00 161.86 ? 1436 PHE   A CB   1 
ATOM   552  C  CG   . PHE   A 1 104  ? 178.566 186.315 225.128 1.00 162.59 ? 1436 PHE   A CG   1 
ATOM   553  C  CD1  . PHE   A 1 104  ? 177.408 187.065 225.006 1.00 159.10 ? 1436 PHE   A CD1  1 
ATOM   554  C  CD2  . PHE   A 1 104  ? 179.574 186.492 224.194 1.00 159.27 ? 1436 PHE   A CD2  1 
ATOM   555  C  CE1  . PHE   A 1 104  ? 177.254 187.965 223.965 1.00 156.49 ? 1436 PHE   A CE1  1 
ATOM   556  C  CE2  . PHE   A 1 104  ? 179.427 187.389 223.154 1.00 148.62 ? 1436 PHE   A CE2  1 
ATOM   557  C  CZ   . PHE   A 1 104  ? 178.266 188.126 223.039 1.00 147.11 ? 1436 PHE   A CZ   1 
ATOM   558  N  N    . ASN   A 1 105  ? 179.107 182.318 224.834 1.00 172.26 ? 1437 ASN   A N    1 
ATOM   559  C  CA   . ASN   A 1 105  ? 179.415 181.569 223.622 1.00 173.27 ? 1437 ASN   A CA   1 
ATOM   560  C  C    . ASN   A 1 105  ? 178.205 180.809 223.098 1.00 175.42 ? 1437 ASN   A C    1 
ATOM   561  O  O    . ASN   A 1 105  ? 178.169 180.463 221.912 1.00 175.01 ? 1437 ASN   A O    1 
ATOM   562  C  CB   . ASN   A 1 105  ? 180.562 180.590 223.883 1.00 173.29 ? 1437 ASN   A CB   1 
ATOM   563  C  CG   . ASN   A 1 105  ? 181.893 181.289 224.095 1.00 168.75 ? 1437 ASN   A CG   1 
ATOM   564  O  OD1  . ASN   A 1 105  ? 182.223 182.246 223.395 1.00 163.38 ? 1437 ASN   A OD1  1 
ATOM   565  N  ND2  . ASN   A 1 105  ? 182.669 180.807 225.061 1.00 167.37 ? 1437 ASN   A ND2  1 
ATOM   566  N  N    . ILE   A 1 106  ? 177.218 180.544 223.956 1.00 177.17 ? 1438 ILE   A N    1 
ATOM   567  C  CA   . ILE   A 1 106  ? 176.068 179.734 223.562 1.00 176.38 ? 1438 ILE   A CA   1 
ATOM   568  C  C    . ILE   A 1 106  ? 175.247 180.448 222.496 1.00 178.62 ? 1438 ILE   A C    1 
ATOM   569  O  O    . ILE   A 1 106  ? 174.913 179.872 221.454 1.00 177.17 ? 1438 ILE   A O    1 
ATOM   570  C  CB   . ILE   A 1 106  ? 175.217 179.399 224.799 1.00 173.58 ? 1438 ILE   A CB   1 
ATOM   571  C  CG1  . ILE   A 1 106  ? 176.036 178.555 225.777 1.00 175.48 ? 1438 ILE   A CG1  1 
ATOM   572  C  CG2  . ILE   A 1 106  ? 173.940 178.685 224.392 1.00 174.37 ? 1438 ILE   A CG2  1 
ATOM   573  C  CD1  . ILE   A 1 106  ? 175.395 178.389 227.132 1.00 177.23 ? 1438 ILE   A CD1  1 
ATOM   574  N  N    . LYS   A 1 107  ? 174.914 181.716 222.738 1.00 178.99 ? 1439 LYS   A N    1 
ATOM   575  C  CA   . LYS   A 1 107  ? 174.180 182.504 221.759 1.00 176.27 ? 1439 LYS   A CA   1 
ATOM   576  C  C    . LYS   A 1 107  ? 175.048 182.942 220.588 1.00 175.27 ? 1439 LYS   A C    1 
ATOM   577  O  O    . LYS   A 1 107  ? 174.512 183.429 219.587 1.00 176.48 ? 1439 LYS   A O    1 
ATOM   578  C  CB   . LYS   A 1 107  ? 173.558 183.728 222.433 1.00 174.62 ? 1439 LYS   A CB   1 
ATOM   579  C  CG   . LYS   A 1 107  ? 174.572 184.691 223.013 1.00 170.17 ? 1439 LYS   A CG   1 
ATOM   580  C  CD   . LYS   A 1 107  ? 173.933 185.569 224.071 1.00 165.74 ? 1439 LYS   A CD   1 
ATOM   581  C  CE   . LYS   A 1 107  ? 173.593 184.758 225.304 1.00 166.30 ? 1439 LYS   A CE   1 
ATOM   582  N  NZ   . LYS   A 1 107  ? 174.764 183.994 225.790 1.00 166.14 ? 1439 LYS   A NZ   1 
ATOM   583  N  N    . ALA   A 1 108  ? 176.364 182.785 220.689 1.00 178.43 ? 1440 ALA   A N    1 
ATOM   584  C  CA   . ALA   A 1 108  ? 177.266 183.135 219.598 1.00 177.38 ? 1440 ALA   A CA   1 
ATOM   585  C  C    . ALA   A 1 108  ? 177.558 181.921 218.723 1.00 177.88 ? 1440 ALA   A C    1 
ATOM   586  O  O    . ALA   A 1 108  ? 176.708 181.047 218.554 1.00 174.62 ? 1440 ALA   A O    1 
ATOM   587  C  CB   . ALA   A 1 108  ? 178.558 183.719 220.144 1.00 171.32 ? 1440 ALA   A CB   1 
ATOM   588  N  N    . PRO   A 1 114  ? 169.296 175.609 226.164 1.00 158.29 ? 1446 PRO   A N    1 
ATOM   589  C  CA   . PRO   A 1 114  ? 169.045 175.044 227.492 1.00 161.40 ? 1446 PRO   A CA   1 
ATOM   590  C  C    . PRO   A 1 114  ? 170.327 174.869 228.298 1.00 165.47 ? 1446 PRO   A C    1 
ATOM   591  O  O    . PRO   A 1 114  ? 171.143 174.017 227.955 1.00 168.51 ? 1446 PRO   A O    1 
ATOM   592  C  CB   . PRO   A 1 114  ? 168.422 173.689 227.169 1.00 165.20 ? 1446 PRO   A CB   1 
ATOM   593  C  CG   . PRO   A 1 114  ? 167.671 173.933 225.904 1.00 162.39 ? 1446 PRO   A CG   1 
ATOM   594  C  CD   . PRO   A 1 114  ? 168.445 174.984 225.135 1.00 156.23 ? 1446 PRO   A CD   1 
ATOM   595  N  N    . VAL   A 1 115  ? 170.504 175.655 229.356 1.00 168.93 ? 1447 VAL   A N    1 
ATOM   596  C  CA   . VAL   A 1 115  ? 171.698 175.582 230.189 1.00 174.25 ? 1447 VAL   A CA   1 
ATOM   597  C  C    . VAL   A 1 115  ? 171.293 175.231 231.614 1.00 173.86 ? 1447 VAL   A C    1 
ATOM   598  O  O    . VAL   A 1 115  ? 170.331 175.789 232.152 1.00 173.19 ? 1447 VAL   A O    1 
ATOM   599  C  CB   . VAL   A 1 115  ? 172.515 176.890 230.147 1.00 175.33 ? 1447 VAL   A CB   1 
ATOM   600  C  CG1  . VAL   A 1 115  ? 171.740 178.048 230.738 1.00 177.39 ? 1447 VAL   A CG1  1 
ATOM   601  C  CG2  . VAL   A 1 115  ? 173.827 176.710 230.887 1.00 169.68 ? 1447 VAL   A CG2  1 
ATOM   602  N  N    . ILE   A 1 116  ? 172.009 174.281 232.208 1.00 175.34 ? 1448 ILE   A N    1 
ATOM   603  C  CA   . ILE   A 1 116  ? 171.803 173.868 233.590 1.00 179.62 ? 1448 ILE   A CA   1 
ATOM   604  C  C    . ILE   A 1 116  ? 173.158 173.871 234.283 1.00 182.44 ? 1448 ILE   A C    1 
ATOM   605  O  O    . ILE   A 1 116  ? 174.148 173.380 233.730 1.00 180.32 ? 1448 ILE   A O    1 
ATOM   606  C  CB   . ILE   A 1 116  ? 171.144 172.475 233.695 1.00 184.01 ? 1448 ILE   A CB   1 
ATOM   607  C  CG1  . ILE   A 1 116  ? 169.750 172.471 233.067 1.00 179.94 ? 1448 ILE   A CG1  1 
ATOM   608  C  CG2  . ILE   A 1 116  ? 171.043 172.040 235.152 1.00 189.42 ? 1448 ILE   A CG2  1 
ATOM   609  C  CD1  . ILE   A 1 116  ? 169.728 172.142 231.587 1.00 181.46 ? 1448 ILE   A CD1  1 
ATOM   610  N  N    . LEU   A 1 117  ? 173.205 174.428 235.489 1.00 186.29 ? 1449 LEU   A N    1 
ATOM   611  C  CA   . LEU   A 1 117  ? 174.448 174.573 236.237 1.00 184.40 ? 1449 LEU   A CA   1 
ATOM   612  C  C    . LEU   A 1 117  ? 174.470 173.561 237.372 1.00 180.94 ? 1449 LEU   A C    1 
ATOM   613  O  O    . LEU   A 1 117  ? 173.515 173.477 238.153 1.00 179.65 ? 1449 LEU   A O    1 
ATOM   614  C  CB   . LEU   A 1 117  ? 174.594 175.995 236.779 1.00 184.48 ? 1449 LEU   A CB   1 
ATOM   615  N  N    . VAL   A 1 118  ? 175.555 172.796 237.462 1.00 178.40 ? 1450 VAL   A N    1 
ATOM   616  C  CA   . VAL   A 1 118  ? 175.732 171.807 238.519 1.00 181.91 ? 1450 VAL   A CA   1 
ATOM   617  C  C    . VAL   A 1 118  ? 177.061 172.066 239.214 1.00 179.16 ? 1450 VAL   A C    1 
ATOM   618  O  O    . VAL   A 1 118  ? 178.063 172.380 238.563 1.00 176.88 ? 1450 VAL   A O    1 
ATOM   619  C  CB   . VAL   A 1 118  ? 175.656 170.361 237.982 1.00 180.50 ? 1450 VAL   A CB   1 
ATOM   620  C  CG1  . VAL   A 1 118  ? 176.798 170.061 237.028 1.00 169.37 ? 1450 VAL   A CG1  1 
ATOM   621  C  CG2  . VAL   A 1 118  ? 175.658 169.368 239.134 1.00 184.77 ? 1450 VAL   A CG2  1 
ATOM   622  N  N    . GLY   A 1 119  ? 177.057 171.979 240.539 1.00 178.18 ? 1451 GLY   A N    1 
ATOM   623  C  CA   . GLY   A 1 119  ? 178.286 172.048 241.293 1.00 173.78 ? 1451 GLY   A CA   1 
ATOM   624  C  C    . GLY   A 1 119  ? 178.981 170.704 241.331 1.00 176.03 ? 1451 GLY   A C    1 
ATOM   625  O  O    . GLY   A 1 119  ? 178.511 169.706 240.789 1.00 179.80 ? 1451 GLY   A O    1 
ATOM   626  N  N    . THR   A 1 120  ? 180.143 170.690 241.977 1.00 178.57 ? 1452 THR   A N    1 
ATOM   627  C  CA   . THR   A 1 120  ? 180.914 169.466 242.163 1.00 181.93 ? 1452 THR   A CA   1 
ATOM   628  C  C    . THR   A 1 120  ? 180.562 168.761 243.466 1.00 188.79 ? 1452 THR   A C    1 
ATOM   629  O  O    . THR   A 1 120  ? 179.484 168.977 244.030 1.00 189.47 ? 1452 THR   A O    1 
ATOM   630  C  CB   . THR   A 1 120  ? 182.414 169.745 242.120 1.00 174.96 ? 1452 THR   A CB   1 
ATOM   631  O  OG1  . THR   A 1 120  ? 182.758 170.644 243.180 1.00 177.47 ? 1452 THR   A OG1  1 
ATOM   632  C  CG2  . THR   A 1 120  ? 182.811 170.329 240.776 1.00 165.41 ? 1452 THR   A CG2  1 
ATOM   633  N  N    . HIS   A 1 121  ? 181.477 167.898 243.921 1.00 189.55 ? 1453 HIS   A N    1 
ATOM   634  C  CA   . HIS   A 1 121  ? 181.221 166.987 245.034 1.00 189.15 ? 1453 HIS   A CA   1 
ATOM   635  C  C    . HIS   A 1 121  ? 180.618 167.699 246.240 1.00 191.74 ? 1453 HIS   A C    1 
ATOM   636  O  O    . HIS   A 1 121  ? 179.662 167.201 246.846 1.00 197.13 ? 1453 HIS   A O    1 
ATOM   637  C  CB   . HIS   A 1 121  ? 182.528 166.302 245.433 1.00 187.28 ? 1453 HIS   A CB   1 
ATOM   638  C  CG   . HIS   A 1 121  ? 183.425 165.995 244.274 1.00 187.62 ? 1453 HIS   A CG   1 
ATOM   639  N  ND1  . HIS   A 1 121  ? 184.673 166.563 244.129 1.00 182.53 ? 1453 HIS   A ND1  1 
ATOM   640  C  CD2  . HIS   A 1 121  ? 183.251 165.192 243.198 1.00 186.53 ? 1453 HIS   A CD2  1 
ATOM   641  C  CE1  . HIS   A 1 121  ? 185.231 166.118 243.018 1.00 178.24 ? 1453 HIS   A CE1  1 
ATOM   642  N  NE2  . HIS   A 1 121  ? 184.390 165.284 242.435 1.00 180.37 ? 1453 HIS   A NE2  1 
ATOM   643  N  N    . LEU   A 1 122  ? 181.180 168.848 246.619 1.00 189.93 ? 1454 LEU   A N    1 
ATOM   644  C  CA   . LEU   A 1 122  ? 180.771 169.673 247.757 1.00 190.33 ? 1454 LEU   A CA   1 
ATOM   645  C  C    . LEU   A 1 122  ? 181.045 169.011 249.102 1.00 193.94 ? 1454 LEU   A C    1 
ATOM   646  O  O    . LEU   A 1 122  ? 180.827 169.646 250.142 1.00 187.29 ? 1454 LEU   A O    1 
ATOM   647  C  CB   . LEU   A 1 122  ? 179.286 170.063 247.706 1.00 185.69 ? 1454 LEU   A CB   1 
ATOM   648  C  CG   . LEU   A 1 122  ? 178.832 171.036 246.621 1.00 178.86 ? 1454 LEU   A CG   1 
ATOM   649  C  CD1  . LEU   A 1 122  ? 177.320 171.156 246.630 1.00 183.96 ? 1454 LEU   A CD1  1 
ATOM   650  C  CD2  . LEU   A 1 122  ? 179.476 172.389 246.836 1.00 177.71 ? 1454 LEU   A CD2  1 
ATOM   651  N  N    . ASP   A 1 123  ? 181.516 167.765 249.124 1.00 197.77 ? 1455 ASP   A N    1 
ATOM   652  C  CA   . ASP   A 1 123  ? 181.790 167.069 250.372 1.00 194.66 ? 1455 ASP   A CA   1 
ATOM   653  C  C    . ASP   A 1 123  ? 183.174 167.365 250.931 1.00 193.26 ? 1455 ASP   A C    1 
ATOM   654  O  O    . ASP   A 1 123  ? 183.475 166.951 252.056 1.00 192.38 ? 1455 ASP   A O    1 
ATOM   655  C  CB   . ASP   A 1 123  ? 181.617 165.557 250.180 1.00 192.78 ? 1455 ASP   A CB   1 
ATOM   656  C  CG   . ASP   A 1 123  ? 182.589 164.975 249.164 1.00 189.57 ? 1455 ASP   A CG   1 
ATOM   657  O  OD1  . ASP   A 1 123  ? 183.376 165.738 248.565 1.00 190.12 ? 1455 ASP   A OD1  1 
ATOM   658  O  OD2  . ASP   A 1 123  ? 182.565 163.743 248.963 1.00 183.52 ? 1455 ASP   A OD2  1 
ATOM   659  N  N    . VAL   A 1 124  ? 184.018 168.060 250.176 1.00 193.60 ? 1456 VAL   A N    1 
ATOM   660  C  CA   . VAL   A 1 124  ? 185.361 168.386 250.630 1.00 186.94 ? 1456 VAL   A CA   1 
ATOM   661  C  C    . VAL   A 1 124  ? 185.649 169.863 250.390 1.00 182.35 ? 1456 VAL   A C    1 
ATOM   662  O  O    . VAL   A 1 124  ? 184.759 170.705 250.510 1.00 179.42 ? 1456 VAL   A O    1 
ATOM   663  C  CB   . VAL   A 1 124  ? 186.411 167.505 249.935 1.00 186.87 ? 1456 VAL   A CB   1 
ATOM   664  C  CG1  . VAL   A 1 124  ? 186.377 166.092 250.502 1.00 186.39 ? 1456 VAL   A CG1  1 
ATOM   665  C  CG2  . VAL   A 1 124  ? 186.177 167.488 248.433 1.00 184.88 ? 1456 VAL   A CG2  1 
ATOM   666  N  N    . GLN   A 1 129  ? 176.714 175.937 255.014 1.00 173.48 ? 1461 GLN   A N    1 
ATOM   667  C  CA   . GLN   A 1 129  ? 178.089 175.746 254.570 1.00 172.52 ? 1461 GLN   A CA   1 
ATOM   668  C  C    . GLN   A 1 129  ? 178.191 175.838 253.051 1.00 178.42 ? 1461 GLN   A C    1 
ATOM   669  O  O    . GLN   A 1 129  ? 178.359 176.925 252.497 1.00 173.65 ? 1461 GLN   A O    1 
ATOM   670  C  CB   . GLN   A 1 129  ? 178.627 174.398 255.054 1.00 164.38 ? 1461 GLN   A CB   1 
ATOM   671  N  N    . ARG   A 1 130  ? 178.096 174.685 252.385 1.00 182.28 ? 1462 ARG   A N    1 
ATOM   672  C  CA   . ARG   A 1 130  ? 178.159 174.660 250.927 1.00 180.29 ? 1462 ARG   A CA   1 
ATOM   673  C  C    . ARG   A 1 130  ? 176.986 175.417 250.315 1.00 179.07 ? 1462 ARG   A C    1 
ATOM   674  O  O    . ARG   A 1 130  ? 177.154 176.170 249.348 1.00 175.11 ? 1462 ARG   A O    1 
ATOM   675  C  CB   . ARG   A 1 130  ? 178.191 173.215 250.429 1.00 173.23 ? 1462 ARG   A CB   1 
ATOM   676  N  N    . LYS   A 1 131  ? 175.785 175.226 250.867 1.00 180.48 ? 1463 LYS   A N    1 
ATOM   677  C  CA   . LYS   A 1 131  ? 174.626 175.974 250.391 1.00 177.70 ? 1463 LYS   A CA   1 
ATOM   678  C  C    . LYS   A 1 131  ? 174.796 177.467 250.642 1.00 177.53 ? 1463 LYS   A C    1 
ATOM   679  O  O    . LYS   A 1 131  ? 174.432 178.293 249.796 1.00 175.05 ? 1463 LYS   A O    1 
ATOM   680  C  CB   . LYS   A 1 131  ? 173.355 175.458 251.065 1.00 172.43 ? 1463 LYS   A CB   1 
ATOM   681  N  N    . ALA   A 1 132  ? 175.346 177.831 251.802 1.00 177.54 ? 1464 ALA   A N    1 
ATOM   682  C  CA   . ALA   A 1 132  ? 175.650 179.232 252.069 1.00 173.86 ? 1464 ALA   A CA   1 
ATOM   683  C  C    . ALA   A 1 132  ? 176.682 179.763 251.083 1.00 177.09 ? 1464 ALA   A C    1 
ATOM   684  O  O    . ALA   A 1 132  ? 176.581 180.905 250.619 1.00 176.19 ? 1464 ALA   A O    1 
ATOM   685  C  CB   . ALA   A 1 132  ? 176.138 179.400 253.507 1.00 166.96 ? 1464 ALA   A CB   1 
ATOM   686  N  N    . CYS   A 1 133  ? 177.688 178.948 250.756 1.00 178.30 ? 1465 CYS   A N    1 
ATOM   687  C  CA   . CYS   A 1 133  ? 178.652 179.339 249.733 1.00 176.80 ? 1465 CYS   A CA   1 
ATOM   688  C  C    . CYS   A 1 133  ? 177.975 179.522 248.383 1.00 172.86 ? 1465 CYS   A C    1 
ATOM   689  O  O    . CYS   A 1 133  ? 178.288 180.466 247.648 1.00 172.96 ? 1465 CYS   A O    1 
ATOM   690  C  CB   . CYS   A 1 133  ? 179.765 178.297 249.635 1.00 173.04 ? 1465 CYS   A CB   1 
ATOM   691  N  N    . MET   A 1 134  ? 177.045 178.630 248.038 1.00 168.43 ? 1466 MET   A N    1 
ATOM   692  C  CA   . MET   A 1 134  ? 176.321 178.768 246.780 1.00 164.81 ? 1466 MET   A CA   1 
ATOM   693  C  C    . MET   A 1 134  ? 175.317 179.911 246.841 1.00 163.64 ? 1466 MET   A C    1 
ATOM   694  O  O    . MET   A 1 134  ? 174.892 180.428 245.802 1.00 163.05 ? 1466 MET   A O    1 
ATOM   695  C  CB   . MET   A 1 134  ? 175.615 177.458 246.433 1.00 162.59 ? 1466 MET   A CB   1 
ATOM   696  N  N    . SER   A 1 135  ? 174.926 180.318 248.052 1.00 164.44 ? 1467 SER   A N    1 
ATOM   697  C  CA   . SER   A 1 135  ? 173.886 181.333 248.192 1.00 165.91 ? 1467 SER   A CA   1 
ATOM   698  C  C    . SER   A 1 135  ? 174.296 182.641 247.529 1.00 169.98 ? 1467 SER   A C    1 
ATOM   699  O  O    . SER   A 1 135  ? 173.503 183.253 246.805 1.00 170.68 ? 1467 SER   A O    1 
ATOM   700  C  CB   . SER   A 1 135  ? 173.568 181.560 249.669 1.00 161.70 ? 1467 SER   A CB   1 
ATOM   701  O  OG   . SER   A 1 135  ? 174.546 182.384 250.276 1.00 159.55 ? 1467 SER   A OG   1 
ATOM   702  N  N    . LYS   A 1 136  ? 175.532 183.084 247.761 1.00 170.96 ? 1468 LYS   A N    1 
ATOM   703  C  CA   . LYS   A 1 136  ? 176.034 184.247 247.038 1.00 164.66 ? 1468 LYS   A CA   1 
ATOM   704  C  C    . LYS   A 1 136  ? 176.161 183.943 245.552 1.00 163.14 ? 1468 LYS   A C    1 
ATOM   705  O  O    . LYS   A 1 136  ? 175.920 184.813 244.708 1.00 164.07 ? 1468 LYS   A O    1 
ATOM   706  C  CB   . LYS   A 1 136  ? 177.377 184.691 247.617 1.00 156.17 ? 1468 LYS   A CB   1 
ATOM   707  N  N    . ILE   A 1 137  ? 176.543 182.711 245.215 1.00 165.28 ? 1469 ILE   A N    1 
ATOM   708  C  CA   . ILE   A 1 137  ? 176.682 182.334 243.814 1.00 165.83 ? 1469 ILE   A CA   1 
ATOM   709  C  C    . ILE   A 1 137  ? 175.324 182.305 243.127 1.00 170.11 ? 1469 ILE   A C    1 
ATOM   710  O  O    . ILE   A 1 137  ? 175.156 182.860 242.035 1.00 170.83 ? 1469 ILE   A O    1 
ATOM   711  C  CB   . ILE   A 1 137  ? 177.399 180.977 243.700 1.00 159.00 ? 1469 ILE   A CB   1 
ATOM   712  N  N    . THR   A 1 138  ? 174.335 181.662 243.753 1.00 168.84 ? 1470 THR   A N    1 
ATOM   713  C  CA   . THR   A 1 138  ? 173.017 181.535 243.135 1.00 170.06 ? 1470 THR   A CA   1 
ATOM   714  C  C    . THR   A 1 138  ? 172.343 182.892 242.986 1.00 166.88 ? 1470 THR   A C    1 
ATOM   715  O  O    . THR   A 1 138  ? 171.703 183.174 241.966 1.00 165.91 ? 1470 THR   A O    1 
ATOM   716  C  CB   . THR   A 1 138  ? 172.138 180.591 243.956 1.00 166.99 ? 1470 THR   A CB   1 
ATOM   717  N  N    . LYS   A 1 139  ? 172.469 183.745 244.004 1.00 162.97 ? 1471 LYS   A N    1 
ATOM   718  C  CA   . LYS   A 1 139  ? 171.870 185.073 243.938 1.00 164.95 ? 1471 LYS   A CA   1 
ATOM   719  C  C    . LYS   A 1 139  ? 172.485 185.896 242.814 1.00 172.81 ? 1471 LYS   A C    1 
ATOM   720  O  O    . LYS   A 1 139  ? 171.780 186.612 242.095 1.00 177.43 ? 1471 LYS   A O    1 
ATOM   721  C  CB   . LYS   A 1 139  ? 172.028 185.787 245.281 1.00 156.34 ? 1471 LYS   A CB   1 
ATOM   722  N  N    . GLU   A 1 140  ? 173.806 185.811 242.650 1.00 171.11 ? 1472 GLU   A N    1 
ATOM   723  C  CA   . GLU   A 1 140  ? 174.467 186.588 241.608 1.00 168.97 ? 1472 GLU   A CA   1 
ATOM   724  C  C    . GLU   A 1 140  ? 174.166 186.028 240.222 1.00 172.91 ? 1472 GLU   A C    1 
ATOM   725  O  O    . GLU   A 1 140  ? 173.857 186.781 239.291 1.00 175.79 ? 1472 GLU   A O    1 
ATOM   726  C  CB   . GLU   A 1 140  ? 175.974 186.624 241.860 1.00 162.38 ? 1472 GLU   A CB   1 
ATOM   727  N  N    . LEU   A 1 141  ? 174.249 184.705 240.066 1.00 168.20 ? 1473 LEU   A N    1 
ATOM   728  C  CA   . LEU   A 1 141  ? 174.136 184.109 238.738 1.00 167.95 ? 1473 LEU   A CA   1 
ATOM   729  C  C    . LEU   A 1 141  ? 172.716 184.196 238.194 1.00 172.62 ? 1473 LEU   A C    1 
ATOM   730  O  O    . LEU   A 1 141  ? 172.513 184.572 237.034 1.00 172.16 ? 1473 LEU   A O    1 
ATOM   731  C  CB   . LEU   A 1 141  ? 174.600 182.655 238.776 1.00 159.08 ? 1473 LEU   A CB   1 
ATOM   732  N  N    . LEU   A 1 142  ? 171.720 183.850 239.013 1.00 168.96 ? 1474 LEU   A N    1 
ATOM   733  C  CA   . LEU   A 1 142  ? 170.350 183.775 238.514 1.00 169.35 ? 1474 LEU   A CA   1 
ATOM   734  C  C    . LEU   A 1 142  ? 169.751 185.160 238.308 1.00 175.91 ? 1474 LEU   A C    1 
ATOM   735  O  O    . LEU   A 1 142  ? 168.800 185.320 237.535 1.00 176.36 ? 1474 LEU   A O    1 
ATOM   736  C  CB   . LEU   A 1 142  ? 169.486 182.956 239.473 1.00 159.64 ? 1474 LEU   A CB   1 
ATOM   737  N  N    . ASN   A 1 143  ? 170.290 186.169 238.988 1.00 179.33 ? 1475 ASN   A N    1 
ATOM   738  C  CA   . ASN   A 1 143  ? 169.704 187.502 238.941 1.00 179.76 ? 1475 ASN   A CA   1 
ATOM   739  C  C    . ASN   A 1 143  ? 169.847 188.119 237.556 1.00 182.76 ? 1475 ASN   A C    1 
ATOM   740  O  O    . ASN   A 1 143  ? 170.852 187.914 236.869 1.00 183.61 ? 1475 ASN   A O    1 
ATOM   741  C  CB   . ASN   A 1 143  ? 170.359 188.404 239.986 1.00 172.65 ? 1475 ASN   A CB   1 
ATOM   742  N  N    . LYS   A 1 144  ? 168.826 188.876 237.153 1.00 180.12 ? 1476 LYS   A N    1 
ATOM   743  C  CA   . LYS   A 1 144  ? 168.820 189.676 235.922 1.00 178.01 ? 1476 LYS   A CA   1 
ATOM   744  C  C    . LYS   A 1 144  ? 169.075 188.747 234.734 1.00 179.87 ? 1476 LYS   A C    1 
ATOM   745  O  O    . LYS   A 1 144  ? 168.570 187.615 234.730 1.00 179.03 ? 1476 LYS   A O    1 
ATOM   746  C  CB   . LYS   A 1 144  ? 169.806 190.825 236.079 1.00 177.10 ? 1476 LYS   A CB   1 
ATOM   747  N  N    . ARG   A 1 145  ? 169.838 189.168 233.730 1.00 178.34 ? 1477 ARG   A N    1 
ATOM   748  C  CA   . ARG   A 1 145  ? 170.031 188.395 232.510 1.00 175.80 ? 1477 ARG   A CA   1 
ATOM   749  C  C    . ARG   A 1 145  ? 171.272 188.922 231.801 1.00 174.03 ? 1477 ARG   A C    1 
ATOM   750  O  O    . ARG   A 1 145  ? 172.126 189.576 232.403 1.00 174.89 ? 1477 ARG   A O    1 
ATOM   751  C  CB   . ARG   A 1 145  ? 168.797 188.465 231.605 1.00 173.06 ? 1477 ARG   A CB   1 
ATOM   752  N  N    . GLY   A 1 146  ? 171.366 188.616 230.511 1.00 169.13 ? 1478 GLY   A N    1 
ATOM   753  C  CA   . GLY   A 1 146  ? 172.534 188.940 229.717 1.00 165.69 ? 1478 GLY   A CA   1 
ATOM   754  C  C    . GLY   A 1 146  ? 173.199 187.643 229.321 1.00 170.66 ? 1478 GLY   A C    1 
ATOM   755  O  O    . GLY   A 1 146  ? 173.684 187.471 228.199 1.00 168.37 ? 1478 GLY   A O    1 
ATOM   756  N  N    . PHE   A 1 147  ? 173.221 186.724 230.277 1.00 174.64 ? 1479 PHE   A N    1 
ATOM   757  C  CA   . PHE   A 1 147  ? 173.572 185.344 230.013 1.00 178.56 ? 1479 PHE   A CA   1 
ATOM   758  C  C    . PHE   A 1 147  ? 172.313 184.574 229.603 1.00 186.28 ? 1479 PHE   A C    1 
ATOM   759  O  O    . PHE   A 1 147  ? 171.193 185.022 229.863 1.00 189.72 ? 1479 PHE   A O    1 
ATOM   760  C  CB   . PHE   A 1 147  ? 174.201 184.715 231.256 1.00 171.97 ? 1479 PHE   A CB   1 
ATOM   761  C  CG   . PHE   A 1 147  ? 175.423 185.439 231.765 1.00 161.93 ? 1479 PHE   A CG   1 
ATOM   762  C  CD1  . PHE   A 1 147  ? 176.675 184.865 231.650 1.00 161.90 ? 1479 PHE   A CD1  1 
ATOM   763  C  CD2  . PHE   A 1 147  ? 175.316 186.671 232.391 1.00 153.77 ? 1479 PHE   A CD2  1 
ATOM   764  C  CE1  . PHE   A 1 147  ? 177.799 185.514 232.124 1.00 157.36 ? 1479 PHE   A CE1  1 
ATOM   765  C  CE2  . PHE   A 1 147  ? 176.436 187.326 232.866 1.00 148.26 ? 1479 PHE   A CE2  1 
ATOM   766  C  CZ   . PHE   A 1 147  ? 177.679 186.745 232.734 1.00 150.03 ? 1479 PHE   A CZ   1 
ATOM   767  N  N    . PRO   A 1 148  ? 172.464 183.423 228.945 1.00 188.92 ? 1480 PRO   A N    1 
ATOM   768  C  CA   . PRO   A 1 148  ? 171.286 182.610 228.626 1.00 193.59 ? 1480 PRO   A CA   1 
ATOM   769  C  C    . PRO   A 1 148  ? 170.579 182.129 229.885 1.00 193.50 ? 1480 PRO   A C    1 
ATOM   770  O  O    . PRO   A 1 148  ? 171.191 181.949 230.941 1.00 186.85 ? 1480 PRO   A O    1 
ATOM   771  C  CB   . PRO   A 1 148  ? 171.866 181.441 227.824 1.00 188.77 ? 1480 PRO   A CB   1 
ATOM   772  C  CG   . PRO   A 1 148  ? 173.270 181.340 228.274 1.00 184.89 ? 1480 PRO   A CG   1 
ATOM   773  C  CD   . PRO   A 1 148  ? 173.709 182.753 228.537 1.00 183.07 ? 1480 PRO   A CD   1 
ATOM   774  N  N    . ALA   A 1 149  ? 169.265 181.942 229.761 1.00 195.48 ? 1481 ALA   A N    1 
ATOM   775  C  CA   . ALA   A 1 149  ? 168.441 181.577 230.904 1.00 194.28 ? 1481 ALA   A CA   1 
ATOM   776  C  C    . ALA   A 1 149  ? 168.851 180.224 231.468 1.00 185.98 ? 1481 ALA   A C    1 
ATOM   777  O  O    . ALA   A 1 149  ? 168.811 179.205 230.775 1.00 181.38 ? 1481 ALA   A O    1 
ATOM   778  C  CB   . ALA   A 1 149  ? 166.967 181.545 230.498 1.00 192.61 ? 1481 ALA   A CB   1 
ATOM   779  N  N    . ILE   A 1 150  ? 169.214 180.218 232.746 1.00 180.08 ? 1482 ILE   A N    1 
ATOM   780  C  CA   . ILE   A 1 150  ? 169.562 178.980 233.430 1.00 172.94 ? 1482 ILE   A CA   1 
ATOM   781  C  C    . ILE   A 1 150  ? 168.300 178.146 233.599 1.00 173.66 ? 1482 ILE   A C    1 
ATOM   782  O  O    . ILE   A 1 150  ? 167.247 178.658 233.995 1.00 173.21 ? 1482 ILE   A O    1 
ATOM   783  C  CB   . ILE   A 1 150  ? 170.246 179.270 234.778 1.00 165.72 ? 1482 ILE   A CB   1 
ATOM   784  C  CG1  . ILE   A 1 150  ? 170.873 177.994 235.346 1.00 170.38 ? 1482 ILE   A CG1  1 
ATOM   785  C  CG2  . ILE   A 1 150  ? 169.290 179.921 235.772 1.00 158.33 ? 1482 ILE   A CG2  1 
ATOM   786  C  CD1  . ILE   A 1 150  ? 172.013 177.460 234.519 1.00 172.47 ? 1482 ILE   A CD1  1 
ATOM   787  N  N    . ARG   A 1 151  ? 168.385 176.868 233.240 1.00 175.02 ? 1483 ARG   A N    1 
ATOM   788  C  CA   . ARG   A 1 151  ? 167.220 176.007 233.390 1.00 180.21 ? 1483 ARG   A CA   1 
ATOM   789  C  C    . ARG   A 1 151  ? 167.064 175.526 234.825 1.00 182.76 ? 1483 ARG   A C    1 
ATOM   790  O  O    . ARG   A 1 151  ? 165.939 175.382 235.315 1.00 184.31 ? 1483 ARG   A O    1 
ATOM   791  C  CB   . ARG   A 1 151  ? 167.312 174.822 232.432 1.00 178.55 ? 1483 ARG   A CB   1 
ATOM   792  N  N    . ASP   A 1 152  ? 168.174 175.281 235.517 1.00 178.19 ? 1484 ASP   A N    1 
ATOM   793  C  CA   . ASP   A 1 152  ? 168.108 174.749 236.874 1.00 185.43 ? 1484 ASP   A CA   1 
ATOM   794  C  C    . ASP   A 1 152  ? 169.425 175.032 237.576 1.00 188.40 ? 1484 ASP   A C    1 
ATOM   795  O  O    . ASP   A 1 152  ? 170.486 174.973 236.947 1.00 186.19 ? 1484 ASP   A O    1 
ATOM   796  C  CB   . ASP   A 1 152  ? 167.816 173.248 236.852 1.00 188.35 ? 1484 ASP   A CB   1 
ATOM   797  C  CG   . ASP   A 1 152  ? 167.514 172.688 238.230 1.00 192.25 ? 1484 ASP   A CG   1 
ATOM   798  O  OD1  . ASP   A 1 152  ? 167.550 173.454 239.215 1.00 195.88 ? 1484 ASP   A OD1  1 
ATOM   799  O  OD2  . ASP   A 1 152  ? 167.240 171.474 238.326 1.00 191.48 ? 1484 ASP   A OD2  1 
ATOM   800  N  N    . TYR   A 1 153  ? 169.354 175.351 238.868 1.00 190.75 ? 1485 TYR   A N    1 
ATOM   801  C  CA   . TYR   A 1 153  ? 170.535 175.478 239.721 1.00 188.89 ? 1485 TYR   A CA   1 
ATOM   802  C  C    . TYR   A 1 153  ? 170.583 174.259 240.638 1.00 187.87 ? 1485 TYR   A C    1 
ATOM   803  O  O    . TYR   A 1 153  ? 169.883 174.202 241.652 1.00 180.88 ? 1485 TYR   A O    1 
ATOM   804  C  CB   . TYR   A 1 153  ? 170.489 176.781 240.511 1.00 182.59 ? 1485 TYR   A CB   1 
ATOM   805  N  N    . HIS   A 1 154  ? 171.417 173.282 240.285 1.00 187.54 ? 1486 HIS   A N    1 
ATOM   806  C  CA   . HIS   A 1 154  ? 171.453 171.989 240.956 1.00 193.59 ? 1486 HIS   A CA   1 
ATOM   807  C  C    . HIS   A 1 154  ? 172.874 171.720 241.442 1.00 195.35 ? 1486 HIS   A C    1 
ATOM   808  O  O    . HIS   A 1 154  ? 173.832 172.376 241.026 1.00 191.01 ? 1486 HIS   A O    1 
ATOM   809  C  CB   . HIS   A 1 154  ? 170.944 170.880 240.009 1.00 197.43 ? 1486 HIS   A CB   1 
ATOM   810  C  CG   . HIS   A 1 154  ? 171.312 169.486 240.422 1.00 203.22 ? 1486 HIS   A CG   1 
ATOM   811  N  ND1  . HIS   A 1 154  ? 170.457 168.672 241.135 1.00 203.42 ? 1486 HIS   A ND1  1 
ATOM   812  C  CD2  . HIS   A 1 154  ? 172.431 168.755 240.204 1.00 202.39 ? 1486 HIS   A CD2  1 
ATOM   813  C  CE1  . HIS   A 1 154  ? 171.037 167.505 241.349 1.00 203.71 ? 1486 HIS   A CE1  1 
ATOM   814  N  NE2  . HIS   A 1 154  ? 172.238 167.532 240.799 1.00 203.56 ? 1486 HIS   A NE2  1 
ATOM   815  N  N    . PHE   A 1 155  ? 173.003 170.745 242.343 1.00 197.28 ? 1487 PHE   A N    1 
ATOM   816  C  CA   . PHE   A 1 155  ? 174.289 170.353 242.899 1.00 194.79 ? 1487 PHE   A CA   1 
ATOM   817  C  C    . PHE   A 1 155  ? 174.331 168.837 243.034 1.00 197.95 ? 1487 PHE   A C    1 
ATOM   818  O  O    . PHE   A 1 155  ? 173.293 168.186 243.179 1.00 198.12 ? 1487 PHE   A O    1 
ATOM   819  C  CB   . PHE   A 1 155  ? 174.528 171.023 244.257 1.00 196.35 ? 1487 PHE   A CB   1 
ATOM   820  C  CG   . PHE   A 1 155  ? 173.540 170.616 245.316 1.00 200.11 ? 1487 PHE   A CG   1 
ATOM   821  C  CD1  . PHE   A 1 155  ? 172.359 171.321 245.486 1.00 198.76 ? 1487 PHE   A CD1  1 
ATOM   822  C  CD2  . PHE   A 1 155  ? 173.795 169.536 246.148 1.00 202.79 ? 1487 PHE   A CD2  1 
ATOM   823  C  CE1  . PHE   A 1 155  ? 171.447 170.951 246.458 1.00 201.97 ? 1487 PHE   A CE1  1 
ATOM   824  C  CE2  . PHE   A 1 155  ? 172.886 169.161 247.122 1.00 204.47 ? 1487 PHE   A CE2  1 
ATOM   825  C  CZ   . PHE   A 1 155  ? 171.711 169.871 247.277 1.00 206.00 ? 1487 PHE   A CZ   1 
ATOM   826  N  N    . VAL   A 1 156  ? 175.544 168.278 242.989 1.00 198.91 ? 1488 VAL   A N    1 
ATOM   827  C  CA   . VAL   A 1 156  ? 175.748 166.837 243.101 1.00 199.47 ? 1488 VAL   A CA   1 
ATOM   828  C  C    . VAL   A 1 156  ? 176.515 166.557 244.385 1.00 200.74 ? 1488 VAL   A C    1 
ATOM   829  O  O    . VAL   A 1 156  ? 177.278 167.397 244.877 1.00 198.42 ? 1488 VAL   A O    1 
ATOM   830  C  CB   . VAL   A 1 156  ? 176.487 166.271 241.866 1.00 191.63 ? 1488 VAL   A CB   1 
ATOM   831  C  CG1  . VAL   A 1 156  ? 177.900 166.817 241.785 1.00 186.92 ? 1488 VAL   A CG1  1 
ATOM   832  C  CG2  . VAL   A 1 156  ? 176.482 164.747 241.867 1.00 196.42 ? 1488 VAL   A CG2  1 
ATOM   833  N  N    . ASN   A 1 157  ? 176.306 165.366 244.942 1.00 203.95 ? 1489 ASN   A N    1 
ATOM   834  C  CA   . ASN   A 1 157  ? 176.886 164.972 246.225 1.00 203.58 ? 1489 ASN   A CA   1 
ATOM   835  C  C    . ASN   A 1 157  ? 177.871 163.826 245.995 1.00 207.13 ? 1489 ASN   A C    1 
ATOM   836  O  O    . ASN   A 1 157  ? 177.474 162.671 245.830 1.00 210.12 ? 1489 ASN   A O    1 
ATOM   837  C  CB   . ASN   A 1 157  ? 175.791 164.577 247.212 1.00 206.22 ? 1489 ASN   A CB   1 
ATOM   838  N  N    . ALA   A 1 158  ? 179.163 164.165 245.976 1.00 204.88 ? 1490 ALA   A N    1 
ATOM   839  C  CA   . ALA   A 1 158  ? 180.264 163.203 245.947 1.00 205.23 ? 1490 ALA   A CA   1 
ATOM   840  C  C    . ALA   A 1 158  ? 180.320 162.396 244.655 1.00 203.18 ? 1490 ALA   A C    1 
ATOM   841  O  O    . ALA   A 1 158  ? 179.396 162.440 243.836 1.00 201.52 ? 1490 ALA   A O    1 
ATOM   842  C  CB   . ALA   A 1 158  ? 180.184 162.256 247.149 1.00 206.51 ? 1490 ALA   A CB   1 
ATOM   843  N  N    . THR   A 1 159  ? 181.417 161.661 244.464 1.00 205.03 ? 1491 THR   A N    1 
ATOM   844  C  CA   . THR   A 1 159  ? 181.603 160.817 243.292 1.00 202.52 ? 1491 THR   A CA   1 
ATOM   845  C  C    . THR   A 1 159  ? 181.243 159.358 243.544 1.00 207.90 ? 1491 THR   A C    1 
ATOM   846  O  O    . THR   A 1 159  ? 180.810 158.672 242.610 1.00 204.43 ? 1491 THR   A O    1 
ATOM   847  C  CB   . THR   A 1 159  ? 183.059 160.907 242.806 1.00 192.51 ? 1491 THR   A CB   1 
ATOM   848  O  OG1  . THR   A 1 159  ? 183.368 162.264 242.470 1.00 190.10 ? 1491 THR   A OG1  1 
ATOM   849  C  CG2  . THR   A 1 159  ? 183.287 160.041 241.574 1.00 184.80 ? 1491 THR   A CG2  1 
ATOM   850  N  N    . GLU   A 1 160  ? 181.383 158.875 244.781 1.00 211.66 ? 1492 GLU   A N    1 
ATOM   851  C  CA   . GLU   A 1 160  ? 181.090 157.473 245.066 1.00 210.17 ? 1492 GLU   A CA   1 
ATOM   852  C  C    . GLU   A 1 160  ? 179.634 157.142 244.759 1.00 213.51 ? 1492 GLU   A C    1 
ATOM   853  O  O    . GLU   A 1 160  ? 179.341 156.166 244.057 1.00 216.00 ? 1492 GLU   A O    1 
ATOM   854  C  CB   . GLU   A 1 160  ? 181.422 157.155 246.524 1.00 204.79 ? 1492 GLU   A CB   1 
ATOM   855  N  N    . GLU   A 1 161  ? 178.708 157.950 245.268 1.00 214.34 ? 1493 GLU   A N    1 
ATOM   856  C  CA   . GLU   A 1 161  ? 177.296 157.783 244.961 1.00 215.01 ? 1493 GLU   A CA   1 
ATOM   857  C  C    . GLU   A 1 161  ? 176.572 159.073 245.316 1.00 213.12 ? 1493 GLU   A C    1 
ATOM   858  O  O    . GLU   A 1 161  ? 176.918 159.744 246.292 1.00 212.47 ? 1493 GLU   A O    1 
ATOM   859  C  CB   . GLU   A 1 161  ? 176.685 156.594 245.714 1.00 213.32 ? 1493 GLU   A CB   1 
ATOM   860  C  CG   . GLU   A 1 161  ? 175.219 156.339 245.396 1.00 208.28 ? 1493 GLU   A CG   1 
ATOM   861  C  CD   . GLU   A 1 161  ? 175.001 155.924 243.952 1.00 205.73 ? 1493 GLU   A CD   1 
ATOM   862  O  OE1  . GLU   A 1 161  ? 175.937 155.368 243.340 1.00 206.27 ? 1493 GLU   A OE1  1 
ATOM   863  O  OE2  . GLU   A 1 161  ? 173.894 156.161 243.426 1.00 203.31 ? 1493 GLU   A OE2  1 
ATOM   864  N  N    . SER   A 1 162  ? 175.564 159.408 244.515 1.00 213.64 ? 1494 SER   A N    1 
ATOM   865  C  CA   . SER   A 1 162  ? 174.819 160.642 244.710 1.00 215.92 ? 1494 SER   A CA   1 
ATOM   866  C  C    . SER   A 1 162  ? 173.335 160.375 244.528 1.00 220.52 ? 1494 SER   A C    1 
ATOM   867  O  O    . SER   A 1 162  ? 172.911 159.863 243.489 1.00 220.43 ? 1494 SER   A O    1 
ATOM   868  C  CB   . SER   A 1 162  ? 175.276 161.730 243.731 1.00 213.73 ? 1494 SER   A CB   1 
ATOM   869  O  OG   . SER   A 1 162  ? 174.333 162.786 243.670 1.00 214.46 ? 1494 SER   A OG   1 
ATOM   870  N  N    . ASP   A 1 163  ? 172.550 160.724 245.549 1.00 222.92 ? 1495 ASP   A N    1 
ATOM   871  C  CA   . ASP   A 1 163  ? 171.100 160.690 245.412 1.00 221.60 ? 1495 ASP   A CA   1 
ATOM   872  C  C    . ASP   A 1 163  ? 170.638 161.787 244.461 1.00 221.26 ? 1495 ASP   A C    1 
ATOM   873  O  O    . ASP   A 1 163  ? 169.729 161.572 243.651 1.00 220.32 ? 1495 ASP   A O    1 
ATOM   874  C  CB   . ASP   A 1 163  ? 170.456 160.815 246.803 1.00 214.90 ? 1495 ASP   A CB   1 
ATOM   875  C  CG   . ASP   A 1 163  ? 168.927 160.944 246.773 1.00 210.98 ? 1495 ASP   A CG   1 
ATOM   876  O  OD1  . ASP   A 1 163  ? 168.352 161.676 245.942 1.00 214.62 ? 1495 ASP   A OD1  1 
ATOM   877  O  OD2  . ASP   A 1 163  ? 168.285 160.283 247.616 1.00 203.19 ? 1495 ASP   A OD2  1 
ATOM   878  N  N    . ALA   A 1 164  ? 171.282 162.955 244.524 1.00 220.77 ? 1496 ALA   A N    1 
ATOM   879  C  CA   . ALA   A 1 164  ? 170.935 164.059 243.640 1.00 216.66 ? 1496 ALA   A CA   1 
ATOM   880  C  C    . ALA   A 1 164  ? 171.201 163.736 242.176 1.00 218.55 ? 1496 ALA   A C    1 
ATOM   881  O  O    . ALA   A 1 164  ? 170.681 164.434 241.299 1.00 218.14 ? 1496 ALA   A O    1 
ATOM   882  C  CB   . ALA   A 1 164  ? 171.702 165.319 244.044 1.00 208.77 ? 1496 ALA   A CB   1 
ATOM   883  N  N    . LEU   A 1 165  ? 172.002 162.705 241.893 1.00 217.93 ? 1497 LEU   A N    1 
ATOM   884  C  CA   . LEU   A 1 165  ? 172.194 162.279 240.511 1.00 215.80 ? 1497 LEU   A CA   1 
ATOM   885  C  C    . LEU   A 1 165  ? 170.871 161.875 239.879 1.00 217.84 ? 1497 LEU   A C    1 
ATOM   886  O  O    . LEU   A 1 165  ? 170.575 162.261 238.742 1.00 214.43 ? 1497 LEU   A O    1 
ATOM   887  C  CB   . LEU   A 1 165  ? 173.192 161.122 240.454 1.00 216.73 ? 1497 LEU   A CB   1 
ATOM   888  C  CG   . LEU   A 1 165  ? 173.682 160.623 239.091 1.00 211.29 ? 1497 LEU   A CG   1 
ATOM   889  C  CD1  . LEU   A 1 165  ? 175.048 160.012 239.261 1.00 208.81 ? 1497 LEU   A CD1  1 
ATOM   890  C  CD2  . LEU   A 1 165  ? 172.737 159.596 238.474 1.00 207.36 ? 1497 LEU   A CD2  1 
ATOM   891  N  N    . ALA   A 1 166  ? 170.060 161.097 240.602 1.00 220.61 ? 1498 ALA   A N    1 
ATOM   892  C  CA   . ALA   A 1 166  ? 168.731 160.763 240.105 1.00 220.25 ? 1498 ALA   A CA   1 
ATOM   893  C  C    . ALA   A 1 166  ? 167.887 162.018 239.936 1.00 220.49 ? 1498 ALA   A C    1 
ATOM   894  O  O    . ALA   A 1 166  ? 167.173 162.167 238.937 1.00 219.87 ? 1498 ALA   A O    1 
ATOM   895  C  CB   . ALA   A 1 166  ? 168.045 159.777 241.050 1.00 214.31 ? 1498 ALA   A CB   1 
ATOM   896  N  N    . LYS   A 1 167  ? 167.963 162.938 240.900 1.00 220.17 ? 1499 LYS   A N    1 
ATOM   897  C  CA   . LYS   A 1 167  ? 167.287 164.219 240.742 1.00 214.02 ? 1499 LYS   A CA   1 
ATOM   898  C  C    . LYS   A 1 167  ? 167.879 164.996 239.573 1.00 213.90 ? 1499 LYS   A C    1 
ATOM   899  O  O    . LYS   A 1 167  ? 167.147 165.628 238.805 1.00 211.65 ? 1499 LYS   A O    1 
ATOM   900  C  CB   . LYS   A 1 167  ? 167.370 165.020 242.041 1.00 207.20 ? 1499 LYS   A CB   1 
ATOM   901  C  CG   . LYS   A 1 167  ? 166.596 166.328 242.023 1.00 199.63 ? 1499 LYS   A CG   1 
ATOM   902  C  CD   . LYS   A 1 167  ? 167.268 167.389 242.881 1.00 194.79 ? 1499 LYS   A CD   1 
ATOM   903  C  CE   . LYS   A 1 167  ? 166.785 168.787 242.522 1.00 193.27 ? 1499 LYS   A CE   1 
ATOM   904  N  NZ   . LYS   A 1 167  ? 167.692 169.509 241.588 1.00 197.57 ? 1499 LYS   A NZ   1 
ATOM   905  N  N    . LEU   A 1 168  ? 169.205 164.948 239.414 1.00 215.10 ? 1500 LEU   A N    1 
ATOM   906  C  CA   . LEU   A 1 168  ? 169.834 165.550 238.241 1.00 213.21 ? 1500 LEU   A CA   1 
ATOM   907  C  C    . LEU   A 1 168  ? 169.422 164.843 236.958 1.00 215.75 ? 1500 LEU   A C    1 
ATOM   908  O  O    . LEU   A 1 168  ? 169.196 165.493 235.930 1.00 217.39 ? 1500 LEU   A O    1 
ATOM   909  C  CB   . LEU   A 1 168  ? 171.356 165.525 238.378 1.00 210.16 ? 1500 LEU   A CB   1 
ATOM   910  C  CG   . LEU   A 1 168  ? 172.101 166.177 237.208 1.00 203.61 ? 1500 LEU   A CG   1 
ATOM   911  C  CD1  . LEU   A 1 168  ? 171.766 167.652 237.087 1.00 196.17 ? 1500 LEU   A CD1  1 
ATOM   912  C  CD2  . LEU   A 1 168  ? 173.602 165.972 237.336 1.00 195.98 ? 1500 LEU   A CD2  1 
ATOM   913  N  N    . ARG   A 1 169  ? 169.327 163.513 236.995 1.00 215.21 ? 1501 ARG   A N    1 
ATOM   914  C  CA   . ARG   A 1 169  ? 169.129 162.755 235.765 1.00 214.50 ? 1501 ARG   A CA   1 
ATOM   915  C  C    . ARG   A 1 169  ? 167.812 163.121 235.094 1.00 215.41 ? 1501 ARG   A C    1 
ATOM   916  O  O    . ARG   A 1 169  ? 167.759 163.304 233.873 1.00 213.08 ? 1501 ARG   A O    1 
ATOM   917  C  CB   . ARG   A 1 169  ? 169.188 161.256 236.058 1.00 211.38 ? 1501 ARG   A CB   1 
ATOM   918  C  CG   . ARG   A 1 169  ? 169.580 160.411 234.862 1.00 204.94 ? 1501 ARG   A CG   1 
ATOM   919  C  CD   . ARG   A 1 169  ? 170.694 161.083 234.068 1.00 204.46 ? 1501 ARG   A CD   1 
ATOM   920  N  NE   . ARG   A 1 169  ? 171.964 161.082 234.786 1.00 206.22 ? 1501 ARG   A NE   1 
ATOM   921  C  CZ   . ARG   A 1 169  ? 172.877 160.125 234.696 1.00 200.77 ? 1501 ARG   A CZ   1 
ATOM   922  N  NH1  . ARG   A 1 169  ? 172.694 159.064 233.927 1.00 197.41 ? 1501 ARG   A NH1  1 
ATOM   923  N  NH2  . ARG   A 1 169  ? 174.003 160.234 235.395 1.00 196.70 ? 1501 ARG   A NH2  1 
ATOM   924  N  N    . LYS   A 1 170  ? 166.740 163.252 235.878 1.00 217.80 ? 1502 LYS   A N    1 
ATOM   925  C  CA   . LYS   A 1 170  ? 165.442 163.580 235.298 1.00 217.09 ? 1502 LYS   A CA   1 
ATOM   926  C  C    . LYS   A 1 170  ? 165.387 165.033 234.840 1.00 214.32 ? 1502 LYS   A C    1 
ATOM   927  O  O    . LYS   A 1 170  ? 164.590 165.384 233.962 1.00 213.32 ? 1502 LYS   A O    1 
ATOM   928  C  CB   . LYS   A 1 170  ? 164.329 163.270 236.300 1.00 215.97 ? 1502 LYS   A CB   1 
ATOM   929  C  CG   . LYS   A 1 170  ? 164.490 163.921 237.668 1.00 213.56 ? 1502 LYS   A CG   1 
ATOM   930  C  CD   . LYS   A 1 170  ? 163.776 165.260 237.753 1.00 210.96 ? 1502 LYS   A CD   1 
ATOM   931  C  CE   . LYS   A 1 170  ? 163.973 165.901 239.115 1.00 203.95 ? 1502 LYS   A CE   1 
ATOM   932  N  NZ   . LYS   A 1 170  ? 163.224 167.180 239.238 1.00 190.00 ? 1502 LYS   A NZ   1 
ATOM   933  N  N    . THR   A 1 171  ? 166.223 165.897 235.424 1.00 214.06 ? 1503 THR   A N    1 
ATOM   934  C  CA   . THR   A 1 171  ? 166.323 167.264 234.920 1.00 210.98 ? 1503 THR   A CA   1 
ATOM   935  C  C    . THR   A 1 171  ? 166.938 167.291 233.528 1.00 210.42 ? 1503 THR   A C    1 
ATOM   936  O  O    . THR   A 1 171  ? 166.595 168.148 232.708 1.00 208.28 ? 1503 THR   A O    1 
ATOM   937  C  CB   . THR   A 1 171  ? 167.130 168.142 235.879 1.00 208.53 ? 1503 THR   A CB   1 
ATOM   938  O  OG1  . THR   A 1 171  ? 168.461 167.627 236.007 1.00 210.38 ? 1503 THR   A OG1  1 
ATOM   939  C  CG2  . THR   A 1 171  ? 166.461 168.212 237.242 1.00 203.95 ? 1503 THR   A CG2  1 
ATOM   940  N  N    . ILE   A 1 172  ? 167.864 166.374 233.246 1.00 210.73 ? 1504 ILE   A N    1 
ATOM   941  C  CA   . ILE   A 1 172  ? 168.376 166.252 231.884 1.00 209.61 ? 1504 ILE   A CA   1 
ATOM   942  C  C    . ILE   A 1 172  ? 167.288 165.724 230.958 1.00 212.80 ? 1504 ILE   A C    1 
ATOM   943  O  O    . ILE   A 1 172  ? 167.131 166.197 229.827 1.00 211.20 ? 1504 ILE   A O    1 
ATOM   944  C  CB   . ILE   A 1 172  ? 169.626 165.353 231.856 1.00 205.25 ? 1504 ILE   A CB   1 
ATOM   945  C  CG1  . ILE   A 1 172  ? 170.758 165.973 232.675 1.00 200.67 ? 1504 ILE   A CG1  1 
ATOM   946  C  CG2  . ILE   A 1 172  ? 170.081 165.113 230.424 1.00 203.63 ? 1504 ILE   A CG2  1 
ATOM   947  C  CD1  . ILE   A 1 172  ? 171.925 165.035 232.906 1.00 193.13 ? 1504 ILE   A CD1  1 
ATOM   948  N  N    . ILE   A 1 173  ? 166.509 164.748 231.433 1.00 214.35 ? 1505 ILE   A N    1 
ATOM   949  C  CA   . ILE   A 1 173  ? 165.563 164.050 230.566 1.00 212.90 ? 1505 ILE   A CA   1 
ATOM   950  C  C    . ILE   A 1 173  ? 164.411 164.963 230.161 1.00 212.32 ? 1505 ILE   A C    1 
ATOM   951  O  O    . ILE   A 1 173  ? 164.020 165.005 228.988 1.00 209.22 ? 1505 ILE   A O    1 
ATOM   952  C  CB   . ILE   A 1 173  ? 165.050 162.773 231.256 1.00 209.39 ? 1505 ILE   A CB   1 
ATOM   953  C  CG1  . ILE   A 1 173  ? 166.215 161.843 231.594 1.00 204.92 ? 1505 ILE   A CG1  1 
ATOM   954  C  CG2  . ILE   A 1 173  ? 164.043 162.057 230.372 1.00 205.11 ? 1505 ILE   A CG2  1 
ATOM   955  C  CD1  . ILE   A 1 173  ? 166.989 161.379 230.390 1.00 202.30 ? 1505 ILE   A CD1  1 
ATOM   956  N  N    . ASN   A 1 174  ? 163.844 165.699 231.120 1.00 214.94 ? 1506 ASN   A N    1 
ATOM   957  C  CA   . ASN   A 1 174  ? 162.625 166.456 230.841 1.00 213.77 ? 1506 ASN   A CA   1 
ATOM   958  C  C    . ASN   A 1 174  ? 162.872 167.574 229.833 1.00 213.57 ? 1506 ASN   A C    1 
ATOM   959  O  O    . ASN   A 1 174  ? 162.035 167.826 228.959 1.00 213.53 ? 1506 ASN   A O    1 
ATOM   960  C  CB   . ASN   A 1 174  ? 162.032 167.005 232.144 1.00 216.48 ? 1506 ASN   A CB   1 
ATOM   961  C  CG   . ASN   A 1 174  ? 162.942 168.007 232.843 1.00 216.68 ? 1506 ASN   A CG   1 
ATOM   962  O  OD1  . ASN   A 1 174  ? 163.977 168.408 232.316 1.00 216.01 ? 1506 ASN   A OD1  1 
ATOM   963  N  ND2  . ASN   A 1 174  ? 162.551 168.413 234.046 1.00 212.56 ? 1506 ASN   A ND2  1 
ATOM   964  N  N    . GLU   A 1 175  ? 164.011 168.258 229.939 1.00 214.19 ? 1507 GLU   A N    1 
ATOM   965  C  CA   . GLU   A 1 175  ? 164.327 169.343 229.019 1.00 215.97 ? 1507 GLU   A CA   1 
ATOM   966  C  C    . GLU   A 1 175  ? 164.985 168.871 227.729 1.00 216.63 ? 1507 GLU   A C    1 
ATOM   967  O  O    . GLU   A 1 175  ? 164.981 169.617 226.743 1.00 216.47 ? 1507 GLU   A O    1 
ATOM   968  C  CB   . GLU   A 1 175  ? 165.216 170.384 229.715 1.00 213.97 ? 1507 GLU   A CB   1 
ATOM   969  C  CG   . GLU   A 1 175  ? 166.561 169.871 230.206 1.00 210.15 ? 1507 GLU   A CG   1 
ATOM   970  C  CD   . GLU   A 1 175  ? 167.646 169.903 229.151 1.00 210.07 ? 1507 GLU   A CD   1 
ATOM   971  O  OE1  . GLU   A 1 175  ? 167.498 170.645 228.158 1.00 206.13 ? 1507 GLU   A OE1  1 
ATOM   972  O  OE2  . GLU   A 1 175  ? 168.655 169.191 229.323 1.00 209.61 ? 1507 GLU   A OE2  1 
ATOM   973  N  N    . SER   A 1 176  ? 165.554 167.663 227.708 1.00 214.71 ? 1508 SER   A N    1 
ATOM   974  C  CA   . SER   A 1 176  ? 166.086 167.126 226.459 1.00 210.00 ? 1508 SER   A CA   1 
ATOM   975  C  C    . SER   A 1 176  ? 164.969 166.897 225.449 1.00 210.51 ? 1508 SER   A C    1 
ATOM   976  O  O    . SER   A 1 176  ? 165.118 167.206 224.261 1.00 206.04 ? 1508 SER   A O    1 
ATOM   977  C  CB   . SER   A 1 176  ? 166.847 165.828 226.722 1.00 207.82 ? 1508 SER   A CB   1 
ATOM   978  O  OG   . SER   A 1 176  ? 167.342 165.277 225.515 1.00 206.89 ? 1508 SER   A OG   1 
ATOM   979  N  N    . LEU   A 1 177  ? 163.840 166.354 225.907 1.00 212.63 ? 1509 LEU   A N    1 
ATOM   980  C  CA   . LEU   A 1 177  ? 162.691 166.144 225.036 1.00 209.29 ? 1509 LEU   A CA   1 
ATOM   981  C  C    . LEU   A 1 177  ? 161.860 167.406 224.855 1.00 208.73 ? 1509 LEU   A C    1 
ATOM   982  O  O    . LEU   A 1 177  ? 160.990 167.438 223.978 1.00 202.88 ? 1509 LEU   A O    1 
ATOM   983  C  CB   . LEU   A 1 177  ? 161.805 165.021 225.587 1.00 202.29 ? 1509 LEU   A CB   1 
ATOM   984  C  CG   . LEU   A 1 177  ? 162.245 163.566 225.385 1.00 192.96 ? 1509 LEU   A CG   1 
ATOM   985  C  CD1  . LEU   A 1 177  ? 163.440 163.203 226.256 1.00 197.72 ? 1509 LEU   A CD1  1 
ATOM   986  C  CD2  . LEU   A 1 177  ? 161.085 162.617 225.648 1.00 179.30 ? 1509 LEU   A CD2  1 
ATOM   987  N  N    . ASN   A 1 178  ? 162.104 168.437 225.658 1.00 213.28 ? 1510 ASN   A N    1 
ATOM   988  C  CA   . ASN   A 1 178  ? 161.358 169.686 225.560 1.00 208.58 ? 1510 ASN   A CA   1 
ATOM   989  C  C    . ASN   A 1 178  ? 162.273 170.889 225.765 1.00 206.64 ? 1510 ASN   A C    1 
ATOM   990  O  O    . ASN   A 1 178  ? 162.571 171.271 226.897 1.00 204.24 ? 1510 ASN   A O    1 
ATOM   991  C  CB   . ASN   A 1 178  ? 160.218 169.712 226.581 1.00 206.85 ? 1510 ASN   A CB   1 
ATOM   992  N  N    . VAL   A 1 196  ? 164.835 164.052 207.873 1.00 164.62 ? 1528 VAL   A N    1 
ATOM   993  C  CA   . VAL   A 1 196  ? 164.358 163.076 206.904 1.00 166.38 ? 1528 VAL   A CA   1 
ATOM   994  C  C    . VAL   A 1 196  ? 165.053 161.744 207.151 1.00 170.13 ? 1528 VAL   A C    1 
ATOM   995  O  O    . VAL   A 1 196  ? 166.249 161.701 207.433 1.00 171.33 ? 1528 VAL   A O    1 
ATOM   996  C  CB   . VAL   A 1 196  ? 164.580 163.569 205.467 1.00 161.95 ? 1528 VAL   A CB   1 
ATOM   997  C  CG1  . VAL   A 1 196  ? 164.179 162.500 204.460 1.00 158.83 ? 1528 VAL   A CG1  1 
ATOM   998  C  CG2  . VAL   A 1 196  ? 163.815 164.860 205.226 1.00 166.36 ? 1528 VAL   A CG2  1 
ATOM   999  N  N    . GLU   A 1 197  ? 164.287 160.657 207.046 1.00 171.82 ? 1529 GLU   A N    1 
ATOM   1000 C  CA   . GLU   A 1 197  ? 164.792 159.348 207.448 1.00 172.31 ? 1529 GLU   A CA   1 
ATOM   1001 C  C    . GLU   A 1 197  ? 165.880 158.843 206.506 1.00 177.20 ? 1529 GLU   A C    1 
ATOM   1002 O  O    . GLU   A 1 197  ? 166.788 158.120 206.932 1.00 180.50 ? 1529 GLU   A O    1 
ATOM   1003 C  CB   . GLU   A 1 197  ? 163.639 158.347 207.518 1.00 167.78 ? 1529 GLU   A CB   1 
ATOM   1004 C  CG   . GLU   A 1 197  ? 162.623 158.660 208.604 1.00 166.50 ? 1529 GLU   A CG   1 
ATOM   1005 C  CD   . GLU   A 1 197  ? 163.195 158.525 210.001 1.00 173.81 ? 1529 GLU   A CD   1 
ATOM   1006 O  OE1  . GLU   A 1 197  ? 164.087 157.674 210.205 1.00 177.39 ? 1529 GLU   A OE1  1 
ATOM   1007 O  OE2  . GLU   A 1 197  ? 162.755 159.277 210.896 1.00 173.07 ? 1529 GLU   A OE2  1 
ATOM   1008 N  N    . LEU   A 1 198  ? 165.798 159.194 205.219 1.00 174.99 ? 1530 LEU   A N    1 
ATOM   1009 C  CA   . LEU   A 1 198  ? 166.678 158.565 204.237 1.00 176.23 ? 1530 LEU   A CA   1 
ATOM   1010 C  C    . LEU   A 1 198  ? 168.137 158.950 204.459 1.00 181.32 ? 1530 LEU   A C    1 
ATOM   1011 O  O    . LEU   A 1 198  ? 169.039 158.136 204.228 1.00 184.02 ? 1530 LEU   A O    1 
ATOM   1012 C  CB   . LEU   A 1 198  ? 166.221 158.905 202.814 1.00 172.21 ? 1530 LEU   A CB   1 
ATOM   1013 C  CG   . LEU   A 1 198  ? 166.175 160.332 202.264 1.00 163.78 ? 1530 LEU   A CG   1 
ATOM   1014 C  CD1  . LEU   A 1 198  ? 167.537 160.768 201.743 1.00 158.36 ? 1530 LEU   A CD1  1 
ATOM   1015 C  CD2  . LEU   A 1 198  ? 165.124 160.441 201.171 1.00 151.07 ? 1530 LEU   A CD2  1 
ATOM   1016 N  N    . GLU   A 1 199  ? 168.397 160.184 204.901 1.00 180.39 ? 1531 GLU   A N    1 
ATOM   1017 C  CA   . GLU   A 1 199  ? 169.770 160.557 205.237 1.00 177.60 ? 1531 GLU   A CA   1 
ATOM   1018 C  C    . GLU   A 1 199  ? 170.265 159.791 206.457 1.00 184.37 ? 1531 GLU   A C    1 
ATOM   1019 O  O    . GLU   A 1 199  ? 171.442 159.420 206.528 1.00 189.58 ? 1531 GLU   A O    1 
ATOM   1020 C  CB   . GLU   A 1 199  ? 169.882 162.063 205.477 1.00 164.29 ? 1531 GLU   A CB   1 
ATOM   1021 C  CG   . GLU   A 1 199  ? 169.663 162.931 204.252 1.00 157.77 ? 1531 GLU   A CG   1 
ATOM   1022 C  CD   . GLU   A 1 199  ? 168.203 163.164 203.973 1.00 152.12 ? 1531 GLU   A CD   1 
ATOM   1023 O  OE1  . GLU   A 1 199  ? 167.380 162.690 204.776 1.00 153.64 ? 1531 GLU   A OE1  1 
ATOM   1024 O  OE2  . GLU   A 1 199  ? 167.879 163.818 202.960 1.00 139.60 ? 1531 GLU   A OE2  1 
ATOM   1025 N  N    . LYS   A 1 200  ? 169.381 159.549 207.428 1.00 185.91 ? 1532 LYS   A N    1 
ATOM   1026 C  CA   . LYS   A 1 200  ? 169.784 158.843 208.641 1.00 184.38 ? 1532 LYS   A CA   1 
ATOM   1027 C  C    . LYS   A 1 200  ? 170.254 157.428 208.330 1.00 187.55 ? 1532 LYS   A C    1 
ATOM   1028 O  O    . LYS   A 1 200  ? 171.248 156.957 208.895 1.00 185.47 ? 1532 LYS   A O    1 
ATOM   1029 C  CB   . LYS   A 1 200  ? 168.629 158.816 209.641 1.00 174.73 ? 1532 LYS   A CB   1 
ATOM   1030 N  N    . ILE   A 1 201  ? 169.548 156.730 207.437 1.00 189.88 ? 1533 ILE   A N    1 
ATOM   1031 C  CA   . ILE   A 1 201  ? 169.970 155.389 207.043 1.00 188.37 ? 1533 ILE   A CA   1 
ATOM   1032 C  C    . ILE   A 1 201  ? 171.313 155.444 206.328 1.00 187.87 ? 1533 ILE   A C    1 
ATOM   1033 O  O    . ILE   A 1 201  ? 172.201 154.619 206.575 1.00 187.26 ? 1533 ILE   A O    1 
ATOM   1034 C  CB   . ILE   A 1 201  ? 168.890 154.723 206.171 1.00 185.81 ? 1533 ILE   A CB   1 
ATOM   1035 N  N    . ILE   A 1 202  ? 171.482 156.415 205.429 1.00 186.33 ? 1534 ILE   A N    1 
ATOM   1036 C  CA   . ILE   A 1 202  ? 172.759 156.577 204.741 1.00 183.84 ? 1534 ILE   A CA   1 
ATOM   1037 C  C    . ILE   A 1 202  ? 173.843 156.991 205.727 1.00 185.36 ? 1534 ILE   A C    1 
ATOM   1038 O  O    . ILE   A 1 202  ? 175.005 156.583 205.605 1.00 181.68 ? 1534 ILE   A O    1 
ATOM   1039 C  CB   . ILE   A 1 202  ? 172.622 157.590 203.590 1.00 186.81 ? 1534 ILE   A CB   1 
ATOM   1040 N  N    . LEU   A 1 203  ? 173.484 157.815 206.714 1.00 189.18 ? 1535 LEU   A N    1 
ATOM   1041 C  CA   . LEU   A 1 203  ? 174.449 158.208 207.734 1.00 186.88 ? 1535 LEU   A CA   1 
ATOM   1042 C  C    . LEU   A 1 203  ? 174.927 157.001 208.528 1.00 187.15 ? 1535 LEU   A C    1 
ATOM   1043 O  O    . LEU   A 1 203  ? 176.121 156.872 208.815 1.00 188.03 ? 1535 LEU   A O    1 
ATOM   1044 C  CB   . LEU   A 1 203  ? 173.835 159.255 208.664 1.00 180.86 ? 1535 LEU   A CB   1 
ATOM   1045 N  N    . SER   A 1 204  ? 174.010 156.101 208.886 1.00 187.08 ? 1536 SER   A N    1 
ATOM   1046 C  CA   . SER   A 1 204  ? 174.404 154.894 209.605 1.00 186.21 ? 1536 SER   A CA   1 
ATOM   1047 C  C    . SER   A 1 204  ? 175.294 154.007 208.744 1.00 186.95 ? 1536 SER   A C    1 
ATOM   1048 O  O    . SER   A 1 204  ? 176.181 153.316 209.259 1.00 183.89 ? 1536 SER   A O    1 
ATOM   1049 C  CB   . SER   A 1 204  ? 173.164 154.126 210.059 1.00 185.93 ? 1536 SER   A CB   1 
ATOM   1050 O  OG   . SER   A 1 204  ? 172.440 153.631 208.947 1.00 188.00 ? 1536 SER   A OG   1 
ATOM   1051 N  N    . GLU   A 1 205  ? 175.069 154.012 207.429 1.00 189.14 ? 1537 GLU   A N    1 
ATOM   1052 C  CA   . GLU   A 1 205  ? 175.815 153.123 206.545 1.00 187.51 ? 1537 GLU   A CA   1 
ATOM   1053 C  C    . GLU   A 1 205  ? 177.281 153.529 206.438 1.00 189.69 ? 1537 GLU   A C    1 
ATOM   1054 O  O    . GLU   A 1 205  ? 178.170 152.670 206.439 1.00 190.54 ? 1537 GLU   A O    1 
ATOM   1055 C  CB   . GLU   A 1 205  ? 175.164 153.099 205.161 1.00 182.82 ? 1537 GLU   A CB   1 
ATOM   1056 N  N    . ARG   A 1 206  ? 177.555 154.832 206.341 1.00 188.73 ? 1538 ARG   A N    1 
ATOM   1057 C  CA   . ARG   A 1 206  ? 178.913 155.272 206.031 1.00 185.52 ? 1538 ARG   A CA   1 
ATOM   1058 C  C    . ARG   A 1 206  ? 179.867 155.010 207.193 1.00 188.14 ? 1538 ARG   A C    1 
ATOM   1059 O  O    . ARG   A 1 206  ? 181.025 154.631 206.983 1.00 189.55 ? 1538 ARG   A O    1 
ATOM   1060 C  CB   . ARG   A 1 206  ? 178.919 156.751 205.642 1.00 179.27 ? 1538 ARG   A CB   1 
ATOM   1061 C  CG   . ARG   A 1 206  ? 178.281 157.688 206.647 1.00 179.77 ? 1538 ARG   A CG   1 
ATOM   1062 C  CD   . ARG   A 1 206  ? 178.551 159.127 206.250 1.00 181.96 ? 1538 ARG   A CD   1 
ATOM   1063 N  NE   . ARG   A 1 206  ? 179.659 159.701 207.004 1.00 188.25 ? 1538 ARG   A NE   1 
ATOM   1064 C  CZ   . ARG   A 1 206  ? 180.099 160.943 206.860 1.00 188.37 ? 1538 ARG   A CZ   1 
ATOM   1065 N  NH1  . ARG   A 1 206  ? 179.557 161.772 205.982 1.00 186.90 ? 1538 ARG   A NH1  1 
ATOM   1066 N  NH2  . ARG   A 1 206  ? 181.115 161.362 207.609 1.00 184.77 ? 1538 ARG   A NH2  1 
ATOM   1067 N  N    . LYS   A 1 207  ? 179.403 155.211 208.430 1.00 185.85 ? 1539 LYS   A N    1 
ATOM   1068 C  CA   . LYS   A 1 207  ? 180.263 154.942 209.581 1.00 183.31 ? 1539 LYS   A CA   1 
ATOM   1069 C  C    . LYS   A 1 207  ? 180.628 153.466 209.667 1.00 189.38 ? 1539 LYS   A C    1 
ATOM   1070 O  O    . LYS   A 1 207  ? 181.711 153.118 210.151 1.00 188.70 ? 1539 LYS   A O    1 
ATOM   1071 C  CB   . LYS   A 1 207  ? 179.599 155.407 210.880 1.00 177.61 ? 1539 LYS   A CB   1 
ATOM   1072 C  CG   . LYS   A 1 207  ? 178.494 156.436 210.725 1.00 177.84 ? 1539 LYS   A CG   1 
ATOM   1073 C  CD   . LYS   A 1 207  ? 179.061 157.787 210.302 1.00 178.13 ? 1539 LYS   A CD   1 
ATOM   1074 C  CE   . LYS   A 1 207  ? 178.024 158.893 210.412 1.00 175.63 ? 1539 LYS   A CE   1 
ATOM   1075 N  NZ   . LYS   A 1 207  ? 178.551 160.206 209.944 1.00 175.62 ? 1539 LYS   A NZ   1 
ATOM   1076 N  N    . ASN   A 1 208  ? 179.739 152.584 209.206 1.00 192.94 ? 1540 ASN   A N    1 
ATOM   1077 C  CA   . ASN   A 1 208  ? 180.075 151.166 209.151 1.00 187.59 ? 1540 ASN   A CA   1 
ATOM   1078 C  C    . ASN   A 1 208  ? 181.240 150.919 208.201 1.00 193.42 ? 1540 ASN   A C    1 
ATOM   1079 O  O    . ASN   A 1 208  ? 182.127 150.108 208.490 1.00 196.75 ? 1540 ASN   A O    1 
ATOM   1080 C  CB   . ASN   A 1 208  ? 178.852 150.351 208.728 1.00 182.47 ? 1540 ASN   A CB   1 
ATOM   1081 N  N    . VAL   A 1 209  ? 181.257 151.615 207.069 1.00 194.78 ? 1541 VAL   A N    1 
ATOM   1082 C  CA   . VAL   A 1 209  ? 182.335 151.487 206.099 1.00 188.68 ? 1541 VAL   A CA   1 
ATOM   1083 C  C    . VAL   A 1 209  ? 183.617 152.093 206.657 1.00 185.87 ? 1541 VAL   A C    1 
ATOM   1084 O  O    . VAL   A 1 209  ? 183.576 152.949 207.541 1.00 187.12 ? 1541 VAL   A O    1 
ATOM   1085 C  CB   . VAL   A 1 209  ? 181.959 152.147 204.761 1.00 176.97 ? 1541 VAL   A CB   1 
ATOM   1086 N  N    . PHE   A 1 243  ? 169.665 166.265 207.542 1.00 168.33 ? 1575 PHE   A N    1 
ATOM   1087 C  CA   . PHE   A 1 243  ? 169.336 166.865 208.829 1.00 175.91 ? 1575 PHE   A CA   1 
ATOM   1088 C  C    . PHE   A 1 243  ? 170.202 166.284 209.941 1.00 178.65 ? 1575 PHE   A C    1 
ATOM   1089 O  O    . PHE   A 1 243  ? 170.128 166.715 211.091 1.00 176.74 ? 1575 PHE   A O    1 
ATOM   1090 C  CB   . PHE   A 1 243  ? 167.856 166.659 209.156 1.00 168.10 ? 1575 PHE   A CB   1 
ATOM   1091 N  N    . LEU   A 1 244  ? 171.016 165.289 209.588 1.00 181.52 ? 1576 LEU   A N    1 
ATOM   1092 C  CA   . LEU   A 1 244  ? 171.869 164.646 210.581 1.00 176.30 ? 1576 LEU   A CA   1 
ATOM   1093 C  C    . LEU   A 1 244  ? 173.070 165.515 210.937 1.00 174.62 ? 1576 LEU   A C    1 
ATOM   1094 O  O    . LEU   A 1 244  ? 173.588 165.436 212.056 1.00 176.28 ? 1576 LEU   A O    1 
ATOM   1095 C  CB   . LEU   A 1 244  ? 172.327 163.280 210.070 1.00 177.27 ? 1576 LEU   A CB   1 
ATOM   1096 N  N    . ASN   A 1 245  ? 173.526 166.346 209.996 1.00 172.41 ? 1577 ASN   A N    1 
ATOM   1097 C  CA   . ASN   A 1 245  ? 174.766 167.090 210.194 1.00 176.17 ? 1577 ASN   A CA   1 
ATOM   1098 C  C    . ASN   A 1 245  ? 174.656 168.037 211.383 1.00 178.94 ? 1577 ASN   A C    1 
ATOM   1099 O  O    . ASN   A 1 245  ? 175.552 168.083 212.233 1.00 180.52 ? 1577 ASN   A O    1 
ATOM   1100 C  CB   . ASN   A 1 245  ? 175.120 167.843 208.907 1.00 176.55 ? 1577 ASN   A CB   1 
ATOM   1101 C  CG   . ASN   A 1 245  ? 176.334 168.763 209.051 1.00 176.14 ? 1577 ASN   A CG   1 
ATOM   1102 O  OD1  . ASN   A 1 245  ? 176.438 169.568 209.978 1.00 169.36 ? 1577 ASN   A OD1  1 
ATOM   1103 N  ND2  . ASN   A 1 245  ? 177.265 168.636 208.115 1.00 175.27 ? 1577 ASN   A ND2  1 
ATOM   1104 N  N    . GLU   A 1 246  ? 173.567 168.800 211.465 1.00 179.36 ? 1578 GLU   A N    1 
ATOM   1105 C  CA   . GLU   A 1 246  ? 173.403 169.705 212.595 1.00 174.41 ? 1578 GLU   A CA   1 
ATOM   1106 C  C    . GLU   A 1 246  ? 173.051 168.965 213.879 1.00 173.09 ? 1578 GLU   A C    1 
ATOM   1107 O  O    . GLU   A 1 246  ? 173.065 169.574 214.954 1.00 165.24 ? 1578 GLU   A O    1 
ATOM   1108 C  CB   . GLU   A 1 246  ? 172.336 170.754 212.284 1.00 171.52 ? 1578 GLU   A CB   1 
ATOM   1109 C  CG   . GLU   A 1 246  ? 170.925 170.201 212.200 1.00 172.56 ? 1578 GLU   A CG   1 
ATOM   1110 C  CD   . GLU   A 1 246  ? 170.594 169.642 210.830 1.00 174.91 ? 1578 GLU   A CD   1 
ATOM   1111 O  OE1  . GLU   A 1 246  ? 171.528 169.406 210.035 1.00 175.19 ? 1578 GLU   A OE1  1 
ATOM   1112 O  OE2  . GLU   A 1 246  ? 169.394 169.441 210.549 1.00 170.97 ? 1578 GLU   A OE2  1 
ATOM   1113 N  N    . SER   A 1 247  ? 172.741 167.674 213.792 1.00 177.78 ? 1579 SER   A N    1 
ATOM   1114 C  CA   . SER   A 1 247  ? 172.458 166.859 214.964 1.00 180.12 ? 1579 SER   A CA   1 
ATOM   1115 C  C    . SER   A 1 247  ? 173.699 166.165 215.511 1.00 181.74 ? 1579 SER   A C    1 
ATOM   1116 O  O    . SER   A 1 247  ? 173.581 165.350 216.431 1.00 185.95 ? 1579 SER   A O    1 
ATOM   1117 C  CB   . SER   A 1 247  ? 171.384 165.816 214.640 1.00 181.17 ? 1579 SER   A CB   1 
ATOM   1118 O  OG   . SER   A 1 247  ? 171.856 164.875 213.695 1.00 179.21 ? 1579 SER   A OG   1 
ATOM   1119 N  N    . GLY   A 1 248  ? 174.876 166.461 214.967 1.00 180.77 ? 1580 GLY   A N    1 
ATOM   1120 C  CA   . GLY   A 1 248  ? 176.113 165.880 215.441 1.00 180.32 ? 1580 GLY   A CA   1 
ATOM   1121 C  C    . GLY   A 1 248  ? 176.558 164.624 214.728 1.00 183.14 ? 1580 GLY   A C    1 
ATOM   1122 O  O    . GLY   A 1 248  ? 177.670 164.148 214.988 1.00 182.50 ? 1580 GLY   A O    1 
ATOM   1123 N  N    . VAL   A 1 249  ? 175.733 164.069 213.840 1.00 186.30 ? 1581 VAL   A N    1 
ATOM   1124 C  CA   . VAL   A 1 249  ? 176.137 162.879 213.098 1.00 184.83 ? 1581 VAL   A CA   1 
ATOM   1125 C  C    . VAL   A 1 249  ? 177.244 163.216 212.105 1.00 184.12 ? 1581 VAL   A C    1 
ATOM   1126 O  O    . VAL   A 1 249  ? 178.173 162.426 211.899 1.00 180.83 ? 1581 VAL   A O    1 
ATOM   1127 C  CB   . VAL   A 1 249  ? 174.916 162.245 212.405 1.00 181.19 ? 1581 VAL   A CB   1 
ATOM   1128 C  CG1  . VAL   A 1 249  ? 175.340 161.069 211.548 1.00 173.86 ? 1581 VAL   A CG1  1 
ATOM   1129 C  CG2  . VAL   A 1 249  ? 173.888 161.808 213.437 1.00 180.63 ? 1581 VAL   A CG2  1 
ATOM   1130 N  N    . LEU   A 1 250  ? 177.167 164.388 211.475 1.00 183.13 ? 1582 LEU   A N    1 
ATOM   1131 C  CA   . LEU   A 1 250  ? 178.171 164.837 210.521 1.00 179.27 ? 1582 LEU   A CA   1 
ATOM   1132 C  C    . LEU   A 1 250  ? 178.680 166.222 210.889 1.00 184.82 ? 1582 LEU   A C    1 
ATOM   1133 O  O    . LEU   A 1 250  ? 177.912 167.099 211.289 1.00 185.39 ? 1582 LEU   A O    1 
ATOM   1134 C  CB   . LEU   A 1 250  ? 177.622 164.867 209.092 1.00 171.05 ? 1582 LEU   A CB   1 
ATOM   1135 C  CG   . LEU   A 1 250  ? 178.658 165.286 208.047 1.00 176.14 ? 1582 LEU   A CG   1 
ATOM   1136 C  CD1  . LEU   A 1 250  ? 179.798 164.297 208.012 1.00 178.27 ? 1582 LEU   A CD1  1 
ATOM   1137 C  CD2  . LEU   A 1 250  ? 178.028 165.410 206.674 1.00 179.68 ? 1582 LEU   A CD2  1 
ATOM   1138 N  N    . LEU   A 1 251  ? 179.988 166.409 210.740 1.00 188.80 ? 1583 LEU   A N    1 
ATOM   1139 C  CA   . LEU   A 1 251  ? 180.612 167.705 210.974 1.00 187.31 ? 1583 LEU   A CA   1 
ATOM   1140 C  C    . LEU   A 1 251  ? 180.474 168.596 209.744 1.00 180.03 ? 1583 LEU   A C    1 
ATOM   1141 O  O    . LEU   A 1 251  ? 181.057 168.318 208.696 1.00 174.64 ? 1583 LEU   A O    1 
ATOM   1142 C  CB   . LEU   A 1 251  ? 182.088 167.533 211.341 1.00 184.82 ? 1583 LEU   A CB   1 
ATOM   1143 N  N    . ASP   A 1 262  ? 176.708 169.008 204.838 1.00 182.82 ? 1594 ASP   A N    1 
ATOM   1144 C  CA   . ASP   A 1 262  ? 178.096 169.228 204.447 1.00 189.15 ? 1594 ASP   A CA   1 
ATOM   1145 C  C    . ASP   A 1 262  ? 178.790 167.894 204.186 1.00 191.72 ? 1594 ASP   A C    1 
ATOM   1146 O  O    . ASP   A 1 262  ? 178.144 166.917 203.810 1.00 189.89 ? 1594 ASP   A O    1 
ATOM   1147 C  CB   . ASP   A 1 262  ? 178.838 170.015 205.529 1.00 185.33 ? 1594 ASP   A CB   1 
ATOM   1148 C  CG   . ASP   A 1 262  ? 178.343 171.444 205.653 1.00 177.96 ? 1594 ASP   A CG   1 
ATOM   1149 O  OD1  . ASP   A 1 262  ? 177.875 172.004 204.640 1.00 174.82 ? 1594 ASP   A OD1  1 
ATOM   1150 O  OD2  . ASP   A 1 262  ? 178.418 172.006 206.766 1.00 171.79 ? 1594 ASP   A OD2  1 
ATOM   1151 N  N    . LEU   A 1 263  ? 180.108 167.858 204.375 1.00 192.75 ? 1595 LEU   A N    1 
ATOM   1152 C  CA   . LEU   A 1 263  ? 180.869 166.625 204.240 1.00 191.25 ? 1595 LEU   A CA   1 
ATOM   1153 C  C    . LEU   A 1 263  ? 182.039 166.630 205.214 1.00 193.61 ? 1595 LEU   A C    1 
ATOM   1154 O  O    . LEU   A 1 263  ? 182.636 167.674 205.490 1.00 193.66 ? 1595 LEU   A O    1 
ATOM   1155 C  CB   . LEU   A 1 263  ? 181.383 166.426 202.808 1.00 184.76 ? 1595 LEU   A CB   1 
ATOM   1156 C  CG   . LEU   A 1 263  ? 180.548 165.481 201.945 1.00 174.14 ? 1595 LEU   A CG   1 
ATOM   1157 C  CD1  . LEU   A 1 263  ? 181.190 165.287 200.581 1.00 159.19 ? 1595 LEU   A CD1  1 
ATOM   1158 C  CD2  . LEU   A 1 263  ? 180.356 164.149 202.651 1.00 175.24 ? 1595 LEU   A CD2  1 
ATOM   1159 N  N    . TYR   A 1 264  ? 182.358 165.446 205.729 1.00 195.92 ? 1596 TYR   A N    1 
ATOM   1160 C  CA   . TYR   A 1 264  ? 183.512 165.260 206.597 1.00 190.90 ? 1596 TYR   A CA   1 
ATOM   1161 C  C    . TYR   A 1 264  ? 183.970 163.815 206.470 1.00 190.24 ? 1596 TYR   A C    1 
ATOM   1162 O  O    . TYR   A 1 264  ? 183.214 162.938 206.047 1.00 189.91 ? 1596 TYR   A O    1 
ATOM   1163 C  CB   . TYR   A 1 264  ? 183.189 165.615 208.051 1.00 183.80 ? 1596 TYR   A CB   1 
ATOM   1164 N  N    . PHE   A 1 265  ? 185.223 163.576 206.846 1.00 189.84 ? 1597 PHE   A N    1 
ATOM   1165 C  CA   . PHE   A 1 265  ? 185.824 162.255 206.727 1.00 188.38 ? 1597 PHE   A CA   1 
ATOM   1166 C  C    . PHE   A 1 265  ? 185.501 161.425 207.961 1.00 191.70 ? 1597 PHE   A C    1 
ATOM   1167 O  O    . PHE   A 1 265  ? 185.787 161.842 209.089 1.00 190.68 ? 1597 PHE   A O    1 
ATOM   1168 C  CB   . PHE   A 1 265  ? 187.338 162.362 206.545 1.00 178.62 ? 1597 PHE   A CB   1 
ATOM   1169 C  CG   . PHE   A 1 265  ? 187.766 162.530 205.116 1.00 171.13 ? 1597 PHE   A CG   1 
ATOM   1170 C  CD1  . PHE   A 1 265  ? 186.834 162.789 204.126 1.00 168.24 ? 1597 PHE   A CD1  1 
ATOM   1171 C  CD2  . PHE   A 1 265  ? 189.100 162.428 204.764 1.00 166.43 ? 1597 PHE   A CD2  1 
ATOM   1172 C  CE1  . PHE   A 1 265  ? 187.224 162.943 202.813 1.00 158.76 ? 1597 PHE   A CE1  1 
ATOM   1173 C  CE2  . PHE   A 1 265  ? 189.497 162.581 203.451 1.00 164.01 ? 1597 PHE   A CE2  1 
ATOM   1174 C  CZ   . PHE   A 1 265  ? 188.557 162.838 202.475 1.00 158.62 ? 1597 PHE   A CZ   1 
ATOM   1175 N  N    . VAL   A 1 266  ? 184.912 160.250 207.737 1.00 191.08 ? 1598 VAL   A N    1 
ATOM   1176 C  CA   . VAL   A 1 266  ? 184.536 159.327 208.804 1.00 188.30 ? 1598 VAL   A CA   1 
ATOM   1177 C  C    . VAL   A 1 266  ? 183.645 160.038 209.814 1.00 191.34 ? 1598 VAL   A C    1 
ATOM   1178 O  O    . VAL   A 1 266  ? 182.864 160.927 209.456 1.00 190.28 ? 1598 VAL   A O    1 
ATOM   1179 C  CB   . VAL   A 1 266  ? 185.777 158.726 209.490 1.00 183.98 ? 1598 VAL   A CB   1 
ATOM   1180 N  N    . GLU   A 1 267  ? 183.752 159.644 211.080 1.00 189.64 ? 1599 GLU   A N    1 
ATOM   1181 C  CA   . GLU   A 1 267  ? 182.934 160.224 212.129 1.00 187.69 ? 1599 GLU   A CA   1 
ATOM   1182 C  C    . GLU   A 1 267  ? 183.386 161.650 212.445 1.00 192.86 ? 1599 GLU   A C    1 
ATOM   1183 O  O    . GLU   A 1 267  ? 184.551 162.003 212.245 1.00 191.75 ? 1599 GLU   A O    1 
ATOM   1184 C  CB   . GLU   A 1 267  ? 183.004 159.360 213.386 1.00 179.25 ? 1599 GLU   A CB   1 
ATOM   1185 N  N    . PRO   A 1 268  ? 182.473 162.493 212.942 1.00 193.07 ? 1600 PRO   A N    1 
ATOM   1186 C  CA   . PRO   A 1 268  ? 182.888 163.839 213.374 1.00 186.93 ? 1600 PRO   A CA   1 
ATOM   1187 C  C    . PRO   A 1 268  ? 183.828 163.811 214.563 1.00 184.19 ? 1600 PRO   A C    1 
ATOM   1188 O  O    . PRO   A 1 268  ? 184.468 164.824 214.872 1.00 178.27 ? 1600 PRO   A O    1 
ATOM   1189 C  CB   . PRO   A 1 268  ? 181.557 164.521 213.711 1.00 182.53 ? 1600 PRO   A CB   1 
ATOM   1190 C  CG   . PRO   A 1 268  ? 180.655 163.404 214.083 1.00 185.30 ? 1600 PRO   A CG   1 
ATOM   1191 C  CD   . PRO   A 1 268  ? 181.047 162.243 213.213 1.00 187.29 ? 1600 PRO   A CD   1 
ATOM   1192 N  N    . LYS   A 1 269  ? 183.909 162.673 215.256 1.00 186.31 ? 1601 LYS   A N    1 
ATOM   1193 C  CA   . LYS   A 1 269  ? 184.835 162.539 216.372 1.00 182.83 ? 1601 LYS   A CA   1 
ATOM   1194 C  C    . LYS   A 1 269  ? 186.276 162.728 215.919 1.00 184.06 ? 1601 LYS   A C    1 
ATOM   1195 O  O    . LYS   A 1 269  ? 187.070 163.361 216.622 1.00 183.64 ? 1601 LYS   A O    1 
ATOM   1196 C  CB   . LYS   A 1 269  ? 184.646 161.165 217.026 1.00 183.98 ? 1601 LYS   A CB   1 
ATOM   1197 C  CG   . LYS   A 1 269  ? 185.854 160.606 217.764 1.00 184.32 ? 1601 LYS   A CG   1 
ATOM   1198 C  CD   . LYS   A 1 269  ? 186.261 161.471 218.943 1.00 187.56 ? 1601 LYS   A CD   1 
ATOM   1199 C  CE   . LYS   A 1 269  ? 187.131 160.696 219.918 1.00 187.20 ? 1601 LYS   A CE   1 
ATOM   1200 N  NZ   . LYS   A 1 269  ? 187.078 161.300 221.280 1.00 187.80 ? 1601 LYS   A NZ   1 
ATOM   1201 N  N    . TRP   A 1 270  ? 186.624 162.215 214.736 1.00 185.96 ? 1602 TRP   A N    1 
ATOM   1202 C  CA   . TRP   A 1 270  ? 188.016 162.252 214.301 1.00 180.32 ? 1602 TRP   A CA   1 
ATOM   1203 C  C    . TRP   A 1 270  ? 188.486 163.691 214.120 1.00 181.87 ? 1602 TRP   A C    1 
ATOM   1204 O  O    . TRP   A 1 270  ? 189.580 164.051 214.568 1.00 184.15 ? 1602 TRP   A O    1 
ATOM   1205 C  CB   . TRP   A 1 270  ? 188.168 161.427 213.015 1.00 178.51 ? 1602 TRP   A CB   1 
ATOM   1206 C  CG   . TRP   A 1 270  ? 189.499 161.481 212.264 1.00 181.97 ? 1602 TRP   A CG   1 
ATOM   1207 C  CD1  . TRP   A 1 270  ? 190.608 162.222 212.567 1.00 181.90 ? 1602 TRP   A CD1  1 
ATOM   1208 C  CD2  . TRP   A 1 270  ? 189.842 160.715 211.099 1.00 183.24 ? 1602 TRP   A CD2  1 
ATOM   1209 N  NE1  . TRP   A 1 270  ? 191.607 161.979 211.656 1.00 183.28 ? 1602 TRP   A NE1  1 
ATOM   1210 C  CE2  . TRP   A 1 270  ? 191.163 161.056 210.746 1.00 180.66 ? 1602 TRP   A CE2  1 
ATOM   1211 C  CE3  . TRP   A 1 270  ? 189.156 159.780 210.317 1.00 179.83 ? 1602 TRP   A CE3  1 
ATOM   1212 C  CZ2  . TRP   A 1 270  ? 191.810 160.497 209.648 1.00 170.88 ? 1602 TRP   A CZ2  1 
ATOM   1213 C  CZ3  . TRP   A 1 270  ? 189.801 159.226 209.226 1.00 170.35 ? 1602 TRP   A CZ3  1 
ATOM   1214 C  CH2  . TRP   A 1 270  ? 191.115 159.586 208.901 1.00 165.77 ? 1602 TRP   A CH2  1 
ATOM   1215 N  N    . LEU   A 1 271  ? 187.652 164.540 213.512 1.00 181.83 ? 1603 LEU   A N    1 
ATOM   1216 C  CA   . LEU   A 1 271  ? 188.041 165.933 213.305 1.00 177.75 ? 1603 LEU   A CA   1 
ATOM   1217 C  C    . LEU   A 1 271  ? 188.337 166.624 214.629 1.00 178.33 ? 1603 LEU   A C    1 
ATOM   1218 O  O    . LEU   A 1 271  ? 189.329 167.352 214.750 1.00 172.16 ? 1603 LEU   A O    1 
ATOM   1219 C  CB   . LEU   A 1 271  ? 186.944 166.678 212.545 1.00 175.63 ? 1603 LEU   A CB   1 
ATOM   1220 N  N    . CYS   A 1 272  ? 187.492 166.403 215.636 1.00 182.77 ? 1604 CYS   A N    1 
ATOM   1221 C  CA   . CYS   A 1 272  ? 187.799 166.907 216.969 1.00 182.57 ? 1604 CYS   A CA   1 
ATOM   1222 C  C    . CYS   A 1 272  ? 188.996 166.177 217.560 1.00 185.11 ? 1604 CYS   A C    1 
ATOM   1223 O  O    . CYS   A 1 272  ? 189.776 166.761 218.321 1.00 182.05 ? 1604 CYS   A O    1 
ATOM   1224 C  CB   . CYS   A 1 272  ? 186.580 166.769 217.879 1.00 186.46 ? 1604 CYS   A CB   1 
ATOM   1225 S  SG   . CYS   A 1 272  ? 185.175 167.792 217.389 1.00 192.48 ? 1604 CYS   A SG   1 
ATOM   1226 N  N    . LYS   A 1 273  ? 189.154 164.893 217.224 1.00 189.38 ? 1605 LYS   A N    1 
ATOM   1227 C  CA   . LYS   A 1 273  ? 190.283 164.127 217.742 1.00 185.85 ? 1605 LYS   A CA   1 
ATOM   1228 C  C    . LYS   A 1 273  ? 191.605 164.632 217.175 1.00 188.49 ? 1605 LYS   A C    1 
ATOM   1229 O  O    . LYS   A 1 273  ? 192.571 164.833 217.920 1.00 182.22 ? 1605 LYS   A O    1 
ATOM   1230 C  CB   . LYS   A 1 273  ? 190.097 162.642 217.430 1.00 179.42 ? 1605 LYS   A CB   1 
ATOM   1231 N  N    . ILE   A 1 274  ? 191.672 164.837 215.857 1.00 189.99 ? 1606 ILE   A N    1 
ATOM   1232 C  CA   . ILE   A 1 274  ? 192.905 165.348 215.266 1.00 183.68 ? 1606 ILE   A CA   1 
ATOM   1233 C  C    . ILE   A 1 274  ? 193.109 166.806 215.655 1.00 180.68 ? 1606 ILE   A C    1 
ATOM   1234 O  O    . ILE   A 1 274  ? 194.247 167.272 215.785 1.00 178.93 ? 1606 ILE   A O    1 
ATOM   1235 C  CB   . ILE   A 1 274  ? 192.899 165.153 213.735 1.00 178.07 ? 1606 ILE   A CB   1 
ATOM   1236 C  CG1  . ILE   A 1 274  ? 194.177 165.719 213.114 1.00 177.79 ? 1606 ILE   A CG1  1 
ATOM   1237 C  CG2  . ILE   A 1 274  ? 191.696 165.829 213.107 1.00 176.57 ? 1606 ILE   A CG2  1 
ATOM   1238 C  CD1  . ILE   A 1 274  ? 195.435 165.002 213.551 1.00 175.08 ? 1606 ILE   A CD1  1 
ATOM   1239 N  N    . MET   A 1 275  ? 192.017 167.549 215.856 1.00 176.79 ? 1607 MET   A N    1 
ATOM   1240 C  CA   . MET   A 1 275  ? 192.142 168.913 216.359 1.00 174.48 ? 1607 MET   A CA   1 
ATOM   1241 C  C    . MET   A 1 275  ? 192.764 168.924 217.749 1.00 182.59 ? 1607 MET   A C    1 
ATOM   1242 O  O    . MET   A 1 275  ? 193.480 169.865 218.111 1.00 181.61 ? 1607 MET   A O    1 
ATOM   1243 C  CB   . MET   A 1 275  ? 190.777 169.597 216.376 1.00 172.55 ? 1607 MET   A CB   1 
ATOM   1244 N  N    . ALA   A 1 276  ? 192.498 167.885 218.545 1.00 186.57 ? 1608 ALA   A N    1 
ATOM   1245 C  CA   . ALA   A 1 276  ? 193.154 167.763 219.842 1.00 185.09 ? 1608 ALA   A CA   1 
ATOM   1246 C  C    . ALA   A 1 276  ? 194.656 167.563 219.677 1.00 184.29 ? 1608 ALA   A C    1 
ATOM   1247 O  O    . ALA   A 1 276  ? 195.446 168.009 220.518 1.00 186.88 ? 1608 ALA   A O    1 
ATOM   1248 C  CB   . ALA   A 1 276  ? 192.540 166.612 220.636 1.00 185.29 ? 1608 ALA   A CB   1 
ATOM   1249 N  N    . GLN   A 1 277  ? 195.068 166.894 218.599 1.00 180.29 ? 1609 GLN   A N    1 
ATOM   1250 C  CA   . GLN   A 1 277  ? 196.490 166.796 218.294 1.00 180.20 ? 1609 GLN   A CA   1 
ATOM   1251 C  C    . GLN   A 1 277  ? 197.081 168.183 218.079 1.00 179.95 ? 1609 GLN   A C    1 
ATOM   1252 O  O    . GLN   A 1 277  ? 198.196 168.475 218.522 1.00 177.61 ? 1609 GLN   A O    1 
ATOM   1253 C  CB   . GLN   A 1 277  ? 196.700 165.914 217.064 1.00 181.39 ? 1609 GLN   A CB   1 
ATOM   1254 C  CG   . GLN   A 1 277  ? 198.150 165.647 216.704 1.00 182.46 ? 1609 GLN   A CG   1 
ATOM   1255 C  CD   . GLN   A 1 277  ? 198.849 164.783 217.734 1.00 180.31 ? 1609 GLN   A CD   1 
ATOM   1256 O  OE1  . GLN   A 1 277  ? 198.275 163.823 218.246 1.00 179.46 ? 1609 GLN   A OE1  1 
ATOM   1257 N  NE2  . GLN   A 1 277  ? 200.102 165.105 218.027 1.00 175.64 ? 1609 GLN   A NE2  1 
ATOM   1258 N  N    . ILE   A 1 278  ? 196.334 169.058 217.402 1.00 179.38 ? 1610 ILE   A N    1 
ATOM   1259 C  CA   . ILE   A 1 278  ? 196.736 170.456 217.304 1.00 177.11 ? 1610 ILE   A CA   1 
ATOM   1260 C  C    . ILE   A 1 278  ? 196.736 171.107 218.680 1.00 176.52 ? 1610 ILE   A C    1 
ATOM   1261 O  O    . ILE   A 1 278  ? 197.609 171.923 218.996 1.00 174.05 ? 1610 ILE   A O    1 
ATOM   1262 C  CB   . ILE   A 1 278  ? 195.820 171.209 216.322 1.00 178.67 ? 1610 ILE   A CB   1 
ATOM   1263 C  CG1  . ILE   A 1 278  ? 195.887 170.571 214.938 1.00 177.75 ? 1610 ILE   A CG1  1 
ATOM   1264 C  CG2  . ILE   A 1 278  ? 196.206 172.675 216.244 1.00 178.70 ? 1610 ILE   A CG2  1 
ATOM   1265 C  CD1  . ILE   A 1 278  ? 197.267 170.602 214.326 1.00 174.87 ? 1610 ILE   A CD1  1 
ATOM   1266 N  N    . LEU   A 1 279  ? 195.759 170.760 219.519 1.00 178.77 ? 1611 LEU   A N    1 
ATOM   1267 C  CA   . LEU   A 1 279  ? 195.691 171.350 220.850 1.00 177.96 ? 1611 LEU   A CA   1 
ATOM   1268 C  C    . LEU   A 1 279  ? 196.912 170.977 221.682 1.00 174.89 ? 1611 LEU   A C    1 
ATOM   1269 O  O    . LEU   A 1 279  ? 197.493 171.825 222.367 1.00 169.23 ? 1611 LEU   A O    1 
ATOM   1270 C  CB   . LEU   A 1 279  ? 194.404 170.913 221.551 1.00 176.77 ? 1611 LEU   A CB   1 
ATOM   1271 N  N    . THR   A 1 280  ? 197.319 169.707 221.634 1.00 179.02 ? 1612 THR   A N    1 
ATOM   1272 C  CA   . THR   A 1 280  ? 198.444 169.277 222.458 1.00 176.46 ? 1612 THR   A CA   1 
ATOM   1273 C  C    . THR   A 1 280  ? 199.778 169.716 221.863 1.00 176.36 ? 1612 THR   A C    1 
ATOM   1274 O  O    . THR   A 1 280  ? 200.696 170.087 222.603 1.00 175.92 ? 1612 THR   A O    1 
ATOM   1275 C  CB   . THR   A 1 280  ? 198.402 167.758 222.671 1.00 178.56 ? 1612 THR   A CB   1 
ATOM   1276 O  OG1  . THR   A 1 280  ? 199.412 167.374 223.613 1.00 171.14 ? 1612 THR   A OG1  1 
ATOM   1277 C  CG2  . THR   A 1 280  ? 198.601 166.996 221.365 1.00 177.13 ? 1612 THR   A CG2  1 
ATOM   1278 N  N    . VAL   A 1 281  ? 199.909 169.686 220.540 1.00 176.88 ? 1613 VAL   A N    1 
ATOM   1279 C  CA   . VAL   A 1 281  ? 201.154 170.088 219.894 1.00 171.94 ? 1613 VAL   A CA   1 
ATOM   1280 C  C    . VAL   A 1 281  ? 200.869 170.960 218.677 1.00 167.03 ? 1613 VAL   A C    1 
ATOM   1281 O  O    . VAL   A 1 281  ? 199.872 170.774 217.982 1.00 165.30 ? 1613 VAL   A O    1 
ATOM   1282 C  CB   . VAL   A 1 281  ? 202.017 168.866 219.491 1.00 166.07 ? 1613 VAL   A CB   1 
ATOM   1283 C  CG1  . VAL   A 1 281  ? 202.289 167.963 220.687 1.00 164.60 ? 1613 VAL   A CG1  1 
ATOM   1284 C  CG2  . VAL   A 1 281  ? 201.359 168.087 218.371 1.00 161.90 ? 1613 VAL   A CG2  1 
ATOM   1285 N  N    . ARG   A 1 307  ? 197.450 161.098 216.320 1.00 179.81 ? 1639 ARG   A N    1 
ATOM   1286 C  CA   . ARG   A 1 307  ? 198.783 160.508 216.373 1.00 186.22 ? 1639 ARG   A CA   1 
ATOM   1287 C  C    . ARG   A 1 307  ? 199.453 160.558 215.004 1.00 192.81 ? 1639 ARG   A C    1 
ATOM   1288 O  O    . ARG   A 1 307  ? 199.506 161.612 214.369 1.00 193.13 ? 1639 ARG   A O    1 
ATOM   1289 C  CB   . ARG   A 1 307  ? 198.711 159.064 216.874 1.00 187.45 ? 1639 ARG   A CB   1 
ATOM   1290 N  N    . LYS   A 1 308  ? 199.970 159.415 214.558 1.00 193.63 ? 1640 LYS   A N    1 
ATOM   1291 C  CA   . LYS   A 1 308  ? 200.586 159.342 213.240 1.00 193.28 ? 1640 LYS   A CA   1 
ATOM   1292 C  C    . LYS   A 1 308  ? 199.541 159.564 212.154 1.00 196.88 ? 1640 LYS   A C    1 
ATOM   1293 O  O    . LYS   A 1 308  ? 198.487 158.922 212.141 1.00 195.85 ? 1640 LYS   A O    1 
ATOM   1294 C  CB   . LYS   A 1 308  ? 201.270 157.988 213.049 1.00 190.24 ? 1640 LYS   A CB   1 
ATOM   1295 N  N    . PHE   A 1 309  ? 199.841 160.477 211.238 1.00 199.67 ? 1641 PHE   A N    1 
ATOM   1296 C  CA   . PHE   A 1 309  ? 198.910 160.852 210.189 1.00 201.20 ? 1641 PHE   A CA   1 
ATOM   1297 C  C    . PHE   A 1 309  ? 199.642 160.991 208.863 1.00 206.70 ? 1641 PHE   A C    1 
ATOM   1298 O  O    . PHE   A 1 309  ? 200.823 161.356 208.836 1.00 202.44 ? 1641 PHE   A O    1 
ATOM   1299 C  CB   . PHE   A 1 309  ? 198.201 162.170 210.536 1.00 194.34 ? 1641 PHE   A CB   1 
ATOM   1300 N  N    . PRO   A 1 310  ? 198.969 160.701 207.748 1.00 211.23 ? 1642 PRO   A N    1 
ATOM   1301 C  CA   . PRO   A 1 310  ? 199.642 160.763 206.445 1.00 211.80 ? 1642 PRO   A CA   1 
ATOM   1302 C  C    . PRO   A 1 310  ? 200.055 162.183 206.088 1.00 212.23 ? 1642 PRO   A C    1 
ATOM   1303 O  O    . PRO   A 1 310  ? 199.349 163.149 206.382 1.00 211.05 ? 1642 PRO   A O    1 
ATOM   1304 C  CB   . PRO   A 1 310  ? 198.586 160.221 205.477 1.00 207.43 ? 1642 PRO   A CB   1 
ATOM   1305 C  CG   . PRO   A 1 310  ? 197.289 160.529 206.137 1.00 207.67 ? 1642 PRO   A CG   1 
ATOM   1306 C  CD   . PRO   A 1 310  ? 197.535 160.388 207.613 1.00 208.55 ? 1642 PRO   A CD   1 
ATOM   1307 N  N    . LYS   A 1 311  ? 201.217 162.300 205.440 1.00 212.43 ? 1643 LYS   A N    1 
ATOM   1308 C  CA   . LYS   A 1 311  ? 201.712 163.613 205.042 1.00 209.39 ? 1643 LYS   A CA   1 
ATOM   1309 C  C    . LYS   A 1 311  ? 201.068 164.082 203.743 1.00 210.35 ? 1643 LYS   A C    1 
ATOM   1310 O  O    . LYS   A 1 311  ? 201.170 165.261 203.385 1.00 208.10 ? 1643 LYS   A O    1 
ATOM   1311 C  CB   . LYS   A 1 311  ? 203.234 163.580 204.905 1.00 207.88 ? 1643 LYS   A CB   1 
ATOM   1312 N  N    . ASN   A 1 312  ? 200.402 163.175 203.023 1.00 213.47 ? 1644 ASN   A N    1 
ATOM   1313 C  CA   . ASN   A 1 312  ? 199.841 163.528 201.722 1.00 213.33 ? 1644 ASN   A CA   1 
ATOM   1314 C  C    . ASN   A 1 312  ? 198.677 164.505 201.851 1.00 212.35 ? 1644 ASN   A C    1 
ATOM   1315 O  O    . ASN   A 1 312  ? 198.455 165.338 200.965 1.00 210.96 ? 1644 ASN   A O    1 
ATOM   1316 C  CB   . ASN   A 1 312  ? 199.438 162.252 200.966 1.00 206.76 ? 1644 ASN   A CB   1 
ATOM   1317 C  CG   . ASN   A 1 312  ? 198.208 161.551 201.554 1.00 204.21 ? 1644 ASN   A CG   1 
ATOM   1318 O  OD1  . ASN   A 1 312  ? 197.262 162.178 202.027 1.00 207.89 ? 1644 ASN   A OD1  1 
ATOM   1319 N  ND2  . ASN   A 1 312  ? 198.231 160.223 201.518 1.00 192.30 ? 1644 ASN   A ND2  1 
ATOM   1320 N  N    . TYR   A 1 313  ? 197.920 164.418 202.944 1.00 211.94 ? 1645 TYR   A N    1 
ATOM   1321 C  CA   . TYR   A 1 313  ? 196.752 165.261 203.154 1.00 209.92 ? 1645 TYR   A CA   1 
ATOM   1322 C  C    . TYR   A 1 313  ? 197.002 166.379 204.161 1.00 212.52 ? 1645 TYR   A C    1 
ATOM   1323 O  O    . TYR   A 1 313  ? 196.048 167.037 204.587 1.00 213.43 ? 1645 TYR   A O    1 
ATOM   1324 C  CB   . TYR   A 1 313  ? 195.565 164.405 203.604 1.00 203.16 ? 1645 TYR   A CB   1 
ATOM   1325 C  CG   . TYR   A 1 313  ? 194.221 164.900 203.114 1.00 199.46 ? 1645 TYR   A CG   1 
ATOM   1326 C  CD1  . TYR   A 1 313  ? 193.379 165.626 203.947 1.00 196.00 ? 1645 TYR   A CD1  1 
ATOM   1327 C  CD2  . TYR   A 1 313  ? 193.794 164.640 201.819 1.00 196.08 ? 1645 TYR   A CD2  1 
ATOM   1328 C  CE1  . TYR   A 1 313  ? 192.151 166.079 203.505 1.00 190.30 ? 1645 TYR   A CE1  1 
ATOM   1329 C  CE2  . TYR   A 1 313  ? 192.567 165.090 201.367 1.00 188.99 ? 1645 TYR   A CE2  1 
ATOM   1330 C  CZ   . TYR   A 1 313  ? 191.751 165.809 202.214 1.00 185.97 ? 1645 TYR   A CZ   1 
ATOM   1331 O  OH   . TYR   A 1 313  ? 190.530 166.258 201.768 1.00 174.75 ? 1645 TYR   A OH   1 
ATOM   1332 N  N    . MET   A 1 314  ? 198.258 166.617 204.543 1.00 214.10 ? 1646 MET   A N    1 
ATOM   1333 C  CA   . MET   A 1 314  ? 198.541 167.657 205.529 1.00 209.63 ? 1646 MET   A CA   1 
ATOM   1334 C  C    . MET   A 1 314  ? 198.350 169.051 204.947 1.00 209.77 ? 1646 MET   A C    1 
ATOM   1335 O  O    . MET   A 1 314  ? 198.021 169.993 205.677 1.00 210.04 ? 1646 MET   A O    1 
ATOM   1336 C  CB   . MET   A 1 314  ? 199.955 167.490 206.082 1.00 208.43 ? 1646 MET   A CB   1 
ATOM   1337 C  CG   . MET   A 1 314  ? 200.113 166.268 206.956 1.00 204.55 ? 1646 MET   A CG   1 
ATOM   1338 S  SD   . MET   A 1 314  ? 199.344 166.558 208.558 1.00 187.32 ? 1646 MET   A SD   1 
ATOM   1339 C  CE   . MET   A 1 314  ? 198.276 165.133 208.685 1.00 194.68 ? 1646 MET   A CE   1 
ATOM   1340 N  N    . SER   A 1 315  ? 198.551 169.205 203.637 1.00 211.52 ? 1647 SER   A N    1 
ATOM   1341 C  CA   . SER   A 1 315  ? 198.343 170.506 203.010 1.00 215.08 ? 1647 SER   A CA   1 
ATOM   1342 C  C    . SER   A 1 315  ? 196.892 170.955 203.141 1.00 214.90 ? 1647 SER   A C    1 
ATOM   1343 O  O    . SER   A 1 315  ? 196.618 172.130 203.416 1.00 217.85 ? 1647 SER   A O    1 
ATOM   1344 C  CB   . SER   A 1 315  ? 198.762 170.454 201.540 1.00 215.06 ? 1647 SER   A CB   1 
ATOM   1345 O  OG   . SER   A 1 315  ? 198.540 171.699 200.901 1.00 215.00 ? 1647 SER   A OG   1 
ATOM   1346 N  N    . GLN   A 1 316  ? 195.947 170.032 202.949 1.00 210.40 ? 1648 GLN   A N    1 
ATOM   1347 C  CA   . GLN   A 1 316  ? 194.539 170.367 203.139 1.00 207.39 ? 1648 GLN   A CA   1 
ATOM   1348 C  C    . GLN   A 1 316  ? 194.222 170.618 204.607 1.00 207.77 ? 1648 GLN   A C    1 
ATOM   1349 O  O    . GLN   A 1 316  ? 193.402 171.485 204.932 1.00 205.54 ? 1648 GLN   A O    1 
ATOM   1350 C  CB   . GLN   A 1 316  ? 193.655 169.250 202.584 1.00 201.65 ? 1648 GLN   A CB   1 
ATOM   1351 C  CG   . GLN   A 1 316  ? 192.162 169.529 202.683 1.00 195.54 ? 1648 GLN   A CG   1 
ATOM   1352 C  CD   . GLN   A 1 316  ? 191.740 170.753 201.897 1.00 191.27 ? 1648 GLN   A CD   1 
ATOM   1353 O  OE1  . GLN   A 1 316  ? 191.474 171.809 202.469 1.00 194.84 ? 1648 GLN   A OE1  1 
ATOM   1354 N  NE2  . GLN   A 1 316  ? 191.674 170.616 200.579 1.00 181.57 ? 1648 GLN   A NE2  1 
ATOM   1355 N  N    . TYR   A 1 317  ? 194.858 169.866 205.509 1.00 208.75 ? 1649 TYR   A N    1 
ATOM   1356 C  CA   . TYR   A 1 317  ? 194.525 169.979 206.926 1.00 207.15 ? 1649 TYR   A CA   1 
ATOM   1357 C  C    . TYR   A 1 317  ? 194.895 171.350 207.476 1.00 210.63 ? 1649 TYR   A C    1 
ATOM   1358 O  O    . TYR   A 1 317  ? 194.147 171.929 208.273 1.00 210.41 ? 1649 TYR   A O    1 
ATOM   1359 C  CB   . TYR   A 1 317  ? 195.218 168.876 207.724 1.00 201.85 ? 1649 TYR   A CB   1 
ATOM   1360 C  CG   . TYR   A 1 317  ? 194.862 168.897 209.192 1.00 196.48 ? 1649 TYR   A CG   1 
ATOM   1361 C  CD1  . TYR   A 1 317  ? 193.624 168.445 209.626 1.00 192.67 ? 1649 TYR   A CD1  1 
ATOM   1362 C  CD2  . TYR   A 1 317  ? 195.758 169.371 210.142 1.00 192.78 ? 1649 TYR   A CD2  1 
ATOM   1363 C  CE1  . TYR   A 1 317  ? 193.284 168.463 210.961 1.00 191.56 ? 1649 TYR   A CE1  1 
ATOM   1364 C  CE2  . TYR   A 1 317  ? 195.427 169.391 211.485 1.00 187.48 ? 1649 TYR   A CE2  1 
ATOM   1365 C  CZ   . TYR   A 1 317  ? 194.187 168.936 211.888 1.00 188.01 ? 1649 TYR   A CZ   1 
ATOM   1366 O  OH   . TYR   A 1 317  ? 193.842 168.949 213.219 1.00 184.03 ? 1649 TYR   A OH   1 
ATOM   1367 N  N    . PHE   A 1 318  ? 196.048 171.884 207.067 1.00 212.08 ? 1650 PHE   A N    1 
ATOM   1368 C  CA   . PHE   A 1 318  ? 196.443 173.213 207.525 1.00 211.04 ? 1650 PHE   A CA   1 
ATOM   1369 C  C    . PHE   A 1 318  ? 195.464 174.273 207.040 1.00 208.93 ? 1650 PHE   A C    1 
ATOM   1370 O  O    . PHE   A 1 318  ? 195.226 175.270 207.732 1.00 205.80 ? 1650 PHE   A O    1 
ATOM   1371 C  CB   . PHE   A 1 318  ? 197.869 173.538 207.070 1.00 211.54 ? 1650 PHE   A CB   1 
ATOM   1372 C  CG   . PHE   A 1 318  ? 198.865 172.434 207.323 1.00 211.97 ? 1650 PHE   A CG   1 
ATOM   1373 C  CD1  . PHE   A 1 318  ? 198.710 171.562 208.391 1.00 206.71 ? 1650 PHE   A CD1  1 
ATOM   1374 C  CD2  . PHE   A 1 318  ? 199.966 172.279 206.495 1.00 211.72 ? 1650 PHE   A CD2  1 
ATOM   1375 C  CE1  . PHE   A 1 318  ? 199.626 170.553 208.622 1.00 203.40 ? 1650 PHE   A CE1  1 
ATOM   1376 C  CE2  . PHE   A 1 318  ? 200.886 171.270 206.721 1.00 212.14 ? 1650 PHE   A CE2  1 
ATOM   1377 C  CZ   . PHE   A 1 318  ? 200.716 170.409 207.787 1.00 208.35 ? 1650 PHE   A CZ   1 
ATOM   1378 N  N    . LYS   A 1 319  ? 194.885 174.078 205.852 1.00 209.77 ? 1651 LYS   A N    1 
ATOM   1379 C  CA   . LYS   A 1 319  ? 193.850 174.992 205.381 1.00 208.07 ? 1651 LYS   A CA   1 
ATOM   1380 C  C    . LYS   A 1 319  ? 192.649 174.988 206.318 1.00 209.43 ? 1651 LYS   A C    1 
ATOM   1381 O  O    . LYS   A 1 319  ? 192.112 176.049 206.658 1.00 208.14 ? 1651 LYS   A O    1 
ATOM   1382 C  CB   . LYS   A 1 319  ? 193.427 174.619 203.961 1.00 199.90 ? 1651 LYS   A CB   1 
ATOM   1383 N  N    . LEU   A 1 320  ? 192.210 173.801 206.745 1.00 210.96 ? 1652 LEU   A N    1 
ATOM   1384 C  CA   . LEU   A 1 320  ? 191.167 173.723 207.763 1.00 210.45 ? 1652 LEU   A CA   1 
ATOM   1385 C  C    . LEU   A 1 320  ? 191.665 174.261 209.098 1.00 208.12 ? 1652 LEU   A C    1 
ATOM   1386 O  O    . LEU   A 1 320  ? 190.919 174.928 209.823 1.00 201.64 ? 1652 LEU   A O    1 
ATOM   1387 C  CB   . LEU   A 1 320  ? 190.683 172.281 207.909 1.00 212.73 ? 1652 LEU   A CB   1 
ATOM   1388 N  N    . LEU   A 1 321  ? 192.922 173.968 209.442 1.00 210.25 ? 1653 LEU   A N    1 
ATOM   1389 C  CA   . LEU   A 1 321  ? 193.496 174.499 210.674 1.00 206.95 ? 1653 LEU   A CA   1 
ATOM   1390 C  C    . LEU   A 1 321  ? 193.607 176.017 210.620 1.00 201.80 ? 1653 LEU   A C    1 
ATOM   1391 O  O    . LEU   A 1 321  ? 193.365 176.701 211.621 1.00 194.39 ? 1653 LEU   A O    1 
ATOM   1392 C  CB   . LEU   A 1 321  ? 194.865 173.868 210.928 1.00 205.61 ? 1653 LEU   A CB   1 
ATOM   1393 N  N    . GLU   A 1 322  ? 193.982 176.563 209.459 1.00 204.25 ? 1654 GLU   A N    1 
ATOM   1394 C  CA   . GLU   A 1 322  ? 194.067 178.014 209.320 1.00 203.13 ? 1654 GLU   A CA   1 
ATOM   1395 C  C    . GLU   A 1 322  ? 192.699 178.665 209.475 1.00 204.51 ? 1654 GLU   A C    1 
ATOM   1396 O  O    . GLU   A 1 322  ? 192.596 179.812 209.927 1.00 198.31 ? 1654 GLU   A O    1 
ATOM   1397 C  CB   . GLU   A 1 322  ? 194.684 178.379 207.969 1.00 202.74 ? 1654 GLU   A CB   1 
ATOM   1398 N  N    . LYS   A 1 323  ? 191.634 177.948 209.107 1.00 205.89 ? 1655 LYS   A N    1 
ATOM   1399 C  CA   . LYS   A 1 323  ? 190.284 178.476 209.265 1.00 202.01 ? 1655 LYS   A CA   1 
ATOM   1400 C  C    . LYS   A 1 323  ? 189.890 178.640 210.725 1.00 199.39 ? 1655 LYS   A C    1 
ATOM   1401 O  O    . LYS   A 1 323  ? 188.897 179.319 211.008 1.00 198.00 ? 1655 LYS   A O    1 
ATOM   1402 C  CB   . LYS   A 1 323  ? 189.276 177.568 208.557 1.00 197.95 ? 1655 LYS   A CB   1 
ATOM   1403 N  N    . PHE   A 1 324  ? 190.632 178.036 211.653 1.00 195.87 ? 1656 PHE   A N    1 
ATOM   1404 C  CA   . PHE   A 1 324  ? 190.372 178.183 213.080 1.00 188.85 ? 1656 PHE   A CA   1 
ATOM   1405 C  C    . PHE   A 1 324  ? 191.436 179.034 213.763 1.00 185.22 ? 1656 PHE   A C    1 
ATOM   1406 O  O    . PHE   A 1 324  ? 191.716 178.839 214.951 1.00 179.83 ? 1656 PHE   A O    1 
ATOM   1407 C  CB   . PHE   A 1 324  ? 190.263 176.812 213.746 1.00 184.58 ? 1656 PHE   A CB   1 
ATOM   1408 C  CG   . PHE   A 1 324  ? 188.959 176.120 213.481 1.00 186.48 ? 1656 PHE   A CG   1 
ATOM   1409 C  CD1  . PHE   A 1 324  ? 188.884 174.738 213.444 1.00 185.69 ? 1656 PHE   A CD1  1 
ATOM   1410 C  CD2  . PHE   A 1 324  ? 187.806 176.855 213.259 1.00 191.04 ? 1656 PHE   A CD2  1 
ATOM   1411 C  CE1  . PHE   A 1 324  ? 187.685 174.102 213.194 1.00 184.08 ? 1656 PHE   A CE1  1 
ATOM   1412 C  CE2  . PHE   A 1 324  ? 186.603 176.225 213.010 1.00 192.28 ? 1656 PHE   A CE2  1 
ATOM   1413 C  CZ   . PHE   A 1 324  ? 186.543 174.846 212.977 1.00 188.00 ? 1656 PHE   A CZ   1 
ATOM   1414 N  N    . GLN   A 1 325  ? 192.051 179.957 213.021 1.00 186.32 ? 1657 GLN   A N    1 
ATOM   1415 C  CA   . GLN   A 1 325  ? 193.021 180.920 213.532 1.00 180.27 ? 1657 GLN   A CA   1 
ATOM   1416 C  C    . GLN   A 1 325  ? 194.258 180.258 214.125 1.00 179.74 ? 1657 GLN   A C    1 
ATOM   1417 O  O    . GLN   A 1 325  ? 195.047 180.917 214.809 1.00 175.54 ? 1657 GLN   A O    1 
ATOM   1418 C  CB   . GLN   A 1 325  ? 192.383 181.854 214.568 1.00 172.36 ? 1657 GLN   A CB   1 
ATOM   1419 N  N    . ILE   A 1 326  ? 194.448 178.963 213.875 1.00 185.04 ? 1658 ILE   A N    1 
ATOM   1420 C  CA   . ILE   A 1 326  ? 195.616 178.271 214.407 1.00 180.95 ? 1658 ILE   A CA   1 
ATOM   1421 C  C    . ILE   A 1 326  ? 196.881 178.745 213.702 1.00 174.71 ? 1658 ILE   A C    1 
ATOM   1422 O  O    . ILE   A 1 326  ? 197.913 178.990 214.340 1.00 162.84 ? 1658 ILE   A O    1 
ATOM   1423 C  CB   . ILE   A 1 326  ? 195.427 176.749 214.282 1.00 181.03 ? 1658 ILE   A CB   1 
ATOM   1424 C  CG1  . ILE   A 1 326  ? 194.171 176.310 215.038 1.00 176.33 ? 1658 ILE   A CG1  1 
ATOM   1425 C  CG2  . ILE   A 1 326  ? 196.649 176.015 214.807 1.00 177.18 ? 1658 ILE   A CG2  1 
ATOM   1426 C  CD1  . ILE   A 1 326  ? 194.210 176.603 216.520 1.00 164.71 ? 1658 ILE   A CD1  1 
ATOM   1427 N  N    . ALA   A 1 327  ? 196.819 178.895 212.382 1.00 178.40 ? 1659 ALA   A N    1 
ATOM   1428 C  CA   . ALA   A 1 327  ? 197.970 179.288 211.589 1.00 167.79 ? 1659 ALA   A CA   1 
ATOM   1429 C  C    . ALA   A 1 327  ? 198.210 180.792 211.684 1.00 161.43 ? 1659 ALA   A C    1 
ATOM   1430 O  O    . ALA   A 1 327  ? 197.507 181.525 212.384 1.00 157.84 ? 1659 ALA   A O    1 
ATOM   1431 C  CB   . ALA   A 1 327  ? 197.781 178.873 210.131 1.00 162.09 ? 1659 ALA   A CB   1 
ATOM   1432 N  N    . LEU   A 1 328  ? 199.234 181.246 210.969 1.00 163.48 ? 1660 LEU   A N    1 
ATOM   1433 C  CA   . LEU   A 1 328  ? 199.620 182.653 210.959 1.00 158.38 ? 1660 LEU   A CA   1 
ATOM   1434 C  C    . LEU   A 1 328  ? 198.993 183.393 209.783 1.00 145.16 ? 1660 LEU   A C    1 
ATOM   1435 O  O    . LEU   A 1 328  ? 199.181 184.600 209.627 1.00 126.35 ? 1660 LEU   A O    1 
ATOM   1436 C  CB   . LEU   A 1 328  ? 201.146 182.792 210.912 1.00 155.95 ? 1660 LEU   A CB   1 
ATOM   1437 C  CG   . LEU   A 1 328  ? 201.893 182.469 209.611 1.00 151.68 ? 1660 LEU   A CG   1 
ATOM   1438 C  CD1  . LEU   A 1 328  ? 203.309 183.027 209.669 1.00 140.82 ? 1660 LEU   A CD1  1 
ATOM   1439 C  CD2  . LEU   A 1 328  ? 201.929 180.974 209.325 1.00 149.98 ? 1660 LEU   A CD2  1 
ATOM   1440 N  N    . LEU   A 1 336  ? 200.532 181.033 213.677 1.00 148.31 ? 1668 LEU   A N    1 
ATOM   1441 C  CA   . LEU   A 1 336  ? 200.951 181.820 214.827 1.00 152.94 ? 1668 LEU   A CA   1 
ATOM   1442 C  C    . LEU   A 1 336  ? 201.019 180.940 216.062 1.00 157.62 ? 1668 LEU   A C    1 
ATOM   1443 O  O    . LEU   A 1 336  ? 201.674 181.289 217.045 1.00 157.06 ? 1668 LEU   A O    1 
ATOM   1444 C  CB   . LEU   A 1 336  ? 199.995 182.990 215.062 1.00 149.25 ? 1668 LEU   A CB   1 
ATOM   1445 N  N    . VAL   A 1 337  ? 200.336 179.800 215.994 1.00 155.69 ? 1669 VAL   A N    1 
ATOM   1446 C  CA   . VAL   A 1 337  ? 200.292 178.828 217.084 1.00 155.04 ? 1669 VAL   A CA   1 
ATOM   1447 C  C    . VAL   A 1 337  ? 199.792 179.528 218.343 1.00 155.77 ? 1669 VAL   A C    1 
ATOM   1448 O  O    . VAL   A 1 337  ? 200.570 179.736 219.286 1.00 153.88 ? 1669 VAL   A O    1 
ATOM   1449 C  CB   . VAL   A 1 337  ? 201.664 178.173 217.307 1.00 153.36 ? 1669 VAL   A CB   1 
ATOM   1450 N  N    . PRO   A 1 338  ? 198.515 179.916 218.396 1.00 155.53 ? 1670 PRO   A N    1 
ATOM   1451 C  CA   . PRO   A 1 338  ? 198.037 180.704 219.542 1.00 151.22 ? 1670 PRO   A CA   1 
ATOM   1452 C  C    . PRO   A 1 338  ? 198.176 179.995 220.873 1.00 148.85 ? 1670 PRO   A C    1 
ATOM   1453 O  O    . PRO   A 1 338  ? 198.358 180.657 221.901 1.00 145.90 ? 1670 PRO   A O    1 
ATOM   1454 C  CB   . PRO   A 1 338  ? 196.567 180.964 219.191 1.00 145.00 ? 1670 PRO   A CB   1 
ATOM   1455 C  CG   . PRO   A 1 338  ? 196.189 179.826 218.314 1.00 150.07 ? 1670 PRO   A CG   1 
ATOM   1456 C  CD   . PRO   A 1 338  ? 197.414 179.494 217.514 1.00 154.02 ? 1670 PRO   A CD   1 
ATOM   1457 N  N    . SER   A 1 339  ? 198.096 178.671 220.893 1.00 149.31 ? 1671 SER   A N    1 
ATOM   1458 C  CA   . SER   A 1 339  ? 198.232 177.937 222.140 1.00 145.08 ? 1671 SER   A CA   1 
ATOM   1459 C  C    . SER   A 1 339  ? 199.683 177.674 222.517 1.00 147.54 ? 1671 SER   A C    1 
ATOM   1460 O  O    . SER   A 1 339  ? 199.941 177.223 223.637 1.00 148.54 ? 1671 SER   A O    1 
ATOM   1461 C  CB   . SER   A 1 339  ? 197.474 176.612 222.047 1.00 145.21 ? 1671 SER   A CB   1 
ATOM   1462 O  OG   . SER   A 1 339  ? 196.084 176.835 221.892 1.00 141.68 ? 1671 SER   A OG   1 
ATOM   1463 N  N    . SER   A 1 340  ? 200.629 177.948 221.617 1.00 151.17 ? 1672 SER   A N    1 
ATOM   1464 C  CA   . SER   A 1 340  ? 202.031 177.634 221.877 1.00 157.51 ? 1672 SER   A CA   1 
ATOM   1465 C  C    . SER   A 1 340  ? 202.592 178.475 223.018 1.00 156.56 ? 1672 SER   A C    1 
ATOM   1466 O  O    . SER   A 1 340  ? 203.199 177.945 223.955 1.00 155.74 ? 1672 SER   A O    1 
ATOM   1467 C  CB   . SER   A 1 340  ? 202.855 177.839 220.605 1.00 156.74 ? 1672 SER   A CB   1 
ATOM   1468 O  OG   . SER   A 1 340  ? 202.877 179.207 220.234 1.00 152.40 ? 1672 SER   A OG   1 
ATOM   1469 N  N    . LEU   A 1 341  ? 202.403 179.789 222.954 1.00 149.13 ? 1673 LEU   A N    1 
ATOM   1470 C  CA   . LEU   A 1 341  ? 202.871 180.677 224.012 1.00 142.67 ? 1673 LEU   A CA   1 
ATOM   1471 C  C    . LEU   A 1 341  ? 201.920 180.555 225.194 1.00 142.21 ? 1673 LEU   A C    1 
ATOM   1472 O  O    . LEU   A 1 341  ? 200.702 180.457 225.014 1.00 142.62 ? 1673 LEU   A O    1 
ATOM   1473 C  CB   . LEU   A 1 341  ? 202.967 182.119 223.524 1.00 137.45 ? 1673 LEU   A CB   1 
ATOM   1474 C  CG   . LEU   A 1 341  ? 201.693 182.930 223.288 1.00 137.69 ? 1673 LEU   A CG   1 
ATOM   1475 C  CD1  . LEU   A 1 341  ? 202.040 184.403 223.185 1.00 131.58 ? 1673 LEU   A CD1  1 
ATOM   1476 C  CD2  . LEU   A 1 341  ? 200.964 182.472 222.040 1.00 141.27 ? 1673 LEU   A CD2  1 
ATOM   1477 N  N    . SER   A 1 342  ? 202.474 180.528 226.400 1.00 140.83 ? 1674 SER   A N    1 
ATOM   1478 C  CA   . SER   A 1 342  ? 201.670 180.389 227.604 1.00 141.24 ? 1674 SER   A CA   1 
ATOM   1479 C  C    . SER   A 1 342  ? 202.181 181.301 228.712 1.00 140.86 ? 1674 SER   A C    1 
ATOM   1480 O  O    . SER   A 1 342  ? 202.715 180.831 229.716 1.00 141.66 ? 1674 SER   A O    1 
ATOM   1481 C  CB   . SER   A 1 342  ? 201.664 178.935 228.074 1.00 145.71 ? 1674 SER   A CB   1 
ATOM   1482 O  OG   . SER   A 1 342  ? 202.956 178.531 228.489 1.00 152.61 ? 1674 SER   A OG   1 
ATOM   1483 N  N    . HIS   A 1 352  ? 209.224 204.628 226.597 1.00 115.71 ? 1684 HIS   A N    1 
ATOM   1484 C  CA   . HIS   A 1 352  ? 209.312 205.853 227.383 1.00 125.28 ? 1684 HIS   A CA   1 
ATOM   1485 C  C    . HIS   A 1 352  ? 207.999 206.621 227.334 1.00 128.61 ? 1684 HIS   A C    1 
ATOM   1486 O  O    . HIS   A 1 352  ? 207.862 207.594 226.595 1.00 130.61 ? 1684 HIS   A O    1 
ATOM   1487 C  CB   . HIS   A 1 352  ? 210.457 206.733 226.881 1.00 127.25 ? 1684 HIS   A CB   1 
ATOM   1488 N  N    . CYS   A 1 353  ? 207.034 206.173 228.130 1.00 127.91 ? 1685 CYS   A N    1 
ATOM   1489 C  CA   . CYS   A 1 353  ? 205.715 206.788 228.130 1.00 125.35 ? 1685 CYS   A CA   1 
ATOM   1490 C  C    . CYS   A 1 353  ? 205.718 208.092 228.919 1.00 126.30 ? 1685 CYS   A C    1 
ATOM   1491 O  O    . CYS   A 1 353  ? 206.412 208.227 229.931 1.00 122.82 ? 1685 CYS   A O    1 
ATOM   1492 C  CB   . CYS   A 1 353  ? 204.682 205.826 228.716 1.00 124.17 ? 1685 CYS   A CB   1 
ATOM   1493 N  N    . GLU   A 1 354  ? 204.941 209.059 228.439 1.00 124.49 ? 1686 GLU   A N    1 
ATOM   1494 C  CA   . GLU   A 1 354  ? 204.715 210.316 229.134 1.00 124.53 ? 1686 GLU   A CA   1 
ATOM   1495 C  C    . GLU   A 1 354  ? 203.236 210.662 229.058 1.00 120.45 ? 1686 GLU   A C    1 
ATOM   1496 O  O    . GLU   A 1 354  ? 202.542 210.245 228.128 1.00 118.92 ? 1686 GLU   A O    1 
ATOM   1497 C  CB   . GLU   A 1 354  ? 205.555 211.448 228.539 1.00 115.19 ? 1686 GLU   A CB   1 
ATOM   1498 N  N    . ASN   A 1 355  ? 202.759 211.424 230.044 1.00 119.00 ? 1687 ASN   A N    1 
ATOM   1499 C  CA   . ASN   A 1 355  ? 201.334 211.726 230.131 1.00 114.64 ? 1687 ASN   A CA   1 
ATOM   1500 C  C    . ASN   A 1 355  ? 200.846 212.504 228.915 1.00 117.14 ? 1687 ASN   A C    1 
ATOM   1501 O  O    . ASN   A 1 355  ? 199.830 212.146 228.309 1.00 116.48 ? 1687 ASN   A O    1 
ATOM   1502 C  CB   . ASN   A 1 355  ? 201.053 212.509 231.414 1.00 115.39 ? 1687 ASN   A CB   1 
ATOM   1503 C  CG   . ASN   A 1 355  ? 199.571 212.686 231.689 1.00 113.60 ? 1687 ASN   A CG   1 
ATOM   1504 O  OD1  . ASN   A 1 355  ? 198.724 212.252 230.915 1.00 116.75 ? 1687 ASN   A OD1  1 
ATOM   1505 N  ND2  . ASN   A 1 355  ? 199.254 213.335 232.801 1.00 117.48 ? 1687 ASN   A ND2  1 
ATOM   1506 N  N    . SER   A 1 356  ? 201.557 213.566 228.536 1.00 118.07 ? 1688 SER   A N    1 
ATOM   1507 C  CA   . SER   A 1 356  ? 201.019 214.491 227.544 1.00 113.00 ? 1688 SER   A CA   1 
ATOM   1508 C  C    . SER   A 1 356  ? 201.118 213.936 226.128 1.00 105.06 ? 1688 SER   A C    1 
ATOM   1509 O  O    . SER   A 1 356  ? 200.218 214.152 225.309 1.00 103.66 ? 1688 SER   A O    1 
ATOM   1510 C  CB   . SER   A 1 356  ? 201.738 215.835 227.637 1.00 119.75 ? 1688 SER   A CB   1 
ATOM   1511 O  OG   . SER   A 1 356  ? 200.966 216.860 227.037 1.00 126.36 ? 1688 SER   A OG   1 
ATOM   1512 N  N    . GLU   A 1 357  ? 202.195 213.221 225.821 1.00 105.14 ? 1689 GLU   A N    1 
ATOM   1513 C  CA   . GLU   A 1 357  ? 202.503 212.864 224.443 1.00 107.82 ? 1689 GLU   A CA   1 
ATOM   1514 C  C    . GLU   A 1 357  ? 201.734 211.652 223.933 1.00 104.72 ? 1689 GLU   A C    1 
ATOM   1515 O  O    . GLU   A 1 357  ? 201.814 211.356 222.737 1.00 104.62 ? 1689 GLU   A O    1 
ATOM   1516 C  CB   . GLU   A 1 357  ? 204.002 212.600 224.299 1.00 117.35 ? 1689 GLU   A CB   1 
ATOM   1517 C  CG   . GLU   A 1 357  ? 204.493 211.450 225.155 1.00 119.57 ? 1689 GLU   A CG   1 
ATOM   1518 C  CD   . GLU   A 1 357  ? 205.751 210.808 224.614 1.00 127.92 ? 1689 GLU   A CD   1 
ATOM   1519 O  OE1  . GLU   A 1 357  ? 206.035 210.973 223.410 1.00 126.96 ? 1689 GLU   A OE1  1 
ATOM   1520 O  OE2  . GLU   A 1 357  ? 206.458 210.135 225.392 1.00 130.08 ? 1689 GLU   A OE2  1 
ATOM   1521 N  N    . ILE   A 1 358  ? 200.995 210.946 224.786 1.00 103.10 ? 1690 ILE   A N    1 
ATOM   1522 C  CA   . ILE   A 1 358  ? 200.352 209.694 224.408 1.00 92.47  ? 1690 ILE   A CA   1 
ATOM   1523 C  C    . ILE   A 1 358  ? 198.847 209.812 224.589 1.00 86.51  ? 1690 ILE   A C    1 
ATOM   1524 O  O    . ILE   A 1 358  ? 198.366 210.551 225.455 1.00 85.77  ? 1690 ILE   A O    1 
ATOM   1525 C  CB   . ILE   A 1 358  ? 200.912 208.502 225.211 1.00 91.77  ? 1690 ILE   A CB   1 
ATOM   1526 C  CG1  . ILE   A 1 358  ? 200.382 208.517 226.642 1.00 95.50  ? 1690 ILE   A CG1  1 
ATOM   1527 C  CG2  . ILE   A 1 358  ? 202.424 208.504 225.194 1.00 102.23 ? 1690 ILE   A CG2  1 
ATOM   1528 C  CD1  . ILE   A 1 358  ? 200.687 207.263 227.403 1.00 98.63  ? 1690 ILE   A CD1  1 
ATOM   1529 N  N    . ILE   A 1 359  ? 198.108 209.084 223.759 1.00 86.15  ? 1691 ILE   A N    1 
ATOM   1530 C  CA   . ILE   A 1 359  ? 196.652 209.048 223.806 1.00 76.70  ? 1691 ILE   A CA   1 
ATOM   1531 C  C    . ILE   A 1 359  ? 196.231 207.671 224.288 1.00 78.56  ? 1691 ILE   A C    1 
ATOM   1532 O  O    . ILE   A 1 359  ? 196.585 206.656 223.678 1.00 85.19  ? 1691 ILE   A O    1 
ATOM   1533 C  CB   . ILE   A 1 359  ? 196.044 209.345 222.428 1.00 61.09  ? 1691 ILE   A CB   1 
ATOM   1534 C  CG1  . ILE   A 1 359  ? 196.237 210.815 222.067 1.00 67.62  ? 1691 ILE   A CG1  1 
ATOM   1535 C  CG2  . ILE   A 1 359  ? 194.579 208.986 222.426 1.00 56.45  ? 1691 ILE   A CG2  1 
ATOM   1536 C  CD1  . ILE   A 1 359  ? 196.495 211.047 220.605 1.00 68.78  ? 1691 ILE   A CD1  1 
ATOM   1537 N  N    . ILE   A 1 360  ? 195.463 207.630 225.370 1.00 74.17  ? 1692 ILE   A N    1 
ATOM   1538 C  CA   . ILE   A 1 360  ? 195.052 206.380 225.992 1.00 69.05  ? 1692 ILE   A CA   1 
ATOM   1539 C  C    . ILE   A 1 360  ? 193.590 206.136 225.663 1.00 68.21  ? 1692 ILE   A C    1 
ATOM   1540 O  O    . ILE   A 1 360  ? 192.729 206.969 225.969 1.00 65.31  ? 1692 ILE   A O    1 
ATOM   1541 C  CB   . ILE   A 1 360  ? 195.277 206.404 227.513 1.00 71.00  ? 1692 ILE   A CB   1 
ATOM   1542 C  CG1  . ILE   A 1 360  ? 196.747 206.632 227.822 1.00 80.20  ? 1692 ILE   A CG1  1 
ATOM   1543 C  CG2  . ILE   A 1 360  ? 194.840 205.109 228.132 1.00 64.97  ? 1692 ILE   A CG2  1 
ATOM   1544 C  CD1  . ILE   A 1 360  ? 197.606 205.545 227.275 1.00 74.77  ? 1692 ILE   A CD1  1 
ATOM   1545 N  N    . ARG   A 1 361  ? 193.316 204.996 225.043 1.00 62.44  ? 1693 ARG   A N    1 
ATOM   1546 C  CA   . ARG   A 1 361  ? 191.961 204.583 224.734 1.00 53.38  ? 1693 ARG   A CA   1 
ATOM   1547 C  C    . ARG   A 1 361  ? 191.676 203.327 225.528 1.00 53.45  ? 1693 ARG   A C    1 
ATOM   1548 O  O    . ARG   A 1 361  ? 192.370 202.320 225.370 1.00 58.40  ? 1693 ARG   A O    1 
ATOM   1549 C  CB   . ARG   A 1 361  ? 191.787 204.319 223.247 1.00 54.64  ? 1693 ARG   A CB   1 
ATOM   1550 C  CG   . ARG   A 1 361  ? 190.443 203.760 222.890 1.00 56.95  ? 1693 ARG   A CG   1 
ATOM   1551 C  CD   . ARG   A 1 361  ? 189.509 204.891 222.578 1.00 52.02  ? 1693 ARG   A CD   1 
ATOM   1552 N  NE   . ARG   A 1 361  ? 190.122 205.799 221.621 1.00 55.84  ? 1693 ARG   A NE   1 
ATOM   1553 C  CZ   . ARG   A 1 361  ? 189.483 206.789 221.019 1.00 60.35  ? 1693 ARG   A CZ   1 
ATOM   1554 N  NH1  . ARG   A 1 361  ? 188.204 207.021 221.247 1.00 53.75  ? 1693 ARG   A NH1  1 
ATOM   1555 N  NH2  . ARG   A 1 361  ? 190.144 207.562 220.164 1.00 58.53  ? 1693 ARG   A NH2  1 
ATOM   1556 N  N    . LEU   A 1 362  ? 190.657 203.389 226.369 1.00 56.56  ? 1694 LEU   A N    1 
ATOM   1557 C  CA   . LEU   A 1 362  ? 190.340 202.337 227.324 1.00 49.90  ? 1694 LEU   A CA   1 
ATOM   1558 C  C    . LEU   A 1 362  ? 189.027 201.691 226.907 1.00 67.27  ? 1694 LEU   A C    1 
ATOM   1559 O  O    . LEU   A 1 362  ? 188.012 202.378 226.760 1.00 71.63  ? 1694 LEU   A O    1 
ATOM   1560 C  CB   . LEU   A 1 362  ? 190.245 202.923 228.728 1.00 40.87  ? 1694 LEU   A CB   1 
ATOM   1561 C  CG   . LEU   A 1 362  ? 189.983 202.013 229.915 1.00 54.24  ? 1694 LEU   A CG   1 
ATOM   1562 C  CD1  . LEU   A 1 362  ? 191.112 201.046 230.065 1.00 67.39  ? 1694 LEU   A CD1  1 
ATOM   1563 C  CD2  . LEU   A 1 362  ? 189.822 202.837 231.174 1.00 60.13  ? 1694 LEU   A CD2  1 
ATOM   1564 N  N    . TYR   A 1 363  ? 189.052 200.379 226.701 1.00 67.65  ? 1695 TYR   A N    1 
ATOM   1565 C  CA   . TYR   A 1 363  ? 187.846 199.581 226.515 1.00 59.32  ? 1695 TYR   A CA   1 
ATOM   1566 C  C    . TYR   A 1 363  ? 187.563 198.774 227.769 1.00 69.83  ? 1695 TYR   A C    1 
ATOM   1567 O  O    . TYR   A 1 363  ? 188.321 197.863 228.113 1.00 63.62  ? 1695 TYR   A O    1 
ATOM   1568 C  CB   . TYR   A 1 363  ? 187.961 198.650 225.314 1.00 44.41  ? 1695 TYR   A CB   1 
ATOM   1569 C  CG   . TYR   A 1 363  ? 187.941 199.322 223.974 1.00 51.17  ? 1695 TYR   A CG   1 
ATOM   1570 C  CD1  . TYR   A 1 363  ? 187.514 200.631 223.837 1.00 55.91  ? 1695 TYR   A CD1  1 
ATOM   1571 C  CD2  . TYR   A 1 363  ? 188.323 198.637 222.837 1.00 55.08  ? 1695 TYR   A CD2  1 
ATOM   1572 C  CE1  . TYR   A 1 363  ? 187.479 201.233 222.603 1.00 57.20  ? 1695 TYR   A CE1  1 
ATOM   1573 C  CE2  . TYR   A 1 363  ? 188.297 199.232 221.607 1.00 44.33  ? 1695 TYR   A CE2  1 
ATOM   1574 C  CZ   . TYR   A 1 363  ? 187.876 200.526 221.493 1.00 47.93  ? 1695 TYR   A CZ   1 
ATOM   1575 O  OH   . TYR   A 1 363  ? 187.849 201.111 220.255 1.00 54.75  ? 1695 TYR   A OH   1 
ATOM   1576 N  N    . GLU   A 1 364  ? 186.461 199.092 228.439 1.00 81.98  ? 1696 GLU   A N    1 
ATOM   1577 C  CA   . GLU   A 1 364  ? 185.942 198.230 229.484 1.00 89.77  ? 1696 GLU   A CA   1 
ATOM   1578 C  C    . GLU   A 1 364  ? 184.904 197.318 228.860 1.00 100.24 ? 1696 GLU   A C    1 
ATOM   1579 O  O    . GLU   A 1 364  ? 184.086 197.761 228.047 1.00 103.98 ? 1696 GLU   A O    1 
ATOM   1580 C  CB   . GLU   A 1 364  ? 185.308 198.996 230.644 1.00 86.74  ? 1696 GLU   A CB   1 
ATOM   1581 C  CG   . GLU   A 1 364  ? 184.049 199.771 230.349 1.00 86.33  ? 1696 GLU   A CG   1 
ATOM   1582 C  CD   . GLU   A 1 364  ? 183.570 200.506 231.580 1.00 94.70  ? 1696 GLU   A CD   1 
ATOM   1583 O  OE1  . GLU   A 1 364  ? 184.254 200.410 232.620 1.00 90.93  ? 1696 GLU   A OE1  1 
ATOM   1584 O  OE2  . GLU   A 1 364  ? 182.500 201.142 231.534 1.00 105.02 ? 1696 GLU   A OE2  1 
ATOM   1585 N  N    . MET   A 1 365  ? 184.962 196.043 229.215 1.00 96.03  ? 1697 MET   A N    1 
ATOM   1586 C  CA   . MET   A 1 365  ? 183.941 195.096 228.817 1.00 92.74  ? 1697 MET   A CA   1 
ATOM   1587 C  C    . MET   A 1 365  ? 183.851 194.043 229.904 1.00 99.93  ? 1697 MET   A C    1 
ATOM   1588 O  O    . MET   A 1 365  ? 184.863 193.727 230.542 1.00 98.33  ? 1697 MET   A O    1 
ATOM   1589 C  CB   . MET   A 1 365  ? 184.257 194.476 227.449 1.00 83.55  ? 1697 MET   A CB   1 
ATOM   1590 C  CG   . MET   A 1 365  ? 185.510 193.641 227.410 1.00 85.87  ? 1697 MET   A CG   1 
ATOM   1591 S  SD   . MET   A 1 365  ? 185.838 193.067 225.740 1.00 98.78  ? 1697 MET   A SD   1 
ATOM   1592 C  CE   . MET   A 1 365  ? 186.392 194.589 224.995 1.00 87.59  ? 1697 MET   A CE   1 
ATOM   1593 N  N    . PRO   A 1 366  ? 182.655 193.519 230.173 1.00 108.60 ? 1698 PRO   A N    1 
ATOM   1594 C  CA   . PRO   A 1 366  ? 182.505 192.586 231.299 1.00 109.34 ? 1698 PRO   A CA   1 
ATOM   1595 C  C    . PRO   A 1 366  ? 183.361 191.343 231.170 1.00 106.40 ? 1698 PRO   A C    1 
ATOM   1596 O  O    . PRO   A 1 366  ? 183.768 190.771 232.189 1.00 105.67 ? 1698 PRO   A O    1 
ATOM   1597 C  CB   . PRO   A 1 366  ? 181.008 192.249 231.270 1.00 117.25 ? 1698 PRO   A CB   1 
ATOM   1598 C  CG   . PRO   A 1 366  ? 180.373 193.417 230.592 1.00 112.80 ? 1698 PRO   A CG   1 
ATOM   1599 C  CD   . PRO   A 1 366  ? 181.361 193.850 229.553 1.00 111.90 ? 1698 PRO   A CD   1 
ATOM   1600 N  N    . TYR   A 1 367  ? 183.664 190.915 229.950 1.00 103.75 ? 1699 TYR   A N    1 
ATOM   1601 C  CA   . TYR   A 1 367  ? 184.356 189.656 229.744 1.00 102.78 ? 1699 TYR   A CA   1 
ATOM   1602 C  C    . TYR   A 1 367  ? 185.112 189.699 228.428 1.00 105.21 ? 1699 TYR   A C    1 
ATOM   1603 O  O    . TYR   A 1 367  ? 184.800 190.487 227.534 1.00 108.02 ? 1699 TYR   A O    1 
ATOM   1604 C  CB   . TYR   A 1 367  ? 183.362 188.490 229.781 1.00 107.46 ? 1699 TYR   A CB   1 
ATOM   1605 C  CG   . TYR   A 1 367  ? 182.191 188.669 228.844 1.00 115.73 ? 1699 TYR   A CG   1 
ATOM   1606 C  CD1  . TYR   A 1 367  ? 180.908 188.810 229.343 1.00 120.82 ? 1699 TYR   A CD1  1 
ATOM   1607 C  CD2  . TYR   A 1 367  ? 182.363 188.690 227.465 1.00 123.06 ? 1699 TYR   A CD2  1 
ATOM   1608 C  CE1  . TYR   A 1 367  ? 179.832 188.979 228.502 1.00 138.98 ? 1699 TYR   A CE1  1 
ATOM   1609 C  CE2  . TYR   A 1 367  ? 181.295 188.861 226.616 1.00 134.55 ? 1699 TYR   A CE2  1 
ATOM   1610 C  CZ   . TYR   A 1 367  ? 180.031 189.002 227.139 1.00 145.82 ? 1699 TYR   A CZ   1 
ATOM   1611 O  OH   . TYR   A 1 367  ? 178.963 189.172 226.294 1.00 143.84 ? 1699 TYR   A OH   1 
ATOM   1612 N  N    . PHE   A 1 368  ? 186.107 188.828 228.316 1.00 103.74 ? 1700 PHE   A N    1 
ATOM   1613 C  CA   . PHE   A 1 368  ? 186.797 188.635 227.054 1.00 100.84 ? 1700 PHE   A CA   1 
ATOM   1614 C  C    . PHE   A 1 368  ? 186.316 187.326 226.462 1.00 107.74 ? 1700 PHE   A C    1 
ATOM   1615 O  O    . PHE   A 1 368  ? 186.752 186.259 226.920 1.00 111.23 ? 1700 PHE   A O    1 
ATOM   1616 C  CB   . PHE   A 1 368  ? 188.304 188.600 227.264 1.00 95.50  ? 1700 PHE   A CB   1 
ATOM   1617 C  CG   . PHE   A 1 368  ? 188.909 189.945 227.493 1.00 83.07  ? 1700 PHE   A CG   1 
ATOM   1618 C  CD1  . PHE   A 1 368  ? 190.144 190.065 228.090 1.00 78.82  ? 1700 PHE   A CD1  1 
ATOM   1619 C  CD2  . PHE   A 1 368  ? 188.241 191.089 227.112 1.00 85.07  ? 1700 PHE   A CD2  1 
ATOM   1620 C  CE1  . PHE   A 1 368  ? 190.699 191.298 228.295 1.00 87.13  ? 1700 PHE   A CE1  1 
ATOM   1621 C  CE2  . PHE   A 1 368  ? 188.792 192.322 227.317 1.00 82.79  ? 1700 PHE   A CE2  1 
ATOM   1622 C  CZ   . PHE   A 1 368  ? 190.021 192.429 227.908 1.00 83.60  ? 1700 PHE   A CZ   1 
ATOM   1623 N  N    . PRO   A 1 369  ? 185.447 187.344 225.455 1.00 114.11 ? 1701 PRO   A N    1 
ATOM   1624 C  CA   . PRO   A 1 369  ? 184.862 186.092 224.969 1.00 129.96 ? 1701 PRO   A CA   1 
ATOM   1625 C  C    . PRO   A 1 369  ? 185.934 185.147 224.453 1.00 127.56 ? 1701 PRO   A C    1 
ATOM   1626 O  O    . PRO   A 1 369  ? 187.004 185.568 224.013 1.00 124.22 ? 1701 PRO   A O    1 
ATOM   1627 C  CB   . PRO   A 1 369  ? 183.925 186.550 223.845 1.00 126.08 ? 1701 PRO   A CB   1 
ATOM   1628 C  CG   . PRO   A 1 369  ? 183.599 187.963 224.191 1.00 107.58 ? 1701 PRO   A CG   1 
ATOM   1629 C  CD   . PRO   A 1 369  ? 184.853 188.519 224.798 1.00 101.44 ? 1701 PRO   A CD   1 
ATOM   1630 N  N    . MET   A 1 370  ? 185.652 183.853 224.554 1.00 125.46 ? 1702 MET   A N    1 
ATOM   1631 C  CA   . MET   A 1 370  ? 186.608 182.853 224.110 1.00 129.34 ? 1702 MET   A CA   1 
ATOM   1632 C  C    . MET   A 1 370  ? 186.850 183.004 222.615 1.00 136.78 ? 1702 MET   A C    1 
ATOM   1633 O  O    . MET   A 1 370  ? 185.907 183.023 221.820 1.00 139.66 ? 1702 MET   A O    1 
ATOM   1634 C  CB   . MET   A 1 370  ? 186.097 181.450 224.432 1.00 136.15 ? 1702 MET   A CB   1 
ATOM   1635 N  N    . GLY   A 1 371  ? 188.120 183.125 222.235 1.00 136.27 ? 1703 GLY   A N    1 
ATOM   1636 C  CA   . GLY   A 1 371  ? 188.512 183.334 220.866 1.00 129.84 ? 1703 GLY   A CA   1 
ATOM   1637 C  C    . GLY   A 1 371  ? 188.662 184.794 220.484 1.00 121.99 ? 1703 GLY   A C    1 
ATOM   1638 O  O    . GLY   A 1 371  ? 189.321 185.096 219.480 1.00 116.98 ? 1703 GLY   A O    1 
ATOM   1639 N  N    . PHE   A 1 372  ? 188.070 185.703 221.266 1.00 120.08 ? 1704 PHE   A N    1 
ATOM   1640 C  CA   . PHE   A 1 372  ? 188.202 187.132 220.998 1.00 106.04 ? 1704 PHE   A CA   1 
ATOM   1641 C  C    . PHE   A 1 372  ? 189.665 187.509 220.847 1.00 101.03 ? 1704 PHE   A C    1 
ATOM   1642 O  O    . PHE   A 1 372  ? 190.088 188.012 219.802 1.00 101.04 ? 1704 PHE   A O    1 
ATOM   1643 C  CB   . PHE   A 1 372  ? 187.541 187.937 222.125 1.00 100.56 ? 1704 PHE   A CB   1 
ATOM   1644 C  CG   . PHE   A 1 372  ? 187.536 189.437 221.911 1.00 104.61 ? 1704 PHE   A CG   1 
ATOM   1645 C  CD1  . PHE   A 1 372  ? 188.699 190.184 221.985 1.00 103.26 ? 1704 PHE   A CD1  1 
ATOM   1646 C  CD2  . PHE   A 1 372  ? 186.349 190.102 221.662 1.00 109.89 ? 1704 PHE   A CD2  1 
ATOM   1647 C  CE1  . PHE   A 1 372  ? 188.674 191.556 221.794 1.00 99.76  ? 1704 PHE   A CE1  1 
ATOM   1648 C  CE2  . PHE   A 1 372  ? 186.325 191.473 221.473 1.00 99.45  ? 1704 PHE   A CE2  1 
ATOM   1649 C  CZ   . PHE   A 1 372  ? 187.484 192.196 221.539 1.00 90.65  ? 1704 PHE   A CZ   1 
ATOM   1650 N  N    . TRP   A 1 373  ? 190.457 187.246 221.880 1.00 98.19  ? 1705 TRP   A N    1 
ATOM   1651 C  CA   . TRP   A 1 373  ? 191.847 187.670 221.860 1.00 100.67 ? 1705 TRP   A CA   1 
ATOM   1652 C  C    . TRP   A 1 373  ? 192.652 186.901 220.821 1.00 104.27 ? 1705 TRP   A C    1 
ATOM   1653 O  O    . TRP   A 1 373  ? 193.492 187.483 220.126 1.00 99.11  ? 1705 TRP   A O    1 
ATOM   1654 C  CB   . TRP   A 1 373  ? 192.454 187.504 223.247 1.00 89.21  ? 1705 TRP   A CB   1 
ATOM   1655 C  CG   . TRP   A 1 373  ? 192.386 188.754 224.029 1.00 81.48  ? 1705 TRP   A CG   1 
ATOM   1656 C  CD1  . TRP   A 1 373  ? 191.428 189.105 224.921 1.00 80.13  ? 1705 TRP   A CD1  1 
ATOM   1657 C  CD2  . TRP   A 1 373  ? 193.304 189.848 223.971 1.00 80.41  ? 1705 TRP   A CD2  1 
ATOM   1658 N  NE1  . TRP   A 1 373  ? 191.696 190.344 225.435 1.00 82.39  ? 1705 TRP   A NE1  1 
ATOM   1659 C  CE2  . TRP   A 1 373  ? 192.846 190.821 224.866 1.00 78.89  ? 1705 TRP   A CE2  1 
ATOM   1660 C  CE3  . TRP   A 1 373  ? 194.475 190.094 223.252 1.00 84.66  ? 1705 TRP   A CE3  1 
ATOM   1661 C  CZ2  . TRP   A 1 373  ? 193.518 192.018 225.067 1.00 80.46  ? 1705 TRP   A CZ2  1 
ATOM   1662 C  CZ3  . TRP   A 1 373  ? 195.132 191.284 223.446 1.00 77.31  ? 1705 TRP   A CZ3  1 
ATOM   1663 C  CH2  . TRP   A 1 373  ? 194.657 192.229 224.348 1.00 76.80  ? 1705 TRP   A CH2  1 
ATOM   1664 N  N    . SER   A 1 374  ? 192.410 185.594 220.698 1.00 106.94 ? 1706 SER   A N    1 
ATOM   1665 C  CA   . SER   A 1 374  ? 193.190 184.785 219.764 1.00 112.00 ? 1706 SER   A CA   1 
ATOM   1666 C  C    . SER   A 1 374  ? 192.964 185.228 218.324 1.00 111.40 ? 1706 SER   A C    1 
ATOM   1667 O  O    . SER   A 1 374  ? 193.861 185.102 217.483 1.00 116.37 ? 1706 SER   A O    1 
ATOM   1668 C  CB   . SER   A 1 374  ? 192.852 183.305 219.929 1.00 126.94 ? 1706 SER   A CB   1 
ATOM   1669 O  OG   . SER   A 1 374  ? 193.582 182.517 219.007 1.00 133.68 ? 1706 SER   A OG   1 
ATOM   1670 N  N    . ARG   A 1 375  ? 191.766 185.727 218.016 1.00 107.18 ? 1707 ARG   A N    1 
ATOM   1671 C  CA   . ARG   A 1 375  ? 191.502 186.270 216.687 1.00 112.58 ? 1707 ARG   A CA   1 
ATOM   1672 C  C    . ARG   A 1 375  ? 192.018 187.701 216.544 1.00 112.87 ? 1707 ARG   A C    1 
ATOM   1673 O  O    . ARG   A 1 375  ? 192.485 188.090 215.463 1.00 113.70 ? 1707 ARG   A O    1 
ATOM   1674 C  CB   . ARG   A 1 375  ? 190.002 186.196 216.413 1.00 106.21 ? 1707 ARG   A CB   1 
ATOM   1675 C  CG   . ARG   A 1 375  ? 189.460 187.044 215.272 1.00 112.28 ? 1707 ARG   A CG   1 
ATOM   1676 C  CD   . ARG   A 1 375  ? 189.087 188.418 215.795 1.00 107.91 ? 1707 ARG   A CD   1 
ATOM   1677 N  NE   . ARG   A 1 375  ? 188.321 188.294 217.025 1.00 113.12 ? 1707 ARG   A NE   1 
ATOM   1678 C  CZ   . ARG   A 1 375  ? 187.087 187.825 217.098 1.00 116.41 ? 1707 ARG   A CZ   1 
ATOM   1679 N  NH1  . ARG   A 1 375  ? 186.409 187.510 216.016 1.00 115.07 ? 1707 ARG   A NH1  1 
ATOM   1680 N  NH2  . ARG   A 1 375  ? 186.522 187.665 218.289 1.00 115.55 ? 1707 ARG   A NH2  1 
ATOM   1681 N  N    . LEU   A 1 376  ? 191.906 188.505 217.604 1.00 103.79 ? 1708 LEU   A N    1 
ATOM   1682 C  CA   . LEU   A 1 376  ? 192.377 189.881 217.537 1.00 97.63  ? 1708 LEU   A CA   1 
ATOM   1683 C  C    . LEU   A 1 376  ? 193.870 189.908 217.271 1.00 99.05  ? 1708 LEU   A C    1 
ATOM   1684 O  O    . LEU   A 1 376  ? 194.359 190.726 216.482 1.00 105.71 ? 1708 LEU   A O    1 
ATOM   1685 C  CB   . LEU   A 1 376  ? 192.051 190.599 218.847 1.00 96.51  ? 1708 LEU   A CB   1 
ATOM   1686 C  CG   . LEU   A 1 376  ? 192.361 192.082 219.039 1.00 80.86  ? 1708 LEU   A CG   1 
ATOM   1687 C  CD1  . LEU   A 1 376  ? 191.550 192.884 218.059 1.00 79.62  ? 1708 LEU   A CD1  1 
ATOM   1688 C  CD2  . LEU   A 1 376  ? 192.082 192.523 220.464 1.00 66.52  ? 1708 LEU   A CD2  1 
ATOM   1689 N  N    . ILE   A 1 377  ? 194.605 189.000 217.912 1.00 92.80  ? 1709 ILE   A N    1 
ATOM   1690 C  CA   . ILE   A 1 377  ? 196.037 188.881 217.677 1.00 97.35  ? 1709 ILE   A CA   1 
ATOM   1691 C  C    . ILE   A 1 377  ? 196.315 188.595 216.207 1.00 111.23 ? 1709 ILE   A C    1 
ATOM   1692 O  O    . ILE   A 1 377  ? 197.218 189.187 215.604 1.00 112.03 ? 1709 ILE   A O    1 
ATOM   1693 C  CB   . ILE   A 1 377  ? 196.624 187.785 218.581 1.00 88.41  ? 1709 ILE   A CB   1 
ATOM   1694 C  CG1  . ILE   A 1 377  ? 196.368 188.109 220.052 1.00 85.77  ? 1709 ILE   A CG1  1 
ATOM   1695 C  CG2  . ILE   A 1 377  ? 198.095 187.605 218.305 1.00 99.64  ? 1709 ILE   A CG2  1 
ATOM   1696 C  CD1  . ILE   A 1 377  ? 196.976 189.379 220.527 1.00 87.98  ? 1709 ILE   A CD1  1 
ATOM   1697 N  N    . ASN   A 1 378  ? 195.542 187.686 215.609 1.00 118.40 ? 1710 ASN   A N    1 
ATOM   1698 C  CA   . ASN   A 1 378  ? 195.744 187.343 214.205 1.00 116.32 ? 1710 ASN   A CA   1 
ATOM   1699 C  C    . ASN   A 1 378  ? 195.493 188.542 213.302 1.00 111.70 ? 1710 ASN   A C    1 
ATOM   1700 O  O    . ASN   A 1 378  ? 196.261 188.802 212.369 1.00 112.02 ? 1710 ASN   A O    1 
ATOM   1701 C  CB   . ASN   A 1 378  ? 194.832 186.179 213.812 1.00 118.86 ? 1710 ASN   A CB   1 
ATOM   1702 C  CG   . ASN   A 1 378  ? 195.534 184.836 213.881 1.00 135.69 ? 1710 ASN   A CG   1 
ATOM   1703 O  OD1  . ASN   A 1 378  ? 196.367 184.513 213.036 1.00 144.20 ? 1710 ASN   A OD1  1 
ATOM   1704 N  ND2  . ASN   A 1 378  ? 195.202 184.047 214.897 1.00 137.12 ? 1710 ASN   A ND2  1 
ATOM   1705 N  N    . ARG   A 1 379  ? 194.418 189.289 213.560 1.00 108.97 ? 1711 ARG   A N    1 
ATOM   1706 C  CA   . ARG   A 1 379  ? 194.064 190.355 212.624 1.00 110.98 ? 1711 ARG   A CA   1 
ATOM   1707 C  C    . ARG   A 1 379  ? 194.918 191.605 212.819 1.00 108.06 ? 1711 ARG   A C    1 
ATOM   1708 O  O    . ARG   A 1 379  ? 195.037 192.423 211.901 1.00 106.86 ? 1711 ARG   A O    1 
ATOM   1709 C  CB   . ARG   A 1 379  ? 192.575 190.684 212.716 1.00 106.21 ? 1711 ARG   A CB   1 
ATOM   1710 C  CG   . ARG   A 1 379  ? 192.169 191.881 211.873 1.00 97.45  ? 1711 ARG   A CG   1 
ATOM   1711 C  CD   . ARG   A 1 379  ? 190.702 191.893 211.594 1.00 89.48  ? 1711 ARG   A CD   1 
ATOM   1712 N  NE   . ARG   A 1 379  ? 189.933 191.718 212.812 1.00 90.34  ? 1711 ARG   A NE   1 
ATOM   1713 C  CZ   . ARG   A 1 379  ? 188.612 191.683 212.845 1.00 84.55  ? 1711 ARG   A CZ   1 
ATOM   1714 N  NH1  . ARG   A 1 379  ? 187.890 191.883 211.756 1.00 86.82  ? 1711 ARG   A NH1  1 
ATOM   1715 N  NH2  . ARG   A 1 379  ? 188.003 191.434 213.993 1.00 73.02  ? 1711 ARG   A NH2  1 
ATOM   1716 N  N    . LEU   A 1 380  ? 195.537 191.770 213.981 1.00 106.97 ? 1712 LEU   A N    1 
ATOM   1717 C  CA   . LEU   A 1 380  ? 196.514 192.845 214.132 1.00 113.37 ? 1712 LEU   A CA   1 
ATOM   1718 C  C    . LEU   A 1 380  ? 197.934 192.420 213.788 1.00 122.80 ? 1712 LEU   A C    1 
ATOM   1719 O  O    . LEU   A 1 380  ? 198.876 192.876 214.441 1.00 132.84 ? 1712 LEU   A O    1 
ATOM   1720 C  CB   . LEU   A 1 380  ? 196.457 193.448 215.540 1.00 107.46 ? 1712 LEU   A CB   1 
ATOM   1721 C  CG   . LEU   A 1 380  ? 195.320 194.449 215.778 1.00 101.02 ? 1712 LEU   A CG   1 
ATOM   1722 C  CD1  . LEU   A 1 380  ? 193.950 193.817 215.830 1.00 94.23  ? 1712 LEU   A CD1  1 
ATOM   1723 C  CD2  . LEU   A 1 380  ? 195.589 195.182 217.068 1.00 82.64  ? 1712 LEU   A CD2  1 
ATOM   1724 N  N    . LEU   A 1 381  ? 198.111 191.543 212.802 1.00 125.63 ? 1713 LEU   A N    1 
ATOM   1725 C  CA   . LEU   A 1 381  ? 199.411 191.335 212.178 1.00 128.26 ? 1713 LEU   A CA   1 
ATOM   1726 C  C    . LEU   A 1 381  ? 199.516 192.021 210.817 1.00 130.86 ? 1713 LEU   A C    1 
ATOM   1727 O  O    . LEU   A 1 381  ? 200.307 191.589 209.972 1.00 132.22 ? 1713 LEU   A O    1 
ATOM   1728 C  CB   . LEU   A 1 381  ? 199.716 189.843 212.050 1.00 122.88 ? 1713 LEU   A CB   1 
ATOM   1729 C  CG   . LEU   A 1 381  ? 199.745 189.025 213.343 1.00 118.00 ? 1713 LEU   A CG   1 
ATOM   1730 C  CD1  . LEU   A 1 381  ? 200.582 187.773 213.153 1.00 123.66 ? 1713 LEU   A CD1  1 
ATOM   1731 C  CD2  . LEU   A 1 381  ? 200.287 189.843 214.495 1.00 113.00 ? 1713 LEU   A CD2  1 
ATOM   1732 N  N    . GLU   A 1 382  ? 198.733 193.073 210.588 1.00 130.98 ? 1714 GLU   A N    1 
ATOM   1733 C  CA   . GLU   A 1 382  ? 198.726 193.744 209.297 1.00 138.88 ? 1714 GLU   A CA   1 
ATOM   1734 C  C    . GLU   A 1 382  ? 199.850 194.775 209.200 1.00 146.96 ? 1714 GLU   A C    1 
ATOM   1735 O  O    . GLU   A 1 382  ? 200.645 194.973 210.125 1.00 138.81 ? 1714 GLU   A O    1 
ATOM   1736 C  CB   . GLU   A 1 382  ? 197.381 194.420 209.044 1.00 135.91 ? 1714 GLU   A CB   1 
ATOM   1737 C  CG   . GLU   A 1 382  ? 196.186 193.537 209.294 1.00 128.98 ? 1714 GLU   A CG   1 
ATOM   1738 C  CD   . GLU   A 1 382  ? 196.123 192.358 208.349 1.00 129.43 ? 1714 GLU   A CD   1 
ATOM   1739 O  OE1  . GLU   A 1 382  ? 196.693 191.299 208.683 1.00 127.71 ? 1714 GLU   A OE1  1 
ATOM   1740 O  OE2  . GLU   A 1 382  ? 195.502 192.490 207.274 1.00 125.89 ? 1714 GLU   A OE2  1 
ATOM   1741 N  N    . ILE   A 1 383  ? 199.906 195.432 208.042 1.00 150.86 ? 1715 ILE   A N    1 
ATOM   1742 C  CA   . ILE   A 1 383  ? 200.893 196.460 207.732 1.00 152.00 ? 1715 ILE   A CA   1 
ATOM   1743 C  C    . ILE   A 1 383  ? 200.174 197.722 207.274 1.00 146.54 ? 1715 ILE   A C    1 
ATOM   1744 O  O    . ILE   A 1 383  ? 199.187 197.649 206.531 1.00 145.63 ? 1715 ILE   A O    1 
ATOM   1745 C  CB   . ILE   A 1 383  ? 201.900 195.978 206.670 1.00 148.94 ? 1715 ILE   A CB   1 
ATOM   1746 C  CG1  . ILE   A 1 383  ? 203.020 197.009 206.481 1.00 150.24 ? 1715 ILE   A CG1  1 
ATOM   1747 C  CG2  . ILE   A 1 383  ? 201.198 195.633 205.361 1.00 132.15 ? 1715 ILE   A CG2  1 
ATOM   1748 C  CD1  . ILE   A 1 383  ? 203.726 197.399 207.748 1.00 146.62 ? 1715 ILE   A CD1  1 
ATOM   1749 N  N    . SER   A 1 384  ? 200.652 198.872 207.747 1.00 147.83 ? 1716 SER   A N    1 
ATOM   1750 C  CA   . SER   A 1 384  ? 200.166 200.177 207.323 1.00 152.20 ? 1716 SER   A CA   1 
ATOM   1751 C  C    . SER   A 1 384  ? 201.120 201.243 207.834 1.00 151.75 ? 1716 SER   A C    1 
ATOM   1752 O  O    . SER   A 1 384  ? 201.536 201.192 208.998 1.00 150.46 ? 1716 SER   A O    1 
ATOM   1753 C  CB   . SER   A 1 384  ? 198.750 200.455 207.840 1.00 149.89 ? 1716 SER   A CB   1 
ATOM   1754 O  OG   . SER   A 1 384  ? 198.313 201.742 207.442 1.00 141.08 ? 1716 SER   A OG   1 
ATOM   1755 N  N    . PRO   A 1 385  ? 201.487 202.221 206.994 1.00 152.29 ? 1717 PRO   A N    1 
ATOM   1756 C  CA   . PRO   A 1 385  ? 202.352 203.338 207.392 1.00 146.51 ? 1717 PRO   A CA   1 
ATOM   1757 C  C    . PRO   A 1 385  ? 201.760 204.179 208.522 1.00 136.61 ? 1717 PRO   A C    1 
ATOM   1758 O  O    . PRO   A 1 385  ? 200.574 204.047 208.821 1.00 125.52 ? 1717 PRO   A O    1 
ATOM   1759 C  CB   . PRO   A 1 385  ? 202.468 204.165 206.108 1.00 145.50 ? 1717 PRO   A CB   1 
ATOM   1760 C  CG   . PRO   A 1 385  ? 202.201 203.194 205.009 1.00 142.67 ? 1717 PRO   A CG   1 
ATOM   1761 C  CD   . PRO   A 1 385  ? 201.172 202.255 205.556 1.00 147.01 ? 1717 PRO   A CD   1 
ATOM   1762 N  N    . ARG   A 1 399  ? 207.952 193.563 218.084 1.00 111.15 ? 1731 ARG   A N    1 
ATOM   1763 C  CA   . ARG   A 1 399  ? 206.638 193.016 217.766 1.00 110.90 ? 1731 ARG   A CA   1 
ATOM   1764 C  C    . ARG   A 1 399  ? 206.162 192.202 218.959 1.00 105.53 ? 1731 ARG   A C    1 
ATOM   1765 O  O    . ARG   A 1 399  ? 205.166 191.485 218.877 1.00 105.41 ? 1731 ARG   A O    1 
ATOM   1766 C  CB   . ARG   A 1 399  ? 206.688 192.130 216.518 1.00 105.45 ? 1731 ARG   A CB   1 
ATOM   1767 C  CG   . ARG   A 1 399  ? 206.553 192.849 215.179 1.00 109.08 ? 1731 ARG   A CG   1 
ATOM   1768 C  CD   . ARG   A 1 399  ? 207.341 194.144 215.154 1.00 115.50 ? 1731 ARG   A CD   1 
ATOM   1769 N  NE   . ARG   A 1 399  ? 207.617 194.598 213.800 1.00 126.80 ? 1731 ARG   A NE   1 
ATOM   1770 C  CZ   . ARG   A 1 399  ? 208.457 195.580 213.506 1.00 129.98 ? 1731 ARG   A CZ   1 
ATOM   1771 N  NH1  . ARG   A 1 399  ? 209.082 196.260 214.453 1.00 131.59 ? 1731 ARG   A NH1  1 
ATOM   1772 N  NH2  . ARG   A 1 399  ? 208.685 195.879 212.232 1.00 129.21 ? 1731 ARG   A NH2  1 
ATOM   1773 N  N    . MET   A 1 400  ? 206.897 192.326 220.063 1.00 103.34 ? 1732 MET   A N    1 
ATOM   1774 C  CA   . MET   A 1 400  ? 206.692 191.465 221.219 1.00 105.47 ? 1732 MET   A CA   1 
ATOM   1775 C  C    . MET   A 1 400  ? 205.256 191.554 221.706 1.00 107.71 ? 1732 MET   A C    1 
ATOM   1776 O  O    . MET   A 1 400  ? 204.683 192.642 221.790 1.00 107.31 ? 1732 MET   A O    1 
ATOM   1777 C  CB   . MET   A 1 400  ? 207.655 191.852 222.341 1.00 112.40 ? 1732 MET   A CB   1 
ATOM   1778 N  N    . TYR   A 1 401  ? 204.672 190.401 222.017 1.00 111.96 ? 1733 TYR   A N    1 
ATOM   1779 C  CA   . TYR   A 1 401  ? 203.273 190.353 222.405 1.00 112.49 ? 1733 TYR   A CA   1 
ATOM   1780 C  C    . TYR   A 1 401  ? 203.043 189.274 223.447 1.00 112.28 ? 1733 TYR   A C    1 
ATOM   1781 O  O    . TYR   A 1 401  ? 203.798 188.304 223.541 1.00 114.67 ? 1733 TYR   A O    1 
ATOM   1782 C  CB   . TYR   A 1 401  ? 202.368 190.134 221.187 1.00 106.49 ? 1733 TYR   A CB   1 
ATOM   1783 C  CG   . TYR   A 1 401  ? 202.654 188.924 220.326 1.00 98.48  ? 1733 TYR   A CG   1 
ATOM   1784 C  CD1  . TYR   A 1 401  ? 202.509 187.635 220.813 1.00 99.83  ? 1733 TYR   A CD1  1 
ATOM   1785 C  CD2  . TYR   A 1 401  ? 203.061 189.083 219.010 1.00 95.36  ? 1733 TYR   A CD2  1 
ATOM   1786 C  CE1  . TYR   A 1 401  ? 202.769 186.543 220.014 1.00 108.60 ? 1733 TYR   A CE1  1 
ATOM   1787 C  CE2  . TYR   A 1 401  ? 203.323 188.001 218.207 1.00 93.95  ? 1733 TYR   A CE2  1 
ATOM   1788 C  CZ   . TYR   A 1 401  ? 203.176 186.732 218.712 1.00 104.97 ? 1733 TYR   A CZ   1 
ATOM   1789 O  OH   . TYR   A 1 401  ? 203.438 185.648 217.908 1.00 107.65 ? 1733 TYR   A OH   1 
ATOM   1790 N  N    . TRP   A 1 402  ? 201.989 189.461 224.225 1.00 108.84 ? 1734 TRP   A N    1 
ATOM   1791 C  CA   . TRP   A 1 402  ? 201.550 188.495 225.210 1.00 115.46 ? 1734 TRP   A CA   1 
ATOM   1792 C  C    . TRP   A 1 402  ? 200.301 187.810 224.662 1.00 121.28 ? 1734 TRP   A C    1 
ATOM   1793 O  O    . TRP   A 1 402  ? 199.811 188.149 223.581 1.00 114.14 ? 1734 TRP   A O    1 
ATOM   1794 C  CB   . TRP   A 1 402  ? 201.303 189.209 226.542 1.00 108.76 ? 1734 TRP   A CB   1 
ATOM   1795 C  CG   . TRP   A 1 402  ? 202.527 189.289 227.415 1.00 119.25 ? 1734 TRP   A CG   1 
ATOM   1796 C  CD1  . TRP   A 1 402  ? 203.573 190.154 227.271 1.00 117.53 ? 1734 TRP   A CD1  1 
ATOM   1797 C  CD2  . TRP   A 1 402  ? 202.827 188.489 228.567 1.00 128.29 ? 1734 TRP   A CD2  1 
ATOM   1798 N  NE1  . TRP   A 1 402  ? 204.507 189.938 228.254 1.00 118.03 ? 1734 TRP   A NE1  1 
ATOM   1799 C  CE2  . TRP   A 1 402  ? 204.072 188.922 229.063 1.00 122.20 ? 1734 TRP   A CE2  1 
ATOM   1800 C  CE3  . TRP   A 1 402  ? 202.166 187.449 229.224 1.00 128.18 ? 1734 TRP   A CE3  1 
ATOM   1801 C  CZ2  . TRP   A 1 402  ? 204.667 188.351 230.183 1.00 118.75 ? 1734 TRP   A CZ2  1 
ATOM   1802 C  CZ3  . TRP   A 1 402  ? 202.760 186.884 230.336 1.00 125.06 ? 1734 TRP   A CZ3  1 
ATOM   1803 C  CH2  . TRP   A 1 402  ? 203.997 187.335 230.803 1.00 119.71 ? 1734 TRP   A CH2  1 
ATOM   1804 N  N    . ARG   A 1 403  ? 199.770 186.835 225.396 1.00 124.90 ? 1735 ARG   A N    1 
ATOM   1805 C  CA   . ARG   A 1 403  ? 198.451 186.306 225.080 1.00 118.11 ? 1735 ARG   A CA   1 
ATOM   1806 C  C    . ARG   A 1 403  ? 197.370 187.325 225.377 1.00 100.86 ? 1735 ARG   A C    1 
ATOM   1807 O  O    . ARG   A 1 403  ? 196.273 187.241 224.822 1.00 89.86  ? 1735 ARG   A O    1 
ATOM   1808 C  CB   . ARG   A 1 403  ? 198.178 185.016 225.852 1.00 121.29 ? 1735 ARG   A CB   1 
ATOM   1809 C  CG   . ARG   A 1 403  ? 198.896 183.810 225.300 1.00 123.65 ? 1735 ARG   A CG   1 
ATOM   1810 C  CD   . ARG   A 1 403  ? 199.394 182.922 226.415 1.00 127.53 ? 1735 ARG   A CD   1 
ATOM   1811 N  NE   . ARG   A 1 403  ? 200.308 183.623 227.306 1.00 129.32 ? 1735 ARG   A NE   1 
ATOM   1812 C  CZ   . ARG   A 1 403  ? 200.021 183.948 228.558 1.00 129.75 ? 1735 ARG   A CZ   1 
ATOM   1813 N  NH1  . ARG   A 1 403  ? 198.855 183.640 229.102 1.00 131.87 ? 1735 ARG   A NH1  1 
ATOM   1814 N  NH2  . ARG   A 1 403  ? 200.926 184.592 229.284 1.00 122.48 ? 1735 ARG   A NH2  1 
ATOM   1815 N  N    . GLN   A 1 404  ? 197.672 188.287 226.243 1.00 99.83  ? 1736 GLN   A N    1 
ATOM   1816 C  CA   . GLN   A 1 404  ? 196.819 189.438 226.519 1.00 99.64  ? 1736 GLN   A CA   1 
ATOM   1817 C  C    . GLN   A 1 404  ? 197.698 190.673 226.306 1.00 103.11 ? 1736 GLN   A C    1 
ATOM   1818 O  O    . GLN   A 1 404  ? 198.360 191.147 227.231 1.00 95.66  ? 1736 GLN   A O    1 
ATOM   1819 C  CB   . GLN   A 1 404  ? 196.246 189.379 227.926 1.00 102.94 ? 1736 GLN   A CB   1 
ATOM   1820 C  CG   . GLN   A 1 404  ? 195.439 188.122 228.250 1.00 111.73 ? 1736 GLN   A CG   1 
ATOM   1821 C  CD   . GLN   A 1 404  ? 194.144 188.012 227.463 1.00 101.01 ? 1736 GLN   A CD   1 
ATOM   1822 O  OE1  . GLN   A 1 404  ? 193.053 188.142 228.013 1.00 90.25  ? 1736 GLN   A OE1  1 
ATOM   1823 N  NE2  . GLN   A 1 404  ? 194.264 187.777 226.161 1.00 99.65  ? 1736 GLN   A NE2  1 
ATOM   1824 N  N    . GLY   A 1 405  ? 197.697 191.174 225.072 1.00 109.80 ? 1737 GLY   A N    1 
ATOM   1825 C  CA   . GLY   A 1 405  ? 198.503 192.315 224.684 1.00 105.83 ? 1737 GLY   A CA   1 
ATOM   1826 C  C    . GLY   A 1 405  ? 199.438 192.057 223.520 1.00 104.79 ? 1737 GLY   A C    1 
ATOM   1827 O  O    . GLY   A 1 405  ? 200.348 191.229 223.617 1.00 108.47 ? 1737 GLY   A O    1 
ATOM   1828 N  N    . ILE   A 1 406  ? 199.222 192.769 222.413 1.00 93.28  ? 1738 ILE   A N    1 
ATOM   1829 C  CA   . ILE   A 1 406  ? 200.091 192.684 221.243 1.00 94.90  ? 1738 ILE   A CA   1 
ATOM   1830 C  C    . ILE   A 1 406  ? 200.604 194.061 220.846 1.00 104.37 ? 1738 ILE   A C    1 
ATOM   1831 O  O    . ILE   A 1 406  ? 200.056 194.719 219.959 1.00 117.05 ? 1738 ILE   A O    1 
ATOM   1832 C  CB   . ILE   A 1 406  ? 199.379 191.974 220.071 1.00 95.44  ? 1738 ILE   A CB   1 
ATOM   1833 C  CG1  . ILE   A 1 406  ? 200.355 191.699 218.929 1.00 96.69  ? 1738 ILE   A CG1  1 
ATOM   1834 C  CG2  . ILE   A 1 406  ? 198.094 192.682 219.628 1.00 97.63  ? 1738 ILE   A CG2  1 
ATOM   1835 C  CD1  . ILE   A 1 406  ? 199.823 190.747 217.909 1.00 98.89  ? 1738 ILE   A CD1  1 
ATOM   1836 N  N    . TYR   A 1 407  ? 201.699 194.489 221.463 1.00 107.59 ? 1739 TYR   A N    1 
ATOM   1837 C  CA   . TYR   A 1 407  ? 202.171 195.841 221.205 1.00 109.42 ? 1739 TYR   A CA   1 
ATOM   1838 C  C    . TYR   A 1 407  ? 203.129 195.881 220.018 1.00 113.81 ? 1739 TYR   A C    1 
ATOM   1839 O  O    . TYR   A 1 407  ? 204.344 195.738 220.164 1.00 120.34 ? 1739 TYR   A O    1 
ATOM   1840 C  CB   . TYR   A 1 407  ? 202.758 196.435 222.492 1.00 107.08 ? 1739 TYR   A CB   1 
ATOM   1841 C  CG   . TYR   A 1 407  ? 203.966 195.749 223.087 1.00 116.74 ? 1739 TYR   A CG   1 
ATOM   1842 C  CD1  . TYR   A 1 407  ? 203.810 194.714 224.000 1.00 117.16 ? 1739 TYR   A CD1  1 
ATOM   1843 C  CD2  . TYR   A 1 407  ? 205.255 196.193 222.819 1.00 124.82 ? 1739 TYR   A CD2  1 
ATOM   1844 C  CE1  . TYR   A 1 407  ? 204.903 194.093 224.573 1.00 122.74 ? 1739 TYR   A CE1  1 
ATOM   1845 C  CE2  . TYR   A 1 407  ? 206.357 195.577 223.385 1.00 129.65 ? 1739 TYR   A CE2  1 
ATOM   1846 C  CZ   . TYR   A 1 407  ? 206.174 194.528 224.265 1.00 129.31 ? 1739 TYR   A CZ   1 
ATOM   1847 O  OH   . TYR   A 1 407  ? 207.263 193.914 224.841 1.00 130.27 ? 1739 TYR   A OH   1 
ATOM   1848 N  N    . LEU   A 1 408  ? 202.568 196.062 218.823 1.00 109.77 ? 1740 LEU   A N    1 
ATOM   1849 C  CA   . LEU   A 1 408  ? 203.364 196.135 217.606 1.00 116.18 ? 1740 LEU   A CA   1 
ATOM   1850 C  C    . LEU   A 1 408  ? 203.916 197.546 217.425 1.00 125.05 ? 1740 LEU   A C    1 
ATOM   1851 O  O    . LEU   A 1 408  ? 203.235 198.447 216.928 1.00 128.14 ? 1740 LEU   A O    1 
ATOM   1852 C  CB   . LEU   A 1 408  ? 202.535 195.647 216.405 1.00 120.10 ? 1740 LEU   A CB   1 
ATOM   1853 C  CG   . LEU   A 1 408  ? 201.501 196.466 215.625 1.00 119.85 ? 1740 LEU   A CG   1 
ATOM   1854 C  CD1  . LEU   A 1 408  ? 201.022 195.695 214.408 1.00 121.10 ? 1740 LEU   A CD1  1 
ATOM   1855 C  CD2  . LEU   A 1 408  ? 200.330 196.849 216.508 1.00 114.45 ? 1740 LEU   A CD2  1 
ATOM   1856 N  N    . ASN   A 1 409  ? 205.156 197.749 217.868 1.00 130.80 ? 1741 ASN   A N    1 
ATOM   1857 C  CA   . ASN   A 1 409  ? 205.770 199.070 217.895 1.00 142.39 ? 1741 ASN   A CA   1 
ATOM   1858 C  C    . ASN   A 1 409  ? 205.955 199.661 216.505 1.00 145.36 ? 1741 ASN   A C    1 
ATOM   1859 O  O    . ASN   A 1 409  ? 205.667 200.841 216.288 1.00 139.89 ? 1741 ASN   A O    1 
ATOM   1860 C  CB   . ASN   A 1 409  ? 207.117 199.003 218.615 1.00 146.30 ? 1741 ASN   A CB   1 
ATOM   1861 C  CG   . ASN   A 1 409  ? 207.539 200.339 219.181 1.00 147.93 ? 1741 ASN   A CG   1 
ATOM   1862 O  OD1  . ASN   A 1 409  ? 206.760 201.289 219.197 1.00 144.37 ? 1741 ASN   A OD1  1 
ATOM   1863 N  ND2  . ASN   A 1 409  ? 208.774 200.417 219.661 1.00 147.95 ? 1741 ASN   A ND2  1 
ATOM   1864 N  N    . TRP   A 1 410  ? 206.432 198.845 215.564 1.00 149.35 ? 1742 TRP   A N    1 
ATOM   1865 C  CA   . TRP   A 1 410  ? 206.777 199.305 214.223 1.00 150.34 ? 1742 TRP   A CA   1 
ATOM   1866 C  C    . TRP   A 1 410  ? 207.716 200.499 214.298 1.00 152.29 ? 1742 TRP   A C    1 
ATOM   1867 O  O    . TRP   A 1 410  ? 208.859 200.363 214.747 1.00 152.83 ? 1742 TRP   A O    1 
ATOM   1868 C  CB   . TRP   A 1 410  ? 205.516 199.631 213.416 1.00 146.78 ? 1742 TRP   A CB   1 
ATOM   1869 C  CG   . TRP   A 1 410  ? 204.929 198.401 212.810 1.00 145.86 ? 1742 TRP   A CG   1 
ATOM   1870 C  CD1  . TRP   A 1 410  ? 203.801 197.752 213.206 1.00 140.04 ? 1742 TRP   A CD1  1 
ATOM   1871 C  CD2  . TRP   A 1 410  ? 205.472 197.638 211.726 1.00 148.86 ? 1742 TRP   A CD2  1 
ATOM   1872 N  NE1  . TRP   A 1 410  ? 203.593 196.643 212.422 1.00 144.67 ? 1742 TRP   A NE1  1 
ATOM   1873 C  CE2  . TRP   A 1 410  ? 204.607 196.551 211.506 1.00 145.81 ? 1742 TRP   A CE2  1 
ATOM   1874 C  CE3  . TRP   A 1 410  ? 206.598 197.779 210.911 1.00 147.09 ? 1742 TRP   A CE3  1 
ATOM   1875 C  CZ2  . TRP   A 1 410  ? 204.835 195.604 210.510 1.00 143.00 ? 1742 TRP   A CZ2  1 
ATOM   1876 C  CZ3  . TRP   A 1 410  ? 206.822 196.839 209.920 1.00 146.00 ? 1742 TRP   A CZ3  1 
ATOM   1877 C  CH2  . TRP   A 1 410  ? 205.948 195.764 209.731 1.00 143.58 ? 1742 TRP   A CH2  1 
ATOM   1878 N  N    . SER   A 1 411  ? 207.256 201.662 213.855 1.00 152.86 ? 1743 SER   A N    1 
ATOM   1879 C  CA   . SER   A 1 411  ? 208.074 202.857 213.968 1.00 154.02 ? 1743 SER   A CA   1 
ATOM   1880 C  C    . SER   A 1 411  ? 208.367 203.140 215.439 1.00 151.71 ? 1743 SER   A C    1 
ATOM   1881 O  O    . SER   A 1 411  ? 207.472 203.020 216.283 1.00 147.90 ? 1743 SER   A O    1 
ATOM   1882 C  CB   . SER   A 1 411  ? 207.370 204.055 213.331 1.00 150.43 ? 1743 SER   A CB   1 
ATOM   1883 O  OG   . SER   A 1 411  ? 207.196 203.867 211.938 1.00 142.74 ? 1743 SER   A OG   1 
ATOM   1884 N  N    . PRO   A 1 412  ? 209.605 203.502 215.784 1.00 152.85 ? 1744 PRO   A N    1 
ATOM   1885 C  CA   . PRO   A 1 412  ? 209.916 203.761 217.199 1.00 154.33 ? 1744 PRO   A CA   1 
ATOM   1886 C  C    . PRO   A 1 412  ? 209.143 204.935 217.766 1.00 151.33 ? 1744 PRO   A C    1 
ATOM   1887 O  O    . PRO   A 1 412  ? 209.025 205.073 218.989 1.00 150.25 ? 1744 PRO   A O    1 
ATOM   1888 C  CB   . PRO   A 1 412  ? 211.427 204.024 217.178 1.00 155.06 ? 1744 PRO   A CB   1 
ATOM   1889 C  CG   . PRO   A 1 412  ? 211.690 204.542 215.809 1.00 151.54 ? 1744 PRO   A CG   1 
ATOM   1890 C  CD   . PRO   A 1 412  ? 210.738 203.819 214.899 1.00 149.29 ? 1744 PRO   A CD   1 
ATOM   1891 N  N    . GLU   A 1 413  ? 208.621 205.794 216.900 1.00 150.32 ? 1745 GLU   A N    1 
ATOM   1892 C  CA   . GLU   A 1 413  ? 207.849 206.954 217.309 1.00 149.04 ? 1745 GLU   A CA   1 
ATOM   1893 C  C    . GLU   A 1 413  ? 206.344 206.708 217.186 1.00 147.55 ? 1745 GLU   A C    1 
ATOM   1894 O  O    . GLU   A 1 413  ? 205.551 207.615 217.441 1.00 145.02 ? 1745 GLU   A O    1 
ATOM   1895 C  CB   . GLU   A 1 413  ? 208.313 208.162 216.476 1.00 150.34 ? 1745 GLU   A CB   1 
ATOM   1896 C  CG   . GLU   A 1 413  ? 207.824 209.544 216.889 1.00 148.76 ? 1745 GLU   A CG   1 
ATOM   1897 C  CD   . GLU   A 1 413  ? 206.462 209.883 216.337 1.00 146.05 ? 1745 GLU   A CD   1 
ATOM   1898 O  OE1  . GLU   A 1 413  ? 206.113 209.370 215.253 1.00 138.66 ? 1745 GLU   A OE1  1 
ATOM   1899 O  OE2  . GLU   A 1 413  ? 205.729 210.637 217.007 1.00 146.49 ? 1745 GLU   A OE2  1 
ATOM   1900 N  N    . ALA   A 1 414  ? 205.930 205.474 216.880 1.00 151.12 ? 1746 ALA   A N    1 
ATOM   1901 C  CA   . ALA   A 1 414  ? 204.535 205.150 216.570 1.00 146.90 ? 1746 ALA   A CA   1 
ATOM   1902 C  C    . ALA   A 1 414  ? 204.068 204.001 217.470 1.00 138.67 ? 1746 ALA   A C    1 
ATOM   1903 O  O    . ALA   A 1 414  ? 203.542 202.993 216.995 1.00 127.79 ? 1746 ALA   A O    1 
ATOM   1904 C  CB   . ALA   A 1 414  ? 204.366 204.807 215.091 1.00 139.67 ? 1746 ALA   A CB   1 
ATOM   1905 N  N    . TYR   A 1 415  ? 204.274 204.162 218.774 1.00 134.97 ? 1747 TYR   A N    1 
ATOM   1906 C  CA   . TYR   A 1 415  ? 203.924 203.131 219.742 1.00 132.44 ? 1747 TYR   A CA   1 
ATOM   1907 C  C    . TYR   A 1 415  ? 202.453 202.736 219.632 1.00 117.43 ? 1747 TYR   A C    1 
ATOM   1908 O  O    . TYR   A 1 415  ? 201.569 203.580 219.478 1.00 114.87 ? 1747 TYR   A O    1 
ATOM   1909 C  CB   . TYR   A 1 415  ? 204.206 203.626 221.162 1.00 134.02 ? 1747 TYR   A CB   1 
ATOM   1910 C  CG   . TYR   A 1 415  ? 205.669 203.842 221.478 1.00 149.47 ? 1747 TYR   A CG   1 
ATOM   1911 C  CD1  . TYR   A 1 415  ? 206.492 202.775 221.818 1.00 149.84 ? 1747 TYR   A CD1  1 
ATOM   1912 C  CD2  . TYR   A 1 415  ? 206.225 205.114 221.449 1.00 147.95 ? 1747 TYR   A CD2  1 
ATOM   1913 C  CE1  . TYR   A 1 415  ? 207.829 202.966 222.110 1.00 148.68 ? 1747 TYR   A CE1  1 
ATOM   1914 C  CE2  . TYR   A 1 415  ? 207.562 205.316 221.742 1.00 150.63 ? 1747 TYR   A CE2  1 
ATOM   1915 C  CZ   . TYR   A 1 415  ? 208.359 204.237 222.072 1.00 150.41 ? 1747 TYR   A CZ   1 
ATOM   1916 O  OH   . TYR   A 1 415  ? 209.690 204.429 222.363 1.00 147.64 ? 1747 TYR   A OH   1 
ATOM   1917 N  N    . CYS   A 1 416  ? 202.193 201.417 219.705 1.00 117.57 ? 1748 CYS   A N    1 
ATOM   1918 C  CA   . CYS   A 1 416  ? 200.826 200.880 219.762 1.00 107.87 ? 1748 CYS   A CA   1 
ATOM   1919 C  C    . CYS   A 1 416  ? 200.793 199.787 220.828 1.00 89.65  ? 1748 CYS   A C    1 
ATOM   1920 O  O    . CYS   A 1 416  ? 200.954 198.603 220.539 1.00 85.78  ? 1748 CYS   A O    1 
ATOM   1921 C  CB   . CYS   A 1 416  ? 200.366 200.346 218.410 1.00 104.09 ? 1748 CYS   A CB   1 
ATOM   1922 S  SG   . CYS   A 1 416  ? 198.667 199.731 218.404 1.00 83.88  ? 1748 CYS   A SG   1 
ATOM   1923 N  N    . LEU   A 1 417  ? 200.547 200.190 222.071 1.00 83.70  ? 1749 LEU   A N    1 
ATOM   1924 C  CA   . LEU   A 1 417  ? 200.537 199.261 223.197 1.00 85.66  ? 1749 LEU   A CA   1 
ATOM   1925 C  C    . LEU   A 1 417  ? 199.125 198.722 223.437 1.00 81.44  ? 1749 LEU   A C    1 
ATOM   1926 O  O    . LEU   A 1 417  ? 198.537 198.887 224.504 1.00 82.64  ? 1749 LEU   A O    1 
ATOM   1927 C  CB   . LEU   A 1 417  ? 201.072 199.948 224.447 1.00 92.16  ? 1749 LEU   A CB   1 
ATOM   1928 C  CG   . LEU   A 1 417  ? 202.527 200.411 224.541 1.00 100.59 ? 1749 LEU   A CG   1 
ATOM   1929 C  CD1  . LEU   A 1 417  ? 202.737 201.187 225.827 1.00 89.81  ? 1749 LEU   A CD1  1 
ATOM   1930 C  CD2  . LEU   A 1 417  ? 203.482 199.241 224.485 1.00 110.46 ? 1749 LEU   A CD2  1 
ATOM   1931 N  N    . VAL   A 1 418  ? 198.568 198.070 222.419 1.00 79.84  ? 1750 VAL   A N    1 
ATOM   1932 C  CA   . VAL   A 1 418  ? 197.250 197.473 222.596 1.00 79.43  ? 1750 VAL   A CA   1 
ATOM   1933 C  C    . VAL   A 1 418  ? 197.389 196.248 223.490 1.00 85.95  ? 1750 VAL   A C    1 
ATOM   1934 O  O    . VAL   A 1 418  ? 198.268 195.402 223.289 1.00 90.09  ? 1750 VAL   A O    1 
ATOM   1935 C  CB   . VAL   A 1 418  ? 196.592 197.139 221.248 1.00 75.17  ? 1750 VAL   A CB   1 
ATOM   1936 C  CG1  . VAL   A 1 418  ? 197.207 195.931 220.610 1.00 79.45  ? 1750 VAL   A CG1  1 
ATOM   1937 C  CG2  . VAL   A 1 418  ? 195.113 196.896 221.444 1.00 66.77  ? 1750 VAL   A CG2  1 
ATOM   1938 N  N    . GLY   A 1 419  ? 196.562 196.185 224.527 1.00 86.61  ? 1751 GLY   A N    1 
ATOM   1939 C  CA   . GLY   A 1 419  ? 196.613 195.072 225.454 1.00 86.04  ? 1751 GLY   A CA   1 
ATOM   1940 C  C    . GLY   A 1 419  ? 195.647 195.287 226.594 1.00 84.27  ? 1751 GLY   A C    1 
ATOM   1941 O  O    . GLY   A 1 419  ? 195.080 196.368 226.761 1.00 91.39  ? 1751 GLY   A O    1 
ATOM   1942 N  N    . SER   A 1 420  ? 195.471 194.235 227.386 1.00 78.27  ? 1752 SER   A N    1 
ATOM   1943 C  CA   . SER   A 1 420  ? 194.573 194.293 228.529 1.00 71.36  ? 1752 SER   A CA   1 
ATOM   1944 C  C    . SER   A 1 420  ? 195.293 194.832 229.755 1.00 69.24  ? 1752 SER   A C    1 
ATOM   1945 O  O    . SER   A 1 420  ? 196.470 194.547 229.964 1.00 75.69  ? 1752 SER   A O    1 
ATOM   1946 C  CB   . SER   A 1 420  ? 194.001 192.918 228.832 1.00 71.86  ? 1752 SER   A CB   1 
ATOM   1947 O  OG   . SER   A 1 420  ? 195.046 191.996 229.061 1.00 75.34  ? 1752 SER   A OG   1 
ATOM   1948 N  N    . GLU   A 1 428  ? 184.772 193.998 235.661 1.00 104.33 ? 1760 GLU   A N    1 
ATOM   1949 C  CA   . GLU   A 1 428  ? 184.941 194.270 234.239 1.00 99.62  ? 1760 GLU   A CA   1 
ATOM   1950 C  C    . GLU   A 1 428  ? 186.405 194.165 233.846 1.00 95.82  ? 1760 GLU   A C    1 
ATOM   1951 O  O    . GLU   A 1 428  ? 187.290 194.450 234.650 1.00 93.51  ? 1760 GLU   A O    1 
ATOM   1952 C  CB   . GLU   A 1 428  ? 184.399 195.656 233.887 1.00 76.95  ? 1760 GLU   A CB   1 
ATOM   1953 N  N    . SER   A 1 429  ? 186.662 193.750 232.613 1.00 89.20  ? 1761 SER   A N    1 
ATOM   1954 C  CA   . SER   A 1 429  ? 188.018 193.658 232.103 1.00 84.49  ? 1761 SER   A CA   1 
ATOM   1955 C  C    . SER   A 1 429  ? 188.293 194.817 231.155 1.00 90.73  ? 1761 SER   A C    1 
ATOM   1956 O  O    . SER   A 1 429  ? 187.374 195.433 230.608 1.00 92.01  ? 1761 SER   A O    1 
ATOM   1957 C  CB   . SER   A 1 429  ? 188.252 192.324 231.394 1.00 79.43  ? 1761 SER   A CB   1 
ATOM   1958 O  OG   . SER   A 1 429  ? 189.566 192.262 230.885 1.00 80.49  ? 1761 SER   A OG   1 
ATOM   1959 N  N    . PHE   A 1 430  ? 189.577 195.098 230.950 1.00 87.07  ? 1762 PHE   A N    1 
ATOM   1960 C  CA   . PHE   A 1 430  ? 189.999 196.341 230.325 1.00 75.21  ? 1762 PHE   A CA   1 
ATOM   1961 C  C    . PHE   A 1 430  ? 190.879 196.064 229.117 1.00 76.70  ? 1762 PHE   A C    1 
ATOM   1962 O  O    . PHE   A 1 430  ? 191.674 195.124 229.112 1.00 68.23  ? 1762 PHE   A O    1 
ATOM   1963 C  CB   . PHE   A 1 430  ? 190.762 197.217 231.320 1.00 74.03  ? 1762 PHE   A CB   1 
ATOM   1964 C  CG   . PHE   A 1 430  ? 189.878 197.988 232.252 1.00 81.19  ? 1762 PHE   A CG   1 
ATOM   1965 C  CD1  . PHE   A 1 430  ? 190.334 198.363 233.500 1.00 91.94  ? 1762 PHE   A CD1  1 
ATOM   1966 C  CD2  . PHE   A 1 430  ? 188.601 198.349 231.880 1.00 76.38  ? 1762 PHE   A CD2  1 
ATOM   1967 C  CE1  . PHE   A 1 430  ? 189.529 199.077 234.359 1.00 90.71  ? 1762 PHE   A CE1  1 
ATOM   1968 C  CE2  . PHE   A 1 430  ? 187.799 199.065 232.740 1.00 81.24  ? 1762 PHE   A CE2  1 
ATOM   1969 C  CZ   . PHE   A 1 430  ? 188.260 199.427 233.975 1.00 88.29  ? 1762 PHE   A CZ   1 
ATOM   1970 N  N    . LEU   A 1 431  ? 190.728 196.907 228.094 1.00 77.13  ? 1763 LEU   A N    1 
ATOM   1971 C  CA   . LEU   A 1 431  ? 191.603 196.938 226.926 1.00 67.88  ? 1763 LEU   A CA   1 
ATOM   1972 C  C    . LEU   A 1 431  ? 192.107 198.363 226.730 1.00 68.96  ? 1763 LEU   A C    1 
ATOM   1973 O  O    . LEU   A 1 431  ? 191.307 199.300 226.656 1.00 71.86  ? 1763 LEU   A O    1 
ATOM   1974 C  CB   . LEU   A 1 431  ? 190.877 196.450 225.675 1.00 50.02  ? 1763 LEU   A CB   1 
ATOM   1975 C  CG   . LEU   A 1 431  ? 191.729 196.401 224.410 1.00 39.77  ? 1763 LEU   A CG   1 
ATOM   1976 C  CD1  . LEU   A 1 431  ? 192.865 195.435 224.572 1.00 53.46  ? 1763 LEU   A CD1  1 
ATOM   1977 C  CD2  . LEU   A 1 431  ? 190.881 196.011 223.228 1.00 42.86  ? 1763 LEU   A CD2  1 
ATOM   1978 N  N    . LYS   A 1 432  ? 193.427 198.523 226.649 1.00 64.33  ? 1764 LYS   A N    1 
ATOM   1979 C  CA   . LYS   A 1 432  ? 194.060 199.833 226.559 1.00 57.33  ? 1764 LYS   A CA   1 
ATOM   1980 C  C    . LYS   A 1 432  ? 194.835 199.946 225.258 1.00 60.16  ? 1764 LYS   A C    1 
ATOM   1981 O  O    . LYS   A 1 432  ? 195.576 199.030 224.891 1.00 59.69  ? 1764 LYS   A O    1 
ATOM   1982 C  CB   . LYS   A 1 432  ? 194.993 200.076 227.742 1.00 49.50  ? 1764 LYS   A CB   1 
ATOM   1983 C  CG   . LYS   A 1 432  ? 194.288 200.238 229.058 1.00 52.08  ? 1764 LYS   A CG   1 
ATOM   1984 C  CD   . LYS   A 1 432  ? 195.282 200.402 230.187 1.00 69.17  ? 1764 LYS   A CD   1 
ATOM   1985 C  CE   . LYS   A 1 432  ? 195.987 201.745 230.126 1.00 66.30  ? 1764 LYS   A CE   1 
ATOM   1986 N  NZ   . LYS   A 1 432  ? 195.065 202.868 230.407 1.00 69.23  ? 1764 LYS   A NZ   1 
ATOM   1987 N  N    . ILE   A 1 433  ? 194.673 201.075 224.575 1.00 59.68  ? 1765 ILE   A N    1 
ATOM   1988 C  CA   . ILE   A 1 433  ? 195.473 201.435 223.411 1.00 53.88  ? 1765 ILE   A CA   1 
ATOM   1989 C  C    . ILE   A 1 433  ? 196.305 202.651 223.785 1.00 64.30  ? 1765 ILE   A C    1 
ATOM   1990 O  O    . ILE   A 1 433  ? 195.759 203.701 224.144 1.00 62.98  ? 1765 ILE   A O    1 
ATOM   1991 C  CB   . ILE   A 1 433  ? 194.596 201.732 222.189 1.00 49.82  ? 1765 ILE   A CB   1 
ATOM   1992 C  CG1  . ILE   A 1 433  ? 193.623 200.582 221.943 1.00 54.82  ? 1765 ILE   A CG1  1 
ATOM   1993 C  CG2  . ILE   A 1 433  ? 195.462 201.967 220.976 1.00 58.40  ? 1765 ILE   A CG2  1 
ATOM   1994 C  CD1  . ILE   A 1 433  ? 192.279 201.024 221.439 1.00 50.17  ? 1765 ILE   A CD1  1 
ATOM   1995 N  N    . THR   A 1 434  ? 197.620 202.516 223.702 1.00 76.65  ? 1766 THR   A N    1 
ATOM   1996 C  CA   . THR   A 1 434  ? 198.543 203.578 224.076 1.00 79.83  ? 1766 THR   A CA   1 
ATOM   1997 C  C    . THR   A 1 434  ? 199.346 203.984 222.847 1.00 86.68  ? 1766 THR   A C    1 
ATOM   1998 O  O    . THR   A 1 434  ? 200.209 203.229 222.388 1.00 91.48  ? 1766 THR   A O    1 
ATOM   1999 C  CB   . THR   A 1 434  ? 199.469 203.109 225.195 1.00 81.01  ? 1766 THR   A CB   1 
ATOM   2000 O  OG1  . THR   A 1 434  ? 198.694 202.824 226.364 1.00 73.59  ? 1766 THR   A OG1  1 
ATOM   2001 C  CG2  . THR   A 1 434  ? 200.490 204.178 225.522 1.00 84.53  ? 1766 THR   A CG2  1 
ATOM   2002 N  N    . VAL   A 1 435  ? 199.067 205.171 222.320 1.00 79.92  ? 1767 VAL   A N    1 
ATOM   2003 C  CA   . VAL   A 1 435  ? 199.708 205.627 221.090 1.00 79.40  ? 1767 VAL   A CA   1 
ATOM   2004 C  C    . VAL   A 1 435  ? 200.179 207.062 221.298 1.00 91.02  ? 1767 VAL   A C    1 
ATOM   2005 O  O    . VAL   A 1 435  ? 199.610 207.802 222.112 1.00 88.09  ? 1767 VAL   A O    1 
ATOM   2006 C  CB   . VAL   A 1 435  ? 198.751 205.532 219.883 1.00 71.91  ? 1767 VAL   A CB   1 
ATOM   2007 C  CG1  . VAL   A 1 435  ? 198.338 204.094 219.643 1.00 67.39  ? 1767 VAL   A CG1  1 
ATOM   2008 C  CG2  . VAL   A 1 435  ? 197.551 206.394 220.125 1.00 75.95  ? 1767 VAL   A CG2  1 
ATOM   2009 N  N    . PRO   A 1 436  ? 201.211 207.483 220.573 1.00 103.24 ? 1768 PRO   A N    1 
ATOM   2010 C  CA   . PRO   A 1 436  ? 201.747 208.835 220.754 1.00 106.96 ? 1768 PRO   A CA   1 
ATOM   2011 C  C    . PRO   A 1 436  ? 200.936 209.863 219.980 1.00 108.87 ? 1768 PRO   A C    1 
ATOM   2012 O  O    . PRO   A 1 436  ? 200.080 209.536 219.159 1.00 106.48 ? 1768 PRO   A O    1 
ATOM   2013 C  CB   . PRO   A 1 436  ? 203.158 208.729 220.181 1.00 115.34 ? 1768 PRO   A CB   1 
ATOM   2014 C  CG   . PRO   A 1 436  ? 203.019 207.712 219.122 1.00 117.97 ? 1768 PRO   A CG   1 
ATOM   2015 C  CD   . PRO   A 1 436  ? 201.997 206.719 219.592 1.00 112.00 ? 1768 PRO   A CD   1 
ATOM   2016 N  N    . SER   A 1 437  ? 201.243 211.133 220.244 1.00 112.00 ? 1769 SER   A N    1 
ATOM   2017 C  CA   . SER   A 1 437  ? 200.583 212.241 219.556 1.00 115.52 ? 1769 SER   A CA   1 
ATOM   2018 C  C    . SER   A 1 437  ? 201.420 212.636 218.343 1.00 122.92 ? 1769 SER   A C    1 
ATOM   2019 O  O    . SER   A 1 437  ? 202.292 213.505 218.391 1.00 128.77 ? 1769 SER   A O    1 
ATOM   2020 C  CB   . SER   A 1 437  ? 200.361 213.411 220.505 1.00 114.00 ? 1769 SER   A CB   1 
ATOM   2021 O  OG   . SER   A 1 437  ? 199.471 213.050 221.546 1.00 100.71 ? 1769 SER   A OG   1 
ATOM   2022 N  N    . CYS   A 1 438  ? 201.137 211.967 217.231 1.00 119.12 ? 1770 CYS   A N    1 
ATOM   2023 C  CA   . CYS   A 1 438  ? 201.723 212.295 215.943 1.00 119.44 ? 1770 CYS   A CA   1 
ATOM   2024 C  C    . CYS   A 1 438  ? 200.742 211.852 214.873 1.00 110.97 ? 1770 CYS   A C    1 
ATOM   2025 O  O    . CYS   A 1 438  ? 199.703 211.261 215.167 1.00 113.35 ? 1770 CYS   A O    1 
ATOM   2026 C  CB   . CYS   A 1 438  ? 203.077 211.621 215.740 1.00 126.11 ? 1770 CYS   A CB   1 
ATOM   2027 S  SG   . CYS   A 1 438  ? 202.985 209.827 215.671 1.00 136.06 ? 1770 CYS   A SG   1 
ATOM   2028 N  N    . ARG   A 1 439  ? 201.066 212.159 213.619 1.00 106.78 ? 1771 ARG   A N    1 
ATOM   2029 C  CA   A ARG   A 1 439  ? 200.194 211.752 212.524 0.74 105.11 ? 1771 ARG   A CA   1 
ATOM   2030 C  CA   B ARG   A 1 439  ? 200.197 211.750 212.522 0.26 105.09 ? 1771 ARG   A CA   1 
ATOM   2031 C  C    . ARG   A 1 439  ? 200.133 210.234 212.414 1.00 101.16 ? 1771 ARG   A C    1 
ATOM   2032 O  O    . ARG   A 1 439  ? 199.056 209.661 212.216 1.00 98.61  ? 1771 ARG   A O    1 
ATOM   2033 C  CB   A ARG   A 1 439  ? 200.670 212.376 211.214 0.74 104.39 ? 1771 ARG   A CB   1 
ATOM   2034 C  CB   B ARG   A 1 439  ? 200.683 212.365 211.213 0.26 104.34 ? 1771 ARG   A CB   1 
ATOM   2035 C  CG   A ARG   A 1 439  ? 200.107 211.720 209.967 0.74 101.55 ? 1771 ARG   A CG   1 
ATOM   2036 C  CG   B ARG   A 1 439  ? 199.914 213.602 210.789 0.26 102.52 ? 1771 ARG   A CG   1 
ATOM   2037 C  CD   A ARG   A 1 439  ? 198.650 212.096 209.766 0.74 97.30  ? 1771 ARG   A CD   1 
ATOM   2038 C  CD   B ARG   A 1 439  ? 199.476 214.425 211.996 0.26 100.71 ? 1771 ARG   A CD   1 
ATOM   2039 N  NE   A ARG   A 1 439  ? 198.485 213.476 209.327 0.74 95.57  ? 1771 ARG   A NE   1 
ATOM   2040 N  NE   B ARG   A 1 439  ? 200.602 214.979 212.741 0.26 102.22 ? 1771 ARG   A NE   1 
ATOM   2041 C  CZ   A ARG   A 1 439  ? 197.311 214.065 209.141 0.74 87.87  ? 1771 ARG   A CZ   1 
ATOM   2042 C  CZ   B ARG   A 1 439  ? 201.404 215.938 212.300 0.26 104.63 ? 1771 ARG   A CZ   1 
ATOM   2043 N  NH1  A ARG   A 1 439  ? 196.174 213.422 209.349 0.74 84.20  ? 1771 ARG   A NH1  1 
ATOM   2044 N  NH1  B ARG   A 1 439  ? 201.230 216.495 211.113 0.26 103.96 ? 1771 ARG   A NH1  1 
ATOM   2045 N  NH2  A ARG   A 1 439  ? 197.278 215.332 208.739 0.74 88.27  ? 1771 ARG   A NH2  1 
ATOM   2046 N  NH2  B ARG   A 1 439  ? 202.403 216.354 213.072 0.26 103.95 ? 1771 ARG   A NH2  1 
ATOM   2047 N  N    . LYS   A 1 440  ? 201.279 209.566 212.551 1.00 102.25 ? 1772 LYS   A N    1 
ATOM   2048 C  CA   . LYS   A 1 440  ? 201.293 208.109 212.486 1.00 111.99 ? 1772 LYS   A CA   1 
ATOM   2049 C  C    . LYS   A 1 440  ? 200.539 207.495 213.658 1.00 103.95 ? 1772 LYS   A C    1 
ATOM   2050 O  O    . LYS   A 1 440  ? 199.800 206.522 213.483 1.00 94.86  ? 1772 LYS   A O    1 
ATOM   2051 C  CB   . LYS   A 1 440  ? 202.733 207.603 212.430 1.00 119.84 ? 1772 LYS   A CB   1 
ATOM   2052 C  CG   . LYS   A 1 440  ? 203.454 208.001 211.153 1.00 118.70 ? 1772 LYS   A CG   1 
ATOM   2053 C  CD   . LYS   A 1 440  ? 204.873 207.476 211.110 1.00 126.17 ? 1772 LYS   A CD   1 
ATOM   2054 C  CE   . LYS   A 1 440  ? 205.531 207.815 209.787 1.00 123.41 ? 1772 LYS   A CE   1 
ATOM   2055 N  NZ   . LYS   A 1 440  ? 205.727 209.282 209.640 1.00 117.23 ? 1772 LYS   A NZ   1 
ATOM   2056 N  N    . GLY   A 1 441  ? 200.706 208.049 214.859 1.00 103.16 ? 1773 GLY   A N    1 
ATOM   2057 C  CA   . GLY   A 1 441  ? 199.945 207.553 215.992 1.00 90.83  ? 1773 GLY   A CA   1 
ATOM   2058 C  C    . GLY   A 1 441  ? 198.453 207.758 215.820 1.00 82.71  ? 1773 GLY   A C    1 
ATOM   2059 O  O    . GLY   A 1 441  ? 197.653 206.882 216.147 1.00 86.13  ? 1773 GLY   A O    1 
ATOM   2060 N  N    . CYS   A 1 442  ? 198.061 208.916 215.295 1.00 84.72  ? 1774 CYS   A N    1 
ATOM   2061 C  CA   . CYS   A 1 442  ? 196.651 209.180 215.049 1.00 82.83  ? 1774 CYS   A CA   1 
ATOM   2062 C  C    . CYS   A 1 442  ? 196.083 208.187 214.045 1.00 89.55  ? 1774 CYS   A C    1 
ATOM   2063 O  O    . CYS   A 1 442  ? 195.011 207.611 214.265 1.00 102.27 ? 1774 CYS   A O    1 
ATOM   2064 C  CB   . CYS   A 1 442  ? 196.481 210.609 214.538 1.00 92.16  ? 1774 CYS   A CB   1 
ATOM   2065 S  SG   . CYS   A 1 442  ? 196.585 211.886 215.802 1.00 100.51 ? 1774 CYS   A SG   1 
ATOM   2066 N  N    . ILE   A 1 443  ? 196.806 207.955 212.946 1.00 86.10  ? 1775 ILE   A N    1 
ATOM   2067 C  CA   . ILE   A 1 443  ? 196.336 207.025 211.924 1.00 80.71  ? 1775 ILE   A CA   1 
ATOM   2068 C  C    . ILE   A 1 443  ? 196.252 205.614 212.481 1.00 79.80  ? 1775 ILE   A C    1 
ATOM   2069 O  O    . ILE   A 1 443  ? 195.301 204.873 212.203 1.00 78.85  ? 1775 ILE   A O    1 
ATOM   2070 C  CB   . ILE   A 1 443  ? 197.248 207.078 210.687 1.00 83.48  ? 1775 ILE   A CB   1 
ATOM   2071 C  CG1  . ILE   A 1 443  ? 197.202 208.459 210.040 1.00 91.15  ? 1775 ILE   A CG1  1 
ATOM   2072 C  CG2  . ILE   A 1 443  ? 196.845 206.014 209.689 1.00 85.46  ? 1775 ILE   A CG2  1 
ATOM   2073 C  CD1  . ILE   A 1 443  ? 198.260 208.655 208.986 1.00 94.76  ? 1775 ILE   A CD1  1 
ATOM   2074 N  N    . LEU   A 1 444  ? 197.255 205.209 213.256 1.00 81.23  ? 1776 LEU   A N    1 
ATOM   2075 C  CA   . LEU   A 1 444  ? 197.280 203.851 213.779 1.00 82.67  ? 1776 LEU   A CA   1 
ATOM   2076 C  C    . LEU   A 1 444  ? 196.167 203.631 214.798 1.00 73.03  ? 1776 LEU   A C    1 
ATOM   2077 O  O    . LEU   A 1 444  ? 195.538 202.567 214.819 1.00 71.34  ? 1776 LEU   A O    1 
ATOM   2078 C  CB   . LEU   A 1 444  ? 198.655 203.568 214.372 1.00 88.08  ? 1776 LEU   A CB   1 
ATOM   2079 C  CG   . LEU   A 1 444  ? 198.938 202.179 214.912 1.00 89.31  ? 1776 LEU   A CG   1 
ATOM   2080 C  CD1  . LEU   A 1 444  ? 198.834 201.176 213.786 1.00 91.82  ? 1776 LEU   A CD1  1 
ATOM   2081 C  CD2  . LEU   A 1 444  ? 200.336 202.179 215.482 1.00 99.48  ? 1776 LEU   A CD2  1 
ATOM   2082 N  N    . LEU   A 1 445  ? 195.905 204.627 215.649 1.00 70.46  ? 1777 LEU   A N    1 
ATOM   2083 C  CA   . LEU   A 1 445  ? 194.751 204.552 216.537 1.00 57.80  ? 1777 LEU   A CA   1 
ATOM   2084 C  C    . LEU   A 1 445  ? 193.464 204.447 215.739 1.00 60.28  ? 1777 LEU   A C    1 
ATOM   2085 O  O    . LEU   A 1 445  ? 192.569 203.672 216.093 1.00 66.43  ? 1777 LEU   A O    1 
ATOM   2086 C  CB   . LEU   A 1 445  ? 194.705 205.771 217.457 1.00 54.38  ? 1777 LEU   A CB   1 
ATOM   2087 C  CG   . LEU   A 1 445  ? 193.920 205.717 218.774 1.00 47.04  ? 1777 LEU   A CG   1 
ATOM   2088 C  CD1  . LEU   A 1 445  ? 194.180 206.968 219.553 1.00 51.13  ? 1777 LEU   A CD1  1 
ATOM   2089 C  CD2  . LEU   A 1 445  ? 192.435 205.597 218.572 1.00 49.37  ? 1777 LEU   A CD2  1 
ATOM   2090 N  N    . GLY   A 1 446  ? 193.335 205.240 214.678 1.00 69.59  ? 1778 GLY   A N    1 
ATOM   2091 C  CA   . GLY   A 1 446  ? 192.149 205.136 213.848 1.00 70.37  ? 1778 GLY   A CA   1 
ATOM   2092 C  C    . GLY   A 1 446  ? 191.968 203.739 213.289 1.00 73.70  ? 1778 GLY   A C    1 
ATOM   2093 O  O    . GLY   A 1 446  ? 190.867 203.184 213.321 1.00 79.36  ? 1778 GLY   A O    1 
ATOM   2094 N  N    . GLN   A 1 447  ? 193.054 203.139 212.807 1.00 69.21  ? 1779 GLN   A N    1 
ATOM   2095 C  CA   . GLN   A 1 447  ? 192.968 201.798 212.241 1.00 67.62  ? 1779 GLN   A CA   1 
ATOM   2096 C  C    . GLN   A 1 447  ? 192.588 200.771 213.300 1.00 68.44  ? 1779 GLN   A C    1 
ATOM   2097 O  O    . GLN   A 1 447  ? 191.757 199.892 213.056 1.00 73.85  ? 1779 GLN   A O    1 
ATOM   2098 C  CB   . GLN   A 1 447  ? 194.289 201.420 211.578 1.00 71.04  ? 1779 GLN   A CB   1 
ATOM   2099 C  CG   . GLN   A 1 447  ? 194.392 201.863 210.139 1.00 83.83  ? 1779 GLN   A CG   1 
ATOM   2100 C  CD   . GLN   A 1 447  ? 195.665 201.388 209.481 1.00 106.53 ? 1779 GLN   A CD   1 
ATOM   2101 O  OE1  . GLN   A 1 447  ? 196.399 200.572 210.037 1.00 111.63 ? 1779 GLN   A OE1  1 
ATOM   2102 N  NE2  . GLN   A 1 447  ? 195.936 201.898 208.287 1.00 118.39 ? 1779 GLN   A NE2  1 
ATOM   2103 N  N    . VAL   A 1 448  ? 193.196 200.857 214.485 1.00 64.45  ? 1780 VAL   A N    1 
ATOM   2104 C  CA   . VAL   A 1 448  ? 192.897 199.881 215.533 1.00 54.02  ? 1780 VAL   A CA   1 
ATOM   2105 C  C    . VAL   A 1 448  ? 191.456 200.007 216.000 1.00 53.62  ? 1780 VAL   A C    1 
ATOM   2106 O  O    . VAL   A 1 448  ? 190.759 199.001 216.181 1.00 63.63  ? 1780 VAL   A O    1 
ATOM   2107 C  CB   . VAL   A 1 448  ? 193.881 200.018 216.703 1.00 55.89  ? 1780 VAL   A CB   1 
ATOM   2108 C  CG1  . VAL   A 1 448  ? 193.480 199.094 217.816 1.00 50.27  ? 1780 VAL   A CG1  1 
ATOM   2109 C  CG2  . VAL   A 1 448  ? 195.267 199.657 216.239 1.00 67.99  ? 1780 VAL   A CG2  1 
ATOM   2110 N  N    . VAL   A 1 449  ? 190.984 201.235 216.216 1.00 54.30  ? 1781 VAL   A N    1 
ATOM   2111 C  CA   . VAL   A 1 449  ? 189.597 201.414 216.626 1.00 55.41  ? 1781 VAL   A CA   1 
ATOM   2112 C  C    . VAL   A 1 449  ? 188.663 200.893 215.549 1.00 58.76  ? 1781 VAL   A C    1 
ATOM   2113 O  O    . VAL   A 1 449  ? 187.663 200.231 215.845 1.00 67.01  ? 1781 VAL   A O    1 
ATOM   2114 C  CB   . VAL   A 1 449  ? 189.314 202.887 216.962 1.00 48.70  ? 1781 VAL   A CB   1 
ATOM   2115 C  CG1  . VAL   A 1 449  ? 187.828 203.167 216.894 1.00 43.48  ? 1781 VAL   A CG1  1 
ATOM   2116 C  CG2  . VAL   A 1 449  ? 189.820 203.197 218.343 1.00 49.35  ? 1781 VAL   A CG2  1 
ATOM   2117 N  N    . ASP   A 1 450  ? 188.980 201.163 214.284 1.00 57.19  ? 1782 ASP   A N    1 
ATOM   2118 C  CA   . ASP   A 1 450  ? 188.131 200.669 213.210 1.00 68.02  ? 1782 ASP   A CA   1 
ATOM   2119 C  C    . ASP   A 1 450  ? 188.107 199.149 213.173 1.00 74.84  ? 1782 ASP   A C    1 
ATOM   2120 O  O    . ASP   A 1 450  ? 187.047 198.548 212.982 1.00 74.24  ? 1782 ASP   A O    1 
ATOM   2121 C  CB   . ASP   A 1 450  ? 188.595 201.230 211.874 1.00 70.46  ? 1782 ASP   A CB   1 
ATOM   2122 C  CG   . ASP   A 1 450  ? 187.453 201.440 210.922 1.00 82.22  ? 1782 ASP   A CG   1 
ATOM   2123 O  OD1  . ASP   A 1 450  ? 186.308 201.109 211.296 1.00 85.05  ? 1782 ASP   A OD1  1 
ATOM   2124 O  OD2  . ASP   A 1 450  ? 187.697 201.930 209.805 1.00 81.77  ? 1782 ASP   A OD2  1 
ATOM   2125 N  N    . HIS   A 1 451  ? 189.259 198.507 213.360 1.00 74.04  ? 1783 HIS   A N    1 
ATOM   2126 C  CA   . HIS   A 1 451  ? 189.310 197.051 213.325 1.00 63.17  ? 1783 HIS   A CA   1 
ATOM   2127 C  C    . HIS   A 1 451  ? 188.506 196.445 214.468 1.00 62.43  ? 1783 HIS   A C    1 
ATOM   2128 O  O    . HIS   A 1 451  ? 187.733 195.502 214.273 1.00 74.37  ? 1783 HIS   A O    1 
ATOM   2129 C  CB   . HIS   A 1 451  ? 190.759 196.583 213.372 1.00 54.75  ? 1783 HIS   A CB   1 
ATOM   2130 C  CG   . HIS   A 1 451  ? 191.473 196.727 212.069 1.00 68.68  ? 1783 HIS   A CG   1 
ATOM   2131 N  ND1  . HIS   A 1 451  ? 190.895 196.388 210.866 1.00 80.41  ? 1783 HIS   A ND1  1 
ATOM   2132 C  CD2  . HIS   A 1 451  ? 192.715 197.178 211.776 1.00 78.58  ? 1783 HIS   A CD2  1 
ATOM   2133 C  CE1  . HIS   A 1 451  ? 191.751 196.619 209.888 1.00 86.49  ? 1783 HIS   A CE1  1 
ATOM   2134 N  NE2  . HIS   A 1 451  ? 192.863 197.099 210.413 1.00 87.22  ? 1783 HIS   A NE2  1 
ATOM   2135 N  N    . ILE   A 1 452  ? 188.671 196.986 215.676 1.00 55.95  ? 1784 ILE   A N    1 
ATOM   2136 C  CA   . ILE   A 1 452  ? 187.950 196.447 216.825 1.00 48.34  ? 1784 ILE   A CA   1 
ATOM   2137 C  C    . ILE   A 1 452  ? 186.452 196.654 216.657 1.00 60.09  ? 1784 ILE   A C    1 
ATOM   2138 O  O    . ILE   A 1 452  ? 185.647 195.764 216.960 1.00 73.77  ? 1784 ILE   A O    1 
ATOM   2139 C  CB   . ILE   A 1 452  ? 188.465 197.086 218.123 1.00 44.83  ? 1784 ILE   A CB   1 
ATOM   2140 C  CG1  . ILE   A 1 452  ? 189.719 196.370 218.599 1.00 54.19  ? 1784 ILE   A CG1  1 
ATOM   2141 C  CG2  . ILE   A 1 452  ? 187.417 197.013 219.193 1.00 47.24  ? 1784 ILE   A CG2  1 
ATOM   2142 C  CD1  . ILE   A 1 452  ? 190.419 197.092 219.711 1.00 56.58  ? 1784 ILE   A CD1  1 
ATOM   2143 N  N    . ASP   A 1 453  ? 186.049 197.833 216.183 1.00 60.95  ? 1785 ASP   A N    1 
ATOM   2144 C  CA   . ASP   A 1 453  ? 184.628 198.084 215.986 1.00 63.65  ? 1785 ASP   A CA   1 
ATOM   2145 C  C    . ASP   A 1 453  ? 184.067 197.203 214.881 1.00 74.21  ? 1785 ASP   A C    1 
ATOM   2146 O  O    . ASP   A 1 453  ? 182.911 196.777 214.950 1.00 90.50  ? 1785 ASP   A O    1 
ATOM   2147 C  CB   . ASP   A 1 453  ? 184.383 199.559 215.683 1.00 69.30  ? 1785 ASP   A CB   1 
ATOM   2148 C  CG   . ASP   A 1 453  ? 184.212 200.389 216.938 1.00 77.95  ? 1785 ASP   A CG   1 
ATOM   2149 O  OD1  . ASP   A 1 453  ? 183.381 200.013 217.790 1.00 69.31  ? 1785 ASP   A OD1  1 
ATOM   2150 O  OD2  . ASP   A 1 453  ? 184.900 201.422 217.071 1.00 83.31  ? 1785 ASP   A OD2  1 
ATOM   2151 N  N    . SER   A 1 454  ? 184.871 196.911 213.856 1.00 66.46  ? 1786 SER   A N    1 
ATOM   2152 C  CA   . SER   A 1 454  ? 184.436 195.978 212.822 1.00 69.84  ? 1786 SER   A CA   1 
ATOM   2153 C  C    . SER   A 1 454  ? 184.240 194.582 213.399 1.00 73.06  ? 1786 SER   A C    1 
ATOM   2154 O  O    . SER   A 1 454  ? 183.261 193.902 213.085 1.00 73.91  ? 1786 SER   A O    1 
ATOM   2155 C  CB   . SER   A 1 454  ? 185.447 195.959 211.679 1.00 70.63  ? 1786 SER   A CB   1 
ATOM   2156 O  OG   . SER   A 1 454  ? 186.682 195.431 212.112 1.00 74.95  ? 1786 SER   A OG   1 
ATOM   2157 N  N    . LEU   A 1 455  ? 185.165 194.147 214.255 1.00 73.05  ? 1787 LEU   A N    1 
ATOM   2158 C  CA   . LEU   A 1 455  ? 185.021 192.888 214.981 1.00 69.05  ? 1787 LEU   A CA   1 
ATOM   2159 C  C    . LEU   A 1 455  ? 183.687 192.819 215.710 1.00 70.28  ? 1787 LEU   A C    1 
ATOM   2160 O  O    . LEU   A 1 455  ? 182.873 191.911 215.492 1.00 85.70  ? 1787 LEU   A O    1 
ATOM   2161 C  CB   . LEU   A 1 455  ? 186.167 192.770 215.986 1.00 72.82  ? 1787 LEU   A CB   1 
ATOM   2162 C  CG   . LEU   A 1 455  ? 186.445 191.515 216.806 1.00 79.17  ? 1787 LEU   A CG   1 
ATOM   2163 C  CD1  . LEU   A 1 455  ? 187.917 191.465 217.182 1.00 75.99  ? 1787 LEU   A CD1  1 
ATOM   2164 C  CD2  . LEU   A 1 455  ? 185.579 191.498 218.043 1.00 80.02  ? 1787 LEU   A CD2  1 
ATOM   2165 N  N    . MET   A 1 456  ? 183.461 193.788 216.594 1.00 63.52  ? 1788 MET   A N    1 
ATOM   2166 C  CA   . MET   A 1 456  ? 182.303 193.785 217.475 1.00 66.31  ? 1788 MET   A CA   1 
ATOM   2167 C  C    . MET   A 1 456  ? 180.997 194.085 216.752 1.00 80.68  ? 1788 MET   A C    1 
ATOM   2168 O  O    . MET   A 1 456  ? 179.930 193.797 217.301 1.00 93.44  ? 1788 MET   A O    1 
ATOM   2169 C  CB   . MET   A 1 456  ? 182.497 194.800 218.596 1.00 61.52  ? 1788 MET   A CB   1 
ATOM   2170 C  CG   . MET   A 1 456  ? 183.397 194.334 219.712 1.00 71.19  ? 1788 MET   A CG   1 
ATOM   2171 S  SD   . MET   A 1 456  ? 184.136 195.729 220.571 1.00 109.27 ? 1788 MET   A SD   1 
ATOM   2172 C  CE   . MET   A 1 456  ? 184.250 195.059 222.218 1.00 87.41  ? 1788 MET   A CE   1 
ATOM   2173 N  N    . GLU   A 1 457  ? 181.042 194.677 215.561 1.00 77.45  ? 1789 GLU   A N    1 
ATOM   2174 C  CA   . GLU   A 1 457  ? 179.826 194.915 214.802 1.00 84.46  ? 1789 GLU   A CA   1 
ATOM   2175 C  C    . GLU   A 1 457  ? 179.568 193.848 213.756 1.00 90.55  ? 1789 GLU   A C    1 
ATOM   2176 O  O    . GLU   A 1 457  ? 178.447 193.760 213.247 1.00 104.99 ? 1789 GLU   A O    1 
ATOM   2177 C  CB   . GLU   A 1 457  ? 179.889 196.284 214.114 1.00 89.65  ? 1789 GLU   A CB   1 
ATOM   2178 N  N    . GLU   A 1 458  ? 180.568 193.032 213.439 1.00 87.87  ? 1790 GLU   A N    1 
ATOM   2179 C  CA   . GLU   A 1 458  ? 180.423 191.972 212.459 1.00 94.17  ? 1790 GLU   A CA   1 
ATOM   2180 C  C    . GLU   A 1 458  ? 180.065 190.642 213.089 1.00 96.54  ? 1790 GLU   A C    1 
ATOM   2181 O  O    . GLU   A 1 458  ? 179.245 189.908 212.530 1.00 100.40 ? 1790 GLU   A O    1 
ATOM   2182 C  CB   . GLU   A 1 458  ? 181.710 191.814 211.643 1.00 95.63  ? 1790 GLU   A CB   1 
ATOM   2183 N  N    . TRP   A 1 459  ? 180.652 190.290 214.234 1.00 98.27  ? 1791 TRP   A N    1 
ATOM   2184 C  CA   . TRP   A 1 459  ? 180.346 188.976 214.789 1.00 96.65  ? 1791 TRP   A CA   1 
ATOM   2185 C  C    . TRP   A 1 459  ? 179.503 189.041 216.059 1.00 82.19  ? 1791 TRP   A C    1 
ATOM   2186 O  O    . TRP   A 1 459  ? 178.437 188.423 216.115 1.00 83.96  ? 1791 TRP   A O    1 
ATOM   2187 C  CB   . TRP   A 1 459  ? 181.624 188.158 215.021 1.00 95.34  ? 1791 TRP   A CB   1 
ATOM   2188 C  CG   . TRP   A 1 459  ? 182.280 187.786 213.733 1.00 110.13 ? 1791 TRP   A CG   1 
ATOM   2189 C  CD1  . TRP   A 1 459  ? 181.800 188.023 212.482 1.00 118.15 ? 1791 TRP   A CD1  1 
ATOM   2190 C  CD2  . TRP   A 1 459  ? 183.426 186.946 213.562 1.00 123.97 ? 1791 TRP   A CD2  1 
ATOM   2191 N  NE1  . TRP   A 1 459  ? 182.635 187.481 211.539 1.00 129.95 ? 1791 TRP   A NE1  1 
ATOM   2192 C  CE2  . TRP   A 1 459  ? 183.634 186.799 212.178 1.00 128.48 ? 1791 TRP   A CE2  1 
ATOM   2193 C  CE3  . TRP   A 1 459  ? 184.310 186.327 214.441 1.00 123.96 ? 1791 TRP   A CE3  1 
ATOM   2194 C  CZ2  . TRP   A 1 459  ? 184.697 186.068 211.654 1.00 128.43 ? 1791 TRP   A CZ2  1 
ATOM   2195 C  CZ3  . TRP   A 1 459  ? 185.370 185.605 213.919 1.00 127.03 ? 1791 TRP   A CZ3  1 
ATOM   2196 C  CH2  . TRP   A 1 459  ? 185.554 185.482 212.541 1.00 129.95 ? 1791 TRP   A CH2  1 
ATOM   2197 N  N    . PHE   A 1 460  ? 179.940 189.766 217.077 1.00 75.07  ? 1792 PHE   A N    1 
ATOM   2198 C  CA   . PHE   A 1 460  ? 179.167 189.654 218.307 1.00 79.87  ? 1792 PHE   A CA   1 
ATOM   2199 C  C    . PHE   A 1 460  ? 178.998 190.974 219.042 1.00 84.96  ? 1792 PHE   A C    1 
ATOM   2200 O  O    . PHE   A 1 460  ? 179.977 191.539 219.542 1.00 87.85  ? 1792 PHE   A O    1 
ATOM   2201 C  CB   . PHE   A 1 460  ? 179.794 188.627 219.251 1.00 96.04  ? 1792 PHE   A CB   1 
ATOM   2202 C  CG   . PHE   A 1 460  ? 181.287 188.716 219.359 1.00 95.80  ? 1792 PHE   A CG   1 
ATOM   2203 C  CD1  . PHE   A 1 460  ? 182.101 188.163 218.387 1.00 91.93  ? 1792 PHE   A CD1  1 
ATOM   2204 C  CD2  . PHE   A 1 460  ? 181.876 189.330 220.442 1.00 95.54  ? 1792 PHE   A CD2  1 
ATOM   2205 C  CE1  . PHE   A 1 460  ? 183.460 188.235 218.488 1.00 87.42  ? 1792 PHE   A CE1  1 
ATOM   2206 C  CE2  . PHE   A 1 460  ? 183.238 189.402 220.545 1.00 100.21 ? 1792 PHE   A CE2  1 
ATOM   2207 C  CZ   . PHE   A 1 460  ? 184.029 188.851 219.569 1.00 94.25  ? 1792 PHE   A CZ   1 
ATOM   2208 N  N    . PRO   A 1 461  ? 177.770 191.476 219.147 1.00 90.02  ? 1793 PRO   A N    1 
ATOM   2209 C  CA   . PRO   A 1 461  ? 177.526 192.670 219.961 1.00 93.45  ? 1793 PRO   A CA   1 
ATOM   2210 C  C    . PRO   A 1 461  ? 177.955 192.460 221.406 1.00 91.45  ? 1793 PRO   A C    1 
ATOM   2211 O  O    . PRO   A 1 461  ? 177.803 191.374 221.968 1.00 96.65  ? 1793 PRO   A O    1 
ATOM   2212 C  CB   . PRO   A 1 461  ? 176.010 192.867 219.852 1.00 84.92  ? 1793 PRO   A CB   1 
ATOM   2213 C  CG   . PRO   A 1 461  ? 175.639 192.232 218.564 1.00 92.64  ? 1793 PRO   A CG   1 
ATOM   2214 C  CD   . PRO   A 1 461  ? 176.612 191.115 218.315 1.00 89.03  ? 1793 PRO   A CD   1 
ATOM   2215 N  N    . GLY   A 1 462  ? 178.495 193.517 222.005 1.00 89.05  ? 1794 GLY   A N    1 
ATOM   2216 C  CA   . GLY   A 1 462  ? 178.960 193.461 223.378 1.00 89.05  ? 1794 GLY   A CA   1 
ATOM   2217 C  C    . GLY   A 1 462  ? 180.467 193.546 223.500 1.00 84.61  ? 1794 GLY   A C    1 
ATOM   2218 O  O    . GLY   A 1 462  ? 181.164 192.534 223.463 1.00 85.72  ? 1794 GLY   A O    1 
ATOM   2219 N  N    . THR   A 1 474  ? 175.615 200.363 229.205 1.00 132.55 ? 1806 THR   A N    1 
ATOM   2220 C  CA   . THR   A 1 474  ? 175.019 199.783 228.007 1.00 133.26 ? 1806 THR   A CA   1 
ATOM   2221 C  C    . THR   A 1 474  ? 176.065 199.025 227.196 1.00 129.17 ? 1806 THR   A C    1 
ATOM   2222 O  O    . THR   A 1 474  ? 176.865 199.635 226.486 1.00 126.32 ? 1806 THR   A O    1 
ATOM   2223 C  CB   . THR   A 1 474  ? 174.373 200.861 227.115 1.00 135.56 ? 1806 THR   A CB   1 
ATOM   2224 O  OG1  . THR   A 1 474  ? 173.345 201.539 227.847 1.00 135.53 ? 1806 THR   A OG1  1 
ATOM   2225 C  CG2  . THR   A 1 474  ? 173.763 200.229 225.873 1.00 126.65 ? 1806 THR   A CG2  1 
ATOM   2226 N  N    . LEU   A 1 475  ? 176.046 197.698 227.306 1.00 132.42 ? 1807 LEU   A N    1 
ATOM   2227 C  CA   . LEU   A 1 475  ? 176.984 196.811 226.603 1.00 130.03 ? 1807 LEU   A CA   1 
ATOM   2228 C  C    . LEU   A 1 475  ? 178.394 197.223 227.023 1.00 126.13 ? 1807 LEU   A C    1 
ATOM   2229 O  O    . LEU   A 1 475  ? 178.663 197.311 228.231 1.00 114.34 ? 1807 LEU   A O    1 
ATOM   2230 C  CB   . LEU   A 1 475  ? 176.700 196.853 225.106 1.00 121.80 ? 1807 LEU   A CB   1 
ATOM   2231 N  N    . LEU   A 1 476  ? 179.310 197.470 226.095 1.00 124.42 ? 1808 LEU   A N    1 
ATOM   2232 C  CA   . LEU   A 1 476  ? 180.620 197.986 226.451 1.00 113.30 ? 1808 LEU   A CA   1 
ATOM   2233 C  C    . LEU   A 1 476  ? 180.563 199.502 226.563 1.00 108.14 ? 1808 LEU   A C    1 
ATOM   2234 O  O    . LEU   A 1 476  ? 179.654 200.158 226.051 1.00 103.66 ? 1808 LEU   A O    1 
ATOM   2235 C  CB   . LEU   A 1 476  ? 181.677 197.609 225.418 1.00 104.47 ? 1808 LEU   A CB   1 
ATOM   2236 C  CG   . LEU   A 1 476  ? 181.626 198.357 224.085 1.00 94.08  ? 1808 LEU   A CG   1 
ATOM   2237 C  CD1  . LEU   A 1 476  ? 182.931 198.157 223.351 1.00 83.94  ? 1808 LEU   A CD1  1 
ATOM   2238 C  CD2  . LEU   A 1 476  ? 180.463 197.919 223.213 1.00 97.12  ? 1808 LEU   A CD2  1 
ATOM   2239 N  N    . LYS   A 1 477  ? 181.563 200.063 227.231 1.00 102.04 ? 1809 LYS   A N    1 
ATOM   2240 C  CA   . LYS   A 1 477  ? 181.696 201.505 227.331 1.00 98.70  ? 1809 LYS   A CA   1 
ATOM   2241 C  C    . LYS   A 1 477  ? 183.033 201.928 226.746 1.00 96.77  ? 1809 LYS   A C    1 
ATOM   2242 O  O    . LYS   A 1 477  ? 184.044 201.234 226.890 1.00 84.89  ? 1809 LYS   A O    1 
ATOM   2243 C  CB   . LYS   A 1 477  ? 181.571 201.990 228.776 1.00 90.78  ? 1809 LYS   A CB   1 
ATOM   2244 N  N    . LYS   A 1 478  ? 183.019 203.083 226.088 1.00 97.76  ? 1810 LYS   A N    1 
ATOM   2245 C  CA   . LYS   A 1 478  ? 184.170 203.625 225.382 1.00 78.86  ? 1810 LYS   A CA   1 
ATOM   2246 C  C    . LYS   A 1 478  ? 184.756 204.735 226.239 1.00 84.31  ? 1810 LYS   A C    1 
ATOM   2247 O  O    . LYS   A 1 478  ? 184.028 205.643 226.654 1.00 90.01  ? 1810 LYS   A O    1 
ATOM   2248 C  CB   . LYS   A 1 478  ? 183.751 204.170 224.017 1.00 65.51  ? 1810 LYS   A CB   1 
ATOM   2249 C  CG   . LYS   A 1 478  ? 182.828 203.261 223.234 1.00 55.34  ? 1810 LYS   A CG   1 
ATOM   2250 C  CD   . LYS   A 1 478  ? 183.530 201.999 222.792 1.00 58.91  ? 1810 LYS   A CD   1 
ATOM   2251 C  CE   . LYS   A 1 478  ? 184.387 202.252 221.573 1.00 53.62  ? 1810 LYS   A CE   1 
ATOM   2252 N  NZ   . LYS   A 1 478  ? 184.438 201.060 220.688 1.00 56.12  ? 1810 LYS   A NZ   1 
ATOM   2253 N  N    . TRP   A 1 479  ? 186.057 204.671 226.507 1.00 65.55  ? 1811 TRP   A N    1 
ATOM   2254 C  CA   . TRP   A 1 479  ? 186.708 205.666 227.346 1.00 61.77  ? 1811 TRP   A CA   1 
ATOM   2255 C  C    . TRP   A 1 479  ? 187.683 206.473 226.514 1.00 66.71  ? 1811 TRP   A C    1 
ATOM   2256 O  O    . TRP   A 1 479  ? 188.221 205.969 225.526 1.00 73.94  ? 1811 TRP   A O    1 
ATOM   2257 C  CB   . TRP   A 1 479  ? 187.447 205.038 228.526 1.00 61.37  ? 1811 TRP   A CB   1 
ATOM   2258 C  CG   . TRP   A 1 479  ? 186.560 204.665 229.662 1.00 71.75  ? 1811 TRP   A CG   1 
ATOM   2259 C  CD1  . TRP   A 1 479  ? 186.029 203.443 229.915 1.00 76.71  ? 1811 TRP   A CD1  1 
ATOM   2260 C  CD2  . TRP   A 1 479  ? 186.039 205.544 230.663 1.00 76.00  ? 1811 TRP   A CD2  1 
ATOM   2261 N  NE1  . TRP   A 1 479  ? 185.243 203.492 231.035 1.00 82.61  ? 1811 TRP   A NE1  1 
ATOM   2262 C  CE2  . TRP   A 1 479  ? 185.227 204.776 231.509 1.00 79.07  ? 1811 TRP   A CE2  1 
ATOM   2263 C  CE3  . TRP   A 1 479  ? 186.188 206.905 230.929 1.00 80.45  ? 1811 TRP   A CE3  1 
ATOM   2264 C  CZ2  . TRP   A 1 479  ? 184.571 205.320 232.606 1.00 84.10  ? 1811 TRP   A CZ2  1 
ATOM   2265 C  CZ3  . TRP   A 1 479  ? 185.539 207.444 232.018 1.00 84.64  ? 1811 TRP   A CZ3  1 
ATOM   2266 C  CH2  . TRP   A 1 479  ? 184.741 206.654 232.844 1.00 88.45  ? 1811 TRP   A CH2  1 
ATOM   2267 N  N    . ALA   A 1 480  ? 187.885 207.726 226.905 1.00 60.06  ? 1812 ALA   A N    1 
ATOM   2268 C  CA   . ALA   A 1 480  ? 188.902 208.594 226.332 1.00 44.80  ? 1812 ALA   A CA   1 
ATOM   2269 C  C    . ALA   A 1 480  ? 189.639 209.291 227.462 1.00 47.54  ? 1812 ALA   A C    1 
ATOM   2270 O  O    . ALA   A 1 480  ? 189.010 209.780 228.404 1.00 56.15  ? 1812 ALA   A O    1 
ATOM   2271 C  CB   . ALA   A 1 480  ? 188.278 209.622 225.395 1.00 60.24  ? 1812 ALA   A CB   1 
ATOM   2272 N  N    . LEU   A 1 481  ? 190.962 209.341 227.367 1.00 47.13  ? 1813 LEU   A N    1 
ATOM   2273 C  CA   . LEU   A 1 481  ? 191.798 209.813 228.461 1.00 68.72  ? 1813 LEU   A CA   1 
ATOM   2274 C  C    . LEU   A 1 481  ? 192.420 211.170 228.144 1.00 73.52  ? 1813 LEU   A C    1 
ATOM   2275 O  O    . LEU   A 1 481  ? 192.933 211.397 227.047 1.00 76.66  ? 1813 LEU   A O    1 
ATOM   2276 C  CB   . LEU   A 1 481  ? 192.900 208.797 228.765 1.00 71.30  ? 1813 LEU   A CB   1 
ATOM   2277 C  CG   . LEU   A 1 481  ? 192.607 207.589 229.663 1.00 65.16  ? 1813 LEU   A CG   1 
ATOM   2278 C  CD1  . LEU   A 1 481  ? 192.259 208.028 231.065 1.00 68.46  ? 1813 LEU   A CD1  1 
ATOM   2279 C  CD2  . LEU   A 1 481  ? 191.517 206.710 229.099 1.00 66.75  ? 1813 LEU   A CD2  1 
ATOM   2280 N  N    . TYR   A 1 482  ? 192.396 212.065 229.130 1.00 73.08  ? 1814 TYR   A N    1 
ATOM   2281 C  CA   . TYR   A 1 482  ? 192.918 213.414 228.952 1.00 73.25  ? 1814 TYR   A CA   1 
ATOM   2282 C  C    . TYR   A 1 482  ? 193.526 213.889 230.263 1.00 92.08  ? 1814 TYR   A C    1 
ATOM   2283 O  O    . TYR   A 1 482  ? 193.259 213.336 231.332 1.00 99.64  ? 1814 TYR   A O    1 
ATOM   2284 C  CB   . TYR   A 1 482  ? 191.829 214.379 228.482 1.00 74.20  ? 1814 TYR   A CB   1 
ATOM   2285 C  CG   . TYR   A 1 482  ? 190.689 214.611 229.443 1.00 75.78  ? 1814 TYR   A CG   1 
ATOM   2286 C  CD1  . TYR   A 1 482  ? 189.428 214.115 229.176 1.00 76.33  ? 1814 TYR   A CD1  1 
ATOM   2287 C  CD2  . TYR   A 1 482  ? 190.858 215.376 230.583 1.00 87.86  ? 1814 TYR   A CD2  1 
ATOM   2288 C  CE1  . TYR   A 1 482  ? 188.383 214.341 230.034 1.00 81.97  ? 1814 TYR   A CE1  1 
ATOM   2289 C  CE2  . TYR   A 1 482  ? 189.818 215.604 231.449 1.00 94.75  ? 1814 TYR   A CE2  1 
ATOM   2290 C  CZ   . TYR   A 1 482  ? 188.579 215.083 231.170 1.00 90.56  ? 1814 TYR   A CZ   1 
ATOM   2291 O  OH   . TYR   A 1 482  ? 187.529 215.307 232.031 1.00 90.78  ? 1814 TYR   A OH   1 
ATOM   2292 N  N    . SER   A 1 483  ? 194.336 214.942 230.172 1.00 100.71 ? 1815 SER   A N    1 
ATOM   2293 C  CA   . SER   A 1 483  ? 194.926 215.561 231.352 1.00 112.14 ? 1815 SER   A CA   1 
ATOM   2294 C  C    . SER   A 1 483  ? 195.393 216.978 231.041 1.00 113.86 ? 1815 SER   A C    1 
ATOM   2295 O  O    . SER   A 1 483  ? 196.321 217.171 230.251 1.00 117.54 ? 1815 SER   A O    1 
ATOM   2296 C  CB   . SER   A 1 483  ? 196.091 214.719 231.868 1.00 123.35 ? 1815 SER   A CB   1 
ATOM   2297 O  OG   . SER   A 1 483  ? 197.154 214.702 230.932 1.00 130.29 ? 1815 SER   A OG   1 
ATOM   2298 N  N    . PHE   A 1 484  ? 194.754 217.975 231.655 1.00 108.21 ? 1816 PHE   A N    1 
ATOM   2299 C  CA   . PHE   A 1 484  ? 195.112 219.363 231.383 1.00 111.81 ? 1816 PHE   A CA   1 
ATOM   2300 C  C    . PHE   A 1 484  ? 196.542 219.658 231.817 1.00 118.40 ? 1816 PHE   A C    1 
ATOM   2301 O  O    . PHE   A 1 484  ? 197.344 220.184 231.038 1.00 118.18 ? 1816 PHE   A O    1 
ATOM   2302 C  CB   . PHE   A 1 484  ? 194.124 220.290 232.083 1.00 106.44 ? 1816 PHE   A CB   1 
ATOM   2303 C  CG   . PHE   A 1 484  ? 192.702 220.042 231.695 1.00 105.89 ? 1816 PHE   A CG   1 
ATOM   2304 C  CD1  . PHE   A 1 484  ? 192.343 219.969 230.365 1.00 108.62 ? 1816 PHE   A CD1  1 
ATOM   2305 C  CD2  . PHE   A 1 484  ? 191.731 219.842 232.655 1.00 108.55 ? 1816 PHE   A CD2  1 
ATOM   2306 C  CE1  . PHE   A 1 484  ? 191.034 219.732 230.000 1.00 113.40 ? 1816 PHE   A CE1  1 
ATOM   2307 C  CE2  . PHE   A 1 484  ? 190.423 219.598 232.293 1.00 113.20 ? 1816 PHE   A CE2  1 
ATOM   2308 C  CZ   . PHE   A 1 484  ? 190.074 219.547 230.967 1.00 116.16 ? 1816 PHE   A CZ   1 
ATOM   2309 N  N    . ASN   A 1 485  ? 196.886 219.307 233.050 1.00 121.13 ? 1817 ASN   A N    1 
ATOM   2310 C  CA   . ASN   A 1 485  ? 198.264 219.348 233.512 1.00 122.66 ? 1817 ASN   A CA   1 
ATOM   2311 C  C    . ASN   A 1 485  ? 198.648 217.985 234.057 1.00 128.92 ? 1817 ASN   A C    1 
ATOM   2312 O  O    . ASN   A 1 485  ? 197.819 217.256 234.608 1.00 130.26 ? 1817 ASN   A O    1 
ATOM   2313 C  CB   . ASN   A 1 485  ? 198.506 220.422 234.580 1.00 116.71 ? 1817 ASN   A CB   1 
ATOM   2314 C  CG   . ASN   A 1 485  ? 198.446 221.823 234.018 1.00 121.89 ? 1817 ASN   A CG   1 
ATOM   2315 O  OD1  . ASN   A 1 485  ? 198.962 222.089 232.933 1.00 113.42 ? 1817 ASN   A OD1  1 
ATOM   2316 N  ND2  . ASN   A 1 485  ? 197.837 222.735 234.763 1.00 136.53 ? 1817 ASN   A ND2  1 
ATOM   2317 N  N    . ASP   A 1 486  ? 199.928 217.659 233.904 1.00 131.58 ? 1818 ASP   A N    1 
ATOM   2318 C  CA   . ASP   A 1 486  ? 200.406 216.306 234.126 1.00 126.46 ? 1818 ASP   A CA   1 
ATOM   2319 C  C    . ASP   A 1 486  ? 200.339 215.881 235.586 1.00 128.97 ? 1818 ASP   A C    1 
ATOM   2320 O  O    . ASP   A 1 486  ? 200.512 214.692 235.873 1.00 126.61 ? 1818 ASP   A O    1 
ATOM   2321 C  CB   . ASP   A 1 486  ? 201.829 216.200 233.594 1.00 121.51 ? 1818 ASP   A CB   1 
ATOM   2322 C  CG   . ASP   A 1 486  ? 201.882 216.312 232.088 1.00 125.49 ? 1818 ASP   A CG   1 
ATOM   2323 O  OD1  . ASP   A 1 486  ? 200.892 215.925 231.434 1.00 119.25 ? 1818 ASP   A OD1  1 
ATOM   2324 O  OD2  . ASP   A 1 486  ? 202.901 216.801 231.558 1.00 130.78 ? 1818 ASP   A OD2  1 
ATOM   2325 N  N    . GLY   A 1 487  ? 200.095 216.814 236.509 1.00 130.22 ? 1819 GLY   A N    1 
ATOM   2326 C  CA   . GLY   A 1 487  ? 199.923 216.429 237.900 1.00 122.29 ? 1819 GLY   A CA   1 
ATOM   2327 C  C    . GLY   A 1 487  ? 198.760 215.478 238.086 1.00 127.79 ? 1819 GLY   A C    1 
ATOM   2328 O  O    . GLY   A 1 487  ? 198.867 214.471 238.791 1.00 131.45 ? 1819 GLY   A O    1 
ATOM   2329 N  N    . GLU   A 1 488  ? 197.631 215.783 237.453 1.00 131.95 ? 1820 GLU   A N    1 
ATOM   2330 C  CA   . GLU   A 1 488  ? 196.515 214.853 237.408 1.00 131.82 ? 1820 GLU   A CA   1 
ATOM   2331 C  C    . GLU   A 1 488  ? 196.867 213.715 236.463 1.00 127.37 ? 1820 GLU   A C    1 
ATOM   2332 O  O    . GLU   A 1 488  ? 197.367 213.950 235.360 1.00 127.73 ? 1820 GLU   A O    1 
ATOM   2333 C  CB   . GLU   A 1 488  ? 195.241 215.558 236.946 1.00 132.99 ? 1820 GLU   A CB   1 
ATOM   2334 N  N    . GLU   A 1 489  ? 196.623 212.486 236.896 1.00 120.54 ? 1821 GLU   A N    1 
ATOM   2335 C  CA   . GLU   A 1 489  ? 197.028 211.312 236.133 1.00 126.03 ? 1821 GLU   A CA   1 
ATOM   2336 C  C    . GLU   A 1 489  ? 195.812 210.811 235.360 1.00 121.22 ? 1821 GLU   A C    1 
ATOM   2337 O  O    . GLU   A 1 489  ? 194.990 210.057 235.887 1.00 118.44 ? 1821 GLU   A O    1 
ATOM   2338 C  CB   . GLU   A 1 489  ? 197.614 210.242 237.053 1.00 126.13 ? 1821 GLU   A CB   1 
ATOM   2339 C  CG   . GLU   A 1 489  ? 197.693 208.801 236.501 1.00 130.21 ? 1821 GLU   A CG   1 
ATOM   2340 C  CD   . GLU   A 1 489  ? 198.255 208.671 235.084 1.00 131.95 ? 1821 GLU   A CD   1 
ATOM   2341 O  OE1  . GLU   A 1 489  ? 198.159 207.562 234.518 1.00 119.14 ? 1821 GLU   A OE1  1 
ATOM   2342 O  OE2  . GLU   A 1 489  ? 198.843 209.634 234.552 1.00 132.39 ? 1821 GLU   A OE2  1 
ATOM   2343 N  N    . HIS   A 1 490  ? 195.690 211.263 234.113 1.00 113.08 ? 1822 HIS   A N    1 
ATOM   2344 C  CA   . HIS   A 1 490  ? 194.753 210.703 233.141 1.00 101.48 ? 1822 HIS   A CA   1 
ATOM   2345 C  C    . HIS   A 1 490  ? 193.315 210.686 233.653 1.00 91.89  ? 1822 HIS   A C    1 
ATOM   2346 O  O    . HIS   A 1 490  ? 192.720 209.635 233.888 1.00 91.60  ? 1822 HIS   A O    1 
ATOM   2347 C  CB   . HIS   A 1 490  ? 195.195 209.306 232.711 1.00 97.99  ? 1822 HIS   A CB   1 
ATOM   2348 C  CG   . HIS   A 1 490  ? 196.215 209.311 231.619 1.00 96.39  ? 1822 HIS   A CG   1 
ATOM   2349 N  ND1  . HIS   A 1 490  ? 196.219 210.254 230.615 1.00 95.36  ? 1822 HIS   A ND1  1 
ATOM   2350 C  CD2  . HIS   A 1 490  ? 197.256 208.485 231.364 1.00 100.50 ? 1822 HIS   A CD2  1 
ATOM   2351 C  CE1  . HIS   A 1 490  ? 197.215 210.006 229.786 1.00 101.48 ? 1822 HIS   A CE1  1 
ATOM   2352 N  NE2  . HIS   A 1 490  ? 197.863 208.940 230.220 1.00 106.10 ? 1822 HIS   A NE2  1 
ATOM   2353 N  N    . GLN   A 1 491  ? 192.762 211.879 233.833 1.00 88.51  ? 1823 GLN   A N    1 
ATOM   2354 C  CA   . GLN   A 1 491  ? 191.323 211.985 234.003 1.00 89.54  ? 1823 GLN   A CA   1 
ATOM   2355 C  C    . GLN   A 1 491  ? 190.634 211.472 232.746 1.00 87.20  ? 1823 GLN   A C    1 
ATOM   2356 O  O    . GLN   A 1 491  ? 190.957 211.894 231.634 1.00 90.76  ? 1823 GLN   A O    1 
ATOM   2357 C  CB   . GLN   A 1 491  ? 190.928 213.434 234.274 1.00 97.95  ? 1823 GLN   A CB   1 
ATOM   2358 C  CG   . GLN   A 1 491  ? 191.399 213.970 235.608 1.00 113.46 ? 1823 GLN   A CG   1 
ATOM   2359 C  CD   . GLN   A 1 491  ? 190.910 215.378 235.868 1.00 128.57 ? 1823 GLN   A CD   1 
ATOM   2360 O  OE1  . GLN   A 1 491  ? 190.679 216.151 234.938 1.00 116.87 ? 1823 GLN   A OE1  1 
ATOM   2361 N  NE2  . GLN   A 1 491  ? 190.749 215.721 237.139 1.00 132.21 ? 1823 GLN   A NE2  1 
ATOM   2362 N  N    . LYS   A 1 492  ? 189.681 210.569 232.920 1.00 85.97  ? 1824 LYS   A N    1 
ATOM   2363 C  CA   . LYS   A 1 492  ? 189.059 209.885 231.799 1.00 83.34  ? 1824 LYS   A CA   1 
ATOM   2364 C  C    . LYS   A 1 492  ? 187.663 210.432 231.533 1.00 84.43  ? 1824 LYS   A C    1 
ATOM   2365 O  O    . LYS   A 1 492  ? 186.974 210.896 232.444 1.00 85.36  ? 1824 LYS   A O    1 
ATOM   2366 C  CB   . LYS   A 1 492  ? 188.984 208.383 232.065 1.00 74.47  ? 1824 LYS   A CB   1 
ATOM   2367 N  N    . ILE   A 1 493  ? 187.251 210.375 230.268 1.00 78.82  ? 1825 ILE   A N    1 
ATOM   2368 C  CA   . ILE   A 1 493  ? 185.920 210.809 229.863 1.00 84.19  ? 1825 ILE   A CA   1 
ATOM   2369 C  C    . ILE   A 1 493  ? 185.311 209.777 228.927 1.00 87.01  ? 1825 ILE   A C    1 
ATOM   2370 O  O    . ILE   A 1 493  ? 186.008 209.131 228.138 1.00 79.29  ? 1825 ILE   A O    1 
ATOM   2371 C  CB   . ILE   A 1 493  ? 185.937 212.199 229.191 1.00 82.33  ? 1825 ILE   A CB   1 
ATOM   2372 C  CG1  . ILE   A 1 493  ? 184.511 212.727 229.008 1.00 92.00  ? 1825 ILE   A CG1  1 
ATOM   2373 C  CG2  . ILE   A 1 493  ? 186.683 212.155 227.871 1.00 68.01  ? 1825 ILE   A CG2  1 
ATOM   2374 C  CD1  . ILE   A 1 493  ? 184.440 214.188 228.661 1.00 96.81  ? 1825 ILE   A CD1  1 
ATOM   2375 N  N    . LEU   A 1 494  ? 183.994 209.620 229.028 1.00 95.27  ? 1826 LEU   A N    1 
ATOM   2376 C  CA   . LEU   A 1 494  ? 183.263 208.793 228.083 1.00 91.56  ? 1826 LEU   A CA   1 
ATOM   2377 C  C    . LEU   A 1 494  ? 183.381 209.389 226.691 1.00 88.99  ? 1826 LEU   A C    1 
ATOM   2378 O  O    . LEU   A 1 494  ? 183.546 210.600 226.531 1.00 90.97  ? 1826 LEU   A O    1 
ATOM   2379 C  CB   . LEU   A 1 494  ? 181.792 208.695 228.481 1.00 104.02 ? 1826 LEU   A CB   1 
ATOM   2380 C  CG   . LEU   A 1 494  ? 181.362 207.768 229.620 1.00 121.90 ? 1826 LEU   A CG   1 
ATOM   2381 C  CD1  . LEU   A 1 494  ? 181.802 208.305 230.973 1.00 111.63 ? 1826 LEU   A CD1  1 
ATOM   2382 C  CD2  . LEU   A 1 494  ? 179.851 207.577 229.589 1.00 136.57 ? 1826 LEU   A CD2  1 
ATOM   2383 N  N    . LEU   A 1 495  ? 183.299 208.529 225.677 1.00 82.47  ? 1827 LEU   A N    1 
ATOM   2384 C  CA   . LEU   A 1 495  ? 183.537 208.981 224.311 1.00 67.97  ? 1827 LEU   A CA   1 
ATOM   2385 C  C    . LEU   A 1 495  ? 182.385 209.814 223.774 1.00 73.73  ? 1827 LEU   A C    1 
ATOM   2386 O  O    . LEU   A 1 495  ? 182.594 210.695 222.939 1.00 79.03  ? 1827 LEU   A O    1 
ATOM   2387 C  CB   . LEU   A 1 495  ? 183.790 207.793 223.396 1.00 59.23  ? 1827 LEU   A CB   1 
ATOM   2388 C  CG   . LEU   A 1 495  ? 184.733 208.125 222.249 1.00 52.19  ? 1827 LEU   A CG   1 
ATOM   2389 C  CD1  . LEU   A 1 495  ? 186.000 208.735 222.785 1.00 51.85  ? 1827 LEU   A CD1  1 
ATOM   2390 C  CD2  . LEU   A 1 495  ? 185.037 206.877 221.460 1.00 54.00  ? 1827 LEU   A CD2  1 
ATOM   2391 N  N    . ASP   A 1 496  ? 181.162 209.536 224.205 1.00 85.88  ? 1828 ASP   A N    1 
ATOM   2392 C  CA   . ASP   A 1 496  ? 180.011 210.242 223.654 1.00 94.27  ? 1828 ASP   A CA   1 
ATOM   2393 C  C    . ASP   A 1 496  ? 180.042 211.731 223.989 1.00 99.35  ? 1828 ASP   A C    1 
ATOM   2394 O  O    . ASP   A 1 496  ? 179.817 212.586 223.120 1.00 101.48 ? 1828 ASP   A O    1 
ATOM   2395 C  CB   . ASP   A 1 496  ? 178.726 209.605 224.174 1.00 110.48 ? 1828 ASP   A CB   1 
ATOM   2396 C  CG   . ASP   A 1 496  ? 178.508 208.218 223.618 1.00 121.71 ? 1828 ASP   A CG   1 
ATOM   2397 O  OD1  . ASP   A 1 496  ? 178.967 207.956 222.487 1.00 105.63 ? 1828 ASP   A OD1  1 
ATOM   2398 O  OD2  . ASP   A 1 496  ? 177.894 207.385 224.317 1.00 137.86 ? 1828 ASP   A OD2  1 
ATOM   2399 N  N    . ASP   A 1 497  ? 180.324 212.047 225.250 1.00 99.13  ? 1829 ASP   A N    1 
ATOM   2400 C  CA   . ASP   A 1 497  ? 180.367 213.432 225.690 1.00 98.45  ? 1829 ASP   A CA   1 
ATOM   2401 C  C    . ASP   A 1 497  ? 181.430 214.167 224.892 1.00 90.12  ? 1829 ASP   A C    1 
ATOM   2402 O  O    . ASP   A 1 497  ? 181.211 215.285 224.412 1.00 87.27  ? 1829 ASP   A O    1 
ATOM   2403 C  CB   . ASP   A 1 497  ? 180.670 213.502 227.184 1.00 108.81 ? 1829 ASP   A CB   1 
ATOM   2404 C  CG   . ASP   A 1 497  ? 179.538 212.972 228.025 1.00 124.38 ? 1829 ASP   A CG   1 
ATOM   2405 O  OD1  . ASP   A 1 497  ? 178.378 213.068 227.581 1.00 133.67 ? 1829 ASP   A OD1  1 
ATOM   2406 O  OD2  . ASP   A 1 497  ? 179.811 212.450 229.125 1.00 128.26 ? 1829 ASP   A OD2  1 
ATOM   2407 N  N    . LEU   A 1 498  ? 182.582 213.521 224.728 1.00 87.00  ? 1830 LEU   A N    1 
ATOM   2408 C  CA   . LEU   A 1 498  ? 183.650 214.118 223.945 1.00 78.81  ? 1830 LEU   A CA   1 
ATOM   2409 C  C    . LEU   A 1 498  ? 183.254 214.243 222.483 1.00 81.17  ? 1830 LEU   A C    1 
ATOM   2410 O  O    . LEU   A 1 498  ? 183.712 215.156 221.793 1.00 88.99  ? 1830 LEU   A O    1 
ATOM   2411 C  CB   . LEU   A 1 498  ? 184.924 213.296 224.105 1.00 69.83  ? 1830 LEU   A CB   1 
ATOM   2412 C  CG   . LEU   A 1 498  ? 186.199 213.848 223.493 1.00 54.76  ? 1830 LEU   A CG   1 
ATOM   2413 C  CD1  . LEU   A 1 498  ? 187.339 213.510 224.402 1.00 41.40  ? 1830 LEU   A CD1  1 
ATOM   2414 C  CD2  . LEU   A 1 498  ? 186.418 213.236 222.139 1.00 55.41  ? 1830 LEU   A CD2  1 
ATOM   2415 N  N    . MET   A 1 499  ? 182.392 213.355 221.996 1.00 79.29  ? 1831 MET   A N    1 
ATOM   2416 C  CA   . MET   A 1 499  ? 181.919 213.483 220.626 1.00 84.43  ? 1831 MET   A CA   1 
ATOM   2417 C  C    . MET   A 1 499  ? 181.083 214.741 220.459 1.00 97.07  ? 1831 MET   A C    1 
ATOM   2418 O  O    . MET   A 1 499  ? 181.220 215.453 219.460 1.00 101.24 ? 1831 MET   A O    1 
ATOM   2419 C  CB   . MET   A 1 499  ? 181.120 212.247 220.223 1.00 85.75  ? 1831 MET   A CB   1 
ATOM   2420 N  N    . LYS   A 1 500  ? 180.206 215.029 221.422 1.00 96.96  ? 1832 LYS   A N    1 
ATOM   2421 C  CA   . LYS   A 1 500  ? 179.470 216.296 221.364 1.00 99.12  ? 1832 LYS   A CA   1 
ATOM   2422 C  C    . LYS   A 1 500  ? 180.407 217.493 221.500 1.00 97.59  ? 1832 LYS   A C    1 
ATOM   2423 O  O    . LYS   A 1 500  ? 180.246 218.503 220.800 1.00 99.66  ? 1832 LYS   A O    1 
ATOM   2424 C  CB   . LYS   A 1 500  ? 178.365 216.358 222.423 1.00 105.16 ? 1832 LYS   A CB   1 
ATOM   2425 C  CG   . LYS   A 1 500  ? 177.023 215.762 221.994 1.00 111.52 ? 1832 LYS   A CG   1 
ATOM   2426 C  CD   . LYS   A 1 500  ? 177.056 214.280 221.687 1.00 115.80 ? 1832 LYS   A CD   1 
ATOM   2427 C  CE   . LYS   A 1 500  ? 176.958 213.469 222.964 1.00 113.53 ? 1832 LYS   A CE   1 
ATOM   2428 N  NZ   . LYS   A 1 500  ? 176.816 212.015 222.686 1.00 111.23 ? 1832 LYS   A NZ   1 
ATOM   2429 N  N    . LYS   A 1 501  ? 181.389 217.396 222.397 1.00 95.26  ? 1833 LYS   A N    1 
ATOM   2430 C  CA   A LYS   A 1 501  ? 182.346 218.483 222.563 0.72 92.03  ? 1833 LYS   A CA   1 
ATOM   2431 C  CA   B LYS   A 1 501  ? 182.353 218.478 222.569 0.28 92.17  ? 1833 LYS   A CA   1 
ATOM   2432 C  C    . LYS   A 1 501  ? 183.183 218.703 221.312 1.00 90.59  ? 1833 LYS   A C    1 
ATOM   2433 O  O    . LYS   A 1 501  ? 183.699 219.803 221.105 1.00 94.50  ? 1833 LYS   A O    1 
ATOM   2434 C  CB   A LYS   A 1 501  ? 183.260 218.194 223.751 0.72 91.09  ? 1833 LYS   A CB   1 
ATOM   2435 C  CB   B LYS   A 1 501  ? 183.265 218.178 223.759 0.28 91.16  ? 1833 LYS   A CB   1 
ATOM   2436 C  CG   A LYS   A 1 501  ? 183.918 219.418 224.359 0.72 94.00  ? 1833 LYS   A CG   1 
ATOM   2437 C  CG   B LYS   A 1 501  ? 183.360 219.281 224.802 0.28 93.42  ? 1833 LYS   A CG   1 
ATOM   2438 C  CD   A LYS   A 1 501  ? 183.081 219.984 225.493 0.72 94.48  ? 1833 LYS   A CD   1 
ATOM   2439 C  CD   B LYS   A 1 501  ? 183.442 220.650 224.153 0.28 94.18  ? 1833 LYS   A CD   1 
ATOM   2440 C  CE   A LYS   A 1 501  ? 183.515 219.442 226.848 0.72 87.24  ? 1833 LYS   A CE   1 
ATOM   2441 C  CE   B LYS   A 1 501  ? 183.904 221.706 225.139 0.28 94.15  ? 1833 LYS   A CE   1 
ATOM   2442 N  NZ   A LYS   A 1 501  ? 184.016 218.042 226.796 0.72 84.34  ? 1833 LYS   A NZ   1 
ATOM   2443 N  NZ   B LYS   A 1 501  ? 183.994 223.044 224.498 0.28 93.83  ? 1833 LYS   A NZ   1 
ATOM   2444 N  N    . ALA   A 1 502  ? 183.339 217.680 220.482 1.00 88.56  ? 1834 ALA   A N    1 
ATOM   2445 C  CA   . ALA   A 1 502  ? 184.059 217.831 219.228 1.00 83.97  ? 1834 ALA   A CA   1 
ATOM   2446 C  C    . ALA   A 1 502  ? 183.161 218.292 218.096 1.00 91.59  ? 1834 ALA   A C    1 
ATOM   2447 O  O    . ALA   A 1 502  ? 183.625 218.997 217.194 1.00 90.48  ? 1834 ALA   A O    1 
ATOM   2448 C  CB   . ALA   A 1 502  ? 184.723 216.512 218.840 1.00 85.36  ? 1834 ALA   A CB   1 
ATOM   2449 N  N    . GLU   A 1 503  ? 181.890 217.894 218.112 1.00 99.75  ? 1835 GLU   A N    1 
ATOM   2450 C  CA   . GLU   A 1 503  ? 180.956 218.386 217.108 1.00 106.19 ? 1835 GLU   A CA   1 
ATOM   2451 C  C    . GLU   A 1 503  ? 180.751 219.885 217.259 1.00 108.56 ? 1835 GLU   A C    1 
ATOM   2452 O  O    . GLU   A 1 503  ? 180.730 220.618 216.263 1.00 112.89 ? 1835 GLU   A O    1 
ATOM   2453 C  CB   . GLU   A 1 503  ? 179.634 217.610 217.196 1.00 103.30 ? 1835 GLU   A CB   1 
ATOM   2454 C  CG   . GLU   A 1 503  ? 178.467 218.132 216.343 1.00 117.18 ? 1835 GLU   A CG   1 
ATOM   2455 C  CD   . GLU   A 1 503  ? 177.790 219.379 216.887 1.00 123.29 ? 1835 GLU   A CD   1 
ATOM   2456 O  OE1  . GLU   A 1 503  ? 176.979 219.983 216.155 1.00 116.10 ? 1835 GLU   A OE1  1 
ATOM   2457 O  OE2  . GLU   A 1 503  ? 178.019 219.720 218.064 1.00 124.39 ? 1835 GLU   A OE2  1 
ATOM   2458 N  N    . GLU   A 1 504  ? 180.612 220.366 218.494 1.00 106.61 ? 1836 GLU   A N    1 
ATOM   2459 C  CA   . GLU   A 1 504  ? 180.496 221.799 218.754 1.00 103.36 ? 1836 GLU   A CA   1 
ATOM   2460 C  C    . GLU   A 1 504  ? 181.796 222.281 219.388 1.00 102.33 ? 1836 GLU   A C    1 
ATOM   2461 O  O    . GLU   A 1 504  ? 182.154 221.864 220.492 1.00 105.56 ? 1836 GLU   A O    1 
ATOM   2462 C  CB   . GLU   A 1 504  ? 179.270 222.111 219.616 1.00 104.46 ? 1836 GLU   A CB   1 
ATOM   2463 C  CG   . GLU   A 1 504  ? 179.319 221.660 221.065 1.00 100.74 ? 1836 GLU   A CG   1 
ATOM   2464 C  CD   . GLU   A 1 504  ? 177.957 221.668 221.720 1.00 104.93 ? 1836 GLU   A CD   1 
ATOM   2465 O  OE1  . GLU   A 1 504  ? 177.205 220.687 221.544 1.00 105.27 ? 1836 GLU   A OE1  1 
ATOM   2466 O  OE2  . GLU   A 1 504  ? 177.636 222.660 222.406 1.00 111.53 ? 1836 GLU   A OE2  1 
ATOM   2467 N  N    . GLY   A 1 505  ? 182.516 223.137 218.678 1.00 100.02 ? 1837 GLY   A N    1 
ATOM   2468 C  CA   . GLY   A 1 505  ? 183.815 223.560 219.146 1.00 104.03 ? 1837 GLY   A CA   1 
ATOM   2469 C  C    . GLY   A 1 505  ? 184.855 222.486 218.904 1.00 103.24 ? 1837 GLY   A C    1 
ATOM   2470 O  O    . GLY   A 1 505  ? 184.594 221.440 218.312 1.00 104.61 ? 1837 GLY   A O    1 
ATOM   2471 N  N    . ASP   A 1 506  ? 186.070 222.758 219.371 1.00 100.91 ? 1838 ASP   A N    1 
ATOM   2472 C  CA   . ASP   A 1 506  ? 187.158 221.812 219.183 1.00 99.99  ? 1838 ASP   A CA   1 
ATOM   2473 C  C    . ASP   A 1 506  ? 188.024 221.638 220.427 1.00 93.24  ? 1838 ASP   A C    1 
ATOM   2474 O  O    . ASP   A 1 506  ? 188.742 220.640 220.517 1.00 95.72  ? 1838 ASP   A O    1 
ATOM   2475 C  CB   . ASP   A 1 506  ? 188.008 222.251 217.969 1.00 99.25  ? 1838 ASP   A CB   1 
ATOM   2476 C  CG   . ASP   A 1 506  ? 189.272 221.421 217.774 1.00 97.40  ? 1838 ASP   A CG   1 
ATOM   2477 O  OD1  . ASP   A 1 506  ? 190.235 221.563 218.554 1.00 98.93  ? 1838 ASP   A OD1  1 
ATOM   2478 O  OD2  . ASP   A 1 506  ? 189.303 220.620 216.819 1.00 87.87  ? 1838 ASP   A OD2  1 
ATOM   2479 N  N    . LEU   A 1 507  ? 187.942 222.530 221.407 1.00 94.46  ? 1839 LEU   A N    1 
ATOM   2480 C  CA   . LEU   A 1 507  ? 188.837 222.516 222.556 1.00 102.74 ? 1839 LEU   A CA   1 
ATOM   2481 C  C    . LEU   A 1 507  ? 188.153 221.891 223.765 1.00 101.83 ? 1839 LEU   A C    1 
ATOM   2482 O  O    . LEU   A 1 507  ? 186.957 221.593 223.749 1.00 99.16  ? 1839 LEU   A O    1 
ATOM   2483 C  CB   . LEU   A 1 507  ? 189.300 223.937 222.891 1.00 111.23 ? 1839 LEU   A CB   1 
ATOM   2484 C  CG   . LEU   A 1 507  ? 190.175 224.647 221.859 1.00 111.95 ? 1839 LEU   A CG   1 
ATOM   2485 C  CD1  . LEU   A 1 507  ? 190.421 226.080 222.288 1.00 116.80 ? 1839 LEU   A CD1  1 
ATOM   2486 C  CD2  . LEU   A 1 507  ? 191.487 223.919 221.652 1.00 101.48 ? 1839 LEU   A CD2  1 
ATOM   2487 N  N    . LEU   A 1 508  ? 188.935 221.696 224.828 1.00 101.13 ? 1840 LEU   A N    1 
ATOM   2488 C  CA   . LEU   A 1 508  ? 188.424 221.290 226.137 1.00 98.48  ? 1840 LEU   A CA   1 
ATOM   2489 C  C    . LEU   A 1 508  ? 188.699 222.416 227.126 1.00 105.03 ? 1840 LEU   A C    1 
ATOM   2490 O  O    . LEU   A 1 508  ? 189.840 222.608 227.551 1.00 108.05 ? 1840 LEU   A O    1 
ATOM   2491 C  CB   . LEU   A 1 508  ? 189.065 219.991 226.614 1.00 95.08  ? 1840 LEU   A CB   1 
ATOM   2492 C  CG   . LEU   A 1 508  ? 188.721 218.700 225.885 1.00 95.47  ? 1840 LEU   A CG   1 
ATOM   2493 C  CD1  . LEU   A 1 508  ? 189.857 217.716 226.020 1.00 88.36  ? 1840 LEU   A CD1  1 
ATOM   2494 C  CD2  . LEU   A 1 508  ? 187.442 218.111 226.447 1.00 95.75  ? 1840 LEU   A CD2  1 
ATOM   2495 N  N    . VAL   A 1 509  ? 187.653 223.148 227.507 1.00 104.09 ? 1841 VAL   A N    1 
ATOM   2496 C  CA   . VAL   A 1 509  ? 187.815 224.214 228.485 1.00 106.09 ? 1841 VAL   A CA   1 
ATOM   2497 C  C    . VAL   A 1 509  ? 188.202 223.620 229.833 1.00 109.20 ? 1841 VAL   A C    1 
ATOM   2498 O  O    . VAL   A 1 509  ? 187.674 222.583 230.257 1.00 107.70 ? 1841 VAL   A O    1 
ATOM   2499 C  CB   . VAL   A 1 509  ? 186.532 225.058 228.588 1.00 106.51 ? 1841 VAL   A CB   1 
ATOM   2500 C  CG1  . VAL   A 1 509  ? 186.237 225.731 227.262 1.00 115.39 ? 1841 VAL   A CG1  1 
ATOM   2501 C  CG2  . VAL   A 1 509  ? 185.353 224.194 229.012 1.00 104.02 ? 1841 VAL   A CG2  1 
ATOM   2502 N  N    . ASN   A 1 510  ? 189.147 224.264 230.498 1.00 115.47 ? 1842 ASN   A N    1 
ATOM   2503 C  CA   . ASN   A 1 510  ? 189.610 223.810 231.796 1.00 117.79 ? 1842 ASN   A CA   1 
ATOM   2504 C  C    . ASN   A 1 510  ? 188.596 224.159 232.884 1.00 119.97 ? 1842 ASN   A C    1 
ATOM   2505 O  O    . ASN   A 1 510  ? 187.825 225.110 232.739 1.00 123.69 ? 1842 ASN   A O    1 
ATOM   2506 C  CB   . ASN   A 1 510  ? 190.957 224.444 232.126 1.00 118.25 ? 1842 ASN   A CB   1 
ATOM   2507 N  N    . PRO   A 1 511  ? 188.571 223.393 233.978 1.00 116.03 ? 1843 PRO   A N    1 
ATOM   2508 C  CA   . PRO   A 1 511  ? 187.704 223.774 235.106 1.00 122.66 ? 1843 PRO   A CA   1 
ATOM   2509 C  C    . PRO   A 1 511  ? 187.997 225.166 235.630 1.00 125.17 ? 1843 PRO   A C    1 
ATOM   2510 O  O    . PRO   A 1 511  ? 187.072 225.893 236.012 1.00 121.65 ? 1843 PRO   A O    1 
ATOM   2511 C  CB   . PRO   A 1 511  ? 188.007 222.698 236.157 1.00 115.43 ? 1843 PRO   A CB   1 
ATOM   2512 C  CG   . PRO   A 1 511  ? 188.513 221.538 235.386 1.00 106.56 ? 1843 PRO   A CG   1 
ATOM   2513 C  CD   . PRO   A 1 511  ? 189.200 222.079 234.172 1.00 106.57 ? 1843 PRO   A CD   1 
ATOM   2514 N  N    . ASP   A 1 512  ? 189.266 225.558 235.658 1.00 128.03 ? 1844 ASP   A N    1 
ATOM   2515 C  CA   . ASP   A 1 512  ? 189.677 226.912 236.003 1.00 126.55 ? 1844 ASP   A CA   1 
ATOM   2516 C  C    . ASP   A 1 512  ? 190.179 227.576 234.728 1.00 127.94 ? 1844 ASP   A C    1 
ATOM   2517 O  O    . ASP   A 1 512  ? 191.305 227.315 234.291 1.00 127.22 ? 1844 ASP   A O    1 
ATOM   2518 C  CB   . ASP   A 1 512  ? 190.753 226.901 237.086 1.00 119.62 ? 1844 ASP   A CB   1 
ATOM   2519 N  N    . GLN   A 1 513  ? 189.343 228.427 234.139 1.00 127.63 ? 1845 GLN   A N    1 
ATOM   2520 C  CA   . GLN   A 1 513  ? 189.655 229.104 232.884 1.00 124.34 ? 1845 GLN   A CA   1 
ATOM   2521 C  C    . GLN   A 1 513  ? 190.004 228.105 231.787 1.00 116.42 ? 1845 GLN   A C    1 
ATOM   2522 O  O    . GLN   A 1 513  ? 190.901 228.343 230.980 1.00 115.61 ? 1845 GLN   A O    1 
ATOM   2523 C  CB   . GLN   A 1 513  ? 190.800 230.100 233.078 1.00 127.16 ? 1845 GLN   A CB   1 
ATOM   2524 N  N    . THR   A 1 517  ? 194.442 225.560 226.430 1.00 124.83 ? 1849 THR   A N    1 
ATOM   2525 C  CA   . THR   A 1 517  ? 193.939 224.248 226.814 1.00 114.60 ? 1849 THR   A CA   1 
ATOM   2526 C  C    . THR   A 1 517  ? 194.225 223.217 225.730 1.00 113.02 ? 1849 THR   A C    1 
ATOM   2527 O  O    . THR   A 1 517  ? 194.962 223.494 224.786 1.00 108.49 ? 1849 THR   A O    1 
ATOM   2528 C  CB   . THR   A 1 517  ? 192.439 224.288 227.095 1.00 106.60 ? 1849 THR   A CB   1 
ATOM   2529 O  OG1  . THR   A 1 517  ? 192.021 223.026 227.626 1.00 98.98  ? 1849 THR   A OG1  1 
ATOM   2530 C  CG2  . THR   A 1 517  ? 191.667 224.590 225.820 1.00 110.37 ? 1849 THR   A CG2  1 
ATOM   2531 N  N    . ILE   A 1 518  ? 193.644 222.029 225.865 1.00 114.61 ? 1850 ILE   A N    1 
ATOM   2532 C  CA   . ILE   A 1 518  ? 193.957 220.925 224.960 1.00 110.37 ? 1850 ILE   A CA   1 
ATOM   2533 C  C    . ILE   A 1 518  ? 192.818 220.696 223.972 1.00 97.07  ? 1850 ILE   A C    1 
ATOM   2534 O  O    . ILE   A 1 518  ? 191.639 220.712 224.353 1.00 97.62  ? 1850 ILE   A O    1 
ATOM   2535 C  CB   . ILE   A 1 518  ? 194.300 219.650 225.753 1.00 106.03 ? 1850 ILE   A CB   1 
ATOM   2536 C  CG1  . ILE   A 1 518  ? 194.969 218.614 224.847 1.00 96.53  ? 1850 ILE   A CG1  1 
ATOM   2537 C  CG2  . ILE   A 1 518  ? 193.081 219.086 226.462 1.00 92.89  ? 1850 ILE   A CG2  1 
ATOM   2538 C  CD1  . ILE   A 1 518  ? 195.864 217.652 225.586 1.00 89.27  ? 1850 ILE   A CD1  1 
ATOM   2539 N  N    . PRO   A 1 519  ? 193.122 220.515 222.694 1.00 86.42  ? 1851 PRO   A N    1 
ATOM   2540 C  CA   . PRO   A 1 519  ? 192.064 220.277 221.709 1.00 92.50  ? 1851 PRO   A CA   1 
ATOM   2541 C  C    . PRO   A 1 519  ? 191.690 218.809 221.622 1.00 86.36  ? 1851 PRO   A C    1 
ATOM   2542 O  O    . PRO   A 1 519  ? 192.380 217.958 222.187 1.00 85.78  ? 1851 PRO   A O    1 
ATOM   2543 C  CB   . PRO   A 1 519  ? 192.695 220.760 220.401 1.00 86.48  ? 1851 PRO   A CB   1 
ATOM   2544 C  CG   . PRO   A 1 519  ? 194.140 220.541 220.607 1.00 83.91  ? 1851 PRO   A CG   1 
ATOM   2545 C  CD   . PRO   A 1 519  ? 194.414 220.798 222.055 1.00 86.29  ? 1851 PRO   A CD   1 
ATOM   2546 N  N    . ILE   A 1 520  ? 190.614 218.500 220.896 1.00 75.95  ? 1852 ILE   A N    1 
ATOM   2547 C  CA   . ILE   A 1 520  ? 190.214 217.110 220.721 1.00 52.24  ? 1852 ILE   A CA   1 
ATOM   2548 C  C    . ILE   A 1 520  ? 191.271 216.338 219.949 1.00 58.09  ? 1852 ILE   A C    1 
ATOM   2549 O  O    . ILE   A 1 520  ? 191.522 215.164 220.235 1.00 62.08  ? 1852 ILE   A O    1 
ATOM   2550 C  CB   . ILE   A 1 520  ? 188.843 217.046 220.032 1.00 48.74  ? 1852 ILE   A CB   1 
ATOM   2551 C  CG1  . ILE   A 1 520  ? 187.795 217.707 220.913 1.00 54.12  ? 1852 ILE   A CG1  1 
ATOM   2552 C  CG2  . ILE   A 1 520  ? 188.452 215.631 219.727 1.00 47.06  ? 1852 ILE   A CG2  1 
ATOM   2553 C  CD1  . ILE   A 1 520  ? 187.882 217.298 222.340 1.00 58.04  ? 1852 ILE   A CD1  1 
ATOM   2554 N  N    . SER   A 1 521  ? 191.942 216.985 219.000 1.00 62.55  ? 1853 SER   A N    1 
ATOM   2555 C  CA   . SER   A 1 521  ? 192.875 216.298 218.117 1.00 63.07  ? 1853 SER   A CA   1 
ATOM   2556 C  C    . SER   A 1 521  ? 193.991 215.622 218.897 1.00 61.28  ? 1853 SER   A C    1 
ATOM   2557 O  O    . SER   A 1 521  ? 194.652 214.717 218.383 1.00 58.32  ? 1853 SER   A O    1 
ATOM   2558 C  CB   . SER   A 1 521  ? 193.470 217.272 217.105 1.00 67.82  ? 1853 SER   A CB   1 
ATOM   2559 O  OG   . SER   A 1 521  ? 194.399 216.614 216.268 1.00 61.54  ? 1853 SER   A OG   1 
ATOM   2560 N  N    . GLN   A 1 522  ? 194.223 216.068 220.128 1.00 66.98  ? 1854 GLN   A N    1 
ATOM   2561 C  CA   . GLN   A 1 522  ? 195.167 215.409 221.013 1.00 67.30  ? 1854 GLN   A CA   1 
ATOM   2562 C  C    . GLN   A 1 522  ? 194.517 214.497 222.035 1.00 65.32  ? 1854 GLN   A C    1 
ATOM   2563 O  O    . GLN   A 1 522  ? 195.226 213.973 222.899 1.00 72.70  ? 1854 GLN   A O    1 
ATOM   2564 C  CB   . GLN   A 1 522  ? 196.025 216.440 221.761 1.00 74.74  ? 1854 GLN   A CB   1 
ATOM   2565 C  CG   . GLN   A 1 522  ? 196.323 217.686 220.967 1.00 82.09  ? 1854 GLN   A CG   1 
ATOM   2566 C  CD   . GLN   A 1 522  ? 197.242 218.623 221.706 1.00 86.02  ? 1854 GLN   A CD   1 
ATOM   2567 O  OE1  . GLN   A 1 522  ? 197.802 218.271 222.744 1.00 83.71  ? 1854 GLN   A OE1  1 
ATOM   2568 N  NE2  . GLN   A 1 522  ? 197.419 219.821 221.168 1.00 88.28  ? 1854 GLN   A NE2  1 
ATOM   2569 N  N    . ILE   A 1 523  ? 193.207 214.290 221.973 1.00 63.47  ? 1855 ILE   A N    1 
ATOM   2570 C  CA   . ILE   A 1 523  ? 192.521 213.452 222.941 1.00 55.80  ? 1855 ILE   A CA   1 
ATOM   2571 C  C    . ILE   A 1 523  ? 191.877 212.246 222.278 1.00 52.88  ? 1855 ILE   A C    1 
ATOM   2572 O  O    . ILE   A 1 523  ? 192.064 211.115 222.720 1.00 59.75  ? 1855 ILE   A O    1 
ATOM   2573 C  CB   . ILE   A 1 523  ? 191.469 214.277 223.702 1.00 53.16  ? 1855 ILE   A CB   1 
ATOM   2574 C  CG1  . ILE   A 1 523  ? 192.140 215.456 224.393 1.00 70.10  ? 1855 ILE   A CG1  1 
ATOM   2575 C  CG2  . ILE   A 1 523  ? 190.780 213.410 224.702 1.00 43.65  ? 1855 ILE   A CG2  1 
ATOM   2576 C  CD1  . ILE   A 1 523  ? 193.170 215.062 225.383 1.00 77.85  ? 1855 ILE   A CD1  1 
ATOM   2577 N  N    . ALA   A 1 524  ? 191.119 212.478 221.226 1.00 52.93  ? 1856 ALA   A N    1 
ATOM   2578 C  CA   . ALA   A 1 524  ? 190.475 211.425 220.463 1.00 49.23  ? 1856 ALA   A CA   1 
ATOM   2579 C  C    . ALA   A 1 524  ? 190.499 211.800 218.991 1.00 47.26  ? 1856 ALA   A C    1 
ATOM   2580 O  O    . ALA   A 1 524  ? 189.490 212.270 218.454 1.00 45.70  ? 1856 ALA   A O    1 
ATOM   2581 C  CB   . ALA   A 1 524  ? 189.046 211.216 220.944 1.00 57.81  ? 1856 ALA   A CB   1 
ATOM   2582 N  N    . PRO   A 1 525  ? 191.623 211.598 218.317 1.00 51.18  ? 1857 PRO   A N    1 
ATOM   2583 C  CA   . PRO   A 1 525  ? 191.788 212.104 216.950 1.00 54.13  ? 1857 PRO   A CA   1 
ATOM   2584 C  C    . PRO   A 1 525  ? 190.725 211.608 215.991 1.00 57.70  ? 1857 PRO   A C    1 
ATOM   2585 O  O    . PRO   A 1 525  ? 190.280 212.346 215.110 1.00 64.57  ? 1857 PRO   A O    1 
ATOM   2586 C  CB   . PRO   A 1 525  ? 193.166 211.570 216.551 1.00 57.95  ? 1857 PRO   A CB   1 
ATOM   2587 C  CG   . PRO   A 1 525  ? 193.862 211.358 217.831 1.00 64.71  ? 1857 PRO   A CG   1 
ATOM   2588 C  CD   . PRO   A 1 525  ? 192.825 210.903 218.792 1.00 62.74  ? 1857 PRO   A CD   1 
ATOM   2589 N  N    . ASP   A 1 526  ? 190.308 210.357 216.158 1.00 52.68  ? 1858 ASP   A N    1 
ATOM   2590 C  CA   . ASP   A 1 526  ? 189.366 209.773 215.220 1.00 51.76  ? 1858 ASP   A CA   1 
ATOM   2591 C  C    . ASP   A 1 526  ? 187.980 210.395 215.300 1.00 53.95  ? 1858 ASP   A C    1 
ATOM   2592 O  O    . ASP   A 1 526  ? 187.187 210.205 214.374 1.00 60.89  ? 1858 ASP   A O    1 
ATOM   2593 C  CB   . ASP   A 1 526  ? 189.334 208.254 215.419 1.00 53.25  ? 1858 ASP   A CB   1 
ATOM   2594 C  CG   . ASP   A 1 526  ? 188.650 207.821 216.709 1.00 57.29  ? 1858 ASP   A CG   1 
ATOM   2595 O  OD1  . ASP   A 1 526  ? 188.865 206.666 217.125 1.00 62.96  ? 1858 ASP   A OD1  1 
ATOM   2596 O  OD2  . ASP   A 1 526  ? 187.920 208.610 217.326 1.00 57.26  ? 1858 ASP   A OD2  1 
ATOM   2597 N  N    . LEU   A 1 527  ? 187.659 211.126 216.368 1.00 50.30  ? 1859 LEU   A N    1 
ATOM   2598 C  CA   . LEU   A 1 527  ? 186.396 211.860 216.382 1.00 52.17  ? 1859 LEU   A CA   1 
ATOM   2599 C  C    . LEU   A 1 527  ? 186.396 212.991 215.363 1.00 56.12  ? 1859 LEU   A C    1 
ATOM   2600 O  O    . LEU   A 1 527  ? 185.400 213.204 214.666 1.00 57.08  ? 1859 LEU   A O    1 
ATOM   2601 C  CB   . LEU   A 1 527  ? 186.088 212.401 217.779 1.00 54.22  ? 1859 LEU   A CB   1 
ATOM   2602 C  CG   . LEU   A 1 527  ? 185.403 211.542 218.846 1.00 51.26  ? 1859 LEU   A CG   1 
ATOM   2603 C  CD1  . LEU   A 1 527  ? 184.001 211.183 218.396 1.00 48.92  ? 1859 LEU   A CD1  1 
ATOM   2604 C  CD2  . LEU   A 1 527  ? 186.165 210.302 219.165 1.00 55.43  ? 1859 LEU   A CD2  1 
ATOM   2605 N  N    . ILE   A 1 528  ? 187.495 213.736 215.262 1.00 58.52  ? 1860 ILE   A N    1 
ATOM   2606 C  CA   . ILE   A 1 528  ? 187.523 214.879 214.358 1.00 55.78  ? 1860 ILE   A CA   1 
ATOM   2607 C  C    . ILE   A 1 528  ? 188.335 214.534 213.119 1.00 52.09  ? 1860 ILE   A C    1 
ATOM   2608 O  O    . ILE   A 1 528  ? 188.876 215.423 212.452 1.00 47.74  ? 1860 ILE   A O    1 
ATOM   2609 C  CB   . ILE   A 1 528  ? 188.078 216.142 215.035 1.00 52.23  ? 1860 ILE   A CB   1 
ATOM   2610 C  CG1  . ILE   A 1 528  ? 189.520 215.941 215.460 1.00 57.43  ? 1860 ILE   A CG1  1 
ATOM   2611 C  CG2  . ILE   A 1 528  ? 187.259 216.488 216.251 1.00 50.31  ? 1860 ILE   A CG2  1 
ATOM   2612 C  CD1  . ILE   A 1 528  ? 190.155 217.216 215.902 1.00 66.38  ? 1860 ILE   A CD1  1 
ATOM   2613 N  N    . LEU   A 1 529  ? 188.439 213.241 212.818 1.00 54.65  ? 1861 LEU   A N    1 
ATOM   2614 C  CA   . LEU   A 1 529  ? 189.029 212.775 211.571 1.00 52.86  ? 1861 LEU   A CA   1 
ATOM   2615 C  C    . LEU   A 1 529  ? 190.402 213.380 211.340 1.00 61.84  ? 1861 LEU   A C    1 
ATOM   2616 O  O    . LEU   A 1 529  ? 190.749 213.723 210.209 1.00 72.44  ? 1861 LEU   A O    1 
ATOM   2617 C  CB   . LEU   A 1 529  ? 188.112 213.097 210.394 1.00 47.34  ? 1861 LEU   A CB   1 
ATOM   2618 C  CG   . LEU   A 1 529  ? 186.719 212.475 210.378 1.00 46.15  ? 1861 LEU   A CG   1 
ATOM   2619 C  CD1  . LEU   A 1 529  ? 185.697 213.368 211.029 1.00 49.85  ? 1861 LEU   A CD1  1 
ATOM   2620 C  CD2  . LEU   A 1 529  ? 186.348 212.239 208.955 1.00 45.11  ? 1861 LEU   A CD2  1 
ATOM   2621 N  N    . ALA   A 1 530  ? 191.188 213.524 212.402 1.00 60.85  ? 1862 ALA   A N    1 
ATOM   2622 C  CA   . ALA   A 1 530  ? 192.503 214.132 212.267 1.00 64.98  ? 1862 ALA   A CA   1 
ATOM   2623 C  C    . ALA   A 1 530  ? 193.500 213.231 211.554 1.00 75.98  ? 1862 ALA   A C    1 
ATOM   2624 O  O    . ALA   A 1 530  ? 194.611 213.682 211.257 1.00 81.21  ? 1862 ALA   A O    1 
ATOM   2625 C  CB   . ALA   A 1 530  ? 193.048 214.521 213.639 1.00 63.78  ? 1862 ALA   A CB   1 
ATOM   2626 N  N    . ASP   A 1 531  ? 193.143 211.980 211.282 1.00 69.88  ? 1863 ASP   A N    1 
ATOM   2627 C  CA   . ASP   A 1 531  ? 194.038 211.044 210.621 1.00 75.71  ? 1863 ASP   A CA   1 
ATOM   2628 C  C    . ASP   A 1 531  ? 193.762 210.896 209.128 1.00 80.35  ? 1863 ASP   A C    1 
ATOM   2629 O  O    . ASP   A 1 531  ? 194.345 210.017 208.488 1.00 83.21  ? 1863 ASP   A O    1 
ATOM   2630 C  CB   . ASP   A 1 531  ? 193.975 209.686 211.321 1.00 82.64  ? 1863 ASP   A CB   1 
ATOM   2631 C  CG   . ASP   A 1 531  ? 192.584 209.089 211.326 1.00 93.01  ? 1863 ASP   A CG   1 
ATOM   2632 O  OD1  . ASP   A 1 531  ? 192.315 208.251 212.212 1.00 87.67  ? 1863 ASP   A OD1  1 
ATOM   2633 O  OD2  . ASP   A 1 531  ? 191.752 209.456 210.472 1.00 95.18  ? 1863 ASP   A OD2  1 
ATOM   2634 N  N    . LEU   A 1 532  ? 192.891 211.731 208.560 1.00 85.13  ? 1864 LEU   A N    1 
ATOM   2635 C  CA   . LEU   A 1 532  ? 192.679 211.728 207.122 1.00 81.76  ? 1864 LEU   A CA   1 
ATOM   2636 C  C    . LEU   A 1 532  ? 193.963 212.117 206.399 1.00 82.39  ? 1864 LEU   A C    1 
ATOM   2637 O  O    . LEU   A 1 532  ? 194.782 212.868 206.932 1.00 85.33  ? 1864 LEU   A O    1 
ATOM   2638 C  CB   . LEU   A 1 532  ? 191.568 212.704 206.737 1.00 71.95  ? 1864 LEU   A CB   1 
ATOM   2639 C  CG   . LEU   A 1 532  ? 190.156 212.391 207.198 1.00 65.73  ? 1864 LEU   A CG   1 
ATOM   2640 C  CD1  . LEU   A 1 532  ? 189.236 213.533 206.854 1.00 58.28  ? 1864 LEU   A CD1  1 
ATOM   2641 C  CD2  . LEU   A 1 532  ? 189.715 211.146 206.493 1.00 66.00  ? 1864 LEU   A CD2  1 
ATOM   2642 N  N    . PRO   A 1 533  ? 194.170 211.601 205.190 1.00 79.70  ? 1865 PRO   A N    1 
ATOM   2643 C  CA   . PRO   A 1 533  ? 195.291 212.087 204.384 1.00 88.28  ? 1865 PRO   A CA   1 
ATOM   2644 C  C    . PRO   A 1 533  ? 195.133 213.570 204.098 1.00 88.48  ? 1865 PRO   A C    1 
ATOM   2645 O  O    . PRO   A 1 533  ? 194.030 214.064 203.852 1.00 87.26  ? 1865 PRO   A O    1 
ATOM   2646 C  CB   . PRO   A 1 533  ? 195.209 211.237 203.113 1.00 86.66  ? 1865 PRO   A CB   1 
ATOM   2647 C  CG   . PRO   A 1 533  ? 193.779 210.862 203.012 1.00 80.20  ? 1865 PRO   A CG   1 
ATOM   2648 C  CD   . PRO   A 1 533  ? 193.298 210.692 204.426 1.00 77.38  ? 1865 PRO   A CD   1 
ATOM   2649 N  N    A ARG   A 1 534  ? 196.262 214.280 204.122 0.43 90.37  ? 1866 ARG   A N    1 
ATOM   2650 N  N    B ARG   A 1 534  ? 196.262 214.280 204.119 0.57 90.39  ? 1866 ARG   A N    1 
ATOM   2651 C  CA   A ARG   A 1 534  ? 196.235 215.734 204.040 0.43 91.39  ? 1866 ARG   A CA   1 
ATOM   2652 C  CA   B ARG   A 1 534  ? 196.233 215.734 204.041 0.57 91.41  ? 1866 ARG   A CA   1 
ATOM   2653 C  C    A ARG   A 1 534  ? 195.658 216.236 202.725 0.43 92.83  ? 1866 ARG   A C    1 
ATOM   2654 C  C    B ARG   A 1 534  ? 195.663 216.237 202.724 0.57 92.89  ? 1866 ARG   A C    1 
ATOM   2655 O  O    A ARG   A 1 534  ? 195.275 217.407 202.640 0.43 92.66  ? 1866 ARG   A O    1 
ATOM   2656 O  O    B ARG   A 1 534  ? 195.288 217.411 202.635 0.57 92.71  ? 1866 ARG   A O    1 
ATOM   2657 C  CB   A ARG   A 1 534  ? 197.643 216.296 204.239 0.43 93.28  ? 1866 ARG   A CB   1 
ATOM   2658 C  CB   B ARG   A 1 534  ? 197.639 216.298 204.249 0.57 93.28  ? 1866 ARG   A CB   1 
ATOM   2659 N  N    . ASN   A 1 535  ? 195.588 215.386 201.699 1.00 94.83  ? 1867 ASN   A N    1 
ATOM   2660 C  CA   . ASN   A 1 535  ? 195.017 215.814 200.429 1.00 95.88  ? 1867 ASN   A CA   1 
ATOM   2661 C  C    . ASN   A 1 535  ? 193.510 216.015 200.518 1.00 93.03  ? 1867 ASN   A C    1 
ATOM   2662 O  O    . ASN   A 1 535  ? 192.925 216.633 199.622 1.00 87.67  ? 1867 ASN   A O    1 
ATOM   2663 C  CB   . ASN   A 1 535  ? 195.341 214.802 199.329 1.00 89.13  ? 1867 ASN   A CB   1 
ATOM   2664 C  CG   . ASN   A 1 535  ? 194.710 213.452 199.577 1.00 92.08  ? 1867 ASN   A CG   1 
ATOM   2665 O  OD1  . ASN   A 1 535  ? 194.395 213.103 200.712 1.00 95.90  ? 1867 ASN   A OD1  1 
ATOM   2666 N  ND2  . ASN   A 1 535  ? 194.519 212.683 198.512 1.00 94.58  ? 1867 ASN   A ND2  1 
ATOM   2667 N  N    . ILE   A 1 536  ? 192.875 215.517 201.574 1.00 90.15  ? 1868 ILE   A N    1 
ATOM   2668 C  CA   . ILE   A 1 536  ? 191.427 215.585 201.733 1.00 72.92  ? 1868 ILE   A CA   1 
ATOM   2669 C  C    . ILE   A 1 536  ? 191.101 216.217 203.081 1.00 62.95  ? 1868 ILE   A C    1 
ATOM   2670 O  O    . ILE   A 1 536  ? 191.252 215.595 204.135 1.00 67.83  ? 1868 ILE   A O    1 
ATOM   2671 C  CB   . ILE   A 1 536  ? 190.766 214.211 201.569 1.00 63.06  ? 1868 ILE   A CB   1 
ATOM   2672 C  CG1  . ILE   A 1 536  ? 189.262 214.355 201.534 1.00 47.18  ? 1868 ILE   A CG1  1 
ATOM   2673 C  CG2  . ILE   A 1 536  ? 191.226 213.189 202.590 1.00 74.86  ? 1868 ILE   A CG2  1 
ATOM   2674 C  CD1  . ILE   A 1 536  ? 188.611 213.142 201.080 1.00 48.07  ? 1868 ILE   A CD1  1 
ATOM   2675 N  N    . MET   A 1 537  ? 190.659 217.468 203.053 1.00 59.87  ? 1869 MET   A N    1 
ATOM   2676 C  CA   . MET   A 1 537  ? 190.059 218.107 204.213 1.00 57.73  ? 1869 MET   A CA   1 
ATOM   2677 C  C    . MET   A 1 537  ? 188.983 219.050 203.703 1.00 55.88  ? 1869 MET   A C    1 
ATOM   2678 O  O    . MET   A 1 537  ? 189.221 219.800 202.756 1.00 58.51  ? 1869 MET   A O    1 
ATOM   2679 C  CB   . MET   A 1 537  ? 191.083 218.901 205.041 1.00 70.10  ? 1869 MET   A CB   1 
ATOM   2680 C  CG   . MET   A 1 537  ? 192.482 218.295 205.210 1.00 76.06  ? 1869 MET   A CG   1 
ATOM   2681 S  SD   . MET   A 1 537  ? 192.607 216.923 206.374 1.00 88.07  ? 1869 MET   A SD   1 
ATOM   2682 C  CE   . MET   A 1 537  ? 193.326 217.739 207.796 1.00 57.70  ? 1869 MET   A CE   1 
ATOM   2683 N  N    . LEU   A 1 538  ? 187.812 219.032 204.335 1.00 49.69  ? 1870 LEU   A N    1 
ATOM   2684 C  CA   . LEU   A 1 538  ? 186.822 220.045 203.994 1.00 55.44  ? 1870 LEU   A CA   1 
ATOM   2685 C  C    . LEU   A 1 538  ? 187.357 221.399 204.418 1.00 75.63  ? 1870 LEU   A C    1 
ATOM   2686 O  O    . LEU   A 1 538  ? 187.095 221.851 205.536 1.00 86.90  ? 1870 LEU   A O    1 
ATOM   2687 C  CB   . LEU   A 1 538  ? 185.472 219.781 204.672 1.00 58.55  ? 1870 LEU   A CB   1 
ATOM   2688 C  CG   . LEU   A 1 538  ? 184.143 220.213 204.026 1.00 50.43  ? 1870 LEU   A CG   1 
ATOM   2689 C  CD1  . LEU   A 1 538  ? 183.968 219.726 202.626 1.00 39.88  ? 1870 LEU   A CD1  1 
ATOM   2690 C  CD2  . LEU   A 1 538  ? 182.946 219.780 204.855 1.00 48.52  ? 1870 LEU   A CD2  1 
ATOM   2691 N  N    . ASN   A 1 539  ? 188.100 222.063 203.535 1.00 69.20  ? 1871 ASN   A N    1 
ATOM   2692 C  CA   . ASN   A 1 539  ? 188.622 223.394 203.834 1.00 73.43  ? 1871 ASN   A CA   1 
ATOM   2693 C  C    . ASN   A 1 539  ? 187.512 224.428 203.649 1.00 77.05  ? 1871 ASN   A C    1 
ATOM   2694 O  O    . ASN   A 1 539  ? 187.564 225.326 202.810 1.00 79.71  ? 1871 ASN   A O    1 
ATOM   2695 C  CB   . ASN   A 1 539  ? 189.860 223.684 202.992 1.00 77.30  ? 1871 ASN   A CB   1 
ATOM   2696 C  CG   . ASN   A 1 539  ? 189.581 223.699 201.502 1.00 86.00  ? 1871 ASN   A CG   1 
ATOM   2697 O  OD1  . ASN   A 1 539  ? 188.439 223.603 201.062 1.00 92.22  ? 1871 ASN   A OD1  1 
ATOM   2698 N  ND2  . ASN   A 1 539  ? 190.639 223.832 200.714 1.00 87.71  ? 1871 ASN   A ND2  1 
ATOM   2699 N  N    . ASN   A 1 540  ? 186.502 224.306 204.509 1.00 71.64  ? 1872 ASN   A N    1 
ATOM   2700 C  CA   . ASN   A 1 540  ? 185.329 225.159 204.413 1.00 80.71  ? 1872 ASN   A CA   1 
ATOM   2701 C  C    . ASN   A 1 540  ? 185.726 226.587 204.739 1.00 100.94 ? 1872 ASN   A C    1 
ATOM   2702 O  O    . ASN   A 1 540  ? 185.673 227.018 205.895 1.00 118.79 ? 1872 ASN   A O    1 
ATOM   2703 C  CB   . ASN   A 1 540  ? 184.226 224.675 205.356 1.00 73.03  ? 1872 ASN   A CB   1 
ATOM   2704 C  CG   . ASN   A 1 540  ? 182.839 224.916 204.801 1.00 79.90  ? 1872 ASN   A CG   1 
ATOM   2705 O  OD1  . ASN   A 1 540  ? 182.667 225.655 203.837 1.00 86.91  ? 1872 ASN   A OD1  1 
ATOM   2706 N  ND2  . ASN   A 1 540  ? 181.842 224.292 205.410 1.00 67.91  ? 1872 ASN   A ND2  1 
ATOM   2707 N  N    . ASP   A 1 541  ? 186.122 227.323 203.710 1.00 101.88 ? 1873 ASP   A N    1 
ATOM   2708 C  CA   . ASP   A 1 541  ? 186.580 228.700 203.809 1.00 113.97 ? 1873 ASP   A CA   1 
ATOM   2709 C  C    . ASP   A 1 541  ? 185.839 229.551 202.793 1.00 120.94 ? 1873 ASP   A C    1 
ATOM   2710 O  O    . ASP   A 1 541  ? 186.426 230.298 202.008 1.00 132.55 ? 1873 ASP   A O    1 
ATOM   2711 C  CB   . ASP   A 1 541  ? 188.103 228.770 203.653 1.00 116.69 ? 1873 ASP   A CB   1 
ATOM   2712 C  CG   . ASP   A 1 541  ? 188.591 228.278 202.296 1.00 113.45 ? 1873 ASP   A CG   1 
ATOM   2713 O  OD1  . ASP   A 1 541  ? 187.764 227.837 201.471 1.00 107.07 ? 1873 ASP   A OD1  1 
ATOM   2714 O  OD2  . ASP   A 1 541  ? 189.815 228.327 202.058 1.00 115.54 ? 1873 ASP   A OD2  1 
ATOM   2715 N  N    . GLU   A 1 542  ? 184.511 229.417 202.806 1.00 110.99 ? 1874 GLU   A N    1 
ATOM   2716 C  CA   . GLU   A 1 542  ? 183.638 229.979 201.779 1.00 109.85 ? 1874 GLU   A CA   1 
ATOM   2717 C  C    . GLU   A 1 542  ? 183.961 229.358 200.425 1.00 108.41 ? 1874 GLU   A C    1 
ATOM   2718 O  O    . GLU   A 1 542  ? 184.158 230.049 199.423 1.00 104.37 ? 1874 GLU   A O    1 
ATOM   2719 C  CB   . GLU   A 1 542  ? 183.726 231.507 201.726 1.00 113.90 ? 1874 GLU   A CB   1 
ATOM   2720 N  N    . LEU   A 1 543  ? 184.031 228.026 200.408 1.00 96.90  ? 1875 LEU   A N    1 
ATOM   2721 C  CA   . LEU   A 1 543  ? 184.267 227.291 199.171 1.00 86.77  ? 1875 LEU   A CA   1 
ATOM   2722 C  C    . LEU   A 1 543  ? 183.113 226.341 198.873 1.00 70.16  ? 1875 LEU   A C    1 
ATOM   2723 O  O    . LEU   A 1 543  ? 182.615 226.335 197.750 1.00 75.20  ? 1875 LEU   A O    1 
ATOM   2724 C  CB   . LEU   A 1 543  ? 185.598 226.554 199.244 1.00 81.14  ? 1875 LEU   A CB   1 
ATOM   2725 C  CG   . LEU   A 1 543  ? 185.902 225.849 197.941 1.00 79.39  ? 1875 LEU   A CG   1 
ATOM   2726 C  CD1  . LEU   A 1 543  ? 186.001 226.905 196.872 1.00 83.62  ? 1875 LEU   A CD1  1 
ATOM   2727 C  CD2  . LEU   A 1 543  ? 187.213 225.125 198.084 1.00 73.75  ? 1875 LEU   A CD2  1 
ATOM   2728 N  N    . GLU   A 1 544  ? 182.660 225.560 199.838 1.00 58.12  ? 1876 GLU   A N    1 
ATOM   2729 C  CA   . GLU   A 1 544  ? 181.546 224.662 199.585 1.00 51.11  ? 1876 GLU   A CA   1 
ATOM   2730 C  C    . GLU   A 1 544  ? 180.237 225.403 199.826 1.00 61.90  ? 1876 GLU   A C    1 
ATOM   2731 O  O    . GLU   A 1 544  ? 180.140 226.225 200.741 1.00 69.53  ? 1876 GLU   A O    1 
ATOM   2732 C  CB   . GLU   A 1 544  ? 181.674 223.427 200.473 1.00 44.12  ? 1876 GLU   A CB   1 
ATOM   2733 C  CG   . GLU   A 1 544  ? 180.753 222.282 200.124 1.00 46.70  ? 1876 GLU   A CG   1 
ATOM   2734 C  CD   . GLU   A 1 544  ? 179.376 222.375 200.742 1.00 52.07  ? 1876 GLU   A CD   1 
ATOM   2735 O  OE1  . GLU   A 1 544  ? 178.638 221.380 200.637 1.00 48.83  ? 1876 GLU   A OE1  1 
ATOM   2736 O  OE2  . GLU   A 1 544  ? 179.038 223.400 201.359 1.00 57.79  ? 1876 GLU   A OE2  1 
ATOM   2737 N  N    . PHE   A 1 545  ? 179.236 225.138 198.989 1.00 61.59  ? 1877 PHE   A N    1 
ATOM   2738 C  CA   . PHE   A 1 545  ? 177.948 225.821 199.045 1.00 69.27  ? 1877 PHE   A CA   1 
ATOM   2739 C  C    . PHE   A 1 545  ? 176.857 224.771 198.886 1.00 76.45  ? 1877 PHE   A C    1 
ATOM   2740 O  O    . PHE   A 1 545  ? 176.870 224.036 197.897 1.00 88.94  ? 1877 PHE   A O    1 
ATOM   2741 C  CB   . PHE   A 1 545  ? 177.835 226.836 197.908 1.00 77.09  ? 1877 PHE   A CB   1 
ATOM   2742 C  CG   . PHE   A 1 545  ? 178.810 227.977 197.993 1.00 89.48  ? 1877 PHE   A CG   1 
ATOM   2743 C  CD1  . PHE   A 1 545  ? 178.581 229.061 198.826 1.00 94.95  ? 1877 PHE   A CD1  1 
ATOM   2744 C  CD2  . PHE   A 1 545  ? 179.943 227.981 197.191 1.00 81.13  ? 1877 PHE   A CD2  1 
ATOM   2745 C  CE1  . PHE   A 1 545  ? 179.482 230.109 198.881 1.00 93.91  ? 1877 PHE   A CE1  1 
ATOM   2746 C  CE2  . PHE   A 1 545  ? 180.840 229.025 197.236 1.00 81.04  ? 1877 PHE   A CE2  1 
ATOM   2747 C  CZ   . PHE   A 1 545  ? 180.611 230.091 198.082 1.00 93.68  ? 1877 PHE   A CZ   1 
ATOM   2748 N  N    . GLU   A 1 546  ? 175.890 224.714 199.805 1.00 70.53  ? 1878 GLU   A N    1 
ATOM   2749 C  CA   . GLU   A 1 546  ? 174.842 223.710 199.626 1.00 74.67  ? 1878 GLU   A CA   1 
ATOM   2750 C  C    . GLU   A 1 546  ? 173.624 224.061 200.470 1.00 88.64  ? 1878 GLU   A C    1 
ATOM   2751 O  O    . GLU   A 1 546  ? 173.538 225.139 201.063 1.00 90.65  ? 1878 GLU   A O    1 
ATOM   2752 C  CB   . GLU   A 1 546  ? 175.360 222.305 199.966 1.00 69.57  ? 1878 GLU   A CB   1 
ATOM   2753 C  CG   . GLU   A 1 546  ? 175.801 222.082 201.407 1.00 76.54  ? 1878 GLU   A CG   1 
ATOM   2754 C  CD   . GLU   A 1 546  ? 174.663 221.648 202.309 1.00 85.67  ? 1878 GLU   A CD   1 
ATOM   2755 O  OE1  . GLU   A 1 546  ? 173.660 221.152 201.770 1.00 86.78  ? 1878 GLU   A OE1  1 
ATOM   2756 O  OE2  . GLU   A 1 546  ? 174.762 221.804 203.542 1.00 90.47  ? 1878 GLU   A OE2  1 
ATOM   2757 N  N    . GLN   A 1 547  ? 172.669 223.122 200.480 1.00 98.75  ? 1879 GLN   A N    1 
ATOM   2758 C  CA   . GLN   A 1 547  ? 171.434 223.070 201.267 1.00 100.59 ? 1879 GLN   A CA   1 
ATOM   2759 C  C    . GLN   A 1 547  ? 170.275 223.821 200.623 1.00 107.64 ? 1879 GLN   A C    1 
ATOM   2760 O  O    . GLN   A 1 547  ? 169.181 223.881 201.192 1.00 106.04 ? 1879 GLN   A O    1 
ATOM   2761 C  CB   . GLN   A 1 547  ? 171.667 223.568 202.699 1.00 97.70  ? 1879 GLN   A CB   1 
ATOM   2762 C  CG   . GLN   A 1 547  ? 170.565 223.204 203.710 1.00 107.17 ? 1879 GLN   A CG   1 
ATOM   2763 C  CD   . GLN   A 1 547  ? 170.082 221.759 203.604 1.00 102.79 ? 1879 GLN   A CD   1 
ATOM   2764 O  OE1  . GLN   A 1 547  ? 169.395 221.380 202.653 1.00 101.30 ? 1879 GLN   A OE1  1 
ATOM   2765 N  NE2  . GLN   A 1 547  ? 170.433 220.951 204.595 1.00 91.02  ? 1879 GLN   A NE2  1 
ATOM   2766 N  N    . ALA   A 1 548  ? 170.471 224.359 199.426 1.00 110.90 ? 1880 ALA   A N    1 
ATOM   2767 C  CA   . ALA   A 1 548  ? 169.338 224.904 198.707 1.00 112.20 ? 1880 ALA   A CA   1 
ATOM   2768 C  C    . ALA   A 1 548  ? 168.440 223.763 198.231 1.00 113.48 ? 1880 ALA   A C    1 
ATOM   2769 O  O    . ALA   A 1 548  ? 168.919 222.669 197.923 1.00 105.15 ? 1880 ALA   A O    1 
ATOM   2770 C  CB   . ALA   A 1 548  ? 169.801 225.755 197.528 1.00 103.40 ? 1880 ALA   A CB   1 
ATOM   2771 N  N    . PRO   A 1 549  ? 167.124 223.988 198.187 1.00 120.57 ? 1881 PRO   A N    1 
ATOM   2772 C  CA   . PRO   A 1 549  ? 166.219 222.899 197.784 1.00 112.51 ? 1881 PRO   A CA   1 
ATOM   2773 C  C    . PRO   A 1 549  ? 166.473 222.401 196.375 1.00 102.59 ? 1881 PRO   A C    1 
ATOM   2774 O  O    . PRO   A 1 549  ? 166.254 221.217 196.089 1.00 88.37  ? 1881 PRO   A O    1 
ATOM   2775 C  CB   . PRO   A 1 549  ? 164.832 223.535 197.928 1.00 116.83 ? 1881 PRO   A CB   1 
ATOM   2776 C  CG   . PRO   A 1 549  ? 165.067 224.994 197.741 1.00 112.59 ? 1881 PRO   A CG   1 
ATOM   2777 C  CD   . PRO   A 1 549  ? 166.416 225.272 198.339 1.00 113.11 ? 1881 PRO   A CD   1 
ATOM   2778 N  N    . GLU   A 1 550  ? 166.927 223.281 195.480 1.00 106.77 ? 1882 GLU   A N    1 
ATOM   2779 C  CA   . GLU   A 1 550  ? 167.229 222.861 194.117 1.00 103.18 ? 1882 GLU   A CA   1 
ATOM   2780 C  C    . GLU   A 1 550  ? 168.482 221.997 194.071 1.00 98.35  ? 1882 GLU   A C    1 
ATOM   2781 O  O    . GLU   A 1 550  ? 168.694 221.248 193.111 1.00 90.62  ? 1882 GLU   A O    1 
ATOM   2782 C  CB   . GLU   A 1 550  ? 167.390 224.085 193.215 1.00 94.35  ? 1882 GLU   A CB   1 
ATOM   2783 N  N    . PHE   A 1 551  ? 169.329 222.092 195.099 1.00 94.97  ? 1883 PHE   A N    1 
ATOM   2784 C  CA   . PHE   A 1 551  ? 170.568 221.325 195.100 1.00 86.23  ? 1883 PHE   A CA   1 
ATOM   2785 C  C    . PHE   A 1 551  ? 170.369 219.858 195.458 1.00 86.18  ? 1883 PHE   A C    1 
ATOM   2786 O  O    . PHE   A 1 551  ? 171.328 219.088 195.363 1.00 85.25  ? 1883 PHE   A O    1 
ATOM   2787 C  CB   . PHE   A 1 551  ? 171.595 221.940 196.050 1.00 88.38  ? 1883 PHE   A CB   1 
ATOM   2788 C  CG   . PHE   A 1 551  ? 172.109 223.284 195.614 1.00 89.56  ? 1883 PHE   A CG   1 
ATOM   2789 C  CD1  . PHE   A 1 551  ? 172.174 223.615 194.273 1.00 87.43  ? 1883 PHE   A CD1  1 
ATOM   2790 C  CD2  . PHE   A 1 551  ? 172.594 224.187 196.541 1.00 84.68  ? 1883 PHE   A CD2  1 
ATOM   2791 C  CE1  . PHE   A 1 551  ? 172.666 224.841 193.872 1.00 88.95  ? 1883 PHE   A CE1  1 
ATOM   2792 C  CE2  . PHE   A 1 551  ? 173.082 225.412 196.145 1.00 85.70  ? 1883 PHE   A CE2  1 
ATOM   2793 C  CZ   . PHE   A 1 551  ? 173.120 225.739 194.811 1.00 86.95  ? 1883 PHE   A CZ   1 
ATOM   2794 N  N    . LEU   A 1 552  ? 169.173 219.449 195.875 1.00 89.62  ? 1884 LEU   A N    1 
ATOM   2795 C  CA   . LEU   A 1 552  ? 168.964 218.044 196.208 1.00 86.64  ? 1884 LEU   A CA   1 
ATOM   2796 C  C    . LEU   A 1 552  ? 169.263 217.152 195.011 1.00 81.88  ? 1884 LEU   A C    1 
ATOM   2797 O  O    . LEU   A 1 552  ? 168.852 217.436 193.883 1.00 85.42  ? 1884 LEU   A O    1 
ATOM   2798 C  CB   . LEU   A 1 552  ? 167.534 217.802 196.685 1.00 94.05  ? 1884 LEU   A CB   1 
ATOM   2799 C  CG   . LEU   A 1 552  ? 167.364 216.500 197.475 1.00 88.44  ? 1884 LEU   A CG   1 
ATOM   2800 C  CD1  . LEU   A 1 552  ? 167.848 216.642 198.906 1.00 76.06  ? 1884 LEU   A CD1  1 
ATOM   2801 C  CD2  . LEU   A 1 552  ? 165.927 216.016 197.436 1.00 86.90  ? 1884 LEU   A CD2  1 
ATOM   2802 N  N    . LEU   A 1 553  ? 169.985 216.067 195.266 1.00 74.15  ? 1885 LEU   A N    1 
ATOM   2803 C  CA   . LEU   A 1 553  ? 170.368 215.129 194.220 1.00 74.62  ? 1885 LEU   A CA   1 
ATOM   2804 C  C    . LEU   A 1 553  ? 169.966 213.706 194.585 1.00 76.58  ? 1885 LEU   A C    1 
ATOM   2805 O  O    . LEU   A 1 553  ? 169.638 212.899 193.716 1.00 84.06  ? 1885 LEU   A O    1 
ATOM   2806 C  CB   . LEU   A 1 553  ? 171.871 215.198 193.974 1.00 66.43  ? 1885 LEU   A CB   1 
ATOM   2807 C  CG   . LEU   A 1 553  ? 172.426 214.189 192.979 1.00 65.39  ? 1885 LEU   A CG   1 
ATOM   2808 C  CD1  . LEU   A 1 553  ? 171.723 214.344 191.650 1.00 76.34  ? 1885 LEU   A CD1  1 
ATOM   2809 C  CD2  . LEU   A 1 553  ? 173.915 214.368 192.827 1.00 55.70  ? 1885 LEU   A CD2  1 
ATOM   2810 N  N    . GLY   A 1 559  ? 168.563 210.849 197.474 1.00 80.49  ? 1891 GLY   A N    1 
ATOM   2811 C  CA   . GLY   A 1 559  ? 168.262 210.687 198.884 1.00 97.54  ? 1891 GLY   A CA   1 
ATOM   2812 C  C    . GLY   A 1 559  ? 169.355 211.203 199.800 1.00 103.91 ? 1891 GLY   A C    1 
ATOM   2813 O  O    . GLY   A 1 559  ? 170.356 210.525 200.023 1.00 108.69 ? 1891 GLY   A O    1 
ATOM   2814 N  N    . SER   A 1 560  ? 169.150 212.406 200.339 1.00 100.36 ? 1892 SER   A N    1 
ATOM   2815 C  CA   . SER   A 1 560  ? 170.109 213.061 201.232 1.00 93.33  ? 1892 SER   A CA   1 
ATOM   2816 C  C    . SER   A 1 560  ? 171.475 213.224 200.570 1.00 85.95  ? 1892 SER   A C    1 
ATOM   2817 O  O    . SER   A 1 560  ? 172.517 213.046 201.203 1.00 82.38  ? 1892 SER   A O    1 
ATOM   2818 C  CB   . SER   A 1 560  ? 170.240 212.315 202.561 1.00 84.01  ? 1892 SER   A CB   1 
ATOM   2819 O  OG   . SER   A 1 560  ? 170.815 211.036 202.376 1.00 90.66  ? 1892 SER   A OG   1 
ATOM   2820 N  N    . VAL   A 1 561  ? 171.472 213.558 199.281 1.00 78.73  ? 1893 VAL   A N    1 
ATOM   2821 C  CA   . VAL   A 1 561  ? 172.672 213.965 198.562 1.00 77.43  ? 1893 VAL   A CA   1 
ATOM   2822 C  C    . VAL   A 1 561  ? 172.355 215.266 197.837 1.00 81.36  ? 1893 VAL   A C    1 
ATOM   2823 O  O    . VAL   A 1 561  ? 171.355 215.346 197.117 1.00 78.68  ? 1893 VAL   A O    1 
ATOM   2824 C  CB   . VAL   A 1 561  ? 173.148 212.887 197.569 1.00 72.95  ? 1893 VAL   A CB   1 
ATOM   2825 C  CG1  . VAL   A 1 561  ? 174.334 213.382 196.769 1.00 66.51  ? 1893 VAL   A CG1  1 
ATOM   2826 C  CG2  . VAL   A 1 561  ? 173.508 211.616 198.298 1.00 73.24  ? 1893 VAL   A CG2  1 
ATOM   2827 N  N    . TYR   A 1 562  ? 173.186 216.287 198.039 1.00 73.07  ? 1894 TYR   A N    1 
ATOM   2828 C  CA   . TYR   A 1 562  ? 172.968 217.591 197.428 1.00 65.61  ? 1894 TYR   A CA   1 
ATOM   2829 C  C    . TYR   A 1 562  ? 174.055 217.923 196.417 1.00 56.63  ? 1894 TYR   A C    1 
ATOM   2830 O  O    . TYR   A 1 562  ? 175.127 217.316 196.388 1.00 52.41  ? 1894 TYR   A O    1 
ATOM   2831 C  CB   . TYR   A 1 562  ? 172.914 218.714 198.468 1.00 67.80  ? 1894 TYR   A CB   1 
ATOM   2832 C  CG   . TYR   A 1 562  ? 172.123 218.406 199.696 1.00 69.77  ? 1894 TYR   A CG   1 
ATOM   2833 C  CD1  . TYR   A 1 562  ? 170.774 218.694 199.755 1.00 79.99  ? 1894 TYR   A CD1  1 
ATOM   2834 C  CD2  . TYR   A 1 562  ? 172.723 217.842 200.800 1.00 71.98  ? 1894 TYR   A CD2  1 
ATOM   2835 C  CE1  . TYR   A 1 562  ? 170.042 218.424 200.879 1.00 93.62  ? 1894 TYR   A CE1  1 
ATOM   2836 C  CE2  . TYR   A 1 562  ? 172.001 217.562 201.924 1.00 84.17  ? 1894 TYR   A CE2  1 
ATOM   2837 C  CZ   . TYR   A 1 562  ? 170.658 217.855 201.963 1.00 102.29 ? 1894 TYR   A CZ   1 
ATOM   2838 O  OH   . TYR   A 1 562  ? 169.923 217.580 203.092 1.00 120.23 ? 1894 TYR   A OH   1 
ATOM   2839 N  N    . ARG   A 1 563  ? 173.765 218.939 195.612 1.00 58.72  ? 1895 ARG   A N    1 
ATOM   2840 C  CA   . ARG   A 1 563  ? 174.698 219.484 194.640 1.00 52.59  ? 1895 ARG   A CA   1 
ATOM   2841 C  C    . ARG   A 1 563  ? 175.388 220.688 195.253 1.00 52.02  ? 1895 ARG   A C    1 
ATOM   2842 O  O    . ARG   A 1 563  ? 174.730 221.578 195.796 1.00 57.38  ? 1895 ARG   A O    1 
ATOM   2843 C  CB   . ARG   A 1 563  ? 173.977 219.894 193.359 1.00 56.46  ? 1895 ARG   A CB   1 
ATOM   2844 C  CG   . ARG   A 1 563  ? 173.409 218.738 192.579 1.00 62.94  ? 1895 ARG   A CG   1 
ATOM   2845 C  CD   . ARG   A 1 563  ? 172.697 219.206 191.326 1.00 79.24  ? 1895 ARG   A CD   1 
ATOM   2846 N  NE   . ARG   A 1 563  ? 172.133 218.079 190.593 1.00 92.21  ? 1895 ARG   A NE   1 
ATOM   2847 C  CZ   . ARG   A 1 563  ? 171.407 218.188 189.490 1.00 103.31 ? 1895 ARG   A CZ   1 
ATOM   2848 N  NH1  . ARG   A 1 563  ? 171.114 219.367 188.969 1.00 105.67 ? 1895 ARG   A NH1  1 
ATOM   2849 N  NH2  . ARG   A 1 563  ? 170.964 217.085 188.895 1.00 111.42 ? 1895 ARG   A NH2  1 
ATOM   2850 N  N    . ALA   A 1 564  ? 176.707 220.713 195.169 1.00 46.48  ? 1896 ALA   A N    1 
ATOM   2851 C  CA   . ALA   A 1 564  ? 177.490 221.779 195.759 1.00 41.00  ? 1896 ALA   A CA   1 
ATOM   2852 C  C    . ALA   A 1 564  ? 178.522 222.229 194.750 1.00 38.65  ? 1896 ALA   A C    1 
ATOM   2853 O  O    . ALA   A 1 564  ? 178.719 221.594 193.716 1.00 59.02  ? 1896 ALA   A O    1 
ATOM   2854 C  CB   . ALA   A 1 564  ? 178.180 221.328 197.045 1.00 60.17  ? 1896 ALA   A CB   1 
ATOM   2855 N  N    . ALA   A 1 565  ? 179.182 223.335 195.054 1.00 38.76  ? 1897 ALA   A N    1 
ATOM   2856 C  CA   . ALA   A 1 565  ? 180.241 223.851 194.199 1.00 57.37  ? 1897 ALA   A CA   1 
ATOM   2857 C  C    . ALA   A 1 565  ? 181.516 223.878 195.025 1.00 57.70  ? 1897 ALA   A C    1 
ATOM   2858 O  O    . ALA   A 1 565  ? 181.783 224.847 195.733 1.00 78.90  ? 1897 ALA   A O    1 
ATOM   2859 C  CB   . ALA   A 1 565  ? 179.890 225.228 193.658 1.00 70.80  ? 1897 ALA   A CB   1 
ATOM   2860 N  N    . TYR   A 1 566  ? 182.311 222.827 194.925 1.00 42.80  ? 1898 TYR   A N    1 
ATOM   2861 C  CA   . TYR   A 1 566  ? 183.555 222.727 195.669 1.00 52.56  ? 1898 TYR   A CA   1 
ATOM   2862 C  C    . TYR   A 1 566  ? 184.697 223.098 194.740 1.00 62.70  ? 1898 TYR   A C    1 
ATOM   2863 O  O    . TYR   A 1 566  ? 184.816 222.534 193.650 1.00 77.11  ? 1898 TYR   A O    1 
ATOM   2864 C  CB   . TYR   A 1 566  ? 183.740 221.318 196.224 1.00 54.33  ? 1898 TYR   A CB   1 
ATOM   2865 C  CG   . TYR   A 1 566  ? 184.960 221.118 197.096 1.00 54.40  ? 1898 TYR   A CG   1 
ATOM   2866 C  CD1  . TYR   A 1 566  ? 184.962 221.502 198.428 1.00 46.90  ? 1898 TYR   A CD1  1 
ATOM   2867 C  CD2  . TYR   A 1 566  ? 186.097 220.520 196.590 1.00 59.61  ? 1898 TYR   A CD2  1 
ATOM   2868 C  CE1  . TYR   A 1 566  ? 186.065 221.305 199.219 1.00 49.00  ? 1898 TYR   A CE1  1 
ATOM   2869 C  CE2  . TYR   A 1 566  ? 187.202 220.320 197.374 1.00 58.64  ? 1898 TYR   A CE2  1 
ATOM   2870 C  CZ   . TYR   A 1 566  ? 187.183 220.712 198.684 1.00 54.06  ? 1898 TYR   A CZ   1 
ATOM   2871 O  OH   . TYR   A 1 566  ? 188.301 220.507 199.455 1.00 58.21  ? 1898 TYR   A OH   1 
ATOM   2872 N  N    . GLU   A 1 567  ? 185.525 224.050 195.169 1.00 67.33  ? 1899 GLU   A N    1 
ATOM   2873 C  CA   . GLU   A 1 567  ? 186.662 224.532 194.380 1.00 80.49  ? 1899 GLU   A CA   1 
ATOM   2874 C  C    . GLU   A 1 567  ? 186.222 225.043 193.009 1.00 83.86  ? 1899 GLU   A C    1 
ATOM   2875 O  O    . GLU   A 1 567  ? 186.906 224.845 192.004 1.00 91.57  ? 1899 GLU   A O    1 
ATOM   2876 C  CB   . GLU   A 1 567  ? 187.734 223.451 194.236 1.00 85.93  ? 1899 GLU   A CB   1 
ATOM   2877 C  CG   . GLU   A 1 567  ? 188.761 223.446 195.347 1.00 92.09  ? 1899 GLU   A CG   1 
ATOM   2878 C  CD   . GLU   A 1 567  ? 189.990 222.644 194.994 1.00 104.10 ? 1899 GLU   A CD   1 
ATOM   2879 O  OE1  . GLU   A 1 567  ? 190.624 222.089 195.915 1.00 103.29 ? 1899 GLU   A OE1  1 
ATOM   2880 O  OE2  . GLU   A 1 567  ? 190.323 222.569 193.795 1.00 98.50  ? 1899 GLU   A OE2  1 
ATOM   2881 N  N    . GLY   A 1 568  ? 185.067 225.700 192.961 1.00 72.71  ? 1900 GLY   A N    1 
ATOM   2882 C  CA   . GLY   A 1 568  ? 184.588 226.234 191.704 1.00 76.28  ? 1900 GLY   A CA   1 
ATOM   2883 C  C    . GLY   A 1 568  ? 184.130 225.196 190.710 1.00 81.94  ? 1900 GLY   A C    1 
ATOM   2884 O  O    . GLY   A 1 568  ? 183.751 225.554 189.592 1.00 90.24  ? 1900 GLY   A O    1 
ATOM   2885 N  N    . GLU   A 1 569  ? 184.147 223.923 191.085 1.00 76.72  ? 1901 GLU   A N    1 
ATOM   2886 C  CA   . GLU   A 1 569  ? 183.622 222.838 190.273 1.00 68.43  ? 1901 GLU   A CA   1 
ATOM   2887 C  C    . GLU   A 1 569  ? 182.402 222.286 190.980 1.00 56.55  ? 1901 GLU   A C    1 
ATOM   2888 O  O    . GLU   A 1 569  ? 182.312 222.355 192.208 1.00 61.95  ? 1901 GLU   A O    1 
ATOM   2889 C  CB   . GLU   A 1 569  ? 184.648 221.722 190.066 1.00 73.33  ? 1901 GLU   A CB   1 
ATOM   2890 C  CG   . GLU   A 1 569  ? 185.687 222.019 189.010 1.00 95.07  ? 1901 GLU   A CG   1 
ATOM   2891 C  CD   . GLU   A 1 569  ? 187.079 221.648 189.458 1.00 108.68 ? 1901 GLU   A CD   1 
ATOM   2892 O  OE1  . GLU   A 1 569  ? 187.211 220.704 190.264 1.00 114.19 ? 1901 GLU   A OE1  1 
ATOM   2893 O  OE2  . GLU   A 1 569  ? 188.040 222.303 189.007 1.00 114.14 ? 1901 GLU   A OE2  1 
ATOM   2894 N  N    . GLU   A 1 570  ? 181.453 221.769 190.216 1.00 45.55  ? 1902 GLU   A N    1 
ATOM   2895 C  CA   . GLU   A 1 570  ? 180.226 221.295 190.828 1.00 46.55  ? 1902 GLU   A CA   1 
ATOM   2896 C  C    . GLU   A 1 570  ? 180.372 219.836 191.240 1.00 43.23  ? 1902 GLU   A C    1 
ATOM   2897 O  O    . GLU   A 1 570  ? 180.821 218.998 190.454 1.00 40.76  ? 1902 GLU   A O    1 
ATOM   2898 C  CB   . GLU   A 1 570  ? 179.051 221.479 189.881 1.00 47.75  ? 1902 GLU   A CB   1 
ATOM   2899 C  CG   . GLU   A 1 570  ? 177.868 220.646 190.251 1.00 54.81  ? 1902 GLU   A CG   1 
ATOM   2900 C  CD   . GLU   A 1 570  ? 176.582 221.227 189.738 1.00 64.88  ? 1902 GLU   A CD   1 
ATOM   2901 O  OE1  . GLU   A 1 570  ? 175.577 221.177 190.474 1.00 66.75  ? 1902 GLU   A OE1  1 
ATOM   2902 O  OE2  . GLU   A 1 570  ? 176.577 221.742 188.604 1.00 72.55  ? 1902 GLU   A OE2  1 
ATOM   2903 N  N    . VAL   A 1 571  ? 180.007 219.543 192.489 1.00 44.64  ? 1903 VAL   A N    1 
ATOM   2904 C  CA   . VAL   A 1 571  ? 180.176 218.238 193.110 1.00 34.57  ? 1903 VAL   A CA   1 
ATOM   2905 C  C    . VAL   A 1 571  ? 178.885 217.849 193.815 1.00 36.19  ? 1903 VAL   A C    1 
ATOM   2906 O  O    . VAL   A 1 571  ? 177.949 218.638 193.927 1.00 49.18  ? 1903 VAL   A O    1 
ATOM   2907 C  CB   . VAL   A 1 571  ? 181.337 218.231 194.110 1.00 29.47  ? 1903 VAL   A CB   1 
ATOM   2908 C  CG1  . VAL   A 1 571  ? 182.616 218.648 193.435 1.00 30.21  ? 1903 VAL   A CG1  1 
ATOM   2909 C  CG2  . VAL   A 1 571  ? 181.011 219.203 195.197 1.00 35.25  ? 1903 VAL   A CG2  1 
ATOM   2910 N  N    . ALA   A 1 572  ? 178.854 216.618 194.313 1.00 28.63  ? 1904 ALA   A N    1 
ATOM   2911 C  CA   . ALA   A 1 572  ? 177.696 216.078 195.010 1.00 31.29  ? 1904 ALA   A CA   1 
ATOM   2912 C  C    . ALA   A 1 572  ? 178.076 215.745 196.439 1.00 40.06  ? 1904 ALA   A C    1 
ATOM   2913 O  O    . ALA   A 1 572  ? 179.050 215.023 196.669 1.00 48.10  ? 1904 ALA   A O    1 
ATOM   2914 C  CB   . ALA   A 1 572  ? 177.172 214.822 194.324 1.00 35.41  ? 1904 ALA   A CB   1 
ATOM   2915 N  N    . VAL   A 1 573  ? 177.286 216.233 197.390 1.00 41.87  ? 1905 VAL   A N    1 
ATOM   2916 C  CA   . VAL   A 1 573  ? 177.573 216.085 198.810 1.00 41.03  ? 1905 VAL   A CA   1 
ATOM   2917 C  C    . VAL   A 1 573  ? 176.473 215.244 199.434 1.00 54.01  ? 1905 VAL   A C    1 
ATOM   2918 O  O    . VAL   A 1 573  ? 175.293 215.425 199.116 1.00 60.64  ? 1905 VAL   A O    1 
ATOM   2919 C  CB   . VAL   A 1 573  ? 177.686 217.449 199.511 1.00 41.11  ? 1905 VAL   A CB   1 
ATOM   2920 C  CG1  . VAL   A 1 573  ? 178.822 218.233 198.938 1.00 37.39  ? 1905 VAL   A CG1  1 
ATOM   2921 C  CG2  . VAL   A 1 573  ? 176.423 218.237 199.328 1.00 57.03  ? 1905 VAL   A CG2  1 
ATOM   2922 N  N    . LYS   A 1 574  ? 176.860 214.309 200.299 1.00 56.40  ? 1906 LYS   A N    1 
ATOM   2923 C  CA   . LYS   A 1 574  ? 175.916 213.493 201.053 1.00 65.42  ? 1906 LYS   A CA   1 
ATOM   2924 C  C    . LYS   A 1 574  ? 176.180 213.721 202.532 1.00 72.37  ? 1906 LYS   A C    1 
ATOM   2925 O  O    . LYS   A 1 574  ? 177.313 213.556 202.993 1.00 71.44  ? 1906 LYS   A O    1 
ATOM   2926 C  CB   . LYS   A 1 574  ? 176.050 212.013 200.703 1.00 66.58  ? 1906 LYS   A CB   1 
ATOM   2927 C  CG   . LYS   A 1 574  ? 175.589 211.058 201.790 1.00 69.83  ? 1906 LYS   A CG   1 
ATOM   2928 C  CD   . LYS   A 1 574  ? 176.031 209.639 201.479 1.00 69.36  ? 1906 LYS   A CD   1 
ATOM   2929 C  CE   . LYS   A 1 574  ? 175.355 208.628 202.385 1.00 85.67  ? 1906 LYS   A CE   1 
ATOM   2930 N  NZ   . LYS   A 1 574  ? 173.883 208.622 202.191 1.00 93.58  ? 1906 LYS   A NZ   1 
ATOM   2931 N  N    . ILE   A 1 575  ? 175.145 214.099 203.269 1.00 77.38  ? 1907 ILE   A N    1 
ATOM   2932 C  CA   . ILE   A 1 575  ? 175.298 214.507 204.657 1.00 78.41  ? 1907 ILE   A CA   1 
ATOM   2933 C  C    . ILE   A 1 575  ? 174.774 213.411 205.571 1.00 86.34  ? 1907 ILE   A C    1 
ATOM   2934 O  O    . ILE   A 1 575  ? 173.857 212.660 205.224 1.00 92.07  ? 1907 ILE   A O    1 
ATOM   2935 C  CB   . ILE   A 1 575  ? 174.575 215.835 204.938 1.00 85.37  ? 1907 ILE   A CB   1 
ATOM   2936 C  CG1  . ILE   A 1 575  ? 173.077 215.679 204.703 1.00 93.97  ? 1907 ILE   A CG1  1 
ATOM   2937 C  CG2  . ILE   A 1 575  ? 175.127 216.921 204.051 1.00 77.79  ? 1907 ILE   A CG2  1 
ATOM   2938 C  CD1  . ILE   A 1 575  ? 172.271 216.855 205.184 1.00 98.37  ? 1907 ILE   A CD1  1 
ATOM   2939 N  N    . PHE   A 1 576  ? 175.374 213.323 206.752 1.00 84.74  ? 1908 PHE   A N    1 
ATOM   2940 C  CA   . PHE   A 1 576  ? 174.992 212.354 207.771 1.00 91.29  ? 1908 PHE   A CA   1 
ATOM   2941 C  C    . PHE   A 1 576  ? 174.243 213.067 208.893 1.00 98.13  ? 1908 PHE   A C    1 
ATOM   2942 O  O    . PHE   A 1 576  ? 174.830 213.530 209.872 1.00 98.66  ? 1908 PHE   A O    1 
ATOM   2943 C  CB   . PHE   A 1 576  ? 176.230 211.637 208.282 1.00 88.76  ? 1908 PHE   A CB   1 
ATOM   2944 C  CG   . PHE   A 1 576  ? 176.954 210.866 207.226 1.00 76.67  ? 1908 PHE   A CG   1 
ATOM   2945 C  CD1  . PHE   A 1 576  ? 176.296 210.431 206.101 1.00 72.92  ? 1908 PHE   A CD1  1 
ATOM   2946 C  CD2  . PHE   A 1 576  ? 178.300 210.607 207.342 1.00 71.21  ? 1908 PHE   A CD2  1 
ATOM   2947 C  CE1  . PHE   A 1 576  ? 176.960 209.729 205.135 1.00 76.89  ? 1908 PHE   A CE1  1 
ATOM   2948 C  CE2  . PHE   A 1 576  ? 178.965 209.912 206.368 1.00 70.28  ? 1908 PHE   A CE2  1 
ATOM   2949 C  CZ   . PHE   A 1 576  ? 178.296 209.472 205.267 1.00 75.85  ? 1908 PHE   A CZ   1 
ATOM   2950 N  N    . ASN   A 1 577  ? 172.921 213.160 208.735 1.00 104.54 ? 1909 ASN   A N    1 
ATOM   2951 C  CA   . ASN   A 1 577  ? 172.109 213.863 209.723 1.00 115.31 ? 1909 ASN   A CA   1 
ATOM   2952 C  C    . ASN   A 1 577  ? 171.944 213.054 211.003 1.00 124.57 ? 1909 ASN   A C    1 
ATOM   2953 O  O    . ASN   A 1 577  ? 172.417 213.463 212.069 1.00 117.68 ? 1909 ASN   A O    1 
ATOM   2954 C  CB   . ASN   A 1 577  ? 170.740 214.203 209.135 1.00 110.69 ? 1909 ASN   A CB   1 
ATOM   2955 C  CG   . ASN   A 1 577  ? 170.814 215.279 208.076 1.00 109.13 ? 1909 ASN   A CG   1 
ATOM   2956 O  OD1  . ASN   A 1 577  ? 171.532 216.265 208.229 1.00 107.40 ? 1909 ASN   A OD1  1 
ATOM   2957 N  ND2  . ASN   A 1 577  ? 170.069 215.096 206.994 1.00 122.16 ? 1909 ASN   A ND2  1 
ATOM   2958 N  N    . LYS   A 1 578  ? 171.282 211.903 210.922 1.00 127.70 ? 1910 LYS   A N    1 
ATOM   2959 C  CA   . LYS   A 1 578  ? 170.814 211.188 212.100 1.00 131.97 ? 1910 LYS   A CA   1 
ATOM   2960 C  C    . LYS   A 1 578  ? 171.507 209.839 212.209 1.00 136.28 ? 1910 LYS   A C    1 
ATOM   2961 O  O    . LYS   A 1 578  ? 171.766 209.184 211.193 1.00 134.95 ? 1910 LYS   A O    1 
ATOM   2962 C  CB   . LYS   A 1 578  ? 169.296 210.990 212.053 1.00 132.03 ? 1910 LYS   A CB   1 
ATOM   2963 C  CG   . LYS   A 1 578  ? 168.459 212.271 212.002 1.00 131.81 ? 1910 LYS   A CG   1 
ATOM   2964 C  CD   . LYS   A 1 578  ? 168.465 213.058 213.311 1.00 126.54 ? 1910 LYS   A CD   1 
ATOM   2965 C  CE   . LYS   A 1 578  ? 169.527 214.147 213.335 1.00 132.47 ? 1910 LYS   A CE   1 
ATOM   2966 N  NZ   . LYS   A 1 578  ? 169.443 214.968 214.572 1.00 135.11 ? 1910 LYS   A NZ   1 
ATOM   2967 N  N    . HIS   A 1 579  ? 171.816 209.440 213.444 1.00 138.95 ? 1911 HIS   A N    1 
ATOM   2968 C  CA   . HIS   A 1 579  ? 172.366 208.119 213.746 1.00 132.20 ? 1911 HIS   A CA   1 
ATOM   2969 C  C    . HIS   A 1 579  ? 173.674 207.867 213.002 1.00 122.56 ? 1911 HIS   A C    1 
ATOM   2970 O  O    . HIS   A 1 579  ? 174.037 206.723 212.718 1.00 110.12 ? 1911 HIS   A O    1 
ATOM   2971 C  CB   . HIS   A 1 579  ? 171.349 207.015 213.444 1.00 121.79 ? 1911 HIS   A CB   1 
ATOM   2972 N  N    . THR   A 1 580  ? 174.393 208.944 212.682 1.00 125.58 ? 1912 THR   A N    1 
ATOM   2973 C  CA   . THR   A 1 580  ? 175.702 208.786 212.061 1.00 118.18 ? 1912 THR   A CA   1 
ATOM   2974 C  C    . THR   A 1 580  ? 176.668 208.082 213.005 1.00 108.44 ? 1912 THR   A C    1 
ATOM   2975 O  O    . THR   A 1 580  ? 177.419 207.192 212.592 1.00 100.10 ? 1912 THR   A O    1 
ATOM   2976 C  CB   . THR   A 1 580  ? 176.246 210.149 211.610 1.00 117.77 ? 1912 THR   A CB   1 
ATOM   2977 O  OG1  . THR   A 1 580  ? 177.456 209.965 210.866 1.00 114.89 ? 1912 THR   A OG1  1 
ATOM   2978 C  CG2  . THR   A 1 580  ? 176.495 211.097 212.781 1.00 113.09 ? 1912 THR   A CG2  1 
ATOM   2979 N  N    . SER   A 1 581  ? 176.661 208.472 214.280 1.00 110.73 ? 1913 SER   A N    1 
ATOM   2980 C  CA   . SER   A 1 581  ? 177.494 207.887 215.329 1.00 110.04 ? 1913 SER   A CA   1 
ATOM   2981 C  C    . SER   A 1 581  ? 178.971 207.835 214.950 1.00 113.10 ? 1913 SER   A C    1 
ATOM   2982 O  O    . SER   A 1 581  ? 179.767 207.209 215.656 1.00 113.50 ? 1913 SER   A O    1 
ATOM   2983 C  CB   . SER   A 1 581  ? 177.000 206.486 215.711 1.00 106.89 ? 1913 SER   A CB   1 
ATOM   2984 O  OG   . SER   A 1 581  ? 175.703 206.545 216.276 1.00 113.27 ? 1913 SER   A OG   1 
ATOM   2985 N  N    . LEU   A 1 582  ? 179.353 208.498 213.856 1.00 101.93 ? 1914 LEU   A N    1 
ATOM   2986 C  CA   . LEU   A 1 582  ? 180.714 208.432 213.330 1.00 86.37  ? 1914 LEU   A CA   1 
ATOM   2987 C  C    . LEU   A 1 582  ? 181.168 206.982 213.174 1.00 91.02  ? 1914 LEU   A C    1 
ATOM   2988 O  O    . LEU   A 1 582  ? 182.315 206.628 213.425 1.00 87.10  ? 1914 LEU   A O    1 
ATOM   2989 C  CB   . LEU   A 1 582  ? 181.660 209.278 214.191 1.00 80.89  ? 1914 LEU   A CB   1 
ATOM   2990 C  CG   . LEU   A 1 582  ? 183.124 209.587 213.880 1.00 65.54  ? 1914 LEU   A CG   1 
ATOM   2991 C  CD1  . LEU   A 1 582  ? 183.417 210.902 214.504 1.00 76.13  ? 1914 LEU   A CD1  1 
ATOM   2992 C  CD2  . LEU   A 1 582  ? 184.036 208.608 214.565 1.00 64.08  ? 1914 LEU   A CD2  1 
ATOM   2993 N  N    . ARG   A 1 583  ? 180.252 206.112 212.764 1.00 89.32  ? 1915 ARG   A N    1 
ATOM   2994 C  CA   . ARG   A 1 583  ? 180.621 204.776 212.323 1.00 80.02  ? 1915 ARG   A CA   1 
ATOM   2995 C  C    . ARG   A 1 583  ? 180.374 204.605 210.832 1.00 76.45  ? 1915 ARG   A C    1 
ATOM   2996 O  O    . ARG   A 1 583  ? 181.231 204.073 210.120 1.00 76.20  ? 1915 ARG   A O    1 
ATOM   2997 C  CB   . ARG   A 1 583  ? 179.873 203.706 213.124 1.00 85.02  ? 1915 ARG   A CB   1 
ATOM   2998 C  CG   . ARG   A 1 583  ? 180.589 203.310 214.399 1.00 85.92  ? 1915 ARG   A CG   1 
ATOM   2999 C  CD   . ARG   A 1 583  ? 182.060 202.988 214.136 1.00 89.99  ? 1915 ARG   A CD   1 
ATOM   3000 N  NE   . ARG   A 1 583  ? 182.249 202.050 213.035 1.00 88.32  ? 1915 ARG   A NE   1 
ATOM   3001 C  CZ   . ARG   A 1 583  ? 183.430 201.619 212.614 1.00 79.27  ? 1915 ARG   A CZ   1 
ATOM   3002 N  NH1  . ARG   A 1 583  ? 184.556 202.043 213.162 1.00 77.61  ? 1915 ARG   A NH1  1 
ATOM   3003 N  NH2  . ARG   A 1 583  ? 183.483 200.743 211.616 1.00 66.11  ? 1915 ARG   A NH2  1 
ATOM   3004 N  N    . LEU   A 1 584  ? 179.227 205.066 210.334 1.00 80.88  ? 1916 LEU   A N    1 
ATOM   3005 C  CA   . LEU   A 1 584  ? 179.009 205.050 208.895 1.00 77.90  ? 1916 LEU   A CA   1 
ATOM   3006 C  C    . LEU   A 1 584  ? 180.082 205.855 208.174 1.00 71.82  ? 1916 LEU   A C    1 
ATOM   3007 O  O    . LEU   A 1 584  ? 180.668 205.384 207.195 1.00 70.62  ? 1916 LEU   A O    1 
ATOM   3008 C  CB   . LEU   A 1 584  ? 177.618 205.585 208.561 1.00 84.17  ? 1916 LEU   A CB   1 
ATOM   3009 C  CG   . LEU   A 1 584  ? 176.430 204.643 208.777 1.00 80.98  ? 1916 LEU   A CG   1 
ATOM   3010 C  CD1  . LEU   A 1 584  ? 176.128 204.420 210.253 1.00 79.41  ? 1916 LEU   A CD1  1 
ATOM   3011 C  CD2  . LEU   A 1 584  ? 175.198 205.154 208.040 1.00 95.18  ? 1916 LEU   A CD2  1 
ATOM   3012 N  N    . LEU   A 1 585  ? 180.382 207.055 208.669 1.00 63.13  ? 1917 LEU   A N    1 
ATOM   3013 C  CA   . LEU   A 1 585  ? 181.352 207.905 207.990 1.00 53.94  ? 1917 LEU   A CA   1 
ATOM   3014 C  C    . LEU   A 1 585  ? 182.741 207.283 207.994 1.00 58.00  ? 1917 LEU   A C    1 
ATOM   3015 O  O    . LEU   A 1 585  ? 183.433 207.286 206.967 1.00 64.51  ? 1917 LEU   A O    1 
ATOM   3016 C  CB   . LEU   A 1 585  ? 181.370 209.286 208.641 1.00 57.13  ? 1917 LEU   A CB   1 
ATOM   3017 C  CG   . LEU   A 1 585  ? 182.106 210.421 207.938 1.00 51.22  ? 1917 LEU   A CG   1 
ATOM   3018 C  CD1  . LEU   A 1 585  ? 181.484 211.737 208.318 1.00 58.95  ? 1917 LEU   A CD1  1 
ATOM   3019 C  CD2  . LEU   A 1 585  ? 183.533 210.427 208.357 1.00 49.49  ? 1917 LEU   A CD2  1 
ATOM   3020 N  N    . ARG   A 1 586  ? 183.177 206.753 209.136 1.00 56.01  ? 1918 ARG   A N    1 
ATOM   3021 C  CA   . ARG   A 1 586  ? 184.507 206.162 209.190 1.00 46.07  ? 1918 ARG   A CA   1 
ATOM   3022 C  C    . ARG   A 1 586  ? 184.599 204.914 208.336 1.00 52.12  ? 1918 ARG   A C    1 
ATOM   3023 O  O    . ARG   A 1 586  ? 185.561 204.752 207.582 1.00 60.14  ? 1918 ARG   A O    1 
ATOM   3024 C  CB   . ARG   A 1 586  ? 184.905 205.862 210.626 1.00 51.88  ? 1918 ARG   A CB   1 
ATOM   3025 C  CG   . ARG   A 1 586  ? 184.646 207.003 211.553 1.00 65.79  ? 1918 ARG   A CG   1 
ATOM   3026 C  CD   . ARG   A 1 586  ? 185.928 207.771 211.803 1.00 61.54  ? 1918 ARG   A CD   1 
ATOM   3027 N  NE   . ARG   A 1 586  ? 187.061 206.867 211.939 1.00 65.64  ? 1918 ARG   A NE   1 
ATOM   3028 C  CZ   . ARG   A 1 586  ? 188.308 207.173 211.619 1.00 65.42  ? 1918 ARG   A CZ   1 
ATOM   3029 N  NH1  . ARG   A 1 586  ? 188.630 208.370 211.161 1.00 61.22  ? 1918 ARG   A NH1  1 
ATOM   3030 N  NH2  . ARG   A 1 586  ? 189.257 206.256 211.767 1.00 64.22  ? 1918 ARG   A NH2  1 
ATOM   3031 N  N    . GLN   A 1 587  ? 183.618 204.017 208.425 1.00 54.94  ? 1919 GLN   A N    1 
ATOM   3032 C  CA   . GLN   A 1 587  ? 183.708 202.821 207.602 1.00 58.47  ? 1919 GLN   A CA   1 
ATOM   3033 C  C    . GLN   A 1 587  ? 183.492 203.121 206.127 1.00 56.37  ? 1919 GLN   A C    1 
ATOM   3034 O  O    . GLN   A 1 587  ? 183.819 202.279 205.287 1.00 62.57  ? 1919 GLN   A O    1 
ATOM   3035 C  CB   . GLN   A 1 587  ? 182.713 201.767 208.075 1.00 68.25  ? 1919 GLN   A CB   1 
ATOM   3036 C  CG   . GLN   A 1 587  ? 181.318 201.943 207.553 1.00 71.55  ? 1919 GLN   A CG   1 
ATOM   3037 C  CD   . GLN   A 1 587  ? 180.301 201.280 208.445 1.00 73.76  ? 1919 GLN   A CD   1 
ATOM   3038 O  OE1  . GLN   A 1 587  ? 179.161 201.728 208.540 1.00 82.48  ? 1919 GLN   A OE1  1 
ATOM   3039 N  NE2  . GLN   A 1 587  ? 180.705 200.208 209.107 1.00 67.56  ? 1919 GLN   A NE2  1 
ATOM   3040 N  N    . GLU   A 1 588  ? 182.965 204.299 205.790 1.00 49.50  ? 1920 GLU   A N    1 
ATOM   3041 C  CA   . GLU   A 1 588  ? 182.849 204.670 204.387 1.00 46.55  ? 1920 GLU   A CA   1 
ATOM   3042 C  C    . GLU   A 1 588  ? 184.159 205.226 203.856 1.00 43.74  ? 1920 GLU   A C    1 
ATOM   3043 O  O    . GLU   A 1 588  ? 184.632 204.816 202.793 1.00 51.82  ? 1920 GLU   A O    1 
ATOM   3044 C  CB   . GLU   A 1 588  ? 181.723 205.682 204.207 1.00 54.07  ? 1920 GLU   A CB   1 
ATOM   3045 C  CG   . GLU   A 1 588  ? 181.158 205.739 202.810 1.00 58.83  ? 1920 GLU   A CG   1 
ATOM   3046 C  CD   . GLU   A 1 588  ? 179.729 206.246 202.798 1.00 66.32  ? 1920 GLU   A CD   1 
ATOM   3047 O  OE1  . GLU   A 1 588  ? 179.413 207.160 202.011 1.00 56.02  ? 1920 GLU   A OE1  1 
ATOM   3048 O  OE2  . GLU   A 1 588  ? 178.918 205.736 203.594 1.00 74.46  ? 1920 GLU   A OE2  1 
ATOM   3049 N  N    . LEU   A 1 589  ? 184.778 206.151 204.582 1.00 40.81  ? 1921 LEU   A N    1 
ATOM   3050 C  CA   . LEU   A 1 589  ? 185.998 206.718 204.030 1.00 41.15  ? 1921 LEU   A CA   1 
ATOM   3051 C  C    . LEU   A 1 589  ? 187.224 205.839 204.251 1.00 49.41  ? 1921 LEU   A C    1 
ATOM   3052 O  O    . LEU   A 1 589  ? 188.235 206.057 203.583 1.00 54.22  ? 1921 LEU   A O    1 
ATOM   3053 C  CB   . LEU   A 1 589  ? 186.252 208.126 204.559 1.00 36.49  ? 1921 LEU   A CB   1 
ATOM   3054 C  CG   . LEU   A 1 589  ? 186.460 208.447 206.023 1.00 38.88  ? 1921 LEU   A CG   1 
ATOM   3055 C  CD1  . LEU   A 1 589  ? 187.887 208.198 206.424 1.00 45.69  ? 1921 LEU   A CD1  1 
ATOM   3056 C  CD2  . LEU   A 1 589  ? 186.145 209.901 206.172 1.00 34.92  ? 1921 LEU   A CD2  1 
ATOM   3057 N  N    . VAL   A 1 590  ? 187.183 204.846 205.143 1.00 49.57  ? 1922 VAL   A N    1 
ATOM   3058 C  CA   . VAL   A 1 590  ? 188.359 203.984 205.239 1.00 49.93  ? 1922 VAL   A CA   1 
ATOM   3059 C  C    . VAL   A 1 590  ? 188.432 203.034 204.058 1.00 50.99  ? 1922 VAL   A C    1 
ATOM   3060 O  O    . VAL   A 1 590  ? 189.460 202.380 203.850 1.00 59.34  ? 1922 VAL   A O    1 
ATOM   3061 C  CB   . VAL   A 1 590  ? 188.398 203.209 206.564 1.00 57.18  ? 1922 VAL   A CB   1 
ATOM   3062 C  CG1  . VAL   A 1 590  ? 188.493 204.166 207.736 1.00 61.52  ? 1922 VAL   A CG1  1 
ATOM   3063 C  CG2  . VAL   A 1 590  ? 187.193 202.287 206.674 1.00 58.36  ? 1922 VAL   A CG2  1 
ATOM   3064 N  N    . VAL   A 1 591  ? 187.361 202.920 203.277 1.00 47.06  ? 1923 VAL   A N    1 
ATOM   3065 C  CA   . VAL   A 1 591  ? 187.433 202.152 202.042 1.00 48.24  ? 1923 VAL   A CA   1 
ATOM   3066 C  C    . VAL   A 1 591  ? 187.529 203.111 200.865 1.00 48.46  ? 1923 VAL   A C    1 
ATOM   3067 O  O    . VAL   A 1 591  ? 188.205 202.821 199.874 1.00 51.30  ? 1923 VAL   A O    1 
ATOM   3068 C  CB   . VAL   A 1 591  ? 186.242 201.189 201.887 1.00 41.42  ? 1923 VAL   A CB   1 
ATOM   3069 C  CG1  . VAL   A 1 591  ? 184.952 201.937 201.751 1.00 46.17  ? 1923 VAL   A CG1  1 
ATOM   3070 C  CG2  . VAL   A 1 591  ? 186.444 200.316 200.682 1.00 41.01  ? 1923 VAL   A CG2  1 
ATOM   3071 N  N    . LEU   A 1 592  ? 186.891 204.277 200.972 1.00 47.59  ? 1924 LEU   A N    1 
ATOM   3072 C  CA   . LEU   A 1 592  ? 186.923 205.223 199.865 1.00 42.00  ? 1924 LEU   A CA   1 
ATOM   3073 C  C    . LEU   A 1 592  ? 188.269 205.914 199.724 1.00 43.65  ? 1924 LEU   A C    1 
ATOM   3074 O  O    . LEU   A 1 592  ? 188.621 206.345 198.624 1.00 51.22  ? 1924 LEU   A O    1 
ATOM   3075 C  CB   . LEU   A 1 592  ? 185.805 206.240 200.030 1.00 39.31  ? 1924 LEU   A CB   1 
ATOM   3076 C  CG   . LEU   A 1 592  ? 184.546 205.723 199.359 1.00 33.20  ? 1924 LEU   A CG   1 
ATOM   3077 C  CD1  . LEU   A 1 592  ? 183.459 206.727 199.461 1.00 33.80  ? 1924 LEU   A CD1  1 
ATOM   3078 C  CD2  . LEU   A 1 592  ? 184.864 205.456 197.910 1.00 28.87  ? 1924 LEU   A CD2  1 
ATOM   3079 N  N    . CYS   A 1 593  ? 189.029 206.048 200.806 1.00 47.74  ? 1925 CYS   A N    1 
ATOM   3080 C  CA   . CYS   A 1 593  ? 190.363 206.606 200.668 1.00 61.59  ? 1925 CYS   A CA   1 
ATOM   3081 C  C    . CYS   A 1 593  ? 191.380 205.581 200.196 1.00 72.59  ? 1925 CYS   A C    1 
ATOM   3082 O  O    . CYS   A 1 593  ? 192.531 205.950 199.946 1.00 83.53  ? 1925 CYS   A O    1 
ATOM   3083 C  CB   . CYS   A 1 593  ? 190.824 207.225 201.987 1.00 69.28  ? 1925 CYS   A CB   1 
ATOM   3084 S  SG   . CYS   A 1 593  ? 189.732 208.502 202.634 1.00 99.21  ? 1925 CYS   A SG   1 
ATOM   3085 N  N    . HIS   A 1 594  ? 191.000 204.313 200.072 1.00 66.70  ? 1926 HIS   A N    1 
ATOM   3086 C  CA   . HIS   A 1 594  ? 191.919 203.280 199.611 1.00 67.63  ? 1926 HIS   A CA   1 
ATOM   3087 C  C    . HIS   A 1 594  ? 191.452 202.637 198.309 1.00 66.69  ? 1926 HIS   A C    1 
ATOM   3088 O  O    . HIS   A 1 594  ? 191.754 201.475 198.042 1.00 75.92  ? 1926 HIS   A O    1 
ATOM   3089 C  CB   . HIS   A 1 594  ? 192.137 202.226 200.693 1.00 64.60  ? 1926 HIS   A CB   1 
ATOM   3090 C  CG   . HIS   A 1 594  ? 192.724 202.777 201.956 1.00 74.36  ? 1926 HIS   A CG   1 
ATOM   3091 N  ND1  . HIS   A 1 594  ? 193.487 203.924 201.979 1.00 75.98  ? 1926 HIS   A ND1  1 
ATOM   3092 C  CD2  . HIS   A 1 594  ? 192.669 202.335 203.234 1.00 89.82  ? 1926 HIS   A CD2  1 
ATOM   3093 C  CE1  . HIS   A 1 594  ? 193.873 204.168 203.219 1.00 80.82  ? 1926 HIS   A CE1  1 
ATOM   3094 N  NE2  . HIS   A 1 594  ? 193.390 203.219 203.999 1.00 95.76  ? 1926 HIS   A NE2  1 
ATOM   3095 N  N    . LEU   A 1 595  ? 190.714 203.386 197.490 1.00 60.24  ? 1927 LEU   A N    1 
ATOM   3096 C  CA   . LEU   A 1 595  ? 190.320 202.945 196.152 1.00 57.92  ? 1927 LEU   A CA   1 
ATOM   3097 C  C    . LEU   A 1 595  ? 190.455 204.122 195.194 1.00 59.55  ? 1927 LEU   A C    1 
ATOM   3098 O  O    . LEU   A 1 595  ? 189.600 205.011 195.166 1.00 57.22  ? 1927 LEU   A O    1 
ATOM   3099 C  CB   . LEU   A 1 595  ? 188.907 202.382 196.139 1.00 53.37  ? 1927 LEU   A CB   1 
ATOM   3100 C  CG   . LEU   A 1 595  ? 188.767 201.105 196.951 1.00 48.34  ? 1927 LEU   A CG   1 
ATOM   3101 C  CD1  . LEU   A 1 595  ? 187.321 200.713 197.115 1.00 46.04  ? 1927 LEU   A CD1  1 
ATOM   3102 C  CD2  . LEU   A 1 595  ? 189.550 200.018 196.246 1.00 43.98  ? 1927 LEU   A CD2  1 
ATOM   3103 N  N    . HIS   A 1 596  ? 191.524 204.114 194.406 1.00 64.04  ? 1928 HIS   A N    1 
ATOM   3104 C  CA   . HIS   A 1 596  ? 191.792 205.145 193.411 1.00 67.70  ? 1928 HIS   A CA   1 
ATOM   3105 C  C    . HIS   A 1 596  ? 191.939 204.456 192.058 1.00 59.15  ? 1928 HIS   A C    1 
ATOM   3106 O  O    . HIS   A 1 596  ? 193.019 203.982 191.702 1.00 69.33  ? 1928 HIS   A O    1 
ATOM   3107 C  CB   . HIS   A 1 596  ? 193.032 205.936 193.766 1.00 80.34  ? 1928 HIS   A CB   1 
ATOM   3108 C  CG   . HIS   A 1 596  ? 193.105 206.332 195.205 1.00 83.14  ? 1928 HIS   A CG   1 
ATOM   3109 N  ND1  . HIS   A 1 596  ? 192.642 207.544 195.667 1.00 88.20  ? 1928 HIS   A ND1  1 
ATOM   3110 C  CD2  . HIS   A 1 596  ? 193.613 205.687 196.280 1.00 82.37  ? 1928 HIS   A CD2  1 
ATOM   3111 C  CE1  . HIS   A 1 596  ? 192.849 207.623 196.969 1.00 94.13  ? 1928 HIS   A CE1  1 
ATOM   3112 N  NE2  . HIS   A 1 596  ? 193.438 206.510 197.365 1.00 88.55  ? 1928 HIS   A NE2  1 
ATOM   3113 N  N    . HIS   A 1 597  ? 190.846 204.400 191.309 1.00 47.97  ? 1929 HIS   A N    1 
ATOM   3114 C  CA   . HIS   A 1 597  ? 190.819 203.787 189.994 1.00 55.25  ? 1929 HIS   A CA   1 
ATOM   3115 C  C    . HIS   A 1 597  ? 190.007 204.680 189.072 1.00 55.96  ? 1929 HIS   A C    1 
ATOM   3116 O  O    . HIS   A 1 597  ? 189.090 205.370 189.531 1.00 56.73  ? 1929 HIS   A O    1 
ATOM   3117 C  CB   . HIS   A 1 597  ? 190.196 202.386 190.058 1.00 52.93  ? 1929 HIS   A CB   1 
ATOM   3118 C  CG   . HIS   A 1 597  ? 190.399 201.562 188.827 1.00 54.36  ? 1929 HIS   A CG   1 
ATOM   3119 N  ND1  . HIS   A 1 597  ? 189.359 201.194 188.003 1.00 49.51  ? 1929 HIS   A ND1  1 
ATOM   3120 C  CD2  . HIS   A 1 597  ? 191.513 201.006 188.299 1.00 59.64  ? 1929 HIS   A CD2  1 
ATOM   3121 C  CE1  . HIS   A 1 597  ? 189.826 200.460 187.011 1.00 46.93  ? 1929 HIS   A CE1  1 
ATOM   3122 N  NE2  . HIS   A 1 597  ? 191.130 200.331 187.166 1.00 56.12  ? 1929 HIS   A NE2  1 
ATOM   3123 N  N    . PRO   A 1 598  ? 190.327 204.706 187.777 1.00 49.36  ? 1930 PRO   A N    1 
ATOM   3124 C  CA   . PRO   A 1 598  ? 189.533 205.535 186.863 1.00 47.63  ? 1930 PRO   A CA   1 
ATOM   3125 C  C    . PRO   A 1 598  ? 188.073 205.148 186.829 1.00 43.51  ? 1930 PRO   A C    1 
ATOM   3126 O  O    . PRO   A 1 598  ? 187.222 206.010 186.588 1.00 47.15  ? 1930 PRO   A O    1 
ATOM   3127 C  CB   . PRO   A 1 598  ? 190.217 205.308 185.510 1.00 37.50  ? 1930 PRO   A CB   1 
ATOM   3128 C  CG   . PRO   A 1 598  ? 191.598 204.923 185.855 1.00 43.04  ? 1930 PRO   A CG   1 
ATOM   3129 C  CD   . PRO   A 1 598  ? 191.488 204.114 187.099 1.00 43.01  ? 1930 PRO   A CD   1 
ATOM   3130 N  N    . SER   A 1 599  ? 187.749 203.887 187.083 1.00 39.35  ? 1931 SER   A N    1 
ATOM   3131 C  CA   . SER   A 1 599  ? 186.366 203.440 187.076 1.00 33.03  ? 1931 SER   A CA   1 
ATOM   3132 C  C    . SER   A 1 599  ? 185.755 203.331 188.463 1.00 35.87  ? 1931 SER   A C    1 
ATOM   3133 O  O    . SER   A 1 599  ? 184.622 202.861 188.580 1.00 33.90  ? 1931 SER   A O    1 
ATOM   3134 C  CB   . SER   A 1 599  ? 186.249 202.093 186.382 1.00 37.37  ? 1931 SER   A CB   1 
ATOM   3135 O  OG   . SER   A 1 599  ? 185.000 201.514 186.683 1.00 45.05  ? 1931 SER   A OG   1 
ATOM   3136 N  N    . LEU   A 1 600  ? 186.472 203.727 189.511 1.00 44.62  ? 1932 LEU   A N    1 
ATOM   3137 C  CA   . LEU   A 1 600  ? 185.941 203.762 190.867 1.00 42.55  ? 1932 LEU   A CA   1 
ATOM   3138 C  C    . LEU   A 1 600  ? 185.753 205.209 191.288 1.00 45.41  ? 1932 LEU   A C    1 
ATOM   3139 O  O    . LEU   A 1 600  ? 186.670 206.021 191.138 1.00 54.77  ? 1932 LEU   A O    1 
ATOM   3140 C  CB   . LEU   A 1 600  ? 186.872 203.047 191.849 1.00 37.47  ? 1932 LEU   A CB   1 
ATOM   3141 C  CG   . LEU   A 1 600  ? 187.096 201.553 191.651 1.00 39.05  ? 1932 LEU   A CG   1 
ATOM   3142 C  CD1  . LEU   A 1 600  ? 188.171 201.027 192.569 1.00 41.67  ? 1932 LEU   A CD1  1 
ATOM   3143 C  CD2  . LEU   A 1 600  ? 185.806 200.838 191.916 1.00 42.44  ? 1932 LEU   A CD2  1 
ATOM   3144 N  N    . ILE   A 1 601  ? 184.572 205.530 191.821 1.00 33.61  ? 1933 ILE   A N    1 
ATOM   3145 C  CA   . ILE   A 1 601  ? 184.286 206.915 192.158 1.00 31.98  ? 1933 ILE   A CA   1 
ATOM   3146 C  C    . ILE   A 1 601  ? 185.254 207.386 193.237 1.00 37.26  ? 1933 ILE   A C    1 
ATOM   3147 O  O    . ILE   A 1 601  ? 185.656 206.624 194.124 1.00 41.61  ? 1933 ILE   A O    1 
ATOM   3148 C  CB   . ILE   A 1 601  ? 182.827 207.100 192.600 1.00 28.50  ? 1933 ILE   A CB   1 
ATOM   3149 C  CG1  . ILE   A 1 601  ? 182.477 208.577 192.610 1.00 28.77  ? 1933 ILE   A CG1  1 
ATOM   3150 C  CG2  . ILE   A 1 601  ? 182.604 206.538 193.967 1.00 37.08  ? 1933 ILE   A CG2  1 
ATOM   3151 C  CD1  . ILE   A 1 601  ? 181.028 208.834 192.592 1.00 27.30  ? 1933 ILE   A CD1  1 
ATOM   3152 N  N    . SER   A 1 602  ? 185.659 208.646 193.139 1.00 37.81  ? 1934 SER   A N    1 
ATOM   3153 C  CA   . SER   A 1 602  ? 186.707 209.197 193.983 1.00 40.10  ? 1934 SER   A CA   1 
ATOM   3154 C  C    . SER   A 1 602  ? 186.127 210.148 195.021 1.00 38.87  ? 1934 SER   A C    1 
ATOM   3155 O  O    . SER   A 1 602  ? 185.030 210.685 194.860 1.00 47.50  ? 1934 SER   A O    1 
ATOM   3156 C  CB   . SER   A 1 602  ? 187.757 209.919 193.143 1.00 43.27  ? 1934 SER   A CB   1 
ATOM   3157 O  OG   . SER   A 1 602  ? 187.200 211.058 192.529 1.00 42.86  ? 1934 SER   A OG   1 
ATOM   3158 N  N    . LEU   A 1 603  ? 186.878 210.336 196.100 1.00 32.75  ? 1935 LEU   A N    1 
ATOM   3159 C  CA   . LEU   A 1 603  ? 186.441 211.106 197.255 1.00 31.24  ? 1935 LEU   A CA   1 
ATOM   3160 C  C    . LEU   A 1 603  ? 187.128 212.463 197.287 1.00 44.32  ? 1935 LEU   A C    1 
ATOM   3161 O  O    . LEU   A 1 603  ? 188.350 212.552 197.130 1.00 49.41  ? 1935 LEU   A O    1 
ATOM   3162 C  CB   . LEU   A 1 603  ? 186.739 210.337 198.541 1.00 28.02  ? 1935 LEU   A CB   1 
ATOM   3163 C  CG   . LEU   A 1 603  ? 186.324 210.919 199.888 1.00 26.57  ? 1935 LEU   A CG   1 
ATOM   3164 C  CD1  . LEU   A 1 603  ? 184.840 211.083 200.010 1.00 34.13  ? 1935 LEU   A CD1  1 
ATOM   3165 C  CD2  . LEU   A 1 603  ? 186.843 210.036 200.995 1.00 35.66  ? 1935 LEU   A CD2  1 
ATOM   3166 N  N    . LEU   A 1 604  ? 186.339 213.512 197.501 1.00 52.66  ? 1936 LEU   A N    1 
ATOM   3167 C  CA   . LEU   A 1 604  ? 186.858 214.850 197.725 1.00 47.13  ? 1936 LEU   A CA   1 
ATOM   3168 C  C    . LEU   A 1 604  ? 186.265 215.391 199.013 1.00 41.44  ? 1936 LEU   A C    1 
ATOM   3169 O  O    . LEU   A 1 604  ? 185.051 215.347 199.207 1.00 40.16  ? 1936 LEU   A O    1 
ATOM   3170 C  CB   . LEU   A 1 604  ? 186.497 215.783 196.574 1.00 40.73  ? 1936 LEU   A CB   1 
ATOM   3171 C  CG   . LEU   A 1 604  ? 186.980 215.354 195.195 1.00 45.98  ? 1936 LEU   A CG   1 
ATOM   3172 C  CD1  . LEU   A 1 604  ? 186.410 216.281 194.140 1.00 44.57  ? 1936 LEU   A CD1  1 
ATOM   3173 C  CD2  . LEU   A 1 604  ? 188.494 215.311 195.143 1.00 49.97  ? 1936 LEU   A CD2  1 
ATOM   3174 N  N    . ALA   A 1 605  ? 187.115 215.907 199.888 1.00 40.24  ? 1937 ALA   A N    1 
ATOM   3175 C  CA   . ALA   A 1 605  ? 186.664 216.659 201.050 1.00 50.29  ? 1937 ALA   A CA   1 
ATOM   3176 C  C    . ALA   A 1 605  ? 185.683 215.862 201.916 1.00 45.67  ? 1937 ALA   A C    1 
ATOM   3177 O  O    . ALA   A 1 605  ? 184.467 215.982 201.792 1.00 51.91  ? 1937 ALA   A O    1 
ATOM   3178 C  CB   . ALA   A 1 605  ? 186.051 217.979 200.600 1.00 55.09  ? 1937 ALA   A CB   1 
ATOM   3179 N  N    . ALA   A 1 606  ? 186.235 215.008 202.775 1.00 41.16  ? 1938 ALA   A N    1 
ATOM   3180 C  CA   . ALA   A 1 606  ? 185.456 214.365 203.830 1.00 38.01  ? 1938 ALA   A CA   1 
ATOM   3181 C  C    . ALA   A 1 606  ? 185.449 215.275 205.047 1.00 41.60  ? 1938 ALA   A C    1 
ATOM   3182 O  O    . ALA   A 1 606  ? 186.497 215.519 205.649 1.00 46.48  ? 1938 ALA   A O    1 
ATOM   3183 C  CB   . ALA   A 1 606  ? 186.040 213.004 204.181 1.00 49.43  ? 1938 ALA   A CB   1 
ATOM   3184 N  N    . GLY   A 1 607  ? 184.270 215.769 205.431 1.00 43.77  ? 1939 GLY   A N    1 
ATOM   3185 C  CA   . GLY   A 1 607  ? 184.168 216.827 206.407 1.00 49.34  ? 1939 GLY   A CA   1 
ATOM   3186 C  C    . GLY   A 1 607  ? 183.313 216.460 207.608 1.00 45.33  ? 1939 GLY   A C    1 
ATOM   3187 O  O    . GLY   A 1 607  ? 182.471 215.559 207.561 1.00 53.81  ? 1939 GLY   A O    1 
ATOM   3188 N  N    . ILE   A 1 608  ? 183.517 217.217 208.681 1.00 38.13  ? 1940 ILE   A N    1 
ATOM   3189 C  CA   . ILE   A 1 608  ? 182.936 216.915 209.976 1.00 45.17  ? 1940 ILE   A CA   1 
ATOM   3190 C  C    . ILE   A 1 608  ? 181.909 217.953 210.404 1.00 58.18  ? 1940 ILE   A C    1 
ATOM   3191 O  O    . ILE   A 1 608  ? 180.901 217.600 211.019 1.00 65.45  ? 1940 ILE   A O    1 
ATOM   3192 C  CB   . ILE   A 1 608  ? 184.027 216.751 211.054 1.00 47.65  ? 1940 ILE   A CB   1 
ATOM   3193 C  CG1  . ILE   A 1 608  ? 183.391 216.215 212.329 1.00 51.46  ? 1940 ILE   A CG1  1 
ATOM   3194 C  CG2  . ILE   A 1 608  ? 184.770 218.044 211.304 1.00 47.60  ? 1940 ILE   A CG2  1 
ATOM   3195 C  CD1  . ILE   A 1 608  ? 184.358 215.740 213.321 1.00 48.64  ? 1940 ILE   A CD1  1 
ATOM   3196 N  N    . ARG   A 1 609  ? 182.146 219.233 210.118 1.00 55.06  ? 1941 ARG   A N    1 
ATOM   3197 C  CA   . ARG   A 1 609  ? 181.304 220.266 210.717 1.00 56.36  ? 1941 ARG   A CA   1 
ATOM   3198 C  C    . ARG   A 1 609  ? 179.835 220.084 210.368 1.00 55.56  ? 1941 ARG   A C    1 
ATOM   3199 O  O    . ARG   A 1 609  ? 179.000 220.145 211.286 1.00 65.99  ? 1941 ARG   A O    1 
ATOM   3200 C  CB   . ARG   A 1 609  ? 181.837 221.654 210.352 1.00 63.06  ? 1941 ARG   A CB   1 
ATOM   3201 C  CG   . ARG   A 1 609  ? 181.421 222.742 211.327 1.00 79.67  ? 1941 ARG   A CG   1 
ATOM   3202 C  CD   . ARG   A 1 609  ? 181.709 222.385 212.781 1.00 84.04  ? 1941 ARG   A CD   1 
ATOM   3203 N  NE   . ARG   A 1 609  ? 182.994 221.726 212.977 1.00 85.35  ? 1941 ARG   A NE   1 
ATOM   3204 C  CZ   . ARG   A 1 609  ? 183.450 221.315 214.151 1.00 87.99  ? 1941 ARG   A CZ   1 
ATOM   3205 N  NH1  . ARG   A 1 609  ? 182.746 221.474 215.259 1.00 91.75  ? 1941 ARG   A NH1  1 
ATOM   3206 N  NH2  . ARG   A 1 609  ? 184.641 220.729 214.216 1.00 88.75  ? 1941 ARG   A NH2  1 
ATOM   3207 N  N    . PRO   A 1 610  ? 179.439 219.860 209.112 1.00 52.55  ? 1942 PRO   A N    1 
ATOM   3208 C  CA   . PRO   A 1 610  ? 178.126 219.247 208.877 1.00 58.79  ? 1942 PRO   A CA   1 
ATOM   3209 C  C    . PRO   A 1 610  ? 178.164 217.727 208.847 1.00 64.29  ? 1942 PRO   A C    1 
ATOM   3210 O  O    . PRO   A 1 610  ? 177.099 217.104 208.744 1.00 71.73  ? 1942 PRO   A O    1 
ATOM   3211 C  CB   . PRO   A 1 610  ? 177.717 219.803 207.510 1.00 62.15  ? 1942 PRO   A CB   1 
ATOM   3212 C  CG   . PRO   A 1 610  ? 178.556 221.010 207.312 1.00 58.33  ? 1942 PRO   A CG   1 
ATOM   3213 C  CD   . PRO   A 1 610  ? 179.858 220.659 207.951 1.00 54.09  ? 1942 PRO   A CD   1 
ATOM   3214 N  N    . ARG   A 1 611  ? 179.351 217.118 208.936 1.00 61.52  ? 1943 ARG   A N    1 
ATOM   3215 C  CA   . ARG   A 1 611  ? 179.543 215.669 208.848 1.00 58.83  ? 1943 ARG   A CA   1 
ATOM   3216 C  C    . ARG   A 1 611  ? 179.057 215.134 207.498 1.00 65.44  ? 1943 ARG   A C    1 
ATOM   3217 O  O    . ARG   A 1 611  ? 178.081 214.392 207.399 1.00 82.46  ? 1943 ARG   A O    1 
ATOM   3218 C  CB   . ARG   A 1 611  ? 178.848 214.951 210.009 1.00 63.29  ? 1943 ARG   A CB   1 
ATOM   3219 N  N    . MET   A 1 612  ? 179.766 215.548 206.450 1.00 57.44  ? 1944 MET   A N    1 
ATOM   3220 C  CA   . MET   A 1 612  ? 179.351 215.209 205.099 1.00 59.21  ? 1944 MET   A CA   1 
ATOM   3221 C  C    . MET   A 1 612  ? 180.524 214.633 204.325 1.00 51.56  ? 1944 MET   A C    1 
ATOM   3222 O  O    . MET   A 1 612  ? 181.689 214.847 204.665 1.00 47.41  ? 1944 MET   A O    1 
ATOM   3223 C  CB   . MET   A 1 612  ? 178.806 216.427 204.345 1.00 59.36  ? 1944 MET   A CB   1 
ATOM   3224 C  CG   . MET   A 1 612  ? 179.720 217.642 204.348 1.00 57.10  ? 1944 MET   A CG   1 
ATOM   3225 S  SD   . MET   A 1 612  ? 178.771 219.164 204.276 1.00 69.52  ? 1944 MET   A SD   1 
ATOM   3226 C  CE   . MET   A 1 612  ? 177.858 218.916 202.766 1.00 54.50  ? 1944 MET   A CE   1 
ATOM   3227 N  N    . LEU   A 1 613  ? 180.188 213.895 203.272 1.00 44.21  ? 1945 LEU   A N    1 
ATOM   3228 C  CA   . LEU   A 1 613  ? 181.116 213.500 202.226 1.00 37.82  ? 1945 LEU   A CA   1 
ATOM   3229 C  C    . LEU   A 1 613  ? 180.778 214.249 200.950 1.00 41.69  ? 1945 LEU   A C    1 
ATOM   3230 O  O    . LEU   A 1 613  ? 179.605 214.385 200.592 1.00 39.78  ? 1945 LEU   A O    1 
ATOM   3231 C  CB   . LEU   A 1 613  ? 181.062 211.999 201.952 1.00 37.98  ? 1945 LEU   A CB   1 
ATOM   3232 C  CG   . LEU   A 1 613  ? 181.531 211.019 203.012 1.00 41.58  ? 1945 LEU   A CG   1 
ATOM   3233 C  CD1  . LEU   A 1 613  ? 181.230 209.636 202.543 1.00 45.89  ? 1945 LEU   A CD1  1 
ATOM   3234 C  CD2  . LEU   A 1 613  ? 183.015 211.176 203.181 1.00 42.06  ? 1945 LEU   A CD2  1 
ATOM   3235 N  N    . VAL   A 1 614  ? 181.809 214.732 200.268 1.00 37.71  ? 1946 VAL   A N    1 
ATOM   3236 C  CA   . VAL   A 1 614  ? 181.658 215.475 199.028 1.00 27.81  ? 1946 VAL   A CA   1 
ATOM   3237 C  C    . VAL   A 1 614  ? 182.159 214.581 197.900 1.00 35.81  ? 1946 VAL   A C    1 
ATOM   3238 O  O    . VAL   A 1 614  ? 183.285 214.077 197.948 1.00 38.84  ? 1946 VAL   A O    1 
ATOM   3239 C  CB   . VAL   A 1 614  ? 182.424 216.802 199.083 1.00 23.47  ? 1946 VAL   A CB   1 
ATOM   3240 C  CG1  . VAL   A 1 614  ? 182.333 217.511 197.785 1.00 30.68  ? 1946 VAL   A CG1  1 
ATOM   3241 C  CG2  . VAL   A 1 614  ? 181.926 217.663 200.212 1.00 28.81  ? 1946 VAL   A CG2  1 
ATOM   3242 N  N    . MET   A 1 615  ? 181.318 214.357 196.900 1.00 36.18  ? 1947 MET   A N    1 
ATOM   3243 C  CA   . MET   A 1 615  ? 181.606 213.422 195.825 1.00 27.85  ? 1947 MET   A CA   1 
ATOM   3244 C  C    . MET   A 1 615  ? 181.577 214.109 194.468 1.00 33.36  ? 1947 MET   A C    1 
ATOM   3245 O  O    . MET   A 1 615  ? 180.795 215.035 194.245 1.00 38.43  ? 1947 MET   A O    1 
ATOM   3246 C  CB   . MET   A 1 615  ? 180.596 212.278 195.817 1.00 34.61  ? 1947 MET   A CB   1 
ATOM   3247 C  CG   . MET   A 1 615  ? 180.632 211.362 197.000 1.00 35.46  ? 1947 MET   A CG   1 
ATOM   3248 S  SD   . MET   A 1 615  ? 182.200 210.497 197.062 1.00 32.13  ? 1947 MET   A SD   1 
ATOM   3249 C  CE   . MET   A 1 615  ? 182.001 209.707 198.635 1.00 39.74  ? 1947 MET   A CE   1 
ATOM   3250 N  N    . GLU   A 1 616  ? 182.414 213.616 193.554 1.00 34.50  ? 1948 GLU   A N    1 
ATOM   3251 C  CA   . GLU   A 1 616  ? 182.379 214.073 192.171 1.00 32.69  ? 1948 GLU   A CA   1 
ATOM   3252 C  C    . GLU   A 1 616  ? 181.003 213.856 191.568 1.00 31.21  ? 1948 GLU   A C    1 
ATOM   3253 O  O    . GLU   A 1 616  ? 180.388 212.805 191.752 1.00 35.07  ? 1948 GLU   A O    1 
ATOM   3254 C  CB   . GLU   A 1 616  ? 183.402 213.322 191.331 1.00 32.84  ? 1948 GLU   A CB   1 
ATOM   3255 C  CG   . GLU   A 1 616  ? 184.829 213.613 191.674 1.00 52.34  ? 1948 GLU   A CG   1 
ATOM   3256 C  CD   . GLU   A 1 616  ? 185.790 212.822 190.814 1.00 63.67  ? 1948 GLU   A CD   1 
ATOM   3257 O  OE1  . GLU   A 1 616  ? 185.323 211.957 190.048 1.00 58.66  ? 1948 GLU   A OE1  1 
ATOM   3258 O  OE2  . GLU   A 1 616  ? 187.011 213.068 190.896 1.00 69.70  ? 1948 GLU   A OE2  1 
ATOM   3259 N  N    . LEU   A 1 617  ? 180.521 214.854 190.835 1.00 32.00  ? 1949 LEU   A N    1 
ATOM   3260 C  CA   . LEU   A 1 617  ? 179.220 214.758 190.199 1.00 42.74  ? 1949 LEU   A CA   1 
ATOM   3261 C  C    . LEU   A 1 617  ? 179.259 213.792 189.030 1.00 52.83  ? 1949 LEU   A C    1 
ATOM   3262 O  O    . LEU   A 1 617  ? 180.257 213.700 188.311 1.00 61.40  ? 1949 LEU   A O    1 
ATOM   3263 C  CB   . LEU   A 1 617  ? 178.733 216.113 189.697 1.00 45.17  ? 1949 LEU   A CB   1 
ATOM   3264 C  CG   . LEU   A 1 617  ? 177.206 216.218 189.723 1.00 46.70  ? 1949 LEU   A CG   1 
ATOM   3265 C  CD1  . LEU   A 1 617  ? 176.659 215.892 191.075 1.00 47.07  ? 1949 LEU   A CD1  1 
ATOM   3266 C  CD2  . LEU   A 1 617  ? 176.703 217.557 189.245 1.00 46.47  ? 1949 LEU   A CD2  1 
ATOM   3267 N  N    . ALA   A 1 618  ? 178.161 213.072 188.845 1.00 45.21  ? 1950 ALA   A N    1 
ATOM   3268 C  CA   . ALA   A 1 618  ? 177.920 212.361 187.600 1.00 42.38  ? 1950 ALA   A CA   1 
ATOM   3269 C  C    . ALA   A 1 618  ? 177.138 213.303 186.700 1.00 48.57  ? 1950 ALA   A C    1 
ATOM   3270 O  O    . ALA   A 1 618  ? 175.938 213.507 186.889 1.00 56.86  ? 1950 ALA   A O    1 
ATOM   3271 C  CB   . ALA   A 1 618  ? 177.172 211.062 187.858 1.00 49.21  ? 1950 ALA   A CB   1 
ATOM   3272 N  N    . SER   A 1 619  ? 177.824 213.886 185.716 1.00 42.24  ? 1951 SER   A N    1 
ATOM   3273 C  CA   . SER   A 1 619  ? 177.220 214.946 184.919 1.00 46.55  ? 1951 SER   A CA   1 
ATOM   3274 C  C    . SER   A 1 619  ? 175.969 214.457 184.204 1.00 51.50  ? 1951 SER   A C    1 
ATOM   3275 O  O    . SER   A 1 619  ? 174.938 215.137 184.211 1.00 58.62  ? 1951 SER   A O    1 
ATOM   3276 C  CB   . SER   A 1 619  ? 178.238 215.476 183.917 1.00 56.07  ? 1951 SER   A CB   1 
ATOM   3277 O  OG   . SER   A 1 619  ? 179.330 216.073 184.588 1.00 68.31  ? 1951 SER   A OG   1 
ATOM   3278 N  N    . LYS   A 1 620  ? 176.038 213.279 183.588 1.00 46.98  ? 1952 LYS   A N    1 
ATOM   3279 C  CA   . LYS   A 1 620  ? 174.866 212.649 182.997 1.00 42.44  ? 1952 LYS   A CA   1 
ATOM   3280 C  C    . LYS   A 1 620  ? 174.184 211.663 183.929 1.00 44.82  ? 1952 LYS   A C    1 
ATOM   3281 O  O    . LYS   A 1 620  ? 173.064 211.236 183.638 1.00 52.83  ? 1952 LYS   A O    1 
ATOM   3282 C  CB   . LYS   A 1 620  ? 175.231 211.954 181.683 1.00 31.74  ? 1952 LYS   A CB   1 
ATOM   3283 C  CG   . LYS   A 1 620  ? 175.307 212.896 180.492 1.00 33.76  ? 1952 LYS   A CG   1 
ATOM   3284 C  CD   . LYS   A 1 620  ? 176.525 213.783 180.521 1.00 40.10  ? 1952 LYS   A CD   1 
ATOM   3285 C  CE   . LYS   A 1 620  ? 176.617 214.640 179.277 1.00 49.12  ? 1952 LYS   A CE   1 
ATOM   3286 N  NZ   . LYS   A 1 620  ? 177.752 215.595 179.361 1.00 48.61  ? 1952 LYS   A NZ   1 
ATOM   3287 N  N    . GLY   A 1 621  ? 174.822 211.286 185.023 1.00 40.86  ? 1953 GLY   A N    1 
ATOM   3288 C  CA   . GLY   A 1 621  ? 174.102 210.677 186.123 1.00 39.45  ? 1953 GLY   A CA   1 
ATOM   3289 C  C    . GLY   A 1 621  ? 174.088 209.167 186.072 1.00 50.94  ? 1953 GLY   A C    1 
ATOM   3290 O  O    . GLY   A 1 621  ? 174.872 208.520 185.380 1.00 54.31  ? 1953 GLY   A O    1 
ATOM   3291 N  N    . SER   A 1 622  ? 173.167 208.601 186.844 1.00 60.97  ? 1954 SER   A N    1 
ATOM   3292 C  CA   . SER   A 1 622  ? 173.082 207.155 186.975 1.00 63.86  ? 1954 SER   A CA   1 
ATOM   3293 C  C    . SER   A 1 622  ? 172.723 206.510 185.643 1.00 66.96  ? 1954 SER   A C    1 
ATOM   3294 O  O    . SER   A 1 622  ? 171.942 207.050 184.856 1.00 68.77  ? 1954 SER   A O    1 
ATOM   3295 C  CB   . SER   A 1 622  ? 172.041 206.777 188.023 1.00 66.05  ? 1954 SER   A CB   1 
ATOM   3296 O  OG   . SER   A 1 622  ? 170.746 207.148 187.589 1.00 81.09  ? 1954 SER   A OG   1 
ATOM   3297 N  N    . LEU   A 1 623  ? 173.290 205.324 185.409 1.00 54.87  ? 1955 LEU   A N    1 
ATOM   3298 C  CA   . LEU   A 1 623  ? 173.055 204.624 184.152 1.00 47.20  ? 1955 LEU   A CA   1 
ATOM   3299 C  C    . LEU   A 1 623  ? 171.579 204.356 183.919 1.00 63.10  ? 1955 LEU   A C    1 
ATOM   3300 O  O    . LEU   A 1 623  ? 171.078 204.568 182.813 1.00 71.17  ? 1955 LEU   A O    1 
ATOM   3301 C  CB   . LEU   A 1 623  ? 173.840 203.318 184.126 1.00 39.20  ? 1955 LEU   A CB   1 
ATOM   3302 C  CG   . LEU   A 1 623  ? 173.687 202.518 182.839 1.00 39.14  ? 1955 LEU   A CG   1 
ATOM   3303 C  CD1  . LEU   A 1 623  ? 174.194 203.276 181.670 1.00 35.46  ? 1955 LEU   A CD1  1 
ATOM   3304 C  CD2  . LEU   A 1 623  ? 174.430 201.213 182.957 1.00 47.06  ? 1955 LEU   A CD2  1 
ATOM   3305 N  N    . ASP   A 1 624  ? 170.859 203.915 184.949 1.00 66.03  ? 1956 ASP   A N    1 
ATOM   3306 C  CA   . ASP   A 1 624  ? 169.485 203.471 184.745 1.00 64.36  ? 1956 ASP   A CA   1 
ATOM   3307 C  C    . ASP   A 1 624  ? 168.611 204.594 184.203 1.00 77.61  ? 1956 ASP   A C    1 
ATOM   3308 O  O    . ASP   A 1 624  ? 167.765 204.376 183.327 1.00 81.96  ? 1956 ASP   A O    1 
ATOM   3309 C  CB   . ASP   A 1 624  ? 168.943 202.865 186.046 1.00 62.36  ? 1956 ASP   A CB   1 
ATOM   3310 C  CG   . ASP   A 1 624  ? 168.426 203.898 187.057 1.00 74.61  ? 1956 ASP   A CG   1 
ATOM   3311 O  OD1  . ASP   A 1 624  ? 168.290 205.102 186.765 1.00 74.60  ? 1956 ASP   A OD1  1 
ATOM   3312 O  OD2  . ASP   A 1 624  ? 168.155 203.478 188.200 1.00 81.99  ? 1956 ASP   A OD2  1 
ATOM   3313 N  N    . ARG   A 1 625  ? 168.811 205.808 184.711 1.00 78.58  ? 1957 ARG   A N    1 
ATOM   3314 C  CA   . ARG   A 1 625  ? 168.047 206.955 184.237 1.00 87.90  ? 1957 ARG   A CA   1 
ATOM   3315 C  C    . ARG   A 1 625  ? 168.330 207.226 182.765 1.00 93.32  ? 1957 ARG   A C    1 
ATOM   3316 O  O    . ARG   A 1 625  ? 167.469 207.741 182.043 1.00 98.20  ? 1957 ARG   A O    1 
ATOM   3317 C  CB   . ARG   A 1 625  ? 168.368 208.162 185.122 1.00 83.40  ? 1957 ARG   A CB   1 
ATOM   3318 C  CG   . ARG   A 1 625  ? 167.577 209.433 184.883 1.00 98.12  ? 1957 ARG   A CG   1 
ATOM   3319 C  CD   . ARG   A 1 625  ? 168.300 210.370 183.932 1.00 109.91 ? 1957 ARG   A CD   1 
ATOM   3320 N  NE   . ARG   A 1 625  ? 167.571 211.618 183.753 1.00 115.29 ? 1957 ARG   A NE   1 
ATOM   3321 C  CZ   . ARG   A 1 625  ? 166.590 211.790 182.880 1.00 111.14 ? 1957 ARG   A CZ   1 
ATOM   3322 N  NH1  . ARG   A 1 625  ? 166.202 210.812 182.081 1.00 102.53 ? 1957 ARG   A NH1  1 
ATOM   3323 N  NH2  . ARG   A 1 625  ? 165.986 212.972 182.804 1.00 120.94 ? 1957 ARG   A NH2  1 
ATOM   3324 N  N    . LEU   A 1 626  ? 169.532 206.879 182.301 1.00 89.41  ? 1958 LEU   A N    1 
ATOM   3325 C  CA   . LEU   A 1 626  ? 169.856 207.025 180.886 1.00 91.35  ? 1958 LEU   A CA   1 
ATOM   3326 C  C    . LEU   A 1 626  ? 169.246 205.906 180.053 1.00 86.63  ? 1958 LEU   A C    1 
ATOM   3327 O  O    . LEU   A 1 626  ? 168.755 206.143 178.944 1.00 88.39  ? 1958 LEU   A O    1 
ATOM   3328 C  CB   . LEU   A 1 626  ? 171.371 207.092 180.709 1.00 81.32  ? 1958 LEU   A CB   1 
ATOM   3329 C  CG   . LEU   A 1 626  ? 171.891 207.403 179.311 1.00 70.88  ? 1958 LEU   A CG   1 
ATOM   3330 C  CD1  . LEU   A 1 626  ? 173.206 208.084 179.410 1.00 67.70  ? 1958 LEU   A CD1  1 
ATOM   3331 C  CD2  . LEU   A 1 626  ? 172.104 206.109 178.581 1.00 56.13  ? 1958 LEU   A CD2  1 
ATOM   3332 N  N    . LEU   A 1 627  ? 169.277 204.677 180.560 1.00 78.33  ? 1959 LEU   A N    1 
ATOM   3333 C  CA   . LEU   A 1 627  ? 168.727 203.564 179.798 1.00 78.93  ? 1959 LEU   A CA   1 
ATOM   3334 C  C    . LEU   A 1 627  ? 167.228 203.725 179.622 1.00 96.15  ? 1959 LEU   A C    1 
ATOM   3335 O  O    . LEU   A 1 627  ? 166.671 203.384 178.573 1.00 103.70 ? 1959 LEU   A O    1 
ATOM   3336 C  CB   . LEU   A 1 627  ? 169.042 202.234 180.479 1.00 68.84  ? 1959 LEU   A CB   1 
ATOM   3337 C  CG   . LEU   A 1 627  ? 170.455 201.684 180.290 1.00 61.16  ? 1959 LEU   A CG   1 
ATOM   3338 C  CD1  . LEU   A 1 627  ? 170.844 200.790 181.452 1.00 47.35  ? 1959 LEU   A CD1  1 
ATOM   3339 C  CD2  . LEU   A 1 627  ? 170.586 200.955 178.975 1.00 60.70  ? 1959 LEU   A CD2  1 
ATOM   3340 N  N    . GLN   A 1 628  ? 166.552 204.238 180.648 1.00 97.10  ? 1960 GLN   A N    1 
ATOM   3341 C  CA   . GLN   A 1 628  ? 165.098 204.325 180.589 1.00 106.40 ? 1960 GLN   A CA   1 
ATOM   3342 C  C    . GLN   A 1 628  ? 164.628 205.474 179.701 1.00 112.59 ? 1960 GLN   A C    1 
ATOM   3343 O  O    . GLN   A 1 628  ? 163.569 205.380 179.070 1.00 115.99 ? 1960 GLN   A O    1 
ATOM   3344 C  CB   . GLN   A 1 628  ? 164.529 204.459 181.999 1.00 101.32 ? 1960 GLN   A CB   1 
ATOM   3345 C  CG   . GLN   A 1 628  ? 164.741 203.214 182.845 1.00 110.96 ? 1960 GLN   A CG   1 
ATOM   3346 C  CD   . GLN   A 1 628  ? 164.193 203.356 184.249 1.00 118.42 ? 1960 GLN   A CD   1 
ATOM   3347 O  OE1  . GLN   A 1 628  ? 163.701 204.417 184.632 1.00 113.95 ? 1960 GLN   A OE1  1 
ATOM   3348 N  NE2  . GLN   A 1 628  ? 164.281 202.284 185.028 1.00 114.39 ? 1960 GLN   A NE2  1 
ATOM   3349 N  N    . GLN   A 1 629  ? 165.387 206.567 179.639 1.00 109.52 ? 1961 GLN   A N    1 
ATOM   3350 C  CA   . GLN   A 1 629  ? 164.891 207.784 179.010 1.00 114.45 ? 1961 GLN   A CA   1 
ATOM   3351 C  C    . GLN   A 1 629  ? 165.733 208.268 177.834 1.00 111.81 ? 1961 GLN   A C    1 
ATOM   3352 O  O    . GLN   A 1 629  ? 165.227 209.031 177.007 1.00 115.28 ? 1961 GLN   A O    1 
ATOM   3353 C  CB   . GLN   A 1 629  ? 164.784 208.899 180.056 1.00 115.39 ? 1961 GLN   A CB   1 
ATOM   3354 C  CG   . GLN   A 1 629  ? 163.987 210.139 179.638 1.00 123.05 ? 1961 GLN   A CG   1 
ATOM   3355 C  CD   . GLN   A 1 629  ? 162.810 209.832 178.725 1.00 128.16 ? 1961 GLN   A CD   1 
ATOM   3356 O  OE1  . GLN   A 1 629  ? 161.996 208.954 179.013 1.00 132.04 ? 1961 GLN   A OE1  1 
ATOM   3357 N  NE2  . GLN   A 1 629  ? 162.708 210.567 177.623 1.00 123.59 ? 1961 GLN   A NE2  1 
ATOM   3358 N  N    . ASP   A 1 630  ? 166.991 207.848 177.721 1.00 104.21 ? 1962 ASP   A N    1 
ATOM   3359 C  CA   . ASP   A 1 630  ? 167.862 208.433 176.704 1.00 108.32 ? 1962 ASP   A CA   1 
ATOM   3360 C  C    . ASP   A 1 630  ? 168.424 207.312 175.824 1.00 106.19 ? 1962 ASP   A C    1 
ATOM   3361 O  O    . ASP   A 1 630  ? 169.618 207.206 175.560 1.00 101.05 ? 1962 ASP   A O    1 
ATOM   3362 C  CB   . ASP   A 1 630  ? 168.978 209.269 177.333 1.00 111.41 ? 1962 ASP   A CB   1 
ATOM   3363 C  CG   . ASP   A 1 630  ? 169.813 210.005 176.300 1.00 118.20 ? 1962 ASP   A CG   1 
ATOM   3364 O  OD1  . ASP   A 1 630  ? 169.318 211.003 175.735 1.00 130.95 ? 1962 ASP   A OD1  1 
ATOM   3365 O  OD2  . ASP   A 1 630  ? 170.965 209.589 176.054 1.00 106.19 ? 1962 ASP   A OD2  1 
ATOM   3366 N  N    . LYS   A 1 631  ? 167.532 206.450 175.342 1.00 103.38 ? 1963 LYS   A N    1 
ATOM   3367 C  CA   . LYS   A 1 631  ? 167.930 205.340 174.488 1.00 92.83  ? 1963 LYS   A CA   1 
ATOM   3368 C  C    . LYS   A 1 631  ? 168.535 205.789 173.166 1.00 90.05  ? 1963 LYS   A C    1 
ATOM   3369 O  O    . LYS   A 1 631  ? 169.162 204.972 172.485 1.00 90.29  ? 1963 LYS   A O    1 
ATOM   3370 C  CB   . LYS   A 1 631  ? 166.729 204.436 174.206 1.00 94.67  ? 1963 LYS   A CB   1 
ATOM   3371 C  CG   . LYS   A 1 631  ? 166.189 203.720 175.426 1.00 98.06  ? 1963 LYS   A CG   1 
ATOM   3372 C  CD   . LYS   A 1 631  ? 164.785 203.201 175.182 1.00 93.93  ? 1963 LYS   A CD   1 
ATOM   3373 C  CE   . LYS   A 1 631  ? 164.592 201.836 175.813 1.00 87.76  ? 1963 LYS   A CE   1 
ATOM   3374 N  NZ   . LYS   A 1 631  ? 164.032 201.933 177.187 1.00 91.60  ? 1963 LYS   A NZ   1 
ATOM   3375 N  N    . ALA   A 1 632  ? 168.360 207.055 172.785 1.00 93.91  ? 1964 ALA   A N    1 
ATOM   3376 C  CA   . ALA   A 1 632  ? 168.844 207.515 171.488 1.00 93.50  ? 1964 ALA   A CA   1 
ATOM   3377 C  C    . ALA   A 1 632  ? 170.364 207.478 171.395 1.00 95.12  ? 1964 ALA   A C    1 
ATOM   3378 O  O    . ALA   A 1 632  ? 170.908 207.211 170.318 1.00 89.21  ? 1964 ALA   A O    1 
ATOM   3379 C  CB   . ALA   A 1 632  ? 168.333 208.927 171.211 1.00 100.36 ? 1964 ALA   A CB   1 
ATOM   3380 N  N    . SER   A 1 633  ? 171.063 207.736 172.496 1.00 93.37  ? 1965 SER   A N    1 
ATOM   3381 C  CA   . SER   A 1 633  ? 172.512 207.879 172.472 1.00 89.30  ? 1965 SER   A CA   1 
ATOM   3382 C  C    . SER   A 1 633  ? 173.258 206.564 172.618 1.00 81.17  ? 1965 SER   A C    1 
ATOM   3383 O  O    . SER   A 1 633  ? 174.491 206.568 172.587 1.00 74.90  ? 1965 SER   A O    1 
ATOM   3384 C  CB   . SER   A 1 633  ? 172.971 208.829 173.578 1.00 82.50  ? 1965 SER   A CB   1 
ATOM   3385 O  OG   . SER   A 1 633  ? 174.382 208.939 173.578 1.00 70.10  ? 1965 SER   A OG   1 
ATOM   3386 N  N    . LEU   A 1 634  ? 172.558 205.443 172.776 1.00 77.16  ? 1966 LEU   A N    1 
ATOM   3387 C  CA   . LEU   A 1 634  ? 173.220 204.166 173.029 1.00 67.45  ? 1966 LEU   A CA   1 
ATOM   3388 C  C    . LEU   A 1 634  ? 173.784 203.612 171.722 1.00 67.80  ? 1966 LEU   A C    1 
ATOM   3389 O  O    . LEU   A 1 634  ? 173.214 202.734 171.074 1.00 61.43  ? 1966 LEU   A O    1 
ATOM   3390 C  CB   . LEU   A 1 634  ? 172.267 203.171 173.675 1.00 70.78  ? 1966 LEU   A CB   1 
ATOM   3391 C  CG   . LEU   A 1 634  ? 171.967 203.278 175.170 1.00 69.47  ? 1966 LEU   A CG   1 
ATOM   3392 C  CD1  . LEU   A 1 634  ? 173.205 202.975 176.005 1.00 64.26  ? 1966 LEU   A CD1  1 
ATOM   3393 C  CD2  . LEU   A 1 634  ? 171.386 204.620 175.516 1.00 78.01  ? 1966 LEU   A CD2  1 
ATOM   3394 N  N    . THR   A 1 635  ? 174.934 204.146 171.334 1.00 64.14  ? 1967 THR   A N    1 
ATOM   3395 C  CA   . THR   A 1 635  ? 175.662 203.524 170.246 1.00 56.52  ? 1967 THR   A CA   1 
ATOM   3396 C  C    . THR   A 1 635  ? 176.307 202.236 170.740 1.00 48.42  ? 1967 THR   A C    1 
ATOM   3397 O  O    . THR   A 1 635  ? 176.561 202.058 171.932 1.00 44.36  ? 1967 THR   A O    1 
ATOM   3398 C  CB   . THR   A 1 635  ? 176.731 204.460 169.689 1.00 48.48  ? 1967 THR   A CB   1 
ATOM   3399 O  OG1  . THR   A 1 635  ? 177.681 204.764 170.712 1.00 42.68  ? 1967 THR   A OG1  1 
ATOM   3400 C  CG2  . THR   A 1 635  ? 176.102 205.747 169.208 1.00 56.67  ? 1967 THR   A CG2  1 
ATOM   3401 N  N    . ARG   A 1 636  ? 176.563 201.322 169.804 1.00 48.06  ? 1968 ARG   A N    1 
ATOM   3402 C  CA   . ARG   A 1 636  ? 177.182 200.056 170.172 1.00 39.69  ? 1968 ARG   A CA   1 
ATOM   3403 C  C    . ARG   A 1 636  ? 178.536 200.282 170.820 1.00 38.36  ? 1968 ARG   A C    1 
ATOM   3404 O  O    . ARG   A 1 636  ? 178.884 199.615 171.800 1.00 51.08  ? 1968 ARG   A O    1 
ATOM   3405 C  CB   . ARG   A 1 636  ? 177.320 199.164 168.943 1.00 39.29  ? 1968 ARG   A CB   1 
ATOM   3406 C  CG   . ARG   A 1 636  ? 176.093 198.322 168.631 1.00 52.51  ? 1968 ARG   A CG   1 
ATOM   3407 C  CD   . ARG   A 1 636  ? 176.144 196.978 169.341 1.00 59.64  ? 1968 ARG   A CD   1 
ATOM   3408 N  NE   . ARG   A 1 636  ? 174.889 196.247 169.229 1.00 70.09  ? 1968 ARG   A NE   1 
ATOM   3409 C  CZ   . ARG   A 1 636  ? 173.884 196.350 170.086 1.00 66.11  ? 1968 ARG   A CZ   1 
ATOM   3410 N  NH1  . ARG   A 1 636  ? 173.956 197.138 171.143 1.00 57.64  ? 1968 ARG   A NH1  1 
ATOM   3411 N  NH2  . ARG   A 1 636  ? 172.780 195.641 169.877 1.00 72.29  ? 1968 ARG   A NH2  1 
ATOM   3412 N  N    . THR   A 1 637  ? 179.312 201.227 170.297 1.00 34.63  ? 1969 THR   A N    1 
ATOM   3413 C  CA   . THR   A 1 637  ? 180.607 201.506 170.901 1.00 31.54  ? 1969 THR   A CA   1 
ATOM   3414 C  C    . THR   A 1 637  ? 180.448 202.074 172.304 1.00 37.01  ? 1969 THR   A C    1 
ATOM   3415 O  O    . THR   A 1 637  ? 181.229 201.745 173.200 1.00 38.04  ? 1969 THR   A O    1 
ATOM   3416 C  CB   . THR   A 1 637  ? 181.422 202.442 170.011 1.00 30.59  ? 1969 THR   A CB   1 
ATOM   3417 O  OG1  . THR   A 1 637  ? 182.745 202.570 170.542 1.00 35.84  ? 1969 THR   A OG1  1 
ATOM   3418 C  CG2  . THR   A 1 637  ? 180.778 203.806 169.903 1.00 37.27  ? 1969 THR   A CG2  1 
ATOM   3419 N  N    . LEU   A 1 638  ? 179.420 202.892 172.533 1.00 40.50  ? 1970 LEU   A N    1 
ATOM   3420 C  CA   . LEU   A 1 638  ? 179.210 203.423 173.875 1.00 34.99  ? 1970 LEU   A CA   1 
ATOM   3421 C  C    . LEU   A 1 638  ? 178.782 202.327 174.844 1.00 34.10  ? 1970 LEU   A C    1 
ATOM   3422 O  O    . LEU   A 1 638  ? 179.223 202.309 175.998 1.00 31.58  ? 1970 LEU   A O    1 
ATOM   3423 C  CB   . LEU   A 1 638  ? 178.180 204.545 173.846 1.00 35.58  ? 1970 LEU   A CB   1 
ATOM   3424 C  CG   . LEU   A 1 638  ? 177.570 204.891 175.194 1.00 40.21  ? 1970 LEU   A CG   1 
ATOM   3425 C  CD1  . LEU   A 1 638  ? 178.590 205.620 176.025 1.00 36.44  ? 1970 LEU   A CD1  1 
ATOM   3426 C  CD2  . LEU   A 1 638  ? 176.344 205.740 175.007 1.00 49.62  ? 1970 LEU   A CD2  1 
ATOM   3427 N  N    . GLN   A 1 639  ? 177.917 201.413 174.402 1.00 33.50  ? 1971 GLN   A N    1 
ATOM   3428 C  CA   . GLN   A 1 639  ? 177.522 200.293 175.249 1.00 25.10  ? 1971 GLN   A CA   1 
ATOM   3429 C  C    . GLN   A 1 639  ? 178.728 199.456 175.627 1.00 21.72  ? 1971 GLN   A C    1 
ATOM   3430 O  O    . GLN   A 1 639  ? 178.910 199.081 176.794 1.00 29.39  ? 1971 GLN   A O    1 
ATOM   3431 C  CB   . GLN   A 1 639  ? 176.501 199.429 174.522 1.00 23.74  ? 1971 GLN   A CB   1 
ATOM   3432 C  CG   . GLN   A 1 639  ? 175.180 200.090 174.283 1.00 34.86  ? 1971 GLN   A CG   1 
ATOM   3433 C  CD   . GLN   A 1 639  ? 174.202 199.161 173.617 1.00 47.57  ? 1971 GLN   A CD   1 
ATOM   3434 O  OE1  . GLN   A 1 639  ? 174.148 197.980 173.931 1.00 53.63  ? 1971 GLN   A OE1  1 
ATOM   3435 N  NE2  . GLN   A 1 639  ? 173.421 199.690 172.691 1.00 52.72  ? 1971 GLN   A NE2  1 
ATOM   3436 N  N    . HIS   A 1 640  ? 179.571 199.152 174.648 1.00 21.34  ? 1972 HIS   A N    1 
ATOM   3437 C  CA   . HIS   A 1 640  ? 180.752 198.365 174.950 1.00 22.40  ? 1972 HIS   A CA   1 
ATOM   3438 C  C    . HIS   A 1 640  ? 181.671 199.121 175.892 1.00 29.07  ? 1972 HIS   A C    1 
ATOM   3439 O  O    . HIS   A 1 640  ? 182.300 198.516 176.759 1.00 30.72  ? 1972 HIS   A O    1 
ATOM   3440 C  CB   . HIS   A 1 640  ? 181.484 197.983 173.672 1.00 18.40  ? 1972 HIS   A CB   1 
ATOM   3441 C  CG   . HIS   A 1 640  ? 182.821 197.365 173.910 1.00 17.78  ? 1972 HIS   A CG   1 
ATOM   3442 N  ND1  . HIS   A 1 640  ? 183.996 198.071 173.800 1.00 23.28  ? 1972 HIS   A ND1  1 
ATOM   3443 C  CD2  . HIS   A 1 640  ? 183.168 196.109 174.264 1.00 20.28  ? 1972 HIS   A CD2  1 
ATOM   3444 C  CE1  . HIS   A 1 640  ? 185.012 197.271 174.063 1.00 27.88  ? 1972 HIS   A CE1  1 
ATOM   3445 N  NE2  . HIS   A 1 640  ? 184.536 196.076 174.352 1.00 25.74  ? 1972 HIS   A NE2  1 
ATOM   3446 N  N    . ARG   A 1 641  ? 181.756 200.445 175.752 1.00 28.77  ? 1973 ARG   A N    1 
ATOM   3447 C  CA   . ARG   A 1 641  ? 182.591 201.219 176.664 1.00 22.10  ? 1973 ARG   A CA   1 
ATOM   3448 C  C    . ARG   A 1 641  ? 182.058 201.193 178.089 1.00 23.35  ? 1973 ARG   A C    1 
ATOM   3449 O  O    . ARG   A 1 641  ? 182.834 201.067 179.040 1.00 27.11  ? 1973 ARG   A O    1 
ATOM   3450 C  CB   . ARG   A 1 641  ? 182.716 202.653 176.176 1.00 21.46  ? 1973 ARG   A CB   1 
ATOM   3451 C  CG   . ARG   A 1 641  ? 183.491 202.794 174.904 1.00 30.69  ? 1973 ARG   A CG   1 
ATOM   3452 C  CD   . ARG   A 1 641  ? 184.800 202.048 174.982 1.00 37.81  ? 1973 ARG   A CD   1 
ATOM   3453 N  NE   . ARG   A 1 641  ? 185.216 201.586 173.667 1.00 49.39  ? 1973 ARG   A NE   1 
ATOM   3454 C  CZ   . ARG   A 1 641  ? 185.811 202.349 172.764 1.00 64.32  ? 1973 ARG   A CZ   1 
ATOM   3455 N  NH1  . ARG   A 1 641  ? 186.070 203.623 173.000 1.00 79.17  ? 1973 ARG   A NH1  1 
ATOM   3456 N  NH2  . ARG   A 1 641  ? 186.144 201.823 171.590 1.00 50.15  ? 1973 ARG   A NH2  1 
ATOM   3457 N  N    . ILE   A 1 642  ? 180.747 201.327 178.266 1.00 21.21  ? 1974 ILE   A N    1 
ATOM   3458 C  CA   . ILE   A 1 642  ? 180.192 201.278 179.615 1.00 16.01  ? 1974 ILE   A CA   1 
ATOM   3459 C  C    . ILE   A 1 642  ? 180.491 199.930 180.252 1.00 18.59  ? 1974 ILE   A C    1 
ATOM   3460 O  O    . ILE   A 1 642  ? 180.964 199.851 181.394 1.00 22.04  ? 1974 ILE   A O    1 
ATOM   3461 C  CB   . ILE   A 1 642  ? 178.683 201.556 179.593 1.00 13.85  ? 1974 ILE   A CB   1 
ATOM   3462 C  CG1  . ILE   A 1 642  ? 178.396 202.957 179.088 1.00 16.09  ? 1974 ILE   A CG1  1 
ATOM   3463 C  CG2  . ILE   A 1 642  ? 178.109 201.390 180.965 1.00 15.14  ? 1974 ILE   A CG2  1 
ATOM   3464 C  CD1  . ILE   A 1 642  ? 176.942 203.186 178.807 1.00 19.80  ? 1974 ILE   A CD1  1 
ATOM   3465 N  N    . ALA   A 1 643  ? 180.231 198.847 179.516 1.00 20.82  ? 1975 ALA   A N    1 
ATOM   3466 C  CA   . ALA   A 1 643  ? 180.483 197.517 180.060 1.00 21.66  ? 1975 ALA   A CA   1 
ATOM   3467 C  C    . ALA   A 1 643  ? 181.961 197.320 180.353 1.00 23.62  ? 1975 ALA   A C    1 
ATOM   3468 O  O    . ALA   A 1 643  ? 182.330 196.748 181.383 1.00 29.89  ? 1975 ALA   A O    1 
ATOM   3469 C  CB   . ALA   A 1 643  ? 179.982 196.452 179.093 1.00 17.80  ? 1975 ALA   A CB   1 
ATOM   3470 N  N    . LEU   A 1 644  ? 182.818 197.809 179.465 1.00 20.17  ? 1976 LEU   A N    1 
ATOM   3471 C  CA   . LEU   A 1 644  ? 184.253 197.678 179.647 1.00 22.36  ? 1976 LEU   A CA   1 
ATOM   3472 C  C    . LEU   A 1 644  ? 184.708 198.394 180.909 1.00 34.96  ? 1976 LEU   A C    1 
ATOM   3473 O  O    . LEU   A 1 644  ? 185.528 197.870 181.671 1.00 45.62  ? 1976 LEU   A O    1 
ATOM   3474 C  CB   . LEU   A 1 644  ? 184.957 198.257 178.428 1.00 17.74  ? 1976 LEU   A CB   1 
ATOM   3475 C  CG   . LEU   A 1 644  ? 186.458 198.363 178.548 1.00 16.48  ? 1976 LEU   A CG   1 
ATOM   3476 C  CD1  . LEU   A 1 644  ? 186.919 196.965 178.667 1.00 21.45  ? 1976 LEU   A CD1  1 
ATOM   3477 C  CD2  . LEU   A 1 644  ? 187.069 199.038 177.350 1.00 28.69  ? 1976 LEU   A CD2  1 
ATOM   3478 N  N    . HIS   A 1 645  ? 184.182 199.599 181.147 1.00 33.01  ? 1977 HIS   A N    1 
ATOM   3479 C  CA   . HIS   A 1 645  ? 184.606 200.393 182.295 1.00 26.51  ? 1977 HIS   A CA   1 
ATOM   3480 C  C    . HIS   A 1 645  ? 184.128 199.779 183.603 1.00 24.03  ? 1977 HIS   A C    1 
ATOM   3481 O  O    . HIS   A 1 645  ? 184.879 199.730 184.586 1.00 27.18  ? 1977 HIS   A O    1 
ATOM   3482 C  CB   . HIS   A 1 645  ? 184.092 201.820 182.146 1.00 25.40  ? 1977 HIS   A CB   1 
ATOM   3483 C  CG   . HIS   A 1 645  ? 184.874 202.637 181.170 1.00 32.94  ? 1977 HIS   A CG   1 
ATOM   3484 N  ND1  . HIS   A 1 645  ? 186.241 202.780 181.245 1.00 38.84  ? 1977 HIS   A ND1  1 
ATOM   3485 C  CD2  . HIS   A 1 645  ? 184.482 203.342 180.084 1.00 36.27  ? 1977 HIS   A CD2  1 
ATOM   3486 C  CE1  . HIS   A 1 645  ? 186.656 203.545 180.253 1.00 42.81  ? 1977 HIS   A CE1  1 
ATOM   3487 N  NE2  . HIS   A 1 645  ? 185.608 203.899 179.533 1.00 38.67  ? 1977 HIS   A NE2  1 
ATOM   3488 N  N    . VAL   A 1 646  ? 182.882 199.304 183.637 1.00 22.67  ? 1978 VAL   A N    1 
ATOM   3489 C  CA   . VAL   A 1 646  ? 182.398 198.640 184.842 1.00 24.17  ? 1978 VAL   A CA   1 
ATOM   3490 C  C    . VAL   A 1 646  ? 183.206 197.382 185.127 1.00 27.21  ? 1978 VAL   A C    1 
ATOM   3491 O  O    . VAL   A 1 646  ? 183.563 197.108 186.277 1.00 30.27  ? 1978 VAL   A O    1 
ATOM   3492 C  CB   . VAL   A 1 646  ? 180.899 198.334 184.728 1.00 23.05  ? 1978 VAL   A CB   1 
ATOM   3493 C  CG1  . VAL   A 1 646  ? 180.455 197.550 185.922 1.00 21.74  ? 1978 VAL   A CG1  1 
ATOM   3494 C  CG2  . VAL   A 1 646  ? 180.124 199.620 184.655 1.00 21.80  ? 1978 VAL   A CG2  1 
ATOM   3495 N  N    . ALA   A 1 647  ? 183.506 196.593 184.092 1.00 23.97  ? 1979 ALA   A N    1 
ATOM   3496 C  CA   . ALA   A 1 647  ? 184.318 195.398 184.297 1.00 22.42  ? 1979 ALA   A CA   1 
ATOM   3497 C  C    . ALA   A 1 647  ? 185.710 195.752 184.796 1.00 29.64  ? 1979 ALA   A C    1 
ATOM   3498 O  O    . ALA   A 1 647  ? 186.261 195.054 185.646 1.00 41.68  ? 1979 ALA   A O    1 
ATOM   3499 C  CB   . ALA   A 1 647  ? 184.411 194.588 183.010 1.00 26.43  ? 1979 ALA   A CB   1 
ATOM   3500 N  N    . ASP   A 1 648  ? 186.299 196.827 184.274 1.00 30.42  ? 1980 ASP   A N    1 
ATOM   3501 C  CA   . ASP   A 1 648  ? 187.608 197.261 184.752 1.00 31.96  ? 1980 ASP   A CA   1 
ATOM   3502 C  C    . ASP   A 1 648  ? 187.561 197.601 186.236 1.00 38.98  ? 1980 ASP   A C    1 
ATOM   3503 O  O    . ASP   A 1 648  ? 188.386 197.125 187.032 1.00 45.49  ? 1980 ASP   A O    1 
ATOM   3504 C  CB   . ASP   A 1 648  ? 188.068 198.470 183.940 1.00 37.11  ? 1980 ASP   A CB   1 
ATOM   3505 C  CG   . ASP   A 1 648  ? 189.500 198.861 184.226 1.00 48.57  ? 1980 ASP   A CG   1 
ATOM   3506 O  OD1  . ASP   A 1 648  ? 190.146 198.217 185.076 1.00 52.78  ? 1980 ASP   A OD1  1 
ATOM   3507 O  OD2  . ASP   A 1 648  ? 189.980 199.831 183.605 1.00 49.04  ? 1980 ASP   A OD2  1 
ATOM   3508 N  N    . GLY   A 1 649  ? 186.588 198.417 186.630 1.00 41.72  ? 1981 GLY   A N    1 
ATOM   3509 C  CA   . GLY   A 1 649  ? 186.498 198.810 188.024 1.00 36.21  ? 1981 GLY   A CA   1 
ATOM   3510 C  C    . GLY   A 1 649  ? 186.259 197.632 188.944 1.00 39.57  ? 1981 GLY   A C    1 
ATOM   3511 O  O    . GLY   A 1 649  ? 186.888 197.516 189.997 1.00 48.55  ? 1981 GLY   A O    1 
ATOM   3512 N  N    . LEU   A 1 650  ? 185.361 196.731 188.552 1.00 36.59  ? 1982 LEU   A N    1 
ATOM   3513 C  CA   . LEU   A 1 650  ? 185.035 195.604 189.415 1.00 34.12  ? 1982 LEU   A CA   1 
ATOM   3514 C  C    . LEU   A 1 650  ? 186.174 194.591 189.461 1.00 34.41  ? 1982 LEU   A C    1 
ATOM   3515 O  O    . LEU   A 1 650  ? 186.392 193.941 190.491 1.00 43.22  ? 1982 LEU   A O    1 
ATOM   3516 C  CB   . LEU   A 1 650  ? 183.728 194.978 188.951 1.00 24.73  ? 1982 LEU   A CB   1 
ATOM   3517 C  CG   . LEU   A 1 650  ? 183.298 193.675 189.576 1.00 30.14  ? 1982 LEU   A CG   1 
ATOM   3518 C  CD1  . LEU   A 1 650  ? 181.819 193.695 189.748 1.00 37.15  ? 1982 LEU   A CD1  1 
ATOM   3519 C  CD2  . LEU   A 1 650  ? 183.652 192.600 188.625 1.00 34.52  ? 1982 LEU   A CD2  1 
ATOM   3520 N  N    . ARG   A 1 651  ? 186.944 194.471 188.379 1.00 35.74  ? 1983 ARG   A N    1 
ATOM   3521 C  CA   . ARG   A 1 651  ? 188.175 193.701 188.463 1.00 38.25  ? 1983 ARG   A CA   1 
ATOM   3522 C  C    . ARG   A 1 651  ? 189.115 194.292 189.497 1.00 44.41  ? 1983 ARG   A C    1 
ATOM   3523 O  O    . ARG   A 1 651  ? 189.700 193.550 190.291 1.00 56.48  ? 1983 ARG   A O    1 
ATOM   3524 C  CB   . ARG   A 1 651  ? 188.898 193.662 187.121 1.00 46.22  ? 1983 ARG   A CB   1 
ATOM   3525 C  CG   . ARG   A 1 651  ? 190.380 193.448 187.329 1.00 44.46  ? 1983 ARG   A CG   1 
ATOM   3526 C  CD   . ARG   A 1 651  ? 191.222 193.430 186.088 1.00 46.76  ? 1983 ARG   A CD   1 
ATOM   3527 N  NE   . ARG   A 1 651  ? 191.514 194.783 185.642 1.00 45.71  ? 1983 ARG   A NE   1 
ATOM   3528 C  CZ   . ARG   A 1 651  ? 192.248 195.071 184.580 1.00 55.34  ? 1983 ARG   A CZ   1 
ATOM   3529 N  NH1  . ARG   A 1 651  ? 192.877 194.128 183.902 1.00 53.19  ? 1983 ARG   A NH1  1 
ATOM   3530 N  NH2  . ARG   A 1 651  ? 192.390 196.341 184.216 1.00 59.21  ? 1983 ARG   A NH2  1 
ATOM   3531 N  N    . TYR   A 1 652  ? 189.281 195.617 189.501 1.00 40.69  ? 1984 TYR   A N    1 
ATOM   3532 C  CA   . TYR   A 1 652  ? 190.162 196.222 190.498 1.00 43.18  ? 1984 TYR   A CA   1 
ATOM   3533 C  C    . TYR   A 1 652  ? 189.648 195.968 191.908 1.00 42.93  ? 1984 TYR   A C    1 
ATOM   3534 O  O    . TYR   A 1 652  ? 190.432 195.662 192.814 1.00 48.07  ? 1984 TYR   A O    1 
ATOM   3535 C  CB   . TYR   A 1 652  ? 190.318 197.718 190.225 1.00 50.86  ? 1984 TYR   A CB   1 
ATOM   3536 C  CG   . TYR   A 1 652  ? 191.223 198.482 191.179 1.00 57.14  ? 1984 TYR   A CG   1 
ATOM   3537 C  CD1  . TYR   A 1 652  ? 190.857 198.718 192.497 1.00 49.56  ? 1984 TYR   A CD1  1 
ATOM   3538 C  CD2  . TYR   A 1 652  ? 192.452 198.959 190.754 1.00 55.17  ? 1984 TYR   A CD2  1 
ATOM   3539 C  CE1  . TYR   A 1 652  ? 191.679 199.411 193.350 1.00 52.93  ? 1984 TYR   A CE1  1 
ATOM   3540 C  CE2  . TYR   A 1 652  ? 193.279 199.652 191.602 1.00 54.07  ? 1984 TYR   A CE2  1 
ATOM   3541 C  CZ   . TYR   A 1 652  ? 192.891 199.874 192.898 1.00 63.70  ? 1984 TYR   A CZ   1 
ATOM   3542 O  OH   . TYR   A 1 652  ? 193.722 200.566 193.747 1.00 75.26  ? 1984 TYR   A OH   1 
ATOM   3543 N  N    . LEU   A 1 653  ? 188.337 196.090 192.109 1.00 37.31  ? 1985 LEU   A N    1 
ATOM   3544 C  CA   . LEU   A 1 653  ? 187.767 195.811 193.423 1.00 36.34  ? 1985 LEU   A CA   1 
ATOM   3545 C  C    . LEU   A 1 653  ? 188.113 194.404 193.877 1.00 45.31  ? 1985 LEU   A C    1 
ATOM   3546 O  O    . LEU   A 1 653  ? 188.568 194.199 195.006 1.00 48.03  ? 1985 LEU   A O    1 
ATOM   3547 C  CB   . LEU   A 1 653  ? 186.255 195.985 193.388 1.00 25.89  ? 1985 LEU   A CB   1 
ATOM   3548 C  CG   . LEU   A 1 653  ? 185.810 197.422 193.545 1.00 28.68  ? 1985 LEU   A CG   1 
ATOM   3549 C  CD1  . LEU   A 1 653  ? 184.324 197.477 193.557 1.00 28.51  ? 1985 LEU   A CD1  1 
ATOM   3550 C  CD2  . LEU   A 1 653  ? 186.363 197.972 194.824 1.00 45.85  ? 1985 LEU   A CD2  1 
ATOM   3551 N  N    . HIS   A 1 654  ? 187.923 193.424 192.999 1.00 50.84  ? 1986 HIS   A N    1 
ATOM   3552 C  CA   . HIS   A 1 654  ? 188.218 192.045 193.361 1.00 51.11  ? 1986 HIS   A CA   1 
ATOM   3553 C  C    . HIS   A 1 654  ? 189.707 191.850 193.593 1.00 52.95  ? 1986 HIS   A C    1 
ATOM   3554 O  O    . HIS   A 1 654  ? 190.112 190.996 194.388 1.00 57.19  ? 1986 HIS   A O    1 
ATOM   3555 C  CB   . HIS   A 1 654  ? 187.707 191.129 192.266 1.00 52.69  ? 1986 HIS   A CB   1 
ATOM   3556 C  CG   . HIS   A 1 654  ? 186.230 190.945 192.307 1.00 56.24  ? 1986 HIS   A CG   1 
ATOM   3557 N  ND1  . HIS   A 1 654  ? 185.584 189.932 191.637 1.00 64.70  ? 1986 HIS   A ND1  1 
ATOM   3558 C  CD2  . HIS   A 1 654  ? 185.269 191.651 192.945 1.00 51.02  ? 1986 HIS   A CD2  1 
ATOM   3559 C  CE1  . HIS   A 1 654  ? 184.286 190.025 191.858 1.00 59.41  ? 1986 HIS   A CE1  1 
ATOM   3560 N  NE2  . HIS   A 1 654  ? 184.069 191.058 192.650 1.00 51.52  ? 1986 HIS   A NE2  1 
ATOM   3561 N  N    . SER   A 1 655  ? 190.537 192.621 192.892 1.00 52.98  ? 1987 SER   A N    1 
ATOM   3562 C  CA   . SER   A 1 655  ? 191.973 192.581 193.135 1.00 57.16  ? 1987 SER   A CA   1 
ATOM   3563 C  C    . SER   A 1 655  ? 192.317 193.084 194.529 1.00 63.03  ? 1987 SER   A C    1 
ATOM   3564 O  O    . SER   A 1 655  ? 193.206 192.533 195.186 1.00 62.54  ? 1987 SER   A O    1 
ATOM   3565 C  CB   . SER   A 1 655  ? 192.705 193.406 192.080 1.00 59.47  ? 1987 SER   A CB   1 
ATOM   3566 O  OG   . SER   A 1 655  ? 194.100 193.410 192.317 1.00 62.75  ? 1987 SER   A OG   1 
ATOM   3567 N  N    . ALA   A 1 656  ? 191.630 194.122 194.995 1.00 61.45  ? 1988 ALA   A N    1 
ATOM   3568 C  CA   . ALA   A 1 656  ? 191.857 194.656 196.332 1.00 57.90  ? 1988 ALA   A CA   1 
ATOM   3569 C  C    . ALA   A 1 656  ? 191.171 193.842 197.423 1.00 56.05  ? 1988 ALA   A C    1 
ATOM   3570 O  O    . ALA   A 1 656  ? 191.070 194.320 198.557 1.00 58.17  ? 1988 ALA   A O    1 
ATOM   3571 C  CB   . ALA   A 1 656  ? 191.394 196.113 196.406 1.00 54.62  ? 1988 ALA   A CB   1 
ATOM   3572 N  N    . MET   A 1 657  ? 190.696 192.639 197.101 1.00 57.11  ? 1989 MET   A N    1 
ATOM   3573 C  CA   . MET   A 1 657  ? 190.033 191.752 198.056 1.00 67.99  ? 1989 MET   A CA   1 
ATOM   3574 C  C    . MET   A 1 657  ? 188.779 192.384 198.651 1.00 70.39  ? 1989 MET   A C    1 
ATOM   3575 O  O    . MET   A 1 657  ? 188.390 192.071 199.776 1.00 70.22  ? 1989 MET   A O    1 
ATOM   3576 C  CB   . MET   A 1 657  ? 190.988 191.315 199.170 1.00 74.74  ? 1989 MET   A CB   1 
ATOM   3577 N  N    . ILE   A 1 658  ? 188.122 193.257 197.896 1.00 62.61  ? 1990 ILE   A N    1 
ATOM   3578 C  CA   . ILE   A 1 658  ? 186.861 193.864 198.302 1.00 60.43  ? 1990 ILE   A CA   1 
ATOM   3579 C  C    . ILE   A 1 658  ? 185.751 193.258 197.468 1.00 59.73  ? 1990 ILE   A C    1 
ATOM   3580 O  O    . ILE   A 1 658  ? 185.841 193.218 196.237 1.00 67.18  ? 1990 ILE   A O    1 
ATOM   3581 C  CB   . ILE   A 1 658  ? 186.879 195.391 198.142 1.00 51.24  ? 1990 ILE   A CB   1 
ATOM   3582 C  CG1  . ILE   A 1 658  ? 188.202 195.956 198.639 1.00 56.56  ? 1990 ILE   A CG1  1 
ATOM   3583 C  CG2  . ILE   A 1 658  ? 185.679 196.018 198.831 1.00 51.15  ? 1990 ILE   A CG2  1 
ATOM   3584 C  CD1  . ILE   A 1 658  ? 188.426 197.367 198.231 1.00 55.12  ? 1990 ILE   A CD1  1 
ATOM   3585 N  N    . ILE   A 1 659  ? 184.713 192.782 198.131 1.00 55.62  ? 1991 ILE   A N    1 
ATOM   3586 C  CA   . ILE   A 1 659  ? 183.551 192.259 197.438 1.00 62.50  ? 1991 ILE   A CA   1 
ATOM   3587 C  C    . ILE   A 1 659  ? 182.574 193.407 197.275 1.00 61.44  ? 1991 ILE   A C    1 
ATOM   3588 O  O    . ILE   A 1 659  ? 182.106 193.980 198.263 1.00 59.72  ? 1991 ILE   A O    1 
ATOM   3589 C  CB   . ILE   A 1 659  ? 182.915 191.098 198.208 1.00 74.59  ? 1991 ILE   A CB   1 
ATOM   3590 C  CG1  . ILE   A 1 659  ? 183.916 189.957 198.343 1.00 79.98  ? 1991 ILE   A CG1  1 
ATOM   3591 C  CG2  . ILE   A 1 659  ? 181.681 190.617 197.482 1.00 75.00  ? 1991 ILE   A CG2  1 
ATOM   3592 C  CD1  . ILE   A 1 659  ? 184.646 189.636 197.077 1.00 76.90  ? 1991 ILE   A CD1  1 
ATOM   3593 N  N    . TYR   A 1 660  ? 182.271 193.753 196.034 1.00 60.63  ? 1992 TYR   A N    1 
ATOM   3594 C  CA   . TYR   A 1 660  ? 181.372 194.859 195.750 1.00 60.94  ? 1992 TYR   A CA   1 
ATOM   3595 C  C    . TYR   A 1 660  ? 179.956 194.305 195.802 1.00 65.01  ? 1992 TYR   A C    1 
ATOM   3596 O  O    . TYR   A 1 660  ? 179.537 193.576 194.902 1.00 69.07  ? 1992 TYR   A O    1 
ATOM   3597 C  CB   . TYR   A 1 660  ? 181.706 195.477 194.397 1.00 47.56  ? 1992 TYR   A CB   1 
ATOM   3598 C  CG   . TYR   A 1 660  ? 180.756 196.544 193.954 1.00 43.57  ? 1992 TYR   A CG   1 
ATOM   3599 C  CD1  . TYR   A 1 660  ? 179.644 196.241 193.205 1.00 49.71  ? 1992 TYR   A CD1  1 
ATOM   3600 C  CD2  . TYR   A 1 660  ? 180.968 197.864 194.304 1.00 47.11  ? 1992 TYR   A CD2  1 
ATOM   3601 C  CE1  . TYR   A 1 660  ? 178.781 197.217 192.806 1.00 55.75  ? 1992 TYR   A CE1  1 
ATOM   3602 C  CE2  . TYR   A 1 660  ? 180.104 198.848 193.910 1.00 54.72  ? 1992 TYR   A CE2  1 
ATOM   3603 C  CZ   . TYR   A 1 660  ? 179.005 198.517 193.162 1.00 52.95  ? 1992 TYR   A CZ   1 
ATOM   3604 O  OH   . TYR   A 1 660  ? 178.124 199.486 192.752 1.00 47.92  ? 1992 TYR   A OH   1 
ATOM   3605 N  N    . ARG   A 1 661  ? 179.220 194.649 196.859 1.00 69.33  ? 1993 ARG   A N    1 
ATOM   3606 C  CA   . ARG   A 1 661  ? 178.016 193.899 197.202 1.00 72.00  ? 1993 ARG   A CA   1 
ATOM   3607 C  C    . ARG   A 1 661  ? 176.996 193.920 196.072 1.00 68.05  ? 1993 ARG   A C    1 
ATOM   3608 O  O    . ARG   A 1 661  ? 176.516 192.867 195.640 1.00 65.06  ? 1993 ARG   A O    1 
ATOM   3609 C  CB   . ARG   A 1 661  ? 177.388 194.468 198.476 1.00 88.19  ? 1993 ARG   A CB   1 
ATOM   3610 C  CG   . ARG   A 1 661  ? 178.300 194.533 199.690 1.00 95.00  ? 1993 ARG   A CG   1 
ATOM   3611 C  CD   . ARG   A 1 661  ? 177.917 193.519 200.752 1.00 93.34  ? 1993 ARG   A CD   1 
ATOM   3612 N  NE   . ARG   A 1 661  ? 178.438 192.195 200.445 1.00 104.58 ? 1993 ARG   A NE   1 
ATOM   3613 C  CZ   . ARG   A 1 661  ? 179.686 191.815 200.684 1.00 105.56 ? 1993 ARG   A CZ   1 
ATOM   3614 N  NH1  . ARG   A 1 661  ? 180.573 192.645 201.206 1.00 101.51 ? 1993 ARG   A NH1  1 
ATOM   3615 N  NH2  . ARG   A 1 661  ? 180.053 190.572 200.394 1.00 111.20 ? 1993 ARG   A NH2  1 
ATOM   3616 N  N    . ASP   A 1 662  ? 176.666 195.104 195.567 1.00 65.69  ? 1994 ASP   A N    1 
ATOM   3617 C  CA   . ASP   A 1 662  ? 175.448 195.298 194.791 1.00 72.96  ? 1994 ASP   A CA   1 
ATOM   3618 C  C    . ASP   A 1 662  ? 175.739 196.121 193.547 1.00 62.56  ? 1994 ASP   A C    1 
ATOM   3619 O  O    . ASP   A 1 662  ? 175.959 197.333 193.641 1.00 58.17  ? 1994 ASP   A O    1 
ATOM   3620 C  CB   . ASP   A 1 662  ? 174.385 195.969 195.663 1.00 89.48  ? 1994 ASP   A CB   1 
ATOM   3621 C  CG   . ASP   A 1 662  ? 173.054 196.084 194.976 1.00 91.30  ? 1994 ASP   A CG   1 
ATOM   3622 O  OD1  . ASP   A 1 662  ? 172.357 195.059 194.830 1.00 91.64  ? 1994 ASP   A OD1  1 
ATOM   3623 O  OD2  . ASP   A 1 662  ? 172.686 197.217 194.619 1.00 81.70  ? 1994 ASP   A OD2  1 
ATOM   3624 N  N    . LEU   A 1 663  ? 175.703 195.468 192.383 1.00 54.33  ? 1995 LEU   A N    1 
ATOM   3625 C  CA   . LEU   A 1 663  ? 176.054 196.080 191.104 1.00 48.49  ? 1995 LEU   A CA   1 
ATOM   3626 C  C    . LEU   A 1 663  ? 174.819 196.104 190.216 1.00 43.66  ? 1995 LEU   A C    1 
ATOM   3627 O  O    . LEU   A 1 663  ? 174.346 195.052 189.779 1.00 50.77  ? 1995 LEU   A O    1 
ATOM   3628 C  CB   . LEU   A 1 663  ? 177.188 195.311 190.430 1.00 38.86  ? 1995 LEU   A CB   1 
ATOM   3629 C  CG   . LEU   A 1 663  ? 177.738 195.843 189.114 1.00 28.73  ? 1995 LEU   A CG   1 
ATOM   3630 C  CD1  . LEU   A 1 663  ? 178.348 197.204 189.317 1.00 31.35  ? 1995 LEU   A CD1  1 
ATOM   3631 C  CD2  . LEU   A 1 663  ? 178.763 194.894 188.571 1.00 23.01  ? 1995 LEU   A CD2  1 
ATOM   3632 N  N    . LYS   A 1 664  ? 174.304 197.292 189.937 1.00 41.99  ? 1996 LYS   A N    1 
ATOM   3633 C  CA   . LYS   A 1 664  ? 173.109 197.489 189.141 1.00 49.91  ? 1996 LYS   A CA   1 
ATOM   3634 C  C    . LYS   A 1 664  ? 173.332 198.626 188.158 1.00 51.05  ? 1996 LYS   A C    1 
ATOM   3635 O  O    . LYS   A 1 664  ? 174.346 199.322 188.224 1.00 56.49  ? 1996 LYS   A O    1 
ATOM   3636 C  CB   . LYS   A 1 664  ? 171.898 197.805 190.035 1.00 53.89  ? 1996 LYS   A CB   1 
ATOM   3637 C  CG   . LYS   A 1 664  ? 171.858 197.087 191.350 1.00 58.26  ? 1996 LYS   A CG   1 
ATOM   3638 C  CD   . LYS   A 1 664  ? 170.885 197.775 192.273 1.00 69.49  ? 1996 LYS   A CD   1 
ATOM   3639 C  CE   . LYS   A 1 664  ? 171.278 199.208 192.519 1.00 68.08  ? 1996 LYS   A CE   1 
ATOM   3640 N  NZ   . LYS   A 1 664  ? 170.518 199.787 193.652 1.00 67.09  ? 1996 LYS   A NZ   1 
ATOM   3641 N  N    . PRO   A 1 665  ? 172.410 198.831 187.216 1.00 48.78  ? 1997 PRO   A N    1 
ATOM   3642 C  CA   . PRO   A 1 665  ? 172.443 200.081 186.452 1.00 50.61  ? 1997 PRO   A CA   1 
ATOM   3643 C  C    . PRO   A 1 665  ? 172.188 201.315 187.298 1.00 58.38  ? 1997 PRO   A C    1 
ATOM   3644 O  O    . PRO   A 1 665  ? 172.575 202.413 186.887 1.00 62.33  ? 1997 PRO   A O    1 
ATOM   3645 C  CB   . PRO   A 1 665  ? 171.355 199.872 185.393 1.00 44.82  ? 1997 PRO   A CB   1 
ATOM   3646 C  CG   . PRO   A 1 665  ? 170.434 198.922 185.984 1.00 51.31  ? 1997 PRO   A CG   1 
ATOM   3647 C  CD   . PRO   A 1 665  ? 171.271 197.995 186.812 1.00 57.11  ? 1997 PRO   A CD   1 
ATOM   3648 N  N    . HIS   A 1 666  ? 171.556 201.184 188.465 1.00 56.68  ? 1998 HIS   A N    1 
ATOM   3649 C  CA   . HIS   A 1 666  ? 171.387 202.348 189.328 1.00 58.75  ? 1998 HIS   A CA   1 
ATOM   3650 C  C    . HIS   A 1 666  ? 172.731 202.868 189.822 1.00 49.85  ? 1998 HIS   A C    1 
ATOM   3651 O  O    . HIS   A 1 666  ? 172.932 204.080 189.937 1.00 47.49  ? 1998 HIS   A O    1 
ATOM   3652 C  CB   . HIS   A 1 666  ? 170.489 202.010 190.516 1.00 62.21  ? 1998 HIS   A CB   1 
ATOM   3653 C  CG   . HIS   A 1 666  ? 169.231 201.287 190.149 1.00 73.81  ? 1998 HIS   A CG   1 
ATOM   3654 N  ND1  . HIS   A 1 666  ? 168.667 201.356 188.894 1.00 79.37  ? 1998 HIS   A ND1  1 
ATOM   3655 C  CD2  . HIS   A 1 666  ? 168.421 200.485 190.879 1.00 79.21  ? 1998 HIS   A CD2  1 
ATOM   3656 C  CE1  . HIS   A 1 666  ? 167.568 200.624 188.865 1.00 79.90  ? 1998 HIS   A CE1  1 
ATOM   3657 N  NE2  . HIS   A 1 666  ? 167.395 200.086 190.058 1.00 85.61  ? 1998 HIS   A NE2  1 
ATOM   3658 N  N    . ASN   A 1 667  ? 173.664 201.965 190.119 1.00 47.64  ? 1999 ASN   A N    1 
ATOM   3659 C  CA   . ASN   A 1 667  ? 174.925 202.308 190.758 1.00 39.12  ? 1999 ASN   A CA   1 
ATOM   3660 C  C    . ASN   A 1 667  ? 176.073 202.438 189.774 1.00 39.99  ? 1999 ASN   A C    1 
ATOM   3661 O  O    . ASN   A 1 667  ? 177.233 202.351 190.184 1.00 40.69  ? 1999 ASN   A O    1 
ATOM   3662 C  CB   . ASN   A 1 667  ? 175.288 201.270 191.818 1.00 38.05  ? 1999 ASN   A CB   1 
ATOM   3663 C  CG   . ASN   A 1 667  ? 174.223 201.112 192.876 1.00 53.21  ? 1999 ASN   A CG   1 
ATOM   3664 O  OD1  . ASN   A 1 667  ? 173.278 201.894 192.934 1.00 49.41  ? 1999 ASN   A OD1  1 
ATOM   3665 N  ND2  . ASN   A 1 667  ? 174.358 200.093 193.710 1.00 66.07  ? 1999 ASN   A ND2  1 
ATOM   3666 N  N    . VAL   A 1 668  ? 175.785 202.620 188.492 1.00 32.96  ? 2000 VAL   A N    1 
ATOM   3667 C  CA   . VAL   A 1 668  ? 176.804 202.901 187.490 1.00 29.98  ? 2000 VAL   A CA   1 
ATOM   3668 C  C    . VAL   A 1 668  ? 176.579 204.329 187.023 1.00 39.50  ? 2000 VAL   A C    1 
ATOM   3669 O  O    . VAL   A 1 668  ? 175.523 204.647 186.463 1.00 52.63  ? 2000 VAL   A O    1 
ATOM   3670 C  CB   . VAL   A 1 668  ? 176.753 201.917 186.317 1.00 29.89  ? 2000 VAL   A CB   1 
ATOM   3671 C  CG1  . VAL   A 1 668  ? 177.749 202.310 185.258 1.00 29.17  ? 2000 VAL   A CG1  1 
ATOM   3672 C  CG2  . VAL   A 1 668  ? 177.054 200.526 186.804 1.00 33.09  ? 2000 VAL   A CG2  1 
ATOM   3673 N  N    . LEU   A 1 669  ? 177.565 205.189 187.251 1.00 33.66  ? 2001 LEU   A N    1 
ATOM   3674 C  CA   . LEU   A 1 669  ? 177.446 206.612 186.982 1.00 32.24  ? 2001 LEU   A CA   1 
ATOM   3675 C  C    . LEU   A 1 669  ? 178.181 206.955 185.701 1.00 34.99  ? 2001 LEU   A C    1 
ATOM   3676 O  O    . LEU   A 1 669  ? 179.375 206.668 185.569 1.00 44.32  ? 2001 LEU   A O    1 
ATOM   3677 C  CB   . LEU   A 1 669  ? 178.012 207.436 188.131 1.00 24.54  ? 2001 LEU   A CB   1 
ATOM   3678 C  CG   . LEU   A 1 669  ? 177.631 206.963 189.517 1.00 34.28  ? 2001 LEU   A CG   1 
ATOM   3679 C  CD1  . LEU   A 1 669  ? 178.581 207.576 190.475 1.00 37.37  ? 2001 LEU   A CD1  1 
ATOM   3680 C  CD2  . LEU   A 1 669  ? 176.219 207.380 189.826 1.00 43.20  ? 2001 LEU   A CD2  1 
ATOM   3681 N  N    . LEU   A 1 670  ? 177.469 207.582 184.773 1.00 27.94  ? 2002 LEU   A N    1 
ATOM   3682 C  CA   . LEU   A 1 670  ? 178.012 208.006 183.498 1.00 25.81  ? 2002 LEU   A CA   1 
ATOM   3683 C  C    . LEU   A 1 670  ? 178.309 209.491 183.575 1.00 35.24  ? 2002 LEU   A C    1 
ATOM   3684 O  O    . LEU   A 1 670  ? 177.423 210.289 183.908 1.00 49.06  ? 2002 LEU   A O    1 
ATOM   3685 C  CB   . LEU   A 1 670  ? 177.022 207.743 182.372 1.00 22.95  ? 2002 LEU   A CB   1 
ATOM   3686 C  CG   . LEU   A 1 670  ? 176.677 206.306 182.051 1.00 31.43  ? 2002 LEU   A CG   1 
ATOM   3687 C  CD1  . LEU   A 1 670  ? 175.608 206.336 181.025 1.00 45.24  ? 2002 LEU   A CD1  1 
ATOM   3688 C  CD2  . LEU   A 1 670  ? 177.876 205.574 181.531 1.00 37.78  ? 2002 LEU   A CD2  1 
ATOM   3689 N  N    . PHE   A 1 671  ? 179.541 209.859 183.257 1.00 29.78  ? 2003 PHE   A N    1 
ATOM   3690 C  CA   . PHE   A 1 671  ? 179.897 211.263 183.214 1.00 32.83  ? 2003 PHE   A CA   1 
ATOM   3691 C  C    . PHE   A 1 671  ? 179.664 211.861 181.836 1.00 40.73  ? 2003 PHE   A C    1 
ATOM   3692 O  O    . PHE   A 1 671  ? 179.113 212.956 181.721 1.00 51.84  ? 2003 PHE   A O    1 
ATOM   3693 C  CB   . PHE   A 1 671  ? 181.355 211.452 183.615 1.00 32.72  ? 2003 PHE   A CB   1 
ATOM   3694 C  CG   . PHE   A 1 671  ? 181.631 211.098 185.032 1.00 38.85  ? 2003 PHE   A CG   1 
ATOM   3695 C  CD1  . PHE   A 1 671  ? 182.873 210.648 185.415 1.00 47.19  ? 2003 PHE   A CD1  1 
ATOM   3696 C  CD2  . PHE   A 1 671  ? 180.635 211.185 185.982 1.00 36.60  ? 2003 PHE   A CD2  1 
ATOM   3697 C  CE1  . PHE   A 1 671  ? 183.120 210.331 186.721 1.00 42.32  ? 2003 PHE   A CE1  1 
ATOM   3698 C  CE2  . PHE   A 1 671  ? 180.877 210.852 187.288 1.00 34.41  ? 2003 PHE   A CE2  1 
ATOM   3699 C  CZ   . PHE   A 1 671  ? 182.116 210.422 187.660 1.00 37.42  ? 2003 PHE   A CZ   1 
ATOM   3700 N  N    . THR   A 1 672  ? 180.080 211.157 180.787 1.00 42.00  ? 2004 THR   A N    1 
ATOM   3701 C  CA   . THR   A 1 672  ? 180.053 211.674 179.429 1.00 43.33  ? 2004 THR   A CA   1 
ATOM   3702 C  C    . THR   A 1 672  ? 179.334 210.694 178.519 1.00 38.95  ? 2004 THR   A C    1 
ATOM   3703 O  O    . THR   A 1 672  ? 179.227 209.505 178.819 1.00 42.84  ? 2004 THR   A O    1 
ATOM   3704 C  CB   . THR   A 1 672  ? 181.469 211.918 178.886 1.00 43.14  ? 2004 THR   A CB   1 
ATOM   3705 O  OG1  . THR   A 1 672  ? 182.088 210.664 178.587 1.00 43.07  ? 2004 THR   A OG1  1 
ATOM   3706 C  CG2  . THR   A 1 672  ? 182.319 212.646 179.902 1.00 41.26  ? 2004 THR   A CG2  1 
ATOM   3707 N  N    . LEU   A 1 673  ? 178.832 211.206 177.401 1.00 36.02  ? 2005 LEU   A N    1 
ATOM   3708 C  CA   . LEU   A 1 673  ? 178.275 210.362 176.351 1.00 43.23  ? 2005 LEU   A CA   1 
ATOM   3709 C  C    . LEU   A 1 673  ? 179.091 210.446 175.073 1.00 56.99  ? 2005 LEU   A C    1 
ATOM   3710 O  O    . LEU   A 1 673  ? 178.559 210.336 173.968 1.00 56.70  ? 2005 LEU   A O    1 
ATOM   3711 C  CB   . LEU   A 1 673  ? 176.821 210.727 176.093 1.00 45.11  ? 2005 LEU   A CB   1 
ATOM   3712 C  CG   . LEU   A 1 673  ? 175.964 210.400 177.307 1.00 40.92  ? 2005 LEU   A CG   1 
ATOM   3713 C  CD1  . LEU   A 1 673  ? 174.533 210.870 177.123 1.00 42.34  ? 2005 LEU   A CD1  1 
ATOM   3714 C  CD2  . LEU   A 1 673  ? 176.027 208.921 177.561 1.00 42.44  ? 2005 LEU   A CD2  1 
ATOM   3715 N  N    . TYR   A 1 674  ? 180.398 210.639 175.206 1.00 65.23  ? 2006 TYR   A N    1 
ATOM   3716 C  CA   . TYR   A 1 674  ? 181.279 210.774 174.064 1.00 62.49  ? 2006 TYR   A CA   1 
ATOM   3717 C  C    . TYR   A 1 674  ? 182.121 209.514 173.964 1.00 58.23  ? 2006 TYR   A C    1 
ATOM   3718 O  O    . TYR   A 1 674  ? 183.030 209.317 174.783 1.00 60.27  ? 2006 TYR   A O    1 
ATOM   3719 C  CB   . TYR   A 1 674  ? 182.154 212.014 174.228 1.00 67.69  ? 2006 TYR   A CB   1 
ATOM   3720 C  CG   . TYR   A 1 674  ? 182.860 212.467 172.980 1.00 75.34  ? 2006 TYR   A CG   1 
ATOM   3721 C  CD1  . TYR   A 1 674  ? 182.220 212.435 171.751 1.00 80.56  ? 2006 TYR   A CD1  1 
ATOM   3722 C  CD2  . TYR   A 1 674  ? 184.142 212.986 173.037 1.00 84.24  ? 2006 TYR   A CD2  1 
ATOM   3723 C  CE1  . TYR   A 1 674  ? 182.854 212.868 170.607 1.00 94.53  ? 2006 TYR   A CE1  1 
ATOM   3724 C  CE2  . TYR   A 1 674  ? 184.783 213.430 171.902 1.00 92.74  ? 2006 TYR   A CE2  1 
ATOM   3725 C  CZ   . TYR   A 1 674  ? 184.138 213.363 170.688 1.00 100.04 ? 2006 TYR   A CZ   1 
ATOM   3726 O  OH   . TYR   A 1 674  ? 184.778 213.803 169.553 1.00 109.55 ? 2006 TYR   A OH   1 
ATOM   3727 N  N    . PRO   A 1 675  ? 181.861 208.651 172.979 1.00 49.50  ? 2007 PRO   A N    1 
ATOM   3728 C  CA   . PRO   A 1 675  ? 182.415 207.287 173.018 1.00 48.51  ? 2007 PRO   A CA   1 
ATOM   3729 C  C    . PRO   A 1 675  ? 183.924 207.192 173.159 1.00 56.41  ? 2007 PRO   A C    1 
ATOM   3730 O  O    . PRO   A 1 675  ? 184.412 206.232 173.765 1.00 50.58  ? 2007 PRO   A O    1 
ATOM   3731 C  CB   . PRO   A 1 675  ? 181.937 206.693 171.691 1.00 42.32  ? 2007 PRO   A CB   1 
ATOM   3732 C  CG   . PRO   A 1 675  ? 180.684 207.419 171.388 1.00 48.42  ? 2007 PRO   A CG   1 
ATOM   3733 C  CD   . PRO   A 1 675  ? 180.773 208.782 171.999 1.00 52.18  ? 2007 PRO   A CD   1 
ATOM   3734 N  N    . ASN   A 1 676  ? 184.689 208.127 172.617 1.00 60.11  ? 2008 ASN   A N    1 
ATOM   3735 C  CA   . ASN   A 1 676  ? 186.138 208.020 172.702 1.00 64.27  ? 2008 ASN   A CA   1 
ATOM   3736 C  C    . ASN   A 1 676  ? 186.710 208.676 173.956 1.00 63.62  ? 2008 ASN   A C    1 
ATOM   3737 O  O    . ASN   A 1 676  ? 187.935 208.761 174.090 1.00 73.05  ? 2008 ASN   A O    1 
ATOM   3738 C  CB   . ASN   A 1 676  ? 186.789 208.611 171.450 1.00 80.68  ? 2008 ASN   A CB   1 
ATOM   3739 C  CG   . ASN   A 1 676  ? 186.308 210.007 171.147 1.00 86.18  ? 2008 ASN   A CG   1 
ATOM   3740 O  OD1  . ASN   A 1 676  ? 186.213 210.847 172.036 1.00 81.93  ? 2008 ASN   A OD1  1 
ATOM   3741 N  ND2  . ASN   A 1 676  ? 185.993 210.264 169.884 1.00 89.78  ? 2008 ASN   A ND2  1 
ATOM   3742 N  N    . ALA   A 1 677  ? 185.861 209.149 174.864 1.00 54.22  ? 2009 ALA   A N    1 
ATOM   3743 C  CA   . ALA   A 1 677  ? 186.339 209.716 176.115 1.00 51.37  ? 2009 ALA   A CA   1 
ATOM   3744 C  C    . ALA   A 1 677  ? 186.967 208.639 176.988 1.00 49.87  ? 2009 ALA   A C    1 
ATOM   3745 O  O    . ALA   A 1 677  ? 186.556 207.479 176.970 1.00 51.73  ? 2009 ALA   A O    1 
ATOM   3746 C  CB   . ALA   A 1 677  ? 185.198 210.389 176.871 1.00 51.04  ? 2009 ALA   A CB   1 
ATOM   3747 N  N    . ALA   A 1 678  ? 187.981 209.034 177.755 1.00 46.67  ? 2010 ALA   A N    1 
ATOM   3748 C  CA   . ALA   A 1 678  ? 188.654 208.081 178.631 1.00 46.96  ? 2010 ALA   A CA   1 
ATOM   3749 C  C    . ALA   A 1 678  ? 187.739 207.598 179.749 1.00 45.44  ? 2010 ALA   A C    1 
ATOM   3750 O  O    . ALA   A 1 678  ? 187.738 206.410 180.084 1.00 45.74  ? 2010 ALA   A O    1 
ATOM   3751 C  CB   . ALA   A 1 678  ? 189.923 208.702 179.208 1.00 50.45  ? 2010 ALA   A CB   1 
ATOM   3752 N  N    . ILE   A 1 679  ? 186.958 208.495 180.344 1.00 42.44  ? 2011 ILE   A N    1 
ATOM   3753 C  CA   . ILE   A 1 679  ? 186.116 208.173 181.492 1.00 34.71  ? 2011 ILE   A CA   1 
ATOM   3754 C  C    . ILE   A 1 679  ? 184.658 208.321 181.092 1.00 40.46  ? 2011 ILE   A C    1 
ATOM   3755 O  O    . ILE   A 1 679  ? 184.187 209.436 180.838 1.00 45.30  ? 2011 ILE   A O    1 
ATOM   3756 C  CB   . ILE   A 1 679  ? 186.435 209.068 182.694 1.00 29.25  ? 2011 ILE   A CB   1 
ATOM   3757 C  CG1  . ILE   A 1 679  ? 187.862 208.819 183.188 1.00 29.45  ? 2011 ILE   A CG1  1 
ATOM   3758 C  CG2  . ILE   A 1 679  ? 185.404 208.858 183.773 1.00 28.73  ? 2011 ILE   A CG2  1 
ATOM   3759 C  CD1  . ILE   A 1 679  ? 188.216 207.373 183.306 1.00 33.41  ? 2011 ILE   A CD1  1 
ATOM   3760 N  N    . ILE   A 1 680  ? 183.934 207.203 181.069 1.00 36.29  ? 2012 ILE   A N    1 
ATOM   3761 C  CA   . ILE   A 1 680  ? 182.539 207.163 180.655 1.00 27.05  ? 2012 ILE   A CA   1 
ATOM   3762 C  C    . ILE   A 1 680  ? 181.642 206.609 181.753 1.00 21.62  ? 2012 ILE   A C    1 
ATOM   3763 O  O    . ILE   A 1 680  ? 180.510 207.056 181.925 1.00 23.83  ? 2012 ILE   A O    1 
ATOM   3764 C  CB   . ILE   A 1 680  ? 182.358 206.364 179.350 1.00 18.51  ? 2012 ILE   A CB   1 
ATOM   3765 C  CG1  . ILE   A 1 680  ? 183.491 206.685 178.389 1.00 25.47  ? 2012 ILE   A CG1  1 
ATOM   3766 C  CG2  . ILE   A 1 680  ? 181.021 206.661 178.719 1.00 17.77  ? 2012 ILE   A CG2  1 
ATOM   3767 C  CD1  . ILE   A 1 680  ? 183.516 205.823 177.190 1.00 37.90  ? 2012 ILE   A CD1  1 
ATOM   3768 N  N    . ALA   A 1 681  ? 182.120 205.615 182.486 1.00 19.36  ? 2013 ALA   A N    1 
ATOM   3769 C  CA   . ALA   A 1 681  ? 181.349 205.069 183.589 1.00 20.47  ? 2013 ALA   A CA   1 
ATOM   3770 C  C    . ALA   A 1 681  ? 182.253 204.766 184.767 1.00 25.91  ? 2013 ALA   A C    1 
ATOM   3771 O  O    . ALA   A 1 681  ? 183.405 204.366 184.591 1.00 30.84  ? 2013 ALA   A O    1 
ATOM   3772 C  CB   . ALA   A 1 681  ? 180.605 203.807 183.183 1.00 20.97  ? 2013 ALA   A CB   1 
ATOM   3773 N  N    . LYS   A 1 682  ? 181.725 204.985 185.967 1.00 21.51  ? 2014 LYS   A N    1 
ATOM   3774 C  CA   . LYS   A 1 682  ? 182.319 204.478 187.191 1.00 23.79  ? 2014 LYS   A CA   1 
ATOM   3775 C  C    . LYS   A 1 682  ? 181.261 203.746 187.998 1.00 24.09  ? 2014 LYS   A C    1 
ATOM   3776 O  O    . LYS   A 1 682  ? 180.063 203.874 187.750 1.00 24.37  ? 2014 LYS   A O    1 
ATOM   3777 C  CB   . LYS   A 1 682  ? 182.925 205.572 188.062 1.00 30.41  ? 2014 LYS   A CB   1 
ATOM   3778 C  CG   . LYS   A 1 682  ? 183.964 206.449 187.420 1.00 32.61  ? 2014 LYS   A CG   1 
ATOM   3779 C  CD   . LYS   A 1 682  ? 184.111 207.680 188.277 1.00 38.72  ? 2014 LYS   A CD   1 
ATOM   3780 C  CE   . LYS   A 1 682  ? 185.491 208.279 188.212 1.00 36.81  ? 2014 LYS   A CE   1 
ATOM   3781 N  NZ   . LYS   A 1 682  ? 185.993 208.301 186.837 1.00 31.68  ? 2014 LYS   A NZ   1 
ATOM   3782 N  N    . ILE   A 1 683  ? 181.719 202.985 188.985 1.00 22.77  ? 2015 ILE   A N    1 
ATOM   3783 C  CA   . ILE   A 1 683  ? 180.846 202.237 189.879 1.00 27.67  ? 2015 ILE   A CA   1 
ATOM   3784 C  C    . ILE   A 1 683  ? 180.902 202.874 191.260 1.00 32.09  ? 2015 ILE   A C    1 
ATOM   3785 O  O    . ILE   A 1 683  ? 181.987 203.148 191.783 1.00 34.60  ? 2015 ILE   A O    1 
ATOM   3786 C  CB   . ILE   A 1 683  ? 181.234 200.748 189.922 1.00 32.98  ? 2015 ILE   A CB   1 
ATOM   3787 C  CG1  . ILE   A 1 683  ? 182.739 200.580 190.103 1.00 28.61  ? 2015 ILE   A CG1  1 
ATOM   3788 C  CG2  . ILE   A 1 683  ? 180.771 200.044 188.680 1.00 35.40  ? 2015 ILE   A CG2  1 
ATOM   3789 C  CD1  . ILE   A 1 683  ? 183.199 199.151 190.040 1.00 26.23  ? 2015 ILE   A CD1  1 
ATOM   3790 N  N    . ALA   A 1 684  ? 179.730 203.118 191.842 1.00 36.36  ? 2016 ALA   A N    1 
ATOM   3791 C  CA   . ALA   A 1 684  ? 179.624 203.779 193.135 1.00 42.21  ? 2016 ALA   A CA   1 
ATOM   3792 C  C    . ALA   A 1 684  ? 178.477 203.161 193.914 1.00 46.57  ? 2016 ALA   A C    1 
ATOM   3793 O  O    . ALA   A 1 684  ? 177.340 203.157 193.434 1.00 45.15  ? 2016 ALA   A O    1 
ATOM   3794 C  CB   . ALA   A 1 684  ? 179.389 205.277 192.963 1.00 29.23  ? 2016 ALA   A CB   1 
ATOM   3795 N  N    . ASP   A 1 685  ? 178.770 202.681 195.122 1.00 46.39  ? 2017 ASP   A N    1 
ATOM   3796 C  CA   . ASP   A 1 685  ? 177.822 201.904 195.914 1.00 43.84  ? 2017 ASP   A CA   1 
ATOM   3797 C  C    . ASP   A 1 685  ? 177.020 202.868 196.782 1.00 47.80  ? 2017 ASP   A C    1 
ATOM   3798 O  O    . ASP   A 1 685  ? 177.596 203.587 197.607 1.00 51.19  ? 2017 ASP   A O    1 
ATOM   3799 C  CB   . ASP   A 1 685  ? 178.582 200.883 196.768 1.00 45.43  ? 2017 ASP   A CB   1 
ATOM   3800 C  CG   . ASP   A 1 685  ? 177.704 200.146 197.774 1.00 65.28  ? 2017 ASP   A CG   1 
ATOM   3801 O  OD1  . ASP   A 1 685  ? 178.214 199.175 198.372 1.00 69.16  ? 2017 ASP   A OD1  1 
ATOM   3802 O  OD2  . ASP   A 1 685  ? 176.509 200.476 197.931 1.00 86.43  ? 2017 ASP   A OD2  1 
ATOM   3803 N  N    . TYR   A 1 686  ? 175.702 202.881 196.606 1.00 52.02  ? 2018 TYR   A N    1 
ATOM   3804 C  CA   . TYR   A 1 686  ? 174.844 203.759 197.387 1.00 63.07  ? 2018 TYR   A CA   1 
ATOM   3805 C  C    . TYR   A 1 686  ? 174.190 202.905 198.471 1.00 75.83  ? 2018 TYR   A C    1 
ATOM   3806 O  O    . TYR   A 1 686  ? 173.382 202.015 198.176 1.00 70.98  ? 2018 TYR   A O    1 
ATOM   3807 C  CB   . TYR   A 1 686  ? 173.824 204.451 196.486 1.00 62.31  ? 2018 TYR   A CB   1 
ATOM   3808 C  CG   . TYR   A 1 686  ? 172.930 205.449 197.179 1.00 72.43  ? 2018 TYR   A CG   1 
ATOM   3809 C  CD1  . TYR   A 1 686  ? 173.431 206.698 197.546 1.00 67.84  ? 2018 TYR   A CD1  1 
ATOM   3810 C  CD2  . TYR   A 1 686  ? 171.582 205.189 197.410 1.00 90.34  ? 2018 TYR   A CD2  1 
ATOM   3811 C  CE1  . TYR   A 1 686  ? 172.636 207.647 198.160 1.00 81.65  ? 2018 TYR   A CE1  1 
ATOM   3812 C  CE2  . TYR   A 1 686  ? 170.765 206.137 198.021 1.00 99.98  ? 2018 TYR   A CE2  1 
ATOM   3813 C  CZ   . TYR   A 1 686  ? 171.296 207.354 198.395 1.00 97.55  ? 2018 TYR   A CZ   1 
ATOM   3814 O  OH   . TYR   A 1 686  ? 170.507 208.297 198.998 1.00 103.44 ? 2018 TYR   A OH   1 
ATOM   3815 N  N    . GLY   A 1 687  ? 174.552 203.176 199.726 1.00 81.70  ? 2019 GLY   A N    1 
ATOM   3816 C  CA   . GLY   A 1 687  ? 174.356 202.188 200.777 1.00 85.65  ? 2019 GLY   A CA   1 
ATOM   3817 C  C    . GLY   A 1 687  ? 172.906 201.848 201.072 1.00 108.48 ? 2019 GLY   A C    1 
ATOM   3818 O  O    . GLY   A 1 687  ? 172.564 200.672 201.230 1.00 116.98 ? 2019 GLY   A O    1 
ATOM   3819 N  N    . ILE   A 1 688  ? 172.037 202.859 201.137 1.00 111.39 ? 2020 ILE   A N    1 
ATOM   3820 C  CA   . ILE   A 1 688  ? 170.731 202.751 201.816 1.00 118.09 ? 2020 ILE   A CA   1 
ATOM   3821 C  C    . ILE   A 1 688  ? 170.762 201.776 202.984 1.00 118.71 ? 2020 ILE   A C    1 
ATOM   3822 O  O    . ILE   A 1 688  ? 171.169 202.142 204.088 1.00 104.97 ? 2020 ILE   A O    1 
ATOM   3823 C  CB   . ILE   A 1 688  ? 169.558 202.342 200.848 1.00 117.85 ? 2020 ILE   A CB   1 
ATOM   3824 C  CG1  . ILE   A 1 688  ? 169.748 200.934 200.229 1.00 116.23 ? 2020 ILE   A CG1  1 
ATOM   3825 C  CG2  . ILE   A 1 688  ? 169.277 203.435 199.838 1.00 108.40 ? 2020 ILE   A CG2  1 
ATOM   3826 C  CD1  . ILE   A 1 688  ? 168.537 200.408 199.478 1.00 116.02 ? 2020 ILE   A CD1  1 
ATOM   3827 N  N    . GLU   A 1 701  ? 172.735 192.215 200.657 1.00 117.48 ? 2033 GLU   A N    1 
ATOM   3828 C  CA   . GLU   A 1 701  ? 173.116 191.094 199.814 1.00 124.28 ? 2033 GLU   A CA   1 
ATOM   3829 C  C    . GLU   A 1 701  ? 172.819 191.383 198.353 1.00 125.87 ? 2033 GLU   A C    1 
ATOM   3830 O  O    . GLU   A 1 701  ? 173.338 190.708 197.475 1.00 124.04 ? 2033 GLU   A O    1 
ATOM   3831 C  CB   . GLU   A 1 701  ? 172.374 189.835 200.246 1.00 123.77 ? 2033 GLU   A CB   1 
ATOM   3832 C  CG   . GLU   A 1 701  ? 170.916 190.073 200.593 1.00 118.82 ? 2033 GLU   A CG   1 
ATOM   3833 C  CD   . GLU   A 1 701  ? 170.741 190.829 201.895 1.00 122.14 ? 2033 GLU   A CD   1 
ATOM   3834 O  OE1  . GLU   A 1 701  ? 171.120 192.016 201.950 1.00 116.71 ? 2033 GLU   A OE1  1 
ATOM   3835 O  OE2  . GLU   A 1 701  ? 170.224 190.236 202.863 1.00 129.61 ? 2033 GLU   A OE2  1 
ATOM   3836 N  N    . GLY   A 1 702  ? 171.986 192.386 198.092 1.00 121.12 ? 2034 GLY   A N    1 
ATOM   3837 C  CA   . GLY   A 1 702  ? 171.635 192.727 196.729 1.00 110.88 ? 2034 GLY   A CA   1 
ATOM   3838 C  C    . GLY   A 1 702  ? 170.140 192.900 196.546 1.00 116.82 ? 2034 GLY   A C    1 
ATOM   3839 O  O    . GLY   A 1 702  ? 169.322 192.358 197.298 1.00 125.24 ? 2034 GLY   A O    1 
ATOM   3840 N  N    . THR   A 1 703  ? 169.772 193.674 195.530 1.00 108.74 ? 2035 THR   A N    1 
ATOM   3841 C  CA   . THR   A 1 703  ? 168.371 193.948 195.264 1.00 107.60 ? 2035 THR   A CA   1 
ATOM   3842 C  C    . THR   A 1 703  ? 167.668 192.693 194.746 1.00 109.01 ? 2035 THR   A C    1 
ATOM   3843 O  O    . THR   A 1 703  ? 168.315 191.779 194.231 1.00 107.27 ? 2035 THR   A O    1 
ATOM   3844 C  CB   . THR   A 1 703  ? 168.237 195.089 194.260 1.00 100.13 ? 2035 THR   A CB   1 
ATOM   3845 O  OG1  . THR   A 1 703  ? 168.865 194.719 193.029 1.00 100.23 ? 2035 THR   A OG1  1 
ATOM   3846 C  CG2  . THR   A 1 703  ? 168.870 196.354 194.806 1.00 90.59  ? 2035 THR   A CG2  1 
ATOM   3847 N  N    . PRO   A 1 704  ? 166.338 192.617 194.882 1.00 109.16 ? 2036 PRO   A N    1 
ATOM   3848 C  CA   . PRO   A 1 704  ? 165.629 191.380 194.525 1.00 109.96 ? 2036 PRO   A CA   1 
ATOM   3849 C  C    . PRO   A 1 704  ? 165.561 191.093 193.035 1.00 115.27 ? 2036 PRO   A C    1 
ATOM   3850 O  O    . PRO   A 1 704  ? 164.863 190.151 192.642 1.00 116.85 ? 2036 PRO   A O    1 
ATOM   3851 C  CB   . PRO   A 1 704  ? 164.225 191.606 195.101 1.00 106.22 ? 2036 PRO   A CB   1 
ATOM   3852 C  CG   . PRO   A 1 704  ? 164.061 193.068 195.114 1.00 102.19 ? 2036 PRO   A CG   1 
ATOM   3853 C  CD   . PRO   A 1 704  ? 165.415 193.636 195.414 1.00 104.49 ? 2036 PRO   A CD   1 
ATOM   3854 N  N    . GLY   A 1 705  ? 166.249 191.856 192.192 1.00 108.37 ? 2037 GLY   A N    1 
ATOM   3855 C  CA   . GLY   A 1 705  ? 166.226 191.582 190.770 1.00 92.82  ? 2037 GLY   A CA   1 
ATOM   3856 C  C    . GLY   A 1 705  ? 167.591 191.464 190.126 1.00 82.24  ? 2037 GLY   A C    1 
ATOM   3857 O  O    . GLY   A 1 705  ? 167.683 191.253 188.915 1.00 80.79  ? 2037 GLY   A O    1 
ATOM   3858 N  N    . PHE   A 1 706  ? 168.663 191.602 190.911 1.00 83.26  ? 2038 PHE   A N    1 
ATOM   3859 C  CA   . PHE   A 1 706  ? 169.998 191.613 190.326 1.00 79.07  ? 2038 PHE   A CA   1 
ATOM   3860 C  C    . PHE   A 1 706  ? 171.005 190.750 191.074 1.00 78.34  ? 2038 PHE   A C    1 
ATOM   3861 O  O    . PHE   A 1 706  ? 172.211 190.917 190.854 1.00 73.55  ? 2038 PHE   A O    1 
ATOM   3862 C  CB   . PHE   A 1 706  ? 170.567 193.037 190.242 1.00 74.56  ? 2038 PHE   A CB   1 
ATOM   3863 C  CG   . PHE   A 1 706  ? 169.709 194.000 189.483 1.00 76.64  ? 2038 PHE   A CG   1 
ATOM   3864 C  CD1  . PHE   A 1 706  ? 170.097 194.447 188.239 1.00 73.67  ? 2038 PHE   A CD1  1 
ATOM   3865 C  CD2  . PHE   A 1 706  ? 168.555 194.513 190.037 1.00 78.24  ? 2038 PHE   A CD2  1 
ATOM   3866 C  CE1  . PHE   A 1 706  ? 169.318 195.335 187.543 1.00 70.86  ? 2038 PHE   A CE1  1 
ATOM   3867 C  CE2  . PHE   A 1 706  ? 167.780 195.407 189.347 1.00 78.41  ? 2038 PHE   A CE2  1 
ATOM   3868 C  CZ   . PHE   A 1 706  ? 168.164 195.821 188.103 1.00 74.73  ? 2038 PHE   A CZ   1 
ATOM   3869 N  N    . ARG   A 1 707  ? 170.574 189.842 191.940 1.00 76.65  ? 2039 ARG   A N    1 
ATOM   3870 C  CA   . ARG   A 1 707  ? 171.542 189.122 192.751 1.00 77.62  ? 2039 ARG   A CA   1 
ATOM   3871 C  C    . ARG   A 1 707  ? 171.865 187.765 192.135 1.00 67.31  ? 2039 ARG   A C    1 
ATOM   3872 O  O    . ARG   A 1 707  ? 171.142 187.245 191.284 1.00 63.11  ? 2039 ARG   A O    1 
ATOM   3873 C  CB   . ARG   A 1 707  ? 171.034 188.937 194.181 1.00 91.32  ? 2039 ARG   A CB   1 
ATOM   3874 C  CG   . ARG   A 1 707  ? 169.833 188.023 194.319 1.00 100.20 ? 2039 ARG   A CG   1 
ATOM   3875 C  CD   . ARG   A 1 707  ? 169.339 187.992 195.757 1.00 104.04 ? 2039 ARG   A CD   1 
ATOM   3876 N  NE   . ARG   A 1 707  ? 168.246 187.044 195.942 1.00 114.33 ? 2039 ARG   A NE   1 
ATOM   3877 C  CZ   . ARG   A 1 707  ? 166.965 187.325 195.757 1.00 116.06 ? 2039 ARG   A CZ   1 
ATOM   3878 N  NH1  . ARG   A 1 707  ? 166.569 188.529 195.392 1.00 110.64 ? 2039 ARG   A NH1  1 
ATOM   3879 N  NH2  . ARG   A 1 707  ? 166.058 186.372 195.947 1.00 117.24 ? 2039 ARG   A NH2  1 
ATOM   3880 N  N    . ALA   A 1 708  ? 172.975 187.190 192.583 1.00 62.90  ? 2040 ALA   A N    1 
ATOM   3881 C  CA   . ALA   A 1 708  ? 173.336 185.848 192.170 1.00 64.56  ? 2040 ALA   A CA   1 
ATOM   3882 C  C    . ALA   A 1 708  ? 172.351 184.842 192.765 1.00 80.85  ? 2040 ALA   A C    1 
ATOM   3883 O  O    . ALA   A 1 708  ? 171.715 185.121 193.784 1.00 91.24  ? 2040 ALA   A O    1 
ATOM   3884 C  CB   . ALA   A 1 708  ? 174.756 185.529 192.616 1.00 68.45  ? 2040 ALA   A CB   1 
ATOM   3885 N  N    . PRO   A 1 709  ? 172.189 183.670 192.142 1.00 78.51  ? 2041 PRO   A N    1 
ATOM   3886 C  CA   . PRO   A 1 709  ? 171.146 182.747 192.617 1.00 87.42  ? 2041 PRO   A CA   1 
ATOM   3887 C  C    . PRO   A 1 709  ? 171.357 182.280 194.043 1.00 96.05  ? 2041 PRO   A C    1 
ATOM   3888 O  O    . PRO   A 1 709  ? 170.377 182.056 194.764 1.00 105.35 ? 2041 PRO   A O    1 
ATOM   3889 C  CB   . PRO   A 1 709  ? 171.233 181.584 191.622 1.00 87.43  ? 2041 PRO   A CB   1 
ATOM   3890 C  CG   . PRO   A 1 709  ? 172.628 181.605 191.152 1.00 75.42  ? 2041 PRO   A CG   1 
ATOM   3891 C  CD   . PRO   A 1 709  ? 173.031 183.046 191.107 1.00 74.10  ? 2041 PRO   A CD   1 
ATOM   3892 N  N    . GLU   A 1 710  ? 172.609 182.138 194.481 1.00 100.32 ? 2042 GLU   A N    1 
ATOM   3893 C  CA   . GLU   A 1 710  ? 172.881 181.675 195.835 1.00 104.41 ? 2042 GLU   A CA   1 
ATOM   3894 C  C    . GLU   A 1 710  ? 172.451 182.677 196.895 1.00 104.91 ? 2042 GLU   A C    1 
ATOM   3895 O  O    . GLU   A 1 710  ? 172.300 182.294 198.059 1.00 110.88 ? 2042 GLU   A O    1 
ATOM   3896 C  CB   . GLU   A 1 710  ? 174.370 181.361 195.990 1.00 109.83 ? 2042 GLU   A CB   1 
ATOM   3897 C  CG   . GLU   A 1 710  ? 175.273 182.554 195.773 1.00 102.36 ? 2042 GLU   A CG   1 
ATOM   3898 C  CD   . GLU   A 1 710  ? 175.979 182.503 194.437 1.00 101.53 ? 2042 GLU   A CD   1 
ATOM   3899 O  OE1  . GLU   A 1 710  ? 175.508 181.772 193.542 1.00 103.74 ? 2042 GLU   A OE1  1 
ATOM   3900 O  OE2  . GLU   A 1 710  ? 177.002 183.197 194.278 1.00 100.62 ? 2042 GLU   A OE2  1 
ATOM   3901 N  N    . VAL   A 1 711  ? 172.242 183.933 196.527 1.00 98.36  ? 2043 VAL   A N    1 
ATOM   3902 C  CA   . VAL   A 1 711  ? 171.798 184.932 197.480 1.00 102.46 ? 2043 VAL   A CA   1 
ATOM   3903 C  C    . VAL   A 1 711  ? 170.290 185.100 197.383 1.00 104.76 ? 2043 VAL   A C    1 
ATOM   3904 O  O    . VAL   A 1 711  ? 169.674 184.679 196.405 1.00 100.51 ? 2043 VAL   A O    1 
ATOM   3905 C  CB   . VAL   A 1 711  ? 172.511 186.263 197.254 1.00 98.62  ? 2043 VAL   A CB   1 
ATOM   3906 C  CG1  . VAL   A 1 711  ? 172.220 187.204 198.398 1.00 102.94 ? 2043 VAL   A CG1  1 
ATOM   3907 C  CG2  . VAL   A 1 711  ? 174.004 186.036 197.107 1.00 96.43  ? 2043 VAL   A CG2  1 
ATOM   3908 N  N    . TYR   A 1 718  ? 178.521 183.593 197.161 1.00 109.60 ? 2050 TYR   A N    1 
ATOM   3909 C  CA   . TYR   A 1 718  ? 178.447 184.971 197.631 1.00 110.01 ? 2050 TYR   A CA   1 
ATOM   3910 C  C    . TYR   A 1 718  ? 179.870 185.536 197.610 1.00 101.55 ? 2050 TYR   A C    1 
ATOM   3911 O  O    . TYR   A 1 718  ? 180.191 186.530 198.259 1.00 96.85  ? 2050 TYR   A O    1 
ATOM   3912 C  CB   . TYR   A 1 718  ? 177.798 185.029 199.021 1.00 116.32 ? 2050 TYR   A CB   1 
ATOM   3913 C  CG   . TYR   A 1 718  ? 177.616 186.419 199.594 1.00 118.11 ? 2050 TYR   A CG   1 
ATOM   3914 C  CD1  . TYR   A 1 718  ? 176.615 187.262 199.122 1.00 115.31 ? 2050 TYR   A CD1  1 
ATOM   3915 C  CD2  . TYR   A 1 718  ? 178.403 186.867 200.644 1.00 121.82 ? 2050 TYR   A CD2  1 
ATOM   3916 C  CE1  . TYR   A 1 718  ? 176.437 188.532 199.653 1.00 110.82 ? 2050 TYR   A CE1  1 
ATOM   3917 C  CE2  . TYR   A 1 718  ? 178.226 188.128 201.184 1.00 125.72 ? 2050 TYR   A CE2  1 
ATOM   3918 C  CZ   . TYR   A 1 718  ? 177.243 188.958 200.685 1.00 118.54 ? 2050 TYR   A CZ   1 
ATOM   3919 O  OH   . TYR   A 1 718  ? 177.071 190.215 201.219 1.00 114.71 ? 2050 TYR   A OH   1 
ATOM   3920 N  N    . ASN   A 1 719  ? 180.708 184.879 196.820 1.00 94.07  ? 2051 ASN   A N    1 
ATOM   3921 C  CA   . ASN   A 1 719  ? 182.107 185.232 196.642 1.00 90.90  ? 2051 ASN   A CA   1 
ATOM   3922 C  C    . ASN   A 1 719  ? 182.212 186.240 195.494 1.00 83.73  ? 2051 ASN   A C    1 
ATOM   3923 O  O    . ASN   A 1 719  ? 181.225 186.882 195.128 1.00 79.43  ? 2051 ASN   A O    1 
ATOM   3924 C  CB   . ASN   A 1 719  ? 182.922 183.955 196.402 1.00 87.82  ? 2051 ASN   A CB   1 
ATOM   3925 C  CG   . ASN   A 1 719  ? 184.349 184.068 196.890 1.00 89.93  ? 2051 ASN   A CG   1 
ATOM   3926 O  OD1  . ASN   A 1 719  ? 184.653 184.869 197.769 1.00 83.02  ? 2051 ASN   A OD1  1 
ATOM   3927 N  ND2  . ASN   A 1 719  ? 185.233 183.258 196.324 1.00 88.50  ? 2051 ASN   A ND2  1 
ATOM   3928 N  N    . GLN   A 1 720  ? 183.413 186.412 194.937 1.00 84.97  ? 2052 GLN   A N    1 
ATOM   3929 C  CA   . GLN   A 1 720  ? 183.579 187.126 193.675 1.00 69.71  ? 2052 GLN   A CA   1 
ATOM   3930 C  C    . GLN   A 1 720  ? 182.636 186.619 192.592 1.00 58.71  ? 2052 GLN   A C    1 
ATOM   3931 O  O    . GLN   A 1 720  ? 182.324 187.350 191.643 1.00 58.70  ? 2052 GLN   A O    1 
ATOM   3932 C  CB   . GLN   A 1 720  ? 185.016 186.961 193.180 1.00 72.64  ? 2052 GLN   A CB   1 
ATOM   3933 C  CG   . GLN   A 1 720  ? 186.066 187.807 193.877 1.00 67.28  ? 2052 GLN   A CG   1 
ATOM   3934 C  CD   . GLN   A 1 720  ? 186.410 187.323 195.261 1.00 78.75  ? 2052 GLN   A CD   1 
ATOM   3935 O  OE1  . GLN   A 1 720  ? 185.578 186.749 195.956 1.00 84.52  ? 2052 GLN   A OE1  1 
ATOM   3936 N  NE2  . GLN   A 1 720  ? 187.653 187.542 195.667 1.00 82.48  ? 2052 GLN   A NE2  1 
ATOM   3937 N  N    . GLN   A 1 721  ? 182.190 185.373 192.699 1.00 61.08  ? 2053 GLN   A N    1 
ATOM   3938 C  CA   . GLN   A 1 721  ? 181.451 184.767 191.608 1.00 55.93  ? 2053 GLN   A CA   1 
ATOM   3939 C  C    . GLN   A 1 721  ? 180.023 185.298 191.565 1.00 54.53  ? 2053 GLN   A C    1 
ATOM   3940 O  O    . GLN   A 1 721  ? 179.426 185.410 190.487 1.00 57.03  ? 2053 GLN   A O    1 
ATOM   3941 C  CB   . GLN   A 1 721  ? 181.482 183.256 191.778 1.00 66.57  ? 2053 GLN   A CB   1 
ATOM   3942 C  CG   . GLN   A 1 721  ? 182.903 182.712 191.709 1.00 73.55  ? 2053 GLN   A CG   1 
ATOM   3943 C  CD   . GLN   A 1 721  ? 183.591 182.962 190.398 1.00 75.73  ? 2053 GLN   A CD   1 
ATOM   3944 O  OE1  . GLN   A 1 721  ? 184.504 183.780 190.321 1.00 75.66  ? 2053 GLN   A OE1  1 
ATOM   3945 N  NE2  . GLN   A 1 721  ? 183.210 182.222 189.374 1.00 74.23  ? 2053 GLN   A NE2  1 
ATOM   3946 N  N    . ALA   A 1 722  ? 179.467 185.643 192.726 1.00 61.78  ? 2054 ALA   A N    1 
ATOM   3947 C  CA   . ALA   A 1 722  ? 178.202 186.365 192.753 1.00 59.03  ? 2054 ALA   A CA   1 
ATOM   3948 C  C    . ALA   A 1 722  ? 178.343 187.727 192.094 1.00 52.26  ? 2054 ALA   A C    1 
ATOM   3949 O  O    . ALA   A 1 722  ? 177.420 188.205 191.424 1.00 50.61  ? 2054 ALA   A O    1 
ATOM   3950 C  CB   . ALA   A 1 722  ? 177.717 186.517 194.191 1.00 71.63  ? 2054 ALA   A CB   1 
ATOM   3951 N  N    . ASP   A 1 723  ? 179.498 188.369 192.271 1.00 53.00  ? 2055 ASP   A N    1 
ATOM   3952 C  CA   . ASP   A 1 723  ? 179.761 189.614 191.562 1.00 50.25  ? 2055 ASP   A CA   1 
ATOM   3953 C  C    . ASP   A 1 723  ? 179.753 189.397 190.060 1.00 51.73  ? 2055 ASP   A C    1 
ATOM   3954 O  O    . ASP   A 1 723  ? 179.224 190.221 189.311 1.00 50.23  ? 2055 ASP   A O    1 
ATOM   3955 C  CB   . ASP   A 1 723  ? 181.111 190.182 191.971 1.00 48.11  ? 2055 ASP   A CB   1 
ATOM   3956 C  CG   . ASP   A 1 723  ? 181.019 191.116 193.128 1.00 59.88  ? 2055 ASP   A CG   1 
ATOM   3957 O  OD1  . ASP   A 1 723  ? 182.077 191.543 193.629 1.00 64.66  ? 2055 ASP   A OD1  1 
ATOM   3958 O  OD2  . ASP   A 1 723  ? 179.887 191.397 193.553 1.00 70.67  ? 2055 ASP   A OD2  1 
ATOM   3959 N  N    . VAL   A 1 724  ? 180.371 188.308 189.599 1.00 47.72  ? 2056 VAL   A N    1 
ATOM   3960 C  CA   . VAL   A 1 724  ? 180.409 188.034 188.164 1.00 24.52  ? 2056 VAL   A CA   1 
ATOM   3961 C  C    . VAL   A 1 724  ? 179.007 187.802 187.618 1.00 24.46  ? 2056 VAL   A C    1 
ATOM   3962 O  O    . VAL   A 1 724  ? 178.668 188.268 186.527 1.00 25.07  ? 2056 VAL   A O    1 
ATOM   3963 C  CB   . VAL   A 1 724  ? 181.334 186.850 187.861 1.00 32.06  ? 2056 VAL   A CB   1 
ATOM   3964 C  CG1  . VAL   A 1 724  ? 181.256 186.528 186.410 1.00 33.85  ? 2056 VAL   A CG1  1 
ATOM   3965 C  CG2  . VAL   A 1 724  ? 182.746 187.207 188.216 1.00 38.02  ? 2056 VAL   A CG2  1 
ATOM   3966 N  N    . TYR   A 1 725  ? 178.176 187.066 188.349 1.00 33.04  ? 2057 TYR   A N    1 
ATOM   3967 C  CA   . TYR   A 1 725  ? 176.779 186.934 187.941 1.00 29.22  ? 2057 TYR   A CA   1 
ATOM   3968 C  C    . TYR   A 1 725  ? 176.085 188.287 187.887 1.00 32.17  ? 2057 TYR   A C    1 
ATOM   3969 O  O    . TYR   A 1 725  ? 175.288 188.551 186.978 1.00 39.62  ? 2057 TYR   A O    1 
ATOM   3970 C  CB   . TYR   A 1 725  ? 176.044 186.004 188.895 1.00 39.29  ? 2057 TYR   A CB   1 
ATOM   3971 C  CG   . TYR   A 1 725  ? 174.683 185.535 188.440 1.00 39.53  ? 2057 TYR   A CG   1 
ATOM   3972 C  CD1  . TYR   A 1 725  ? 173.609 186.407 188.385 1.00 39.48  ? 2057 TYR   A CD1  1 
ATOM   3973 C  CD2  . TYR   A 1 725  ? 174.461 184.215 188.112 1.00 42.76  ? 2057 TYR   A CD2  1 
ATOM   3974 C  CE1  . TYR   A 1 725  ? 172.366 185.980 187.996 1.00 41.22  ? 2057 TYR   A CE1  1 
ATOM   3975 C  CE2  . TYR   A 1 725  ? 173.219 183.779 187.723 1.00 48.12  ? 2057 TYR   A CE2  1 
ATOM   3976 C  CZ   . TYR   A 1 725  ? 172.176 184.666 187.668 1.00 45.80  ? 2057 TYR   A CZ   1 
ATOM   3977 O  OH   . TYR   A 1 725  ? 170.934 184.238 187.276 1.00 60.71  ? 2057 TYR   A OH   1 
ATOM   3978 N  N    . SER   A 1 726  ? 176.352 189.153 188.862 1.00 36.04  ? 2058 SER   A N    1 
ATOM   3979 C  CA   . SER   A 1 726  ? 175.759 190.485 188.832 1.00 34.36  ? 2058 SER   A CA   1 
ATOM   3980 C  C    . SER   A 1 726  ? 176.229 191.266 187.611 1.00 33.31  ? 2058 SER   A C    1 
ATOM   3981 O  O    . SER   A 1 726  ? 175.450 192.000 186.993 1.00 37.77  ? 2058 SER   A O    1 
ATOM   3982 C  CB   . SER   A 1 726  ? 176.091 191.228 190.121 1.00 35.92  ? 2058 SER   A CB   1 
ATOM   3983 O  OG   . SER   A 1 726  ? 177.480 191.470 190.216 1.00 39.05  ? 2058 SER   A OG   1 
ATOM   3984 N  N    . PHE   A 1 727  ? 177.501 191.115 187.247 1.00 30.25  ? 2059 PHE   A N    1 
ATOM   3985 C  CA   . PHE   A 1 727  ? 178.021 191.774 186.056 1.00 23.61  ? 2059 PHE   A CA   1 
ATOM   3986 C  C    . PHE   A 1 727  ? 177.346 191.247 184.802 1.00 23.73  ? 2059 PHE   A C    1 
ATOM   3987 O  O    . PHE   A 1 727  ? 177.087 192.005 183.865 1.00 24.96  ? 2059 PHE   A O    1 
ATOM   3988 C  CB   . PHE   A 1 727  ? 179.527 191.572 185.946 1.00 25.29  ? 2059 PHE   A CB   1 
ATOM   3989 C  CG   . PHE   A 1 727  ? 180.135 192.263 184.769 1.00 18.94  ? 2059 PHE   A CG   1 
ATOM   3990 C  CD1  . PHE   A 1 727  ? 180.349 193.621 184.787 1.00 19.64  ? 2059 PHE   A CD1  1 
ATOM   3991 C  CD2  . PHE   A 1 727  ? 180.430 191.569 183.621 1.00 23.13  ? 2059 PHE   A CD2  1 
ATOM   3992 C  CE1  . PHE   A 1 727  ? 180.895 194.258 183.705 1.00 21.56  ? 2059 PHE   A CE1  1 
ATOM   3993 C  CE2  . PHE   A 1 727  ? 180.959 192.213 182.534 1.00 22.90  ? 2059 PHE   A CE2  1 
ATOM   3994 C  CZ   . PHE   A 1 727  ? 181.194 193.552 182.579 1.00 24.47  ? 2059 PHE   A CZ   1 
ATOM   3995 N  N    . GLY   A 1 728  ? 177.097 189.943 184.749 1.00 27.78  ? 2060 GLY   A N    1 
ATOM   3996 C  CA   . GLY   A 1 728  ? 176.381 189.382 183.617 1.00 22.99  ? 2060 GLY   A CA   1 
ATOM   3997 C  C    . GLY   A 1 728  ? 174.976 189.933 183.502 1.00 27.85  ? 2060 GLY   A C    1 
ATOM   3998 O  O    . GLY   A 1 728  ? 174.498 190.216 182.405 1.00 35.33  ? 2060 GLY   A O    1 
ATOM   3999 N  N    . LEU   A 1 729  ? 174.297 190.098 184.634 1.00 28.13  ? 2061 LEU   A N    1 
ATOM   4000 C  CA   . LEU   A 1 729  ? 172.991 190.750 184.603 1.00 30.63  ? 2061 LEU   A CA   1 
ATOM   4001 C  C    . LEU   A 1 729  ? 173.105 192.192 184.122 1.00 42.79  ? 2061 LEU   A C    1 
ATOM   4002 O  O    . LEU   A 1 729  ? 172.267 192.663 183.345 1.00 48.26  ? 2061 LEU   A O    1 
ATOM   4003 C  CB   . LEU   A 1 729  ? 172.339 190.701 185.978 1.00 31.69  ? 2061 LEU   A CB   1 
ATOM   4004 C  CG   . LEU   A 1 729  ? 171.975 189.307 186.453 1.00 33.73  ? 2061 LEU   A CG   1 
ATOM   4005 C  CD1  . LEU   A 1 729  ? 171.472 189.366 187.865 1.00 51.31  ? 2061 LEU   A CD1  1 
ATOM   4006 C  CD2  . LEU   A 1 729  ? 170.926 188.733 185.550 1.00 36.36  ? 2061 LEU   A CD2  1 
ATOM   4007 N  N    . LEU   A 1 730  ? 174.142 192.906 184.566 1.00 39.10  ? 2062 LEU   A N    1 
ATOM   4008 C  CA   . LEU   A 1 730  ? 174.371 194.268 184.086 1.00 35.81  ? 2062 LEU   A CA   1 
ATOM   4009 C  C    . LEU   A 1 730  ? 174.551 194.310 182.577 1.00 39.36  ? 2062 LEU   A C    1 
ATOM   4010 O  O    . LEU   A 1 730  ? 173.957 195.148 181.894 1.00 39.08  ? 2062 LEU   A O    1 
ATOM   4011 C  CB   . LEU   A 1 730  ? 175.611 194.855 184.748 1.00 28.03  ? 2062 LEU   A CB   1 
ATOM   4012 C  CG   . LEU   A 1 730  ? 175.885 196.291 184.332 1.00 27.98  ? 2062 LEU   A CG   1 
ATOM   4013 C  CD1  . LEU   A 1 730  ? 174.750 197.180 184.775 1.00 40.68  ? 2062 LEU   A CD1  1 
ATOM   4014 C  CD2  . LEU   A 1 730  ? 177.199 196.756 184.887 1.00 30.01  ? 2062 LEU   A CD2  1 
ATOM   4015 N  N    . LEU   A 1 731  ? 175.395 193.429 182.047 1.00 40.90  ? 2063 LEU   A N    1 
ATOM   4016 C  CA   . LEU   A 1 731  ? 175.692 193.421 180.622 1.00 31.94  ? 2063 LEU   A CA   1 
ATOM   4017 C  C    . LEU   A 1 731  ? 174.476 193.016 179.810 1.00 29.39  ? 2063 LEU   A C    1 
ATOM   4018 O  O    . LEU   A 1 731  ? 174.242 193.549 178.723 1.00 28.24  ? 2063 LEU   A O    1 
ATOM   4019 C  CB   . LEU   A 1 731  ? 176.875 192.500 180.361 1.00 23.18  ? 2063 LEU   A CB   1 
ATOM   4020 C  CG   . LEU   A 1 731  ? 177.375 192.397 178.942 1.00 18.18  ? 2063 LEU   A CG   1 
ATOM   4021 C  CD1  . LEU   A 1 731  ? 177.844 193.737 178.491 1.00 21.52  ? 2063 LEU   A CD1  1 
ATOM   4022 C  CD2  . LEU   A 1 731  ? 178.533 191.457 178.973 1.00 19.33  ? 2063 LEU   A CD2  1 
ATOM   4023 N  N    . TYR   A 1 732  ? 173.685 192.083 180.326 1.00 31.61  ? 2064 TYR   A N    1 
ATOM   4024 C  CA   . TYR   A 1 732  ? 172.397 191.786 179.716 1.00 41.02  ? 2064 TYR   A CA   1 
ATOM   4025 C  C    . TYR   A 1 732  ? 171.517 193.027 179.689 1.00 53.14  ? 2064 TYR   A C    1 
ATOM   4026 O  O    . TYR   A 1 732  ? 170.814 193.280 178.704 1.00 60.99  ? 2064 TYR   A O    1 
ATOM   4027 C  CB   . TYR   A 1 732  ? 171.732 190.651 180.492 1.00 39.72  ? 2064 TYR   A CB   1 
ATOM   4028 C  CG   . TYR   A 1 732  ? 170.420 190.158 179.949 1.00 44.71  ? 2064 TYR   A CG   1 
ATOM   4029 C  CD1  . TYR   A 1 732  ? 170.320 188.911 179.370 1.00 53.52  ? 2064 TYR   A CD1  1 
ATOM   4030 C  CD2  . TYR   A 1 732  ? 169.274 190.915 180.066 1.00 55.75  ? 2064 TYR   A CD2  1 
ATOM   4031 C  CE1  . TYR   A 1 732  ? 169.126 188.453 178.890 1.00 73.57  ? 2064 TYR   A CE1  1 
ATOM   4032 C  CE2  . TYR   A 1 732  ? 168.080 190.467 179.588 1.00 70.85  ? 2064 TYR   A CE2  1 
ATOM   4033 C  CZ   . TYR   A 1 732  ? 168.006 189.236 179.003 1.00 78.69  ? 2064 TYR   A CZ   1 
ATOM   4034 O  OH   . TYR   A 1 732  ? 166.796 188.795 178.529 1.00 95.97  ? 2064 TYR   A OH   1 
ATOM   4035 N  N    . ASP   A 1 733  ? 171.536 193.807 180.769 1.00 47.28  ? 2065 ASP   A N    1 
ATOM   4036 C  CA   . ASP   A 1 733  ? 170.732 195.023 180.839 1.00 42.16  ? 2065 ASP   A CA   1 
ATOM   4037 C  C    . ASP   A 1 733  ? 171.196 196.059 179.823 1.00 51.71  ? 2065 ASP   A C    1 
ATOM   4038 O  O    . ASP   A 1 733  ? 170.373 196.742 179.206 1.00 60.15  ? 2065 ASP   A O    1 
ATOM   4039 C  CB   . ASP   A 1 733  ? 170.799 195.585 182.252 1.00 44.76  ? 2065 ASP   A CB   1 
ATOM   4040 C  CG   . ASP   A 1 733  ? 170.095 194.705 183.249 1.00 60.52  ? 2065 ASP   A CG   1 
ATOM   4041 O  OD1  . ASP   A 1 733  ? 169.134 194.026 182.848 1.00 72.14  ? 2065 ASP   A OD1  1 
ATOM   4042 O  OD2  . ASP   A 1 733  ? 170.520 194.660 184.421 1.00 53.82  ? 2065 ASP   A OD2  1 
ATOM   4043 N  N    . ILE   A 1 734  ? 172.511 196.204 179.661 1.00 49.74  ? 2066 ILE   A N    1 
ATOM   4044 C  CA   . ILE   A 1 734  ? 173.055 197.139 178.678 1.00 44.07  ? 2066 ILE   A CA   1 
ATOM   4045 C  C    . ILE   A 1 734  ? 172.672 196.706 177.271 1.00 43.29  ? 2066 ILE   A C    1 
ATOM   4046 O  O    . ILE   A 1 734  ? 172.137 197.494 176.485 1.00 46.06  ? 2066 ILE   A O    1 
ATOM   4047 C  CB   . ILE   A 1 734  ? 174.582 197.242 178.817 1.00 31.06  ? 2066 ILE   A CB   1 
ATOM   4048 C  CG1  . ILE   A 1 734  ? 174.981 198.249 179.878 1.00 24.02  ? 2066 ILE   A CG1  1 
ATOM   4049 C  CG2  . ILE   A 1 734  ? 175.203 197.655 177.516 1.00 34.78  ? 2066 ILE   A CG2  1 
ATOM   4050 C  CD1  . ILE   A 1 734  ? 176.449 198.180 180.205 1.00 16.38  ? 2066 ILE   A CD1  1 
ATOM   4051 N  N    . LEU   A 1 735  ? 172.923 195.438 176.939 1.00 38.15  ? 2067 LEU   A N    1 
ATOM   4052 C  CA   . LEU   A 1 735  ? 172.667 194.952 175.588 1.00 41.79  ? 2067 LEU   A CA   1 
ATOM   4053 C  C    . LEU   A 1 735  ? 171.187 195.042 175.249 1.00 52.50  ? 2067 LEU   A C    1 
ATOM   4054 O  O    . LEU   A 1 735  ? 170.813 195.448 174.145 1.00 62.93  ? 2067 LEU   A O    1 
ATOM   4055 C  CB   . LEU   A 1 735  ? 173.168 193.516 175.457 1.00 46.67  ? 2067 LEU   A CB   1 
ATOM   4056 C  CG   . LEU   A 1 735  ? 173.481 192.933 174.083 1.00 47.16  ? 2067 LEU   A CG   1 
ATOM   4057 C  CD1  . LEU   A 1 735  ? 174.326 191.708 174.269 1.00 42.44  ? 2067 LEU   A CD1  1 
ATOM   4058 C  CD2  . LEU   A 1 735  ? 172.221 192.571 173.327 1.00 57.10  ? 2067 LEU   A CD2  1 
ATOM   4059 N  N    . THR   A 1 736  ? 170.328 194.663 176.189 1.00 52.34  ? 2068 THR   A N    1 
ATOM   4060 C  CA   . THR   A 1 736  ? 168.896 194.802 175.985 1.00 60.30  ? 2068 THR   A CA   1 
ATOM   4061 C  C    . THR   A 1 736  ? 168.446 196.256 176.037 1.00 66.56  ? 2068 THR   A C    1 
ATOM   4062 O  O    . THR   A 1 736  ? 167.409 196.595 175.456 1.00 67.27  ? 2068 THR   A O    1 
ATOM   4063 C  CB   . THR   A 1 736  ? 168.165 193.979 177.040 1.00 67.70  ? 2068 THR   A CB   1 
ATOM   4064 O  OG1  . THR   A 1 736  ? 168.540 192.605 176.906 1.00 75.87  ? 2068 THR   A OG1  1 
ATOM   4065 C  CG2  . THR   A 1 736  ? 166.673 194.104 176.894 1.00 79.30  ? 2068 THR   A CG2  1 
ATOM   4066 N  N    . THR   A 1 737  ? 169.223 197.124 176.686 1.00 66.39  ? 2069 THR   A N    1 
ATOM   4067 C  CA   . THR   A 1 737  ? 168.845 198.512 176.954 1.00 68.31  ? 2069 THR   A CA   1 
ATOM   4068 C  C    . THR   A 1 737  ? 167.564 198.575 177.787 1.00 77.32  ? 2069 THR   A C    1 
ATOM   4069 O  O    . THR   A 1 737  ? 166.538 199.115 177.370 1.00 79.27  ? 2069 THR   A O    1 
ATOM   4070 C  CB   . THR   A 1 737  ? 168.704 199.324 175.664 1.00 65.58  ? 2069 THR   A CB   1 
ATOM   4071 O  OG1  . THR   A 1 737  ? 167.591 198.836 174.907 1.00 66.92  ? 2069 THR   A OG1  1 
ATOM   4072 C  CG2  . THR   A 1 737  ? 169.964 199.217 174.835 1.00 56.89  ? 2069 THR   A CG2  1 
ATOM   4073 N  N    . GLY   A 1 738  ? 167.641 197.988 178.978 1.00 74.78  ? 2070 GLY   A N    1 
ATOM   4074 C  CA   . GLY   A 1 738  ? 166.598 198.163 179.966 1.00 85.41  ? 2070 GLY   A CA   1 
ATOM   4075 C  C    . GLY   A 1 738  ? 165.274 197.516 179.642 1.00 98.17  ? 2070 GLY   A C    1 
ATOM   4076 O  O    . GLY   A 1 738  ? 164.250 197.923 180.196 1.00 106.21 ? 2070 GLY   A O    1 
ATOM   4077 N  N    . GLY   A 1 739  ? 165.255 196.522 178.755 1.00 90.98  ? 2071 GLY   A N    1 
ATOM   4078 C  CA   . GLY   A 1 739  ? 164.003 195.846 178.460 1.00 89.30  ? 2071 GLY   A CA   1 
ATOM   4079 C  C    . GLY   A 1 739  ? 163.456 195.091 179.655 1.00 92.45  ? 2071 GLY   A C    1 
ATOM   4080 O  O    . GLY   A 1 739  ? 162.271 195.194 179.983 1.00 92.48  ? 2071 GLY   A O    1 
ATOM   4081 N  N    . ARG   A 1 740  ? 164.315 194.323 180.327 1.00 95.16  ? 2072 ARG   A N    1 
ATOM   4082 C  CA   . ARG   A 1 740  ? 163.877 193.593 181.511 1.00 95.54  ? 2072 ARG   A CA   1 
ATOM   4083 C  C    . ARG   A 1 740  ? 163.758 194.515 182.717 1.00 101.54 ? 2072 ARG   A C    1 
ATOM   4084 O  O    . ARG   A 1 740  ? 163.080 194.183 183.696 1.00 101.48 ? 2072 ARG   A O    1 
ATOM   4085 C  CB   . ARG   A 1 740  ? 164.837 192.444 181.806 1.00 76.00  ? 2072 ARG   A CB   1 
ATOM   4086 C  CG   . ARG   A 1 740  ? 166.191 192.907 182.264 1.00 71.64  ? 2072 ARG   A CG   1 
ATOM   4087 C  CD   . ARG   A 1 740  ? 167.005 191.789 182.868 1.00 62.85  ? 2072 ARG   A CD   1 
ATOM   4088 N  NE   . ARG   A 1 740  ? 166.788 191.696 184.305 1.00 69.33  ? 2072 ARG   A NE   1 
ATOM   4089 C  CZ   . ARG   A 1 740  ? 167.714 191.323 185.174 1.00 57.92  ? 2072 ARG   A CZ   1 
ATOM   4090 N  NH1  . ARG   A 1 740  ? 168.945 191.039 184.790 1.00 50.70  ? 2072 ARG   A NH1  1 
ATOM   4091 N  NH2  . ARG   A 1 740  ? 167.403 191.253 186.464 1.00 59.66  ? 2072 ARG   A NH2  1 
ATOM   4092 N  N    . ILE   A 1 741  ? 164.415 195.675 182.665 1.00 102.26 ? 2073 ILE   A N    1 
ATOM   4093 C  CA   . ILE   A 1 741  ? 164.340 196.623 183.772 1.00 103.71 ? 2073 ILE   A CA   1 
ATOM   4094 C  C    . ILE   A 1 741  ? 162.913 197.119 183.948 1.00 110.53 ? 2073 ILE   A C    1 
ATOM   4095 O  O    . ILE   A 1 741  ? 162.392 197.177 185.069 1.00 115.10 ? 2073 ILE   A O    1 
ATOM   4096 C  CB   . ILE   A 1 741  ? 165.318 197.788 183.536 1.00 101.10 ? 2073 ILE   A CB   1 
ATOM   4097 C  CG1  . ILE   A 1 741  ? 166.758 197.317 183.723 1.00 84.62  ? 2073 ILE   A CG1  1 
ATOM   4098 C  CG2  . ILE   A 1 741  ? 165.005 198.946 184.465 1.00 106.61 ? 2073 ILE   A CG2  1 
ATOM   4099 C  CD1  . ILE   A 1 741  ? 167.014 196.688 185.050 1.00 75.55  ? 2073 ILE   A CD1  1 
ATOM   4100 N  N    . VAL   A 1 742  ? 162.256 197.471 182.849 1.00 109.16 ? 2074 VAL   A N    1 
ATOM   4101 C  CA   . VAL   A 1 742  ? 160.877 197.933 182.892 1.00 112.54 ? 2074 VAL   A CA   1 
ATOM   4102 C  C    . VAL   A 1 742  ? 159.931 196.784 182.565 1.00 115.71 ? 2074 VAL   A C    1 
ATOM   4103 O  O    . VAL   A 1 742  ? 160.347 195.628 182.488 1.00 115.85 ? 2074 VAL   A O    1 
ATOM   4104 C  CB   . VAL   A 1 742  ? 160.655 199.111 181.932 1.00 109.06 ? 2074 VAL   A CB   1 
ATOM   4105 C  CG1  . VAL   A 1 742  ? 161.521 200.290 182.335 1.00 107.46 ? 2074 VAL   A CG1  1 
ATOM   4106 C  CG2  . VAL   A 1 742  ? 160.954 198.691 180.503 1.00 105.82 ? 2074 VAL   A CG2  1 
ATOM   4107 N  N    . GLN   A 1 757  ? 166.183 181.720 191.942 1.00 168.57 ? 2089 GLN   A N    1 
ATOM   4108 C  CA   . GLN   A 1 757  ? 166.224 181.134 190.606 1.00 178.21 ? 2089 GLN   A CA   1 
ATOM   4109 C  C    . GLN   A 1 757  ? 166.188 182.208 189.526 1.00 168.11 ? 2089 GLN   A C    1 
ATOM   4110 O  O    . GLN   A 1 757  ? 165.844 183.359 189.792 1.00 163.64 ? 2089 GLN   A O    1 
ATOM   4111 C  CB   . GLN   A 1 757  ? 165.076 180.118 190.440 1.00 180.73 ? 2089 GLN   A CB   1 
ATOM   4112 C  CG   . GLN   A 1 757  ? 163.652 180.605 190.780 1.00 178.36 ? 2089 GLN   A CG   1 
ATOM   4113 C  CD   . GLN   A 1 757  ? 163.098 181.702 189.878 1.00 177.66 ? 2089 GLN   A CD   1 
ATOM   4114 O  OE1  . GLN   A 1 757  ? 163.557 181.904 188.755 1.00 178.05 ? 2089 GLN   A OE1  1 
ATOM   4115 N  NE2  . GLN   A 1 757  ? 162.105 182.423 190.382 1.00 171.60 ? 2089 GLN   A NE2  1 
ATOM   4116 N  N    . GLY   A 1 758  ? 166.548 181.822 188.306 1.00 160.91 ? 2090 GLY   A N    1 
ATOM   4117 C  CA   . GLY   A 1 758  ? 166.513 182.736 187.183 1.00 149.14 ? 2090 GLY   A CA   1 
ATOM   4118 C  C    . GLY   A 1 758  ? 166.689 182.035 185.853 1.00 147.58 ? 2090 GLY   A C    1 
ATOM   4119 O  O    . GLY   A 1 758  ? 167.583 181.198 185.700 1.00 147.12 ? 2090 GLY   A O    1 
ATOM   4120 N  N    . LYS   A 1 759  ? 165.842 182.368 184.881 1.00 148.61 ? 2091 LYS   A N    1 
ATOM   4121 C  CA   . LYS   A 1 759  ? 165.921 181.804 183.535 1.00 141.50 ? 2091 LYS   A CA   1 
ATOM   4122 C  C    . LYS   A 1 759  ? 165.719 182.942 182.541 1.00 128.73 ? 2091 LYS   A C    1 
ATOM   4123 O  O    . LYS   A 1 759  ? 164.588 183.377 182.303 1.00 121.89 ? 2091 LYS   A O    1 
ATOM   4124 C  CB   . LYS   A 1 759  ? 164.892 180.694 183.331 1.00 143.32 ? 2091 LYS   A CB   1 
ATOM   4125 N  N    . LEU   A 1 760  ? 166.818 183.418 181.962 1.00 121.62 ? 2092 LEU   A N    1 
ATOM   4126 C  CA   . LEU   A 1 760  ? 166.779 184.584 181.097 1.00 109.23 ? 2092 LEU   A CA   1 
ATOM   4127 C  C    . LEU   A 1 760  ? 166.897 184.149 179.648 1.00 110.48 ? 2092 LEU   A C    1 
ATOM   4128 O  O    . LEU   A 1 760  ? 167.980 183.713 179.228 1.00 111.31 ? 2092 LEU   A O    1 
ATOM   4129 C  CB   . LEU   A 1 760  ? 167.906 185.542 181.460 1.00 90.97  ? 2092 LEU   A CB   1 
ATOM   4130 C  CG   . LEU   A 1 760  ? 167.733 186.131 182.855 1.00 84.63  ? 2092 LEU   A CG   1 
ATOM   4131 C  CD1  . LEU   A 1 760  ? 168.927 186.962 183.228 1.00 65.68  ? 2092 LEU   A CD1  1 
ATOM   4132 C  CD2  . LEU   A 1 760  ? 166.459 186.947 182.926 1.00 101.10 ? 2092 LEU   A CD2  1 
ATOM   4133 N  N    . PRO   A 1 761  ? 165.839 184.249 178.852 1.00 116.65 ? 2093 PRO   A N    1 
ATOM   4134 C  CA   . PRO   A 1 761  ? 165.927 183.855 177.443 1.00 120.52 ? 2093 PRO   A CA   1 
ATOM   4135 C  C    . PRO   A 1 761  ? 166.694 184.884 176.630 1.00 121.64 ? 2093 PRO   A C    1 
ATOM   4136 O  O    . PRO   A 1 761  ? 167.066 185.954 177.113 1.00 121.44 ? 2093 PRO   A O    1 
ATOM   4137 C  CB   . PRO   A 1 761  ? 164.464 183.769 177.011 1.00 128.04 ? 2093 PRO   A CB   1 
ATOM   4138 C  CG   . PRO   A 1 761  ? 163.771 184.713 177.917 1.00 129.17 ? 2093 PRO   A CG   1 
ATOM   4139 C  CD   . PRO   A 1 761  ? 164.477 184.649 179.233 1.00 119.45 ? 2093 PRO   A CD   1 
ATOM   4140 N  N    . ASP   A 1 762  ? 166.919 184.543 175.366 1.00 124.66 ? 2094 ASP   A N    1 
ATOM   4141 C  CA   . ASP   A 1 762  ? 167.811 185.333 174.529 1.00 125.02 ? 2094 ASP   A CA   1 
ATOM   4142 C  C    . ASP   A 1 762  ? 167.256 186.739 174.333 1.00 118.12 ? 2094 ASP   A C    1 
ATOM   4143 O  O    . ASP   A 1 762  ? 166.054 186.897 174.079 1.00 118.28 ? 2094 ASP   A O    1 
ATOM   4144 C  CB   . ASP   A 1 762  ? 168.024 184.659 173.176 1.00 135.52 ? 2094 ASP   A CB   1 
ATOM   4145 C  CG   . ASP   A 1 762  ? 169.301 183.848 173.127 1.00 142.36 ? 2094 ASP   A CG   1 
ATOM   4146 O  OD1  . ASP   A 1 762  ? 169.667 183.376 172.032 1.00 138.92 ? 2094 ASP   A OD1  1 
ATOM   4147 O  OD2  . ASP   A 1 762  ? 169.940 183.681 174.187 1.00 131.89 ? 2094 ASP   A OD2  1 
ATOM   4148 N  N    . PRO   A 1 763  ? 168.085 187.776 174.457 1.00 110.83 ? 2095 PRO   A N    1 
ATOM   4149 C  CA   . PRO   A 1 763  ? 167.586 189.147 174.272 1.00 113.61 ? 2095 PRO   A CA   1 
ATOM   4150 C  C    . PRO   A 1 763  ? 167.006 189.407 172.894 1.00 119.20 ? 2095 PRO   A C    1 
ATOM   4151 O  O    . PRO   A 1 763  ? 166.046 190.177 172.768 1.00 114.15 ? 2095 PRO   A O    1 
ATOM   4152 C  CB   . PRO   A 1 763  ? 168.836 190.000 174.517 1.00 110.63 ? 2095 PRO   A CB   1 
ATOM   4153 C  CG   . PRO   A 1 763  ? 169.717 189.141 175.365 1.00 101.81 ? 2095 PRO   A CG   1 
ATOM   4154 C  CD   . PRO   A 1 763  ? 169.491 187.748 174.888 1.00 99.14  ? 2095 PRO   A CD   1 
ATOM   4155 N  N    . VAL   A 1 764  ? 167.566 188.794 171.852 1.00 122.06 ? 2096 VAL   A N    1 
ATOM   4156 C  CA   . VAL   A 1 764  ? 167.092 189.053 170.497 1.00 119.83 ? 2096 VAL   A CA   1 
ATOM   4157 C  C    . VAL   A 1 764  ? 165.692 188.488 170.308 1.00 126.24 ? 2096 VAL   A C    1 
ATOM   4158 O  O    . VAL   A 1 764  ? 164.881 189.036 169.552 1.00 126.99 ? 2096 VAL   A O    1 
ATOM   4159 C  CB   . VAL   A 1 764  ? 168.082 188.475 169.472 1.00 103.41 ? 2096 VAL   A CB   1 
ATOM   4160 C  CG1  . VAL   A 1 764  ? 167.557 188.655 168.059 1.00 102.40 ? 2096 VAL   A CG1  1 
ATOM   4161 C  CG2  . VAL   A 1 764  ? 169.437 189.121 169.637 1.00 92.42  ? 2096 VAL   A CG2  1 
ATOM   4162 N  N    . LYS   A 1 765  ? 165.381 187.390 171.001 1.00 124.93 ? 2097 LYS   A N    1 
ATOM   4163 C  CA   . LYS   A 1 765  ? 164.104 186.716 170.794 1.00 124.54 ? 2097 LYS   A CA   1 
ATOM   4164 C  C    . LYS   A 1 765  ? 162.926 187.623 171.131 1.00 131.29 ? 2097 LYS   A C    1 
ATOM   4165 O  O    . LYS   A 1 765  ? 161.949 187.686 170.375 1.00 136.52 ? 2097 LYS   A O    1 
ATOM   4166 C  CB   . LYS   A 1 765  ? 164.050 185.436 171.626 1.00 122.25 ? 2097 LYS   A CB   1 
ATOM   4167 N  N    . GLU   A 1 766  ? 162.994 188.337 172.254 1.00 126.67 ? 2098 GLU   A N    1 
ATOM   4168 C  CA   . GLU   A 1 766  ? 161.864 189.171 172.647 1.00 121.56 ? 2098 GLU   A CA   1 
ATOM   4169 C  C    . GLU   A 1 766  ? 162.031 190.621 172.213 1.00 125.22 ? 2098 GLU   A C    1 
ATOM   4170 O  O    . GLU   A 1 766  ? 161.197 191.154 171.474 1.00 124.44 ? 2098 GLU   A O    1 
ATOM   4171 C  CB   . GLU   A 1 766  ? 161.661 189.129 174.162 1.00 110.96 ? 2098 GLU   A CB   1 
ATOM   4172 C  CG   . GLU   A 1 766  ? 161.889 187.791 174.807 1.00 119.28 ? 2098 GLU   A CG   1 
ATOM   4173 C  CD   . GLU   A 1 766  ? 161.764 187.878 176.307 1.00 128.71 ? 2098 GLU   A CD   1 
ATOM   4174 O  OE1  . GLU   A 1 766  ? 162.559 187.241 177.016 1.00 124.80 ? 2098 GLU   A OE1  1 
ATOM   4175 O  OE2  . GLU   A 1 766  ? 160.852 188.581 176.781 1.00 132.63 ? 2098 GLU   A OE2  1 
ATOM   4176 N  N    . TYR   A 1 767  ? 163.100 191.270 172.670 1.00 125.01 ? 2099 TYR   A N    1 
ATOM   4177 C  CA   . TYR   A 1 767  ? 163.238 192.711 172.515 1.00 128.81 ? 2099 TYR   A CA   1 
ATOM   4178 C  C    . TYR   A 1 767  ? 163.601 193.130 171.099 1.00 132.73 ? 2099 TYR   A C    1 
ATOM   4179 O  O    . TYR   A 1 767  ? 163.489 194.316 170.772 1.00 135.19 ? 2099 TYR   A O    1 
ATOM   4180 C  CB   . TYR   A 1 767  ? 164.284 193.229 173.501 1.00 116.50 ? 2099 TYR   A CB   1 
ATOM   4181 C  CG   . TYR   A 1 767  ? 164.234 192.512 174.829 1.00 111.33 ? 2099 TYR   A CG   1 
ATOM   4182 C  CD1  . TYR   A 1 767  ? 165.238 191.635 175.204 1.00 108.05 ? 2099 TYR   A CD1  1 
ATOM   4183 C  CD2  . TYR   A 1 767  ? 163.177 192.710 175.705 1.00 112.36 ? 2099 TYR   A CD2  1 
ATOM   4184 C  CE1  . TYR   A 1 767  ? 165.197 190.978 176.413 1.00 105.37 ? 2099 TYR   A CE1  1 
ATOM   4185 C  CE2  . TYR   A 1 767  ? 163.127 192.056 176.918 1.00 106.71 ? 2099 TYR   A CE2  1 
ATOM   4186 C  CZ   . TYR   A 1 767  ? 164.140 191.191 177.266 1.00 101.98 ? 2099 TYR   A CZ   1 
ATOM   4187 O  OH   . TYR   A 1 767  ? 164.097 190.535 178.471 1.00 102.70 ? 2099 TYR   A OH   1 
ATOM   4188 N  N    . GLY   A 1 768  ? 164.026 192.196 170.254 1.00 127.83 ? 2100 GLY   A N    1 
ATOM   4189 C  CA   . GLY   A 1 768  ? 164.383 192.563 168.902 1.00 127.13 ? 2100 GLY   A CA   1 
ATOM   4190 C  C    . GLY   A 1 768  ? 165.610 193.432 168.802 1.00 129.86 ? 2100 GLY   A C    1 
ATOM   4191 O  O    . GLY   A 1 768  ? 165.765 194.156 167.816 1.00 138.32 ? 2100 GLY   A O    1 
ATOM   4192 N  N    . CYS   A 1 769  ? 166.486 193.386 169.801 1.00 117.01 ? 2101 CYS   A N    1 
ATOM   4193 C  CA   . CYS   A 1 769  ? 167.712 194.162 169.759 1.00 98.38  ? 2101 CYS   A CA   1 
ATOM   4194 C  C    . CYS   A 1 769  ? 168.629 193.654 168.654 1.00 95.51  ? 2101 CYS   A C    1 
ATOM   4195 O  O    . CYS   A 1 769  ? 168.488 192.536 168.153 1.00 95.13  ? 2101 CYS   A O    1 
ATOM   4196 C  CB   . CYS   A 1 769  ? 168.440 194.094 171.098 1.00 92.75  ? 2101 CYS   A CB   1 
ATOM   4197 S  SG   . CYS   A 1 769  ? 169.942 195.082 171.143 1.00 96.13  ? 2101 CYS   A SG   1 
ATOM   4198 N  N    . ALA   A 1 770  ? 169.572 194.498 168.271 1.00 90.38  ? 2102 ALA   A N    1 
ATOM   4199 C  CA   . ALA   A 1 770  ? 170.521 194.111 167.244 1.00 75.74  ? 2102 ALA   A CA   1 
ATOM   4200 C  C    . ALA   A 1 770  ? 171.374 192.957 167.755 1.00 73.46  ? 2102 ALA   A C    1 
ATOM   4201 O  O    . ALA   A 1 770  ? 171.995 193.078 168.818 1.00 72.49  ? 2102 ALA   A O    1 
ATOM   4202 C  CB   . ALA   A 1 770  ? 171.405 195.293 166.855 1.00 67.39  ? 2102 ALA   A CB   1 
ATOM   4203 N  N    . PRO   A 1 771  ? 171.413 191.828 167.054 1.00 74.20  ? 2103 PRO   A N    1 
ATOM   4204 C  CA   . PRO   A 1 771  ? 172.244 190.713 167.511 1.00 64.41  ? 2103 PRO   A CA   1 
ATOM   4205 C  C    . PRO   A 1 771  ? 173.697 191.130 167.621 1.00 48.16  ? 2103 PRO   A C    1 
ATOM   4206 O  O    . PRO   A 1 771  ? 174.260 191.733 166.707 1.00 53.36  ? 2103 PRO   A O    1 
ATOM   4207 C  CB   . PRO   A 1 771  ? 172.043 189.652 166.426 1.00 61.93  ? 2103 PRO   A CB   1 
ATOM   4208 C  CG   . PRO   A 1 771  ? 170.724 189.983 165.822 1.00 69.67  ? 2103 PRO   A CG   1 
ATOM   4209 C  CD   . PRO   A 1 771  ? 170.615 191.476 165.870 1.00 70.39  ? 2103 PRO   A CD   1 
ATOM   4210 N  N    . TRP   A 1 772  ? 174.301 190.805 168.756 1.00 37.61  ? 2104 TRP   A N    1 
ATOM   4211 C  CA   . TRP   A 1 772  ? 175.689 191.149 169.043 1.00 35.75  ? 2104 TRP   A CA   1 
ATOM   4212 C  C    . TRP   A 1 772  ? 176.387 189.889 169.524 1.00 35.27  ? 2104 TRP   A C    1 
ATOM   4213 O  O    . TRP   A 1 772  ? 176.565 189.688 170.731 1.00 37.84  ? 2104 TRP   A O    1 
ATOM   4214 C  CB   . TRP   A 1 772  ? 175.777 192.265 170.079 1.00 39.26  ? 2104 TRP   A CB   1 
ATOM   4215 C  CG   . TRP   A 1 772  ? 177.163 192.743 170.347 1.00 45.06  ? 2104 TRP   A CG   1 
ATOM   4216 C  CD1  . TRP   A 1 772  ? 178.313 192.320 169.750 1.00 46.00  ? 2104 TRP   A CD1  1 
ATOM   4217 C  CD2  . TRP   A 1 772  ? 177.546 193.749 171.284 1.00 54.24  ? 2104 TRP   A CD2  1 
ATOM   4218 N  NE1  . TRP   A 1 772  ? 179.389 193.000 170.262 1.00 47.95  ? 2104 TRP   A NE1  1 
ATOM   4219 C  CE2  . TRP   A 1 772  ? 178.942 193.884 171.207 1.00 51.85  ? 2104 TRP   A CE2  1 
ATOM   4220 C  CE3  . TRP   A 1 772  ? 176.841 194.550 172.185 1.00 54.38  ? 2104 TRP   A CE3  1 
ATOM   4221 C  CZ2  . TRP   A 1 772  ? 179.643 194.782 171.996 1.00 43.67  ? 2104 TRP   A CZ2  1 
ATOM   4222 C  CZ3  . TRP   A 1 772  ? 177.540 195.438 172.963 1.00 51.89  ? 2104 TRP   A CZ3  1 
ATOM   4223 C  CH2  . TRP   A 1 772  ? 178.925 195.548 172.866 1.00 41.80  ? 2104 TRP   A CH2  1 
ATOM   4224 N  N    . PRO   A 1 773  ? 176.789 189.015 168.608 1.00 33.36  ? 2105 PRO   A N    1 
ATOM   4225 C  CA   . PRO   A 1 773  ? 177.457 187.779 169.016 1.00 33.46  ? 2105 PRO   A CA   1 
ATOM   4226 C  C    . PRO   A 1 773  ? 178.750 188.044 169.764 1.00 37.03  ? 2105 PRO   A C    1 
ATOM   4227 O  O    . PRO   A 1 773  ? 179.280 189.154 169.783 1.00 38.93  ? 2105 PRO   A O    1 
ATOM   4228 C  CB   . PRO   A 1 773  ? 177.714 187.063 167.690 1.00 32.57  ? 2105 PRO   A CB   1 
ATOM   4229 C  CG   . PRO   A 1 773  ? 176.673 187.592 166.792 1.00 39.50  ? 2105 PRO   A CG   1 
ATOM   4230 C  CD   . PRO   A 1 773  ? 176.493 189.023 167.172 1.00 35.38  ? 2105 PRO   A CD   1 
ATOM   4231 N  N    . MET   A 1 774  ? 179.232 186.983 170.406 1.00 40.61  ? 2106 MET   A N    1 
ATOM   4232 C  CA   . MET   A 1 774  ? 180.345 186.983 171.356 1.00 46.29  ? 2106 MET   A CA   1 
ATOM   4233 C  C    . MET   A 1 774  ? 180.164 188.027 172.456 1.00 47.06  ? 2106 MET   A C    1 
ATOM   4234 O  O    . MET   A 1 774  ? 181.124 188.408 173.129 1.00 52.68  ? 2106 MET   A O    1 
ATOM   4235 C  CB   . MET   A 1 774  ? 181.703 187.111 170.653 1.00 40.91  ? 2106 MET   A CB   1 
ATOM   4236 C  CG   . MET   A 1 774  ? 182.122 188.458 170.149 1.00 42.18  ? 2106 MET   A CG   1 
ATOM   4237 S  SD   . MET   A 1 774  ? 183.627 188.285 169.179 1.00 53.93  ? 2106 MET   A SD   1 
ATOM   4238 C  CE   . MET   A 1 774  ? 184.492 187.042 170.125 1.00 50.21  ? 2106 MET   A CE   1 
ATOM   4239 N  N    . VAL   A 1 775  ? 178.930 188.484 172.657 1.00 45.57  ? 2107 VAL   A N    1 
ATOM   4240 C  CA   . VAL   A 1 775  ? 178.499 189.075 173.914 1.00 44.23  ? 2107 VAL   A CA   1 
ATOM   4241 C  C    . VAL   A 1 775  ? 177.302 188.336 174.488 1.00 43.85  ? 2107 VAL   A C    1 
ATOM   4242 O  O    . VAL   A 1 775  ? 177.171 188.227 175.704 1.00 54.01  ? 2107 VAL   A O    1 
ATOM   4243 C  CB   . VAL   A 1 775  ? 178.194 190.578 173.782 1.00 43.54  ? 2107 VAL   A CB   1 
ATOM   4244 C  CG1  . VAL   A 1 775  ? 177.650 191.110 175.071 1.00 31.96  ? 2107 VAL   A CG1  1 
ATOM   4245 C  CG2  . VAL   A 1 775  ? 179.433 191.298 173.488 1.00 48.16  ? 2107 VAL   A CG2  1 
ATOM   4246 N  N    . GLU   A 1 776  ? 176.405 187.839 173.640 1.00 37.93  ? 2108 GLU   A N    1 
ATOM   4247 C  CA   . GLU   A 1 776  ? 175.460 186.857 174.143 1.00 34.00  ? 2108 GLU   A CA   1 
ATOM   4248 C  C    . GLU   A 1 776  ? 176.186 185.649 174.707 1.00 35.52  ? 2108 GLU   A C    1 
ATOM   4249 O  O    . GLU   A 1 776  ? 175.753 185.087 175.719 1.00 39.90  ? 2108 GLU   A O    1 
ATOM   4250 C  CB   . GLU   A 1 776  ? 174.489 186.454 173.044 1.00 38.11  ? 2108 GLU   A CB   1 
ATOM   4251 C  CG   . GLU   A 1 776  ? 174.068 187.615 172.177 1.00 43.23  ? 2108 GLU   A CG   1 
ATOM   4252 C  CD   . GLU   A 1 776  ? 173.002 187.237 171.177 1.00 53.17  ? 2108 GLU   A CD   1 
ATOM   4253 O  OE1  . GLU   A 1 776  ? 172.072 188.040 170.966 1.00 52.83  ? 2108 GLU   A OE1  1 
ATOM   4254 O  OE2  . GLU   A 1 776  ? 173.096 186.138 170.597 1.00 60.75  ? 2108 GLU   A OE2  1 
ATOM   4255 N  N    . LYS   A 1 777  ? 177.314 185.276 174.112 1.00 37.58  ? 2109 LYS   A N    1 
ATOM   4256 C  CA   . LYS   A 1 777  ? 178.135 184.222 174.686 1.00 47.32  ? 2109 LYS   A CA   1 
ATOM   4257 C  C    . LYS   A 1 777  ? 178.695 184.618 176.045 1.00 47.60  ? 2109 LYS   A C    1 
ATOM   4258 O  O    . LYS   A 1 777  ? 178.729 183.793 176.959 1.00 56.19  ? 2109 LYS   A O    1 
ATOM   4259 C  CB   . LYS   A 1 777  ? 179.271 183.856 173.739 1.00 57.00  ? 2109 LYS   A CB   1 
ATOM   4260 C  CG   . LYS   A 1 777  ? 180.241 182.850 174.331 1.00 56.77  ? 2109 LYS   A CG   1 
ATOM   4261 C  CD   . LYS   A 1 777  ? 181.504 182.711 173.505 1.00 67.29  ? 2109 LYS   A CD   1 
ATOM   4262 C  CE   . LYS   A 1 777  ? 181.208 182.696 172.014 1.00 71.89  ? 2109 LYS   A CE   1 
ATOM   4263 N  NZ   . LYS   A 1 777  ? 180.127 181.737 171.649 1.00 71.48  ? 2109 LYS   A NZ   1 
ATOM   4264 N  N    . LEU   A 1 778  ? 179.147 185.861 176.208 1.00 39.54  ? 2110 LEU   A N    1 
ATOM   4265 C  CA   . LEU   A 1 778  ? 179.669 186.274 177.510 1.00 35.47  ? 2110 LEU   A CA   1 
ATOM   4266 C  C    . LEU   A 1 778  ? 178.570 186.386 178.556 1.00 28.37  ? 2110 LEU   A C    1 
ATOM   4267 O  O    . LEU   A 1 778  ? 178.781 186.036 179.718 1.00 37.30  ? 2110 LEU   A O    1 
ATOM   4268 C  CB   . LEU   A 1 778  ? 180.433 187.585 177.391 1.00 36.71  ? 2110 LEU   A CB   1 
ATOM   4269 C  CG   . LEU   A 1 778  ? 181.120 187.954 178.695 1.00 29.17  ? 2110 LEU   A CG   1 
ATOM   4270 C  CD1  . LEU   A 1 778  ? 182.400 187.204 178.825 1.00 28.61  ? 2110 LEU   A CD1  1 
ATOM   4271 C  CD2  . LEU   A 1 778  ? 181.406 189.424 178.693 1.00 28.39  ? 2110 LEU   A CD2  1 
ATOM   4272 N  N    . ILE   A 1 779  ? 177.399 186.882 178.173 1.00 25.99  ? 2111 ILE   A N    1 
ATOM   4273 C  CA   . ILE   A 1 779  ? 176.277 186.890 179.099 1.00 24.77  ? 2111 ILE   A CA   1 
ATOM   4274 C  C    . ILE   A 1 779  ? 175.958 185.477 179.545 1.00 38.55  ? 2111 ILE   A C    1 
ATOM   4275 O  O    . ILE   A 1 779  ? 175.738 185.227 180.733 1.00 57.92  ? 2111 ILE   A O    1 
ATOM   4276 C  CB   . ILE   A 1 779  ? 175.048 187.563 178.468 1.00 24.20  ? 2111 ILE   A CB   1 
ATOM   4277 C  CG1  . ILE   A 1 779  ? 175.326 189.026 178.170 1.00 30.44  ? 2111 ILE   A CG1  1 
ATOM   4278 C  CG2  . ILE   A 1 779  ? 173.847 187.430 179.364 1.00 30.29  ? 2111 ILE   A CG2  1 
ATOM   4279 C  CD1  . ILE   A 1 779  ? 174.256 189.662 177.325 1.00 43.34  ? 2111 ILE   A CD1  1 
ATOM   4280 N  N    . LYS   A 1 780  ? 175.947 184.523 178.617 1.00 35.74  ? 2112 LYS   A N    1 
ATOM   4281 C  CA   A LYS   A 1 780  ? 175.599 183.153 178.983 0.62 40.39  ? 2112 LYS   A CA   1 
ATOM   4282 C  CA   B LYS   A 1 780  ? 175.591 183.162 178.999 0.38 40.31  ? 2112 LYS   A CA   1 
ATOM   4283 C  C    . LYS   A 1 780  ? 176.716 182.483 179.771 1.00 38.09  ? 2112 LYS   A C    1 
ATOM   4284 O  O    . LYS   A 1 780  ? 176.462 181.583 180.575 1.00 47.21  ? 2112 LYS   A O    1 
ATOM   4285 C  CB   A LYS   A 1 780  ? 175.264 182.336 177.738 0.62 42.48  ? 2112 LYS   A CB   1 
ATOM   4286 C  CB   B LYS   A 1 780  ? 175.202 182.360 177.762 0.38 40.04  ? 2112 LYS   A CB   1 
ATOM   4287 C  CG   A LYS   A 1 780  ? 173.777 182.094 177.548 0.62 46.43  ? 2112 LYS   A CG   1 
ATOM   4288 C  CG   B LYS   A 1 780  ? 173.697 182.171 177.623 0.38 44.02  ? 2112 LYS   A CG   1 
ATOM   4289 C  CD   A LYS   A 1 780  ? 173.467 181.297 176.286 0.62 42.50  ? 2112 LYS   A CD   1 
ATOM   4290 C  CD   B LYS   A 1 780  ? 172.933 183.200 178.461 0.38 43.09  ? 2112 LYS   A CD   1 
ATOM   4291 C  CE   A LYS   A 1 780  ? 174.662 181.177 175.358 0.62 43.48  ? 2112 LYS   A CE   1 
ATOM   4292 C  CE   B LYS   A 1 780  ? 171.503 183.396 177.984 0.38 54.12  ? 2112 LYS   A CE   1 
ATOM   4293 N  NZ   A LYS   A 1 780  ? 174.259 181.368 173.939 0.62 49.05  ? 2112 LYS   A NZ   1 
ATOM   4294 N  NZ   B LYS   A 1 780  ? 171.325 184.701 177.288 0.38 59.47  ? 2112 LYS   A NZ   1 
ATOM   4295 N  N    . GLN   A 1 781  ? 177.961 182.888 179.540 1.00 30.90  ? 2113 GLN   A N    1 
ATOM   4296 C  CA   . GLN   A 1 781  ? 179.068 182.272 180.259 1.00 38.47  ? 2113 GLN   A CA   1 
ATOM   4297 C  C    . GLN   A 1 781  ? 179.173 182.801 181.686 1.00 48.00  ? 2113 GLN   A C    1 
ATOM   4298 O  O    . GLN   A 1 781  ? 179.395 182.025 182.620 1.00 57.82  ? 2113 GLN   A O    1 
ATOM   4299 C  CB   . GLN   A 1 781  ? 180.368 182.487 179.493 1.00 43.04  ? 2113 GLN   A CB   1 
ATOM   4300 C  CG   . GLN   A 1 781  ? 181.613 182.253 180.306 1.00 50.46  ? 2113 GLN   A CG   1 
ATOM   4301 C  CD   . GLN   A 1 781  ? 182.791 181.850 179.448 1.00 62.47  ? 2113 GLN   A CD   1 
ATOM   4302 O  OE1  . GLN   A 1 781  ? 183.093 182.497 178.447 1.00 59.05  ? 2113 GLN   A OE1  1 
ATOM   4303 N  NE2  . GLN   A 1 781  ? 183.465 180.776 179.835 1.00 57.92  ? 2113 GLN   A NE2  1 
ATOM   4304 N  N    . CYS   A 1 782  ? 179.023 184.114 181.883 1.00 46.44  ? 2114 CYS   A N    1 
ATOM   4305 C  CA   . CYS   A 1 782  ? 178.984 184.650 183.240 1.00 32.55  ? 2114 CYS   A CA   1 
ATOM   4306 C  C    . CYS   A 1 782  ? 177.744 184.171 183.970 1.00 38.50  ? 2114 CYS   A C    1 
ATOM   4307 O  O    . CYS   A 1 782  ? 177.830 183.612 185.067 1.00 59.45  ? 2114 CYS   A O    1 
ATOM   4308 C  CB   . CYS   A 1 782  ? 179.013 186.178 183.222 1.00 27.32  ? 2114 CYS   A CB   1 
ATOM   4309 S  SG   . CYS   A 1 782  ? 180.523 186.933 182.600 1.00 42.71  ? 2114 CYS   A SG   1 
ATOM   4310 N  N    . LEU   A 1 783  ? 176.583 184.340 183.349 1.00 32.53  ? 2115 LEU   A N    1 
ATOM   4311 C  CA   . LEU   A 1 783  ? 175.295 184.091 183.983 1.00 42.92  ? 2115 LEU   A CA   1 
ATOM   4312 C  C    . LEU   A 1 783  ? 175.024 182.584 183.991 1.00 60.95  ? 2115 LEU   A C    1 
ATOM   4313 O  O    . LEU   A 1 783  ? 174.235 182.044 183.214 1.00 68.39  ? 2115 LEU   A O    1 
ATOM   4314 C  CB   . LEU   A 1 783  ? 174.232 184.876 183.236 1.00 33.32  ? 2115 LEU   A CB   1 
ATOM   4315 C  CG   . LEU   A 1 783  ? 172.792 185.029 183.673 1.00 41.87  ? 2115 LEU   A CG   1 
ATOM   4316 C  CD1  . LEU   A 1 783  ? 172.334 186.324 183.086 1.00 36.18  ? 2115 LEU   A CD1  1 
ATOM   4317 C  CD2  . LEU   A 1 783  ? 171.910 183.908 183.177 1.00 52.81  ? 2115 LEU   A CD2  1 
ATOM   4318 N  N    . LYS   A 1 784  ? 175.705 181.894 184.898 1.00 67.52  ? 2116 LYS   A N    1 
ATOM   4319 C  CA   . LYS   A 1 784  ? 175.587 180.450 185.025 1.00 63.64  ? 2116 LYS   A CA   1 
ATOM   4320 C  C    . LYS   A 1 784  ? 174.837 180.087 186.300 1.00 74.10  ? 2116 LYS   A C    1 
ATOM   4321 O  O    . LYS   A 1 784  ? 174.813 180.840 187.273 1.00 83.13  ? 2116 LYS   A O    1 
ATOM   4322 C  CB   . LYS   A 1 784  ? 176.967 179.791 185.025 1.00 57.82  ? 2116 LYS   A CB   1 
ATOM   4323 C  CG   . LYS   A 1 784  ? 177.515 179.498 183.652 1.00 58.52  ? 2116 LYS   A CG   1 
ATOM   4324 C  CD   . LYS   A 1 784  ? 178.720 178.583 183.733 1.00 68.96  ? 2116 LYS   A CD   1 
ATOM   4325 C  CE   . LYS   A 1 784  ? 179.438 178.499 182.399 1.00 69.59  ? 2116 LYS   A CE   1 
ATOM   4326 N  NZ   . LYS   A 1 784  ? 178.729 177.619 181.432 1.00 56.78  ? 2116 LYS   A NZ   1 
ATOM   4327 N  N    . GLU   A 1 785  ? 174.228 178.904 186.290 1.00 71.22  ? 2117 GLU   A N    1 
ATOM   4328 C  CA   . GLU   A 1 785  ? 173.491 178.427 187.450 1.00 79.77  ? 2117 GLU   A CA   1 
ATOM   4329 C  C    . GLU   A 1 785  ? 174.390 178.034 188.608 1.00 78.47  ? 2117 GLU   A C    1 
ATOM   4330 O  O    . GLU   A 1 785  ? 173.923 178.007 189.751 1.00 84.46  ? 2117 GLU   A O    1 
ATOM   4331 C  CB   . GLU   A 1 785  ? 172.607 177.235 187.071 1.00 92.35  ? 2117 GLU   A CB   1 
ATOM   4332 C  CG   . GLU   A 1 785  ? 171.214 177.611 186.594 1.00 106.31 ? 2117 GLU   A CG   1 
ATOM   4333 C  CD   . GLU   A 1 785  ? 170.550 178.666 187.462 1.00 107.79 ? 2117 GLU   A CD   1 
ATOM   4334 O  OE1  . GLU   A 1 785  ? 169.895 179.568 186.902 1.00 112.18 ? 2117 GLU   A OE1  1 
ATOM   4335 O  OE2  . GLU   A 1 785  ? 170.652 178.575 188.704 1.00 101.68 ? 2117 GLU   A OE2  1 
ATOM   4336 N  N    . ASN   A 1 786  ? 175.656 177.737 188.353 1.00 79.12  ? 2118 ASN   A N    1 
ATOM   4337 C  CA   . ASN   A 1 786  ? 176.563 177.432 189.442 1.00 82.67  ? 2118 ASN   A CA   1 
ATOM   4338 C  C    . ASN   A 1 786  ? 177.847 178.238 189.326 1.00 84.13  ? 2118 ASN   A C    1 
ATOM   4339 O  O    . ASN   A 1 786  ? 178.296 178.558 188.223 1.00 87.05  ? 2118 ASN   A O    1 
ATOM   4340 C  CB   . ASN   A 1 786  ? 176.828 175.913 189.527 1.00 86.57  ? 2118 ASN   A CB   1 
ATOM   4341 C  CG   . ASN   A 1 786  ? 177.840 175.384 188.505 1.00 89.70  ? 2118 ASN   A CG   1 
ATOM   4342 O  OD1  . ASN   A 1 786  ? 178.501 176.118 187.784 1.00 87.57  ? 2118 ASN   A OD1  1 
ATOM   4343 N  ND2  . ASN   A 1 786  ? 177.953 174.063 188.455 1.00 92.35  ? 2118 ASN   A ND2  1 
ATOM   4344 N  N    . PRO   A 1 787  ? 178.421 178.640 190.461 1.00 84.05  ? 2119 PRO   A N    1 
ATOM   4345 C  CA   . PRO   A 1 787  ? 179.593 179.522 190.423 1.00 82.44  ? 2119 PRO   A CA   1 
ATOM   4346 C  C    . PRO   A 1 787  ? 180.898 178.811 190.123 1.00 83.21  ? 2119 PRO   A C    1 
ATOM   4347 O  O    . PRO   A 1 787  ? 181.962 179.430 190.253 1.00 76.75  ? 2119 PRO   A O    1 
ATOM   4348 C  CB   . PRO   A 1 787  ? 179.616 180.119 191.834 1.00 81.03  ? 2119 PRO   A CB   1 
ATOM   4349 C  CG   . PRO   A 1 787  ? 178.215 180.017 192.314 1.00 86.25  ? 2119 PRO   A CG   1 
ATOM   4350 C  CD   . PRO   A 1 787  ? 177.702 178.736 191.739 1.00 88.28  ? 2119 PRO   A CD   1 
ATOM   4351 N  N    . GLN   A 1 788  ? 180.861 177.537 189.748 1.00 90.53  ? 2120 GLN   A N    1 
ATOM   4352 C  CA   . GLN   A 1 788  ? 182.097 176.776 189.671 1.00 99.99  ? 2120 GLN   A CA   1 
ATOM   4353 C  C    . GLN   A 1 788  ? 182.926 177.113 188.438 1.00 102.64 ? 2120 GLN   A C    1 
ATOM   4354 O  O    . GLN   A 1 788  ? 184.153 177.207 188.546 1.00 109.76 ? 2120 GLN   A O    1 
ATOM   4355 C  CB   . GLN   A 1 788  ? 181.789 175.281 189.714 1.00 104.20 ? 2120 GLN   A CB   1 
ATOM   4356 N  N    . GLU   A 1 789  ? 182.302 177.298 187.273 1.00 94.22  ? 2121 GLU   A N    1 
ATOM   4357 C  CA   . GLU   A 1 789  ? 183.056 177.593 186.059 1.00 89.57  ? 2121 GLU   A CA   1 
ATOM   4358 C  C    . GLU   A 1 789  ? 182.657 178.886 185.366 1.00 87.49  ? 2121 GLU   A C    1 
ATOM   4359 O  O    . GLU   A 1 789  ? 183.141 179.132 184.256 1.00 87.01  ? 2121 GLU   A O    1 
ATOM   4360 C  CB   . GLU   A 1 789  ? 182.948 176.445 185.038 1.00 91.80  ? 2121 GLU   A CB   1 
ATOM   4361 N  N    . ARG   A 1 790  ? 181.793 179.703 185.955 1.00 84.05  ? 2122 ARG   A N    1 
ATOM   4362 C  CA   . ARG   A 1 790  ? 181.558 181.028 185.407 1.00 73.66  ? 2122 ARG   A CA   1 
ATOM   4363 C  C    . ARG   A 1 790  ? 182.838 181.849 185.534 1.00 73.06  ? 2122 ARG   A C    1 
ATOM   4364 O  O    . ARG   A 1 790  ? 183.596 181.670 186.492 1.00 78.46  ? 2122 ARG   A O    1 
ATOM   4365 C  CB   . ARG   A 1 790  ? 180.398 181.709 186.130 1.00 61.13  ? 2122 ARG   A CB   1 
ATOM   4366 C  CG   . ARG   A 1 790  ? 180.752 182.183 187.499 1.00 64.22  ? 2122 ARG   A CG   1 
ATOM   4367 C  CD   . ARG   A 1 790  ? 179.667 183.019 188.101 1.00 62.35  ? 2122 ARG   A CD   1 
ATOM   4368 N  NE   . ARG   A 1 790  ? 178.378 182.351 188.014 1.00 66.82  ? 2122 ARG   A NE   1 
ATOM   4369 C  CZ   . ARG   A 1 790  ? 177.401 182.517 188.891 1.00 67.74  ? 2122 ARG   A CZ   1 
ATOM   4370 N  NH1  . ARG   A 1 790  ? 177.556 183.281 189.958 1.00 63.82  ? 2122 ARG   A NH1  1 
ATOM   4371 N  NH2  . ARG   A 1 790  ? 176.251 181.881 188.709 1.00 75.76  ? 2122 ARG   A NH2  1 
ATOM   4372 N  N    . PRO   A 1 791  ? 183.125 182.729 184.582 1.00 66.68  ? 2123 PRO   A N    1 
ATOM   4373 C  CA   . PRO   A 1 791  ? 184.456 183.337 184.522 1.00 69.19  ? 2123 PRO   A CA   1 
ATOM   4374 C  C    . PRO   A 1 791  ? 184.733 184.245 185.706 1.00 66.41  ? 2123 PRO   A C    1 
ATOM   4375 O  O    . PRO   A 1 791  ? 183.827 184.833 186.297 1.00 61.94  ? 2123 PRO   A O    1 
ATOM   4376 C  CB   . PRO   A 1 791  ? 184.416 184.137 183.217 1.00 56.54  ? 2123 PRO   A CB   1 
ATOM   4377 C  CG   . PRO   A 1 791  ? 182.986 184.467 183.044 1.00 48.85  ? 2123 PRO   A CG   1 
ATOM   4378 C  CD   . PRO   A 1 791  ? 182.212 183.309 183.586 1.00 52.05  ? 2123 PRO   A CD   1 
ATOM   4379 N  N    . THR   A 1 792  ? 186.007 184.339 186.061 1.00 63.57  ? 2124 THR   A N    1 
ATOM   4380 C  CA   . THR   A 1 792  ? 186.420 185.365 186.998 1.00 58.38  ? 2124 THR   A CA   1 
ATOM   4381 C  C    . THR   A 1 792  ? 186.502 186.710 186.284 1.00 64.66  ? 2124 THR   A C    1 
ATOM   4382 O  O    . THR   A 1 792  ? 186.727 186.794 185.073 1.00 64.19  ? 2124 THR   A O    1 
ATOM   4383 C  CB   . THR   A 1 792  ? 187.763 185.006 187.634 1.00 62.31  ? 2124 THR   A CB   1 
ATOM   4384 O  OG1  . THR   A 1 792  ? 187.980 185.823 188.789 1.00 68.18  ? 2124 THR   A OG1  1 
ATOM   4385 C  CG2  . THR   A 1 792  ? 188.902 185.209 186.652 1.00 61.69  ? 2124 THR   A CG2  1 
ATOM   4386 N  N    . SER   A 1 793  ? 186.291 187.781 187.043 1.00 62.80  ? 2125 SER   A N    1 
ATOM   4387 C  CA   . SER   A 1 793  ? 186.332 189.099 186.428 1.00 55.47  ? 2125 SER   A CA   1 
ATOM   4388 C  C    . SER   A 1 793  ? 187.739 189.533 186.059 1.00 56.96  ? 2125 SER   A C    1 
ATOM   4389 O  O    . SER   A 1 793  ? 187.898 190.567 185.407 1.00 53.23  ? 2125 SER   A O    1 
ATOM   4390 C  CB   . SER   A 1 793  ? 185.681 190.121 187.340 1.00 53.35  ? 2125 SER   A CB   1 
ATOM   4391 O  OG   . SER   A 1 793  ? 184.309 189.814 187.491 1.00 55.23  ? 2125 SER   A OG   1 
ATOM   4392 N  N    . ALA   A 1 794  ? 188.758 188.783 186.466 1.00 62.10  ? 2126 ALA   A N    1 
ATOM   4393 C  CA   . ALA   A 1 794  ? 190.076 189.002 185.893 1.00 60.55  ? 2126 ALA   A CA   1 
ATOM   4394 C  C    . ALA   A 1 794  ? 190.079 188.694 184.405 1.00 58.61  ? 2126 ALA   A C    1 
ATOM   4395 O  O    . ALA   A 1 794  ? 190.868 189.279 183.656 1.00 56.14  ? 2126 ALA   A O    1 
ATOM   4396 C  CB   . ALA   A 1 794  ? 191.118 188.150 186.615 1.00 54.81  ? 2126 ALA   A CB   1 
ATOM   4397 N  N    . GLN   A 1 795  ? 189.211 187.781 183.960 1.00 55.46  ? 2127 GLN   A N    1 
ATOM   4398 C  CA   . GLN   A 1 795  ? 189.128 187.430 182.551 1.00 55.45  ? 2127 GLN   A CA   1 
ATOM   4399 C  C    . GLN   A 1 795  ? 187.878 187.944 181.855 1.00 53.55  ? 2127 GLN   A C    1 
ATOM   4400 O  O    . GLN   A 1 795  ? 187.852 187.963 180.624 1.00 54.60  ? 2127 GLN   A O    1 
ATOM   4401 C  CB   . GLN   A 1 795  ? 189.210 185.908 182.360 1.00 62.45  ? 2127 GLN   A CB   1 
ATOM   4402 C  CG   . GLN   A 1 795  ? 188.077 185.111 182.972 1.00 62.14  ? 2127 GLN   A CG   1 
ATOM   4403 C  CD   . GLN   A 1 795  ? 188.532 183.756 183.480 1.00 74.69  ? 2127 GLN   A CD   1 
ATOM   4404 O  OE1  . GLN   A 1 795  ? 189.706 183.404 183.375 1.00 89.79  ? 2127 GLN   A OE1  1 
ATOM   4405 N  NE2  . GLN   A 1 795  ? 187.602 182.987 184.026 1.00 66.22  ? 2127 GLN   A NE2  1 
ATOM   4406 N  N    . VAL   A 1 796  ? 186.850 188.364 182.592 1.00 47.12  ? 2128 VAL   A N    1 
ATOM   4407 C  CA   . VAL   A 1 796  ? 185.717 189.016 181.937 1.00 40.01  ? 2128 VAL   A CA   1 
ATOM   4408 C  C    . VAL   A 1 796  ? 186.166 190.317 181.281 1.00 31.99  ? 2128 VAL   A C    1 
ATOM   4409 O  O    . VAL   A 1 796  ? 185.757 190.645 180.160 1.00 34.51  ? 2128 VAL   A O    1 
ATOM   4410 C  CB   . VAL   A 1 796  ? 184.574 189.249 182.936 1.00 36.80  ? 2128 VAL   A CB   1 
ATOM   4411 C  CG1  . VAL   A 1 796  ? 183.581 190.197 182.356 1.00 26.06  ? 2128 VAL   A CG1  1 
ATOM   4412 C  CG2  . VAL   A 1 796  ? 183.898 187.950 183.263 1.00 45.43  ? 2128 VAL   A CG2  1 
ATOM   4413 N  N    . PHE   A 1 797  ? 187.023 191.074 181.964 1.00 36.14  ? 2129 PHE   A N    1 
ATOM   4414 C  CA   . PHE   A 1 797  ? 187.647 192.234 181.340 1.00 37.21  ? 2129 PHE   A CA   1 
ATOM   4415 C  C    . PHE   A 1 797  ? 188.415 191.845 180.089 1.00 48.59  ? 2129 PHE   A C    1 
ATOM   4416 O  O    . PHE   A 1 797  ? 188.298 192.505 179.051 1.00 57.82  ? 2129 PHE   A O    1 
ATOM   4417 C  CB   . PHE   A 1 797  ? 188.599 192.904 182.317 1.00 48.72  ? 2129 PHE   A CB   1 
ATOM   4418 C  CG   . PHE   A 1 797  ? 189.340 194.061 181.733 1.00 47.24  ? 2129 PHE   A CG   1 
ATOM   4419 C  CD1  . PHE   A 1 797  ? 188.699 195.022 180.995 1.00 37.85  ? 2129 PHE   A CD1  1 
ATOM   4420 C  CD2  . PHE   A 1 797  ? 190.705 194.135 181.860 1.00 51.82  ? 2129 PHE   A CD2  1 
ATOM   4421 C  CE1  . PHE   A 1 797  ? 189.408 196.069 180.462 1.00 44.67  ? 2129 PHE   A CE1  1 
ATOM   4422 C  CE2  . PHE   A 1 797  ? 191.411 195.178 181.318 1.00 52.21  ? 2129 PHE   A CE2  1 
ATOM   4423 C  CZ   . PHE   A 1 797  ? 190.760 196.142 180.615 1.00 50.52  ? 2129 PHE   A CZ   1 
ATOM   4424 N  N    . ASP   A 1 798  ? 189.223 190.788 180.171 1.00 48.95  ? 2130 ASP   A N    1 
ATOM   4425 C  CA   . ASP   A 1 798  ? 190.030 190.396 179.022 1.00 53.41  ? 2130 ASP   A CA   1 
ATOM   4426 C  C    . ASP   A 1 798  ? 189.150 190.020 177.843 1.00 44.04  ? 2130 ASP   A C    1 
ATOM   4427 O  O    . ASP   A 1 798  ? 189.493 190.293 176.689 1.00 41.94  ? 2130 ASP   A O    1 
ATOM   4428 C  CB   . ASP   A 1 798  ? 190.948 189.238 179.400 1.00 61.52  ? 2130 ASP   A CB   1 
ATOM   4429 C  CG   . ASP   A 1 798  ? 192.029 189.651 180.370 1.00 71.80  ? 2130 ASP   A CG   1 
ATOM   4430 O  OD1  . ASP   A 1 798  ? 192.435 190.830 180.339 1.00 72.39  ? 2130 ASP   A OD1  1 
ATOM   4431 O  OD2  . ASP   A 1 798  ? 192.477 188.798 181.163 1.00 81.20  ? 2130 ASP   A OD2  1 
ATOM   4432 N  N    . ILE   A 1 799  ? 188.012 189.386 178.115 1.00 39.29  ? 2131 ILE   A N    1 
ATOM   4433 C  CA   . ILE   A 1 799  ? 187.084 189.037 177.047 1.00 35.21  ? 2131 ILE   A CA   1 
ATOM   4434 C  C    . ILE   A 1 799  ? 186.487 190.295 176.432 1.00 35.59  ? 2131 ILE   A C    1 
ATOM   4435 O  O    . ILE   A 1 799  ? 186.423 190.433 175.206 1.00 43.01  ? 2131 ILE   A O    1 
ATOM   4436 C  CB   . ILE   A 1 799  ? 185.986 188.100 177.572 1.00 30.39  ? 2131 ILE   A CB   1 
ATOM   4437 C  CG1  . ILE   A 1 799  ? 186.513 186.672 177.657 1.00 33.45  ? 2131 ILE   A CG1  1 
ATOM   4438 C  CG2  . ILE   A 1 799  ? 184.794 188.147 176.646 1.00 28.18  ? 2131 ILE   A CG2  1 
ATOM   4439 C  CD1  . ILE   A 1 799  ? 185.671 185.773 178.513 1.00 36.14  ? 2131 ILE   A CD1  1 
ATOM   4440 N  N    . LEU   A 1 800  ? 186.041 191.236 177.271 1.00 31.12  ? 2132 LEU   A N    1 
ATOM   4441 C  CA   . LEU   A 1 800  ? 185.420 192.448 176.739 1.00 25.28  ? 2132 LEU   A CA   1 
ATOM   4442 C  C    . LEU   A 1 800  ? 186.410 193.364 176.045 1.00 31.70  ? 2132 LEU   A C    1 
ATOM   4443 O  O    . LEU   A 1 800  ? 185.993 194.252 175.298 1.00 35.91  ? 2132 LEU   A O    1 
ATOM   4444 C  CB   . LEU   A 1 800  ? 184.715 193.229 177.838 1.00 22.68  ? 2132 LEU   A CB   1 
ATOM   4445 C  CG   . LEU   A 1 800  ? 183.352 192.703 178.236 1.00 21.06  ? 2132 LEU   A CG   1 
ATOM   4446 C  CD1  . LEU   A 1 800  ? 183.104 193.090 179.650 1.00 25.98  ? 2132 LEU   A CD1  1 
ATOM   4447 C  CD2  . LEU   A 1 800  ? 182.304 193.305 177.349 1.00 16.42  ? 2132 LEU   A CD2  1 
ATOM   4448 N  N    . ASN   A 1 801  ? 187.704 193.180 176.280 1.00 29.89  ? 2133 ASN   A N    1 
ATOM   4449 C  CA   . ASN   A 1 801  ? 188.721 194.015 175.653 1.00 37.60  ? 2133 ASN   A CA   1 
ATOM   4450 C  C    . ASN   A 1 801  ? 189.165 193.347 174.354 1.00 49.24  ? 2133 ASN   A C    1 
ATOM   4451 O  O    . ASN   A 1 801  ? 190.216 192.710 174.270 1.00 55.39  ? 2133 ASN   A O    1 
ATOM   4452 C  CB   . ASN   A 1 801  ? 189.879 194.229 176.615 1.00 34.22  ? 2133 ASN   A CB   1 
ATOM   4453 C  CG   . ASN   A 1 801  ? 191.030 194.955 175.982 1.00 51.13  ? 2133 ASN   A CG   1 
ATOM   4454 O  OD1  . ASN   A 1 801  ? 190.875 196.057 175.461 1.00 53.10  ? 2133 ASN   A OD1  1 
ATOM   4455 N  ND2  . ASN   A 1 801  ? 192.203 194.348 176.033 1.00 64.50  ? 2133 ASN   A ND2  1 
ATOM   4456 N  N    . SER   A 1 802  ? 188.336 193.495 173.317 1.00 45.67  ? 2134 SER   A N    1 
ATOM   4457 C  CA   . SER   A 1 802  ? 188.659 192.909 172.020 1.00 45.39  ? 2134 SER   A CA   1 
ATOM   4458 C  C    . SER   A 1 802  ? 187.818 193.540 170.916 1.00 45.33  ? 2134 SER   A C    1 
ATOM   4459 O  O    . SER   A 1 802  ? 186.581 193.545 170.981 1.00 44.03  ? 2134 SER   A O    1 
ATOM   4460 C  CB   . SER   A 1 802  ? 188.459 191.392 172.040 1.00 47.10  ? 2134 SER   A CB   1 
ATOM   4461 O  OG   . SER   A 1 802  ? 187.088 191.061 172.081 1.00 49.90  ? 2134 SER   A OG   1 
ATOM   4462 N  N    . ALA   A 1 803  ? 188.499 194.045 169.885 1.00 45.55  ? 2135 ALA   A N    1 
ATOM   4463 C  CA   . ALA   A 1 803  ? 187.809 194.605 168.732 1.00 49.82  ? 2135 ALA   A CA   1 
ATOM   4464 C  C    . ALA   A 1 803  ? 186.985 193.567 167.984 1.00 57.61  ? 2135 ALA   A C    1 
ATOM   4465 O  O    . ALA   A 1 803  ? 186.009 193.935 167.325 1.00 62.45  ? 2135 ALA   A O    1 
ATOM   4466 C  CB   . ALA   A 1 803  ? 188.811 195.253 167.782 1.00 51.69  ? 2135 ALA   A CB   1 
ATOM   4467 N  N    . GLU   A 1 804  ? 187.355 192.286 168.061 1.00 52.21  ? 2136 GLU   A N    1 
ATOM   4468 C  CA   . GLU   A 1 804  ? 186.488 191.245 167.525 1.00 44.04  ? 2136 GLU   A CA   1 
ATOM   4469 C  C    . GLU   A 1 804  ? 185.128 191.298 168.195 1.00 48.29  ? 2136 GLU   A C    1 
ATOM   4470 O  O    . GLU   A 1 804  ? 184.093 191.204 167.531 1.00 51.32  ? 2136 GLU   A O    1 
ATOM   4471 C  CB   . GLU   A 1 804  ? 187.109 189.871 167.741 1.00 45.96  ? 2136 GLU   A CB   1 
ATOM   4472 C  CG   . GLU   A 1 804  ? 188.343 189.603 166.938 1.00 57.45  ? 2136 GLU   A CG   1 
ATOM   4473 C  CD   . GLU   A 1 804  ? 189.587 189.658 167.788 1.00 60.55  ? 2136 GLU   A CD   1 
ATOM   4474 O  OE1  . GLU   A 1 804  ? 190.306 188.642 167.883 1.00 61.87  ? 2136 GLU   A OE1  1 
ATOM   4475 O  OE2  . GLU   A 1 804  ? 189.850 190.728 168.366 1.00 57.55  ? 2136 GLU   A OE2  1 
ATOM   4476 N  N    . LEU   A 1 805  ? 185.117 191.451 169.516 1.00 45.75  ? 2137 LEU   A N    1 
ATOM   4477 C  CA   . LEU   A 1 805  ? 183.868 191.661 170.235 1.00 44.14  ? 2137 LEU   A CA   1 
ATOM   4478 C  C    . LEU   A 1 805  ? 183.182 192.941 169.797 1.00 43.52  ? 2137 LEU   A C    1 
ATOM   4479 O  O    . LEU   A 1 805  ? 181.952 192.982 169.681 1.00 42.50  ? 2137 LEU   A O    1 
ATOM   4480 C  CB   . LEU   A 1 805  ? 184.142 191.660 171.738 1.00 42.52  ? 2137 LEU   A CB   1 
ATOM   4481 C  CG   . LEU   A 1 805  ? 183.010 191.406 172.715 1.00 37.84  ? 2137 LEU   A CG   1 
ATOM   4482 C  CD1  . LEU   A 1 805  ? 183.574 191.013 174.032 1.00 37.38  ? 2137 LEU   A CD1  1 
ATOM   4483 C  CD2  . LEU   A 1 805  ? 182.331 192.730 172.895 1.00 35.68  ? 2137 LEU   A CD2  1 
ATOM   4484 N  N    . VAL   A 1 806  ? 183.954 194.002 169.573 1.00 40.90  ? 2138 VAL   A N    1 
ATOM   4485 C  CA   . VAL   A 1 806  ? 183.325 195.279 169.253 1.00 37.77  ? 2138 VAL   A CA   1 
ATOM   4486 C  C    . VAL   A 1 806  ? 182.596 195.213 167.915 1.00 52.42  ? 2138 VAL   A C    1 
ATOM   4487 O  O    . VAL   A 1 806  ? 181.462 195.690 167.792 1.00 62.00  ? 2138 VAL   A O    1 
ATOM   4488 C  CB   . VAL   A 1 806  ? 184.359 196.414 169.265 1.00 36.22  ? 2138 VAL   A CB   1 
ATOM   4489 C  CG1  . VAL   A 1 806  ? 183.650 197.741 169.164 1.00 37.24  ? 2138 VAL   A CG1  1 
ATOM   4490 C  CG2  . VAL   A 1 806  ? 185.189 196.350 170.514 1.00 41.56  ? 2138 VAL   A CG2  1 
ATOM   4491 N  N    . CYS   A 1 807  ? 183.219 194.610 166.898 1.00 47.68  ? 2139 CYS   A N    1 
ATOM   4492 C  CA   . CYS   A 1 807  ? 182.799 194.798 165.514 1.00 38.21  ? 2139 CYS   A CA   1 
ATOM   4493 C  C    . CYS   A 1 807  ? 182.182 193.578 164.849 1.00 42.95  ? 2139 CYS   A C    1 
ATOM   4494 O  O    . CYS   A 1 807  ? 181.590 193.726 163.778 1.00 50.99  ? 2139 CYS   A O    1 
ATOM   4495 C  CB   . CYS   A 1 807  ? 183.982 195.273 164.671 1.00 39.37  ? 2139 CYS   A CB   1 
ATOM   4496 S  SG   . CYS   A 1 807  ? 184.575 196.898 165.127 1.00 54.69  ? 2139 CYS   A SG   1 
ATOM   4497 N  N    . LEU   A 1 808  ? 182.276 192.389 165.432 1.00 41.93  ? 2140 LEU   A N    1 
ATOM   4498 C  CA   . LEU   A 1 808  ? 181.685 191.216 164.787 1.00 38.81  ? 2140 LEU   A CA   1 
ATOM   4499 C  C    . LEU   A 1 808  ? 180.176 191.377 164.858 1.00 36.61  ? 2140 LEU   A C    1 
ATOM   4500 O  O    . LEU   A 1 808  ? 179.523 190.952 165.807 1.00 34.98  ? 2140 LEU   A O    1 
ATOM   4501 C  CB   . LEU   A 1 808  ? 182.157 189.930 165.450 1.00 39.46  ? 2140 LEU   A CB   1 
ATOM   4502 C  CG   . LEU   A 1 808  ? 182.068 188.630 164.652 1.00 27.11  ? 2140 LEU   A CG   1 
ATOM   4503 C  CD1  . LEU   A 1 808  ? 182.942 187.572 165.272 1.00 24.98  ? 2140 LEU   A CD1  1 
ATOM   4504 C  CD2  . LEU   A 1 808  ? 180.649 188.130 164.575 1.00 27.69  ? 2140 LEU   A CD2  1 
ATOM   4505 N  N    . THR   A 1 809  ? 179.618 191.993 163.818 1.00 36.77  ? 2141 THR   A N    1 
ATOM   4506 C  CA   . THR   A 1 809  ? 178.213 192.374 163.842 1.00 37.97  ? 2141 THR   A CA   1 
ATOM   4507 C  C    . THR   A 1 809  ? 177.301 191.157 163.871 1.00 33.79  ? 2141 THR   A C    1 
ATOM   4508 O  O    . THR   A 1 809  ? 176.281 191.161 164.566 1.00 39.95  ? 2141 THR   A O    1 
ATOM   4509 C  CB   . THR   A 1 809  ? 177.890 193.249 162.634 1.00 50.29  ? 2141 THR   A CB   1 
ATOM   4510 O  OG1  . THR   A 1 809  ? 178.643 194.463 162.705 1.00 58.91  ? 2141 THR   A OG1  1 
ATOM   4511 C  CG2  . THR   A 1 809  ? 176.416 193.590 162.605 1.00 48.34  ? 2141 THR   A CG2  1 
ATOM   4512 N  N    . ARG   A 1 810  ? 177.640 190.111 163.123 1.00 31.51  ? 2142 ARG   A N    1 
ATOM   4513 C  CA   . ARG   A 1 810  ? 176.755 188.961 163.025 1.00 32.60  ? 2142 ARG   A CA   1 
ATOM   4514 C  C    . ARG   A 1 810  ? 177.568 187.721 162.701 1.00 34.57  ? 2142 ARG   A C    1 
ATOM   4515 O  O    . ARG   A 1 810  ? 178.675 187.807 162.175 1.00 41.65  ? 2142 ARG   A O    1 
ATOM   4516 C  CB   . ARG   A 1 810  ? 175.685 189.178 161.953 1.00 33.60  ? 2142 ARG   A CB   1 
ATOM   4517 C  CG   . ARG   A 1 810  ? 174.542 188.203 162.010 1.00 36.00  ? 2142 ARG   A CG   1 
ATOM   4518 C  CD   . ARG   A 1 810  ? 173.356 188.837 162.669 1.00 45.60  ? 2142 ARG   A CD   1 
ATOM   4519 N  NE   . ARG   A 1 810  ? 173.069 190.124 162.057 1.00 49.55  ? 2142 ARG   A NE   1 
ATOM   4520 C  CZ   . ARG   A 1 810  ? 172.249 190.288 161.031 1.00 64.15  ? 2142 ARG   A CZ   1 
ATOM   4521 N  NH1  . ARG   A 1 810  ? 171.602 189.266 160.496 1.00 73.17  ? 2142 ARG   A NH1  1 
ATOM   4522 N  NH2  . ARG   A 1 810  ? 172.070 191.507 160.533 1.00 67.83  ? 2142 ARG   A NH2  1 
ATOM   4523 N  N    . ARG   A 1 811  ? 176.997 186.560 163.002 1.00 30.12  ? 2143 ARG   A N    1 
ATOM   4524 C  CA   . ARG   A 1 811  ? 177.574 185.297 162.566 1.00 31.46  ? 2143 ARG   A CA   1 
ATOM   4525 C  C    . ARG   A 1 811  ? 176.435 184.323 162.327 1.00 36.71  ? 2143 ARG   A C    1 
ATOM   4526 O  O    . ARG   A 1 811  ? 175.504 184.250 163.133 1.00 33.29  ? 2143 ARG   A O    1 
ATOM   4527 C  CB   . ARG   A 1 811  ? 178.554 184.736 163.596 1.00 29.19  ? 2143 ARG   A CB   1 
ATOM   4528 C  CG   . ARG   A 1 811  ? 178.711 183.237 163.532 1.00 35.62  ? 2143 ARG   A CG   1 
ATOM   4529 C  CD   . ARG   A 1 811  ? 179.477 182.718 164.720 1.00 44.13  ? 2143 ARG   A CD   1 
ATOM   4530 N  NE   . ARG   A 1 811  ? 180.877 183.116 164.680 1.00 64.71  ? 2143 ARG   A NE   1 
ATOM   4531 C  CZ   . ARG   A 1 811  ? 181.894 182.268 164.638 1.00 72.10  ? 2143 ARG   A CZ   1 
ATOM   4532 N  NH1  . ARG   A 1 811  ? 181.702 180.960 164.610 1.00 65.61  ? 2143 ARG   A NH1  1 
ATOM   4533 N  NH2  . ARG   A 1 811  ? 183.136 182.744 164.628 1.00 80.45  ? 2143 ARG   A NH2  1 
ATOM   4534 N  N    . ILE   A 1 812  ? 176.500 183.593 161.218 1.00 45.41  ? 2144 ILE   A N    1 
ATOM   4535 C  CA   . ILE   A 1 812  ? 175.428 182.700 160.803 1.00 46.61  ? 2144 ILE   A CA   1 
ATOM   4536 C  C    . ILE   A 1 812  ? 176.026 181.339 160.476 1.00 59.09  ? 2144 ILE   A C    1 
ATOM   4537 O  O    . ILE   A 1 812  ? 177.093 181.249 159.861 1.00 56.55  ? 2144 ILE   A O    1 
ATOM   4538 C  CB   . ILE   A 1 812  ? 174.673 183.273 159.591 1.00 37.26  ? 2144 ILE   A CB   1 
ATOM   4539 C  CG1  . ILE   A 1 812  ? 173.656 184.303 160.050 1.00 41.38  ? 2144 ILE   A CG1  1 
ATOM   4540 C  CG2  . ILE   A 1 812  ? 173.927 182.185 158.873 1.00 47.08  ? 2144 ILE   A CG2  1 
ATOM   4541 C  CD1  . ILE   A 1 812  ? 172.913 184.941 158.919 1.00 49.91  ? 2144 ILE   A CD1  1 
ATOM   4542 N  N    . LEU   A 1 813  ? 175.349 180.280 160.907 1.00 64.74  ? 2145 LEU   A N    1 
ATOM   4543 C  CA   . LEU   A 1 813  ? 175.757 178.917 160.604 1.00 70.10  ? 2145 LEU   A CA   1 
ATOM   4544 C  C    . LEU   A 1 813  ? 174.808 178.324 159.573 1.00 76.64  ? 2145 LEU   A C    1 
ATOM   4545 O  O    . LEU   A 1 813  ? 173.589 178.325 159.767 1.00 70.98  ? 2145 LEU   A O    1 
ATOM   4546 C  CB   . LEU   A 1 813  ? 175.781 178.052 161.864 1.00 75.78  ? 2145 LEU   A CB   1 
ATOM   4547 C  CG   . LEU   A 1 813  ? 177.024 178.107 162.757 1.00 78.28  ? 2145 LEU   A CG   1 
ATOM   4548 C  CD1  . LEU   A 1 813  ? 178.232 177.587 162.012 1.00 69.26  ? 2145 LEU   A CD1  1 
ATOM   4549 C  CD2  . LEU   A 1 813  ? 177.291 179.498 163.286 1.00 71.12  ? 2145 LEU   A CD2  1 
ATOM   4550 N  N    . LEU   A 1 814  ? 175.370 177.829 158.481 1.00 77.03  ? 2146 LEU   A N    1 
ATOM   4551 C  CA   . LEU   A 1 814  ? 174.602 177.217 157.414 1.00 71.05  ? 2146 LEU   A CA   1 
ATOM   4552 C  C    . LEU   A 1 814  ? 174.178 175.804 157.802 1.00 85.01  ? 2146 LEU   A C    1 
ATOM   4553 O  O    . LEU   A 1 814  ? 174.731 175.218 158.734 1.00 102.99 ? 2146 LEU   A O    1 
ATOM   4554 C  CB   . LEU   A 1 814  ? 175.433 177.195 156.138 1.00 72.44  ? 2146 LEU   A CB   1 
ATOM   4555 C  CG   . LEU   A 1 814  ? 175.805 178.578 155.615 1.00 63.35  ? 2146 LEU   A CG   1 
ATOM   4556 C  CD1  . LEU   A 1 814  ? 176.751 178.450 154.457 1.00 68.38  ? 2146 LEU   A CD1  1 
ATOM   4557 C  CD2  . LEU   A 1 814  ? 174.563 179.328 155.203 1.00 54.83  ? 2146 LEU   A CD2  1 
ATOM   4558 N  N    . PRO   A 1 815  ? 173.186 175.238 157.113 1.00 83.99  ? 2147 PRO   A N    1 
ATOM   4559 C  CA   . PRO   A 1 815  ? 172.798 173.850 157.385 1.00 92.15  ? 2147 PRO   A CA   1 
ATOM   4560 C  C    . PRO   A 1 815  ? 173.974 172.892 157.251 1.00 95.08  ? 2147 PRO   A C    1 
ATOM   4561 O  O    . PRO   A 1 815  ? 174.938 173.154 156.532 1.00 92.37  ? 2147 PRO   A O    1 
ATOM   4562 C  CB   . PRO   A 1 815  ? 171.722 173.574 156.333 1.00 86.78  ? 2147 PRO   A CB   1 
ATOM   4563 C  CG   . PRO   A 1 815  ? 171.104 174.895 156.122 1.00 87.82  ? 2147 PRO   A CG   1 
ATOM   4564 C  CD   . PRO   A 1 815  ? 172.225 175.895 156.213 1.00 81.15  ? 2147 PRO   A CD   1 
ATOM   4565 N  N    . LYS   A 1 816  ? 173.876 171.774 157.966 1.00 100.20 ? 2148 LYS   A N    1 
ATOM   4566 C  CA   . LYS   A 1 816  ? 175.018 170.892 158.160 1.00 101.04 ? 2148 LYS   A CA   1 
ATOM   4567 C  C    . LYS   A 1 816  ? 175.476 170.272 156.849 1.00 102.72 ? 2148 LYS   A C    1 
ATOM   4568 O  O    . LYS   A 1 816  ? 174.663 169.917 155.991 1.00 105.24 ? 2148 LYS   A O    1 
ATOM   4569 C  CB   . LYS   A 1 816  ? 174.670 169.792 159.160 1.00 97.70  ? 2148 LYS   A CB   1 
ATOM   4570 N  N    . ASN   A 1 817  ? 176.796 170.148 156.706 1.00 98.07  ? 2149 ASN   A N    1 
ATOM   4571 C  CA   . ASN   A 1 817  ? 177.422 169.496 155.557 1.00 99.80  ? 2149 ASN   A CA   1 
ATOM   4572 C  C    . ASN   A 1 817  ? 176.990 170.147 154.245 1.00 98.01  ? 2149 ASN   A C    1 
ATOM   4573 O  O    . ASN   A 1 817  ? 176.516 169.484 153.320 1.00 90.11  ? 2149 ASN   A O    1 
ATOM   4574 C  CB   . ASN   A 1 817  ? 177.123 167.996 155.555 1.00 108.00 ? 2149 ASN   A CB   1 
ATOM   4575 C  CG   . ASN   A 1 817  ? 177.820 167.265 156.682 1.00 107.54 ? 2149 ASN   A CG   1 
ATOM   4576 O  OD1  . ASN   A 1 817  ? 178.742 167.794 157.303 1.00 101.71 ? 2149 ASN   A OD1  1 
ATOM   4577 N  ND2  . ASN   A 1 817  ? 177.382 166.043 156.956 1.00 109.61 ? 2149 ASN   A ND2  1 
ATOM   4578 N  N    . VAL   A 1 818  ? 177.150 171.466 154.175 1.00 96.64  ? 2150 VAL   A N    1 
ATOM   4579 C  CA   . VAL   A 1 818  ? 176.908 172.234 152.962 1.00 86.87  ? 2150 VAL   A CA   1 
ATOM   4580 C  C    . VAL   A 1 818  ? 178.189 172.973 152.616 1.00 80.45  ? 2150 VAL   A C    1 
ATOM   4581 O  O    . VAL   A 1 818  ? 178.715 173.728 153.440 1.00 87.29  ? 2150 VAL   A O    1 
ATOM   4582 C  CB   . VAL   A 1 818  ? 175.743 173.226 153.125 1.00 80.40  ? 2150 VAL   A CB   1 
ATOM   4583 C  CG1  . VAL   A 1 818  ? 175.710 174.180 151.959 1.00 71.80  ? 2150 VAL   A CG1  1 
ATOM   4584 C  CG2  . VAL   A 1 818  ? 174.433 172.481 153.232 1.00 87.19  ? 2150 VAL   A CG2  1 
ATOM   4585 N  N    . ILE   A 1 819  ? 178.686 172.759 151.413 1.00 76.20  ? 2151 ILE   A N    1 
ATOM   4586 C  CA   . ILE   A 1 819  ? 179.925 173.378 150.968 1.00 76.68  ? 2151 ILE   A CA   1 
ATOM   4587 C  C    . ILE   A 1 819  ? 179.598 174.465 149.962 1.00 83.35  ? 2151 ILE   A C    1 
ATOM   4588 O  O    . ILE   A 1 819  ? 178.957 174.225 148.933 1.00 85.34  ? 2151 ILE   A O    1 
ATOM   4589 C  CB   . ILE   A 1 819  ? 180.900 172.344 150.374 1.00 83.81  ? 2151 ILE   A CB   1 
ATOM   4590 C  CG1  . ILE   A 1 819  ? 181.232 171.287 151.417 1.00 92.86  ? 2151 ILE   A CG1  1 
ATOM   4591 C  CG2  . ILE   A 1 819  ? 182.171 173.022 149.911 1.00 78.30  ? 2151 ILE   A CG2  1 
ATOM   4592 C  CD1  . ILE   A 1 819  ? 181.897 171.863 152.632 1.00 84.13  ? 2151 ILE   A CD1  1 
ATOM   4593 N  N    . VAL   A 1 820  ? 180.036 175.680 150.275 1.00 82.68  ? 2152 VAL   A N    1 
ATOM   4594 C  CA   . VAL   A 1 820  ? 179.835 176.844 149.423 1.00 74.69  ? 2152 VAL   A CA   1 
ATOM   4595 C  C    . VAL   A 1 820  ? 181.172 177.546 149.245 1.00 65.27  ? 2152 VAL   A C    1 
ATOM   4596 O  O    . VAL   A 1 820  ? 181.894 177.791 150.215 1.00 66.73  ? 2152 VAL   A O    1 
ATOM   4597 C  CB   . VAL   A 1 820  ? 178.767 177.781 150.016 1.00 62.20  ? 2152 VAL   A CB   1 
ATOM   4598 C  CG1  . VAL   A 1 820  ? 177.444 177.070 150.080 1.00 72.88  ? 2152 VAL   A CG1  1 
ATOM   4599 C  CG2  . VAL   A 1 820  ? 179.159 178.155 151.412 1.00 49.53  ? 2152 VAL   A CG2  1 
ATOM   4600 N  N    . GLU   A 1 821  ? 181.514 177.846 147.994 1.00 61.00  ? 2153 GLU   A N    1 
ATOM   4601 C  CA   . GLU   A 1 821  ? 182.784 178.479 147.676 1.00 63.98  ? 2153 GLU   A CA   1 
ATOM   4602 C  C    . GLU   A 1 821  ? 182.647 179.793 146.928 1.00 70.94  ? 2153 GLU   A C    1 
ATOM   4603 O  O    . GLU   A 1 821  ? 183.654 180.482 146.743 1.00 73.23  ? 2153 GLU   A O    1 
ATOM   4604 C  CB   . GLU   A 1 821  ? 183.666 177.525 146.856 1.00 69.85  ? 2153 GLU   A CB   1 
ATOM   4605 C  CG   . GLU   A 1 821  ? 183.187 177.299 145.436 1.00 69.09  ? 2153 GLU   A CG   1 
ATOM   4606 C  CD   . GLU   A 1 821  ? 182.129 176.218 145.352 1.00 74.92  ? 2153 GLU   A CD   1 
ATOM   4607 O  OE1  . GLU   A 1 821  ? 181.068 176.376 145.988 1.00 71.79  ? 2153 GLU   A OE1  1 
ATOM   4608 O  OE2  . GLU   A 1 821  ? 182.362 175.203 144.665 1.00 72.39  ? 2153 GLU   A OE2  1 
ATOM   4609 N  N    . CYS   A 1 822  ? 181.445 180.153 146.492 1.00 67.84  ? 2154 CYS   A N    1 
ATOM   4610 C  CA   . CYS   A 1 822  ? 181.192 181.412 145.810 1.00 51.40  ? 2154 CYS   A CA   1 
ATOM   4611 C  C    . CYS   A 1 822  ? 179.872 181.993 146.287 1.00 43.09  ? 2154 CYS   A C    1 
ATOM   4612 O  O    . CYS   A 1 822  ? 178.904 181.257 146.495 1.00 47.24  ? 2154 CYS   A O    1 
ATOM   4613 C  CB   . CYS   A 1 822  ? 181.184 181.191 144.308 1.00 51.29  ? 2154 CYS   A CB   1 
ATOM   4614 S  SG   . CYS   A 1 822  ? 179.685 180.411 143.722 1.00 66.21  ? 2154 CYS   A SG   1 
ATOM   4615 N  N    . MET   A 1 823  ? 179.829 183.312 146.443 1.00 37.11  ? 2155 MET   A N    1 
ATOM   4616 C  CA   . MET   A 1 823  ? 178.683 183.962 147.055 1.00 30.42  ? 2155 MET   A CA   1 
ATOM   4617 C  C    . MET   A 1 823  ? 178.590 185.393 146.552 1.00 41.10  ? 2155 MET   A C    1 
ATOM   4618 O  O    . MET   A 1 823  ? 179.600 186.019 146.225 1.00 51.66  ? 2155 MET   A O    1 
ATOM   4619 C  CB   . MET   A 1 823  ? 178.791 183.919 148.583 1.00 25.59  ? 2155 MET   A CB   1 
ATOM   4620 C  CG   . MET   A 1 823  ? 178.123 185.059 149.312 1.00 36.23  ? 2155 MET   A CG   1 
ATOM   4621 S  SD   . MET   A 1 823  ? 178.424 185.013 151.079 1.00 36.94  ? 2155 MET   A SD   1 
ATOM   4622 C  CE   . MET   A 1 823  ? 180.202 185.058 151.072 1.00 39.42  ? 2155 MET   A CE   1 
ATOM   4623 N  N    . VAL   A 1 824  ? 177.364 185.892 146.468 1.00 32.87  ? 2156 VAL   A N    1 
ATOM   4624 C  CA   . VAL   A 1 824  ? 177.099 187.256 146.040 1.00 29.98  ? 2156 VAL   A CA   1 
ATOM   4625 C  C    . VAL   A 1 824  ? 176.075 187.857 146.986 1.00 37.74  ? 2156 VAL   A C    1 
ATOM   4626 O  O    . VAL   A 1 824  ? 175.246 187.140 147.553 1.00 47.11  ? 2156 VAL   A O    1 
ATOM   4627 C  CB   . VAL   A 1 824  ? 176.594 187.301 144.589 1.00 33.53  ? 2156 VAL   A CB   1 
ATOM   4628 C  CG1  . VAL   A 1 824  ? 175.258 186.618 144.485 1.00 40.33  ? 2156 VAL   A CG1  1 
ATOM   4629 C  CG2  . VAL   A 1 824  ? 176.496 188.724 144.104 1.00 40.40  ? 2156 VAL   A CG2  1 
ATOM   4630 N  N    . ALA   A 1 825  ? 176.147 189.165 147.182 1.00 42.03  ? 2157 ALA   A N    1 
ATOM   4631 C  CA   . ALA   A 1 825  ? 175.160 189.866 147.982 1.00 50.35  ? 2157 ALA   A CA   1 
ATOM   4632 C  C    . ALA   A 1 825  ? 174.085 190.454 147.079 1.00 56.46  ? 2157 ALA   A C    1 
ATOM   4633 O  O    . ALA   A 1 825  ? 174.134 190.338 145.856 1.00 61.72  ? 2157 ALA   A O    1 
ATOM   4634 C  CB   . ALA   A 1 825  ? 175.821 190.963 148.814 1.00 45.71  ? 2157 ALA   A CB   1 
ATOM   4635 N  N    . THR   A 1 826  ? 173.095 191.082 147.700 1.00 56.69  ? 2158 THR   A N    1 
ATOM   4636 C  CA   . THR   A 1 826  ? 172.034 191.775 146.984 1.00 73.25  ? 2158 THR   A CA   1 
ATOM   4637 C  C    . THR   A 1 826  ? 172.211 193.275 147.148 1.00 88.37  ? 2158 THR   A C    1 
ATOM   4638 O  O    . THR   A 1 826  ? 172.424 193.761 148.263 1.00 93.21  ? 2158 THR   A O    1 
ATOM   4639 C  CB   . THR   A 1 826  ? 170.655 191.348 147.485 1.00 75.92  ? 2158 THR   A CB   1 
ATOM   4640 O  OG1  . THR   A 1 826  ? 170.486 189.942 147.279 1.00 77.48  ? 2158 THR   A OG1  1 
ATOM   4641 C  CG2  . THR   A 1 826  ? 169.560 192.101 146.752 1.00 82.34  ? 2158 THR   A CG2  1 
ATOM   4642 N  N    . HIS   A 1 827  ? 172.141 194.003 146.035 1.00 97.92  ? 2159 HIS   A N    1 
ATOM   4643 C  CA   . HIS   A 1 827  ? 172.219 195.463 146.057 1.00 105.86 ? 2159 HIS   A CA   1 
ATOM   4644 C  C    . HIS   A 1 827  ? 170.806 196.040 146.173 1.00 110.02 ? 2159 HIS   A C    1 
ATOM   4645 O  O    . HIS   A 1 827  ? 170.290 196.716 145.281 1.00 104.11 ? 2159 HIS   A O    1 
ATOM   4646 C  CB   . HIS   A 1 827  ? 172.944 195.973 144.819 1.00 107.28 ? 2159 HIS   A CB   1 
ATOM   4647 C  CG   . HIS   A 1 827  ? 173.537 197.337 144.983 1.00 119.85 ? 2159 HIS   A CG   1 
ATOM   4648 N  ND1  . HIS   A 1 827  ? 173.933 198.109 143.912 1.00 118.66 ? 2159 HIS   A ND1  1 
ATOM   4649 C  CD2  . HIS   A 1 827  ? 173.805 198.066 146.092 1.00 126.23 ? 2159 HIS   A CD2  1 
ATOM   4650 C  CE1  . HIS   A 1 827  ? 174.417 199.256 144.353 1.00 122.11 ? 2159 HIS   A CE1  1 
ATOM   4651 N  NE2  . HIS   A 1 827  ? 174.351 199.255 145.673 1.00 129.86 ? 2159 HIS   A NE2  1 
ATOM   4652 N  N    . HIS   A 1 828  ? 170.187 195.755 147.317 1.00 111.67 ? 2160 HIS   A N    1 
ATOM   4653 C  CA   . HIS   A 1 828  ? 168.846 196.237 147.651 1.00 111.29 ? 2160 HIS   A CA   1 
ATOM   4654 C  C    . HIS   A 1 828  ? 167.808 195.848 146.602 1.00 110.99 ? 2160 HIS   A C    1 
ATOM   4655 O  O    . HIS   A 1 828  ? 166.608 196.047 146.798 1.00 107.39 ? 2160 HIS   A O    1 
ATOM   4656 C  CB   . HIS   A 1 828  ? 168.859 197.755 147.834 1.00 109.66 ? 2160 HIS   A CB   1 
ATOM   4657 C  CG   . HIS   A 1 828  ? 170.154 198.285 148.362 1.00 105.97 ? 2160 HIS   A CG   1 
ATOM   4658 N  ND1  . HIS   A 1 828  ? 170.604 198.015 149.636 1.00 105.30 ? 2160 HIS   A ND1  1 
ATOM   4659 C  CD2  . HIS   A 1 828  ? 171.102 199.059 147.784 1.00 111.99 ? 2160 HIS   A CD2  1 
ATOM   4660 C  CE1  . HIS   A 1 828  ? 171.771 198.606 149.822 1.00 107.47 ? 2160 HIS   A CE1  1 
ATOM   4661 N  NE2  . HIS   A 1 828  ? 172.096 199.246 148.713 1.00 109.99 ? 2160 HIS   A NE2  1 
ATOM   4662 N  N    . ASN   A 1 832  ? 165.412 193.412 153.253 1.00 100.86 ? 2164 ASN   A N    1 
ATOM   4663 C  CA   . ASN   A 1 832  ? 166.173 194.439 152.552 1.00 108.87 ? 2164 ASN   A CA   1 
ATOM   4664 C  C    . ASN   A 1 832  ? 167.595 193.973 152.278 1.00 110.05 ? 2164 ASN   A C    1 
ATOM   4665 O  O    . ASN   A 1 832  ? 168.325 194.602 151.515 1.00 112.53 ? 2164 ASN   A O    1 
ATOM   4666 C  CB   . ASN   A 1 832  ? 166.194 195.741 153.357 1.00 105.88 ? 2164 ASN   A CB   1 
ATOM   4667 N  N    . ALA   A 1 833  ? 167.986 192.872 152.910 1.00 106.17 ? 2165 ALA   A N    1 
ATOM   4668 C  CA   . ALA   A 1 833  ? 169.304 192.283 152.724 1.00 98.05  ? 2165 ALA   A CA   1 
ATOM   4669 C  C    . ALA   A 1 833  ? 169.149 190.821 152.339 1.00 94.25  ? 2165 ALA   A C    1 
ATOM   4670 O  O    . ALA   A 1 833  ? 168.301 190.116 152.893 1.00 99.75  ? 2165 ALA   A O    1 
ATOM   4671 C  CB   . ALA   A 1 833  ? 170.149 192.416 153.990 1.00 87.81  ? 2165 ALA   A CB   1 
ATOM   4672 N  N    . SER   A 1 834  ? 169.963 190.371 151.388 1.00 78.17  ? 2166 SER   A N    1 
ATOM   4673 C  CA   . SER   A 1 834  ? 169.888 189.003 150.904 1.00 73.85  ? 2166 SER   A CA   1 
ATOM   4674 C  C    . SER   A 1 834  ? 171.243 188.594 150.351 1.00 63.68  ? 2166 SER   A C    1 
ATOM   4675 O  O    . SER   A 1 834  ? 172.044 189.441 149.950 1.00 64.29  ? 2166 SER   A O    1 
ATOM   4676 C  CB   . SER   A 1 834  ? 168.807 188.856 149.834 1.00 80.56  ? 2166 SER   A CB   1 
ATOM   4677 O  OG   . SER   A 1 834  ? 167.527 189.117 150.375 1.00 91.86  ? 2166 SER   A OG   1 
ATOM   4678 N  N    . ILE   A 1 835  ? 171.493 187.287 150.334 1.00 57.09  ? 2167 ILE   A N    1 
ATOM   4679 C  CA   . ILE   A 1 835  ? 172.735 186.720 149.824 1.00 45.75  ? 2167 ILE   A CA   1 
ATOM   4680 C  C    . ILE   A 1 835  ? 172.401 185.456 149.042 1.00 52.12  ? 2167 ILE   A C    1 
ATOM   4681 O  O    . ILE   A 1 835  ? 171.448 184.748 149.372 1.00 64.72  ? 2167 ILE   A O    1 
ATOM   4682 C  CB   . ILE   A 1 835  ? 173.730 186.433 150.967 1.00 33.73  ? 2167 ILE   A CB   1 
ATOM   4683 C  CG1  . ILE   A 1 835  ? 174.133 187.724 151.660 1.00 38.21  ? 2167 ILE   A CG1  1 
ATOM   4684 C  CG2  . ILE   A 1 835  ? 174.968 185.774 150.470 1.00 34.46  ? 2167 ILE   A CG2  1 
ATOM   4685 C  CD1  . ILE   A 1 835  ? 174.893 187.495 152.923 1.00 41.65  ? 2167 ILE   A CD1  1 
ATOM   4686 N  N    . TRP   A 1 836  ? 173.155 185.197 147.977 1.00 45.42  ? 2168 TRP   A N    1 
ATOM   4687 C  CA   . TRP   A 1 836  ? 173.004 183.999 147.165 1.00 40.84  ? 2168 TRP   A CA   1 
ATOM   4688 C  C    . TRP   A 1 836  ? 174.323 183.248 147.160 1.00 40.65  ? 2168 TRP   A C    1 
ATOM   4689 O  O    . TRP   A 1 836  ? 175.364 183.828 146.845 1.00 42.94  ? 2168 TRP   A O    1 
ATOM   4690 C  CB   . TRP   A 1 836  ? 172.597 184.346 145.737 1.00 40.91  ? 2168 TRP   A CB   1 
ATOM   4691 C  CG   . TRP   A 1 836  ? 171.357 185.158 145.648 1.00 48.12  ? 2168 TRP   A CG   1 
ATOM   4692 C  CD1  . TRP   A 1 836  ? 171.126 186.358 146.233 1.00 47.29  ? 2168 TRP   A CD1  1 
ATOM   4693 C  CD2  . TRP   A 1 836  ? 170.179 184.840 144.908 1.00 65.16  ? 2168 TRP   A CD2  1 
ATOM   4694 N  NE1  . TRP   A 1 836  ? 169.874 186.807 145.918 1.00 60.67  ? 2168 TRP   A NE1  1 
ATOM   4695 C  CE2  . TRP   A 1 836  ? 169.269 185.890 145.103 1.00 70.23  ? 2168 TRP   A CE2  1 
ATOM   4696 C  CE3  . TRP   A 1 836  ? 169.802 183.766 144.103 1.00 73.29  ? 2168 TRP   A CE3  1 
ATOM   4697 C  CZ2  . TRP   A 1 836  ? 168.005 185.899 144.527 1.00 74.54  ? 2168 TRP   A CZ2  1 
ATOM   4698 C  CZ3  . TRP   A 1 836  ? 168.549 183.776 143.532 1.00 82.11  ? 2168 TRP   A CZ3  1 
ATOM   4699 C  CH2  . TRP   A 1 836  ? 167.664 184.835 143.746 1.00 78.40  ? 2168 TRP   A CH2  1 
ATOM   4700 N  N    . LEU   A 1 837  ? 174.279 181.968 147.504 1.00 41.31  ? 2169 LEU   A N    1 
ATOM   4701 C  CA   . LEU   A 1 837  ? 175.469 181.140 147.611 1.00 42.36  ? 2169 LEU   A CA   1 
ATOM   4702 C  C    . LEU   A 1 837  ? 175.457 180.052 146.547 1.00 58.58  ? 2169 LEU   A C    1 
ATOM   4703 O  O    . LEU   A 1 837  ? 174.402 179.532 146.178 1.00 65.67  ? 2169 LEU   A O    1 
ATOM   4704 C  CB   . LEU   A 1 837  ? 175.578 180.479 148.988 1.00 41.01  ? 2169 LEU   A CB   1 
ATOM   4705 C  CG   . LEU   A 1 837  ? 176.050 181.286 150.194 1.00 40.66  ? 2169 LEU   A CG   1 
ATOM   4706 C  CD1  . LEU   A 1 837  ? 174.991 182.255 150.624 1.00 36.36  ? 2169 LEU   A CD1  1 
ATOM   4707 C  CD2  . LEU   A 1 837  ? 176.406 180.372 151.330 1.00 43.80  ? 2169 LEU   A CD2  1 
ATOM   4708 N  N    . GLY   A 1 838  ? 176.646 179.705 146.067 1.00 56.73  ? 2170 GLY   A N    1 
ATOM   4709 C  CA   . GLY   A 1 838  ? 176.783 178.588 145.158 1.00 57.68  ? 2170 GLY   A CA   1 
ATOM   4710 C  C    . GLY   A 1 838  ? 177.247 177.343 145.882 1.00 72.45  ? 2170 GLY   A C    1 
ATOM   4711 O  O    . GLY   A 1 838  ? 178.433 177.200 146.187 1.00 71.56  ? 2170 GLY   A O    1 
ATOM   4712 N  N    . CYS   A 1 839  ? 176.319 176.435 146.165 1.00 77.92  ? 2171 CYS   A N    1 
ATOM   4713 C  CA   . CYS   A 1 839  ? 176.632 175.259 146.962 1.00 74.28  ? 2171 CYS   A CA   1 
ATOM   4714 C  C    . CYS   A 1 839  ? 177.332 174.210 146.113 1.00 77.09  ? 2171 CYS   A C    1 
ATOM   4715 O  O    . CYS   A 1 839  ? 176.985 174.003 144.949 1.00 83.43  ? 2171 CYS   A O    1 
ATOM   4716 C  CB   . CYS   A 1 839  ? 175.362 174.674 147.574 1.00 79.35  ? 2171 CYS   A CB   1 
ATOM   4717 S  SG   . CYS   A 1 839  ? 174.458 175.788 148.668 1.00 102.48 ? 2171 CYS   A SG   1 
ATOM   4718 N  N    . GLY   A 1 840  ? 178.312 173.538 146.710 1.00 78.02  ? 2172 GLY   A N    1 
ATOM   4719 C  CA   . GLY   A 1 840  ? 179.103 172.562 145.989 1.00 81.57  ? 2172 GLY   A CA   1 
ATOM   4720 C  C    . GLY   A 1 840  ? 179.272 171.237 146.703 1.00 93.93  ? 2172 GLY   A C    1 
ATOM   4721 O  O    . GLY   A 1 840  ? 180.180 170.466 146.379 1.00 103.27 ? 2172 GLY   A O    1 
ATOM   4722 N  N    . HIS   A 1 841  ? 178.407 170.957 147.682 1.00 94.92  ? 2173 HIS   A N    1 
ATOM   4723 C  CA   . HIS   A 1 841  ? 178.497 169.688 148.399 1.00 96.93  ? 2173 HIS   A CA   1 
ATOM   4724 C  C    . HIS   A 1 841  ? 178.128 168.508 147.505 1.00 103.11 ? 2173 HIS   A C    1 
ATOM   4725 O  O    . HIS   A 1 841  ? 178.725 167.430 147.612 1.00 110.50 ? 2173 HIS   A O    1 
ATOM   4726 C  CB   . HIS   A 1 841  ? 177.632 169.733 149.662 1.00 94.14  ? 2173 HIS   A CB   1 
ATOM   4727 C  CG   . HIS   A 1 841  ? 176.216 170.165 149.431 1.00 93.39  ? 2173 HIS   A CG   1 
ATOM   4728 N  ND1  . HIS   A 1 841  ? 175.370 169.527 148.552 1.00 93.81  ? 2173 HIS   A ND1  1 
ATOM   4729 C  CD2  . HIS   A 1 841  ? 175.493 171.166 149.985 1.00 91.15  ? 2173 HIS   A CD2  1 
ATOM   4730 C  CE1  . HIS   A 1 841  ? 174.191 170.120 148.565 1.00 91.85  ? 2173 HIS   A CE1  1 
ATOM   4731 N  NE2  . HIS   A 1 841  ? 174.238 171.117 149.428 1.00 94.83  ? 2173 HIS   A NE2  1 
ATOM   4732 N  N    . THR   A 1 842  ? 177.159 168.690 146.615 1.00 99.91  ? 2174 THR   A N    1 
ATOM   4733 C  CA   . THR   A 1 842  ? 176.801 167.693 145.615 1.00 102.05 ? 2174 THR   A CA   1 
ATOM   4734 C  C    . THR   A 1 842  ? 177.324 168.164 144.269 1.00 100.30 ? 2174 THR   A C    1 
ATOM   4735 O  O    . THR   A 1 842  ? 177.164 169.338 143.917 1.00 97.49  ? 2174 THR   A O    1 
ATOM   4736 C  CB   . THR   A 1 842  ? 175.290 167.480 145.550 1.00 107.21 ? 2174 THR   A CB   1 
ATOM   4737 O  OG1  . THR   A 1 842  ? 174.650 168.712 145.192 1.00 108.89 ? 2174 THR   A OG1  1 
ATOM   4738 C  CG2  . THR   A 1 842  ? 174.750 166.970 146.877 1.00 96.46  ? 2174 THR   A CG2  1 
ATOM   4739 N  N    . ASP   A 1 843  ? 177.917 167.248 143.505 1.00 103.14 ? 2175 ASP   A N    1 
ATOM   4740 C  CA   . ASP   A 1 843  ? 178.562 167.645 142.262 1.00 106.93 ? 2175 ASP   A CA   1 
ATOM   4741 C  C    . ASP   A 1 843  ? 177.534 167.831 141.157 1.00 96.52  ? 2175 ASP   A C    1 
ATOM   4742 O  O    . ASP   A 1 843  ? 177.693 167.315 140.048 1.00 90.08  ? 2175 ASP   A O    1 
ATOM   4743 C  CB   . ASP   A 1 843  ? 179.620 166.621 141.854 1.00 108.99 ? 2175 ASP   A CB   1 
ATOM   4744 C  CG   . ASP   A 1 843  ? 180.813 166.621 142.788 1.00 113.73 ? 2175 ASP   A CG   1 
ATOM   4745 O  OD1  . ASP   A 1 843  ? 181.110 167.686 143.368 1.00 106.52 ? 2175 ASP   A OD1  1 
ATOM   4746 O  OD2  . ASP   A 1 843  ? 181.453 165.560 142.943 1.00 119.73 ? 2175 ASP   A OD2  1 
ATOM   4747 N  N    . ARG   A 1 844  ? 176.491 168.597 141.466 1.00 94.83  ? 2176 ARG   A N    1 
ATOM   4748 C  CA   . ARG   A 1 844  ? 175.552 169.138 140.498 1.00 93.18  ? 2176 ARG   A CA   1 
ATOM   4749 C  C    . ARG   A 1 844  ? 175.342 170.603 140.852 1.00 95.87  ? 2176 ARG   A C    1 
ATOM   4750 O  O    . ARG   A 1 844  ? 176.009 171.122 141.753 1.00 98.19  ? 2176 ARG   A O    1 
ATOM   4751 C  CB   . ARG   A 1 844  ? 174.226 168.375 140.518 1.00 97.84  ? 2176 ARG   A CB   1 
ATOM   4752 C  CG   . ARG   A 1 844  ? 174.341 166.880 140.279 1.00 100.26 ? 2176 ARG   A CG   1 
ATOM   4753 C  CD   . ARG   A 1 844  ? 174.975 166.569 138.927 1.00 106.57 ? 2176 ARG   A CD   1 
ATOM   4754 N  NE   . ARG   A 1 844  ? 174.066 166.682 137.788 1.00 110.65 ? 2176 ARG   A NE   1 
ATOM   4755 C  CZ   . ARG   A 1 844  ? 172.872 166.111 137.687 1.00 113.80 ? 2176 ARG   A CZ   1 
ATOM   4756 N  NH1  . ARG   A 1 844  ? 172.416 165.280 138.610 1.00 114.68 ? 2176 ARG   A NH1  1 
ATOM   4757 N  NH2  . ARG   A 1 844  ? 172.126 166.358 136.614 1.00 111.02 ? 2176 ARG   A NH2  1 
ATOM   4758 N  N    . GLY   A 1 845  ? 174.421 171.278 140.174 1.00 91.37  ? 2177 GLY   A N    1 
ATOM   4759 C  CA   . GLY   A 1 845  ? 174.178 172.677 140.461 1.00 86.57  ? 2177 GLY   A CA   1 
ATOM   4760 C  C    . GLY   A 1 845  ? 173.297 172.909 141.668 1.00 89.27  ? 2177 GLY   A C    1 
ATOM   4761 O  O    . GLY   A 1 845  ? 172.180 172.392 141.734 1.00 92.68  ? 2177 GLY   A O    1 
ATOM   4762 N  N    . GLN   A 1 846  ? 173.779 173.700 142.623 1.00 84.62  ? 2178 GLN   A N    1 
ATOM   4763 C  CA   . GLN   A 1 846  ? 173.074 173.921 143.879 1.00 84.83  ? 2178 GLN   A CA   1 
ATOM   4764 C  C    . GLN   A 1 846  ? 173.211 175.385 144.256 1.00 85.07  ? 2178 GLN   A C    1 
ATOM   4765 O  O    . GLN   A 1 846  ? 174.319 175.845 144.543 1.00 86.47  ? 2178 GLN   A O    1 
ATOM   4766 C  CB   . GLN   A 1 846  ? 173.647 173.028 144.981 1.00 84.43  ? 2178 GLN   A CB   1 
ATOM   4767 C  CG   . GLN   A 1 846  ? 172.700 172.739 146.126 1.00 87.42  ? 2178 GLN   A CG   1 
ATOM   4768 C  CD   . GLN   A 1 846  ? 171.391 172.155 145.660 1.00 98.54  ? 2178 GLN   A CD   1 
ATOM   4769 O  OE1  . GLN   A 1 846  ? 171.366 171.202 144.882 1.00 102.12 ? 2178 GLN   A OE1  1 
ATOM   4770 N  NE2  . GLN   A 1 846  ? 170.289 172.724 146.130 1.00 95.05  ? 2178 GLN   A NE2  1 
ATOM   4771 N  N    . LEU   A 1 847  ? 172.094 176.114 144.271 1.00 87.42  ? 2179 LEU   A N    1 
ATOM   4772 C  CA   . LEU   A 1 847  ? 172.116 177.542 144.563 1.00 74.82  ? 2179 LEU   A CA   1 
ATOM   4773 C  C    . LEU   A 1 847  ? 171.211 177.826 145.748 1.00 73.14  ? 2179 LEU   A C    1 
ATOM   4774 O  O    . LEU   A 1 847  ? 170.049 177.416 145.753 1.00 85.95  ? 2179 LEU   A O    1 
ATOM   4775 C  CB   . LEU   A 1 847  ? 171.678 178.356 143.341 1.00 73.22  ? 2179 LEU   A CB   1 
ATOM   4776 C  CG   . LEU   A 1 847  ? 171.433 179.856 143.490 1.00 71.68  ? 2179 LEU   A CG   1 
ATOM   4777 C  CD1  . LEU   A 1 847  ? 171.945 180.579 142.269 1.00 70.63  ? 2179 LEU   A CD1  1 
ATOM   4778 C  CD2  . LEU   A 1 847  ? 169.950 180.137 143.665 1.00 67.64  ? 2179 LEU   A CD2  1 
ATOM   4779 N  N    . SER   A 1 848  ? 171.735 178.540 146.738 1.00 63.62  ? 2180 SER   A N    1 
ATOM   4780 C  CA   . SER   A 1 848  ? 171.038 178.764 147.994 1.00 69.51  ? 2180 SER   A CA   1 
ATOM   4781 C  C    . SER   A 1 848  ? 170.769 180.247 148.195 1.00 61.27  ? 2180 SER   A C    1 
ATOM   4782 O  O    . SER   A 1 848  ? 171.584 181.093 147.835 1.00 65.10  ? 2180 SER   A O    1 
ATOM   4783 C  CB   . SER   A 1 848  ? 171.855 178.231 149.170 1.00 72.36  ? 2180 SER   A CB   1 
ATOM   4784 O  OG   . SER   A 1 848  ? 172.012 176.827 149.087 1.00 86.79  ? 2180 SER   A OG   1 
ATOM   4785 N  N    . PHE   A 1 849  ? 169.624 180.556 148.788 1.00 61.58  ? 2181 PHE   A N    1 
ATOM   4786 C  CA   . PHE   A 1 849  ? 169.235 181.921 149.101 1.00 55.84  ? 2181 PHE   A CA   1 
ATOM   4787 C  C    . PHE   A 1 849  ? 169.195 182.086 150.612 1.00 64.83  ? 2181 PHE   A C    1 
ATOM   4788 O  O    . PHE   A 1 849  ? 168.515 181.320 151.300 1.00 79.20  ? 2181 PHE   A O    1 
ATOM   4789 C  CB   . PHE   A 1 849  ? 167.868 182.246 148.500 1.00 66.17  ? 2181 PHE   A CB   1 
ATOM   4790 C  CG   . PHE   A 1 849  ? 167.412 183.651 148.752 1.00 74.39  ? 2181 PHE   A CG   1 
ATOM   4791 C  CD1  . PHE   A 1 849  ? 167.944 184.707 148.040 1.00 72.73  ? 2181 PHE   A CD1  1 
ATOM   4792 C  CD2  . PHE   A 1 849  ? 166.457 183.917 149.711 1.00 84.86  ? 2181 PHE   A CD2  1 
ATOM   4793 C  CE1  . PHE   A 1 849  ? 167.521 185.998 148.273 1.00 71.35  ? 2181 PHE   A CE1  1 
ATOM   4794 C  CE2  . PHE   A 1 849  ? 166.035 185.208 149.949 1.00 85.16  ? 2181 PHE   A CE2  1 
ATOM   4795 C  CZ   . PHE   A 1 849  ? 166.568 186.247 149.229 1.00 78.88  ? 2181 PHE   A CZ   1 
ATOM   4796 N  N    . LEU   A 1 850  ? 169.910 183.085 151.121 1.00 65.59  ? 2182 LEU   A N    1 
ATOM   4797 C  CA   . LEU   A 1 850  ? 169.992 183.370 152.544 1.00 74.52  ? 2182 LEU   A CA   1 
ATOM   4798 C  C    . LEU   A 1 850  ? 169.502 184.786 152.804 1.00 75.37  ? 2182 LEU   A C    1 
ATOM   4799 O  O    . LEU   A 1 850  ? 169.757 185.700 152.018 1.00 77.39  ? 2182 LEU   A O    1 
ATOM   4800 C  CB   . LEU   A 1 850  ? 171.428 183.222 153.051 1.00 66.50  ? 2182 LEU   A CB   1 
ATOM   4801 C  CG   . LEU   A 1 850  ? 171.697 183.305 154.553 1.00 52.91  ? 2182 LEU   A CG   1 
ATOM   4802 C  CD1  . LEU   A 1 850  ? 172.946 182.521 154.877 1.00 47.61  ? 2182 LEU   A CD1  1 
ATOM   4803 C  CD2  . LEU   A 1 850  ? 171.848 184.730 155.034 1.00 56.85  ? 2182 LEU   A CD2  1 
ATOM   4804 N  N    . ASP   A 1 851  ? 168.801 184.969 153.916 1.00 79.38  ? 2183 ASP   A N    1 
ATOM   4805 C  CA   . ASP   A 1 851  ? 168.305 186.277 154.312 1.00 88.89  ? 2183 ASP   A CA   1 
ATOM   4806 C  C    . ASP   A 1 851  ? 168.914 186.663 155.650 1.00 95.72  ? 2183 ASP   A C    1 
ATOM   4807 O  O    . ASP   A 1 851  ? 168.818 185.912 156.624 1.00 101.21 ? 2183 ASP   A O    1 
ATOM   4808 C  CB   . ASP   A 1 851  ? 166.784 186.281 154.402 1.00 97.41  ? 2183 ASP   A CB   1 
ATOM   4809 C  CG   . ASP   A 1 851  ? 166.225 187.654 154.668 1.00 104.28 ? 2183 ASP   A CG   1 
ATOM   4810 O  OD1  . ASP   A 1 851  ? 166.220 188.477 153.733 1.00 111.10 ? 2183 ASP   A OD1  1 
ATOM   4811 O  OD2  . ASP   A 1 851  ? 165.802 187.918 155.813 1.00 103.11 ? 2183 ASP   A OD2  1 
ATOM   4812 N  N    . LEU   A 1 852  ? 169.536 187.840 155.697 1.00 91.39  ? 2184 LEU   A N    1 
ATOM   4813 C  CA   . LEU   A 1 852  ? 170.325 188.242 156.855 1.00 91.10  ? 2184 LEU   A CA   1 
ATOM   4814 C  C    . LEU   A 1 852  ? 169.467 188.672 158.039 1.00 102.66 ? 2184 LEU   A C    1 
ATOM   4815 O  O    . LEU   A 1 852  ? 169.755 188.302 159.181 1.00 103.75 ? 2184 LEU   A O    1 
ATOM   4816 C  CB   . LEU   A 1 852  ? 171.285 189.363 156.463 1.00 81.70  ? 2184 LEU   A CB   1 
ATOM   4817 C  CG   . LEU   A 1 852  ? 172.361 188.926 155.477 1.00 72.61  ? 2184 LEU   A CG   1 
ATOM   4818 C  CD1  . LEU   A 1 852  ? 173.181 190.107 155.021 1.00 66.08  ? 2184 LEU   A CD1  1 
ATOM   4819 C  CD2  . LEU   A 1 852  ? 173.247 187.896 156.134 1.00 59.56  ? 2184 LEU   A CD2  1 
ATOM   4820 N  N    . ASN   A 1 853  ? 168.420 189.460 157.791 1.00 112.36 ? 2185 ASN   A N    1 
ATOM   4821 C  CA   . ASN   A 1 853  ? 167.575 189.920 158.888 1.00 113.90 ? 2185 ASN   A CA   1 
ATOM   4822 C  C    . ASN   A 1 853  ? 166.773 188.770 159.487 1.00 113.71 ? 2185 ASN   A C    1 
ATOM   4823 O  O    . ASN   A 1 853  ? 166.745 188.588 160.710 1.00 111.70 ? 2185 ASN   A O    1 
ATOM   4824 C  CB   . ASN   A 1 853  ? 166.651 191.037 158.404 1.00 119.20 ? 2185 ASN   A CB   1 
ATOM   4825 C  CG   . ASN   A 1 853  ? 167.384 192.083 157.590 1.00 121.37 ? 2185 ASN   A CG   1 
ATOM   4826 O  OD1  . ASN   A 1 853  ? 168.483 192.505 157.950 1.00 121.79 ? 2185 ASN   A OD1  1 
ATOM   4827 N  ND2  . ASN   A 1 853  ? 166.780 192.508 156.487 1.00 114.89 ? 2185 ASN   A ND2  1 
ATOM   4828 N  N    . THR   A 1 854  ? 166.124 187.974 158.641 1.00 109.95 ? 2186 THR   A N    1 
ATOM   4829 C  CA   . THR   A 1 854  ? 165.305 186.847 159.080 1.00 109.38 ? 2186 THR   A CA   1 
ATOM   4830 C  C    . THR   A 1 854  ? 165.804 185.598 158.371 1.00 104.87 ? 2186 THR   A C    1 
ATOM   4831 O  O    . THR   A 1 854  ? 165.657 185.480 157.152 1.00 105.57 ? 2186 THR   A O    1 
ATOM   4832 C  CB   . THR   A 1 854  ? 163.829 187.088 158.776 1.00 112.32 ? 2186 THR   A CB   1 
ATOM   4833 O  OG1  . THR   A 1 854  ? 163.652 187.223 157.361 1.00 107.34 ? 2186 THR   A OG1  1 
ATOM   4834 C  CG2  . THR   A 1 854  ? 163.348 188.356 159.456 1.00 110.29 ? 2186 THR   A CG2  1 
ATOM   4835 N  N    . GLU   A 1 855  ? 166.370 184.663 159.130 1.00 103.50 ? 2187 GLU   A N    1 
ATOM   4836 C  CA   . GLU   A 1 855  ? 167.039 183.505 158.545 1.00 107.83 ? 2187 GLU   A CA   1 
ATOM   4837 C  C    . GLU   A 1 855  ? 166.092 182.720 157.644 1.00 104.31 ? 2187 GLU   A C    1 
ATOM   4838 O  O    . GLU   A 1 855  ? 165.089 182.171 158.107 1.00 112.15 ? 2187 GLU   A O    1 
ATOM   4839 C  CB   . GLU   A 1 855  ? 167.585 182.609 159.654 1.00 110.32 ? 2187 GLU   A CB   1 
ATOM   4840 C  CG   . GLU   A 1 855  ? 168.381 183.341 160.730 1.00 113.33 ? 2187 GLU   A CG   1 
ATOM   4841 C  CD   . GLU   A 1 855  ? 169.179 184.510 160.192 1.00 107.96 ? 2187 GLU   A CD   1 
ATOM   4842 O  OE1  . GLU   A 1 855  ? 169.075 185.615 160.762 1.00 105.34 ? 2187 GLU   A OE1  1 
ATOM   4843 O  OE2  . GLU   A 1 855  ? 169.915 184.323 159.204 1.00 95.14  ? 2187 GLU   A OE2  1 
ATOM   4844 N  N    . GLY   A 1 856  ? 166.420 182.666 156.355 1.00 91.54  ? 2188 GLY   A N    1 
ATOM   4845 C  CA   . GLY   A 1 856  ? 165.541 182.074 155.365 1.00 84.75  ? 2188 GLY   A CA   1 
ATOM   4846 C  C    . GLY   A 1 856  ? 166.238 181.188 154.353 1.00 87.38  ? 2188 GLY   A C    1 
ATOM   4847 O  O    . GLY   A 1 856  ? 165.872 181.191 153.175 1.00 83.99  ? 2188 GLY   A O    1 
ATOM   4848 N  N    . TYR   A 1 857  ? 167.253 180.447 154.791 1.00 89.57  ? 2189 TYR   A N    1 
ATOM   4849 C  CA   . TYR   A 1 857  ? 168.043 179.613 153.891 1.00 81.52  ? 2189 TYR   A CA   1 
ATOM   4850 C  C    . TYR   A 1 857  ? 167.157 178.645 153.119 1.00 79.12  ? 2189 TYR   A C    1 
ATOM   4851 O  O    . TYR   A 1 857  ? 166.539 177.752 153.702 1.00 81.49  ? 2189 TYR   A O    1 
ATOM   4852 C  CB   . TYR   A 1 857  ? 169.101 178.853 154.696 1.00 79.86  ? 2189 TYR   A CB   1 
ATOM   4853 C  CG   . TYR   A 1 857  ? 170.055 178.020 153.871 1.00 80.37  ? 2189 TYR   A CG   1 
ATOM   4854 C  CD1  . TYR   A 1 857  ? 169.636 176.869 153.225 1.00 79.73  ? 2189 TYR   A CD1  1 
ATOM   4855 C  CD2  . TYR   A 1 857  ? 171.378 178.399 153.731 1.00 85.01  ? 2189 TYR   A CD2  1 
ATOM   4856 C  CE1  . TYR   A 1 857  ? 170.506 176.118 152.471 1.00 82.05  ? 2189 TYR   A CE1  1 
ATOM   4857 C  CE2  . TYR   A 1 857  ? 172.255 177.653 152.978 1.00 85.65  ? 2189 TYR   A CE2  1 
ATOM   4858 C  CZ   . TYR   A 1 857  ? 171.814 176.514 152.351 1.00 81.56  ? 2189 TYR   A CZ   1 
ATOM   4859 O  OH   . TYR   A 1 857  ? 172.684 175.766 151.599 1.00 79.65  ? 2189 TYR   A OH   1 
ATOM   4860 N  N    . THR   A 1 858  ? 167.109 178.822 151.801 1.00 80.72  ? 2190 THR   A N    1 
ATOM   4861 C  CA   . THR   A 1 858  ? 166.356 177.946 150.909 1.00 85.63  ? 2190 THR   A CA   1 
ATOM   4862 C  C    . THR   A 1 858  ? 167.247 177.557 149.742 1.00 74.38  ? 2190 THR   A C    1 
ATOM   4863 O  O    . THR   A 1 858  ? 167.730 178.426 149.015 1.00 73.85  ? 2190 THR   A O    1 
ATOM   4864 C  CB   . THR   A 1 858  ? 165.086 178.626 150.394 1.00 88.19  ? 2190 THR   A CB   1 
ATOM   4865 O  OG1  . THR   A 1 858  ? 165.438 179.794 149.647 1.00 83.69  ? 2190 THR   A OG1  1 
ATOM   4866 C  CG2  . THR   A 1 858  ? 164.182 179.023 151.547 1.00 87.42  ? 2190 THR   A CG2  1 
ATOM   4867 N  N    . SER   A 1 859  ? 167.453 176.261 149.551 1.00 78.64  ? 2191 SER   A N    1 
ATOM   4868 C  CA   . SER   A 1 859  ? 168.367 175.763 148.535 1.00 84.70  ? 2191 SER   A CA   1 
ATOM   4869 C  C    . SER   A 1 859  ? 167.592 175.123 147.391 1.00 91.86  ? 2191 SER   A C    1 
ATOM   4870 O  O    . SER   A 1 859  ? 166.676 174.328 147.618 1.00 101.09 ? 2191 SER   A O    1 
ATOM   4871 C  CB   . SER   A 1 859  ? 169.342 174.749 149.134 1.00 86.74  ? 2191 SER   A CB   1 
ATOM   4872 O  OG   . SER   A 1 859  ? 169.978 173.996 148.119 1.00 88.76  ? 2191 SER   A OG   1 
ATOM   4873 N  N    . GLU   A 1 860  ? 167.963 175.476 146.160 1.00 86.02  ? 2192 GLU   A N    1 
ATOM   4874 C  CA   . GLU   A 1 860  ? 167.334 174.944 144.963 1.00 84.75  ? 2192 GLU   A CA   1 
ATOM   4875 C  C    . GLU   A 1 860  ? 168.371 174.249 144.095 1.00 84.12  ? 2192 GLU   A C    1 
ATOM   4876 O  O    . GLU   A 1 860  ? 169.543 174.640 144.051 1.00 83.65  ? 2192 GLU   A O    1 
ATOM   4877 C  CB   . GLU   A 1 860  ? 166.631 176.041 144.151 1.00 85.80  ? 2192 GLU   A CB   1 
ATOM   4878 C  CG   . GLU   A 1 860  ? 165.174 176.294 144.532 1.00 92.31  ? 2192 GLU   A CG   1 
ATOM   4879 C  CD   . GLU   A 1 860  ? 164.998 177.271 145.685 1.00 104.51 ? 2192 GLU   A CD   1 
ATOM   4880 O  OE1  . GLU   A 1 860  ? 165.878 177.344 146.565 1.00 96.27  ? 2192 GLU   A OE1  1 
ATOM   4881 O  OE2  . GLU   A 1 860  ? 163.966 177.974 145.707 1.00 113.19 ? 2192 GLU   A OE2  1 
ATOM   4882 N  N    . GLU   A 1 861  ? 167.917 173.208 143.402 1.00 90.94  ? 2193 GLU   A N    1 
ATOM   4883 C  CA   . GLU   A 1 861  ? 168.744 172.389 142.520 1.00 96.69  ? 2193 GLU   A CA   1 
ATOM   4884 C  C    . GLU   A 1 861  ? 168.550 172.937 141.112 1.00 99.60  ? 2193 GLU   A C    1 
ATOM   4885 O  O    . GLU   A 1 861  ? 167.526 172.683 140.473 1.00 107.87 ? 2193 GLU   A O    1 
ATOM   4886 C  CB   . GLU   A 1 861  ? 168.339 170.917 142.610 1.00 100.70 ? 2193 GLU   A CB   1 
ATOM   4887 C  CG   . GLU   A 1 861  ? 168.799 170.015 141.452 1.00 111.46 ? 2193 GLU   A CG   1 
ATOM   4888 C  CD   . GLU   A 1 861  ? 170.302 170.019 141.229 1.00 106.54 ? 2193 GLU   A CD   1 
ATOM   4889 O  OE1  . GLU   A 1 861  ? 171.055 170.018 142.225 1.00 97.29  ? 2193 GLU   A OE1  1 
ATOM   4890 O  OE2  . GLU   A 1 861  ? 170.730 170.015 140.057 1.00 107.58 ? 2193 GLU   A OE2  1 
ATOM   4891 N  N    . VAL   A 1 862  ? 169.521 173.714 140.639 1.00 93.76  ? 2194 VAL   A N    1 
ATOM   4892 C  CA   . VAL   A 1 862  ? 169.467 174.324 139.318 1.00 92.57  ? 2194 VAL   A CA   1 
ATOM   4893 C  C    . VAL   A 1 862  ? 170.802 174.106 138.627 1.00 94.43  ? 2194 VAL   A C    1 
ATOM   4894 O  O    . VAL   A 1 862  ? 171.848 174.083 139.282 1.00 92.06  ? 2194 VAL   A O    1 
ATOM   4895 C  CB   . VAL   A 1 862  ? 169.125 175.825 139.394 1.00 88.39  ? 2194 VAL   A CB   1 
ATOM   4896 C  CG1  . VAL   A 1 862  ? 167.899 176.041 140.257 1.00 98.09  ? 2194 VAL   A CG1  1 
ATOM   4897 C  CG2  . VAL   A 1 862  ? 170.298 176.606 139.946 1.00 87.05  ? 2194 VAL   A CG2  1 
ATOM   4898 N  N    . ALA   A 1 863  ? 170.753 173.884 137.311 1.00 96.34  ? 2195 ALA   A N    1 
ATOM   4899 C  CA   . ALA   A 1 863  ? 171.925 173.708 136.457 1.00 90.96  ? 2195 ALA   A CA   1 
ATOM   4900 C  C    . ALA   A 1 863  ? 172.565 172.342 136.666 1.00 96.50  ? 2195 ALA   A C    1 
ATOM   4901 O  O    . ALA   A 1 863  ? 172.442 171.746 137.740 1.00 94.02  ? 2195 ALA   A O    1 
ATOM   4902 C  CB   . ALA   A 1 863  ? 172.949 174.821 136.681 1.00 85.85  ? 2195 ALA   A CB   1 
ATOM   4903 N  N    . ASP   A 1 864  ? 173.265 171.846 135.646 1.00 100.04 ? 2196 ASP   A N    1 
ATOM   4904 C  CA   . ASP   A 1 864  ? 173.733 170.466 135.628 1.00 105.32 ? 2196 ASP   A CA   1 
ATOM   4905 C  C    . ASP   A 1 864  ? 174.894 170.210 136.583 1.00 101.54 ? 2196 ASP   A C    1 
ATOM   4906 O  O    . ASP   A 1 864  ? 174.887 169.212 137.307 1.00 101.86 ? 2196 ASP   A O    1 
ATOM   4907 C  CB   . ASP   A 1 864  ? 174.128 170.061 134.203 1.00 102.46 ? 2196 ASP   A CB   1 
ATOM   4908 C  CG   . ASP   A 1 864  ? 175.284 170.879 133.652 1.00 113.31 ? 2196 ASP   A CG   1 
ATOM   4909 O  OD1  . ASP   A 1 864  ? 175.773 171.797 134.345 1.00 98.07  ? 2196 ASP   A OD1  1 
ATOM   4910 O  OD2  . ASP   A 1 864  ? 175.702 170.597 132.510 1.00 126.21 ? 2196 ASP   A OD2  1 
ATOM   4911 N  N    . SER   A 1 865  ? 175.894 171.082 136.600 1.00 91.37  ? 2197 SER   A N    1 
ATOM   4912 C  CA   . SER   A 1 865  ? 177.083 170.840 137.397 1.00 92.42  ? 2197 SER   A CA   1 
ATOM   4913 C  C    . SER   A 1 865  ? 177.232 171.915 138.468 1.00 90.88  ? 2197 SER   A C    1 
ATOM   4914 O  O    . SER   A 1 865  ? 176.479 172.887 138.522 1.00 92.21  ? 2197 SER   A O    1 
ATOM   4915 C  CB   . SER   A 1 865  ? 178.321 170.775 136.505 1.00 80.86  ? 2197 SER   A CB   1 
ATOM   4916 O  OG   . SER   A 1 865  ? 179.485 170.569 137.283 1.00 80.60  ? 2197 SER   A OG   1 
ATOM   4917 N  N    . ARG   A 1 866  ? 178.233 171.732 139.323 1.00 81.81  ? 2198 ARG   A N    1 
ATOM   4918 C  CA   . ARG   A 1 866  ? 178.438 172.622 140.455 1.00 68.23  ? 2198 ARG   A CA   1 
ATOM   4919 C  C    . ARG   A 1 866  ? 178.629 174.055 139.982 1.00 76.67  ? 2198 ARG   A C    1 
ATOM   4920 O  O    . ARG   A 1 866  ? 179.295 174.307 138.977 1.00 80.73  ? 2198 ARG   A O    1 
ATOM   4921 C  CB   . ARG   A 1 866  ? 179.652 172.151 141.255 1.00 74.70  ? 2198 ARG   A CB   1 
ATOM   4922 C  CG   . ARG   A 1 866  ? 180.375 173.220 142.046 1.00 80.21  ? 2198 ARG   A CG   1 
ATOM   4923 C  CD   . ARG   A 1 866  ? 181.428 172.630 142.985 1.00 87.56  ? 2198 ARG   A CD   1 
ATOM   4924 N  NE   . ARG   A 1 866  ? 182.475 171.902 142.278 1.00 91.22  ? 2198 ARG   A NE   1 
ATOM   4925 C  CZ   . ARG   A 1 866  ? 182.457 170.599 142.034 1.00 90.36  ? 2198 ARG   A CZ   1 
ATOM   4926 N  NH1  . ARG   A 1 866  ? 181.478 169.826 142.472 1.00 90.53  ? 2198 ARG   A NH1  1 
ATOM   4927 N  NH2  . ARG   A 1 866  ? 183.450 170.056 141.336 1.00 90.42  ? 2198 ARG   A NH2  1 
ATOM   4928 N  N    . ILE   A 1 867  ? 178.013 174.994 140.695 1.00 72.69  ? 2199 ILE   A N    1 
ATOM   4929 C  CA   . ILE   A 1 867  ? 178.139 176.410 140.368 1.00 62.07  ? 2199 ILE   A CA   1 
ATOM   4930 C  C    . ILE   A 1 867  ? 179.460 176.940 140.905 1.00 53.20  ? 2199 ILE   A C    1 
ATOM   4931 O  O    . ILE   A 1 867  ? 179.780 176.768 142.085 1.00 58.13  ? 2199 ILE   A O    1 
ATOM   4932 C  CB   . ILE   A 1 867  ? 176.951 177.203 140.922 1.00 48.29  ? 2199 ILE   A CB   1 
ATOM   4933 C  CG1  . ILE   A 1 867  ? 175.663 176.745 140.259 1.00 53.18  ? 2199 ILE   A CG1  1 
ATOM   4934 C  CG2  . ILE   A 1 867  ? 177.152 178.664 140.709 1.00 51.22  ? 2199 ILE   A CG2  1 
ATOM   4935 C  CD1  . ILE   A 1 867  ? 174.440 177.293 140.913 1.00 59.89  ? 2199 ILE   A CD1  1 
ATOM   4936 N  N    . LEU   A 1 868  ? 180.232 177.590 140.039 1.00 48.76  ? 2200 LEU   A N    1 
ATOM   4937 C  CA   . LEU   A 1 868  ? 181.570 178.047 140.389 1.00 48.46  ? 2200 LEU   A CA   1 
ATOM   4938 C  C    . LEU   A 1 868  ? 181.622 179.487 140.866 1.00 49.45  ? 2200 LEU   A C    1 
ATOM   4939 O  O    . LEU   A 1 868  ? 182.349 179.778 141.816 1.00 59.11  ? 2200 LEU   A O    1 
ATOM   4940 C  CB   . LEU   A 1 868  ? 182.524 177.881 139.207 1.00 54.10  ? 2200 LEU   A CB   1 
ATOM   4941 C  CG   . LEU   A 1 868  ? 183.171 176.517 139.007 1.00 41.02  ? 2200 LEU   A CG   1 
ATOM   4942 C  CD1  . LEU   A 1 868  ? 184.064 176.217 140.185 1.00 52.50  ? 2200 LEU   A CD1  1 
ATOM   4943 C  CD2  . LEU   A 1 868  ? 182.142 175.448 138.868 1.00 44.38  ? 2200 LEU   A CD2  1 
ATOM   4944 N  N    . CYS   A 1 869  ? 180.901 180.408 140.231 1.00 41.56  ? 2201 CYS   A N    1 
ATOM   4945 C  CA   . CYS   A 1 869  ? 180.871 181.770 140.738 1.00 41.38  ? 2201 CYS   A CA   1 
ATOM   4946 C  C    . CYS   A 1 869  ? 179.623 182.482 140.256 1.00 37.99  ? 2201 CYS   A C    1 
ATOM   4947 O  O    . CYS   A 1 869  ? 179.173 182.264 139.131 1.00 35.17  ? 2201 CYS   A O    1 
ATOM   4948 C  CB   . CYS   A 1 869  ? 182.103 182.564 140.319 1.00 41.08  ? 2201 CYS   A CB   1 
ATOM   4949 S  SG   . CYS   A 1 869  ? 182.113 184.231 141.017 1.00 82.08  ? 2201 CYS   A SG   1 
ATOM   4950 N  N    . LEU   A 1 870  ? 179.081 183.341 141.110 1.00 37.13  ? 2202 LEU   A N    1 
ATOM   4951 C  CA   . LEU   A 1 870  ? 177.928 184.158 140.779 1.00 40.03  ? 2202 LEU   A CA   1 
ATOM   4952 C  C    . LEU   A 1 870  ? 178.331 185.614 140.626 1.00 47.69  ? 2202 LEU   A C    1 
ATOM   4953 O  O    . LEU   A 1 870  ? 179.386 186.046 141.094 1.00 52.74  ? 2202 LEU   A O    1 
ATOM   4954 C  CB   . LEU   A 1 870  ? 176.823 184.078 141.837 1.00 35.49  ? 2202 LEU   A CB   1 
ATOM   4955 C  CG   . LEU   A 1 870  ? 176.046 182.802 142.106 1.00 37.63  ? 2202 LEU   A CG   1 
ATOM   4956 C  CD1  . LEU   A 1 870  ? 176.776 181.924 143.056 1.00 43.32  ? 2202 LEU   A CD1  1 
ATOM   4957 C  CD2  . LEU   A 1 870  ? 174.699 183.181 142.656 1.00 42.50  ? 2202 LEU   A CD2  1 
ATOM   4958 N  N    . ALA   A 1 871  ? 177.459 186.364 139.961 1.00 44.36  ? 2203 ALA   A N    1 
ATOM   4959 C  CA   . ALA   A 1 871  ? 177.573 187.811 139.876 1.00 40.90  ? 2203 ALA   A CA   1 
ATOM   4960 C  C    . ALA   A 1 871  ? 176.193 188.371 139.580 1.00 50.26  ? 2203 ALA   A C    1 
ATOM   4961 O  O    . ALA   A 1 871  ? 175.287 187.652 139.157 1.00 49.58  ? 2203 ALA   A O    1 
ATOM   4962 C  CB   . ALA   A 1 871  ? 178.582 188.238 138.816 1.00 43.82  ? 2203 ALA   A CB   1 
ATOM   4963 N  N    . LEU   A 1 872  ? 176.049 189.668 139.808 1.00 54.77  ? 2204 LEU   A N    1 
ATOM   4964 C  CA   . LEU   A 1 872  ? 174.782 190.365 139.684 1.00 63.57  ? 2204 LEU   A CA   1 
ATOM   4965 C  C    . LEU   A 1 872  ? 174.814 191.315 138.498 1.00 71.96  ? 2204 LEU   A C    1 
ATOM   4966 O  O    . LEU   A 1 872  ? 175.833 191.939 138.195 1.00 75.41  ? 2204 LEU   A O    1 
ATOM   4967 C  CB   . LEU   A 1 872  ? 174.459 191.146 140.963 1.00 64.47  ? 2204 LEU   A CB   1 
ATOM   4968 C  CG   . LEU   A 1 872  ? 173.003 191.358 141.371 1.00 69.29  ? 2204 LEU   A CG   1 
ATOM   4969 C  CD1  . LEU   A 1 872  ? 172.254 190.051 141.423 1.00 65.43  ? 2204 LEU   A CD1  1 
ATOM   4970 C  CD2  . LEU   A 1 872  ? 172.956 192.064 142.719 1.00 73.39  ? 2204 LEU   A CD2  1 
ATOM   4971 N  N    . VAL   A 1 873  ? 173.684 191.394 137.807 1.00 78.04  ? 2205 VAL   A N    1 
ATOM   4972 C  CA   . VAL   A 1 873  ? 173.457 192.439 136.820 1.00 87.96  ? 2205 VAL   A CA   1 
ATOM   4973 C  C    . VAL   A 1 873  ? 172.105 193.077 137.109 1.00 95.96  ? 2205 VAL   A C    1 
ATOM   4974 O  O    . VAL   A 1 873  ? 171.110 192.379 137.329 1.00 95.78  ? 2205 VAL   A O    1 
ATOM   4975 C  CB   . VAL   A 1 873  ? 173.561 191.912 135.376 1.00 83.90  ? 2205 VAL   A CB   1 
ATOM   4976 C  CG1  . VAL   A 1 873  ? 175.000 191.565 135.060 1.00 71.00  ? 2205 VAL   A CG1  1 
ATOM   4977 C  CG2  . VAL   A 1 873  ? 172.730 190.690 135.204 1.00 82.17  ? 2205 VAL   A CG2  1 
ATOM   4978 N  N    A HIS   A 1 874  ? 172.085 194.407 137.157 0.47 98.38  ? 2206 HIS   A N    1 
ATOM   4979 N  N    B HIS   A 1 874  ? 172.073 194.401 137.081 0.53 98.38  ? 2206 HIS   A N    1 
ATOM   4980 C  CA   A HIS   A 1 874  ? 170.920 195.199 137.522 0.47 102.78 ? 2206 HIS   A CA   1 
ATOM   4981 C  CA   B HIS   A 1 874  ? 170.949 195.210 137.518 0.53 102.78 ? 2206 HIS   A CA   1 
ATOM   4982 C  C    A HIS   A 1 874  ? 170.201 195.708 136.282 0.47 107.77 ? 2206 HIS   A C    1 
ATOM   4983 C  C    B HIS   A 1 874  ? 170.239 195.825 136.318 0.53 107.78 ? 2206 HIS   A C    1 
ATOM   4984 O  O    A HIS   A 1 874  ? 170.761 195.759 135.183 0.47 107.45 ? 2206 HIS   A O    1 
ATOM   4985 O  O    B HIS   A 1 874  ? 170.848 196.062 135.271 0.53 107.42 ? 2206 HIS   A O    1 
ATOM   4986 C  CB   A HIS   A 1 874  ? 171.315 196.393 138.397 0.47 102.58 ? 2206 HIS   A CB   1 
ATOM   4987 C  CB   B HIS   A 1 874  ? 171.455 196.297 138.466 0.53 102.52 ? 2206 HIS   A CB   1 
ATOM   4988 C  CG   A HIS   A 1 874  ? 171.297 196.110 139.866 0.47 100.45 ? 2206 HIS   A CG   1 
ATOM   4989 C  CG   B HIS   A 1 874  ? 172.948 196.298 138.618 0.53 99.83  ? 2206 HIS   A CG   1 
ATOM   4990 N  ND1  A HIS   A 1 874  ? 170.462 196.774 140.738 0.47 99.87  ? 2206 HIS   A ND1  1 
ATOM   4991 N  ND1  B HIS   A 1 874  ? 173.804 196.580 137.574 0.53 94.99  ? 2206 HIS   A ND1  1 
ATOM   4992 C  CD2  A HIS   A 1 874  ? 172.019 195.248 140.620 0.47 97.86  ? 2206 HIS   A CD2  1 
ATOM   4993 C  CD2  B HIS   A 1 874  ? 173.737 196.019 139.683 0.53 96.97  ? 2206 HIS   A CD2  1 
ATOM   4994 C  CE1  A HIS   A 1 874  ? 170.667 196.330 141.965 0.47 99.41  ? 2206 HIS   A CE1  1 
ATOM   4995 C  CE1  B HIS   A 1 874  ? 175.053 196.491 137.993 0.53 89.70  ? 2206 HIS   A CE1  1 
ATOM   4996 N  NE2  A HIS   A 1 874  ? 171.605 195.402 141.921 0.47 97.74  ? 2206 HIS   A NE2  1 
ATOM   4997 N  NE2  B HIS   A 1 874  ? 175.040 196.153 139.270 0.53 88.31  ? 2206 HIS   A NE2  1 
ATOM   4998 N  N    . LEU   A 1 875  ? 168.942 196.089 136.478 1.00 114.20 ? 2207 LEU   A N    1 
ATOM   4999 C  CA   . LEU   A 1 875  ? 168.100 196.629 135.409 1.00 122.61 ? 2207 LEU   A CA   1 
ATOM   5000 C  C    . LEU   A 1 875  ? 167.366 197.868 135.905 1.00 131.08 ? 2207 LEU   A C    1 
ATOM   5001 O  O    . LEU   A 1 875  ? 166.157 197.830 136.163 1.00 129.88 ? 2207 LEU   A O    1 
ATOM   5002 C  CB   . LEU   A 1 875  ? 167.112 195.575 134.911 1.00 119.20 ? 2207 LEU   A CB   1 
ATOM   5003 C  CG   . LEU   A 1 875  ? 167.700 194.538 133.959 1.00 116.23 ? 2207 LEU   A CG   1 
ATOM   5004 C  CD1  . LEU   A 1 875  ? 166.618 193.591 133.473 1.00 115.34 ? 2207 LEU   A CD1  1 
ATOM   5005 C  CD2  . LEU   A 1 875  ? 168.399 195.215 132.794 1.00 102.22 ? 2207 LEU   A CD2  1 
ATOM   5006 N  N    . PRO   A 1 876  ? 168.072 198.999 136.043 1.00 136.36 ? 2208 PRO   A N    1 
ATOM   5007 C  CA   . PRO   A 1 876  ? 167.428 200.234 136.504 1.00 134.04 ? 2208 PRO   A CA   1 
ATOM   5008 C  C    . PRO   A 1 876  ? 166.442 200.797 135.483 1.00 131.75 ? 2208 PRO   A C    1 
ATOM   5009 O  O    . PRO   A 1 876  ? 166.421 200.323 134.348 1.00 124.36 ? 2208 PRO   A O    1 
ATOM   5010 C  CB   . PRO   A 1 876  ? 168.606 201.187 136.703 1.00 129.96 ? 2208 PRO   A CB   1 
ATOM   5011 C  CG   . PRO   A 1 876  ? 169.645 200.695 135.755 1.00 132.03 ? 2208 PRO   A CG   1 
ATOM   5012 C  CD   . PRO   A 1 876  ? 169.496 199.203 135.724 1.00 130.61 ? 2208 PRO   A CD   1 
ATOM   5013 N  N    . SER   A 1 881  ? 166.024 192.607 138.368 1.00 115.15 ? 2213 SER   A N    1 
ATOM   5014 C  CA   . SER   A 1 881  ? 167.426 192.361 138.067 1.00 109.23 ? 2213 SER   A CA   1 
ATOM   5015 C  C    . SER   A 1 881  ? 167.682 190.886 137.780 1.00 111.33 ? 2213 SER   A C    1 
ATOM   5016 O  O    . SER   A 1 881  ? 166.773 190.063 137.852 1.00 115.64 ? 2213 SER   A O    1 
ATOM   5017 C  CB   . SER   A 1 881  ? 168.312 192.829 139.218 1.00 104.89 ? 2213 SER   A CB   1 
ATOM   5018 O  OG   . SER   A 1 881  ? 169.671 192.560 138.937 1.00 101.92 ? 2213 SER   A OG   1 
ATOM   5019 N  N    . TRP   A 1 882  ? 168.931 190.563 137.460 1.00 102.93 ? 2214 TRP   A N    1 
ATOM   5020 C  CA   . TRP   A 1 882  ? 169.325 189.235 137.012 1.00 93.07  ? 2214 TRP   A CA   1 
ATOM   5021 C  C    . TRP   A 1 882  ? 170.514 188.760 137.832 1.00 84.03  ? 2214 TRP   A C    1 
ATOM   5022 O  O    . TRP   A 1 882  ? 171.437 189.533 138.098 1.00 81.84  ? 2214 TRP   A O    1 
ATOM   5023 C  CB   . TRP   A 1 882  ? 169.713 189.271 135.539 1.00 95.13  ? 2214 TRP   A CB   1 
ATOM   5024 C  CG   . TRP   A 1 882  ? 168.602 189.510 134.570 1.00 107.95 ? 2214 TRP   A CG   1 
ATOM   5025 C  CD1  . TRP   A 1 882  ? 168.645 190.353 133.506 1.00 112.25 ? 2214 TRP   A CD1  1 
ATOM   5026 C  CD2  . TRP   A 1 882  ? 167.343 188.827 134.484 1.00 111.58 ? 2214 TRP   A CD2  1 
ATOM   5027 N  NE1  . TRP   A 1 882  ? 167.471 190.302 132.808 1.00 115.82 ? 2214 TRP   A NE1  1 
ATOM   5028 C  CE2  . TRP   A 1 882  ? 166.657 189.363 133.380 1.00 118.54 ? 2214 TRP   A CE2  1 
ATOM   5029 C  CE3  . TRP   A 1 882  ? 166.719 187.838 135.243 1.00 104.96 ? 2214 TRP   A CE3  1 
ATOM   5030 C  CZ2  . TRP   A 1 882  ? 165.383 188.946 133.018 1.00 120.92 ? 2214 TRP   A CZ2  1 
ATOM   5031 C  CZ3  . TRP   A 1 882  ? 165.451 187.426 134.876 1.00 103.39 ? 2214 TRP   A CZ3  1 
ATOM   5032 C  CH2  . TRP   A 1 882  ? 164.798 187.979 133.779 1.00 109.80 ? 2214 TRP   A CH2  1 
ATOM   5033 N  N    . ILE   A 1 883  ? 170.491 187.490 138.225 1.00 78.90  ? 2215 ILE   A N    1 
ATOM   5034 C  CA   . ILE   A 1 883  ? 171.633 186.817 138.840 1.00 69.00  ? 2215 ILE   A CA   1 
ATOM   5035 C  C    . ILE   A 1 883  ? 172.214 185.852 137.818 1.00 68.16  ? 2215 ILE   A C    1 
ATOM   5036 O  O    . ILE   A 1 883  ? 171.486 185.060 137.209 1.00 75.37  ? 2215 ILE   A O    1 
ATOM   5037 C  CB   . ILE   A 1 883  ? 171.245 186.106 140.149 1.00 72.84  ? 2215 ILE   A CB   1 
ATOM   5038 C  CG1  . ILE   A 1 883  ? 172.480 185.640 140.918 1.00 66.67  ? 2215 ILE   A CG1  1 
ATOM   5039 C  CG2  . ILE   A 1 883  ? 170.301 184.966 139.918 1.00 78.43  ? 2215 ILE   A CG2  1 
ATOM   5040 C  CD1  . ILE   A 1 883  ? 173.334 186.732 141.429 1.00 69.10  ? 2215 ILE   A CD1  1 
ATOM   5041 N  N    . VAL   A 1 884  ? 173.520 185.939 137.604 1.00 60.49  ? 2216 VAL   A N    1 
ATOM   5042 C  CA   . VAL   A 1 884  ? 174.206 185.132 136.608 1.00 58.25  ? 2216 VAL   A CA   1 
ATOM   5043 C  C    . VAL   A 1 884  ? 175.068 184.125 137.341 1.00 62.26  ? 2216 VAL   A C    1 
ATOM   5044 O  O    . VAL   A 1 884  ? 176.049 184.499 137.992 1.00 67.66  ? 2216 VAL   A O    1 
ATOM   5045 C  CB   . VAL   A 1 884  ? 175.045 185.998 135.663 1.00 48.06  ? 2216 VAL   A CB   1 
ATOM   5046 C  CG1  . VAL   A 1 884  ? 175.835 185.132 134.719 1.00 38.90  ? 2216 VAL   A CG1  1 
ATOM   5047 C  CG2  . VAL   A 1 884  ? 174.135 186.904 134.881 1.00 61.52  ? 2216 VAL   A CG2  1 
ATOM   5048 N  N    . SER   A 1 885  ? 174.712 182.852 137.221 1.00 53.79  ? 2217 SER   A N    1 
ATOM   5049 C  CA   . SER   A 1 885  ? 175.420 181.762 137.869 1.00 40.57  ? 2217 SER   A CA   1 
ATOM   5050 C  C    . SER   A 1 885  ? 176.232 181.038 136.816 1.00 36.80  ? 2217 SER   A C    1 
ATOM   5051 O  O    . SER   A 1 885  ? 175.705 180.690 135.757 1.00 42.86  ? 2217 SER   A O    1 
ATOM   5052 C  CB   . SER   A 1 885  ? 174.447 180.792 138.537 1.00 53.95  ? 2217 SER   A CB   1 
ATOM   5053 O  OG   . SER   A 1 885  ? 173.733 181.423 139.579 1.00 67.44  ? 2217 SER   A OG   1 
ATOM   5054 N  N    . GLY   A 1 886  ? 177.509 180.815 137.099 1.00 32.49  ? 2218 GLY   A N    1 
ATOM   5055 C  CA   . GLY   A 1 886  ? 178.394 180.145 136.175 1.00 44.27  ? 2218 GLY   A CA   1 
ATOM   5056 C  C    . GLY   A 1 886  ? 178.729 178.747 136.670 1.00 47.68  ? 2218 GLY   A C    1 
ATOM   5057 O  O    . GLY   A 1 886  ? 179.189 178.577 137.797 1.00 58.80  ? 2218 GLY   A O    1 
ATOM   5058 N  N    . THR   A 1 887  ? 178.512 177.765 135.808 1.00 38.59  ? 2219 THR   A N    1 
ATOM   5059 C  CA   . THR   A 1 887  ? 178.596 176.366 136.194 1.00 48.22  ? 2219 THR   A CA   1 
ATOM   5060 C  C    . THR   A 1 887  ? 179.789 175.697 135.530 1.00 60.20  ? 2219 THR   A C    1 
ATOM   5061 O  O    . THR   A 1 887  ? 180.246 176.108 134.465 1.00 64.25  ? 2219 THR   A O    1 
ATOM   5062 C  CB   . THR   A 1 887  ? 177.322 175.626 135.806 1.00 59.44  ? 2219 THR   A CB   1 
ATOM   5063 O  OG1  . THR   A 1 887  ? 177.203 175.642 134.384 1.00 66.93  ? 2219 THR   A OG1  1 
ATOM   5064 C  CG2  . THR   A 1 887  ? 176.118 176.313 136.398 1.00 53.87  ? 2219 THR   A CG2  1 
ATOM   5065 N  N    . GLN   A 1 888  ? 180.263 174.618 136.158 1.00 63.53  ? 2220 GLN   A N    1 
ATOM   5066 C  CA   . GLN   A 1 888  ? 181.450 173.918 135.680 1.00 66.24  ? 2220 GLN   A CA   1 
ATOM   5067 C  C    . GLN   A 1 888  ? 181.276 173.337 134.286 1.00 69.69  ? 2220 GLN   A C    1 
ATOM   5068 O  O    . GLN   A 1 888  ? 182.264 173.225 133.555 1.00 61.97  ? 2220 GLN   A O    1 
ATOM   5069 C  CB   . GLN   A 1 888  ? 181.827 172.801 136.652 1.00 67.27  ? 2220 GLN   A CB   1 
ATOM   5070 C  CG   . GLN   A 1 888  ? 183.091 172.056 136.289 1.00 76.15  ? 2220 GLN   A CG   1 
ATOM   5071 C  CD   . GLN   A 1 888  ? 183.632 171.255 137.448 1.00 85.42  ? 2220 GLN   A CD   1 
ATOM   5072 O  OE1  . GLN   A 1 888  ? 182.875 170.646 138.201 1.00 93.80  ? 2220 GLN   A OE1  1 
ATOM   5073 N  NE2  . GLN   A 1 888  ? 184.948 171.256 137.604 1.00 79.81  ? 2220 GLN   A NE2  1 
ATOM   5074 N  N    . SER   A 1 889  ? 180.055 172.969 133.898 1.00 73.47  ? 2221 SER   A N    1 
ATOM   5075 C  CA   . SER   A 1 889  ? 179.839 172.499 132.535 1.00 73.45  ? 2221 SER   A CA   1 
ATOM   5076 C  C    . SER   A 1 889  ? 180.173 173.586 131.530 1.00 68.53  ? 2221 SER   A C    1 
ATOM   5077 O  O    . SER   A 1 889  ? 180.525 173.295 130.382 1.00 70.08  ? 2221 SER   A O    1 
ATOM   5078 C  CB   . SER   A 1 889  ? 178.397 172.033 132.357 1.00 76.72  ? 2221 SER   A CB   1 
ATOM   5079 O  OG   . SER   A 1 889  ? 177.474 173.041 132.720 1.00 74.86  ? 2221 SER   A OG   1 
ATOM   5080 N  N    . GLY   A 1 890  ? 180.073 174.840 131.946 1.00 64.21  ? 2222 GLY   A N    1 
ATOM   5081 C  CA   . GLY   A 1 890  ? 180.367 175.967 131.100 1.00 72.87  ? 2222 GLY   A CA   1 
ATOM   5082 C  C    . GLY   A 1 890  ? 179.180 176.846 130.801 1.00 69.90  ? 2222 GLY   A C    1 
ATOM   5083 O  O    . GLY   A 1 890  ? 179.375 177.989 130.378 1.00 72.62  ? 2222 GLY   A O    1 
ATOM   5084 N  N    . THR   A 1 891  ? 177.963 176.358 131.007 1.00 67.40  ? 2223 THR   A N    1 
ATOM   5085 C  CA   . THR   A 1 891  ? 176.792 177.175 130.737 1.00 60.64  ? 2223 THR   A CA   1 
ATOM   5086 C  C    . THR   A 1 891  ? 176.688 178.260 131.793 1.00 52.84  ? 2223 THR   A C    1 
ATOM   5087 O  O    . THR   A 1 891  ? 177.035 178.040 132.956 1.00 60.78  ? 2223 THR   A O    1 
ATOM   5088 C  CB   . THR   A 1 891  ? 175.519 176.327 130.699 1.00 67.27  ? 2223 THR   A CB   1 
ATOM   5089 O  OG1  . THR   A 1 891  ? 174.421 177.135 130.267 1.00 76.72  ? 2223 THR   A OG1  1 
ATOM   5090 C  CG2  . THR   A 1 891  ? 175.180 175.759 132.056 1.00 57.61  ? 2223 THR   A CG2  1 
ATOM   5091 N  N    . LEU   A 1 892  ? 176.264 179.443 131.375 1.00 48.32  ? 2224 LEU   A N    1 
ATOM   5092 C  CA   . LEU   A 1 892  ? 175.925 180.515 132.294 1.00 51.63  ? 2224 LEU   A CA   1 
ATOM   5093 C  C    . LEU   A 1 892  ? 174.413 180.609 132.366 1.00 49.29  ? 2224 LEU   A C    1 
ATOM   5094 O  O    . LEU   A 1 892  ? 173.753 180.774 131.338 1.00 53.95  ? 2224 LEU   A O    1 
ATOM   5095 C  CB   . LEU   A 1 892  ? 176.515 181.845 131.833 1.00 45.64  ? 2224 LEU   A CB   1 
ATOM   5096 C  CG   . LEU   A 1 892  ? 178.022 182.068 131.919 1.00 34.65  ? 2224 LEU   A CG   1 
ATOM   5097 C  CD1  . LEU   A 1 892  ? 178.752 181.387 130.794 1.00 41.84  ? 2224 LEU   A CD1  1 
ATOM   5098 C  CD2  . LEU   A 1 892  ? 178.296 183.544 131.902 1.00 35.66  ? 2224 LEU   A CD2  1 
ATOM   5099 N  N    . LEU   A 1 893  ? 173.861 180.497 133.565 1.00 44.74  ? 2225 LEU   A N    1 
ATOM   5100 C  CA   . LEU   A 1 893  ? 172.419 180.446 133.720 1.00 58.41  ? 2225 LEU   A CA   1 
ATOM   5101 C  C    . LEU   A 1 893  ? 171.984 181.685 134.480 1.00 71.57  ? 2225 LEU   A C    1 
ATOM   5102 O  O    . LEU   A 1 893  ? 172.613 182.059 135.472 1.00 72.35  ? 2225 LEU   A O    1 
ATOM   5103 C  CB   . LEU   A 1 893  ? 171.981 179.166 134.439 1.00 64.20  ? 2225 LEU   A CB   1 
ATOM   5104 C  CG   . LEU   A 1 893  ? 170.479 178.847 134.499 1.00 71.52  ? 2225 LEU   A CG   1 
ATOM   5105 C  CD1  . LEU   A 1 893  ? 170.258 177.349 134.618 1.00 78.57  ? 2225 LEU   A CD1  1 
ATOM   5106 C  CD2  . LEU   A 1 893  ? 169.761 179.538 135.614 1.00 73.58  ? 2225 LEU   A CD2  1 
ATOM   5107 N  N    . VAL   A 1 894  ? 170.925 182.327 133.999 1.00 78.31  ? 2226 VAL   A N    1 
ATOM   5108 C  CA   . VAL   A 1 894  ? 170.418 183.573 134.559 1.00 77.94  ? 2226 VAL   A CA   1 
ATOM   5109 C  C    . VAL   A 1 894  ? 169.076 183.294 135.223 1.00 86.32  ? 2226 VAL   A C    1 
ATOM   5110 O  O    . VAL   A 1 894  ? 168.201 182.662 134.620 1.00 89.84  ? 2226 VAL   A O    1 
ATOM   5111 C  CB   . VAL   A 1 894  ? 170.287 184.649 133.470 1.00 72.51  ? 2226 VAL   A CB   1 
ATOM   5112 C  CG1  . VAL   A 1 894  ? 169.437 185.803 133.953 1.00 84.32  ? 2226 VAL   A CG1  1 
ATOM   5113 C  CG2  . VAL   A 1 894  ? 171.658 185.122 133.043 1.00 67.49  ? 2226 VAL   A CG2  1 
ATOM   5114 N  N    . ILE   A 1 895  ? 168.913 183.763 136.461 1.00 85.98  ? 2227 ILE   A N    1 
ATOM   5115 C  CA   . ILE   A 1 895  ? 167.692 183.559 137.231 1.00 88.01  ? 2227 ILE   A CA   1 
ATOM   5116 C  C    . ILE   A 1 895  ? 167.077 184.924 137.500 1.00 92.18  ? 2227 ILE   A C    1 
ATOM   5117 O  O    . ILE   A 1 895  ? 167.798 185.901 137.726 1.00 94.44  ? 2227 ILE   A O    1 
ATOM   5118 C  CB   . ILE   A 1 895  ? 167.949 182.837 138.572 1.00 87.45  ? 2227 ILE   A CB   1 
ATOM   5119 C  CG1  . ILE   A 1 895  ? 168.564 181.457 138.370 1.00 84.37  ? 2227 ILE   A CG1  1 
ATOM   5120 C  CG2  . ILE   A 1 895  ? 166.664 182.690 139.361 1.00 100.73 ? 2227 ILE   A CG2  1 
ATOM   5121 C  CD1  . ILE   A 1 895  ? 170.077 181.489 138.359 1.00 80.16  ? 2227 ILE   A CD1  1 
ATOM   5122 N  N    . ASN   A 1 896  ? 165.750 184.998 137.468 1.00 96.67  ? 2228 ASN   A N    1 
ATOM   5123 C  CA   . ASN   A 1 896  ? 165.076 186.217 137.891 1.00 104.63 ? 2228 ASN   A CA   1 
ATOM   5124 C  C    . ASN   A 1 896  ? 165.280 186.442 139.380 1.00 106.35 ? 2228 ASN   A C    1 
ATOM   5125 O  O    . ASN   A 1 896  ? 165.046 185.549 140.198 1.00 110.31 ? 2228 ASN   A O    1 
ATOM   5126 C  CB   . ASN   A 1 896  ? 163.585 186.144 137.570 1.00 114.57 ? 2228 ASN   A CB   1 
ATOM   5127 N  N    . THR   A 1 897  ? 165.712 187.649 139.732 1.00 102.52 ? 2229 THR   A N    1 
ATOM   5128 C  CA   . THR   A 1 897  ? 165.962 187.981 141.125 1.00 105.38 ? 2229 THR   A CA   1 
ATOM   5129 C  C    . THR   A 1 897  ? 164.688 188.202 141.923 1.00 109.27 ? 2229 THR   A C    1 
ATOM   5130 O  O    . THR   A 1 897  ? 164.597 187.722 143.058 1.00 107.18 ? 2229 THR   A O    1 
ATOM   5131 C  CB   . THR   A 1 897  ? 166.838 189.234 141.224 1.00 103.72 ? 2229 THR   A CB   1 
ATOM   5132 O  OG1  . THR   A 1 897  ? 168.088 188.993 140.569 1.00 98.98  ? 2229 THR   A OG1  1 
ATOM   5133 C  CG2  . THR   A 1 897  ? 167.101 189.591 142.676 1.00 99.96  ? 2229 THR   A CG2  1 
ATOM   5134 N  N    . GLU   A 1 898  ? 163.702 188.893 141.358 1.00 112.53 ? 2230 GLU   A N    1 
ATOM   5135 C  CA   . GLU   A 1 898  ? 162.483 189.203 142.091 1.00 121.79 ? 2230 GLU   A CA   1 
ATOM   5136 C  C    . GLU   A 1 898  ? 161.397 188.166 141.836 1.00 129.71 ? 2230 GLU   A C    1 
ATOM   5137 O  O    . GLU   A 1 898  ? 160.969 187.468 142.761 1.00 131.03 ? 2230 GLU   A O    1 
ATOM   5138 C  CB   . GLU   A 1 898  ? 161.981 190.598 141.715 1.00 121.73 ? 2230 GLU   A CB   1 
ATOM   5139 N  N    . ASP   A 1 899  ? 160.948 188.054 140.583 1.00 128.33 ? 2231 ASP   A N    1 
ATOM   5140 C  CA   . ASP   A 1 899  ? 159.849 187.145 140.266 1.00 132.23 ? 2231 ASP   A CA   1 
ATOM   5141 C  C    . ASP   A 1 899  ? 160.266 185.692 140.453 1.00 130.63 ? 2231 ASP   A C    1 
ATOM   5142 O  O    . ASP   A 1 899  ? 159.536 184.896 141.052 1.00 135.49 ? 2231 ASP   A O    1 
ATOM   5143 C  CB   . ASP   A 1 899  ? 159.362 187.387 138.838 1.00 127.26 ? 2231 ASP   A CB   1 
ATOM   5144 N  N    . GLY   A 1 900  ? 161.440 185.328 139.941 1.00 125.17 ? 2232 GLY   A N    1 
ATOM   5145 C  CA   . GLY   A 1 900  ? 161.951 183.984 140.080 1.00 123.57 ? 2232 GLY   A CA   1 
ATOM   5146 C  C    . GLY   A 1 900  ? 161.390 182.975 139.107 1.00 122.29 ? 2232 GLY   A C    1 
ATOM   5147 O  O    . GLY   A 1 900  ? 161.772 181.800 139.173 1.00 123.34 ? 2232 GLY   A O    1 
ATOM   5148 N  N    . LYS   A 1 901  ? 160.498 183.385 138.205 1.00 119.41 ? 2233 LYS   A N    1 
ATOM   5149 C  CA   . LYS   A 1 901  ? 159.939 182.445 137.239 1.00 118.25 ? 2233 LYS   A CA   1 
ATOM   5150 C  C    . LYS   A 1 901  ? 160.670 182.530 135.905 1.00 113.49 ? 2233 LYS   A C    1 
ATOM   5151 O  O    . LYS   A 1 901  ? 161.032 181.505 135.317 1.00 111.23 ? 2233 LYS   A O    1 
ATOM   5152 C  CB   . LYS   A 1 901  ? 158.445 182.709 137.054 1.00 116.84 ? 2233 LYS   A CB   1 
ATOM   5153 N  N    . LYS   A 1 902  ? 160.902 183.746 135.416 1.00 119.05 ? 2234 LYS   A N    1 
ATOM   5154 C  CA   . LYS   A 1 902  ? 161.559 183.951 134.130 1.00 121.18 ? 2234 LYS   A CA   1 
ATOM   5155 C  C    . LYS   A 1 902  ? 163.036 183.609 134.271 1.00 118.54 ? 2234 LYS   A C    1 
ATOM   5156 O  O    . LYS   A 1 902  ? 163.819 184.401 134.803 1.00 117.73 ? 2234 LYS   A O    1 
ATOM   5157 C  CB   . LYS   A 1 902  ? 161.370 185.389 133.657 1.00 119.52 ? 2234 LYS   A CB   1 
ATOM   5158 N  N    . ARG   A 1 903  ? 163.416 182.426 133.796 1.00 117.63 ? 2235 ARG   A N    1 
ATOM   5159 C  CA   . ARG   A 1 903  ? 164.775 181.929 133.931 1.00 109.64 ? 2235 ARG   A CA   1 
ATOM   5160 C  C    . ARG   A 1 903  ? 165.218 181.327 132.607 1.00 103.09 ? 2235 ARG   A C    1 
ATOM   5161 O  O    . ARG   A 1 903  ? 164.417 180.731 131.883 1.00 110.19 ? 2235 ARG   A O    1 
ATOM   5162 C  CB   . ARG   A 1 903  ? 164.867 180.883 135.046 1.00 109.25 ? 2235 ARG   A CB   1 
ATOM   5163 C  CG   . ARG   A 1 903  ? 164.151 181.285 136.328 1.00 107.43 ? 2235 ARG   A CG   1 
ATOM   5164 C  CD   . ARG   A 1 903  ? 163.660 180.069 137.079 1.00 108.68 ? 2235 ARG   A CD   1 
ATOM   5165 N  NE   . ARG   A 1 903  ? 164.735 179.458 137.847 1.00 104.79 ? 2235 ARG   A NE   1 
ATOM   5166 C  CZ   . ARG   A 1 903  ? 165.426 178.399 137.451 1.00 107.40 ? 2235 ARG   A CZ   1 
ATOM   5167 N  NH1  . ARG   A 1 903  ? 165.170 177.798 136.302 1.00 117.48 ? 2235 ARG   A NH1  1 
ATOM   5168 N  NH2  . ARG   A 1 903  ? 166.402 177.938 138.223 1.00 93.51  ? 2235 ARG   A NH2  1 
ATOM   5169 N  N    . HIS   A 1 904  ? 166.501 181.482 132.295 1.00 96.06  ? 2236 HIS   A N    1 
ATOM   5170 C  CA   . HIS   A 1 904  ? 167.019 180.979 131.030 1.00 100.70 ? 2236 HIS   A CA   1 
ATOM   5171 C  C    . HIS   A 1 904  ? 168.532 180.873 131.111 1.00 96.88  ? 2236 HIS   A C    1 
ATOM   5172 O  O    . HIS   A 1 904  ? 169.152 181.402 132.037 1.00 92.78  ? 2236 HIS   A O    1 
ATOM   5173 C  CB   . HIS   A 1 904  ? 166.606 181.877 129.859 1.00 94.00  ? 2236 HIS   A CB   1 
ATOM   5174 C  CG   . HIS   A 1 904  ? 167.138 183.272 129.948 1.00 95.40  ? 2236 HIS   A CG   1 
ATOM   5175 N  ND1  . HIS   A 1 904  ? 168.486 183.555 129.992 1.00 93.00  ? 2236 HIS   A ND1  1 
ATOM   5176 C  CD2  . HIS   A 1 904  ? 166.500 184.464 130.003 1.00 103.77 ? 2236 HIS   A CD2  1 
ATOM   5177 C  CE1  . HIS   A 1 904  ? 168.655 184.862 130.072 1.00 102.72 ? 2236 HIS   A CE1  1 
ATOM   5178 N  NE2  . HIS   A 1 904  ? 167.466 185.437 130.078 1.00 110.26 ? 2236 HIS   A NE2  1 
ATOM   5179 N  N    . THR   A 1 905  ? 169.115 180.193 130.127 1.00 91.67  ? 2237 THR   A N    1 
ATOM   5180 C  CA   . THR   A 1 905  ? 170.555 180.013 130.065 1.00 82.58  ? 2237 THR   A CA   1 
ATOM   5181 C  C    . THR   A 1 905  ? 171.180 181.017 129.102 1.00 80.72  ? 2237 THR   A C    1 
ATOM   5182 O  O    . THR   A 1 905  ? 170.516 181.903 128.560 1.00 78.32  ? 2237 THR   A O    1 
ATOM   5183 C  CB   . THR   A 1 905  ? 170.898 178.590 129.642 1.00 74.32  ? 2237 THR   A CB   1 
ATOM   5184 O  OG1  . THR   A 1 905  ? 172.311 178.394 129.750 1.00 72.28  ? 2237 THR   A OG1  1 
ATOM   5185 C  CG2  . THR   A 1 905  ? 170.482 178.355 128.210 1.00 69.85  ? 2237 THR   A CG2  1 
ATOM   5186 N  N    . LEU   A 1 906  ? 172.490 180.881 128.902 1.00 81.15  ? 2238 LEU   A N    1 
ATOM   5187 C  CA   . LEU   A 1 906  ? 173.217 181.685 127.930 1.00 84.75  ? 2238 LEU   A CA   1 
ATOM   5188 C  C    . LEU   A 1 906  ? 174.122 180.792 127.093 1.00 89.20  ? 2238 LEU   A C    1 
ATOM   5189 O  O    . LEU   A 1 906  ? 173.976 179.566 127.119 1.00 93.98  ? 2238 LEU   A O    1 
ATOM   5190 C  CB   . LEU   A 1 906  ? 174.026 182.780 128.620 1.00 77.28  ? 2238 LEU   A CB   1 
ATOM   5191 C  CG   . LEU   A 1 906  ? 173.184 183.840 129.323 1.00 83.89  ? 2238 LEU   A CG   1 
ATOM   5192 C  CD1  . LEU   A 1 906  ? 174.074 184.802 130.082 1.00 71.83  ? 2238 LEU   A CD1  1 
ATOM   5193 C  CD2  . LEU   A 1 906  ? 172.304 184.577 128.338 1.00 91.16  ? 2238 LEU   A CD2  1 
ATOM   5194 N  N    . GLU   A 1 907  ? 175.041 181.386 126.338 1.00 81.92  ? 2239 GLU   A N    1 
ATOM   5195 C  CA   . GLU   A 1 907  ? 175.911 180.598 125.479 1.00 79.32  ? 2239 GLU   A CA   1 
ATOM   5196 C  C    . GLU   A 1 907  ? 176.764 179.633 126.286 1.00 81.99  ? 2239 GLU   A C    1 
ATOM   5197 O  O    . GLU   A 1 907  ? 177.498 180.031 127.191 1.00 78.18  ? 2239 GLU   A O    1 
ATOM   5198 C  CB   . GLU   A 1 907  ? 176.830 181.502 124.665 1.00 83.57  ? 2239 GLU   A CB   1 
ATOM   5199 C  CG   . GLU   A 1 907  ? 177.713 180.723 123.697 1.00 95.80  ? 2239 GLU   A CG   1 
ATOM   5200 C  CD   . GLU   A 1 907  ? 178.602 181.613 122.856 1.00 106.25 ? 2239 GLU   A CD   1 
ATOM   5201 O  OE1  . GLU   A 1 907  ? 178.550 182.840 123.040 1.00 93.86  ? 2239 GLU   A OE1  1 
ATOM   5202 O  OE2  . GLU   A 1 907  ? 179.359 181.085 122.016 1.00 118.71 ? 2239 GLU   A OE2  1 
ATOM   5203 N  N    . LYS   A 1 908  ? 176.692 178.360 125.921 1.00 89.52  ? 2240 LYS   A N    1 
ATOM   5204 C  CA   . LYS   A 1 908  ? 177.600 177.357 126.451 1.00 86.10  ? 2240 LYS   A CA   1 
ATOM   5205 C  C    . LYS   A 1 908  ? 179.028 177.730 126.083 1.00 92.12  ? 2240 LYS   A C    1 
ATOM   5206 O  O    . LYS   A 1 908  ? 179.300 178.130 124.948 1.00 102.06 ? 2240 LYS   A O    1 
ATOM   5207 C  CB   . LYS   A 1 908  ? 177.240 175.983 125.889 1.00 90.76  ? 2240 LYS   A CB   1 
ATOM   5208 C  CG   . LYS   A 1 908  ? 176.361 175.134 126.781 1.00 75.89  ? 2240 LYS   A CG   1 
ATOM   5209 C  CD   . LYS   A 1 908  ? 177.179 174.498 127.879 1.00 81.71  ? 2240 LYS   A CD   1 
ATOM   5210 C  CE   . LYS   A 1 908  ? 178.416 173.833 127.289 1.00 90.31  ? 2240 LYS   A CE   1 
ATOM   5211 N  NZ   . LYS   A 1 908  ? 179.241 173.119 128.300 1.00 91.12  ? 2240 LYS   A NZ   1 
ATOM   5212 N  N    . MET   A 1 909  ? 179.934 177.622 127.041 1.00 82.33  ? 2241 MET   A N    1 
ATOM   5213 C  CA   . MET   A 1 909  ? 181.317 177.993 126.806 1.00 91.82  ? 2241 MET   A CA   1 
ATOM   5214 C  C    . MET   A 1 909  ? 182.189 176.748 126.736 1.00 96.57  ? 2241 MET   A C    1 
ATOM   5215 O  O    . MET   A 1 909  ? 181.803 175.667 127.184 1.00 97.25  ? 2241 MET   A O    1 
ATOM   5216 C  CB   . MET   A 1 909  ? 181.801 178.948 127.894 1.00 88.22  ? 2241 MET   A CB   1 
ATOM   5217 C  CG   . MET   A 1 909  ? 181.098 180.294 127.795 1.00 87.21  ? 2241 MET   A CG   1 
ATOM   5218 S  SD   . MET   A 1 909  ? 182.085 181.737 128.202 1.00 76.88  ? 2241 MET   A SD   1 
ATOM   5219 C  CE   . MET   A 1 909  ? 181.010 183.031 127.598 1.00 42.97  ? 2241 MET   A CE   1 
ATOM   5220 N  N    . THR   A 1 910  ? 183.376 176.912 126.149 1.00 93.71  ? 2242 THR   A N    1 
ATOM   5221 C  CA   . THR   A 1 910  ? 184.208 175.756 125.826 1.00 91.91  ? 2242 THR   A CA   1 
ATOM   5222 C  C    . THR   A 1 910  ? 184.577 174.970 127.077 1.00 93.96  ? 2242 THR   A C    1 
ATOM   5223 O  O    . THR   A 1 910  ? 184.447 173.741 127.112 1.00 104.89 ? 2242 THR   A O    1 
ATOM   5224 C  CB   . THR   A 1 910  ? 185.464 176.202 125.081 1.00 84.74  ? 2242 THR   A CB   1 
ATOM   5225 O  OG1  . THR   A 1 910  ? 186.230 177.078 125.916 1.00 94.37  ? 2242 THR   A OG1  1 
ATOM   5226 C  CG2  . THR   A 1 910  ? 185.094 176.925 123.806 1.00 83.15  ? 2242 THR   A CG2  1 
ATOM   5227 N  N    . ASP   A 1 911  ? 185.029 175.657 128.115 1.00 82.10  ? 2243 ASP   A N    1 
ATOM   5228 C  CA   . ASP   A 1 911  ? 185.376 175.016 129.372 1.00 77.55  ? 2243 ASP   A CA   1 
ATOM   5229 C  C    . ASP   A 1 911  ? 184.597 175.674 130.503 1.00 77.14  ? 2243 ASP   A C    1 
ATOM   5230 O  O    . ASP   A 1 911  ? 183.717 176.506 130.276 1.00 76.19  ? 2243 ASP   A O    1 
ATOM   5231 C  CB   . ASP   A 1 911  ? 186.882 175.079 129.613 1.00 83.69  ? 2243 ASP   A CB   1 
ATOM   5232 C  CG   . ASP   A 1 911  ? 187.657 174.213 128.652 1.00 103.62 ? 2243 ASP   A CG   1 
ATOM   5233 O  OD1  . ASP   A 1 911  ? 187.106 173.190 128.196 1.00 112.99 ? 2243 ASP   A OD1  1 
ATOM   5234 O  OD2  . ASP   A 1 911  ? 188.819 174.551 128.351 1.00 107.72 ? 2243 ASP   A OD2  1 
ATOM   5235 N  N    . SER   A 1 912  ? 184.935 175.294 131.731 1.00 80.66  ? 2244 SER   A N    1 
ATOM   5236 C  CA   . SER   A 1 912  ? 184.234 175.819 132.891 1.00 70.43  ? 2244 SER   A CA   1 
ATOM   5237 C  C    . SER   A 1 912  ? 184.431 177.323 133.003 1.00 69.10  ? 2244 SER   A C    1 
ATOM   5238 O  O    . SER   A 1 912  ? 185.448 177.870 132.578 1.00 78.80  ? 2244 SER   A O    1 
ATOM   5239 C  CB   . SER   A 1 912  ? 184.731 175.144 134.163 1.00 58.99  ? 2244 SER   A CB   1 
ATOM   5240 O  OG   . SER   A 1 912  ? 184.074 175.682 135.292 1.00 62.63  ? 2244 SER   A OG   1 
ATOM   5241 N  N    . VAL   A 1 913  ? 183.439 177.995 133.571 1.00 59.14  ? 2245 VAL   A N    1 
ATOM   5242 C  CA   . VAL   A 1 913  ? 183.532 179.417 133.866 1.00 54.99  ? 2245 VAL   A CA   1 
ATOM   5243 C  C    . VAL   A 1 913  ? 184.072 179.571 135.274 1.00 48.97  ? 2245 VAL   A C    1 
ATOM   5244 O  O    . VAL   A 1 913  ? 183.767 178.769 136.163 1.00 50.80  ? 2245 VAL   A O    1 
ATOM   5245 C  CB   . VAL   A 1 913  ? 182.174 180.120 133.722 1.00 47.51  ? 2245 VAL   A CB   1 
ATOM   5246 C  CG1  . VAL   A 1 913  ? 181.680 180.011 132.308 1.00 57.40  ? 2245 VAL   A CG1  1 
ATOM   5247 C  CG2  . VAL   A 1 913  ? 181.214 179.494 134.629 1.00 43.90  ? 2245 VAL   A CG2  1 
ATOM   5248 N  N    . THR   A 1 914  ? 184.899 180.586 135.477 1.00 50.30  ? 2246 THR   A N    1 
ATOM   5249 C  CA   . THR   A 1 914  ? 185.555 180.792 136.756 1.00 58.91  ? 2246 THR   A CA   1 
ATOM   5250 C  C    . THR   A 1 914  ? 185.111 182.071 137.445 1.00 56.70  ? 2246 THR   A C    1 
ATOM   5251 O  O    . THR   A 1 914  ? 184.640 182.025 138.584 1.00 52.96  ? 2246 THR   A O    1 
ATOM   5252 C  CB   . THR   A 1 914  ? 187.077 180.804 136.566 1.00 66.61  ? 2246 THR   A CB   1 
ATOM   5253 O  OG1  . THR   A 1 914  ? 187.500 179.553 136.017 1.00 61.05  ? 2246 THR   A OG1  1 
ATOM   5254 C  CG2  . THR   A 1 914  ? 187.769 181.013 137.892 1.00 71.69  ? 2246 THR   A CG2  1 
ATOM   5255 N  N    . CYS   A 1 915  ? 185.230 183.215 136.778 1.00 49.61  ? 2247 CYS   A N    1 
ATOM   5256 C  CA   . CYS   A 1 915  ? 184.978 184.502 137.408 1.00 45.31  ? 2247 CYS   A CA   1 
ATOM   5257 C  C    . CYS   A 1 915  ? 183.946 185.280 136.613 1.00 38.64  ? 2247 CYS   A C    1 
ATOM   5258 O  O    . CYS   A 1 915  ? 183.889 185.183 135.390 1.00 41.64  ? 2247 CYS   A O    1 
ATOM   5259 C  CB   . CYS   A 1 915  ? 186.247 185.321 137.511 1.00 44.91  ? 2247 CYS   A CB   1 
ATOM   5260 S  SG   . CYS   A 1 915  ? 186.918 185.771 135.917 1.00 66.08  ? 2247 CYS   A SG   1 
ATOM   5261 N  N    . LEU   A 1 916  ? 183.126 186.056 137.314 1.00 30.85  ? 2248 LEU   A N    1 
ATOM   5262 C  CA   . LEU   A 1 916  ? 182.106 186.858 136.655 1.00 31.26  ? 2248 LEU   A CA   1 
ATOM   5263 C  C    . LEU   A 1 916  ? 182.160 188.302 137.133 1.00 40.80  ? 2248 LEU   A C    1 
ATOM   5264 O  O    . LEU   A 1 916  ? 182.181 188.564 138.338 1.00 46.86  ? 2248 LEU   A O    1 
ATOM   5265 C  CB   . LEU   A 1 916  ? 180.704 186.297 136.896 1.00 27.86  ? 2248 LEU   A CB   1 
ATOM   5266 C  CG   . LEU   A 1 916  ? 180.113 185.260 135.951 1.00 21.69  ? 2248 LEU   A CG   1 
ATOM   5267 C  CD1  . LEU   A 1 916  ? 181.055 184.142 135.671 1.00 29.92  ? 2248 LEU   A CD1  1 
ATOM   5268 C  CD2  . LEU   A 1 916  ? 178.833 184.727 136.516 1.00 32.94  ? 2248 LEU   A CD2  1 
ATOM   5269 N  N    . TYR   A 1 917  ? 182.181 189.225 136.177 1.00 35.99  ? 2249 TYR   A N    1 
ATOM   5270 C  CA   . TYR   A 1 917  ? 181.930 190.655 136.364 1.00 38.39  ? 2249 TYR   A CA   1 
ATOM   5271 C  C    . TYR   A 1 917  ? 183.054 191.221 137.225 1.00 45.42  ? 2249 TYR   A C    1 
ATOM   5272 O  O    . TYR   A 1 917  ? 184.219 191.160 136.804 1.00 45.30  ? 2249 TYR   A O    1 
ATOM   5273 C  CB   . TYR   A 1 917  ? 180.519 190.840 136.905 1.00 41.12  ? 2249 TYR   A CB   1 
ATOM   5274 C  CG   . TYR   A 1 917  ? 180.068 192.277 136.977 1.00 41.76  ? 2249 TYR   A CG   1 
ATOM   5275 C  CD1  . TYR   A 1 917  ? 180.088 192.979 138.166 1.00 53.96  ? 2249 TYR   A CD1  1 
ATOM   5276 C  CD2  . TYR   A 1 917  ? 179.588 192.919 135.851 1.00 36.88  ? 2249 TYR   A CD2  1 
ATOM   5277 C  CE1  . TYR   A 1 917  ? 179.678 194.283 138.226 1.00 60.28  ? 2249 TYR   A CE1  1 
ATOM   5278 C  CE2  . TYR   A 1 917  ? 179.171 194.216 135.899 1.00 42.32  ? 2249 TYR   A CE2  1 
ATOM   5279 C  CZ   . TYR   A 1 917  ? 179.218 194.898 137.089 1.00 65.96  ? 2249 TYR   A CZ   1 
ATOM   5280 O  OH   . TYR   A 1 917  ? 178.798 196.207 137.147 1.00 90.95  ? 2249 TYR   A OH   1 
ATOM   5281 N  N    . CYS   A 1 918  ? 182.767 191.746 138.412 1.00 53.52  ? 2250 CYS   A N    1 
ATOM   5282 C  CA   . CYS   A 1 918  ? 183.668 192.620 139.161 1.00 71.83  ? 2250 CYS   A CA   1 
ATOM   5283 C  C    . CYS   A 1 918  ? 184.080 193.811 138.293 1.00 67.22  ? 2250 CYS   A C    1 
ATOM   5284 O  O    . CYS   A 1 918  ? 185.247 194.009 137.954 1.00 64.01  ? 2250 CYS   A O    1 
ATOM   5285 C  CB   . CYS   A 1 918  ? 184.884 191.861 139.695 1.00 72.72  ? 2250 CYS   A CB   1 
ATOM   5286 S  SG   . CYS   A 1 918  ? 185.981 192.879 140.705 1.00 89.68  ? 2250 CYS   A SG   1 
ATOM   5287 N  N    . ASN   A 1 919  ? 183.075 194.592 137.917 1.00 68.16  ? 2251 ASN   A N    1 
ATOM   5288 C  CA   . ASN   A 1 919  ? 183.255 195.784 137.101 1.00 71.17  ? 2251 ASN   A CA   1 
ATOM   5289 C  C    . ASN   A 1 919  ? 182.889 197.032 137.892 1.00 78.34  ? 2251 ASN   A C    1 
ATOM   5290 O  O    . ASN   A 1 919  ? 181.716 197.364 138.048 1.00 82.40  ? 2251 ASN   A O    1 
ATOM   5291 C  CB   . ASN   A 1 919  ? 182.406 195.704 135.835 1.00 67.28  ? 2251 ASN   A CB   1 
ATOM   5292 C  CG   . ASN   A 1 919  ? 182.895 196.627 134.754 1.00 64.30  ? 2251 ASN   A CG   1 
ATOM   5293 O  OD1  . ASN   A 1 919  ? 183.627 196.215 133.856 1.00 74.85  ? 2251 ASN   A OD1  1 
ATOM   5294 N  ND2  . ASN   A 1 919  ? 182.511 197.890 134.840 1.00 58.36  ? 2251 ASN   A ND2  1 
ATOM   5295 N  N    . PHE   A 1 930  ? 181.301 195.436 131.863 1.00 60.99  ? 2262 PHE   A N    1 
ATOM   5296 C  CA   . PHE   A 1 930  ? 179.937 194.925 131.830 1.00 68.39  ? 2262 PHE   A CA   1 
ATOM   5297 C  C    . PHE   A 1 930  ? 179.822 193.459 131.379 1.00 63.40  ? 2262 PHE   A C    1 
ATOM   5298 O  O    . PHE   A 1 930  ? 180.220 193.078 130.288 1.00 73.90  ? 2262 PHE   A O    1 
ATOM   5299 C  CB   . PHE   A 1 930  ? 179.063 195.871 130.994 1.00 76.74  ? 2262 PHE   A CB   1 
ATOM   5300 C  CG   . PHE   A 1 930  ? 179.485 196.017 129.555 1.00 80.18  ? 2262 PHE   A CG   1 
ATOM   5301 C  CD1  . PHE   A 1 930  ? 180.371 197.003 129.176 1.00 81.69  ? 2262 PHE   A CD1  1 
ATOM   5302 C  CD2  . PHE   A 1 930  ? 178.995 195.180 128.589 1.00 83.23  ? 2262 PHE   A CD2  1 
ATOM   5303 C  CE1  . PHE   A 1 930  ? 180.733 197.153 127.854 1.00 87.54  ? 2262 PHE   A CE1  1 
ATOM   5304 C  CE2  . PHE   A 1 930  ? 179.368 195.318 127.268 1.00 86.81  ? 2262 PHE   A CE2  1 
ATOM   5305 C  CZ   . PHE   A 1 930  ? 180.236 196.302 126.903 1.00 87.80  ? 2262 PHE   A CZ   1 
ATOM   5306 N  N    . LEU   A 1 931  ? 179.269 192.666 132.298 1.00 55.28  ? 2263 LEU   A N    1 
ATOM   5307 C  CA   . LEU   A 1 931  ? 179.265 191.210 132.435 1.00 45.98  ? 2263 LEU   A CA   1 
ATOM   5308 C  C    . LEU   A 1 931  ? 180.519 190.558 131.859 1.00 34.41  ? 2263 LEU   A C    1 
ATOM   5309 O  O    . LEU   A 1 931  ? 180.444 189.798 130.895 1.00 41.69  ? 2263 LEU   A O    1 
ATOM   5310 C  CB   . LEU   A 1 931  ? 177.993 190.602 131.855 1.00 44.02  ? 2263 LEU   A CB   1 
ATOM   5311 C  CG   . LEU   A 1 931  ? 177.794 189.134 132.253 1.00 38.43  ? 2263 LEU   A CG   1 
ATOM   5312 C  CD1  . LEU   A 1 931  ? 178.124 188.931 133.706 1.00 35.90  ? 2263 LEU   A CD1  1 
ATOM   5313 C  CD2  . LEU   A 1 931  ? 176.364 188.745 132.029 1.00 43.21  ? 2263 LEU   A CD2  1 
ATOM   5314 N  N    . LEU   A 1 932  ? 181.679 190.891 132.395 1.00 29.91  ? 2264 LEU   A N    1 
ATOM   5315 C  CA   . LEU   A 1 932  ? 182.875 190.148 132.051 1.00 29.38  ? 2264 LEU   A CA   1 
ATOM   5316 C  C    . LEU   A 1 932  ? 182.675 188.695 132.454 1.00 31.34  ? 2264 LEU   A C    1 
ATOM   5317 O  O    . LEU   A 1 932  ? 182.009 188.412 133.447 1.00 37.57  ? 2264 LEU   A O    1 
ATOM   5318 C  CB   . LEU   A 1 932  ? 184.056 190.747 132.793 1.00 39.75  ? 2264 LEU   A CB   1 
ATOM   5319 C  CG   . LEU   A 1 932  ? 184.420 192.174 132.408 1.00 40.48  ? 2264 LEU   A CG   1 
ATOM   5320 C  CD1  . LEU   A 1 932  ? 185.492 192.658 133.330 1.00 41.75  ? 2264 LEU   A CD1  1 
ATOM   5321 C  CD2  . LEU   A 1 932  ? 184.897 192.240 130.990 1.00 43.46  ? 2264 LEU   A CD2  1 
ATOM   5322 N  N    . VAL   A 1 933  ? 183.217 187.760 131.677 1.00 32.79  ? 2265 VAL   A N    1 
ATOM   5323 C  CA   . VAL   A 1 933  ? 183.101 186.334 131.991 1.00 28.27  ? 2265 VAL   A CA   1 
ATOM   5324 C  C    . VAL   A 1 933  ? 184.437 185.663 131.734 1.00 34.54  ? 2265 VAL   A C    1 
ATOM   5325 O  O    . VAL   A 1 933  ? 184.856 185.540 130.582 1.00 51.97  ? 2265 VAL   A O    1 
ATOM   5326 C  CB   . VAL   A 1 933  ? 182.005 185.643 131.177 1.00 28.11  ? 2265 VAL   A CB   1 
ATOM   5327 C  CG1  . VAL   A 1 933  ? 182.024 184.174 131.467 1.00 28.20  ? 2265 VAL   A CG1  1 
ATOM   5328 C  CG2  . VAL   A 1 933  ? 180.656 186.214 131.514 1.00 29.86  ? 2265 VAL   A CG2  1 
ATOM   5329 N  N    . GLY   A 1 934  ? 185.087 185.193 132.785 1.00 31.92  ? 2266 GLY   A N    1 
ATOM   5330 C  CA   . GLY   A 1 934  ? 186.355 184.522 132.614 1.00 42.49  ? 2266 GLY   A CA   1 
ATOM   5331 C  C    . GLY   A 1 934  ? 186.255 183.035 132.853 1.00 53.95  ? 2266 GLY   A C    1 
ATOM   5332 O  O    . GLY   A 1 934  ? 185.925 182.606 133.963 1.00 63.47  ? 2266 GLY   A O    1 
ATOM   5333 N  N    . THR   A 1 935  ? 186.556 182.246 131.827 1.00 57.49  ? 2267 THR   A N    1 
ATOM   5334 C  CA   . THR   A 1 935  ? 186.427 180.801 131.855 1.00 59.88  ? 2267 THR   A CA   1 
ATOM   5335 C  C    . THR   A 1 935  ? 187.709 180.160 132.382 1.00 64.92  ? 2267 THR   A C    1 
ATOM   5336 O  O    . THR   A 1 935  ? 188.590 180.828 132.929 1.00 66.19  ? 2267 THR   A O    1 
ATOM   5337 C  CB   . THR   A 1 935  ? 186.088 180.279 130.463 1.00 56.29  ? 2267 THR   A CB   1 
ATOM   5338 O  OG1  . THR   A 1 935  ? 187.287 180.204 129.685 1.00 62.81  ? 2267 THR   A OG1  1 
ATOM   5339 C  CG2  . THR   A 1 935  ? 185.124 181.205 129.779 1.00 49.64  ? 2267 THR   A CG2  1 
ATOM   5340 N  N    . ALA   A 1 936  ? 187.809 178.842 132.227 1.00 73.12  ? 2268 ALA   A N    1 
ATOM   5341 C  CA   . ALA   A 1 936  ? 188.944 178.073 132.716 1.00 75.87  ? 2268 ALA   A CA   1 
ATOM   5342 C  C    . ALA   A 1 936  ? 189.990 177.812 131.647 1.00 78.46  ? 2268 ALA   A C    1 
ATOM   5343 O  O    . ALA   A 1 936  ? 190.905 177.017 131.880 1.00 82.31  ? 2268 ALA   A O    1 
ATOM   5344 C  CB   . ALA   A 1 936  ? 188.475 176.737 133.300 1.00 69.55  ? 2268 ALA   A CB   1 
ATOM   5345 N  N    . ASP   A 1 937  ? 189.871 178.439 130.479 1.00 77.13  ? 2269 ASP   A N    1 
ATOM   5346 C  CA   . ASP   A 1 937  ? 190.879 178.337 129.433 1.00 86.71  ? 2269 ASP   A CA   1 
ATOM   5347 C  C    . ASP   A 1 937  ? 191.438 179.694 129.016 1.00 89.05  ? 2269 ASP   A C    1 
ATOM   5348 O  O    . ASP   A 1 937  ? 192.098 179.788 127.975 1.00 86.42  ? 2269 ASP   A O    1 
ATOM   5349 C  CB   . ASP   A 1 937  ? 190.308 177.590 128.225 1.00 83.55  ? 2269 ASP   A CB   1 
ATOM   5350 C  CG   . ASP   A 1 937  ? 188.997 178.167 127.752 1.00 84.98  ? 2269 ASP   A CG   1 
ATOM   5351 O  OD1  . ASP   A 1 937  ? 188.690 179.315 128.122 1.00 85.22  ? 2269 ASP   A OD1  1 
ATOM   5352 O  OD2  . ASP   A 1 937  ? 188.273 177.476 127.008 1.00 91.47  ? 2269 ASP   A OD2  1 
ATOM   5353 N  N    . GLY   A 1 938  ? 191.196 180.743 129.799 1.00 82.60  ? 2270 GLY   A N    1 
ATOM   5354 C  CA   . GLY   A 1 938  ? 191.660 182.072 129.478 1.00 78.44  ? 2270 GLY   A CA   1 
ATOM   5355 C  C    . GLY   A 1 938  ? 190.786 182.817 128.501 1.00 73.09  ? 2270 GLY   A C    1 
ATOM   5356 O  O    . GLY   A 1 938  ? 191.064 183.984 128.204 1.00 70.09  ? 2270 GLY   A O    1 
ATOM   5357 N  N    . LYS   A 1 939  ? 189.731 182.187 128.009 1.00 74.98  ? 2271 LYS   A N    1 
ATOM   5358 C  CA   . LYS   A 1 939  ? 188.902 182.736 126.944 1.00 69.73  ? 2271 LYS   A CA   1 
ATOM   5359 C  C    . LYS   A 1 939  ? 187.892 183.677 127.579 1.00 57.67  ? 2271 LYS   A C    1 
ATOM   5360 O  O    . LYS   A 1 939  ? 186.780 183.285 127.922 1.00 56.96  ? 2271 LYS   A O    1 
ATOM   5361 C  CB   . LYS   A 1 939  ? 188.230 181.602 126.184 1.00 74.00  ? 2271 LYS   A CB   1 
ATOM   5362 C  CG   . LYS   A 1 939  ? 187.465 182.007 124.974 1.00 75.12  ? 2271 LYS   A CG   1 
ATOM   5363 C  CD   . LYS   A 1 939  ? 186.836 180.812 124.287 1.00 73.29  ? 2271 LYS   A CD   1 
ATOM   5364 C  CE   . LYS   A 1 939  ? 187.887 179.955 123.610 1.00 68.89  ? 2271 LYS   A CE   1 
ATOM   5365 N  NZ   . LYS   A 1 939  ? 188.509 180.678 122.468 1.00 80.55  ? 2271 LYS   A NZ   1 
ATOM   5366 N  N    . LEU   A 1 940  ? 188.277 184.939 127.740 1.00 48.53  ? 2272 LEU   A N    1 
ATOM   5367 C  CA   . LEU   A 1 940  ? 187.442 185.889 128.461 1.00 44.33  ? 2272 LEU   A CA   1 
ATOM   5368 C  C    . LEU   A 1 940  ? 186.421 186.484 127.503 1.00 46.45  ? 2272 LEU   A C    1 
ATOM   5369 O  O    . LEU   A 1 940  ? 186.779 186.981 126.433 1.00 59.45  ? 2272 LEU   A O    1 
ATOM   5370 C  CB   . LEU   A 1 940  ? 188.307 186.981 129.087 1.00 45.51  ? 2272 LEU   A CB   1 
ATOM   5371 C  CG   . LEU   A 1 940  ? 187.710 188.081 129.972 1.00 47.29  ? 2272 LEU   A CG   1 
ATOM   5372 C  CD1  . LEU   A 1 940  ? 188.826 188.748 130.741 1.00 57.01  ? 2272 LEU   A CD1  1 
ATOM   5373 C  CD2  . LEU   A 1 940  ? 186.951 189.131 129.203 1.00 46.24  ? 2272 LEU   A CD2  1 
ATOM   5374 N  N    . ALA   A 1 941  ? 185.160 186.460 127.890 1.00 39.06  ? 2273 ALA   A N    1 
ATOM   5375 C  CA   . ALA   A 1 941  ? 184.091 186.990 127.065 1.00 43.71  ? 2273 ALA   A CA   1 
ATOM   5376 C  C    . ALA   A 1 941  ? 183.512 188.255 127.683 1.00 42.10  ? 2273 ALA   A C    1 
ATOM   5377 O  O    . ALA   A 1 941  ? 183.658 188.511 128.878 1.00 49.69  ? 2273 ALA   A O    1 
ATOM   5378 C  CB   . ALA   A 1 941  ? 182.994 185.944 126.886 1.00 48.80  ? 2273 ALA   A CB   1 
ATOM   5379 N  N    . ILE   A 1 942  ? 182.847 189.050 126.851 1.00 39.27  ? 2274 ILE   A N    1 
ATOM   5380 C  CA   . ILE   A 1 942  ? 182.123 190.230 127.307 1.00 35.65  ? 2274 ILE   A CA   1 
ATOM   5381 C  C    . ILE   A 1 942  ? 180.641 189.967 127.107 1.00 41.12  ? 2274 ILE   A C    1 
ATOM   5382 O  O    . ILE   A 1 942  ? 180.232 189.521 126.033 1.00 52.78  ? 2274 ILE   A O    1 
ATOM   5383 C  CB   . ILE   A 1 942  ? 182.542 191.489 126.539 1.00 43.25  ? 2274 ILE   A CB   1 
ATOM   5384 C  CG1  . ILE   A 1 942  ? 184.050 191.530 126.331 1.00 56.35  ? 2274 ILE   A CG1  1 
ATOM   5385 C  CG2  . ILE   A 1 942  ? 182.106 192.720 127.287 1.00 49.06  ? 2274 ILE   A CG2  1 
ATOM   5386 C  CD1  . ILE   A 1 942  ? 184.830 191.439 127.579 1.00 55.45  ? 2274 ILE   A CD1  1 
ATOM   5387 N  N    . PHE   A 1 943  ? 179.830 190.251 128.118 1.00 45.78  ? 2275 PHE   A N    1 
ATOM   5388 C  CA   . PHE   A 1 943  ? 178.380 190.191 127.993 1.00 57.54  ? 2275 PHE   A CA   1 
ATOM   5389 C  C    . PHE   A 1 943  ? 177.798 191.519 128.464 1.00 67.13  ? 2275 PHE   A C    1 
ATOM   5390 O  O    . PHE   A 1 943  ? 178.008 191.932 129.618 1.00 65.76  ? 2275 PHE   A O    1 
ATOM   5391 C  CB   . PHE   A 1 943  ? 177.793 189.052 128.821 1.00 55.76  ? 2275 PHE   A CB   1 
ATOM   5392 C  CG   . PHE   A 1 943  ? 177.729 187.732 128.124 1.00 48.79  ? 2275 PHE   A CG   1 
ATOM   5393 C  CD1  . PHE   A 1 943  ? 178.688 187.352 127.221 1.00 47.67  ? 2275 PHE   A CD1  1 
ATOM   5394 C  CD2  . PHE   A 1 943  ? 176.707 186.852 128.413 1.00 59.82  ? 2275 PHE   A CD2  1 
ATOM   5395 C  CE1  . PHE   A 1 943  ? 178.615 186.128 126.611 1.00 64.70  ? 2275 PHE   A CE1  1 
ATOM   5396 C  CE2  . PHE   A 1 943  ? 176.631 185.631 127.806 1.00 68.24  ? 2275 PHE   A CE2  1 
ATOM   5397 C  CZ   . PHE   A 1 943  ? 177.584 185.267 126.902 1.00 70.84  ? 2275 PHE   A CZ   1 
ATOM   5398 N  N    . GLU   A 1 944  ? 177.045 192.171 127.585 1.00 65.33  ? 2276 GLU   A N    1 
ATOM   5399 C  CA   . GLU   A 1 944  ? 176.432 193.443 127.926 1.00 71.59  ? 2276 GLU   A CA   1 
ATOM   5400 C  C    . GLU   A 1 944  ? 175.195 193.249 128.788 1.00 77.88  ? 2276 GLU   A C    1 
ATOM   5401 O  O    . GLU   A 1 944  ? 174.536 192.208 128.750 1.00 80.80  ? 2276 GLU   A O    1 
ATOM   5402 C  CB   . GLU   A 1 944  ? 176.070 194.223 126.662 1.00 82.55  ? 2276 GLU   A CB   1 
ATOM   5403 N  N    . ASP   A 1 945  ? 174.877 194.290 129.557 1.00 74.65  ? 2277 ASP   A N    1 
ATOM   5404 C  CA   . ASP   A 1 945  ? 173.746 194.233 130.471 1.00 82.23  ? 2277 ASP   A CA   1 
ATOM   5405 C  C    . ASP   A 1 945  ? 172.445 193.969 129.720 1.00 87.08  ? 2277 ASP   A C    1 
ATOM   5406 O  O    . ASP   A 1 945  ? 171.556 193.283 130.236 1.00 88.42  ? 2277 ASP   A O    1 
ATOM   5407 C  CB   . ASP   A 1 945  ? 173.677 195.541 131.264 1.00 81.82  ? 2277 ASP   A CB   1 
ATOM   5408 C  CG   . ASP   A 1 945  ? 172.674 195.499 132.403 1.00 94.51  ? 2277 ASP   A CG   1 
ATOM   5409 O  OD1  . ASP   A 1 945  ? 171.994 194.476 132.588 1.00 101.99 ? 2277 ASP   A OD1  1 
ATOM   5410 O  OD2  . ASP   A 1 945  ? 172.573 196.511 133.128 1.00 97.74  ? 2277 ASP   A OD2  1 
ATOM   5411 N  N    . LYS   A 1 946  ? 172.322 194.472 128.495 1.00 88.92  ? 2278 LYS   A N    1 
ATOM   5412 C  CA   . LYS   A 1 946  ? 171.110 194.246 127.721 1.00 91.83  ? 2278 LYS   A CA   1 
ATOM   5413 C  C    . LYS   A 1 946  ? 171.057 192.865 127.083 1.00 88.50  ? 2278 LYS   A C    1 
ATOM   5414 O  O    . LYS   A 1 946  ? 169.969 192.422 126.699 1.00 94.84  ? 2278 LYS   A O    1 
ATOM   5415 C  CB   . LYS   A 1 946  ? 170.979 195.311 126.631 1.00 91.40  ? 2278 LYS   A CB   1 
ATOM   5416 N  N    . THR   A 1 947  ? 172.194 192.179 126.960 1.00 81.86  ? 2279 THR   A N    1 
ATOM   5417 C  CA   . THR   A 1 947  ? 172.208 190.889 126.277 1.00 93.25  ? 2279 THR   A CA   1 
ATOM   5418 C  C    . THR   A 1 947  ? 171.507 189.811 127.094 1.00 102.74 ? 2279 THR   A C    1 
ATOM   5419 O  O    . THR   A 1 947  ? 170.806 188.959 126.536 1.00 98.06  ? 2279 THR   A O    1 
ATOM   5420 C  CB   . THR   A 1 947  ? 173.646 190.480 125.972 1.00 90.91  ? 2279 THR   A CB   1 
ATOM   5421 O  OG1  . THR   A 1 947  ? 174.373 190.355 127.199 1.00 84.18  ? 2279 THR   A OG1  1 
ATOM   5422 C  CG2  . THR   A 1 947  ? 174.319 191.511 125.093 1.00 86.41  ? 2279 THR   A CG2  1 
ATOM   5423 N  N    . VAL   A 1 948  ? 171.678 189.832 128.417 1.00 104.55 ? 2280 VAL   A N    1 
ATOM   5424 C  CA   . VAL   A 1 948  ? 171.119 188.799 129.276 1.00 99.17  ? 2280 VAL   A CA   1 
ATOM   5425 C  C    . VAL   A 1 948  ? 169.600 188.774 129.258 1.00 99.39  ? 2280 VAL   A C    1 
ATOM   5426 O  O    . VAL   A 1 948  ? 169.000 187.777 129.665 1.00 98.06  ? 2280 VAL   A O    1 
ATOM   5427 C  CB   . VAL   A 1 948  ? 171.633 188.985 130.716 1.00 91.54  ? 2280 VAL   A CB   1 
ATOM   5428 C  CG1  . VAL   A 1 948  ? 173.137 188.908 130.732 1.00 80.36  ? 2280 VAL   A CG1  1 
ATOM   5429 C  CG2  . VAL   A 1 948  ? 171.168 190.312 131.267 1.00 87.50  ? 2280 VAL   A CG2  1 
ATOM   5430 N  N    . LYS   A 1 949  ? 168.961 189.847 128.794 1.00 102.88 ? 2281 LYS   A N    1 
ATOM   5431 C  CA   . LYS   A 1 949  ? 167.512 189.834 128.649 1.00 102.93 ? 2281 LYS   A CA   1 
ATOM   5432 C  C    . LYS   A 1 949  ? 167.060 188.806 127.620 1.00 107.70 ? 2281 LYS   A C    1 
ATOM   5433 O  O    . LYS   A 1 949  ? 165.915 188.343 127.671 1.00 107.86 ? 2281 LYS   A O    1 
ATOM   5434 C  CB   . LYS   A 1 949  ? 167.012 191.225 128.264 1.00 91.18  ? 2281 LYS   A CB   1 
ATOM   5435 N  N    . LEU   A 1 950  ? 167.931 188.444 126.680 1.00 104.33 ? 2282 LEU   A N    1 
ATOM   5436 C  CA   . LEU   A 1 950  ? 167.568 187.516 125.618 1.00 102.95 ? 2282 LEU   A CA   1 
ATOM   5437 C  C    . LEU   A 1 950  ? 168.254 186.171 125.819 1.00 103.46 ? 2282 LEU   A C    1 
ATOM   5438 O  O    . LEU   A 1 950  ? 169.419 186.106 126.219 1.00 99.87  ? 2282 LEU   A O    1 
ATOM   5439 C  CB   . LEU   A 1 950  ? 167.914 188.110 124.248 1.00 108.16 ? 2282 LEU   A CB   1 
ATOM   5440 C  CG   . LEU   A 1 950  ? 169.354 188.466 123.861 1.00 102.03 ? 2282 LEU   A CG   1 
ATOM   5441 C  CD1  . LEU   A 1 950  ? 170.121 187.266 123.340 1.00 91.27  ? 2282 LEU   A CD1  1 
ATOM   5442 C  CD2  . LEU   A 1 950  ? 169.382 189.603 122.851 1.00 108.38 ? 2282 LEU   A CD2  1 
ATOM   5443 N  N    . LYS   A 1 951  ? 167.515 185.100 125.538 1.00 107.48 ? 2283 LYS   A N    1 
ATOM   5444 C  CA   . LYS   A 1 951  ? 167.985 183.741 125.770 1.00 99.16  ? 2283 LYS   A CA   1 
ATOM   5445 C  C    . LYS   A 1 951  ? 169.127 183.412 124.817 1.00 92.82  ? 2283 LYS   A C    1 
ATOM   5446 O  O    . LYS   A 1 951  ? 169.085 183.772 123.638 1.00 88.83  ? 2283 LYS   A O    1 
ATOM   5447 C  CB   . LYS   A 1 951  ? 166.819 182.759 125.600 1.00 95.95  ? 2283 LYS   A CB   1 
ATOM   5448 C  CG   . LYS   A 1 951  ? 167.072 181.293 125.981 1.00 102.91 ? 2283 LYS   A CG   1 
ATOM   5449 C  CD   . LYS   A 1 951  ? 167.886 180.521 124.947 1.00 99.14  ? 2283 LYS   A CD   1 
ATOM   5450 C  CE   . LYS   A 1 951  ? 168.288 179.148 125.453 1.00 95.94  ? 2283 LYS   A CE   1 
ATOM   5451 N  NZ   . LYS   A 1 951  ? 169.142 178.432 124.470 1.00 84.69  ? 2283 LYS   A NZ   1 
ATOM   5452 N  N    . GLY   A 1 952  ? 170.145 182.726 125.333 1.00 87.96  ? 2284 GLY   A N    1 
ATOM   5453 C  CA   . GLY   A 1 952  ? 171.249 182.258 124.517 1.00 81.36  ? 2284 GLY   A CA   1 
ATOM   5454 C  C    . GLY   A 1 952  ? 172.034 183.385 123.887 1.00 79.42  ? 2284 GLY   A C    1 
ATOM   5455 O  O    . GLY   A 1 952  ? 172.267 183.391 122.677 1.00 80.35  ? 2284 GLY   A O    1 
ATOM   5456 N  N    . ALA   A 1 953  ? 172.460 184.336 124.708 1.00 84.39  ? 2285 ALA   A N    1 
ATOM   5457 C  CA   . ALA   A 1 953  ? 173.073 185.550 124.204 1.00 83.47  ? 2285 ALA   A CA   1 
ATOM   5458 C  C    . ALA   A 1 953  ? 174.438 185.259 123.588 1.00 77.21  ? 2285 ALA   A C    1 
ATOM   5459 O  O    . ALA   A 1 953  ? 174.995 184.165 123.707 1.00 80.31  ? 2285 ALA   A O    1 
ATOM   5460 C  CB   . ALA   A 1 953  ? 173.204 186.588 125.316 1.00 81.51  ? 2285 ALA   A CB   1 
ATOM   5461 N  N    . ALA   A 1 954  ? 174.964 186.265 122.900 1.00 70.00  ? 2286 ALA   A N    1 
ATOM   5462 C  CA   . ALA   A 1 954  ? 176.255 186.194 122.256 1.00 68.62  ? 2286 ALA   A CA   1 
ATOM   5463 C  C    . ALA   A 1 954  ? 177.142 187.305 122.795 1.00 67.68  ? 2286 ALA   A C    1 
ATOM   5464 O  O    . ALA   A 1 954  ? 176.657 188.406 123.081 1.00 67.02  ? 2286 ALA   A O    1 
ATOM   5465 C  CB   . ALA   A 1 954  ? 176.121 186.320 120.733 1.00 64.18  ? 2286 ALA   A CB   1 
ATOM   5466 N  N    . PRO   A 1 955  ? 178.433 187.042 122.966 1.00 65.01  ? 2287 PRO   A N    1 
ATOM   5467 C  CA   . PRO   A 1 955  ? 179.335 188.069 123.483 1.00 59.27  ? 2287 PRO   A CA   1 
ATOM   5468 C  C    . PRO   A 1 955  ? 179.536 189.199 122.492 1.00 67.12  ? 2287 PRO   A C    1 
ATOM   5469 O  O    . PRO   A 1 955  ? 179.541 188.999 121.276 1.00 70.99  ? 2287 PRO   A O    1 
ATOM   5470 C  CB   . PRO   A 1 955  ? 180.644 187.308 123.702 1.00 52.79  ? 2287 PRO   A CB   1 
ATOM   5471 C  CG   . PRO   A 1 955  ? 180.258 185.883 123.721 1.00 54.70  ? 2287 PRO   A CG   1 
ATOM   5472 C  CD   . PRO   A 1 955  ? 179.130 185.766 122.776 1.00 63.45  ? 2287 PRO   A CD   1 
ATOM   5473 N  N    . LEU   A 1 956  ? 179.731 190.401 123.032 1.00 65.81  ? 2288 LEU   A N    1 
ATOM   5474 C  CA   . LEU   A 1 956  ? 180.200 191.496 122.195 1.00 66.63  ? 2288 LEU   A CA   1 
ATOM   5475 C  C    . LEU   A 1 956  ? 181.550 191.149 121.592 1.00 68.23  ? 2288 LEU   A C    1 
ATOM   5476 O  O    . LEU   A 1 956  ? 181.789 191.395 120.405 1.00 76.40  ? 2288 LEU   A O    1 
ATOM   5477 C  CB   . LEU   A 1 956  ? 180.288 192.790 123.002 1.00 70.09  ? 2288 LEU   A CB   1 
ATOM   5478 C  CG   . LEU   A 1 956  ? 179.021 193.625 123.196 1.00 74.19  ? 2288 LEU   A CG   1 
ATOM   5479 C  CD1  . LEU   A 1 956  ? 178.526 194.141 121.862 1.00 70.54  ? 2288 LEU   A CD1  1 
ATOM   5480 C  CD2  . LEU   A 1 956  ? 177.933 192.840 123.907 1.00 74.10  ? 2288 LEU   A CD2  1 
ATOM   5481 N  N    . LYS   A 1 957  ? 182.438 190.566 122.391 1.00 58.09  ? 2289 LYS   A N    1 
ATOM   5482 C  CA   . LYS   A 1 957  ? 183.659 189.974 121.872 1.00 51.08  ? 2289 LYS   A CA   1 
ATOM   5483 C  C    . LYS   A 1 957  ? 184.194 188.982 122.887 1.00 47.58  ? 2289 LYS   A C    1 
ATOM   5484 O  O    . LYS   A 1 957  ? 184.009 189.143 124.099 1.00 58.48  ? 2289 LYS   A O    1 
ATOM   5485 C  CB   . LYS   A 1 957  ? 184.719 191.034 121.551 1.00 62.53  ? 2289 LYS   A CB   1 
ATOM   5486 C  CG   . LYS   A 1 957  ? 185.565 191.463 122.732 1.00 68.57  ? 2289 LYS   A CG   1 
ATOM   5487 C  CD   . LYS   A 1 957  ? 186.375 192.712 122.417 1.00 70.26  ? 2289 LYS   A CD   1 
ATOM   5488 C  CE   . LYS   A 1 957  ? 187.115 192.589 121.098 1.00 69.37  ? 2289 LYS   A CE   1 
ATOM   5489 N  NZ   . LYS   A 1 957  ? 188.326 191.739 121.220 1.00 57.57  ? 2289 LYS   A NZ   1 
ATOM   5490 N  N    . ILE   A 1 958  ? 184.846 187.950 122.372 1.00 51.68  ? 2290 ILE   A N    1 
ATOM   5491 C  CA   . ILE   A 1 958  ? 185.575 186.980 123.174 1.00 64.06  ? 2290 ILE   A CA   1 
ATOM   5492 C  C    . ILE   A 1 958  ? 187.043 187.102 122.817 1.00 67.24  ? 2290 ILE   A C    1 
ATOM   5493 O  O    . ILE   A 1 958  ? 187.437 186.827 121.677 1.00 75.31  ? 2290 ILE   A O    1 
ATOM   5494 C  CB   . ILE   A 1 958  ? 185.097 185.545 122.928 1.00 59.82  ? 2290 ILE   A CB   1 
ATOM   5495 C  CG1  . ILE   A 1 958  ? 183.653 185.349 123.350 1.00 53.24  ? 2290 ILE   A CG1  1 
ATOM   5496 C  CG2  . ILE   A 1 958  ? 185.966 184.599 123.649 1.00 49.23  ? 2290 ILE   A CG2  1 
ATOM   5497 C  CD1  . ILE   A 1 958  ? 183.097 184.029 122.888 1.00 60.98  ? 2290 ILE   A CD1  1 
ATOM   5498 N  N    . LEU   A 1 959  ? 187.858 187.486 123.786 1.00 60.11  ? 2291 LEU   A N    1 
ATOM   5499 C  CA   . LEU   A 1 959  ? 189.291 187.589 123.585 1.00 60.50  ? 2291 LEU   A CA   1 
ATOM   5500 C  C    . LEU   A 1 959  ? 189.977 186.459 124.332 1.00 64.66  ? 2291 LEU   A C    1 
ATOM   5501 O  O    . LEU   A 1 959  ? 189.674 186.200 125.500 1.00 73.20  ? 2291 LEU   A O    1 
ATOM   5502 C  CB   . LEU   A 1 959  ? 189.810 188.961 124.023 1.00 56.86  ? 2291 LEU   A CB   1 
ATOM   5503 C  CG   . LEU   A 1 959  ? 189.902 189.361 125.490 1.00 57.38  ? 2291 LEU   A CG   1 
ATOM   5504 C  CD1  . LEU   A 1 959  ? 190.784 190.577 125.641 1.00 52.81  ? 2291 LEU   A CD1  1 
ATOM   5505 C  CD2  . LEU   A 1 959  ? 188.523 189.685 125.994 1.00 58.26  ? 2291 LEU   A CD2  1 
ATOM   5506 N  N    . ASN   A 1 960  ? 190.869 185.762 123.640 1.00 65.49  ? 2292 ASN   A N    1 
ATOM   5507 C  CA   . ASN   A 1 960  ? 191.611 184.683 124.266 1.00 74.33  ? 2292 ASN   A CA   1 
ATOM   5508 C  C    . ASN   A 1 960  ? 192.904 185.233 124.843 1.00 80.93  ? 2292 ASN   A C    1 
ATOM   5509 O  O    . ASN   A 1 960  ? 193.637 185.967 124.177 1.00 82.72  ? 2292 ASN   A O    1 
ATOM   5510 C  CB   . ASN   A 1 960  ? 191.900 183.579 123.252 1.00 72.45  ? 2292 ASN   A CB   1 
ATOM   5511 C  CG   . ASN   A 1 960  ? 192.484 182.337 123.891 1.00 83.96  ? 2292 ASN   A CG   1 
ATOM   5512 O  OD1  . ASN   A 1 960  ? 192.707 182.290 125.099 1.00 91.51  ? 2292 ASN   A OD1  1 
ATOM   5513 N  ND2  . ASN   A 1 960  ? 192.728 181.317 123.081 1.00 80.34  ? 2292 ASN   A ND2  1 
ATOM   5514 N  N    . ILE   A 1 961  ? 193.183 184.883 126.096 1.00 78.51  ? 2293 ILE   A N    1 
ATOM   5515 C  CA   . ILE   A 1 961  ? 194.284 185.489 126.818 1.00 79.57  ? 2293 ILE   A CA   1 
ATOM   5516 C  C    . ILE   A 1 961  ? 195.443 184.517 127.022 1.00 81.03  ? 2293 ILE   A C    1 
ATOM   5517 O  O    . ILE   A 1 961  ? 196.602 184.946 127.027 1.00 83.02  ? 2293 ILE   A O    1 
ATOM   5518 C  CB   . ILE   A 1 961  ? 193.789 186.038 128.169 1.00 76.54  ? 2293 ILE   A CB   1 
ATOM   5519 C  CG1  . ILE   A 1 961  ? 192.660 187.043 127.952 1.00 62.37  ? 2293 ILE   A CG1  1 
ATOM   5520 C  CG2  . ILE   A 1 961  ? 194.913 186.754 128.887 1.00 70.15  ? 2293 ILE   A CG2  1 
ATOM   5521 C  CD1  . ILE   A 1 961  ? 193.045 188.231 127.149 1.00 60.76  ? 2293 ILE   A CD1  1 
ATOM   5522 N  N    . GLY   A 1 962  ? 195.169 183.226 127.156 1.00 79.03  ? 2294 GLY   A N    1 
ATOM   5523 C  CA   . GLY   A 1 962  ? 196.207 182.242 127.346 1.00 87.05  ? 2294 GLY   A CA   1 
ATOM   5524 C  C    . GLY   A 1 962  ? 195.734 180.881 126.888 1.00 99.48  ? 2294 GLY   A C    1 
ATOM   5525 O  O    . GLY   A 1 962  ? 194.599 180.719 126.434 1.00 103.31 ? 2294 GLY   A O    1 
ATOM   5526 N  N    . ASN   A 1 963  ? 196.618 179.896 127.017 1.00 97.46  ? 2295 ASN   A N    1 
ATOM   5527 C  CA   . ASN   A 1 963  ? 196.302 178.554 126.554 1.00 98.15  ? 2295 ASN   A CA   1 
ATOM   5528 C  C    . ASN   A 1 963  ? 195.194 177.939 127.407 1.00 97.74  ? 2295 ASN   A C    1 
ATOM   5529 O  O    . ASN   A 1 963  ? 194.750 178.504 128.410 1.00 97.24  ? 2295 ASN   A O    1 
ATOM   5530 C  CB   . ASN   A 1 963  ? 197.553 177.676 126.547 1.00 102.39 ? 2295 ASN   A CB   1 
ATOM   5531 C  CG   . ASN   A 1 963  ? 198.139 177.464 127.932 1.00 104.13 ? 2295 ASN   A CG   1 
ATOM   5532 O  OD1  . ASN   A 1 963  ? 197.564 177.870 128.939 1.00 107.82 ? 2295 ASN   A OD1  1 
ATOM   5533 N  ND2  . ASN   A 1 963  ? 199.287 176.798 127.987 1.00 95.98  ? 2295 ASN   A ND2  1 
ATOM   5534 N  N    . VAL   A 1 964  ? 194.743 176.754 126.998 1.00 99.86  ? 2296 VAL   A N    1 
ATOM   5535 C  CA   . VAL   A 1 964  ? 193.646 176.092 127.693 1.00 100.68 ? 2296 VAL   A CA   1 
ATOM   5536 C  C    . VAL   A 1 964  ? 194.071 175.670 129.095 1.00 94.03  ? 2296 VAL   A C    1 
ATOM   5537 O  O    . VAL   A 1 964  ? 193.272 175.709 130.038 1.00 93.22  ? 2296 VAL   A O    1 
ATOM   5538 C  CB   . VAL   A 1 964  ? 193.148 174.896 126.862 1.00 101.33 ? 2296 VAL   A CB   1 
ATOM   5539 C  CG1  . VAL   A 1 964  ? 192.072 174.127 127.613 1.00 105.38 ? 2296 VAL   A CG1  1 
ATOM   5540 C  CG2  . VAL   A 1 964  ? 192.636 175.371 125.512 1.00 92.02  ? 2296 VAL   A CG2  1 
ATOM   5541 N  N    . SER   A 1 965  ? 195.331 175.266 129.258 1.00 92.90  ? 2297 SER   A N    1 
ATOM   5542 C  CA   . SER   A 1 965  ? 195.802 174.763 130.543 1.00 97.21  ? 2297 SER   A CA   1 
ATOM   5543 C  C    . SER   A 1 965  ? 195.880 175.837 131.620 1.00 99.44  ? 2297 SER   A C    1 
ATOM   5544 O  O    . SER   A 1 965  ? 196.050 175.491 132.794 1.00 97.46  ? 2297 SER   A O    1 
ATOM   5545 C  CB   . SER   A 1 965  ? 197.173 174.109 130.378 1.00 99.97  ? 2297 SER   A CB   1 
ATOM   5546 O  OG   . SER   A 1 965  ? 198.009 174.886 129.541 1.00 100.66 ? 2297 SER   A OG   1 
ATOM   5547 N  N    . THR   A 1 966  ? 195.773 177.118 131.262 1.00 97.23  ? 2298 THR   A N    1 
ATOM   5548 C  CA   . THR   A 1 966  ? 195.832 178.204 132.237 1.00 88.73  ? 2298 THR   A CA   1 
ATOM   5549 C  C    . THR   A 1 966  ? 194.465 178.858 132.366 1.00 82.25  ? 2298 THR   A C    1 
ATOM   5550 O  O    . THR   A 1 966  ? 194.041 179.595 131.464 1.00 69.12  ? 2298 THR   A O    1 
ATOM   5551 C  CB   . THR   A 1 966  ? 196.884 179.241 131.835 1.00 86.02  ? 2298 THR   A CB   1 
ATOM   5552 O  OG1  . THR   A 1 966  ? 196.769 179.520 130.435 1.00 92.14  ? 2298 THR   A OG1  1 
ATOM   5553 C  CG2  . THR   A 1 966  ? 198.281 178.722 132.130 1.00 82.18  ? 2298 THR   A CG2  1 
ATOM   5554 N  N    . PRO   A 1 967  ? 193.734 178.616 133.450 1.00 86.13  ? 2299 PRO   A N    1 
ATOM   5555 C  CA   . PRO   A 1 967  ? 192.429 179.257 133.613 1.00 78.97  ? 2299 PRO   A CA   1 
ATOM   5556 C  C    . PRO   A 1 967  ? 192.567 180.732 133.947 1.00 80.92  ? 2299 PRO   A C    1 
ATOM   5557 O  O    . PRO   A 1 967  ? 193.515 181.152 134.611 1.00 82.11  ? 2299 PRO   A O    1 
ATOM   5558 C  CB   . PRO   A 1 967  ? 191.802 178.484 134.776 1.00 75.41  ? 2299 PRO   A CB   1 
ATOM   5559 C  CG   . PRO   A 1 967  ? 192.961 177.999 135.554 1.00 76.24  ? 2299 PRO   A CG   1 
ATOM   5560 C  CD   . PRO   A 1 967  ? 194.040 177.699 134.558 1.00 87.74  ? 2299 PRO   A CD   1 
ATOM   5561 N  N    . LEU   A 1 968  ? 191.592 181.513 133.492 1.00 80.59  ? 2300 LEU   A N    1 
ATOM   5562 C  CA   . LEU   A 1 968  ? 191.490 182.925 133.840 1.00 65.75  ? 2300 LEU   A CA   1 
ATOM   5563 C  C    . LEU   A 1 968  ? 190.646 183.028 135.101 1.00 57.44  ? 2300 LEU   A C    1 
ATOM   5564 O  O    . LEU   A 1 968  ? 189.459 182.691 135.090 1.00 55.48  ? 2300 LEU   A O    1 
ATOM   5565 C  CB   . LEU   A 1 968  ? 190.886 183.717 132.683 1.00 60.61  ? 2300 LEU   A CB   1 
ATOM   5566 C  CG   . LEU   A 1 968  ? 190.841 185.239 132.771 1.00 55.66  ? 2300 LEU   A CG   1 
ATOM   5567 C  CD1  . LEU   A 1 968  ? 190.865 185.828 131.387 1.00 56.83  ? 2300 LEU   A CD1  1 
ATOM   5568 C  CD2  . LEU   A 1 968  ? 189.574 185.667 133.465 1.00 48.95  ? 2300 LEU   A CD2  1 
ATOM   5569 N  N    . MET   A 1 969  ? 191.255 183.497 136.188 1.00 55.15  ? 2301 MET   A N    1 
ATOM   5570 C  CA   . MET   A 1 969  ? 190.660 183.336 137.506 1.00 60.97  ? 2301 MET   A CA   1 
ATOM   5571 C  C    . MET   A 1 969  ? 190.096 184.618 138.100 1.00 57.73  ? 2301 MET   A C    1 
ATOM   5572 O  O    . MET   A 1 969  ? 189.007 184.586 138.677 1.00 49.19  ? 2301 MET   A O    1 
ATOM   5573 C  CB   . MET   A 1 969  ? 191.686 182.745 138.472 1.00 63.30  ? 2301 MET   A CB   1 
ATOM   5574 C  CG   . MET   A 1 969  ? 192.229 181.405 138.035 1.00 72.35  ? 2301 MET   A CG   1 
ATOM   5575 S  SD   . MET   A 1 969  ? 192.531 180.319 139.435 1.00 83.54  ? 2301 MET   A SD   1 
ATOM   5576 C  CE   . MET   A 1 969  ? 190.862 179.783 139.799 1.00 71.30  ? 2301 MET   A CE   1 
ATOM   5577 N  N    . CYS   A 1 970  ? 190.795 185.744 137.995 1.00 51.20  ? 2302 CYS   A N    1 
ATOM   5578 C  CA   . CYS   A 1 970  ? 190.372 186.937 138.711 1.00 33.39  ? 2302 CYS   A CA   1 
ATOM   5579 C  C    . CYS   A 1 970  ? 190.300 188.136 137.781 1.00 43.00  ? 2302 CYS   A C    1 
ATOM   5580 O  O    . CYS   A 1 970  ? 191.222 188.375 136.997 1.00 53.78  ? 2302 CYS   A O    1 
ATOM   5581 C  CB   . CYS   A 1 970  ? 191.322 187.249 139.861 1.00 34.43  ? 2302 CYS   A CB   1 
ATOM   5582 S  SG   . CYS   A 1 970  ? 190.831 188.672 140.840 1.00 80.27  ? 2302 CYS   A SG   1 
ATOM   5583 N  N    . LEU   A 1 971  ? 189.201 188.888 137.890 1.00 40.20  ? 2303 LEU   A N    1 
ATOM   5584 C  CA   . LEU   A 1 971  ? 189.030 190.193 137.260 1.00 42.83  ? 2303 LEU   A CA   1 
ATOM   5585 C  C    . LEU   A 1 971  ? 188.639 191.204 138.324 1.00 50.15  ? 2303 LEU   A C    1 
ATOM   5586 O  O    . LEU   A 1 971  ? 187.809 190.908 139.186 1.00 46.58  ? 2303 LEU   A O    1 
ATOM   5587 C  CB   . LEU   A 1 971  ? 187.966 190.166 136.164 1.00 36.70  ? 2303 LEU   A CB   1 
ATOM   5588 C  CG   . LEU   A 1 971  ? 188.080 189.052 135.142 1.00 39.45  ? 2303 LEU   A CG   1 
ATOM   5589 C  CD1  . LEU   A 1 971  ? 186.971 189.160 134.139 1.00 37.04  ? 2303 LEU   A CD1  1 
ATOM   5590 C  CD2  . LEU   A 1 971  ? 189.409 189.185 134.458 1.00 46.05  ? 2303 LEU   A CD2  1 
ATOM   5591 N  N    . SER   A 1 972  ? 189.221 192.399 138.249 1.00 54.77  ? 2304 SER   A N    1 
ATOM   5592 C  CA   . SER   A 1 972  ? 189.104 193.403 139.295 1.00 54.13  ? 2304 SER   A CA   1 
ATOM   5593 C  C    . SER   A 1 972  ? 188.872 194.787 138.706 1.00 63.95  ? 2304 SER   A C    1 
ATOM   5594 O  O    . SER   A 1 972  ? 189.437 195.146 137.668 1.00 72.90  ? 2304 SER   A O    1 
ATOM   5595 C  CB   . SER   A 1 972  ? 190.356 193.435 140.173 1.00 56.08  ? 2304 SER   A CB   1 
ATOM   5596 O  OG   . SER   A 1 972  ? 190.464 194.675 140.844 1.00 66.49  ? 2304 SER   A OG   1 
ATOM   5597 N  N    . GLU   A 1 973  ? 188.045 195.563 139.401 1.00 59.36  ? 2305 GLU   A N    1 
ATOM   5598 C  CA   . GLU   A 1 973  ? 187.782 196.965 139.111 1.00 60.31  ? 2305 GLU   A CA   1 
ATOM   5599 C  C    . GLU   A 1 973  ? 188.701 197.852 139.934 1.00 68.72  ? 2305 GLU   A C    1 
ATOM   5600 O  O    . GLU   A 1 973  ? 188.929 197.588 141.116 1.00 77.58  ? 2305 GLU   A O    1 
ATOM   5601 C  CB   . GLU   A 1 973  ? 186.330 197.318 139.429 1.00 67.08  ? 2305 GLU   A CB   1 
ATOM   5602 C  CG   . GLU   A 1 973  ? 186.028 198.806 139.397 1.00 80.31  ? 2305 GLU   A CG   1 
ATOM   5603 C  CD   . GLU   A 1 973  ? 185.462 199.276 138.081 1.00 93.17  ? 2305 GLU   A CD   1 
ATOM   5604 O  OE1  . GLU   A 1 973  ? 185.174 200.484 137.957 1.00 94.39  ? 2305 GLU   A OE1  1 
ATOM   5605 O  OE2  . GLU   A 1 973  ? 185.312 198.444 137.168 1.00 90.80  ? 2305 GLU   A OE2  1 
ATOM   5606 N  N    . SER   A 1 974  ? 189.219 198.908 139.317 1.00 76.45  ? 2306 SER   A N    1 
ATOM   5607 C  CA   . SER   A 1 974  ? 190.078 199.840 140.042 1.00 76.06  ? 2306 SER   A CA   1 
ATOM   5608 C  C    . SER   A 1 974  ? 189.294 201.042 140.553 1.00 70.88  ? 2306 SER   A C    1 
ATOM   5609 O  O    . SER   A 1 974  ? 189.095 201.198 141.758 1.00 64.23  ? 2306 SER   A O    1 
ATOM   5610 C  CB   . SER   A 1 974  ? 191.231 200.303 139.157 1.00 85.88  ? 2306 SER   A CB   1 
ATOM   5611 O  OG   . SER   A 1 974  ? 192.072 199.216 138.819 1.00 93.24  ? 2306 SER   A OG   1 
ATOM   5612 N  N    . ARG   A 1 980  ? 191.414 206.200 135.082 1.00 100.73 ? 2312 ARG   A N    1 
ATOM   5613 C  CA   . ARG   A 1 980  ? 191.388 205.280 136.212 1.00 101.51 ? 2312 ARG   A CA   1 
ATOM   5614 C  C    . ARG   A 1 980  ? 190.272 204.252 136.072 1.00 101.08 ? 2312 ARG   A C    1 
ATOM   5615 O  O    . ARG   A 1 980  ? 189.896 203.602 137.047 1.00 93.21  ? 2312 ARG   A O    1 
ATOM   5616 C  CB   . ARG   A 1 980  ? 191.227 206.049 137.524 1.00 108.29 ? 2312 ARG   A CB   1 
ATOM   5617 C  CG   . ARG   A 1 980  ? 190.036 206.992 137.537 1.00 105.88 ? 2312 ARG   A CG   1 
ATOM   5618 C  CD   . ARG   A 1 980  ? 189.920 207.733 138.857 1.00 107.88 ? 2312 ARG   A CD   1 
ATOM   5619 N  NE   . ARG   A 1 980  ? 189.988 206.826 139.995 1.00 119.94 ? 2312 ARG   A NE   1 
ATOM   5620 C  CZ   . ARG   A 1 980  ? 188.931 206.379 140.660 1.00 121.03 ? 2312 ARG   A CZ   1 
ATOM   5621 N  NH1  . ARG   A 1 980  ? 187.703 206.741 140.328 1.00 119.53 ? 2312 ARG   A NH1  1 
ATOM   5622 N  NH2  . ARG   A 1 980  ? 189.111 205.546 141.680 1.00 121.85 ? 2312 ARG   A NH2  1 
ATOM   5623 N  N    . ASN   A 1 981  ? 189.738 204.112 134.861 1.00 103.74 ? 2313 ASN   A N    1 
ATOM   5624 C  CA   . ASN   A 1 981  ? 188.707 203.121 134.559 1.00 107.48 ? 2313 ASN   A CA   1 
ATOM   5625 C  C    . ASN   A 1 981  ? 189.354 202.058 133.679 1.00 100.84 ? 2313 ASN   A C    1 
ATOM   5626 O  O    . ASN   A 1 981  ? 189.258 202.098 132.451 1.00 92.38  ? 2313 ASN   A O    1 
ATOM   5627 C  CB   . ASN   A 1 981  ? 187.491 203.745 133.881 1.00 104.90 ? 2313 ASN   A CB   1 
ATOM   5628 C  CG   . ASN   A 1 981  ? 186.271 202.841 133.932 1.00 105.54 ? 2313 ASN   A CG   1 
ATOM   5629 O  OD1  . ASN   A 1 981  ? 185.958 202.258 134.969 1.00 96.56  ? 2313 ASN   A OD1  1 
ATOM   5630 N  ND2  . ASN   A 1 981  ? 185.579 202.719 132.805 1.00 99.54  ? 2313 ASN   A ND2  1 
ATOM   5631 N  N    . VAL   A 1 982  ? 190.014 201.105 134.322 1.00 94.73  ? 2314 VAL   A N    1 
ATOM   5632 C  CA   . VAL   A 1 982  ? 190.666 199.995 133.645 1.00 87.02  ? 2314 VAL   A CA   1 
ATOM   5633 C  C    . VAL   A 1 982  ? 190.367 198.734 134.441 1.00 88.04  ? 2314 VAL   A C    1 
ATOM   5634 O  O    . VAL   A 1 982  ? 190.281 198.774 135.672 1.00 88.71  ? 2314 VAL   A O    1 
ATOM   5635 C  CB   . VAL   A 1 982  ? 192.184 200.238 133.493 1.00 78.43  ? 2314 VAL   A CB   1 
ATOM   5636 C  CG1  . VAL   A 1 982  ? 192.899 200.078 134.817 1.00 71.67  ? 2314 VAL   A CG1  1 
ATOM   5637 C  CG2  . VAL   A 1 982  ? 192.769 199.298 132.463 1.00 68.63  ? 2314 VAL   A CG2  1 
ATOM   5638 N  N    . MET   A 1 983  ? 190.158 197.625 133.739 1.00 81.90  ? 2315 MET   A N    1 
ATOM   5639 C  CA   . MET   A 1 983  ? 189.882 196.347 134.379 1.00 61.13  ? 2315 MET   A CA   1 
ATOM   5640 C  C    . MET   A 1 983  ? 191.160 195.529 134.416 1.00 65.14  ? 2315 MET   A C    1 
ATOM   5641 O  O    . MET   A 1 983  ? 191.796 195.334 133.378 1.00 73.04  ? 2315 MET   A O    1 
ATOM   5642 C  CB   . MET   A 1 983  ? 188.810 195.571 133.627 1.00 54.30  ? 2315 MET   A CB   1 
ATOM   5643 C  CG   . MET   A 1 983  ? 188.106 194.567 134.478 1.00 60.53  ? 2315 MET   A CG   1 
ATOM   5644 S  SD   . MET   A 1 983  ? 187.037 195.346 135.693 1.00 90.90  ? 2315 MET   A SD   1 
ATOM   5645 C  CE   . MET   A 1 983  ? 186.551 196.824 134.813 1.00 66.81  ? 2315 MET   A CE   1 
ATOM   5646 N  N    . TRP   A 1 984  ? 191.528 195.039 135.593 1.00 60.25  ? 2316 TRP   A N    1 
ATOM   5647 C  CA   . TRP   A 1 984  ? 192.722 194.219 135.721 1.00 57.69  ? 2316 TRP   A CA   1 
ATOM   5648 C  C    . TRP   A 1 984  ? 192.343 192.761 135.904 1.00 52.48  ? 2316 TRP   A C    1 
ATOM   5649 O  O    . TRP   A 1 984  ? 191.197 192.428 136.190 1.00 52.76  ? 2316 TRP   A O    1 
ATOM   5650 C  CB   . TRP   A 1 984  ? 193.585 194.685 136.888 1.00 55.47  ? 2316 TRP   A CB   1 
ATOM   5651 C  CG   . TRP   A 1 984  ? 194.368 195.891 136.558 1.00 63.10  ? 2316 TRP   A CG   1 
ATOM   5652 C  CD1  . TRP   A 1 984  ? 193.924 197.171 136.552 1.00 67.51  ? 2316 TRP   A CD1  1 
ATOM   5653 C  CD2  . TRP   A 1 984  ? 195.738 195.937 136.153 1.00 59.96  ? 2316 TRP   A CD2  1 
ATOM   5654 N  NE1  . TRP   A 1 984  ? 194.935 198.019 136.183 1.00 67.32  ? 2316 TRP   A NE1  1 
ATOM   5655 C  CE2  . TRP   A 1 984  ? 196.059 197.282 135.929 1.00 67.02  ? 2316 TRP   A CE2  1 
ATOM   5656 C  CE3  . TRP   A 1 984  ? 196.725 194.972 135.962 1.00 55.68  ? 2316 TRP   A CE3  1 
ATOM   5657 C  CZ2  . TRP   A 1 984  ? 197.321 197.686 135.526 1.00 72.35  ? 2316 TRP   A CZ2  1 
ATOM   5658 C  CZ3  . TRP   A 1 984  ? 197.974 195.377 135.562 1.00 65.74  ? 2316 TRP   A CZ3  1 
ATOM   5659 C  CH2  . TRP   A 1 984  ? 198.263 196.719 135.348 1.00 66.54  ? 2316 TRP   A CH2  1 
ATOM   5660 N  N    . GLY   A 1 985  ? 193.321 191.888 135.731 1.00 54.57  ? 2317 GLY   A N    1 
ATOM   5661 C  CA   . GLY   A 1 985  ? 193.016 190.474 135.841 1.00 56.69  ? 2317 GLY   A CA   1 
ATOM   5662 C  C    . GLY   A 1 985  ? 194.271 189.639 135.913 1.00 59.98  ? 2317 GLY   A C    1 
ATOM   5663 O  O    . GLY   A 1 985  ? 195.373 190.097 135.609 1.00 71.13  ? 2317 GLY   A O    1 
ATOM   5664 N  N    . GLY   A 1 986  ? 194.078 188.393 136.320 1.00 47.40  ? 2318 GLY   A N    1 
ATOM   5665 C  CA   . GLY   A 1 986  ? 195.169 187.443 136.373 1.00 43.50  ? 2318 GLY   A CA   1 
ATOM   5666 C  C    . GLY   A 1 986  ? 194.749 186.093 135.840 1.00 58.80  ? 2318 GLY   A C    1 
ATOM   5667 O  O    . GLY   A 1 986  ? 193.733 185.552 136.281 1.00 69.29  ? 2318 GLY   A O    1 
ATOM   5668 N  N    . CYS   A 1 987  ? 195.490 185.544 134.881 1.00 59.13  ? 2319 CYS   A N    1 
ATOM   5669 C  CA   . CYS   A 1 987  ? 195.221 184.210 134.362 1.00 54.41  ? 2319 CYS   A CA   1 
ATOM   5670 C  C    . CYS   A 1 987  ? 196.509 183.410 134.378 1.00 58.93  ? 2319 CYS   A C    1 
ATOM   5671 O  O    . CYS   A 1 987  ? 197.550 183.900 133.933 1.00 56.77  ? 2319 CYS   A O    1 
ATOM   5672 C  CB   . CYS   A 1 987  ? 194.659 184.246 132.939 1.00 54.65  ? 2319 CYS   A CB   1 
ATOM   5673 S  SG   . CYS   A 1 987  ? 195.789 184.888 131.694 1.00 76.48  ? 2319 CYS   A SG   1 
ATOM   5674 N  N    . GLY   A 1 988  ? 196.435 182.182 134.873 1.00 68.66  ? 2320 GLY   A N    1 
ATOM   5675 C  CA   . GLY   A 1 988  ? 197.621 181.361 134.940 1.00 73.26  ? 2320 GLY   A CA   1 
ATOM   5676 C  C    . GLY   A 1 988  ? 198.675 182.031 135.787 1.00 72.01  ? 2320 GLY   A C    1 
ATOM   5677 O  O    . GLY   A 1 988  ? 198.550 182.083 137.011 1.00 73.76  ? 2320 GLY   A O    1 
ATOM   5678 N  N    . THR   A 1 989  ? 199.712 182.566 135.151 1.00 72.04  ? 2321 THR   A N    1 
ATOM   5679 C  CA   . THR   A 1 989  ? 200.772 183.252 135.874 1.00 78.15  ? 2321 THR   A CA   1 
ATOM   5680 C  C    . THR   A 1 989  ? 201.023 184.639 135.281 1.00 76.25  ? 2321 THR   A C    1 
ATOM   5681 O  O    . THR   A 1 989  ? 202.085 185.232 135.488 1.00 82.01  ? 2321 THR   A O    1 
ATOM   5682 C  CB   . THR   A 1 989  ? 202.032 182.385 135.859 1.00 89.82  ? 2321 THR   A CB   1 
ATOM   5683 O  OG1  . THR   A 1 989  ? 201.681 181.063 136.280 1.00 93.52  ? 2321 THR   A OG1  1 
ATOM   5684 C  CG2  . THR   A 1 989  ? 203.038 182.875 136.874 1.00 89.80  ? 2321 THR   A CG2  1 
ATOM   5685 N  N    . LYS   A 1 990  ? 200.051 185.178 134.551 1.00 66.99  ? 2322 LYS   A N    1 
ATOM   5686 C  CA   . LYS   A 1 990  ? 200.201 186.439 133.841 1.00 60.69  ? 2322 LYS   A CA   1 
ATOM   5687 C  C    . LYS   A 1 990  ? 199.093 187.397 134.243 1.00 55.17  ? 2322 LYS   A C    1 
ATOM   5688 O  O    . LYS   A 1 990  ? 197.920 187.017 134.278 1.00 54.51  ? 2322 LYS   A O    1 
ATOM   5689 C  CB   . LYS   A 1 990  ? 200.171 186.221 132.330 1.00 67.96  ? 2322 LYS   A CB   1 
ATOM   5690 C  CG   . LYS   A 1 990  ? 201.194 185.231 131.815 1.00 75.88  ? 2322 LYS   A CG   1 
ATOM   5691 C  CD   . LYS   A 1 990  ? 202.428 185.928 131.285 1.00 77.63  ? 2322 LYS   A CD   1 
ATOM   5692 C  CE   . LYS   A 1 990  ? 203.419 184.915 130.750 1.00 85.61  ? 2322 LYS   A CE   1 
ATOM   5693 N  NZ   . LYS   A 1 990  ? 203.617 183.785 131.700 1.00 86.01  ? 2322 LYS   A NZ   1 
ATOM   5694 N  N    . ILE   A 1 991  ? 199.465 188.633 134.515 1.00 59.00  ? 2323 ILE   A N    1 
ATOM   5695 C  CA   . ILE   A 1 991  ? 198.523 189.703 134.808 1.00 59.53  ? 2323 ILE   A CA   1 
ATOM   5696 C  C    . ILE   A 1 991  ? 198.200 190.416 133.507 1.00 60.09  ? 2323 ILE   A C    1 
ATOM   5697 O  O    . ILE   A 1 991  ? 198.963 190.365 132.542 1.00 57.28  ? 2323 ILE   A O    1 
ATOM   5698 C  CB   . ILE   A 1 991  ? 199.097 190.684 135.851 1.00 54.38  ? 2323 ILE   A CB   1 
ATOM   5699 C  CG1  . ILE   A 1 991  ? 199.812 189.925 136.961 1.00 60.53  ? 2323 ILE   A CG1  1 
ATOM   5700 C  CG2  . ILE   A 1 991  ? 198.003 191.526 136.460 1.00 47.58  ? 2323 ILE   A CG2  1 
ATOM   5701 C  CD1  . ILE   A 1 991  ? 200.307 190.814 138.072 1.00 65.47  ? 2323 ILE   A CD1  1 
ATOM   5702 N  N    . PHE   A 1 992  ? 197.048 191.073 133.467 1.00 58.16  ? 2324 PHE   A N    1 
ATOM   5703 C  CA   . PHE   A 1 992  ? 196.666 191.830 132.289 1.00 54.97  ? 2324 PHE   A CA   1 
ATOM   5704 C  C    . PHE   A 1 992  ? 195.727 192.948 132.701 1.00 55.95  ? 2324 PHE   A C    1 
ATOM   5705 O  O    . PHE   A 1 992  ? 195.211 192.973 133.819 1.00 61.44  ? 2324 PHE   A O    1 
ATOM   5706 C  CB   . PHE   A 1 992  ? 196.026 190.938 131.217 1.00 57.33  ? 2324 PHE   A CB   1 
ATOM   5707 C  CG   . PHE   A 1 992  ? 194.733 190.297 131.630 1.00 56.37  ? 2324 PHE   A CG   1 
ATOM   5708 C  CD1  . PHE   A 1 992  ? 194.676 188.944 131.866 1.00 53.98  ? 2324 PHE   A CD1  1 
ATOM   5709 C  CD2  . PHE   A 1 992  ? 193.567 191.031 131.718 1.00 57.66  ? 2324 PHE   A CD2  1 
ATOM   5710 C  CE1  . PHE   A 1 992  ? 193.498 188.347 132.229 1.00 61.44  ? 2324 PHE   A CE1  1 
ATOM   5711 C  CE2  . PHE   A 1 992  ? 192.389 190.437 132.080 1.00 58.19  ? 2324 PHE   A CE2  1 
ATOM   5712 C  CZ   . PHE   A 1 992  ? 192.354 189.094 132.336 1.00 66.03  ? 2324 PHE   A CZ   1 
ATOM   5713 N  N    . SER   A 1 993  ? 195.507 193.875 131.778 1.00 48.62  ? 2325 SER   A N    1 
ATOM   5714 C  CA   . SER   A 1 993  ? 194.577 194.963 132.010 1.00 54.26  ? 2325 SER   A CA   1 
ATOM   5715 C  C    . SER   A 1 993  ? 193.999 195.390 130.678 1.00 58.52  ? 2325 SER   A C    1 
ATOM   5716 O  O    . SER   A 1 993  ? 194.634 195.233 129.636 1.00 71.04  ? 2325 SER   A O    1 
ATOM   5717 C  CB   . SER   A 1 993  ? 195.256 196.145 132.694 1.00 62.91  ? 2325 SER   A CB   1 
ATOM   5718 O  OG   . SER   A 1 993  ? 196.220 196.726 131.839 1.00 69.57  ? 2325 SER   A OG   1 
ATOM   5719 N  N    . PHE   A 1 994  ? 192.785 195.923 130.714 1.00 55.76  ? 2326 PHE   A N    1 
ATOM   5720 C  CA   . PHE   A 1 994  ? 192.162 196.375 129.481 1.00 64.18  ? 2326 PHE   A CA   1 
ATOM   5721 C  C    . PHE   A 1 994  ? 191.183 197.504 129.761 1.00 70.84  ? 2326 PHE   A C    1 
ATOM   5722 O  O    . PHE   A 1 994  ? 190.606 197.598 130.846 1.00 76.97  ? 2326 PHE   A O    1 
ATOM   5723 C  CB   . PHE   A 1 994  ? 191.476 195.218 128.748 1.00 71.36  ? 2326 PHE   A CB   1 
ATOM   5724 C  CG   . PHE   A 1 994  ? 190.347 194.595 129.505 1.00 70.79  ? 2326 PHE   A CG   1 
ATOM   5725 C  CD1  . PHE   A 1 994  ? 189.059 195.058 129.357 1.00 74.14  ? 2326 PHE   A CD1  1 
ATOM   5726 C  CD2  . PHE   A 1 994  ? 190.574 193.528 130.345 1.00 63.34  ? 2326 PHE   A CD2  1 
ATOM   5727 C  CE1  . PHE   A 1 994  ? 188.025 194.480 130.044 1.00 60.64  ? 2326 PHE   A CE1  1 
ATOM   5728 C  CE2  . PHE   A 1 994  ? 189.545 192.951 131.034 1.00 61.36  ? 2326 PHE   A CE2  1 
ATOM   5729 C  CZ   . PHE   A 1 994  ? 188.269 193.426 130.883 1.00 59.19  ? 2326 PHE   A CZ   1 
ATOM   5730 N  N    . SER   A 1 995  ? 191.025 198.367 128.767 1.00 70.34  ? 2327 SER   A N    1 
ATOM   5731 C  CA   . SER   A 1 995  ? 190.164 199.533 128.823 1.00 80.36  ? 2327 SER   A CA   1 
ATOM   5732 C  C    . SER   A 1 995  ? 188.822 199.226 128.159 1.00 87.14  ? 2327 SER   A C    1 
ATOM   5733 O  O    . SER   A 1 995  ? 188.516 198.078 127.829 1.00 91.75  ? 2327 SER   A O    1 
ATOM   5734 C  CB   . SER   A 1 995  ? 190.874 200.716 128.168 1.00 87.04  ? 2327 SER   A CB   1 
ATOM   5735 O  OG   . SER   A 1 995  ? 191.063 200.489 126.784 1.00 95.89  ? 2327 SER   A OG   1 
ATOM   5736 N  N    . ASN   A 1 996  ? 188.003 200.264 127.961 1.00 91.83  ? 2328 ASN   A N    1 
ATOM   5737 C  CA   . ASN   A 1 996  ? 186.692 200.077 127.346 1.00 95.93  ? 2328 ASN   A CA   1 
ATOM   5738 C  C    . ASN   A 1 996  ? 186.788 199.643 125.890 1.00 92.66  ? 2328 ASN   A C    1 
ATOM   5739 O  O    . ASN   A 1 996  ? 185.783 199.213 125.317 1.00 94.24  ? 2328 ASN   A O    1 
ATOM   5740 C  CB   . ASN   A 1 996  ? 185.865 201.356 127.454 1.00 106.19 ? 2328 ASN   A CB   1 
ATOM   5741 C  CG   . ASN   A 1 996  ? 184.921 201.337 128.640 1.00 115.59 ? 2328 ASN   A CG   1 
ATOM   5742 O  OD1  . ASN   A 1 996  ? 184.405 200.286 129.022 1.00 103.97 ? 2328 ASN   A OD1  1 
ATOM   5743 N  ND2  . ASN   A 1 996  ? 184.693 202.502 129.232 1.00 114.04 ? 2328 ASN   A ND2  1 
ATOM   5744 N  N    . ASP   A 1 997  ? 187.963 199.768 125.275 1.00 88.55  ? 2329 ASP   A N    1 
ATOM   5745 C  CA   . ASP   A 1 997  ? 188.190 199.178 123.963 1.00 87.14  ? 2329 ASP   A CA   1 
ATOM   5746 C  C    . ASP   A 1 997  ? 188.106 197.655 124.035 1.00 89.08  ? 2329 ASP   A C    1 
ATOM   5747 O  O    . ASP   A 1 997  ? 187.751 197.014 123.043 1.00 89.20  ? 2329 ASP   A O    1 
ATOM   5748 C  CB   . ASP   A 1 997  ? 189.555 199.657 123.444 1.00 96.56  ? 2329 ASP   A CB   1 
ATOM   5749 C  CG   . ASP   A 1 997  ? 189.985 199.004 122.132 1.00 117.00 ? 2329 ASP   A CG   1 
ATOM   5750 O  OD1  . ASP   A 1 997  ? 191.151 199.218 121.738 1.00 124.42 ? 2329 ASP   A OD1  1 
ATOM   5751 O  OD2  . ASP   A 1 997  ? 189.166 198.362 121.447 1.00 124.07 ? 2329 ASP   A OD2  1 
ATOM   5752 N  N    . PHE   A 1 998  ? 188.391 197.077 125.205 1.00 90.19  ? 2330 PHE   A N    1 
ATOM   5753 C  CA   . PHE   A 1 998  ? 188.326 195.634 125.445 1.00 82.44  ? 2330 PHE   A CA   1 
ATOM   5754 C  C    . PHE   A 1 998  ? 189.412 194.882 124.681 1.00 84.11  ? 2330 PHE   A C    1 
ATOM   5755 O  O    . PHE   A 1 998  ? 189.175 193.804 124.134 1.00 90.83  ? 2330 PHE   A O    1 
ATOM   5756 C  CB   . PHE   A 1 998  ? 186.947 195.061 125.120 1.00 78.53  ? 2330 PHE   A CB   1 
ATOM   5757 C  CG   . PHE   A 1 998  ? 185.860 195.535 126.036 1.00 89.04  ? 2330 PHE   A CG   1 
ATOM   5758 C  CD1  . PHE   A 1 998  ? 186.092 195.680 127.391 1.00 86.94  ? 2330 PHE   A CD1  1 
ATOM   5759 C  CD2  . PHE   A 1 998  ? 184.598 195.822 125.542 1.00 90.11  ? 2330 PHE   A CD2  1 
ATOM   5760 C  CE1  . PHE   A 1 998  ? 185.093 196.112 128.233 1.00 88.56  ? 2330 PHE   A CE1  1 
ATOM   5761 C  CE2  . PHE   A 1 998  ? 183.599 196.253 126.380 1.00 88.46  ? 2330 PHE   A CE2  1 
ATOM   5762 C  CZ   . PHE   A 1 998  ? 183.849 196.396 127.727 1.00 95.58  ? 2330 PHE   A CZ   1 
ATOM   5763 N  N    . THR   A 1 999  ? 190.614 195.450 124.645 1.00 79.88  ? 2331 THR   A N    1 
ATOM   5764 C  CA   . THR   A 1 999  ? 191.807 194.730 124.224 1.00 73.43  ? 2331 THR   A CA   1 
ATOM   5765 C  C    . THR   A 1 999  ? 192.905 194.975 125.247 1.00 71.48  ? 2331 THR   A C    1 
ATOM   5766 O  O    . THR   A 1 999  ? 193.050 196.089 125.759 1.00 72.23  ? 2331 THR   A O    1 
ATOM   5767 C  CB   . THR   A 1 999  ? 192.274 195.150 122.828 1.00 83.11  ? 2331 THR   A CB   1 
ATOM   5768 O  OG1  . THR   A 1 999  ? 193.343 194.294 122.409 1.00 91.11  ? 2331 THR   A OG1  1 
ATOM   5769 C  CG2  . THR   A 1 999  ? 192.747 196.593 122.817 1.00 78.47  ? 2331 THR   A CG2  1 
ATOM   5770 N  N    . ILE   A 1 1000 ? 193.669 193.926 125.554 1.00 65.88  ? 2332 ILE   A N    1 
ATOM   5771 C  CA   . ILE   A 1 1000 ? 194.614 194.001 126.660 1.00 66.02  ? 2332 ILE   A CA   1 
ATOM   5772 C  C    . ILE   A 1 1000 ? 195.711 195.003 126.332 1.00 71.82  ? 2332 ILE   A C    1 
ATOM   5773 O  O    . ILE   A 1 1000 ? 196.334 194.949 125.264 1.00 79.19  ? 2332 ILE   A O    1 
ATOM   5774 C  CB   . ILE   A 1 1000 ? 195.191 192.615 126.984 1.00 50.86  ? 2332 ILE   A CB   1 
ATOM   5775 C  CG1  . ILE   A 1 1000 ? 195.965 192.046 125.801 1.00 58.31  ? 2332 ILE   A CG1  1 
ATOM   5776 C  CG2  . ILE   A 1 1000 ? 194.087 191.669 127.364 1.00 62.31  ? 2332 ILE   A CG2  1 
ATOM   5777 C  CD1  . ILE   A 1 1000 ? 196.742 190.809 126.137 1.00 70.46  ? 2332 ILE   A CD1  1 
ATOM   5778 N  N    . GLN   A 1 1001 ? 195.945 195.937 127.248 1.00 63.85  ? 2333 GLN   A N    1 
ATOM   5779 C  CA   . GLN   A 1 1001 ? 196.946 196.966 127.040 1.00 63.79  ? 2333 GLN   A CA   1 
ATOM   5780 C  C    . GLN   A 1 1001 ? 198.248 196.677 127.767 1.00 70.03  ? 2333 GLN   A C    1 
ATOM   5781 O  O    . GLN   A 1 1001 ? 199.251 197.345 127.498 1.00 81.76  ? 2333 GLN   A O    1 
ATOM   5782 C  CB   . GLN   A 1 1001 ? 196.400 198.323 127.486 1.00 58.53  ? 2333 GLN   A CB   1 
ATOM   5783 C  CG   . GLN   A 1 1001 ? 196.309 198.475 128.980 1.00 65.10  ? 2333 GLN   A CG   1 
ATOM   5784 C  CD   . GLN   A 1 1001 ? 195.905 199.870 129.387 1.00 82.09  ? 2333 GLN   A CD   1 
ATOM   5785 O  OE1  . GLN   A 1 1001 ? 195.346 200.621 128.590 1.00 75.37  ? 2333 GLN   A OE1  1 
ATOM   5786 N  NE2  . GLN   A 1 1001 ? 196.195 200.233 130.629 1.00 84.43  ? 2333 GLN   A NE2  1 
ATOM   5787 N  N    . LYS   A 1 1002 ? 198.262 195.697 128.663 1.00 62.22  ? 2334 LYS   A N    1 
ATOM   5788 C  CA   . LYS   A 1 1002 ? 199.465 195.325 129.390 1.00 63.55  ? 2334 LYS   A CA   1 
ATOM   5789 C  C    . LYS   A 1 1002 ? 199.319 193.878 129.816 1.00 69.20  ? 2334 LYS   A C    1 
ATOM   5790 O  O    . LYS   A 1 1002 ? 198.229 193.456 130.200 1.00 75.48  ? 2334 LYS   A O    1 
ATOM   5791 C  CB   . LYS   A 1 1002 ? 199.684 196.218 130.614 1.00 59.65  ? 2334 LYS   A CB   1 
ATOM   5792 C  CG   . LYS   A 1 1002 ? 201.070 196.112 131.214 1.00 65.98  ? 2334 LYS   A CG   1 
ATOM   5793 C  CD   . LYS   A 1 1002 ? 201.474 197.391 131.924 1.00 73.69  ? 2334 LYS   A CD   1 
ATOM   5794 C  CE   . LYS   A 1 1002 ? 201.933 198.453 130.944 1.00 84.37  ? 2334 LYS   A CE   1 
ATOM   5795 N  NZ   . LYS   A 1 1002 ? 202.892 197.912 129.949 1.00 79.80  ? 2334 LYS   A NZ   1 
ATOM   5796 N  N    . LEU   A 1 1003 ? 200.410 193.121 129.744 1.00 70.37  ? 2335 LEU   A N    1 
ATOM   5797 C  CA   . LEU   A 1 1003 ? 200.392 191.701 130.090 1.00 69.61  ? 2335 LEU   A CA   1 
ATOM   5798 C  C    . LEU   A 1 1003 ? 201.645 191.432 130.920 1.00 74.51  ? 2335 LEU   A C    1 
ATOM   5799 O  O    . LEU   A 1 1003 ? 202.699 191.086 130.382 1.00 76.33  ? 2335 LEU   A O    1 
ATOM   5800 C  CB   . LEU   A 1 1003 ? 200.328 190.844 128.835 1.00 61.59  ? 2335 LEU   A CB   1 
ATOM   5801 C  CG   . LEU   A 1 1003 ? 200.214 189.332 128.985 1.00 59.60  ? 2335 LEU   A CG   1 
ATOM   5802 C  CD1  . LEU   A 1 1003 ? 198.916 188.986 129.678 1.00 63.80  ? 2335 LEU   A CD1  1 
ATOM   5803 C  CD2  . LEU   A 1 1003 ? 200.276 188.668 127.628 1.00 61.16  ? 2335 LEU   A CD2  1 
ATOM   5804 N  N    . ILE   A 1 1004 ? 201.519 191.599 132.236 1.00 70.42  ? 2336 ILE   A N    1 
ATOM   5805 C  CA   . ILE   A 1 1004 ? 202.653 191.483 133.143 1.00 74.39  ? 2336 ILE   A CA   1 
ATOM   5806 C  C    . ILE   A 1 1004 ? 203.010 190.017 133.343 1.00 80.73  ? 2336 ILE   A C    1 
ATOM   5807 O  O    . ILE   A 1 1004 ? 202.136 189.171 133.570 1.00 82.21  ? 2336 ILE   A O    1 
ATOM   5808 C  CB   . ILE   A 1 1004 ? 202.331 192.162 134.481 1.00 65.94  ? 2336 ILE   A CB   1 
ATOM   5809 C  CG1  . ILE   A 1 1004 ? 202.095 193.654 134.274 1.00 72.74  ? 2336 ILE   A CG1  1 
ATOM   5810 C  CG2  . ILE   A 1 1004 ? 203.457 191.961 135.468 1.00 77.12  ? 2336 ILE   A CG2  1 
ATOM   5811 C  CD1  . ILE   A 1 1004 ? 201.527 194.342 135.482 1.00 79.70  ? 2336 ILE   A CD1  1 
ATOM   5812 N  N    . GLU   A 1 1005 ? 204.300 189.712 133.269 1.00 81.01  ? 2337 GLU   A N    1 
ATOM   5813 C  CA   . GLU   A 1 1005 ? 204.817 188.362 133.443 1.00 84.04  ? 2337 GLU   A CA   1 
ATOM   5814 C  C    . GLU   A 1 1005 ? 205.285 188.209 134.883 1.00 87.94  ? 2337 GLU   A C    1 
ATOM   5815 O  O    . GLU   A 1 1005 ? 206.051 189.042 135.375 1.00 88.84  ? 2337 GLU   A O    1 
ATOM   5816 C  CB   . GLU   A 1 1005 ? 205.950 188.130 132.436 1.00 87.30  ? 2337 GLU   A CB   1 
ATOM   5817 C  CG   . GLU   A 1 1005 ? 206.478 186.708 132.229 1.00 102.15 ? 2337 GLU   A CG   1 
ATOM   5818 C  CD   . GLU   A 1 1005 ? 207.179 186.082 133.417 1.00 113.60 ? 2337 GLU   A CD   1 
ATOM   5819 O  OE1  . GLU   A 1 1005 ? 207.432 184.868 133.348 1.00 115.76 ? 2337 GLU   A OE1  1 
ATOM   5820 O  OE2  . GLU   A 1 1005 ? 207.548 186.790 134.375 1.00 116.34 ? 2337 GLU   A OE2  1 
ATOM   5821 N  N    . THR   A 1 1006 ? 204.830 187.147 135.560 1.00 91.07  ? 2338 THR   A N    1 
ATOM   5822 C  CA   . THR   A 1 1006 ? 205.040 187.029 136.999 1.00 99.26  ? 2338 THR   A CA   1 
ATOM   5823 C  C    . THR   A 1 1006 ? 205.830 185.810 137.463 1.00 110.64 ? 2338 THR   A C    1 
ATOM   5824 O  O    . THR   A 1 1006 ? 206.364 185.847 138.578 1.00 111.80 ? 2338 THR   A O    1 
ATOM   5825 C  CB   . THR   A 1 1006 ? 203.697 187.030 137.749 1.00 85.52  ? 2338 THR   A CB   1 
ATOM   5826 O  OG1  . THR   A 1 1006 ? 202.907 185.913 137.335 1.00 83.71  ? 2338 THR   A OG1  1 
ATOM   5827 C  CG2  . THR   A 1 1006 ? 202.936 188.294 137.473 1.00 82.26  ? 2338 THR   A CG2  1 
ATOM   5828 N  N    . ARG   A 1 1007 ? 205.919 184.737 136.674 1.00 111.03 ? 2339 ARG   A N    1 
ATOM   5829 C  CA   . ARG   A 1 1007 ? 206.623 183.558 137.173 1.00 111.72 ? 2339 ARG   A CA   1 
ATOM   5830 C  C    . ARG   A 1 1007 ? 208.109 183.834 137.356 1.00 117.67 ? 2339 ARG   A C    1 
ATOM   5831 O  O    . ARG   A 1 1007 ? 208.742 183.247 138.240 1.00 121.92 ? 2339 ARG   A O    1 
ATOM   5832 C  CB   . ARG   A 1 1007 ? 206.403 182.363 136.239 1.00 120.03 ? 2339 ARG   A CB   1 
ATOM   5833 C  CG   . ARG   A 1 1007 ? 207.226 182.375 134.968 1.00 117.90 ? 2339 ARG   A CG   1 
ATOM   5834 C  CD   . ARG   A 1 1007 ? 206.848 181.243 134.022 1.00 114.25 ? 2339 ARG   A CD   1 
ATOM   5835 N  NE   . ARG   A 1 1007 ? 206.331 180.071 134.717 1.00 125.55 ? 2339 ARG   A NE   1 
ATOM   5836 C  CZ   . ARG   A 1 1007 ? 205.759 179.038 134.113 1.00 125.00 ? 2339 ARG   A CZ   1 
ATOM   5837 N  NH1  . ARG   A 1 1007 ? 205.617 178.998 132.799 1.00 126.57 ? 2339 ARG   A NH1  1 
ATOM   5838 N  NH2  . ARG   A 1 1007 ? 205.317 178.022 134.847 1.00 119.77 ? 2339 ARG   A NH2  1 
ATOM   5839 N  N    . THR   A 1 1008 ? 208.668 184.757 136.566 1.00 118.59 ? 2340 THR   A N    1 
ATOM   5840 C  CA   . THR   A 1 1008 ? 210.089 185.076 136.655 1.00 117.35 ? 2340 THR   A CA   1 
ATOM   5841 C  C    . THR   A 1 1008 ? 210.456 185.618 138.031 1.00 119.79 ? 2340 THR   A C    1 
ATOM   5842 O  O    . THR   A 1 1008 ? 211.630 185.578 138.416 1.00 124.11 ? 2340 THR   A O    1 
ATOM   5843 C  CB   . THR   A 1 1008 ? 210.462 186.078 135.555 1.00 114.63 ? 2340 THR   A CB   1 
ATOM   5844 O  OG1  . THR   A 1 1008 ? 210.174 185.503 134.274 1.00 118.49 ? 2340 THR   A OG1  1 
ATOM   5845 C  CG2  . THR   A 1 1008 ? 211.945 186.426 135.596 1.00 110.87 ? 2340 THR   A CG2  1 
ATOM   5846 N  N    . SER   A 1 1009 ? 209.468 186.069 138.802 1.00 120.57 ? 2341 SER   A N    1 
ATOM   5847 C  CA   . SER   A 1 1009 ? 209.698 186.538 140.161 1.00 123.51 ? 2341 SER   A CA   1 
ATOM   5848 C  C    . SER   A 1 1009 ? 210.108 185.400 141.088 1.00 120.30 ? 2341 SER   A C    1 
ATOM   5849 O  O    . SER   A 1 1009 ? 210.251 185.609 142.295 1.00 118.13 ? 2341 SER   A O    1 
ATOM   5850 C  CB   . SER   A 1 1009 ? 208.442 187.214 140.712 1.00 118.34 ? 2341 SER   A CB   1 
ATOM   5851 O  OG   . SER   A 1 1009 ? 207.393 186.273 140.862 1.00 117.44 ? 2341 SER   A OG   1 
ATOM   5852 N  N    . GLN   A 1 1010 ? 210.298 184.195 140.542 1.00 120.49 ? 2342 GLN   A N    1 
ATOM   5853 C  CA   . GLN   A 1 1010 ? 210.688 183.068 141.380 1.00 118.27 ? 2342 GLN   A CA   1 
ATOM   5854 C  C    . GLN   A 1 1010 ? 212.026 183.302 142.064 1.00 125.66 ? 2342 GLN   A C    1 
ATOM   5855 O  O    . GLN   A 1 1010 ? 212.337 182.608 143.038 1.00 126.71 ? 2342 GLN   A O    1 
ATOM   5856 C  CB   . GLN   A 1 1010 ? 210.754 181.781 140.561 1.00 116.18 ? 2342 GLN   A CB   1 
ATOM   5857 C  CG   . GLN   A 1 1010 ? 211.416 181.931 139.212 1.00 117.19 ? 2342 GLN   A CG   1 
ATOM   5858 C  CD   . GLN   A 1 1010 ? 211.376 180.650 138.408 1.00 119.99 ? 2342 GLN   A CD   1 
ATOM   5859 O  OE1  . GLN   A 1 1010 ? 210.435 180.405 137.654 1.00 118.54 ? 2342 GLN   A OE1  1 
ATOM   5860 N  NE2  . GLN   A 1 1010 ? 212.400 179.821 138.570 1.00 121.58 ? 2342 GLN   A NE2  1 
ATOM   5861 N  N    . LEU   A 1 1011 ? 212.830 184.249 141.570 1.00 129.56 ? 2343 LEU   A N    1 
ATOM   5862 C  CA   . LEU   A 1 1011 ? 214.048 184.627 142.279 1.00 131.82 ? 2343 LEU   A CA   1 
ATOM   5863 C  C    . LEU   A 1 1011 ? 213.733 185.005 143.718 1.00 130.37 ? 2343 LEU   A C    1 
ATOM   5864 O  O    . LEU   A 1 1011 ? 214.474 184.653 144.643 1.00 126.65 ? 2343 LEU   A O    1 
ATOM   5865 C  CB   . LEU   A 1 1011 ? 214.744 185.790 141.565 1.00 124.64 ? 2343 LEU   A CB   1 
ATOM   5866 C  CG   . LEU   A 1 1011 ? 215.665 185.514 140.372 1.00 121.51 ? 2343 LEU   A CG   1 
ATOM   5867 C  CD1  . LEU   A 1 1011 ? 216.870 184.693 140.808 1.00 121.16 ? 2343 LEU   A CD1  1 
ATOM   5868 C  CD2  . LEU   A 1 1011 ? 214.934 184.839 139.220 1.00 117.23 ? 2343 LEU   A CD2  1 
ATOM   5869 N  N    . PHE   A 1 1012 ? 212.633 185.717 143.922 1.00 129.59 ? 2344 PHE   A N    1 
ATOM   5870 C  CA   . PHE   A 1 1012 ? 212.110 185.979 145.251 1.00 124.39 ? 2344 PHE   A CA   1 
ATOM   5871 C  C    . PHE   A 1 1012 ? 211.171 184.845 145.635 1.00 124.94 ? 2344 PHE   A C    1 
ATOM   5872 O  O    . PHE   A 1 1012 ? 210.487 184.279 144.778 1.00 125.16 ? 2344 PHE   A O    1 
ATOM   5873 C  CB   . PHE   A 1 1012 ? 211.380 187.321 145.276 1.00 123.26 ? 2344 PHE   A CB   1 
ATOM   5874 C  CG   . PHE   A 1 1012 ? 212.229 188.473 144.817 1.00 135.59 ? 2344 PHE   A CG   1 
ATOM   5875 C  CD1  . PHE   A 1 1012 ? 212.255 188.838 143.483 1.00 137.85 ? 2344 PHE   A CD1  1 
ATOM   5876 C  CD2  . PHE   A 1 1012 ? 213.012 189.178 145.713 1.00 138.57 ? 2344 PHE   A CD2  1 
ATOM   5877 C  CE1  . PHE   A 1 1012 ? 213.036 189.890 143.053 1.00 131.85 ? 2344 PHE   A CE1  1 
ATOM   5878 C  CE2  . PHE   A 1 1012 ? 213.795 190.234 145.288 1.00 133.87 ? 2344 PHE   A CE2  1 
ATOM   5879 C  CZ   . PHE   A 1 1012 ? 213.806 190.589 143.956 1.00 129.23 ? 2344 PHE   A CZ   1 
ATOM   5880 N  N    . SER   A 1 1013 ? 211.154 184.509 146.919 1.00 127.81 ? 2345 SER   A N    1 
ATOM   5881 C  CA   . SER   A 1 1013 ? 210.446 183.315 147.414 1.00 124.01 ? 2345 SER   A CA   1 
ATOM   5882 C  C    . SER   A 1 1013 ? 211.045 182.114 146.676 1.00 122.42 ? 2345 SER   A C    1 
ATOM   5883 O  O    . SER   A 1 1013 ? 212.268 182.067 146.474 1.00 118.04 ? 2345 SER   A O    1 
ATOM   5884 C  CB   . SER   A 1 1013 ? 208.947 183.483 147.265 1.00 118.52 ? 2345 SER   A CB   1 
ATOM   5885 O  OG   . SER   A 1 1013 ? 208.257 182.330 147.716 1.00 114.60 ? 2345 SER   A OG   1 
ATOM   5886 N  N    . TYR   A 1 1014 ? 210.238 181.141 146.259 1.00 125.96 ? 2346 TYR   A N    1 
ATOM   5887 C  CA   . TYR   A 1 1014 ? 210.765 180.010 145.511 1.00 122.61 ? 2346 TYR   A CA   1 
ATOM   5888 C  C    . TYR   A 1 1014 ? 209.665 179.366 144.677 1.00 118.48 ? 2346 TYR   A C    1 
ATOM   5889 O  O    . TYR   A 1 1014 ? 208.493 179.746 144.747 1.00 119.78 ? 2346 TYR   A O    1 
ATOM   5890 C  CB   . TYR   A 1 1014 ? 211.447 178.997 146.438 1.00 122.27 ? 2346 TYR   A CB   1 
ATOM   5891 C  CG   . TYR   A 1 1014 ? 210.571 178.327 147.472 1.00 122.28 ? 2346 TYR   A CG   1 
ATOM   5892 C  CD1  . TYR   A 1 1014 ? 210.406 178.885 148.730 1.00 121.91 ? 2346 TYR   A CD1  1 
ATOM   5893 C  CD2  . TYR   A 1 1014 ? 209.934 177.127 147.202 1.00 122.16 ? 2346 TYR   A CD2  1 
ATOM   5894 C  CE1  . TYR   A 1 1014 ? 209.624 178.273 149.687 1.00 120.76 ? 2346 TYR   A CE1  1 
ATOM   5895 C  CE2  . TYR   A 1 1014 ? 209.144 176.508 148.154 1.00 125.79 ? 2346 TYR   A CE2  1 
ATOM   5896 C  CZ   . TYR   A 1 1014 ? 208.993 177.085 149.395 1.00 121.78 ? 2346 TYR   A CZ   1 
ATOM   5897 O  OH   . TYR   A 1 1014 ? 208.208 176.472 150.346 1.00 109.06 ? 2346 TYR   A OH   1 
ATOM   5898 N  N    . ALA   A 1 1015 ? 210.074 178.375 143.879 1.00 115.39 ? 2347 ALA   A N    1 
ATOM   5899 C  CA   . ALA   A 1 1015 ? 209.272 177.900 142.756 1.00 115.76 ? 2347 ALA   A CA   1 
ATOM   5900 C  C    . ALA   A 1 1015 ? 207.928 177.317 143.169 1.00 114.13 ? 2347 ALA   A C    1 
ATOM   5901 O  O    . ALA   A 1 1015 ? 206.925 177.592 142.503 1.00 114.06 ? 2347 ALA   A O    1 
ATOM   5902 C  CB   . ALA   A 1 1015 ? 210.056 176.857 141.961 1.00 112.12 ? 2347 ALA   A CB   1 
ATOM   5903 N  N    . ALA   A 1 1016 ? 207.883 176.526 144.242 1.00 114.04 ? 2348 ALA   A N    1 
ATOM   5904 C  CA   . ALA   A 1 1016 ? 206.642 175.860 144.620 1.00 110.16 ? 2348 ALA   A CA   1 
ATOM   5905 C  C    . ALA   A 1 1016 ? 205.532 176.857 144.895 1.00 113.53 ? 2348 ALA   A C    1 
ATOM   5906 O  O    . ALA   A 1 1016 ? 204.349 176.516 144.785 1.00 112.12 ? 2348 ALA   A O    1 
ATOM   5907 C  CB   . ALA   A 1 1016 ? 206.867 174.985 145.848 1.00 107.00 ? 2348 ALA   A CB   1 
ATOM   5908 N  N    . PHE   A 1 1017 ? 205.889 178.087 145.252 1.00 113.31 ? 2349 PHE   A N    1 
ATOM   5909 C  CA   . PHE   A 1 1017 ? 204.924 179.147 145.497 1.00 107.05 ? 2349 PHE   A CA   1 
ATOM   5910 C  C    . PHE   A 1 1017 ? 204.776 180.082 144.308 1.00 109.80 ? 2349 PHE   A C    1 
ATOM   5911 O  O    . PHE   A 1 1017 ? 203.658 180.473 143.965 1.00 106.32 ? 2349 PHE   A O    1 
ATOM   5912 C  CB   . PHE   A 1 1017 ? 205.342 179.953 146.726 1.00 91.92  ? 2349 PHE   A CB   1 
ATOM   5913 C  CG   . PHE   A 1 1017 ? 205.137 179.227 148.010 1.00 90.70  ? 2349 PHE   A CG   1 
ATOM   5914 C  CD1  . PHE   A 1 1017 ? 204.061 178.381 148.172 1.00 88.18  ? 2349 PHE   A CD1  1 
ATOM   5915 C  CD2  . PHE   A 1 1017 ? 206.031 179.372 149.050 1.00 102.57 ? 2349 PHE   A CD2  1 
ATOM   5916 C  CE1  . PHE   A 1 1017 ? 203.877 177.699 149.351 1.00 89.02  ? 2349 PHE   A CE1  1 
ATOM   5917 C  CE2  . PHE   A 1 1017 ? 205.849 178.695 150.234 1.00 101.39 ? 2349 PHE   A CE2  1 
ATOM   5918 C  CZ   . PHE   A 1 1017 ? 204.773 177.858 150.385 1.00 91.38  ? 2349 PHE   A CZ   1 
ATOM   5919 N  N    . SER   A 1 1018 ? 205.887 180.422 143.654 1.00 109.18 ? 2350 SER   A N    1 
ATOM   5920 C  CA   . SER   A 1 1018 ? 205.848 181.423 142.599 1.00 104.40 ? 2350 SER   A CA   1 
ATOM   5921 C  C    . SER   A 1 1018 ? 205.220 180.888 141.320 1.00 108.75 ? 2350 SER   A C    1 
ATOM   5922 O  O    . SER   A 1 1018 ? 204.601 181.653 140.575 1.00 113.68 ? 2350 SER   A O    1 
ATOM   5923 C  CB   . SER   A 1 1018 ? 207.258 181.932 142.322 1.00 105.79 ? 2350 SER   A CB   1 
ATOM   5924 O  OG   . SER   A 1 1018 ? 207.925 182.221 143.536 1.00 104.25 ? 2350 SER   A OG   1 
ATOM   5925 N  N    . ASP   A 1 1019 ? 205.355 179.595 141.046 1.00 108.98 ? 2351 ASP   A N    1 
ATOM   5926 C  CA   . ASP   A 1 1019 ? 204.908 179.053 139.770 1.00 111.01 ? 2351 ASP   A CA   1 
ATOM   5927 C  C    . ASP   A 1 1019 ? 203.458 178.591 139.784 1.00 106.94 ? 2351 ASP   A C    1 
ATOM   5928 O  O    . ASP   A 1 1019 ? 202.991 178.043 138.782 1.00 108.76 ? 2351 ASP   A O    1 
ATOM   5929 C  CB   . ASP   A 1 1019 ? 205.812 177.896 139.344 1.00 116.42 ? 2351 ASP   A CB   1 
ATOM   5930 C  CG   . ASP   A 1 1019 ? 205.872 177.734 137.843 1.00 118.54 ? 2351 ASP   A CG   1 
ATOM   5931 O  OD1  . ASP   A 1 1019 ? 205.615 178.727 137.133 1.00 115.19 ? 2351 ASP   A OD1  1 
ATOM   5932 O  OD2  . ASP   A 1 1019 ? 206.169 176.619 137.371 1.00 122.08 ? 2351 ASP   A OD2  1 
ATOM   5933 N  N    . SER   A 1 1020 ? 202.734 178.795 140.879 1.00 92.53  ? 2352 SER   A N    1 
ATOM   5934 C  CA   . SER   A 1 1020 ? 201.337 178.402 140.926 1.00 88.96  ? 2352 SER   A CA   1 
ATOM   5935 C  C    . SER   A 1 1020 ? 200.493 179.357 140.079 1.00 91.66  ? 2352 SER   A C    1 
ATOM   5936 O  O    . SER   A 1 1020 ? 201.003 180.243 139.390 1.00 94.07  ? 2352 SER   A O    1 
ATOM   5937 C  CB   . SER   A 1 1020 ? 200.850 178.364 142.370 1.00 85.29  ? 2352 SER   A CB   1 
ATOM   5938 O  OG   . SER   A 1 1020 ? 199.622 177.668 142.470 1.00 82.48  ? 2352 SER   A OG   1 
ATOM   5939 N  N    . ASN   A 1 1021 ? 199.179 179.166 140.123 1.00 86.23  ? 2353 ASN   A N    1 
ATOM   5940 C  CA   . ASN   A 1 1021 ? 198.267 180.034 139.397 1.00 79.33  ? 2353 ASN   A CA   1 
ATOM   5941 C  C    . ASN   A 1 1021 ? 198.175 181.393 140.087 1.00 78.57  ? 2353 ASN   A C    1 
ATOM   5942 O  O    . ASN   A 1 1021 ? 198.874 181.676 141.058 1.00 81.57  ? 2353 ASN   A O    1 
ATOM   5943 C  CB   . ASN   A 1 1021 ? 196.889 179.389 139.303 1.00 86.96  ? 2353 ASN   A CB   1 
ATOM   5944 C  CG   . ASN   A 1 1021 ? 196.762 178.459 138.125 1.00 96.43  ? 2353 ASN   A CG   1 
ATOM   5945 O  OD1  . ASN   A 1 1021 ? 197.601 178.459 137.228 1.00 95.36  ? 2353 ASN   A OD1  1 
ATOM   5946 N  ND2  . ASN   A 1 1021 ? 195.706 177.659 138.116 1.00 95.59  ? 2353 ASN   A ND2  1 
ATOM   5947 N  N    . ILE   A 1 1022 ? 197.305 182.254 139.564 1.00 73.53  ? 2354 ILE   A N    1 
ATOM   5948 C  CA   . ILE   A 1 1022 ? 196.886 183.480 140.239 1.00 59.69  ? 2354 ILE   A CA   1 
ATOM   5949 C  C    . ILE   A 1 1022 ? 195.376 183.436 140.405 1.00 56.75  ? 2354 ILE   A C    1 
ATOM   5950 O  O    . ILE   A 1 1022 ? 194.649 183.188 139.438 1.00 51.95  ? 2354 ILE   A O    1 
ATOM   5951 C  CB   . ILE   A 1 1022 ? 197.331 184.740 139.481 1.00 45.59  ? 2354 ILE   A CB   1 
ATOM   5952 C  CG1  . ILE   A 1 1022 ? 198.852 184.814 139.449 1.00 51.90  ? 2354 ILE   A CG1  1 
ATOM   5953 C  CG2  . ILE   A 1 1022 ? 196.756 185.970 140.115 1.00 44.11  ? 2354 ILE   A CG2  1 
ATOM   5954 C  CD1  . ILE   A 1 1022 ? 199.390 185.863 138.534 1.00 62.51  ? 2354 ILE   A CD1  1 
ATOM   5955 N  N    . ILE   A 1 1023 ? 194.906 183.652 141.630 1.00 59.95  ? 2355 ILE   A N    1 
ATOM   5956 C  CA   . ILE   A 1 1023 ? 193.508 183.470 141.967 1.00 55.99  ? 2355 ILE   A CA   1 
ATOM   5957 C  C    . ILE   A 1 1023 ? 192.827 184.787 142.316 1.00 58.92  ? 2355 ILE   A C    1 
ATOM   5958 O  O    . ILE   A 1 1023 ? 191.639 184.958 142.036 1.00 64.09  ? 2355 ILE   A O    1 
ATOM   5959 C  CB   . ILE   A 1 1023 ? 193.348 182.440 143.106 1.00 56.94  ? 2355 ILE   A CB   1 
ATOM   5960 C  CG1  . ILE   A 1 1023 ? 194.045 182.911 144.381 1.00 59.23  ? 2355 ILE   A CG1  1 
ATOM   5961 C  CG2  . ILE   A 1 1023 ? 193.899 181.104 142.680 1.00 66.26  ? 2355 ILE   A CG2  1 
ATOM   5962 C  CD1  . ILE   A 1 1023 ? 193.734 182.062 145.589 1.00 59.20  ? 2355 ILE   A CD1  1 
ATOM   5963 N  N    . THR   A 1 1024 ? 193.542 185.725 142.935 1.00 55.58  ? 2356 THR   A N    1 
ATOM   5964 C  CA   . THR   A 1 1024 ? 192.975 187.036 143.228 1.00 47.11  ? 2356 THR   A CA   1 
ATOM   5965 C  C    . THR   A 1 1024 ? 194.009 188.126 143.002 1.00 53.19  ? 2356 THR   A C    1 
ATOM   5966 O  O    . THR   A 1 1024 ? 195.190 187.953 143.314 1.00 50.14  ? 2356 THR   A O    1 
ATOM   5967 C  CB   . THR   A 1 1024 ? 192.457 187.148 144.666 1.00 45.88  ? 2356 THR   A CB   1 
ATOM   5968 O  OG1  . THR   A 1 1024 ? 193.523 186.879 145.575 1.00 49.40  ? 2356 THR   A OG1  1 
ATOM   5969 C  CG2  . THR   A 1 1024 ? 191.309 186.196 144.923 1.00 65.39  ? 2356 THR   A CG2  1 
ATOM   5970 N  N    . VAL   A 1 1025 ? 193.543 189.252 142.464 1.00 55.37  ? 2357 VAL   A N    1 
ATOM   5971 C  CA   . VAL   A 1 1025 ? 194.331 190.469 142.328 1.00 49.41  ? 2357 VAL   A CA   1 
ATOM   5972 C  C    . VAL   A 1 1025 ? 193.485 191.620 142.846 1.00 57.11  ? 2357 VAL   A C    1 
ATOM   5973 O  O    . VAL   A 1 1025 ? 192.279 191.676 142.578 1.00 47.14  ? 2357 VAL   A O    1 
ATOM   5974 C  CB   . VAL   A 1 1025 ? 194.744 190.736 140.871 1.00 35.09  ? 2357 VAL   A CB   1 
ATOM   5975 C  CG1  . VAL   A 1 1025 ? 195.651 189.654 140.379 1.00 41.52  ? 2357 VAL   A CG1  1 
ATOM   5976 C  CG2  . VAL   A 1 1025 ? 193.532 190.842 139.991 1.00 37.12  ? 2357 VAL   A CG2  1 
ATOM   5977 N  N    . VAL   A 1 1026 ? 194.103 192.521 143.611 1.00 61.00  ? 2358 VAL   A N    1 
ATOM   5978 C  CA   . VAL   A 1 1026 ? 193.489 193.802 143.929 1.00 60.00  ? 2358 VAL   A CA   1 
ATOM   5979 C  C    . VAL   A 1 1026 ? 194.540 194.875 143.707 1.00 64.31  ? 2358 VAL   A C    1 
ATOM   5980 O  O    . VAL   A 1 1026 ? 195.741 194.602 143.652 1.00 63.11  ? 2358 VAL   A O    1 
ATOM   5981 C  CB   . VAL   A 1 1026 ? 192.937 193.900 145.363 1.00 47.71  ? 2358 VAL   A CB   1 
ATOM   5982 C  CG1  . VAL   A 1 1026 ? 191.649 193.099 145.504 1.00 44.55  ? 2358 VAL   A CG1  1 
ATOM   5983 C  CG2  . VAL   A 1 1026 ? 193.976 193.499 146.345 1.00 51.30  ? 2358 VAL   A CG2  1 
ATOM   5984 N  N    . VAL   A 1 1027 ? 194.067 196.109 143.577 1.00 63.96  ? 2359 VAL   A N    1 
ATOM   5985 C  CA   . VAL   A 1 1027 ? 194.926 197.210 143.176 1.00 70.60  ? 2359 VAL   A CA   1 
ATOM   5986 C  C    . VAL   A 1 1027 ? 194.318 198.515 143.667 1.00 77.42  ? 2359 VAL   A C    1 
ATOM   5987 O  O    . VAL   A 1 1027 ? 193.107 198.730 143.575 1.00 89.31  ? 2359 VAL   A O    1 
ATOM   5988 C  CB   . VAL   A 1 1027 ? 195.134 197.211 141.645 1.00 70.87  ? 2359 VAL   A CB   1 
ATOM   5989 C  CG1  . VAL   A 1 1027 ? 193.819 197.459 140.926 1.00 61.44  ? 2359 VAL   A CG1  1 
ATOM   5990 C  CG2  . VAL   A 1 1027 ? 196.140 198.267 141.266 1.00 85.03  ? 2359 VAL   A CG2  1 
ATOM   5991 N  N    . ASP   A 1 1028 ? 195.155 199.351 144.234 1.00 67.57  ? 2360 ASP   A N    1 
ATOM   5992 C  CA   . ASP   A 1 1028 ? 194.867 200.771 144.377 1.00 75.55  ? 2360 ASP   A CA   1 
ATOM   5993 C  C    . ASP   A 1 1028 ? 196.056 201.630 143.981 1.00 89.18  ? 2360 ASP   A C    1 
ATOM   5994 O  O    . ASP   A 1 1028 ? 195.877 202.668 143.340 1.00 94.53  ? 2360 ASP   A O    1 
ATOM   5995 C  CB   . ASP   A 1 1028 ? 194.430 201.092 145.811 1.00 82.19  ? 2360 ASP   A CB   1 
ATOM   5996 C  CG   . ASP   A 1 1028 ? 195.576 201.041 146.796 1.00 89.44  ? 2360 ASP   A CG   1 
ATOM   5997 O  OD1  . ASP   A 1 1028 ? 196.576 200.347 146.518 1.00 88.88  ? 2360 ASP   A OD1  1 
ATOM   5998 O  OD2  . ASP   A 1 1028 ? 195.485 201.714 147.843 1.00 88.43  ? 2360 ASP   A OD2  1 
ATOM   5999 N  N    . THR   A 1 1029 ? 197.267 201.215 144.343 1.00 90.82  ? 2361 THR   A N    1 
ATOM   6000 C  CA   . THR   A 1 1029 ? 198.500 201.819 143.862 1.00 96.01  ? 2361 THR   A CA   1 
ATOM   6001 C  C    . THR   A 1 1029 ? 199.484 200.796 143.328 1.00 95.79  ? 2361 THR   A C    1 
ATOM   6002 O  O    . THR   A 1 1029 ? 200.445 201.184 142.653 1.00 98.58  ? 2361 THR   A O    1 
ATOM   6003 C  CB   . THR   A 1 1029 ? 199.182 202.631 144.974 1.00 100.09 ? 2361 THR   A CB   1 
ATOM   6004 O  OG1  . THR   A 1 1029 ? 200.295 203.348 144.430 1.00 96.14  ? 2361 THR   A OG1  1 
ATOM   6005 C  CG2  . THR   A 1 1029 ? 199.678 201.716 146.078 1.00 96.96  ? 2361 THR   A CG2  1 
ATOM   6006 N  N    . ALA   A 1 1030 ? 199.290 199.514 143.622 1.00 92.45  ? 2362 ALA   A N    1 
ATOM   6007 C  CA   . ALA   A 1 1030 ? 200.032 198.429 143.009 1.00 89.62  ? 2362 ALA   A CA   1 
ATOM   6008 C  C    . ALA   A 1 1030 ? 199.164 197.184 143.078 1.00 83.00  ? 2362 ALA   A C    1 
ATOM   6009 O  O    . ALA   A 1 1030 ? 198.342 197.040 143.986 1.00 81.82  ? 2362 ALA   A O    1 
ATOM   6010 C  CB   . ALA   A 1 1030 ? 201.375 198.201 143.703 1.00 83.72  ? 2362 ALA   A CB   1 
ATOM   6011 N  N    . LEU   A 1 1031 ? 199.338 196.293 142.107 1.00 81.99  ? 2363 LEU   A N    1 
ATOM   6012 C  CA   . LEU   A 1 1031 ? 198.568 195.056 142.080 1.00 72.48  ? 2363 LEU   A CA   1 
ATOM   6013 C  C    . LEU   A 1 1031 ? 198.960 194.173 143.252 1.00 76.11  ? 2363 LEU   A C    1 
ATOM   6014 O  O    . LEU   A 1 1031 ? 200.142 193.865 143.439 1.00 79.65  ? 2363 LEU   A O    1 
ATOM   6015 C  CB   . LEU   A 1 1031 ? 198.780 194.306 140.769 1.00 73.28  ? 2363 LEU   A CB   1 
ATOM   6016 C  CG   . LEU   A 1 1031 ? 197.960 194.679 139.536 1.00 75.66  ? 2363 LEU   A CG   1 
ATOM   6017 C  CD1  . LEU   A 1 1031 ? 196.499 194.405 139.806 1.00 74.17  ? 2363 LEU   A CD1  1 
ATOM   6018 C  CD2  . LEU   A 1 1031 ? 198.163 196.102 139.125 1.00 73.04  ? 2363 LEU   A CD2  1 
ATOM   6019 N  N    . TYR   A 1 1032 ? 197.969 193.763 144.035 1.00 68.10  ? 2364 TYR   A N    1 
ATOM   6020 C  CA   . TYR   A 1 1032 ? 198.166 192.854 145.156 1.00 62.96  ? 2364 TYR   A CA   1 
ATOM   6021 C  C    . TYR   A 1 1032 ? 197.624 191.506 144.704 1.00 66.10  ? 2364 TYR   A C    1 
ATOM   6022 O  O    . TYR   A 1 1032 ? 196.413 191.276 144.746 1.00 65.79  ? 2364 TYR   A O    1 
ATOM   6023 C  CB   . TYR   A 1 1032 ? 197.456 193.367 146.403 1.00 62.72  ? 2364 TYR   A CB   1 
ATOM   6024 C  CG   . TYR   A 1 1032 ? 198.106 194.589 147.005 1.00 70.22  ? 2364 TYR   A CG   1 
ATOM   6025 C  CD1  . TYR   A 1 1032 ? 199.366 194.520 147.573 1.00 72.23  ? 2364 TYR   A CD1  1 
ATOM   6026 C  CD2  . TYR   A 1 1032 ? 197.464 195.818 146.986 1.00 75.93  ? 2364 TYR   A CD2  1 
ATOM   6027 C  CE1  . TYR   A 1 1032 ? 199.962 195.637 148.113 1.00 76.09  ? 2364 TYR   A CE1  1 
ATOM   6028 C  CE2  . TYR   A 1 1032 ? 198.054 196.938 147.522 1.00 76.04  ? 2364 TYR   A CE2  1 
ATOM   6029 C  CZ   . TYR   A 1 1032 ? 199.304 196.842 148.083 1.00 76.23  ? 2364 TYR   A CZ   1 
ATOM   6030 O  OH   . TYR   A 1 1032 ? 199.903 197.954 148.624 1.00 76.77  ? 2364 TYR   A OH   1 
ATOM   6031 N  N    . ILE   A 1 1033 ? 198.514 190.625 144.250 1.00 71.32  ? 2365 ILE   A N    1 
ATOM   6032 C  CA   . ILE   A 1 1033 ? 198.114 189.359 143.647 1.00 56.67  ? 2365 ILE   A CA   1 
ATOM   6033 C  C    . ILE   A 1 1033 ? 198.300 188.250 144.670 1.00 56.47  ? 2365 ILE   A C    1 
ATOM   6034 O  O    . ILE   A 1 1033 ? 199.305 188.211 145.390 1.00 64.99  ? 2365 ILE   A O    1 
ATOM   6035 C  CB   . ILE   A 1 1033 ? 198.899 189.030 142.362 1.00 51.35  ? 2365 ILE   A CB   1 
ATOM   6036 C  CG1  . ILE   A 1 1033 ? 200.374 188.849 142.641 1.00 59.06  ? 2365 ILE   A CG1  1 
ATOM   6037 C  CG2  . ILE   A 1 1033 ? 198.848 190.178 141.404 1.00 62.72  ? 2365 ILE   A CG2  1 
ATOM   6038 C  CD1  . ILE   A 1 1033 ? 201.099 188.300 141.457 1.00 66.02  ? 2365 ILE   A CD1  1 
ATOM   6039 N  N    . ALA   A 1 1034 ? 197.329 187.350 144.733 1.00 49.50  ? 2366 ALA   A N    1 
ATOM   6040 C  CA   . ALA   A 1 1034 ? 197.431 186.149 145.540 1.00 52.75  ? 2366 ALA   A CA   1 
ATOM   6041 C  C    . ALA   A 1 1034 ? 197.389 184.944 144.621 1.00 60.75  ? 2366 ALA   A C    1 
ATOM   6042 O  O    . ALA   A 1 1034 ? 196.552 184.870 143.716 1.00 64.25  ? 2366 ALA   A O    1 
ATOM   6043 C  CB   . ALA   A 1 1034 ? 196.312 186.059 146.565 1.00 54.90  ? 2366 ALA   A CB   1 
ATOM   6044 N  N    . LYS   A 1 1035 ? 198.301 184.014 144.849 1.00 67.67  ? 2367 LYS   A N    1 
ATOM   6045 C  CA   . LYS   A 1 1035 ? 198.421 182.815 144.042 1.00 60.63  ? 2367 LYS   A CA   1 
ATOM   6046 C  C    . LYS   A 1 1035 ? 197.637 181.687 144.693 1.00 61.68  ? 2367 LYS   A C    1 
ATOM   6047 O  O    . LYS   A 1 1035 ? 197.107 181.822 145.794 1.00 72.46  ? 2367 LYS   A O    1 
ATOM   6048 C  CB   . LYS   A 1 1035 ? 199.891 182.441 143.879 1.00 64.80  ? 2367 LYS   A CB   1 
ATOM   6049 C  CG   . LYS   A 1 1035 ? 200.624 183.324 142.895 1.00 67.24  ? 2367 LYS   A CG   1 
ATOM   6050 C  CD   . LYS   A 1 1035 ? 202.093 183.413 143.222 1.00 77.43  ? 2367 LYS   A CD   1 
ATOM   6051 C  CE   . LYS   A 1 1035 ? 202.809 184.314 142.244 1.00 80.05  ? 2367 LYS   A CE   1 
ATOM   6052 N  NZ   . LYS   A 1 1035 ? 202.272 184.165 140.869 1.00 82.73  ? 2367 LYS   A NZ   1 
ATOM   6053 N  N    . GLN   A 1 1036 ? 197.531 180.572 143.985 1.00 59.65  ? 2368 GLN   A N    1 
ATOM   6054 C  CA   . GLN   A 1 1036 ? 196.846 179.415 144.541 1.00 71.88  ? 2368 GLN   A CA   1 
ATOM   6055 C  C    . GLN   A 1 1036 ? 197.783 178.686 145.492 1.00 84.12  ? 2368 GLN   A C    1 
ATOM   6056 O  O    . GLN   A 1 1036 ? 198.846 178.209 145.079 1.00 88.68  ? 2368 GLN   A O    1 
ATOM   6057 C  CB   . GLN   A 1 1036 ? 196.360 178.481 143.439 1.00 81.17  ? 2368 GLN   A CB   1 
ATOM   6058 C  CG   . GLN   A 1 1036 ? 195.581 177.298 143.972 1.00 93.03  ? 2368 GLN   A CG   1 
ATOM   6059 C  CD   . GLN   A 1 1036 ? 194.429 176.906 143.081 1.00 99.78  ? 2368 GLN   A CD   1 
ATOM   6060 O  OE1  . GLN   A 1 1036 ? 194.590 176.745 141.874 1.00 105.77 ? 2368 GLN   A OE1  1 
ATOM   6061 N  NE2  . GLN   A 1 1036 ? 193.254 176.745 143.675 1.00 88.15  ? 2368 GLN   A NE2  1 
ATOM   6062 N  N    . ASN   A 1 1037 ? 197.388 178.606 146.763 1.00 84.71  ? 2369 ASN   A N    1 
ATOM   6063 C  CA   . ASN   A 1 1037 ? 198.149 177.909 147.797 1.00 80.79  ? 2369 ASN   A CA   1 
ATOM   6064 C  C    . ASN   A 1 1037 ? 199.579 178.442 147.882 1.00 85.79  ? 2369 ASN   A C    1 
ATOM   6065 O  O    . ASN   A 1 1037 ? 200.556 177.742 147.611 1.00 88.66  ? 2369 ASN   A O    1 
ATOM   6066 C  CB   . ASN   A 1 1037 ? 198.126 176.400 147.558 1.00 77.67  ? 2369 ASN   A CB   1 
ATOM   6067 C  CG   . ASN   A 1 1037 ? 196.746 175.822 147.699 1.00 80.19  ? 2369 ASN   A CG   1 
ATOM   6068 O  OD1  . ASN   A 1 1037 ? 195.953 176.283 148.516 1.00 82.27  ? 2369 ASN   A OD1  1 
ATOM   6069 N  ND2  . ASN   A 1 1037 ? 196.444 174.807 146.902 1.00 83.34  ? 2369 ASN   A ND2  1 
ATOM   6070 N  N    . SER   A 1 1038 ? 199.678 179.708 148.259 1.00 81.77  ? 2370 SER   A N    1 
ATOM   6071 C  CA   . SER   A 1 1038 ? 200.955 180.385 148.413 1.00 85.29  ? 2370 SER   A CA   1 
ATOM   6072 C  C    . SER   A 1 1038 ? 200.831 181.505 149.433 1.00 79.91  ? 2370 SER   A C    1 
ATOM   6073 O  O    . SER   A 1 1038 ? 200.090 182.468 149.204 1.00 80.95  ? 2370 SER   A O    1 
ATOM   6074 C  CB   . SER   A 1 1038 ? 201.432 180.944 147.076 1.00 80.96  ? 2370 SER   A CB   1 
ATOM   6075 O  OG   . SER   A 1 1038 ? 202.655 181.636 147.233 1.00 85.67  ? 2370 SER   A OG   1 
ATOM   6076 N  N    . PRO   A 1 1039 ? 201.533 181.423 150.562 1.00 76.35  ? 2371 PRO   A N    1 
ATOM   6077 C  CA   . PRO   A 1 1039 ? 201.428 182.494 151.559 1.00 77.19  ? 2371 PRO   A CA   1 
ATOM   6078 C  C    . PRO   A 1 1039 ? 201.870 183.847 151.043 1.00 79.00  ? 2371 PRO   A C    1 
ATOM   6079 O  O    . PRO   A 1 1039 ? 201.316 184.869 151.463 1.00 83.43  ? 2371 PRO   A O    1 
ATOM   6080 C  CB   . PRO   A 1 1039 ? 202.336 182.001 152.690 1.00 83.29  ? 2371 PRO   A CB   1 
ATOM   6081 C  CG   . PRO   A 1 1039 ? 203.322 181.137 152.022 1.00 87.18  ? 2371 PRO   A CG   1 
ATOM   6082 C  CD   . PRO   A 1 1039 ? 202.591 180.462 150.901 1.00 80.83  ? 2371 PRO   A CD   1 
ATOM   6083 N  N    . VAL   A 1 1040 ? 202.842 183.893 150.137 1.00 70.86  ? 2372 VAL   A N    1 
ATOM   6084 C  CA   . VAL   A 1 1040 ? 203.361 185.173 149.677 1.00 65.72  ? 2372 VAL   A CA   1 
ATOM   6085 C  C    . VAL   A 1 1040 ? 202.300 185.868 148.837 1.00 70.24  ? 2372 VAL   A C    1 
ATOM   6086 O  O    . VAL   A 1 1040 ? 201.805 185.310 147.852 1.00 80.76  ? 2372 VAL   A O    1 
ATOM   6087 C  CB   . VAL   A 1 1040 ? 204.658 184.984 148.885 1.00 69.86  ? 2372 VAL   A CB   1 
ATOM   6088 C  CG1  . VAL   A 1 1040 ? 205.175 186.319 148.407 1.00 72.23  ? 2372 VAL   A CG1  1 
ATOM   6089 C  CG2  . VAL   A 1 1040 ? 205.695 184.290 149.743 1.00 86.09  ? 2372 VAL   A CG2  1 
ATOM   6090 N  N    . VAL   A 1 1041 ? 201.938 187.083 149.233 1.00 64.89  ? 2373 VAL   A N    1 
ATOM   6091 C  CA   . VAL   A 1 1041 ? 201.045 187.940 148.463 1.00 66.87  ? 2373 VAL   A CA   1 
ATOM   6092 C  C    . VAL   A 1 1041 ? 201.900 189.024 147.830 1.00 67.45  ? 2373 VAL   A C    1 
ATOM   6093 O  O    . VAL   A 1 1041 ? 202.625 189.739 148.531 1.00 69.22  ? 2373 VAL   A O    1 
ATOM   6094 C  CB   . VAL   A 1 1041 ? 199.943 188.541 149.346 1.00 53.08  ? 2373 VAL   A CB   1 
ATOM   6095 C  CG1  . VAL   A 1 1041 ? 199.354 189.764 148.686 1.00 61.59  ? 2373 VAL   A CG1  1 
ATOM   6096 C  CG2  . VAL   A 1 1041 ? 198.867 187.510 149.613 1.00 38.13  ? 2373 VAL   A CG2  1 
ATOM   6097 N  N    . GLU   A 1 1042 ? 201.826 189.151 146.511 1.00 65.28  ? 2374 GLU   A N    1 
ATOM   6098 C  CA   . GLU   A 1 1042 ? 202.831 189.884 145.756 1.00 72.98  ? 2374 GLU   A CA   1 
ATOM   6099 C  C    . GLU   A 1 1042 ? 202.341 191.268 145.348 1.00 75.98  ? 2374 GLU   A C    1 
ATOM   6100 O  O    . GLU   A 1 1042 ? 201.145 191.495 145.147 1.00 69.51  ? 2374 GLU   A O    1 
ATOM   6101 C  CB   . GLU   A 1 1042 ? 203.242 189.093 144.516 1.00 78.59  ? 2374 GLU   A CB   1 
ATOM   6102 C  CG   . GLU   A 1 1042 ? 203.981 187.812 144.826 1.00 81.82  ? 2374 GLU   A CG   1 
ATOM   6103 C  CD   . GLU   A 1 1042 ? 204.349 187.045 143.580 1.00 82.11  ? 2374 GLU   A CD   1 
ATOM   6104 O  OE1  . GLU   A 1 1042 ? 203.913 187.453 142.486 1.00 86.87  ? 2374 GLU   A OE1  1 
ATOM   6105 O  OE2  . GLU   A 1 1042 ? 205.082 186.042 143.690 1.00 82.04  ? 2374 GLU   A OE2  1 
ATOM   6106 N  N    . VAL   A 1 1043 ? 203.295 192.188 145.214 1.00 84.03  ? 2375 VAL   A N    1 
ATOM   6107 C  CA   . VAL   A 1 1043 ? 203.031 193.588 144.906 1.00 81.12  ? 2375 VAL   A CA   1 
ATOM   6108 C  C    . VAL   A 1 1043 ? 203.689 193.918 143.573 1.00 85.03  ? 2375 VAL   A C    1 
ATOM   6109 O  O    . VAL   A 1 1043 ? 204.922 193.882 143.454 1.00 89.52  ? 2375 VAL   A O    1 
ATOM   6110 C  CB   . VAL   A 1 1043 ? 203.557 194.513 146.010 1.00 80.80  ? 2375 VAL   A CB   1 
ATOM   6111 C  CG1  . VAL   A 1 1043 ? 203.358 195.961 145.629 1.00 86.19  ? 2375 VAL   A CG1  1 
ATOM   6112 C  CG2  . VAL   A 1 1043 ? 202.893 194.189 147.329 1.00 78.31  ? 2375 VAL   A CG2  1 
ATOM   6113 N  N    . TRP   A 1 1044 ? 202.869 194.273 142.587 1.00 84.71  ? 2376 TRP   A N    1 
ATOM   6114 C  CA   . TRP   A 1 1044 ? 203.308 194.524 141.217 1.00 91.87  ? 2376 TRP   A CA   1 
ATOM   6115 C  C    . TRP   A 1 1044 ? 202.952 195.951 140.824 1.00 91.21  ? 2376 TRP   A C    1 
ATOM   6116 O  O    . TRP   A 1 1044 ? 201.776 196.264 140.625 1.00 90.58  ? 2376 TRP   A O    1 
ATOM   6117 C  CB   . TRP   A 1 1044 ? 202.661 193.523 140.260 1.00 88.38  ? 2376 TRP   A CB   1 
ATOM   6118 C  CG   . TRP   A 1 1044 ? 203.322 192.187 140.247 1.00 89.64  ? 2376 TRP   A CG   1 
ATOM   6119 C  CD1  . TRP   A 1 1044 ? 202.906 191.067 140.889 1.00 87.36  ? 2376 TRP   A CD1  1 
ATOM   6120 C  CD2  . TRP   A 1 1044 ? 204.490 191.817 139.509 1.00 89.21  ? 2376 TRP   A CD2  1 
ATOM   6121 N  NE1  . TRP   A 1 1044 ? 203.760 190.026 140.627 1.00 89.49  ? 2376 TRP   A NE1  1 
ATOM   6122 C  CE2  . TRP   A 1 1044 ? 204.739 190.462 139.776 1.00 89.51  ? 2376 TRP   A CE2  1 
ATOM   6123 C  CE3  . TRP   A 1 1044 ? 205.355 192.504 138.656 1.00 89.72  ? 2376 TRP   A CE3  1 
ATOM   6124 C  CZ2  . TRP   A 1 1044 ? 205.815 189.780 139.224 1.00 92.85  ? 2376 TRP   A CZ2  1 
ATOM   6125 C  CZ3  . TRP   A 1 1044 ? 206.420 191.824 138.107 1.00 91.24  ? 2376 TRP   A CZ3  1 
ATOM   6126 C  CH2  . TRP   A 1 1044 ? 206.643 190.478 138.394 1.00 91.15  ? 2376 TRP   A CH2  1 
ATOM   6127 N  N    . ASP   A 1 1045 ? 203.960 196.806 140.678 1.00 88.64  ? 2377 ASP   A N    1 
ATOM   6128 C  CA   . ASP   A 1 1045 ? 203.699 198.176 140.259 1.00 91.21  ? 2377 ASP   A CA   1 
ATOM   6129 C  C    . ASP   A 1 1045 ? 203.133 198.211 138.848 1.00 93.40  ? 2377 ASP   A C    1 
ATOM   6130 O  O    . ASP   A 1 1045 ? 203.615 197.513 137.953 1.00 97.95  ? 2377 ASP   A O    1 
ATOM   6131 C  CB   . ASP   A 1 1045 ? 204.972 199.011 140.324 1.00 103.08 ? 2377 ASP   A CB   1 
ATOM   6132 C  CG   . ASP   A 1 1045 ? 204.718 200.471 140.010 1.00 114.41 ? 2377 ASP   A CG   1 
ATOM   6133 O  OD1  . ASP   A 1 1045 ? 204.146 201.180 140.866 1.00 122.04 ? 2377 ASP   A OD1  1 
ATOM   6134 O  OD2  . ASP   A 1 1045 ? 205.083 200.910 138.899 1.00 109.90 ? 2377 ASP   A OD2  1 
ATOM   6135 N  N    . LYS   A 1 1046 ? 202.108 199.040 138.653 1.00 92.81  ? 2378 LYS   A N    1 
ATOM   6136 C  CA   . LYS   A 1 1046 ? 201.475 199.163 137.348 1.00 97.65  ? 2378 LYS   A CA   1 
ATOM   6137 C  C    . LYS   A 1 1046 ? 202.379 199.826 136.321 1.00 101.37 ? 2378 LYS   A C    1 
ATOM   6138 O  O    . LYS   A 1 1046 ? 202.407 199.390 135.167 1.00 94.44  ? 2378 LYS   A O    1 
ATOM   6139 C  CB   . LYS   A 1 1046 ? 200.182 199.962 137.476 1.00 99.77  ? 2378 LYS   A CB   1 
ATOM   6140 C  CG   . LYS   A 1 1046 ? 199.129 199.269 138.295 1.00 93.65  ? 2378 LYS   A CG   1 
ATOM   6141 C  CD   . LYS   A 1 1046 ? 198.522 200.195 139.322 1.00 91.33  ? 2378 LYS   A CD   1 
ATOM   6142 C  CE   . LYS   A 1 1046 ? 197.302 200.899 138.775 1.00 87.24  ? 2378 LYS   A CE   1 
ATOM   6143 N  NZ   . LYS   A 1 1046 ? 196.478 201.474 139.869 1.00 86.17  ? 2378 LYS   A NZ   1 
ATOM   6144 N  N    . LYS   A 1 1047 ? 203.123 200.858 136.715 1.00 106.95 ? 2379 LYS   A N    1 
ATOM   6145 C  CA   . LYS   A 1 1047 ? 203.911 201.620 135.754 1.00 109.20 ? 2379 LYS   A CA   1 
ATOM   6146 C  C    . LYS   A 1 1047 ? 205.193 200.883 135.387 1.00 107.26 ? 2379 LYS   A C    1 
ATOM   6147 O  O    . LYS   A 1 1047 ? 205.414 200.537 134.223 1.00 103.13 ? 2379 LYS   A O    1 
ATOM   6148 C  CB   . LYS   A 1 1047 ? 204.238 203.003 136.325 1.00 109.42 ? 2379 LYS   A CB   1 
ATOM   6149 C  CG   . LYS   A 1 1047 ? 203.035 203.905 136.544 1.00 111.25 ? 2379 LYS   A CG   1 
ATOM   6150 C  CD   . LYS   A 1 1047 ? 202.000 203.753 135.445 1.00 116.64 ? 2379 LYS   A CD   1 
ATOM   6151 C  CE   . LYS   A 1 1047 ? 200.948 204.844 135.536 1.00 116.94 ? 2379 LYS   A CE   1 
ATOM   6152 N  NZ   . LYS   A 1 1047 ? 200.275 204.852 136.865 1.00 111.51 ? 2379 LYS   A NZ   1 
ATOM   6153 N  N    . THR   A 1 1048 ? 206.045 200.631 136.377 1.00 110.07 ? 2380 THR   A N    1 
ATOM   6154 C  CA   . THR   A 1 1048 ? 207.315 199.961 136.146 1.00 109.06 ? 2380 THR   A CA   1 
ATOM   6155 C  C    . THR   A 1 1048 ? 207.137 198.524 135.680 1.00 107.44 ? 2380 THR   A C    1 
ATOM   6156 O  O    . THR   A 1 1048 ? 208.007 198.008 134.969 1.00 105.37 ? 2380 THR   A O    1 
ATOM   6157 C  CB   . THR   A 1 1048 ? 208.158 200.003 137.426 1.00 109.98 ? 2380 THR   A CB   1 
ATOM   6158 O  OG1  . THR   A 1 1048 ? 208.391 201.367 137.796 1.00 114.57 ? 2380 THR   A OG1  1 
ATOM   6159 C  CG2  . THR   A 1 1048 ? 209.503 199.324 137.224 1.00 104.29 ? 2380 THR   A CG2  1 
ATOM   6160 N  N    . GLU   A 1 1049 ? 206.023 197.886 136.034 1.00 104.23 ? 2381 GLU   A N    1 
ATOM   6161 C  CA   . GLU   A 1 1049 ? 205.756 196.493 135.693 1.00 97.48  ? 2381 GLU   A CA   1 
ATOM   6162 C  C    . GLU   A 1 1049 ? 206.891 195.620 136.231 1.00 94.61  ? 2381 GLU   A C    1 
ATOM   6163 O  O    . GLU   A 1 1049 ? 207.678 195.019 135.498 1.00 93.01  ? 2381 GLU   A O    1 
ATOM   6164 C  CB   . GLU   A 1 1049 ? 205.546 196.337 134.179 1.00 101.07 ? 2381 GLU   A CB   1 
ATOM   6165 C  CG   . GLU   A 1 1049 ? 205.422 194.911 133.645 1.00 103.04 ? 2381 GLU   A CG   1 
ATOM   6166 C  CD   . GLU   A 1 1049 ? 205.834 194.795 132.188 1.00 99.60  ? 2381 GLU   A CD   1 
ATOM   6167 O  OE1  . GLU   A 1 1049 ? 205.497 195.701 131.399 1.00 96.42  ? 2381 GLU   A OE1  1 
ATOM   6168 O  OE2  . GLU   A 1 1049 ? 206.493 193.797 131.831 1.00 94.78  ? 2381 GLU   A OE2  1 
ATOM   6169 N  N    . LYS   A 1 1050 ? 206.998 195.618 137.555 1.00 91.15  ? 2382 LYS   A N    1 
ATOM   6170 C  CA   . LYS   A 1 1050 ? 208.092 194.931 138.219 1.00 93.36  ? 2382 LYS   A CA   1 
ATOM   6171 C  C    . LYS   A 1 1050 ? 207.703 194.726 139.674 1.00 87.16  ? 2382 LYS   A C    1 
ATOM   6172 O  O    . LYS   A 1 1050 ? 207.110 195.607 140.300 1.00 85.48  ? 2382 LYS   A O    1 
ATOM   6173 C  CB   . LYS   A 1 1050 ? 209.394 195.732 138.097 1.00 97.18  ? 2382 LYS   A CB   1 
ATOM   6174 C  CG   . LYS   A 1 1050 ? 210.641 195.066 138.649 1.00 97.78  ? 2382 LYS   A CG   1 
ATOM   6175 C  CD   . LYS   A 1 1050 ? 210.825 193.670 138.085 1.00 94.27  ? 2382 LYS   A CD   1 
ATOM   6176 C  CE   . LYS   A 1 1050 ? 211.529 192.760 139.078 1.00 88.62  ? 2382 LYS   A CE   1 
ATOM   6177 N  NZ   . LYS   A 1 1050 ? 210.763 192.554 140.328 1.00 88.78  ? 2382 LYS   A NZ   1 
ATOM   6178 N  N    . LEU   A 1 1051 ? 208.027 193.547 140.194 1.00 87.36  ? 2383 LEU   A N    1 
ATOM   6179 C  CA   . LEU   A 1 1051 ? 207.698 193.207 141.571 1.00 88.79  ? 2383 LEU   A CA   1 
ATOM   6180 C  C    . LEU   A 1 1051 ? 208.446 194.127 142.524 1.00 91.86  ? 2383 LEU   A C    1 
ATOM   6181 O  O    . LEU   A 1 1051 ? 209.680 194.183 142.505 1.00 93.45  ? 2383 LEU   A O    1 
ATOM   6182 C  CB   . LEU   A 1 1051 ? 208.052 191.749 141.848 1.00 94.34  ? 2383 LEU   A CB   1 
ATOM   6183 C  CG   . LEU   A 1 1051 ? 207.541 191.147 143.150 1.00 92.72  ? 2383 LEU   A CG   1 
ATOM   6184 C  CD1  . LEU   A 1 1051 ? 206.124 190.660 142.968 1.00 88.72  ? 2383 LEU   A CD1  1 
ATOM   6185 C  CD2  . LEU   A 1 1051 ? 208.449 190.017 143.592 1.00 95.72  ? 2383 LEU   A CD2  1 
ATOM   6186 N  N    . CYS   A 1 1052 ? 207.703 194.849 143.361 1.00 94.53  ? 2384 CYS   A N    1 
ATOM   6187 C  CA   . CYS   A 1 1052 ? 208.316 195.746 144.327 1.00 96.13  ? 2384 CYS   A CA   1 
ATOM   6188 C  C    . CYS   A 1 1052 ? 207.975 195.404 145.767 1.00 99.27  ? 2384 CYS   A C    1 
ATOM   6189 O  O    . CYS   A 1 1052 ? 208.493 196.059 146.678 1.00 95.17  ? 2384 CYS   A O    1 
ATOM   6190 C  CB   . CYS   A 1 1052 ? 207.916 197.200 144.041 1.00 102.13 ? 2384 CYS   A CB   1 
ATOM   6191 S  SG   . CYS   A 1 1052 ? 206.162 197.550 144.237 1.00 117.91 ? 2384 CYS   A SG   1 
ATOM   6192 N  N    . GLY   A 1 1053 ? 207.137 194.400 146.001 1.00 99.50  ? 2385 GLY   A N    1 
ATOM   6193 C  CA   . GLY   A 1 1053 ? 206.827 193.989 147.355 1.00 98.38  ? 2385 GLY   A CA   1 
ATOM   6194 C  C    . GLY   A 1 1053 ? 206.271 192.586 147.388 1.00 87.82  ? 2385 GLY   A C    1 
ATOM   6195 O  O    . GLY   A 1 1053 ? 205.612 192.137 146.446 1.00 84.53  ? 2385 GLY   A O    1 
ATOM   6196 N  N    . LEU   A 1 1054 ? 206.545 191.889 148.485 1.00 89.08  ? 2386 LEU   A N    1 
ATOM   6197 C  CA   . LEU   A 1 1054 ? 206.001 190.565 148.736 1.00 87.76  ? 2386 LEU   A CA   1 
ATOM   6198 C  C    . LEU   A 1 1054 ? 205.791 190.415 150.233 1.00 90.48  ? 2386 LEU   A C    1 
ATOM   6199 O  O    . LEU   A 1 1054 ? 206.667 190.762 151.030 1.00 88.59  ? 2386 LEU   A O    1 
ATOM   6200 C  CB   . LEU   A 1 1054 ? 206.918 189.454 148.206 1.00 87.35  ? 2386 LEU   A CB   1 
ATOM   6201 C  CG   . LEU   A 1 1054 ? 208.247 189.143 148.901 1.00 100.04 ? 2386 LEU   A CG   1 
ATOM   6202 C  CD1  . LEU   A 1 1054 ? 208.872 187.900 148.297 1.00 104.82 ? 2386 LEU   A CD1  1 
ATOM   6203 C  CD2  . LEU   A 1 1054 ? 209.221 190.308 148.814 1.00 93.20  ? 2386 LEU   A CD2  1 
ATOM   6204 N  N    . ILE   A 1 1055 ? 204.625 189.904 150.610 1.00 82.34  ? 2387 ILE   A N    1 
ATOM   6205 C  CA   . ILE   A 1 1055 ? 204.212 189.816 152.005 1.00 76.58  ? 2387 ILE   A CA   1 
ATOM   6206 C  C    . ILE   A 1 1055 ? 204.253 188.356 152.423 1.00 85.56  ? 2387 ILE   A C    1 
ATOM   6207 O  O    . ILE   A 1 1055 ? 203.422 187.555 151.979 1.00 92.83  ? 2387 ILE   A O    1 
ATOM   6208 C  CB   . ILE   A 1 1055 ? 202.811 190.409 152.215 1.00 70.38  ? 2387 ILE   A CB   1 
ATOM   6209 C  CG1  . ILE   A 1 1055 ? 202.805 191.915 151.946 1.00 73.10  ? 2387 ILE   A CG1  1 
ATOM   6210 C  CG2  . ILE   A 1 1055 ? 202.307 190.109 153.605 1.00 72.12  ? 2387 ILE   A CG2  1 
ATOM   6211 C  CD1  . ILE   A 1 1055 ? 202.479 192.296 150.528 1.00 70.68  ? 2387 ILE   A CD1  1 
ATOM   6212 N  N    . ASP   A 1 1056 ? 205.203 188.010 153.287 1.00 85.67  ? 2388 ASP   A N    1 
ATOM   6213 C  CA   . ASP   A 1 1056 ? 205.289 186.651 153.816 1.00 91.08  ? 2388 ASP   A CA   1 
ATOM   6214 C  C    . ASP   A 1 1056 ? 204.209 186.492 154.871 1.00 86.22  ? 2388 ASP   A C    1 
ATOM   6215 O  O    . ASP   A 1 1056 ? 204.377 186.911 156.017 1.00 94.07  ? 2388 ASP   A O    1 
ATOM   6216 C  CB   . ASP   A 1 1056 ? 206.672 186.366 154.389 1.00 98.22  ? 2388 ASP   A CB   1 
ATOM   6217 C  CG   . ASP   A 1 1056 ? 207.744 186.278 153.322 1.00 106.30 ? 2388 ASP   A CG   1 
ATOM   6218 O  OD1  . ASP   A 1 1056 ? 207.417 185.886 152.183 1.00 104.79 ? 2388 ASP   A OD1  1 
ATOM   6219 O  OD2  . ASP   A 1 1056 ? 208.915 186.594 153.621 1.00 110.56 ? 2388 ASP   A OD2  1 
ATOM   6220 N  N    . CYS   A 1 1057 ? 203.092 185.878 154.482 1.00 72.02  ? 2389 CYS   A N    1 
ATOM   6221 C  CA   . CYS   A 1 1057 ? 201.973 185.726 155.403 1.00 70.57  ? 2389 CYS   A CA   1 
ATOM   6222 C  C    . CYS   A 1 1057 ? 202.357 184.883 156.610 1.00 90.21  ? 2389 CYS   A C    1 
ATOM   6223 O  O    . CYS   A 1 1057 ? 201.965 185.191 157.742 1.00 96.56  ? 2389 CYS   A O    1 
ATOM   6224 C  CB   . CYS   A 1 1057 ? 200.785 185.107 154.681 1.00 65.48  ? 2389 CYS   A CB   1 
ATOM   6225 S  SG   . CYS   A 1 1057 ? 199.348 184.927 155.720 1.00 69.06  ? 2389 CYS   A SG   1 
ATOM   6226 N  N    . VAL   A 1 1058 ? 203.124 183.814 156.394 1.00 90.36  ? 2390 VAL   A N    1 
ATOM   6227 C  CA   . VAL   A 1 1058 ? 203.525 182.978 157.519 1.00 92.28  ? 2390 VAL   A CA   1 
ATOM   6228 C  C    . VAL   A 1 1058 ? 204.421 183.759 158.469 1.00 90.81  ? 2390 VAL   A C    1 
ATOM   6229 O  O    . VAL   A 1 1058 ? 204.423 183.508 159.678 1.00 87.96  ? 2390 VAL   A O    1 
ATOM   6230 C  CB   . VAL   A 1 1058 ? 204.210 181.695 157.022 1.00 92.97  ? 2390 VAL   A CB   1 
ATOM   6231 C  CG1  . VAL   A 1 1058 ? 205.508 182.027 156.327 1.00 99.97  ? 2390 VAL   A CG1  1 
ATOM   6232 C  CG2  . VAL   A 1 1058 ? 204.439 180.740 158.170 1.00 100.30 ? 2390 VAL   A CG2  1 
ATOM   6233 N  N    . HIS   A 1 1059 ? 205.192 184.715 157.949 1.00 93.41  ? 2391 HIS   A N    1 
ATOM   6234 C  CA   . HIS   A 1 1059 ? 206.022 185.538 158.818 1.00 93.96  ? 2391 HIS   A CA   1 
ATOM   6235 C  C    . HIS   A 1 1059 ? 205.175 186.381 159.758 1.00 92.55  ? 2391 HIS   A C    1 
ATOM   6236 O  O    . HIS   A 1 1059 ? 205.535 186.556 160.927 1.00 99.36  ? 2391 HIS   A O    1 
ATOM   6237 C  CB   . HIS   A 1 1059 ? 206.939 186.426 157.983 1.00 97.25  ? 2391 HIS   A CB   1 
ATOM   6238 C  CG   . HIS   A 1 1059 ? 207.872 187.261 158.798 1.00 109.05 ? 2391 HIS   A CG   1 
ATOM   6239 N  ND1  . HIS   A 1 1059 ? 209.171 186.881 159.059 1.00 124.82 ? 2391 HIS   A ND1  1 
ATOM   6240 C  CD2  . HIS   A 1 1059 ? 207.699 188.457 159.407 1.00 111.70 ? 2391 HIS   A CD2  1 
ATOM   6241 C  CE1  . HIS   A 1 1059 ? 209.757 187.806 159.797 1.00 130.31 ? 2391 HIS   A CE1  1 
ATOM   6242 N  NE2  . HIS   A 1 1059 ? 208.886 188.773 160.023 1.00 131.76 ? 2391 HIS   A NE2  1 
ATOM   6243 N  N    . PHE   A 1 1060 ? 204.056 186.913 159.270 1.00 85.65  ? 2392 PHE   A N    1 
ATOM   6244 C  CA   . PHE   A 1 1060 ? 203.127 187.600 160.158 1.00 79.15  ? 2392 PHE   A CA   1 
ATOM   6245 C  C    . PHE   A 1 1060 ? 202.480 186.625 161.127 1.00 76.52  ? 2392 PHE   A C    1 
ATOM   6246 O  O    . PHE   A 1 1060 ? 202.232 186.966 162.288 1.00 83.37  ? 2392 PHE   A O    1 
ATOM   6247 C  CB   . PHE   A 1 1060 ? 202.052 188.324 159.350 1.00 75.33  ? 2392 PHE   A CB   1 
ATOM   6248 C  CG   . PHE   A 1 1060 ? 202.555 189.498 158.565 1.00 75.25  ? 2392 PHE   A CG   1 
ATOM   6249 C  CD1  . PHE   A 1 1060 ? 203.876 189.889 158.632 1.00 82.13  ? 2392 PHE   A CD1  1 
ATOM   6250 C  CD2  . PHE   A 1 1060 ? 201.696 190.215 157.762 1.00 63.84  ? 2392 PHE   A CD2  1 
ATOM   6251 C  CE1  . PHE   A 1 1060 ? 204.323 190.969 157.910 1.00 76.17  ? 2392 PHE   A CE1  1 
ATOM   6252 C  CE2  . PHE   A 1 1060 ? 202.139 191.290 157.044 1.00 66.43  ? 2392 PHE   A CE2  1 
ATOM   6253 C  CZ   . PHE   A 1 1060 ? 203.452 191.670 157.114 1.00 71.39  ? 2392 PHE   A CZ   1 
ATOM   6254 N  N    . LEU   A 1 1061 ? 202.193 185.406 160.670 1.00 75.91  ? 2393 LEU   A N    1 
ATOM   6255 C  CA   . LEU   A 1 1061 ? 201.493 184.453 161.521 1.00 84.86  ? 2393 LEU   A CA   1 
ATOM   6256 C  C    . LEU   A 1 1061 ? 202.381 183.837 162.592 1.00 97.40  ? 2393 LEU   A C    1 
ATOM   6257 O  O    . LEU   A 1 1061 ? 201.859 183.258 163.550 1.00 95.80  ? 2393 LEU   A O    1 
ATOM   6258 C  CB   . LEU   A 1 1061 ? 200.881 183.341 160.681 1.00 86.49  ? 2393 LEU   A CB   1 
ATOM   6259 C  CG   . LEU   A 1 1061 ? 199.406 183.583 160.420 1.00 80.21  ? 2393 LEU   A CG   1 
ATOM   6260 C  CD1  . LEU   A 1 1061 ? 198.798 182.422 159.660 1.00 77.86  ? 2393 LEU   A CD1  1 
ATOM   6261 C  CD2  . LEU   A 1 1061 ? 198.739 183.806 161.748 1.00 75.04  ? 2393 LEU   A CD2  1 
ATOM   6262 N  N    . ARG   A 1 1062 ? 203.703 183.923 162.439 1.00 102.50 ? 2394 ARG   A N    1 
ATOM   6263 C  CA   . ARG   A 1 1062 ? 204.599 183.343 163.435 1.00 104.23 ? 2394 ARG   A CA   1 
ATOM   6264 C  C    . ARG   A 1 1062 ? 204.378 183.937 164.818 1.00 104.66 ? 2394 ARG   A C    1 
ATOM   6265 O  O    . ARG   A 1 1062 ? 204.597 183.257 165.826 1.00 107.25 ? 2394 ARG   A O    1 
ATOM   6266 C  CB   . ARG   A 1 1062 ? 206.056 183.537 163.009 1.00 107.92 ? 2394 ARG   A CB   1 
ATOM   6267 C  CG   . ARG   A 1 1062 ? 206.529 182.592 161.915 1.00 106.60 ? 2394 ARG   A CG   1 
ATOM   6268 C  CD   . ARG   A 1 1062 ? 206.876 181.220 162.477 1.00 106.55 ? 2394 ARG   A CD   1 
ATOM   6269 N  NE   . ARG   A 1 1062 ? 205.706 180.376 162.685 1.00 108.95 ? 2394 ARG   A NE   1 
ATOM   6270 C  CZ   . ARG   A 1 1062 ? 205.755 179.146 163.177 1.00 117.62 ? 2394 ARG   A CZ   1 
ATOM   6271 N  NH1  . ARG   A 1 1062 ? 206.900 178.593 163.540 1.00 126.64 ? 2394 ARG   A NH1  1 
ATOM   6272 N  NH2  . ARG   A 1 1062 ? 204.627 178.455 163.313 1.00 116.93 ? 2394 ARG   A NH2  1 
ATOM   6273 N  N    . GLU   A 1 1063 ? 203.943 185.197 164.890 1.00 104.84 ? 2395 GLU   A N    1 
ATOM   6274 C  CA   . GLU   A 1 1063 ? 203.729 185.829 166.187 1.00 105.70 ? 2395 GLU   A CA   1 
ATOM   6275 C  C    . GLU   A 1 1063 ? 202.643 185.116 166.981 1.00 107.35 ? 2395 GLU   A C    1 
ATOM   6276 O  O    . GLU   A 1 1063 ? 202.806 184.864 168.180 1.00 104.58 ? 2395 GLU   A O    1 
ATOM   6277 C  CB   . GLU   A 1 1063 ? 203.370 187.300 165.999 1.00 102.85 ? 2395 GLU   A CB   1 
ATOM   6278 C  CG   . GLU   A 1 1063 ? 204.491 188.134 165.416 1.00 115.25 ? 2395 GLU   A CG   1 
ATOM   6279 C  CD   . GLU   A 1 1063 ? 205.675 188.255 166.352 1.00 131.39 ? 2395 GLU   A CD   1 
ATOM   6280 O  OE1  . GLU   A 1 1063 ? 205.470 188.248 167.583 1.00 128.68 ? 2395 GLU   A OE1  1 
ATOM   6281 O  OE2  . GLU   A 1 1063 ? 206.814 188.363 165.854 1.00 139.43 ? 2395 GLU   A OE2  1 
ATOM   6282 N  N    . VAL   A 1 1064 ? 201.533 184.780 166.334 1.00 107.67 ? 2396 VAL   A N    1 
ATOM   6283 C  CA   . VAL   A 1 1064 ? 200.423 184.126 167.015 1.00 110.97 ? 2396 VAL   A CA   1 
ATOM   6284 C  C    . VAL   A 1 1064 ? 199.992 182.873 166.263 1.00 114.03 ? 2396 VAL   A C    1 
ATOM   6285 O  O    . VAL   A 1 1064 ? 200.642 181.831 166.348 1.00 101.91 ? 2396 VAL   A O    1 
ATOM   6286 C  CB   . VAL   A 1 1064 ? 199.239 185.090 167.187 1.00 105.09 ? 2396 VAL   A CB   1 
ATOM   6287 C  CG1  . VAL   A 1 1064 ? 199.638 186.272 168.049 1.00 103.01 ? 2396 VAL   A CG1  1 
ATOM   6288 C  CG2  . VAL   A 1 1064 ? 198.757 185.569 165.837 1.00 94.36  ? 2396 VAL   A CG2  1 
ATOM   6289 N  N    . TYR   A 1 1078 ? 195.832 176.567 161.190 1.00 107.51 ? 2410 TYR   A N    1 
ATOM   6290 C  CA   . TYR   A 1 1078 ? 197.109 177.257 161.104 1.00 109.55 ? 2410 TYR   A CA   1 
ATOM   6291 C  C    . TYR   A 1 1078 ? 197.812 176.895 159.802 1.00 109.44 ? 2410 TYR   A C    1 
ATOM   6292 O  O    . TYR   A 1 1078 ? 198.624 175.974 159.769 1.00 111.31 ? 2410 TYR   A O    1 
ATOM   6293 C  CB   . TYR   A 1 1078 ? 197.998 176.895 162.293 1.00 106.99 ? 2410 TYR   A CB   1 
ATOM   6294 C  CG   . TYR   A 1 1078 ? 199.318 177.621 162.292 1.00 112.79 ? 2410 TYR   A CG   1 
ATOM   6295 C  CD1  . TYR   A 1 1078 ? 199.391 178.951 162.664 1.00 115.19 ? 2410 TYR   A CD1  1 
ATOM   6296 C  CD2  . TYR   A 1 1078 ? 200.487 176.987 161.900 1.00 111.89 ? 2410 TYR   A CD2  1 
ATOM   6297 C  CE1  . TYR   A 1 1078 ? 200.588 179.626 162.661 1.00 119.92 ? 2410 TYR   A CE1  1 
ATOM   6298 C  CE2  . TYR   A 1 1078 ? 201.691 177.656 161.890 1.00 114.94 ? 2410 TYR   A CE2  1 
ATOM   6299 C  CZ   . TYR   A 1 1078 ? 201.735 178.976 162.271 1.00 124.09 ? 2410 TYR   A CZ   1 
ATOM   6300 O  OH   . TYR   A 1 1078 ? 202.932 179.652 162.266 1.00 124.32 ? 2410 TYR   A OH   1 
ATOM   6301 N  N    . SER   A 1 1079 ? 197.488 177.606 158.721 1.00 97.89  ? 2411 SER   A N    1 
ATOM   6302 C  CA   . SER   A 1 1079 ? 198.059 177.311 157.412 1.00 89.26  ? 2411 SER   A CA   1 
ATOM   6303 C  C    . SER   A 1 1079 ? 199.020 178.395 156.940 1.00 89.65  ? 2411 SER   A C    1 
ATOM   6304 O  O    . SER   A 1 1079 ? 200.214 178.143 156.768 1.00 99.06  ? 2411 SER   A O    1 
ATOM   6305 C  CB   . SER   A 1 1079 ? 196.933 177.118 156.393 1.00 78.17  ? 2411 SER   A CB   1 
ATOM   6306 O  OG   . SER   A 1 1079 ? 196.155 175.993 156.738 1.00 80.88  ? 2411 SER   A OG   1 
ATOM   6307 N  N    . GLY   A 1 1080 ? 198.521 179.604 156.738 1.00 78.54  ? 2412 GLY   A N    1 
ATOM   6308 C  CA   . GLY   A 1 1080 ? 199.314 180.689 156.223 1.00 74.99  ? 2412 GLY   A CA   1 
ATOM   6309 C  C    . GLY   A 1 1080 ? 199.188 180.908 154.729 1.00 76.23  ? 2412 GLY   A C    1 
ATOM   6310 O  O    . GLY   A 1 1080 ? 199.488 182.008 154.255 1.00 81.61  ? 2412 GLY   A O    1 
ATOM   6311 N  N    . ARG   A 1 1081 ? 198.759 179.902 153.974 1.00 72.66  ? 2413 ARG   A N    1 
ATOM   6312 C  CA   . ARG   A 1 1081 ? 198.491 180.108 152.561 1.00 67.80  ? 2413 ARG   A CA   1 
ATOM   6313 C  C    . ARG   A 1 1081 ? 197.244 180.953 152.396 1.00 68.70  ? 2413 ARG   A C    1 
ATOM   6314 O  O    . ARG   A 1 1081 ? 196.206 180.662 152.997 1.00 65.05  ? 2413 ARG   A O    1 
ATOM   6315 C  CB   . ARG   A 1 1081 ? 198.277 178.795 151.833 1.00 74.72  ? 2413 ARG   A CB   1 
ATOM   6316 C  CG   . ARG   A 1 1081 ? 199.486 177.992 151.541 1.00 89.44  ? 2413 ARG   A CG   1 
ATOM   6317 C  CD   . ARG   A 1 1081 ? 199.022 176.571 151.496 1.00 103.94 ? 2413 ARG   A CD   1 
ATOM   6318 N  NE   . ARG   A 1 1081 ? 200.079 175.594 151.669 1.00 105.05 ? 2413 ARG   A NE   1 
ATOM   6319 C  CZ   . ARG   A 1 1081 ? 200.779 175.101 150.658 1.00 101.40 ? 2413 ARG   A CZ   1 
ATOM   6320 N  NH1  . ARG   A 1 1081 ? 200.718 175.635 149.450 1.00 95.21  ? 2413 ARG   A NH1  1 
ATOM   6321 N  NH2  . ARG   A 1 1081 ? 201.548 174.041 150.860 1.00 98.93  ? 2413 ARG   A NH2  1 
ATOM   6322 N  N    . VAL   A 1 1082 ? 197.335 181.983 151.559 1.00 63.39  ? 2414 VAL   A N    1 
ATOM   6323 C  CA   . VAL   A 1 1082 ? 196.193 182.854 151.338 1.00 40.16  ? 2414 VAL   A CA   1 
ATOM   6324 C  C    . VAL   A 1 1082 ? 195.143 182.127 150.519 1.00 32.86  ? 2414 VAL   A C    1 
ATOM   6325 O  O    . VAL   A 1 1082 ? 195.460 181.402 149.570 1.00 43.67  ? 2414 VAL   A O    1 
ATOM   6326 C  CB   . VAL   A 1 1082 ? 196.640 184.155 150.657 1.00 33.22  ? 2414 VAL   A CB   1 
ATOM   6327 C  CG1  . VAL   A 1 1082 ? 197.188 183.869 149.294 1.00 42.45  ? 2414 VAL   A CG1  1 
ATOM   6328 C  CG2  . VAL   A 1 1082 ? 195.470 185.082 150.534 1.00 33.85  ? 2414 VAL   A CG2  1 
ATOM   6329 N  N    . LYS   A 1 1083 ? 193.884 182.289 150.897 1.00 29.82  ? 2415 LYS   A N    1 
ATOM   6330 C  CA   . LYS   A 1 1083 ? 192.809 181.751 150.083 1.00 41.65  ? 2415 LYS   A CA   1 
ATOM   6331 C  C    . LYS   A 1 1083 ? 191.822 182.798 149.613 1.00 47.45  ? 2415 LYS   A C    1 
ATOM   6332 O  O    . LYS   A 1 1083 ? 191.190 182.602 148.574 1.00 54.92  ? 2415 LYS   A O    1 
ATOM   6333 C  CB   . LYS   A 1 1083 ? 192.051 180.648 150.827 1.00 40.23  ? 2415 LYS   A CB   1 
ATOM   6334 C  CG   . LYS   A 1 1083 ? 192.572 179.267 150.476 1.00 49.50  ? 2415 LYS   A CG   1 
ATOM   6335 C  CD   . LYS   A 1 1083 ? 191.788 178.149 151.129 1.00 60.48  ? 2415 LYS   A CD   1 
ATOM   6336 C  CE   . LYS   A 1 1083 ? 190.301 178.418 151.078 1.00 67.70  ? 2415 LYS   A CE   1 
ATOM   6337 N  NZ   . LYS   A 1 1083 ? 189.500 177.190 151.329 1.00 72.97  ? 2415 LYS   A NZ   1 
ATOM   6338 N  N    . THR   A 1 1084 ? 191.670 183.904 150.335 1.00 35.20  ? 2416 THR   A N    1 
ATOM   6339 C  CA   . THR   A 1 1084 ? 190.930 185.035 149.798 1.00 29.43  ? 2416 THR   A CA   1 
ATOM   6340 C  C    . THR   A 1 1084 ? 191.620 186.314 150.234 1.00 29.78  ? 2416 THR   A C    1 
ATOM   6341 O  O    . THR   A 1 1084 ? 192.459 186.311 151.131 1.00 42.03  ? 2416 THR   A O    1 
ATOM   6342 C  CB   . THR   A 1 1084 ? 189.470 185.028 150.236 1.00 29.47  ? 2416 THR   A CB   1 
ATOM   6343 O  OG1  . THR   A 1 1084 ? 188.773 186.074 149.557 1.00 43.78  ? 2416 THR   A OG1  1 
ATOM   6344 C  CG2  . THR   A 1 1084 ? 189.366 185.243 151.713 1.00 29.77  ? 2416 THR   A CG2  1 
ATOM   6345 N  N    . LEU   A 1 1085 ? 191.264 187.415 149.588 1.00 24.65  ? 2417 LEU   A N    1 
ATOM   6346 C  CA   . LEU   A 1 1085 ? 192.022 188.646 149.765 1.00 22.39  ? 2417 LEU   A CA   1 
ATOM   6347 C  C    . LEU   A 1 1085 ? 191.160 189.805 149.303 1.00 32.95  ? 2417 LEU   A C    1 
ATOM   6348 O  O    . LEU   A 1 1085 ? 190.809 189.868 148.124 1.00 37.05  ? 2417 LEU   A O    1 
ATOM   6349 C  CB   . LEU   A 1 1085 ? 193.309 188.557 148.968 1.00 15.74  ? 2417 LEU   A CB   1 
ATOM   6350 C  CG   . LEU   A 1 1085 ? 194.386 189.614 149.079 1.00 20.62  ? 2417 LEU   A CG   1 
ATOM   6351 C  CD1  . LEU   A 1 1085 ? 195.729 189.014 148.755 1.00 29.94  ? 2417 LEU   A CD1  1 
ATOM   6352 C  CD2  . LEU   A 1 1085 ? 194.076 190.659 148.091 1.00 23.44  ? 2417 LEU   A CD2  1 
ATOM   6353 N  N    . CYS   A 1 1086 ? 190.822 190.721 150.209 1.00 32.45  ? 2418 CYS   A N    1 
ATOM   6354 C  CA   . CYS   A 1 1086 ? 189.880 191.781 149.867 1.00 30.70  ? 2418 CYS   A CA   1 
ATOM   6355 C  C    . CYS   A 1 1086 ? 190.352 193.113 150.418 1.00 39.07  ? 2418 CYS   A C    1 
ATOM   6356 O  O    . CYS   A 1 1086 ? 190.725 193.201 151.586 1.00 41.97  ? 2418 CYS   A O    1 
ATOM   6357 C  CB   . CYS   A 1 1086 ? 188.490 191.475 150.407 1.00 25.50  ? 2418 CYS   A CB   1 
ATOM   6358 S  SG   . CYS   A 1 1086 ? 187.298 192.717 149.940 1.00 55.33  ? 2418 CYS   A SG   1 
ATOM   6359 N  N    . LEU   A 1 1087 ? 190.303 194.153 149.594 1.00 46.50  ? 2419 LEU   A N    1 
ATOM   6360 C  CA   . LEU   A 1 1087 ? 190.857 195.457 149.929 1.00 43.93  ? 2419 LEU   A CA   1 
ATOM   6361 C  C    . LEU   A 1 1087 ? 189.738 196.469 150.099 1.00 45.56  ? 2419 LEU   A C    1 
ATOM   6362 O  O    . LEU   A 1 1087 ? 188.830 196.544 149.267 1.00 46.23  ? 2419 LEU   A O    1 
ATOM   6363 C  CB   . LEU   A 1 1087 ? 191.820 195.925 148.837 1.00 47.34  ? 2419 LEU   A CB   1 
ATOM   6364 C  CG   . LEU   A 1 1087 ? 192.539 197.258 148.999 1.00 51.95  ? 2419 LEU   A CG   1 
ATOM   6365 C  CD1  . LEU   A 1 1087 ? 193.997 197.085 148.667 1.00 58.62  ? 2419 LEU   A CD1  1 
ATOM   6366 C  CD2  . LEU   A 1 1087 ? 191.922 198.296 148.093 1.00 54.18  ? 2419 LEU   A CD2  1 
ATOM   6367 N  N    . GLN   A 1 1088 ? 189.806 197.256 151.171 1.00 52.80  ? 2420 GLN   A N    1 
ATOM   6368 C  CA   . GLN   A 1 1088 ? 188.759 198.222 151.486 1.00 60.54  ? 2420 GLN   A CA   1 
ATOM   6369 C  C    . GLN   A 1 1088 ? 189.357 199.617 151.584 1.00 69.65  ? 2420 GLN   A C    1 
ATOM   6370 O  O    . GLN   A 1 1088 ? 190.314 199.836 152.334 1.00 70.70  ? 2420 GLN   A O    1 
ATOM   6371 C  CB   . GLN   A 1 1088 ? 188.027 197.845 152.778 1.00 59.74  ? 2420 GLN   A CB   1 
ATOM   6372 C  CG   . GLN   A 1 1088 ? 188.880 197.835 154.032 1.00 66.36  ? 2420 GLN   A CG   1 
ATOM   6373 C  CD   . GLN   A 1 1088 ? 188.642 199.045 154.906 1.00 78.69  ? 2420 GLN   A CD   1 
ATOM   6374 O  OE1  . GLN   A 1 1088 ? 187.713 199.816 154.678 1.00 87.55  ? 2420 GLN   A OE1  1 
ATOM   6375 N  NE2  . GLN   A 1 1088 ? 189.476 199.213 155.923 1.00 75.57  ? 2420 GLN   A NE2  1 
ATOM   6376 N  N    . LYS   A 1 1089 ? 188.793 200.551 150.814 1.00 68.70  ? 2421 LYS   A N    1 
ATOM   6377 C  CA   . LYS   A 1 1089 ? 189.170 201.969 150.811 1.00 75.76  ? 2421 LYS   A CA   1 
ATOM   6378 C  C    . LYS   A 1 1089 ? 190.688 202.041 150.641 1.00 72.95  ? 2421 LYS   A C    1 
ATOM   6379 O  O    . LYS   A 1 1089 ? 191.222 201.428 149.707 1.00 63.12  ? 2421 LYS   A O    1 
ATOM   6380 C  CB   . LYS   A 1 1089 ? 188.600 202.624 152.065 1.00 79.78  ? 2421 LYS   A CB   1 
ATOM   6381 C  CG   . LYS   A 1 1089 ? 188.796 204.133 152.171 1.00 87.36  ? 2421 LYS   A CG   1 
ATOM   6382 C  CD   . LYS   A 1 1089 ? 187.613 204.887 151.596 1.00 82.18  ? 2421 LYS   A CD   1 
ATOM   6383 C  CE   . LYS   A 1 1089 ? 187.927 206.365 151.457 1.00 83.47  ? 2421 LYS   A CE   1 
ATOM   6384 N  NZ   . LYS   A 1 1089 ? 189.043 206.602 150.504 1.00 86.61  ? 2421 LYS   A NZ   1 
ATOM   6385 N  N    . ASN   A 1 1090 ? 191.412 202.763 151.494 1.00 78.76  ? 2422 ASN   A N    1 
ATOM   6386 C  CA   . ASN   A 1 1090 ? 192.868 202.782 151.478 1.00 78.42  ? 2422 ASN   A CA   1 
ATOM   6387 C  C    . ASN   A 1 1090 ? 193.432 202.614 152.883 1.00 82.32  ? 2422 ASN   A C    1 
ATOM   6388 O  O    . ASN   A 1 1090 ? 194.574 203.005 153.142 1.00 84.54  ? 2422 ASN   A O    1 
ATOM   6389 C  CB   . ASN   A 1 1090 ? 193.394 204.066 150.829 1.00 85.05  ? 2422 ASN   A CB   1 
ATOM   6390 C  CG   . ASN   A 1 1090 ? 192.854 205.325 151.484 1.00 86.76  ? 2422 ASN   A CG   1 
ATOM   6391 O  OD1  . ASN   A 1 1090 ? 192.638 205.375 152.693 1.00 80.66  ? 2422 ASN   A OD1  1 
ATOM   6392 N  ND2  . ASN   A 1 1090 ? 192.630 206.354 150.676 1.00 86.31  ? 2422 ASN   A ND2  1 
ATOM   6393 N  N    . THR   A 1 1091 ? 192.646 202.043 153.792 1.00 77.29  ? 2423 THR   A N    1 
ATOM   6394 C  CA   . THR   A 1 1091 ? 193.059 201.845 155.173 1.00 75.65  ? 2423 THR   A CA   1 
ATOM   6395 C  C    . THR   A 1 1091 ? 193.735 200.493 155.372 1.00 75.65  ? 2423 THR   A C    1 
ATOM   6396 O  O    . THR   A 1 1091 ? 194.784 200.413 156.017 1.00 78.47  ? 2423 THR   A O    1 
ATOM   6397 C  CB   . THR   A 1 1091 ? 191.851 201.967 156.103 1.00 71.81  ? 2423 THR   A CB   1 
ATOM   6398 O  OG1  . THR   A 1 1091 ? 190.898 200.950 155.782 1.00 73.26  ? 2423 THR   A OG1  1 
ATOM   6399 C  CG2  . THR   A 1 1091 ? 191.187 203.319 155.923 1.00 72.54  ? 2423 THR   A CG2  1 
ATOM   6400 N  N    . ALA   A 1 1092 ? 193.158 199.429 154.818 1.00 74.67  ? 2424 ALA   A N    1 
ATOM   6401 C  CA   . ALA   A 1 1092 ? 193.658 198.086 155.069 1.00 68.58  ? 2424 ALA   A CA   1 
ATOM   6402 C  C    . ALA   A 1 1092 ? 193.233 197.155 153.944 1.00 58.54  ? 2424 ALA   A C    1 
ATOM   6403 O  O    . ALA   A 1 1092 ? 192.238 197.394 153.258 1.00 54.49  ? 2424 ALA   A O    1 
ATOM   6404 C  CB   . ALA   A 1 1092 ? 193.148 197.559 156.413 1.00 63.04  ? 2424 ALA   A CB   1 
ATOM   6405 N  N    . LEU   A 1 1093 ? 194.002 196.083 153.773 1.00 60.09  ? 2425 LEU   A N    1 
ATOM   6406 C  CA   . LEU   A 1 1093 ? 193.576 194.934 152.985 1.00 55.81  ? 2425 LEU   A CA   1 
ATOM   6407 C  C    . LEU   A 1 1093 ? 193.528 193.728 153.902 1.00 44.24  ? 2425 LEU   A C    1 
ATOM   6408 O  O    . LEU   A 1 1093 ? 194.433 193.523 154.718 1.00 49.10  ? 2425 LEU   A O    1 
ATOM   6409 C  CB   . LEU   A 1 1093 ? 194.505 194.626 151.797 1.00 55.94  ? 2425 LEU   A CB   1 
ATOM   6410 C  CG   . LEU   A 1 1093 ? 195.888 193.999 151.994 1.00 49.44  ? 2425 LEU   A CG   1 
ATOM   6411 C  CD1  . LEU   A 1 1093 ? 196.404 193.469 150.674 1.00 47.66  ? 2425 LEU   A CD1  1 
ATOM   6412 C  CD2  . LEU   A 1 1093 ? 196.873 194.983 152.568 1.00 62.12  ? 2425 LEU   A CD2  1 
ATOM   6413 N  N    . TRP   A 1 1094 ? 192.475 192.931 153.779 1.00 34.08  ? 2426 TRP   A N    1 
ATOM   6414 C  CA   . TRP   A 1 1094 ? 192.269 191.818 154.676 1.00 29.78  ? 2426 TRP   A CA   1 
ATOM   6415 C  C    . TRP   A 1 1094 ? 192.690 190.578 153.906 1.00 30.09  ? 2426 TRP   A C    1 
ATOM   6416 O  O    . TRP   A 1 1094 ? 192.345 190.437 152.730 1.00 39.39  ? 2426 TRP   A O    1 
ATOM   6417 C  CB   . TRP   A 1 1094 ? 190.805 191.664 155.088 1.00 28.37  ? 2426 TRP   A CB   1 
ATOM   6418 C  CG   . TRP   A 1 1094 ? 190.242 192.815 155.860 1.00 35.62  ? 2426 TRP   A CG   1 
ATOM   6419 C  CD1  . TRP   A 1 1094 ? 190.900 193.924 156.261 1.00 45.76  ? 2426 TRP   A CD1  1 
ATOM   6420 C  CD2  . TRP   A 1 1094 ? 188.972 192.854 156.526 1.00 51.20  ? 2426 TRP   A CD2  1 
ATOM   6421 N  NE1  . TRP   A 1 1094 ? 190.073 194.731 156.998 1.00 59.05  ? 2426 TRP   A NE1  1 
ATOM   6422 C  CE2  . TRP   A 1 1094 ? 188.890 194.078 157.199 1.00 58.76  ? 2426 TRP   A CE2  1 
ATOM   6423 C  CE3  . TRP   A 1 1094 ? 187.884 191.984 156.588 1.00 48.14  ? 2426 TRP   A CE3  1 
ATOM   6424 C  CZ2  . TRP   A 1 1094 ? 187.764 194.461 157.914 1.00 48.99  ? 2426 TRP   A CZ2  1 
ATOM   6425 C  CZ3  . TRP   A 1 1094 ? 186.765 192.373 157.287 1.00 42.64  ? 2426 TRP   A CZ3  1 
ATOM   6426 C  CH2  . TRP   A 1 1094 ? 186.717 193.592 157.948 1.00 43.36  ? 2426 TRP   A CH2  1 
ATOM   6427 N  N    . ILE   A 1 1095 ? 193.421 189.677 154.547 1.00 24.00  ? 2427 ILE   A N    1 
ATOM   6428 C  CA   . ILE   A 1 1095 ? 193.945 188.484 153.907 1.00 18.93  ? 2427 ILE   A CA   1 
ATOM   6429 C  C    . ILE   A 1 1095 ? 193.331 187.287 154.606 1.00 22.19  ? 2427 ILE   A C    1 
ATOM   6430 O  O    . ILE   A 1 1095 ? 193.767 186.919 155.701 1.00 39.66  ? 2427 ILE   A O    1 
ATOM   6431 C  CB   . ILE   A 1 1095 ? 195.473 188.428 153.981 1.00 17.04  ? 2427 ILE   A CB   1 
ATOM   6432 C  CG1  . ILE   A 1 1095 ? 196.080 189.681 153.369 1.00 18.39  ? 2427 ILE   A CG1  1 
ATOM   6433 C  CG2  . ILE   A 1 1095 ? 195.996 187.187 153.336 1.00 17.36  ? 2427 ILE   A CG2  1 
ATOM   6434 C  CD1  . ILE   A 1 1095 ? 197.579 189.678 153.378 1.00 22.57  ? 2427 ILE   A CD1  1 
ATOM   6435 N  N    . GLY   A 1 1096 ? 192.331 186.678 153.985 1.00 18.65  ? 2428 GLY   A N    1 
ATOM   6436 C  CA   . GLY   A 1 1096 ? 191.694 185.504 154.536 1.00 21.76  ? 2428 GLY   A CA   1 
ATOM   6437 C  C    . GLY   A 1 1096 ? 192.525 184.272 154.265 1.00 29.38  ? 2428 GLY   A C    1 
ATOM   6438 O  O    . GLY   A 1 1096 ? 192.312 183.595 153.253 1.00 47.11  ? 2428 GLY   A O    1 
ATOM   6439 N  N    . THR   A 1 1097 ? 193.536 184.043 155.102 1.00 31.85  ? 2429 THR   A N    1 
ATOM   6440 C  CA   . THR   A 1 1097 ? 194.446 182.920 154.946 1.00 36.82  ? 2429 THR   A CA   1 
ATOM   6441 C  C    . THR   A 1 1097 ? 193.731 181.596 155.163 1.00 41.98  ? 2429 THR   A C    1 
ATOM   6442 O  O    . THR   A 1 1097 ? 192.770 181.503 155.926 1.00 42.57  ? 2429 THR   A O    1 
ATOM   6443 C  CB   . THR   A 1 1097 ? 195.582 183.037 155.943 1.00 41.58  ? 2429 THR   A CB   1 
ATOM   6444 O  OG1  . THR   A 1 1097 ? 195.121 182.585 157.217 1.00 51.65  ? 2429 THR   A OG1  1 
ATOM   6445 C  CG2  . THR   A 1 1097 ? 195.992 184.475 156.064 1.00 41.77  ? 2429 THR   A CG2  1 
ATOM   6446 N  N    . GLY   A 1 1098 ? 194.246 180.551 154.514 1.00 50.14  ? 2430 GLY   A N    1 
ATOM   6447 C  CA   . GLY   A 1 1098 ? 193.560 179.270 154.485 1.00 53.31  ? 2430 GLY   A CA   1 
ATOM   6448 C  C    . GLY   A 1 1098 ? 193.374 178.625 155.841 1.00 61.28  ? 2430 GLY   A C    1 
ATOM   6449 O  O    . GLY   A 1 1098 ? 192.530 177.737 155.983 1.00 61.84  ? 2430 GLY   A O    1 
ATOM   6450 N  N    . GLY   A 1 1099 ? 194.133 179.053 156.840 1.00 67.71  ? 2431 GLY   A N    1 
ATOM   6451 C  CA   . GLY   A 1 1099 ? 194.046 178.483 158.165 1.00 70.70  ? 2431 GLY   A CA   1 
ATOM   6452 C  C    . GLY   A 1 1099 ? 192.946 179.029 159.037 1.00 65.14  ? 2431 GLY   A C    1 
ATOM   6453 O  O    . GLY   A 1 1099 ? 192.871 178.672 160.214 1.00 68.61  ? 2431 GLY   A O    1 
ATOM   6454 N  N    . GLY   A 1 1100 ? 192.088 179.887 158.501 1.00 65.11  ? 2432 GLY   A N    1 
ATOM   6455 C  CA   . GLY   A 1 1100 ? 191.032 180.504 159.272 1.00 69.92  ? 2432 GLY   A CA   1 
ATOM   6456 C  C    . GLY   A 1 1100 ? 191.351 181.871 159.826 1.00 54.33  ? 2432 GLY   A C    1 
ATOM   6457 O  O    . GLY   A 1 1100 ? 190.531 182.424 160.564 1.00 48.89  ? 2432 GLY   A O    1 
ATOM   6458 N  N    . HIS   A 1 1101 ? 192.500 182.440 159.481 1.00 46.68  ? 2433 HIS   A N    1 
ATOM   6459 C  CA   . HIS   A 1 1101 ? 192.948 183.709 160.033 1.00 40.70  ? 2433 HIS   A CA   1 
ATOM   6460 C  C    . HIS   A 1 1101 ? 192.743 184.810 159.010 1.00 33.81  ? 2433 HIS   A C    1 
ATOM   6461 O  O    . HIS   A 1 1101 ? 193.310 184.751 157.918 1.00 50.10  ? 2433 HIS   A O    1 
ATOM   6462 C  CB   . HIS   A 1 1101 ? 194.429 183.667 160.400 1.00 52.54  ? 2433 HIS   A CB   1 
ATOM   6463 C  CG   . HIS   A 1 1101 ? 194.841 182.456 161.171 1.00 65.83  ? 2433 HIS   A CG   1 
ATOM   6464 N  ND1  . HIS   A 1 1101 ? 196.149 182.225 161.529 1.00 73.74  ? 2433 HIS   A ND1  1 
ATOM   6465 C  CD2  . HIS   A 1 1101 ? 194.135 181.399 161.628 1.00 72.31  ? 2433 HIS   A CD2  1 
ATOM   6466 C  CE1  . HIS   A 1 1101 ? 196.230 181.088 162.193 1.00 81.87  ? 2433 HIS   A CE1  1 
ATOM   6467 N  NE2  . HIS   A 1 1101 ? 195.020 180.566 162.267 1.00 81.99  ? 2433 HIS   A NE2  1 
ATOM   6468 N  N    . ILE   A 1 1102 ? 191.968 185.823 159.366 1.00 22.70  ? 2434 ILE   A N    1 
ATOM   6469 C  CA   . ILE   A 1 1102 ? 191.853 187.021 158.544 1.00 22.13  ? 2434 ILE   A CA   1 
ATOM   6470 C  C    . ILE   A 1 1102 ? 192.951 187.977 158.980 1.00 26.46  ? 2434 ILE   A C    1 
ATOM   6471 O  O    . ILE   A 1 1102 ? 192.720 188.952 159.681 1.00 41.01  ? 2434 ILE   A O    1 
ATOM   6472 C  CB   . ILE   A 1 1102 ? 190.469 187.639 158.624 1.00 23.55  ? 2434 ILE   A CB   1 
ATOM   6473 C  CG1  . ILE   A 1 1102 ? 189.436 186.535 158.506 1.00 26.09  ? 2434 ILE   A CG1  1 
ATOM   6474 C  CG2  . ILE   A 1 1102 ? 190.300 188.701 157.589 1.00 36.18  ? 2434 ILE   A CG2  1 
ATOM   6475 C  CD1  . ILE   A 1 1102 ? 188.089 186.941 158.906 1.00 31.18  ? 2434 ILE   A CD1  1 
ATOM   6476 N  N    . LEU   A 1 1103 ? 194.154 187.716 158.496 1.00 23.57  ? 2435 LEU   A N    1 
ATOM   6477 C  CA   . LEU   A 1 1103 ? 195.317 188.516 158.839 1.00 29.98  ? 2435 LEU   A CA   1 
ATOM   6478 C  C    . LEU   A 1 1103 ? 195.264 189.788 158.005 1.00 28.04  ? 2435 LEU   A C    1 
ATOM   6479 O  O    . LEU   A 1 1103 ? 195.273 189.724 156.776 1.00 36.80  ? 2435 LEU   A O    1 
ATOM   6480 C  CB   . LEU   A 1 1103 ? 196.564 187.679 158.578 1.00 31.62  ? 2435 LEU   A CB   1 
ATOM   6481 C  CG   . LEU   A 1 1103 ? 197.999 188.110 158.828 1.00 43.13  ? 2435 LEU   A CG   1 
ATOM   6482 C  CD1  . LEU   A 1 1103 ? 198.860 186.869 158.854 1.00 60.24  ? 2435 LEU   A CD1  1 
ATOM   6483 C  CD2  . LEU   A 1 1103 ? 198.466 188.983 157.726 1.00 36.52  ? 2435 LEU   A CD2  1 
ATOM   6484 N  N    . LEU   A 1 1104 ? 195.168 190.950 158.644 1.00 27.07  ? 2436 LEU   A N    1 
ATOM   6485 C  CA   . LEU   A 1 1104 ? 194.823 192.169 157.923 1.00 35.66  ? 2436 LEU   A CA   1 
ATOM   6486 C  C    . LEU   A 1 1104 ? 195.897 193.232 158.108 1.00 42.09  ? 2436 LEU   A C    1 
ATOM   6487 O  O    . LEU   A 1 1104 ? 196.448 193.390 159.203 1.00 50.32  ? 2436 LEU   A O    1 
ATOM   6488 C  CB   . LEU   A 1 1104 ? 193.436 192.667 158.347 1.00 36.30  ? 2436 LEU   A CB   1 
ATOM   6489 C  CG   . LEU   A 1 1104 ? 193.035 193.100 159.749 1.00 28.63  ? 2436 LEU   A CG   1 
ATOM   6490 C  CD1  . LEU   A 1 1104 ? 193.414 194.532 159.963 1.00 39.90  ? 2436 LEU   A CD1  1 
ATOM   6491 C  CD2  . LEU   A 1 1104 ? 191.556 192.907 159.948 1.00 28.08  ? 2436 LEU   A CD2  1 
ATOM   6492 N  N    . LEU   A 1 1105 ? 196.208 193.943 157.026 1.00 43.18  ? 2437 LEU   A N    1 
ATOM   6493 C  CA   . LEU   A 1 1105 ? 197.337 194.862 156.986 1.00 56.85  ? 2437 LEU   A CA   1 
ATOM   6494 C  C    . LEU   A 1 1105 ? 196.873 196.273 156.681 1.00 62.96  ? 2437 LEU   A C    1 
ATOM   6495 O  O    . LEU   A 1 1105 ? 195.943 196.468 155.895 1.00 58.71  ? 2437 LEU   A O    1 
ATOM   6496 C  CB   . LEU   A 1 1105 ? 198.361 194.467 155.924 1.00 55.70  ? 2437 LEU   A CB   1 
ATOM   6497 C  CG   . LEU   A 1 1105 ? 199.378 193.360 156.143 1.00 60.77  ? 2437 LEU   A CG   1 
ATOM   6498 C  CD1  . LEU   A 1 1105 ? 198.684 192.121 156.561 1.00 54.36  ? 2437 LEU   A CD1  1 
ATOM   6499 C  CD2  . LEU   A 1 1105 ? 200.158 193.125 154.870 1.00 73.20  ? 2437 LEU   A CD2  1 
ATOM   6500 N  N    . ASP   A 1 1106 ? 197.546 197.251 157.281 1.00 70.87  ? 2438 ASP   A N    1 
ATOM   6501 C  CA   . ASP   A 1 1106 ? 197.454 198.637 156.842 1.00 68.28  ? 2438 ASP   A CA   1 
ATOM   6502 C  C    . ASP   A 1 1106 ? 198.362 198.797 155.633 1.00 72.67  ? 2438 ASP   A C    1 
ATOM   6503 O  O    . ASP   A 1 1106 ? 199.588 198.835 155.769 1.00 79.24  ? 2438 ASP   A O    1 
ATOM   6504 C  CB   . ASP   A 1 1106 ? 197.859 199.594 157.958 1.00 66.77  ? 2438 ASP   A CB   1 
ATOM   6505 N  N    . LEU   A 1 1107 ? 197.764 198.881 154.449 1.00 71.89  ? 2439 LEU   A N    1 
ATOM   6506 C  CA   . LEU   A 1 1107 ? 198.540 198.895 153.217 1.00 81.08  ? 2439 LEU   A CA   1 
ATOM   6507 C  C    . LEU   A 1 1107 ? 199.360 200.164 153.043 1.00 90.98  ? 2439 LEU   A C    1 
ATOM   6508 O  O    . LEU   A 1 1107 ? 200.223 200.201 152.161 1.00 89.79  ? 2439 LEU   A O    1 
ATOM   6509 C  CB   . LEU   A 1 1107 ? 197.616 198.705 152.013 1.00 71.01  ? 2439 LEU   A CB   1 
ATOM   6510 C  CG   . LEU   A 1 1107 ? 196.699 199.854 151.588 1.00 79.96  ? 2439 LEU   A CG   1 
ATOM   6511 C  CD1  . LEU   A 1 1107 ? 196.170 199.603 150.195 1.00 86.32  ? 2439 LEU   A CD1  1 
ATOM   6512 C  CD2  . LEU   A 1 1107 ? 195.546 200.013 152.544 1.00 76.63  ? 2439 LEU   A CD2  1 
ATOM   6513 N  N    . SER   A 1 1108 ? 199.113 201.200 153.845 1.00 94.43  ? 2440 SER   A N    1 
ATOM   6514 C  CA   . SER   A 1 1108 ? 199.890 202.428 153.720 1.00 101.03 ? 2440 SER   A CA   1 
ATOM   6515 C  C    . SER   A 1 1108 ? 201.352 202.201 154.082 1.00 100.57 ? 2440 SER   A C    1 
ATOM   6516 O  O    . SER   A 1 1108 ? 202.250 202.724 153.414 1.00 102.12 ? 2440 SER   A O    1 
ATOM   6517 C  CB   . SER   A 1 1108 ? 199.287 203.523 154.599 1.00 102.65 ? 2440 SER   A CB   1 
ATOM   6518 O  OG   . SER   A 1 1108 ? 199.132 203.075 155.935 1.00 99.91  ? 2440 SER   A OG   1 
ATOM   6519 N  N    . THR   A 1 1109 ? 201.612 201.424 155.133 1.00 101.39 ? 2441 THR   A N    1 
ATOM   6520 C  CA   . THR   A 1 1109 ? 202.966 201.222 155.633 1.00 107.36 ? 2441 THR   A CA   1 
ATOM   6521 C  C    . THR   A 1 1109 ? 203.379 199.758 155.651 1.00 101.39 ? 2441 THR   A C    1 
ATOM   6522 O  O    . THR   A 1 1109 ? 204.461 199.440 156.158 1.00 101.04 ? 2441 THR   A O    1 
ATOM   6523 C  CB   . THR   A 1 1109 ? 203.105 201.806 157.041 1.00 109.57 ? 2441 THR   A CB   1 
ATOM   6524 O  OG1  . THR   A 1 1109 ? 202.206 201.131 157.929 1.00 100.44 ? 2441 THR   A OG1  1 
ATOM   6525 C  CG2  . THR   A 1 1109 ? 202.779 203.289 157.039 1.00 110.00 ? 2441 THR   A CG2  1 
ATOM   6526 N  N    . ARG   A 1 1110 ? 202.554 198.863 155.113 1.00 93.03  ? 2442 ARG   A N    1 
ATOM   6527 C  CA   . ARG   A 1 1110 ? 202.803 197.425 155.152 1.00 89.84  ? 2442 ARG   A CA   1 
ATOM   6528 C  C    . ARG   A 1 1110 ? 203.011 196.957 156.592 1.00 98.59  ? 2442 ARG   A C    1 
ATOM   6529 O  O    . ARG   A 1 1110 ? 204.028 196.358 156.947 1.00 99.29  ? 2442 ARG   A O    1 
ATOM   6530 C  CB   . ARG   A 1 1110 ? 203.992 197.050 154.265 1.00 100.69 ? 2442 ARG   A CB   1 
ATOM   6531 C  CG   . ARG   A 1 1110 ? 203.979 195.608 153.785 1.00 106.96 ? 2442 ARG   A CG   1 
ATOM   6532 C  CD   . ARG   A 1 1110 ? 204.681 195.462 152.441 1.00 104.55 ? 2442 ARG   A CD   1 
ATOM   6533 N  NE   . ARG   A 1 1110 ? 204.385 196.581 151.556 1.00 107.07 ? 2442 ARG   A NE   1 
ATOM   6534 C  CZ   . ARG   A 1 1110 ? 205.113 196.912 150.499 1.00 109.92 ? 2442 ARG   A CZ   1 
ATOM   6535 N  NH1  . ARG   A 1 1110 ? 206.178 196.213 150.148 1.00 112.06 ? 2442 ARG   A NH1  1 
ATOM   6536 N  NH2  . ARG   A 1 1110 ? 204.760 197.970 149.775 1.00 102.85 ? 2442 ARG   A NH2  1 
ATOM   6537 N  N    . ARG   A 1 1111 ? 202.018 197.258 157.426 1.00 95.39  ? 2443 ARG   A N    1 
ATOM   6538 C  CA   . ARG   A 1 1111 ? 202.044 196.915 158.839 1.00 84.56  ? 2443 ARG   A CA   1 
ATOM   6539 C  C    . ARG   A 1 1111 ? 200.821 196.084 159.185 1.00 66.37  ? 2443 ARG   A C    1 
ATOM   6540 O  O    . ARG   A 1 1111 ? 199.710 196.379 158.737 1.00 69.32  ? 2443 ARG   A O    1 
ATOM   6541 C  CB   . ARG   A 1 1111 ? 202.087 198.168 159.718 1.00 82.57  ? 2443 ARG   A CB   1 
ATOM   6542 N  N    . LEU   A 1 1112 ? 201.038 195.042 159.979 1.00 57.80  ? 2444 LEU   A N    1 
ATOM   6543 C  CA   . LEU   A 1 1112 ? 199.982 194.134 160.417 1.00 56.18  ? 2444 LEU   A CA   1 
ATOM   6544 C  C    . LEU   A 1 1112 ? 199.177 194.802 161.519 1.00 55.62  ? 2444 LEU   A C    1 
ATOM   6545 O  O    . LEU   A 1 1112 ? 199.734 195.242 162.524 1.00 62.15  ? 2444 LEU   A O    1 
ATOM   6546 C  CB   . LEU   A 1 1112 ? 200.605 192.834 160.906 1.00 57.10  ? 2444 LEU   A CB   1 
ATOM   6547 C  CG   . LEU   A 1 1112 ? 199.794 191.905 161.798 1.00 50.16  ? 2444 LEU   A CG   1 
ATOM   6548 C  CD1  . LEU   A 1 1112 ? 198.456 191.569 161.179 1.00 56.37  ? 2444 LEU   A CD1  1 
ATOM   6549 C  CD2  . LEU   A 1 1112 ? 200.602 190.656 162.053 1.00 49.75  ? 2444 LEU   A CD2  1 
ATOM   6550 N  N    . ILE   A 1 1113 ? 197.854 194.881 161.354 1.00 47.77  ? 2445 ILE   A N    1 
ATOM   6551 C  CA   . ILE   A 1 1113 ? 197.044 195.508 162.393 1.00 42.59  ? 2445 ILE   A CA   1 
ATOM   6552 C  C    . ILE   A 1 1113 ? 196.501 194.466 163.355 1.00 45.57  ? 2445 ILE   A C    1 
ATOM   6553 O  O    . ILE   A 1 1113 ? 196.646 194.594 164.575 1.00 50.24  ? 2445 ILE   A O    1 
ATOM   6554 C  CB   . ILE   A 1 1113 ? 195.914 196.340 161.770 1.00 42.47  ? 2445 ILE   A CB   1 
ATOM   6555 C  CG1  . ILE   A 1 1113 ? 196.489 197.486 160.951 1.00 49.56  ? 2445 ILE   A CG1  1 
ATOM   6556 C  CG2  . ILE   A 1 1113 ? 194.998 196.864 162.842 1.00 48.05  ? 2445 ILE   A CG2  1 
ATOM   6557 C  CD1  . ILE   A 1 1113 ? 195.459 198.181 160.114 1.00 57.44  ? 2445 ILE   A CD1  1 
ATOM   6558 N  N    . ARG   A 1 1114 ? 195.870 193.422 162.834 1.00 44.57  ? 2446 ARG   A N    1 
ATOM   6559 C  CA   . ARG   A 1 1114 ? 195.328 192.391 163.704 1.00 45.63  ? 2446 ARG   A CA   1 
ATOM   6560 C  C    . ARG   A 1 1114 ? 195.262 191.090 162.920 1.00 40.72  ? 2446 ARG   A C    1 
ATOM   6561 O  O    . ARG   A 1 1114 ? 195.231 191.084 161.689 1.00 43.06  ? 2446 ARG   A O    1 
ATOM   6562 C  CB   . ARG   A 1 1114 ? 193.958 192.797 164.252 1.00 45.58  ? 2446 ARG   A CB   1 
ATOM   6563 C  CG   . ARG   A 1 1114 ? 193.372 191.828 165.254 1.00 48.98  ? 2446 ARG   A CG   1 
ATOM   6564 C  CD   . ARG   A 1 1114 ? 192.290 192.486 166.087 1.00 57.28  ? 2446 ARG   A CD   1 
ATOM   6565 N  NE   . ARG   A 1 1114 ? 191.872 191.679 167.226 1.00 62.54  ? 2446 ARG   A NE   1 
ATOM   6566 C  CZ   . ARG   A 1 1114 ? 192.661 191.297 168.221 1.00 66.19  ? 2446 ARG   A CZ   1 
ATOM   6567 N  NH1  . ARG   A 1 1114 ? 193.931 191.664 168.282 1.00 61.71  ? 2446 ARG   A NH1  1 
ATOM   6568 N  NH2  . ARG   A 1 1114 ? 192.156 190.541 169.190 1.00 69.90  ? 2446 ARG   A NH2  1 
ATOM   6569 N  N    . VAL   A 1 1115 ? 195.238 189.983 163.656 1.00 40.31  ? 2447 VAL   A N    1 
ATOM   6570 C  CA   . VAL   A 1 1115 ? 195.354 188.642 163.100 1.00 40.78  ? 2447 VAL   A CA   1 
ATOM   6571 C  C    . VAL   A 1 1115 ? 194.088 187.892 163.496 1.00 37.81  ? 2447 VAL   A C    1 
ATOM   6572 O  O    . VAL   A 1 1115 ? 194.139 186.739 163.934 1.00 40.93  ? 2447 VAL   A O    1 
ATOM   6573 C  CB   . VAL   A 1 1115 ? 196.639 187.946 163.583 1.00 48.89  ? 2447 VAL   A CB   1 
ATOM   6574 C  CG1  . VAL   A 1 1115 ? 196.852 186.621 162.870 1.00 46.64  ? 2447 VAL   A CG1  1 
ATOM   6575 C  CG2  . VAL   A 1 1115 ? 197.824 188.854 163.381 1.00 42.15  ? 2447 VAL   A CG2  1 
ATOM   6576 N  N    . ILE   A 1 1116 ? 192.957 188.594 163.419 1.00 33.72  ? 2448 ILE   A N    1 
ATOM   6577 C  CA   . ILE   A 1 1116 ? 191.674 188.089 163.891 1.00 42.37  ? 2448 ILE   A CA   1 
ATOM   6578 C  C    . ILE   A 1 1116 ? 191.514 186.618 163.552 1.00 49.13  ? 2448 ILE   A C    1 
ATOM   6579 O  O    . ILE   A 1 1116 ? 191.905 186.168 162.471 1.00 57.84  ? 2448 ILE   A O    1 
ATOM   6580 C  CB   . ILE   A 1 1116 ? 190.536 188.893 163.254 1.00 45.10  ? 2448 ILE   A CB   1 
ATOM   6581 C  CG1  . ILE   A 1 1116 ? 190.617 190.360 163.650 1.00 50.44  ? 2448 ILE   A CG1  1 
ATOM   6582 C  CG2  . ILE   A 1 1116 ? 189.229 188.364 163.741 1.00 43.74  ? 2448 ILE   A CG2  1 
ATOM   6583 C  CD1  . ILE   A 1 1116 ? 189.692 191.246 162.856 1.00 42.13  ? 2448 ILE   A CD1  1 
ATOM   6584 N  N    . TYR   A 1 1117 ? 190.954 185.853 164.483 1.00 54.08  ? 2449 TYR   A N    1 
ATOM   6585 C  CA   . TYR   A 1 1117 ? 190.685 184.431 164.294 1.00 63.33  ? 2449 TYR   A CA   1 
ATOM   6586 C  C    . TYR   A 1 1117 ? 189.176 184.204 164.347 1.00 71.57  ? 2449 TYR   A C    1 
ATOM   6587 O  O    . TYR   A 1 1117 ? 188.521 184.584 165.323 1.00 67.82  ? 2449 TYR   A O    1 
ATOM   6588 C  CB   . TYR   A 1 1117 ? 191.418 183.616 165.354 1.00 69.47  ? 2449 TYR   A CB   1 
ATOM   6589 C  CG   . TYR   A 1 1117 ? 191.447 182.131 165.105 1.00 85.51  ? 2449 TYR   A CG   1 
ATOM   6590 C  CD1  . TYR   A 1 1117 ? 192.375 181.575 164.245 1.00 82.62  ? 2449 TYR   A CD1  1 
ATOM   6591 C  CD2  . TYR   A 1 1117 ? 190.581 181.279 165.765 1.00 90.28  ? 2449 TYR   A CD2  1 
ATOM   6592 C  CE1  . TYR   A 1 1117 ? 192.417 180.214 164.021 1.00 83.69  ? 2449 TYR   A CE1  1 
ATOM   6593 C  CE2  . TYR   A 1 1117 ? 190.623 179.914 165.551 1.00 90.59  ? 2449 TYR   A CE2  1 
ATOM   6594 C  CZ   . TYR   A 1 1117 ? 191.539 179.391 164.674 1.00 85.56  ? 2449 TYR   A CZ   1 
ATOM   6595 O  OH   . TYR   A 1 1117 ? 191.584 178.035 164.456 1.00 82.39  ? 2449 TYR   A OH   1 
ATOM   6596 N  N    . ASN   A 1 1118 ? 188.627 183.577 163.302 1.00 74.87  ? 2450 ASN   A N    1 
ATOM   6597 C  CA   . ASN   A 1 1118 ? 187.180 183.387 163.214 1.00 72.83  ? 2450 ASN   A CA   1 
ATOM   6598 C  C    . ASN   A 1 1118 ? 186.685 182.301 164.157 1.00 81.27  ? 2450 ASN   A C    1 
ATOM   6599 O  O    . ASN   A 1 1118 ? 185.494 182.260 164.486 1.00 76.48  ? 2450 ASN   A O    1 
ATOM   6600 C  CB   . ASN   A 1 1118 ? 186.774 183.016 161.789 1.00 67.48  ? 2450 ASN   A CB   1 
ATOM   6601 C  CG   . ASN   A 1 1118 ? 187.055 184.101 160.799 1.00 62.30  ? 2450 ASN   A CG   1 
ATOM   6602 O  OD1  . ASN   A 1 1118 ? 187.886 183.945 159.910 1.00 70.96  ? 2450 ASN   A OD1  1 
ATOM   6603 N  ND2  . ASN   A 1 1118 ? 186.335 185.196 160.915 1.00 51.44  ? 2450 ASN   A ND2  1 
ATOM   6604 N  N    . PHE   A 1 1119 ? 187.577 181.409 164.578 1.00 87.84  ? 2451 PHE   A N    1 
ATOM   6605 C  CA   . PHE   A 1 1119 ? 187.318 180.102 165.184 1.00 89.49  ? 2451 PHE   A CA   1 
ATOM   6606 C  C    . PHE   A 1 1119 ? 186.902 179.090 164.121 1.00 87.32  ? 2451 PHE   A C    1 
ATOM   6607 O  O    . PHE   A 1 1119 ? 186.818 177.895 164.434 1.00 87.12  ? 2451 PHE   A O    1 
ATOM   6608 C  CB   . PHE   A 1 1119 ? 186.263 180.127 166.302 1.00 93.00  ? 2451 PHE   A CB   1 
ATOM   6609 N  N    . CYS   A 1 1120 ? 186.665 179.511 162.881 1.00 87.83  ? 2452 CYS   A N    1 
ATOM   6610 C  CA   . CYS   A 1 1120 ? 186.379 178.563 161.813 1.00 90.71  ? 2452 CYS   A CA   1 
ATOM   6611 C  C    . CYS   A 1 1120 ? 187.679 178.121 161.153 1.00 81.48  ? 2452 CYS   A C    1 
ATOM   6612 O  O    . CYS   A 1 1120 ? 188.593 178.922 160.942 1.00 76.00  ? 2452 CYS   A O    1 
ATOM   6613 C  CB   . CYS   A 1 1120 ? 185.425 179.178 160.787 1.00 92.63  ? 2452 CYS   A CB   1 
ATOM   6614 S  SG   . CYS   A 1 1120 ? 183.726 179.418 161.398 1.00 104.22 ? 2452 CYS   A SG   1 
ATOM   6615 N  N    . ASN   A 1 1121 ? 187.750 176.829 160.823 1.00 82.52  ? 2453 ASN   A N    1 
ATOM   6616 C  CA   . ASN   A 1 1121 ? 189.027 176.195 160.507 1.00 81.06  ? 2453 ASN   A CA   1 
ATOM   6617 C  C    . ASN   A 1 1121 ? 189.688 176.810 159.282 1.00 74.20  ? 2453 ASN   A C    1 
ATOM   6618 O  O    . ASN   A 1 1121 ? 190.911 176.979 159.249 1.00 69.22  ? 2453 ASN   A O    1 
ATOM   6619 C  CB   . ASN   A 1 1121 ? 188.825 174.694 160.305 1.00 74.27  ? 2453 ASN   A CB   1 
ATOM   6620 N  N    . SER   A 1 1122 ? 188.906 177.128 158.256 1.00 69.17  ? 2454 SER   A N    1 
ATOM   6621 C  CA   . SER   A 1 1122 ? 189.433 177.702 157.029 1.00 64.89  ? 2454 SER   A CA   1 
ATOM   6622 C  C    . SER   A 1 1122 ? 188.492 178.795 156.554 1.00 66.47  ? 2454 SER   A C    1 
ATOM   6623 O  O    . SER   A 1 1122 ? 187.338 178.855 156.973 1.00 67.91  ? 2454 SER   A O    1 
ATOM   6624 C  CB   . SER   A 1 1122 ? 189.603 176.642 155.936 1.00 67.91  ? 2454 SER   A CB   1 
ATOM   6625 O  OG   . SER   A 1 1122 ? 190.089 177.221 154.740 1.00 65.84  ? 2454 SER   A OG   1 
ATOM   6626 N  N    . VAL   A 1 1123 ? 188.989 179.652 155.668 1.00 57.44  ? 2455 VAL   A N    1 
ATOM   6627 C  CA   . VAL   A 1 1123 ? 188.204 180.736 155.092 1.00 45.09  ? 2455 VAL   A CA   1 
ATOM   6628 C  C    . VAL   A 1 1123 ? 188.339 180.697 153.577 1.00 45.84  ? 2455 VAL   A C    1 
ATOM   6629 O  O    . VAL   A 1 1123 ? 189.431 180.480 153.046 1.00 46.45  ? 2455 VAL   A O    1 
ATOM   6630 C  CB   . VAL   A 1 1123 ? 188.626 182.104 155.663 1.00 35.42  ? 2455 VAL   A CB   1 
ATOM   6631 C  CG1  . VAL   A 1 1123 ? 189.959 182.499 155.152 1.00 28.99  ? 2455 VAL   A CG1  1 
ATOM   6632 C  CG2  . VAL   A 1 1123 ? 187.639 183.144 155.259 1.00 39.92  ? 2455 VAL   A CG2  1 
ATOM   6633 N  N    . ARG   A 1 1124 ? 187.221 180.889 152.881 1.00 41.74  ? 2456 ARG   A N    1 
ATOM   6634 C  CA   . ARG   A 1 1124 ? 187.161 180.725 151.438 1.00 37.90  ? 2456 ARG   A CA   1 
ATOM   6635 C  C    . ARG   A 1 1124 ? 187.009 182.052 150.707 1.00 43.43  ? 2456 ARG   A C    1 
ATOM   6636 O  O    . ARG   A 1 1124 ? 187.777 182.338 149.788 1.00 46.48  ? 2456 ARG   A O    1 
ATOM   6637 C  CB   . ARG   A 1 1124 ? 186.007 179.786 151.074 1.00 44.43  ? 2456 ARG   A CB   1 
ATOM   6638 N  N    . VAL   A 1 1125 ? 186.036 182.875 151.084 1.00 44.12  ? 2457 VAL   A N    1 
ATOM   6639 C  CA   . VAL   A 1 1125 ? 185.678 184.057 150.312 1.00 42.40  ? 2457 VAL   A CA   1 
ATOM   6640 C  C    . VAL   A 1 1125 ? 185.509 185.250 151.244 1.00 31.75  ? 2457 VAL   A C    1 
ATOM   6641 O  O    . VAL   A 1 1125 ? 185.054 185.102 152.380 1.00 36.51  ? 2457 VAL   A O    1 
ATOM   6642 C  CB   . VAL   A 1 1125 ? 184.396 183.802 149.488 1.00 43.33  ? 2457 VAL   A CB   1 
ATOM   6643 C  CG1  . VAL   A 1 1125 ? 183.222 183.568 150.387 1.00 28.85  ? 2457 VAL   A CG1  1 
ATOM   6644 C  CG2  . VAL   A 1 1125 ? 184.126 184.943 148.529 1.00 45.09  ? 2457 VAL   A CG2  1 
ATOM   6645 N  N    . MET   A 1 1126 ? 185.890 186.431 150.765 1.00 23.79  ? 2458 MET   A N    1 
ATOM   6646 C  CA   . MET   A 1 1126 ? 185.722 187.676 151.503 1.00 18.39  ? 2458 MET   A CA   1 
ATOM   6647 C  C    . MET   A 1 1126 ? 185.249 188.748 150.543 1.00 23.90  ? 2458 MET   A C    1 
ATOM   6648 O  O    . MET   A 1 1126 ? 185.946 189.055 149.575 1.00 31.32  ? 2458 MET   A O    1 
ATOM   6649 C  CB   . MET   A 1 1126 ? 187.023 188.127 152.156 1.00 20.74  ? 2458 MET   A CB   1 
ATOM   6650 C  CG   . MET   A 1 1126 ? 186.836 188.673 153.527 1.00 31.49  ? 2458 MET   A CG   1 
ATOM   6651 S  SD   . MET   A 1 1126 ? 188.327 189.358 154.227 1.00 61.02  ? 2458 MET   A SD   1 
ATOM   6652 C  CE   . MET   A 1 1126 ? 189.429 187.998 153.984 1.00 30.57  ? 2458 MET   A CE   1 
ATOM   6653 N  N    . MET   A 1 1127 ? 184.093 189.337 150.816 1.00 22.81  ? 2459 MET   A N    1 
ATOM   6654 C  CA   . MET   A 1 1127 ? 183.581 190.378 149.945 1.00 22.85  ? 2459 MET   A CA   1 
ATOM   6655 C  C    . MET   A 1 1127 ? 182.786 191.383 150.756 1.00 24.86  ? 2459 MET   A C    1 
ATOM   6656 O  O    . MET   A 1 1127 ? 182.221 191.060 151.798 1.00 32.21  ? 2459 MET   A O    1 
ATOM   6657 C  CB   . MET   A 1 1127 ? 182.704 189.801 148.843 1.00 22.00  ? 2459 MET   A CB   1 
ATOM   6658 C  CG   . MET   A 1 1127 ? 181.622 188.892 149.331 1.00 22.16  ? 2459 MET   A CG   1 
ATOM   6659 S  SD   . MET   A 1 1127 ? 180.456 188.621 148.003 1.00 56.66  ? 2459 MET   A SD   1 
ATOM   6660 C  CE   . MET   A 1 1127 ? 179.146 189.715 148.506 1.00 39.60  ? 2459 MET   A CE   1 
ATOM   6661 N  N    . THR   A 1 1128 ? 182.708 192.597 150.234 1.00 23.65  ? 2460 THR   A N    1 
ATOM   6662 C  CA   . THR   A 1 1128 ? 182.108 193.722 150.930 1.00 25.30  ? 2460 THR   A CA   1 
ATOM   6663 C  C    . THR   A 1 1128 ? 180.649 193.858 150.535 1.00 29.80  ? 2460 THR   A C    1 
ATOM   6664 O  O    . THR   A 1 1128 ? 180.302 193.712 149.363 1.00 45.40  ? 2460 THR   A O    1 
ATOM   6665 C  CB   . THR   A 1 1128 ? 182.841 195.016 150.591 1.00 38.58  ? 2460 THR   A CB   1 
ATOM   6666 O  OG1  . THR   A 1 1128 ? 184.206 194.917 151.004 1.00 43.91  ? 2460 THR   A OG1  1 
ATOM   6667 C  CG2  . THR   A 1 1128 ? 182.202 196.182 151.306 1.00 39.22  ? 2460 THR   A CG2  1 
ATOM   6668 N  N    . ALA   A 1 1129 ? 179.797 194.152 151.509 1.00 27.71  ? 2461 ALA   A N    1 
ATOM   6669 C  CA   . ALA   A 1 1129 ? 178.380 194.347 151.252 1.00 37.89  ? 2461 ALA   A CA   1 
ATOM   6670 C  C    . ALA   A 1 1129 ? 177.915 195.647 151.884 1.00 52.33  ? 2461 ALA   A C    1 
ATOM   6671 O  O    . ALA   A 1 1129 ? 178.483 196.113 152.872 1.00 53.65  ? 2461 ALA   A O    1 
ATOM   6672 C  CB   . ALA   A 1 1129 ? 177.541 193.191 151.784 1.00 42.31  ? 2461 ALA   A CB   1 
ATOM   6673 N  N    . GLN   A 1 1130 ? 176.881 196.237 151.286 1.00 71.01  ? 2462 GLN   A N    1 
ATOM   6674 C  CA   . GLN   A 1 1130 ? 176.320 197.482 151.795 1.00 73.70  ? 2462 GLN   A CA   1 
ATOM   6675 C  C    . GLN   A 1 1130 ? 175.323 197.244 152.919 1.00 73.34  ? 2462 GLN   A C    1 
ATOM   6676 O  O    . GLN   A 1 1130 ? 175.156 198.110 153.783 1.00 76.58  ? 2462 GLN   A O    1 
ATOM   6677 C  CB   . GLN   A 1 1130 ? 175.652 198.256 150.657 1.00 77.93  ? 2462 GLN   A CB   1 
ATOM   6678 C  CG   . GLN   A 1 1130 ? 175.085 199.612 151.045 1.00 82.61  ? 2462 GLN   A CG   1 
ATOM   6679 C  CD   . GLN   A 1 1130 ? 176.145 200.576 151.537 1.00 82.56  ? 2462 GLN   A CD   1 
ATOM   6680 O  OE1  . GLN   A 1 1130 ? 176.258 200.835 152.735 1.00 74.20  ? 2462 GLN   A OE1  1 
ATOM   6681 N  NE2  . GLN   A 1 1130 ? 176.929 201.115 150.611 1.00 84.02  ? 2462 GLN   A NE2  1 
ATOM   6682 N  N    . LEU   A 1 1131 ? 174.654 196.092 152.920 1.00 71.88  ? 2463 LEU   A N    1 
ATOM   6683 C  CA   . LEU   A 1 1131 ? 173.662 195.732 153.937 1.00 84.64  ? 2463 LEU   A CA   1 
ATOM   6684 C  C    . LEU   A 1 1131 ? 172.568 196.793 153.912 1.00 97.71  ? 2463 LEU   A C    1 
ATOM   6685 O  O    . LEU   A 1 1131 ? 171.871 196.907 152.889 1.00 96.66  ? 2463 LEU   A O    1 
ATOM   6686 C  CB   . LEU   A 1 1131 ? 174.365 195.527 155.281 1.00 83.59  ? 2463 LEU   A CB   1 
ATOM   6687 C  CG   . LEU   A 1 1131 ? 173.528 194.889 156.393 1.00 88.74  ? 2463 LEU   A CG   1 
ATOM   6688 C  CD1  . LEU   A 1 1131 ? 172.913 193.597 155.913 1.00 100.72 ? 2463 LEU   A CD1  1 
ATOM   6689 C  CD2  . LEU   A 1 1131 ? 174.365 194.648 157.637 1.00 76.73  ? 2463 LEU   A CD2  1 
ATOM   6690 N  N    . GLY   A 1 1132 ? 172.380 197.579 154.966 1.00 107.83 ? 2464 GLY   A N    1 
ATOM   6691 C  CA   . GLY   A 1 1132 ? 171.336 198.584 154.992 1.00 111.61 ? 2464 GLY   A CA   1 
ATOM   6692 C  C    . GLY   A 1 1132 ? 170.374 198.397 156.146 1.00 114.42 ? 2464 GLY   A C    1 
ATOM   6693 O  O    . GLY   A 1 1132 ? 170.745 197.870 157.193 1.00 99.27  ? 2464 GLY   A O    1 
ATOM   6694 N  N    . LYS   A 1 1135 ? 174.627 200.467 156.597 1.00 82.99  ? 2467 LYS   A N    1 
ATOM   6695 C  CA   . LYS   A 1 1135 ? 175.898 200.309 157.292 1.00 76.41  ? 2467 LYS   A CA   1 
ATOM   6696 C  C    . LYS   A 1 1135 ? 176.844 199.390 156.529 1.00 79.00  ? 2467 LYS   A C    1 
ATOM   6697 O  O    . LYS   A 1 1135 ? 176.508 198.251 156.222 1.00 84.03  ? 2467 LYS   A O    1 
ATOM   6698 C  CB   . LYS   A 1 1135 ? 175.666 199.779 158.707 1.00 79.27  ? 2467 LYS   A CB   1 
ATOM   6699 C  CG   . LYS   A 1 1135 ? 174.850 198.501 158.789 1.00 89.98  ? 2467 LYS   A CG   1 
ATOM   6700 C  CD   . LYS   A 1 1135 ? 174.840 197.960 160.208 1.00 103.66 ? 2467 LYS   A CD   1 
ATOM   6701 C  CE   . LYS   A 1 1135 ? 173.698 196.984 160.428 1.00 102.79 ? 2467 LYS   A CE   1 
ATOM   6702 N  NZ   . LYS   A 1 1135 ? 172.447 197.676 160.835 1.00 102.49 ? 2467 LYS   A NZ   1 
ATOM   6703 N  N    . ASN   A 1 1136 ? 178.034 199.895 156.223 1.00 70.00  ? 2468 ASN   A N    1 
ATOM   6704 C  CA   . ASN   A 1 1136 ? 178.994 199.117 155.454 1.00 57.37  ? 2468 ASN   A CA   1 
ATOM   6705 C  C    . ASN   A 1 1136 ? 179.574 198.000 156.307 1.00 54.94  ? 2468 ASN   A C    1 
ATOM   6706 O  O    . ASN   A 1 1136 ? 180.020 198.232 157.433 1.00 66.00  ? 2468 ASN   A O    1 
ATOM   6707 C  CB   . ASN   A 1 1136 ? 180.111 200.016 154.932 1.00 62.08  ? 2468 ASN   A CB   1 
ATOM   6708 C  CG   . ASN   A 1 1136 ? 180.530 199.663 153.520 1.00 75.12  ? 2468 ASN   A CG   1 
ATOM   6709 O  OD1  . ASN   A 1 1136 ? 179.702 199.295 152.688 1.00 83.04  ? 2468 ASN   A OD1  1 
ATOM   6710 N  ND2  . ASN   A 1 1136 ? 181.823 199.771 153.242 1.00 71.33  ? 2468 ASN   A ND2  1 
ATOM   6711 N  N    . VAL   A 1 1137 ? 179.564 196.781 155.766 1.00 46.04  ? 2469 VAL   A N    1 
ATOM   6712 C  CA   . VAL   A 1 1137 ? 180.105 195.602 156.427 1.00 36.16  ? 2469 VAL   A CA   1 
ATOM   6713 C  C    . VAL   A 1 1137 ? 180.973 194.857 155.427 1.00 34.97  ? 2469 VAL   A C    1 
ATOM   6714 O  O    . VAL   A 1 1137 ? 180.866 195.051 154.216 1.00 53.55  ? 2469 VAL   A O    1 
ATOM   6715 C  CB   . VAL   A 1 1137 ? 178.994 194.672 156.957 1.00 37.20  ? 2469 VAL   A CB   1 
ATOM   6716 C  CG1  . VAL   A 1 1137 ? 178.157 195.381 157.991 1.00 50.30  ? 2469 VAL   A CG1  1 
ATOM   6717 C  CG2  . VAL   A 1 1137 ? 178.117 194.210 155.822 1.00 42.15  ? 2469 VAL   A CG2  1 
ATOM   6718 N  N    . MET   A 1 1138 ? 181.847 194.001 155.940 1.00 23.81  ? 2470 MET   A N    1 
ATOM   6719 C  CA   . MET   A 1 1138 ? 182.533 193.031 155.104 1.00 25.21  ? 2470 MET   A CA   1 
ATOM   6720 C  C    . MET   A 1 1138 ? 182.251 191.650 155.650 1.00 19.21  ? 2470 MET   A C    1 
ATOM   6721 O  O    . MET   A 1 1138 ? 182.435 191.403 156.841 1.00 27.87  ? 2470 MET   A O    1 
ATOM   6722 C  CB   . MET   A 1 1138 ? 184.031 193.275 155.026 1.00 30.90  ? 2470 MET   A CB   1 
ATOM   6723 C  CG   . MET   A 1 1138 ? 184.688 192.342 154.040 1.00 35.35  ? 2470 MET   A CG   1 
ATOM   6724 S  SD   . MET   A 1 1138 ? 186.447 192.575 153.835 1.00 56.37  ? 2470 MET   A SD   1 
ATOM   6725 C  CE   . MET   A 1 1138 ? 186.461 194.120 152.949 1.00 44.00  ? 2470 MET   A CE   1 
ATOM   6726 N  N    . LEU   A 1 1139 ? 181.771 190.767 154.790 1.00 10.50  ? 2471 LEU   A N    1 
ATOM   6727 C  CA   . LEU   A 1 1139 ? 181.213 189.498 155.217 1.00 11.00  ? 2471 LEU   A CA   1 
ATOM   6728 C  C    . LEU   A 1 1139 ? 182.080 188.358 154.715 1.00 15.67  ? 2471 LEU   A C    1 
ATOM   6729 O  O    . LEU   A 1 1139 ? 182.486 188.345 153.555 1.00 30.10  ? 2471 LEU   A O    1 
ATOM   6730 C  CB   . LEU   A 1 1139 ? 179.764 189.378 154.753 1.00 7.94   ? 2471 LEU   A CB   1 
ATOM   6731 C  CG   . LEU   A 1 1139 ? 179.374 189.410 153.290 1.00 17.61  ? 2471 LEU   A CG   1 
ATOM   6732 C  CD1  . LEU   A 1 1139 ? 179.523 188.062 152.674 1.00 30.04  ? 2471 LEU   A CD1  1 
ATOM   6733 C  CD2  . LEU   A 1 1139 ? 177.944 189.867 153.186 1.00 23.53  ? 2471 LEU   A CD2  1 
ATOM   6734 N  N    . VAL   A 1 1140 ? 182.350 187.405 155.596 1.00 16.27  ? 2472 VAL   A N    1 
ATOM   6735 C  CA   . VAL   A 1 1140 ? 183.403 186.420 155.424 1.00 18.36  ? 2472 VAL   A CA   1 
ATOM   6736 C  C    . VAL   A 1 1140 ? 182.766 185.047 155.516 1.00 26.54  ? 2472 VAL   A C    1 
ATOM   6737 O  O    . VAL   A 1 1140 ? 181.843 184.843 156.307 1.00 35.48  ? 2472 VAL   A O    1 
ATOM   6738 C  CB   . VAL   A 1 1140 ? 184.481 186.585 156.511 1.00 18.15  ? 2472 VAL   A CB   1 
ATOM   6739 C  CG1  . VAL   A 1 1140 ? 185.440 185.434 156.505 1.00 22.69  ? 2472 VAL   A CG1  1 
ATOM   6740 C  CG2  . VAL   A 1 1140 ? 185.190 187.900 156.380 1.00 16.72  ? 2472 VAL   A CG2  1 
ATOM   6741 N  N    . LEU   A 1 1141 ? 183.238 184.107 154.708 1.00 34.82  ? 2473 LEU   A N    1 
ATOM   6742 C  CA   . LEU   A 1 1141 ? 182.701 182.755 154.712 1.00 41.27  ? 2473 LEU   A CA   1 
ATOM   6743 C  C    . LEU   A 1 1141 ? 183.836 181.760 154.883 1.00 49.35  ? 2473 LEU   A C    1 
ATOM   6744 O  O    . LEU   A 1 1141 ? 184.863 181.869 154.212 1.00 54.61  ? 2473 LEU   A O    1 
ATOM   6745 C  CB   . LEU   A 1 1141 ? 181.942 182.479 153.427 1.00 43.38  ? 2473 LEU   A CB   1 
ATOM   6746 C  CG   . LEU   A 1 1141 ? 181.277 181.131 153.250 1.00 43.86  ? 2473 LEU   A CG   1 
ATOM   6747 C  CD1  . LEU   A 1 1141 ? 180.590 180.716 154.507 1.00 51.97  ? 2473 LEU   A CD1  1 
ATOM   6748 C  CD2  . LEU   A 1 1141 ? 180.268 181.298 152.167 1.00 45.85  ? 2473 LEU   A CD2  1 
ATOM   6749 N  N    . GLY   A 1 1142 ? 183.657 180.798 155.782 1.00 52.71  ? 2474 GLY   A N    1 
ATOM   6750 C  CA   . GLY   A 1 1142 ? 184.694 179.822 156.039 1.00 54.38  ? 2474 GLY   A CA   1 
ATOM   6751 C  C    . GLY   A 1 1142 ? 184.106 178.458 156.331 1.00 69.10  ? 2474 GLY   A C    1 
ATOM   6752 O  O    . GLY   A 1 1142 ? 182.913 178.310 156.586 1.00 69.65  ? 2474 GLY   A O    1 
ATOM   6753 N  N    . TYR   A 1 1143 ? 184.975 177.461 156.294 1.00 73.66  ? 2475 TYR   A N    1 
ATOM   6754 C  CA   . TYR   A 1 1143 ? 184.627 176.090 156.627 1.00 73.87  ? 2475 TYR   A CA   1 
ATOM   6755 C  C    . TYR   A 1 1143 ? 185.177 175.726 157.998 1.00 81.44  ? 2475 TYR   A C    1 
ATOM   6756 O  O    . TYR   A 1 1143 ? 186.168 176.289 158.465 1.00 82.08  ? 2475 TYR   A O    1 
ATOM   6757 C  CB   . TYR   A 1 1143 ? 185.167 175.121 155.575 1.00 64.25  ? 2475 TYR   A CB   1 
ATOM   6758 C  CG   . TYR   A 1 1143 ? 184.905 175.547 154.153 1.00 65.87  ? 2475 TYR   A CG   1 
ATOM   6759 C  CD1  . TYR   A 1 1143 ? 183.612 175.730 153.692 1.00 70.97  ? 2475 TYR   A CD1  1 
ATOM   6760 C  CD2  . TYR   A 1 1143 ? 185.949 175.764 153.272 1.00 70.27  ? 2475 TYR   A CD2  1 
ATOM   6761 C  CE1  . TYR   A 1 1143 ? 183.367 176.114 152.393 1.00 76.57  ? 2475 TYR   A CE1  1 
ATOM   6762 C  CE2  . TYR   A 1 1143 ? 185.714 176.152 151.970 1.00 74.57  ? 2475 TYR   A CE2  1 
ATOM   6763 C  CZ   . TYR   A 1 1143 ? 184.422 176.326 151.537 1.00 80.69  ? 2475 TYR   A CZ   1 
ATOM   6764 O  OH   . TYR   A 1 1143 ? 184.187 176.710 150.238 1.00 80.92  ? 2475 TYR   A OH   1 
ATOM   6765 N  N    . ASN   A 1 1144 ? 184.512 174.779 158.647 1.00 87.52  ? 2476 ASN   A N    1 
ATOM   6766 C  CA   . ASN   A 1 1144 ? 184.951 174.317 159.958 1.00 91.49  ? 2476 ASN   A CA   1 
ATOM   6767 C  C    . ASN   A 1 1144 ? 185.770 173.038 159.840 1.00 86.69  ? 2476 ASN   A C    1 
ATOM   6768 O  O    . ASN   A 1 1144 ? 185.918 172.293 160.807 1.00 77.14  ? 2476 ASN   A O    1 
ATOM   6769 C  CB   . ASN   A 1 1144 ? 183.753 174.091 160.878 1.00 95.17  ? 2476 ASN   A CB   1 
ATOM   6770 C  CG   . ASN   A 1 1144 ? 183.431 175.305 161.721 1.00 95.15  ? 2476 ASN   A CG   1 
ATOM   6771 O  OD1  . ASN   A 1 1144 ? 182.298 175.784 161.732 1.00 96.35  ? 2476 ASN   A OD1  1 
ATOM   6772 N  ND2  . ASN   A 1 1144 ? 184.429 175.812 162.434 1.00 91.85  ? 2476 ASN   A ND2  1 
ATOM   6773 N  N    . ILE   A 1 1157 ? 181.173 168.828 158.183 1.00 99.37  ? 2489 ILE   A N    1 
ATOM   6774 C  CA   . ILE   A 1 1157 ? 181.853 170.088 157.917 1.00 103.76 ? 2489 ILE   A CA   1 
ATOM   6775 C  C    . ILE   A 1 1157 ? 180.825 171.211 157.881 1.00 105.68 ? 2489 ILE   A C    1 
ATOM   6776 O  O    . ILE   A 1 1157 ? 179.755 171.067 157.290 1.00 108.08 ? 2489 ILE   A O    1 
ATOM   6777 C  CB   . ILE   A 1 1157 ? 182.670 170.010 156.615 1.00 95.69  ? 2489 ILE   A CB   1 
ATOM   6778 C  CG1  . ILE   A 1 1157 ? 183.358 171.338 156.325 1.00 85.32  ? 2489 ILE   A CG1  1 
ATOM   6779 C  CG2  . ILE   A 1 1157 ? 181.792 169.608 155.450 1.00 90.56  ? 2489 ILE   A CG2  1 
ATOM   6780 C  CD1  . ILE   A 1 1157 ? 184.353 171.253 155.202 1.00 83.44  ? 2489 ILE   A CD1  1 
ATOM   6781 N  N    . GLN   A 1 1158 ? 181.145 172.328 158.530 1.00 96.09  ? 2490 GLN   A N    1 
ATOM   6782 C  CA   . GLN   A 1 1158 ? 180.206 173.425 158.706 1.00 94.99  ? 2490 GLN   A CA   1 
ATOM   6783 C  C    . GLN   A 1 1158 ? 180.761 174.698 158.086 1.00 85.17  ? 2490 GLN   A C    1 
ATOM   6784 O  O    . GLN   A 1 1158 ? 181.962 174.972 158.176 1.00 78.40  ? 2490 GLN   A O    1 
ATOM   6785 C  CB   . GLN   A 1 1158 ? 179.906 173.658 160.190 1.00 87.38  ? 2490 GLN   A CB   1 
ATOM   6786 C  CG   . GLN   A 1 1158 ? 178.597 174.372 160.438 1.00 87.42  ? 2490 GLN   A CG   1 
ATOM   6787 C  CD   . GLN   A 1 1158 ? 177.542 174.002 159.421 1.00 97.25  ? 2490 GLN   A CD   1 
ATOM   6788 O  OE1  . GLN   A 1 1158 ? 177.160 172.841 159.302 1.00 93.30  ? 2490 GLN   A OE1  1 
ATOM   6789 N  NE2  . GLN   A 1 1158 ? 177.079 174.987 158.663 1.00 96.49  ? 2490 GLN   A NE2  1 
ATOM   6790 N  N    . SER   A 1 1159 ? 179.878 175.476 157.466 1.00 77.27  ? 2491 SER   A N    1 
ATOM   6791 C  CA   . SER   A 1 1159 ? 180.242 176.728 156.823 1.00 71.07  ? 2491 SER   A CA   1 
ATOM   6792 C  C    . SER   A 1 1159 ? 179.634 177.897 157.584 1.00 76.10  ? 2491 SER   A C    1 
ATOM   6793 O  O    . SER   A 1 1159 ? 178.416 177.961 157.779 1.00 73.99  ? 2491 SER   A O    1 
ATOM   6794 C  CB   . SER   A 1 1159 ? 179.779 176.748 155.368 1.00 67.38  ? 2491 SER   A CB   1 
ATOM   6795 O  OG   . SER   A 1 1159 ? 180.476 175.783 154.606 1.00 74.54  ? 2491 SER   A OG   1 
ATOM   6796 N  N    . CYS   A 1 1160 ? 180.493 178.829 157.983 1.00 75.56  ? 2492 CYS   A N    1 
ATOM   6797 C  CA   . CYS   A 1 1160 ? 180.144 179.941 158.854 1.00 66.02  ? 2492 CYS   A CA   1 
ATOM   6798 C  C    . CYS   A 1 1160 ? 180.309 181.251 158.103 1.00 54.28  ? 2492 CYS   A C    1 
ATOM   6799 O  O    . CYS   A 1 1160 ? 181.337 181.477 157.458 1.00 58.17  ? 2492 CYS   A O    1 
ATOM   6800 C  CB   . CYS   A 1 1160 ? 181.008 179.925 160.122 1.00 80.31  ? 2492 CYS   A CB   1 
ATOM   6801 S  SG   . CYS   A 1 1160 ? 182.748 180.418 159.919 1.00 94.75  ? 2492 CYS   A SG   1 
ATOM   6802 N  N    . LEU   A 1 1161 ? 179.293 182.106 158.191 1.00 46.45  ? 2493 LEU   A N    1 
ATOM   6803 C  CA   . LEU   A 1 1161 ? 179.251 183.385 157.497 1.00 41.16  ? 2493 LEU   A CA   1 
ATOM   6804 C  C    . LEU   A 1 1161 ? 179.206 184.500 158.533 1.00 35.27  ? 2493 LEU   A C    1 
ATOM   6805 O  O    . LEU   A 1 1161 ? 178.168 184.722 159.160 1.00 40.54  ? 2493 LEU   A O    1 
ATOM   6806 C  CB   . LEU   A 1 1161 ? 178.029 183.444 156.581 1.00 31.01  ? 2493 LEU   A CB   1 
ATOM   6807 C  CG   . LEU   A 1 1161 ? 177.495 184.787 156.096 1.00 23.13  ? 2493 LEU   A CG   1 
ATOM   6808 C  CD1  . LEU   A 1 1161 ? 178.554 185.538 155.350 1.00 29.44  ? 2493 LEU   A CD1  1 
ATOM   6809 C  CD2  . LEU   A 1 1161 ? 176.292 184.564 155.217 1.00 32.17  ? 2493 LEU   A CD2  1 
ATOM   6810 N  N    . THR   A 1 1162 ? 180.325 185.191 158.716 1.00 27.91  ? 2494 THR   A N    1 
ATOM   6811 C  CA   . THR   A 1 1162 ? 180.455 186.208 159.749 1.00 25.55  ? 2494 THR   A CA   1 
ATOM   6812 C  C    . THR   A 1 1162 ? 180.445 187.572 159.087 1.00 22.81  ? 2494 THR   A C    1 
ATOM   6813 O  O    . THR   A 1 1162 ? 181.297 187.855 158.247 1.00 33.22  ? 2494 THR   A O    1 
ATOM   6814 C  CB   . THR   A 1 1162 ? 181.746 186.028 160.538 1.00 24.41  ? 2494 THR   A CB   1 
ATOM   6815 O  OG1  . THR   A 1 1162 ? 182.853 186.185 159.656 1.00 25.17  ? 2494 THR   A OG1  1 
ATOM   6816 C  CG2  . THR   A 1 1162 ? 181.815 184.642 161.106 1.00 33.77  ? 2494 THR   A CG2  1 
ATOM   6817 N  N    . VAL   A 1 1163 ? 179.509 188.419 159.484 1.00 18.13  ? 2495 VAL   A N    1 
ATOM   6818 C  CA   . VAL   A 1 1163 ? 179.356 189.755 158.929 1.00 15.78  ? 2495 VAL   A CA   1 
ATOM   6819 C  C    . VAL   A 1 1163 ? 180.025 190.719 159.886 1.00 23.19  ? 2495 VAL   A C    1 
ATOM   6820 O  O    . VAL   A 1 1163 ? 179.613 190.825 161.045 1.00 32.31  ? 2495 VAL   A O    1 
ATOM   6821 C  CB   . VAL   A 1 1163 ? 177.880 190.110 158.744 1.00 15.30  ? 2495 VAL   A CB   1 
ATOM   6822 C  CG1  . VAL   A 1 1163 ? 177.745 191.367 157.947 1.00 19.31  ? 2495 VAL   A CG1  1 
ATOM   6823 C  CG2  . VAL   A 1 1163 ? 177.156 188.975 158.065 1.00 18.12  ? 2495 VAL   A CG2  1 
ATOM   6824 N  N    . TRP   A 1 1164 ? 181.034 191.449 159.421 1.00 24.71  ? 2496 TRP   A N    1 
ATOM   6825 C  CA   . TRP   A 1 1164 ? 181.827 192.296 160.290 1.00 27.52  ? 2496 TRP   A CA   1 
ATOM   6826 C  C    . TRP   A 1 1164 ? 181.636 193.761 159.949 1.00 33.79  ? 2496 TRP   A C    1 
ATOM   6827 O  O    . TRP   A 1 1164 ? 181.561 194.130 158.778 1.00 43.02  ? 2496 TRP   A O    1 
ATOM   6828 C  CB   . TRP   A 1 1164 ? 183.306 191.959 160.190 1.00 26.91  ? 2496 TRP   A CB   1 
ATOM   6829 C  CG   . TRP   A 1 1164 ? 183.579 190.654 160.729 1.00 32.28  ? 2496 TRP   A CG   1 
ATOM   6830 C  CD1  . TRP   A 1 1164 ? 182.691 189.835 161.320 1.00 46.22  ? 2496 TRP   A CD1  1 
ATOM   6831 C  CD2  . TRP   A 1 1164 ? 184.854 190.074 160.936 1.00 39.32  ? 2496 TRP   A CD2  1 
ATOM   6832 N  NE1  . TRP   A 1 1164 ? 183.311 188.715 161.785 1.00 52.66  ? 2496 TRP   A NE1  1 
ATOM   6833 C  CE2  . TRP   A 1 1164 ? 184.651 188.849 161.578 1.00 44.30  ? 2496 TRP   A CE2  1 
ATOM   6834 C  CE3  . TRP   A 1 1164 ? 186.145 190.450 160.605 1.00 56.82  ? 2496 TRP   A CE3  1 
ATOM   6835 C  CZ2  . TRP   A 1 1164 ? 185.679 188.001 161.896 1.00 43.10  ? 2496 TRP   A CZ2  1 
ATOM   6836 C  CZ3  . TRP   A 1 1164 ? 187.169 189.601 160.922 1.00 63.15  ? 2496 TRP   A CZ3  1 
ATOM   6837 C  CH2  . TRP   A 1 1164 ? 186.927 188.389 161.558 1.00 49.09  ? 2496 TRP   A CH2  1 
ATOM   6838 N  N    . ASP   A 1 1165 ? 181.571 194.598 160.975 1.00 32.07  ? 2497 ASP   A N    1 
ATOM   6839 C  CA   . ASP   A 1 1165 ? 181.488 196.027 160.741 1.00 37.74  ? 2497 ASP   A CA   1 
ATOM   6840 C  C    . ASP   A 1 1165 ? 182.798 196.483 160.117 1.00 37.77  ? 2497 ASP   A C    1 
ATOM   6841 O  O    . ASP   A 1 1165 ? 183.875 196.080 160.554 1.00 38.26  ? 2497 ASP   A O    1 
ATOM   6842 C  CB   . ASP   A 1 1165 ? 181.201 196.755 162.051 1.00 48.76  ? 2497 ASP   A CB   1 
ATOM   6843 C  CG   . ASP   A 1 1165 ? 180.941 198.232 161.856 1.00 67.31  ? 2497 ASP   A CG   1 
ATOM   6844 O  OD1  . ASP   A 1 1165 ? 179.845 198.581 161.368 1.00 75.20  ? 2497 ASP   A OD1  1 
ATOM   6845 O  OD2  . ASP   A 1 1165 ? 181.816 199.045 162.205 1.00 77.13  ? 2497 ASP   A OD2  1 
ATOM   6846 N  N    . ILE   A 1 1166 ? 182.703 197.331 159.101 1.00 43.47  ? 2498 ILE   A N    1 
ATOM   6847 C  CA   . ILE   A 1 1166 ? 183.729 197.457 158.068 1.00 40.40  ? 2498 ILE   A CA   1 
ATOM   6848 C  C    . ILE   A 1 1166 ? 185.072 197.967 158.580 1.00 46.73  ? 2498 ILE   A C    1 
ATOM   6849 O  O    . ILE   A 1 1166 ? 186.072 197.913 157.857 1.00 51.61  ? 2498 ILE   A O    1 
ATOM   6850 C  CB   . ILE   A 1 1166 ? 183.212 198.365 156.940 1.00 45.07  ? 2498 ILE   A CB   1 
ATOM   6851 C  CG1  . ILE   A 1 1166 ? 184.053 198.206 155.676 1.00 46.82  ? 2498 ILE   A CG1  1 
ATOM   6852 C  CG2  . ILE   A 1 1166 ? 183.215 199.802 157.392 1.00 50.85  ? 2498 ILE   A CG2  1 
ATOM   6853 C  CD1  . ILE   A 1 1166 ? 184.189 196.799 155.216 1.00 39.56  ? 2498 ILE   A CD1  1 
ATOM   6854 N  N    . ASN   A 1 1167 ? 185.128 198.447 159.826 1.00 47.98  ? 2499 ASN   A N    1 
ATOM   6855 C  CA   . ASN   A 1 1167 ? 186.275 199.227 160.301 1.00 50.23  ? 2499 ASN   A CA   1 
ATOM   6856 C  C    . ASN   A 1 1167 ? 186.953 198.527 161.484 1.00 43.85  ? 2499 ASN   A C    1 
ATOM   6857 O  O    . ASN   A 1 1167 ? 187.242 199.155 162.504 1.00 52.28  ? 2499 ASN   A O    1 
ATOM   6858 C  CB   . ASN   A 1 1167 ? 185.849 200.648 160.672 1.00 56.76  ? 2499 ASN   A CB   1 
ATOM   6859 C  CG   . ASN   A 1 1167 ? 184.573 200.678 161.468 1.00 61.59  ? 2499 ASN   A CG   1 
ATOM   6860 O  OD1  . ASN   A 1 1167 ? 184.337 199.810 162.301 1.00 71.91  ? 2499 ASN   A OD1  1 
ATOM   6861 N  ND2  . ASN   A 1 1167 ? 183.732 201.669 161.209 1.00 59.00  ? 2499 ASN   A ND2  1 
ATOM   6862 N  N    . LEU   A 1 1168 ? 187.198 197.227 161.351 1.00 38.36  ? 2500 LEU   A N    1 
ATOM   6863 C  CA   . LEU   A 1 1168 ? 188.019 196.550 162.348 1.00 42.42  ? 2500 LEU   A CA   1 
ATOM   6864 C  C    . LEU   A 1 1168 ? 189.349 197.246 162.600 1.00 50.33  ? 2500 LEU   A C    1 
ATOM   6865 O  O    . LEU   A 1 1168 ? 189.749 197.347 163.761 1.00 67.77  ? 2500 LEU   A O    1 
ATOM   6866 C  CB   . LEU   A 1 1168 ? 188.302 195.092 161.986 1.00 44.90  ? 2500 LEU   A CB   1 
ATOM   6867 C  CG   . LEU   A 1 1168 ? 187.306 193.995 162.332 1.00 41.82  ? 2500 LEU   A CG   1 
ATOM   6868 C  CD1  . LEU   A 1 1168 ? 187.201 193.916 163.828 1.00 42.92  ? 2500 LEU   A CD1  1 
ATOM   6869 C  CD2  . LEU   A 1 1168 ? 185.965 194.243 161.730 1.00 44.42  ? 2500 LEU   A CD2  1 
ATOM   6870 N  N    . PRO   A 1 1169 ? 190.093 197.693 161.584 1.00 43.23  ? 2501 PRO   A N    1 
ATOM   6871 C  CA   . PRO   A 1 1169 ? 191.361 198.376 161.891 1.00 50.32  ? 2501 PRO   A CA   1 
ATOM   6872 C  C    . PRO   A 1 1169 ? 191.179 199.635 162.723 1.00 60.32  ? 2501 PRO   A C    1 
ATOM   6873 O  O    . PRO   A 1 1169 ? 191.896 199.824 163.719 1.00 63.23  ? 2501 PRO   A O    1 
ATOM   6874 C  CB   . PRO   A 1 1169 ? 191.938 198.689 160.505 1.00 58.26  ? 2501 PRO   A CB   1 
ATOM   6875 C  CG   . PRO   A 1 1169 ? 190.782 198.610 159.576 1.00 59.37  ? 2501 PRO   A CG   1 
ATOM   6876 C  CD   . PRO   A 1 1169 ? 189.893 197.562 160.132 1.00 46.15  ? 2501 PRO   A CD   1 
ATOM   6877 N  N    . HIS   A 1 1170 ? 190.226 200.492 162.357 1.00 60.64  ? 2502 HIS   A N    1 
ATOM   6878 C  CA   . HIS   A 1 1170 ? 189.967 201.685 163.148 1.00 61.12  ? 2502 HIS   A CA   1 
ATOM   6879 C  C    . HIS   A 1 1170 ? 189.593 201.322 164.573 1.00 58.53  ? 2502 HIS   A C    1 
ATOM   6880 O  O    . HIS   A 1 1170 ? 190.086 201.943 165.519 1.00 62.87  ? 2502 HIS   A O    1 
ATOM   6881 C  CB   . HIS   A 1 1170 ? 188.858 202.513 162.509 1.00 55.99  ? 2502 HIS   A CB   1 
ATOM   6882 C  CG   . HIS   A 1 1170 ? 189.193 203.006 161.140 1.00 62.86  ? 2502 HIS   A CG   1 
ATOM   6883 N  ND1  . HIS   A 1 1170 ? 190.406 203.585 160.836 1.00 68.03  ? 2502 HIS   A ND1  1 
ATOM   6884 C  CD2  . HIS   A 1 1170 ? 188.478 203.005 159.991 1.00 66.89  ? 2502 HIS   A CD2  1 
ATOM   6885 C  CE1  . HIS   A 1 1170 ? 190.423 203.921 159.560 1.00 69.95  ? 2502 HIS   A CE1  1 
ATOM   6886 N  NE2  . HIS   A 1 1170 ? 189.265 203.580 159.024 1.00 69.70  ? 2502 HIS   A NE2  1 
ATOM   6887 N  N    . GLU   A 1 1171 ? 188.736 200.318 164.749 1.00 48.34  ? 2503 GLU   A N    1 
ATOM   6888 C  CA   . GLU   A 1 1171 ? 188.342 199.951 166.100 1.00 46.27  ? 2503 GLU   A CA   1 
ATOM   6889 C  C    . GLU   A 1 1171 ? 189.498 199.359 166.889 1.00 43.42  ? 2503 GLU   A C    1 
ATOM   6890 O  O    . GLU   A 1 1171 ? 189.579 199.559 168.103 1.00 53.02  ? 2503 GLU   A O    1 
ATOM   6891 C  CB   . GLU   A 1 1171 ? 187.181 198.972 166.076 1.00 50.11  ? 2503 GLU   A CB   1 
ATOM   6892 C  CG   . GLU   A 1 1171 ? 186.531 198.761 167.430 1.00 52.37  ? 2503 GLU   A CG   1 
ATOM   6893 C  CD   . GLU   A 1 1171 ? 186.214 200.048 168.186 1.00 51.49  ? 2503 GLU   A CD   1 
ATOM   6894 O  OE1  . GLU   A 1 1171 ? 186.108 201.128 167.566 1.00 51.50  ? 2503 GLU   A OE1  1 
ATOM   6895 O  OE2  . GLU   A 1 1171 ? 186.072 199.976 169.422 1.00 56.68  ? 2503 GLU   A OE2  1 
ATOM   6896 N  N    . VAL   A 1 1172 ? 190.401 198.635 166.231 1.00 39.59  ? 2504 VAL   A N    1 
ATOM   6897 C  CA   . VAL   A 1 1172 ? 191.573 198.120 166.928 1.00 49.12  ? 2504 VAL   A CA   1 
ATOM   6898 C  C    . VAL   A 1 1172 ? 192.416 199.270 167.452 1.00 61.44  ? 2504 VAL   A C    1 
ATOM   6899 O  O    . VAL   A 1 1172 ? 192.785 199.299 168.633 1.00 66.28  ? 2504 VAL   A O    1 
ATOM   6900 C  CB   . VAL   A 1 1172 ? 192.396 197.201 166.011 1.00 56.02  ? 2504 VAL   A CB   1 
ATOM   6901 C  CG1  . VAL   A 1 1172 ? 193.754 196.940 166.629 1.00 54.76  ? 2504 VAL   A CG1  1 
ATOM   6902 C  CG2  . VAL   A 1 1172 ? 191.676 195.905 165.782 1.00 57.31  ? 2504 VAL   A CG2  1 
ATOM   6903 N  N    . GLN   A 1 1173 ? 192.728 200.243 166.589 1.00 60.33  ? 2505 GLN   A N    1 
ATOM   6904 C  CA   . GLN   A 1 1173 ? 193.506 201.382 167.075 1.00 62.65  ? 2505 GLN   A CA   1 
ATOM   6905 C  C    . GLN   A 1 1173 ? 192.774 202.134 168.177 1.00 58.68  ? 2505 GLN   A C    1 
ATOM   6906 O  O    . GLN   A 1 1173 ? 193.387 202.514 169.182 1.00 63.30  ? 2505 GLN   A O    1 
ATOM   6907 C  CB   . GLN   A 1 1173 ? 193.898 202.347 165.950 1.00 69.14  ? 2505 GLN   A CB   1 
ATOM   6908 C  CG   . GLN   A 1 1173 ? 195.230 202.044 165.249 1.00 70.19  ? 2505 GLN   A CG   1 
ATOM   6909 C  CD   . GLN   A 1 1173 ? 195.206 200.876 164.302 1.00 74.47  ? 2505 GLN   A CD   1 
ATOM   6910 O  OE1  . GLN   A 1 1173 ? 194.251 200.687 163.562 1.00 71.20  ? 2505 GLN   A OE1  1 
ATOM   6911 N  NE2  . GLN   A 1 1173 ? 196.263 200.078 164.324 1.00 82.06  ? 2505 GLN   A NE2  1 
ATOM   6912 N  N    . ASN   A 1 1174 ? 191.468 202.352 168.018 1.00 53.73  ? 2506 ASN   A N    1 
ATOM   6913 C  CA   . ASN   A 1 1174 ? 190.728 203.095 169.030 1.00 51.42  ? 2506 ASN   A CA   1 
ATOM   6914 C  C    . ASN   A 1 1174 ? 190.777 202.396 170.377 1.00 52.34  ? 2506 ASN   A C    1 
ATOM   6915 O  O    . ASN   A 1 1174 ? 191.079 203.026 171.395 1.00 54.25  ? 2506 ASN   A O    1 
ATOM   6916 C  CB   . ASN   A 1 1174 ? 189.279 203.297 168.599 1.00 49.76  ? 2506 ASN   A CB   1 
ATOM   6917 C  CG   . ASN   A 1 1174 ? 189.141 204.298 167.485 1.00 55.63  ? 2506 ASN   A CG   1 
ATOM   6918 O  OD1  . ASN   A 1 1174 ? 190.130 204.727 166.896 1.00 65.03  ? 2506 ASN   A OD1  1 
ATOM   6919 N  ND2  . ASN   A 1 1174 ? 187.908 204.685 167.189 1.00 56.00  ? 2506 ASN   A ND2  1 
ATOM   6920 N  N    . LEU   A 1 1175 ? 190.497 201.094 170.408 1.00 50.00  ? 2507 LEU   A N    1 
ATOM   6921 C  CA   . LEU   A 1 1175 ? 190.478 200.397 171.686 1.00 44.45  ? 2507 LEU   A CA   1 
ATOM   6922 C  C    . LEU   A 1 1175 ? 191.871 200.296 172.283 1.00 57.46  ? 2507 LEU   A C    1 
ATOM   6923 O  O    . LEU   A 1 1175 ? 192.026 200.380 173.503 1.00 72.19  ? 2507 LEU   A O    1 
ATOM   6924 C  CB   . LEU   A 1 1175 ? 189.867 199.010 171.542 1.00 42.24  ? 2507 LEU   A CB   1 
ATOM   6925 C  CG   . LEU   A 1 1175 ? 189.147 198.582 172.814 1.00 39.81  ? 2507 LEU   A CG   1 
ATOM   6926 C  CD1  . LEU   A 1 1175 ? 187.995 199.516 173.075 1.00 33.89  ? 2507 LEU   A CD1  1 
ATOM   6927 C  CD2  . LEU   A 1 1175 ? 188.666 197.163 172.709 1.00 41.88  ? 2507 LEU   A CD2  1 
ATOM   6928 N  N    . GLU   A 1 1176 ? 192.900 200.106 171.458 1.00 56.61  ? 2508 GLU   A N    1 
ATOM   6929 C  CA   . GLU   A 1 1176 ? 194.247 200.006 172.008 1.00 65.63  ? 2508 GLU   A CA   1 
ATOM   6930 C  C    . GLU   A 1 1176 ? 194.678 201.330 172.630 1.00 64.62  ? 2508 GLU   A C    1 
ATOM   6931 O  O    . GLU   A 1 1176 ? 195.213 201.363 173.747 1.00 64.82  ? 2508 GLU   A O    1 
ATOM   6932 C  CB   . GLU   A 1 1176 ? 195.222 199.567 170.915 1.00 75.55  ? 2508 GLU   A CB   1 
ATOM   6933 C  CG   . GLU   A 1 1176 ? 196.712 199.594 171.270 1.00 86.71  ? 2508 GLU   A CG   1 
ATOM   6934 C  CD   . GLU   A 1 1176 ? 197.036 199.193 172.704 1.00 91.00  ? 2508 GLU   A CD   1 
ATOM   6935 O  OE1  . GLU   A 1 1176 ? 198.041 199.704 173.235 1.00 93.44  ? 2508 GLU   A OE1  1 
ATOM   6936 O  OE2  . GLU   A 1 1176 ? 196.338 198.334 173.282 1.00 86.02  ? 2508 GLU   A OE2  1 
ATOM   6937 N  N    . LYS   A 1 1177 ? 194.433 202.439 171.928 1.00 60.23  ? 2509 LYS   A N    1 
ATOM   6938 C  CA   . LYS   A 1 1177 ? 194.748 203.750 172.487 1.00 61.95  ? 2509 LYS   A CA   1 
ATOM   6939 C  C    . LYS   A 1 1177 ? 193.932 204.020 173.742 1.00 63.96  ? 2509 LYS   A C    1 
ATOM   6940 O  O    . LYS   A 1 1177 ? 194.447 204.569 174.723 1.00 67.36  ? 2509 LYS   A O    1 
ATOM   6941 C  CB   . LYS   A 1 1177 ? 194.492 204.838 171.449 1.00 70.76  ? 2509 LYS   A CB   1 
ATOM   6942 C  CG   . LYS   A 1 1177 ? 194.874 206.224 171.918 1.00 81.97  ? 2509 LYS   A CG   1 
ATOM   6943 C  CD   . LYS   A 1 1177 ? 194.646 207.263 170.835 1.00 90.93  ? 2509 LYS   A CD   1 
ATOM   6944 C  CE   . LYS   A 1 1177 ? 195.124 208.628 171.294 1.00 98.22  ? 2509 LYS   A CE   1 
ATOM   6945 N  NZ   . LYS   A 1 1177 ? 194.288 209.152 172.405 1.00 93.92  ? 2509 LYS   A NZ   1 
ATOM   6946 N  N    . HIS   A 1 1178 ? 192.655 203.637 173.729 1.00 63.70  ? 2510 HIS   A N    1 
ATOM   6947 C  CA   . HIS   A 1 1178 ? 191.799 203.809 174.894 1.00 56.62  ? 2510 HIS   A CA   1 
ATOM   6948 C  C    . HIS   A 1 1178 ? 192.327 203.046 176.096 1.00 52.67  ? 2510 HIS   A C    1 
ATOM   6949 O  O    . HIS   A 1 1178 ? 192.353 203.573 177.212 1.00 61.67  ? 2510 HIS   A O    1 
ATOM   6950 C  CB   . HIS   A 1 1178 ? 190.395 203.339 174.551 1.00 49.86  ? 2510 HIS   A CB   1 
ATOM   6951 C  CG   . HIS   A 1 1178 ? 189.382 203.653 175.595 1.00 48.03  ? 2510 HIS   A CG   1 
ATOM   6952 N  ND1  . HIS   A 1 1178 ? 188.799 204.893 175.716 1.00 56.44  ? 2510 HIS   A ND1  1 
ATOM   6953 C  CD2  . HIS   A 1 1178 ? 188.830 202.879 176.556 1.00 44.81  ? 2510 HIS   A CD2  1 
ATOM   6954 C  CE1  . HIS   A 1 1178 ? 187.935 204.872 176.714 1.00 57.06  ? 2510 HIS   A CE1  1 
ATOM   6955 N  NE2  . HIS   A 1 1178 ? 187.933 203.661 177.238 1.00 55.63  ? 2510 HIS   A NE2  1 
ATOM   6956 N  N    . ILE   A 1 1179 ? 192.753 201.804 175.893 1.00 47.26  ? 2511 ILE   A N    1 
ATOM   6957 C  CA   . ILE   A 1 1179 ? 193.257 201.013 177.005 1.00 50.95  ? 2511 ILE   A CA   1 
ATOM   6958 C  C    . ILE   A 1 1179 ? 194.575 201.578 177.513 1.00 59.46  ? 2511 ILE   A C    1 
ATOM   6959 O  O    . ILE   A 1 1179 ? 194.845 201.555 178.717 1.00 62.42  ? 2511 ILE   A O    1 
ATOM   6960 C  CB   . ILE   A 1 1179 ? 193.376 199.537 176.596 1.00 53.39  ? 2511 ILE   A CB   1 
ATOM   6961 C  CG1  . ILE   A 1 1179 ? 191.982 198.930 176.484 1.00 45.08  ? 2511 ILE   A CG1  1 
ATOM   6962 C  CG2  . ILE   A 1 1179 ? 194.205 198.763 177.595 1.00 54.86  ? 2511 ILE   A CG2  1 
ATOM   6963 C  CD1  . ILE   A 1 1179 ? 191.157 199.075 177.735 1.00 40.36  ? 2511 ILE   A CD1  1 
ATOM   6964 N  N    . GLU   A 1 1180 ? 195.418 202.096 176.619 1.00 63.69  ? 2512 GLU   A N    1 
ATOM   6965 C  CA   . GLU   A 1 1180 ? 196.640 202.748 177.087 1.00 69.63  ? 2512 GLU   A CA   1 
ATOM   6966 C  C    . GLU   A 1 1180 ? 196.328 203.981 177.927 1.00 71.79  ? 2512 GLU   A C    1 
ATOM   6967 O  O    . GLU   A 1 1180 ? 196.969 204.219 178.961 1.00 77.47  ? 2512 GLU   A O    1 
ATOM   6968 C  CB   . GLU   A 1 1180 ? 197.539 203.118 175.909 1.00 76.92  ? 2512 GLU   A CB   1 
ATOM   6969 C  CG   . GLU   A 1 1180 ? 198.369 201.974 175.309 1.00 90.75  ? 2512 GLU   A CG   1 
ATOM   6970 C  CD   . GLU   A 1 1180 ? 199.268 201.220 176.295 1.00 96.90  ? 2512 GLU   A CD   1 
ATOM   6971 O  OE1  . GLU   A 1 1180 ? 200.086 200.407 175.818 1.00 95.99  ? 2512 GLU   A OE1  1 
ATOM   6972 O  OE2  . GLU   A 1 1180 ? 199.204 201.446 177.522 1.00 94.95  ? 2512 GLU   A OE2  1 
ATOM   6973 N  N    . VAL   A 1 1181 ? 195.351 204.782 177.495 1.00 69.60  ? 2513 VAL   A N    1 
ATOM   6974 C  CA   . VAL   A 1 1181 ? 194.952 205.951 178.275 1.00 66.97  ? 2513 VAL   A CA   1 
ATOM   6975 C  C    . VAL   A 1 1181 ? 194.450 205.530 179.646 1.00 67.90  ? 2513 VAL   A C    1 
ATOM   6976 O  O    . VAL   A 1 1181 ? 194.832 206.112 180.666 1.00 73.99  ? 2513 VAL   A O    1 
ATOM   6977 C  CB   . VAL   A 1 1181 ? 193.892 206.768 177.519 1.00 64.83  ? 2513 VAL   A CB   1 
ATOM   6978 C  CG1  . VAL   A 1 1181 ? 193.406 207.898 178.381 1.00 65.38  ? 2513 VAL   A CG1  1 
ATOM   6979 C  CG2  . VAL   A 1 1181 ? 194.476 207.323 176.246 1.00 76.97  ? 2513 VAL   A CG2  1 
ATOM   6980 N  N    . ARG   A 1 1182 ? 193.602 204.503 179.696 1.00 61.64  ? 2514 ARG   A N    1 
ATOM   6981 C  CA   . ARG   A 1 1182 ? 193.106 204.013 180.978 1.00 55.33  ? 2514 ARG   A CA   1 
ATOM   6982 C  C    . ARG   A 1 1182 ? 194.238 203.506 181.861 1.00 64.66  ? 2514 ARG   A C    1 
ATOM   6983 O  O    . ARG   A 1 1182 ? 194.247 203.755 183.068 1.00 73.85  ? 2514 ARG   A O    1 
ATOM   6984 C  CB   . ARG   A 1 1182 ? 192.085 202.905 180.758 1.00 49.57  ? 2514 ARG   A CB   1 
ATOM   6985 C  CG   . ARG   A 1 1182 ? 190.944 203.318 179.892 1.00 47.22  ? 2514 ARG   A CG   1 
ATOM   6986 C  CD   . ARG   A 1 1182 ? 190.074 204.311 180.600 1.00 34.77  ? 2514 ARG   A CD   1 
ATOM   6987 N  NE   . ARG   A 1 1182 ? 189.688 203.902 181.946 1.00 31.89  ? 2514 ARG   A NE   1 
ATOM   6988 C  CZ   . ARG   A 1 1182 ? 189.169 202.729 182.287 1.00 34.92  ? 2514 ARG   A CZ   1 
ATOM   6989 N  NH1  . ARG   A 1 1182 ? 188.923 201.786 181.395 1.00 35.39  ? 2514 ARG   A NH1  1 
ATOM   6990 N  NH2  . ARG   A 1 1182 ? 188.876 202.500 183.561 1.00 44.12  ? 2514 ARG   A NH2  1 
ATOM   6991 N  N    . LYS   A 1 1183 ? 195.191 202.777 181.286 1.00 67.90  ? 2515 LYS   A N    1 
ATOM   6992 C  CA   . LYS   A 1 1183 ? 196.274 202.222 182.088 1.00 74.73  ? 2515 LYS   A CA   1 
ATOM   6993 C  C    . LYS   A 1 1183 ? 197.130 203.327 182.692 1.00 84.24  ? 2515 LYS   A C    1 
ATOM   6994 O  O    . LYS   A 1 1183 ? 197.429 203.311 183.895 1.00 92.09  ? 2515 LYS   A O    1 
ATOM   6995 C  CB   . LYS   A 1 1183 ? 197.125 201.281 181.238 1.00 88.43  ? 2515 LYS   A CB   1 
ATOM   6996 C  CG   . LYS   A 1 1183 ? 198.558 201.135 181.720 1.00 101.70 ? 2515 LYS   A CG   1 
ATOM   6997 C  CD   . LYS   A 1 1183 ? 199.423 200.442 180.682 1.00 116.63 ? 2515 LYS   A CD   1 
ATOM   6998 C  CE   . LYS   A 1 1183 ? 199.035 198.983 180.530 1.00 133.47 ? 2515 LYS   A CE   1 
ATOM   6999 N  NZ   . LYS   A 1 1183 ? 199.123 198.252 181.823 1.00 138.34 ? 2515 LYS   A NZ   1 
ATOM   7000 N  N    . GLU   A 1 1184 ? 197.532 204.308 181.879 1.00 83.08  ? 2516 GLU   A N    1 
ATOM   7001 C  CA   . GLU   A 1 1184 ? 198.351 205.378 182.439 1.00 84.91  ? 2516 GLU   A CA   1 
ATOM   7002 C  C    . GLU   A 1 1184 ? 197.551 206.212 183.427 1.00 85.10  ? 2516 GLU   A C    1 
ATOM   7003 O  O    . GLU   A 1 1184 ? 198.093 206.671 184.436 1.00 91.31  ? 2516 GLU   A O    1 
ATOM   7004 C  CB   . GLU   A 1 1184 ? 198.943 206.268 181.346 1.00 81.29  ? 2516 GLU   A CB   1 
ATOM   7005 C  CG   . GLU   A 1 1184 ? 197.946 207.075 180.547 1.00 85.96  ? 2516 GLU   A CG   1 
ATOM   7006 C  CD   . GLU   A 1 1184 ? 198.613 207.885 179.458 1.00 99.70  ? 2516 GLU   A CD   1 
ATOM   7007 O  OE1  . GLU   A 1 1184 ? 199.850 207.791 179.326 1.00 114.88 ? 2516 GLU   A OE1  1 
ATOM   7008 O  OE2  . GLU   A 1 1184 ? 197.907 208.621 178.739 1.00 95.18  ? 2516 GLU   A OE2  1 
ATOM   7009 N  N    . LEU   A 1 1185 ? 196.258 206.411 183.164 1.00 80.66  ? 2517 LEU   A N    1 
ATOM   7010 C  CA   . LEU   A 1 1185 ? 195.425 207.170 184.085 1.00 76.11  ? 2517 LEU   A CA   1 
ATOM   7011 C  C    . LEU   A 1 1185 ? 195.320 206.470 185.431 1.00 82.81  ? 2517 LEU   A C    1 
ATOM   7012 O  O    . LEU   A 1 1185 ? 195.418 207.108 186.481 1.00 89.42  ? 2517 LEU   A O    1 
ATOM   7013 C  CB   . LEU   A 1 1185 ? 194.043 207.380 183.476 1.00 67.29  ? 2517 LEU   A CB   1 
ATOM   7014 C  CG   . LEU   A 1 1185 ? 193.150 208.378 184.196 1.00 69.82  ? 2517 LEU   A CG   1 
ATOM   7015 C  CD1  . LEU   A 1 1185 ? 193.772 209.750 184.127 1.00 77.47  ? 2517 LEU   A CD1  1 
ATOM   7016 C  CD2  . LEU   A 1 1185 ? 191.776 208.383 183.561 1.00 58.58  ? 2517 LEU   A CD2  1 
ATOM   7017 N  N    . ALA   A 1 1186 ? 195.132 205.150 185.419 1.00 82.23  ? 2518 ALA   A N    1 
ATOM   7018 C  CA   . ALA   A 1 1186 ? 195.060 204.401 186.668 1.00 84.42  ? 2518 ALA   A CA   1 
ATOM   7019 C  C    . ALA   A 1 1186 ? 196.381 204.456 187.420 1.00 98.40  ? 2518 ALA   A C    1 
ATOM   7020 O  O    . ALA   A 1 1186 ? 196.399 204.656 188.641 1.00 105.95 ? 2518 ALA   A O    1 
ATOM   7021 C  CB   . ALA   A 1 1186 ? 194.666 202.952 186.391 1.00 73.42  ? 2518 ALA   A CB   1 
ATOM   7022 N  N    . GLU   A 1 1187 ? 197.498 204.286 186.710 1.00 100.10 ? 2519 GLU   A N    1 
ATOM   7023 C  CA   . GLU   A 1 1187 ? 198.794 204.325 187.380 1.00 111.49 ? 2519 GLU   A CA   1 
ATOM   7024 C  C    . GLU   A 1 1187 ? 199.043 205.697 187.995 1.00 116.29 ? 2519 GLU   A C    1 
ATOM   7025 O  O    . GLU   A 1 1187 ? 199.487 205.804 189.143 1.00 117.56 ? 2519 GLU   A O    1 
ATOM   7026 C  CB   . GLU   A 1 1187 ? 199.903 203.928 186.397 1.00 115.13 ? 2519 GLU   A CB   1 
ATOM   7027 C  CG   . GLU   A 1 1187 ? 201.341 203.874 186.954 1.00 126.15 ? 2519 GLU   A CG   1 
ATOM   7028 C  CD   . GLU   A 1 1187 ? 202.028 205.228 187.119 1.00 125.71 ? 2519 GLU   A CD   1 
ATOM   7029 O  OE1  . GLU   A 1 1187 ? 201.440 206.275 186.779 1.00 119.93 ? 2519 GLU   A OE1  1 
ATOM   7030 O  OE2  . GLU   A 1 1187 ? 203.181 205.241 187.600 1.00 128.91 ? 2519 GLU   A OE2  1 
ATOM   7031 N  N    . LYS   A 1 1188 ? 198.752 206.763 187.246 1.00 112.46 ? 2520 LYS   A N    1 
ATOM   7032 C  CA   . LYS   A 1 1188 ? 198.960 208.109 187.766 1.00 113.59 ? 2520 LYS   A CA   1 
ATOM   7033 C  C    . LYS   A 1 1188 ? 198.023 208.414 188.923 1.00 117.65 ? 2520 LYS   A C    1 
ATOM   7034 O  O    . LYS   A 1 1188 ? 198.430 209.068 189.888 1.00 127.40 ? 2520 LYS   A O    1 
ATOM   7035 C  CB   . LYS   A 1 1188 ? 198.778 209.137 186.653 1.00 110.91 ? 2520 LYS   A CB   1 
ATOM   7036 C  CG   . LYS   A 1 1188 ? 199.114 210.553 187.065 1.00 115.90 ? 2520 LYS   A CG   1 
ATOM   7037 C  CD   . LYS   A 1 1188 ? 198.922 211.512 185.909 1.00 124.19 ? 2520 LYS   A CD   1 
ATOM   7038 C  CE   . LYS   A 1 1188 ? 199.995 211.303 184.855 1.00 128.21 ? 2520 LYS   A CE   1 
ATOM   7039 N  NZ   . LYS   A 1 1188 ? 201.347 211.683 185.352 1.00 126.27 ? 2520 LYS   A NZ   1 
ATOM   7040 N  N    . MET   A 1 1189 ? 196.773 207.958 188.845 1.00 112.00 ? 2521 MET   A N    1 
ATOM   7041 C  CA   . MET   A 1 1189 ? 195.831 208.164 189.936 1.00 109.73 ? 2521 MET   A CA   1 
ATOM   7042 C  C    . MET   A 1 1189 ? 196.321 207.487 191.207 1.00 111.32 ? 2521 MET   A C    1 
ATOM   7043 O  O    . MET   A 1 1189 ? 196.341 208.096 192.285 1.00 118.61 ? 2521 MET   A O    1 
ATOM   7044 C  CB   . MET   A 1 1189 ? 194.459 207.631 189.529 1.00 97.47  ? 2521 MET   A CB   1 
ATOM   7045 C  CG   . MET   A 1 1189 ? 193.450 207.587 190.641 1.00 87.47  ? 2521 MET   A CG   1 
ATOM   7046 S  SD   . MET   A 1 1189 ? 191.777 207.343 190.021 1.00 94.06  ? 2521 MET   A SD   1 
ATOM   7047 C  CE   . MET   A 1 1189 ? 191.664 208.641 188.796 1.00 51.61  ? 2521 MET   A CE   1 
ATOM   7048 N  N    . ARG   A 1 1190 ? 196.761 206.234 191.091 1.00 109.02 ? 2522 ARG   A N    1 
ATOM   7049 C  CA   . ARG   A 1 1190 ? 197.251 205.520 192.262 1.00 115.61 ? 2522 ARG   A CA   1 
ATOM   7050 C  C    . ARG   A 1 1190 ? 198.543 206.126 192.794 1.00 126.06 ? 2522 ARG   A C    1 
ATOM   7051 O  O    . ARG   A 1 1190 ? 198.764 206.127 194.008 1.00 130.10 ? 2522 ARG   A O    1 
ATOM   7052 C  CB   . ARG   A 1 1190 ? 197.437 204.041 191.927 1.00 117.17 ? 2522 ARG   A CB   1 
ATOM   7053 C  CG   . ARG   A 1 1190 ? 197.854 203.172 193.103 1.00 114.89 ? 2522 ARG   A CG   1 
ATOM   7054 C  CD   . ARG   A 1 1190 ? 198.704 201.975 192.663 1.00 115.69 ? 2522 ARG   A CD   1 
ATOM   7055 N  NE   . ARG   A 1 1190 ? 199.701 202.257 191.633 1.00 126.02 ? 2522 ARG   A NE   1 
ATOM   7056 C  CZ   . ARG   A 1 1190 ? 200.619 203.216 191.681 1.00 124.95 ? 2522 ARG   A CZ   1 
ATOM   7057 N  NH1  . ARG   A 1 1190 ? 200.764 203.987 192.746 1.00 123.79 ? 2522 ARG   A NH1  1 
ATOM   7058 N  NH2  . ARG   A 1 1190 ? 201.431 203.387 190.642 1.00 124.34 ? 2522 ARG   A NH2  1 
ATOM   7059 N  N    . ARG   A 1 1191 ? 199.403 206.647 191.918 1.00 126.50 ? 2523 ARG   A N    1 
ATOM   7060 C  CA   . ARG   A 1 1191 ? 200.661 207.223 192.384 1.00 133.35 ? 2523 ARG   A CA   1 
ATOM   7061 C  C    . ARG   A 1 1191 ? 200.433 208.556 193.086 1.00 137.30 ? 2523 ARG   A C    1 
ATOM   7062 O  O    . ARG   A 1 1191 ? 200.993 208.807 194.159 1.00 139.27 ? 2523 ARG   A O    1 
ATOM   7063 C  CB   . ARG   A 1 1191 ? 201.632 207.378 191.209 1.00 134.18 ? 2523 ARG   A CB   1 
ATOM   7064 C  CG   . ARG   A 1 1191 ? 202.952 208.084 191.525 1.00 138.61 ? 2523 ARG   A CG   1 
ATOM   7065 C  CD   . ARG   A 1 1191 ? 202.896 209.594 191.311 1.00 138.17 ? 2523 ARG   A CD   1 
ATOM   7066 N  NE   . ARG   A 1 1191 ? 202.795 209.953 189.902 1.00 140.34 ? 2523 ARG   A NE   1 
ATOM   7067 C  CZ   . ARG   A 1 1191 ? 202.934 211.186 189.432 1.00 144.94 ? 2523 ARG   A CZ   1 
ATOM   7068 N  NH1  . ARG   A 1 1191 ? 203.193 212.206 190.232 1.00 151.76 ? 2523 ARG   A NH1  1 
ATOM   7069 N  NH2  . ARG   A 1 1191 ? 202.813 211.399 188.125 1.00 142.41 ? 2523 ARG   A NH2  1 
ATOM   7070 N  N    . THR   A 1 1192 ? 199.616 209.427 192.492 1.00 134.17 ? 2524 THR   A N    1 
ATOM   7071 C  CA   . THR   A 1 1192 ? 199.438 210.770 193.030 1.00 135.50 ? 2524 THR   A CA   1 
ATOM   7072 C  C    . THR   A 1 1192 ? 198.530 210.781 194.253 1.00 142.18 ? 2524 THR   A C    1 
ATOM   7073 O  O    . THR   A 1 1192 ? 198.770 211.545 195.195 1.00 145.89 ? 2524 THR   A O    1 
ATOM   7074 C  CB   . THR   A 1 1192 ? 198.878 211.698 191.951 1.00 131.53 ? 2524 THR   A CB   1 
ATOM   7075 O  OG1  . THR   A 1 1192 ? 199.533 211.435 190.705 1.00 131.86 ? 2524 THR   A OG1  1 
ATOM   7076 C  CG2  . THR   A 1 1192 ? 199.092 213.152 192.334 1.00 128.19 ? 2524 THR   A CG2  1 
ATOM   7077 N  N    . SER   A 1 1193 ? 197.484 209.949 194.260 1.00 139.71 ? 2525 SER   A N    1 
ATOM   7078 C  CA   . SER   A 1 1193 ? 196.529 209.987 195.363 1.00 137.89 ? 2525 SER   A CA   1 
ATOM   7079 C  C    . SER   A 1 1193 ? 197.174 209.564 196.677 1.00 141.24 ? 2525 SER   A C    1 
ATOM   7080 O  O    . SER   A 1 1193 ? 196.906 210.158 197.727 1.00 142.44 ? 2525 SER   A O    1 
ATOM   7081 C  CB   . SER   A 1 1193 ? 195.323 209.109 195.041 1.00 123.82 ? 2525 SER   A CB   1 
ATOM   7082 O  OG   . SER   A 1 1193 ? 194.614 209.613 193.923 1.00 121.31 ? 2525 SER   A OG   1 
ATOM   7083 N  N    . VAL   A 1 1194 ? 198.023 208.542 196.643 1.00 143.99 ? 2526 VAL   A N    1 
ATOM   7084 C  CA   . VAL   A 1 1194 ? 198.698 208.092 197.853 1.00 147.95 ? 2526 VAL   A CA   1 
ATOM   7085 C  C    . VAL   A 1 1194 ? 200.159 208.528 197.828 1.00 150.38 ? 2526 VAL   A C    1 
ATOM   7086 O  O    . VAL   A 1 1194 ? 200.514 209.578 198.363 1.00 148.53 ? 2526 VAL   A O    1 
ATOM   7087 C  CB   . VAL   A 1 1194 ? 198.589 206.566 198.024 1.00 145.63 ? 2526 VAL   A CB   1 
ATOM   7088 C  CG1  . VAL   A 1 1194 ? 197.144 206.113 197.867 1.00 132.41 ? 2526 VAL   A CG1  1 
ATOM   7089 C  CG2  . VAL   A 1 1194 ? 199.505 205.850 197.045 1.00 138.49 ? 2526 VAL   A CG2  1 
ATOM   7090 N  N    . PRO   B 2 52   ? 219.497 175.941 151.618 1.00 129.35 ? 52   PRO   B N    1 
ATOM   7091 C  CA   . PRO   B 2 52   ? 220.201 174.683 151.351 1.00 128.15 ? 52   PRO   B CA   1 
ATOM   7092 C  C    . PRO   B 2 52   ? 219.408 173.738 150.451 1.00 121.86 ? 52   PRO   B C    1 
ATOM   7093 O  O    . PRO   B 2 52   ? 219.249 174.006 149.259 1.00 114.57 ? 52   PRO   B O    1 
ATOM   7094 C  CB   . PRO   B 2 52   ? 220.382 174.086 152.746 1.00 128.24 ? 52   PRO   B CB   1 
ATOM   7095 C  CG   . PRO   B 2 52   ? 219.255 174.651 153.543 1.00 117.47 ? 52   PRO   B CG   1 
ATOM   7096 C  CD   . PRO   B 2 52   ? 219.037 176.035 153.016 1.00 116.41 ? 52   PRO   B CD   1 
ATOM   7097 N  N    . LEU   B 2 53   ? 218.913 172.643 151.031 1.00 120.82 ? 53   LEU   B N    1 
ATOM   7098 C  CA   . LEU   B 2 53   ? 218.179 171.655 150.250 1.00 115.23 ? 53   LEU   B CA   1 
ATOM   7099 C  C    . LEU   B 2 53   ? 216.849 172.210 149.763 1.00 120.58 ? 53   LEU   B C    1 
ATOM   7100 O  O    . LEU   B 2 53   ? 216.382 171.861 148.676 1.00 122.84 ? 53   LEU   B O    1 
ATOM   7101 C  CB   . LEU   B 2 53   ? 217.967 170.384 151.071 1.00 108.65 ? 53   LEU   B CB   1 
ATOM   7102 C  CG   . LEU   B 2 53   ? 217.269 169.212 150.380 1.00 95.49  ? 53   LEU   B CG   1 
ATOM   7103 C  CD1  . LEU   B 2 53   ? 218.073 168.704 149.198 1.00 98.45  ? 53   LEU   B CD1  1 
ATOM   7104 C  CD2  . LEU   B 2 53   ? 217.054 168.104 151.384 1.00 103.83 ? 53   LEU   B CD2  1 
ATOM   7105 N  N    . HIS   B 2 54   ? 216.223 173.086 150.552 1.00 121.67 ? 54   HIS   B N    1 
ATOM   7106 C  CA   . HIS   B 2 54   ? 214.955 173.676 150.136 1.00 118.75 ? 54   HIS   B CA   1 
ATOM   7107 C  C    . HIS   B 2 54   ? 215.076 174.403 148.801 1.00 115.44 ? 54   HIS   B C    1 
ATOM   7108 O  O    . HIS   B 2 54   ? 214.270 174.190 147.891 1.00 111.13 ? 54   HIS   B O    1 
ATOM   7109 C  CB   . HIS   B 2 54   ? 214.440 174.629 151.216 1.00 119.22 ? 54   HIS   B CB   1 
ATOM   7110 C  CG   . HIS   B 2 54   ? 214.465 174.053 152.597 1.00 117.64 ? 54   HIS   B CG   1 
ATOM   7111 N  ND1  . HIS   B 2 54   ? 215.625 173.911 153.327 1.00 112.95 ? 54   HIS   B ND1  1 
ATOM   7112 C  CD2  . HIS   B 2 54   ? 213.464 173.605 153.390 1.00 118.21 ? 54   HIS   B CD2  1 
ATOM   7113 C  CE1  . HIS   B 2 54   ? 215.338 173.387 154.505 1.00 118.63 ? 54   HIS   B CE1  1 
ATOM   7114 N  NE2  . HIS   B 2 54   ? 214.034 173.194 154.569 1.00 117.71 ? 54   HIS   B NE2  1 
ATOM   7115 N  N    . LEU   B 2 55   ? 216.085 175.264 148.666 1.00 120.73 ? 55   LEU   B N    1 
ATOM   7116 C  CA   . LEU   B 2 55   ? 216.291 175.969 147.404 1.00 124.22 ? 55   LEU   B CA   1 
ATOM   7117 C  C    . LEU   B 2 55   ? 216.880 175.052 146.339 1.00 118.25 ? 55   LEU   B C    1 
ATOM   7118 O  O    . LEU   B 2 55   ? 216.528 175.149 145.158 1.00 114.34 ? 55   LEU   B O    1 
ATOM   7119 C  CB   . LEU   B 2 55   ? 217.171 177.203 147.617 1.00 131.18 ? 55   LEU   B CB   1 
ATOM   7120 C  CG   . LEU   B 2 55   ? 216.776 178.143 148.759 1.00 130.49 ? 55   LEU   B CG   1 
ATOM   7121 C  CD1  . LEU   B 2 55   ? 217.491 177.815 150.054 1.00 124.06 ? 55   LEU   B CD1  1 
ATOM   7122 C  CD2  . LEU   B 2 55   ? 217.040 179.587 148.354 1.00 122.58 ? 55   LEU   B CD2  1 
ATOM   7123 N  N    . ALA   B 2 56   ? 217.784 174.150 146.730 1.00 115.09 ? 56   ALA   B N    1 
ATOM   7124 C  CA   . ALA   B 2 56   ? 218.345 173.220 145.757 1.00 113.57 ? 56   ALA   B CA   1 
ATOM   7125 C  C    . ALA   B 2 56   ? 217.292 172.280 145.192 1.00 107.59 ? 56   ALA   B C    1 
ATOM   7126 O  O    . ALA   B 2 56   ? 217.529 171.642 144.162 1.00 111.88 ? 56   ALA   B O    1 
ATOM   7127 C  CB   . ALA   B 2 56   ? 219.479 172.413 146.389 1.00 119.96 ? 56   ALA   B CB   1 
ATOM   7128 N  N    . ALA   B 2 57   ? 216.151 172.165 145.854 1.00 100.76 ? 57   ALA   B N    1 
ATOM   7129 C  CA   . ALA   B 2 57   ? 215.058 171.316 145.418 1.00 94.51  ? 57   ALA   B CA   1 
ATOM   7130 C  C    . ALA   B 2 57   ? 214.021 172.057 144.589 1.00 111.20 ? 57   ALA   B C    1 
ATOM   7131 O  O    . ALA   B 2 57   ? 212.889 171.577 144.475 1.00 111.32 ? 57   ALA   B O    1 
ATOM   7132 C  CB   . ALA   B 2 57   ? 214.394 170.685 146.637 1.00 94.34  ? 57   ALA   B CB   1 
ATOM   7133 N  N    . ASP   B 2 58   ? 214.370 173.212 144.023 1.00 120.66 ? 58   ASP   B N    1 
ATOM   7134 C  CA   . ASP   B 2 58   ? 213.482 173.965 143.146 1.00 113.52 ? 58   ASP   B CA   1 
ATOM   7135 C  C    . ASP   B 2 58   ? 213.952 173.925 141.699 1.00 110.22 ? 58   ASP   B C    1 
ATOM   7136 O  O    . ASP   B 2 58   ? 213.200 173.523 140.809 1.00 109.19 ? 58   ASP   B O    1 
ATOM   7137 C  CB   . ASP   B 2 58   ? 213.383 175.421 143.611 1.00 116.03 ? 58   ASP   B CB   1 
ATOM   7138 C  CG   . ASP   B 2 58   ? 212.643 175.564 144.906 1.00 123.48 ? 58   ASP   B CG   1 
ATOM   7139 O  OD1  . ASP   B 2 58   ? 211.756 174.730 145.168 1.00 125.21 ? 58   ASP   B OD1  1 
ATOM   7140 O  OD2  . ASP   B 2 58   ? 212.967 176.492 145.669 1.00 125.09 ? 58   ASP   B OD2  1 
ATOM   7141 N  N    . SER   B 2 59   ? 215.181 174.362 141.442 1.00 113.24 ? 59   SER   B N    1 
ATOM   7142 C  CA   . SER   B 2 59   ? 215.703 174.306 140.086 1.00 115.75 ? 59   SER   B CA   1 
ATOM   7143 C  C    . SER   B 2 59   ? 216.158 172.895 139.737 1.00 111.11 ? 59   SER   B C    1 
ATOM   7144 O  O    . SER   B 2 59   ? 215.963 172.434 138.607 1.00 116.37 ? 59   SER   B O    1 
ATOM   7145 C  CB   . SER   B 2 59   ? 216.838 175.310 139.934 1.00 115.99 ? 59   SER   B CB   1 
ATOM   7146 O  OG   . SER   B 2 59   ? 216.368 176.636 140.108 1.00 108.27 ? 59   SER   B OG   1 
ATOM   7147 N  N    . GLY   B 2 60   ? 216.765 172.197 140.690 1.00 105.59 ? 60   GLY   B N    1 
ATOM   7148 C  CA   . GLY   B 2 60   ? 217.057 170.793 140.514 1.00 108.42 ? 60   GLY   B CA   1 
ATOM   7149 C  C    . GLY   B 2 60   ? 218.370 170.468 139.846 1.00 118.33 ? 60   GLY   B C    1 
ATOM   7150 O  O    . GLY   B 2 60   ? 218.426 169.526 139.049 1.00 121.23 ? 60   GLY   B O    1 
ATOM   7151 N  N    . HIS   B 2 61   ? 219.433 171.211 140.142 1.00 122.60 ? 61   HIS   B N    1 
ATOM   7152 C  CA   . HIS   B 2 61   ? 220.731 170.899 139.558 1.00 127.40 ? 61   HIS   B CA   1 
ATOM   7153 C  C    . HIS   B 2 61   ? 221.258 169.575 140.094 1.00 135.17 ? 61   HIS   B C    1 
ATOM   7154 O  O    . HIS   B 2 61   ? 221.149 169.284 141.289 1.00 136.07 ? 61   HIS   B O    1 
ATOM   7155 C  CB   . HIS   B 2 61   ? 221.741 172.011 139.839 1.00 123.35 ? 61   HIS   B CB   1 
ATOM   7156 C  CG   . HIS   B 2 61   ? 221.233 173.387 139.549 1.00 122.88 ? 61   HIS   B CG   1 
ATOM   7157 N  ND1  . HIS   B 2 61   ? 220.220 173.980 140.270 1.00 118.75 ? 61   HIS   B ND1  1 
ATOM   7158 C  CD2  . HIS   B 2 61   ? 221.596 174.284 138.603 1.00 132.80 ? 61   HIS   B CD2  1 
ATOM   7159 C  CE1  . HIS   B 2 61   ? 219.993 175.189 139.791 1.00 127.23 ? 61   HIS   B CE1  1 
ATOM   7160 N  NE2  . HIS   B 2 61   ? 220.809 175.396 138.774 1.00 133.21 ? 61   HIS   B NE2  1 
ATOM   7161 N  N    . LEU   B 2 62   ? 221.836 168.774 139.200 1.00 133.71 ? 62   LEU   B N    1 
ATOM   7162 C  CA   . LEU   B 2 62   ? 222.510 167.552 139.623 1.00 131.12 ? 62   LEU   B CA   1 
ATOM   7163 C  C    . LEU   B 2 62   ? 223.680 167.871 140.542 1.00 131.97 ? 62   LEU   B C    1 
ATOM   7164 O  O    . LEU   B 2 62   ? 223.900 167.188 141.547 1.00 128.51 ? 62   LEU   B O    1 
ATOM   7165 C  CB   . LEU   B 2 62   ? 222.990 166.770 138.398 1.00 135.05 ? 62   LEU   B CB   1 
ATOM   7166 C  CG   . LEU   B 2 62   ? 222.024 165.843 137.655 1.00 133.21 ? 62   LEU   B CG   1 
ATOM   7167 C  CD1  . LEU   B 2 62   ? 221.596 164.706 138.557 1.00 131.02 ? 62   LEU   B CD1  1 
ATOM   7168 C  CD2  . LEU   B 2 62   ? 220.808 166.594 137.128 1.00 134.29 ? 62   LEU   B CD2  1 
ATOM   7169 N  N    . GLU   B 2 63   ? 224.442 168.916 140.212 1.00 134.56 ? 63   GLU   B N    1 
ATOM   7170 C  CA   . GLU   B 2 63   ? 225.620 169.254 141.003 1.00 134.48 ? 63   GLU   B CA   1 
ATOM   7171 C  C    . GLU   B 2 63   ? 225.241 169.668 142.419 1.00 138.38 ? 63   GLU   B C    1 
ATOM   7172 O  O    . GLU   B 2 63   ? 225.932 169.315 143.380 1.00 142.31 ? 63   GLU   B O    1 
ATOM   7173 C  CB   . GLU   B 2 63   ? 226.413 170.364 140.312 1.00 130.04 ? 63   GLU   B CB   1 
ATOM   7174 N  N    . ILE   B 2 64   ? 224.147 170.419 142.569 1.00 137.73 ? 64   ILE   B N    1 
ATOM   7175 C  CA   . ILE   B 2 64   ? 223.751 170.900 143.892 1.00 134.62 ? 64   ILE   B CA   1 
ATOM   7176 C  C    . ILE   B 2 64   ? 223.392 169.732 144.800 1.00 135.20 ? 64   ILE   B C    1 
ATOM   7177 O  O    . ILE   B 2 64   ? 223.885 169.623 145.929 1.00 139.23 ? 64   ILE   B O    1 
ATOM   7178 C  CB   . ILE   B 2 64   ? 222.584 171.896 143.775 1.00 135.20 ? 64   ILE   B CB   1 
ATOM   7179 N  N    . VAL   B 2 65   ? 222.530 168.835 144.315 1.00 135.11 ? 65   VAL   B N    1 
ATOM   7180 C  CA   . VAL   B 2 65   ? 222.123 167.694 145.122 1.00 139.87 ? 65   VAL   B CA   1 
ATOM   7181 C  C    . VAL   B 2 65   ? 223.262 166.697 145.313 1.00 139.69 ? 65   VAL   B C    1 
ATOM   7182 O  O    . VAL   B 2 65   ? 223.296 165.987 146.325 1.00 126.96 ? 65   VAL   B O    1 
ATOM   7183 C  CB   . VAL   B 2 65   ? 220.878 167.036 144.499 1.00 135.83 ? 65   VAL   B CB   1 
ATOM   7184 C  CG1  . VAL   B 2 65   ? 219.724 168.022 144.491 1.00 120.15 ? 65   VAL   B CG1  1 
ATOM   7185 C  CG2  . VAL   B 2 65   ? 221.175 166.570 143.087 1.00 134.04 ? 65   VAL   B CG2  1 
ATOM   7186 N  N    . GLU   B 2 66   ? 224.200 166.622 144.364 1.00 141.41 ? 66   GLU   B N    1 
ATOM   7187 C  CA   . GLU   B 2 66   ? 225.372 165.772 144.542 1.00 137.87 ? 66   GLU   B CA   1 
ATOM   7188 C  C    . GLU   B 2 66   ? 226.306 166.316 145.613 1.00 138.37 ? 66   GLU   B C    1 
ATOM   7189 O  O    . GLU   B 2 66   ? 226.858 165.544 146.404 1.00 138.53 ? 66   GLU   B O    1 
ATOM   7190 C  CB   . GLU   B 2 66   ? 226.120 165.627 143.217 1.00 135.98 ? 66   GLU   B CB   1 
ATOM   7191 N  N    . VAL   B 2 67   ? 226.513 167.632 145.643 1.00 140.82 ? 67   VAL   B N    1 
ATOM   7192 C  CA   . VAL   B 2 67   ? 227.317 168.229 146.702 1.00 142.61 ? 67   VAL   B CA   1 
ATOM   7193 C  C    . VAL   B 2 67   ? 226.625 168.056 148.046 1.00 143.84 ? 67   VAL   B C    1 
ATOM   7194 O  O    . VAL   B 2 67   ? 227.272 167.783 149.064 1.00 140.12 ? 67   VAL   B O    1 
ATOM   7195 C  CB   . VAL   B 2 67   ? 227.597 169.710 146.391 1.00 137.46 ? 67   VAL   B CB   1 
ATOM   7196 N  N    . LEU   B 2 68   ? 225.299 168.212 148.071 1.00 144.46 ? 68   LEU   B N    1 
ATOM   7197 C  CA   . LEU   B 2 68   ? 224.553 167.949 149.295 1.00 140.47 ? 68   LEU   B CA   1 
ATOM   7198 C  C    . LEU   B 2 68   ? 224.586 166.470 149.651 1.00 146.09 ? 68   LEU   B C    1 
ATOM   7199 O  O    . LEU   B 2 68   ? 224.439 166.102 150.822 1.00 151.05 ? 68   LEU   B O    1 
ATOM   7200 C  CB   . LEU   B 2 68   ? 223.112 168.431 149.152 1.00 135.29 ? 68   LEU   B CB   1 
ATOM   7201 C  CG   . LEU   B 2 68   ? 222.824 169.791 149.780 1.00 128.57 ? 68   LEU   B CG   1 
ATOM   7202 C  CD1  . LEU   B 2 68   ? 223.632 170.884 149.103 1.00 135.43 ? 68   LEU   B CD1  1 
ATOM   7203 C  CD2  . LEU   B 2 68   ? 221.347 170.094 149.707 1.00 114.79 ? 68   LEU   B CD2  1 
ATOM   7204 N  N    . LEU   B 2 69   ? 224.771 165.604 148.653 1.00 145.15 ? 69   LEU   B N    1 
ATOM   7205 C  CA   . LEU   B 2 69   ? 224.867 164.174 148.926 1.00 151.24 ? 69   LEU   B CA   1 
ATOM   7206 C  C    . LEU   B 2 69   ? 226.092 163.859 149.775 1.00 154.44 ? 69   LEU   B C    1 
ATOM   7207 O  O    . LEU   B 2 69   ? 226.022 163.054 150.711 1.00 161.07 ? 69   LEU   B O    1 
ATOM   7208 C  CB   . LEU   B 2 69   ? 224.901 163.389 147.615 1.00 150.30 ? 69   LEU   B CB   1 
ATOM   7209 N  N    . LYS   B 2 70   ? 227.230 164.482 149.461 1.00 150.31 ? 70   LYS   B N    1 
ATOM   7210 C  CA   . LYS   B 2 70   ? 228.428 164.257 150.260 1.00 146.10 ? 70   LYS   B CA   1 
ATOM   7211 C  C    . LYS   B 2 70   ? 228.242 164.763 151.686 1.00 150.22 ? 70   LYS   B C    1 
ATOM   7212 O  O    . LYS   B 2 70   ? 228.469 164.024 152.650 1.00 152.58 ? 70   LYS   B O    1 
ATOM   7213 C  CB   . LYS   B 2 70   ? 229.632 164.930 149.600 1.00 129.54 ? 70   LYS   B CB   1 
ATOM   7214 N  N    . THR   B 2 71   ? 227.824 166.018 151.839 1.00 147.60 ? 71   THR   B N    1 
ATOM   7215 C  CA   . THR   B 2 71   ? 227.583 166.598 153.154 1.00 148.77 ? 71   THR   B CA   1 
ATOM   7216 C  C    . THR   B 2 71   ? 226.302 167.416 153.096 1.00 147.42 ? 71   THR   B C    1 
ATOM   7217 O  O    . THR   B 2 71   ? 225.985 168.027 152.074 1.00 146.50 ? 71   THR   B O    1 
ATOM   7218 C  CB   . THR   B 2 71   ? 228.747 167.487 153.620 1.00 149.32 ? 71   THR   B CB   1 
ATOM   7219 O  OG1  . THR   B 2 71   ? 228.691 168.748 152.941 1.00 148.69 ? 71   THR   B OG1  1 
ATOM   7220 C  CG2  . THR   B 2 71   ? 230.101 166.830 153.361 1.00 145.40 ? 71   THR   B CG2  1 
ATOM   7221 N  N    . GLY   B 2 72   ? 225.578 167.437 154.212 1.00 146.94 ? 72   GLY   B N    1 
ATOM   7222 C  CA   . GLY   B 2 72   ? 224.378 168.258 154.279 1.00 142.38 ? 72   GLY   B CA   1 
ATOM   7223 C  C    . GLY   B 2 72   ? 223.536 167.951 155.500 1.00 138.96 ? 72   GLY   B C    1 
ATOM   7224 O  O    . GLY   B 2 72   ? 224.017 167.364 156.476 1.00 141.03 ? 72   GLY   B O    1 
ATOM   7225 N  N    . ALA   B 2 73   ? 222.268 168.360 155.428 1.00 135.66 ? 73   ALA   B N    1 
ATOM   7226 C  CA   . ALA   B 2 73   ? 221.300 168.131 156.494 1.00 134.44 ? 73   ALA   B CA   1 
ATOM   7227 C  C    . ALA   B 2 73   ? 220.071 167.448 155.914 1.00 123.64 ? 73   ALA   B C    1 
ATOM   7228 O  O    . ALA   B 2 73   ? 218.932 167.832 156.198 1.00 117.52 ? 73   ALA   B O    1 
ATOM   7229 C  CB   . ALA   B 2 73   ? 220.919 169.445 157.177 1.00 134.15 ? 73   ALA   B CB   1 
ATOM   7230 N  N    . ASP   B 2 74   ? 220.312 166.424 155.101 1.00 122.42 ? 74   ASP   B N    1 
ATOM   7231 C  CA   . ASP   B 2 74   ? 219.289 165.781 154.287 1.00 114.81 ? 74   ASP   B CA   1 
ATOM   7232 C  C    . ASP   B 2 74   ? 218.099 165.234 155.071 1.00 113.28 ? 74   ASP   B C    1 
ATOM   7233 O  O    . ASP   B 2 74   ? 218.258 164.592 156.114 1.00 116.32 ? 74   ASP   B O    1 
ATOM   7234 C  CB   . ASP   B 2 74   ? 219.960 164.699 153.430 1.00 117.17 ? 74   ASP   B CB   1 
ATOM   7235 C  CG   . ASP   B 2 74   ? 220.636 163.611 154.257 1.00 125.19 ? 74   ASP   B CG   1 
ATOM   7236 O  OD1  . ASP   B 2 74   ? 220.641 163.696 155.501 1.00 128.62 ? 74   ASP   B OD1  1 
ATOM   7237 O  OD2  . ASP   B 2 74   ? 221.185 162.669 153.649 1.00 122.88 ? 74   ASP   B OD2  1 
ATOM   7238 N  N    . VAL   B 2 75   ? 216.899 165.518 154.559 1.00 108.42 ? 75   VAL   B N    1 
ATOM   7239 C  CA   . VAL   B 2 75   ? 215.609 165.105 155.107 1.00 108.28 ? 75   VAL   B CA   1 
ATOM   7240 C  C    . VAL   B 2 75   ? 215.621 165.400 156.607 1.00 109.05 ? 75   VAL   B C    1 
ATOM   7241 O  O    . VAL   B 2 75   ? 215.024 164.685 157.418 1.00 108.65 ? 75   VAL   B O    1 
ATOM   7242 C  CB   . VAL   B 2 75   ? 215.341 163.619 154.773 1.00 101.15 ? 75   VAL   B CB   1 
ATOM   7243 C  CG1  . VAL   B 2 75   ? 214.031 163.107 155.360 1.00 97.82  ? 75   VAL   B CG1  1 
ATOM   7244 C  CG2  . VAL   B 2 75   ? 215.384 163.391 153.274 1.00 102.78 ? 75   VAL   B CG2  1 
ATOM   7245 N  N    . ASN   B 2 76   ? 216.304 166.482 156.992 1.00 112.45 ? 76   ASN   B N    1 
ATOM   7246 C  CA   . ASN   B 2 76   ? 216.509 166.727 158.416 1.00 123.14 ? 76   ASN   B CA   1 
ATOM   7247 C  C    . ASN   B 2 76   ? 216.302 168.186 158.805 1.00 130.26 ? 76   ASN   B C    1 
ATOM   7248 O  O    . ASN   B 2 76   ? 216.764 168.594 159.877 1.00 133.95 ? 76   ASN   B O    1 
ATOM   7249 C  CB   . ASN   B 2 76   ? 217.919 166.289 158.834 1.00 124.93 ? 76   ASN   B CB   1 
ATOM   7250 N  N    . ALA   B 2 77   ? 215.632 168.979 157.979 1.00 125.20 ? 77   ALA   B N    1 
ATOM   7251 C  CA   . ALA   B 2 77   ? 215.462 170.395 158.241 1.00 126.76 ? 77   ALA   B CA   1 
ATOM   7252 C  C    . ALA   B 2 77   ? 214.017 170.805 158.003 1.00 128.34 ? 77   ALA   B C    1 
ATOM   7253 O  O    . ALA   B 2 77   ? 213.266 170.143 157.282 1.00 121.45 ? 77   ALA   B O    1 
ATOM   7254 C  CB   . ALA   B 2 77   ? 216.397 171.240 157.366 1.00 118.45 ? 77   ALA   B CB   1 
ATOM   7255 N  N    . TRP   B 2 78   ? 213.635 171.901 158.650 1.00 134.79 ? 78   TRP   B N    1 
ATOM   7256 C  CA   . TRP   B 2 78   ? 212.381 172.586 158.380 1.00 128.99 ? 78   TRP   B CA   1 
ATOM   7257 C  C    . TRP   B 2 78   ? 212.686 174.065 158.201 1.00 131.54 ? 78   TRP   B C    1 
ATOM   7258 O  O    . TRP   B 2 78   ? 213.331 174.677 159.059 1.00 130.79 ? 78   TRP   B O    1 
ATOM   7259 C  CB   . TRP   B 2 78   ? 211.370 172.372 159.510 1.00 118.81 ? 78   TRP   B CB   1 
ATOM   7260 N  N    . ASP   B 2 79   ? 212.231 174.633 157.087 1.00 126.70 ? 79   ASP   B N    1 
ATOM   7261 C  CA   . ASP   B 2 79   ? 212.434 176.043 156.800 1.00 124.24 ? 79   ASP   B CA   1 
ATOM   7262 C  C    . ASP   B 2 79   ? 211.450 176.879 157.613 1.00 129.56 ? 79   ASP   B C    1 
ATOM   7263 O  O    . ASP   B 2 79   ? 210.714 176.364 158.456 1.00 133.62 ? 79   ASP   B O    1 
ATOM   7264 C  CB   . ASP   B 2 79   ? 212.282 176.297 155.304 1.00 117.29 ? 79   ASP   B CB   1 
ATOM   7265 C  CG   . ASP   B 2 79   ? 210.890 175.980 154.802 1.00 120.72 ? 79   ASP   B CG   1 
ATOM   7266 O  OD1  . ASP   B 2 79   ? 210.501 176.510 153.742 1.00 128.98 ? 79   ASP   B OD1  1 
ATOM   7267 O  OD2  . ASP   B 2 79   ? 210.181 175.203 155.473 1.00 116.63 ? 79   ASP   B OD2  1 
ATOM   7268 N  N    . HIS   B 2 80   ? 211.422 178.189 157.353 1.00 129.79 ? 80   HIS   B N    1 
ATOM   7269 C  CA   . HIS   B 2 80   ? 210.491 179.054 158.070 1.00 133.34 ? 80   HIS   B CA   1 
ATOM   7270 C  C    . HIS   B 2 80   ? 209.049 178.612 157.874 1.00 128.56 ? 80   HIS   B C    1 
ATOM   7271 O  O    . HIS   B 2 80   ? 208.201 178.877 158.734 1.00 120.25 ? 80   HIS   B O    1 
ATOM   7272 C  CB   . HIS   B 2 80   ? 210.637 180.513 157.621 1.00 133.18 ? 80   HIS   B CB   1 
ATOM   7273 C  CG   . HIS   B 2 80   ? 212.051 181.002 157.572 1.00 134.05 ? 80   HIS   B CG   1 
ATOM   7274 N  ND1  . HIS   B 2 80   ? 212.406 182.176 156.945 1.00 129.58 ? 80   HIS   B ND1  1 
ATOM   7275 C  CD2  . HIS   B 2 80   ? 213.195 180.488 158.082 1.00 134.62 ? 80   HIS   B CD2  1 
ATOM   7276 C  CE1  . HIS   B 2 80   ? 213.709 182.361 157.064 1.00 126.76 ? 80   HIS   B CE1  1 
ATOM   7277 N  NE2  . HIS   B 2 80   ? 214.211 181.350 157.749 1.00 131.05 ? 80   HIS   B NE2  1 
ATOM   7278 N  N    . TYR   B 2 81   ? 208.761 177.937 156.765 1.00 128.88 ? 81   TYR   B N    1 
ATOM   7279 C  CA   . TYR   B 2 81   ? 207.434 177.431 156.442 1.00 122.91 ? 81   TYR   B CA   1 
ATOM   7280 C  C    . TYR   B 2 81   ? 207.210 176.011 156.934 1.00 117.52 ? 81   TYR   B C    1 
ATOM   7281 O  O    . TYR   B 2 81   ? 206.065 175.618 157.164 1.00 116.14 ? 81   TYR   B O    1 
ATOM   7282 C  CB   . TYR   B 2 81   ? 207.197 177.488 154.927 1.00 118.74 ? 81   TYR   B CB   1 
ATOM   7283 C  CG   . TYR   B 2 81   ? 207.581 178.798 154.274 1.00 115.15 ? 81   TYR   B CG   1 
ATOM   7284 C  CD1  . TYR   B 2 81   ? 206.621 179.744 153.967 1.00 109.92 ? 81   TYR   B CD1  1 
ATOM   7285 C  CD2  . TYR   B 2 81   ? 208.906 179.093 153.976 1.00 124.54 ? 81   TYR   B CD2  1 
ATOM   7286 C  CE1  . TYR   B 2 81   ? 206.966 180.941 153.373 1.00 116.93 ? 81   TYR   B CE1  1 
ATOM   7287 C  CE2  . TYR   B 2 81   ? 209.261 180.292 153.388 1.00 123.37 ? 81   TYR   B CE2  1 
ATOM   7288 C  CZ   . TYR   B 2 81   ? 208.288 181.211 153.089 1.00 117.91 ? 81   TYR   B CZ   1 
ATOM   7289 O  OH   . TYR   B 2 81   ? 208.632 182.402 152.500 1.00 111.73 ? 81   TYR   B OH   1 
ATOM   7290 N  N    . GLY   B 2 82   ? 208.267 175.222 157.079 1.00 114.45 ? 82   GLY   B N    1 
ATOM   7291 C  CA   . GLY   B 2 82   ? 208.133 173.875 157.584 1.00 115.94 ? 82   GLY   B CA   1 
ATOM   7292 C  C    . GLY   B 2 82   ? 207.983 172.802 156.531 1.00 112.87 ? 82   GLY   B C    1 
ATOM   7293 O  O    . GLY   B 2 82   ? 207.685 171.656 156.885 1.00 112.22 ? 82   GLY   B O    1 
ATOM   7294 N  N    . PHE   B 2 83   ? 208.168 173.129 155.256 1.00 112.36 ? 83   PHE   B N    1 
ATOM   7295 C  CA   . PHE   B 2 83   ? 208.088 172.117 154.214 1.00 109.45 ? 83   PHE   B CA   1 
ATOM   7296 C  C    . PHE   B 2 83   ? 209.224 171.113 154.305 1.00 104.33 ? 83   PHE   B C    1 
ATOM   7297 O  O    . PHE   B 2 83   ? 210.367 171.449 154.624 1.00 102.74 ? 83   PHE   B O    1 
ATOM   7298 C  CB   . PHE   B 2 83   ? 208.113 172.751 152.828 1.00 116.68 ? 83   PHE   B CB   1 
ATOM   7299 C  CG   . PHE   B 2 83   ? 206.781 173.204 152.355 1.00 116.62 ? 83   PHE   B CG   1 
ATOM   7300 C  CD1  . PHE   B 2 83   ? 205.661 173.026 153.145 1.00 107.38 ? 83   PHE   B CD1  1 
ATOM   7301 C  CD2  . PHE   B 2 83   ? 206.642 173.782 151.114 1.00 111.34 ? 83   PHE   B CD2  1 
ATOM   7302 C  CE1  . PHE   B 2 83   ? 204.437 173.434 152.712 1.00 95.22  ? 83   PHE   B CE1  1 
ATOM   7303 C  CE2  . PHE   B 2 83   ? 205.419 174.186 150.679 1.00 102.53 ? 83   PHE   B CE2  1 
ATOM   7304 C  CZ   . PHE   B 2 83   ? 204.319 174.015 151.481 1.00 92.72  ? 83   PHE   B CZ   1 
ATOM   7305 N  N    . THR   B 2 84   ? 208.896 169.872 154.007 1.00 102.42 ? 84   THR   B N    1 
ATOM   7306 C  CA   . THR   B 2 84   ? 209.927 168.881 153.772 1.00 105.80 ? 84   THR   B CA   1 
ATOM   7307 C  C    . THR   B 2 84   ? 210.620 169.192 152.454 1.00 107.56 ? 84   THR   B C    1 
ATOM   7308 O  O    . THR   B 2 84   ? 209.961 169.224 151.410 1.00 112.27 ? 84   THR   B O    1 
ATOM   7309 C  CB   . THR   B 2 84   ? 209.317 167.489 153.725 1.00 108.61 ? 84   THR   B CB   1 
ATOM   7310 O  OG1  . THR   B 2 84   ? 208.372 167.426 152.648 1.00 99.70  ? 84   THR   B OG1  1 
ATOM   7311 C  CG2  . THR   B 2 84   ? 208.618 167.178 155.029 1.00 120.28 ? 84   THR   B CG2  1 
ATOM   7312 N  N    . PRO   B 2 85   ? 211.934 169.420 152.453 1.00 104.82 ? 85   PRO   B N    1 
ATOM   7313 C  CA   . PRO   B 2 85   ? 212.617 169.705 151.183 1.00 106.22 ? 85   PRO   B CA   1 
ATOM   7314 C  C    . PRO   B 2 85   ? 212.458 168.597 150.167 1.00 105.44 ? 85   PRO   B C    1 
ATOM   7315 O  O    . PRO   B 2 85   ? 212.409 168.867 148.959 1.00 112.67 ? 85   PRO   B O    1 
ATOM   7316 C  CB   . PRO   B 2 85   ? 214.078 169.873 151.607 1.00 98.44  ? 85   PRO   B CB   1 
ATOM   7317 C  CG   . PRO   B 2 85   ? 214.012 170.258 153.033 1.00 103.94 ? 85   PRO   B CG   1 
ATOM   7318 C  CD   . PRO   B 2 85   ? 212.846 169.516 153.602 1.00 100.16 ? 85   PRO   B CD   1 
ATOM   7319 N  N    . LEU   B 2 86   ? 212.370 167.352 150.627 1.00 99.57  ? 86   LEU   B N    1 
ATOM   7320 C  CA   . LEU   B 2 86   ? 212.102 166.252 149.715 1.00 102.44 ? 86   LEU   B CA   1 
ATOM   7321 C  C    . LEU   B 2 86   ? 210.784 166.443 148.986 1.00 120.05 ? 86   LEU   B C    1 
ATOM   7322 O  O    . LEU   B 2 86   ? 210.739 166.420 147.752 1.00 132.76 ? 86   LEU   B O    1 
ATOM   7323 C  CB   . LEU   B 2 86   ? 212.115 164.929 150.469 1.00 111.59 ? 86   LEU   B CB   1 
ATOM   7324 C  CG   . LEU   B 2 86   ? 211.876 163.698 149.597 1.00 126.78 ? 86   LEU   B CG   1 
ATOM   7325 C  CD1  . LEU   B 2 86   ? 212.938 163.509 148.541 1.00 118.90 ? 86   LEU   B CD1  1 
ATOM   7326 C  CD2  . LEU   B 2 86   ? 211.821 162.483 150.497 1.00 142.61 ? 86   LEU   B CD2  1 
ATOM   7327 N  N    . HIS   B 2 87   ? 209.691 166.645 149.715 1.00 123.78 ? 87   HIS   B N    1 
ATOM   7328 C  CA   . HIS   B 2 87   ? 208.478 166.668 148.917 1.00 137.37 ? 87   HIS   B CA   1 
ATOM   7329 C  C    . HIS   B 2 87   ? 208.203 168.067 148.365 1.00 127.40 ? 87   HIS   B C    1 
ATOM   7330 O  O    . HIS   B 2 87   ? 207.404 168.214 147.429 1.00 120.69 ? 87   HIS   B O    1 
ATOM   7331 C  CB   . HIS   B 2 87   ? 207.284 166.141 149.705 1.00 135.20 ? 87   HIS   B CB   1 
ATOM   7332 C  CG   . HIS   B 2 87   ? 206.050 166.028 148.874 1.00 140.73 ? 87   HIS   B CG   1 
ATOM   7333 N  ND1  . HIS   B 2 87   ? 205.900 165.025 147.942 1.00 137.76 ? 87   HIS   B ND1  1 
ATOM   7334 C  CD2  . HIS   B 2 87   ? 204.936 166.786 148.794 1.00 142.74 ? 87   HIS   B CD2  1 
ATOM   7335 C  CE1  . HIS   B 2 87   ? 204.745 165.166 147.323 1.00 132.94 ? 87   HIS   B CE1  1 
ATOM   7336 N  NE2  . HIS   B 2 87   ? 204.133 166.218 147.832 1.00 141.32 ? 87   HIS   B NE2  1 
ATOM   7337 N  N    . LEU   B 2 88   ? 208.871 169.086 148.908 1.00 117.17 ? 88   LEU   B N    1 
ATOM   7338 C  CA   . LEU   B 2 88   ? 209.082 170.315 148.157 1.00 112.08 ? 88   LEU   B CA   1 
ATOM   7339 C  C    . LEU   B 2 88   ? 209.533 169.988 146.744 1.00 117.71 ? 88   LEU   B C    1 
ATOM   7340 O  O    . LEU   B 2 88   ? 208.835 170.291 145.770 1.00 126.42 ? 88   LEU   B O    1 
ATOM   7341 C  CB   . LEU   B 2 88   ? 210.127 171.178 148.870 1.00 106.12 ? 88   LEU   B CB   1 
ATOM   7342 C  CG   . LEU   B 2 88   ? 210.453 172.600 148.420 1.00 100.19 ? 88   LEU   B CG   1 
ATOM   7343 C  CD1  . LEU   B 2 88   ? 210.966 173.402 149.593 1.00 104.08 ? 88   LEU   B CD1  1 
ATOM   7344 C  CD2  . LEU   B 2 88   ? 211.494 172.583 147.331 1.00 101.05 ? 88   LEU   B CD2  1 
ATOM   7345 N  N    . ALA   B 2 89   ? 210.686 169.317 146.622 1.00 116.18 ? 89   ALA   B N    1 
ATOM   7346 C  CA   . ALA   B 2 89   ? 211.198 168.940 145.309 1.00 113.01 ? 89   ALA   B CA   1 
ATOM   7347 C  C    . ALA   B 2 89   ? 210.199 168.080 144.560 1.00 111.66 ? 89   ALA   B C    1 
ATOM   7348 O  O    . ALA   B 2 89   ? 210.144 168.107 143.325 1.00 119.60 ? 89   ALA   B O    1 
ATOM   7349 C  CB   . ALA   B 2 89   ? 212.520 168.192 145.449 1.00 107.69 ? 89   ALA   B CB   1 
ATOM   7350 N  N    . ALA   B 2 90   ? 209.425 167.284 145.288 1.00 102.93 ? 90   ALA   B N    1 
ATOM   7351 C  CA   . ALA   B 2 90   ? 208.469 166.409 144.625 1.00 118.68 ? 90   ALA   B CA   1 
ATOM   7352 C  C    . ALA   B 2 90   ? 207.379 167.200 143.916 1.00 133.45 ? 90   ALA   B C    1 
ATOM   7353 O  O    . ALA   B 2 90   ? 207.058 166.914 142.756 1.00 150.07 ? 90   ALA   B O    1 
ATOM   7354 C  CB   . ALA   B 2 90   ? 207.858 165.439 145.623 1.00 127.69 ? 90   ALA   B CB   1 
ATOM   7355 N  N    . HIS   B 2 91   ? 206.791 168.194 144.582 1.00 127.60 ? 91   HIS   B N    1 
ATOM   7356 C  CA   . HIS   B 2 91   ? 205.689 168.884 143.916 1.00 131.19 ? 91   HIS   B CA   1 
ATOM   7357 C  C    . HIS   B 2 91   ? 206.147 170.068 143.083 1.00 116.28 ? 91   HIS   B C    1 
ATOM   7358 O  O    . HIS   B 2 91   ? 205.362 170.569 142.274 1.00 108.84 ? 91   HIS   B O    1 
ATOM   7359 C  CB   . HIS   B 2 91   ? 204.628 169.386 144.894 1.00 131.93 ? 91   HIS   B CB   1 
ATOM   7360 C  CG   . HIS   B 2 91   ? 205.091 170.474 145.812 1.00 136.33 ? 91   HIS   B CG   1 
ATOM   7361 N  ND1  . HIS   B 2 91   ? 205.822 170.236 146.956 1.00 137.52 ? 91   HIS   B ND1  1 
ATOM   7362 C  CD2  . HIS   B 2 91   ? 204.882 171.811 145.769 1.00 130.32 ? 91   HIS   B CD2  1 
ATOM   7363 C  CE1  . HIS   B 2 91   ? 206.056 171.383 147.570 1.00 134.07 ? 91   HIS   B CE1  1 
ATOM   7364 N  NE2  . HIS   B 2 91   ? 205.497 172.354 146.870 1.00 133.20 ? 91   HIS   B NE2  1 
ATOM   7365 N  N    . VAL   B 2 92   ? 207.389 170.526 143.249 1.00 110.69 ? 92   VAL   B N    1 
ATOM   7366 C  CA   . VAL   B 2 92   ? 207.924 171.489 142.301 1.00 105.23 ? 92   VAL   B CA   1 
ATOM   7367 C  C    . VAL   B 2 92   ? 208.030 170.852 140.925 1.00 107.45 ? 92   VAL   B C    1 
ATOM   7368 O  O    . VAL   B 2 92   ? 208.008 171.557 139.910 1.00 118.01 ? 92   VAL   B O    1 
ATOM   7369 C  CB   . VAL   B 2 92   ? 209.279 172.039 142.804 1.00 103.58 ? 92   VAL   B CB   1 
ATOM   7370 C  CG1  . VAL   B 2 92   ? 210.005 172.801 141.721 1.00 104.63 ? 92   VAL   B CG1  1 
ATOM   7371 C  CG2  . VAL   B 2 92   ? 209.087 172.921 144.012 1.00 109.30 ? 92   VAL   B CG2  1 
ATOM   7372 N  N    . GLY   B 2 93   ? 208.054 169.521 140.870 1.00 105.13 ? 93   GLY   B N    1 
ATOM   7373 C  CA   . GLY   B 2 93   ? 207.994 168.790 139.622 1.00 117.14 ? 93   GLY   B CA   1 
ATOM   7374 C  C    . GLY   B 2 93   ? 209.295 168.206 139.114 1.00 125.13 ? 93   GLY   B C    1 
ATOM   7375 O  O    . GLY   B 2 93   ? 209.622 168.355 137.933 1.00 128.66 ? 93   GLY   B O    1 
ATOM   7376 N  N    . HIS   B 2 94   ? 210.043 167.529 139.982 1.00 119.66 ? 94   HIS   B N    1 
ATOM   7377 C  CA   . HIS   B 2 94   ? 211.235 166.806 139.565 1.00 120.93 ? 94   HIS   B CA   1 
ATOM   7378 C  C    . HIS   B 2 94   ? 211.072 165.318 139.817 1.00 125.91 ? 94   HIS   B C    1 
ATOM   7379 O  O    . HIS   B 2 94   ? 210.139 164.878 140.495 1.00 122.66 ? 94   HIS   B O    1 
ATOM   7380 C  CB   . HIS   B 2 94   ? 212.498 167.273 140.282 1.00 111.69 ? 94   HIS   B CB   1 
ATOM   7381 C  CG   . HIS   B 2 94   ? 212.667 168.752 140.311 1.00 97.07  ? 94   HIS   B CG   1 
ATOM   7382 N  ND1  . HIS   B 2 94   ? 211.955 169.562 141.165 1.00 95.87  ? 94   HIS   B ND1  1 
ATOM   7383 C  CD2  . HIS   B 2 94   ? 213.465 169.571 139.587 1.00 95.84  ? 94   HIS   B CD2  1 
ATOM   7384 C  CE1  . HIS   B 2 94   ? 212.315 170.816 140.973 1.00 100.84 ? 94   HIS   B CE1  1 
ATOM   7385 N  NE2  . HIS   B 2 94   ? 213.224 170.851 140.017 1.00 98.31  ? 94   HIS   B NE2  1 
ATOM   7386 N  N    . LEU   B 2 95   ? 211.991 164.547 139.238 1.00 131.19 ? 95   LEU   B N    1 
ATOM   7387 C  CA   . LEU   B 2 95   ? 212.094 163.117 139.478 1.00 126.98 ? 95   LEU   B CA   1 
ATOM   7388 C  C    . LEU   B 2 95   ? 213.440 162.736 140.083 1.00 123.36 ? 95   LEU   B C    1 
ATOM   7389 O  O    . LEU   B 2 95   ? 213.490 162.121 141.155 1.00 115.03 ? 95   LEU   B O    1 
ATOM   7390 C  CB   . LEU   B 2 95   ? 211.867 162.360 138.166 1.00 126.09 ? 95   LEU   B CB   1 
ATOM   7391 C  CG   . LEU   B 2 95   ? 211.882 160.842 138.286 1.00 121.39 ? 95   LEU   B CG   1 
ATOM   7392 C  CD1  . LEU   B 2 95   ? 210.749 160.405 139.185 1.00 116.27 ? 95   LEU   B CD1  1 
ATOM   7393 C  CD2  . LEU   B 2 95   ? 211.770 160.197 136.914 1.00 119.25 ? 95   LEU   B CD2  1 
ATOM   7394 N  N    . GLU   B 2 96   ? 214.544 163.104 139.423 1.00 128.25 ? 96   GLU   B N    1 
ATOM   7395 C  CA   . GLU   B 2 96   ? 215.839 162.585 139.842 1.00 127.32 ? 96   GLU   B CA   1 
ATOM   7396 C  C    . GLU   B 2 96   ? 216.271 163.191 141.167 1.00 128.70 ? 96   GLU   B C    1 
ATOM   7397 O  O    . GLU   B 2 96   ? 216.885 162.500 141.985 1.00 128.11 ? 96   GLU   B O    1 
ATOM   7398 C  CB   . GLU   B 2 96   ? 216.900 162.814 138.755 1.00 125.20 ? 96   GLU   B CB   1 
ATOM   7399 C  CG   . GLU   B 2 96   ? 217.418 164.240 138.527 1.00 129.39 ? 96   GLU   B CG   1 
ATOM   7400 C  CD   . GLU   B 2 96   ? 218.417 164.691 139.591 1.00 132.40 ? 96   GLU   B CD   1 
ATOM   7401 O  OE1  . GLU   B 2 96   ? 218.986 163.820 140.281 1.00 134.54 ? 96   GLU   B OE1  1 
ATOM   7402 O  OE2  . GLU   B 2 96   ? 218.678 165.904 139.707 1.00 131.41 ? 96   GLU   B OE2  1 
ATOM   7403 N  N    . ILE   B 2 97   ? 215.957 164.469 141.398 1.00 128.56 ? 97   ILE   B N    1 
ATOM   7404 C  CA   . ILE   B 2 97   ? 216.271 165.090 142.682 1.00 125.92 ? 97   ILE   B CA   1 
ATOM   7405 C  C    . ILE   B 2 97   ? 215.548 164.356 143.797 1.00 123.48 ? 97   ILE   B C    1 
ATOM   7406 O  O    . ILE   B 2 97   ? 216.122 164.058 144.855 1.00 119.10 ? 97   ILE   B O    1 
ATOM   7407 C  CB   . ILE   B 2 97   ? 215.897 166.583 142.673 1.00 123.41 ? 97   ILE   B CB   1 
ATOM   7408 C  CG1  . ILE   B 2 97   ? 216.702 167.354 141.628 1.00 121.08 ? 97   ILE   B CG1  1 
ATOM   7409 C  CG2  . ILE   B 2 97   ? 216.101 167.182 144.053 1.00 119.80 ? 97   ILE   B CG2  1 
ATOM   7410 C  CD1  . ILE   B 2 97   ? 216.049 167.392 140.257 1.00 111.56 ? 97   ILE   B CD1  1 
ATOM   7411 N  N    . VAL   B 2 98   ? 214.277 164.037 143.564 1.00 125.09 ? 98   VAL   B N    1 
ATOM   7412 C  CA   . VAL   B 2 98   ? 213.484 163.357 144.576 1.00 129.19 ? 98   VAL   B CA   1 
ATOM   7413 C  C    . VAL   B 2 98   ? 214.053 161.972 144.859 1.00 130.63 ? 98   VAL   B C    1 
ATOM   7414 O  O    . VAL   B 2 98   ? 214.172 161.563 146.017 1.00 127.59 ? 98   VAL   B O    1 
ATOM   7415 C  CB   . VAL   B 2 98   ? 212.016 163.286 144.139 1.00 126.49 ? 98   VAL   B CB   1 
ATOM   7416 C  CG1  . VAL   B 2 98   ? 211.178 162.752 145.265 1.00 115.32 ? 98   VAL   B CG1  1 
ATOM   7417 C  CG2  . VAL   B 2 98   ? 211.543 164.652 143.697 1.00 126.58 ? 98   VAL   B CG2  1 
ATOM   7418 N  N    . GLU   B 2 99   ? 214.428 161.228 143.812 1.00 129.81 ? 99   GLU   B N    1 
ATOM   7419 C  CA   . GLU   B 2 99   ? 214.921 159.875 144.066 1.00 123.09 ? 99   GLU   B CA   1 
ATOM   7420 C  C    . GLU   B 2 99   ? 216.290 159.893 144.741 1.00 119.01 ? 99   GLU   B C    1 
ATOM   7421 O  O    . GLU   B 2 99   ? 216.544 159.090 145.648 1.00 114.01 ? 99   GLU   B O    1 
ATOM   7422 C  CB   . GLU   B 2 99   ? 214.960 159.046 142.779 1.00 125.23 ? 99   GLU   B CB   1 
ATOM   7423 C  CG   . GLU   B 2 99   ? 215.716 159.647 141.617 1.00 126.61 ? 99   GLU   B CG   1 
ATOM   7424 C  CD   . GLU   B 2 99   ? 217.197 159.314 141.637 1.00 123.12 ? 99   GLU   B CD   1 
ATOM   7425 O  OE1  . GLU   B 2 99   ? 218.000 160.126 141.131 1.00 120.92 ? 99   GLU   B OE1  1 
ATOM   7426 O  OE2  . GLU   B 2 99   ? 217.558 158.236 142.151 1.00 122.60 ? 99   GLU   B OE2  1 
ATOM   7427 N  N    . VAL   B 2 100  ? 217.185 160.802 144.335 1.00 120.13 ? 100  VAL   B N    1 
ATOM   7428 C  CA   . VAL   B 2 100  ? 218.498 160.835 144.971 1.00 112.83 ? 100  VAL   B CA   1 
ATOM   7429 C  C    . VAL   B 2 100  ? 218.358 161.245 146.428 1.00 110.83 ? 100  VAL   B C    1 
ATOM   7430 O  O    . VAL   B 2 100  ? 219.078 160.746 147.299 1.00 109.43 ? 100  VAL   B O    1 
ATOM   7431 C  CB   . VAL   B 2 100  ? 219.473 161.761 144.217 1.00 106.50 ? 100  VAL   B CB   1 
ATOM   7432 C  CG1  . VAL   B 2 100  ? 218.916 163.148 144.079 1.00 110.82 ? 100  VAL   B CG1  1 
ATOM   7433 C  CG2  . VAL   B 2 100  ? 220.813 161.813 144.926 1.00 102.78 ? 100  VAL   B CG2  1 
ATOM   7434 N  N    . LEU   B 2 101  ? 217.419 162.143 146.724 1.00 113.61 ? 101  LEU   B N    1 
ATOM   7435 C  CA   . LEU   B 2 101  ? 217.212 162.521 148.114 1.00 114.96 ? 101  LEU   B CA   1 
ATOM   7436 C  C    . LEU   B 2 101  ? 216.477 161.432 148.894 1.00 120.68 ? 101  LEU   B C    1 
ATOM   7437 O  O    . LEU   B 2 101  ? 216.587 161.376 150.124 1.00 119.76 ? 101  LEU   B O    1 
ATOM   7438 C  CB   . LEU   B 2 101  ? 216.484 163.860 148.167 1.00 116.90 ? 101  LEU   B CB   1 
ATOM   7439 C  CG   . LEU   B 2 101  ? 216.235 164.465 149.538 1.00 118.86 ? 101  LEU   B CG   1 
ATOM   7440 C  CD1  . LEU   B 2 101  ? 217.560 164.734 150.204 1.00 119.74 ? 101  LEU   B CD1  1 
ATOM   7441 C  CD2  . LEU   B 2 101  ? 215.502 165.760 149.332 1.00 106.17 ? 101  LEU   B CD2  1 
ATOM   7442 N  N    . LEU   B 2 102  ? 215.725 160.565 148.205 1.00 124.24 ? 102  LEU   B N    1 
ATOM   7443 C  CA   . LEU   B 2 102  ? 215.195 159.359 148.839 1.00 129.86 ? 102  LEU   B CA   1 
ATOM   7444 C  C    . LEU   B 2 102  ? 216.278 158.352 149.196 1.00 131.44 ? 102  LEU   B C    1 
ATOM   7445 O  O    . LEU   B 2 102  ? 216.234 157.768 150.284 1.00 129.22 ? 102  LEU   B O    1 
ATOM   7446 C  CB   . LEU   B 2 102  ? 214.165 158.670 147.937 1.00 133.67 ? 102  LEU   B CB   1 
ATOM   7447 C  CG   . LEU   B 2 102  ? 212.825 159.322 147.634 1.00 131.67 ? 102  LEU   B CG   1 
ATOM   7448 C  CD1  . LEU   B 2 102  ? 212.065 158.514 146.596 1.00 130.73 ? 102  LEU   B CD1  1 
ATOM   7449 C  CD2  . LEU   B 2 102  ? 212.037 159.351 148.925 1.00 126.55 ? 102  LEU   B CD2  1 
ATOM   7450 N  N    . LYS   B 2 103  ? 217.253 158.132 148.314 1.00 128.65 ? 103  LYS   B N    1 
ATOM   7451 C  CA   . LYS   B 2 103  ? 218.229 157.097 148.621 1.00 127.67 ? 103  LYS   B CA   1 
ATOM   7452 C  C    . LYS   B 2 103  ? 219.170 157.497 149.749 1.00 131.81 ? 103  LYS   B C    1 
ATOM   7453 O  O    . LYS   B 2 103  ? 219.950 156.656 150.207 1.00 133.68 ? 103  LYS   B O    1 
ATOM   7454 C  CB   . LYS   B 2 103  ? 219.043 156.701 147.386 1.00 115.74 ? 103  LYS   B CB   1 
ATOM   7455 C  CG   . LYS   B 2 103  ? 220.103 157.686 146.930 1.00 111.33 ? 103  LYS   B CG   1 
ATOM   7456 C  CD   . LYS   B 2 103  ? 220.783 157.146 145.672 1.00 111.58 ? 103  LYS   B CD   1 
ATOM   7457 C  CE   . LYS   B 2 103  ? 221.714 158.149 145.010 1.00 106.95 ? 103  LYS   B CE   1 
ATOM   7458 N  NZ   . LYS   B 2 103  ? 221.050 158.847 143.884 1.00 98.57  ? 103  LYS   B NZ   1 
ATOM   7459 N  N    . ALA   B 2 104  ? 219.129 158.753 150.198 1.00 130.19 ? 104  ALA   B N    1 
ATOM   7460 C  CA   . ALA   B 2 104  ? 219.861 159.168 151.384 1.00 122.87 ? 104  ALA   B CA   1 
ATOM   7461 C  C    . ALA   B 2 104  ? 218.967 159.479 152.574 1.00 122.66 ? 104  ALA   B C    1 
ATOM   7462 O  O    . ALA   B 2 104  ? 219.460 159.483 153.705 1.00 125.60 ? 104  ALA   B O    1 
ATOM   7463 C  CB   . ALA   B 2 104  ? 220.726 160.398 151.077 1.00 121.33 ? 104  ALA   B CB   1 
ATOM   7464 N  N    . GLY   B 2 105  ? 217.682 159.744 152.356 1.00 124.36 ? 105  GLY   B N    1 
ATOM   7465 C  CA   . GLY   B 2 105  ? 216.791 160.054 153.457 1.00 127.43 ? 105  GLY   B CA   1 
ATOM   7466 C  C    . GLY   B 2 105  ? 215.788 158.967 153.784 1.00 136.92 ? 105  GLY   B C    1 
ATOM   7467 O  O    . GLY   B 2 105  ? 215.544 158.679 154.959 1.00 133.93 ? 105  GLY   B O    1 
ATOM   7468 N  N    . ALA   B 2 106  ? 215.209 158.356 152.751 1.00 143.17 ? 106  ALA   B N    1 
ATOM   7469 C  CA   . ALA   B 2 106  ? 214.240 157.272 152.900 1.00 145.56 ? 106  ALA   B CA   1 
ATOM   7470 C  C    . ALA   B 2 106  ? 213.081 157.667 153.815 1.00 153.86 ? 106  ALA   B C    1 
ATOM   7471 O  O    . ALA   B 2 106  ? 212.718 156.945 154.745 1.00 155.54 ? 106  ALA   B O    1 
ATOM   7472 C  CB   . ALA   B 2 106  ? 214.921 156.000 153.405 1.00 146.39 ? 106  ALA   B CB   1 
ATOM   7473 N  N    . ASP   B 2 107  ? 212.486 158.827 153.542 1.00 154.81 ? 107  ASP   B N    1 
ATOM   7474 C  CA   . ASP   B 2 107  ? 211.332 159.305 154.292 1.00 143.86 ? 107  ASP   B CA   1 
ATOM   7475 C  C    . ASP   B 2 107  ? 210.217 159.578 153.295 1.00 143.22 ? 107  ASP   B C    1 
ATOM   7476 O  O    . ASP   B 2 107  ? 210.451 160.190 152.249 1.00 139.92 ? 107  ASP   B O    1 
ATOM   7477 C  CB   . ASP   B 2 107  ? 211.690 160.561 155.101 1.00 128.51 ? 107  ASP   B CB   1 
ATOM   7478 C  CG   . ASP   B 2 107  ? 210.475 161.318 155.648 1.00 126.34 ? 107  ASP   B CG   1 
ATOM   7479 O  OD1  . ASP   B 2 107  ? 210.707 162.260 156.432 1.00 126.80 ? 107  ASP   B OD1  1 
ATOM   7480 O  OD2  . ASP   B 2 107  ? 209.307 160.975 155.369 1.00 126.92 ? 107  ASP   B OD2  1 
ATOM   7481 N  N    . VAL   B 2 108  ? 209.011 159.114 153.617 1.00 146.94 ? 108  VAL   B N    1 
ATOM   7482 C  CA   . VAL   B 2 108  ? 207.853 159.288 152.747 1.00 150.91 ? 108  VAL   B CA   1 
ATOM   7483 C  C    . VAL   B 2 108  ? 206.739 159.975 153.527 1.00 148.21 ? 108  VAL   B C    1 
ATOM   7484 O  O    . VAL   B 2 108  ? 205.880 160.646 152.946 1.00 154.02 ? 108  VAL   B O    1 
ATOM   7485 C  CB   . VAL   B 2 108  ? 207.395 157.937 152.166 1.00 147.76 ? 108  VAL   B CB   1 
ATOM   7486 C  CG1  . VAL   B 2 108  ? 206.130 158.091 151.347 1.00 148.42 ? 108  VAL   B CG1  1 
ATOM   7487 C  CG2  . VAL   B 2 108  ? 208.487 157.364 151.302 1.00 148.49 ? 108  VAL   B CG2  1 
ATOM   7488 N  N    . ASN   B 2 109  ? 206.755 159.836 154.844 1.00 144.12 ? 109  ASN   B N    1 
ATOM   7489 C  CA   . ASN   B 2 109  ? 205.772 160.483 155.706 1.00 148.98 ? 109  ASN   B CA   1 
ATOM   7490 C  C    . ASN   B 2 109  ? 206.481 161.487 156.606 1.00 146.46 ? 109  ASN   B C    1 
ATOM   7491 O  O    . ASN   B 2 109  ? 207.249 161.108 157.494 1.00 147.94 ? 109  ASN   B O    1 
ATOM   7492 C  CB   . ASN   B 2 109  ? 204.992 159.460 156.523 1.00 155.01 ? 109  ASN   B CB   1 
ATOM   7493 C  CG   . ASN   B 2 109  ? 204.131 158.568 155.663 1.00 153.66 ? 109  ASN   B CG   1 
ATOM   7494 O  OD1  . ASN   B 2 109  ? 204.419 158.351 154.487 1.00 148.13 ? 109  ASN   B OD1  1 
ATOM   7495 N  ND2  . ASN   B 2 109  ? 203.042 158.072 156.237 1.00 151.85 ? 109  ASN   B ND2  1 
ATOM   7496 N  N    . ALA   B 2 110  ? 206.226 162.768 156.362 1.00 141.80 ? 110  ALA   B N    1 
ATOM   7497 C  CA   . ALA   B 2 110  ? 206.657 163.842 157.244 1.00 144.02 ? 110  ALA   B CA   1 
ATOM   7498 C  C    . ALA   B 2 110  ? 205.701 165.012 157.083 1.00 144.43 ? 110  ALA   B C    1 
ATOM   7499 O  O    . ALA   B 2 110  ? 205.436 165.452 155.960 1.00 142.21 ? 110  ALA   B O    1 
ATOM   7500 C  CB   . ALA   B 2 110  ? 208.095 164.269 156.945 1.00 142.77 ? 110  ALA   B CB   1 
ATOM   7501 N  N    . GLN   B 2 111  ? 205.186 165.512 158.199 1.00 141.71 ? 111  GLN   B N    1 
ATOM   7502 C  CA   . GLN   B 2 111  ? 204.194 166.572 158.164 1.00 133.69 ? 111  GLN   B CA   1 
ATOM   7503 C  C    . GLN   B 2 111  ? 204.865 167.941 158.101 1.00 137.28 ? 111  GLN   B C    1 
ATOM   7504 O  O    . GLN   B 2 111  ? 206.088 168.077 158.191 1.00 136.83 ? 111  GLN   B O    1 
ATOM   7505 C  CB   . GLN   B 2 111  ? 203.274 166.481 159.381 1.00 120.42 ? 111  GLN   B CB   1 
ATOM   7506 N  N    . ASP   B 2 112  ? 204.034 168.967 157.949 1.00 135.83 ? 112  ASP   B N    1 
ATOM   7507 C  CA   . ASP   B 2 112  ? 204.484 170.351 157.867 1.00 125.38 ? 112  ASP   B CA   1 
ATOM   7508 C  C    . ASP   B 2 112  ? 203.503 171.197 158.669 1.00 121.64 ? 112  ASP   B C    1 
ATOM   7509 O  O    . ASP   B 2 112  ? 202.700 170.677 159.449 1.00 126.94 ? 112  ASP   B O    1 
ATOM   7510 C  CB   . ASP   B 2 112  ? 204.604 170.811 156.410 1.00 118.66 ? 112  ASP   B CB   1 
ATOM   7511 C  CG   . ASP   B 2 112  ? 203.293 170.722 155.665 1.00 125.60 ? 112  ASP   B CG   1 
ATOM   7512 O  OD1  . ASP   B 2 112  ? 202.302 170.234 156.247 1.00 127.47 ? 112  ASP   B OD1  1 
ATOM   7513 O  OD2  . ASP   B 2 112  ? 203.248 171.168 154.501 1.00 127.71 ? 112  ASP   B OD2  1 
ATOM   7514 N  N    A HIS   B 2 113  ? 203.572 172.516 158.473 0.49 115.46 ? 113  HIS   B N    1 
ATOM   7515 N  N    B HIS   B 2 113  ? 203.559 172.516 158.475 0.51 115.44 ? 113  HIS   B N    1 
ATOM   7516 C  CA   A HIS   B 2 113  ? 202.725 173.424 159.240 0.49 113.83 ? 113  HIS   B CA   1 
ATOM   7517 C  CA   B HIS   B 2 113  ? 202.721 173.410 159.266 0.51 113.82 ? 113  HIS   B CA   1 
ATOM   7518 C  C    A HIS   B 2 113  ? 201.249 173.137 159.008 0.49 112.82 ? 113  HIS   B C    1 
ATOM   7519 C  C    B HIS   B 2 113  ? 201.239 173.163 159.009 0.51 112.78 ? 113  HIS   B C    1 
ATOM   7520 O  O    A HIS   B 2 113  ? 200.456 173.120 159.955 0.49 111.50 ? 113  HIS   B O    1 
ATOM   7521 O  O    B HIS   B 2 113  ? 200.428 173.202 159.941 0.51 111.46 ? 113  HIS   B O    1 
ATOM   7522 C  CB   A HIS   B 2 113  ? 203.044 174.872 158.880 0.49 111.40 ? 113  HIS   B CB   1 
ATOM   7523 C  CB   B HIS   B 2 113  ? 203.091 174.865 158.984 0.51 111.38 ? 113  HIS   B CB   1 
ATOM   7524 C  CG   A HIS   B 2 113  ? 204.305 175.385 159.497 0.49 111.68 ? 113  HIS   B CG   1 
ATOM   7525 C  CG   B HIS   B 2 113  ? 202.917 175.274 157.555 0.51 111.04 ? 113  HIS   B CG   1 
ATOM   7526 N  ND1  A HIS   B 2 113  ? 204.911 176.554 159.091 0.49 112.43 ? 113  HIS   B ND1  1 
ATOM   7527 N  ND1  B HIS   B 2 113  ? 203.964 175.316 156.660 0.51 110.76 ? 113  HIS   B ND1  1 
ATOM   7528 C  CD2  A HIS   B 2 113  ? 205.075 174.889 160.494 0.49 113.15 ? 113  HIS   B CD2  1 
ATOM   7529 C  CD2  B HIS   B 2 113  ? 201.820 175.673 156.868 0.51 108.30 ? 113  HIS   B CD2  1 
ATOM   7530 C  CE1  A HIS   B 2 113  ? 205.997 176.759 159.814 0.49 113.53 ? 113  HIS   B CE1  1 
ATOM   7531 C  CE1  B HIS   B 2 113  ? 203.519 175.719 155.483 0.51 106.73 ? 113  HIS   B CE1  1 
ATOM   7532 N  NE2  A HIS   B 2 113  ? 206.122 175.761 160.670 0.49 115.43 ? 113  HIS   B NE2  1 
ATOM   7533 N  NE2  B HIS   B 2 113  ? 202.221 175.943 155.582 0.51 101.35 ? 113  HIS   B NE2  1 
ATOM   7534 N  N    . ALA   B 2 114  ? 200.863 172.904 157.759 1.00 113.91 ? 114  ALA   B N    1 
ATOM   7535 C  CA   . ALA   B 2 114  ? 199.473 172.659 157.405 1.00 116.00 ? 114  ALA   B CA   1 
ATOM   7536 C  C    . ALA   B 2 114  ? 199.109 171.182 157.435 1.00 123.16 ? 114  ALA   B C    1 
ATOM   7537 O  O    . ALA   B 2 114  ? 197.950 170.836 157.190 1.00 131.02 ? 114  ALA   B O    1 
ATOM   7538 C  CB   . ALA   B 2 114  ? 199.172 173.241 156.024 1.00 119.18 ? 114  ALA   B CB   1 
ATOM   7539 N  N    . GLY   B 2 115  ? 200.059 170.308 157.748 1.00 125.39 ? 115  GLY   B N    1 
ATOM   7540 C  CA   . GLY   B 2 115  ? 199.811 168.884 157.710 1.00 129.85 ? 115  GLY   B CA   1 
ATOM   7541 C  C    . GLY   B 2 115  ? 199.992 168.234 156.360 1.00 127.43 ? 115  GLY   B C    1 
ATOM   7542 O  O    . GLY   B 2 115  ? 199.553 167.092 156.180 1.00 127.99 ? 115  GLY   B O    1 
ATOM   7543 N  N    . TRP   B 2 116  ? 200.616 168.916 155.403 1.00 126.55 ? 116  TRP   B N    1 
ATOM   7544 C  CA   . TRP   B 2 116  ? 200.834 168.319 154.094 1.00 134.43 ? 116  TRP   B CA   1 
ATOM   7545 C  C    . TRP   B 2 116  ? 201.933 167.267 154.127 1.00 134.90 ? 116  TRP   B C    1 
ATOM   7546 O  O    . TRP   B 2 116  ? 203.115 167.586 153.960 1.00 128.25 ? 116  TRP   B O    1 
ATOM   7547 C  CB   . TRP   B 2 116  ? 201.200 169.369 153.045 1.00 136.20 ? 116  TRP   B CB   1 
ATOM   7548 C  CG   . TRP   B 2 116  ? 200.178 170.420 152.745 1.00 132.43 ? 116  TRP   B CG   1 
ATOM   7549 C  CD1  . TRP   B 2 116  ? 200.366 171.769 152.777 1.00 125.33 ? 116  TRP   B CD1  1 
ATOM   7550 C  CD2  . TRP   B 2 116  ? 198.821 170.214 152.331 1.00 135.99 ? 116  TRP   B CD2  1 
ATOM   7551 N  NE1  . TRP   B 2 116  ? 199.211 172.417 152.419 1.00 126.13 ? 116  TRP   B NE1  1 
ATOM   7552 C  CE2  . TRP   B 2 116  ? 198.246 171.484 152.142 1.00 133.82 ? 116  TRP   B CE2  1 
ATOM   7553 C  CE3  . TRP   B 2 116  ? 198.034 169.080 152.113 1.00 139.17 ? 116  TRP   B CE3  1 
ATOM   7554 C  CZ2  . TRP   B 2 116  ? 196.922 171.651 151.747 1.00 137.26 ? 116  TRP   B CZ2  1 
ATOM   7555 C  CZ3  . TRP   B 2 116  ? 196.720 169.249 151.723 1.00 133.61 ? 116  TRP   B CZ3  1 
ATOM   7556 C  CH2  . TRP   B 2 116  ? 196.178 170.523 151.543 1.00 132.19 ? 116  TRP   B CH2  1 
ATOM   7557 N  N    . THR   B 2 117  ? 201.558 166.014 154.344 1.00 143.24 ? 117  THR   B N    1 
ATOM   7558 C  CA   . THR   B 2 117  ? 202.484 164.932 154.089 1.00 143.47 ? 117  THR   B CA   1 
ATOM   7559 C  C    . THR   B 2 117  ? 202.702 164.816 152.586 1.00 136.65 ? 117  THR   B C    1 
ATOM   7560 O  O    . THR   B 2 117  ? 201.867 165.261 151.797 1.00 134.52 ? 117  THR   B O    1 
ATOM   7561 C  CB   . THR   B 2 117  ? 201.950 163.621 154.658 1.00 143.89 ? 117  THR   B CB   1 
ATOM   7562 O  OG1  . THR   B 2 117  ? 200.708 163.291 154.025 1.00 138.59 ? 117  THR   B OG1  1 
ATOM   7563 C  CG2  . THR   B 2 117  ? 201.740 163.748 156.156 1.00 142.37 ? 117  THR   B CG2  1 
ATOM   7564 N  N    . PRO   B 2 118  ? 203.828 164.242 152.165 1.00 135.73 ? 118  PRO   B N    1 
ATOM   7565 C  CA   . PRO   B 2 118  ? 204.101 164.162 150.724 1.00 135.46 ? 118  PRO   B CA   1 
ATOM   7566 C  C    . PRO   B 2 118  ? 202.981 163.534 149.920 1.00 139.09 ? 118  PRO   B C    1 
ATOM   7567 O  O    . PRO   B 2 118  ? 202.641 164.035 148.842 1.00 142.11 ? 118  PRO   B O    1 
ATOM   7568 C  CB   . PRO   B 2 118  ? 205.380 163.320 150.672 1.00 133.31 ? 118  PRO   B CB   1 
ATOM   7569 C  CG   . PRO   B 2 118  ? 206.080 163.658 151.931 1.00 137.90 ? 118  PRO   B CG   1 
ATOM   7570 C  CD   . PRO   B 2 118  ? 205.007 163.874 152.967 1.00 139.33 ? 118  PRO   B CD   1 
ATOM   7571 N  N    . LEU   B 2 119  ? 202.363 162.473 150.432 1.00 138.11 ? 119  LEU   B N    1 
ATOM   7572 C  CA   . LEU   B 2 119  ? 201.315 161.811 149.668 1.00 145.49 ? 119  LEU   B CA   1 
ATOM   7573 C  C    . LEU   B 2 119  ? 200.126 162.739 149.449 1.00 147.33 ? 119  LEU   B C    1 
ATOM   7574 O  O    . LEU   B 2 119  ? 199.546 162.768 148.355 1.00 148.27 ? 119  LEU   B O    1 
ATOM   7575 C  CB   . LEU   B 2 119  ? 200.893 160.522 150.374 1.00 150.91 ? 119  LEU   B CB   1 
ATOM   7576 C  CG   . LEU   B 2 119  ? 199.903 159.612 149.650 1.00 149.97 ? 119  LEU   B CG   1 
ATOM   7577 C  CD1  . LEU   B 2 119  ? 200.616 158.861 148.551 1.00 145.50 ? 119  LEU   B CD1  1 
ATOM   7578 C  CD2  . LEU   B 2 119  ? 199.296 158.630 150.631 1.00 149.63 ? 119  LEU   B CD2  1 
ATOM   7579 N  N    . HIS   B 2 120  ? 199.776 163.534 150.464 1.00 144.82 ? 120  HIS   B N    1 
ATOM   7580 C  CA   . HIS   B 2 120  ? 198.639 164.442 150.347 1.00 143.96 ? 120  HIS   B CA   1 
ATOM   7581 C  C    . HIS   B 2 120  ? 198.783 165.376 149.154 1.00 142.42 ? 120  HIS   B C    1 
ATOM   7582 O  O    . HIS   B 2 120  ? 197.970 165.342 148.222 1.00 144.79 ? 120  HIS   B O    1 
ATOM   7583 C  CB   . HIS   B 2 120  ? 198.466 165.243 151.636 1.00 139.98 ? 120  HIS   B CB   1 
ATOM   7584 C  CG   . HIS   B 2 120  ? 197.587 164.579 152.645 1.00 140.25 ? 120  HIS   B CG   1 
ATOM   7585 N  ND1  . HIS   B 2 120  ? 197.790 164.691 154.002 1.00 141.80 ? 120  HIS   B ND1  1 
ATOM   7586 C  CD2  . HIS   B 2 120  ? 196.469 163.832 152.492 1.00 143.32 ? 120  HIS   B CD2  1 
ATOM   7587 C  CE1  . HIS   B 2 120  ? 196.850 164.018 154.642 1.00 147.36 ? 120  HIS   B CE1  1 
ATOM   7588 N  NE2  . HIS   B 2 120  ? 196.036 163.487 153.748 1.00 143.33 ? 120  HIS   B NE2  1 
ATOM   7589 N  N    . LEU   B 2 121  ? 199.807 166.222 149.150 1.00 138.27 ? 121  LEU   B N    1 
ATOM   7590 C  CA   . LEU   B 2 121  ? 199.832 167.215 148.090 1.00 143.25 ? 121  LEU   B CA   1 
ATOM   7591 C  C    . LEU   B 2 121  ? 200.433 166.661 146.807 1.00 144.27 ? 121  LEU   B C    1 
ATOM   7592 O  O    . LEU   B 2 121  ? 200.312 167.301 145.759 1.00 145.97 ? 121  LEU   B O    1 
ATOM   7593 C  CB   . LEU   B 2 121  ? 200.566 168.486 148.543 1.00 140.56 ? 121  LEU   B CB   1 
ATOM   7594 C  CG   . LEU   B 2 121  ? 202.041 168.603 148.891 1.00 130.80 ? 121  LEU   B CG   1 
ATOM   7595 C  CD1  . LEU   B 2 121  ? 202.730 168.872 147.604 1.00 133.20 ? 121  LEU   B CD1  1 
ATOM   7596 C  CD2  . LEU   B 2 121  ? 202.315 169.730 149.838 1.00 126.16 ? 121  LEU   B CD2  1 
ATOM   7597 N  N    . ALA   B 2 122  ? 201.043 165.474 146.853 1.00 142.13 ? 122  ALA   B N    1 
ATOM   7598 C  CA   . ALA   B 2 122  ? 201.339 164.759 145.617 1.00 140.01 ? 122  ALA   B CA   1 
ATOM   7599 C  C    . ALA   B 2 122  ? 200.052 164.372 144.905 1.00 140.61 ? 122  ALA   B C    1 
ATOM   7600 O  O    . ALA   B 2 122  ? 199.929 164.531 143.685 1.00 141.86 ? 122  ALA   B O    1 
ATOM   7601 C  CB   . ALA   B 2 122  ? 202.181 163.521 145.909 1.00 141.07 ? 122  ALA   B CB   1 
ATOM   7602 N  N    . ALA   B 2 123  ? 199.076 163.858 145.657 1.00 141.80 ? 123  ALA   B N    1 
ATOM   7603 C  CA   . ALA   B 2 123  ? 197.768 163.581 145.073 1.00 147.40 ? 123  ALA   B CA   1 
ATOM   7604 C  C    . ALA   B 2 123  ? 197.064 164.870 144.669 1.00 146.07 ? 123  ALA   B C    1 
ATOM   7605 O  O    . ALA   B 2 123  ? 196.346 164.905 143.664 1.00 147.57 ? 123  ALA   B O    1 
ATOM   7606 C  CB   . ALA   B 2 123  ? 196.914 162.785 146.058 1.00 147.77 ? 123  ALA   B CB   1 
ATOM   7607 N  N    . LEU   B 2 124  ? 197.253 165.936 145.449 1.00 146.71 ? 124  LEU   B N    1 
ATOM   7608 C  CA   . LEU   B 2 124  ? 196.608 167.211 145.141 1.00 145.17 ? 124  LEU   B CA   1 
ATOM   7609 C  C    . LEU   B 2 124  ? 197.118 167.797 143.827 1.00 143.70 ? 124  LEU   B C    1 
ATOM   7610 O  O    . LEU   B 2 124  ? 196.333 168.298 143.014 1.00 144.64 ? 124  LEU   B O    1 
ATOM   7611 C  CB   . LEU   B 2 124  ? 196.827 168.199 146.287 1.00 137.60 ? 124  LEU   B CB   1 
ATOM   7612 N  N    . TYR   B 2 125  ? 198.430 167.742 143.599 1.00 141.30 ? 125  TYR   B N    1 
ATOM   7613 C  CA   . TYR   B 2 125  ? 199.030 168.372 142.427 1.00 136.52 ? 125  TYR   B CA   1 
ATOM   7614 C  C    . TYR   B 2 125  ? 198.935 167.521 141.170 1.00 136.60 ? 125  TYR   B C    1 
ATOM   7615 O  O    . TYR   B 2 125  ? 199.407 167.957 140.116 1.00 135.86 ? 125  TYR   B O    1 
ATOM   7616 C  CB   . TYR   B 2 125  ? 200.494 168.718 142.697 1.00 133.14 ? 125  TYR   B CB   1 
ATOM   7617 C  CG   . TYR   B 2 125  ? 200.700 170.076 143.324 1.00 136.51 ? 125  TYR   B CG   1 
ATOM   7618 C  CD1  . TYR   B 2 125  ? 201.929 170.714 143.250 1.00 133.48 ? 125  TYR   B CD1  1 
ATOM   7619 C  CD2  . TYR   B 2 125  ? 199.667 170.723 143.990 1.00 139.47 ? 125  TYR   B CD2  1 
ATOM   7620 C  CE1  . TYR   B 2 125  ? 202.126 171.953 143.820 1.00 131.06 ? 125  TYR   B CE1  1 
ATOM   7621 C  CE2  . TYR   B 2 125  ? 199.856 171.967 144.565 1.00 132.48 ? 125  TYR   B CE2  1 
ATOM   7622 C  CZ   . TYR   B 2 125  ? 201.089 172.575 144.475 1.00 127.60 ? 125  TYR   B CZ   1 
ATOM   7623 O  OH   . TYR   B 2 125  ? 201.289 173.811 145.042 1.00 116.31 ? 125  TYR   B OH   1 
ATOM   7624 N  N    . GLY   B 2 126  ? 198.355 166.328 141.253 1.00 139.61 ? 126  GLY   B N    1 
ATOM   7625 C  CA   . GLY   B 2 126  ? 198.153 165.503 140.078 1.00 143.34 ? 126  GLY   B CA   1 
ATOM   7626 C  C    . GLY   B 2 126  ? 199.429 165.052 139.397 1.00 149.65 ? 126  GLY   B C    1 
ATOM   7627 O  O    . GLY   B 2 126  ? 199.546 165.138 138.171 1.00 151.81 ? 126  GLY   B O    1 
ATOM   7628 N  N    . HIS   B 2 127  ? 200.393 164.574 140.178 1.00 147.34 ? 127  HIS   B N    1 
ATOM   7629 C  CA   . HIS   B 2 127  ? 201.634 164.022 139.650 1.00 139.08 ? 127  HIS   B CA   1 
ATOM   7630 C  C    . HIS   B 2 127  ? 201.516 162.504 139.630 1.00 142.73 ? 127  HIS   B C    1 
ATOM   7631 O  O    . HIS   B 2 127  ? 201.426 161.872 140.687 1.00 141.97 ? 127  HIS   B O    1 
ATOM   7632 C  CB   . HIS   B 2 127  ? 202.827 164.466 140.492 1.00 131.02 ? 127  HIS   B CB   1 
ATOM   7633 C  CG   . HIS   B 2 127  ? 203.413 165.773 140.063 1.00 131.42 ? 127  HIS   B CG   1 
ATOM   7634 N  ND1  . HIS   B 2 127  ? 202.744 166.657 139.244 1.00 136.20 ? 127  HIS   B ND1  1 
ATOM   7635 C  CD2  . HIS   B 2 127  ? 204.605 166.351 140.344 1.00 126.52 ? 127  HIS   B CD2  1 
ATOM   7636 C  CE1  . HIS   B 2 127  ? 203.500 167.719 139.035 1.00 131.42 ? 127  HIS   B CE1  1 
ATOM   7637 N  NE2  . HIS   B 2 127  ? 204.634 167.559 139.693 1.00 124.31 ? 127  HIS   B NE2  1 
ATOM   7638 N  N    . LEU   B 2 128  ? 201.521 161.924 138.428 1.00 148.40 ? 128  LEU   B N    1 
ATOM   7639 C  CA   . LEU   B 2 128  ? 201.178 160.512 138.284 1.00 151.50 ? 128  LEU   B CA   1 
ATOM   7640 C  C    . LEU   B 2 128  ? 202.308 159.597 138.741 1.00 154.03 ? 128  LEU   B C    1 
ATOM   7641 O  O    . LEU   B 2 128  ? 202.055 158.547 139.342 1.00 148.54 ? 128  LEU   B O    1 
ATOM   7642 C  CB   . LEU   B 2 128  ? 200.802 160.212 136.833 1.00 139.39 ? 128  LEU   B CB   1 
ATOM   7643 N  N    . GLU   B 2 129  ? 203.560 159.970 138.465 1.00 156.52 ? 129  GLU   B N    1 
ATOM   7644 C  CA   . GLU   B 2 129  ? 204.688 159.071 138.663 1.00 150.29 ? 129  GLU   B CA   1 
ATOM   7645 C  C    . GLU   B 2 129  ? 205.516 159.346 139.910 1.00 143.04 ? 129  GLU   B C    1 
ATOM   7646 O  O    . GLU   B 2 129  ? 206.000 158.387 140.524 1.00 139.82 ? 129  GLU   B O    1 
ATOM   7647 C  CB   . GLU   B 2 129  ? 205.619 159.108 137.440 1.00 142.64 ? 129  GLU   B CB   1 
ATOM   7648 N  N    . ILE   B 2 130  ? 205.710 160.607 140.303 1.00 140.78 ? 130  ILE   B N    1 
ATOM   7649 C  CA   . ILE   B 2 130  ? 206.571 160.862 141.454 1.00 135.91 ? 130  ILE   B CA   1 
ATOM   7650 C  C    . ILE   B 2 130  ? 205.938 160.337 142.732 1.00 134.94 ? 130  ILE   B C    1 
ATOM   7651 O  O    . ILE   B 2 130  ? 206.648 159.947 143.667 1.00 139.66 ? 130  ILE   B O    1 
ATOM   7652 C  CB   . ILE   B 2 130  ? 206.928 162.355 141.570 1.00 131.60 ? 130  ILE   B CB   1 
ATOM   7653 C  CG1  . ILE   B 2 130  ? 208.059 162.534 142.579 1.00 124.06 ? 130  ILE   B CG1  1 
ATOM   7654 C  CG2  . ILE   B 2 130  ? 205.731 163.169 141.996 1.00 135.64 ? 130  ILE   B CG2  1 
ATOM   7655 C  CD1  . ILE   B 2 130  ? 209.350 161.911 142.144 1.00 126.29 ? 130  ILE   B CD1  1 
ATOM   7656 N  N    . VAL   B 2 131  ? 204.607 160.298 142.800 1.00 135.35 ? 131  VAL   B N    1 
ATOM   7657 C  CA   . VAL   B 2 131  ? 203.966 159.703 143.966 1.00 139.85 ? 131  VAL   B CA   1 
ATOM   7658 C  C    . VAL   B 2 131  ? 204.352 158.236 144.087 1.00 147.01 ? 131  VAL   B C    1 
ATOM   7659 O  O    . VAL   B 2 131  ? 204.661 157.753 145.181 1.00 148.48 ? 131  VAL   B O    1 
ATOM   7660 C  CB   . VAL   B 2 131  ? 202.439 159.900 143.912 1.00 142.59 ? 131  VAL   B CB   1 
ATOM   7661 C  CG1  . VAL   B 2 131  ? 201.828 159.166 142.732 1.00 145.55 ? 131  VAL   B CG1  1 
ATOM   7662 C  CG2  . VAL   B 2 131  ? 201.812 159.417 145.201 1.00 141.76 ? 131  VAL   B CG2  1 
ATOM   7663 N  N    . GLU   B 2 132  ? 204.377 157.512 142.965 1.00 149.03 ? 132  GLU   B N    1 
ATOM   7664 C  CA   . GLU   B 2 132  ? 204.798 156.116 143.002 1.00 147.04 ? 132  GLU   B CA   1 
ATOM   7665 C  C    . GLU   B 2 132  ? 206.284 156.001 143.311 1.00 146.48 ? 132  GLU   B C    1 
ATOM   7666 O  O    . GLU   B 2 132  ? 206.722 155.040 143.953 1.00 147.98 ? 132  GLU   B O    1 
ATOM   7667 C  CB   . GLU   B 2 132  ? 204.464 155.428 141.679 1.00 149.41 ? 132  GLU   B CB   1 
ATOM   7668 N  N    . VAL   B 2 133  ? 207.078 156.968 142.851 1.00 143.98 ? 133  VAL   B N    1 
ATOM   7669 C  CA   . VAL   B 2 133  ? 208.508 156.947 143.148 1.00 140.64 ? 133  VAL   B CA   1 
ATOM   7670 C  C    . VAL   B 2 133  ? 208.746 157.062 144.649 1.00 140.86 ? 133  VAL   B C    1 
ATOM   7671 O  O    . VAL   B 2 133  ? 209.622 156.389 145.205 1.00 138.05 ? 133  VAL   B O    1 
ATOM   7672 C  CB   . VAL   B 2 133  ? 209.239 158.049 142.365 1.00 138.32 ? 133  VAL   B CB   1 
ATOM   7673 C  CG1  . VAL   B 2 133  ? 210.714 158.044 142.712 1.00 134.69 ? 133  VAL   B CG1  1 
ATOM   7674 C  CG2  . VAL   B 2 133  ? 209.052 157.829 140.880 1.00 131.98 ? 133  VAL   B CG2  1 
ATOM   7675 N  N    . LEU   B 2 134  ? 207.989 157.924 145.330 1.00 146.07 ? 134  LEU   B N    1 
ATOM   7676 C  CA   . LEU   B 2 134  ? 208.035 157.917 146.791 1.00 143.68 ? 134  LEU   B CA   1 
ATOM   7677 C  C    . LEU   B 2 134  ? 207.372 156.670 147.364 1.00 146.47 ? 134  LEU   B C    1 
ATOM   7678 O  O    . LEU   B 2 134  ? 207.640 156.297 148.510 1.00 149.18 ? 134  LEU   B O    1 
ATOM   7679 C  CB   . LEU   B 2 134  ? 207.394 159.176 147.381 1.00 141.98 ? 134  LEU   B CB   1 
ATOM   7680 C  CG   . LEU   B 2 134  ? 208.178 160.492 147.384 1.00 137.77 ? 134  LEU   B CG   1 
ATOM   7681 C  CD1  . LEU   B 2 134  ? 208.285 161.063 145.988 1.00 137.58 ? 134  LEU   B CD1  1 
ATOM   7682 C  CD2  . LEU   B 2 134  ? 207.556 161.498 148.337 1.00 124.41 ? 134  LEU   B CD2  1 
ATOM   7683 N  N    . LEU   B 2 135  ? 206.476 156.031 146.610 1.00 148.64 ? 135  LEU   B N    1 
ATOM   7684 C  CA   . LEU   B 2 135  ? 205.889 154.791 147.106 1.00 153.83 ? 135  LEU   B CA   1 
ATOM   7685 C  C    . LEU   B 2 135  ? 206.888 153.638 147.130 1.00 156.82 ? 135  LEU   B C    1 
ATOM   7686 O  O    . LEU   B 2 135  ? 206.960 152.918 148.133 1.00 153.29 ? 135  LEU   B O    1 
ATOM   7687 C  CB   . LEU   B 2 135  ? 204.671 154.387 146.271 1.00 154.80 ? 135  LEU   B CB   1 
ATOM   7688 C  CG   . LEU   B 2 135  ? 203.403 155.242 146.274 1.00 152.25 ? 135  LEU   B CG   1 
ATOM   7689 C  CD1  . LEU   B 2 135  ? 202.403 154.703 145.266 1.00 150.90 ? 135  LEU   B CD1  1 
ATOM   7690 C  CD2  . LEU   B 2 135  ? 202.787 155.304 147.654 1.00 152.33 ? 135  LEU   B CD2  1 
ATOM   7691 N  N    . LYS   B 2 136  ? 207.661 153.448 146.058 1.00 157.74 ? 136  LYS   B N    1 
ATOM   7692 C  CA   . LYS   B 2 136  ? 208.569 152.306 145.994 1.00 155.43 ? 136  LYS   B CA   1 
ATOM   7693 C  C    . LYS   B 2 136  ? 209.731 152.460 146.970 1.00 151.38 ? 136  LYS   B C    1 
ATOM   7694 O  O    . LYS   B 2 136  ? 210.030 151.545 147.744 1.00 151.16 ? 136  LYS   B O    1 
ATOM   7695 C  CB   . LYS   B 2 136  ? 209.082 152.127 144.565 1.00 149.33 ? 136  LYS   B CB   1 
ATOM   7696 N  N    . HIS   B 2 137  ? 210.391 153.615 146.959 1.00 148.77 ? 137  HIS   B N    1 
ATOM   7697 C  CA   . HIS   B 2 137  ? 211.534 153.863 147.823 1.00 142.41 ? 137  HIS   B CA   1 
ATOM   7698 C  C    . HIS   B 2 137  ? 211.106 154.693 149.022 1.00 147.25 ? 137  HIS   B C    1 
ATOM   7699 O  O    . HIS   B 2 137  ? 210.243 155.567 148.917 1.00 155.12 ? 137  HIS   B O    1 
ATOM   7700 C  CB   . HIS   B 2 137  ? 212.668 154.574 147.081 1.00 140.15 ? 137  HIS   B CB   1 
ATOM   7701 C  CG   . HIS   B 2 137  ? 213.011 153.961 145.761 1.00 138.59 ? 137  HIS   B CG   1 
ATOM   7702 N  ND1  . HIS   B 2 137  ? 212.149 153.968 144.686 1.00 143.61 ? 137  HIS   B ND1  1 
ATOM   7703 C  CD2  . HIS   B 2 137  ? 214.129 153.322 145.343 1.00 134.67 ? 137  HIS   B CD2  1 
ATOM   7704 C  CE1  . HIS   B 2 137  ? 212.721 153.359 143.663 1.00 138.89 ? 137  HIS   B CE1  1 
ATOM   7705 N  NE2  . HIS   B 2 137  ? 213.922 152.957 144.035 1.00 137.36 ? 137  HIS   B NE2  1 
ATOM   7706 N  N    . GLY   B 2 138  ? 211.718 154.410 150.165 1.00 142.95 ? 138  GLY   B N    1 
ATOM   7707 C  CA   . GLY   B 2 138  ? 211.242 154.945 151.418 1.00 145.50 ? 138  GLY   B CA   1 
ATOM   7708 C  C    . GLY   B 2 138  ? 209.954 154.316 151.897 1.00 153.19 ? 138  GLY   B C    1 
ATOM   7709 O  O    . GLY   B 2 138  ? 209.363 154.817 152.861 1.00 154.97 ? 138  GLY   B O    1 
ATOM   7710 N  N    . ALA   B 2 139  ? 209.503 153.241 151.245 1.00 151.69 ? 139  ALA   B N    1 
ATOM   7711 C  CA   . ALA   B 2 139  ? 208.271 152.537 151.578 1.00 157.34 ? 139  ALA   B CA   1 
ATOM   7712 C  C    . ALA   B 2 139  ? 207.073 153.453 151.385 1.00 161.81 ? 139  ALA   B C    1 
ATOM   7713 O  O    . ALA   B 2 139  ? 207.166 154.458 150.672 1.00 160.10 ? 139  ALA   B O    1 
ATOM   7714 C  CB   . ALA   B 2 139  ? 208.312 151.989 153.007 1.00 159.78 ? 139  ALA   B CB   1 
ATOM   7715 N  N    . ASP   B 2 140  ? 205.947 153.120 152.019 1.00 165.93 ? 140  ASP   B N    1 
ATOM   7716 C  CA   . ASP   B 2 140  ? 204.737 153.925 151.903 1.00 163.44 ? 140  ASP   B CA   1 
ATOM   7717 C  C    . ASP   B 2 140  ? 203.781 153.718 153.073 1.00 157.97 ? 140  ASP   B C    1 
ATOM   7718 O  O    . ASP   B 2 140  ? 203.471 152.584 153.450 1.00 157.43 ? 140  ASP   B O    1 
ATOM   7719 C  CB   . ASP   B 2 140  ? 204.034 153.661 150.561 1.00 165.55 ? 140  ASP   B CB   1 
ATOM   7720 C  CG   . ASP   B 2 140  ? 203.572 152.216 150.385 1.00 169.20 ? 140  ASP   B CG   1 
ATOM   7721 O  OD1  . ASP   B 2 140  ? 203.819 151.365 151.260 1.00 171.15 ? 140  ASP   B OD1  1 
ATOM   7722 O  OD2  . ASP   B 2 140  ? 202.943 151.930 149.345 1.00 168.04 ? 140  ASP   B OD2  1 
ATOM   7723 N  N    . VAL   B 2 141  ? 203.346 154.821 153.684 1.00 157.09 ? 141  VAL   B N    1 
ATOM   7724 C  CA   . VAL   B 2 141  ? 202.330 154.809 154.729 1.00 160.27 ? 141  VAL   B CA   1 
ATOM   7725 C  C    . VAL   B 2 141  ? 201.428 156.020 154.519 1.00 161.74 ? 141  VAL   B C    1 
ATOM   7726 O  O    . VAL   B 2 141  ? 201.889 157.118 154.200 1.00 156.50 ? 141  VAL   B O    1 
ATOM   7727 C  CB   . VAL   B 2 141  ? 202.939 154.825 156.156 1.00 154.65 ? 141  VAL   B CB   1 
ATOM   7728 C  CG1  . VAL   B 2 141  ? 201.850 154.917 157.209 1.00 149.43 ? 141  VAL   B CG1  1 
ATOM   7729 C  CG2  . VAL   B 2 141  ? 203.797 153.593 156.404 1.00 151.67 ? 141  VAL   B CG2  1 
ATOM   7730 N  N    . ASN   B 2 142  ? 200.126 155.806 154.682 1.00 163.22 ? 142  ASN   B N    1 
ATOM   7731 C  CA   . ASN   B 2 142  ? 199.169 156.899 154.623 1.00 155.31 ? 142  ASN   B CA   1 
ATOM   7732 C  C    . ASN   B 2 142  ? 199.261 157.747 155.890 1.00 153.91 ? 142  ASN   B C    1 
ATOM   7733 O  O    . ASN   B 2 142  ? 199.781 157.318 156.921 1.00 151.41 ? 142  ASN   B O    1 
ATOM   7734 C  CB   . ASN   B 2 142  ? 197.750 156.365 154.435 1.00 151.19 ? 142  ASN   B CB   1 
ATOM   7735 C  CG   . ASN   B 2 142  ? 197.414 156.115 152.982 1.00 142.69 ? 142  ASN   B CG   1 
ATOM   7736 O  OD1  . ASN   B 2 142  ? 198.305 155.948 152.150 1.00 142.99 ? 142  ASN   B OD1  1 
ATOM   7737 N  ND2  . ASN   B 2 142  ? 196.125 156.097 152.665 1.00 139.17 ? 142  ASN   B ND2  1 
ATOM   7738 N  N    . ALA   B 2 143  ? 198.749 158.970 155.805 1.00 152.11 ? 143  ALA   B N    1 
ATOM   7739 C  CA   . ALA   B 2 143  ? 198.864 159.913 156.912 1.00 152.22 ? 143  ALA   B CA   1 
ATOM   7740 C  C    . ALA   B 2 143  ? 197.641 160.824 156.915 1.00 152.94 ? 143  ALA   B C    1 
ATOM   7741 O  O    . ALA   B 2 143  ? 196.683 160.612 156.163 1.00 149.96 ? 143  ALA   B O    1 
ATOM   7742 C  CB   . ALA   B 2 143  ? 200.174 160.698 156.817 1.00 149.52 ? 143  ALA   B CB   1 
ATOM   7743 N  N    . GLN   B 2 144  ? 197.674 161.847 157.769 1.00 152.68 ? 144  GLN   B N    1 
ATOM   7744 C  CA   . GLN   B 2 144  ? 196.530 162.721 157.986 1.00 149.28 ? 144  GLN   B CA   1 
ATOM   7745 C  C    . GLN   B 2 144  ? 196.997 164.162 158.116 1.00 149.22 ? 144  GLN   B C    1 
ATOM   7746 O  O    . GLN   B 2 144  ? 198.013 164.429 158.765 1.00 144.55 ? 144  GLN   B O    1 
ATOM   7747 C  CB   . GLN   B 2 144  ? 195.762 162.307 159.246 1.00 143.78 ? 144  GLN   B CB   1 
ATOM   7748 C  CG   . GLN   B 2 144  ? 194.520 163.124 159.480 1.00 144.10 ? 144  GLN   B CG   1 
ATOM   7749 C  CD   . GLN   B 2 144  ? 193.529 162.956 158.355 1.00 151.11 ? 144  GLN   B CD   1 
ATOM   7750 O  OE1  . GLN   B 2 144  ? 193.377 163.838 157.514 1.00 152.37 ? 144  GLN   B OE1  1 
ATOM   7751 N  NE2  . GLN   B 2 144  ? 192.843 161.820 158.334 1.00 152.32 ? 144  GLN   B NE2  1 
ATOM   7752 N  N    . ASP   B 2 145  ? 196.251 165.086 157.513 1.00 151.32 ? 145  ASP   B N    1 
ATOM   7753 C  CA   . ASP   B 2 145  ? 196.519 166.511 157.624 1.00 142.79 ? 145  ASP   B CA   1 
ATOM   7754 C  C    . ASP   B 2 145  ? 195.612 167.116 158.694 1.00 142.52 ? 145  ASP   B C    1 
ATOM   7755 O  O    . ASP   B 2 145  ? 194.851 166.413 159.364 1.00 146.06 ? 145  ASP   B O    1 
ATOM   7756 C  CB   . ASP   B 2 145  ? 196.346 167.197 156.267 1.00 138.97 ? 145  ASP   B CB   1 
ATOM   7757 C  CG   . ASP   B 2 145  ? 194.931 167.104 155.735 1.00 144.26 ? 145  ASP   B CG   1 
ATOM   7758 O  OD1  . ASP   B 2 145  ? 194.072 166.474 156.386 1.00 144.49 ? 145  ASP   B OD1  1 
ATOM   7759 O  OD2  . ASP   B 2 145  ? 194.678 167.666 154.651 1.00 145.16 ? 145  ASP   B OD2  1 
ATOM   7760 N  N    . MET   B 2 146  ? 195.678 168.436 158.854 1.00 138.89 ? 146  MET   B N    1 
ATOM   7761 C  CA   . MET   B 2 146  ? 194.977 169.085 159.953 1.00 137.89 ? 146  MET   B CA   1 
ATOM   7762 C  C    . MET   B 2 146  ? 193.489 169.276 159.702 1.00 136.20 ? 146  MET   B C    1 
ATOM   7763 O  O    . MET   B 2 146  ? 192.748 169.535 160.657 1.00 135.22 ? 146  MET   B O    1 
ATOM   7764 C  CB   . MET   B 2 146  ? 195.599 170.446 160.257 1.00 131.36 ? 146  MET   B CB   1 
ATOM   7765 C  CG   . MET   B 2 146  ? 195.461 171.448 159.140 1.00 128.47 ? 146  MET   B CG   1 
ATOM   7766 S  SD   . MET   B 2 146  ? 196.196 173.013 159.620 1.00 136.13 ? 146  MET   B SD   1 
ATOM   7767 C  CE   . MET   B 2 146  ? 194.974 173.549 160.812 1.00 126.82 ? 146  MET   B CE   1 
ATOM   7768 N  N    . TRP   B 2 147  ? 193.032 169.174 158.457 1.00 136.19 ? 147  TRP   B N    1 
ATOM   7769 C  CA   . TRP   B 2 147  ? 191.612 169.331 158.172 1.00 138.24 ? 147  TRP   B CA   1 
ATOM   7770 C  C    . TRP   B 2 147  ? 190.860 168.011 158.117 1.00 141.84 ? 147  TRP   B C    1 
ATOM   7771 O  O    . TRP   B 2 147  ? 189.627 168.022 158.030 1.00 143.51 ? 147  TRP   B O    1 
ATOM   7772 C  CB   . TRP   B 2 147  ? 191.409 170.074 156.849 1.00 136.61 ? 147  TRP   B CB   1 
ATOM   7773 C  CG   . TRP   B 2 147  ? 192.004 171.440 156.837 1.00 132.49 ? 147  TRP   B CG   1 
ATOM   7774 C  CD1  . TRP   B 2 147  ? 191.664 172.489 157.637 1.00 124.20 ? 147  TRP   B CD1  1 
ATOM   7775 C  CD2  . TRP   B 2 147  ? 193.053 171.907 155.986 1.00 127.53 ? 147  TRP   B CD2  1 
ATOM   7776 N  NE1  . TRP   B 2 147  ? 192.435 173.582 157.335 1.00 122.35 ? 147  TRP   B NE1  1 
ATOM   7777 C  CE2  . TRP   B 2 147  ? 193.296 173.249 156.323 1.00 125.06 ? 147  TRP   B CE2  1 
ATOM   7778 C  CE3  . TRP   B 2 147  ? 193.809 171.321 154.969 1.00 118.48 ? 147  TRP   B CE3  1 
ATOM   7779 C  CZ2  . TRP   B 2 147  ? 194.259 174.013 155.681 1.00 115.59 ? 147  TRP   B CZ2  1 
ATOM   7780 C  CZ3  . TRP   B 2 147  ? 194.764 172.081 154.335 1.00 118.63 ? 147  TRP   B CZ3  1 
ATOM   7781 C  CH2  . TRP   B 2 147  ? 194.983 173.413 154.692 1.00 117.14 ? 147  TRP   B CH2  1 
ATOM   7782 N  N    . GLY   B 2 148  ? 191.560 166.885 158.173 1.00 142.37 ? 148  GLY   B N    1 
ATOM   7783 C  CA   . GLY   B 2 148  ? 190.902 165.603 158.030 1.00 148.16 ? 148  GLY   B CA   1 
ATOM   7784 C  C    . GLY   B 2 148  ? 190.645 165.264 156.578 1.00 146.48 ? 148  GLY   B C    1 
ATOM   7785 O  O    . GLY   B 2 148  ? 189.513 164.959 156.193 1.00 140.52 ? 148  GLY   B O    1 
ATOM   7786 N  N    . GLU   B 2 149  ? 191.694 165.313 155.761 1.00 146.76 ? 149  GLU   B N    1 
ATOM   7787 C  CA   . GLU   B 2 149  ? 191.578 165.038 154.338 1.00 149.55 ? 149  GLU   B CA   1 
ATOM   7788 C  C    . GLU   B 2 149  ? 192.568 163.950 153.949 1.00 151.65 ? 149  GLU   B C    1 
ATOM   7789 O  O    . GLU   B 2 149  ? 193.729 163.962 154.367 1.00 146.65 ? 149  GLU   B O    1 
ATOM   7790 C  CB   . GLU   B 2 149  ? 191.825 166.298 153.500 1.00 149.36 ? 149  GLU   B CB   1 
ATOM   7791 N  N    . THR   B 2 150  ? 192.098 163.017 153.137 1.00 155.92 ? 150  THR   B N    1 
ATOM   7792 C  CA   . THR   B 2 150  ? 192.883 161.898 152.649 1.00 152.51 ? 150  THR   B CA   1 
ATOM   7793 C  C    . THR   B 2 150  ? 193.327 162.151 151.218 1.00 153.12 ? 150  THR   B C    1 
ATOM   7794 O  O    . THR   B 2 150  ? 192.645 162.844 150.458 1.00 154.01 ? 150  THR   B O    1 
ATOM   7795 C  CB   . THR   B 2 150  ? 192.064 160.606 152.714 1.00 156.43 ? 150  THR   B CB   1 
ATOM   7796 O  OG1  . THR   B 2 150  ? 190.908 160.730 151.876 1.00 155.88 ? 150  THR   B OG1  1 
ATOM   7797 C  CG2  . THR   B 2 150  ? 191.614 160.334 154.141 1.00 154.34 ? 150  THR   B CG2  1 
ATOM   7798 N  N    . PRO   B 2 151  ? 194.469 161.593 150.808 1.00 146.01 ? 151  PRO   B N    1 
ATOM   7799 C  CA   . PRO   B 2 151  ? 194.971 161.865 149.452 1.00 146.10 ? 151  PRO   B CA   1 
ATOM   7800 C  C    . PRO   B 2 151  ? 194.023 161.431 148.350 1.00 155.71 ? 151  PRO   B C    1 
ATOM   7801 O  O    . PRO   B 2 151  ? 194.116 161.956 147.234 1.00 153.74 ? 151  PRO   B O    1 
ATOM   7802 C  CB   . PRO   B 2 151  ? 196.283 161.074 149.401 1.00 137.86 ? 151  PRO   B CB   1 
ATOM   7803 C  CG   . PRO   B 2 151  ? 196.692 160.954 150.820 1.00 135.43 ? 151  PRO   B CG   1 
ATOM   7804 C  CD   . PRO   B 2 151  ? 195.426 160.804 151.598 1.00 138.88 ? 151  PRO   B CD   1 
ATOM   7805 N  N    . PHE   B 2 152  ? 193.117 160.489 148.619 1.00 160.40 ? 152  PHE   B N    1 
ATOM   7806 C  CA   . PHE   B 2 152  ? 192.138 160.110 147.606 1.00 160.99 ? 152  PHE   B CA   1 
ATOM   7807 C  C    . PHE   B 2 152  ? 191.239 161.285 147.245 1.00 165.21 ? 152  PHE   B C    1 
ATOM   7808 O  O    . PHE   B 2 152  ? 190.973 161.533 146.063 1.00 166.23 ? 152  PHE   B O    1 
ATOM   7809 C  CB   . PHE   B 2 152  ? 191.304 158.927 148.097 1.00 155.55 ? 152  PHE   B CB   1 
ATOM   7810 N  N    . ASP   B 2 153  ? 190.770 162.028 148.251 1.00 167.84 ? 153  ASP   B N    1 
ATOM   7811 C  CA   . ASP   B 2 153  ? 189.908 163.175 147.982 1.00 171.97 ? 153  ASP   B CA   1 
ATOM   7812 C  C    . ASP   B 2 153  ? 190.662 164.271 147.240 1.00 168.93 ? 153  ASP   B C    1 
ATOM   7813 O  O    . ASP   B 2 153  ? 190.118 164.891 146.318 1.00 171.83 ? 153  ASP   B O    1 
ATOM   7814 C  CB   . ASP   B 2 153  ? 189.326 163.710 149.289 1.00 170.32 ? 153  ASP   B CB   1 
ATOM   7815 N  N    . LEU   B 2 154  ? 191.914 164.524 147.628 1.00 163.70 ? 154  LEU   B N    1 
ATOM   7816 C  CA   . LEU   B 2 154  ? 192.708 165.550 146.959 1.00 155.48 ? 154  LEU   B CA   1 
ATOM   7817 C  C    . LEU   B 2 154  ? 192.994 165.189 145.509 1.00 150.29 ? 154  LEU   B C    1 
ATOM   7818 O  O    . LEU   B 2 154  ? 193.034 166.075 144.649 1.00 144.32 ? 154  LEU   B O    1 
ATOM   7819 C  CB   . LEU   B 2 154  ? 194.017 165.779 147.713 1.00 146.50 ? 154  LEU   B CB   1 
ATOM   7820 C  CG   . LEU   B 2 154  ? 193.970 166.622 148.988 1.00 144.13 ? 154  LEU   B CG   1 
ATOM   7821 C  CD1  . LEU   B 2 154  ? 193.290 165.898 150.130 1.00 150.53 ? 154  LEU   B CD1  1 
ATOM   7822 C  CD2  . LEU   B 2 154  ? 195.378 167.017 149.386 1.00 141.21 ? 154  LEU   B CD2  1 
ATOM   7823 N  N    . ALA   B 2 155  ? 193.198 163.910 145.220 1.00 146.48 ? 155  ALA   B N    1 
ATOM   7824 C  CA   . ALA   B 2 155  ? 193.483 163.470 143.862 1.00 143.22 ? 155  ALA   B CA   1 
ATOM   7825 C  C    . ALA   B 2 155  ? 192.265 163.637 142.960 1.00 143.46 ? 155  ALA   B C    1 
ATOM   7826 O  O    . ALA   B 2 155  ? 192.395 163.968 141.782 1.00 146.56 ? 155  ALA   B O    1 
ATOM   7827 C  CB   . ALA   B 2 155  ? 193.945 162.029 143.864 1.00 148.61 ? 155  ALA   B CB   1 
ATOM   7828 N  N    . ASP   B 2 162  ? 193.227 159.229 138.983 1.00 166.86 ? 162  ASP   B N    1 
ATOM   7829 C  CA   . ASP   B 2 162  ? 194.432 158.498 138.608 1.00 167.20 ? 162  ASP   B CA   1 
ATOM   7830 C  C    . ASP   B 2 162  ? 195.282 158.115 139.820 1.00 168.50 ? 162  ASP   B C    1 
ATOM   7831 O  O    . ASP   B 2 162  ? 195.738 156.978 139.930 1.00 166.17 ? 162  ASP   B O    1 
ATOM   7832 C  CB   . ASP   B 2 162  ? 195.256 159.313 137.601 1.00 161.07 ? 162  ASP   B CB   1 
ATOM   7833 C  CG   . ASP   B 2 162  ? 195.747 160.639 138.164 1.00 161.27 ? 162  ASP   B CG   1 
ATOM   7834 O  OD1  . ASP   B 2 162  ? 195.458 160.949 139.337 1.00 160.24 ? 162  ASP   B OD1  1 
ATOM   7835 O  OD2  . ASP   B 2 162  ? 196.438 161.372 137.427 1.00 155.84 ? 162  ASP   B OD2  1 
ATOM   7836 N  N    . ILE   B 2 163  ? 195.498 159.070 140.725 1.00 168.52 ? 163  ILE   B N    1 
ATOM   7837 C  CA   . ILE   B 2 163  ? 196.277 158.785 141.924 1.00 169.39 ? 163  ILE   B CA   1 
ATOM   7838 C  C    . ILE   B 2 163  ? 195.463 157.943 142.900 1.00 170.63 ? 163  ILE   B C    1 
ATOM   7839 O  O    . ILE   B 2 163  ? 196.011 157.102 143.622 1.00 172.40 ? 163  ILE   B O    1 
ATOM   7840 C  CB   . ILE   B 2 163  ? 196.769 160.093 142.568 1.00 165.82 ? 163  ILE   B CB   1 
ATOM   7841 C  CG1  . ILE   B 2 163  ? 197.621 160.880 141.575 1.00 155.56 ? 163  ILE   B CG1  1 
ATOM   7842 C  CG2  . ILE   B 2 163  ? 197.587 159.801 143.815 1.00 164.20 ? 163  ILE   B CG2  1 
ATOM   7843 C  CD1  . ILE   B 2 163  ? 198.847 160.147 141.123 1.00 151.22 ? 163  ILE   B CD1  1 
ATOM   7844 N  N    . ALA   B 2 164  ? 194.145 158.152 142.933 1.00 170.18 ? 164  ALA   B N    1 
ATOM   7845 C  CA   . ALA   B 2 164  ? 193.298 157.421 143.871 1.00 170.56 ? 164  ALA   B CA   1 
ATOM   7846 C  C    . ALA   B 2 164  ? 193.380 155.918 143.637 1.00 173.52 ? 164  ALA   B C    1 
ATOM   7847 O  O    . ALA   B 2 164  ? 193.444 155.135 144.592 1.00 172.09 ? 164  ALA   B O    1 
ATOM   7848 C  CB   . ALA   B 2 164  ? 191.852 157.905 143.758 1.00 166.08 ? 164  ALA   B CB   1 
ATOM   7849 N  N    . GLU   B 2 165  ? 193.379 155.496 142.371 1.00 175.26 ? 165  GLU   B N    1 
ATOM   7850 C  CA   . GLU   B 2 165  ? 193.517 154.077 142.065 1.00 171.01 ? 165  GLU   B CA   1 
ATOM   7851 C  C    . GLU   B 2 165  ? 194.867 153.542 142.523 1.00 171.49 ? 165  GLU   B C    1 
ATOM   7852 O  O    . GLU   B 2 165  ? 194.963 152.405 143.000 1.00 171.99 ? 165  GLU   B O    1 
ATOM   7853 C  CB   . GLU   B 2 165  ? 193.320 153.839 140.568 1.00 169.19 ? 165  GLU   B CB   1 
ATOM   7854 C  CG   . GLU   B 2 165  ? 192.053 154.462 139.992 1.00 173.32 ? 165  GLU   B CG   1 
ATOM   7855 C  CD   . GLU   B 2 165  ? 192.230 155.915 139.591 1.00 175.74 ? 165  GLU   B CD   1 
ATOM   7856 O  OE1  . GLU   B 2 165  ? 192.059 156.227 138.394 1.00 172.47 ? 165  GLU   B OE1  1 
ATOM   7857 O  OE2  . GLU   B 2 165  ? 192.524 156.747 140.476 1.00 175.85 ? 165  GLU   B OE2  1 
ATOM   7858 N  N    . VAL   B 2 166  ? 195.924 154.344 142.385 1.00 173.24 ? 166  VAL   B N    1 
ATOM   7859 C  CA   . VAL   B 2 166  ? 197.233 153.928 142.880 1.00 172.95 ? 166  VAL   B CA   1 
ATOM   7860 C  C    . VAL   B 2 166  ? 197.211 153.809 144.398 1.00 174.83 ? 166  VAL   B C    1 
ATOM   7861 O  O    . VAL   B 2 166  ? 197.881 152.946 144.977 1.00 172.44 ? 166  VAL   B O    1 
ATOM   7862 C  CB   . VAL   B 2 166  ? 198.325 154.902 142.403 1.00 169.97 ? 166  VAL   B CB   1 
ATOM   7863 C  CG1  . VAL   B 2 166  ? 199.702 154.352 142.732 1.00 162.82 ? 166  VAL   B CG1  1 
ATOM   7864 C  CG2  . VAL   B 2 166  ? 198.192 155.154 140.910 1.00 164.73 ? 166  VAL   B CG2  1 
ATOM   7865 N  N    . LEU   B 2 167  ? 196.448 154.677 145.065 1.00 176.68 ? 167  LEU   B N    1 
ATOM   7866 C  CA   . LEU   B 2 167  ? 196.338 154.608 146.518 1.00 175.01 ? 167  LEU   B CA   1 
ATOM   7867 C  C    . LEU   B 2 167  ? 195.720 153.290 146.964 1.00 176.96 ? 167  LEU   B C    1 
ATOM   7868 O  O    . LEU   B 2 167  ? 196.179 152.677 147.935 1.00 176.57 ? 167  LEU   B O    1 
ATOM   7869 C  CB   . LEU   B 2 167  ? 195.512 155.785 147.032 1.00 168.39 ? 167  LEU   B CB   1 
ATOM   7870 C  CG   . LEU   B 2 167  ? 196.149 157.158 146.830 1.00 166.33 ? 167  LEU   B CG   1 
ATOM   7871 C  CD1  . LEU   B 2 167  ? 195.189 158.249 147.245 1.00 161.63 ? 167  LEU   B CD1  1 
ATOM   7872 C  CD2  . LEU   B 2 167  ? 197.447 157.260 147.610 1.00 163.89 ? 167  LEU   B CD2  1 
ATOM   7873 N  N    . GLN   B 2 168  ? 194.675 152.838 146.266 1.00 179.50 ? 168  GLN   B N    1 
ATOM   7874 C  CA   . GLN   B 2 168  ? 194.006 151.601 146.653 1.00 179.74 ? 168  GLN   B CA   1 
ATOM   7875 C  C    . GLN   B 2 168  ? 194.940 150.402 146.538 1.00 183.53 ? 168  GLN   B C    1 
ATOM   7876 O  O    . GLN   B 2 168  ? 194.957 149.537 147.421 1.00 185.40 ? 168  GLN   B O    1 
ATOM   7877 C  CB   . GLN   B 2 168  ? 192.753 151.398 145.800 1.00 178.92 ? 168  GLN   B CB   1 
ATOM   7878 C  CG   . GLN   B 2 168  ? 191.729 152.521 145.927 1.00 176.95 ? 168  GLN   B CG   1 
ATOM   7879 C  CD   . GLN   B 2 168  ? 190.785 152.595 144.740 1.00 174.47 ? 168  GLN   B CD   1 
ATOM   7880 O  OE1  . GLN   B 2 168  ? 190.900 153.483 143.896 1.00 171.24 ? 168  GLN   B OE1  1 
ATOM   7881 N  NE2  . GLN   B 2 168  ? 189.848 151.660 144.670 1.00 171.99 ? 168  GLN   B NE2  1 
ATOM   7882 N  N    . LYS   B 2 169  ? 195.728 150.333 145.460 1.00 183.67 ? 169  LYS   B N    1 
ATOM   7883 C  CA   . LYS   B 2 169  ? 196.633 149.197 145.291 1.00 182.45 ? 169  LYS   B CA   1 
ATOM   7884 C  C    . LYS   B 2 169  ? 197.850 149.295 146.202 1.00 181.73 ? 169  LYS   B C    1 
ATOM   7885 O  O    . LYS   B 2 169  ? 198.350 148.268 146.675 1.00 181.44 ? 169  LYS   B O    1 
ATOM   7886 C  CB   . LYS   B 2 169  ? 197.064 149.064 143.829 1.00 178.59 ? 169  LYS   B CB   1 
ATOM   7887 C  CG   . LYS   B 2 169  ? 197.671 150.311 143.215 1.00 173.25 ? 169  LYS   B CG   1 
ATOM   7888 C  CD   . LYS   B 2 169  ? 198.237 150.028 141.828 1.00 167.30 ? 169  LYS   B CD   1 
ATOM   7889 C  CE   . LYS   B 2 169  ? 197.332 149.120 141.002 1.00 157.85 ? 169  LYS   B CE   1 
ATOM   7890 N  NZ   . LYS   B 2 169  ? 195.928 149.614 140.918 1.00 154.79 ? 169  LYS   B NZ   1 
ATOM   7891 N  N    . ALA   B 2 170  ? 198.349 150.507 146.450 1.00 181.08 ? 170  ALA   B N    1 
ATOM   7892 C  CA   . ALA   B 2 170  ? 199.419 150.663 147.428 1.00 179.52 ? 170  ALA   B CA   1 
ATOM   7893 C  C    . ALA   B 2 170  ? 198.933 150.319 148.830 1.00 181.74 ? 170  ALA   B C    1 
ATOM   7894 O  O    . ALA   B 2 170  ? 199.633 149.635 149.586 1.00 180.34 ? 170  ALA   B O    1 
ATOM   7895 C  CB   . ALA   B 2 170  ? 199.975 152.086 147.382 1.00 169.87 ? 170  ALA   B CB   1 
ATOM   7896 N  N    . ALA   B 2 171  ? 197.736 150.771 149.189 1.00 180.19 ? 171  ALA   B N    1 
ATOM   7897 C  CA   . ALA   B 2 171  ? 197.176 150.485 150.502 1.00 171.68 ? 171  ALA   B CA   1 
ATOM   7898 C  C    . ALA   B 2 171  ? 196.438 149.155 150.484 1.00 172.42 ? 171  ALA   B C    1 
ATOM   7899 O  O    . ALA   B 2 171  ? 196.654 148.329 149.598 1.00 172.77 ? 171  ALA   B O    1 
ATOM   7900 C  CB   . ALA   B 2 171  ? 196.249 151.604 150.942 1.00 165.05 ? 171  ALA   B CB   1 
HETATM 7901 C  C13  . A1A7Q C 3 .    ? 177.397 209.366 195.454 1.00 38.38  ? 2601 A1A7Q A C13  1 
HETATM 7902 C  C15  . A1A7Q C 3 .    ? 178.638 210.779 193.706 1.00 35.15  ? 2601 A1A7Q A C15  1 
HETATM 7903 C  C17  . A1A7Q C 3 .    ? 177.043 211.101 192.112 1.00 42.14  ? 2601 A1A7Q A C17  1 
HETATM 7904 C  C21  . A1A7Q C 3 .    ? 173.000 209.388 194.129 1.00 56.95  ? 2601 A1A7Q A C21  1 
HETATM 7905 C  C22  . A1A7Q C 3 .    ? 172.114 208.458 193.306 1.00 70.24  ? 2601 A1A7Q A C22  1 
HETATM 7906 C  C24  . A1A7Q C 3 .    ? 173.745 206.764 193.388 1.00 66.32  ? 2601 A1A7Q A C24  1 
HETATM 7907 C  C01  . A1A7Q C 3 .    ? 178.939 201.766 203.777 1.00 62.07  ? 2601 A1A7Q A C01  1 
HETATM 7908 C  C02  . A1A7Q C 3 .    ? 179.599 202.018 202.426 1.00 57.40  ? 2601 A1A7Q A C02  1 
HETATM 7909 C  C03  . A1A7Q C 3 .    ? 181.074 201.694 202.227 1.00 48.12  ? 2601 A1A7Q A C03  1 
HETATM 7910 C  C04  . A1A7Q C 3 .    ? 181.634 201.909 201.061 1.00 40.88  ? 2601 A1A7Q A C04  1 
HETATM 7911 C  C05  . A1A7Q C 3 .    ? 180.812 202.493 199.922 1.00 45.80  ? 2601 A1A7Q A C05  1 
HETATM 7912 C  C07  . A1A7Q C 3 .    ? 181.387 203.886 197.869 1.00 50.44  ? 2601 A1A7Q A C07  1 
HETATM 7913 C  C09  . A1A7Q C 3 .    ? 179.788 205.799 197.344 1.00 36.20  ? 2601 A1A7Q A C09  1 
HETATM 7914 C  C11  . A1A7Q C 3 .    ? 178.260 207.887 197.211 1.00 37.28  ? 2601 A1A7Q A C11  1 
HETATM 7915 C  C12  . A1A7Q C 3 .    ? 178.475 208.458 196.043 1.00 36.73  ? 2601 A1A7Q A C12  1 
HETATM 7916 C  C14  . A1A7Q C 3 .    ? 177.513 210.110 194.119 1.00 40.09  ? 2601 A1A7Q A C14  1 
HETATM 7917 C  C18  . A1A7Q C 3 .    ? 176.397 210.294 193.112 1.00 44.33  ? 2601 A1A7Q A C18  1 
HETATM 7918 C  C19  . A1A7Q C 3 .    ? 175.093 209.925 192.921 1.00 45.88  ? 2601 A1A7Q A C19  1 
HETATM 7919 C  C25  . A1A7Q C 3 .    ? 174.804 207.711 193.924 1.00 55.94  ? 2601 A1A7Q A C25  1 
HETATM 7920 C  C27  . A1A7Q C 3 .    ? 175.115 211.066 190.912 1.00 63.99  ? 2601 A1A7Q A C27  1 
HETATM 7921 C  C30  . A1A7Q C 3 .    ? 176.311 209.599 196.153 1.00 41.49  ? 2601 A1A7Q A C30  1 
HETATM 7922 C  C31  . A1A7Q C 3 .    ? 176.069 208.945 197.497 1.00 44.03  ? 2601 A1A7Q A C31  1 
HETATM 7923 C  C32  . A1A7Q C 3 .    ? 176.984 208.155 197.986 1.00 44.89  ? 2601 A1A7Q A C32  1 
HETATM 7924 C  C34  . A1A7Q C 3 .    ? 182.121 203.675 196.744 1.00 42.77  ? 2601 A1A7Q A C34  1 
HETATM 7925 C  C35  . A1A7Q C 3 .    ? 182.627 202.355 196.802 1.00 34.83  ? 2601 A1A7Q A C35  1 
HETATM 7926 C  C36  . A1A7Q C 3 .    ? 183.500 201.697 195.756 1.00 34.84  ? 2601 A1A7Q A C36  1 
HETATM 7927 C  C37  . A1A7Q C 3 .    ? 184.729 202.571 195.547 1.00 34.89  ? 2601 A1A7Q A C37  1 
HETATM 7928 C  C38  . A1A7Q C 3 .    ? 182.712 201.570 194.463 1.00 38.10  ? 2601 A1A7Q A C38  1 
HETATM 7929 C  C39  . A1A7Q C 3 .    ? 183.910 200.316 196.241 1.00 41.66  ? 2601 A1A7Q A C39  1 
HETATM 7930 C  C41  . A1A7Q C 3 .    ? 179.541 202.773 200.092 1.00 50.36  ? 2601 A1A7Q A C41  1 
HETATM 7931 C  C42  . A1A7Q C 3 .    ? 178.887 202.518 201.442 1.00 56.74  ? 2601 A1A7Q A C42  1 
HETATM 7932 N  N06  . A1A7Q C 3 .    ? 181.442 202.722 198.642 1.00 46.22  ? 2601 A1A7Q A N06  1 
HETATM 7933 N  N08  . A1A7Q C 3 .    ? 180.705 205.108 198.221 1.00 48.73  ? 2601 A1A7Q A N08  1 
HETATM 7934 N  N10  . A1A7Q C 3 .    ? 179.209 207.013 197.863 1.00 35.84  ? 2601 A1A7Q A N10  1 
HETATM 7935 N  N16  . A1A7Q C 3 .    ? 178.302 211.308 192.560 1.00 35.61  ? 2601 A1A7Q A N16  1 
HETATM 7936 N  N20  . A1A7Q C 3 .    ? 174.394 209.101 193.875 1.00 46.68  ? 2601 A1A7Q A N20  1 
HETATM 7937 N  N26  . A1A7Q C 3 .    ? 174.477 210.318 191.816 1.00 56.28  ? 2601 A1A7Q A N26  1 
HETATM 7938 N  N29  . A1A7Q C 3 .    ? 176.379 211.460 191.043 1.00 47.14  ? 2601 A1A7Q A N29  1 
HETATM 7939 N  N40  . A1A7Q C 3 .    ? 182.211 201.785 197.956 1.00 41.66  ? 2601 A1A7Q A N40  1 
HETATM 7940 O  O23  . A1A7Q C 3 .    ? 172.851 207.496 192.603 1.00 70.15  ? 2601 A1A7Q A O23  1 
HETATM 7941 O  O33  . A1A7Q C 3 .    ? 179.533 205.394 196.269 1.00 38.21  ? 2601 A1A7Q A O33  1 
HETATM 7942 CL CL28 . A1A7Q C 3 .    ? 174.214 211.555 189.455 1.00 100.77 ? 2601 A1A7Q A CL28 1 
# 
